data_7HEU
# 
_entry.id   7HEU 
# 
_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   7HEU         pdb_00007heu 10.2210/pdb7heu/pdb 
WWPDB D_1001407384 ?            ?                   
# 
_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                        7HEU 
_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 '2-ethyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' 234.298   2   ?                      ? ? ? 
3 water       nat water                                                          18.015    421 ?                      ? ? ? 
# 
_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 '2-ethyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' A1BAA 
3 water                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAA non-polymer         . '2-ethyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]butan-1-ol' ? 'C12 H18 N4 O'   234.298 
ALA   'L-peptide linking' y ALANINE                                                        ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                       ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                     ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                       ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                          ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                  ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                        ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                         ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BAA 1   201 201  A1BAA LA1 A . 
D 2 A1BAA 1   202 301  A1BAA LA2 A . 
E 3 HOH   1   301 5    HOH   HOH A . 
E 3 HOH   2   302 196  HOH   HOH A . 
E 3 HOH   3   303 405  HOH   HOH A . 
E 3 HOH   4   304 153  HOH   HOH A . 
E 3 HOH   5   305 209  HOH   HOH A . 
E 3 HOH   6   306 86   HOH   HOH A . 
E 3 HOH   7   307 192  HOH   HOH A . 
E 3 HOH   8   308 625  HOH   HOH A . 
E 3 HOH   9   309 109  HOH   HOH A . 
E 3 HOH   10  310 74   HOH   HOH A . 
E 3 HOH   11  311 493  HOH   HOH A . 
E 3 HOH   12  312 292  HOH   HOH A . 
E 3 HOH   13  313 151  HOH   HOH A . 
E 3 HOH   14  314 105  HOH   HOH A . 
E 3 HOH   15  315 93   HOH   HOH A . 
E 3 HOH   16  316 1290 HOH   HOH A . 
E 3 HOH   17  317 78   HOH   HOH A . 
E 3 HOH   18  318 96   HOH   HOH A . 
E 3 HOH   19  319 76   HOH   HOH A . 
E 3 HOH   20  320 148  HOH   HOH A . 
E 3 HOH   21  321 247  HOH   HOH A . 
E 3 HOH   22  322 136  HOH   HOH A . 
E 3 HOH   23  323 1283 HOH   HOH A . 
E 3 HOH   24  324 236  HOH   HOH A . 
E 3 HOH   25  325 13   HOH   HOH A . 
E 3 HOH   26  326 124  HOH   HOH A . 
E 3 HOH   27  327 1295 HOH   HOH A . 
E 3 HOH   28  328 225  HOH   HOH A . 
E 3 HOH   29  329 164  HOH   HOH A . 
E 3 HOH   30  330 241  HOH   HOH A . 
E 3 HOH   31  331 140  HOH   HOH A . 
E 3 HOH   32  332 1300 HOH   HOH A . 
E 3 HOH   33  333 337  HOH   HOH A . 
E 3 HOH   34  334 36   HOH   HOH A . 
E 3 HOH   35  335 1301 HOH   HOH A . 
E 3 HOH   36  336 662  HOH   HOH A . 
E 3 HOH   37  337 57   HOH   HOH A . 
E 3 HOH   38  338 1309 HOH   HOH A . 
E 3 HOH   39  339 964  HOH   HOH A . 
E 3 HOH   40  340 396  HOH   HOH A . 
E 3 HOH   41  341 229  HOH   HOH A . 
E 3 HOH   42  342 320  HOH   HOH A . 
E 3 HOH   43  343 469  HOH   HOH A . 
E 3 HOH   44  344 661  HOH   HOH A . 
E 3 HOH   45  345 42   HOH   HOH A . 
E 3 HOH   46  346 21   HOH   HOH A . 
E 3 HOH   47  347 14   HOH   HOH A . 
E 3 HOH   48  348 139  HOH   HOH A . 
E 3 HOH   49  349 939  HOH   HOH A . 
E 3 HOH   50  350 81   HOH   HOH A . 
E 3 HOH   51  351 354  HOH   HOH A . 
E 3 HOH   52  352 92   HOH   HOH A . 
E 3 HOH   53  353 630  HOH   HOH A . 
E 3 HOH   54  354 66   HOH   HOH A . 
E 3 HOH   55  355 165  HOH   HOH A . 
E 3 HOH   56  356 2    HOH   HOH A . 
E 3 HOH   57  357 33   HOH   HOH A . 
E 3 HOH   58  358 26   HOH   HOH A . 
E 3 HOH   59  359 409  HOH   HOH A . 
E 3 HOH   60  360 138  HOH   HOH A . 
E 3 HOH   61  361 5    HOH   HOH A . 
E 3 HOH   62  362 39   HOH   HOH A . 
E 3 HOH   63  363 19   HOH   HOH A . 
E 3 HOH   64  364 24   HOH   HOH A . 
E 3 HOH   65  365 102  HOH   HOH A . 
E 3 HOH   66  366 169  HOH   HOH A . 
E 3 HOH   67  367 186  HOH   HOH A . 
E 3 HOH   68  368 45   HOH   HOH A . 
E 3 HOH   69  369 155  HOH   HOH A . 
E 3 HOH   70  370 122  HOH   HOH A . 
E 3 HOH   71  371 162  HOH   HOH A . 
E 3 HOH   72  372 159  HOH   HOH A . 
E 3 HOH   73  373 4    HOH   HOH A . 
E 3 HOH   74  374 17   HOH   HOH A . 
E 3 HOH   75  375 4    HOH   HOH A . 
E 3 HOH   76  376 34   HOH   HOH A . 
E 3 HOH   77  377 49   HOH   HOH A . 
E 3 HOH   78  378 218  HOH   HOH A . 
E 3 HOH   79  379 56   HOH   HOH A . 
E 3 HOH   80  380 46   HOH   HOH A . 
E 3 HOH   81  381 8    HOH   HOH A . 
E 3 HOH   82  382 393  HOH   HOH A . 
E 3 HOH   83  383 154  HOH   HOH A . 
E 3 HOH   84  384 27   HOH   HOH A . 
E 3 HOH   85  385 18   HOH   HOH A . 
E 3 HOH   86  386 6    HOH   HOH A . 
E 3 HOH   87  387 134  HOH   HOH A . 
E 3 HOH   88  388 461  HOH   HOH A . 
E 3 HOH   89  389 366  HOH   HOH A . 
E 3 HOH   90  390 296  HOH   HOH A . 
E 3 HOH   91  391 1275 HOH   HOH A . 
E 3 HOH   92  392 35   HOH   HOH A . 
E 3 HOH   93  393 3    HOH   HOH A . 
E 3 HOH   94  394 1313 HOH   HOH A . 
E 3 HOH   95  395 1315 HOH   HOH A . 
E 3 HOH   96  396 58   HOH   HOH A . 
E 3 HOH   97  397 195  HOH   HOH A . 
E 3 HOH   98  398 1308 HOH   HOH A . 
E 3 HOH   99  399 116  HOH   HOH A . 
E 3 HOH   100 400 1238 HOH   HOH A . 
E 3 HOH   101 401 85   HOH   HOH A . 
E 3 HOH   102 402 397  HOH   HOH A . 
E 3 HOH   103 403 303  HOH   HOH A . 
E 3 HOH   104 404 70   HOH   HOH A . 
E 3 HOH   105 405 7    HOH   HOH A . 
E 3 HOH   106 406 83   HOH   HOH A . 
E 3 HOH   107 407 12   HOH   HOH A . 
E 3 HOH   108 408 6    HOH   HOH A . 
E 3 HOH   109 409 199  HOH   HOH A . 
E 3 HOH   110 410 1068 HOH   HOH A . 
E 3 HOH   111 411 67   HOH   HOH A . 
E 3 HOH   112 412 68   HOH   HOH A . 
E 3 HOH   113 413 333  HOH   HOH A . 
E 3 HOH   114 414 281  HOH   HOH A . 
E 3 HOH   115 415 278  HOH   HOH A . 
E 3 HOH   116 416 121  HOH   HOH A . 
E 3 HOH   117 417 25   HOH   HOH A . 
E 3 HOH   118 418 132  HOH   HOH A . 
E 3 HOH   119 419 53   HOH   HOH A . 
E 3 HOH   120 420 1310 HOH   HOH A . 
E 3 HOH   121 421 115  HOH   HOH A . 
E 3 HOH   122 422 51   HOH   HOH A . 
E 3 HOH   123 423 123  HOH   HOH A . 
E 3 HOH   124 424 156  HOH   HOH A . 
E 3 HOH   125 425 1279 HOH   HOH A . 
E 3 HOH   126 426 351  HOH   HOH A . 
E 3 HOH   127 427 381  HOH   HOH A . 
E 3 HOH   128 428 582  HOH   HOH A . 
E 3 HOH   129 429 95   HOH   HOH A . 
E 3 HOH   130 430 212  HOH   HOH A . 
E 3 HOH   131 431 125  HOH   HOH A . 
E 3 HOH   132 432 7    HOH   HOH A . 
E 3 HOH   133 433 1289 HOH   HOH A . 
E 3 HOH   134 434 1222 HOH   HOH A . 
E 3 HOH   135 435 10   HOH   HOH A . 
E 3 HOH   136 436 9    HOH   HOH A . 
E 3 HOH   137 437 944  HOH   HOH A . 
E 3 HOH   138 438 576  HOH   HOH A . 
E 3 HOH   139 439 73   HOH   HOH A . 
E 3 HOH   140 440 40   HOH   HOH A . 
E 3 HOH   141 441 16   HOH   HOH A . 
E 3 HOH   142 442 71   HOH   HOH A . 
E 3 HOH   143 443 80   HOH   HOH A . 
E 3 HOH   144 444 1189 HOH   HOH A . 
E 3 HOH   145 445 94   HOH   HOH A . 
E 3 HOH   146 446 952  HOH   HOH A . 
E 3 HOH   147 447 188  HOH   HOH A . 
E 3 HOH   148 448 97   HOH   HOH A . 
E 3 HOH   149 449 104  HOH   HOH A . 
E 3 HOH   150 450 330  HOH   HOH A . 
E 3 HOH   151 451 79   HOH   HOH A . 
E 3 HOH   152 452 1119 HOH   HOH A . 
E 3 HOH   153 453 1094 HOH   HOH A . 
E 3 HOH   154 454 1296 HOH   HOH A . 
E 3 HOH   155 455 11   HOH   HOH A . 
E 3 HOH   156 456 3    HOH   HOH A . 
E 3 HOH   157 457 107  HOH   HOH A . 
E 3 HOH   158 458 509  HOH   HOH A . 
E 3 HOH   159 459 1134 HOH   HOH A . 
E 3 HOH   160 460 163  HOH   HOH A . 
E 3 HOH   161 461 1286 HOH   HOH A . 
E 3 HOH   162 462 2    HOH   HOH A . 
E 3 HOH   163 463 726  HOH   HOH A . 
E 3 HOH   164 464 408  HOH   HOH A . 
E 3 HOH   165 465 756  HOH   HOH A . 
E 3 HOH   166 466 342  HOH   HOH A . 
E 3 HOH   167 467 361  HOH   HOH A . 
E 3 HOH   168 468 1    HOH   HOH A . 
E 3 HOH   169 469 280  HOH   HOH A . 
E 3 HOH   170 470 556  HOH   HOH A . 
E 3 HOH   171 471 801  HOH   HOH A . 
E 3 HOH   172 472 126  HOH   HOH A . 
E 3 HOH   173 473 1284 HOH   HOH A . 
E 3 HOH   174 474 319  HOH   HOH A . 
E 3 HOH   175 475 1276 HOH   HOH A . 
E 3 HOH   176 476 370  HOH   HOH A . 
E 3 HOH   177 477 1307 HOH   HOH A . 
E 3 HOH   178 478 250  HOH   HOH A . 
E 3 HOH   179 479 63   HOH   HOH A . 
E 3 HOH   180 480 1306 HOH   HOH A . 
E 3 HOH   181 481 202  HOH   HOH A . 
E 3 HOH   182 482 711  HOH   HOH A . 
E 3 HOH   183 483 1287 HOH   HOH A . 
E 3 HOH   184 484 135  HOH   HOH A . 
E 3 HOH   185 485 695  HOH   HOH A . 
E 3 HOH   186 486 224  HOH   HOH A . 
E 3 HOH   187 487 8    HOH   HOH A . 
E 3 HOH   188 488 919  HOH   HOH A . 
E 3 HOH   189 489 267  HOH   HOH A . 
E 3 HOH   190 490 674  HOH   HOH A . 
E 3 HOH   191 491 521  HOH   HOH A . 
E 3 HOH   192 492 1299 HOH   HOH A . 
E 3 HOH   193 493 318  HOH   HOH A . 
E 3 HOH   194 494 315  HOH   HOH A . 
E 3 HOH   195 495 309  HOH   HOH A . 
E 3 HOH   196 496 1314 HOH   HOH A . 
E 3 HOH   197 497 331  HOH   HOH A . 
E 3 HOH   198 498 805  HOH   HOH A . 
E 3 HOH   199 499 941  HOH   HOH A . 
E 3 HOH   200 500 263  HOH   HOH A . 
E 3 HOH   201 501 208  HOH   HOH A . 
E 3 HOH   202 502 152  HOH   HOH A . 
E 3 HOH   203 503 12   HOH   HOH A . 
E 3 HOH   204 504 1071 HOH   HOH A . 
E 3 HOH   205 505 350  HOH   HOH A . 
E 3 HOH   206 506 180  HOH   HOH A . 
E 3 HOH   207 507 356  HOH   HOH A . 
E 3 HOH   208 508 326  HOH   HOH A . 
E 3 HOH   209 509 363  HOH   HOH A . 
E 3 HOH   210 510 313  HOH   HOH A . 
E 3 HOH   211 511 371  HOH   HOH A . 
E 3 HOH   212 512 185  HOH   HOH A . 
E 3 HOH   213 513 429  HOH   HOH A . 
E 3 HOH   214 514 772  HOH   HOH A . 
E 3 HOH   215 515 376  HOH   HOH A . 
E 3 HOH   216 516 1292 HOH   HOH A . 
E 3 HOH   217 517 1074 HOH   HOH A . 
E 3 HOH   218 518 346  HOH   HOH A . 
E 3 HOH   219 519 1078 HOH   HOH A . 
F 3 HOH   1   201 64   HOH   HOH B . 
F 3 HOH   2   202 358  HOH   HOH B . 
F 3 HOH   3   203 654  HOH   HOH B . 
F 3 HOH   4   204 549  HOH   HOH B . 
F 3 HOH   5   205 900  HOH   HOH B . 
F 3 HOH   6   206 398  HOH   HOH B . 
F 3 HOH   7   207 364  HOH   HOH B . 
F 3 HOH   8   208 240  HOH   HOH B . 
F 3 HOH   9   209 531  HOH   HOH B . 
F 3 HOH   10  210 1249 HOH   HOH B . 
F 3 HOH   11  211 758  HOH   HOH B . 
F 3 HOH   12  212 743  HOH   HOH B . 
F 3 HOH   13  213 232  HOH   HOH B . 
F 3 HOH   14  214 120  HOH   HOH B . 
F 3 HOH   15  215 264  HOH   HOH B . 
F 3 HOH   16  216 50   HOH   HOH B . 
F 3 HOH   17  217 353  HOH   HOH B . 
F 3 HOH   18  218 15   HOH   HOH B . 
F 3 HOH   19  219 452  HOH   HOH B . 
F 3 HOH   20  220 276  HOH   HOH B . 
F 3 HOH   21  221 332  HOH   HOH B . 
F 3 HOH   22  222 444  HOH   HOH B . 
F 3 HOH   23  223 131  HOH   HOH B . 
F 3 HOH   24  224 1140 HOH   HOH B . 
F 3 HOH   25  225 1278 HOH   HOH B . 
F 3 HOH   26  226 54   HOH   HOH B . 
F 3 HOH   27  227 282  HOH   HOH B . 
F 3 HOH   28  228 343  HOH   HOH B . 
F 3 HOH   29  229 723  HOH   HOH B . 
F 3 HOH   30  230 272  HOH   HOH B . 
F 3 HOH   31  231 205  HOH   HOH B . 
F 3 HOH   32  232 1312 HOH   HOH B . 
F 3 HOH   33  233 75   HOH   HOH B . 
F 3 HOH   34  234 110  HOH   HOH B . 
F 3 HOH   35  235 181  HOH   HOH B . 
F 3 HOH   36  236 127  HOH   HOH B . 
F 3 HOH   37  237 128  HOH   HOH B . 
F 3 HOH   38  238 1    HOH   HOH B . 
F 3 HOH   39  239 166  HOH   HOH B . 
F 3 HOH   40  240 82   HOH   HOH B . 
F 3 HOH   41  241 60   HOH   HOH B . 
F 3 HOH   42  242 252  HOH   HOH B . 
F 3 HOH   43  243 69   HOH   HOH B . 
F 3 HOH   44  244 30   HOH   HOH B . 
F 3 HOH   45  245 325  HOH   HOH B . 
F 3 HOH   46  246 300  HOH   HOH B . 
F 3 HOH   47  247 9    HOH   HOH B . 
F 3 HOH   48  248 129  HOH   HOH B . 
F 3 HOH   49  249 231  HOH   HOH B . 
F 3 HOH   50  250 72   HOH   HOH B . 
F 3 HOH   51  251 52   HOH   HOH B . 
F 3 HOH   52  252 14   HOH   HOH B . 
F 3 HOH   53  253 143  HOH   HOH B . 
F 3 HOH   54  254 31   HOH   HOH B . 
F 3 HOH   55  255 144  HOH   HOH B . 
F 3 HOH   56  256 41   HOH   HOH B . 
F 3 HOH   57  257 133  HOH   HOH B . 
F 3 HOH   58  258 47   HOH   HOH B . 
F 3 HOH   59  259 103  HOH   HOH B . 
F 3 HOH   60  260 172  HOH   HOH B . 
F 3 HOH   61  261 391  HOH   HOH B . 
F 3 HOH   62  262 10   HOH   HOH B . 
F 3 HOH   63  263 62   HOH   HOH B . 
F 3 HOH   64  264 150  HOH   HOH B . 
F 3 HOH   65  265 84   HOH   HOH B . 
F 3 HOH   66  266 271  HOH   HOH B . 
F 3 HOH   67  267 114  HOH   HOH B . 
F 3 HOH   68  268 117  HOH   HOH B . 
F 3 HOH   69  269 59   HOH   HOH B . 
F 3 HOH   70  270 61   HOH   HOH B . 
F 3 HOH   71  271 20   HOH   HOH B . 
F 3 HOH   72  272 77   HOH   HOH B . 
F 3 HOH   73  273 242  HOH   HOH B . 
F 3 HOH   74  274 11   HOH   HOH B . 
F 3 HOH   75  275 1277 HOH   HOH B . 
F 3 HOH   76  276 221  HOH   HOH B . 
F 3 HOH   77  277 302  HOH   HOH B . 
F 3 HOH   78  278 1305 HOH   HOH B . 
F 3 HOH   79  279 347  HOH   HOH B . 
F 3 HOH   80  280 175  HOH   HOH B . 
F 3 HOH   81  281 43   HOH   HOH B . 
F 3 HOH   82  282 416  HOH   HOH B . 
F 3 HOH   83  283 243  HOH   HOH B . 
F 3 HOH   84  284 1106 HOH   HOH B . 
F 3 HOH   85  285 287  HOH   HOH B . 
F 3 HOH   86  286 147  HOH   HOH B . 
F 3 HOH   87  287 22   HOH   HOH B . 
F 3 HOH   88  288 106  HOH   HOH B . 
F 3 HOH   89  289 1066 HOH   HOH B . 
F 3 HOH   90  290 13   HOH   HOH B . 
F 3 HOH   91  291 89   HOH   HOH B . 
F 3 HOH   92  292 235  HOH   HOH B . 
F 3 HOH   93  293 1291 HOH   HOH B . 
F 3 HOH   94  294 299  HOH   HOH B . 
F 3 HOH   95  295 99   HOH   HOH B . 
F 3 HOH   96  296 88   HOH   HOH B . 
F 3 HOH   97  297 311  HOH   HOH B . 
F 3 HOH   98  298 112  HOH   HOH B . 
F 3 HOH   99  299 220  HOH   HOH B . 
F 3 HOH   100 300 316  HOH   HOH B . 
F 3 HOH   101 301 387  HOH   HOH B . 
F 3 HOH   102 302 137  HOH   HOH B . 
F 3 HOH   103 303 216  HOH   HOH B . 
F 3 HOH   104 304 635  HOH   HOH B . 
F 3 HOH   105 305 215  HOH   HOH B . 
F 3 HOH   106 306 160  HOH   HOH B . 
F 3 HOH   107 307 1126 HOH   HOH B . 
F 3 HOH   108 308 118  HOH   HOH B . 
F 3 HOH   109 309 37   HOH   HOH B . 
F 3 HOH   110 310 101  HOH   HOH B . 
F 3 HOH   111 311 48   HOH   HOH B . 
F 3 HOH   112 312 38   HOH   HOH B . 
F 3 HOH   113 313 341  HOH   HOH B . 
F 3 HOH   114 314 142  HOH   HOH B . 
F 3 HOH   115 315 297  HOH   HOH B . 
F 3 HOH   116 316 91   HOH   HOH B . 
F 3 HOH   117 317 704  HOH   HOH B . 
F 3 HOH   118 318 32   HOH   HOH B . 
F 3 HOH   119 319 170  HOH   HOH B . 
F 3 HOH   120 320 141  HOH   HOH B . 
F 3 HOH   121 321 23   HOH   HOH B . 
F 3 HOH   122 322 100  HOH   HOH B . 
F 3 HOH   123 323 44   HOH   HOH B . 
F 3 HOH   124 324 28   HOH   HOH B . 
F 3 HOH   125 325 177  HOH   HOH B . 
F 3 HOH   126 326 161  HOH   HOH B . 
F 3 HOH   127 327 197  HOH   HOH B . 
F 3 HOH   128 328 1274 HOH   HOH B . 
F 3 HOH   129 329 29   HOH   HOH B . 
F 3 HOH   130 330 334  HOH   HOH B . 
F 3 HOH   131 331 339  HOH   HOH B . 
F 3 HOH   132 332 1285 HOH   HOH B . 
F 3 HOH   133 333 717  HOH   HOH B . 
F 3 HOH   134 334 98   HOH   HOH B . 
F 3 HOH   135 335 1294 HOH   HOH B . 
F 3 HOH   136 336 55   HOH   HOH B . 
F 3 HOH   137 337 445  HOH   HOH B . 
F 3 HOH   138 338 234  HOH   HOH B . 
F 3 HOH   139 339 182  HOH   HOH B . 
F 3 HOH   140 340 65   HOH   HOH B . 
F 3 HOH   141 341 207  HOH   HOH B . 
F 3 HOH   142 342 619  HOH   HOH B . 
F 3 HOH   143 343 1293 HOH   HOH B . 
F 3 HOH   144 344 362  HOH   HOH B . 
F 3 HOH   145 345 960  HOH   HOH B . 
F 3 HOH   146 346 178  HOH   HOH B . 
F 3 HOH   147 347 90   HOH   HOH B . 
F 3 HOH   148 348 463  HOH   HOH B . 
F 3 HOH   149 349 191  HOH   HOH B . 
F 3 HOH   150 350 1304 HOH   HOH B . 
F 3 HOH   151 351 203  HOH   HOH B . 
F 3 HOH   152 352 623  HOH   HOH B . 
F 3 HOH   153 353 1046 HOH   HOH B . 
F 3 HOH   154 354 1280 HOH   HOH B . 
F 3 HOH   155 355 335  HOH   HOH B . 
F 3 HOH   156 356 304  HOH   HOH B . 
F 3 HOH   157 357 87   HOH   HOH B . 
F 3 HOH   158 358 290  HOH   HOH B . 
F 3 HOH   159 359 541  HOH   HOH B . 
F 3 HOH   160 360 1077 HOH   HOH B . 
F 3 HOH   161 361 389  HOH   HOH B . 
F 3 HOH   162 362 479  HOH   HOH B . 
F 3 HOH   163 363 283  HOH   HOH B . 
F 3 HOH   164 364 718  HOH   HOH B . 
F 3 HOH   165 365 1072 HOH   HOH B . 
F 3 HOH   166 366 898  HOH   HOH B . 
F 3 HOH   167 367 1316 HOH   HOH B . 
F 3 HOH   168 368 340  HOH   HOH B . 
F 3 HOH   169 369 291  HOH   HOH B . 
F 3 HOH   170 370 373  HOH   HOH B . 
F 3 HOH   171 371 667  HOH   HOH B . 
F 3 HOH   172 372 1303 HOH   HOH B . 
F 3 HOH   173 373 615  HOH   HOH B . 
F 3 HOH   174 374 190  HOH   HOH B . 
F 3 HOH   175 375 310  HOH   HOH B . 
F 3 HOH   176 376 431  HOH   HOH B . 
F 3 HOH   177 377 149  HOH   HOH B . 
F 3 HOH   178 378 183  HOH   HOH B . 
F 3 HOH   179 379 1163 HOH   HOH B . 
F 3 HOH   180 380 1173 HOH   HOH B . 
F 3 HOH   181 381 418  HOH   HOH B . 
F 3 HOH   182 382 1311 HOH   HOH B . 
F 3 HOH   183 383 1000 HOH   HOH B . 
F 3 HOH   184 384 176  HOH   HOH B . 
F 3 HOH   185 385 424  HOH   HOH B . 
F 3 HOH   186 386 491  HOH   HOH B . 
F 3 HOH   187 387 470  HOH   HOH B . 
F 3 HOH   188 388 248  HOH   HOH B . 
F 3 HOH   189 389 265  HOH   HOH B . 
F 3 HOH   190 390 1298 HOH   HOH B . 
F 3 HOH   191 391 981  HOH   HOH B . 
F 3 HOH   192 392 184  HOH   HOH B . 
F 3 HOH   193 393 360  HOH   HOH B . 
F 3 HOH   194 394 410  HOH   HOH B . 
F 3 HOH   195 395 355  HOH   HOH B . 
F 3 HOH   196 396 566  HOH   HOH B . 
F 3 HOH   197 397 274  HOH   HOH B . 
F 3 HOH   198 398 314  HOH   HOH B . 
F 3 HOH   199 399 792  HOH   HOH B . 
F 3 HOH   200 400 157  HOH   HOH B . 
F 3 HOH   201 401 321  HOH   HOH B . 
F 3 HOH   202 402 558  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           7HEU 
_cell.length_a           88.771 
_cell.length_b           88.771 
_cell.length_c           39.592 
_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                         7HEU 
_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          7HEU 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.76 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HEU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165000 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.200 
_reflns.pdbx_Rmerge_I_obs            0.037 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.100 
_reflns.B_iso_Wilson_estimate        11.890 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.040 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1056156 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33203 7144 ? 1.131 ? ? ? 4.600 ? 1.000  ? ? ? ? ? ? 86.900 1.269 0.561 0.688 
1 2 5.480 44.390 ? 7524  1095 ? 0.024 ? ? ? 6.900 ? 65.700 ? ? ? ? ? ? 99.700 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HEU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.7000 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.1400 
_refine.ls_number_reflns_obs                     164919 
_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                          0.1454 
_refine.ls_R_factor_R_work                       0.1447 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1587 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7945 
_refine.ls_number_reflns_R_work                  156974 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.2740 
_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                            0.1000 
_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                                54.350 
_refine.B_iso_min                                8.820 
_refine.pdbx_overall_phase_error                 18.3300 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.7000 
_refine_hist.pdbx_number_atoms_ligand         70 
_refine_hist.number_atoms_solvent             421 
_refine_hist.number_atoms_total               3033 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.08 
_refine_hist.pdbx_B_iso_mean_solvent          30.30 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 84.0000  4442 . 0.4050 0.3754 . 233 0.0000 4675 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 93.0000  4937 . 0.3241 0.3592 . 211 0.0000 5148 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5219 . 0.2794 0.2878 . 250 0.0000 5469 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5214 . 0.2381 0.2396 . 279 0.0000 5493 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5208 . 0.2163 0.2292 . 317 0.0000 5525 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5245 . 0.2067 0.2447 . 254 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5286 . 0.1886 0.2046 . 262 0.0000 5548 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5237 . 0.1723 0.1922 . 255 0.0000 5492 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5218 . 0.1636 0.1860 . 280 0.0000 5498 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5288 . 0.1533 0.1892 . 243 0.0000 5531 . 'X-RAY DIFFRACTION' 
1.1500 1.1600  30 100.0000 5276 . 0.1436 0.1739 . 251 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5263 . 0.1330 0.1671 . 276 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5189 . 0.1259 0.1596 . 284 0.0000 5473 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5320 . 0.1200 0.1378 . 240 0.0000 5560 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5199 . 0.1225 0.1321 . 264 0.0000 5463 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5304 . 0.1223 0.1409 . 272 0.0000 5576 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5269 . 0.1237 0.1465 . 283 0.0000 5552 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5209 . 0.1291 0.1437 . 276 0.0000 5485 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5263 . 0.1275 0.1616 . 252 0.0000 5515 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5280 . 0.1264 0.1537 . 266 0.0000 5546 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5312 . 0.1217 0.1275 . 255 0.0000 5567 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5222 . 0.1177 0.1296 . 275 0.0000 5497 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5290 . 0.1177 0.1313 . 261 0.0000 5551 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5336 . 0.1254 0.1456 . 266 0.0000 5602 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5267 . 0.1367 0.1402 . 256 0.0000 5523 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5278 . 0.1367 0.1337 . 281 0.0000 5559 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5282 . 0.1386 0.1490 . 284 0.0000 5566 . 'X-RAY DIFFRACTION' 
2.1600 2.4700  30 100.0000 5311 . 0.1397 0.1466 . 290 0.0000 5601 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5322 . 0.1518 0.1702 . 260 0.0000 5582 . 'X-RAY DIFFRACTION' 
3.1100 39.7000 30 100.0000 5488 . 0.1511 0.1682 . 269 0.0000 5757 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEU 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003695' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEU 
_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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEU A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEU 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 7HEU SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEU MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEU SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEU MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HEU 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    308 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.82   -133.62 
2 1 SER A 128 ? B 67.13   -4.87   
3 1 PHE A 156 ? B -95.98  55.29   
4 1 ASP A 157 ? B -160.19 112.00  
5 1 HIS B 86  ? ? 57.85   -128.07 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 519 ? 7.51 . 
2 1 O ? B HOH 402 ? 6.26 . 
# 
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 
A1BAA O1   O N N 1   
A1BAA C1   C N N 2   
A1BAA C2   C N N 3   
A1BAA C3   C N N 4   
A1BAA C4   C N N 5   
A1BAA C5   C N N 6   
A1BAA C6   C N N 7   
A1BAA C7   C Y N 8   
A1BAA C8   C Y N 9   
A1BAA C10  C Y N 10  
A1BAA C11  C Y N 11  
A1BAA C12  C Y N 12  
A1BAA C9   C Y N 13  
A1BAA N1   N N N 14  
A1BAA N2   N Y N 15  
A1BAA N3   N Y N 16  
A1BAA N4   N Y N 17  
A1BAA H13  H N N 18  
A1BAA H2   H N N 19  
A1BAA H1   H N N 20  
A1BAA H3   H N N 21  
A1BAA H4   H N N 22  
A1BAA H5   H N N 23  
A1BAA H6   H N N 24  
A1BAA H7   H N N 25  
A1BAA H8   H N N 26  
A1BAA H10  H N N 27  
A1BAA H9   H N N 28  
A1BAA H12  H N N 29  
A1BAA H11  H N N 30  
A1BAA H15  H N N 31  
A1BAA H16  H N N 32  
A1BAA H17  H N N 33  
A1BAA H14  H N N 34  
A1BAA H18  H N N 35  
ALA   N    N N N 36  
ALA   CA   C N S 37  
ALA   C    C N N 38  
ALA   O    O N N 39  
ALA   CB   C N N 40  
ALA   OXT  O N N 41  
ALA   H    H N N 42  
ALA   H2   H N N 43  
ALA   HA   H N N 44  
ALA   HB1  H N N 45  
ALA   HB2  H N N 46  
ALA   HB3  H N N 47  
ALA   HXT  H N N 48  
ARG   N    N N N 49  
ARG   CA   C N S 50  
ARG   C    C N N 51  
ARG   O    O N N 52  
ARG   CB   C N N 53  
ARG   CG   C N N 54  
ARG   CD   C N N 55  
ARG   NE   N N N 56  
ARG   CZ   C N N 57  
ARG   NH1  N N N 58  
ARG   NH2  N N N 59  
ARG   OXT  O N N 60  
ARG   H    H N N 61  
ARG   H2   H N N 62  
ARG   HA   H N N 63  
ARG   HB2  H N N 64  
ARG   HB3  H N N 65  
ARG   HG2  H N N 66  
ARG   HG3  H N N 67  
ARG   HD2  H N N 68  
ARG   HD3  H N N 69  
ARG   HE   H N N 70  
ARG   HH11 H N N 71  
ARG   HH12 H N N 72  
ARG   HH21 H N N 73  
ARG   HH22 H N N 74  
ARG   HXT  H N N 75  
ASN   N    N N N 76  
ASN   CA   C N S 77  
ASN   C    C N N 78  
ASN   O    O N N 79  
ASN   CB   C N N 80  
ASN   CG   C N N 81  
ASN   OD1  O N N 82  
ASN   ND2  N N N 83  
ASN   OXT  O N N 84  
ASN   H    H N N 85  
ASN   H2   H N N 86  
ASN   HA   H N N 87  
ASN   HB2  H N N 88  
ASN   HB3  H N N 89  
ASN   HD21 H N N 90  
ASN   HD22 H N N 91  
ASN   HXT  H N N 92  
ASP   N    N N N 93  
ASP   CA   C N S 94  
ASP   C    C N N 95  
ASP   O    O N N 96  
ASP   CB   C N N 97  
ASP   CG   C N N 98  
ASP   OD1  O N N 99  
ASP   OD2  O N N 100 
ASP   OXT  O N N 101 
ASP   H    H N N 102 
ASP   H2   H N N 103 
ASP   HA   H N N 104 
ASP   HB2  H N N 105 
ASP   HB3  H N N 106 
ASP   HD2  H N N 107 
ASP   HXT  H N N 108 
CYS   N    N N N 109 
CYS   CA   C N R 110 
CYS   C    C N N 111 
CYS   O    O N N 112 
CYS   CB   C N N 113 
CYS   SG   S N N 114 
CYS   OXT  O N N 115 
CYS   H    H N N 116 
CYS   H2   H N N 117 
CYS   HA   H N N 118 
CYS   HB2  H N N 119 
CYS   HB3  H N N 120 
CYS   HG   H N N 121 
CYS   HXT  H N N 122 
GLN   N    N N N 123 
GLN   CA   C N S 124 
GLN   C    C N N 125 
GLN   O    O N N 126 
GLN   CB   C N N 127 
GLN   CG   C N N 128 
GLN   CD   C N N 129 
GLN   OE1  O N N 130 
GLN   NE2  N N N 131 
GLN   OXT  O N N 132 
GLN   H    H N N 133 
GLN   H2   H N N 134 
GLN   HA   H N N 135 
GLN   HB2  H N N 136 
GLN   HB3  H N N 137 
GLN   HG2  H N N 138 
GLN   HG3  H N N 139 
GLN   HE21 H N N 140 
GLN   HE22 H N N 141 
GLN   HXT  H N N 142 
GLU   N    N N N 143 
GLU   CA   C N S 144 
GLU   C    C N N 145 
GLU   O    O N N 146 
GLU   CB   C N N 147 
GLU   CG   C N N 148 
GLU   CD   C N N 149 
GLU   OE1  O N N 150 
GLU   OE2  O N N 151 
GLU   OXT  O N N 152 
GLU   H    H N N 153 
GLU   H2   H N N 154 
GLU   HA   H N N 155 
GLU   HB2  H N N 156 
GLU   HB3  H N N 157 
GLU   HG2  H N N 158 
GLU   HG3  H N N 159 
GLU   HE2  H N N 160 
GLU   HXT  H N N 161 
GLY   N    N N N 162 
GLY   CA   C N N 163 
GLY   C    C N N 164 
GLY   O    O N N 165 
GLY   OXT  O N N 166 
GLY   H    H N N 167 
GLY   H2   H N N 168 
GLY   HA2  H N N 169 
GLY   HA3  H N N 170 
GLY   HXT  H N N 171 
HIS   N    N N N 172 
HIS   CA   C N S 173 
HIS   C    C N N 174 
HIS   O    O N N 175 
HIS   CB   C N N 176 
HIS   CG   C Y N 177 
HIS   ND1  N Y N 178 
HIS   CD2  C Y N 179 
HIS   CE1  C Y N 180 
HIS   NE2  N Y N 181 
HIS   OXT  O N N 182 
HIS   H    H N N 183 
HIS   H2   H N N 184 
HIS   HA   H N N 185 
HIS   HB2  H N N 186 
HIS   HB3  H N N 187 
HIS   HD1  H N N 188 
HIS   HD2  H N N 189 
HIS   HE1  H N N 190 
HIS   HE2  H N N 191 
HIS   HXT  H N N 192 
HOH   O    O N N 193 
HOH   H1   H N N 194 
HOH   H2   H N N 195 
ILE   N    N N N 196 
ILE   CA   C N S 197 
ILE   C    C N N 198 
ILE   O    O N N 199 
ILE   CB   C N S 200 
ILE   CG1  C N N 201 
ILE   CG2  C N N 202 
ILE   CD1  C N N 203 
ILE   OXT  O N N 204 
ILE   H    H N N 205 
ILE   H2   H N N 206 
ILE   HA   H N N 207 
ILE   HB   H N N 208 
ILE   HG12 H N N 209 
ILE   HG13 H N N 210 
ILE   HG21 H N N 211 
ILE   HG22 H N N 212 
ILE   HG23 H N N 213 
ILE   HD11 H N N 214 
ILE   HD12 H N N 215 
ILE   HD13 H N N 216 
ILE   HXT  H N N 217 
LEU   N    N N N 218 
LEU   CA   C N S 219 
LEU   C    C N N 220 
LEU   O    O N N 221 
LEU   CB   C N N 222 
LEU   CG   C N N 223 
LEU   CD1  C N N 224 
LEU   CD2  C N N 225 
LEU   OXT  O N N 226 
LEU   H    H N N 227 
LEU   H2   H N N 228 
LEU   HA   H N N 229 
LEU   HB2  H N N 230 
LEU   HB3  H N N 231 
LEU   HG   H N N 232 
LEU   HD11 H N N 233 
LEU   HD12 H N N 234 
LEU   HD13 H N N 235 
LEU   HD21 H N N 236 
LEU   HD22 H N N 237 
LEU   HD23 H N N 238 
LEU   HXT  H N N 239 
LYS   N    N N N 240 
LYS   CA   C N S 241 
LYS   C    C N N 242 
LYS   O    O N N 243 
LYS   CB   C N N 244 
LYS   CG   C N N 245 
LYS   CD   C N N 246 
LYS   CE   C N N 247 
LYS   NZ   N N N 248 
LYS   OXT  O N N 249 
LYS   H    H N N 250 
LYS   H2   H N N 251 
LYS   HA   H N N 252 
LYS   HB2  H N N 253 
LYS   HB3  H N N 254 
LYS   HG2  H N N 255 
LYS   HG3  H N N 256 
LYS   HD2  H N N 257 
LYS   HD3  H N N 258 
LYS   HE2  H N N 259 
LYS   HE3  H N N 260 
LYS   HZ1  H N N 261 
LYS   HZ2  H N N 262 
LYS   HZ3  H N N 263 
LYS   HXT  H N N 264 
MET   N    N N N 265 
MET   CA   C N S 266 
MET   C    C N N 267 
MET   O    O N N 268 
MET   CB   C N N 269 
MET   CG   C N N 270 
MET   SD   S N N 271 
MET   CE   C N N 272 
MET   OXT  O N N 273 
MET   H    H N N 274 
MET   H2   H N N 275 
MET   HA   H N N 276 
MET   HB2  H N N 277 
MET   HB3  H N N 278 
MET   HG2  H N N 279 
MET   HG3  H N N 280 
MET   HE1  H N N 281 
MET   HE2  H N N 282 
MET   HE3  H N N 283 
MET   HXT  H N N 284 
PHE   N    N N N 285 
PHE   CA   C N S 286 
PHE   C    C N N 287 
PHE   O    O N N 288 
PHE   CB   C N N 289 
PHE   CG   C Y N 290 
PHE   CD1  C Y N 291 
PHE   CD2  C Y N 292 
PHE   CE1  C Y N 293 
PHE   CE2  C Y N 294 
PHE   CZ   C Y N 295 
PHE   OXT  O N N 296 
PHE   H    H N N 297 
PHE   H2   H N N 298 
PHE   HA   H N N 299 
PHE   HB2  H N N 300 
PHE   HB3  H N N 301 
PHE   HD1  H N N 302 
PHE   HD2  H N N 303 
PHE   HE1  H N N 304 
PHE   HE2  H N N 305 
PHE   HZ   H N N 306 
PHE   HXT  H N N 307 
PRO   N    N N N 308 
PRO   CA   C N S 309 
PRO   C    C N N 310 
PRO   O    O N N 311 
PRO   CB   C N N 312 
PRO   CG   C N N 313 
PRO   CD   C N N 314 
PRO   OXT  O N N 315 
PRO   H    H N N 316 
PRO   HA   H N N 317 
PRO   HB2  H N N 318 
PRO   HB3  H N N 319 
PRO   HG2  H N N 320 
PRO   HG3  H N N 321 
PRO   HD2  H N N 322 
PRO   HD3  H N N 323 
PRO   HXT  H N N 324 
SER   N    N N N 325 
SER   CA   C N S 326 
SER   C    C N N 327 
SER   O    O N N 328 
SER   CB   C N N 329 
SER   OG   O N N 330 
SER   OXT  O N N 331 
SER   H    H N N 332 
SER   H2   H N N 333 
SER   HA   H N N 334 
SER   HB2  H N N 335 
SER   HB3  H N N 336 
SER   HG   H N N 337 
SER   HXT  H N N 338 
THR   N    N N N 339 
THR   CA   C N S 340 
THR   C    C N N 341 
THR   O    O N N 342 
THR   CB   C N R 343 
THR   OG1  O N N 344 
THR   CG2  C N N 345 
THR   OXT  O N N 346 
THR   H    H N N 347 
THR   H2   H N N 348 
THR   HA   H N N 349 
THR   HB   H N N 350 
THR   HG1  H N N 351 
THR   HG21 H N N 352 
THR   HG22 H N N 353 
THR   HG23 H N N 354 
THR   HXT  H N N 355 
TYR   N    N N N 356 
TYR   CA   C N S 357 
TYR   C    C N N 358 
TYR   O    O N N 359 
TYR   CB   C N N 360 
TYR   CG   C Y N 361 
TYR   CD1  C Y N 362 
TYR   CD2  C Y N 363 
TYR   CE1  C Y N 364 
TYR   CE2  C Y N 365 
TYR   CZ   C Y N 366 
TYR   OH   O N N 367 
TYR   OXT  O N N 368 
TYR   H    H N N 369 
TYR   H2   H N N 370 
TYR   HA   H N N 371 
TYR   HB2  H N N 372 
TYR   HB3  H N N 373 
TYR   HD1  H N N 374 
TYR   HD2  H N N 375 
TYR   HE1  H N N 376 
TYR   HE2  H N N 377 
TYR   HH   H N N 378 
TYR   HXT  H N N 379 
VAL   N    N N N 380 
VAL   CA   C N S 381 
VAL   C    C N N 382 
VAL   O    O N N 383 
VAL   CB   C N N 384 
VAL   CG1  C N N 385 
VAL   CG2  C N N 386 
VAL   OXT  O N N 387 
VAL   H    H N N 388 
VAL   H2   H N N 389 
VAL   HA   H N N 390 
VAL   HB   H N N 391 
VAL   HG11 H N N 392 
VAL   HG12 H N N 393 
VAL   HG13 H N N 394 
VAL   HG21 H N N 395 
VAL   HG22 H N N 396 
VAL   HG23 H N N 397 
VAL   HXT  H N N 398 
# 
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 
A1BAA O1  C6   sing N N 1   
A1BAA C2  C1   sing N N 2   
A1BAA C2  C3   sing N N 3   
A1BAA C6  C3   sing N N 4   
A1BAA C3  N1   sing N N 5   
A1BAA C3  C4   sing N N 6   
A1BAA N1  C7   sing N N 7   
A1BAA C4  C5   sing N N 8   
A1BAA C7  C10  doub Y N 9   
A1BAA C7  N2   sing Y N 10  
A1BAA C11 C10  sing Y N 11  
A1BAA C11 C12  doub Y N 12  
A1BAA C10 C9   sing Y N 13  
A1BAA N2  C8   doub Y N 14  
A1BAA C12 N4   sing Y N 15  
A1BAA C8  N3   sing Y N 16  
A1BAA C9  N4   sing Y N 17  
A1BAA C9  N3   doub Y N 18  
A1BAA O1  H13  sing N N 19  
A1BAA C1  H2   sing N N 20  
A1BAA C1  H1   sing N N 21  
A1BAA C1  H3   sing N N 22  
A1BAA C2  H4   sing N N 23  
A1BAA C2  H5   sing N N 24  
A1BAA C4  H6   sing N N 25  
A1BAA C4  H7   sing N N 26  
A1BAA C5  H8   sing N N 27  
A1BAA C5  H10  sing N N 28  
A1BAA C5  H9   sing N N 29  
A1BAA C6  H12  sing N N 30  
A1BAA C6  H11  sing N N 31  
A1BAA C8  H15  sing N N 32  
A1BAA C11 H16  sing N N 33  
A1BAA C12 H17  sing N N 34  
A1BAA N1  H14  sing N N 35  
A1BAA N4  H18  sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7HEU 
_atom_sites.fract_transf_matrix[1][1]   0.011265 
_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]   0.011265 
_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]   0.025258 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.701 -16.365 22.253  0.70 39.98 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.195 -15.297 23.033  0.30 39.30 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.741 -15.278 22.413  0.70 39.60 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.204 -14.230 23.088  0.30 39.01 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.402 -13.938 22.115  0.70 37.66 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 18.891 -12.885 22.887  0.30 37.68 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.524 -13.678 22.551  0.70 37.84 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 19.896 -12.590 23.534  0.30 37.90 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.099 -15.301 23.819  0.70 40.80 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.412 -14.269 24.407  0.30 39.76 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.078 -14.177 23.967  0.70 41.24 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.025 -13.672 24.211  0.30 40.06 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.447 -16.651 24.078  0.70 41.28 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.321 -15.695 24.931  0.30 39.99 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.029 -15.390 21.772  0.70 47.51 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.570 -14.346 22.365  0.30 46.81 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.786 -15.168 24.489  0.70 48.96 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 17.874 -13.737 25.072  0.30 47.71 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.562 -14.324 24.776  0.70 49.49 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 15.549 -13.692 25.056  0.30 48.07 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.544 -13.329 24.025  0.70 49.49 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 16.116 -12.756 23.905  0.30 48.07 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.489 -14.182 23.197  0.70 49.49 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 15.546 -14.196 23.549  0.30 48.07 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.991 -16.625 24.933  0.70 49.53 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.660 -15.729 25.639  0.30 47.99 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.811 -16.834 23.368  0.70 49.53 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 17.057 -16.281 24.204  0.30 47.99 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.134 -17.335 24.090  0.70 49.53 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.188 -15.963 25.274  0.30 47.99 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.706 -13.096 21.352  0.70 35.19 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.346 -12.078 21.985  0.30 35.93 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.145 -11.736 21.069  0.70 32.76 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.901 -10.775 21.642  0.30 34.14 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.982 -10.777 21.311  0.70 30.66 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.886 -9.683  21.983  0.30 32.91 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.867 -11.188 21.647  0.70 30.46 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.846 -9.940  22.596  0.30 32.88 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.720 -11.610 19.651  0.70 32.39 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.311 -10.743 20.168  0.30 33.56 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.728 -12.002 18.577  0.70 31.92 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.263 -11.351 19.258  0.30 33.10 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.607 -11.497 18.536  0.70 31.63 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.075 -11.047 19.368  0.30 33.00 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.139 -12.911 17.698  0.70 31.77 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.699 -12.229 18.361  0.30 32.84 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.958 -13.297 20.974  0.70 42.23 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.630 -12.270 21.547  0.30 43.12 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.850 -11.502 21.687  0.70 39.32 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.700 -10.630 22.173  0.30 40.97 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.980 -10.687 19.496  0.70 38.87 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.451 -9.823  19.893  0.30 40.27 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.492 -12.189 19.574  0.70 38.87 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.129 -11.248 20.063  0.30 40.27 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.615 -13.167 17.066  0.70 38.13 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.145 -12.606 17.822  0.30 39.41 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.932 -13.240 17.757  0.70 38.13 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.537 -12.418 18.318  0.30 39.41 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.251 -9.485  21.131  0.70 28.69 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.195 -8.453  21.572  0.30 31.70 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.314 -8.433  21.505  0.70 27.04 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.338 -7.305  21.832  0.30 30.44 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.430 -7.968  20.355  0.70 24.63 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.438 -6.963  20.650  0.30 28.59 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.649 -7.029  20.539  0.70 24.86 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.748 -5.940  20.686  0.30 28.61 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.071 -7.242  22.107  0.70 27.76 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.175 -6.087  22.236  0.30 30.95 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.099 -6.801  21.240  0.70 28.18 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 19.100 -5.735  21.225  0.30 31.28 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.976 -9.187  20.779  0.70 34.43 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.903 -8.263  21.122  0.30 38.04 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.729 -8.768  22.194  0.70 32.45 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.766 -7.517  22.583  0.30 36.53 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.451 -6.509  22.258  0.70 33.31 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.580 -5.336  22.393  0.30 37.14 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.467 -7.513  22.952  0.70 33.31 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.662 -6.295  23.049  0.30 37.14 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.509 -6.147  21.585  0.70 33.82 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.547 -5.065  21.465  0.30 37.54 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.514 -8.598  19.186  0.70 21.84 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.433 -7.789  19.604  0.30 26.74 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.622 -8.244  18.089  0.70 19.70 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.488 -7.602  18.510  0.30 24.81 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.189 -8.616  18.457  0.70 19.74 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.087 -7.954  18.995  0.30 24.59 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.926 -9.736  18.903  0.70 20.47 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.834 -9.088  19.414  0.30 24.56 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.041 -8.966  16.810  0.70 18.26 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.872 -8.479  17.321  0.30 23.33 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.313 -8.431  16.195  0.70 17.37 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.153 -8.067  16.648  0.30 22.15 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.311 -7.241  15.484  0.70 17.20 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.218 -6.899  15.906  0.30 21.64 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.502 -9.131  16.317  0.70 17.52 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.286 -8.856  16.748  0.30 21.98 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.477 -6.754  14.917  0.70 17.37 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.395 -6.520  15.285  0.30 21.39 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.666 -8.650  15.751  0.70 17.91 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.464 -8.484  16.129  0.30 21.73 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.655 -7.459  15.051  0.70 17.65 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.518 -7.315  15.396  0.30 21.51 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.069 -9.230  19.011  0.70 26.21 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.964 -8.457  19.504  0.30 32.09 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.660 -7.293  17.933  0.70 23.64 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.496 -6.676  18.230  0.30 29.78 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.181 -9.909  17.014  0.70 21.91 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.978 -9.393  17.627  0.30 28.00 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.332 -8.880  16.154  0.70 21.91 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.163 -8.435  16.660  0.30 28.00 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.517 -6.767  15.393  0.70 20.64 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.464 -6.360  15.830  0.30 25.96 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.516 -9.934  16.791  0.70 21.02 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.255 -9.644  17.241  0.30 26.37 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.466 -5.954  14.443  0.70 20.84 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.428 -5.732  14.790  0.30 25.66 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.461 -9.125  15.845  0.70 21.49 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.220 -9.020  16.204  0.30 26.07 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.439 -7.134  14.669  0.70 21.18 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.310 -7.062  14.978  0.30 25.82 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.260 -7.676  18.272  0.70 19.56 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.180 -6.984  18.941  0.30 24.34 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.892 -7.825  18.756  0.70 20.31 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.831 -7.136  19.463  0.30 24.15 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.889 -7.544  17.644  0.70 18.91 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.821 -6.973  18.335  0.30 23.14 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.087 -6.638  16.830  0.70 19.04 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.939 -6.064  17.508  0.30 23.37 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.638 -6.867  19.927  0.70 22.44 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.559 -6.093  20.556  0.30 24.81 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.291 -6.935  20.350  0.70 23.91 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.330 -6.345  21.213  0.30 25.32 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.405 -6.935  17.861  0.70 23.47 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.329 -6.208  18.600  0.30 29.20 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.754 -8.732  19.067  0.70 24.37 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.725 -8.018  19.851  0.30 28.98 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.213 -7.115  20.670  0.70 26.93 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.279 -6.124  21.209  0.30 29.78 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.835 -5.960  19.646  0.70 26.93 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.520 -5.213  20.152  0.30 29.78 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.161 -6.408  20.991  0.70 28.69 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.200 -5.770  21.813  0.30 30.38 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.808  -8.327  17.616  0.70 18.52 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.831  -7.863  18.306  0.30 21.96 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.715  -8.071  16.698  0.70 17.99 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.726  -7.735  17.377  0.30 20.81 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.906  -8.574  15.285  0.70 17.02 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.968  -8.253  15.978  0.30 19.66 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.159  -8.162  14.391  0.70 17.86 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.223  -7.886  15.065  0.30 19.72 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.697  -9.013  18.115  0.70 22.22 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.777  -8.544  18.825  0.30 26.36 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.912  -8.484  17.054  0.70 21.59 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.961  -8.208  17.739  0.30 24.97 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.563  -7.116  16.649  0.70 21.59 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.488  -6.798  17.301  0.30 24.97 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.875  -9.454  15.048  0.70 15.58 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.978  -9.094  15.772  0.30 18.76 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.122 -9.976  13.714  0.70 14.35 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.242 -9.626  14.442  0.30 17.98 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.252  -11.195 13.434  0.70 14.06 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.325  -10.805 14.121  0.30 17.15 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.964  -12.006 14.320  0.70 15.51 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 8.924  -11.571 15.002  0.30 17.25 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.601 -10.351 13.526  0.70 14.40 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.704 -10.062 14.313  0.30 18.25 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.507 -9.142  13.396  0.70 15.14 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.634 -8.971  13.832  0.30 18.35 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.795 -8.351  14.498  0.70 15.60 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 13.136 -8.019  14.708  0.30 18.49 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.049 -8.775  12.167  0.70 14.79 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.007 -8.893  12.497  0.30 18.29 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.603 -7.230  14.389  0.70 15.84 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.983 -7.022  14.266  0.30 18.58 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.856 -7.651  12.046  0.70 15.24 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.851 -7.903  12.046  0.30 18.57 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.123 -6.884  13.159  0.70 15.61 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.334 -6.971  12.931  0.30 18.76 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.922 -5.775  13.039  0.70 16.39 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 15.174 -5.989  12.469  0.30 19.05 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.398 -9.774  15.649  0.70 18.70 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.530 -9.364  16.380  0.30 22.51 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.902  -9.300  13.059  0.70 17.23 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 10.083 -8.928  13.788  0.30 21.58 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.898 -10.869 14.291  0.70 17.28 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 12.035 -10.364 15.169  0.30 21.90 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.689 -10.880 12.716  0.70 17.28 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.751 -10.786 13.675  0.30 21.90 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.430 -8.578  15.327  0.70 18.72 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.901 -8.053  15.608  0.30 22.18 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.864 -9.288  11.413  0.70 17.74 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.684 -9.522  11.895  0.30 21.94 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.778 -6.713  15.140  0.70 19.00 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 14.314 -6.390  14.863  0.30 22.30 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.218 -7.417  11.221  0.70 18.29 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.093 -7.866  11.148  0.30 22.28 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.018 -5.402  13.789  0.70 19.67 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 15.400 -5.490  13.102  0.30 22.86 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.848  -11.318 12.176  0.70 13.35 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.982  -10.924 12.839  0.30 16.59 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.249  -12.539 11.662  0.70 13.32 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.270  -12.077 12.304  0.30 16.39 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.372  -13.471 11.214  0.70 13.00 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.291  -13.065 11.758  0.30 15.38 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.320 -13.036 10.550  0.70 12.95 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.212 -12.680 11.031  0.30 15.06 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.351  -12.190 10.478  0.70 14.39 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.330  -11.632 11.182  0.30 17.07 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.600  -13.363 9.851   0.70 16.53 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.472  -12.662 10.440  0.30 17.73 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.524  -13.896 10.791  0.70 17.81 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.172  -12.005 10.005  0.30 18.19 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.010  -12.960 8.509   0.70 18.08 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 7.195  -13.226 9.226   0.30 17.78 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.918  -10.698 11.579  0.70 16.02 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 9.150  -10.323 12.251  0.30 19.91 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.724  -12.975 12.351  0.70 15.98 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.751  -12.502 13.007  0.30 19.67 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.687  -11.550 10.776  0.70 17.26 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.718  -10.983 11.556  0.30 20.48 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.896  -11.794 9.783   0.70 17.26 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.874  -11.196 10.509  0.30 20.48 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.225  -14.087 9.688   0.70 19.84 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 6.255  -13.394 11.036  0.30 21.27 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.102  -14.670 10.384  0.70 21.38 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 4.654  -12.640 9.490   0.30 21.83 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.932  -14.147 11.633  0.70 21.38 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 4.677  -11.732 10.793  0.30 21.83 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.862  -13.200 10.939  0.70 21.38 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.380  -11.228 9.460   0.30 21.83 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.535  -13.718 8.133   0.70 21.69 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 6.589  -13.804 8.738   0.30 21.34 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.400  -12.219 8.644   0.70 21.69 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 7.477  -12.490 8.657   0.30 21.34 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.731  -12.694 7.918   0.70 21.69 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 7.968  -13.729 9.522   0.30 21.34 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.273  -14.746 11.588  0.70 12.92 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.127  -14.335 12.105  0.30 14.99 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.276 -15.745 11.236  0.70 13.06 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.081 -15.364 11.715  0.30 14.42 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.923  -16.328 9.874   0.70 12.78 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.725  -15.878 10.324  0.30 13.98 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.863  -16.939 9.718   0.70 14.87 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.614  -16.374 10.106  0.30 14.11 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.312 -16.837 12.308  0.70 12.87 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.057 -16.497 12.736  0.30 14.39 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.352 -17.940 12.109  0.70 13.15 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.057 -17.598 12.471  0.30 14.25 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.476 -18.778 13.391  0.70 13.80 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.068 -18.578 13.626  0.30 14.05 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.466 -19.932 13.267  0.70 13.88 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.038 -19.718 13.381  0.30 13.81 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.839 -19.464 12.959  0.70 13.80 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.450 -19.247 13.306  0.30 13.76 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.619  -15.068 12.052  0.70 15.50 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.460  -14.625 12.569  0.30 17.98 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.149 -15.335 11.181  0.70 15.67 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 10.973 -14.981 11.690  0.30 17.30 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.501 -16.421 13.162  0.70 15.44 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.248 -16.125 13.613  0.30 17.27 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.444  -17.268 12.343  0.70 15.44 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.173  -16.892 12.736  0.30 17.27 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.074 -18.528 11.385  0.70 15.78 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.807 -18.074 11.664  0.30 17.10 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.216 -17.548 11.914  0.70 15.78 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 11.944 -17.215 12.381  0.30 17.10 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.776 -18.206 14.112  0.70 16.55 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.338 -18.113 14.435  0.30 16.86 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.609 -19.156 13.605  0.70 16.55 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.178 -18.949 13.736  0.30 16.86 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.499 -20.420 14.109  0.70 16.66 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 11.969 -20.355 14.108  0.30 16.57 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.184 -20.525 12.554  0.70 16.66 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.817 -20.146 12.538  0.30 16.57 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.387 -20.164 12.873  0.70 16.57 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 13.994 -19.938 13.174  0.30 16.51 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.839 -19.004 12.200  0.70 16.57 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.544 -18.671 12.633  0.30 16.51 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.138 -18.945 13.616  0.70 16.57 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.676 -18.841 14.066  0.30 16.51 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.805 -16.154 8.890   0.70 12.02 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.657 -15.746 9.381   0.30 14.04 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.546 -16.727 7.570   0.70 12.49 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.434 -16.232 8.023   0.30 14.33 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.126 -18.128 7.416   0.70 12.38 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 10.975 -17.644 7.822   0.30 13.73 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.494 -18.996 6.805   0.70 12.65 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.282 -18.508 7.274   0.30 13.82 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.101 -15.825 6.463   0.70 13.34 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.081 -15.286 7.011   0.30 15.55 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.424 -14.464 6.290   0.70 14.63 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.392 -13.943 6.789   0.30 16.39 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.162 -13.631 5.249   0.70 15.09 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.336 -13.010 6.060   0.30 17.12 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 8.956  -14.631 5.911   0.70 15.67 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 9.100  -14.120 6.003   0.30 16.64 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.555 -15.721 8.956   0.70 14.43 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.420 -15.358 9.501   0.30 16.85 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.592  -16.797 7.448   0.70 14.99 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.481  -16.244 7.852   0.30 17.20 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.040 -15.662 6.650   0.70 16.00 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 11.985 -15.099 7.307   0.30 18.66 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.021 -16.300 5.621   0.70 16.00 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.109 -15.739 6.156   0.30 18.66 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.463 -13.986 7.130   0.70 17.56 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.173 -13.547 7.648   0.30 19.66 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.717 -12.775 5.150   0.70 18.10 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.885 -12.169 5.895   0.30 20.55 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.079 -13.490 5.545   0.70 18.10 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.121 -12.863 6.612   0.30 20.55 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.164 -14.104 4.401   0.70 18.10 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 11.596 -13.419 5.220   0.30 20.55 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.594  -13.765 5.668   0.70 18.80 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.696  -13.249 5.861   0.30 19.97 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.893  -15.239 5.157   0.70 18.80 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 9.309  -14.529 5.147   0.30 19.97 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.475  -14.992 6.670   0.70 18.80 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.497  -14.688 6.504   0.30 19.97 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.332 -18.351 7.932   0.70 12.21 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.216 -17.883 8.233   0.30 13.46 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.023 -19.632 7.833   0.70 12.55 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.835 -19.195 8.128   0.30 13.43 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.807 -19.856 9.119   0.70 12.60 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.569 -19.475 9.432   0.30 13.79 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.721 -19.078 10.076  0.70 12.75 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.469 -18.724 10.407  0.30 13.73 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 13.993 -19.689 6.642   0.70 13.55 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.811 -19.249 6.945   0.30 13.41 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.071 -18.784 6.880   0.70 13.67 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.885 -18.334 7.183   0.30 13.04 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.315 -19.330 5.331   0.70 14.76 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.115 -18.901 5.632   0.30 13.37 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.789 -17.762 8.351   0.70 14.66 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.733 -17.282 8.572   0.30 16.15 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.381 -20.356 7.735   0.70 15.06 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.150 -19.868 7.995   0.30 16.11 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.354 -20.587 6.556   0.70 16.26 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.171 -20.143 6.865   0.30 16.09 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.609 -18.797 6.229   0.70 16.41 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.419 -18.342 6.535   0.30 15.65 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.908 -19.531 4.588   0.70 17.71 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.740 -18.988 4.893   0.30 16.04 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.502 -19.846 5.231   0.70 17.71 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.369 -19.505 5.482   0.30 16.04 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.098 -18.387 5.318   0.70 17.71 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 12.784 -17.992 5.659   0.30 16.04 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.616 -20.918 9.120   0.70 13.15 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.324 -20.571 9.435   0.30 14.30 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.461 -21.201 10.271  0.70 13.76 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.182 -20.885 10.568  0.30 15.12 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.293 -19.993 10.686  0.70 13.46 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.091 -19.713 10.921  0.30 14.24 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.545 -19.795 11.879  0.70 14.59 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.318 -19.431 12.104  0.30 14.37 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.384 -22.380 9.973   0.70 16.26 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.014 -22.118 10.225  0.30 17.15 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.267 -22.708 11.147  0.70 20.13 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.093 -22.406 11.252  0.30 19.14 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.716 -23.168 12.172  0.70 20.86 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.800 -22.387 12.467  0.30 19.90 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.489 -22.463 11.054  0.70 23.18 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.239 -22.670 10.839  0.30 20.21 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.710 -21.482 8.468   0.70 15.78 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.350 -21.141 8.796   0.30 17.16 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.908 -21.449 11.024  0.70 16.52 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.628 -21.089 11.340  0.30 18.15 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.842 -23.176 9.767   0.70 19.52 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.419 -22.883 10.158  0.30 20.59 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.956 -22.182 9.220   0.70 19.52 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.450 -21.967 9.370   0.30 20.59 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.753 -19.185 9.718   0.70 13.19 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.595 -18.996 9.906   0.30 13.85 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.719 -18.127 10.010  0.70 14.08 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.681 -18.038 10.093  0.30 13.75 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.327 -16.733 9.536   0.70 13.95 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.376 -16.654 9.524   0.30 13.82 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 18.041 -15.777 9.876   0.70 14.25 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.302 -15.855 9.349   0.30 14.20 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 19.106 -18.471 9.429   0.70 14.24 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 18.988 -18.571 9.488   0.30 13.39 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 19.086 -18.627 7.922   0.70 14.83 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 18.991 -18.543 7.966   0.30 13.58 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.298 -19.403 7.379   0.70 15.93 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.385 -19.398 7.318   0.30 14.05 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.931 -17.863 7.232   0.70 14.14 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.688 -17.563 7.389   0.30 12.88 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.528 -19.241 8.889   0.70 15.82 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.313 -19.045 9.100   0.30 16.62 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.834 -18.079 10.970  0.70 16.89 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.833 -17.927 11.045  0.30 16.50 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.733 -17.756 9.653   0.70 17.09 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.725 -18.023 9.797   0.30 16.06 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.422 -19.306 9.815   0.70 17.09 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.113 -19.490 9.766   0.30 16.06 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 19.955 -17.922 6.374   0.70 16.97 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.721 -17.499 6.529   0.30 15.46 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.477 -17.336 7.640   0.70 16.97 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.104 -16.986 7.874   0.30 15.46 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.243 -16.582 8.768   0.70 12.84 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.114 -16.336 9.239   0.30 13.16 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.841 -15.306 8.178   0.70 12.59 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.762 -15.027 8.692   0.30 12.44 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.563 -14.808 8.848   0.70 12.00 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.505 -14.512 9.383   0.30 12.20 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.558 -15.531 8.923   0.70 12.13 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.501 -15.225 9.481   0.30 12.50 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.655 -15.411 6.654   0.70 13.10 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.589 -15.046 7.158   0.30 12.08 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.173 -14.079 6.078   0.70 13.87 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.305 -13.644 6.645   0.30 11.77 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 16.942 -15.860 5.973   0.70 13.82 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.826 -15.614 6.469   0.30 12.91 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.720 -17.236 8.573   0.70 15.41 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.440 -16.857 9.364   0.30 15.80 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.546 -14.660 8.344   0.70 15.10 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.477 -14.406 8.896   0.30 14.93 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 14.979 -16.087 6.472   0.70 15.72 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 14.834 -15.607 6.930   0.30 14.49 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.256 -14.111 5.114   0.70 16.65 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 15.361 -13.645 5.678   0.30 14.12 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.242 -13.953 6.326   0.70 16.65 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.415 -13.381 6.924   0.30 14.12 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.716 -13.369 6.440   0.70 16.65 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.963 -13.034 7.014   0.30 14.12 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.828 -15.792 5.014   0.70 16.58 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.827 -15.338 5.536   0.30 15.49 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.666 -15.286 6.264   0.70 16.58 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.618 -15.279 6.912   0.30 15.49 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 17.129 -16.780 6.221   0.70 16.58 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 16.801 -16.581 6.525   0.30 15.49 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.596 -13.544 9.273   0.70 11.87 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.566 -13.262 9.847   0.30 12.10 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.521 -12.868 9.981   0.70 12.03 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.480 -12.590 10.544  0.30 12.16 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.242 -11.542 9.284   0.70 12.15 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.240 -11.244 9.878   0.30 12.05 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.139 -10.973 8.658   0.70 12.02 ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 14.163 -10.654 9.313   0.30 11.77 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.960 -12.606 11.427  0.70 12.74 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 13.841 -12.381 12.022  0.30 12.90 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 14.132 -13.865 12.253  0.70 13.63 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 14.153 -13.675 12.747  0.30 13.93 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.293 -14.633 12.178  0.70 14.25 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 15.405 -14.271 12.645  0.30 14.51 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 13.126 -14.290 13.108  0.70 14.16 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 13.193 -14.303 13.528  0.30 14.69 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.438 -15.798 12.933  0.70 14.51 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 15.691 -15.455 13.301  0.30 15.29 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 13.259 -15.450 13.862  0.70 14.90 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 13.471 -15.490 14.189  0.30 15.29 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.418 -16.198 13.777  0.70 14.84 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 14.721 -16.060 14.072  0.30 15.57 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.540 -17.344 14.536  0.70 15.48 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 15.003 -17.237 14.729  0.30 15.94 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.284 -13.038 9.147   0.70 14.24 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.260 -12.759 9.759   0.30 14.52 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.726 -13.424 9.976   0.70 14.44 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.669 -13.109 10.487  0.30 14.59 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.813 -12.148 11.417  0.70 15.28 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 14.623 -11.806 12.079  0.30 15.48 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 13.292 -12.065 11.858  0.70 15.28 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.092 -11.958 12.471  0.30 15.48 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 15.983 -14.376 11.608  0.70 17.10 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 16.063 -13.866 12.127  0.30 17.41 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.342 -13.799 13.172  0.70 16.99 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 12.349 -13.920 13.608  0.30 17.63 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 16.223 -16.302 12.873  0.70 17.42 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 16.535 -15.840 13.223  0.30 18.35 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.576 -15.715 14.434  0.70 17.88 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 12.818 -15.898 14.708  0.30 18.35 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 13.807 -17.519 14.904  0.70 18.57 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 15.737 -17.549 14.463  0.30 19.13 ?  17  TYR   A HH   1 
ATOM   473  N N    A ILE   A 1 18  ? 12.011 -11.029 9.400   0.70 12.49 ?  18  ILE   A N    1 
ATOM   474  N N    B ILE   A 1 18  ? 12.001 -10.752 9.941   0.30 11.90 ?  18  ILE   A N    1 
ATOM   475  C CA   A ILE   A 1 18  ? 11.624 -9.822  8.667   0.70 13.02 ?  18  ILE   A CA   1 
ATOM   476  C CA   B ILE   A 1 18  ? 11.631 -9.530  9.231   0.30 11.83 ?  18  ILE   A CA   1 
ATOM   477  C C    A ILE   A 1 18  ? 10.658 -8.977  9.492   0.70 13.48 ?  18  ILE   A C    1 
ATOM   478  C C    B ILE   A 1 18  ? 10.714 -8.672  10.094  0.30 12.02 ?  18  ILE   A C    1 
ATOM   479  O O    A ILE   A 1 18  ? 9.831  -9.503  10.243  0.70 13.79 ?  18  ILE   A O    1 
ATOM   480  O O    B ILE   A 1 18  ? 9.855  -9.186  10.820  0.30 12.11 ?  18  ILE   A O    1 
ATOM   481  C CB   A ILE   A 1 18  ? 11.056 -10.194 7.276   0.70 13.23 ?  18  ILE   A CB   1 
ATOM   482  C CB   B ILE   A 1 18  ? 11.000 -9.840  7.856   0.30 11.47 ?  18  ILE   A CB   1 
ATOM   483  C CG1  A ILE   A 1 18  ? 11.003 -8.971  6.362   0.70 13.66 ?  18  ILE   A CG1  1 
ATOM   484  C CG1  B ILE   A 1 18  ? 10.903 -8.569  7.009   0.30 12.05 ?  18  ILE   A CG1  1 
ATOM   485  C CG2  A ILE   A 1 18  ? 9.703  -10.904 7.415   0.70 13.58 ?  18  ILE   A CG2  1 
ATOM   486  C CG2  B ILE   A 1 18  ? 9.630  -10.490 8.022   0.30 11.50 ?  18  ILE   A CG2  1 
ATOM   487  C CD1  A ILE   A 1 18  ? 10.730 -9.317  4.922   0.70 15.20 ?  18  ILE   A CD1  1 
ATOM   488  C CD1  B ILE   A 1 18  ? 10.489 -8.837  5.582   0.30 12.66 ?  18  ILE   A CD1  1 
ATOM   489  H H    A ILE   A 1 18  ? 11.393 -11.377 9.894   0.70 14.99 ?  18  ILE   A H    1 
ATOM   490  H H    B ILE   A 1 18  ? 11.361 -11.107 10.391  0.30 14.28 ?  18  ILE   A H    1 
ATOM   491  H HA   A ILE   A 1 18  ? 12.423 -9.301  8.521   0.70 15.62 ?  18  ILE   A HA   1 
ATOM   492  H HA   B ILE   A 1 18  ? 12.438 -9.015  9.071   0.30 14.19 ?  18  ILE   A HA   1 
ATOM   493  H HB   A ILE   A 1 18  ? 11.666 -10.833 6.874   0.70 15.88 ?  18  ILE   A HB   1 
ATOM   494  H HB   B ILE   A 1 18  ? 11.581 -10.462 7.397   0.30 13.76 ?  18  ILE   A HB   1 
ATOM   495  H HG12 A ILE   A 1 18  ? 10.301 -8.382  6.667   0.70 16.40 ?  18  ILE   A HG12 1 
ATOM   496  H HG12 B ILE   A 1 18  ? 10.246 -7.974  7.404   0.30 14.47 ?  18  ILE   A HG12 1 
ATOM   497  H HG13 A ILE   A 1 18  ? 11.861 -8.521  6.400   0.70 16.40 ?  18  ILE   A HG13 1 
ATOM   498  H HG13 B ILE   A 1 18  ? 11.771 -8.133  6.991   0.30 14.47 ?  18  ILE   A HG13 1 
ATOM   499  H HG21 A ILE   A 1 18  ? 9.442  -11.263 6.549   0.70 16.30 ?  18  ILE   A HG21 1 
ATOM   500  H HG21 B ILE   A 1 18  ? 9.346  -10.847 7.165   0.30 13.80 ?  18  ILE   A HG21 1 
ATOM   501  H HG22 A ILE   A 1 18  ? 9.785  -11.629 8.056   0.70 16.30 ?  18  ILE   A HG22 1 
ATOM   502  H HG22 B ILE   A 1 18  ? 9.697  -11.207 8.671   0.30 13.80 ?  18  ILE   A HG22 1 
ATOM   503  H HG23 A ILE   A 1 18  ? 9.037  -10.269 7.721   0.70 16.30 ?  18  ILE   A HG23 1 
ATOM   504  H HG23 B ILE   A 1 18  ? 8.994  -9.824  8.329   0.30 13.80 ?  18  ILE   A HG23 1 
ATOM   505  H HD11 A ILE   A 1 18  ? 10.757 -8.502  4.393   0.70 18.24 ?  18  ILE   A HD11 1 
ATOM   506  H HD11 B ILE   A 1 18  ? 10.534 -8.009  5.078   0.30 15.19 ?  18  ILE   A HD11 1 
ATOM   507  H HD12 A ILE   A 1 18  ? 11.406 -9.936  4.607   0.70 18.24 ?  18  ILE   A HD12 1 
ATOM   508  H HD12 B ILE   A 1 18  ? 11.093 -9.491  5.196   0.30 15.19 ?  18  ILE   A HD12 1 
ATOM   509  H HD13 A ILE   A 1 18  ? 9.851  -9.723  4.854   0.70 18.24 ?  18  ILE   A HD13 1 
ATOM   510  H HD13 B ILE   A 1 18  ? 9.582  -9.180  5.574   0.30 15.19 ?  18  ILE   A HD13 1 
ATOM   511  N N    A LYS   A 1 19  ? 10.738 -7.654  9.311   0.70 13.77 ?  19  LYS   A N    1 
ATOM   512  N N    B LYS   A 1 19  ? 10.907 -7.354  10.008  0.30 12.59 ?  19  LYS   A N    1 
ATOM   513  C CA   A LYS   A 1 19  ? 9.929  -6.705  10.069  0.70 14.77 ?  19  LYS   A CA   1 
ATOM   514  C CA   B LYS   A 1 19  ? 10.130 -6.381  10.764  0.30 13.52 ?  19  LYS   A CA   1 
ATOM   515  C C    A LYS   A 1 19  ? 9.729  -5.432  9.254   0.70 15.15 ?  19  LYS   A C    1 
ATOM   516  C C    B LYS   A 1 19  ? 9.891  -5.157  9.893   0.30 14.15 ?  19  LYS   A C    1 
ATOM   517  O O    A LYS   A 1 19  ? 10.626 -5.015  8.516   0.70 15.04 ?  19  LYS   A O    1 
ATOM   518  O O    B LYS   A 1 19  ? 10.773 -4.747  9.135   0.30 14.20 ?  19  LYS   A O    1 
ATOM   519  C CB   A LYS   A 1 19  ? 10.641 -6.367  11.385  0.70 15.91 ?  19  LYS   A CB   1 
ATOM   520  C CB   B LYS   A 1 19  ? 10.879 -5.964  12.041  0.30 14.27 ?  19  LYS   A CB   1 
ATOM   521  C CG   A LYS   A 1 19  ? 9.907  -5.433  12.331  0.70 17.21 ?  19  LYS   A CG   1 
ATOM   522  C CG   B LYS   A 1 19  ? 10.111 -5.034  12.968  0.30 15.18 ?  19  LYS   A CG   1 
ATOM   523  C CD   A LYS   A 1 19  ? 10.792 -5.151  13.542  0.70 18.26 ?  19  LYS   A CD   1 
ATOM   524  C CD   B LYS   A 1 19  ? 10.945 -4.686  14.194  0.30 15.90 ?  19  LYS   A CD   1 
ATOM   525  C CE   A LYS   A 1 19  ? 10.132 -4.233  14.551  0.70 18.73 ?  19  LYS   A CE   1 
ATOM   526  C CE   B LYS   A 1 19  ? 10.205 -3.740  15.127  0.30 16.60 ?  19  LYS   A CE   1 
ATOM   527  N NZ   A LYS   A 1 19  ? 11.032 -3.985  15.716  0.70 18.99 ?  19  LYS   A NZ   1 
ATOM   528  N NZ   B LYS   A 1 19  ? 11.004 -3.407  16.337  0.30 17.19 ?  19  LYS   A NZ   1 
ATOM   529  H H    A LYS   A 1 19  ? 11.264 -7.292  8.745   0.70 16.53 ?  19  LYS   A H    1 
ATOM   530  H H    B LYS   A 1 19  ? 11.514 -6.990  9.511   0.30 15.11 ?  19  LYS   A H    1 
ATOM   531  H HA   A LYS   A 1 19  ? 9.063  -7.110  10.273  0.70 17.72 ?  19  LYS   A HA   1 
ATOM   532  H HA   B LYS   A 1 19  ? 9.278  -6.766  11.018  0.30 16.22 ?  19  LYS   A HA   1 
ATOM   533  H HB2  A LYS   A 1 19  ? 10.799 -7.196  11.867  0.70 19.09 ?  19  LYS   A HB2  1 
ATOM   534  H HB2  B LYS   A 1 19  ? 11.099 -6.760  12.551  0.30 17.12 ?  19  LYS   A HB2  1 
ATOM   535  H HB3  A LYS   A 1 19  ? 11.488 -5.955  11.167  0.70 19.09 ?  19  LYS   A HB3  1 
ATOM   536  H HB3  B LYS   A 1 19  ? 11.697 -5.507  11.787  0.30 17.12 ?  19  LYS   A HB3  1 
ATOM   537  H HG2  A LYS   A 1 19  ? 9.717  -4.595  11.882  0.70 20.65 ?  19  LYS   A HG2  1 
ATOM   538  H HG2  B LYS   A 1 19  ? 9.901  -4.210  12.502  0.30 18.21 ?  19  LYS   A HG2  1 
ATOM   539  H HG3  A LYS   A 1 19  ? 9.086  -5.853  12.636  0.70 20.65 ?  19  LYS   A HG3  1 
ATOM   540  H HG3  B LYS   A 1 19  ? 9.299  -5.471  13.268  0.30 18.21 ?  19  LYS   A HG3  1 
ATOM   541  H HD2  A LYS   A 1 19  ? 10.994 -5.989  13.987  0.70 21.91 ?  19  LYS   A HD2  1 
ATOM   542  H HD2  B LYS   A 1 19  ? 11.151 -5.497  14.687  0.30 19.08 ?  19  LYS   A HD2  1 
ATOM   543  H HD3  A LYS   A 1 19  ? 11.611 -4.728  13.242  0.70 21.91 ?  19  LYS   A HD3  1 
ATOM   544  H HD3  B LYS   A 1 19  ? 11.762 -4.255  13.907  0.30 19.08 ?  19  LYS   A HD3  1 
ATOM   545  H HE2  A LYS   A 1 19  ? 9.936  -3.379  14.132  0.70 22.48 ?  19  LYS   A HE2  1 
ATOM   546  H HE2  B LYS   A 1 19  ? 10.012 -2.915  14.656  0.30 19.92 ?  19  LYS   A HE2  1 
ATOM   547  H HE3  A LYS   A 1 19  ? 9.316  -4.642  14.878  0.70 22.48 ?  19  LYS   A HE3  1 
ATOM   548  H HE3  B LYS   A 1 19  ? 9.380  -4.161  15.417  0.30 19.92 ?  19  LYS   A HE3  1 
ATOM   549  H HZ1  A LYS   A 1 19  ? 10.626 -3.459  16.307  0.70 22.79 ?  19  LYS   A HZ1  1 
ATOM   550  H HZ1  B LYS   A 1 19  ? 10.545 -2.853  16.862  0.30 20.63 ?  19  LYS   A HZ1  1 
ATOM   551  H HZ2  A LYS   A 1 19  ? 11.239 -4.756  16.108  0.70 22.79 ?  19  LYS   A HZ2  1 
ATOM   552  H HZ2  B LYS   A 1 19  ? 11.191 -4.148  16.793  0.30 20.63 ?  19  LYS   A HZ2  1 
ATOM   553  H HZ3  A LYS   A 1 19  ? 11.780 -3.590  15.442  0.70 22.79 ?  19  LYS   A HZ3  1 
ATOM   554  H HZ3  B LYS   A 1 19  ? 11.766 -3.013  16.100  0.30 20.63 ?  19  LYS   A HZ3  1 
ATOM   555  N N    A ASN   A 1 20  ? 8.546  -4.825  9.383   0.70 16.63 ?  20  ASN   A N    1 
ATOM   556  N N    B ASN   A 1 20  ? 8.694  -4.582  9.997   0.30 15.26 ?  20  ASN   A N    1 
ATOM   557  C CA   A ASN   A 1 20  ? 8.306  -3.489  8.843   0.70 18.30 ?  20  ASN   A CA   1 
ATOM   558  C CA   B ASN   A 1 20  ? 8.333  -3.369  9.261   0.30 16.72 ?  20  ASN   A CA   1 
ATOM   559  C C    A ASN   A 1 20  ? 8.926  -2.485  9.807   0.70 18.70 ?  20  ASN   A C    1 
ATOM   560  C C    B ASN   A 1 20  ? 8.867  -2.178  10.047  0.30 17.32 ?  20  ASN   A C    1 
ATOM   561  O O    A ASN   A 1 20  ? 8.402  -2.258  10.903  0.70 19.32 ?  20  ASN   A O    1 
ATOM   562  O O    B ASN   A 1 20  ? 8.179  -1.610  10.897  0.30 17.92 ?  20  ASN   A O    1 
ATOM   563  C CB   A ASN   A 1 20  ? 6.807  -3.244  8.669   0.70 19.60 ?  20  ASN   A CB   1 
ATOM   564  C CB   B ASN   A 1 20  ? 6.815  -3.290  9.097   0.30 17.42 ?  20  ASN   A CB   1 
ATOM   565  C CG   A ASN   A 1 20  ? 6.471  -1.783  8.371   0.70 20.82 ?  20  ASN   A CG   1 
ATOM   566  C CG   B ASN   A 1 20  ? 6.361  -2.123  8.216   0.30 17.98 ?  20  ASN   A CG   1 
ATOM   567  O OD1  A ASN   A 1 20  ? 5.553  -1.209  8.965   0.70 22.55 ?  20  ASN   A OD1  1 
ATOM   568  O OD1  B ASN   A 1 20  ? 5.190  -1.724  8.254   0.30 17.91 ?  20  ASN   A OD1  1 
ATOM   569  N ND2  A ASN   A 1 20  ? 7.213  -1.179  7.451   0.70 20.94 ?  20  ASN   A ND2  1 
ATOM   570  N ND2  B ASN   A 1 20  ? 7.278  -1.574  7.424   0.30 18.70 ?  20  ASN   A ND2  1 
ATOM   571  H H    A ASN   A 1 20  ? 7.866  -5.183  9.779   0.70 19.96 ?  20  ASN   A H    1 
ATOM   572  H H    B ASN   A 1 20  ? 8.066  -4.889  10.486  0.30 18.31 ?  20  ASN   A H    1 
ATOM   573  H HA   A ASN   A 1 20  ? 8.740  -3.414  7.981   0.70 21.96 ?  20  ASN   A HA   1 
ATOM   574  H HA   B ASN   A 1 20  ? 8.755  -3.394  8.386   0.30 20.06 ?  20  ASN   A HA   1 
ATOM   575  H HB2  A ASN   A 1 20  ? 6.486  -3.786  7.931   0.70 23.52 ?  20  ASN   A HB2  1 
ATOM   576  H HB2  B ASN   A 1 20  ? 6.492  -4.113  8.703   0.30 20.90 ?  20  ASN   A HB2  1 
ATOM   577  H HB3  A ASN   A 1 20  ? 6.353  -3.502  9.488   0.70 23.52 ?  20  ASN   A HB3  1 
ATOM   578  H HB3  B ASN   A 1 20  ? 6.414  -3.170  9.971   0.30 20.90 ?  20  ASN   A HB3  1 
ATOM   579  H HD21 A ASN   A 1 20  ? 7.065  -0.359  7.252   0.70 25.13 ?  20  ASN   A HD21 1 
ATOM   580  H HD21 B ASN   A 1 20  ? 7.061  -0.919  6.915   0.30 22.44 ?  20  ASN   A HD21 1 
ATOM   581  H HD22 A ASN   A 1 20  ? 7.848  -1.611  7.057   0.70 25.13 ?  20  ASN   A HD22 1 
ATOM   582  H HD22 B ASN   A 1 20  ? 8.085  -1.868  7.412   0.30 22.44 ?  20  ASN   A HD22 1 
ATOM   583  N N    A ALA   A 1 21  ? 10.058 -1.901  9.421   0.70 19.08 ?  21  ALA   A N    1 
ATOM   584  N N    B ALA   A 1 21  ? 10.111 -1.790  9.764   0.30 17.51 ?  21  ALA   A N    1 
ATOM   585  C CA   A ALA   A 1 21  ? 10.756 -0.995  10.323  0.70 19.08 ?  21  ALA   A CA   1 
ATOM   586  C CA   B ALA   A 1 21  ? 10.742 -0.706  10.503  0.30 17.48 ?  21  ALA   A CA   1 
ATOM   587  C C    A ALA   A 1 21  ? 11.728 -0.130  9.540   0.70 18.67 ?  21  ALA   A C    1 
ATOM   588  C C    B ALA   A 1 21  ? 11.899 -0.135  9.696   0.30 16.89 ?  21  ALA   A C    1 
ATOM   589  O O    A ALA   A 1 21  ? 12.173 -0.494  8.448   0.70 18.68 ?  21  ALA   A O    1 
ATOM   590  O O    B ALA   A 1 21  ? 12.465 -0.802  8.826   0.30 16.88 ?  21  ALA   A O    1 
ATOM   591  C CB   A ALA   A 1 21  ? 11.501 -1.758  11.421  0.70 19.76 ?  21  ALA   A CB   1 
ATOM   592  C CB   B ALA   A 1 21  ? 11.233 -1.178  11.876  0.30 17.83 ?  21  ALA   A CB   1 
ATOM   593  H H    A ALA   A 1 21  ? 10.433 -2.011  8.654   0.70 22.90 ?  21  ALA   A H    1 
ATOM   594  H H    B ALA   A 1 21  ? 10.609 -2.137  9.153   0.30 21.01 ?  21  ALA   A H    1 
ATOM   595  H HA   A ALA   A 1 21  ? 10.103 -0.414  10.747  0.70 22.89 ?  21  ALA   A HA   1 
ATOM   596  H HA   B ALA   A 1 21  ? 10.097 0.003   10.644  0.30 20.97 ?  21  ALA   A HA   1 
ATOM   597  H HB1  A ALA   A 1 21  ? 11.939 -1.119  12.002  0.70 23.71 ?  21  ALA   A HB1  1 
ATOM   598  H HB1  B ALA   A 1 21  ? 11.646 -0.431  12.338  0.30 21.40 ?  21  ALA   A HB1  1 
ATOM   599  H HB2  A ALA   A 1 21  ? 10.860 -2.283  11.929  0.70 23.71 ?  21  ALA   A HB2  1 
ATOM   600  H HB2  B ALA   A 1 21  ? 10.475 -1.505  12.386  0.30 21.40 ?  21  ALA   A HB2  1 
ATOM   601  H HB3  A ALA   A 1 21  ? 12.155 -2.342  11.011  0.70 23.71 ?  21  ALA   A HB3  1 
ATOM   602  H HB3  B ALA   A 1 21  ? 11.880 -1.890  11.752  0.30 21.40 ?  21  ALA   A HB3  1 
ATOM   603  N N    A ASP   A 1 22  ? 12.035 1.031   10.124  0.70 18.81 ?  22  ASP   A N    1 
ATOM   604  N N    B ASP   A 1 22  ? 12.226 1.123   9.992   0.30 16.58 ?  22  ASP   A N    1 
ATOM   605  C CA   A ASP   A 1 22  ? 13.090 1.915   9.643   0.70 18.65 ?  22  ASP   A CA   1 
ATOM   606  C CA   B ASP   A 1 22  ? 13.424 1.755   9.456   0.30 16.42 ?  22  ASP   A CA   1 
ATOM   607  C C    A ASP   A 1 22  ? 14.415 1.427   10.219  0.70 17.29 ?  22  ASP   A C    1 
ATOM   608  C C    B ASP   A 1 22  ? 14.654 1.088   10.063  0.30 15.17 ?  22  ASP   A C    1 
ATOM   609  O O    A ASP   A 1 22  ? 14.606 1.434   11.439  0.70 17.59 ?  22  ASP   A O    1 
ATOM   610  O O    B ASP   A 1 22  ? 14.756 0.948   11.286  0.30 15.01 ?  22  ASP   A O    1 
ATOM   611  C CB   A ASP   A 1 22  ? 12.793 3.343   10.103  0.70 20.35 ?  22  ASP   A CB   1 
ATOM   612  C CB   B ASP   A 1 22  ? 13.401 3.243   9.822   0.30 17.52 ?  22  ASP   A CB   1 
ATOM   613  C CG   A ASP   A 1 22  ? 13.846 4.357   9.643   0.70 21.84 ?  22  ASP   A CG   1 
ATOM   614  C CG   B ASP   A 1 22  ? 14.456 4.060   9.102   0.30 18.26 ?  22  ASP   A CG   1 
ATOM   615  O OD1  A ASP   A 1 22  ? 14.918 3.966   9.136   0.70 21.81 ?  22  ASP   A OD1  1 
ATOM   616  O OD1  B ASP   A 1 22  ? 15.424 3.475   8.577   0.30 18.16 ?  22  ASP   A OD1  1 
ATOM   617  O OD2  A ASP   A 1 22  ? 13.594 5.572   9.795   0.70 23.36 -1 22  ASP   A OD2  1 
ATOM   618  O OD2  B ASP   A 1 22  ? 14.321 5.303   9.075   0.30 18.66 -1 22  ASP   A OD2  1 
ATOM   619  H H    A ASP   A 1 22  ? 11.626 1.334   10.822  0.70 22.57 ?  22  ASP   A H    1 
ATOM   620  H H    B ASP   A 1 22  ? 11.758 1.638   10.501  0.30 19.90 ?  22  ASP   A H    1 
ATOM   621  H HA   A ASP   A 1 22  ? 13.133 1.891   8.676   0.70 22.38 ?  22  ASP   A HA   1 
ATOM   622  H HA   B ASP   A 1 22  ? 13.450 1.660   8.490   0.30 19.70 ?  22  ASP   A HA   1 
ATOM   623  H HB2  A ASP   A 1 22  ? 11.929 3.614   9.747   0.70 24.42 ?  22  ASP   A HB2  1 
ATOM   624  H HB2  B ASP   A 1 22  ? 12.534 3.609   9.596   0.30 21.02 ?  22  ASP   A HB2  1 
ATOM   625  H HB3  A ASP   A 1 22  ? 12.762 3.360   11.074  0.70 24.42 ?  22  ASP   A HB3  1 
ATOM   626  H HB3  B ASP   A 1 22  ? 13.570 3.332   10.767  0.30 21.02 ?  22  ASP   A HB3  1 
ATOM   627  N N    A ILE   A 1 23  ? 15.322 0.993   9.340   0.70 16.51 ?  23  ILE   A N    1 
ATOM   628  N N    B ILE   A 1 23  ? 15.588 0.664   9.206   0.30 14.54 ?  23  ILE   A N    1 
ATOM   629  C CA   A ILE   A 1 23  ? 16.580 0.397   9.782   0.70 15.45 ?  23  ILE   A CA   1 
ATOM   630  C CA   B ILE   A 1 23  ? 16.814 0.030   9.680   0.30 13.92 ?  23  ILE   A CA   1 
ATOM   631  C C    A ILE   A 1 23  ? 17.369 1.357   10.658  0.70 15.58 ?  23  ILE   A C    1 
ATOM   632  C C    B ILE   A 1 23  ? 17.574 0.968   10.604  0.30 14.43 ?  23  ILE   A C    1 
ATOM   633  O O    A ILE   A 1 23  ? 18.091 0.927   11.565  0.70 16.00 ?  23  ILE   A O    1 
ATOM   634  O O    B ILE   A 1 23  ? 18.235 0.524   11.551  0.30 14.41 ?  23  ILE   A O    1 
ATOM   635  C CB   A ILE   A 1 23  ? 17.394 -0.102  8.567   0.70 14.94 ?  23  ILE   A CB   1 
ATOM   636  C CB   B ILE   A 1 23  ? 17.680 -0.460  8.495   0.30 12.93 ?  23  ILE   A CB   1 
ATOM   637  C CG1  A ILE   A 1 23  ? 18.555 -0.987  9.026   0.70 14.99 ?  23  ILE   A CG1  1 
ATOM   638  C CG1  B ILE   A 1 23  ? 18.782 -1.401  8.998   0.30 12.71 ?  23  ILE   A CG1  1 
ATOM   639  C CG2  A ILE   A 1 23  ? 17.873 1.070   7.714   0.70 15.09 ?  23  ILE   A CG2  1 
ATOM   640  C CG2  B ILE   A 1 23  ? 18.282 0.716   7.723   0.30 12.59 ?  23  ILE   A CG2  1 
ATOM   641  C CD1  A ILE   A 1 23  ? 19.264 -1.699  7.891   0.70 14.97 ?  23  ILE   A CD1  1 
ATOM   642  C CD1  B ILE   A 1 23  ? 19.628 -2.016  7.895   0.30 12.64 ?  23  ILE   A CD1  1 
ATOM   643  H H    A ILE   A 1 23  ? 15.223 1.027   8.495   0.70 19.81 ?  23  ILE   A H    1 
ATOM   644  H H    B ILE   A 1 23  ? 15.545 0.729   8.364   0.30 17.45 ?  23  ILE   A H    1 
ATOM   645  H HA   A ILE   A 1 23  ? 16.379 -0.376  10.330  0.70 18.54 ?  23  ILE   A HA   1 
ATOM   646  H HA   B ILE   A 1 23  ? 16.566 -0.750  10.192  0.30 16.71 ?  23  ILE   A HA   1 
ATOM   647  H HB   A ILE   A 1 23  ? 16.804 -0.646  8.024   0.70 17.93 ?  23  ILE   A HB   1 
ATOM   648  H HB   B ILE   A 1 23  ? 17.114 -0.963  7.889   0.30 15.51 ?  23  ILE   A HB   1 
ATOM   649  H HG12 A ILE   A 1 23  ? 19.211 -0.436  9.482   0.70 17.99 ?  23  ILE   A HG12 1 
ATOM   650  H HG12 B ILE   A 1 23  ? 19.377 -0.905  9.581   0.30 15.25 ?  23  ILE   A HG12 1 
ATOM   651  H HG13 A ILE   A 1 23  ? 18.216 -1.664  9.633   0.70 17.99 ?  23  ILE   A HG13 1 
ATOM   652  H HG13 B ILE   A 1 23  ? 18.370 -2.128  9.491   0.30 15.25 ?  23  ILE   A HG13 1 
ATOM   653  H HG21 A ILE   A 1 23  ? 18.232 0.727   6.882   0.70 18.11 ?  23  ILE   A HG21 1 
ATOM   654  H HG21 B ILE   A 1 23  ? 18.651 0.387   6.885   0.30 15.11 ?  23  ILE   A HG21 1 
ATOM   655  H HG22 A ILE   A 1 23  ? 17.118 1.654   7.531   0.70 18.11 ?  23  ILE   A HG22 1 
ATOM   656  H HG22 B ILE   A 1 23  ? 17.584 1.362   7.543   0.30 15.11 ?  23  ILE   A HG22 1 
ATOM   657  H HG23 A ILE   A 1 23  ? 18.557 1.557   8.197   0.70 18.11 ?  23  ILE   A HG23 1 
ATOM   658  H HG23 B ILE   A 1 23  ? 18.983 1.120   8.255   0.30 15.11 ?  23  ILE   A HG23 1 
ATOM   659  H HD11 A ILE   A 1 23  ? 19.943 -2.284  8.261   0.70 17.97 ?  23  ILE   A HD11 1 
ATOM   660  H HD11 B ILE   A 1 23  ? 20.230 -2.671  8.286   0.30 15.17 ?  23  ILE   A HD11 1 
ATOM   661  H HD12 A ILE   A 1 23  ? 18.614 -2.220  7.394   0.70 17.97 ?  23  ILE   A HD12 1 
ATOM   662  H HD12 B ILE   A 1 23  ? 19.044 -2.449  7.253   0.30 15.17 ?  23  ILE   A HD12 1 
ATOM   663  H HD13 A ILE   A 1 23  ? 19.673 -1.039  7.312   0.70 17.97 ?  23  ILE   A HD13 1 
ATOM   664  H HD13 B ILE   A 1 23  ? 20.139 -1.318  7.459   0.30 15.17 ?  23  ILE   A HD13 1 
ATOM   665  N N    A VAL   A 1 24  ? 17.233 2.665   10.425  0.70 16.18 ?  24  VAL   A N    1 
ATOM   666  N N    B VAL   A 1 24  ? 17.478 2.275   10.359  0.30 15.58 ?  24  VAL   A N    1 
ATOM   667  C CA   A VAL   A 1 24  ? 17.922 3.647   11.261  0.70 17.44 ?  24  VAL   A CA   1 
ATOM   668  C CA   B VAL   A 1 24  ? 18.111 3.253   11.238  0.30 16.68 ?  24  VAL   A CA   1 
ATOM   669  C C    A VAL   A 1 24  ? 17.430 3.555   12.699  0.70 18.31 ?  24  VAL   A C    1 
ATOM   670  C C    B VAL   A 1 24  ? 17.488 3.198   12.627  0.30 17.49 ?  24  VAL   A C    1 
ATOM   671  O O    A VAL   A 1 24  ? 18.224 3.493   13.646  0.70 18.71 ?  24  VAL   A O    1 
ATOM   672  O O    B VAL   A 1 24  ? 18.193 3.240   13.643  0.30 17.72 ?  24  VAL   A O    1 
ATOM   673  C CB   A VAL   A 1 24  ? 17.737 5.063   10.687  0.70 18.11 ?  24  VAL   A CB   1 
ATOM   674  C CB   B VAL   A 1 24  ? 18.010 4.657   10.616  0.30 17.26 ?  24  VAL   A CB   1 
ATOM   675  C CG1  A VAL   A 1 24  ? 18.265 6.114   11.662  0.70 18.67 ?  24  VAL   A CG1  1 
ATOM   676  C CG1  B VAL   A 1 24  ? 18.660 5.687   11.519  0.30 17.74 ?  24  VAL   A CG1  1 
ATOM   677  C CG2  A VAL   A 1 24  ? 18.424 5.181   9.336   0.70 18.64 ?  24  VAL   A CG2  1 
ATOM   678  C CG2  B VAL   A 1 24  ? 18.647 4.663   9.232   0.30 17.10 ?  24  VAL   A CG2  1 
ATOM   679  H H    A VAL   A 1 24  ? 16.755 3.007   9.800   0.70 19.42 ?  24  VAL   A H    1 
ATOM   680  H H    B VAL   A 1 24  ? 17.052 2.617   9.700   0.30 18.69 ?  24  VAL   A H    1 
ATOM   681  H HA   A VAL   A 1 24  ? 18.872 3.454   11.263  0.70 20.92 ?  24  VAL   A HA   1 
ATOM   682  H HA   B VAL   A 1 24  ? 19.051 3.033   11.326  0.30 20.02 ?  24  VAL   A HA   1 
ATOM   683  H HB   A VAL   A 1 24  ? 16.791 5.231   10.554  0.70 21.73 ?  24  VAL   A HB   1 
ATOM   684  H HB   B VAL   A 1 24  ? 17.074 4.891   10.515  0.30 20.71 ?  24  VAL   A HB   1 
ATOM   685  H HG11 A VAL   A 1 24  ? 18.400 6.947   11.183  0.70 22.40 ?  24  VAL   A HG11 1 
ATOM   686  H HG11 B VAL   A 1 24  ? 18.737 6.522   11.034  0.30 21.29 ?  24  VAL   A HG11 1 
ATOM   687  H HG12 A VAL   A 1 24  ? 17.618 6.243   12.371  0.70 22.40 ?  24  VAL   A HG12 1 
ATOM   688  H HG12 B VAL   A 1 24  ? 18.106 5.811   12.305  0.30 21.29 ?  24  VAL   A HG12 1 
ATOM   689  H HG13 A VAL   A 1 24  ? 19.109 5.806   12.030  0.70 22.40 ?  24  VAL   A HG13 1 
ATOM   690  H HG13 B VAL   A 1 24  ? 19.538 5.369   11.776  0.30 21.29 ?  24  VAL   A HG13 1 
ATOM   691  H HG21 A VAL   A 1 24  ? 18.195 6.035   8.937   0.70 22.37 ?  24  VAL   A HG21 1 
ATOM   692  H HG21 B VAL   A 1 24  ? 18.675 5.574   8.902   0.30 20.52 ?  24  VAL   A HG21 1 
ATOM   693  H HG22 A VAL   A 1 24  ? 19.385 5.126   9.465   0.70 22.37 ?  24  VAL   A HG22 1 
ATOM   694  H HG22 B VAL   A 1 24  ? 19.546 4.307   9.298   0.30 20.52 ?  24  VAL   A HG22 1 
ATOM   695  H HG23 A VAL   A 1 24  ? 18.125 4.458   8.763   0.70 22.37 ?  24  VAL   A HG23 1 
ATOM   696  H HG23 B VAL   A 1 24  ? 18.117 4.111   8.636   0.30 20.52 ?  24  VAL   A HG23 1 
ATOM   697  N N    A GLU   A 1 25  ? 16.108 3.551   12.882  0.70 19.31 ?  25  GLU   A N    1 
ATOM   698  N N    B GLU   A 1 25  ? 16.159 3.096   12.694  0.30 18.12 ?  25  GLU   A N    1 
ATOM   699  C CA   A GLU   A 1 25  ? 15.551 3.480   14.228  0.70 20.61 ?  25  GLU   A CA   1 
ATOM   700  C CA   B GLU   A 1 25  ? 15.490 2.996   13.987  0.30 18.98 ?  25  GLU   A CA   1 
ATOM   701  C C    A GLU   A 1 25  ? 15.797 2.119   14.865  0.70 19.68 ?  25  GLU   A C    1 
ATOM   702  C C    B GLU   A 1 25  ? 15.772 1.653   14.650  0.30 18.62 ?  25  GLU   A C    1 
ATOM   703  O O    A GLU   A 1 25  ? 16.033 2.039   16.076  0.70 20.29 ?  25  GLU   A O    1 
ATOM   704  O O    B GLU   A 1 25  ? 16.008 1.592   15.862  0.30 18.70 ?  25  GLU   A O    1 
ATOM   705  C CB   A GLU   A 1 25  ? 14.059 3.818   14.195  0.70 22.87 ?  25  GLU   A CB   1 
ATOM   706  C CB   B GLU   A 1 25  ? 13.988 3.236   13.824  0.30 20.07 ?  25  GLU   A CB   1 
ATOM   707  C CG   A GLU   A 1 25  ? 13.782 5.258   13.783  0.70 25.29 ?  25  GLU   A CG   1 
ATOM   708  C CG   B GLU   A 1 25  ? 13.647 4.629   13.314  0.30 21.44 ?  25  GLU   A CG   1 
ATOM   709  C CD   A GLU   A 1 25  ? 14.536 6.265   14.634  0.70 27.34 ?  25  GLU   A CD   1 
ATOM   710  C CD   B GLU   A 1 25  ? 14.088 5.720   14.267  0.30 22.55 ?  25  GLU   A CD   1 
ATOM   711  O OE1  A GLU   A 1 25  ? 14.552 6.110   15.873  0.70 27.92 ?  25  GLU   A OE1  1 
ATOM   712  O OE1  B GLU   A 1 25  ? 14.094 5.471   15.492  0.30 22.94 ?  25  GLU   A OE1  1 
ATOM   713  O OE2  A GLU   A 1 25  ? 15.131 7.201   14.059  0.70 28.42 -1 25  GLU   A OE2  1 
ATOM   714  O OE2  B GLU   A 1 25  ? 14.431 6.824   13.793  0.30 23.19 -1 25  GLU   A OE2  1 
ATOM   715  H H    A GLU   A 1 25  ? 15.523 3.594   12.253  0.70 23.17 ?  25  GLU   A H    1 
ATOM   716  H H    B GLU   A 1 25  ? 15.633 3.079   12.017  0.30 21.74 ?  25  GLU   A H    1 
ATOM   717  H HA   A GLU   A 1 25  ? 15.991 4.138   14.784  0.70 24.73 ?  25  GLU   A HA   1 
ATOM   718  H HA   B GLU   A 1 25  ? 15.839 3.683   14.571  0.30 22.77 ?  25  GLU   A HA   1 
ATOM   719  H HB2  A GLU   A 1 25  ? 13.613 3.238   13.555  0.70 27.44 ?  25  GLU   A HB2  1 
ATOM   720  H HB2  B GLU   A 1 25  ? 13.632 2.595   13.192  0.30 24.09 ?  25  GLU   A HB2  1 
ATOM   721  H HB3  A GLU   A 1 25  ? 13.680 3.686   15.078  0.70 27.44 ?  25  GLU   A HB3  1 
ATOM   722  H HB3  B GLU   A 1 25  ? 13.558 3.125   14.687  0.30 24.09 ?  25  GLU   A HB3  1 
ATOM   723  H HG2  A GLU   A 1 25  ? 14.063 5.382   12.864  0.70 30.35 ?  25  GLU   A HG2  1 
ATOM   724  H HG2  B GLU   A 1 25  ? 14.088 4.772   12.461  0.30 25.73 ?  25  GLU   A HG2  1 
ATOM   725  H HG3  A GLU   A 1 25  ? 12.830 5.434   13.868  0.70 30.35 ?  25  GLU   A HG3  1 
ATOM   726  H HG3  B GLU   A 1 25  ? 12.687 4.703   13.207  0.30 25.73 ?  25  GLU   A HG3  1 
ATOM   727  N N    A GLU   A 1 26  ? 15.773 1.047   14.070  0.70 19.26 ?  26  GLU   A N    1 
ATOM   728  N N    B GLU   A 1 26  ? 15.768 0.567   13.873  0.30 18.46 ?  26  GLU   A N    1 
ATOM   729  C CA   A GLU   A 1 26  ? 16.075 -0.279  14.603  0.70 19.30 ?  26  GLU   A CA   1 
ATOM   730  C CA   B GLU   A 1 26  ? 16.170 -0.720  14.428  0.30 18.44 ?  26  GLU   A CA   1 
ATOM   731  C C    A GLU   A 1 26  ? 17.508 -0.346  15.119  0.70 18.21 ?  26  GLU   A C    1 
ATOM   732  C C    B GLU   A 1 26  ? 17.598 -0.671  14.946  0.30 18.11 ?  26  GLU   A C    1 
ATOM   733  O O    A GLU   A 1 26  ? 17.761 -0.838  16.225  0.70 17.59 ?  26  GLU   A O    1 
ATOM   734  O O    B GLU   A 1 26  ? 17.922 -1.341  15.933  0.30 18.23 ?  26  GLU   A O    1 
ATOM   735  C CB   A GLU   A 1 26  ? 15.861 -1.335  13.517  0.70 21.04 ?  26  GLU   A CB   1 
ATOM   736  C CB   B GLU   A 1 26  ? 16.024 -1.827  13.379  0.30 18.92 ?  26  GLU   A CB   1 
ATOM   737  C CG   A GLU   A 1 26  ? 14.447 -1.853  13.401  0.70 23.23 ?  26  GLU   A CG   1 
ATOM   738  C CG   B GLU   A 1 26  ? 14.591 -2.181  13.044  0.30 18.87 ?  26  GLU   A CG   1 
ATOM   739  C CD   A GLU   A 1 26  ? 14.014 -2.610  14.641  0.70 24.80 ?  26  GLU   A CD   1 
ATOM   740  C CD   B GLU   A 1 26  ? 13.877 -2.837  14.205  0.30 18.48 ?  26  GLU   A CD   1 
ATOM   741  O OE1  A GLU   A 1 26  ? 14.565 -3.700  14.916  0.70 25.43 ?  26  GLU   A OE1  1 
ATOM   742  O OE1  B GLU   A 1 26  ? 14.285 -3.943  14.640  0.30 18.98 ?  26  GLU   A OE1  1 
ATOM   743  O OE2  A GLU   A 1 26  ? 13.137 -2.092  15.354  0.70 25.84 -1 26  GLU   A OE2  1 
ATOM   744  O OE2  B GLU   A 1 26  ? 12.892 -2.242  14.680  0.30 17.77 -1 26  GLU   A OE2  1 
ATOM   745  H H    A GLU   A 1 26  ? 15.601 1.066   13.227  0.70 23.11 ?  26  GLU   A H    1 
ATOM   746  H H    B GLU   A 1 26  ? 15.551 0.548   13.043  0.30 22.15 ?  26  GLU   A H    1 
ATOM   747  H HA   A GLU   A 1 26  ? 15.477 -0.467  15.339  0.70 23.16 ?  26  GLU   A HA   1 
ATOM   748  H HA   B GLU   A 1 26  ? 15.596 -0.940  15.176  0.30 22.13 ?  26  GLU   A HA   1 
ATOM   749  H HB2  A GLU   A 1 26  ? 16.107 -0.953  12.661  0.70 25.25 ?  26  GLU   A HB2  1 
ATOM   750  H HB2  B GLU   A 1 26  ? 16.452 -1.544  12.559  0.30 22.70 ?  26  GLU   A HB2  1 
ATOM   751  H HB3  A GLU   A 1 26  ? 16.435 -2.093  13.711  0.70 25.25 ?  26  GLU   A HB3  1 
ATOM   752  H HB3  B GLU   A 1 26  ? 16.450 -2.635  13.711  0.30 22.70 ?  26  GLU   A HB3  1 
ATOM   753  H HG2  A GLU   A 1 26  ? 13.844 -1.101  13.283  0.70 27.88 ?  26  GLU   A HG2  1 
ATOM   754  H HG2  B GLU   A 1 26  ? 14.107 -1.370  12.805  0.30 22.64 ?  26  GLU   A HG2  1 
ATOM   755  H HG3  A GLU   A 1 26  ? 14.389 -2.443  12.629  0.70 27.88 ?  26  GLU   A HG3  1 
ATOM   756  H HG3  B GLU   A 1 26  ? 14.572 -2.804  12.302  0.30 22.64 ?  26  GLU   A HG3  1 
ATOM   757  N N    . ALA   A 1 27  ? 18.462 0.130   14.320  1.00 17.68 ?  27  ALA   A N    1 
ATOM   758  C CA   . ALA   A 1 27  ? 19.856 0.144   14.749  1.00 17.87 ?  27  ALA   A CA   1 
ATOM   759  C C    . ALA   A 1 27  ? 20.026 0.945   16.034  1.00 19.97 ?  27  ALA   A C    1 
ATOM   760  O O    . ALA   A 1 27  ? 20.698 0.501   16.970  1.00 19.76 ?  27  ALA   A O    1 
ATOM   761  C CB   . ALA   A 1 27  ? 20.751 0.687   13.632  1.00 17.17 ?  27  ALA   A CB   1 
ATOM   762  H H    A ALA   A 1 27  ? 18.328 0.444   13.530  0.70 21.21 ?  27  ALA   A H    1 
ATOM   763  H H    B ALA   A 1 27  ? 18.269 0.663   13.674  0.30 21.21 ?  27  ALA   A H    1 
ATOM   764  H HA   . ALA   A 1 27  ? 20.136 -0.764  14.930  1.00 21.44 ?  27  ALA   A HA   1 
ATOM   765  H HB1  . ALA   A 1 27  ? 21.675 0.689   13.938  1.00 20.60 ?  27  ALA   A HB1  1 
ATOM   766  H HB2  . ALA   A 1 27  ? 20.668 0.116   12.851  1.00 20.60 ?  27  ALA   A HB2  1 
ATOM   767  H HB3  . ALA   A 1 27  ? 20.477 1.590   13.411  1.00 20.60 ?  27  ALA   A HB3  1 
ATOM   768  N N    A LYS   A 1 28  ? 19.408 2.126   16.105  0.70 21.47 ?  28  LYS   A N    1 
ATOM   769  N N    B LYS   A 1 28  ? 19.409 2.128   16.105  0.30 21.81 ?  28  LYS   A N    1 
ATOM   770  C CA   A LYS   A 1 28  ? 19.539 2.951   17.302  0.70 24.09 ?  28  LYS   A CA   1 
ATOM   771  C CA   B LYS   A 1 28  ? 19.535 2.952   17.303  0.30 24.14 ?  28  LYS   A CA   1 
ATOM   772  C C    A LYS   A 1 28  ? 18.991 2.247   18.537  0.70 24.93 ?  28  LYS   A C    1 
ATOM   773  C C    B LYS   A 1 28  ? 18.994 2.242   18.537  0.30 24.85 ?  28  LYS   A C    1 
ATOM   774  O O    A LYS   A 1 28  ? 19.505 2.450   19.643  0.70 26.17 ?  28  LYS   A O    1 
ATOM   775  O O    B LYS   A 1 28  ? 19.511 2.441   19.642  0.30 25.54 ?  28  LYS   A O    1 
ATOM   776  C CB   A LYS   A 1 28  ? 18.867 4.310   17.091  0.70 26.27 ?  28  LYS   A CB   1 
ATOM   777  C CB   B LYS   A 1 28  ? 18.834 4.298   17.099  0.30 25.82 ?  28  LYS   A CB   1 
ATOM   778  C CG   A LYS   A 1 28  ? 19.692 5.258   16.232  0.70 28.44 ?  28  LYS   A CG   1 
ATOM   779  C CG   B LYS   A 1 28  ? 19.598 5.252   16.194  0.30 27.36 ?  28  LYS   A CG   1 
ATOM   780  C CD   A LYS   A 1 28  ? 19.183 6.687   16.294  0.70 30.65 ?  28  LYS   A CD   1 
ATOM   781  C CD   B LYS   A 1 28  ? 19.078 6.680   16.292  0.30 28.76 ?  28  LYS   A CD   1 
ATOM   782  C CE   A LYS   A 1 28  ? 17.896 6.852   15.514  0.70 32.16 ?  28  LYS   A CE   1 
ATOM   783  C CE   B LYS   A 1 28  ? 17.755 6.851   15.568  0.30 29.76 ?  28  LYS   A CE   1 
ATOM   784  N NZ   A LYS   A 1 28  ? 17.477 8.280   15.455  0.70 33.04 ?  28  LYS   A NZ   1 
ATOM   785  N NZ   B LYS   A 1 28  ? 17.354 8.284   15.495  0.30 30.28 ?  28  LYS   A NZ   1 
ATOM   786  H H    A LYS   A 1 28  ? 18.914 2.462   15.489  0.70 25.77 ?  28  LYS   A H    1 
ATOM   787  H H    B LYS   A 1 28  ? 18.920 2.465   15.486  0.30 26.17 ?  28  LYS   A H    1 
ATOM   788  H HA   A LYS   A 1 28  ? 20.478 3.115   17.465  0.70 28.91 ?  28  LYS   A HA   1 
ATOM   789  H HA   B LYS   A 1 28  ? 20.472 3.133   17.461  0.30 28.97 ?  28  LYS   A HA   1 
ATOM   790  H HB2  A LYS   A 1 28  ? 18.014 4.178   16.649  0.70 31.53 ?  28  LYS   A HB2  1 
ATOM   791  H HB2  B LYS   A 1 28  ? 17.966 4.143   16.697  0.30 30.98 ?  28  LYS   A HB2  1 
ATOM   792  H HB3  A LYS   A 1 28  ? 18.731 4.735   17.953  0.70 31.53 ?  28  LYS   A HB3  1 
ATOM   793  H HB3  B LYS   A 1 28  ? 18.727 4.731   17.960  0.30 30.98 ?  28  LYS   A HB3  1 
ATOM   794  H HG2  A LYS   A 1 28  ? 20.610 5.253   16.545  0.70 34.12 ?  28  LYS   A HG2  1 
ATOM   795  H HG2  B LYS   A 1 28  ? 20.533 5.254   16.451  0.30 32.83 ?  28  LYS   A HG2  1 
ATOM   796  H HG3  A LYS   A 1 28  ? 19.653 4.965   15.308  0.70 34.12 ?  28  LYS   A HG3  1 
ATOM   797  H HG3  B LYS   A 1 28  ? 19.505 4.961   15.274  0.30 32.83 ?  28  LYS   A HG3  1 
ATOM   798  H HD2  A LYS   A 1 28  ? 19.011 6.926   17.218  0.70 36.77 ?  28  LYS   A HD2  1 
ATOM   799  H HD2  B LYS   A 1 28  ? 18.944 6.908   17.226  0.30 34.51 ?  28  LYS   A HD2  1 
ATOM   800  H HD3  A LYS   A 1 28  ? 19.848 7.281   15.912  0.70 36.77 ?  28  LYS   A HD3  1 
ATOM   801  H HD3  B LYS   A 1 28  ? 19.723 7.283   15.891  0.30 34.51 ?  28  LYS   A HD3  1 
ATOM   802  H HE2  A LYS   A 1 28  ? 18.029 6.536   14.606  0.70 38.59 ?  28  LYS   A HE2  1 
ATOM   803  H HE2  B LYS   A 1 28  ? 17.839 6.512   14.663  0.30 35.71 ?  28  LYS   A HE2  1 
ATOM   804  H HE3  A LYS   A 1 28  ? 17.191 6.345   15.946  0.70 38.59 ?  28  LYS   A HE3  1 
ATOM   805  H HE3  B LYS   A 1 28  ? 17.063 6.366   16.045  0.30 35.71 ?  28  LYS   A HE3  1 
ATOM   806  H HZ1  A LYS   A 1 28  ? 16.721 8.357   14.993  0.70 39.65 ?  28  LYS   A HZ1  1 
ATOM   807  H HZ1  B LYS   A 1 28  ? 16.578 8.363   15.067  0.30 36.33 ?  28  LYS   A HZ1  1 
ATOM   808  H HZ2  A LYS   A 1 28  ? 17.347 8.592   16.278  0.70 39.65 ?  28  LYS   A HZ2  1 
ATOM   809  H HZ2  B LYS   A 1 28  ? 17.268 8.618   16.316  0.30 36.33 ?  28  LYS   A HZ2  1 
ATOM   810  H HZ3  A LYS   A 1 28  ? 18.110 8.766   15.058  0.70 39.65 ?  28  LYS   A HZ3  1 
ATOM   811  H HZ3  B LYS   A 1 28  ? 17.974 8.751   15.058  0.30 36.33 ?  28  LYS   A HZ3  1 
ATOM   812  N N    . LYS   A 1 29  ? 17.967 1.407   18.372  1.00 25.07 ?  29  LYS   A N    1 
ATOM   813  C CA   . LYS   A 1 29  ? 17.385 0.700   19.511  1.00 27.00 ?  29  LYS   A CA   1 
ATOM   814  C C    . LYS   A 1 29  ? 18.212 -0.522  19.902  1.00 26.27 ?  29  LYS   A C    1 
ATOM   815  O O    . LYS   A 1 29  ? 18.502 -0.735  21.085  1.00 27.13 ?  29  LYS   A O    1 
ATOM   816  C CB   . LYS   A 1 29  ? 15.955 0.273   19.176  1.00 30.15 ?  29  LYS   A CB   1 
ATOM   817  C CG   . LYS   A 1 29  ? 15.203 -0.358  20.339  1.00 33.17 ?  29  LYS   A CG   1 
ATOM   818  C CD   . LYS   A 1 29  ? 14.855 0.677   21.396  1.00 35.94 ?  29  LYS   A CD   1 
ATOM   819  C CE   . LYS   A 1 29  ? 14.022 0.071   22.514  1.00 37.90 ?  29  LYS   A CE   1 
ATOM   820  N NZ   . LYS   A 1 29  ? 13.612 1.091   23.519  1.00 38.94 ?  29  LYS   A NZ   1 
ATOM   821  H H    A LYS   A 1 29  ? 17.595 1.231   17.618  0.70 30.08 ?  29  LYS   A H    1 
ATOM   822  H H    B LYS   A 1 29  ? 17.587 1.241   17.619  0.30 30.08 ?  29  LYS   A H    1 
ATOM   823  H HA   . LYS   A 1 29  ? 17.351 1.298   20.273  1.00 32.40 ?  29  LYS   A HA   1 
ATOM   824  H HB2  . LYS   A 1 29  ? 15.454 1.052   18.891  1.00 36.18 ?  29  LYS   A HB2  1 
ATOM   825  H HB3  . LYS   A 1 29  ? 15.984 -0.380  18.458  1.00 36.18 ?  29  LYS   A HB3  1 
ATOM   826  H HG2  . LYS   A 1 29  ? 14.376 -0.746  20.013  1.00 39.81 ?  29  LYS   A HG2  1 
ATOM   827  H HG3  . LYS   A 1 29  ? 15.753 -1.043  20.753  1.00 39.81 ?  29  LYS   A HG3  1 
ATOM   828  H HD2  . LYS   A 1 29  ? 15.673 1.028   21.783  1.00 43.13 ?  29  LYS   A HD2  1 
ATOM   829  H HD3  . LYS   A 1 29  ? 14.344 1.393   20.987  1.00 43.13 ?  29  LYS   A HD3  1 
ATOM   830  H HE2  . LYS   A 1 29  ? 13.219 -0.321  22.136  1.00 45.48 ?  29  LYS   A HE2  1 
ATOM   831  H HE3  . LYS   A 1 29  ? 14.544 -0.609  22.968  1.00 45.48 ?  29  LYS   A HE3  1 
ATOM   832  H HZ1  . LYS   A 1 29  ? 13.127 0.709   24.160  1.00 46.73 ?  29  LYS   A HZ1  1 
ATOM   833  H HZ2  . LYS   A 1 29  ? 14.333 1.463   23.885  1.00 46.73 ?  29  LYS   A HZ2  1 
ATOM   834  H HZ3  . LYS   A 1 29  ? 13.126 1.725   23.127  1.00 46.73 ?  29  LYS   A HZ3  1 
ATOM   835  N N    . VAL   A 1 30  ? 18.575 -1.349  18.921  1.00 25.03 ?  30  VAL   A N    1 
ATOM   836  C CA   . VAL   A 1 30  ? 19.227 -2.623  19.210  1.00 24.14 ?  30  VAL   A CA   1 
ATOM   837  C C    . VAL   A 1 30  ? 20.731 -2.462  19.421  1.00 22.83 ?  30  VAL   A C    1 
ATOM   838  O O    . VAL   A 1 30  ? 21.332 -3.197  20.213  1.00 23.32 ?  30  VAL   A O    1 
ATOM   839  C CB   . VAL   A 1 30  ? 18.918 -3.611  18.071  1.00 25.18 ?  30  VAL   A CB   1 
ATOM   840  C CG1  . VAL   A 1 30  ? 19.712 -4.900  18.238  1.00 25.66 ?  30  VAL   A CG1  1 
ATOM   841  C CG2  . VAL   A 1 30  ? 17.427 -3.898  18.008  1.00 26.00 ?  30  VAL   A CG2  1 
ATOM   842  H H    . VAL   A 1 30  ? 18.438 -1.204  18.084  1.00 30.03 ?  30  VAL   A H    1 
ATOM   843  H HA   . VAL   A 1 30  ? 18.843 -2.986  20.023  1.00 28.96 ?  30  VAL   A HA   1 
ATOM   844  H HB   . VAL   A 1 30  ? 19.181 -3.210  17.228  1.00 30.21 ?  30  VAL   A HB   1 
ATOM   845  H HG11 . VAL   A 1 30  ? 19.189 -5.638  17.887  1.00 30.79 ?  30  VAL   A HG11 1 
ATOM   846  H HG12 . VAL   A 1 30  ? 20.545 -4.823  17.748  1.00 30.79 ?  30  VAL   A HG12 1 
ATOM   847  H HG13 . VAL   A 1 30  ? 19.892 -5.042  19.178  1.00 30.79 ?  30  VAL   A HG13 1 
ATOM   848  H HG21 . VAL   A 1 30  ? 17.252 -4.493  17.263  1.00 31.20 ?  30  VAL   A HG21 1 
ATOM   849  H HG22 . VAL   A 1 30  ? 17.151 -4.318  18.838  1.00 31.20 ?  30  VAL   A HG22 1 
ATOM   850  H HG23 . VAL   A 1 30  ? 16.949 -3.065  17.883  1.00 31.20 ?  30  VAL   A HG23 1 
ATOM   851  N N    . LYS   A 1 31  ? 21.360 -1.512  18.738  1.00 21.75 ?  31  LYS   A N    1 
ATOM   852  C CA   . LYS   A 1 31  ? 22.813 -1.404  18.680  1.00 22.57 ?  31  LYS   A CA   1 
ATOM   853  C C    . LYS   A 1 31  ? 23.431 -2.757  18.316  1.00 20.27 ?  31  LYS   A C    1 
ATOM   854  O O    . LYS   A 1 31  ? 24.222 -3.316  19.085  1.00 20.83 ?  31  LYS   A O    1 
ATOM   855  C CB   . LYS   A 1 31  ? 23.400 -0.865  19.977  1.00 27.21 ?  31  LYS   A CB   1 
ATOM   856  C CG   . LYS   A 1 31  ? 22.749 0.414   20.479  1.00 32.37 ?  31  LYS   A CG   1 
ATOM   857  C CD   . LYS   A 1 31  ? 23.776 1.517   20.686  1.00 36.48 ?  31  LYS   A CD   1 
ATOM   858  C CE   . LYS   A 1 31  ? 23.266 2.585   21.642  1.00 39.15 ?  31  LYS   A CE   1 
ATOM   859  N NZ   . LYS   A 1 31  ? 21.945 3.139   21.238  1.00 40.49 ?  31  LYS   A NZ   1 
ATOM   860  H H    . LYS   A 1 31  ? 20.953 -0.900  18.293  1.00 26.09 ?  31  LYS   A H    1 
ATOM   861  H HA   . LYS   A 1 31  ? 23.037 -0.780  17.980  1.00 27.08 ?  31  LYS   A HA   1 
ATOM   862  H HB2  . LYS   A 1 31  ? 23.286 -1.537  20.657  1.00 32.65 ?  31  LYS   A HB2  1 
ATOM   863  H HB3  . LYS   A 1 31  ? 24.347 -0.688  19.841  1.00 32.65 ?  31  LYS   A HB3  1 
ATOM   864  H HG2  . LYS   A 1 31  ? 22.100 0.721   19.827  1.00 38.85 ?  31  LYS   A HG2  1 
ATOM   865  H HG3  . LYS   A 1 31  ? 22.314 0.238   21.329  1.00 38.85 ?  31  LYS   A HG3  1 
ATOM   866  H HD2  . LYS   A 1 31  ? 24.585 1.137   21.061  1.00 43.78 ?  31  LYS   A HD2  1 
ATOM   867  H HD3  . LYS   A 1 31  ? 23.966 1.938   19.833  1.00 43.78 ?  31  LYS   A HD3  1 
ATOM   868  H HE2  . LYS   A 1 31  ? 23.169 2.196   22.525  1.00 46.98 ?  31  LYS   A HE2  1 
ATOM   869  H HE3  . LYS   A 1 31  ? 23.904 3.315   21.670  1.00 46.98 ?  31  LYS   A HE3  1 
ATOM   870  H HZ1  . LYS   A 1 31  ? 21.695 3.776   21.808  1.00 48.59 ?  31  LYS   A HZ1  1 
ATOM   871  H HZ2  . LYS   A 1 31  ? 21.999 3.487   20.421  1.00 48.59 ?  31  LYS   A HZ2  1 
ATOM   872  H HZ3  . LYS   A 1 31  ? 21.331 2.494   21.238  1.00 48.59 ?  31  LYS   A HZ3  1 
ATOM   873  N N    . PRO   A 1 32  ? 23.083 -3.307  17.159  1.00 18.16 ?  32  PRO   A N    1 
ATOM   874  C CA   . PRO   A 1 32  ? 23.559 -4.643  16.802  1.00 18.18 ?  32  PRO   A CA   1 
ATOM   875  C C    . PRO   A 1 32  ? 25.059 -4.655  16.584  1.00 18.25 ?  32  PRO   A C    1 
ATOM   876  O O    . PRO   A 1 32  ? 25.698 -3.622  16.376  1.00 18.01 ?  32  PRO   A O    1 
ATOM   877  C CB   . PRO   A 1 32  ? 22.818 -4.936  15.494  1.00 18.27 ?  32  PRO   A CB   1 
ATOM   878  C CG   . PRO   A 1 32  ? 22.607 -3.578  14.888  1.00 17.65 ?  32  PRO   A CG   1 
ATOM   879  C CD   . PRO   A 1 32  ? 22.324 -2.682  16.063  1.00 17.41 ?  32  PRO   A CD   1 
ATOM   880  H HA   . PRO   A 1 32  ? 23.317 -5.293  17.476  1.00 21.82 ?  32  PRO   A HA   1 
ATOM   881  H HB2  . PRO   A 1 32  ? 23.368 -5.494  14.918  1.00 21.92 ?  32  PRO   A HB2  1 
ATOM   882  H HB3  . PRO   A 1 32  ? 21.970 -5.369  15.685  1.00 21.92 ?  32  PRO   A HB3  1 
ATOM   883  H HG2  . PRO   A 1 32  ? 23.409 -3.304  14.421  1.00 21.18 ?  32  PRO   A HG2  1 
ATOM   884  H HG3  . PRO   A 1 32  ? 21.848 -3.610  14.283  1.00 21.18 ?  32  PRO   A HG3  1 
ATOM   885  H HD2  . PRO   A 1 32  ? 22.655 -1.788  15.878  1.00 20.90 ?  32  PRO   A HD2  1 
ATOM   886  H HD3  . PRO   A 1 32  ? 21.378 -2.680  16.261  1.00 20.90 ?  32  PRO   A HD3  1 
ATOM   887  N N    . THR   A 1 33  ? 25.618 -5.864  16.615  1.00 18.08 ?  33  THR   A N    1 
ATOM   888  C CA   . THR   A 1 33  ? 27.027 -6.020  16.281  1.00 18.08 ?  33  THR   A CA   1 
ATOM   889  C C    . THR   A 1 33  ? 27.304 -5.549  14.860  1.00 16.45 ?  33  THR   A C    1 
ATOM   890  O O    . THR   A 1 33  ? 28.329 -4.902  14.603  1.00 16.37 ?  33  THR   A O    1 
ATOM   891  C CB   . THR   A 1 33  ? 27.442 -7.478  16.473  1.00 19.40 ?  33  THR   A CB   1 
ATOM   892  O OG1  . THR   A 1 33  ? 27.154 -7.872  17.817  1.00 20.96 ?  33  THR   A OG1  1 
ATOM   893  C CG2  . THR   A 1 33  ? 28.932 -7.660  16.208  1.00 20.32 ?  33  THR   A CG2  1 
ATOM   894  H H    . THR   A 1 33  ? 25.211 -6.595  16.811  1.00 21.69 ?  33  THR   A H    1 
ATOM   895  H HA   . THR   A 1 33  ? 27.559 -5.482  16.882  1.00 21.70 ?  33  THR   A HA   1 
ATOM   896  H HB   . THR   A 1 33  ? 26.953 -8.052  15.859  1.00 23.28 ?  33  THR   A HB   1 
ATOM   897  H HG1  . THR   A 1 33  ? 27.587 -7.396  18.360  1.00 25.16 ?  33  THR   A HG1  1 
ATOM   898  H HG21 . THR   A 1 33  ? 29.216 -8.546  16.486  1.00 24.38 ?  33  THR   A HG21 1 
ATOM   899  H HG22 . THR   A 1 33  ? 29.118 -7.554  15.262  1.00 24.38 ?  33  THR   A HG22 1 
ATOM   900  H HG23 . THR   A 1 33  ? 29.438 -6.999  16.706  1.00 24.38 ?  33  THR   A HG23 1 
ATOM   901  N N    . VAL   A 1 34  ? 26.401 -5.859  13.927  1.00 14.77 ?  34  VAL   A N    1 
ATOM   902  C CA   . VAL   A 1 34  ? 26.577 -5.519  12.519  1.00 13.81 ?  34  VAL   A CA   1 
ATOM   903  C C    . VAL   A 1 34  ? 25.270 -4.958  11.967  1.00 13.10 ?  34  VAL   A C    1 
ATOM   904  O O    . VAL   A 1 34  ? 24.229 -5.624  12.027  1.00 13.37 ?  34  VAL   A O    1 
ATOM   905  C CB   . VAL   A 1 34  ? 27.023 -6.727  11.673  1.00 14.27 ?  34  VAL   A CB   1 
ATOM   906  C CG1  . VAL   A 1 34  ? 27.210 -6.317  10.221  1.00 14.50 ?  34  VAL   A CG1  1 
ATOM   907  C CG2  . VAL   A 1 34  ? 28.303 -7.354  12.230  1.00 15.34 ?  34  VAL   A CG2  1 
ATOM   908  H H    . VAL   A 1 34  ? 25.667 -6.281  14.088  1.00 17.72 ?  34  VAL   A H    1 
ATOM   909  H HA   . VAL   A 1 34  ? 27.255 -4.828  12.439  1.00 16.57 ?  34  VAL   A HA   1 
ATOM   910  H HB   . VAL   A 1 34  ? 26.327 -7.398  11.699  1.00 17.13 ?  34  VAL   A HB   1 
ATOM   911  H HG11 . VAL   A 1 34  ? 27.690 -7.021  9.754   1.00 17.41 ?  34  VAL   A HG11 1 
ATOM   912  H HG12 . VAL   A 1 34  ? 26.345 -6.178  9.810   1.00 17.41 ?  34  VAL   A HG12 1 
ATOM   913  H HG13 . VAL   A 1 34  ? 27.730 -5.494  10.188  1.00 17.41 ?  34  VAL   A HG13 1 
ATOM   914  H HG21 . VAL   A 1 34  ? 28.578 -8.083  11.650  1.00 18.41 ?  34  VAL   A HG21 1 
ATOM   915  H HG22 . VAL   A 1 34  ? 29.002 -6.680  12.262  1.00 18.41 ?  34  VAL   A HG22 1 
ATOM   916  H HG23 . VAL   A 1 34  ? 28.129 -7.691  13.122  1.00 18.41 ?  34  VAL   A HG23 1 
ATOM   917  N N    . VAL   A 1 35  ? 25.324 -3.743  11.417  1.00 12.26 ?  35  VAL   A N    1 
ATOM   918  C CA   . VAL   A 1 35  ? 24.283 -3.226  10.538  1.00 11.88 ?  35  VAL   A CA   1 
ATOM   919  C C    . VAL   A 1 35  ? 24.831 -3.221  9.119   1.00 11.22 ?  35  VAL   A C    1 
ATOM   920  O O    . VAL   A 1 35  ? 25.975 -2.811  8.886   1.00 11.66 ?  35  VAL   A O    1 
ATOM   921  C CB   . VAL   A 1 35  ? 23.755 -1.835  10.958  1.00 12.58 ?  35  VAL   A CB   1 
ATOM   922  C CG1  . VAL   A 1 35  ? 24.831 -0.744  10.835  1.00 13.34 ?  35  VAL   A CG1  1 
ATOM   923  C CG2  . VAL   A 1 35  ? 22.519 -1.468  10.138  1.00 13.05 ?  35  VAL   A CG2  1 
ATOM   924  H H    . VAL   A 1 35  ? 25.967 -3.187  11.539  1.00 14.71 ?  35  VAL   A H    1 
ATOM   925  H HA   . VAL   A 1 35  ? 23.524 -3.837  10.559  1.00 14.25 ?  35  VAL   A HA   1 
ATOM   926  H HB   . VAL   A 1 35  ? 23.478 -1.872  11.884  1.00 15.10 ?  35  VAL   A HB   1 
ATOM   927  H HG11 . VAL   A 1 35  ? 24.486 0.087   11.207  1.00 16.00 ?  35  VAL   A HG11 1 
ATOM   928  H HG12 . VAL   A 1 35  ? 25.617 -1.021  11.329  1.00 16.00 ?  35  VAL   A HG12 1 
ATOM   929  H HG13 . VAL   A 1 35  ? 25.055 -0.615  9.901   1.00 16.00 ?  35  VAL   A HG13 1 
ATOM   930  H HG21 . VAL   A 1 35  ? 22.164 -0.624  10.454  1.00 15.66 ?  35  VAL   A HG21 1 
ATOM   931  H HG22 . VAL   A 1 35  ? 22.773 -1.386  9.200   1.00 15.66 ?  35  VAL   A HG22 1 
ATOM   932  H HG23 . VAL   A 1 35  ? 21.854 -2.167  10.236  1.00 15.66 ?  35  VAL   A HG23 1 
ATOM   933  N N    . VAL   A 1 36  ? 24.011 -3.668  8.171   1.00 10.78 ?  36  VAL   A N    1 
ATOM   934  C CA   . VAL   A 1 36  ? 24.379 -3.671  6.761   1.00 10.31 ?  36  VAL   A CA   1 
ATOM   935  C C    . VAL   A 1 36  ? 23.915 -2.378  6.108   1.00 10.68 ?  36  VAL   A C    1 
ATOM   936  O O    . VAL   A 1 36  ? 22.755 -1.968  6.263   1.00 11.21 ?  36  VAL   A O    1 
ATOM   937  C CB   . VAL   A 1 36  ? 23.769 -4.885  6.043   1.00 10.50 ?  36  VAL   A CB   1 
ATOM   938  C CG1  . VAL   A 1 36  ? 24.028 -4.809  4.555   1.00 11.19 ?  36  VAL   A CG1  1 
ATOM   939  C CG2  . VAL   A 1 36  ? 24.317 -6.184  6.622   1.00 11.37 ?  36  VAL   A CG2  1 
ATOM   940  H H    . VAL   A 1 36  ? 23.218 -3.983  8.324   1.00 12.94 ?  36  VAL   A H    1 
ATOM   941  H HA   . VAL   A 1 36  ? 25.347 -3.732  6.687   1.00 12.37 ?  36  VAL   A HA   1 
ATOM   942  H HB   . VAL   A 1 36  ? 22.809 -4.877  6.180   1.00 12.60 ?  36  VAL   A HB   1 
ATOM   943  H HG11 . VAL   A 1 36  ? 23.881 -5.684  4.162   1.00 13.43 ?  36  VAL   A HG11 1 
ATOM   944  H HG12 . VAL   A 1 36  ? 23.422 -4.164  4.155   1.00 13.43 ?  36  VAL   A HG12 1 
ATOM   945  H HG13 . VAL   A 1 36  ? 24.948 -4.534  4.406   1.00 13.43 ?  36  VAL   A HG13 1 
ATOM   946  H HG21 . VAL   A 1 36  ? 23.928 -6.936  6.144   1.00 13.65 ?  36  VAL   A HG21 1 
ATOM   947  H HG22 . VAL   A 1 36  ? 25.282 -6.197  6.525   1.00 13.65 ?  36  VAL   A HG22 1 
ATOM   948  H HG23 . VAL   A 1 36  ? 24.081 -6.242  7.564   1.00 13.65 ?  36  VAL   A HG23 1 
ATOM   949  N N    . ASN   A 1 37  ? 24.821 -1.750  5.361   1.00 9.89  ?  37  ASN   A N    1 
ATOM   950  C CA   . ASN   A 1 37  ? 24.487 -0.627  4.502   1.00 9.45  ?  37  ASN   A CA   1 
ATOM   951  C C    . ASN   A 1 37  ? 24.349 -1.081  3.059   1.00 9.71  ?  37  ASN   A C    1 
ATOM   952  O O    . ASN   A 1 37  ? 25.125 -1.913  2.576   1.00 10.32 ?  37  ASN   A O    1 
ATOM   953  C CB   . ASN   A 1 37  ? 25.563 0.454   4.586   1.00 10.11 ?  37  ASN   A CB   1 
ATOM   954  C CG   . ASN   A 1 37  ? 25.232 1.665   3.746   1.00 10.41 ?  37  ASN   A CG   1 
ATOM   955  O OD1  . ASN   A 1 37  ? 24.055 2.001   3.569   1.00 10.67 ?  37  ASN   A OD1  1 
ATOM   956  N ND2  . ASN   A 1 37  ? 26.260 2.319   3.220   1.00 10.69 ?  37  ASN   A ND2  1 
ATOM   957  H H    . ASN   A 1 37  ? 25.659 -1.961  5.343   1.00 11.87 ?  37  ASN   A H    1 
ATOM   958  H HA   . ASN   A 1 37  ? 23.649 -0.243  4.791   1.00 11.35 ?  37  ASN   A HA   1 
ATOM   959  H HB2  . ASN   A 1 37  ? 25.651 0.748   5.508   1.00 12.13 ?  37  ASN   A HB2  1 
ATOM   960  H HB3  . ASN   A 1 37  ? 26.410 0.090   4.276   1.00 12.13 ?  37  ASN   A HB3  1 
ATOM   961  H HD21 . ASN   A 1 37  ? 26.121 3.013   2.730   1.00 12.83 ?  37  ASN   A HD21 1 
ATOM   962  H HD22 . ASN   A 1 37  ? 27.059 2.057   3.366   1.00 12.83 ?  37  ASN   A HD22 1 
ATOM   963  N N    A ALA   A 1 38  ? 23.327 -0.533  2.394   0.70 10.50 ?  38  ALA   A N    1 
ATOM   964  N N    B ALA   A 1 38  ? 23.356 -0.527  2.363   0.30 10.34 ?  38  ALA   A N    1 
ATOM   965  C CA   A ALA   A 1 38  ? 23.110 -0.654  0.954   0.70 10.76 ?  38  ALA   A CA   1 
ATOM   966  C CA   B ALA   A 1 38  ? 23.184 -0.779  0.932   0.30 10.69 ?  38  ALA   A CA   1 
ATOM   967  C C    A ALA   A 1 38  ? 24.039 0.335   0.249   0.70 10.60 ?  38  ALA   A C    1 
ATOM   968  C C    B ALA   A 1 38  ? 24.009 0.244   0.156   0.30 10.50 ?  38  ALA   A C    1 
ATOM   969  O O    A ALA   A 1 38  ? 23.651 1.441   -0.135  0.70 10.25 ?  38  ALA   A O    1 
ATOM   970  O O    B ALA   A 1 38  ? 23.506 1.244   -0.363  0.30 10.28 ?  38  ALA   A O    1 
ATOM   971  C CB   A ALA   A 1 38  ? 21.648 -0.370  0.628   0.70 11.95 ?  38  ALA   A CB   1 
ATOM   972  C CB   B ALA   A 1 38  ? 21.713 -0.714  0.558   0.30 11.41 ?  38  ALA   A CB   1 
ATOM   973  H H    A ALA   A 1 38  ? 22.730 -0.049  2.782   0.70 12.61 ?  38  ALA   A H    1 
ATOM   974  H H    B ALA   A 1 38  ? 22.763 -0.001  2.705   0.30 12.40 ?  38  ALA   A H    1 
ATOM   975  H HA   A ALA   A 1 38  ? 23.327 -1.550  0.664   0.70 12.91 ?  38  ALA   A HA   1 
ATOM   976  H HA   B ALA   A 1 38  ? 23.517 -1.669  0.724   0.30 12.82 ?  38  ALA   A HA   1 
ATOM   977  H HB1  A ALA   A 1 38  ? 21.513 -0.459  -0.327  0.70 14.34 ?  38  ALA   A HB1  1 
ATOM   978  H HB1  B ALA   A 1 38  ? 21.616 -0.970  -0.370  0.30 13.69 ?  38  ALA   A HB1  1 
ATOM   979  H HB2  A ALA   A 1 38  ? 21.089 -1.007  1.103   0.70 14.34 ?  38  ALA   A HB2  1 
ATOM   980  H HB2  B ALA   A 1 38  ? 21.224 -1.319  1.131   0.30 13.69 ?  38  ALA   A HB2  1 
ATOM   981  H HB3  A ALA   A 1 38  ? 21.429 0.533   0.911   0.70 14.34 ?  38  ALA   A HB3  1 
ATOM   982  H HB3  B ALA   A 1 38  ? 21.400 0.195   0.691   0.30 13.69 ?  38  ALA   A HB3  1 
ATOM   983  N N    A ALA   A 1 39  ? 25.294 -0.073  0.086   0.70 10.45 ?  39  ALA   A N    1 
ATOM   984  N N    B ALA   A 1 39  ? 25.306 -0.026  0.067   0.30 10.62 ?  39  ALA   A N    1 
ATOM   985  C CA   A ALA   A 1 39  ? 26.360 0.795   -0.384  0.70 9.91  ?  39  ALA   A CA   1 
ATOM   986  C CA   B ALA   A 1 39  ? 26.259 0.930   -0.467  0.30 10.85 ?  39  ALA   A CA   1 
ATOM   987  C C    A ALA   A 1 39  ? 26.481 0.769   -1.906  0.70 10.15 ?  39  ALA   A C    1 
ATOM   988  C C    B ALA   A 1 39  ? 26.404 0.788   -1.981  0.30 10.66 ?  39  ALA   A C    1 
ATOM   989  O O    A ALA   A 1 39  ? 25.981 -0.134  -2.583  0.70 10.76 ?  39  ALA   A O    1 
ATOM   990  O O    B ALA   A 1 39  ? 25.974 -0.194  -2.590  0.30 10.95 ?  39  ALA   A O    1 
ATOM   991  C CB   A ALA   A 1 39  ? 27.680 0.360   0.254   0.70 10.26 ?  39  ALA   A CB   1 
ATOM   992  C CB   B ALA   A 1 39  ? 27.616 0.734   0.204   0.30 11.31 ?  39  ALA   A CB   1 
ATOM   993  H H    A ALA   A 1 39  ? 25.557 -0.880  0.250   0.70 12.55 ?  39  ALA   A H    1 
ATOM   994  H H    B ALA   A 1 39  ? 25.659 -0.775  0.314   0.30 12.75 ?  39  ALA   A H    1 
ATOM   995  H HA   A ALA   A 1 39  ? 26.172 1.707   -0.111  0.70 11.89 ?  39  ALA   A HA   1 
ATOM   996  H HA   B ALA   A 1 39  ? 25.947 1.825   -0.263  0.30 13.02 ?  39  ALA   A HA   1 
ATOM   997  H HB1  A ALA   A 1 39  ? 28.386 0.947   -0.058  0.70 12.32 ?  39  ALA   A HB1  1 
ATOM   998  H HB1  B ALA   A 1 39  ? 28.240 1.377   -0.163  0.30 13.57 ?  39  ALA   A HB1  1 
ATOM   999  H HB2  A ALA   A 1 39  ? 27.598 0.432   1.222   0.70 12.32 ?  39  ALA   A HB2  1 
ATOM   1000 H HB2  B ALA   A 1 39  ? 27.520 0.871   1.160   0.30 13.57 ?  39  ALA   A HB2  1 
ATOM   1001 H HB3  A ALA   A 1 39  ? 27.866 -0.553  0.005   0.70 12.32 ?  39  ALA   A HB3  1 
ATOM   1002 H HB3  B ALA   A 1 39  ? 27.925 -0.169  0.028   0.30 13.57 ?  39  ALA   A HB3  1 
ATOM   1003 N N    A ASN   A 1 40  ? 27.181 1.775   -2.437  0.70 10.37 ?  40  ASN   A N    1 
ATOM   1004 N N    B ASN   A 1 40  ? 27.027 1.798   -2.587  0.30 10.54 ?  40  ASN   A N    1 
ATOM   1005 C CA   A ASN   A 1 40  ? 27.710 1.745   -3.796  0.70 10.62 ?  40  ASN   A CA   1 
ATOM   1006 C CA   B ASN   A 1 40  ? 27.539 1.721   -3.949  0.30 10.76 ?  40  ASN   A CA   1 
ATOM   1007 C C    A ASN   A 1 40  ? 29.235 1.628   -3.749  0.70 10.29 ?  40  ASN   A C    1 
ATOM   1008 C C    B ASN   A 1 40  ? 29.066 1.609   -3.901  0.30 10.37 ?  40  ASN   A C    1 
ATOM   1009 O O    A ASN   A 1 40  ? 29.849 1.744   -2.685  0.70 10.45 ?  40  ASN   A O    1 
ATOM   1010 O O    B ASN   A 1 40  ? 29.679 1.654   -2.833  0.30 10.13 ?  40  ASN   A O    1 
ATOM   1011 C CB   A ASN   A 1 40  ? 27.217 2.939   -4.633  0.70 11.30 ?  40  ASN   A CB   1 
ATOM   1012 C CB   B ASN   A 1 40  ? 27.061 2.910   -4.791  0.30 11.22 ?  40  ASN   A CB   1 
ATOM   1013 C CG   A ASN   A 1 40  ? 27.615 4.284   -4.058  0.70 12.30 ?  40  ASN   A CG   1 
ATOM   1014 C CG   B ASN   A 1 40  ? 27.387 4.246   -4.158  0.30 11.51 ?  40  ASN   A CG   1 
ATOM   1015 O OD1  A ASN   A 1 40  ? 28.786 4.519   -3.740  0.70 13.14 ?  40  ASN   A OD1  1 
ATOM   1016 O OD1  B ASN   A 1 40  ? 28.556 4.589   -3.967  0.30 12.42 ?  40  ASN   A OD1  1 
ATOM   1017 N ND2  A ASN   A 1 40  ? 26.638 5.186   -3.939  0.70 13.13 ?  40  ASN   A ND2  1 
ATOM   1018 N ND2  B ASN   A 1 40  ? 26.352 5.019   -3.849  0.30 11.62 ?  40  ASN   A ND2  1 
ATOM   1019 H H    A ASN   A 1 40  ? 27.375 2.492   -2.013  0.70 12.44 ?  40  ASN   A H    1 
ATOM   1020 H H    B ASN   A 1 40  ? 27.168 2.555   -2.210  0.30 12.65 ?  40  ASN   A H    1 
ATOM   1021 H HA   A ASN   A 1 40  ? 27.385 0.941   -4.230  0.70 12.75 ?  40  ASN   A HA   1 
ATOM   1022 H HA   B ASN   A 1 40  ? 27.189 0.910   -4.362  0.30 12.91 ?  40  ASN   A HA   1 
ATOM   1023 H HB2  A ASN   A 1 40  ? 27.586 2.866   -5.530  0.70 13.56 ?  40  ASN   A HB2  1 
ATOM   1024 H HB2  B ASN   A 1 40  ? 27.493 2.872   -5.656  0.30 13.46 ?  40  ASN   A HB2  1 
ATOM   1025 H HB3  A ASN   A 1 40  ? 26.248 2.904   -4.677  0.70 13.56 ?  40  ASN   A HB3  1 
ATOM   1026 H HB3  B ASN   A 1 40  ? 26.096 2.851   -4.902  0.30 13.46 ?  40  ASN   A HB3  1 
ATOM   1027 H HD21 A ASN   A 1 40  ? 26.811 5.968   -3.627  0.70 15.75 ?  40  ASN   A HD21 1 
ATOM   1028 H HD21 B ASN   A 1 40  ? 26.484 5.786   -3.488  0.30 13.95 ?  40  ASN   A HD21 1 
ATOM   1029 H HD22 A ASN   A 1 40  ? 25.832 4.983   -4.166  0.70 15.75 ?  40  ASN   A HD22 1 
ATOM   1030 H HD22 B ASN   A 1 40  ? 25.548 4.749   -4.004  0.30 13.95 ?  40  ASN   A HD22 1 
ATOM   1031 N N    A VAL   A 1 41  ? 29.843 1.354   -4.909  0.70 10.85 ?  41  VAL   A N    1 
ATOM   1032 N N    B VAL   A 1 41  ? 29.680 1.462   -5.078  0.30 10.52 ?  41  VAL   A N    1 
ATOM   1033 C CA   A VAL   A 1 41  ? 31.273 1.057   -4.934  0.70 11.42 ?  41  VAL   A CA   1 
ATOM   1034 C CA   B VAL   A 1 41  ? 31.103 1.116   -5.148  0.30 10.73 ?  41  VAL   A CA   1 
ATOM   1035 C C    A VAL   A 1 41  ? 32.102 2.236   -4.474  0.70 11.70 ?  41  VAL   A C    1 
ATOM   1036 C C    B VAL   A 1 41  ? 32.033 2.210   -4.619  0.30 10.90 ?  41  VAL   A C    1 
ATOM   1037 O O    A VAL   A 1 41  ? 33.243 2.047   -4.032  0.70 12.18 ?  41  VAL   A O    1 
ATOM   1038 O O    B VAL   A 1 41  ? 33.184 1.922   -4.264  0.30 10.50 ?  41  VAL   A O    1 
ATOM   1039 C CB   A VAL   A 1 41  ? 31.780 0.562   -6.310  0.70 11.60 ?  41  VAL   A CB   1 
ATOM   1040 C CB   B VAL   A 1 41  ? 31.497 0.710   -6.580  0.30 11.10 ?  41  VAL   A CB   1 
ATOM   1041 C CG1  A VAL   A 1 41  ? 31.064 -0.718  -6.720  0.70 12.82 ?  41  VAL   A CG1  1 
ATOM   1042 C CG1  B VAL   A 1 41  ? 30.877 -0.633  -6.937  0.30 12.01 ?  41  VAL   A CG1  1 
ATOM   1043 C CG2  A VAL   A 1 41  ? 31.673 1.649   -7.384  0.70 11.80 ?  41  VAL   A CG2  1 
ATOM   1044 C CG2  B VAL   A 1 41  ? 31.091 1.783   -7.586  0.30 11.26 ?  41  VAL   A CG2  1 
ATOM   1045 H H    A VAL   A 1 41  ? 29.459 1.324   -5.679  0.70 13.02 ?  41  VAL   A H    1 
ATOM   1046 H H    B VAL   A 1 41  ? 29.279 1.537   -5.838  0.30 12.62 ?  41  VAL   A H    1 
ATOM   1047 H HA   A VAL   A 1 41  ? 31.446 0.340   -4.303  0.70 13.71 ?  41  VAL   A HA   1 
ATOM   1048 H HA   B VAL   A 1 41  ? 31.232 0.340   -4.589  0.30 12.88 ?  41  VAL   A HA   1 
ATOM   1049 H HB   A VAL   A 1 41  ? 32.722 0.338   -6.224  0.70 13.91 ?  41  VAL   A HB   1 
ATOM   1050 H HB   B VAL   A 1 41  ? 32.456 0.613   -6.617  0.30 13.32 ?  41  VAL   A HB   1 
ATOM   1051 H HG11 A VAL   A 1 41  ? 31.411 -1.018  -7.573  0.70 15.38 ?  41  VAL   A HG11 1 
ATOM   1052 H HG11 B VAL   A 1 41  ? 31.153 -0.878  -7.832  0.30 14.41 ?  41  VAL   A HG11 1 
ATOM   1053 H HG12 A VAL   A 1 41  ? 31.214 -1.396  -6.042  0.70 15.38 ?  41  VAL   A HG12 1 
ATOM   1054 H HG12 B VAL   A 1 41  ? 31.184 -1.299  -6.301  0.30 14.41 ?  41  VAL   A HG12 1 
ATOM   1055 H HG13 A VAL   A 1 41  ? 30.113 -0.534  -6.796  0.70 15.38 ?  41  VAL   A HG13 1 
ATOM   1056 H HG13 B VAL   A 1 41  ? 29.911 -0.558  -6.895  0.30 14.41 ?  41  VAL   A HG13 1 
ATOM   1057 H HG21 A VAL   A 1 41  ? 31.865 1.255   -8.252  0.70 14.16 ?  41  VAL   A HG21 1 
ATOM   1058 H HG21 B VAL   A 1 41  ? 31.508 1.585   -8.438  0.30 13.51 ?  41  VAL   A HG21 1 
ATOM   1059 H HG22 A VAL   A 1 41  ? 30.779 2.014   -7.375  0.70 14.16 ?  41  VAL   A HG22 1 
ATOM   1060 H HG22 B VAL   A 1 41  ? 30.125 1.783   -7.685  0.30 13.51 ?  41  VAL   A HG22 1 
ATOM   1061 H HG23 A VAL   A 1 41  ? 32.321 2.347   -7.192  0.70 14.16 ?  41  VAL   A HG23 1 
ATOM   1062 H HG23 B VAL   A 1 41  ? 31.390 2.646   -7.264  0.30 13.51 ?  41  VAL   A HG23 1 
ATOM   1063 N N    . TYR   A 1 42  ? 31.569 3.457   -4.581  1.00 11.23 ?  42  TYR   A N    1 
ATOM   1064 C CA   . TYR   A 1 42  ? 32.320 4.636   -4.160  1.00 11.36 ?  42  TYR   A CA   1 
ATOM   1065 C C    . TYR   A 1 42  ? 32.066 5.008   -2.708  1.00 11.29 ?  42  TYR   A C    1 
ATOM   1066 O O    . TYR   A 1 42  ? 32.627 6.001   -2.218  1.00 11.77 ?  42  TYR   A O    1 
ATOM   1067 C CB   . TYR   A 1 42  ? 31.976 5.830   -5.071  1.00 12.23 ?  42  TYR   A CB   1 
ATOM   1068 C CG   . TYR   A 1 42  ? 32.164 5.529   -6.544  1.00 13.09 ?  42  TYR   A CG   1 
ATOM   1069 C CD1  . TYR   A 1 42  ? 33.426 5.327   -7.079  1.00 13.98 ?  42  TYR   A CD1  1 
ATOM   1070 C CD2  . TYR   A 1 42  ? 31.072 5.408   -7.393  1.00 14.50 ?  42  TYR   A CD2  1 
ATOM   1071 C CE1  . TYR   A 1 42  ? 33.599 5.022   -8.422  1.00 14.47 ?  42  TYR   A CE1  1 
ATOM   1072 C CE2  . TYR   A 1 42  ? 31.237 5.119   -8.736  1.00 15.34 ?  42  TYR   A CE2  1 
ATOM   1073 C CZ   . TYR   A 1 42  ? 32.503 4.925   -9.246  1.00 15.17 ?  42  TYR   A CZ   1 
ATOM   1074 O OH   . TYR   A 1 42  ? 32.665 4.627   -10.579 1.00 17.07 ?  42  TYR   A OH   1 
ATOM   1075 H H    A TYR   A 1 42  ? 30.781 3.625   -4.887  0.70 13.48 ?  42  TYR   A H    1 
ATOM   1076 H H    B TYR   A 1 42  ? 30.768 3.660   -4.826  0.30 13.48 ?  42  TYR   A H    1 
ATOM   1077 H HA   . TYR   A 1 42  ? 33.266 4.462   -4.260  1.00 13.63 ?  42  TYR   A HA   1 
ATOM   1078 H HB2  . TYR   A 1 42  ? 31.046 6.079   -4.933  1.00 14.67 ?  42  TYR   A HB2  1 
ATOM   1079 H HB3  . TYR   A 1 42  ? 32.551 6.580   -4.845  1.00 14.67 ?  42  TYR   A HB3  1 
ATOM   1080 H HD1  . TYR   A 1 42  ? 34.172 5.388   -6.525  1.00 16.77 ?  42  TYR   A HD1  1 
ATOM   1081 H HD2  . TYR   A 1 42  ? 30.216 5.544   -7.056  1.00 17.40 ?  42  TYR   A HD2  1 
ATOM   1082 H HE1  . TYR   A 1 42  ? 34.456 4.894   -8.769  1.00 17.37 ?  42  TYR   A HE1  1 
ATOM   1083 H HE2  . TYR   A 1 42  ? 30.496 5.052   -9.296  1.00 18.41 ?  42  TYR   A HE2  1 
ATOM   1084 H HH   . TYR   A 1 42  ? 33.482 4.530   -10.759 1.00 20.49 ?  42  TYR   A HH   1 
ATOM   1085 N N    . LEU   A 1 43  ? 31.207 4.252   -2.021  1.00 10.68 ?  43  LEU   A N    1 
ATOM   1086 C CA   . LEU   A 1 43  ? 30.767 4.584   -0.668  1.00 10.61 ?  43  LEU   A CA   1 
ATOM   1087 C C    . LEU   A 1 43  ? 30.279 6.027   -0.565  1.00 10.85 ?  43  LEU   A C    1 
ATOM   1088 O O    . LEU   A 1 43  ? 30.543 6.725   0.414   1.00 11.99 ?  43  LEU   A O    1 
ATOM   1089 C CB   . LEU   A 1 43  ? 31.826 4.271   0.390   1.00 11.28 ?  43  LEU   A CB   1 
ATOM   1090 C CG   . LEU   A 1 43  ? 32.318 2.821   0.477   1.00 11.35 ?  43  LEU   A CG   1 
ATOM   1091 C CD1  . LEU   A 1 43  ? 33.369 2.704   1.571   1.00 12.30 ?  43  LEU   A CD1  1 
ATOM   1092 C CD2  . LEU   A 1 43  ? 31.169 1.843   0.715   1.00 11.80 ?  43  LEU   A CD2  1 
ATOM   1093 H H    . LEU   A 1 43  ? 30.851 3.525   -2.322  1.00 12.81 ?  43  LEU   A H    1 
ATOM   1094 H HA   . LEU   A 1 43  ? 30.001 4.021   -0.461  1.00 12.73 ?  43  LEU   A HA   1 
ATOM   1095 H HB2  . LEU   A 1 43  ? 32.597 4.829   0.221   1.00 13.54 ?  43  LEU   A HB2  1 
ATOM   1096 H HB3  . LEU   A 1 43  ? 31.454 4.493   1.261   1.00 13.54 ?  43  LEU   A HB3  1 
ATOM   1097 H HG   . LEU   A 1 43  ? 32.745 2.586   -0.362  1.00 13.62 ?  43  LEU   A HG   1 
ATOM   1098 H HD11 . LEU   A 1 43  ? 33.679 1.785   1.619   1.00 14.75 ?  43  LEU   A HD11 1 
ATOM   1099 H HD12 . LEU   A 1 43  ? 34.113 3.292   1.366   1.00 14.75 ?  43  LEU   A HD12 1 
ATOM   1100 H HD13 . LEU   A 1 43  ? 32.973 2.961   2.421   1.00 14.75 ?  43  LEU   A HD13 1 
ATOM   1101 H HD21 . LEU   A 1 43  ? 31.541 0.958   0.861   1.00 14.16 ?  43  LEU   A HD21 1 
ATOM   1102 H HD22 . LEU   A 1 43  ? 30.674 2.128   1.496   1.00 14.16 ?  43  LEU   A HD22 1 
ATOM   1103 H HD23 . LEU   A 1 43  ? 30.598 1.839   -0.065  1.00 14.16 ?  43  LEU   A HD23 1 
ATOM   1104 N N    A LYS   A 1 44  ? 29.563 6.479   -1.595  0.70 10.65 ?  44  LYS   A N    1 
ATOM   1105 N N    B LYS   A 1 44  ? 29.530 6.459   -1.581  0.30 11.58 ?  44  LYS   A N    1 
ATOM   1106 C CA   A LYS   A 1 44  ? 28.932 7.798   -1.587  0.70 10.94 ?  44  LYS   A CA   1 
ATOM   1107 C CA   B LYS   A 1 44  ? 28.851 7.754   -1.569  0.30 12.67 ?  44  LYS   A CA   1 
ATOM   1108 C C    A LYS   A 1 44  ? 27.505 7.619   -1.082  0.70 10.24 ?  44  LYS   A C    1 
ATOM   1109 C C    B LYS   A 1 44  ? 27.432 7.523   -1.068  0.30 11.92 ?  44  LYS   A C    1 
ATOM   1110 O O    A LYS   A 1 44  ? 26.635 7.114   -1.796  0.70 11.52 ?  44  LYS   A O    1 
ATOM   1111 O O    B LYS   A 1 44  ? 26.570 7.027   -1.799  0.30 12.10 ?  44  LYS   A O    1 
ATOM   1112 C CB   A LYS   A 1 44  ? 28.978 8.425   -2.973  0.70 13.29 ?  44  LYS   A CB   1 
ATOM   1113 C CB   B LYS   A 1 44  ? 28.862 8.381   -2.958  0.30 14.92 ?  44  LYS   A CB   1 
ATOM   1114 C CG   A LYS   A 1 44  ? 30.361 8.885   -3.400  0.70 16.95 ?  44  LYS   A CG   1 
ATOM   1115 C CG   B LYS   A 1 44  ? 30.226 8.872   -3.409  0.30 17.58 ?  44  LYS   A CG   1 
ATOM   1116 C CD   A LYS   A 1 44  ? 31.021 9.805   -2.372  0.70 22.16 ?  44  LYS   A CD   1 
ATOM   1117 C CD   B LYS   A 1 44  ? 30.884 9.747   -2.350  0.30 20.66 ?  44  LYS   A CD   1 
ATOM   1118 C CE   A LYS   A 1 44  ? 32.346 10.347  -2.879  0.70 25.47 ?  44  LYS   A CE   1 
ATOM   1119 C CE   B LYS   A 1 44  ? 32.173 10.360  -2.858  0.30 22.68 ?  44  LYS   A CE   1 
ATOM   1120 N NZ   A LYS   A 1 44  ? 33.165 10.942  -1.789  0.70 27.17 ?  44  LYS   A NZ   1 
ATOM   1121 N NZ   B LYS   A 1 44  ? 32.905 11.076  -1.779  0.30 23.87 ?  44  LYS   A NZ   1 
ATOM   1122 H H    A LYS   A 1 44  ? 29.434 6.032   -2.321  0.70 12.77 ?  44  LYS   A H    1 
ATOM   1123 H H    B LYS   A 1 44  ? 29.394 6.008   -2.301  0.30 13.89 ?  44  LYS   A H    1 
ATOM   1124 H HA   A LYS   A 1 44  ? 29.396 8.370   -0.958  0.70 13.13 ?  44  LYS   A HA   1 
ATOM   1125 H HA   B LYS   A 1 44  ? 29.291 8.347   -0.940  0.30 15.20 ?  44  LYS   A HA   1 
ATOM   1126 H HB2  A LYS   A 1 44  ? 28.671 7.774   -3.622  0.70 15.94 ?  44  LYS   A HB2  1 
ATOM   1127 H HB2  B LYS   A 1 44  ? 28.561 7.720   -3.602  0.30 17.91 ?  44  LYS   A HB2  1 
ATOM   1128 H HB3  A LYS   A 1 44  ? 28.395 9.200   -2.983  0.70 15.94 ?  44  LYS   A HB3  1 
ATOM   1129 H HB3  B LYS   A 1 44  ? 28.261 9.142   -2.964  0.30 17.91 ?  44  LYS   A HB3  1 
ATOM   1130 H HG2  A LYS   A 1 44  ? 30.933 8.110   -3.521  0.70 20.34 ?  44  LYS   A HG2  1 
ATOM   1131 H HG2  B LYS   A 1 44  ? 30.802 8.109   -3.576  0.30 21.09 ?  44  LYS   A HG2  1 
ATOM   1132 H HG3  A LYS   A 1 44  ? 30.290 9.377   -4.237  0.70 20.34 ?  44  LYS   A HG3  1 
ATOM   1133 H HG3  B LYS   A 1 44  ? 30.125 9.399   -4.219  0.30 21.09 ?  44  LYS   A HG3  1 
ATOM   1134 H HD2  A LYS   A 1 44  ? 30.425 10.547  -2.184  0.70 26.59 ?  44  LYS   A HD2  1 
ATOM   1135 H HD2  B LYS   A 1 44  ? 30.272 10.458  -2.098  0.30 24.79 ?  44  LYS   A HD2  1 
ATOM   1136 H HD3  A LYS   A 1 44  ? 31.195 9.300   -1.561  0.70 26.59 ?  44  LYS   A HD3  1 
ATOM   1137 H HD3  B LYS   A 1 44  ? 31.103 9.202   -1.575  0.30 24.79 ?  44  LYS   A HD3  1 
ATOM   1138 H HE2  A LYS   A 1 44  ? 32.852 9.620   -3.276  0.70 30.57 ?  44  LYS   A HE2  1 
ATOM   1139 H HE2  B LYS   A 1 44  ? 32.747 9.655   -3.199  0.30 27.22 ?  44  LYS   A HE2  1 
ATOM   1140 H HE3  A LYS   A 1 44  ? 32.172 11.033  -3.540  0.70 30.57 ?  44  LYS   A HE3  1 
ATOM   1141 H HE3  B LYS   A 1 44  ? 31.968 10.995  -3.560  0.30 27.22 ?  44  LYS   A HE3  1 
ATOM   1142 H HZ1  A LYS   A 1 44  ? 33.931 11.248  -2.119  0.70 32.60 ?  44  LYS   A HZ1  1 
ATOM   1143 H HZ1  B LYS   A 1 44  ? 33.657 11.425  -2.104  0.30 28.64 ?  44  LYS   A HZ1  1 
ATOM   1144 H HZ2  A LYS   A 1 44  ? 32.722 11.618  -1.412  0.70 32.60 ?  44  LYS   A HZ2  1 
ATOM   1145 H HZ2  B LYS   A 1 44  ? 32.400 11.730  -1.451  0.30 28.64 ?  44  LYS   A HZ2  1 
ATOM   1146 H HZ3  A LYS   A 1 44  ? 33.338 10.330  -1.168  0.70 32.60 ?  44  LYS   A HZ3  1 
ATOM   1147 H HZ3  B LYS   A 1 44  ? 33.110 10.510  -1.122  0.30 28.64 ?  44  LYS   A HZ3  1 
ATOM   1148 N N    A HIS   A 1 45  ? 27.274 8.015   0.166   0.70 9.97  ?  45  HIS   A N    1 
ATOM   1149 N N    B HIS   A 1 45  ? 27.195 7.876   0.192   0.30 11.59 ?  45  HIS   A N    1 
ATOM   1150 C CA   A HIS   A 1 45  ? 26.046 7.655   0.874   0.70 10.44 ?  45  HIS   A CA   1 
ATOM   1151 C CA   B HIS   A 1 45  ? 25.927 7.600   0.864   0.30 11.51 ?  45  HIS   A CA   1 
ATOM   1152 C C    A HIS   A 1 45  ? 25.005 8.769   0.737   0.70 11.44 ?  45  HIS   A C    1 
ATOM   1153 C C    B HIS   A 1 45  ? 24.989 8.774   0.625   0.30 11.61 ?  45  HIS   A C    1 
ATOM   1154 O O    A HIS   A 1 45  ? 24.620 9.435   1.698   0.70 12.00 ?  45  HIS   A O    1 
ATOM   1155 O O    B HIS   A 1 45  ? 24.929 9.720   1.411   0.30 12.06 ?  45  HIS   A O    1 
ATOM   1156 C CB   A HIS   A 1 45  ? 26.360 7.364   2.331   0.70 10.00 ?  45  HIS   A CB   1 
ATOM   1157 C CB   B HIS   A 1 45  ? 26.176 7.389   2.348   0.30 11.36 ?  45  HIS   A CB   1 
ATOM   1158 C CG   A HIS   A 1 45  ? 27.463 6.372   2.524   0.70 9.84  ?  45  HIS   A CG   1 
ATOM   1159 C CG   B HIS   A 1 45  ? 27.329 6.483   2.636   0.30 10.46 ?  45  HIS   A CG   1 
ATOM   1160 N ND1  A HIS   A 1 45  ? 27.423 5.091   2.008   0.70 10.35 ?  45  HIS   A ND1  1 
ATOM   1161 N ND1  B HIS   A 1 45  ? 27.390 5.187   2.169   0.30 10.88 ?  45  HIS   A ND1  1 
ATOM   1162 C CD2  A HIS   A 1 45  ? 28.649 6.494   3.168   0.70 10.09 ?  45  HIS   A CD2  1 
ATOM   1163 C CD2  B HIS   A 1 45  ? 28.474 6.693   3.328   0.30 9.38  ?  45  HIS   A CD2  1 
ATOM   1164 C CE1  A HIS   A 1 45  ? 28.540 4.466   2.344   0.70 10.36 ?  45  HIS   A CE1  1 
ATOM   1165 C CE1  B HIS   A 1 45  ? 28.522 4.637   2.570   0.30 9.64  ?  45  HIS   A CE1  1 
ATOM   1166 N NE2  A HIS   A 1 45  ? 29.299 5.293   3.045   0.70 10.55 ?  45  HIS   A NE2  1 
ATOM   1167 N NE2  B HIS   A 1 45  ? 29.197 5.528   3.275   0.30 8.82  ?  45  HIS   A NE2  1 
ATOM   1168 H H    A HIS   A 1 45  ? 27.814 8.507   0.630   0.70 11.96 ?  45  HIS   A H    1 
ATOM   1169 H H    B HIS   A 1 45  ? 27.768 8.280   0.690   0.30 13.90 ?  45  HIS   A H    1 
ATOM   1170 H HA   A HIS   A 1 45  ? 25.676 6.857   0.475   0.70 12.53 ?  45  HIS   A HA   1 
ATOM   1171 H HA   B HIS   A 1 45  ? 25.527 6.797   0.492   0.30 13.82 ?  45  HIS   A HA   1 
ATOM   1172 H HB2  A HIS   A 1 45  ? 26.614 8.187   2.772   0.70 12.00 ?  45  HIS   A HB2  1 
ATOM   1173 H HB2  B HIS   A 1 45  ? 26.360 8.249   2.756   0.30 13.64 ?  45  HIS   A HB2  1 
ATOM   1174 H HB3  A HIS   A 1 45  ? 25.561 7.000   2.753   0.70 12.00 ?  45  HIS   A HB3  1 
ATOM   1175 H HB3  B HIS   A 1 45  ? 25.382 6.999   2.742   0.30 13.64 ?  45  HIS   A HB3  1 
ATOM   1176 H HD2  A HIS   A 1 45  ? 28.965 7.252   3.613   0.70 12.10 ?  45  HIS   A HD2  1 
ATOM   1177 H HD2  B HIS   A 1 45  ? 28.720 7.481   3.762   0.30 11.25 ?  45  HIS   A HD2  1 
ATOM   1178 H HE1  A HIS   A 1 45  ? 28.757 3.587   2.135   0.70 12.44 ?  45  HIS   A HE1  1 
ATOM   1179 H HE1  B HIS   A 1 45  ? 28.794 3.771   2.387   0.30 11.56 ?  45  HIS   A HE1  1 
ATOM   1180 H HE2  A HIS   A 1 45  ? 30.077 5.109   3.374   0.70 12.66 ?  45  HIS   A HE2  1 
ATOM   1181 H HE2  B HIS   A 1 45  ? 29.961 5.400   3.642   0.30 10.58 ?  45  HIS   A HE2  1 
ATOM   1182 N N    A GLY   A 1 46  ? 24.536 8.951   -0.493  0.70 12.41 ?  46  GLY   A N    1 
ATOM   1183 N N    B GLY   A 1 46  ? 24.235 8.712   -0.468  0.30 11.33 ?  46  GLY   A N    1 
ATOM   1184 C CA   A GLY   A 1 46  ? 23.740 10.122  -0.815  0.70 13.06 ?  46  GLY   A CA   1 
ATOM   1185 C CA   B GLY   A 1 46  ? 23.411 9.841   -0.846  0.30 11.46 ?  46  GLY   A CA   1 
ATOM   1186 C C    A GLY   A 1 46  ? 22.248 9.984   -0.597  0.70 12.84 ?  46  GLY   A C    1 
ATOM   1187 C C    B GLY   A 1 46  ? 21.959 9.731   -0.433  0.30 11.53 ?  46  GLY   A C    1 
ATOM   1188 O O    A GLY   A 1 46  ? 21.567 10.981  -0.335  0.70 13.87 ?  46  GLY   A O    1 
ATOM   1189 O O    B GLY   A 1 46  ? 21.360 10.713  0.018   0.30 11.95 ?  46  GLY   A O    1 
ATOM   1190 H H    A GLY   A 1 46  ? 24.651 8.413   -1.148  0.70 14.89 ?  46  GLY   A H    1 
ATOM   1191 H H    B GLY   A 1 46  ? 24.183 8.032   -0.999  0.30 13.59 ?  46  GLY   A H    1 
ATOM   1192 H HA2  A GLY   A 1 46  ? 24.045 10.870  -0.276  0.70 15.68 ?  46  GLY   A HA2  1 
ATOM   1193 H HA2  B GLY   A 1 46  ? 23.765 10.644  -0.436  0.30 13.76 ?  46  GLY   A HA2  1 
ATOM   1194 H HA3  A GLY   A 1 46  ? 23.874 10.349  -1.745  0.70 15.68 ?  46  GLY   A HA3  1 
ATOM   1195 H HA3  B GLY   A 1 46  ? 23.447 9.949   -1.805  0.30 13.76 ?  46  GLY   A HA3  1 
ATOM   1196 N N    A GLY   A 1 47  ? 21.722 8.770   -0.726  0.70 12.66 ?  47  GLY   A N    1 
ATOM   1197 N N    B GLY   A 1 47  ? 21.378 8.547   -0.577  0.30 11.65 ?  47  GLY   A N    1 
ATOM   1198 C CA   A GLY   A 1 47  ? 20.287 8.560   -0.724  0.70 12.54 ?  47  GLY   A CA   1 
ATOM   1199 C CA   B GLY   A 1 47  ? 19.964 8.389   -0.329  0.30 11.35 ?  47  GLY   A CA   1 
ATOM   1200 C C    A GLY   A 1 47  ? 19.967 7.121   -0.376  0.70 11.90 ?  47  GLY   A C    1 
ATOM   1201 C C    B GLY   A 1 47  ? 19.626 6.960   0.013   0.30 10.71 ?  47  GLY   A C    1 
ATOM   1202 O O    A GLY   A 1 47  ? 20.857 6.298   -0.149  0.70 12.02 ?  47  GLY   A O    1 
ATOM   1203 O O    B GLY   A 1 47  ? 20.508 6.111   0.166   0.30 10.43 ?  47  GLY   A O    1 
ATOM   1204 H H    A GLY   A 1 47  ? 22.183 8.052   -0.800  0.70 15.19 ?  47  GLY   A H    1 
ATOM   1205 H H    B GLY   A 1 47  ? 21.783 7.818   -0.802  0.30 13.98 ?  47  GLY   A H    1 
ATOM   1206 H HA2  A GLY   A 1 47  ? 19.861 9.146   -0.078  0.70 15.05 ?  47  GLY   A HA2  1 
ATOM   1207 H HA2  B GLY   A 1 47  ? 19.692 8.944   0.416   0.30 13.62 ?  47  GLY   A HA2  1 
ATOM   1208 H HA3  A GLY   A 1 47  ? 19.929 8.752   -1.606  0.70 15.05 ?  47  GLY   A HA3  1 
ATOM   1209 H HA3  B GLY   A 1 47  ? 19.459 8.651   -1.115  0.30 13.62 ?  47  GLY   A HA3  1 
ATOM   1210 N N    A GLY   A 1 48  ? 18.676 6.815   -0.356  0.70 12.04 ?  48  GLY   A N    1 
ATOM   1211 N N    B GLY   A 1 48  ? 18.326 6.704   0.131   0.30 10.84 ?  48  GLY   A N    1 
ATOM   1212 C CA   A GLY   A 1 48  ? 18.264 5.481   0.024   0.70 12.04 ?  48  GLY   A CA   1 
ATOM   1213 C CA   B GLY   A 1 48  ? 17.892 5.378   0.515   0.30 10.28 ?  48  GLY   A CA   1 
ATOM   1214 C C    A GLY   A 1 48  ? 18.656 5.165   1.457   0.70 11.53 ?  48  GLY   A C    1 
ATOM   1215 C C    B GLY   A 1 48  ? 18.474 4.985   1.857   0.30 10.33 ?  48  GLY   A C    1 
ATOM   1216 O O    A GLY   A 1 48  ? 18.803 6.056   2.308   0.70 11.50 ?  48  GLY   A O    1 
ATOM   1217 O O    B GLY   A 1 48  ? 18.632 5.810   2.767   0.30 10.31 ?  48  GLY   A O    1 
ATOM   1218 H H    A GLY   A 1 48  ? 18.034 7.350   -0.554  0.70 14.45 ?  48  GLY   A H    1 
ATOM   1219 H H    B GLY   A 1 48  ? 17.682 7.269   -0.001  0.30 13.01 ?  48  GLY   A H    1 
ATOM   1220 H HA2  A GLY   A 1 48  ? 17.310 5.390   -0.064  0.70 14.45 ?  48  GLY   A HA2  1 
ATOM   1221 H HA2  B GLY   A 1 48  ? 16.927 5.362   0.563   0.30 12.34 ?  48  GLY   A HA2  1 
ATOM   1222 H HA3  A GLY   A 1 48  ? 18.699 4.829   -0.550  0.70 14.45 ?  48  GLY   A HA3  1 
ATOM   1223 H HA3  B GLY   A 1 48  ? 18.182 4.729   -0.149  0.30 12.34 ?  48  GLY   A HA3  1 
ATOM   1224 N N    A VAL   A 1 49  ? 18.832 3.868   1.727   0.70 11.68 ?  49  VAL   A N    1 
ATOM   1225 N N    B VAL   A 1 49  ? 18.799 3.698   1.980   0.30 10.33 ?  49  VAL   A N    1 
ATOM   1226 C CA   A VAL   A 1 49  ? 19.270 3.424   3.049   0.70 11.67 ?  49  VAL   A CA   1 
ATOM   1227 C CA   B VAL   A 1 49  ? 19.407 3.185   3.204   0.30 10.46 ?  49  VAL   A CA   1 
ATOM   1228 C C    A VAL   A 1 49  ? 20.591 4.090   3.437   0.70 10.68 ?  49  VAL   A C    1 
ATOM   1229 C C    B VAL   A 1 49  ? 20.696 3.931   3.515   0.30 10.01 ?  49  VAL   A C    1 
ATOM   1230 O O    A VAL   A 1 49  ? 20.767 4.533   4.576   0.70 11.14 ?  49  VAL   A O    1 
ATOM   1231 O O    B VAL   A 1 49  ? 20.955 4.294   4.668   0.30 9.43  ?  49  VAL   A O    1 
ATOM   1232 C CB   A VAL   A 1 49  ? 19.368 1.884   3.086   0.70 12.88 ?  49  VAL   A CB   1 
ATOM   1233 C CB   B VAL   A 1 49  ? 19.655 1.672   3.082   0.30 10.79 ?  49  VAL   A CB   1 
ATOM   1234 C CG1  A VAL   A 1 49  ? 20.092 1.410   4.349   0.70 13.38 ?  49  VAL   A CG1  1 
ATOM   1235 C CG1  B VAL   A 1 49  ? 20.569 1.202   4.207   0.30 10.15 ?  49  VAL   A CG1  1 
ATOM   1236 C CG2  A VAL   A 1 49  ? 17.980 1.252   2.994   0.70 14.45 ?  49  VAL   A CG2  1 
ATOM   1237 C CG2  B VAL   A 1 49  ? 18.340 0.919   3.093   0.30 11.39 ?  49  VAL   A CG2  1 
ATOM   1238 H H    A VAL   A 1 49  ? 18.707 3.227   1.166   0.70 14.01 ?  49  VAL   A H    1 
ATOM   1239 H H    B VAL   A 1 49  ? 18.680 3.108   1.370   0.30 12.40 ?  49  VAL   A H    1 
ATOM   1240 H HA   A VAL   A 1 49  ? 18.611 3.680   3.707   0.70 14.00 ?  49  VAL   A HA   1 
ATOM   1241 H HA   B VAL   A 1 49  ? 18.799 3.326   3.946   0.30 12.55 ?  49  VAL   A HA   1 
ATOM   1242 H HB   A VAL   A 1 49  ? 19.886 1.575   2.324   0.70 15.46 ?  49  VAL   A HB   1 
ATOM   1243 H HB   B VAL   A 1 49  ? 20.101 1.491   2.239   0.30 12.95 ?  49  VAL   A HB   1 
ATOM   1244 H HG11 A VAL   A 1 49  ? 19.902 0.468   4.488   0.70 16.05 ?  49  VAL   A HG11 1 
ATOM   1245 H HG11 B VAL   A 1 49  ? 20.475 0.243   4.308   0.30 12.18 ?  49  VAL   A HG11 1 
ATOM   1246 H HG12 A VAL   A 1 49  ? 21.043 1.544   4.244   0.70 16.05 ?  49  VAL   A HG12 1 
ATOM   1247 H HG12 B VAL   A 1 49  ? 21.491 1.418   3.983   0.30 12.18 ?  49  VAL   A HG12 1 
ATOM   1248 H HG13 A VAL   A 1 49  ? 19.762 1.923   5.107   0.70 16.05 ?  49  VAL   A HG13 1 
ATOM   1249 H HG13 B VAL   A 1 49  ? 20.315 1.647   5.030   0.30 12.18 ?  49  VAL   A HG13 1 
ATOM   1250 H HG21 A VAL   A 1 49  ? 18.067 0.285   3.017   0.70 17.34 ?  49  VAL   A HG21 1 
ATOM   1251 H HG21 B VAL   A 1 49  ? 18.518 -0.026  2.984   0.30 13.67 ?  49  VAL   A HG21 1 
ATOM   1252 H HG22 A VAL   A 1 49  ? 17.448 1.553   3.747   0.70 17.34 ?  49  VAL   A HG22 1 
ATOM   1253 H HG22 B VAL   A 1 49  ? 17.894 1.079   3.939   0.30 13.67 ?  49  VAL   A HG22 1 
ATOM   1254 H HG23 A VAL   A 1 49  ? 17.567 1.527   2.163   0.70 17.34 ?  49  VAL   A HG23 1 
ATOM   1255 H HG23 B VAL   A 1 49  ? 17.790 1.241   2.362   0.30 13.67 ?  49  VAL   A HG23 1 
ATOM   1256 N N    . ALA   A 1 50  ? 21.546 4.131   2.504   1.00 10.31 ?  50  ALA   A N    1 
ATOM   1257 C CA   . ALA   A 1 50  ? 22.865 4.691   2.788   1.00 10.39 ?  50  ALA   A CA   1 
ATOM   1258 C C    . ALA   A 1 50  ? 22.771 6.146   3.230   1.00 10.20 ?  50  ALA   A C    1 
ATOM   1259 O O    . ALA   A 1 50  ? 23.403 6.553   4.215   1.00 10.49 ?  50  ALA   A O    1 
ATOM   1260 C CB   . ALA   A 1 50  ? 23.758 4.568   1.557   1.00 10.31 ?  50  ALA   A CB   1 
ATOM   1261 H H    A ALA   A 1 50  ? 21.450 3.842   1.698   0.70 12.38 ?  50  ALA   A H    1 
ATOM   1262 H H    B ALA   A 1 50  ? 21.388 3.954   1.676   0.30 12.38 ?  50  ALA   A H    1 
ATOM   1263 H HA   . ALA   A 1 50  ? 23.275 4.186   3.509   1.00 12.47 ?  50  ALA   A HA   1 
ATOM   1264 H HB1  . ALA   A 1 50  ? 24.629 4.944   1.761   1.00 12.37 ?  50  ALA   A HB1  1 
ATOM   1265 H HB2  . ALA   A 1 50  ? 23.848 3.633   1.320   1.00 12.37 ?  50  ALA   A HB2  1 
ATOM   1266 H HB3  . ALA   A 1 50  ? 23.351 5.058   0.824   1.00 12.37 ?  50  ALA   A HB3  1 
ATOM   1267 N N    . GLY   A 1 51  ? 21.991 6.946   2.505   1.00 10.72 ?  51  GLY   A N    1 
ATOM   1268 C CA   . GLY   A 1 51  ? 21.831 8.333   2.896   1.00 11.13 ?  51  GLY   A CA   1 
ATOM   1269 C C    . GLY   A 1 51  ? 21.228 8.466   4.277   1.00 11.06 ?  51  GLY   A C    1 
ATOM   1270 O O    . GLY   A 1 51  ? 21.613 9.351   5.046   1.00 11.60 ?  51  GLY   A O    1 
ATOM   1271 H H    . GLY   A 1 51  ? 21.556 6.711   1.795   1.00 12.86 ?  51  GLY   A H    1 
ATOM   1272 H HA2  . GLY   A 1 51  ? 22.695 8.769   2.893   1.00 13.36 ?  51  GLY   A HA2  1 
ATOM   1273 H HA3  . GLY   A 1 51  ? 21.253 8.785   2.261   1.00 13.36 ?  51  GLY   A HA3  1 
ATOM   1274 N N    . ALA   A 1 52  ? 20.262 7.599   4.603   1.00 11.20 ?  52  ALA   A N    1 
ATOM   1275 C CA   . ALA   A 1 52  ? 19.620 7.652   5.911   1.00 12.01 ?  52  ALA   A CA   1 
ATOM   1276 C C    . ALA   A 1 52  ? 20.576 7.230   7.026   1.00 11.15 ?  52  ALA   A C    1 
ATOM   1277 O O    . ALA   A 1 52  ? 20.643 7.881   8.074   1.00 12.14 ?  52  ALA   A O    1 
ATOM   1278 C CB   . ALA   A 1 52  ? 18.358 6.789   5.905   1.00 13.18 ?  52  ALA   A CB   1 
ATOM   1279 H H    . ALA   A 1 52  ? 19.977 6.961   4.091   1.00 13.44 ?  52  ALA   A H    1 
ATOM   1280 H HA   . ALA   A 1 52  ? 19.350 8.560   6.084   1.00 14.41 ?  52  ALA   A HA   1 
ATOM   1281 H HB1  . ALA   A 1 52  ? 17.930 6.844   6.777   1.00 15.82 ?  52  ALA   A HB1  1 
ATOM   1282 H HB2  . ALA   A 1 52  ? 17.749 7.121   5.223   1.00 15.82 ?  52  ALA   A HB2  1 
ATOM   1283 H HB3  . ALA   A 1 52  ? 18.594 5.869   5.714   1.00 15.82 ?  52  ALA   A HB3  1 
ATOM   1284 N N    A LEU   A 1 53  ? 21.309 6.131   6.835   0.70 10.80 ?  53  LEU   A N    1 
ATOM   1285 N N    B LEU   A 1 53  ? 21.305 6.125   6.825   0.30 10.79 ?  53  LEU   A N    1 
ATOM   1286 C CA   A LEU   A 1 53  ? 22.278 5.725   7.852   0.70 11.12 ?  53  LEU   A CA   1 
ATOM   1287 C CA   B LEU   A 1 53  ? 22.289 5.693   7.816   0.30 10.83 ?  53  LEU   A CA   1 
ATOM   1288 C C    A LEU   A 1 53  ? 23.331 6.805   8.050   0.70 10.64 ?  53  LEU   A C    1 
ATOM   1289 C C    B LEU   A 1 53  ? 23.336 6.776   8.040   0.30 10.62 ?  53  LEU   A C    1 
ATOM   1290 O O    A LEU   A 1 53  ? 23.664 7.166   9.183   0.70 11.93 ?  53  LEU   A O    1 
ATOM   1291 O O    B LEU   A 1 53  ? 23.673 7.107   9.182   0.30 11.25 ?  53  LEU   A O    1 
ATOM   1292 C CB   A LEU   A 1 53  ? 22.930 4.389   7.479   0.70 11.68 ?  53  LEU   A CB   1 
ATOM   1293 C CB   B LEU   A 1 53  ? 22.968 4.391   7.368   0.30 10.95 ?  53  LEU   A CB   1 
ATOM   1294 C CG   A LEU   A 1 53  ? 21.996 3.166   7.487   0.70 12.10 ?  53  LEU   A CG   1 
ATOM   1295 C CG   B LEU   A 1 53  ? 22.274 3.033   7.561   0.30 10.74 ?  53  LEU   A CG   1 
ATOM   1296 C CD1  A LEU   A 1 53  ? 22.686 1.954   6.872   0.70 12.20 ?  53  LEU   A CD1  1 
ATOM   1297 C CD1  B LEU   A 1 53  ? 23.123 1.925   6.937   0.30 10.80 ?  53  LEU   A CD1  1 
ATOM   1298 C CD2  A LEU   A 1 53  ? 21.513 2.843   8.891   0.70 13.28 ?  53  LEU   A CD2  1 
ATOM   1299 C CD2  B LEU   A 1 53  ? 22.015 2.727   9.028   0.30 10.60 ?  53  LEU   A CD2  1 
ATOM   1300 H H    A LEU   A 1 53  ? 21.263 5.611   6.146   0.70 12.96 ?  53  LEU   A H    1 
ATOM   1301 H H    B LEU   A 1 53  ? 21.250 5.616   6.133   0.30 12.94 ?  53  LEU   A H    1 
ATOM   1302 H HA   A LEU   A 1 53  ? 21.814 5.602   8.694   0.70 13.35 ?  53  LEU   A HA   1 
ATOM   1303 H HA   B LEU   A 1 53  ? 21.843 5.528   8.661   0.30 12.99 ?  53  LEU   A HA   1 
ATOM   1304 H HB2  A LEU   A 1 53  ? 23.303 4.466   6.584   0.70 14.02 ?  53  LEU   A HB2  1 
ATOM   1305 H HB2  B LEU   A 1 53  ? 23.143 4.469   6.418   0.30 13.15 ?  53  LEU   A HB2  1 
ATOM   1306 H HB3  A LEU   A 1 53  ? 23.647 4.209   8.109   0.70 14.02 ?  53  LEU   A HB3  1 
ATOM   1307 H HB3  B LEU   A 1 53  ? 23.813 4.327   7.836   0.30 13.15 ?  53  LEU   A HB3  1 
ATOM   1308 H HG   A LEU   A 1 53  ? 21.221 3.370   6.940   0.70 14.52 ?  53  LEU   A HG   1 
ATOM   1309 H HG   B LEU   A 1 53  ? 21.423 3.042   7.098   0.30 12.89 ?  53  LEU   A HG   1 
ATOM   1310 H HD11 A LEU   A 1 53  ? 22.072 1.203   6.889   0.70 14.64 ?  53  LEU   A HD11 1 
ATOM   1311 H HD11 B LEU   A 1 53  ? 22.676 1.072   7.066   0.30 12.96 ?  53  LEU   A HD11 1 
ATOM   1312 H HD12 A LEU   A 1 53  ? 22.934 2.159   5.957   0.70 14.64 ?  53  LEU   A HD12 1 
ATOM   1313 H HD12 B LEU   A 1 53  ? 23.230 2.101   5.989   0.30 12.96 ?  53  LEU   A HD12 1 
ATOM   1314 H HD13 A LEU   A 1 53  ? 23.478 1.746   7.391   0.70 14.64 ?  53  LEU   A HD13 1 
ATOM   1315 H HD13 B LEU   A 1 53  ? 23.991 1.910   7.371   0.30 12.96 ?  53  LEU   A HD13 1 
ATOM   1316 H HD21 A LEU   A 1 53  ? 20.979 2.034   8.860   0.70 15.93 ?  53  LEU   A HD21 1 
ATOM   1317 H HD21 B LEU   A 1 53  ? 21.443 1.945   9.091   0.30 12.72 ?  53  LEU   A HD21 1 
ATOM   1318 H HD22 A LEU   A 1 53  ? 22.281 2.713   9.467   0.70 15.93 ?  53  LEU   A HD22 1 
ATOM   1319 H HD22 B LEU   A 1 53  ? 22.859 2.557   9.470   0.30 12.72 ?  53  LEU   A HD22 1 
ATOM   1320 H HD23 A LEU   A 1 53  ? 20.975 3.581   9.218   0.70 15.93 ?  53  LEU   A HD23 1 
ATOM   1321 H HD23 B LEU   A 1 53  ? 21.575 3.489   9.436   0.30 12.72 ?  53  LEU   A HD23 1 
ATOM   1322 N N    . ASN   A 1 54  ? 23.861 7.342   6.953   1.00 10.26 ?  54  ASN   A N    1 
ATOM   1323 C CA   . ASN   A 1 54  ? 24.914 8.338   7.084   1.00 10.52 ?  54  ASN   A CA   1 
ATOM   1324 C C    . ASN   A 1 54  ? 24.406 9.581   7.811   1.00 11.27 ?  54  ASN   A C    1 
ATOM   1325 O O    . ASN   A 1 54  ? 25.095 10.127  8.683   1.00 11.47 ?  54  ASN   A O    1 
ATOM   1326 C CB   . ASN   A 1 54  ? 25.472 8.704   5.720   1.00 10.79 ?  54  ASN   A CB   1 
ATOM   1327 C CG   . ASN   A 1 54  ? 26.486 9.807   5.827   1.00 11.00 ?  54  ASN   A CG   1 
ATOM   1328 O OD1  . ASN   A 1 54  ? 27.499 9.660   6.527   1.00 10.82 ?  54  ASN   A OD1  1 
ATOM   1329 N ND2  . ASN   A 1 54  ? 26.224 10.932  5.176   1.00 11.35 ?  54  ASN   A ND2  1 
ATOM   1330 H H    A ASN   A 1 54  ? 23.633 7.148   6.146   0.70 12.31 ?  54  ASN   A H    1 
ATOM   1331 H H    B ASN   A 1 54  ? 23.618 7.171   6.146   0.30 12.31 ?  54  ASN   A H    1 
ATOM   1332 H HA   . ASN   A 1 54  ? 25.633 7.961   7.609   1.00 12.63 ?  54  ASN   A HA   1 
ATOM   1333 H HB2  . ASN   A 1 54  ? 25.907 7.921   5.334   1.00 12.95 ?  54  ASN   A HB2  1 
ATOM   1334 H HB3  . ASN   A 1 54  ? 24.751 8.999   5.143   1.00 12.95 ?  54  ASN   A HB3  1 
ATOM   1335 H HD21 . ASN   A 1 54  ? 26.773 11.589  5.220   1.00 13.62 ?  54  ASN   A HD21 1 
ATOM   1336 H HD22 . ASN   A 1 54  ? 25.500 11.002  4.714   1.00 13.62 ?  54  ASN   A HD22 1 
ATOM   1337 N N    . LYS   A 1 55  ? 23.192 10.032  7.472   1.00 11.43 ?  55  LYS   A N    1 
ATOM   1338 C CA   . LYS   A 1 55  ? 22.611 11.188  8.147   1.00 11.85 ?  55  LYS   A CA   1 
ATOM   1339 C C    . LYS   A 1 55  ? 22.523 10.952  9.648   1.00 11.84 ?  55  LYS   A C    1 
ATOM   1340 O O    . LYS   A 1 55  ? 22.807 11.853  10.449  1.00 12.58 ?  55  LYS   A O    1 
ATOM   1341 C CB   . LYS   A 1 55  ? 21.241 11.499  7.537   1.00 13.02 ?  55  LYS   A CB   1 
ATOM   1342 C CG   . LYS   A 1 55  ? 20.492 12.651  8.180   1.00 14.54 ?  55  LYS   A CG   1 
ATOM   1343 C CD   . LYS   A 1 55  ? 19.185 12.933  7.425   1.00 15.84 ?  55  LYS   A CD   1 
ATOM   1344 C CE   . LYS   A 1 55  ? 18.351 14.014  8.102   1.00 17.73 ?  55  LYS   A CE   1 
ATOM   1345 N NZ   . LYS   A 1 55  ? 17.031 14.210  7.438   1.00 18.57 ?  55  LYS   A NZ   1 
ATOM   1346 H H    . LYS   A 1 55  ? 22.681 9.679   6.868   1.00 13.72 ?  55  LYS   A H    1 
ATOM   1347 H HA   . LYS   A 1 55  ? 23.183 11.953  8.001   1.00 14.22 ?  55  LYS   A HA   1 
ATOM   1348 H HB2  . LYS   A 1 55  ? 21.368 11.723  6.602   1.00 15.62 ?  55  LYS   A HB2  1 
ATOM   1349 H HB3  . LYS   A 1 55  ? 20.684 10.710  7.611   1.00 15.62 ?  55  LYS   A HB3  1 
ATOM   1350 H HG2  . LYS   A 1 55  ? 20.267 12.416  9.096   1.00 17.45 ?  55  LYS   A HG2  1 
ATOM   1351 H HG3  . LYS   A 1 55  ? 21.039 13.447  8.158   1.00 17.45 ?  55  LYS   A HG3  1 
ATOM   1352 H HD2  . LYS   A 1 55  ? 19.400 13.231  6.526   1.00 19.01 ?  55  LYS   A HD2  1 
ATOM   1353 H HD3  . LYS   A 1 55  ? 18.658 12.118  7.386   1.00 19.01 ?  55  LYS   A HD3  1 
ATOM   1354 H HE2  . LYS   A 1 55  ? 18.189 13.756  9.024   1.00 21.28 ?  55  LYS   A HE2  1 
ATOM   1355 H HE3  . LYS   A 1 55  ? 18.833 14.853  8.069   1.00 21.28 ?  55  LYS   A HE3  1 
ATOM   1356 H HZ1  . LYS   A 1 55  ? 16.496 14.690  7.964   1.00 22.28 ?  55  LYS   A HZ1  1 
ATOM   1357 H HZ2  . LYS   A 1 55  ? 17.138 14.641  6.667   1.00 22.28 ?  55  LYS   A HZ2  1 
ATOM   1358 H HZ3  . LYS   A 1 55  ? 16.647 13.422  7.281   1.00 22.28 ?  55  LYS   A HZ3  1 
ATOM   1359 N N    . ALA   A 1 56  ? 22.137 9.737   10.049  1.00 12.32 ?  56  ALA   A N    1 
ATOM   1360 C CA   . ALA   A 1 56  ? 22.018 9.402   11.462  1.00 13.17 ?  56  ALA   A CA   1 
ATOM   1361 C C    . ALA   A 1 56  ? 23.360 9.427   12.186  1.00 13.14 ?  56  ALA   A C    1 
ATOM   1362 O O    . ALA   A 1 56  ? 23.383 9.614   13.405  1.00 14.45 ?  56  ALA   A O    1 
ATOM   1363 C CB   . ALA   A 1 56  ? 21.335 8.037   11.628  1.00 14.08 ?  56  ALA   A CB   1 
ATOM   1364 H H    . ALA   A 1 56  ? 21.937 9.091   9.518   1.00 14.79 ?  56  ALA   A H    1 
ATOM   1365 H HA   . ALA   A 1 56  ? 21.450 10.055  11.890  1.00 15.80 ?  56  ALA   A HA   1 
ATOM   1366 H HB1  . ALA   A 1 56  ? 21.266 7.829   12.577  1.00 16.89 ?  56  ALA   A HB1  1 
ATOM   1367 H HB2  . ALA   A 1 56  ? 20.449 8.077   11.237  1.00 16.89 ?  56  ALA   A HB2  1 
ATOM   1368 H HB3  . ALA   A 1 56  ? 21.864 7.357   11.183  1.00 16.89 ?  56  ALA   A HB3  1 
ATOM   1369 N N    . THR   A 1 57  ? 24.473 9.247   11.468  1.00 12.19 ?  57  THR   A N    1 
ATOM   1370 C CA   . THR   A 1 57  ? 25.815 9.378   12.043  1.00 12.43 ?  57  THR   A CA   1 
ATOM   1371 C C    . THR   A 1 57  ? 26.365 10.799  11.966  1.00 12.58 ?  57  THR   A C    1 
ATOM   1372 O O    . THR   A 1 57  ? 27.552 11.009  12.254  1.00 13.17 ?  57  THR   A O    1 
ATOM   1373 C CB   . THR   A 1 57  ? 26.828 8.432   11.368  1.00 12.08 ?  57  THR   A CB   1 
ATOM   1374 O OG1  . THR   A 1 57  ? 27.205 8.937   10.075  1.00 11.58 ?  57  THR   A OG1  1 
ATOM   1375 C CG2  . THR   A 1 57  ? 26.292 7.016   11.249  1.00 12.20 ?  57  THR   A CG2  1 
ATOM   1376 H H    . THR   A 1 57  ? 24.476 9.023   10.636  1.00 14.62 ?  57  THR   A H    1 
ATOM   1377 H HA   . THR   A 1 57  ? 25.770 9.116   12.981  1.00 14.91 ?  57  THR   A HA   1 
ATOM   1378 H HB   . THR   A 1 57  ? 27.625 8.385   11.925  1.00 14.50 ?  57  THR   A HB   1 
ATOM   1379 H HG1  . THR   A 1 57  ? 26.528 8.999   9.585   1.00 13.89 ?  57  THR   A HG1  1 
ATOM   1380 H HG21 . THR   A 1 57  ? 27.005 6.400   11.020  1.00 14.64 ?  57  THR   A HG21 1 
ATOM   1381 H HG22 . THR   A 1 57  ? 25.894 6.735   12.090  1.00 14.64 ?  57  THR   A HG22 1 
ATOM   1382 H HG23 . THR   A 1 57  ? 25.611 6.975   10.557  1.00 14.64 ?  57  THR   A HG23 1 
ATOM   1383 N N    . ASN   A 1 58  ? 25.546 11.773  11.571  1.00 13.07 ?  58  ASN   A N    1 
ATOM   1384 C CA   . ASN   A 1 58  ? 26.005 13.156  11.473  1.00 13.92 ?  58  ASN   A CA   1 
ATOM   1385 C C    . ASN   A 1 58  ? 27.153 13.288  10.463  1.00 12.62 ?  58  ASN   A C    1 
ATOM   1386 O O    . ASN   A 1 58  ? 28.051 14.120  10.623  1.00 13.41 ?  58  ASN   A O    1 
ATOM   1387 C CB   . ASN   A 1 58  ? 26.381 13.691  12.868  1.00 16.30 ?  58  ASN   A CB   1 
ATOM   1388 C CG   . ASN   A 1 58  ? 26.788 15.152  12.867  1.00 20.02 ?  58  ASN   A CG   1 
ATOM   1389 O OD1  . ASN   A 1 58  ? 26.167 15.973  12.205  1.00 21.42 ?  58  ASN   A OD1  1 
ATOM   1390 N ND2  . ASN   A 1 58  ? 27.827 15.483  13.632  1.00 21.48 ?  58  ASN   A ND2  1 
ATOM   1391 H H    . ASN   A 1 58  ? 24.722 11.647  11.348  1.00 15.68 ?  58  ASN   A H    1 
ATOM   1392 H HA   . ASN   A 1 58  ? 25.265 13.687  11.148  1.00 16.71 ?  58  ASN   A HA   1 
ATOM   1393 H HB2  . ASN   A 1 58  ? 25.609 13.592  13.458  1.00 19.56 ?  58  ASN   A HB2  1 
ATOM   1394 H HB3  . ASN   A 1 58  ? 27.122 13.179  13.216  1.00 19.56 ?  58  ASN   A HB3  1 
ATOM   1395 H HD21 . ASN   A 1 58  ? 28.086 16.304  13.669  1.00 25.77 ?  58  ASN   A HD21 1 
ATOM   1396 H HD22 . ASN   A 1 58  ? 28.227 14.883  14.091  1.00 25.77 ?  58  ASN   A HD22 1 
ATOM   1397 N N    . ASN   A 1 59  ? 27.135 12.468  9.408   1.00 11.85 ?  59  ASN   A N    1 
ATOM   1398 C CA   . ASN   A 1 59  ? 28.109 12.452  8.308   1.00 11.44 ?  59  ASN   A CA   1 
ATOM   1399 C C    . ASN   A 1 59  ? 29.429 11.770  8.689   1.00 11.27 ?  59  ASN   A C    1 
ATOM   1400 O O    . ASN   A 1 59  ? 30.347 11.736  7.862   1.00 11.32 ?  59  ASN   A O    1 
ATOM   1401 C CB   . ASN   A 1 59  ? 28.392 13.842  7.707   1.00 11.75 ?  59  ASN   A CB   1 
ATOM   1402 C CG   . ASN   A 1 59  ? 28.743 13.783  6.237   1.00 12.31 ?  59  ASN   A CG   1 
ATOM   1403 O OD1  . ASN   A 1 59  ? 28.035 13.159  5.440   1.00 12.24 ?  59  ASN   A OD1  1 
ATOM   1404 N ND2  . ASN   A 1 59  ? 29.834 14.447  5.861   1.00 12.68 ?  59  ASN   A ND2  1 
ATOM   1405 H H    . ASN   A 1 59  ? 26.527 11.872  9.298   1.00 14.22 ?  59  ASN   A H    1 
ATOM   1406 H HA   . ASN   A 1 59  ? 27.727 11.925  7.596   1.00 13.73 ?  59  ASN   A HA   1 
ATOM   1407 H HB2  . ASN   A 1 59  ? 27.604 14.400  7.797   1.00 14.10 ?  59  ASN   A HB2  1 
ATOM   1408 H HB3  . ASN   A 1 59  ? 29.141 14.250  8.173   1.00 14.10 ?  59  ASN   A HB3  1 
ATOM   1409 H HD21 . ASN   A 1 59  ? 30.083 14.448  5.034   1.00 15.22 ?  59  ASN   A HD21 1 
ATOM   1410 H HD22 . ASN   A 1 59  ? 30.310 14.873  6.443   1.00 15.22 ?  59  ASN   A HD22 1 
ATOM   1411 N N    . ALA   A 1 60  ? 29.561 11.225  9.897   1.00 11.20 ?  60  ALA   A N    1 
ATOM   1412 C CA   . ALA   A 1 60  ? 30.800 10.540  10.251  1.00 11.50 ?  60  ALA   A CA   1 
ATOM   1413 C C    . ALA   A 1 60  ? 31.024 9.307   9.383   1.00 11.35 ?  60  ALA   A C    1 
ATOM   1414 O O    . ALA   A 1 60  ? 32.168 8.988   9.038   1.00 11.84 ?  60  ALA   A O    1 
ATOM   1415 C CB   . ALA   A 1 60  ? 30.799 10.173  11.733  1.00 12.17 ?  60  ALA   A CB   1 
ATOM   1416 H H    . ALA   A 1 60  ? 28.962 11.226  10.511  1.00 13.44 ?  60  ALA   A H    1 
ATOM   1417 H HA   . ALA   A 1 60  ? 31.544 11.143  10.096  1.00 13.80 ?  60  ALA   A HA   1 
ATOM   1418 H HB1  . ALA   A 1 60  ? 31.626 9.723   11.950  1.00 14.61 ?  60  ALA   A HB1  1 
ATOM   1419 H HB2  . ALA   A 1 60  ? 30.715 10.988  12.256  1.00 14.61 ?  60  ALA   A HB2  1 
ATOM   1420 H HB3  . ALA   A 1 60  ? 30.044 9.590   11.912  1.00 14.61 ?  60  ALA   A HB3  1 
ATOM   1421 N N    . MET   A 1 61  ? 29.952 8.611   9.003   1.00 10.95 ?  61  MET   A N    1 
ATOM   1422 C CA   . MET   A 1 61  ? 30.093 7.478   8.095   1.00 10.77 ?  61  MET   A CA   1 
ATOM   1423 C C    . MET   A 1 61  ? 30.725 7.907   6.771   1.00 10.71 ?  61  MET   A C    1 
ATOM   1424 O O    . MET   A 1 61  ? 31.619 7.228   6.251   1.00 10.88 ?  61  MET   A O    1 
ATOM   1425 C CB   . MET   A 1 61  ? 28.734 6.810   7.886   1.00 10.91 ?  61  MET   A CB   1 
ATOM   1426 C CG   . MET   A 1 61  ? 28.736 5.664   6.893   1.00 11.42 ?  61  MET   A CG   1 
ATOM   1427 S SD   . MET   A 1 61  ? 27.113 4.910   6.678   1.00 12.42 ?  61  MET   A SD   1 
ATOM   1428 C CE   . MET   A 1 61  ? 26.962 4.012   8.224   1.00 14.03 ?  61  MET   A CE   1 
ATOM   1429 H H    . MET   A 1 61  ? 29.145 8.776   9.250   1.00 13.14 ?  61  MET   A H    1 
ATOM   1430 H HA   . MET   A 1 61  ? 30.677 6.826   8.512   1.00 12.93 ?  61  MET   A HA   1 
ATOM   1431 H HB2  . MET   A 1 61  ? 28.430 6.457   8.738   1.00 13.09 ?  61  MET   A HB2  1 
ATOM   1432 H HB3  . MET   A 1 61  ? 28.106 7.474   7.566   1.00 13.09 ?  61  MET   A HB3  1 
ATOM   1433 H HG2  . MET   A 1 61  ? 29.020 5.991   6.026   1.00 13.71 ?  61  MET   A HG2  1 
ATOM   1434 H HG3  . MET   A 1 61  ? 29.343 4.975   7.203   1.00 13.71 ?  61  MET   A HG3  1 
ATOM   1435 H HE1  . MET   A 1 61  ? 26.120 3.526   8.228   1.00 16.84 ?  61  MET   A HE1  1 
ATOM   1436 H HE2  . MET   A 1 61  ? 27.702 3.390   8.300   1.00 16.84 ?  61  MET   A HE2  1 
ATOM   1437 H HE3  . MET   A 1 61  ? 26.981 4.644   8.959   1.00 16.84 ?  61  MET   A HE3  1 
ATOM   1438 N N    . GLN   A 1 62  ? 30.279 9.039   6.214   1.00 10.67 ?  62  GLN   A N    1 
ATOM   1439 C CA   . GLN   A 1 62  ? 30.834 9.515   4.950   1.00 11.04 ?  62  GLN   A CA   1 
ATOM   1440 C C    . GLN   A 1 62  ? 32.305 9.894   5.090   1.00 11.03 ?  62  GLN   A C    1 
ATOM   1441 O O    . GLN   A 1 62  ? 33.111 9.590   4.204   1.00 11.28 ?  62  GLN   A O    1 
ATOM   1442 C CB   . GLN   A 1 62  ? 30.026 10.705  4.427   1.00 10.75 ?  62  GLN   A CB   1 
ATOM   1443 C CG   . GLN   A 1 62  ? 30.392 11.080  3.000   1.00 10.87 ?  62  GLN   A CG   1 
ATOM   1444 C CD   . GLN   A 1 62  ? 30.067 9.950   2.049   1.00 11.26 ?  62  GLN   A CD   1 
ATOM   1445 O OE1  . GLN   A 1 62  ? 28.890 9.641   1.840   1.00 11.71 ?  62  GLN   A OE1  1 
ATOM   1446 N NE2  . GLN   A 1 62  ? 31.088 9.285   1.517   1.00 11.91 ?  62  GLN   A NE2  1 
ATOM   1447 H H    . GLN   A 1 62  ? 29.658 9.534   6.541   1.00 12.80 ?  62  GLN   A H    1 
ATOM   1448 H HA   . GLN   A 1 62  ? 30.779 8.800   4.297   1.00 13.25 ?  62  GLN   A HA   1 
ATOM   1449 H HB2  . GLN   A 1 62  ? 29.086 10.484  4.450   1.00 12.90 ?  62  GLN   A HB2  1 
ATOM   1450 H HB3  . GLN   A 1 62  ? 30.204 11.477  4.991   1.00 12.90 ?  62  GLN   A HB3  1 
ATOM   1451 H HG2  . GLN   A 1 62  ? 29.876 11.857  2.730   1.00 13.04 ?  62  GLN   A HG2  1 
ATOM   1452 H HG3  . GLN   A 1 62  ? 31.340 11.266  2.941   1.00 13.04 ?  62  GLN   A HG3  1 
ATOM   1453 H HE21 . GLN   A 1 62  ? 31.895 9.522   1.699   1.00 14.30 ?  62  GLN   A HE21 1 
ATOM   1454 H HE22 . GLN   A 1 62  ? 30.943 8.629   0.981   1.00 14.30 ?  62  GLN   A HE22 1 
ATOM   1455 N N    . VAL   A 1 63  ? 32.669 10.577  6.184   1.00 11.24 ?  63  VAL   A N    1 
ATOM   1456 C CA   . VAL   A 1 63  ? 34.059 10.972  6.399   1.00 12.05 ?  63  VAL   A CA   1 
ATOM   1457 C C    . VAL   A 1 63  ? 34.959 9.741   6.457   1.00 11.46 ?  63  VAL   A C    1 
ATOM   1458 O O    . VAL   A 1 63  ? 36.008 9.680   5.799   1.00 11.84 ?  63  VAL   A O    1 
ATOM   1459 C CB   . VAL   A 1 63  ? 34.170 11.842  7.664   1.00 13.67 ?  63  VAL   A CB   1 
ATOM   1460 C CG1  . VAL   A 1 63  ? 35.620 12.093  8.015   1.00 15.35 ?  63  VAL   A CG1  1 
ATOM   1461 C CG2  . VAL   A 1 63  ? 33.434 13.164  7.453   1.00 14.19 ?  63  VAL   A CG2  1 
ATOM   1462 H H    . VAL   A 1 63  ? 32.123 10.819  6.809   1.00 13.49 ?  63  VAL   A H    1 
ATOM   1463 H HA   . VAL   A 1 63  ? 34.340 11.511  5.647   1.00 14.46 ?  63  VAL   A HA   1 
ATOM   1464 H HB   . VAL   A 1 63  ? 33.753 11.381  8.409   1.00 16.40 ?  63  VAL   A HB   1 
ATOM   1465 H HG11 . VAL   A 1 63  ? 35.667 12.829  8.644   1.00 18.42 ?  63  VAL   A HG11 1 
ATOM   1466 H HG12 . VAL   A 1 63  ? 35.994 11.293  8.411   1.00 18.42 ?  63  VAL   A HG12 1 
ATOM   1467 H HG13 . VAL   A 1 63  ? 36.103 12.322  7.204   1.00 18.42 ?  63  VAL   A HG13 1 
ATOM   1468 H HG21 . VAL   A 1 63  ? 33.525 13.710  8.251   1.00 17.02 ?  63  VAL   A HG21 1 
ATOM   1469 H HG22 . VAL   A 1 63  ? 33.822 13.627  6.693   1.00 17.02 ?  63  VAL   A HG22 1 
ATOM   1470 H HG23 . VAL   A 1 63  ? 32.495 12.984  7.284   1.00 17.02 ?  63  VAL   A HG23 1 
ATOM   1471 N N    . GLU   A 1 64  ? 34.547 8.730   7.226   1.00 11.57 ?  64  GLU   A N    1 
ATOM   1472 C CA   . GLU   A 1 64  ? 35.312 7.494   7.313   1.00 11.67 ?  64  GLU   A CA   1 
ATOM   1473 C C    . GLU   A 1 64  ? 35.395 6.808   5.954   1.00 11.20 ?  64  GLU   A C    1 
ATOM   1474 O O    . GLU   A 1 64  ? 36.445 6.268   5.571   1.00 11.64 ?  64  GLU   A O    1 
ATOM   1475 C CB   . GLU   A 1 64  ? 34.631 6.579   8.332   1.00 12.18 ?  64  GLU   A CB   1 
ATOM   1476 C CG   . GLU   A 1 64  ? 35.290 5.235   8.485   1.00 12.73 ?  64  GLU   A CG   1 
ATOM   1477 C CD   . GLU   A 1 64  ? 34.408 4.231   9.201   1.00 13.45 ?  64  GLU   A CD   1 
ATOM   1478 O OE1  . GLU   A 1 64  ? 33.170 4.319   9.058   1.00 14.00 ?  64  GLU   A OE1  1 
ATOM   1479 O OE2  . GLU   A 1 64  ? 34.954 3.338   9.890   1.00 13.75 -1 64  GLU   A OE2  1 
ATOM   1480 H H    . GLU   A 1 64  ? 33.821 8.734   7.692   1.00 13.89 ?  64  GLU   A H    1 
ATOM   1481 H HA   . GLU   A 1 64  ? 36.211 7.697   7.623   1.00 14.00 ?  64  GLU   A HA   1 
ATOM   1482 H HB2  . GLU   A 1 64  ? 34.651 7.023   9.202   1.00 14.62 ?  64  GLU   A HB2  1 
ATOM   1483 H HB3  . GLU   A 1 64  ? 33.715 6.446   8.058   1.00 14.62 ?  64  GLU   A HB3  1 
ATOM   1484 H HG2  . GLU   A 1 64  ? 35.500 4.872   7.609   1.00 15.28 ?  64  GLU   A HG2  1 
ATOM   1485 H HG3  . GLU   A 1 64  ? 36.104 5.339   9.001   1.00 15.28 ?  64  GLU   A HG3  1 
ATOM   1486 N N    . SER   A 1 65  ? 34.275 6.799   5.225   1.00 10.85 ?  65  SER   A N    1 
ATOM   1487 C CA   . SER   A 1 65  ? 34.220 6.149   3.919   1.00 10.87 ?  65  SER   A CA   1 
ATOM   1488 C C    . SER   A 1 65  ? 35.141 6.823   2.909   1.00 11.34 ?  65  SER   A C    1 
ATOM   1489 O O    . SER   A 1 65  ? 35.780 6.145   2.096   1.00 11.82 ?  65  SER   A O    1 
ATOM   1490 C CB   . SER   A 1 65  ? 32.787 6.156   3.388   1.00 10.96 ?  65  SER   A CB   1 
ATOM   1491 O OG   . SER   A 1 65  ? 31.934 5.339   4.179   1.00 11.32 ?  65  SER   A OG   1 
ATOM   1492 H H    . SER   A 1 65  ? 33.537 7.170   5.464   1.00 13.03 ?  65  SER   A H    1 
ATOM   1493 H HA   . SER   A 1 65  ? 34.505 5.229   4.014   1.00 13.04 ?  65  SER   A HA   1 
ATOM   1494 H HB2  . SER   A 1 65  ? 32.450 7.064   3.402   1.00 13.15 ?  65  SER   A HB2  1 
ATOM   1495 H HB3  . SER   A 1 65  ? 32.791 5.817   2.480   1.00 13.15 ?  65  SER   A HB3  1 
ATOM   1496 H HG   . SER   A 1 65  ? 31.926 5.620   4.977   1.00 13.59 ?  65  SER   A HG   1 
ATOM   1497 N N    . ASP   A 1 66  ? 35.210 8.157   2.929   1.00 11.52 ?  66  ASP   A N    1 
ATOM   1498 C CA   . ASP   A 1 66  ? 36.069 8.860   1.982   1.00 12.33 ?  66  ASP   A CA   1 
ATOM   1499 C C    . ASP   A 1 66  ? 37.532 8.501   2.210   1.00 11.90 ?  66  ASP   A C    1 
ATOM   1500 O O    . ASP   A 1 66  ? 38.300 8.337   1.252   1.00 12.88 ?  66  ASP   A O    1 
ATOM   1501 C CB   . ASP   A 1 66  ? 35.849 10.367  2.096   1.00 13.63 ?  66  ASP   A CB   1 
ATOM   1502 C CG   . ASP   A 1 66  ? 34.507 10.829  1.512   1.00 15.35 ?  66  ASP   A CG   1 
ATOM   1503 O OD1  . ASP   A 1 66  ? 33.790 10.038  0.859   1.00 15.49 ?  66  ASP   A OD1  1 
ATOM   1504 O OD2  . ASP   A 1 66  ? 34.195 12.021  1.699   1.00 18.22 -1 66  ASP   A OD2  1 
ATOM   1505 H H    . ASP   A 1 66  ? 34.762 8.669   3.461   1.00 13.83 ?  66  ASP   A H    1 
ATOM   1506 H HA   . ASP   A 1 66  ? 35.830 8.591   1.082   1.00 14.79 ?  66  ASP   A HA   1 
ATOM   1507 H HB2  . ASP   A 1 66  ? 35.867 10.621  3.030   1.00 16.35 ?  66  ASP   A HB2  1 
ATOM   1508 H HB3  . ASP   A 1 66  ? 36.560 10.825  1.615   1.00 16.35 ?  66  ASP   A HB3  1 
ATOM   1509 N N    . ASP   A 1 67  ? 37.939 8.372   3.473   1.00 12.21 ?  67  ASP   A N    1 
ATOM   1510 C CA   . ASP   A 1 67  ? 39.296 7.920   3.765   1.00 13.06 ?  67  ASP   A CA   1 
ATOM   1511 C C    . ASP   A 1 67  ? 39.515 6.486   3.291   1.00 12.85 ?  67  ASP   A C    1 
ATOM   1512 O O    . ASP   A 1 67  ? 40.575 6.161   2.741   1.00 13.56 ?  67  ASP   A O    1 
ATOM   1513 C CB   . ASP   A 1 67  ? 39.569 8.047   5.260   1.00 14.27 ?  67  ASP   A CB   1 
ATOM   1514 C CG   . ASP   A 1 67  ? 40.865 7.386   5.670   1.00 15.30 ?  67  ASP   A CG   1 
ATOM   1515 O OD1  . ASP   A 1 67  ? 41.936 8.019   5.525   1.00 17.97 ?  67  ASP   A OD1  1 
ATOM   1516 O OD2  . ASP   A 1 67  ? 40.814 6.224   6.132   1.00 15.29 -1 67  ASP   A OD2  1 
ATOM   1517 H H    . ASP   A 1 67  ? 37.460 8.538   4.163   1.00 14.65 ?  67  ASP   A H    1 
ATOM   1518 H HA   . ASP   A 1 67  ? 39.926 8.483   3.291   1.00 15.67 ?  67  ASP   A HA   1 
ATOM   1519 H HB2  . ASP   A 1 67  ? 39.626 8.983   5.485   1.00 17.12 ?  67  ASP   A HB2  1 
ATOM   1520 H HB3  . ASP   A 1 67  ? 38.846 7.623   5.748   1.00 17.12 ?  67  ASP   A HB3  1 
ATOM   1521 N N    . TYR   A 1 68  ? 38.520 5.610   3.489   1.00 12.14 ?  68  TYR   A N    1 
ATOM   1522 C CA   . TYR   A 1 68  ? 38.640 4.231   3.011   1.00 12.27 ?  68  TYR   A CA   1 
ATOM   1523 C C    . TYR   A 1 68  ? 38.878 4.188   1.503   1.00 12.41 ?  68  TYR   A C    1 
ATOM   1524 O O    . TYR   A 1 68  ? 39.751 3.453   1.025   1.00 12.85 ?  68  TYR   A O    1 
ATOM   1525 C CB   . TYR   A 1 68  ? 37.393 3.402   3.393   1.00 12.81 ?  68  TYR   A CB   1 
ATOM   1526 C CG   . TYR   A 1 68  ? 37.418 2.015   2.760   1.00 14.06 ?  68  TYR   A CG   1 
ATOM   1527 C CD1  . TYR   A 1 68  ? 36.956 1.825   1.461   1.00 15.58 ?  68  TYR   A CD1  1 
ATOM   1528 C CD2  . TYR   A 1 68  ? 37.958 0.925   3.424   1.00 15.77 ?  68  TYR   A CD2  1 
ATOM   1529 C CE1  . TYR   A 1 68  ? 37.024 0.609   0.840   1.00 16.67 ?  68  TYR   A CE1  1 
ATOM   1530 C CE2  . TYR   A 1 68  ? 38.026 -0.334  2.801   1.00 16.20 ?  68  TYR   A CE2  1 
ATOM   1531 C CZ   . TYR   A 1 68  ? 37.563 -0.461  1.511   1.00 16.98 ?  68  TYR   A CZ   1 
ATOM   1532 O OH   . TYR   A 1 68  ? 37.646 -1.669  0.879   1.00 18.09 ?  68  TYR   A OH   1 
ATOM   1533 H H    . TYR   A 1 68  ? 37.777 5.781   3.894   1.00 14.57 ?  68  TYR   A H    1 
ATOM   1534 H HA   . TYR   A 1 68  ? 39.402 3.816   3.439   1.00 14.72 ?  68  TYR   A HA   1 
ATOM   1535 H HB2  . TYR   A 1 68  ? 37.365 3.288   4.355   1.00 15.38 ?  68  TYR   A HB2  1 
ATOM   1536 H HB3  . TYR   A 1 68  ? 36.595 3.857   3.084   1.00 15.38 ?  68  TYR   A HB3  1 
ATOM   1537 H HD1  . TYR   A 1 68  ? 36.604 2.552   0.995   1.00 18.69 ?  68  TYR   A HD1  1 
ATOM   1538 H HD2  . TYR   A 1 68  ? 38.295 1.028   4.281   1.00 18.92 ?  68  TYR   A HD2  1 
ATOM   1539 H HE1  . TYR   A 1 68  ? 36.700 0.509   -0.026  1.00 20.00 ?  68  TYR   A HE1  1 
ATOM   1540 H HE2  . TYR   A 1 68  ? 38.394 -1.064  3.240   1.00 19.44 ?  68  TYR   A HE2  1 
ATOM   1541 H HH   . TYR   A 1 68  ? 37.973 -2.244  1.398   1.00 21.70 ?  68  TYR   A HH   1 
ATOM   1542 N N    . ILE   A 1 69  ? 38.088 4.949   0.732   1.00 11.98 ?  69  ILE   A N    1 
ATOM   1543 C CA   . ILE   A 1 69  ? 38.223 4.938   -0.724  1.00 12.21 ?  69  ILE   A CA   1 
ATOM   1544 C C    . ILE   A 1 69  ? 39.553 5.551   -1.156  1.00 12.15 ?  69  ILE   A C    1 
ATOM   1545 O O    . ILE   A 1 69  ? 40.202 5.066   -2.090  1.00 12.34 ?  69  ILE   A O    1 
ATOM   1546 C CB   . ILE   A 1 69  ? 37.020 5.642   -1.385  1.00 12.81 ?  69  ILE   A CB   1 
ATOM   1547 C CG1  . ILE   A 1 69  ? 35.713 4.898   -1.098  1.00 13.54 ?  69  ILE   A CG1  1 
ATOM   1548 C CG2  . ILE   A 1 69  ? 37.249 5.822   -2.892  1.00 14.32 ?  69  ILE   A CG2  1 
ATOM   1549 C CD1  . ILE   A 1 69  ? 35.549 3.610   -1.868  1.00 14.21 ?  69  ILE   A CD1  1 
ATOM   1550 H H    . ILE   A 1 69  ? 37.481 5.481   1.029   1.00 14.37 ?  69  ILE   A H    1 
ATOM   1551 H HA   . ILE   A 1 69  ? 38.221 4.014   -1.021  1.00 14.66 ?  69  ILE   A HA   1 
ATOM   1552 H HB   . ILE   A 1 69  ? 36.949 6.522   -0.994  1.00 15.37 ?  69  ILE   A HB   1 
ATOM   1553 H HG12 . ILE   A 1 69  ? 35.681 4.680   -0.152  1.00 16.25 ?  69  ILE   A HG12 1 
ATOM   1554 H HG13 . ILE   A 1 69  ? 34.972 5.475   -1.327  1.00 16.25 ?  69  ILE   A HG13 1 
ATOM   1555 H HG21 . ILE   A 1 69  ? 36.400 6.036   -3.315  1.00 17.19 ?  69  ILE   A HG21 1 
ATOM   1556 H HG22 . ILE   A 1 69  ? 37.875 6.551   -3.036  1.00 17.19 ?  69  ILE   A HG22 1 
ATOM   1557 H HG23 . ILE   A 1 69  ? 37.603 5.002   -3.265  1.00 17.19 ?  69  ILE   A HG23 1 
ATOM   1558 H HD11 . ILE   A 1 69  ? 34.762 3.147   -1.540  1.00 17.05 ?  69  ILE   A HD11 1 
ATOM   1559 H HD12 . ILE   A 1 69  ? 35.440 3.816   -2.811  1.00 17.05 ?  69  ILE   A HD12 1 
ATOM   1560 H HD13 . ILE   A 1 69  ? 36.335 3.057   -1.738  1.00 17.05 ?  69  ILE   A HD13 1 
ATOM   1561 N N    . ALA   A 1 70  ? 39.972 6.631   -0.498  1.00 12.42 ?  70  ALA   A N    1 
ATOM   1562 C CA   . ALA   A 1 70  ? 41.250 7.243   -0.848  1.00 13.07 ?  70  ALA   A CA   1 
ATOM   1563 C C    . ALA   A 1 70  ? 42.398 6.254   -0.688  1.00 13.23 ?  70  ALA   A C    1 
ATOM   1564 O O    . ALA   A 1 70  ? 43.359 6.285   -1.462  1.00 15.37 ?  70  ALA   A O    1 
ATOM   1565 C CB   . ALA   A 1 70  ? 41.493 8.486   0.009   1.00 14.07 ?  70  ALA   A CB   1 
ATOM   1566 H H    . ALA   A 1 70  ? 39.545 7.020   0.135   1.00 14.90 ?  70  ALA   A H    1 
ATOM   1567 H HA   . ALA   A 1 70  ? 41.222 7.524   -1.776  1.00 15.68 ?  70  ALA   A HA   1 
ATOM   1568 H HB1  . ALA   A 1 70  ? 42.350 8.874   -0.236  1.00 16.88 ?  70  ALA   A HB1  1 
ATOM   1569 H HB2  . ALA   A 1 70  ? 40.783 9.122   -0.144  1.00 16.88 ?  70  ALA   A HB2  1 
ATOM   1570 H HB3  . ALA   A 1 70  ? 41.510 8.223   0.945   1.00 16.88 ?  70  ALA   A HB3  1 
ATOM   1571 N N    . THR   A 1 71  ? 42.303 5.355   0.290   1.00 12.74 ?  71  THR   A N    1 
ATOM   1572 C CA   . THR   A 1 71  ? 43.359 4.379   0.533   1.00 14.20 ?  71  THR   A CA   1 
ATOM   1573 C C    . THR   A 1 71  ? 43.239 3.158   -0.369  1.00 14.47 ?  71  THR   A C    1 
ATOM   1574 O O    . THR   A 1 71  ? 44.251 2.655   -0.878  1.00 16.38 ?  71  THR   A O    1 
ATOM   1575 C CB   . THR   A 1 71  ? 43.302 3.927   1.988   1.00 16.17 ?  71  THR   A CB   1 
ATOM   1576 O OG1  . THR   A 1 71  ? 43.554 5.051   2.835   1.00 17.63 ?  71  THR   A OG1  1 
ATOM   1577 C CG2  . THR   A 1 71  ? 44.322 2.823   2.266   1.00 17.73 ?  71  THR   A CG2  1 
ATOM   1578 H H    . THR   A 1 71  ? 41.634 5.282   0.819   1.00 15.29 ?  71  THR   A H    1 
ATOM   1579 H HA   . THR   A 1 71  ? 44.224 4.786   0.370   1.00 17.04 ?  71  THR   A HA   1 
ATOM   1580 H HB   . THR   A 1 71  ? 42.420 3.564   2.173   1.00 19.40 ?  71  THR   A HB   1 
ATOM   1581 H HG1  . THR   A 1 71  ? 42.960 5.630   2.713   1.00 21.15 ?  71  THR   A HG1  1 
ATOM   1582 H HG21 . THR   A 1 71  ? 44.466 2.738   3.223   1.00 21.27 ?  71  THR   A HG21 1 
ATOM   1583 H HG22 . THR   A 1 71  ? 44.009 1.972   1.922   1.00 21.27 ?  71  THR   A HG22 1 
ATOM   1584 H HG23 . THR   A 1 71  ? 45.171 3.039   1.844   1.00 21.27 ?  71  THR   A HG23 1 
ATOM   1585 N N    . ASN   A 1 72  ? 42.016 2.648   -0.550  1.00 13.37 ?  72  ASN   A N    1 
ATOM   1586 C CA   . ASN   A 1 72  ? 41.799 1.321   -1.110  1.00 13.81 ?  72  ASN   A CA   1 
ATOM   1587 C C    . ASN   A 1 72  ? 41.171 1.314   -2.491  1.00 13.88 ?  72  ASN   A C    1 
ATOM   1588 O O    . ASN   A 1 72  ? 41.175 0.261   -3.143  1.00 14.87 ?  72  ASN   A O    1 
ATOM   1589 C CB   . ASN   A 1 72  ? 40.917 0.497   -0.164  1.00 14.46 ?  72  ASN   A CB   1 
ATOM   1590 C CG   . ASN   A 1 72  ? 41.540 0.348   1.198   1.00 15.46 ?  72  ASN   A CG   1 
ATOM   1591 O OD1  . ASN   A 1 72  ? 41.082 0.944   2.171   1.00 16.98 ?  72  ASN   A OD1  1 
ATOM   1592 N ND2  . ASN   A 1 72  ? 42.607 -0.421  1.274   1.00 15.94 ?  72  ASN   A ND2  1 
ATOM   1593 H H    . ASN   A 1 72  ? 41.284 3.065   -0.360  1.00 16.04 ?  72  ASN   A H    1 
ATOM   1594 H HA   . ASN   A 1 72  ? 42.653 0.874   -1.184  1.00 16.57 ?  72  ASN   A HA   1 
ATOM   1595 H HB2  . ASN   A 1 72  ? 40.061 0.935   -0.061  1.00 17.35 ?  72  ASN   A HB2  1 
ATOM   1596 H HB3  . ASN   A 1 72  ? 40.798 -0.392  -0.536  1.00 17.35 ?  72  ASN   A HB3  1 
ATOM   1597 H HD21 . ASN   A 1 72  ? 43.007 -0.526  2.032   1.00 19.12 ?  72  ASN   A HD21 1 
ATOM   1598 H HD22 . ASN   A 1 72  ? 42.912 -0.806  0.572   1.00 19.12 ?  72  ASN   A HD22 1 
ATOM   1599 N N    . GLY   A 1 73  ? 40.619 2.430   -2.947  1.00 13.65 ?  73  GLY   A N    1 
ATOM   1600 C CA   . GLY   A 1 73  ? 39.878 2.447   -4.181  1.00 13.45 ?  73  GLY   A CA   1 
ATOM   1601 C C    . GLY   A 1 73  ? 38.486 1.866   -4.012  1.00 12.83 ?  73  GLY   A C    1 
ATOM   1602 O O    . GLY   A 1 73  ? 38.102 1.401   -2.932  1.00 13.21 ?  73  GLY   A O    1 
ATOM   1603 H H    . GLY   A 1 73  ? 40.662 3.198   -2.556  1.00 16.38 ?  73  GLY   A H    1 
ATOM   1604 H HA2  . GLY   A 1 73  ? 39.800 3.364   -4.499  1.00 16.14 ?  73  GLY   A HA2  1 
ATOM   1605 H HA3  . GLY   A 1 73  ? 40.351 1.931   -4.854  1.00 16.14 ?  73  GLY   A HA3  1 
ATOM   1606 N N    . PRO   A 1 74  ? 37.705 1.887   -5.091  1.00 12.96 ?  74  PRO   A N    1 
ATOM   1607 C CA   . PRO   A 1 74  ? 36.307 1.455   -5.006  1.00 13.15 ?  74  PRO   A CA   1 
ATOM   1608 C C    . PRO   A 1 74  ? 36.161 -0.031  -4.702  1.00 12.63 ?  74  PRO   A C    1 
ATOM   1609 O O    . PRO   A 1 74  ? 37.029 -0.859  -4.996  1.00 13.53 ?  74  PRO   A O    1 
ATOM   1610 C CB   . PRO   A 1 74  ? 35.752 1.773   -6.401  1.00 14.98 ?  74  PRO   A CB   1 
ATOM   1611 C CG   . PRO   A 1 74  ? 36.694 2.774   -6.990  1.00 17.50 ?  74  PRO   A CG   1 
ATOM   1612 C CD   . PRO   A 1 74  ? 38.036 2.428   -6.420  1.00 15.15 ?  74  PRO   A CD   1 
ATOM   1613 H HA   . PRO   A 1 74  ? 35.828 1.975   -4.340  1.00 15.78 ?  74  PRO   A HA   1 
ATOM   1614 H HB2  . PRO   A 1 74  ? 35.727 0.966   -6.936  1.00 17.98 ?  74  PRO   A HB2  1 
ATOM   1615 H HB3  . PRO   A 1 74  ? 34.859 2.154   -6.318  1.00 17.98 ?  74  PRO   A HB3  1 
ATOM   1616 H HG2  . PRO   A 1 74  ? 36.699 2.688   -7.956  1.00 21.00 ?  74  PRO   A HG2  1 
ATOM   1617 H HG3  . PRO   A 1 74  ? 36.429 3.667   -6.726  1.00 21.00 ?  74  PRO   A HG3  1 
ATOM   1618 H HD2  . PRO   A 1 74  ? 38.474 1.755   -6.966  1.00 18.18 ?  74  PRO   A HD2  1 
ATOM   1619 H HD3  . PRO   A 1 74  ? 38.580 3.232   -6.347  1.00 18.18 ?  74  PRO   A HD3  1 
ATOM   1620 N N    . LEU   A 1 75  ? 35.018 -0.357  -4.107  1.00 11.75 ?  75  LEU   A N    1 
ATOM   1621 C CA   . LEU   A 1 75  ? 34.618 -1.749  -3.957  1.00 11.62 ?  75  LEU   A CA   1 
ATOM   1622 C C    . LEU   A 1 75  ? 34.231 -2.326  -5.316  1.00 12.30 ?  75  LEU   A C    1 
ATOM   1623 O O    . LEU   A 1 75  ? 34.095 -1.609  -6.310  1.00 13.74 ?  75  LEU   A O    1 
ATOM   1624 C CB   . LEU   A 1 75  ? 33.432 -1.870  -3.002  1.00 11.73 ?  75  LEU   A CB   1 
ATOM   1625 C CG   . LEU   A 1 75  ? 33.655 -1.461  -1.550  1.00 13.43 ?  75  LEU   A CG   1 
ATOM   1626 C CD1  . LEU   A 1 75  ? 32.370 -1.634  -0.752  1.00 15.39 ?  75  LEU   A CD1  1 
ATOM   1627 C CD2  . LEU   A 1 75  ? 34.795 -2.194  -0.894  1.00 16.69 ?  75  LEU   A CD2  1 
ATOM   1628 H H    . LEU   A 1 75  ? 34.458 0.209   -3.784  1.00 14.10 ?  75  LEU   A H    1 
ATOM   1629 H HA   . LEU   A 1 75  ? 35.360 -2.260  -3.608  1.00 13.94 ?  75  LEU   A HA   1 
ATOM   1630 H HB2  . LEU   A 1 75  ? 32.712 -1.322  -3.346  1.00 14.08 ?  75  LEU   A HB2  1 
ATOM   1631 H HB3  . LEU   A 1 75  ? 33.152 -2.799  -2.996  1.00 14.08 ?  75  LEU   A HB3  1 
ATOM   1632 H HG   . LEU   A 1 75  ? 33.886 -0.515  -1.536  1.00 16.12 ?  75  LEU   A HG   1 
ATOM   1633 H HD11 . LEU   A 1 75  ? 32.534 -1.363  0.165   1.00 18.47 ?  75  LEU   A HD11 1 
ATOM   1634 H HD12 . LEU   A 1 75  ? 31.685 -1.072  -1.146  1.00 18.47 ?  75  LEU   A HD12 1 
ATOM   1635 H HD13 . LEU   A 1 75  ? 32.104 -2.561  -0.787  1.00 18.47 ?  75  LEU   A HD13 1 
ATOM   1636 H HD21 . LEU   A 1 75  ? 34.854 -1.926  0.037   1.00 20.03 ?  75  LEU   A HD21 1 
ATOM   1637 H HD22 . LEU   A 1 75  ? 34.636 -3.149  -0.953  1.00 20.03 ?  75  LEU   A HD22 1 
ATOM   1638 H HD23 . LEU   A 1 75  ? 35.628 -1.972  -1.349  1.00 20.03 ?  75  LEU   A HD23 1 
ATOM   1639 N N    . LYS   A 1 76  ? 34.051 -3.646  -5.340  1.00 12.69 ?  76  LYS   A N    1 
ATOM   1640 C CA   . LYS   A 1 76  ? 33.449 -4.360  -6.460  1.00 13.18 ?  76  LYS   A CA   1 
ATOM   1641 C C    . LYS   A 1 76  ? 31.937 -4.443  -6.261  1.00 11.85 ?  76  LYS   A C    1 
ATOM   1642 O O    . LYS   A 1 76  ? 31.457 -4.563  -5.134  1.00 11.87 ?  76  LYS   A O    1 
ATOM   1643 C CB   . LYS   A 1 76  ? 33.995 -5.799  -6.526  1.00 14.85 ?  76  LYS   A CB   1 
ATOM   1644 C CG   . LYS   A 1 76  ? 35.510 -5.908  -6.705  1.00 16.60 ?  76  LYS   A CG   1 
ATOM   1645 C CD   . LYS   A 1 76  ? 36.027 -7.319  -6.518  1.00 17.94 ?  76  LYS   A CD   1 
ATOM   1646 C CE   . LYS   A 1 76  ? 37.529 -7.382  -6.713  1.00 20.27 ?  76  LYS   A CE   1 
ATOM   1647 N NZ   . LYS   A 1 76  ? 38.065 -8.742  -6.512  1.00 21.22 ?  76  LYS   A NZ   1 
ATOM   1648 H H    . LYS   A 1 76  ? 34.277 -4.165  -4.693  1.00 15.23 ?  76  LYS   A H    1 
ATOM   1649 H HA   . LYS   A 1 76  ? 33.640 -3.905  -7.296  1.00 15.81 ?  76  LYS   A HA   1 
ATOM   1650 H HB2  . LYS   A 1 76  ? 33.762 -6.254  -5.704  1.00 17.81 ?  76  LYS   A HB2  1 
ATOM   1651 H HB3  . LYS   A 1 76  ? 33.579 -6.250  -7.279  1.00 17.81 ?  76  LYS   A HB3  1 
ATOM   1652 H HG2  . LYS   A 1 76  ? 35.743 -5.615  -7.601  1.00 19.92 ?  76  LYS   A HG2  1 
ATOM   1653 H HG3  . LYS   A 1 76  ? 35.945 -5.338  -6.049  1.00 19.92 ?  76  LYS   A HG3  1 
ATOM   1654 H HD2  . LYS   A 1 76  ? 35.821 -7.621  -5.619  1.00 21.53 ?  76  LYS   A HD2  1 
ATOM   1655 H HD3  . LYS   A 1 76  ? 35.608 -7.903  -7.172  1.00 21.53 ?  76  LYS   A HD3  1 
ATOM   1656 H HE2  . LYS   A 1 76  ? 37.741 -7.102  -7.616  1.00 24.33 ?  76  LYS   A HE2  1 
ATOM   1657 H HE3  . LYS   A 1 76  ? 37.953 -6.792  -6.070  1.00 24.33 ?  76  LYS   A HE3  1 
ATOM   1658 H HZ1  . LYS   A 1 76  ? 38.945 -8.749  -6.633  1.00 25.46 ?  76  LYS   A HZ1  1 
ATOM   1659 H HZ2  . LYS   A 1 76  ? 37.884 -9.027  -5.686  1.00 25.46 ?  76  LYS   A HZ2  1 
ATOM   1660 H HZ3  . LYS   A 1 76  ? 37.691 -9.309  -7.094  1.00 25.46 ?  76  LYS   A HZ3  1 
ATOM   1661 N N    . VAL   A 1 77  ? 31.182 -4.408  -7.365  1.00 12.33 ?  77  VAL   A N    1 
ATOM   1662 C CA   . VAL   A 1 77  ? 29.775 -4.795  -7.278  1.00 12.34 ?  77  VAL   A CA   1 
ATOM   1663 C C    . VAL   A 1 77  ? 29.711 -6.249  -6.837  1.00 12.19 ?  77  VAL   A C    1 
ATOM   1664 O O    . VAL   A 1 77  ? 30.370 -7.119  -7.420  1.00 12.50 ?  77  VAL   A O    1 
ATOM   1665 C CB   . VAL   A 1 77  ? 29.050 -4.577  -8.614  1.00 13.78 ?  77  VAL   A CB   1 
ATOM   1666 C CG1  . VAL   A 1 77  ? 27.596 -5.024  -8.507  1.00 14.64 ?  77  VAL   A CG1  1 
ATOM   1667 C CG2  . VAL   A 1 77  ? 29.128 -3.118  -9.034  1.00 15.26 ?  77  VAL   A CG2  1 
ATOM   1668 H H    . VAL   A 1 77  ? 31.457 -4.166  -8.142  1.00 14.80 ?  77  VAL   A H    1 
ATOM   1669 H HA   . VAL   A 1 77  ? 29.341 -4.249  -6.602  1.00 14.80 ?  77  VAL   A HA   1 
ATOM   1670 H HB   . VAL   A 1 77  ? 29.486 -5.109  -9.298  1.00 16.54 ?  77  VAL   A HB   1 
ATOM   1671 H HG11 . VAL   A 1 77  ? 27.121 -4.720  -9.292  1.00 17.56 ?  77  VAL   A HG11 1 
ATOM   1672 H HG12 . VAL   A 1 77  ? 27.569 -5.992  -8.455  1.00 17.56 ?  77  VAL   A HG12 1 
ATOM   1673 H HG13 . VAL   A 1 77  ? 27.208 -4.635  -7.709  1.00 17.56 ?  77  VAL   A HG13 1 
ATOM   1674 H HG21 . VAL   A 1 77  ? 28.623 -3.001  -9.852  1.00 18.31 ?  77  VAL   A HG21 1 
ATOM   1675 H HG22 . VAL   A 1 77  ? 28.749 -2.568  -8.329  1.00 18.31 ?  77  VAL   A HG22 1 
ATOM   1676 H HG23 . VAL   A 1 77  ? 30.056 -2.877  -9.177  1.00 18.31 ?  77  VAL   A HG23 1 
ATOM   1677 N N    . GLY   A 1 78  ? 28.925 -6.520  -5.792  1.00 11.88 ?  78  GLY   A N    1 
ATOM   1678 C CA   . GLY   A 1 78  ? 28.904 -7.810  -5.137  1.00 12.00 ?  78  GLY   A CA   1 
ATOM   1679 C C    . GLY   A 1 78  ? 29.827 -7.911  -3.944  1.00 11.45 ?  78  GLY   A C    1 
ATOM   1680 O O    . GLY   A 1 78  ? 29.768 -8.918  -3.219  1.00 12.16 ?  78  GLY   A O    1 
ATOM   1681 H H    . GLY   A 1 78  ? 28.373 -5.950  -5.449  1.00 14.26 ?  78  GLY   A H    1 
ATOM   1682 H HA2  . GLY   A 1 78  ? 28.002 -7.997  -4.839  1.00 14.40 ?  78  GLY   A HA2  1 
ATOM   1683 H HA3  . GLY   A 1 78  ? 29.161 -8.491  -5.776  1.00 14.40 ?  78  GLY   A HA3  1 
ATOM   1684 N N    . GLY   A 1 79  ? 30.679 -6.906  -3.721  1.00 11.36 ?  79  GLY   A N    1 
ATOM   1685 C CA   . GLY   A 1 79  ? 31.645 -6.923  -2.648  1.00 11.62 ?  79  GLY   A CA   1 
ATOM   1686 C C    . GLY   A 1 79  ? 31.201 -6.124  -1.434  1.00 11.10 ?  79  GLY   A C    1 
ATOM   1687 O O    . GLY   A 1 79  ? 30.082 -5.625  -1.349  1.00 11.68 ?  79  GLY   A O    1 
ATOM   1688 H H    . GLY   A 1 79  ? 30.713 -6.187  -4.196  1.00 13.63 ?  79  GLY   A H    1 
ATOM   1689 H HA2  . GLY   A 1 79  ? 31.795 -7.849  -2.374  1.00 13.94 ?  79  GLY   A HA2  1 
ATOM   1690 H HA3  . GLY   A 1 79  ? 32.484 -6.563  -2.963  1.00 13.94 ?  79  GLY   A HA3  1 
ATOM   1691 N N    . SER   A 1 80  ? 32.109 -6.036  -0.465  1.00 11.90 ?  80  SER   A N    1 
ATOM   1692 C CA   . SER   A 1 80  ? 31.802 -5.409  0.809   1.00 11.31 ?  80  SER   A CA   1 
ATOM   1693 C C    . SER   A 1 80  ? 33.077 -4.965  1.505   1.00 11.30 ?  80  SER   A C    1 
ATOM   1694 O O    . SER   A 1 80  ? 34.188 -5.391  1.163   1.00 12.62 ?  80  SER   A O    1 
ATOM   1695 C CB   . SER   A 1 80  ? 31.045 -6.373  1.733   1.00 12.56 ?  80  SER   A CB   1 
ATOM   1696 O OG   . SER   A 1 80  ? 31.881 -7.422  2.202   1.00 14.00 ?  80  SER   A OG   1 
ATOM   1697 H H    . SER   A 1 80  ? 32.921 -6.316  -0.532  1.00 14.28 ?  80  SER   A H    1 
ATOM   1698 H HA   . SER   A 1 80  ? 31.251 -4.631  0.644   1.00 13.57 ?  80  SER   A HA   1 
ATOM   1699 H HB2  . SER   A 1 80  ? 30.710 -5.876  2.494   1.00 15.07 ?  80  SER   A HB2  1 
ATOM   1700 H HB3  . SER   A 1 80  ? 30.304 -6.760  1.239   1.00 15.07 ?  80  SER   A HB3  1 
ATOM   1701 H HG   . SER   A 1 80  ? 32.179 -7.861  1.548   1.00 16.79 ?  80  SER   A HG   1 
ATOM   1702 N N    . CYS   A 1 81  ? 32.892 -4.117  2.513   1.00 11.02 ?  81  CYS   A N    1 
ATOM   1703 C CA   . CYS   A 1 81  ? 33.947 -3.836  3.475   1.00 11.22 ?  81  CYS   A CA   1 
ATOM   1704 C C    . CYS   A 1 81  ? 33.306 -3.601  4.834   1.00 11.31 ?  81  CYS   A C    1 
ATOM   1705 O O    . CYS   A 1 81  ? 32.140 -3.203  4.927   1.00 12.17 ?  81  CYS   A O    1 
ATOM   1706 C CB   . CYS   A 1 81  ? 34.819 -2.645  3.058   1.00 12.01 ?  81  CYS   A CB   1 
ATOM   1707 S SG   . CYS   A 1 81  ? 33.917 -1.062  3.081   1.00 12.15 ?  81  CYS   A SG   1 
ATOM   1708 H H    . CYS   A 1 81  ? 32.159 -3.686  2.663   1.00 13.23 ?  81  CYS   A H    1 
ATOM   1709 H HA   . CYS   A 1 81  ? 34.521 -4.616  3.545   1.00 13.47 ?  81  CYS   A HA   1 
ATOM   1710 H HB2  . CYS   A 1 81  ? 35.570 -2.575  3.670   1.00 14.42 ?  81  CYS   A HB2  1 
ATOM   1711 H HB3  . CYS   A 1 81  ? 35.146 -2.796  2.155   1.00 14.42 ?  81  CYS   A HB3  1 
ATOM   1712 H HG   . CYS   A 1 81  ? 34.662 -0.181  2.742   1.00 14.58 ?  81  CYS   A HG   1 
ATOM   1713 N N    . VAL   A 1 82  ? 34.079 -3.860  5.886   1.00 11.32 ?  82  VAL   A N    1 
ATOM   1714 C CA   . VAL   A 1 82  ? 33.660 -3.622  7.260   1.00 12.01 ?  82  VAL   A CA   1 
ATOM   1715 C C    . VAL   A 1 82  ? 34.262 -2.308  7.731   1.00 12.43 ?  82  VAL   A C    1 
ATOM   1716 O O    . VAL   A 1 82  ? 35.488 -2.133  7.712   1.00 12.88 ?  82  VAL   A O    1 
ATOM   1717 C CB   . VAL   A 1 82  ? 34.084 -4.764  8.194   1.00 13.52 ?  82  VAL   A CB   1 
ATOM   1718 C CG1  . VAL   A 1 82  ? 33.621 -4.470  9.615   1.00 14.82 ?  82  VAL   A CG1  1 
ATOM   1719 C CG2  . VAL   A 1 82  ? 33.539 -6.100  7.708   1.00 14.48 ?  82  VAL   A CG2  1 
ATOM   1720 H H    . VAL   A 1 82  ? 34.877 -4.196  5.823   1.00 13.58 ?  82  VAL   A H    1 
ATOM   1721 H HA   . VAL   A 1 82  ? 32.694 -3.545  7.288   1.00 14.41 ?  82  VAL   A HA   1 
ATOM   1722 H HB   . VAL   A 1 82  ? 35.050 -4.818  8.206   1.00 16.22 ?  82  VAL   A HB   1 
ATOM   1723 H HG11 . VAL   A 1 82  ? 33.701 -5.274  10.148  1.00 17.78 ?  82  VAL   A HG11 1 
ATOM   1724 H HG12 . VAL   A 1 82  ? 34.170 -3.765  9.995   1.00 17.78 ?  82  VAL   A HG12 1 
ATOM   1725 H HG13 . VAL   A 1 82  ? 32.690 -4.184  9.593   1.00 17.78 ?  82  VAL   A HG13 1 
ATOM   1726 H HG21 . VAL   A 1 82  ? 33.783 -6.789  8.346   1.00 17.38 ?  82  VAL   A HG21 1 
ATOM   1727 H HG22 . VAL   A 1 82  ? 32.574 -6.040  7.637   1.00 17.38 ?  82  VAL   A HG22 1 
ATOM   1728 H HG23 . VAL   A 1 82  ? 33.925 -6.299  6.841   1.00 17.38 ?  82  VAL   A HG23 1 
ATOM   1729 N N    . LEU   A 1 83  ? 33.406 -1.388  8.159   1.00 11.47 ?  83  LEU   A N    1 
ATOM   1730 C CA   . LEU   A 1 83  ? 33.830 -0.126  8.744   1.00 11.52 ?  83  LEU   A CA   1 
ATOM   1731 C C    . LEU   A 1 83  ? 33.118 0.047   10.080  1.00 11.75 ?  83  LEU   A C    1 
ATOM   1732 O O    . LEU   A 1 83  ? 32.397 -0.843  10.542  1.00 12.40 ?  83  LEU   A O    1 
ATOM   1733 C CB   . LEU   A 1 83  ? 33.569 1.039   7.779   1.00 11.93 ?  83  LEU   A CB   1 
ATOM   1734 C CG   . LEU   A 1 83  ? 34.461 1.040   6.531   1.00 12.68 ?  83  LEU   A CG   1 
ATOM   1735 C CD1  . LEU   A 1 83  ? 34.024 2.088   5.531   1.00 13.31 ?  83  LEU   A CD1  1 
ATOM   1736 C CD2  . LEU   A 1 83  ? 35.931 1.249   6.907   1.00 13.49 ?  83  LEU   A CD2  1 
ATOM   1737 H H    . LEU   A 1 83  ? 32.551 -1.476  8.114   1.00 13.76 ?  83  LEU   A H    1 
ATOM   1738 H HA   . LEU   A 1 83  ? 34.782 -0.161  8.917   1.00 13.83 ?  83  LEU   A HA   1 
ATOM   1739 H HB2  . LEU   A 1 83  ? 32.648 0.997   7.475   1.00 14.31 ?  83  LEU   A HB2  1 
ATOM   1740 H HB3  . LEU   A 1 83  ? 33.719 1.875   8.245   1.00 14.31 ?  83  LEU   A HB3  1 
ATOM   1741 H HG   . LEU   A 1 83  ? 34.393 0.175   6.102   1.00 15.22 ?  83  LEU   A HG   1 
ATOM   1742 H HD11 . LEU   A 1 83  ? 34.611 2.045   4.757   1.00 15.97 ?  83  LEU   A HD11 1 
ATOM   1743 H HD12 . LEU   A 1 83  ? 33.112 1.900   5.263   1.00 15.97 ?  83  LEU   A HD12 1 
ATOM   1744 H HD13 . LEU   A 1 83  ? 34.080 2.960   5.943   1.00 15.97 ?  83  LEU   A HD13 1 
ATOM   1745 H HD21 . LEU   A 1 83  ? 36.445 1.414   6.098   1.00 16.19 ?  83  LEU   A HD21 1 
ATOM   1746 H HD22 . LEU   A 1 83  ? 36.004 2.011   7.502   1.00 16.19 ?  83  LEU   A HD22 1 
ATOM   1747 H HD23 . LEU   A 1 83  ? 36.265 0.452   7.349   1.00 16.19 ?  83  LEU   A HD23 1 
ATOM   1748 N N    . SER   A 1 84  ? 33.329 1.196   10.715  1.00 12.18 ?  84  SER   A N    1 
ATOM   1749 C CA   . SER   A 1 84  ? 32.682 1.450   11.991  1.00 12.57 ?  84  SER   A CA   1 
ATOM   1750 C C    . SER   A 1 84  ? 31.164 1.534   11.841  1.00 12.53 ?  84  SER   A C    1 
ATOM   1751 O O    . SER   A 1 84  ? 30.639 1.997   10.828  1.00 12.66 ?  84  SER   A O    1 
ATOM   1752 C CB   . SER   A 1 84  ? 33.178 2.771   12.567  1.00 13.53 ?  84  SER   A CB   1 
ATOM   1753 O OG   . SER   A 1 84  ? 32.552 3.041   13.807  1.00 14.51 ?  84  SER   A OG   1 
ATOM   1754 H H    . SER   A 1 84  ? 33.832 1.835   10.424  1.00 14.61 ?  84  SER   A H    1 
ATOM   1755 H HA   . SER   A 1 84  ? 32.900 0.737   12.607  1.00 15.08 ?  84  SER   A HA   1 
ATOM   1756 H HB2  . SER   A 1 84  ? 34.139 2.717   12.697  1.00 16.24 ?  84  SER   A HB2  1 
ATOM   1757 H HB3  . SER   A 1 84  ? 32.970 3.485   11.943  1.00 16.24 ?  84  SER   A HB3  1 
ATOM   1758 H HG   . SER   A 1 84  ? 32.835 3.768   14.117  1.00 17.41 ?  84  SER   A HG   1 
ATOM   1759 N N    . GLY   A 1 85  ? 30.458 1.115   12.888  1.00 13.24 ?  85  GLY   A N    1 
ATOM   1760 C CA   . GLY   A 1 85  ? 29.035 1.351   12.985  1.00 13.97 ?  85  GLY   A CA   1 
ATOM   1761 C C    . GLY   A 1 85  ? 28.673 2.657   13.651  1.00 13.58 ?  85  GLY   A C    1 
ATOM   1762 O O    . GLY   A 1 85  ? 27.482 2.966   13.772  1.00 13.99 ?  85  GLY   A O    1 
ATOM   1763 H H    . GLY   A 1 85  ? 30.796 0.688   13.557  1.00 15.89 ?  85  GLY   A H    1 
ATOM   1764 H HA2  . GLY   A 1 85  ? 28.657 1.346   12.092  1.00 16.76 ?  85  GLY   A HA2  1 
ATOM   1765 H HA3  . GLY   A 1 85  ? 28.634 0.634   13.491  1.00 16.76 ?  85  GLY   A HA3  1 
ATOM   1766 N N    . HIS   A 1 86  ? 29.662 3.430   14.091  1.00 13.16 ?  86  HIS   A N    1 
ATOM   1767 C CA   . HIS   A 1 86  ? 29.436 4.764   14.661  1.00 13.66 ?  86  HIS   A CA   1 
ATOM   1768 C C    . HIS   A 1 86  ? 28.456 4.635   15.821  1.00 14.75 ?  86  HIS   A C    1 
ATOM   1769 O O    . HIS   A 1 86  ? 28.646 3.753   16.673  1.00 15.91 ?  86  HIS   A O    1 
ATOM   1770 C CB   . HIS   A 1 86  ? 29.050 5.744   13.561  1.00 13.86 ?  86  HIS   A CB   1 
ATOM   1771 C CG   . HIS   A 1 86  ? 30.099 5.852   12.515  1.00 14.01 ?  86  HIS   A CG   1 
ATOM   1772 N ND1  . HIS   A 1 86  ? 31.185 6.691   12.642  1.00 14.83 ?  86  HIS   A ND1  1 
ATOM   1773 C CD2  . HIS   A 1 86  ? 30.278 5.165   11.366  1.00 13.64 ?  86  HIS   A CD2  1 
ATOM   1774 C CE1  . HIS   A 1 86  ? 31.973 6.533   11.594  1.00 14.27 ?  86  HIS   A CE1  1 
ATOM   1775 N NE2  . HIS   A 1 86  ? 31.453 5.604   10.813  1.00 13.66 ?  86  HIS   A NE2  1 
ATOM   1776 H H    . HIS   A 1 86  ? 30.486 3.205   14.082  1.00 15.80 ?  86  HIS   A H    1 
ATOM   1777 H HA   . HIS   A 1 86  ? 30.273 5.081   15.031  1.00 16.39 ?  86  HIS   A HA   1 
ATOM   1778 H HB2  . HIS   A 1 86  ? 28.228 5.453   13.138  1.00 16.64 ?  86  HIS   A HB2  1 
ATOM   1779 H HB3  . HIS   A 1 86  ? 28.923 6.632   13.947  1.00 16.64 ?  86  HIS   A HB3  1 
ATOM   1780 H HD2  . HIS   A 1 86  ? 29.720 4.502   11.020  1.00 16.37 ?  86  HIS   A HD2  1 
ATOM   1781 H HE1  . HIS   A 1 86  ? 32.762 6.997   11.422  1.00 17.13 ?  86  HIS   A HE1  1 
ATOM   1782 H HE2  . HIS   A 1 86  ? 31.785 5.331   10.060  1.00 16.39 ?  86  HIS   A HE2  1 
ATOM   1783 N N    . ASN   A 1 87  ? 27.443 5.487   15.906  1.00 15.77 ?  87  ASN   A N    1 
ATOM   1784 C CA   . ASN   A 1 87  ? 26.460 5.466   16.975  1.00 16.68 ?  87  ASN   A CA   1 
ATOM   1785 C C    . ASN   A 1 87  ? 25.346 4.459   16.736  1.00 17.58 ?  87  ASN   A C    1 
ATOM   1786 O O    . ASN   A 1 87  ? 24.435 4.372   17.563  1.00 20.01 ?  87  ASN   A O    1 
ATOM   1787 C CB   . ASN   A 1 87  ? 25.847 6.864   17.147  1.00 17.90 ?  87  ASN   A CB   1 
ATOM   1788 C CG   . ASN   A 1 87  ? 25.349 7.457   15.832  1.00 18.60 ?  87  ASN   A CG   1 
ATOM   1789 O OD1  . ASN   A 1 87  ? 26.001 7.349   14.795  1.00 19.08 ?  87  ASN   A OD1  1 
ATOM   1790 N ND2  . ASN   A 1 87  ? 24.195 8.096   15.877  1.00 19.76 ?  87  ASN   A ND2  1 
ATOM   1791 H H    . ASN   A 1 87  ? 27.298 6.109   15.336  1.00 18.93 ?  87  ASN   A H    1 
ATOM   1792 H HA   . ASN   A 1 87  ? 26.893 5.227   17.812  1.00 20.01 ?  87  ASN   A HA   1 
ATOM   1793 H HB2  . ASN   A 1 87  ? 25.089 6.803   17.761  1.00 21.48 ?  87  ASN   A HB2  1 
ATOM   1794 H HB3  . ASN   A 1 87  ? 26.517 7.456   17.519  1.00 21.48 ?  87  ASN   A HB3  1 
ATOM   1795 H HD21 . ASN   A 1 87  ? 23.877 8.449   15.164  1.00 23.71 ?  87  ASN   A HD21 1 
ATOM   1796 H HD22 . ASN   A 1 87  ? 23.765 8.162   16.621  1.00 23.71 ?  87  ASN   A HD22 1 
ATOM   1797 N N    . LEU   A 1 88  ? 25.403 3.687   15.654  1.00 16.89 ?  88  LEU   A N    1 
ATOM   1798 C CA   . LEU   A 1 88  ? 24.293 2.826   15.259  1.00 16.81 ?  88  LEU   A CA   1 
ATOM   1799 C C    . LEU   A 1 88  ? 24.514 1.350   15.555  1.00 16.67 ?  88  LEU   A C    1 
ATOM   1800 O O    . LEU   A 1 88  ? 23.537 0.619   15.738  1.00 17.89 ?  88  LEU   A O    1 
ATOM   1801 C CB   . LEU   A 1 88  ? 24.029 2.986   13.761  1.00 17.37 ?  88  LEU   A CB   1 
ATOM   1802 C CG   . LEU   A 1 88  ? 23.728 4.407   13.286  1.00 18.88 ?  88  LEU   A CG   1 
ATOM   1803 C CD1  . LEU   A 1 88  ? 23.530 4.413   11.784  1.00 19.15 ?  88  LEU   A CD1  1 
ATOM   1804 C CD2  . LEU   A 1 88  ? 22.506 4.979   13.995  1.00 20.46 ?  88  LEU   A CD2  1 
ATOM   1805 H H    . LEU   A 1 88  ? 26.083 3.646   15.131  1.00 20.27 ?  88  LEU   A H    1 
ATOM   1806 H HA   . LEU   A 1 88  ? 23.498 3.106   15.733  1.00 20.18 ?  88  LEU   A HA   1 
ATOM   1807 H HB2  . LEU   A 1 88  ? 24.808 2.681   13.273  1.00 20.84 ?  88  LEU   A HB2  1 
ATOM   1808 H HB3  . LEU   A 1 88  ? 23.263 2.441   13.526  1.00 20.84 ?  88  LEU   A HB3  1 
ATOM   1809 H HG   . LEU   A 1 88  ? 24.487 4.978   13.487  1.00 22.66 ?  88  LEU   A HG   1 
ATOM   1810 H HD11 . LEU   A 1 88  ? 23.342 5.320   11.493  1.00 22.98 ?  88  LEU   A HD11 1 
ATOM   1811 H HD12 . LEU   A 1 88  ? 24.339 4.091   11.357  1.00 22.98 ?  88  LEU   A HD12 1 
ATOM   1812 H HD13 . LEU   A 1 88  ? 22.785 3.834   11.561  1.00 22.98 ?  88  LEU   A HD13 1 
ATOM   1813 H HD21 . LEU   A 1 88  ? 22.274 5.828   13.587  1.00 24.56 ?  88  LEU   A HD21 1 
ATOM   1814 H HD22 . LEU   A 1 88  ? 21.771 4.355   13.905  1.00 24.56 ?  88  LEU   A HD22 1 
ATOM   1815 H HD23 . LEU   A 1 88  ? 22.720 5.109   14.932  1.00 24.56 ?  88  LEU   A HD23 1 
ATOM   1816 N N    . ALA   A 1 89  ? 25.764 0.901   15.590  1.00 15.80 ?  89  ALA   A N    1 
ATOM   1817 C CA   . ALA   A 1 89  ? 26.113 -0.509  15.687  1.00 15.60 ?  89  ALA   A CA   1 
ATOM   1818 C C    . ALA   A 1 89  ? 27.599 -0.569  15.997  1.00 15.86 ?  89  ALA   A C    1 
ATOM   1819 O O    . ALA   A 1 89  ? 28.305 0.434   15.893  1.00 16.59 ?  89  ALA   A O    1 
ATOM   1820 C CB   . ALA   A 1 89  ? 25.828 -1.227  14.368  1.00 15.06 ?  89  ALA   A CB   1 
ATOM   1821 H H    . ALA   A 1 89  ? 26.453 1.419   15.547  1.00 18.95 ?  89  ALA   A H    1 
ATOM   1822 H HA   . ALA   A 1 89  ? 25.613 -0.928  16.404  1.00 18.72 ?  89  ALA   A HA   1 
ATOM   1823 H HB1  . ALA   A 1 89  ? 26.087 -2.160  14.457  1.00 18.07 ?  89  ALA   A HB1  1 
ATOM   1824 H HB2  . ALA   A 1 89  ? 24.878 -1.168  14.173  1.00 18.07 ?  89  ALA   A HB2  1 
ATOM   1825 H HB3  . ALA   A 1 89  ? 26.339 -0.809  13.661  1.00 18.07 ?  89  ALA   A HB3  1 
ATOM   1826 N N    . LYS   A 1 90  ? 28.083 -1.752  16.369  1.00 16.40 ?  90  LYS   A N    1 
ATOM   1827 C CA   . LYS   A 1 90  ? 29.526 -1.903  16.511  1.00 16.96 ?  90  LYS   A CA   1 
ATOM   1828 C C    . LYS   A 1 90  ? 30.220 -1.708  15.167  1.00 15.87 ?  90  LYS   A C    1 
ATOM   1829 O O    . LYS   A 1 90  ? 31.152 -0.898  15.040  1.00 17.02 ?  90  LYS   A O    1 
ATOM   1830 C CB   . LYS   A 1 90  ? 29.863 -3.265  17.120  1.00 19.62 ?  90  LYS   A CB   1 
ATOM   1831 C CG   . LYS   A 1 90  ? 31.338 -3.417  17.455  1.00 23.58 ?  90  LYS   A CG   1 
ATOM   1832 C CD   . LYS   A 1 90  ? 31.590 -4.613  18.359  1.00 27.20 ?  90  LYS   A CD   1 
ATOM   1833 C CE   . LYS   A 1 90  ? 33.008 -4.605  18.914  1.00 30.06 ?  90  LYS   A CE   1 
ATOM   1834 N NZ   . LYS   A 1 90  ? 34.033 -4.896  17.875  1.00 32.01 ?  90  LYS   A NZ   1 
ATOM   1835 H H    . LYS   A 1 90  ? 27.613 -2.451  16.538  1.00 19.67 ?  90  LYS   A H    1 
ATOM   1836 H HA   . LYS   A 1 90  ? 29.854 -1.221  17.112  1.00 20.36 ?  90  LYS   A HA   1 
ATOM   1837 H HB2  . LYS   A 1 90  ? 29.354 -3.377  17.942  1.00 23.54 ?  90  LYS   A HB2  1 
ATOM   1838 H HB3  . LYS   A 1 90  ? 29.624 -3.964  16.491  1.00 23.54 ?  90  LYS   A HB3  1 
ATOM   1839 H HG2  . LYS   A 1 90  ? 31.839 -3.544  16.636  1.00 28.29 ?  90  LYS   A HG2  1 
ATOM   1840 H HG3  . LYS   A 1 90  ? 31.643 -2.620  17.916  1.00 28.29 ?  90  LYS   A HG3  1 
ATOM   1841 H HD2  . LYS   A 1 90  ? 30.970 -4.588  19.106  1.00 32.64 ?  90  LYS   A HD2  1 
ATOM   1842 H HD3  . LYS   A 1 90  ? 31.467 -5.431  17.850  1.00 32.64 ?  90  LYS   A HD3  1 
ATOM   1843 H HE2  . LYS   A 1 90  ? 33.197 -3.727  19.284  1.00 36.08 ?  90  LYS   A HE2  1 
ATOM   1844 H HE3  . LYS   A 1 90  ? 33.081 -5.279  19.607  1.00 36.08 ?  90  LYS   A HE3  1 
ATOM   1845 H HZ1  . LYS   A 1 90  ? 33.889 -5.701  17.523  1.00 38.41 ?  90  LYS   A HZ1  1 
ATOM   1846 H HZ2  . LYS   A 1 90  ? 33.995 -4.286  17.229  1.00 38.41 ?  90  LYS   A HZ2  1 
ATOM   1847 H HZ3  . LYS   A 1 90  ? 34.847 -4.883  18.238  1.00 38.41 ?  90  LYS   A HZ3  1 
ATOM   1848 N N    . HIS   A 1 91  ? 29.751 -2.424  14.143  1.00 13.90 ?  91  HIS   A N    1 
ATOM   1849 C CA   . HIS   A 1 91  ? 30.319 -2.393  12.809  1.00 13.39 ?  91  HIS   A CA   1 
ATOM   1850 C C    . HIS   A 1 91  ? 29.226 -2.115  11.793  1.00 12.41 ?  91  HIS   A C    1 
ATOM   1851 O O    . HIS   A 1 91  ? 28.062 -2.479  11.992  1.00 12.90 ?  91  HIS   A O    1 
ATOM   1852 C CB   . HIS   A 1 91  ? 30.927 -3.755  12.436  1.00 15.72 ?  91  HIS   A CB   1 
ATOM   1853 C CG   . HIS   A 1 91  ? 31.924 -4.270  13.426  1.00 19.94 ?  91  HIS   A CG   1 
ATOM   1854 N ND1  . HIS   A 1 91  ? 33.202 -3.765  13.527  1.00 22.15 ?  91  HIS   A ND1  1 
ATOM   1855 C CD2  . HIS   A 1 91  ? 31.837 -5.258  14.348  1.00 21.51 ?  91  HIS   A CD2  1 
ATOM   1856 C CE1  . HIS   A 1 91  ? 33.858 -4.414  14.474  1.00 22.92 ?  91  HIS   A CE1  1 
ATOM   1857 N NE2  . HIS   A 1 91  ? 33.051 -5.326  14.987  1.00 22.84 ?  91  HIS   A NE2  1 
ATOM   1858 H H    . HIS   A 1 91  ? 29.080 -2.972  14.212  1.00 16.69 ?  91  HIS   A H    1 
ATOM   1859 H HA   . HIS   A 1 91  ? 31.003 -1.717  12.748  1.00 16.07 ?  91  HIS   A HA   1 
ATOM   1860 H HB2  . HIS   A 1 91  ? 30.216 -4.415  12.373  1.00 18.87 ?  91  HIS   A HB2  1 
ATOM   1861 H HB3  . HIS   A 1 91  ? 31.377 -3.677  11.581  1.00 18.87 ?  91  HIS   A HB3  1 
ATOM   1862 H HD1  . HIS   A 1 91  ? 33.523 -3.125  13.046  1.00 26.58 ?  91  HIS   A HD1  1 
ATOM   1863 H HD2  . HIS   A 1 91  ? 31.100 -5.792  14.522  1.00 25.82 ?  91  HIS   A HD2  1 
ATOM   1864 H HE1  . HIS   A 1 91  ? 34.741 -4.250  14.731  1.00 27.50 ?  91  HIS   A HE1  1 
ATOM   1865 N N    . CYS   A 1 92  ? 29.624 -1.510  10.677  1.00 11.80 ?  92  CYS   A N    1 
ATOM   1866 C CA   . CYS   A 1 92  ? 28.782 -1.430  9.492   1.00 11.80 ?  92  CYS   A CA   1 
ATOM   1867 C C    . CYS   A 1 92  ? 29.422 -2.246  8.380   1.00 11.23 ?  92  CYS   A C    1 
ATOM   1868 O O    . CYS   A 1 92  ? 30.578 -1.995  8.003   1.00 11.71 ?  92  CYS   A O    1 
ATOM   1869 C CB   . CYS   A 1 92  ? 28.569 0.014   9.035   1.00 12.02 ?  92  CYS   A CB   1 
ATOM   1870 S SG   . CYS   A 1 92  ? 27.541 0.125   7.534   1.00 11.50 ?  92  CYS   A SG   1 
ATOM   1871 H H    . CYS   A 1 92  ? 30.393 -1.129  10.585  1.00 14.16 ?  92  CYS   A H    1 
ATOM   1872 H HA   . CYS   A 1 92  ? 27.916 -1.813  9.693   1.00 14.16 ?  92  CYS   A HA   1 
ATOM   1873 H HB2  . CYS   A 1 92  ? 28.122 0.511   9.741   1.00 14.43 ?  92  CYS   A HB2  1 
ATOM   1874 H HB3  . CYS   A 1 92  ? 29.428 0.419   8.840   1.00 14.43 ?  92  CYS   A HB3  1 
ATOM   1875 H HG   . CYS   A 1 92  ? 27.401 1.280   7.242   1.00 13.80 ?  92  CYS   A HG   1 
ATOM   1876 N N    . LEU   A 1 93  ? 28.681 -3.233  7.879   1.00 11.15 ?  93  LEU   A N    1 
ATOM   1877 C CA   . LEU   A 1 93  ? 29.075 -3.991  6.697   1.00 10.74 ?  93  LEU   A CA   1 
ATOM   1878 C C    . LEU   A 1 93  ? 28.479 -3.292  5.483   1.00 10.33 ?  93  LEU   A C    1 
ATOM   1879 O O    . LEU   A 1 93  ? 27.264 -3.348  5.265   1.00 10.32 ?  93  LEU   A O    1 
ATOM   1880 C CB   . LEU   A 1 93  ? 28.592 -5.437  6.800   1.00 11.15 ?  93  LEU   A CB   1 
ATOM   1881 C CG   . LEU   A 1 93  ? 28.982 -6.329  5.622   1.00 11.34 ?  93  LEU   A CG   1 
ATOM   1882 C CD1  . LEU   A 1 93  ? 30.487 -6.584  5.597   1.00 12.35 ?  93  LEU   A CD1  1 
ATOM   1883 C CD2  . LEU   A 1 93  ? 28.215 -7.660  5.654   1.00 12.11 ?  93  LEU   A CD2  1 
ATOM   1884 H H    . LEU   A 1 93  ? 27.923 -3.474  8.212   1.00 13.37 ?  93  LEU   A H    1 
ATOM   1885 H HA   . LEU   A 1 93  ? 30.038 -3.983  6.622   1.00 12.89 ?  93  LEU   A HA   1 
ATOM   1886 H HB2  . LEU   A 1 93  ? 28.967 -5.827  7.606   1.00 13.38 ?  93  LEU   A HB2  1 
ATOM   1887 H HB3  . LEU   A 1 93  ? 27.625 -5.436  6.860   1.00 13.38 ?  93  LEU   A HB3  1 
ATOM   1888 H HG   . LEU   A 1 93  ? 28.751 -5.883  4.801   1.00 13.60 ?  93  LEU   A HG   1 
ATOM   1889 H HD11 . LEU   A 1 93  ? 30.698 -7.196  4.874   1.00 14.82 ?  93  LEU   A HD11 1 
ATOM   1890 H HD12 . LEU   A 1 93  ? 30.953 -5.743  5.463   1.00 14.82 ?  93  LEU   A HD12 1 
ATOM   1891 H HD13 . LEU   A 1 93  ? 30.764 -6.977  6.446   1.00 14.82 ?  93  LEU   A HD13 1 
ATOM   1892 H HD21 . LEU   A 1 93  ? 28.496 -8.202  4.895   1.00 14.53 ?  93  LEU   A HD21 1 
ATOM   1893 H HD22 . LEU   A 1 93  ? 28.421 -8.128  6.480   1.00 14.53 ?  93  LEU   A HD22 1 
ATOM   1894 H HD23 . LEU   A 1 93  ? 27.268 -7.482  5.599   1.00 14.53 ?  93  LEU   A HD23 1 
ATOM   1895 N N    . HIS   A 1 94  ? 29.328 -2.598  4.722   1.00 9.78  ?  94  HIS   A N    1 
ATOM   1896 C CA   . HIS   A 1 94  ? 28.901 -1.920  3.503   1.00 10.11 ?  94  HIS   A CA   1 
ATOM   1897 C C    . HIS   A 1 94  ? 28.899 -2.947  2.386   1.00 10.21 ?  94  HIS   A C    1 
ATOM   1898 O O    . HIS   A 1 94  ? 29.962 -3.457  2.027   1.00 11.55 ?  94  HIS   A O    1 
ATOM   1899 C CB   . HIS   A 1 94  ? 29.849 -0.768  3.169   1.00 10.32 ?  94  HIS   A CB   1 
ATOM   1900 C CG   . HIS   A 1 94  ? 29.836 0.323   4.182   1.00 10.20 ?  94  HIS   A CG   1 
ATOM   1901 N ND1  . HIS   A 1 94  ? 28.964 1.390   4.129   1.00 10.23 ?  94  HIS   A ND1  1 
ATOM   1902 C CD2  . HIS   A 1 94  ? 30.583 0.488   5.298   1.00 10.71 ?  94  HIS   A CD2  1 
ATOM   1903 C CE1  . HIS   A 1 94  ? 29.182 2.164   5.176   1.00 10.61 ?  94  HIS   A CE1  1 
ATOM   1904 N NE2  . HIS   A 1 94  ? 30.157 1.641   5.900   1.00 10.84 ?  94  HIS   A NE2  1 
ATOM   1905 H H    . HIS   A 1 94  ? 30.169 -2.512  4.888   1.00 11.73 ?  94  HIS   A H    1 
ATOM   1906 H HA   . HIS   A 1 94  ? 27.999 -1.577  3.614   1.00 12.13 ?  94  HIS   A HA   1 
ATOM   1907 H HB2  . HIS   A 1 94  ? 30.746 -1.112  3.107   1.00 12.39 ?  94  HIS   A HB2  1 
ATOM   1908 H HB3  . HIS   A 1 94  ? 29.575 -0.383  2.319   1.00 12.39 ?  94  HIS   A HB3  1 
ATOM   1909 H HD2  . HIS   A 1 94  ? 31.255 -0.074  5.605   1.00 12.85 ?  94  HIS   A HD2  1 
ATOM   1910 H HE1  . HIS   A 1 94  ? 28.720 2.951   5.371   1.00 12.74 ?  94  HIS   A HE1  1 
ATOM   1911 H HE2  . HIS   A 1 94  ? 30.474 1.981   6.624   1.00 13.01 ?  94  HIS   A HE2  1 
ATOM   1912 N N    . VAL   A 1 95  ? 27.725 -3.264  1.841   1.00 9.66  ?  95  VAL   A N    1 
ATOM   1913 C CA   . VAL   A 1 95  ? 27.579 -4.299  0.821   1.00 10.02 ?  95  VAL   A CA   1 
ATOM   1914 C C    . VAL   A 1 95  ? 27.031 -3.660  -0.443  1.00 9.74  ?  95  VAL   A C    1 
ATOM   1915 O O    . VAL   A 1 95  ? 26.030 -2.936  -0.388  1.00 10.28 ?  95  VAL   A O    1 
ATOM   1916 C CB   . VAL   A 1 95  ? 26.647 -5.440  1.271   1.00 10.66 ?  95  VAL   A CB   1 
ATOM   1917 C CG1  . VAL   A 1 95  ? 26.539 -6.483  0.167   1.00 11.52 ?  95  VAL   A CG1  1 
ATOM   1918 C CG2  . VAL   A 1 95  ? 27.156 -6.066  2.546   1.00 10.80 ?  95  VAL   A CG2  1 
ATOM   1919 H H    . VAL   A 1 95  ? 26.980 -2.891  2.055   1.00 11.60 ?  95  VAL   A H    1 
ATOM   1920 H HA   . VAL   A 1 95  ? 28.446 -4.677  0.614   1.00 12.03 ?  95  VAL   A HA   1 
ATOM   1921 H HB   . VAL   A 1 95  ? 25.766 -5.087  1.440   1.00 12.79 ?  95  VAL   A HB   1 
ATOM   1922 H HG11 . VAL   A 1 95  ? 26.145 -7.294  0.531   1.00 13.82 ?  95  VAL   A HG11 1 
ATOM   1923 H HG12 . VAL   A 1 95  ? 25.978 -6.141  -0.547  1.00 13.82 ?  95  VAL   A HG12 1 
ATOM   1924 H HG13 . VAL   A 1 95  ? 27.427 -6.682  -0.178  1.00 13.82 ?  95  VAL   A HG13 1 
ATOM   1925 H HG21 . VAL   A 1 95  ? 26.595 -6.823  2.771   1.00 12.95 ?  95  VAL   A HG21 1 
ATOM   1926 H HG22 . VAL   A 1 95  ? 28.072 -6.359  2.412   1.00 12.95 ?  95  VAL   A HG22 1 
ATOM   1927 H HG23 . VAL   A 1 95  ? 27.121 -5.404  3.254   1.00 12.95 ?  95  VAL   A HG23 1 
ATOM   1928 N N    . VAL   A 1 96  ? 27.659 -3.949  -1.582  1.00 9.78  ?  96  VAL   A N    1 
ATOM   1929 C CA   . VAL   A 1 96  ? 27.249 -3.392  -2.864  1.00 10.32 ?  96  VAL   A CA   1 
ATOM   1930 C C    . VAL   A 1 96  ? 26.441 -4.434  -3.628  1.00 10.80 ?  96  VAL   A C    1 
ATOM   1931 O O    . VAL   A 1 96  ? 26.998 -5.374  -4.200  1.00 11.59 ?  96  VAL   A O    1 
ATOM   1932 C CB   . VAL   A 1 96  ? 28.439 -2.911  -3.691  1.00 10.86 ?  96  VAL   A CB   1 
ATOM   1933 C CG1  . VAL   A 1 96  ? 27.933 -2.265  -4.966  1.00 11.03 ?  96  VAL   A CG1  1 
ATOM   1934 C CG2  . VAL   A 1 96  ? 29.305 -1.944  -2.890  1.00 11.61 ?  96  VAL   A CG2  1 
ATOM   1935 H H    . VAL   A 1 96  ? 28.345 -4.470  -1.637  1.00 11.73 ?  96  VAL   A H    1 
ATOM   1936 H HA   . VAL   A 1 96  ? 26.672 -2.629  -2.702  1.00 12.38 ?  96  VAL   A HA   1 
ATOM   1937 H HB   . VAL   A 1 96  ? 28.985 -3.667  -3.938  1.00 13.03 ?  96  VAL   A HB   1 
ATOM   1938 H HG11 . VAL   A 1 96  ? 28.669 -1.784  -5.385  1.00 13.23 ?  96  VAL   A HG11 1 
ATOM   1939 H HG12 . VAL   A 1 96  ? 27.605 -2.949  -5.563  1.00 13.23 ?  96  VAL   A HG12 1 
ATOM   1940 H HG13 . VAL   A 1 96  ? 27.223 -1.640  -4.745  1.00 13.23 ?  96  VAL   A HG13 1 
ATOM   1941 H HG21 . VAL   A 1 96  ? 30.006 -1.594  -3.462  1.00 13.93 ?  96  VAL   A HG21 1 
ATOM   1942 H HG22 . VAL   A 1 96  ? 28.751 -1.213  -2.565  1.00 13.93 ?  96  VAL   A HG22 1 
ATOM   1943 H HG23 . VAL   A 1 96  ? 29.696 -2.417  -2.138  1.00 13.93 ?  96  VAL   A HG23 1 
ATOM   1944 N N    A GLY   A 1 97  ? 25.121 -4.278  -3.633  0.70 11.09 ?  97  GLY   A N    1 
ATOM   1945 N N    B GLY   A 1 97  ? 25.124 -4.254  -3.679  0.30 11.10 ?  97  GLY   A N    1 
ATOM   1946 C CA   A GLY   A 1 97  ? 24.290 -5.018  -4.544  0.70 11.66 ?  97  GLY   A CA   1 
ATOM   1947 C CA   B GLY   A 1 97  ? 24.305 -5.032  -4.574  0.30 11.48 ?  97  GLY   A CA   1 
ATOM   1948 C C    A GLY   A 1 97  ? 24.272 -4.319  -5.890  0.70 11.48 ?  97  GLY   A C    1 
ATOM   1949 C C    B GLY   A 1 97  ? 24.374 -4.475  -5.984  0.30 11.73 ?  97  GLY   A C    1 
ATOM   1950 O O    A GLY   A 1 97  ? 24.528 -3.114  -5.990  0.70 12.09 ?  97  GLY   A O    1 
ATOM   1951 O O    B GLY   A 1 97  ? 24.761 -3.321  -6.200  0.30 11.90 ?  97  GLY   A O    1 
ATOM   1952 H H    A GLY   A 1 97  ? 24.687 -3.737  -3.115  0.70 13.31 ?  97  GLY   A H    1 
ATOM   1953 H H    B GLY   A 1 97  ? 24.684 -3.685  -3.199  0.30 13.32 ?  97  GLY   A H    1 
ATOM   1954 H HA2  A GLY   A 1 97  ? 24.642 -5.914  -4.648  0.70 13.99 ?  97  GLY   A HA2  1 
ATOM   1955 H HA2  B GLY   A 1 97  ? 24.618 -5.951  -4.577  0.30 13.77 ?  97  GLY   A HA2  1 
ATOM   1956 H HA3  A GLY   A 1 97  ? 23.382 -5.074  -4.194  0.70 13.99 ?  97  GLY   A HA3  1 
ATOM   1957 H HA3  B GLY   A 1 97  ? 23.381 -5.021  -4.273  0.30 13.77 ?  97  GLY   A HA3  1 
ATOM   1958 N N    A PRO   A 1 98  ? 23.954 -5.054  -6.952  0.70 11.33 ?  98  PRO   A N    1 
ATOM   1959 N N    B PRO   A 1 98  ? 23.999 -5.281  -6.975  0.30 12.36 ?  98  PRO   A N    1 
ATOM   1960 C CA   A PRO   A 1 98  ? 23.840 -4.418  -8.267  0.70 11.95 ?  98  PRO   A CA   1 
ATOM   1961 C CA   B PRO   A 1 98  ? 23.996 -4.788  -8.358  0.30 13.24 ?  98  PRO   A CA   1 
ATOM   1962 C C    A PRO   A 1 98  ? 22.720 -3.388  -8.295  0.70 11.63 ?  98  PRO   A C    1 
ATOM   1963 C C    B PRO   A 1 98  ? 22.906 -3.749  -8.584  0.30 13.96 ?  98  PRO   A C    1 
ATOM   1964 O O    A PRO   A 1 98  ? 21.646 -3.585  -7.719  0.70 11.77 ?  98  PRO   A O    1 
ATOM   1965 O O    B PRO   A 1 98  ? 21.799 -3.850  -8.049  0.30 14.11 ?  98  PRO   A O    1 
ATOM   1966 C CB   A PRO   A 1 98  ? 23.541 -5.595  -9.201  0.70 12.49 ?  98  PRO   A CB   1 
ATOM   1967 C CB   B PRO   A 1 98  ? 23.729 -6.052  -9.182  0.30 12.75 ?  98  PRO   A CB   1 
ATOM   1968 C CG   A PRO   A 1 98  ? 22.899 -6.617  -8.323  0.70 12.97 ?  98  PRO   A CG   1 
ATOM   1969 C CG   B PRO   A 1 98  ? 23.005 -6.967  -8.243  0.30 12.84 ?  98  PRO   A CG   1 
ATOM   1970 C CD   A PRO   A 1 98  ? 23.628 -6.491  -7.006  0.70 12.08 ?  98  PRO   A CD   1 
ATOM   1971 C CD   B PRO   A 1 98  ? 23.604 -6.699  -6.891  0.30 12.30 ?  98  PRO   A CD   1 
ATOM   1972 H HA   A PRO   A 1 98  ? 24.679 -4.001  -8.510  0.70 14.34 ?  98  PRO   A HA   1 
ATOM   1973 H HA   B PRO   A 1 98  ? 24.867 -4.419  -8.592  0.30 15.88 ?  98  PRO   A HA   1 
ATOM   1974 H HB2  A PRO   A 1 98  ? 22.933 -5.307  -9.897  0.70 14.99 ?  98  PRO   A HB2  1 
ATOM   1975 H HB2  B PRO   A 1 98  ? 23.173 -5.829  -9.946  0.30 15.29 ?  98  PRO   A HB2  1 
ATOM   1976 H HB3  A PRO   A 1 98  ? 24.368 -5.930  -9.575  0.70 14.99 ?  98  PRO   A HB3  1 
ATOM   1977 H HB3  B PRO   A 1 98  ? 24.568 -6.444  -9.469  0.30 15.29 ?  98  PRO   A HB3  1 
ATOM   1978 H HG2  A PRO   A 1 98  ? 21.957 -6.415  -8.216  0.70 15.56 ?  98  PRO   A HG2  1 
ATOM   1979 H HG2  B PRO   A 1 98  ? 22.058 -6.753  -8.248  0.30 15.41 ?  98  PRO   A HG2  1 
ATOM   1980 H HG3  A PRO   A 1 98  ? 23.025 -7.499  -8.702  0.70 15.56 ?  98  PRO   A HG3  1 
ATOM   1981 H HG3  B PRO   A 1 98  ? 23.151 -7.887  -8.510  0.30 15.41 ?  98  PRO   A HG3  1 
ATOM   1982 H HD2  A PRO   A 1 98  ? 23.042 -6.743  -6.269  0.70 14.49 ?  98  PRO   A HD2  1 
ATOM   1983 H HD2  B PRO   A 1 98  ? 22.938 -6.824  -6.196  0.30 14.76 ?  98  PRO   A HD2  1 
ATOM   1984 H HD3  A PRO   A 1 98  ? 24.439 -7.021  -7.010  0.70 14.49 ?  98  PRO   A HD3  1 
ATOM   1985 H HD3  B PRO   A 1 98  ? 24.379 -7.265  -6.746  0.30 14.76 ?  98  PRO   A HD3  1 
ATOM   1986 N N    A ASN   A 1 99  ? 22.986 -2.279  -8.981  0.70 12.46 ?  99  ASN   A N    1 
ATOM   1987 N N    B ASN   A 1 99  ? 23.231 -2.746  -9.397  0.30 14.60 ?  99  ASN   A N    1 
ATOM   1988 C CA   A ASN   A 1 99  ? 22.007 -1.221  -9.202  0.70 13.30 ?  99  ASN   A CA   1 
ATOM   1989 C CA   B ASN   A 1 99  ? 22.283 -1.712  -9.803  0.30 15.71 ?  99  ASN   A CA   1 
ATOM   1990 C C    A ASN   A 1 99  ? 21.455 -1.382  -10.616 0.70 14.40 ?  99  ASN   A C    1 
ATOM   1991 C C    B ASN   A 1 99  ? 21.829 -2.032  -11.222 0.30 16.50 ?  99  ASN   A C    1 
ATOM   1992 O O    A ASN   A 1 99  ? 22.147 -1.095  -11.601 0.70 15.96 ?  99  ASN   A O    1 
ATOM   1993 O O    B ASN   A 1 99  ? 22.588 -1.848  -12.178 0.30 16.07 ?  99  ASN   A O    1 
ATOM   1994 C CB   A ASN   A 1 99  ? 22.655 0.151   -9.009  0.70 13.67 ?  99  ASN   A CB   1 
ATOM   1995 C CB   B ASN   A 1 99  ? 22.939 -0.335  -9.752  0.30 16.33 ?  99  ASN   A CB   1 
ATOM   1996 C CG   A ASN   A 1 99  ? 21.643 1.291   -9.022  0.70 13.84 ?  99  ASN   A CG   1 
ATOM   1997 C CG   B ASN   A 1 99  ? 21.968 0.790   -10.068 0.30 17.18 ?  99  ASN   A CG   1 
ATOM   1998 O OD1  A ASN   A 1 99  ? 20.657 1.250   -9.755  0.70 14.71 ?  99  ASN   A OD1  1 
ATOM   1999 O OD1  B ASN   A 1 99  ? 20.967 0.586   -10.750 0.30 17.56 ?  99  ASN   A OD1  1 
ATOM   2000 N ND2  A ASN   A 1 99  ? 21.889 2.312   -8.212  0.70 14.55 ?  99  ASN   A ND2  1 
ATOM   2001 N ND2  B ASN   A 1 99  ? 22.261 1.984   -9.570  0.30 18.02 ?  99  ASN   A ND2  1 
ATOM   2002 H H    A ASN   A 1 99  ? 23.758 -2.109  -9.316  0.70 14.96 ?  99  ASN   A H    1 
ATOM   2003 H H    B ASN   A 1 99  ? 24.016 -2.643  -9.731  0.30 17.52 ?  99  ASN   A H    1 
ATOM   2004 H HA   A ASN   A 1 99  ? 21.282 -1.312  -8.557  0.70 15.96 ?  99  ASN   A HA   1 
ATOM   2005 H HA   B ASN   A 1 99  ? 21.510 -1.724  -9.216  0.30 18.85 ?  99  ASN   A HA   1 
ATOM   2006 H HB2  A ASN   A 1 99  ? 23.121 0.172   -8.158  0.70 16.40 ?  99  ASN   A HB2  1 
ATOM   2007 H HB2  B ASN   A 1 99  ? 23.294 -0.187  -8.866  0.30 19.59 ?  99  ASN   A HB2  1 
ATOM   2008 H HB3  A ASN   A 1 99  ? 23.283 0.304   -9.733  0.70 16.40 ?  99  ASN   A HB3  1 
ATOM   2009 H HB3  B ASN   A 1 99  ? 23.651 -0.309  -10.410 0.30 19.59 ?  99  ASN   A HB3  1 
ATOM   2010 H HD21 A ASN   A 1 99  ? 21.345 2.978   -8.181  0.70 17.46 ?  99  ASN   A HD21 1 
ATOM   2011 H HD21 B ASN   A 1 99  ? 21.743 2.653   -9.723  0.30 21.63 ?  99  ASN   A HD21 1 
ATOM   2012 H HD22 A ASN   A 1 99  ? 22.591 2.308   -7.716  0.70 17.46 ?  99  ASN   A HD22 1 
ATOM   2013 H HD22 B ASN   A 1 99  ? 22.971 2.086   -9.099  0.30 21.63 ?  99  ASN   A HD22 1 
ATOM   2014 N N    A VAL   A 1 100 ? 20.208 -1.856  -10.705 0.70 14.72 ?  100 VAL   A N    1 
ATOM   2015 N N    B VAL   A 1 100 ? 20.591 -2.513  -11.359 0.30 18.45 ?  100 VAL   A N    1 
ATOM   2016 C CA   A VAL   A 1 100 ? 19.580 -2.089  -12.001 0.70 17.14 ?  100 VAL   A CA   1 
ATOM   2017 C CA   B VAL   A 1 100 ? 20.106 -2.922  -12.673 0.30 20.38 ?  100 VAL   A CA   1 
ATOM   2018 C C    A VAL   A 1 100 ? 19.452 -0.788  -12.783 0.70 17.66 ?  100 VAL   A C    1 
ATOM   2019 C C    B VAL   A 1 100 ? 19.896 -1.736  -13.608 0.30 21.40 ?  100 VAL   A C    1 
ATOM   2020 O O    A VAL   A 1 100 ? 19.508 -0.788  -14.019 0.70 19.22 ?  100 VAL   A O    1 
ATOM   2021 O O    B VAL   A 1 100 ? 19.790 -1.929  -14.824 0.30 21.64 ?  100 VAL   A O    1 
ATOM   2022 C CB   A VAL   A 1 100 ? 18.222 -2.801  -11.815 0.70 18.86 ?  100 VAL   A CB   1 
ATOM   2023 C CB   B VAL   A 1 100 ? 18.833 -3.779  -12.561 0.30 21.35 ?  100 VAL   A CB   1 
ATOM   2024 C CG1  A VAL   A 1 100 ? 17.534 -3.021  -13.155 0.70 19.65 ?  100 VAL   A CG1  1 
ATOM   2025 C CG1  B VAL   A 1 100 ? 19.178 -5.162  -12.038 0.30 21.78 ?  100 VAL   A CG1  1 
ATOM   2026 C CG2  A VAL   A 1 100 ? 18.414 -4.130  -11.094 0.70 19.55 ?  100 VAL   A CG2  1 
ATOM   2027 C CG2  B VAL   A 1 100 ? 17.825 -3.100  -11.661 0.30 21.63 ?  100 VAL   A CG2  1 
ATOM   2028 H H    A VAL   A 1 100 ? 19.707 -2.050  -10.022 0.70 17.66 ?  100 VAL   A H    1 
ATOM   2029 H H    B VAL   A 1 100 ? 20.030 -2.614  -10.714 0.30 22.14 ?  100 VAL   A H    1 
ATOM   2030 H HA   A VAL   A 1 100 ? 20.148 -2.684  -12.510 0.70 20.57 ?  100 VAL   A HA   1 
ATOM   2031 H HA   B VAL   A 1 100 ? 20.784 -3.485  -13.074 0.30 24.46 ?  100 VAL   A HA   1 
ATOM   2032 H HB   A VAL   A 1 100 ? 17.644 -2.248  -11.267 0.70 22.63 ?  100 VAL   A HB   1 
ATOM   2033 H HB   B VAL   A 1 100 ? 18.437 -3.875  -13.443 0.30 25.62 ?  100 VAL   A HB   1 
ATOM   2034 H HG11 A VAL   A 1 100 ? 16.780 -3.619  -13.027 0.70 23.58 ?  100 VAL   A HG11 1 
ATOM   2035 H HG11 B VAL   A 1 100 ? 18.363 -5.683  -11.969 0.30 26.14 ?  100 VAL   A HG11 1 
ATOM   2036 H HG12 A VAL   A 1 100 ? 17.225 -2.169  -13.496 0.70 23.58 ?  100 VAL   A HG12 1 
ATOM   2037 H HG12 B VAL   A 1 100 ? 19.793 -5.588  -12.655 0.30 26.14 ?  100 VAL   A HG12 1 
ATOM   2038 H HG13 A VAL   A 1 100 ? 18.167 -3.418  -13.773 0.70 23.58 ?  100 VAL   A HG13 1 
ATOM   2039 H HG13 B VAL   A 1 100 ? 19.591 -5.073  -11.166 0.30 26.14 ?  100 VAL   A HG13 1 
ATOM   2040 H HG21 A VAL   A 1 100 ? 17.563 -4.595  -11.056 0.70 23.46 ?  100 VAL   A HG21 1 
ATOM   2041 H HG21 B VAL   A 1 100 ? 16.953 -3.483  -11.828 0.30 25.95 ?  100 VAL   A HG21 1 
ATOM   2042 H HG22 A VAL   A 1 100 ? 19.061 -4.663  -11.581 0.70 23.46 ?  100 VAL   A HG22 1 
ATOM   2043 H HG22 B VAL   A 1 100 ? 18.082 -3.244  -10.738 0.30 25.95 ?  100 VAL   A HG22 1 
ATOM   2044 H HG23 A VAL   A 1 100 ? 18.736 -3.959  -10.194 0.70 23.46 ?  100 VAL   A HG23 1 
ATOM   2045 H HG23 B VAL   A 1 100 ? 17.815 -2.151  -11.861 0.30 25.95 ?  100 VAL   A HG23 1 
ATOM   2046 N N    A ASN   A 1 101 ? 19.282 0.336   -12.090 0.70 18.77 ?  101 ASN   A N    1 
ATOM   2047 N N    B ASN   A 1 101 ? 19.825 -0.513  -13.082 0.30 22.38 ?  101 ASN   A N    1 
ATOM   2048 C CA   A ASN   A 1 101 ? 19.220 1.624   -12.772 0.70 20.39 ?  101 ASN   A CA   1 
ATOM   2049 C CA   B ASN   A 1 101 ? 19.772 0.659   -13.949 0.30 23.47 ?  101 ASN   A CA   1 
ATOM   2050 C C    A ASN   A 1 101 ? 20.576 2.070   -13.321 0.70 22.40 ?  101 ASN   A C    1 
ATOM   2051 C C    B ASN   A 1 101 ? 21.125 0.983   -14.566 0.30 24.18 ?  101 ASN   A C    1 
ATOM   2052 O O    A ASN   A 1 101 ? 20.647 3.126   -13.964 0.70 23.92 ?  101 ASN   A O    1 
ATOM   2053 O O    B ASN   A 1 101 ? 21.172 1.633   -15.616 0.30 24.20 ?  101 ASN   A O    1 
ATOM   2054 C CB   A ASN   A 1 101 ? 18.596 2.667   -11.842 0.70 20.07 ?  101 ASN   A CB   1 
ATOM   2055 C CB   B ASN   A 1 101 ? 19.232 1.871   -13.188 0.30 24.01 ?  101 ASN   A CB   1 
ATOM   2056 C CG   A ASN   A 1 101 ? 17.215 2.247   -11.348 0.70 19.97 ?  101 ASN   A CG   1 
ATOM   2057 C CG   B ASN   A 1 101 ? 17.721 1.898   -13.147 0.30 24.62 ?  101 ASN   A CG   1 
ATOM   2058 O OD1  A ASN   A 1 101 ? 16.399 1.727   -12.115 0.70 20.49 ?  101 ASN   A OD1  1 
ATOM   2059 O OD1  B ASN   A 1 101 ? 17.100 1.295   -12.271 0.30 24.98 ?  101 ASN   A OD1  1 
ATOM   2060 N ND2  A ASN   A 1 101 ? 16.952 2.455   -10.064 0.70 20.01 ?  101 ASN   A ND2  1 
ATOM   2061 N ND2  B ASN   A 1 101 ? 17.118 2.594   -14.105 0.30 24.62 ?  101 ASN   A ND2  1 
ATOM   2062 H H    A ASN   A 1 101 ? 19.195 0.377   -11.235 0.70 22.52 ?  101 ASN   A H    1 
ATOM   2063 H H    B ASN   A 1 101 ? 19.803 -0.338  -12.241 0.30 26.85 ?  101 ASN   A H    1 
ATOM   2064 H HA   A ASN   A 1 101 ? 18.630 1.530   -13.530 0.70 24.46 ?  101 ASN   A HA   1 
ATOM   2065 H HA   B ASN   A 1 101 ? 19.157 0.475   -14.674 0.30 28.16 ?  101 ASN   A HA   1 
ATOM   2066 H HB2  A ASN   A 1 101 ? 19.168 2.791   -11.068 0.70 24.09 ?  101 ASN   A HB2  1 
ATOM   2067 H HB2  B ASN   A 1 101 ? 19.554 1.845   -12.275 0.30 28.81 ?  101 ASN   A HB2  1 
ATOM   2068 H HB3  A ASN   A 1 101 ? 18.503 3.504   -12.325 0.70 24.09 ?  101 ASN   A HB3  1 
ATOM   2069 H HB3  B ASN   A 1 101 ? 19.534 2.682   -13.626 0.30 28.81 ?  101 ASN   A HB3  1 
ATOM   2070 H HD21 A ASN   A 1 101 ? 16.185 2.237   -9.742  0.70 24.01 ?  101 ASN   A HD21 1 
ATOM   2071 H HD21 B ASN   A 1 101 ? 16.260 2.640   -14.130 0.30 29.55 ?  101 ASN   A HD21 1 
ATOM   2072 H HD22 A ASN   A 1 101 ? 17.542 2.821   -9.557  0.70 24.01 ?  101 ASN   A HD22 1 
ATOM   2073 H HD22 B ASN   A 1 101 ? 17.587 3.002   -14.702 0.30 29.55 ?  101 ASN   A HD22 1 
ATOM   2074 N N    A LYS   A 1 102 ? 21.634 1.281   -13.101 0.70 24.32 ?  102 LYS   A N    1 
ATOM   2075 N N    B LYS   A 1 102 ? 22.218 0.549   -13.942 0.30 24.69 ?  102 LYS   A N    1 
ATOM   2076 C CA   A LYS   A 1 102 ? 22.921 1.462   -13.761 0.70 26.03 ?  102 LYS   A CA   1 
ATOM   2077 C CA   B LYS   A 1 102 ? 23.554 0.684   -14.502 0.30 25.04 ?  102 LYS   A CA   1 
ATOM   2078 C C    A LYS   A 1 102 ? 23.226 0.359   -14.766 0.70 26.27 ?  102 LYS   A C    1 
ATOM   2079 C C    B LYS   A 1 102 ? 23.945 -0.498  -15.381 0.30 24.52 ?  102 LYS   A C    1 
ATOM   2080 O O    A LYS   A 1 102 ? 24.304 0.374   -15.369 0.70 26.84 ?  102 LYS   A O    1 
ATOM   2081 O O    B LYS   A 1 102 ? 25.105 -0.588  -15.794 0.30 24.81 ?  102 LYS   A O    1 
ATOM   2082 C CB   A LYS   A 1 102 ? 24.053 1.516   -12.727 0.70 27.48 ?  102 LYS   A CB   1 
ATOM   2083 C CB   B LYS   A 1 102 ? 24.588 0.840   -13.382 0.30 25.75 ?  102 LYS   A CB   1 
ATOM   2084 C CG   A LYS   A 1 102 ? 23.936 2.632   -11.705 0.70 28.80 ?  102 LYS   A CG   1 
ATOM   2085 C CG   B LYS   A 1 102 ? 24.402 2.069   -12.509 0.30 26.53 ?  102 LYS   A CG   1 
ATOM   2086 C CD   A LYS   A 1 102 ? 25.109 2.603   -10.732 0.70 30.12 ?  102 LYS   A CD   1 
ATOM   2087 C CD   B LYS   A 1 102 ? 25.351 2.023   -11.319 0.30 27.34 ?  102 LYS   A CD   1 
ATOM   2088 C CE   A LYS   A 1 102 ? 25.022 3.725   -9.708  0.70 31.10 ?  102 LYS   A CE   1 
ATOM   2089 C CE   B LYS   A 1 102 ? 25.130 3.188   -10.369 0.30 27.93 ?  102 LYS   A CE   1 
ATOM   2090 N NZ   A LYS   A 1 102 ? 26.134 3.658   -8.715  0.70 31.66 ?  102 LYS   A NZ   1 
ATOM   2091 N NZ   B LYS   A 1 102 ? 25.540 2.845   -8.976  0.30 28.36 ?  102 LYS   A NZ   1 
ATOM   2092 H H    A LYS   A 1 102 ? 21.626 0.608   -12.561 0.70 29.18 ?  102 LYS   A H    1 
ATOM   2093 H H    B LYS   A 1 102 ? 22.207 0.167   -13.173 0.30 29.63 ?  102 LYS   A H    1 
ATOM   2094 H HA   A LYS   A 1 102 ? 22.911 2.304   -14.237 0.70 31.23 ?  102 LYS   A HA   1 
ATOM   2095 H HA   B LYS   A 1 102 ? 23.590 1.483   -15.044 0.30 30.05 ?  102 LYS   A HA   1 
ATOM   2096 H HB2  A LYS   A 1 102 ? 24.070 0.675   -12.243 0.70 32.98 ?  102 LYS   A HB2  1 
ATOM   2097 H HB2  B LYS   A 1 102 ? 24.539 0.063   -12.805 0.30 30.91 ?  102 LYS   A HB2  1 
ATOM   2098 H HB3  A LYS   A 1 102 ? 24.893 1.636   -13.197 0.70 32.98 ?  102 LYS   A HB3  1 
ATOM   2099 H HB3  B LYS   A 1 102 ? 25.472 0.894   -13.781 0.30 30.91 ?  102 LYS   A HB3  1 
ATOM   2100 H HG2  A LYS   A 1 102 ? 23.937 3.487   -12.162 0.70 34.56 ?  102 LYS   A HG2  1 
ATOM   2101 H HG2  B LYS   A 1 102 ? 24.596 2.866   -13.027 0.30 31.84 ?  102 LYS   A HG2  1 
ATOM   2102 H HG3  A LYS   A 1 102 ? 23.115 2.519   -11.200 0.70 34.56 ?  102 LYS   A HG3  1 
ATOM   2103 H HG3  B LYS   A 1 102 ? 23.491 2.094   -12.177 0.30 31.84 ?  102 LYS   A HG3  1 
ATOM   2104 H HD2  A LYS   A 1 102 ? 25.108 1.757   -10.257 0.70 36.14 ?  102 LYS   A HD2  1 
ATOM   2105 H HD2  B LYS   A 1 102 ? 25.208 1.200   -10.828 0.30 32.81 ?  102 LYS   A HD2  1 
ATOM   2106 H HD3  A LYS   A 1 102 ? 25.937 2.707   -11.228 0.70 36.14 ?  102 LYS   A HD3  1 
ATOM   2107 H HD3  B LYS   A 1 102 ? 26.265 2.064   -11.641 0.30 32.81 ?  102 LYS   A HD3  1 
ATOM   2108 H HE2  A LYS   A 1 102 ? 25.075 4.579   -10.166 0.70 37.32 ?  102 LYS   A HE2  1 
ATOM   2109 H HE2  B LYS   A 1 102 ? 25.665 3.942   -10.664 0.30 33.52 ?  102 LYS   A HE2  1 
ATOM   2110 H HE3  A LYS   A 1 102 ? 24.181 3.654   -9.229  0.70 37.32 ?  102 LYS   A HE3  1 
ATOM   2111 H HE3  B LYS   A 1 102 ? 24.191 3.427   -10.364 0.30 33.52 ?  102 LYS   A HE3  1 
ATOM   2112 H HZ1  A LYS   A 1 102 ? 26.059 4.323   -8.129  0.70 38.00 ?  102 LYS   A HZ1  1 
ATOM   2113 H HZ1  B LYS   A 1 102 ? 25.402 3.541   -8.439  0.30 34.03 ?  102 LYS   A HZ1  1 
ATOM   2114 H HZ2  A LYS   A 1 102 ? 26.104 2.882   -8.278  0.70 38.00 ?  102 LYS   A HZ2  1 
ATOM   2115 H HZ2  B LYS   A 1 102 ? 25.064 2.153   -8.681  0.30 34.03 ?  102 LYS   A HZ2  1 
ATOM   2116 H HZ3  A LYS   A 1 102 ? 26.918 3.724   -9.131  0.70 38.00 ?  102 LYS   A HZ3  1 
ATOM   2117 H HZ3  B LYS   A 1 102 ? 26.404 2.631   -8.957  0.30 34.03 ?  102 LYS   A HZ3  1 
ATOM   2118 N N    A GLY   A 1 103 ? 22.319 -0.600  -14.954 0.70 26.53 ?  103 GLY   A N    1 
ATOM   2119 N N    B GLY   A 1 103 ? 23.016 -1.409  -15.666 0.30 23.80 ?  103 GLY   A N    1 
ATOM   2120 C CA   A GLY   A 1 103 ? 22.542 -1.695  -15.880 0.70 26.75 ?  103 GLY   A CA   1 
ATOM   2121 C CA   B GLY   A 1 103 ? 23.356 -2.577  -16.450 0.30 23.28 ?  103 GLY   A CA   1 
ATOM   2122 C C    A GLY   A 1 103 ? 23.358 -2.845  -15.336 0.70 26.98 ?  103 GLY   A C    1 
ATOM   2123 C C    B GLY   A 1 103 ? 24.059 -3.662  -15.675 0.30 22.90 ?  103 GLY   A C    1 
ATOM   2124 O O    A GLY   A 1 103 ? 23.832 -3.675  -16.117 0.70 27.96 ?  103 GLY   A O    1 
ATOM   2125 O O    B GLY   A 1 103 ? 24.572 -4.609  -16.284 0.30 22.83 ?  103 GLY   A O    1 
ATOM   2126 H H    A GLY   A 1 103 ? 21.562 -0.638  -14.554 0.70 31.84 ?  103 GLY   A H    1 
ATOM   2127 H H    B GLY   A 1 103 ? 22.192 -1.377  -15.408 0.30 28.56 ?  103 GLY   A H    1 
ATOM   2128 H HA2  A GLY   A 1 103 ? 21.682 -2.047  -16.165 0.70 32.10 ?  103 GLY   A HA2  1 
ATOM   2129 H HA2  B GLY   A 1 103 ? 22.555 -2.960  -16.834 0.30 27.93 ?  103 GLY   A HA2  1 
ATOM   2130 H HA3  A GLY   A 1 103 ? 22.998 -1.357  -16.667 0.70 32.10 ?  103 GLY   A HA3  1 
ATOM   2131 H HA3  B GLY   A 1 103 ? 23.943 -2.299  -17.173 0.30 27.93 ?  103 GLY   A HA3  1 
ATOM   2132 N N    A GLU   A 1 104 ? 23.528 -2.932  -14.020 0.70 25.90 ?  104 GLU   A N    1 
ATOM   2133 N N    B GLU   A 1 104 ? 24.090 -3.561  -14.352 0.30 22.33 ?  104 GLU   A N    1 
ATOM   2134 C CA   A GLU   A 1 104 ? 24.409 -3.930  -13.433 0.70 24.89 ?  104 GLU   A CA   1 
ATOM   2135 C CA   B GLU   A 1 104 ? 24.842 -4.499  -13.536 0.30 21.68 ?  104 GLU   A CA   1 
ATOM   2136 C C    A GLU   A 1 104 ? 23.724 -5.291  -13.332 0.70 25.59 ?  104 GLU   A C    1 
ATOM   2137 C C    B GLU   A 1 104 ? 24.085 -5.815  -13.405 0.30 21.57 ?  104 GLU   A C    1 
ATOM   2138 O O    A GLU   A 1 104 ? 22.506 -5.395  -13.155 0.70 26.04 ?  104 GLU   A O    1 
ATOM   2139 O O    B GLU   A 1 104 ? 22.867 -5.839  -13.205 0.30 21.28 ?  104 GLU   A O    1 
ATOM   2140 C CB   A GLU   A 1 104 ? 24.919 -3.444  -12.073 0.70 23.51 ?  104 GLU   A CB   1 
ATOM   2141 C CB   B GLU   A 1 104 ? 25.130 -3.886  -12.165 0.30 21.60 ?  104 GLU   A CB   1 
ATOM   2142 C CG   A GLU   A 1 104 ? 25.821 -2.215  -12.227 0.70 22.93 ?  104 GLU   A CG   1 
ATOM   2143 C CG   B GLU   A 1 104 ? 25.922 -2.584  -12.260 0.30 21.97 ?  104 GLU   A CG   1 
ATOM   2144 C CD   A GLU   A 1 104 ? 26.224 -1.537  -10.934 0.70 21.78 ?  104 GLU   A CD   1 
ATOM   2145 C CD   B GLU   A 1 104 ? 26.111 -1.887  -10.928 0.30 22.30 ?  104 GLU   A CD   1 
ATOM   2146 O OE1  A GLU   A 1 104 ? 25.618 -1.809  -9.876  0.70 19.85 ?  104 GLU   A OE1  1 
ATOM   2147 O OE1  B GLU   A 1 104 ? 25.783 -2.481  -9.882  0.30 22.53 ?  104 GLU   A OE1  1 
ATOM   2148 O OE2  A GLU   A 1 104 ? 27.154 -0.699  -10.999 0.70 22.20 -1 104 GLU   A OE2  1 
ATOM   2149 O OE2  B GLU   A 1 104 ? 26.584 -0.731  -10.933 0.30 22.50 -1 104 GLU   A OE2  1 
ATOM   2150 H H    A GLU   A 1 104 ? 23.146 -2.420  -13.448 0.70 31.07 ?  104 GLU   A H    1 
ATOM   2151 H H    B GLU   A 1 104 ? 23.674 -2.955  -13.908 0.30 26.79 ?  104 GLU   A H    1 
ATOM   2152 H HA   A GLU   A 1 104 ? 25.179 -4.034  -14.010 0.70 29.87 ?  104 GLU   A HA   1 
ATOM   2153 H HA   B GLU   A 1 104 ? 25.691 -4.681  -13.965 0.30 26.01 ?  104 GLU   A HA   1 
ATOM   2154 H HB2  A GLU   A 1 104 ? 24.163 -3.205  -11.515 0.70 28.21 ?  104 GLU   A HB2  1 
ATOM   2155 H HB2  B GLU   A 1 104 ? 24.291 -3.696  -11.719 0.30 25.92 ?  104 GLU   A HB2  1 
ATOM   2156 H HB3  A GLU   A 1 104 ? 25.434 -4.153  -11.655 0.70 28.21 ?  104 GLU   A HB3  1 
ATOM   2157 H HB3  B GLU   A 1 104 ? 25.651 -4.516  -11.642 0.30 25.92 ?  104 GLU   A HB3  1 
ATOM   2158 H HG2  A GLU   A 1 104 ? 26.637 -2.485  -12.669 0.70 27.52 ?  104 GLU   A HG2  1 
ATOM   2159 H HG2  B GLU   A 1 104 ? 26.799 -2.774  -12.629 0.30 26.37 ?  104 GLU   A HG2  1 
ATOM   2160 H HG3  A GLU   A 1 104 ? 25.355 -1.556  -12.761 0.70 27.52 ?  104 GLU   A HG3  1 
ATOM   2161 H HG3  B GLU   A 1 104 ? 25.449 -1.967  -12.839 0.30 26.37 ?  104 GLU   A HG3  1 
ATOM   2162 N N    A ASP   A 1 105 ? 24.535 -6.341  -13.456 0.70 26.29 ?  105 ASP   A N    1 
ATOM   2163 N N    B ASP   A 1 105 ? 24.828 -6.911  -13.527 0.30 22.35 ?  105 ASP   A N    1 
ATOM   2164 C CA   A ASP   A 1 105 ? 24.039 -7.709  -13.572 0.70 27.31 ?  105 ASP   A CA   1 
ATOM   2165 C CA   B ASP   A 1 105 ? 24.241 -8.241  -13.617 0.30 23.23 ?  105 ASP   A CA   1 
ATOM   2166 C C    A ASP   A 1 105 ? 23.361 -8.148  -12.279 0.70 25.54 ?  105 ASP   A C    1 
ATOM   2167 C C    B ASP   A 1 105 ? 23.514 -8.603  -12.329 0.30 22.44 ?  105 ASP   A C    1 
ATOM   2168 O O    A ASP   A 1 105 ? 23.980 -8.134  -11.212 0.70 23.90 ?  105 ASP   A O    1 
ATOM   2169 O O    B ASP   A 1 105 ? 24.120 -8.654  -11.254 0.30 21.24 ?  105 ASP   A O    1 
ATOM   2170 C CB   A ASP   A 1 105 ? 25.216 -8.631  -13.880 0.70 30.04 ?  105 ASP   A CB   1 
ATOM   2171 C CB   B ASP   A 1 105 ? 25.356 -9.244  -13.902 0.30 24.90 ?  105 ASP   A CB   1 
ATOM   2172 C CG   A ASP   A 1 105 ? 24.782 -10.044 -14.195 0.70 32.35 ?  105 ASP   A CG   1 
ATOM   2173 C CG   B ASP   A 1 105 ? 24.882 -10.672 -13.856 0.30 26.35 ?  105 ASP   A CG   1 
ATOM   2174 O OD1  A ASP   A 1 105 ? 23.560 -10.295 -14.231 0.70 32.69 ?  105 ASP   A OD1  1 
ATOM   2175 O OD1  B ASP   A 1 105 ? 23.783 -10.943 -14.378 0.30 27.09 ?  105 ASP   A OD1  1 
ATOM   2176 O OD2  A ASP   A 1 105 ? 25.668 -10.900 -14.414 0.70 33.68 -1 105 ASP   A OD2  1 
ATOM   2177 O OD2  B ASP   A 1 105 ? 25.624 -11.524 -13.323 0.30 26.95 -1 105 ASP   A OD2  1 
ATOM   2178 H H    A ASP   A 1 105 ? 25.394 -6.283  -13.487 0.70 31.55 ?  105 ASP   A H    1 
ATOM   2179 H H    B ASP   A 1 105 ? 25.684 -6.904  -13.563 0.30 26.82 ?  105 ASP   A H    1 
ATOM   2180 H HA   A ASP   A 1 105 ? 23.398 -7.768  -14.296 0.70 32.77 ?  105 ASP   A HA   1 
ATOM   2181 H HA   B ASP   A 1 105 ? 23.604 -8.266  -14.347 0.30 27.87 ?  105 ASP   A HA   1 
ATOM   2182 H HB2  A ASP   A 1 105 ? 25.693 -8.292  -14.652 0.70 36.05 ?  105 ASP   A HB2  1 
ATOM   2183 H HB2  B ASP   A 1 105 ? 25.702 -9.087  -14.792 0.30 29.89 ?  105 ASP   A HB2  1 
ATOM   2184 H HB3  A ASP   A 1 105 ? 25.808 -8.656  -13.109 0.70 36.05 ?  105 ASP   A HB3  1 
ATOM   2185 H HB3  B ASP   A 1 105 ? 26.059 -9.129  -13.243 0.30 29.89 ?  105 ASP   A HB3  1 
ATOM   2186 N N    A ILE   A 1 106 ? 22.103 -8.584  -12.382 0.70 25.50 ?  106 ILE   A N    1 
ATOM   2187 N N    B ILE   A 1 106 ? 22.210 -8.867  -12.443 0.30 23.04 ?  106 ILE   A N    1 
ATOM   2188 C CA   A ILE   A 1 106 ? 21.350 -8.984  -11.199 0.70 24.97 ?  106 ILE   A CA   1 
ATOM   2189 C CA   B ILE   A 1 106 ? 21.410 -9.212  -11.274 0.30 23.68 ?  106 ILE   A CA   1 
ATOM   2190 C C    A ILE   A 1 106 ? 21.882 -10.276 -10.598 0.70 23.99 ?  106 ILE   A C    1 
ATOM   2191 C C    B ILE   A 1 106 ? 21.914 -10.483 -10.610 0.30 23.78 ?  106 ILE   A C    1 
ATOM   2192 O O    A ILE   A 1 106 ? 21.663 -10.529 -9.409  0.70 23.22 ?  106 ILE   A O    1 
ATOM   2193 O O    B ILE   A 1 106 ? 21.683 -10.685 -9.413  0.30 23.80 ?  106 ILE   A O    1 
ATOM   2194 C CB   A ILE   A 1 106 ? 19.843 -9.069  -11.517 0.70 26.40 ?  106 ILE   A CB   1 
ATOM   2195 C CB   B ILE   A 1 106 ? 19.909 -9.286  -11.638 0.30 24.51 ?  106 ILE   A CB   1 
ATOM   2196 C CG1  A ILE   A 1 106 ? 19.014 -9.161  -10.231 0.70 26.94 ?  106 ILE   A CG1  1 
ATOM   2197 C CG1  B ILE   A 1 106 ? 19.047 -9.364  -10.373 0.30 24.92 ?  106 ILE   A CG1  1 
ATOM   2198 C CG2  A ILE   A 1 106 ? 19.551 -10.257 -12.417 0.70 26.86 ?  106 ILE   A CG2  1 
ATOM   2199 C CG2  B ILE   A 1 106 ? 19.629 -10.474 -12.544 0.30 24.70 ?  106 ILE   A CG2  1 
ATOM   2200 C CD1  A ILE   A 1 106 ? 19.110 -7.935  -9.350  0.70 27.31 ?  106 ILE   A CD1  1 
ATOM   2201 C CD1  B ILE   A 1 106 ? 19.153 -8.142  -9.481  0.30 25.12 ?  106 ILE   A CD1  1 
ATOM   2202 H H    A ILE   A 1 106 ? 21.677 -8.662  -13.119 0.70 30.60 ?  106 ILE   A H    1 
ATOM   2203 H H    B ILE   A 1 106 ? 21.772 -8.849  -13.179 0.30 27.64 ?  106 ILE   A H    1 
ATOM   2204 H HA   A ILE   A 1 106 ? 21.468 -8.301  -10.528 0.70 29.96 ?  106 ILE   A HA   1 
ATOM   2205 H HA   B ILE   A 1 106 ? 21.514 -8.505  -10.625 0.30 28.42 ?  106 ILE   A HA   1 
ATOM   2206 H HB   A ILE   A 1 106 ? 19.588 -8.261  -11.986 0.70 31.68 ?  106 ILE   A HB   1 
ATOM   2207 H HB   B ILE   A 1 106 ? 19.671 -8.476  -12.115 0.30 29.42 ?  106 ILE   A HB   1 
ATOM   2208 H HG12 A ILE   A 1 106 ? 18.082 -9.278  -10.471 0.70 32.32 ?  106 ILE   A HG12 1 
ATOM   2209 H HG12 B ILE   A 1 106 ? 18.118 -9.454  -10.634 0.30 29.90 ?  106 ILE   A HG12 1 
ATOM   2210 H HG13 A ILE   A 1 106 ? 19.318 -9.922  -9.713  0.70 32.32 ?  106 ILE   A HG13 1 
ATOM   2211 H HG13 B ILE   A 1 106 ? 19.318 -10.134 -9.852  0.30 29.90 ?  106 ILE   A HG13 1 
ATOM   2212 H HG21 A ILE   A 1 106 ? 18.644 -10.180 -12.752 0.70 32.23 ?  106 ILE   A HG21 1 
ATOM   2213 H HG21 B ILE   A 1 106 ? 18.720 -10.406 -12.878 0.30 29.64 ?  106 ILE   A HG21 1 
ATOM   2214 H HG22 A ILE   A 1 106 ? 20.179 -10.253 -13.156 0.70 32.23 ?  106 ILE   A HG22 1 
ATOM   2215 H HG22 B ILE   A 1 106 ? 20.255 -10.457 -13.283 0.30 29.64 ?  106 ILE   A HG22 1 
ATOM   2216 H HG23 A ILE   A 1 106 ? 19.647 -11.074 -11.904 0.70 32.23 ?  106 ILE   A HG23 1 
ATOM   2217 H HG23 B ILE   A 1 106 ? 19.734 -11.292 -12.036 0.30 29.64 ?  106 ILE   A HG23 1 
ATOM   2218 H HD11 A ILE   A 1 106 ? 18.403 -7.969  -8.688  0.70 32.78 ?  106 ILE   A HD11 1 
ATOM   2219 H HD11 B ILE   A 1 106 ? 18.426 -8.156  -8.840  0.30 30.14 ?  106 ILE   A HD11 1 
ATOM   2220 H HD12 A ILE   A 1 106 ? 19.975 -7.927  -8.910  0.70 32.78 ?  106 ILE   A HD12 1 
ATOM   2221 H HD12 B ILE   A 1 106 ? 20.004 -8.161  -9.015  0.30 30.14 ?  106 ILE   A HD12 1 
ATOM   2222 H HD13 A ILE   A 1 106 ? 19.010 -7.143  -9.901  0.70 32.78 ?  106 ILE   A HD13 1 
ATOM   2223 H HD13 B ILE   A 1 106 ? 19.093 -7.344  -10.030 0.30 30.14 ?  106 ILE   A HD13 1 
ATOM   2224 N N    A GLN   A 1 107 ? 22.600 -11.091 -11.382 0.70 24.51 ?  107 GLN   A N    1 
ATOM   2225 N N    B GLN   A 1 107 ? 22.612 -11.347 -11.353 0.30 24.00 ?  107 GLN   A N    1 
ATOM   2226 C CA   A GLN   A 1 107 ? 23.185 -12.318 -10.847 0.70 26.23 ?  107 GLN   A CA   1 
ATOM   2227 C CA   B GLN   A 1 107 ? 23.249 -12.499 -10.727 0.30 24.68 ?  107 GLN   A CA   1 
ATOM   2228 C C    A GLN   A 1 107 ? 24.150 -12.019 -9.707  0.70 23.57 ?  107 GLN   A C    1 
ATOM   2229 C C    B GLN   A 1 107 ? 24.274 -12.079 -9.680  0.30 22.47 ?  107 GLN   A C    1 
ATOM   2230 O O    A GLN   A 1 107 ? 24.344 -12.852 -8.814  0.70 24.67 ?  107 GLN   A O    1 
ATOM   2231 O O    B GLN   A 1 107 ? 24.642 -12.897 -8.829  0.30 22.93 ?  107 GLN   A O    1 
ATOM   2232 C CB   A GLN   A 1 107 ? 23.893 -13.087 -11.968 0.70 30.30 ?  107 GLN   A CB   1 
ATOM   2233 C CB   B GLN   A 1 107 ? 23.906 -13.404 -11.777 0.30 27.44 ?  107 GLN   A CB   1 
ATOM   2234 C CG   A GLN   A 1 107 ? 23.036 -13.283 -13.212 0.70 34.45 ?  107 GLN   A CG   1 
ATOM   2235 C CG   B GLN   A 1 107 ? 23.069 -13.651 -13.028 0.30 30.11 ?  107 GLN   A CG   1 
ATOM   2236 C CD   A GLN   A 1 107 ? 21.782 -14.090 -12.934 0.70 37.73 ?  107 GLN   A CD   1 
ATOM   2237 C CD   B GLN   A 1 107 ? 21.672 -14.151 -12.720 0.30 32.41 ?  107 GLN   A CD   1 
ATOM   2238 O OE1  A GLN   A 1 107 ? 21.840 -15.146 -12.303 0.70 39.01 ?  107 GLN   A OE1  1 
ATOM   2239 O OE1  B GLN   A 1 107 ? 21.488 -15.067 -11.918 0.30 33.23 ?  107 GLN   A OE1  1 
ATOM   2240 N NE2  A GLN   A 1 107 ? 20.640 -13.594 -13.398 0.70 39.01 ?  107 GLN   A NE2  1 
ATOM   2241 N NE2  B GLN   A 1 107 ? 20.675 -13.546 -13.358 0.30 33.28 ?  107 GLN   A NE2  1 
ATOM   2242 H H    A GLN   A 1 107 ? 22.776 -10.947 -12.212 0.70 29.42 ?  107 GLN   A H    1 
ATOM   2243 H H    B GLN   A 1 107 ? 22.724 -11.287 -12.204 0.30 28.81 ?  107 GLN   A H    1 
ATOM   2244 H HA   A GLN   A 1 107 ? 22.484 -12.885 -10.502 0.70 31.47 ?  107 GLN   A HA   1 
ATOM   2245 H HA   B GLN   A 1 107 ? 22.569 -13.029 -10.284 0.30 29.62 ?  107 GLN   A HA   1 
ATOM   2246 H HB2  A GLN   A 1 107 ? 24.692 -12.605 -12.235 0.70 36.35 ?  107 GLN   A HB2  1 
ATOM   2247 H HB2  B GLN   A 1 107 ? 24.751 -13.018 -12.048 0.30 32.93 ?  107 GLN   A HB2  1 
ATOM   2248 H HB3  A GLN   A 1 107 ? 24.139 -13.971 -11.645 0.70 36.35 ?  107 GLN   A HB3  1 
ATOM   2249 H HB3  B GLN   A 1 107 ? 24.070 -14.270 -11.374 0.30 32.93 ?  107 GLN   A HB3  1 
ATOM   2250 H HG2  A GLN   A 1 107 ? 22.769 -12.417 -13.559 0.70 41.34 ?  107 GLN   A HG2  1 
ATOM   2251 H HG2  B GLN   A 1 107 ? 22.980 -12.826 -13.525 0.30 36.14 ?  107 GLN   A HG2  1 
ATOM   2252 H HG3  A GLN   A 1 107 ? 23.555 -13.757 -13.879 0.70 41.34 ?  107 GLN   A HG3  1 
ATOM   2253 H HG3  B GLN   A 1 107 ? 23.512 -14.317 -13.578 0.30 36.14 ?  107 GLN   A HG3  1 
ATOM   2254 H HE21 A GLN   A 1 107 ? 20.637 -12.853 -13.834 0.70 46.81 ?  107 GLN   A HE21 1 
ATOM   2255 H HE21 B GLN   A 1 107 ? 20.842 -12.907 -13.910 0.30 39.93 ?  107 GLN   A HE21 1 
ATOM   2256 H HE22 A GLN   A 1 107 ? 19.902 -14.016 -13.264 0.70 46.81 ?  107 GLN   A HE22 1 
ATOM   2257 H HE22 B GLN   A 1 107 ? 19.864 -13.793 -13.220 0.30 39.93 ?  107 GLN   A HE22 1 
ATOM   2258 N N    . LEU   A 1 108 ? 24.743 -10.826 -9.709  1.00 19.98 ?  108 LEU   A N    1 
ATOM   2259 C CA   . LEU   A 1 108 ? 25.651 -10.387 -8.661  1.00 16.45 ?  108 LEU   A CA   1 
ATOM   2260 C C    . LEU   A 1 108 ? 24.949 -10.216 -7.323  1.00 14.58 ?  108 LEU   A C    1 
ATOM   2261 O O    . LEU   A 1 108 ? 25.633 -10.067 -6.308  1.00 14.72 ?  108 LEU   A O    1 
ATOM   2262 C CB   . LEU   A 1 108 ? 26.372 -9.096  -9.075  1.00 16.00 ?  108 LEU   A CB   1 
ATOM   2263 C CG   . LEU   A 1 108 ? 27.389 -9.305  -10.199 1.00 17.38 ?  108 LEU   A CG   1 
ATOM   2264 C CD1  . LEU   A 1 108 ? 27.892 -7.979  -10.745 1.00 18.00 ?  108 LEU   A CD1  1 
ATOM   2265 C CD2  . LEU   A 1 108 ? 28.561 -10.149 -9.715  1.00 19.11 ?  108 LEU   A CD2  1 
ATOM   2266 H H    A LEU   A 1 108 ? 24.628 -10.245 -10.327 0.70 23.97 ?  108 LEU   A H    1 
ATOM   2267 H H    B LEU   A 1 108 ? 24.561 -10.243 -10.309 0.30 23.97 ?  108 LEU   A H    1 
ATOM   2268 H HA   . LEU   A 1 108 ? 26.326 -11.069 -8.534  1.00 19.74 ?  108 LEU   A HA   1 
ATOM   2269 H HB2  . LEU   A 1 108 ? 25.712 -8.456  -9.390  1.00 19.20 ?  108 LEU   A HB2  1 
ATOM   2270 H HB3  . LEU   A 1 108 ? 26.841 -8.738  -8.310  1.00 19.20 ?  108 LEU   A HB3  1 
ATOM   2271 H HG   . LEU   A 1 108 ? 26.963 -9.785  -10.927 1.00 20.85 ?  108 LEU   A HG   1 
ATOM   2272 H HD11 . LEU   A 1 108 ? 28.504 -8.151  -11.480 1.00 21.60 ?  108 LEU   A HD11 1 
ATOM   2273 H HD12 . LEU   A 1 108 ? 27.137 -7.460  -11.059 1.00 21.60 ?  108 LEU   A HD12 1 
ATOM   2274 H HD13 . LEU   A 1 108 ? 28.354 -7.500  -10.039 1.00 21.60 ?  108 LEU   A HD13 1 
ATOM   2275 H HD21 . LEU   A 1 108 ? 29.279 -10.091 -10.361 1.00 22.94 ?  108 LEU   A HD21 1 
ATOM   2276 H HD22 . LEU   A 1 108 ? 28.857 -9.809  -8.856  1.00 22.94 ?  108 LEU   A HD22 1 
ATOM   2277 H HD23 . LEU   A 1 108 ? 28.270 -11.070 -9.623  1.00 22.94 ?  108 LEU   A HD23 1 
ATOM   2278 N N    . LEU   A 1 109 ? 23.616 -10.270 -7.286  1.00 14.07 ?  109 LEU   A N    1 
ATOM   2279 C CA   . LEU   A 1 109 ? 22.919 -10.153 -6.013  1.00 13.43 ?  109 LEU   A CA   1 
ATOM   2280 C C    . LEU   A 1 109 ? 23.265 -11.308 -5.079  1.00 12.36 ?  109 LEU   A C    1 
ATOM   2281 O O    . LEU   A 1 109 ? 23.398 -11.114 -3.867  1.00 12.94 ?  109 LEU   A O    1 
ATOM   2282 C CB   . LEU   A 1 109 ? 21.413 -10.066 -6.259  1.00 13.97 ?  109 LEU   A CB   1 
ATOM   2283 C CG   . LEU   A 1 109 ? 20.531 -9.767  -5.051  1.00 14.29 ?  109 LEU   A CG   1 
ATOM   2284 C CD1  . LEU   A 1 109 ? 20.994 -8.497  -4.360  1.00 14.57 ?  109 LEU   A CD1  1 
ATOM   2285 C CD2  . LEU   A 1 109 ? 19.078 -9.637  -5.480  1.00 15.35 ?  109 LEU   A CD2  1 
ATOM   2286 H H    . LEU   A 1 109 ? 23.103 -10.371 -7.969  1.00 16.88 ?  109 LEU   A H    1 
ATOM   2287 H HA   . LEU   A 1 109 ? 23.199 -9.332  -5.582  1.00 16.11 ?  109 LEU   A HA   1 
ATOM   2288 H HB2  . LEU   A 1 109 ? 21.252 -9.363  -6.907  1.00 16.76 ?  109 LEU   A HB2  1 
ATOM   2289 H HB3  . LEU   A 1 109 ? 21.114 -10.913 -6.623  1.00 16.76 ?  109 LEU   A HB3  1 
ATOM   2290 H HG   . LEU   A 1 109 ? 20.591 -10.497 -4.418  1.00 17.14 ?  109 LEU   A HG   1 
ATOM   2291 H HD11 . LEU   A 1 109 ? 20.319 -8.207  -3.732  1.00 17.48 ?  109 LEU   A HD11 1 
ATOM   2292 H HD12 . LEU   A 1 109 ? 21.828 -8.675  -3.896  1.00 17.48 ?  109 LEU   A HD12 1 
ATOM   2293 H HD13 . LEU   A 1 109 ? 21.136 -7.805  -5.032  1.00 17.48 ?  109 LEU   A HD13 1 
ATOM   2294 H HD21 . LEU   A 1 109 ? 18.547 -9.341  -4.722  1.00 18.42 ?  109 LEU   A HD21 1 
ATOM   2295 H HD22 . LEU   A 1 109 ? 19.014 -8.987  -6.198  1.00 18.42 ?  109 LEU   A HD22 1 
ATOM   2296 H HD23 . LEU   A 1 109 ? 18.758 -10.501 -5.788  1.00 18.42 ?  109 LEU   A HD23 1 
ATOM   2297 N N    . LYS   A 1 110 ? 23.411 -12.521 -5.617  1.00 12.40 ?  110 LYS   A N    1 
ATOM   2298 C CA   . LYS   A 1 110 ? 23.796 -13.644 -4.767  1.00 12.25 ?  110 LYS   A CA   1 
ATOM   2299 C C    . LYS   A 1 110 ? 25.178 -13.419 -4.161  1.00 11.83 ?  110 LYS   A C    1 
ATOM   2300 O O    . LYS   A 1 110 ? 25.379 -13.620 -2.960  1.00 12.11 ?  110 LYS   A O    1 
ATOM   2301 C CB   . LYS   A 1 110 ? 23.720 -14.961 -5.545  1.00 12.95 ?  110 LYS   A CB   1 
ATOM   2302 C CG   . LYS   A 1 110 ? 23.925 -16.181 -4.648  1.00 13.55 ?  110 LYS   A CG   1 
ATOM   2303 C CD   . LYS   A 1 110 ? 23.670 -17.494 -5.363  1.00 13.89 ?  110 LYS   A CD   1 
ATOM   2304 C CE   . LYS   A 1 110 ? 23.789 -18.681 -4.418  1.00 14.88 ?  110 LYS   A CE   1 
ATOM   2305 N NZ   . LYS   A 1 110 ? 22.619 -18.819 -3.512  1.00 15.07 ?  110 LYS   A NZ   1 
ATOM   2306 H H    . LYS   A 1 110 ? 23.297 -12.713 -6.444  1.00 14.88 ?  110 LYS   A H    1 
ATOM   2307 H HA   . LYS   A 1 110 ? 23.161 -13.706 -4.034  1.00 14.70 ?  110 LYS   A HA   1 
ATOM   2308 H HB2  . LYS   A 1 110 ? 22.846 -15.034 -5.960  1.00 15.55 ?  110 LYS   A HB2  1 
ATOM   2309 H HB3  . LYS   A 1 110 ? 24.413 -14.966 -6.224  1.00 15.55 ?  110 LYS   A HB3  1 
ATOM   2310 H HG2  . LYS   A 1 110 ? 24.840 -16.187 -4.328  1.00 16.26 ?  110 LYS   A HG2  1 
ATOM   2311 H HG3  . LYS   A 1 110 ? 23.312 -16.125 -3.898  1.00 16.26 ?  110 LYS   A HG3  1 
ATOM   2312 H HD2  . LYS   A 1 110 ? 22.773 -17.487 -5.731  1.00 16.66 ?  110 LYS   A HD2  1 
ATOM   2313 H HD3  . LYS   A 1 110 ? 24.323 -17.601 -6.072  1.00 16.66 ?  110 LYS   A HD3  1 
ATOM   2314 H HE2  . LYS   A 1 110 ? 23.862 -19.494 -4.941  1.00 17.85 ?  110 LYS   A HE2  1 
ATOM   2315 H HE3  . LYS   A 1 110 ? 24.581 -18.568 -3.868  1.00 17.85 ?  110 LYS   A HE3  1 
ATOM   2316 H HZ1  . LYS   A 1 110 ? 22.726 -19.522 -2.979  1.00 18.09 ?  110 LYS   A HZ1  1 
ATOM   2317 H HZ2  . LYS   A 1 110 ? 22.531 -18.086 -3.014  1.00 18.09 ?  110 LYS   A HZ2  1 
ATOM   2318 H HZ3  . LYS   A 1 110 ? 21.875 -18.931 -3.992  1.00 18.09 ?  110 LYS   A HZ3  1 
ATOM   2319 N N    . SER   A 1 111 ? 26.139 -12.980 -4.979  1.00 11.89 ?  111 SER   A N    1 
ATOM   2320 C CA   . SER   A 1 111 ? 27.467 -12.670 -4.460  1.00 11.95 ?  111 SER   A CA   1 
ATOM   2321 C C    . SER   A 1 111 ? 27.397 -11.630 -3.348  1.00 11.62 ?  111 SER   A C    1 
ATOM   2322 O O    . SER   A 1 111 ? 28.095 -11.731 -2.335  1.00 12.24 ?  111 SER   A O    1 
ATOM   2323 C CB   . SER   A 1 111 ? 28.368 -12.172 -5.594  1.00 13.28 ?  111 SER   A CB   1 
ATOM   2324 O OG   . SER   A 1 111 ? 28.470 -13.153 -6.616  1.00 15.17 ?  111 SER   A OG   1 
ATOM   2325 H H    . SER   A 1 111 ? 26.038 -12.850 -5.822  1.00 14.27 ?  111 SER   A H    1 
ATOM   2326 H HA   . SER   A 1 111 ? 27.858 -13.477 -4.095  1.00 14.34 ?  111 SER   A HA   1 
ATOM   2327 H HB2  . SER   A 1 111 ? 27.983 -11.368 -5.975  1.00 15.93 ?  111 SER   A HB2  1 
ATOM   2328 H HB3  . SER   A 1 111 ? 29.249 -11.982 -5.236  1.00 15.93 ?  111 SER   A HB3  1 
ATOM   2329 H HG   . SER   A 1 111 ? 28.984 -12.871 -7.229  1.00 18.20 ?  111 SER   A HG   1 
ATOM   2330 N N    . ALA   A 1 112 ? 26.552 -10.611 -3.525  1.00 11.86 ?  112 ALA   A N    1 
ATOM   2331 C CA   . ALA   A 1 112 ? 26.404 -9.577  -2.504  1.00 11.57 ?  112 ALA   A CA   1 
ATOM   2332 C C    . ALA   A 1 112 ? 25.930 -10.177 -1.186  1.00 11.50 ?  112 ALA   A C    1 
ATOM   2333 O O    . ALA   A 1 112 ? 26.483 -9.888  -0.119  1.00 11.87 ?  112 ALA   A O    1 
ATOM   2334 C CB   . ALA   A 1 112 ? 25.443 -8.488  -2.989  1.00 12.25 ?  112 ALA   A CB   1 
ATOM   2335 H H    . ALA   A 1 112 ? 26.067 -10.487 -4.223  1.00 14.23 ?  112 ALA   A H    1 
ATOM   2336 H HA   . ALA   A 1 112 ? 27.265 -9.154  -2.344  1.00 13.88 ?  112 ALA   A HA   1 
ATOM   2337 H HB1  . ALA   A 1 112 ? 25.370 -7.797  -2.305  1.00 14.71 ?  112 ALA   A HB1  1 
ATOM   2338 H HB2  . ALA   A 1 112 ? 25.786 -8.099  -3.808  1.00 14.71 ?  112 ALA   A HB2  1 
ATOM   2339 H HB3  . ALA   A 1 112 ? 24.570 -8.881  -3.149  1.00 14.71 ?  112 ALA   A HB3  1 
ATOM   2340 N N    . TYR   A 1 113 ? 24.898 -11.024 -1.239  1.00 11.58 ?  113 TYR   A N    1 
ATOM   2341 C CA   . TYR   A 1 113 ? 24.389 -11.627 -0.010  1.00 11.54 ?  113 TYR   A CA   1 
ATOM   2342 C C    . TYR   A 1 113 ? 25.392 -12.584 0.632   1.00 10.99 ?  113 TYR   A C    1 
ATOM   2343 O O    . TYR   A 1 113 ? 25.353 -12.778 1.851   1.00 11.61 ?  113 TYR   A O    1 
ATOM   2344 C CB   . TYR   A 1 113 ? 23.072 -12.356 -0.287  1.00 12.18 ?  113 TYR   A CB   1 
ATOM   2345 C CG   . TYR   A 1 113 ? 21.853 -11.457 -0.199  1.00 12.10 ?  113 TYR   A CG   1 
ATOM   2346 C CD1  . TYR   A 1 113 ? 21.492 -10.868 1.007   1.00 12.16 ?  113 TYR   A CD1  1 
ATOM   2347 C CD2  . TYR   A 1 113 ? 21.045 -11.227 -1.307  1.00 12.42 ?  113 TYR   A CD2  1 
ATOM   2348 C CE1  . TYR   A 1 113 ? 20.365 -10.069 1.106   1.00 12.55 ?  113 TYR   A CE1  1 
ATOM   2349 C CE2  . TYR   A 1 113 ? 19.904 -10.417 -1.216  1.00 12.31 ?  113 TYR   A CE2  1 
ATOM   2350 C CZ   . TYR   A 1 113 ? 19.578 -9.848  -0.007  1.00 12.36 ?  113 TYR   A CZ   1 
ATOM   2351 O OH   . TYR   A 1 113 ? 18.451 -9.054  0.103   1.00 13.58 ?  113 TYR   A OH   1 
ATOM   2352 H H    . TYR   A 1 113 ? 24.491 -11.258 -1.959  1.00 13.90 ?  113 TYR   A H    1 
ATOM   2353 H HA   . TYR   A 1 113 ? 24.213 -10.919 0.626   1.00 13.84 ?  113 TYR   A HA   1 
ATOM   2354 H HB2  . TYR   A 1 113 ? 23.096 -12.724 -1.182  1.00 14.62 ?  113 TYR   A HB2  1 
ATOM   2355 H HB3  . TYR   A 1 113 ? 22.963 -13.062 0.363   1.00 14.62 ?  113 TYR   A HB3  1 
ATOM   2356 H HD1  . TYR   A 1 113 ? 22.020 -11.018 1.760   1.00 14.59 ?  113 TYR   A HD1  1 
ATOM   2357 H HD2  . TYR   A 1 113 ? 21.262 -11.619 -2.119  1.00 14.90 ?  113 TYR   A HD2  1 
ATOM   2358 H HE1  . TYR   A 1 113 ? 20.144 -9.681  1.920   1.00 15.06 ?  113 TYR   A HE1  1 
ATOM   2359 H HE2  . TYR   A 1 113 ? 19.366 -10.269 -1.961  1.00 14.77 ?  113 TYR   A HE2  1 
ATOM   2360 H HH   . TYR   A 1 113 ? 18.070 -9.003  -0.651  1.00 16.30 ?  113 TYR   A HH   1 
ATOM   2361 N N    . GLU   A 1 114 ? 26.291 -13.193 -0.155  1.00 11.31 ?  114 GLU   A N    1 
ATOM   2362 C CA   . GLU   A 1 114 ? 27.283 -14.096 0.431   1.00 11.46 ?  114 GLU   A CA   1 
ATOM   2363 C C    . GLU   A 1 114 ? 28.138 -13.392 1.482   1.00 11.41 ?  114 GLU   A C    1 
ATOM   2364 O O    . GLU   A 1 114 ? 28.615 -14.032 2.428   1.00 11.72 ?  114 GLU   A O    1 
ATOM   2365 C CB   . GLU   A 1 114 ? 28.149 -14.731 -0.666  1.00 11.76 ?  114 GLU   A CB   1 
ATOM   2366 C CG   . GLU   A 1 114 ? 27.383 -15.788 -1.450  1.00 12.29 ?  114 GLU   A CG   1 
ATOM   2367 C CD   . GLU   A 1 114 ? 28.091 -16.316 -2.692  1.00 12.56 ?  114 GLU   A CD   1 
ATOM   2368 O OE1  . GLU   A 1 114 ? 29.051 -15.685 -3.184  1.00 12.51 ?  114 GLU   A OE1  1 
ATOM   2369 O OE2  . GLU   A 1 114 ? 27.654 -17.384 -3.184  1.00 13.53 -1 114 GLU   A OE2  1 
ATOM   2370 H H    . GLU   A 1 114 ? 26.345 -13.094 -1.015  1.00 13.57 ?  114 GLU   A H    1 
ATOM   2371 H HA   . GLU   A 1 114 ? 26.809 -14.810 0.872   1.00 13.75 ?  114 GLU   A HA   1 
ATOM   2372 H HB2  . GLU   A 1 114 ? 28.434 -14.045 -1.293  1.00 14.11 ?  114 GLU   A HB2  1 
ATOM   2373 H HB3  . GLU   A 1 114 ? 28.916 -15.157 -0.262  1.00 14.11 ?  114 GLU   A HB3  1 
ATOM   2374 H HG2  . GLU   A 1 114 ? 27.219 -16.545 -0.867  1.00 14.75 ?  114 GLU   A HG2  1 
ATOM   2375 H HG3  . GLU   A 1 114 ? 26.534 -15.410 -1.734  1.00 14.75 ?  114 GLU   A HG3  1 
ATOM   2376 N N    . ASN   A 1 115 ? 28.323 -12.071 1.355   1.00 11.14 ?  115 ASN   A N    1 
ATOM   2377 C CA   . ASN   A 1 115 ? 29.089 -11.345 2.362   1.00 11.57 ?  115 ASN   A CA   1 
ATOM   2378 C C    . ASN   A 1 115 ? 28.478 -11.480 3.749   1.00 11.30 ?  115 ASN   A C    1 
ATOM   2379 O O    . ASN   A 1 115 ? 29.197 -11.413 4.754   1.00 11.82 ?  115 ASN   A O    1 
ATOM   2380 C CB   . ASN   A 1 115 ? 29.196 -9.867  1.992   1.00 11.58 ?  115 ASN   A CB   1 
ATOM   2381 C CG   . ASN   A 1 115 ? 29.988 -9.640  0.731   1.00 12.51 ?  115 ASN   A CG   1 
ATOM   2382 O OD1  . ASN   A 1 115 ? 31.206 -9.730  0.743   1.00 15.81 ?  115 ASN   A OD1  1 
ATOM   2383 N ND2  . ASN   A 1 115 ? 29.307 -9.340  -0.360  1.00 12.23 ?  115 ASN   A ND2  1 
ATOM   2384 H H    . ASN   A 1 115 ? 28.014 -11.582 0.711   1.00 13.37 ?  115 ASN   A H    1 
ATOM   2385 H HA   . ASN   A 1 115 ? 29.983 -11.713 2.395   1.00 13.89 ?  115 ASN   A HA   1 
ATOM   2386 H HB2  . ASN   A 1 115 ? 28.306 -9.507  1.866   1.00 13.89 ?  115 ASN   A HB2  1 
ATOM   2387 H HB3  . ASN   A 1 115 ? 29.643 -9.398  2.718   1.00 13.89 ?  115 ASN   A HB3  1 
ATOM   2388 H HD21 . ASN   A 1 115 ? 29.716 -9.196  -1.098  1.00 14.67 ?  115 ASN   A HD21 1 
ATOM   2389 H HD22 . ASN   A 1 115 ? 28.444 -9.299  -0.329  1.00 14.67 ?  115 ASN   A HD22 1 
ATOM   2390 N N    . PHE   A 1 116 ? 27.154 -11.653 3.830   1.00 11.53 ?  116 PHE   A N    1 
ATOM   2391 C CA   . PHE   A 1 116 ? 26.503 -11.756 5.134   1.00 11.51 ?  116 PHE   A CA   1 
ATOM   2392 C C    . PHE   A 1 116 ? 26.984 -12.988 5.900   1.00 11.81 ?  116 PHE   A C    1 
ATOM   2393 O O    . PHE   A 1 116 ? 26.919 -13.009 7.131   1.00 12.31 ?  116 PHE   A O    1 
ATOM   2394 C CB   . PHE   A 1 116 ? 24.976 -11.886 4.996   1.00 11.56 ?  116 PHE   A CB   1 
ATOM   2395 C CG   . PHE   A 1 116 ? 24.217 -10.636 4.544   1.00 11.49 ?  116 PHE   A CG   1 
ATOM   2396 C CD1  . PHE   A 1 116 ? 24.791 -9.613  3.796   1.00 11.65 ?  116 PHE   A CD1  1 
ATOM   2397 C CD2  . PHE   A 1 116 ? 22.864 -10.532 4.871   1.00 12.28 ?  116 PHE   A CD2  1 
ATOM   2398 C CE1  . PHE   A 1 116 ? 24.024 -8.526  3.394   1.00 11.97 ?  116 PHE   A CE1  1 
ATOM   2399 C CE2  . PHE   A 1 116 ? 22.101 -9.457  4.476   1.00 12.51 ?  116 PHE   A CE2  1 
ATOM   2400 C CZ   . PHE   A 1 116 ? 22.674 -8.452  3.735   1.00 12.13 ?  116 PHE   A CZ   1 
ATOM   2401 H H    . PHE   A 1 116 ? 26.617 -11.703 3.155   1.00 13.84 ?  116 PHE   A H    1 
ATOM   2402 H HA   . PHE   A 1 116 ? 26.695 -10.965 5.659   1.00 13.81 ?  116 PHE   A HA   1 
ATOM   2403 H HB2  . PHE   A 1 116 ? 24.786 -12.586 4.349   1.00 13.87 ?  116 PHE   A HB2  1 
ATOM   2404 H HB3  . PHE   A 1 116 ? 24.614 -12.147 5.859   1.00 13.87 ?  116 PHE   A HB3  1 
ATOM   2405 H HD1  . PHE   A 1 116 ? 25.686 -9.672  3.562   1.00 13.97 ?  116 PHE   A HD1  1 
ATOM   2406 H HD2  . PHE   A 1 116 ? 22.462 -11.220 5.364   1.00 14.74 ?  116 PHE   A HD2  1 
ATOM   2407 H HE1  . PHE   A 1 116 ? 24.417 -7.846  2.902   1.00 14.36 ?  116 PHE   A HE1  1 
ATOM   2408 H HE2  . PHE   A 1 116 ? 21.203 -9.416  4.714   1.00 15.01 ?  116 PHE   A HE2  1 
ATOM   2409 H HZ   . PHE   A 1 116 ? 22.168 -7.716  3.479   1.00 14.56 ?  116 PHE   A HZ   1 
ATOM   2410 N N    . ASN   A 1 117 ? 27.427 -14.037 5.194   1.00 11.86 ?  117 ASN   A N    1 
ATOM   2411 C CA   . ASN   A 1 117 ? 27.797 -15.286 5.858   1.00 12.02 ?  117 ASN   A CA   1 
ATOM   2412 C C    . ASN   A 1 117 ? 29.063 -15.169 6.686   1.00 12.34 ?  117 ASN   A C    1 
ATOM   2413 O O    . ASN   A 1 117 ? 29.366 -16.089 7.455   1.00 13.44 ?  117 ASN   A O    1 
ATOM   2414 C CB   . ASN   A 1 117 ? 27.907 -16.409 4.833   1.00 12.22 ?  117 ASN   A CB   1 
ATOM   2415 C CG   . ASN   A 1 117 ? 26.553 -16.792 4.294   1.00 12.18 ?  117 ASN   A CG   1 
ATOM   2416 O OD1  . ASN   A 1 117 ? 25.580 -16.840 5.046   1.00 13.01 ?  117 ASN   A OD1  1 
ATOM   2417 N ND2  . ASN   A 1 117 ? 26.465 -17.038 3.004   1.00 12.23 ?  117 ASN   A ND2  1 
ATOM   2418 H H    . ASN   A 1 117 ? 27.499 -14.052 4.333   1.00 14.24 ?  117 ASN   A H    1 
ATOM   2419 H HA   . ASN   A 1 117 ? 27.076 -15.519 6.464   1.00 14.42 ?  117 ASN   A HA   1 
ATOM   2420 H HB2  . ASN   A 1 117 ? 28.460 -16.113 4.093   1.00 14.66 ?  117 ASN   A HB2  1 
ATOM   2421 H HB3  . ASN   A 1 117 ? 28.297 -17.185 5.259   1.00 14.66 ?  117 ASN   A HB3  1 
ATOM   2422 H HD21 . ASN   A 1 117 ? 25.709 -17.250 2.661   1.00 14.67 ?  117 ASN   A HD21 1 
ATOM   2423 H HD22 . ASN   A 1 117 ? 27.166 -16.977 2.509   1.00 14.67 ?  117 ASN   A HD22 1 
ATOM   2424 N N    . GLN   A 1 118 ? 29.789 -14.059 6.566   1.00 12.38 ?  118 GLN   A N    1 
ATOM   2425 C CA   . GLN   A 1 118 ? 30.971 -13.826 7.385   1.00 13.03 ?  118 GLN   A CA   1 
ATOM   2426 C C    . GLN   A 1 118 ? 30.634 -13.256 8.757   1.00 12.94 ?  118 GLN   A C    1 
ATOM   2427 O O    . GLN   A 1 118 ? 31.552 -12.966 9.531   1.00 14.46 ?  118 GLN   A O    1 
ATOM   2428 C CB   . GLN   A 1 118 ? 31.962 -12.920 6.648   1.00 13.02 ?  118 GLN   A CB   1 
ATOM   2429 C CG   . GLN   A 1 118 ? 32.432 -13.496 5.325   1.00 12.94 ?  118 GLN   A CG   1 
ATOM   2430 C CD   . GLN   A 1 118 ? 33.257 -14.757 5.502   1.00 13.18 ?  118 GLN   A CD   1 
ATOM   2431 O OE1  . GLN   A 1 118 ? 34.120 -14.827 6.386   1.00 14.13 ?  118 GLN   A OE1  1 
ATOM   2432 N NE2  . GLN   A 1 118 ? 33.006 -15.757 4.659   1.00 13.50 ?  118 GLN   A NE2  1 
ATOM   2433 H H    . GLN   A 1 118 ? 29.613 -13.415 6.014   1.00 14.86 ?  118 GLN   A H    1 
ATOM   2434 H HA   . GLN   A 1 118 ? 31.403 -14.679 7.528   1.00 15.63 ?  118 GLN   A HA   1 
ATOM   2435 H HB2  . GLN   A 1 118 ? 31.535 -12.069 6.473   1.00 15.62 ?  118 GLN   A HB2  1 
ATOM   2436 H HB3  . GLN   A 1 118 ? 32.739 -12.793 7.213   1.00 15.62 ?  118 GLN   A HB3  1 
ATOM   2437 H HG2  . GLN   A 1 118 ? 31.659 -13.711 4.777   1.00 15.52 ?  118 GLN   A HG2  1 
ATOM   2438 H HG3  . GLN   A 1 118 ? 32.983 -12.836 4.873   1.00 15.52 ?  118 GLN   A HG3  1 
ATOM   2439 H HE21 . GLN   A 1 118 ? 32.390 -15.671 4.057   1.00 16.20 ?  118 GLN   A HE21 1 
ATOM   2440 H HE22 . GLN   A 1 118 ? 33.441 -16.495 4.718   1.00 16.20 ?  118 GLN   A HE22 1 
ATOM   2441 N N    . HIS   A 1 119 ? 29.348 -13.110 9.081   1.00 12.79 ?  119 HIS   A N    1 
ATOM   2442 C CA   . HIS   A 1 119 ? 28.901 -12.505 10.332  1.00 13.37 ?  119 HIS   A CA   1 
ATOM   2443 C C    . HIS   A 1 119 ? 27.766 -13.333 10.906  1.00 13.51 ?  119 HIS   A C    1 
ATOM   2444 O O    . HIS   A 1 119 ? 26.810 -13.650 10.194  1.00 14.16 ?  119 HIS   A O    1 
ATOM   2445 C CB   . HIS   A 1 119 ? 28.442 -11.069 10.069  1.00 13.87 ?  119 HIS   A CB   1 
ATOM   2446 C CG   . HIS   A 1 119 ? 29.519 -10.253 9.449   1.00 15.13 ?  119 HIS   A CG   1 
ATOM   2447 N ND1  . HIS   A 1 119 ? 30.498 -9.648  10.199  1.00 17.06 ?  119 HIS   A ND1  1 
ATOM   2448 C CD2  . HIS   A 1 119 ? 29.848 -10.052 8.154   1.00 15.85 ?  119 HIS   A CD2  1 
ATOM   2449 C CE1  . HIS   A 1 119 ? 31.358 -9.056  9.389   1.00 17.39 ?  119 HIS   A CE1  1 
ATOM   2450 N NE2  . HIS   A 1 119 ? 30.998 -9.300  8.142   1.00 17.22 ?  119 HIS   A NE2  1 
ATOM   2451 H H    . HIS   A 1 119 ? 28.692 -13.374 8.584   1.00 15.35 ?  119 HIS   A H    1 
ATOM   2452 H HA   . HIS   A 1 119 ? 29.635 -12.495 10.970  1.00 16.04 ?  119 HIS   A HA   1 
ATOM   2453 H HB2  . HIS   A 1 119 ? 27.684 -11.089 9.467   1.00 16.64 ?  119 HIS   A HB2  1 
ATOM   2454 H HB3  . HIS   A 1 119 ? 28.195 -10.661 10.912  1.00 16.64 ?  119 HIS   A HB3  1 
ATOM   2455 H HD1  . HIS   A 1 119 ? 30.535 -9.636  11.055  1.00 20.47 ?  119 HIS   A HD1  1 
ATOM   2456 H HD2  . HIS   A 1 119 ? 29.380 -10.363 7.409   1.00 19.03 ?  119 HIS   A HD2  1 
ATOM   2457 H HE1  . HIS   A 1 119 ? 32.095 -8.553  9.648   1.00 20.87 ?  119 HIS   A HE1  1 
ATOM   2458 N N    . GLU   A 1 120 ? 27.862 -13.660 12.195  1.00 14.45 ?  120 GLU   A N    1 
ATOM   2459 C CA   . GLU   A 1 120 ? 26.912 -14.601 12.785  1.00 16.44 ?  120 GLU   A CA   1 
ATOM   2460 C C    . GLU   A 1 120 ? 25.495 -14.038 12.859  1.00 15.13 ?  120 GLU   A C    1 
ATOM   2461 O O    . GLU   A 1 120 ? 24.520 -14.800 12.743  1.00 15.21 ?  120 GLU   A O    1 
ATOM   2462 C CB   . GLU   A 1 120 ? 27.388 -15.023 14.176  1.00 21.08 ?  120 GLU   A CB   1 
ATOM   2463 C CG   . GLU   A 1 120 ? 28.570 -15.976 14.169  1.00 27.55 ?  120 GLU   A CG   1 
ATOM   2464 C CD   . GLU   A 1 120 ? 28.715 -16.722 15.480  1.00 33.60 ?  120 GLU   A CD   1 
ATOM   2465 O OE1  . GLU   A 1 120 ? 28.293 -16.181 16.525  1.00 35.49 ?  120 GLU   A OE1  1 
ATOM   2466 O OE2  . GLU   A 1 120 ? 29.239 -17.855 15.462  1.00 38.10 -1 120 GLU   A OE2  1 
ATOM   2467 H H    . GLU   A 1 120 ? 28.460 -13.361 12.743  1.00 17.34 ?  120 GLU   A H    1 
ATOM   2468 H HA   . GLU   A 1 120 ? 26.887 -15.399 12.239  1.00 19.73 ?  120 GLU   A HA   1 
ATOM   2469 H HB2  . GLU   A 1 120 ? 27.655 -14.237 14.676  1.00 25.30 ?  120 GLU   A HB2  1 
ATOM   2470 H HB3  . GLU   A 1 120 ? 26.660 -15.472 14.639  1.00 25.30 ?  120 GLU   A HB3  1 
ATOM   2471 H HG2  . GLU   A 1 120 ? 28.452 -16.630 13.463  1.00 33.06 ?  120 GLU   A HG2  1 
ATOM   2472 H HG3  . GLU   A 1 120 ? 29.387 -15.474 14.028  1.00 33.06 ?  120 GLU   A HG3  1 
ATOM   2473 N N    . VAL   A 1 121 ? 25.363 -12.729 13.083  1.00 14.65 ?  121 VAL   A N    1 
ATOM   2474 C CA   . VAL   A 1 121 ? 24.073 -12.058 13.213  1.00 14.69 ?  121 VAL   A CA   1 
ATOM   2475 C C    . VAL   A 1 121 ? 24.185 -10.673 12.582  1.00 13.56 ?  121 VAL   A C    1 
ATOM   2476 O O    . VAL   A 1 121 ? 25.160 -9.954  12.822  1.00 14.42 ?  121 VAL   A O    1 
ATOM   2477 C CB   . VAL   A 1 121 ? 23.652 -11.911 14.692  1.00 17.23 ?  121 VAL   A CB   1 
ATOM   2478 C CG1  . VAL   A 1 121 ? 22.271 -11.276 14.796  1.00 17.88 ?  121 VAL   A CG1  1 
ATOM   2479 C CG2  . VAL   A 1 121 ? 23.674 -13.243 15.421  1.00 19.43 ?  121 VAL   A CG2  1 
ATOM   2480 H H    . VAL   A 1 121 ? 26.034 -12.192 13.170  1.00 17.58 ?  121 VAL   A H    1 
ATOM   2481 H HA   . VAL   A 1 121 ? 23.396 -12.567 12.742  1.00 17.63 ?  121 VAL   A HA   1 
ATOM   2482 H HB   . VAL   A 1 121 ? 24.277 -11.323 15.137  1.00 20.67 ?  121 VAL   A HB   1 
ATOM   2483 H HG11 . VAL   A 1 121 ? 21.964 -11.335 15.715  1.00 21.45 ?  121 VAL   A HG11 1 
ATOM   2484 H HG12 . VAL   A 1 121 ? 22.327 -10.345 14.528  1.00 21.45 ?  121 VAL   A HG12 1 
ATOM   2485 H HG13 . VAL   A 1 121 ? 21.657 -11.751 14.213  1.00 21.45 ?  121 VAL   A HG13 1 
ATOM   2486 H HG21 . VAL   A 1 121 ? 23.332 -13.118 16.325  1.00 23.32 ?  121 VAL   A HG21 1 
ATOM   2487 H HG22 . VAL   A 1 121 ? 23.109 -13.878 14.948  1.00 23.32 ?  121 VAL   A HG22 1 
ATOM   2488 H HG23 . VAL   A 1 121 ? 24.582 -13.575 15.458  1.00 23.32 ?  121 VAL   A HG23 1 
ATOM   2489 N N    . LEU   A 1 122 ? 23.171 -10.276 11.806  1.00 13.23 ?  122 LEU   A N    1 
ATOM   2490 C CA   . LEU   A 1 122 ? 23.171 -8.971  11.144  1.00 12.97 ?  122 LEU   A CA   1 
ATOM   2491 C C    . LEU   A 1 122 ? 21.774 -8.381  11.117  1.00 12.94 ?  122 LEU   A C    1 
ATOM   2492 O O    . LEU   A 1 122 ? 20.788 -9.103  10.975  1.00 14.04 ?  122 LEU   A O    1 
ATOM   2493 C CB   . LEU   A 1 122 ? 23.581 -9.055  9.670   1.00 14.44 ?  122 LEU   A CB   1 
ATOM   2494 C CG   . LEU   A 1 122 ? 24.781 -9.910  9.291   1.00 14.29 ?  122 LEU   A CG   1 
ATOM   2495 C CD1  . LEU   A 1 122 ? 24.373 -11.358 9.060   1.00 14.97 ?  122 LEU   A CD1  1 
ATOM   2496 C CD2  . LEU   A 1 122 ? 25.452 -9.329  8.055   1.00 13.61 ?  122 LEU   A CD2  1 
ATOM   2497 H H    . LEU   A 1 122 ? 22.470 -10.747 11.642  1.00 15.87 ?  122 LEU   A H    1 
ATOM   2498 H HA   . LEU   A 1 122 ? 23.772 -8.360  11.603  1.00 15.57 ?  122 LEU   A HA   1 
ATOM   2499 H HB2  . LEU   A 1 122 ? 22.833 -9.406  9.170   1.00 17.32 ?  122 LEU   A HB2  1 
ATOM   2500 H HB3  . LEU   A 1 122 ? 23.778 -8.158  9.361   1.00 17.32 ?  122 LEU   A HB3  1 
ATOM   2501 H HG   . LEU   A 1 122 ? 25.436 -9.892  10.007  1.00 17.15 ?  122 LEU   A HG   1 
ATOM   2502 H HD11 . LEU   A 1 122 ? 25.145 -11.868 8.766   1.00 17.96 ?  122 LEU   A HD11 1 
ATOM   2503 H HD12 . LEU   A 1 122 ? 24.036 -11.725 9.892   1.00 17.96 ?  122 LEU   A HD12 1 
ATOM   2504 H HD13 . LEU   A 1 122 ? 23.681 -11.388 8.381   1.00 17.96 ?  122 LEU   A HD13 1 
ATOM   2505 H HD21 . LEU   A 1 122 ? 26.194 -9.901  7.787   1.00 16.34 ?  122 LEU   A HD21 1 
ATOM   2506 H HD22 . LEU   A 1 122 ? 24.806 -9.274  7.334   1.00 16.34 ?  122 LEU   A HD22 1 
ATOM   2507 H HD23 . LEU   A 1 122 ? 25.790 -8.439  8.261   1.00 16.34 ?  122 LEU   A HD23 1 
ATOM   2508 N N    . LEU   A 1 123 ? 21.712 -7.053  11.216  1.00 12.45 ?  123 LEU   A N    1 
ATOM   2509 C CA   . LEU   A 1 123 ? 20.535 -6.261  10.861  1.00 12.26 ?  123 LEU   A CA   1 
ATOM   2510 C C    . LEU   A 1 123 ? 20.770 -5.724  9.457   1.00 11.92 ?  123 LEU   A C    1 
ATOM   2511 O O    . LEU   A 1 123 ? 21.812 -5.119  9.206   1.00 12.64 ?  123 LEU   A O    1 
ATOM   2512 C CB   . LEU   A 1 123 ? 20.410 -5.094  11.838  1.00 13.18 ?  123 LEU   A CB   1 
ATOM   2513 C CG   . LEU   A 1 123 ? 19.368 -4.027  11.504  1.00 13.84 ?  123 LEU   A CG   1 
ATOM   2514 C CD1  . LEU   A 1 123 ? 17.975 -4.629  11.508  1.00 14.61 ?  123 LEU   A CD1  1 
ATOM   2515 C CD2  . LEU   A 1 123 ? 19.460 -2.857  12.478  1.00 14.50 ?  123 LEU   A CD2  1 
ATOM   2516 H H    . LEU   A 1 123 ? 22.368 -6.565  11.492  1.00 14.94 ?  123 LEU   A H    1 
ATOM   2517 H HA   . LEU   A 1 123 ? 19.731 -6.805  10.889  1.00 14.71 ?  123 LEU   A HA   1 
ATOM   2518 H HB2  . LEU   A 1 123 ? 20.175 -5.448  12.713  1.00 15.82 ?  123 LEU   A HB2  1 
ATOM   2519 H HB3  . LEU   A 1 123 ? 21.264 -4.645  11.892  1.00 15.82 ?  123 LEU   A HB3  1 
ATOM   2520 H HG   . LEU   A 1 123 ? 19.536 -3.680  10.612  1.00 16.61 ?  123 LEU   A HG   1 
ATOM   2521 H HD11 . LEU   A 1 123 ? 17.323 -3.930  11.354  1.00 17.53 ?  123 LEU   A HD11 1 
ATOM   2522 H HD12 . LEU   A 1 123 ? 17.916 -5.298  10.806  1.00 17.53 ?  123 LEU   A HD12 1 
ATOM   2523 H HD13 . LEU   A 1 123 ? 17.816 -5.046  12.372  1.00 17.53 ?  123 LEU   A HD13 1 
ATOM   2524 H HD21 . LEU   A 1 123 ? 18.791 -2.198  12.245  1.00 17.41 ?  123 LEU   A HD21 1 
ATOM   2525 H HD22 . LEU   A 1 123 ? 19.300 -3.190  13.377  1.00 17.41 ?  123 LEU   A HD22 1 
ATOM   2526 H HD23 . LEU   A 1 123 ? 20.346 -2.472  12.419  1.00 17.41 ?  123 LEU   A HD23 1 
ATOM   2527 N N    A ALA   A 1 124 ? 19.790 -5.863  8.560   0.70 11.51 ?  124 ALA   A N    1 
ATOM   2528 N N    B ALA   A 1 124 ? 19.853 -6.005  8.540   0.30 11.75 ?  124 ALA   A N    1 
ATOM   2529 C CA   A ALA   A 1 124 ? 20.059 -5.560  7.160   0.70 11.28 ?  124 ALA   A CA   1 
ATOM   2530 C CA   B ALA   A 1 124 ? 20.147 -5.777  7.138   0.30 11.80 ?  124 ALA   A CA   1 
ATOM   2531 C C    A ALA   A 1 124 ? 18.804 -5.092  6.431   0.70 11.53 ?  124 ALA   A C    1 
ATOM   2532 C C    B ALA   A 1 124 ? 18.930 -5.252  6.394   0.30 11.59 ?  124 ALA   A C    1 
ATOM   2533 O O    A ALA   A 1 124 ? 17.678 -5.406  6.843   0.70 12.33 ?  124 ALA   A O    1 
ATOM   2534 O O    B ALA   A 1 124 ? 17.793 -5.639  6.691   0.30 11.95 ?  124 ALA   A O    1 
ATOM   2535 C CB   A ALA   A 1 124 ? 20.642 -6.779  6.438   0.70 11.50 ?  124 ALA   A CB   1 
ATOM   2536 C CB   B ALA   A 1 124 ? 20.651 -7.057  6.452   0.30 12.27 ?  124 ALA   A CB   1 
ATOM   2537 H H    A ALA   A 1 124 ? 18.989 -6.128  8.730   0.70 13.82 ?  124 ALA   A H    1 
ATOM   2538 H H    B ALA   A 1 124 ? 19.071 -6.325  8.703   0.30 14.10 ?  124 ALA   A H    1 
ATOM   2539 H HA   A ALA   A 1 124 ? 20.726 -4.854  7.125   0.70 13.54 ?  124 ALA   A HA   1 
ATOM   2540 H HA   B ALA   A 1 124 ? 20.850 -5.118  7.086   0.30 14.16 ?  124 ALA   A HA   1 
ATOM   2541 H HB1  A ALA   A 1 124 ? 20.820 -6.548  5.512   0.70 13.80 ?  124 ALA   A HB1  1 
ATOM   2542 H HB1  B ALA   A 1 124 ? 20.837 -6.867  5.519   0.30 14.72 ?  124 ALA   A HB1  1 
ATOM   2543 H HB2  A ALA   A 1 124 ? 21.475 -7.041  6.873   0.70 13.80 ?  124 ALA   A HB2  1 
ATOM   2544 H HB2  B ALA   A 1 124 ? 21.467 -7.354  6.894   0.30 14.72 ?  124 ALA   A HB2  1 
ATOM   2545 H HB3  A ALA   A 1 124 ? 20.008 -7.510  6.483   0.70 13.80 ?  124 ALA   A HB3  1 
ATOM   2546 H HB3  B ALA   A 1 124 ? 19.973 -7.746  6.521   0.30 14.72 ?  124 ALA   A HB3  1 
ATOM   2547 N N    A PRO   A 1 125 ? 18.976 -4.370  5.319   0.70 11.61 ?  125 PRO   A N    1 
ATOM   2548 N N    B PRO   A 1 125 ? 19.145 -4.389  5.411   0.30 10.58 ?  125 PRO   A N    1 
ATOM   2549 C CA   A PRO   A 1 125 ? 17.908 -4.158  4.340   0.70 12.06 ?  125 PRO   A CA   1 
ATOM   2550 C CA   B PRO   A 1 125 ? 18.062 -3.958  4.533   0.30 10.83 ?  125 PRO   A CA   1 
ATOM   2551 C C    A PRO   A 1 125 ? 17.972 -5.216  3.242   0.70 11.67 ?  125 PRO   A C    1 
ATOM   2552 C C    B PRO   A 1 125 ? 17.958 -4.958  3.387   0.30 11.61 ?  125 PRO   A C    1 
ATOM   2553 O O    A PRO   A 1 125 ? 18.943 -5.966  3.122   0.70 12.14 ?  125 PRO   A O    1 
ATOM   2554 O O    B PRO   A 1 125 ? 18.785 -5.862  3.243   0.30 11.89 ?  125 PRO   A O    1 
ATOM   2555 C CB   A PRO   A 1 125 ? 18.295 -2.800  3.743   0.70 12.52 ?  125 PRO   A CB   1 
ATOM   2556 C CB   B PRO   A 1 125 ? 18.596 -2.619  4.018   0.30 10.37 ?  125 PRO   A CB   1 
ATOM   2557 C CG   A PRO   A 1 125 ? 19.807 -2.900  3.667   0.70 12.86 ?  125 PRO   A CG   1 
ATOM   2558 C CG   B PRO   A 1 125 ? 20.079 -2.898  3.852   0.30 10.10 ?  125 PRO   A CG   1 
ATOM   2559 C CD   A PRO   A 1 125 ? 20.208 -3.651  4.932   0.70 12.23 ?  125 PRO   A CD   1 
ATOM   2560 C CD   B PRO   A 1 125 ? 20.452 -3.902  4.930   0.30 9.99  ?  125 PRO   A CD   1 
ATOM   2561 H HA   A PRO   A 1 125 ? 17.032 -4.136  4.748   0.70 14.47 ?  125 PRO   A HA   1 
ATOM   2562 H HA   B PRO   A 1 125 ? 17.226 -3.843  5.024   0.30 13.00 ?  125 PRO   A HA   1 
ATOM   2563 H HB2  A PRO   A 1 125 ? 17.900 -2.694  2.860   0.70 15.02 ?  125 PRO   A HB2  1 
ATOM   2564 H HB2  B PRO   A 1 125 ? 18.177 -2.405  3.171   0.30 12.45 ?  125 PRO   A HB2  1 
ATOM   2565 H HB3  A PRO   A 1 125 ? 18.015 -2.087  4.339   0.70 15.02 ?  125 PRO   A HB3  1 
ATOM   2566 H HB3  B PRO   A 1 125 ? 18.437 -1.917  4.675   0.30 12.45 ?  125 PRO   A HB3  1 
ATOM   2567 H HG2  A PRO   A 1 125 ? 20.067 -3.399  2.875   0.70 15.44 ?  125 PRO   A HG2  1 
ATOM   2568 H HG2  B PRO   A 1 125 ? 20.241 -3.273  2.973   0.30 12.12 ?  125 PRO   A HG2  1 
ATOM   2569 H HG3  A PRO   A 1 125 ? 20.196 -2.009  3.652   0.70 15.44 ?  125 PRO   A HG3  1 
ATOM   2570 H HG3  B PRO   A 1 125 ? 20.580 -2.076  3.969   0.30 12.12 ?  125 PRO   A HG3  1 
ATOM   2571 H HD2  A PRO   A 1 125 ? 20.932 -4.264  4.743   0.70 14.68 ?  125 PRO   A HD2  1 
ATOM   2572 H HD2  B PRO   A 1 125 ? 20.972 -4.633  4.550   0.30 11.99 ?  125 PRO   A HD2  1 
ATOM   2573 H HD3  A PRO   A 1 125 ? 20.453 -3.016  5.629   0.70 14.68 ?  125 PRO   A HD3  1 
ATOM   2574 H HD3  B PRO   A 1 125 ? 20.941 -3.461  5.645   0.30 11.99 ?  125 PRO   A HD3  1 
ATOM   2575 N N    A LEU   A 1 126 ? 16.925 -5.242  2.415   0.70 11.85 ?  126 LEU   A N    1 
ATOM   2576 N N    B LEU   A 1 126 ? 16.933 -4.776  2.560   0.30 12.73 ?  126 LEU   A N    1 
ATOM   2577 C CA   A LEU   A 1 126 ? 16.945 -6.052  1.203   0.70 12.20 ?  126 LEU   A CA   1 
ATOM   2578 C CA   B LEU   A 1 126 ? 16.777 -5.603  1.368   0.30 13.61 ?  126 LEU   A CA   1 
ATOM   2579 C C    A LEU   A 1 126 ? 17.884 -5.431  0.176   0.70 12.55 ?  126 LEU   A C    1 
ATOM   2580 C C    B LEU   A 1 126 ? 17.710 -5.081  0.280   0.30 13.06 ?  126 LEU   A C    1 
ATOM   2581 O O    A LEU   A 1 126 ? 17.681 -4.294  -0.261  0.70 13.43 ?  126 LEU   A O    1 
ATOM   2582 O O    B LEU   A 1 126 ? 17.440 -4.041  -0.329  0.30 13.42 ?  126 LEU   A O    1 
ATOM   2583 C CB   A LEU   A 1 126 ? 15.540 -6.178  0.624   0.70 13.02 ?  126 LEU   A CB   1 
ATOM   2584 C CB   B LEU   A 1 126 ? 15.328 -5.550  0.900   0.30 15.50 ?  126 LEU   A CB   1 
ATOM   2585 C CG   A LEU   A 1 126 ? 14.620 -7.131  1.382   0.70 14.46 ?  126 LEU   A CG   1 
ATOM   2586 C CG   B LEU   A 1 126 ? 14.844 -6.653  -0.040  0.30 16.91 ?  126 LEU   A CG   1 
ATOM   2587 C CD1  A LEU   A 1 126 ? 13.198 -7.003  0.869   0.70 15.62 ?  126 LEU   A CD1  1 
ATOM   2588 C CD1  B LEU   A 1 126 ? 14.966 -8.012  0.619   0.30 17.30 ?  126 LEU   A CD1  1 
ATOM   2589 C CD2  A LEU   A 1 126 ? 15.103 -8.574  1.251   0.70 14.46 ?  126 LEU   A CD2  1 
ATOM   2590 C CD2  B LEU   A 1 126 ? 13.409 -6.386  -0.453  0.30 17.23 ?  126 LEU   A CD2  1 
ATOM   2591 H H    A LEU   A 1 126 ? 16.195 -4.802  2.525   0.70 14.23 ?  126 LEU   A H    1 
ATOM   2592 H H    B LEU   A 1 126 ? 16.300 -4.192  2.671   0.30 15.27 ?  126 LEU   A H    1 
ATOM   2593 H HA   A LEU   A 1 126 ? 17.268 -6.943  1.405   0.70 14.64 ?  126 LEU   A HA   1 
ATOM   2594 H HA   B LEU   A 1 126 ? 17.018 -6.520  1.582   0.30 16.33 ?  126 LEU   A HA   1 
ATOM   2595 H HB2  A LEU   A 1 126 ? 15.115 -5.307  0.631   0.70 15.63 ?  126 LEU   A HB2  1 
ATOM   2596 H HB2  B LEU   A 1 126 ? 14.757 -5.567  1.681   0.30 18.60 ?  126 LEU   A HB2  1 
ATOM   2597 H HB3  A LEU   A 1 126 ? 15.595 -6.504  -0.290  0.70 15.63 ?  126 LEU   A HB3  1 
ATOM   2598 H HB3  B LEU   A 1 126 ? 15.204 -4.712  0.430   0.30 18.60 ?  126 LEU   A HB3  1 
ATOM   2599 H HG   A LEU   A 1 126 ? 14.615 -6.899  2.324   0.70 17.35 ?  126 LEU   A HG   1 
ATOM   2600 H HG   B LEU   A 1 126 ? 15.393 -6.649  -0.841  0.30 20.30 ?  126 LEU   A HG   1 
ATOM   2601 H HD11 A LEU   A 1 126 ? 12.624 -7.616  1.360   0.70 18.74 ?  126 LEU   A HD11 1 
ATOM   2602 H HD11 B LEU   A 1 126 ? 14.498 -8.665  0.077   0.30 20.76 ?  126 LEU   A HD11 1 
ATOM   2603 H HD12 A LEU   A 1 126 ? 12.894 -6.093  0.998   0.70 18.74 ?  126 LEU   A HD12 1 
ATOM   2604 H HD12 B LEU   A 1 126 ? 15.904 -8.247  0.686   0.30 20.76 ?  126 LEU   A HD12 1 
ATOM   2605 H HD13 A LEU   A 1 126 ? 13.181 -7.228  -0.076  0.70 18.74 ?  126 LEU   A HD13 1 
ATOM   2606 H HD13 B LEU   A 1 126 ? 14.569 -7.969  1.503   0.30 20.76 ?  126 LEU   A HD13 1 
ATOM   2607 H HD21 A LEU   A 1 126 ? 14.417 -9.174  1.577   0.70 17.35 ?  126 LEU   A HD21 1 
ATOM   2608 H HD21 B LEU   A 1 126 ? 13.083 -7.141  -0.965  0.30 20.68 ?  126 LEU   A HD21 1 
ATOM   2609 H HD22 A LEU   A 1 126 ? 15.288 -8.759  0.316   0.70 17.35 ?  126 LEU   A HD22 1 
ATOM   2610 H HD22 B LEU   A 1 126 ? 12.872 -6.267  0.345   0.30 20.68 ?  126 LEU   A HD22 1 
ATOM   2611 H HD23 A LEU   A 1 126 ? 15.914 -8.682  1.774   0.70 17.35 ?  126 LEU   A HD23 1 
ATOM   2612 H HD23 B LEU   A 1 126 ? 13.379 -5.580  -0.993  0.30 20.68 ?  126 LEU   A HD23 1 
ATOM   2613 N N    A LEU   A 1 127 ? 18.901 -6.185  -0.222  0.70 12.23 ?  127 LEU   A N    1 
ATOM   2614 N N    B LEU   A 1 127 ? 18.800 -5.802  0.017   0.30 12.48 ?  127 LEU   A N    1 
ATOM   2615 C CA   A LEU   A 1 127 ? 19.890 -5.681  -1.163  0.70 11.77 ?  127 LEU   A CA   1 
ATOM   2616 C CA   B LEU   A 1 127 ? 19.782 -5.321  -0.947  0.30 12.28 ?  127 LEU   A CA   1 
ATOM   2617 C C    A LEU   A 1 127 ? 19.270 -5.460  -2.533  0.70 11.17 ?  127 LEU   A C    1 
ATOM   2618 C C    B LEU   A 1 127 ? 19.180 -5.246  -2.347  0.30 12.58 ?  127 LEU   A C    1 
ATOM   2619 O O    A LEU   A 1 127 ? 18.435 -6.240  -3.001  0.70 11.31 ?  127 LEU   A O    1 
ATOM   2620 O O    B LEU   A 1 127 ? 18.299 -6.027  -2.718  0.30 12.98 ?  127 LEU   A O    1 
ATOM   2621 C CB   A LEU   A 1 127 ? 21.054 -6.663  -1.279  0.70 12.12 ?  127 LEU   A CB   1 
ATOM   2622 C CB   B LEU   A 1 127 ? 21.003 -6.241  -0.973  0.30 12.29 ?  127 LEU   A CB   1 
ATOM   2623 C CG   A LEU   A 1 127 ? 21.852 -6.895  0.003   0.70 12.30 ?  127 LEU   A CG   1 
ATOM   2624 C CG   B LEU   A 1 127 ? 21.865 -6.265  0.289   0.30 12.28 ?  127 LEU   A CG   1 
ATOM   2625 C CD1  A LEU   A 1 127 ? 22.962 -7.884  -0.268  0.70 12.71 ?  127 LEU   A CD1  1 
ATOM   2626 C CD1  B LEU   A 1 127 ? 23.032 -7.220  0.116   0.30 12.21 ?  127 LEU   A CD1  1 
ATOM   2627 C CD2  A LEU   A 1 127 ? 22.426 -5.599  0.533   0.70 13.08 ?  127 LEU   A CD2  1 
ATOM   2628 C CD2  B LEU   A 1 127 ? 22.360 -4.863  0.623   0.30 12.82 ?  127 LEU   A CD2  1 
ATOM   2629 H H    A LEU   A 1 127 ? 19.043 -6.995  0.045   0.70 14.68 ?  127 LEU   A H    1 
ATOM   2630 H H    B LEU   A 1 127 ? 18.991 -6.561  0.381   0.30 14.98 ?  127 LEU   A H    1 
ATOM   2631 H HA   A LEU   A 1 127 ? 20.234 -4.839  -0.844  0.70 14.13 ?  127 LEU   A HA   1 
ATOM   2632 H HA   B LEU   A 1 127 ? 20.071 -4.430  -0.689  0.30 14.74 ?  127 LEU   A HA   1 
ATOM   2633 H HB2  A LEU   A 1 127 ? 20.707 -7.526  -1.563  0.70 14.54 ?  127 LEU   A HB2  1 
ATOM   2634 H HB2  B LEU   A 1 127 ? 20.694 -7.146  -1.132  0.30 14.75 ?  127 LEU   A HB2  1 
ATOM   2635 H HB3  A LEU   A 1 127 ? 21.673 -6.332  -1.948  0.70 14.54 ?  127 LEU   A HB3  1 
ATOM   2636 H HB3  B LEU   A 1 127 ? 21.572 -5.962  -1.708  0.30 14.75 ?  127 LEU   A HB3  1 
ATOM   2637 H HG   A LEU   A 1 127 ? 21.266 -7.272  0.680   0.70 14.76 ?  127 LEU   A HG   1 
ATOM   2638 H HG   B LEU   A 1 127 ? 21.328 -6.581  1.032   0.30 14.74 ?  127 LEU   A HG   1 
ATOM   2639 H HD11 A LEU   A 1 127 ? 23.443 -8.056  0.559   0.70 15.25 ?  127 LEU   A HD11 1 
ATOM   2640 H HD11 B LEU   A 1 127 ? 23.577 -7.198  0.917   0.30 14.66 ?  127 LEU   A HD11 1 
ATOM   2641 H HD12 A LEU   A 1 127 ? 22.577 -8.713  -0.600  0.70 15.25 ?  127 LEU   A HD12 1 
ATOM   2642 H HD12 B LEU   A 1 127 ? 22.688 -8.116  -0.027  0.30 14.66 ?  127 LEU   A HD12 1 
ATOM   2643 H HD13 A LEU   A 1 127 ? 23.564 -7.513  -0.929  0.70 15.25 ?  127 LEU   A HD13 1 
ATOM   2644 H HD13 B LEU   A 1 127 ? 23.556 -6.940  -0.650  0.30 14.66 ?  127 LEU   A HD13 1 
ATOM   2645 H HD21 A LEU   A 1 127 ? 23.054 -5.798  1.242   0.70 15.69 ?  127 LEU   A HD21 1 
ATOM   2646 H HD21 B LEU   A 1 127 ? 23.049 -4.926  1.301   0.30 15.39 ?  127 LEU   A HD21 1 
ATOM   2647 H HD22 A LEU   A 1 127 ? 22.879 -5.137  -0.192  0.70 15.69 ?  127 LEU   A HD22 1 
ATOM   2648 H HD22 B LEU   A 1 127 ? 22.721 -4.458  -0.181  0.30 15.39 ?  127 LEU   A HD22 1 
ATOM   2649 H HD23 A LEU   A 1 127 ? 21.703 -5.048  0.873   0.70 15.69 ?  127 LEU   A HD23 1 
ATOM   2650 H HD23 B LEU   A 1 127 ? 21.615 -4.337  0.953   0.30 15.39 ?  127 LEU   A HD23 1 
ATOM   2651 N N    A SER   A 1 128 ? 19.698 -4.380  -3.176  0.70 11.21 ?  128 SER   A N    1 
ATOM   2652 N N    B SER   A 1 128 ? 19.670 -4.279  -3.123  0.30 12.54 ?  128 SER   A N    1 
ATOM   2653 C CA   A SER   A 1 128 ? 19.286 -3.979  -4.512  0.70 11.39 ?  128 SER   A CA   1 
ATOM   2654 C CA   B SER   A 1 128 ? 19.321 -4.011  -4.517  0.30 12.55 ?  128 SER   A CA   1 
ATOM   2655 C C    A SER   A 1 128 ? 17.827 -3.538  -4.587  0.70 11.88 ?  128 SER   A C    1 
ATOM   2656 C C    B SER   A 1 128 ? 17.891 -3.528  -4.725  0.30 12.53 ?  128 SER   A C    1 
ATOM   2657 O O    A SER   A 1 128 ? 17.335 -3.270  -5.683  0.70 13.49 ?  128 SER   A O    1 
ATOM   2658 O O    B SER   A 1 128 ? 17.547 -3.162  -5.852  0.30 12.63 ?  128 SER   A O    1 
ATOM   2659 C CB   A SER   A 1 128 ? 19.638 -5.013  -5.591  0.70 11.70 ?  128 SER   A CB   1 
ATOM   2660 C CB   B SER   A 1 128 ? 19.637 -5.173  -5.470  0.30 12.76 ?  128 SER   A CB   1 
ATOM   2661 O OG   A SER   A 1 128 ? 21.047 -5.213  -5.646  0.70 12.45 ?  128 SER   A OG   1 
ATOM   2662 O OG   B SER   A 1 128 ? 21.040 -5.329  -5.623  0.30 13.07 ?  128 SER   A OG   1 
ATOM   2663 H H    A SER   A 1 128 ? 20.281 -3.842  -2.838  0.70 13.46 ?  128 SER   A H    1 
ATOM   2664 H H    B SER   A 1 128 ? 20.264 -3.725  -2.839  0.30 15.04 ?  128 SER   A H    1 
ATOM   2665 H HA   A SER   A 1 128 ? 19.805 -3.199  -4.728  0.70 13.67 ?  128 SER   A HA   1 
ATOM   2666 H HA   B SER   A 1 128 ? 19.874 -3.274  -4.804  0.30 15.06 ?  128 SER   A HA   1 
ATOM   2667 H HB2  A SER   A 1 128 ? 19.199 -5.852  -5.387  0.70 14.04 ?  128 SER   A HB2  1 
ATOM   2668 H HB2  B SER   A 1 128 ? 19.262 -5.989  -5.112  0.30 15.31 ?  128 SER   A HB2  1 
ATOM   2669 H HB3  A SER   A 1 128 ? 19.333 -4.680  -6.454  0.70 14.04 ?  128 SER   A HB3  1 
ATOM   2670 H HB3  B SER   A 1 128 ? 19.242 -4.980  -6.340  0.30 15.31 ?  128 SER   A HB3  1 
ATOM   2671 H HG   A SER   A 1 128 ? 21.432 -4.490  -5.815  0.70 14.95 ?  128 SER   A HG   1 
ATOM   2672 H HG   B SER   A 1 128 ? 21.371 -4.622  -5.937  0.30 15.69 ?  128 SER   A HG   1 
ATOM   2673 N N    A ALA   A 1 129 ? 17.142 -3.417  -3.447  0.70 12.60 ?  129 ALA   A N    1 
ATOM   2674 N N    B ALA   A 1 129 ? 17.060 -3.481  -3.686  0.30 13.23 ?  129 ALA   A N    1 
ATOM   2675 C CA   A ALA   A 1 129 ? 15.774 -2.923  -3.414  0.70 12.77 ?  129 ALA   A CA   1 
ATOM   2676 C CA   B ALA   A 1 129 ? 15.717 -2.940  -3.815  0.30 13.88 ?  129 ALA   A CA   1 
ATOM   2677 C C    A ALA   A 1 129 ? 15.773 -1.392  -3.407  0.70 12.13 ?  129 ALA   A C    1 
ATOM   2678 C C    B ALA   A 1 129 ? 15.771 -1.413  -3.820  0.30 14.18 ?  129 ALA   A C    1 
ATOM   2679 O O    A ALA   A 1 129 ? 16.820 -0.737  -3.491  0.70 12.54 ?  129 ALA   A O    1 
ATOM   2680 O O    B ALA   A 1 129 ? 16.841 -0.797  -3.802  0.30 14.21 ?  129 ALA   A O    1 
ATOM   2681 C CB   A ALA   A 1 129 ? 15.028 -3.499  -2.209  0.70 13.83 ?  129 ALA   A CB   1 
ATOM   2682 C CB   B ALA   A 1 129 ? 14.818 -3.475  -2.701  0.30 14.17 ?  129 ALA   A CB   1 
ATOM   2683 H H    A ALA   A 1 129 ? 17.460 -3.616  -2.669  0.70 15.12 ?  129 ALA   A H    1 
ATOM   2684 H H    B ALA   A 1 129 ? 17.254 -3.748  -2.890  0.30 15.88 ?  129 ALA   A H    1 
ATOM   2685 H HA   A ALA   A 1 129 ? 15.320 -3.216  -4.216  0.70 15.32 ?  129 ALA   A HA   1 
ATOM   2686 H HA   B ALA   A 1 129 ? 15.343 -3.219  -4.661  0.30 16.66 ?  129 ALA   A HA   1 
ATOM   2687 H HB1  A ALA   A 1 129 ? 14.115 -3.165  -2.216  0.70 16.60 ?  129 ALA   A HB1  1 
ATOM   2688 H HB1  B ALA   A 1 129 ? 13.926 -3.108  -2.810  0.30 17.00 ?  129 ALA   A HB1  1 
ATOM   2689 H HB2  A ALA   A 1 129 ? 15.025 -4.466  -2.274  0.70 16.60 ?  129 ALA   A HB2  1 
ATOM   2690 H HB2  B ALA   A 1 129 ? 14.786 -4.442  -2.756  0.30 17.00 ?  129 ALA   A HB2  1 
ATOM   2691 H HB3  A ALA   A 1 129 ? 15.475 -3.221  -1.396  0.70 16.60 ?  129 ALA   A HB3  1 
ATOM   2692 H HB3  B ALA   A 1 129 ? 15.181 -3.205  -1.841  0.30 17.00 ?  129 ALA   A HB3  1 
ATOM   2693 N N    A GLY   A 1 130 ? 14.580 -0.811  -3.311  0.70 12.42 ?  130 GLY   A N    1 
ATOM   2694 N N    B GLY   A 1 130 ? 14.598 -0.793  -3.854  0.30 14.56 ?  130 GLY   A N    1 
ATOM   2695 C CA   A GLY   A 1 130 ? 14.479 0.639   -3.287  0.70 12.96 ?  130 GLY   A CA   1 
ATOM   2696 C CA   B GLY   A 1 130 ? 14.547 0.658   -3.828  0.30 15.62 ?  130 GLY   A CA   1 
ATOM   2697 C C    A GLY   A 1 130 ? 15.093 1.251   -4.530  0.70 12.36 ?  130 GLY   A C    1 
ATOM   2698 C C    B GLY   A 1 130 ? 15.185 1.240   -5.073  0.30 16.18 ?  130 GLY   A C    1 
ATOM   2699 O O    A GLY   A 1 130 ? 14.866 0.790   -5.654  0.70 12.87 ?  130 GLY   A O    1 
ATOM   2700 O O    B GLY   A 1 130 ? 14.887 0.832   -6.202  0.30 16.24 ?  130 GLY   A O    1 
ATOM   2701 H H    A GLY   A 1 130 ? 13.824 -1.225  -3.255  0.70 14.91 ?  130 GLY   A H    1 
ATOM   2702 H H    B GLY   A 1 130 ? 13.835 -1.183  -3.900  0.30 17.47 ?  130 GLY   A H    1 
ATOM   2703 H HA2  A GLY   A 1 130 ? 13.543 0.900   -3.229  0.70 15.55 ?  130 GLY   A HA2  1 
ATOM   2704 H HA2  B GLY   A 1 130 ? 13.622 0.951   -3.769  0.30 18.74 ?  130 GLY   A HA2  1 
ATOM   2705 H HA3  A GLY   A 1 130 ? 14.943 0.986   -2.512  0.70 15.55 ?  130 GLY   A HA3  1 
ATOM   2706 H HA3  B GLY   A 1 130 ? 15.023 0.994   -3.051  0.30 18.74 ?  130 GLY   A HA3  1 
ATOM   2707 N N    A ILE   A 1 131 ? 15.889 2.309   -4.329  0.70 12.29 ?  131 ILE   A N    1 
ATOM   2708 N N    B ILE   A 1 131 ? 16.103 2.194   -4.871  0.30 16.78 ?  131 ILE   A N    1 
ATOM   2709 C CA   A ILE   A 1 131 ? 16.471 3.053   -5.443  0.70 12.34 ?  131 ILE   A CA   1 
ATOM   2710 C CA   B ILE   A 1 131 ? 16.633 2.978   -5.986  0.30 17.50 ?  131 ILE   A CA   1 
ATOM   2711 C C    A ILE   A 1 131 ? 17.484 2.258   -6.259  0.70 11.71 ?  131 ILE   A C    1 
ATOM   2712 C C    B ILE   A 1 131 ? 17.708 2.254   -6.784  0.30 17.85 ?  131 ILE   A C    1 
ATOM   2713 O O    A ILE   A 1 131 ? 17.907 2.740   -7.317  0.70 12.85 ?  131 ILE   A O    1 
ATOM   2714 O O    B ILE   A 1 131 ? 18.188 2.810   -7.781  0.30 17.75 ?  131 ILE   A O    1 
ATOM   2715 C CB   A ILE   A 1 131 ? 17.073 4.401   -4.986  0.70 13.97 ?  131 ILE   A CB   1 
ATOM   2716 C CB   B ILE   A 1 131 ? 17.035 4.415   -5.583  0.30 18.08 ?  131 ILE   A CB   1 
ATOM   2717 C CG1  A ILE   A 1 131 ? 18.324 4.194   -4.124  0.70 14.95 ?  131 ILE   A CG1  1 
ATOM   2718 C CG1  B ILE   A 1 131 ? 18.283 4.426   -4.700  0.30 18.44 ?  131 ILE   A CG1  1 
ATOM   2719 C CG2  A ILE   A 1 131 ? 16.027 5.233   -4.243  0.70 14.70 ?  131 ILE   A CG2  1 
ATOM   2720 C CG2  B ILE   A 1 131 ? 15.879 5.121   -4.867  0.30 18.20 ?  131 ILE   A CG2  1 
ATOM   2721 C CD1  A ILE   A 1 131 ? 19.035 5.497   -3.742  0.70 16.46 ?  131 ILE   A CD1  1 
ATOM   2722 C CD1  B ILE   A 1 131 ? 18.722 5.829   -4.299  0.30 18.46 ?  131 ILE   A CD1  1 
ATOM   2723 H H    A ILE   A 1 131 ? 16.085 2.615   -3.551  0.70 14.75 ?  131 ILE   A H    1 
ATOM   2724 H H    B ILE   A 1 131 ? 16.424 2.399   -4.103  0.30 20.13 ?  131 ILE   A H    1 
ATOM   2725 H HA   A ILE   A 1 131 ? 15.747 3.275   -6.045  0.70 14.80 ?  131 ILE   A HA   1 
ATOM   2726 H HA   B ILE   A 1 131 ? 15.901 3.091   -6.601  0.30 21.00 ?  131 ILE   A HA   1 
ATOM   2727 H HB   A ILE   A 1 131 ? 17.332 4.893   -5.777  0.70 16.76 ?  131 ILE   A HB   1 
ATOM   2728 H HB   B ILE   A 1 131 ? 17.231 4.911   -6.392  0.30 21.69 ?  131 ILE   A HB   1 
ATOM   2729 H HG12 A ILE   A 1 131 ? 18.070 3.742   -3.304  0.70 17.94 ?  131 ILE   A HG12 1 
ATOM   2730 H HG12 B ILE   A 1 131 ? 18.101 3.929   -3.890  0.30 22.13 ?  131 ILE   A HG12 1 
ATOM   2731 H HG13 A ILE   A 1 131 ? 18.960 3.649   -4.615  0.70 17.94 ?  131 ILE   A HG13 1 
ATOM   2732 H HG13 B ILE   A 1 131 ? 19.015 4.015   -5.186  0.30 22.13 ?  131 ILE   A HG13 1 
ATOM   2733 H HG21 A ILE   A 1 131 ? 16.373 6.129   -4.105  0.70 17.64 ?  131 ILE   A HG21 1 
ATOM   2734 H HG21 B ILE   A 1 131 ? 16.077 6.069   -4.794  0.30 21.84 ?  131 ILE   A HG21 1 
ATOM   2735 H HG22 A ILE   A 1 131 ? 15.218 5.270   -4.776  0.70 17.64 ?  131 ILE   A HG22 1 
ATOM   2736 H HG22 B ILE   A 1 131 ? 15.067 4.999   -5.380  0.30 21.84 ?  131 ILE   A HG22 1 
ATOM   2737 H HG23 A ILE   A 1 131 ? 15.839 4.815   -3.387  0.70 17.64 ?  131 ILE   A HG23 1 
ATOM   2738 H HG23 B ILE   A 1 131 ? 15.768 4.736   -3.984  0.30 21.84 ?  131 ILE   A HG23 1 
ATOM   2739 H HD11 A ILE   A 1 131 ? 19.870 5.282   -3.294  0.70 19.76 ?  131 ILE   A HD11 1 
ATOM   2740 H HD11 B ILE   A 1 131 ? 19.605 5.783   -3.901  0.30 22.15 ?  131 ILE   A HD11 1 
ATOM   2741 H HD12 A ILE   A 1 131 ? 19.217 6.007   -4.548  0.70 19.76 ?  131 ILE   A HD12 1 
ATOM   2742 H HD12 B ILE   A 1 131 ? 18.746 6.391   -5.091  0.30 22.15 ?  131 ILE   A HD12 1 
ATOM   2743 H HD13 A ILE   A 1 131 ? 18.465 6.009   -3.148  0.70 19.76 ?  131 ILE   A HD13 1 
ATOM   2744 H HD13 B ILE   A 1 131 ? 18.089 6.191   -3.659  0.30 22.15 ?  131 ILE   A HD13 1 
ATOM   2745 N N    A PHE   A 1 132 ? 17.888 1.060   -5.810  0.70 11.29 ?  132 PHE   A N    1 
ATOM   2746 N N    B PHE   A 1 132 ? 18.106 1.034   -6.397  0.30 18.27 ?  132 PHE   A N    1 
ATOM   2747 C CA   A PHE   A 1 132 ? 18.747 0.210   -6.631  0.70 11.21 ?  132 PHE   A CA   1 
ATOM   2748 C CA   B PHE   A 1 132 ? 18.896 0.222   -7.322  0.30 18.94 ?  132 PHE   A CA   1 
ATOM   2749 C C    A PHE   A 1 132 ? 17.975 -0.546  -7.709  0.70 11.90 ?  132 PHE   A C    1 
ATOM   2750 C C    B PHE   A 1 132 ? 18.043 -0.484  -8.362  0.30 18.85 ?  132 PHE   A C    1 
ATOM   2751 O O    A PHE   A 1 132 ? 18.599 -1.179  -8.568  0.70 12.89 ?  132 PHE   A O    1 
ATOM   2752 O O    B PHE   A 1 132 ? 18.589 -0.999  -9.343  0.30 19.34 ?  132 PHE   A O    1 
ATOM   2753 C CB   A PHE   A 1 132 ? 19.545 -0.774  -5.769  0.70 10.62 ?  132 PHE   A CB   1 
ATOM   2754 C CB   B PHE   A 1 132 ? 19.771 -0.812  -6.600  0.30 19.92 ?  132 PHE   A CB   1 
ATOM   2755 C CG   A PHE   A 1 132 ? 20.772 -0.175  -5.115  0.70 10.63 ?  132 PHE   A CG   1 
ATOM   2756 C CG   B PHE   A 1 132 ? 21.139 -0.301  -6.220  0.30 21.30 ?  132 PHE   A CG   1 
ATOM   2757 C CD1  A PHE   A 1 132 ? 20.653 0.844   -4.185  0.70 11.49 ?  132 PHE   A CD1  1 
ATOM   2758 C CD1  B PHE   A 1 132 ? 21.602 0.919   -6.697  0.30 21.99 ?  132 PHE   A CD1  1 
ATOM   2759 C CD2  A PHE   A 1 132 ? 22.041 -0.661  -5.399  0.70 11.49 ?  132 PHE   A CD2  1 
ATOM   2760 C CD2  B PHE   A 1 132 ? 21.968 -1.051  -5.406  0.30 21.77 ?  132 PHE   A CD2  1 
ATOM   2761 C CE1  A PHE   A 1 132 ? 21.778 1.377   -3.571  0.70 11.61 ?  132 PHE   A CE1  1 
ATOM   2762 C CE1  B PHE   A 1 132 ? 22.845 1.382   -6.363  0.30 22.29 ?  132 PHE   A CE1  1 
ATOM   2763 C CE2  A PHE   A 1 132 ? 23.162 -0.134  -4.781  0.70 11.87 ?  132 PHE   A CE2  1 
ATOM   2764 C CE2  B PHE   A 1 132 ? 23.223 -0.588  -5.067  0.30 22.01 ?  132 PHE   A CE2  1 
ATOM   2765 C CZ   A PHE   A 1 132 ? 23.026 0.882   -3.867  0.70 11.53 ?  132 PHE   A CZ   1 
ATOM   2766 C CZ   B PHE   A 1 132 ? 23.661 0.632   -5.547  0.30 22.15 ?  132 PHE   A CZ   1 
ATOM   2767 H H    A PHE   A 1 132 ? 17.674 0.727   -5.037  0.70 13.55 ?  132 PHE   A H    1 
ATOM   2768 H H    B PHE   A 1 132 ? 17.954 0.674   -5.622  0.30 21.92 ?  132 PHE   A H    1 
ATOM   2769 H HA   A PHE   A 1 132 ? 19.382 0.781   -7.075  0.70 13.45 ?  132 PHE   A HA   1 
ATOM   2770 H HA   B PHE   A 1 132 ? 19.455 0.824   -7.828  0.30 22.73 ?  132 PHE   A HA   1 
ATOM   2771 H HB2  A PHE   A 1 132 ? 18.966 -1.107  -5.057  0.70 12.75 ?  132 PHE   A HB2  1 
ATOM   2772 H HB2  B PHE   A 1 132 ? 19.320 -1.134  -5.809  0.30 23.91 ?  132 PHE   A HB2  1 
ATOM   2773 H HB3  A PHE   A 1 132 ? 19.833 -1.513  -6.324  0.70 12.75 ?  132 PHE   A HB3  1 
ATOM   2774 H HB3  B PHE   A 1 132 ? 19.905 -1.558  -7.206  0.30 23.91 ?  132 PHE   A HB3  1 
ATOM   2775 H HD1  A PHE   A 1 132 ? 19.815 1.178   -3.966  0.70 13.79 ?  132 PHE   A HD1  1 
ATOM   2776 H HD1  B PHE   A 1 132 ? 21.056 1.435   -7.252  0.30 26.39 ?  132 PHE   A HD1  1 
ATOM   2777 H HD2  A PHE   A 1 132 ? 22.140 -1.352  -6.016  0.70 13.79 ?  132 PHE   A HD2  1 
ATOM   2778 H HD2  B PHE   A 1 132 ? 21.676 -1.874  -5.082  0.30 26.13 ?  132 PHE   A HD2  1 
ATOM   2779 H HE1  A PHE   A 1 132 ? 21.691 2.064   -2.950  0.70 13.94 ?  132 PHE   A HE1  1 
ATOM   2780 H HE1  B PHE   A 1 132 ? 23.131 2.203   -6.692  0.30 26.75 ?  132 PHE   A HE1  1 
ATOM   2781 H HE2  A PHE   A 1 132 ? 24.007 -0.460  -4.995  0.70 14.25 ?  132 PHE   A HE2  1 
ATOM   2782 H HE2  B PHE   A 1 132 ? 23.772 -1.096  -4.518  0.30 26.41 ?  132 PHE   A HE2  1 
ATOM   2783 H HZ   A PHE   A 1 132 ? 23.779 1.247   -3.464  0.70 13.83 ?  132 PHE   A HZ   1 
ATOM   2784 H HZ   B PHE   A 1 132 ? 24.503 0.946   -5.322  0.30 26.58 ?  132 PHE   A HZ   1 
ATOM   2785 N N    A GLY   A 1 133 ? 16.644 -0.511  -7.681  0.70 12.80 ?  133 GLY   A N    1 
ATOM   2786 N N    B GLY   A 1 133 ? 16.737 -0.548  -8.154  0.30 18.37 ?  133 GLY   A N    1 
ATOM   2787 C CA   A GLY   A 1 133 ? 15.857 -0.884  -8.835  0.70 13.74 ?  133 GLY   A CA   1 
ATOM   2788 C CA   B GLY   A 1 133 ? 15.811 -0.881  -9.211  0.30 18.11 ?  133 GLY   A CA   1 
ATOM   2789 C C    A GLY   A 1 133 ? 15.492 -2.344  -8.991  0.70 14.07 ?  133 GLY   A C    1 
ATOM   2790 C C    B GLY   A 1 133 ? 15.545 -2.353  -9.425  0.30 17.83 ?  133 GLY   A C    1 
ATOM   2791 O O    A GLY   A 1 133 ? 14.774 -2.666  -9.945  0.70 15.55 ?  133 GLY   A O    1 
ATOM   2792 O O    B GLY   A 1 133 ? 14.953 -2.708  -10.451 0.30 18.05 ?  133 GLY   A O    1 
ATOM   2793 H H    A GLY   A 1 133 ? 16.167 -0.269  -7.002  0.70 15.36 ?  133 GLY   A H    1 
ATOM   2794 H H    B GLY   A 1 133 ? 16.376 -0.415  -7.387  0.30 22.04 ?  133 GLY   A H    1 
ATOM   2795 H HA2  A GLY   A 1 133 ? 15.019 -0.398  -8.818  0.70 16.49 ?  133 GLY   A HA2  1 
ATOM   2796 H HA2  B GLY   A 1 133 ? 14.973 -0.428  -9.028  0.30 21.73 ?  133 GLY   A HA2  1 
ATOM   2797 H HA3  A GLY   A 1 133 ? 16.333 -0.629  -9.637  0.70 16.49 ?  133 GLY   A HA3  1 
ATOM   2798 H HA3  B GLY   A 1 133 ? 16.159 -0.535  -10.046 0.30 21.73 ?  133 GLY   A HA3  1 
ATOM   2799 N N    A ALA   A 1 134 ? 15.939 -3.238  -8.110  0.70 13.55 ?  134 ALA   A N    1 
ATOM   2800 N N    B ALA   A 1 134 ? 15.968 -3.221  -8.510  0.30 17.40 ?  134 ALA   A N    1 
ATOM   2801 C CA   A ALA   A 1 134 ? 15.567 -4.636  -8.262  0.70 13.74 ?  134 ALA   A CA   1 
ATOM   2802 C CA   B ALA   A 1 134 ? 15.711 -4.645  -8.658  0.30 17.20 ?  134 ALA   A CA   1 
ATOM   2803 C C    A ALA   A 1 134 ? 14.214 -4.902  -7.611  0.70 14.17 ?  134 ALA   A C    1 
ATOM   2804 C C    B ALA   A 1 134 ? 14.370 -5.023  -8.030  0.30 17.04 ?  134 ALA   A C    1 
ATOM   2805 O O    A ALA   A 1 134 ? 13.713 -4.110  -6.808  0.70 15.25 ?  134 ALA   A O    1 
ATOM   2806 O O    B ALA   A 1 134 ? 13.766 -4.258  -7.275  0.30 17.21 ?  134 ALA   A O    1 
ATOM   2807 C CB   A ALA   A 1 134 ? 16.623 -5.572  -7.678  0.70 14.39 ?  134 ALA   A CB   1 
ATOM   2808 C CB   B ALA   A 1 134 ? 16.844 -5.464  -8.045  0.30 17.32 ?  134 ALA   A CB   1 
ATOM   2809 H H    A ALA   A 1 134 ? 16.452 -3.065  -7.426  0.70 16.26 ?  134 ALA   A H    1 
ATOM   2810 H H    B ALA   A 1 134 ? 16.420 -3.010  -7.802  0.30 20.88 ?  134 ALA   A H    1 
ATOM   2811 H HA   A ALA   A 1 134 ? 15.485 -4.831  -9.205  0.70 16.49 ?  134 ALA   A HA   1 
ATOM   2812 H HA   B ALA   A 1 134 ? 15.666 -4.852  -9.601  0.30 20.64 ?  134 ALA   A HA   1 
ATOM   2813 H HB1  A ALA   A 1 134 ? 16.342 -6.489  -7.823  0.70 17.27 ?  134 ALA   A HB1  1 
ATOM   2814 H HB1  B ALA   A 1 134 ? 16.654 -6.405  -8.177  0.30 20.79 ?  134 ALA   A HB1  1 
ATOM   2815 H HB2  A ALA   A 1 134 ? 17.467 -5.410  -8.129  0.70 17.27 ?  134 ALA   A HB2  1 
ATOM   2816 H HB2  B ALA   A 1 134 ? 17.675 -5.228  -8.486  0.30 20.79 ?  134 ALA   A HB2  1 
ATOM   2817 H HB3  A ALA   A 1 134 ? 16.714 -5.398  -6.730  0.70 17.27 ?  134 ALA   A HB3  1 
ATOM   2818 H HB3  B ALA   A 1 134 ? 16.902 -5.266  -7.098  0.30 20.79 ?  134 ALA   A HB3  1 
ATOM   2819 N N    A ASP   A 1 135 ? 13.624 -6.032  -7.983  0.70 15.01 ?  135 ASP   A N    1 
ATOM   2820 N N    B ASP   A 1 135 ? 13.905 -6.226  -8.356  0.30 17.08 ?  135 ASP   A N    1 
ATOM   2821 C CA   A ASP   A 1 135 ? 12.373 -6.494  -7.389  0.70 16.22 ?  135 ASP   A CA   1 
ATOM   2822 C CA   B ASP   A 1 135 ? 12.623 -6.709  -7.852  0.30 17.37 ?  135 ASP   A CA   1 
ATOM   2823 C C    A ASP   A 1 135 ? 12.636 -6.947  -5.957  0.70 15.22 ?  135 ASP   A C    1 
ATOM   2824 C C    B ASP   A 1 135 ? 12.777 -7.171  -6.407  0.30 16.27 ?  135 ASP   A C    1 
ATOM   2825 O O    A ASP   A 1 135 ? 13.394 -7.905  -5.754  0.70 14.67 ?  135 ASP   A O    1 
ATOM   2826 O O    B ASP   A 1 135 ? 13.603 -8.049  -6.134  0.30 15.92 ?  135 ASP   A O    1 
ATOM   2827 C CB   A ASP   A 1 135 ? 11.865 -7.666  -8.230  0.70 18.93 ?  135 ASP   A CB   1 
ATOM   2828 C CB   B ASP   A 1 135 ? 12.121 -7.862  -8.712  0.30 19.23 ?  135 ASP   A CB   1 
ATOM   2829 C CG   A ASP   A 1 135 ? 10.565 -8.271  -7.707  0.70 21.14 ?  135 ASP   A CG   1 
ATOM   2830 C CG   B ASP   A 1 135 ? 10.868 -8.518  -8.147  0.30 20.83 ?  135 ASP   A CG   1 
ATOM   2831 O OD1  A ASP   A 1 135 ? 10.051 -7.808  -6.669  0.70 21.51 ?  135 ASP   A OD1  1 
ATOM   2832 O OD1  B ASP   A 1 135 ? 9.821  -7.843  -8.056  0.30 21.71 ?  135 ASP   A OD1  1 
ATOM   2833 O OD2  A ASP   A 1 135 ? 10.056 -9.213  -8.356  0.70 23.83 -1 135 ASP   A OD2  1 
ATOM   2834 O OD2  B ASP   A 1 135 ? 10.930 -9.715  -7.799  0.30 21.37 -1 135 ASP   A OD2  1 
ATOM   2835 H H    A ASP   A 1 135 ? 13.927 -6.555  -8.590  0.70 18.01 ?  135 ASP   A H    1 
ATOM   2836 H H    B ASP   A 1 135 ? 14.312 -6.778  -8.872  0.30 20.50 ?  135 ASP   A H    1 
ATOM   2837 H HA   A ASP   A 1 135 ? 11.709 -5.780  -7.409  0.70 19.47 ?  135 ASP   A HA   1 
ATOM   2838 H HA   B ASP   A 1 135 ? 11.977 -5.989  -7.900  0.30 20.84 ?  135 ASP   A HA   1 
ATOM   2839 H HB2  A ASP   A 1 135 ? 11.703 -7.356  -9.133  0.70 22.72 ?  135 ASP   A HB2  1 
ATOM   2840 H HB2  B ASP   A 1 135 ? 11.924 -7.526  -9.602  0.30 23.08 ?  135 ASP   A HB2  1 
ATOM   2841 H HB3  A ASP   A 1 135 ? 12.542 -8.359  -8.231  0.70 22.72 ?  135 ASP   A HB3  1 
ATOM   2842 H HB3  B ASP   A 1 135 ? 12.805 -8.544  -8.757  0.30 23.08 ?  135 ASP   A HB3  1 
ATOM   2843 N N    A PRO   A 1 136 ? 12.055 -6.297  -4.943  0.70 14.89 ?  136 PRO   A N    1 
ATOM   2844 N N    B PRO   A 1 136 ? 12.007 -6.623  -5.463  0.30 15.49 ?  136 PRO   A N    1 
ATOM   2845 C CA   A PRO   A 1 136 ? 12.322 -6.716  -3.554  0.70 14.94 ?  136 PRO   A CA   1 
ATOM   2846 C CA   B PRO   A 1 136 ? 12.202 -7.005  -4.053  0.30 14.86 ?  136 PRO   A CA   1 
ATOM   2847 C C    A PRO   A 1 136 ? 11.885 -8.143  -3.238  0.70 13.91 ?  136 PRO   A C    1 
ATOM   2848 C C    B PRO   A 1 136 ? 11.833 -8.447  -3.751  0.30 14.23 ?  136 PRO   A C    1 
ATOM   2849 O O    A PRO   A 1 136 ? 12.469 -8.781  -2.353  0.70 13.39 ?  136 PRO   A O    1 
ATOM   2850 O O    B PRO   A 1 136 ? 12.503 -9.089  -2.933  0.30 13.98 ?  136 PRO   A O    1 
ATOM   2851 C CB   A PRO   A 1 136 ? 11.563 -5.668  -2.722  0.70 16.09 ?  136 PRO   A CB   1 
ATOM   2852 C CB   B PRO   A 1 136 ? 11.317 -6.005  -3.296  0.30 15.11 ?  136 PRO   A CB   1 
ATOM   2853 C CG   A PRO   A 1 136 ? 10.535 -5.111  -3.658  0.70 17.05 ?  136 PRO   A CG   1 
ATOM   2854 C CG   B PRO   A 1 136 ? 10.290 -5.572  -4.294  0.30 15.53 ?  136 PRO   A CG   1 
ATOM   2855 C CD   A PRO   A 1 136 ? 11.168 -5.122  -5.005  0.70 15.76 ?  136 PRO   A CD   1 
ATOM   2856 C CD   B PRO   A 1 136 ? 10.971 -5.590  -5.627  0.30 15.57 ?  136 PRO   A CD   1 
ATOM   2857 H HA   A PRO   A 1 136 ? 13.271 -6.625  -3.361  0.70 17.93 ?  136 PRO   A HA   1 
ATOM   2858 H HA   B PRO   A 1 136 ? 13.130 -6.861  -3.794  0.30 17.83 ?  136 PRO   A HA   1 
ATOM   2859 H HB2  A PRO   A 1 136 ? 11.140 -6.090  -1.961  0.70 19.30 ?  136 PRO   A HB2  1 
ATOM   2860 H HB2  B PRO   A 1 136 ? 10.900 -6.446  -2.540  0.30 18.13 ?  136 PRO   A HB2  1 
ATOM   2861 H HB3  A PRO   A 1 136 ? 12.173 -4.965  -2.432  0.70 19.30 ?  136 PRO   A HB3  1 
ATOM   2862 H HB3  B PRO   A 1 136 ? 11.854 -5.251  -3.003  0.30 18.13 ?  136 PRO   A HB3  1 
ATOM   2863 H HG2  A PRO   A 1 136 ? 9.752  -5.681  -3.654  0.70 20.46 ?  136 PRO   A HG2  1 
ATOM   2864 H HG2  B PRO   A 1 136 ? 9.549  -6.195  -4.286  0.30 18.64 ?  136 PRO   A HG2  1 
ATOM   2865 H HG3  A PRO   A 1 136 ? 10.305 -4.207  -3.397  0.70 20.46 ?  136 PRO   A HG3  1 
ATOM   2866 H HG3  B PRO   A 1 136 ? 9.991  -4.676  -4.082  0.30 18.64 ?  136 PRO   A HG3  1 
ATOM   2867 H HD2  A PRO   A 1 136 ? 10.490 -5.242  -5.693  0.70 18.91 ?  136 PRO   A HD2  1 
ATOM   2868 H HD2  B PRO   A 1 136 ? 10.352 -5.853  -6.326  0.30 18.69 ?  136 PRO   A HD2  1 
ATOM   2869 H HD3  A PRO   A 1 136 ? 11.678 -4.307  -5.152  0.70 18.91 ?  136 PRO   A HD3  1 
ATOM   2870 H HD3  B PRO   A 1 136 ? 11.380 -4.731  -5.819  0.30 18.69 ?  136 PRO   A HD3  1 
ATOM   2871 N N    A ILE   A 1 137 ? 10.861 -8.660  -3.919  0.70 14.56 ?  137 ILE   A N    1 
ATOM   2872 N N    B ILE   A 1 137 ? 10.774 -8.975  -4.368  0.30 14.16 ?  137 ILE   A N    1 
ATOM   2873 C CA   A ILE   A 1 137 ? 10.472 -10.053 -3.711  0.70 15.00 ?  137 ILE   A CA   1 
ATOM   2874 C CA   B ILE   A 1 137 ? 10.448 -10.389 -4.196  0.30 14.51 ?  137 ILE   A CA   1 
ATOM   2875 C C    A ILE   A 1 137 ? 11.607 -10.986 -4.123  0.70 14.92 ?  137 ILE   A C    1 
ATOM   2876 C C    B ILE   A 1 137 ? 11.660 -11.241 -4.533  0.30 14.80 ?  137 ILE   A C    1 
ATOM   2877 O O    A ILE   A 1 137 ? 11.925 -11.958 -3.423  0.70 15.16 ?  137 ILE   A O    1 
ATOM   2878 O O    B ILE   A 1 137 ? 11.959 -12.232 -3.856  0.30 15.20 ?  137 ILE   A O    1 
ATOM   2879 C CB   A ILE   A 1 137 ? 9.167  -10.360 -4.469  0.70 16.21 ?  137 ILE   A CB   1 
ATOM   2880 C CB   B ILE   A 1 137 ? 9.226  -10.767 -5.056  0.30 14.95 ?  137 ILE   A CB   1 
ATOM   2881 C CG1  A ILE   A 1 137 ? 8.002  -9.531  -3.914  0.70 17.59 ?  137 ILE   A CG1  1 
ATOM   2882 C CG1  B ILE   A 1 137 ? 7.992  -9.979  -4.609  0.30 15.34 ?  137 ILE   A CG1  1 
ATOM   2883 C CG2  A ILE   A 1 137 ? 8.846  -11.842 -4.392  0.70 16.83 ?  137 ILE   A CG2  1 
ATOM   2884 C CG2  B ILE   A 1 137 ? 8.961  -12.268 -4.985  0.30 15.08 ?  137 ILE   A CG2  1 
ATOM   2885 C CD1  A ILE   A 1 137 ? 6.708  -9.720  -4.671  0.70 18.87 ?  137 ILE   A CD1  1 
ATOM   2886 C CD1  B ILE   A 1 137 ? 6.798  -10.136 -5.530  0.30 15.86 ?  137 ILE   A CD1  1 
ATOM   2887 H H    A ILE   A 1 137 ? 10.385 -8.221  -4.492  0.70 17.47 ?  137 ILE   A H    1 
ATOM   2888 H H    B ILE   A 1 137 ? 10.244 -8.545  -4.882  0.30 17.00 ?  137 ILE   A H    1 
ATOM   2889 H HA   A ILE   A 1 137 ? 10.306 -10.180 -2.768  0.70 18.01 ?  137 ILE   A HA   1 
ATOM   2890 H HA   B ILE   A 1 137 ? 10.223 -10.556 -3.270  0.30 17.42 ?  137 ILE   A HA   1 
ATOM   2891 H HB   A ILE   A 1 137 ? 9.289  -10.115 -5.398  0.70 19.46 ?  137 ILE   A HB   1 
ATOM   2892 H HB   B ILE   A 1 137 ? 9.416  -10.535 -5.977  0.30 17.94 ?  137 ILE   A HB   1 
ATOM   2893 H HG12 A ILE   A 1 137 ? 7.843  -9.785  -2.992  0.70 21.11 ?  137 ILE   A HG12 1 
ATOM   2894 H HG12 B ILE   A 1 137 ? 7.728  -10.284 -3.727  0.30 18.41 ?  137 ILE   A HG12 1 
ATOM   2895 H HG13 A ILE   A 1 137 ? 8.232  -8.586  -3.957  0.70 21.11 ?  137 ILE   A HG13 1 
ATOM   2896 H HG13 B ILE   A 1 137 ? 8.216  -9.035  -4.576  0.30 18.41 ?  137 ILE   A HG13 1 
ATOM   2897 H HG21 A ILE   A 1 137 ? 8.028  -12.017 -4.877  0.70 20.20 ?  137 ILE   A HG21 1 
ATOM   2898 H HG21 B ILE   A 1 137 ? 8.105  -12.461 -5.398  0.30 18.09 ?  137 ILE   A HG21 1 
ATOM   2899 H HG22 A ILE   A 1 137 ? 9.568  -12.344 -4.794  0.70 20.20 ?  137 ILE   A HG22 1 
ATOM   2900 H HG22 B ILE   A 1 137 ? 9.663  -12.736 -5.459  0.30 18.09 ?  137 ILE   A HG22 1 
ATOM   2901 H HG23 A ILE   A 1 137 ? 8.743  -12.089 -3.461  0.70 20.20 ?  137 ILE   A HG23 1 
ATOM   2902 H HG23 B ILE   A 1 137 ? 8.946  -12.540 -4.055  0.30 18.09 ?  137 ILE   A HG23 1 
ATOM   2903 H HD11 A ILE   A 1 137 ? 6.036  -9.174  -4.246  0.70 22.65 ?  137 ILE   A HD11 1 
ATOM   2904 H HD11 B ILE   A 1 137 ? 6.147  -9.449  -5.320  0.30 19.04 ?  137 ILE   A HD11 1 
ATOM   2905 H HD12 A ILE   A 1 137 ? 6.830  -9.445  -5.596  0.70 22.65 ?  137 ILE   A HD12 1 
ATOM   2906 H HD12 B ILE   A 1 137 ? 7.096  -10.039 -6.449  0.30 19.04 ?  137 ILE   A HD12 1 
ATOM   2907 H HD13 A ILE   A 1 137 ? 6.436  -10.651 -4.636  0.70 22.65 ?  137 ILE   A HD13 1 
ATOM   2908 H HD13 B ILE   A 1 137 ? 6.409  -11.013 -5.398  0.30 19.04 ?  137 ILE   A HD13 1 
ATOM   2909 N N    A HIS   A 1 138 ? 12.221 -10.709 -5.277  0.70 15.66 ?  138 HIS   A N    1 
ATOM   2910 N N    B HIS   A 1 138 ? 12.381 -10.861 -5.587  0.30 15.09 ?  138 HIS   A N    1 
ATOM   2911 C CA   A HIS   A 1 138 ? 13.360 -11.502 -5.731  0.70 15.76 ?  138 HIS   A CA   1 
ATOM   2912 C CA   B HIS   A 1 138 ? 13.604 -11.570 -5.932  0.30 15.10 ?  138 HIS   A CA   1 
ATOM   2913 C C    A HIS   A 1 138 ? 14.532 -11.386 -4.765  0.70 15.30 ?  138 HIS   A C    1 
ATOM   2914 C C    B HIS   A 1 138 ? 14.679 -11.382 -4.866  0.30 14.77 ?  138 HIS   A C    1 
ATOM   2915 O O    A HIS   A 1 138 ? 15.173 -12.388 -4.424  0.70 15.32 ?  138 HIS   A O    1 
ATOM   2916 O O    B HIS   A 1 138 ? 15.387 -12.338 -4.525  0.30 14.47 ?  138 HIS   A O    1 
ATOM   2917 C CB   A HIS   A 1 138 ? 13.764 -11.054 -7.136  0.70 16.32 ?  138 HIS   A CB   1 
ATOM   2918 C CB   B HIS   A 1 138 ? 14.102 -11.126 -7.305  0.30 16.04 ?  138 HIS   A CB   1 
ATOM   2919 C CG   A HIS   A 1 138 ? 15.052 -11.649 -7.606  0.70 17.15 ?  138 HIS   A CG   1 
ATOM   2920 C CG   B HIS   A 1 138 ? 15.335 -11.845 -7.752  0.30 17.12 ?  138 HIS   A CG   1 
ATOM   2921 N ND1  A HIS   A 1 138 ? 15.202 -12.996 -7.853  0.70 18.50 ?  138 HIS   A ND1  1 
ATOM   2922 N ND1  B HIS   A 1 138 ? 15.335 -13.178 -8.103  0.30 17.97 ?  138 HIS   A ND1  1 
ATOM   2923 C CD2  A HIS   A 1 138 ? 16.255 -11.082 -7.862  0.70 17.10 ?  138 HIS   A CD2  1 
ATOM   2924 C CD2  B HIS   A 1 138 ? 16.612 -11.420 -7.886  0.30 17.48 ?  138 HIS   A CD2  1 
ATOM   2925 C CE1  A HIS   A 1 138 ? 16.440 -13.232 -8.248  0.70 18.59 ?  138 HIS   A CE1  1 
ATOM   2926 C CE1  B HIS   A 1 138 ? 16.558 -13.540 -8.444  0.30 18.18 ?  138 HIS   A CE1  1 
ATOM   2927 N NE2  A HIS   A 1 138 ? 17.101 -12.089 -8.261  0.70 17.88 ?  138 HIS   A NE2  1 
ATOM   2928 N NE2  B HIS   A 1 138 ? 17.353 -12.493 -8.320  0.30 17.78 ?  138 HIS   A NE2  1 
ATOM   2929 H H    A HIS   A 1 138 ? 11.995 -10.066 -5.814  0.70 18.79 ?  138 HIS   A H    1 
ATOM   2930 H H    B HIS   A 1 138 ? 12.180 -10.210 -6.113  0.30 18.11 ?  138 HIS   A H    1 
ATOM   2931 H HA   A HIS   A 1 138 ? 13.091 -12.428 -5.778  0.70 18.91 ?  138 HIS   A HA   1 
ATOM   2932 H HA   B HIS   A 1 138 ? 13.406 -12.516 -5.989  0.30 18.12 ?  138 HIS   A HA   1 
ATOM   2933 H HB2  A HIS   A 1 138 ? 13.068 -11.320 -7.763  0.70 19.58 ?  138 HIS   A HB2  1 
ATOM   2934 H HB2  B HIS   A 1 138 ? 13.406 -11.294 -7.963  0.30 19.24 ?  138 HIS   A HB2  1 
ATOM   2935 H HB3  A HIS   A 1 138 ? 13.859 -10.089 -7.147  0.70 19.58 ?  138 HIS   A HB3  1 
ATOM   2936 H HB3  B HIS   A 1 138 ? 14.304 -10.178 -7.278  0.30 19.24 ?  138 HIS   A HB3  1 
ATOM   2937 H HD1  A HIS   A 1 138 ? 14.585 -13.590 -7.768  0.70 22.20 ?  138 HIS   A HD1  1 
ATOM   2938 H HD2  A HIS   A 1 138 ? 16.467 -10.180 -7.785  0.70 20.53 ?  138 HIS   A HD2  1 
ATOM   2939 H HD2  B HIS   A 1 138 ? 16.929 -10.561 -7.718  0.30 20.98 ?  138 HIS   A HD2  1 
ATOM   2940 H HE1  A HIS   A 1 138 ? 16.789 -14.064 -8.475  0.70 22.30 ?  138 HIS   A HE1  1 
ATOM   2941 H HE1  B HIS   A 1 138 ? 16.816 -14.388 -8.721  0.30 21.82 ?  138 HIS   A HE1  1 
ATOM   2942 H HE2  B HIS   A 1 138 ? 18.197 -12.483 -8.483  0.30 21.34 ?  138 HIS   A HE2  1 
ATOM   2943 N N    . SER   A 1 139 ? 14.821 -10.170 -4.316  1.00 14.74 ?  139 SER   A N    1 
ATOM   2944 C CA   . SER   A 1 139 ? 15.889 -9.965  -3.345  1.00 14.48 ?  139 SER   A CA   1 
ATOM   2945 C C    . SER   A 1 139 ? 15.674 -10.809 -2.094  1.00 13.96 ?  139 SER   A C    1 
ATOM   2946 O O    . SER   A 1 139 ? 16.625 -11.401 -1.566  1.00 13.91 ?  139 SER   A O    1 
ATOM   2947 C CB   . SER   A 1 139 ? 16.012 -8.486  -2.992  1.00 14.65 ?  139 SER   A CB   1 
ATOM   2948 O OG   . SER   A 1 139 ? 17.100 -8.319  -2.103  1.00 14.66 ?  139 SER   A OG   1 
ATOM   2949 H H    A SER   A 1 139 ? 14.413 -9.449  -4.554  0.70 17.69 ?  139 SER   A H    1 
ATOM   2950 H H    B SER   A 1 139 ? 14.333 -9.480  -4.485  0.30 17.69 ?  139 SER   A H    1 
ATOM   2951 H HA   . SER   A 1 139 ? 16.729 -10.238 -3.743  1.00 17.38 ?  139 SER   A HA   1 
ATOM   2952 H HB2  . SER   A 1 139 ? 16.170 -7.969  -3.800  1.00 17.58 ?  139 SER   A HB2  1 
ATOM   2953 H HB3  . SER   A 1 139 ? 15.199 -8.186  -2.556  1.00 17.58 ?  139 SER   A HB3  1 
ATOM   2954 H HG   . SER   A 1 139 ? 17.194 -7.509  -1.903  1.00 17.59 ?  139 SER   A HG   1 
ATOM   2955 N N    . LEU   A 1 140 ? 14.436 -10.875 -1.602  1.00 14.08 ?  140 LEU   A N    1 
ATOM   2956 C CA   . LEU   A 1 140 ? 14.166 -11.692 -0.424  1.00 14.25 ?  140 LEU   A CA   1 
ATOM   2957 C C    . LEU   A 1 140 ? 14.430 -13.167 -0.707  1.00 14.07 ?  140 LEU   A C    1 
ATOM   2958 O O    . LEU   A 1 140 ? 14.974 -13.883 0.142   1.00 14.69 ?  140 LEU   A O    1 
ATOM   2959 C CB   . LEU   A 1 140 ? 12.724 -11.472 0.033   1.00 14.63 ?  140 LEU   A CB   1 
ATOM   2960 C CG   . LEU   A 1 140 ? 12.270 -12.324 1.216   1.00 15.26 ?  140 LEU   A CG   1 
ATOM   2961 C CD1  . LEU   A 1 140 ? 13.183 -12.142 2.417   1.00 15.77 ?  140 LEU   A CD1  1 
ATOM   2962 C CD2  . LEU   A 1 140 ? 10.816 -12.009 1.587   1.00 15.92 ?  140 LEU   A CD2  1 
ATOM   2963 H H    . LEU   A 1 140 ? 13.752 -10.460 -1.920  1.00 16.89 ?  140 LEU   A H    1 
ATOM   2964 H HA   . LEU   A 1 140 ? 14.749 -11.417 0.296   1.00 17.10 ?  140 LEU   A HA   1 
ATOM   2965 H HB2  . LEU   A 1 140 ? 12.620 -10.546 0.291   1.00 17.56 ?  140 LEU   A HB2  1 
ATOM   2966 H HB3  . LEU   A 1 140 ? 12.132 -11.671 -0.711  1.00 17.56 ?  140 LEU   A HB3  1 
ATOM   2967 H HG   . LEU   A 1 140 ? 12.296 -13.262 0.958   1.00 18.31 ?  140 LEU   A HG   1 
ATOM   2968 H HD11 . LEU   A 1 140 ? 12.797 -12.605 3.178   1.00 18.92 ?  140 LEU   A HD11 1 
ATOM   2969 H HD12 . LEU   A 1 140 ? 14.050 -12.527 2.206   1.00 18.92 ?  140 LEU   A HD12 1 
ATOM   2970 H HD13 . LEU   A 1 140 ? 13.269 -11.201 2.605   1.00 18.92 ?  140 LEU   A HD13 1 
ATOM   2971 H HD21 . LEU   A 1 140 ? 10.572 -12.522 2.378   1.00 19.11 ?  140 LEU   A HD21 1 
ATOM   2972 H HD22 . LEU   A 1 140 ? 10.735 -11.063 1.772   1.00 19.11 ?  140 LEU   A HD22 1 
ATOM   2973 H HD23 . LEU   A 1 140 ? 10.236 -12.255 0.848   1.00 19.11 ?  140 LEU   A HD23 1 
ATOM   2974 N N    . ARG   A 1 141 ? 14.041 -13.638 -1.895  1.00 14.74 ?  141 ARG   A N    1 
ATOM   2975 C CA   . ARG   A 1 141 ? 14.280 -15.027 -2.271  1.00 15.94 ?  141 ARG   A CA   1 
ATOM   2976 C C    . ARG   A 1 141 ? 15.775 -15.335 -2.280  1.00 14.90 ?  141 ARG   A C    1 
ATOM   2977 O O    . ARG   A 1 141 ? 16.221 -16.350 -1.727  1.00 14.91 ?  141 ARG   A O    1 
ATOM   2978 C CB   . ARG   A 1 141 ? 13.663 -15.269 -3.651  1.00 17.82 ?  141 ARG   A CB   1 
ATOM   2979 C CG   . ARG   A 1 141 ? 13.658 -16.702 -4.128  1.00 20.38 ?  141 ARG   A CG   1 
ATOM   2980 C CD   . ARG   A 1 141 ? 12.630 -17.499 -3.385  1.00 22.10 ?  141 ARG   A CD   1 
ATOM   2981 N NE   . ARG   A 1 141 ? 13.235 -18.266 -2.308  1.00 22.41 ?  141 ARG   A NE   1 
ATOM   2982 C CZ   . ARG   A 1 141 ? 12.542 -18.849 -1.340  1.00 23.26 ?  141 ARG   A CZ   1 
ATOM   2983 N NH1  . ARG   A 1 141 ? 11.242 -18.653 -1.208  1.00 23.01 ?  141 ARG   A NH1  1 
ATOM   2984 N NH2  . ARG   A 1 141 ? 13.171 -19.641 -0.476  1.00 24.14 ?  141 ARG   A NH2  1 
ATOM   2985 H H    . ARG   A 1 141 ? 13.642 -13.172 -2.501  1.00 17.69 ?  141 ARG   A H    1 
ATOM   2986 H HA   . ARG   A 1 141 ? 13.849 -15.615 -1.635  1.00 19.12 ?  141 ARG   A HA   1 
ATOM   2987 H HB2  . ARG   A 1 141 ? 12.744 -14.958 -3.636  1.00 21.38 ?  141 ARG   A HB2  1 
ATOM   2988 H HB3  . ARG   A 1 141 ? 14.163 -14.749 -4.302  1.00 21.38 ?  141 ARG   A HB3  1 
ATOM   2989 H HG2  . ARG   A 1 141 ? 13.444 -16.728 -5.076  1.00 24.45 ?  141 ARG   A HG2  1 
ATOM   2990 H HG3  . ARG   A 1 141 ? 14.531 -17.101 -3.973  1.00 24.45 ?  141 ARG   A HG3  1 
ATOM   2991 H HD2  . ARG   A 1 141 ? 11.977 -16.899 -2.992  1.00 26.52 ?  141 ARG   A HD2  1 
ATOM   2992 H HD3  . ARG   A 1 141 ? 12.192 -18.111 -3.999  1.00 26.52 ?  141 ARG   A HD3  1 
ATOM   2993 H HE   . ARG   A 1 141 ? 14.069 -18.458 -2.372  1.00 26.89 ?  141 ARG   A HE   1 
ATOM   2994 H HH11 . ARG   A 1 141 ? 10.814 -18.162 -1.769  1.00 27.62 ?  141 ARG   A HH11 1 
ATOM   2995 H HH12 . ARG   A 1 141 ? 10.807 -19.045 -0.572  1.00 27.62 ?  141 ARG   A HH12 1 
ATOM   2996 H HH21 . ARG   A 1 141 ? 14.017 -19.771 -0.549  1.00 28.97 ?  141 ARG   A HH21 1 
ATOM   2997 H HH22 . ARG   A 1 141 ? 12.733 -20.015 0.165   1.00 28.97 ?  141 ARG   A HH22 1 
ATOM   2998 N N    . VAL   A 1 142 ? 16.569 -14.467 -2.913  1.00 14.31 ?  142 VAL   A N    1 
ATOM   2999 C CA   . VAL   A 1 142 ? 18.014 -14.677 -2.942  1.00 14.02 ?  142 VAL   A CA   1 
ATOM   3000 C C    . VAL   A 1 142 ? 18.583 -14.659 -1.530  1.00 13.18 ?  142 VAL   A C    1 
ATOM   3001 O O    . VAL   A 1 142 ? 19.443 -15.477 -1.183  1.00 13.56 ?  142 VAL   A O    1 
ATOM   3002 C CB   . VAL   A 1 142 ? 18.710 -13.649 -3.855  1.00 14.30 ?  142 VAL   A CB   1 
ATOM   3003 C CG1  . VAL   A 1 142 ? 20.220 -13.861 -3.814  1.00 14.13 ?  142 VAL   A CG1  1 
ATOM   3004 C CG2  . VAL   A 1 142 ? 18.213 -13.773 -5.285  1.00 15.37 ?  142 VAL   A CG2  1 
ATOM   3005 H H    . VAL   A 1 142 ? 16.300 -13.756 -3.328  1.00 17.17 ?  142 VAL   A H    1 
ATOM   3006 H HA   . VAL   A 1 142 ? 18.189 -15.549 -3.318  1.00 16.82 ?  142 VAL   A HA   1 
ATOM   3007 H HB   . VAL   A 1 142 ? 18.525 -12.747 -3.544  1.00 17.16 ?  142 VAL   A HB   1 
ATOM   3008 H HG11 . VAL   A 1 142 ? 20.630 -13.375 -4.549  1.00 16.96 ?  142 VAL   A HG11 1 
ATOM   3009 H HG12 . VAL   A 1 142 ? 20.568 -13.528 -2.970  1.00 16.96 ?  142 VAL   A HG12 1 
ATOM   3010 H HG13 . VAL   A 1 142 ? 20.409 -14.807 -3.901  1.00 16.96 ?  142 VAL   A HG13 1 
ATOM   3011 H HG21 . VAL   A 1 142 ? 18.649 -13.097 -5.830  1.00 18.45 ?  142 VAL   A HG21 1 
ATOM   3012 H HG22 . VAL   A 1 142 ? 18.439 -14.657 -5.615  1.00 18.45 ?  142 VAL   A HG22 1 
ATOM   3013 H HG23 . VAL   A 1 142 ? 17.257 -13.646 -5.296  1.00 18.45 ?  142 VAL   A HG23 1 
ATOM   3014 N N    . CYS   A 1 143 ? 18.121 -13.729 -0.694  1.00 12.99 ?  143 CYS   A N    1 
ATOM   3015 C CA   . CYS   A 1 143 ? 18.582 -13.684 0.689   1.00 13.19 ?  143 CYS   A CA   1 
ATOM   3016 C C    . CYS   A 1 143 ? 18.357 -15.026 1.383   1.00 12.99 ?  143 CYS   A C    1 
ATOM   3017 O O    . CYS   A 1 143 ? 19.280 -15.610 1.957   1.00 13.01 ?  143 CYS   A O    1 
ATOM   3018 C CB   . CYS   A 1 143 ? 17.851 -12.568 1.434   1.00 13.54 ?  143 CYS   A CB   1 
ATOM   3019 S SG   . CYS   A 1 143 ? 18.335 -12.399 3.154   1.00 14.01 ?  143 CYS   A SG   1 
ATOM   3020 H H    . CYS   A 1 143 ? 17.545 -13.129 -0.903  1.00 15.59 ?  143 CYS   A H    1 
ATOM   3021 H HA   . CYS   A 1 143 ? 19.530 -13.495 0.701   1.00 15.82 ?  143 CYS   A HA   1 
ATOM   3022 H HB2  . CYS   A 1 143 ? 18.030 -11.724 0.986   1.00 16.25 ?  143 CYS   A HB2  1 
ATOM   3023 H HB3  . CYS   A 1 143 ? 16.901 -12.747 1.411   1.00 16.25 ?  143 CYS   A HB3  1 
ATOM   3024 H HG   . CYS   A 1 143 ? 17.765 -11.451 3.621   1.00 16.82 ?  143 CYS   A HG   1 
ATOM   3025 N N    . VAL   A 1 144 ? 17.128 -15.532 1.332   1.00 13.85 ?  144 VAL   A N    1 
ATOM   3026 C CA   . VAL   A 1 144 ? 16.795 -16.762 2.039   1.00 15.10 ?  144 VAL   A CA   1 
ATOM   3027 C C    . VAL   A 1 144 ? 17.602 -17.932 1.500   1.00 14.86 ?  144 VAL   A C    1 
ATOM   3028 O O    . VAL   A 1 144 ? 17.970 -18.849 2.248   1.00 15.28 ?  144 VAL   A O    1 
ATOM   3029 C CB   . VAL   A 1 144 ? 15.275 -16.997 1.945   1.00 18.14 ?  144 VAL   A CB   1 
ATOM   3030 C CG1  . VAL   A 1 144 ? 14.914 -18.427 2.296   1.00 19.79 ?  144 VAL   A CG1  1 
ATOM   3031 C CG2  . VAL   A 1 144 ? 14.545 -15.984 2.832   1.00 17.90 ?  144 VAL   A CG2  1 
ATOM   3032 H H    . VAL   A 1 144 ? 16.468 -15.177 0.900   1.00 16.62 ?  144 VAL   A H    1 
ATOM   3033 H HA   . VAL   A 1 144 ? 17.014 -16.656 2.972   1.00 18.11 ?  144 VAL   A HA   1 
ATOM   3034 H HB   . VAL   A 1 144 ? 14.988 -16.838 1.029   1.00 21.77 ?  144 VAL   A HB   1 
ATOM   3035 H HG11 . VAL   A 1 144 ? 13.962 -18.474 2.490   1.00 23.75 ?  144 VAL   A HG11 1 
ATOM   3036 H HG12 . VAL   A 1 144 ? 15.122 -19.002 1.544   1.00 23.75 ?  144 VAL   A HG12 1 
ATOM   3037 H HG13 . VAL   A 1 144 ? 15.420 -18.697 3.076   1.00 23.75 ?  144 VAL   A HG13 1 
ATOM   3038 H HG21 . VAL   A 1 144 ? 13.606 -16.221 2.886   1.00 21.48 ?  144 VAL   A HG21 1 
ATOM   3039 H HG22 . VAL   A 1 144 ? 14.937 -15.994 3.719   1.00 21.48 ?  144 VAL   A HG22 1 
ATOM   3040 H HG23 . VAL   A 1 144 ? 14.635 -15.094 2.445   1.00 21.48 ?  144 VAL   A HG23 1 
ATOM   3041 N N    . ASP   A 1 145 ? 17.860 -17.945 0.196   1.00 15.10 ?  145 ASP   A N    1 
ATOM   3042 C CA   . ASP   A 1 145 ? 18.566 -19.050 -0.439  1.00 15.68 ?  145 ASP   A CA   1 
ATOM   3043 C C    . ASP   A 1 145 ? 20.087 -18.908 -0.399  1.00 15.11 ?  145 ASP   A C    1 
ATOM   3044 O O    . ASP   A 1 145 ? 20.786 -19.809 -0.877  1.00 17.06 ?  145 ASP   A O    1 
ATOM   3045 C CB   . ASP   A 1 145 ? 18.108 -19.199 -1.893  1.00 17.26 ?  145 ASP   A CB   1 
ATOM   3046 C CG   . ASP   A 1 145 ? 16.656 -19.628 -2.009  1.00 19.62 ?  145 ASP   A CG   1 
ATOM   3047 O OD1  . ASP   A 1 145 ? 16.106 -20.172 -1.029  1.00 20.15 ?  145 ASP   A OD1  1 
ATOM   3048 O OD2  . ASP   A 1 145 ? 16.063 -19.414 -3.084  1.00 20.86 -1 145 ASP   A OD2  1 
ATOM   3049 H H    . ASP   A 1 145 ? 17.615 -17.325 -0.353  1.00 18.13 ?  145 ASP   A H    1 
ATOM   3050 H HA   . ASP   A 1 145 ? 18.330 -19.868 0.025   1.00 18.82 ?  145 ASP   A HA   1 
ATOM   3051 H HB2  . ASP   A 1 145 ? 18.211 -18.350 -2.350  1.00 20.71 ?  145 ASP   A HB2  1 
ATOM   3052 H HB3  . ASP   A 1 145 ? 18.645 -19.880 -2.326  1.00 20.71 ?  145 ASP   A HB3  1 
ATOM   3053 N N    . THR   A 1 146 ? 20.617 -17.817 0.156   1.00 13.38 ?  146 THR   A N    1 
ATOM   3054 C CA   . THR   A 1 146 ? 22.057 -17.571 0.167   1.00 12.69 ?  146 THR   A CA   1 
ATOM   3055 C C    . THR   A 1 146 ? 22.613 -17.405 1.569   1.00 12.72 ?  146 THR   A C    1 
ATOM   3056 O O    . THR   A 1 146 ? 23.695 -17.932 1.873   1.00 13.73 ?  146 THR   A O    1 
ATOM   3057 C CB   . THR   A 1 146 ? 22.380 -16.315 -0.668  1.00 12.68 ?  146 THR   A CB   1 
ATOM   3058 O OG1  . THR   A 1 146 ? 21.849 -16.472 -1.984  1.00 13.51 ?  146 THR   A OG1  1 
ATOM   3059 C CG2  . THR   A 1 146 ? 23.885 -16.083 -0.766  1.00 13.44 ?  146 THR   A CG2  1 
ATOM   3060 H H    . THR   A 1 146 ? 20.152 -17.194 0.528   1.00 16.06 ?  146 THR   A H    1 
ATOM   3061 H HA   . THR   A 1 146 ? 22.509 -18.320 -0.242  1.00 15.23 ?  146 THR   A HA   1 
ATOM   3062 H HB   . THR   A 1 146 ? 21.981 -15.536 -0.248  1.00 15.21 ?  146 THR   A HB   1 
ATOM   3063 H HG1  . THR   A 1 146 ? 21.010 -16.545 -1.948  1.00 16.21 ?  146 THR   A HG1  1 
ATOM   3064 H HG21 . THR   A 1 146 ? 24.069 -15.402 -1.427  1.00 16.13 ?  146 THR   A HG21 1 
ATOM   3065 H HG22 . THR   A 1 146 ? 24.232 -15.798 0.092   1.00 16.13 ?  146 THR   A HG22 1 
ATOM   3066 H HG23 . THR   A 1 146 ? 24.324 -16.907 -1.029  1.00 16.13 ?  146 THR   A HG23 1 
ATOM   3067 N N    . VAL   A 1 147 ? 21.941 -16.619 2.404   1.00 12.83 ?  147 VAL   A N    1 
ATOM   3068 C CA   . VAL   A 1 147 ? 22.428 -16.328 3.743   1.00 12.82 ?  147 VAL   A CA   1 
ATOM   3069 C C    . VAL   A 1 147 ? 22.112 -17.502 4.658   1.00 13.18 ?  147 VAL   A C    1 
ATOM   3070 O O    . VAL   A 1 147 ? 20.969 -17.973 4.717   1.00 13.88 ?  147 VAL   A O    1 
ATOM   3071 C CB   . VAL   A 1 147 ? 21.814 -15.025 4.271   1.00 13.13 ?  147 VAL   A CB   1 
ATOM   3072 C CG1  . VAL   A 1 147 ? 22.360 -14.720 5.647   1.00 14.10 ?  147 VAL   A CG1  1 
ATOM   3073 C CG2  . VAL   A 1 147 ? 22.070 -13.878 3.301   1.00 13.33 ?  147 VAL   A CG2  1 
ATOM   3074 H H    . VAL   A 1 147 ? 21.183 -16.247 2.221   1.00 15.40 ?  147 VAL   A H    1 
ATOM   3075 H HA   . VAL   A 1 147 ? 23.390 -16.215 3.710   1.00 15.38 ?  147 VAL   A HA   1 
ATOM   3076 H HB   . VAL   A 1 147 ? 20.856 -15.137 4.354   1.00 15.76 ?  147 VAL   A HB   1 
ATOM   3077 H HG11 . VAL   A 1 147 ? 22.123 -13.814 5.889   1.00 16.91 ?  147 VAL   A HG11 1 
ATOM   3078 H HG12 . VAL   A 1 147 ? 21.974 -15.344 6.287   1.00 16.91 ?  147 VAL   A HG12 1 
ATOM   3079 H HG13 . VAL   A 1 147 ? 23.325 -14.819 5.634   1.00 16.91 ?  147 VAL   A HG13 1 
ATOM   3080 H HG21 . VAL   A 1 147 ? 21.755 -13.053 3.702   1.00 15.99 ?  147 VAL   A HG21 1 
ATOM   3081 H HG22 . VAL   A 1 147 ? 23.019 -13.823 3.124   1.00 15.99 ?  147 VAL   A HG22 1 
ATOM   3082 H HG23 . VAL   A 1 147 ? 21.585 -14.052 2.479   1.00 15.99 ?  147 VAL   A HG23 1 
ATOM   3083 N N    . ARG   A 1 148 ? 23.138 -17.975 5.368   1.00 13.30 ?  148 ARG   A N    1 
ATOM   3084 C CA   . ARG   A 1 148 ? 23.007 -19.063 6.323   1.00 13.50 ?  148 ARG   A CA   1 
ATOM   3085 C C    . ARG   A 1 148 ? 23.138 -18.599 7.763   1.00 13.87 ?  148 ARG   A C    1 
ATOM   3086 O O    . ARG   A 1 148 ? 22.728 -19.327 8.676   1.00 15.64 ?  148 ARG   A O    1 
ATOM   3087 C CB   . ARG   A 1 148 ? 24.044 -20.159 6.031   1.00 14.05 ?  148 ARG   A CB   1 
ATOM   3088 C CG   . ARG   A 1 148 ? 23.869 -20.791 4.659   1.00 15.08 ?  148 ARG   A CG   1 
ATOM   3089 C CD   . ARG   A 1 148 ? 24.944 -21.828 4.356   1.00 16.13 ?  148 ARG   A CD   1 
ATOM   3090 N NE   . ARG   A 1 148 ? 26.281 -21.247 4.376   1.00 16.15 ?  148 ARG   A NE   1 
ATOM   3091 C CZ   . ARG   A 1 148 ? 26.787 -20.501 3.402   1.00 15.42 ?  148 ARG   A CZ   1 
ATOM   3092 N NH1  . ARG   A 1 148 ? 26.110 -20.263 2.289   1.00 15.86 ?  148 ARG   A NH1  1 
ATOM   3093 N NH2  . ARG   A 1 148 ? 28.006 -19.979 3.547   1.00 15.96 ?  148 ARG   A NH2  1 
ATOM   3094 H H    . ARG   A 1 148 ? 23.946 -17.669 5.302   1.00 15.95 ?  148 ARG   A H    1 
ATOM   3095 H HA   . ARG   A 1 148 ? 22.131 -19.454 6.219   1.00 16.20 ?  148 ARG   A HA   1 
ATOM   3096 H HB2  . ARG   A 1 148 ? 24.932 -19.780 6.073   1.00 16.87 ?  148 ARG   A HB2  1 
ATOM   3097 H HB3  . ARG   A 1 148 ? 23.949 -20.863 6.692   1.00 16.87 ?  148 ARG   A HB3  1 
ATOM   3098 H HG2  . ARG   A 1 148 ? 23.005 -21.226 4.618   1.00 18.10 ?  148 ARG   A HG2  1 
ATOM   3099 H HG3  . ARG   A 1 148 ? 23.925 -20.094 3.984   1.00 18.10 ?  148 ARG   A HG3  1 
ATOM   3100 H HD2  . ARG   A 1 148 ? 24.910 -22.528 5.027   1.00 19.36 ?  148 ARG   A HD2  1 
ATOM   3101 H HD3  . ARG   A 1 148 ? 24.786 -22.205 3.474   1.00 19.36 ?  148 ARG   A HD3  1 
ATOM   3102 H HE   . ARG   A 1 148 ? 26.771 -21.389 5.062   1.00 19.38 ?  148 ARG   A HE   1 
ATOM   3103 H HH11 . ARG   A 1 148 ? 25.323 -20.588 2.181   1.00 19.03 ?  148 ARG   A HH11 1 
ATOM   3104 H HH12 . ARG   A 1 148 ? 26.459 -19.774 1.669   1.00 19.03 ?  148 ARG   A HH12 1 
ATOM   3105 H HH21 . ARG   A 1 148 ? 28.452 -20.122 4.266   1.00 19.15 ?  148 ARG   A HH21 1 
ATOM   3106 H HH22 . ARG   A 1 148 ? 28.345 -19.491 2.922   1.00 19.15 ?  148 ARG   A HH22 1 
ATOM   3107 N N    . THR   A 1 149 ? 23.691 -17.408 7.977   1.00 13.84 ?  149 THR   A N    1 
ATOM   3108 C CA   . THR   A 1 149 ? 23.774 -16.815 9.297   1.00 14.00 ?  149 THR   A CA   1 
ATOM   3109 C C    . THR   A 1 149 ? 22.452 -16.119 9.613   1.00 13.60 ?  149 THR   A C    1 
ATOM   3110 O O    . THR   A 1 149 ? 21.514 -16.112 8.809   1.00 14.22 ?  149 THR   A O    1 
ATOM   3111 C CB   . THR   A 1 149 ? 24.974 -15.878 9.357   1.00 14.34 ?  149 THR   A CB   1 
ATOM   3112 O OG1  . THR   A 1 149 ? 24.846 -14.933 8.293   1.00 14.49 ?  149 THR   A OG1  1 
ATOM   3113 C CG2  . THR   A 1 149 ? 26.280 -16.666 9.218   1.00 14.88 ?  149 THR   A CG2  1 
ATOM   3114 H H    . THR   A 1 149 ? 24.039 -16.917 7.357   1.00 16.61 ?  149 THR   A H    1 
ATOM   3115 H HA   . THR   A 1 149 ? 23.906 -17.524 9.948   1.00 16.81 ?  149 THR   A HA   1 
ATOM   3116 H HB   . THR   A 1 149 ? 24.974 -15.417 10.208  1.00 17.21 ?  149 THR   A HB   1 
ATOM   3117 H HG1  . THR   A 1 149 ? 25.498 -14.402 8.304   1.00 17.38 ?  149 THR   A HG1  1 
ATOM   3118 H HG21 . THR   A 1 149 ? 27.037 -16.064 9.279   1.00 17.86 ?  149 THR   A HG21 1 
ATOM   3119 H HG22 . THR   A 1 149 ? 26.348 -17.330 9.923   1.00 17.86 ?  149 THR   A HG22 1 
ATOM   3120 H HG23 . THR   A 1 149 ? 26.308 -17.119 8.359   1.00 17.86 ?  149 THR   A HG23 1 
ATOM   3121 N N    . ASN   A 1 150 ? 22.340 -15.577 10.818  1.00 14.21 ?  150 ASN   A N    1 
ATOM   3122 C CA   . ASN   A 1 150 ? 21.061 -15.071 11.317  1.00 14.52 ?  150 ASN   A CA   1 
ATOM   3123 C C    . ASN   A 1 150 ? 20.878 -13.629 10.861  1.00 13.87 ?  150 ASN   A C    1 
ATOM   3124 O O    . ASN   A 1 150 ? 21.620 -12.734 11.287  1.00 15.09 ?  150 ASN   A O    1 
ATOM   3125 C CB   . ASN   A 1 150 ? 21.015 -15.187 12.836  1.00 17.21 ?  150 ASN   A CB   1 
ATOM   3126 C CG   . ASN   A 1 150 ? 20.861 -16.615 13.297  1.00 21.14 ?  150 ASN   A CG   1 
ATOM   3127 O OD1  . ASN   A 1 150 ? 20.263 -17.435 12.600  1.00 22.41 ?  150 ASN   A OD1  1 
ATOM   3128 N ND2  . ASN   A 1 150 ? 21.406 -16.928 14.467  1.00 23.59 ?  150 ASN   A ND2  1 
ATOM   3129 H H    . ASN   A 1 150 ? 22.993 -15.493 11.369  1.00 17.05 ?  150 ASN   A H    1 
ATOM   3130 H HA   . ASN   A 1 150 ? 20.340 -15.606 10.949  1.00 17.43 ?  150 ASN   A HA   1 
ATOM   3131 H HB2  . ASN   A 1 150 ? 21.841 -14.840 13.208  1.00 20.65 ?  150 ASN   A HB2  1 
ATOM   3132 H HB3  . ASN   A 1 150 ? 20.259 -14.683 13.172  1.00 20.65 ?  150 ASN   A HB3  1 
ATOM   3133 H HD21 . ASN   A 1 150 ? 21.345 -17.733 14.775  1.00 28.31 ?  150 ASN   A HD21 1 
ATOM   3134 H HD22 . ASN   A 1 150 ? 21.816 -16.329 14.929  1.00 28.31 ?  150 ASN   A HD22 1 
ATOM   3135 N N    . VAL   A 1 151 ? 19.892 -13.399 9.998   1.00 13.36 ?  151 VAL   A N    1 
ATOM   3136 C CA   . VAL   A 1 151 ? 19.673 -12.088 9.410   1.00 13.62 ?  151 VAL   A CA   1 
ATOM   3137 C C    . VAL   A 1 151 ? 18.296 -11.565 9.799   1.00 13.59 ?  151 VAL   A C    1 
ATOM   3138 O O    . VAL   A 1 151 ? 17.278 -12.265 9.655   1.00 14.94 ?  151 VAL   A O    1 
ATOM   3139 C CB   . VAL   A 1 151 ? 19.947 -12.065 7.893   1.00 14.87 ?  151 VAL   A CB   1 
ATOM   3140 C CG1  . VAL   A 1 151 ? 19.128 -13.090 7.146   1.00 15.78 ?  151 VAL   A CG1  1 
ATOM   3141 C CG2  . VAL   A 1 151 ? 19.732 -10.656 7.325   1.00 15.33 ?  151 VAL   A CG2  1 
ATOM   3142 H H    . VAL   A 1 151 ? 19.336 -14.000 9.732   1.00 16.03 ?  151 VAL   A H    1 
ATOM   3143 H HA   . VAL   A 1 151 ? 20.321 -11.482 9.802   1.00 16.34 ?  151 VAL   A HA   1 
ATOM   3144 H HB   . VAL   A 1 151 ? 20.882 -12.288 7.746   1.00 17.85 ?  151 VAL   A HB   1 
ATOM   3145 H HG11 . VAL   A 1 151 ? 19.267 -12.980 6.192   1.00 18.93 ?  151 VAL   A HG11 1 
ATOM   3146 H HG12 . VAL   A 1 151 ? 19.412 -13.980 7.418   1.00 18.93 ?  151 VAL   A HG12 1 
ATOM   3147 H HG13 . VAL   A 1 151 ? 18.190 -12.965 7.360   1.00 18.93 ?  151 VAL   A HG13 1 
ATOM   3148 H HG21 . VAL   A 1 151 ? 20.047 -10.636 6.405   1.00 18.40 ?  151 VAL   A HG21 1 
ATOM   3149 H HG22 . VAL   A 1 151 ? 18.787 -10.444 7.353   1.00 18.40 ?  151 VAL   A HG22 1 
ATOM   3150 H HG23 . VAL   A 1 151 ? 20.234 -10.022 7.858   1.00 18.40 ?  151 VAL   A HG23 1 
ATOM   3151 N N    A TYR   A 1 152 ? 18.266 -10.303 10.215  0.70 13.76 ?  152 TYR   A N    1 
ATOM   3152 N N    B TYR   A 1 152 ? 18.310 -10.369 10.395  0.30 12.54 ?  152 TYR   A N    1 
ATOM   3153 C CA   A TYR   A 1 152 ? 17.051 -9.587  10.573  0.70 13.42 ?  152 TYR   A CA   1 
ATOM   3154 C CA   B TYR   A 1 152 ? 17.141 -9.618  10.823  0.30 12.02 ?  152 TYR   A CA   1 
ATOM   3155 C C    A TYR   A 1 152 ? 16.835 -8.482  9.545   0.70 12.87 ?  152 TYR   A C    1 
ATOM   3156 C C    B TYR   A 1 152 ? 16.974 -8.486  9.823   0.30 11.03 ?  152 TYR   A C    1 
ATOM   3157 O O    A TYR   A 1 152 ? 17.562 -7.478  9.527   0.70 13.45 ?  152 TYR   A O    1 
ATOM   3158 O O    B TYR   A 1 152 ? 17.827 -7.594  9.735   0.30 11.10 ?  152 TYR   A O    1 
ATOM   3159 C CB   A TYR   A 1 152 ? 17.182 -9.067  12.000  0.70 13.66 ?  152 TYR   A CB   1 
ATOM   3160 C CB   B TYR   A 1 152 ? 17.368 -9.055  12.224  0.30 12.47 ?  152 TYR   A CB   1 
ATOM   3161 C CG   A TYR   A 1 152 ? 17.164 -10.217 12.984  0.70 13.78 ?  152 TYR   A CG   1 
ATOM   3162 C CG   B TYR   A 1 152 ? 17.330 -10.091 13.323  0.30 13.50 ?  152 TYR   A CG   1 
ATOM   3163 C CD1  A TYR   A 1 152 ? 18.300 -10.981 13.226  0.70 14.67 ?  152 TYR   A CD1  1 
ATOM   3164 C CD1  B TYR   A 1 152 ? 18.472 -10.788 13.690  0.30 14.04 ?  152 TYR   A CD1  1 
ATOM   3165 C CD2  A TYR   A 1 152 ? 15.996 -10.575 13.634  0.70 13.65 ?  152 TYR   A CD2  1 
ATOM   3166 C CD2  B TYR   A 1 152 ? 16.149 -10.369 14.000  0.30 13.99 ?  152 TYR   A CD2  1 
ATOM   3167 C CE1  A TYR   A 1 152 ? 18.279 -12.058 14.103  0.70 14.95 ?  152 TYR   A CE1  1 
ATOM   3168 C CE1  B TYR   A 1 152 ? 18.443 -11.734 14.696  0.30 15.17 ?  152 TYR   A CE1  1 
ATOM   3169 C CE2  A TYR   A 1 152 ? 15.962 -11.659 14.515  0.70 14.15 ?  152 TYR   A CE2  1 
ATOM   3170 C CE2  B TYR   A 1 152 ? 16.108 -11.315 15.008  0.30 15.12 ?  152 TYR   A CE2  1 
ATOM   3171 C CZ   A TYR   A 1 152 ? 17.108 -12.394 14.750  0.70 14.29 ?  152 TYR   A CZ   1 
ATOM   3172 C CZ   B TYR   A 1 152 ? 17.258 -11.994 15.350  0.30 15.81 ?  152 TYR   A CZ   1 
ATOM   3173 O OH   A TYR   A 1 152 ? 17.077 -13.473 15.619  0.70 15.44 ?  152 TYR   A OH   1 
ATOM   3174 O OH   B TYR   A 1 152 ? 17.228 -12.934 16.354  0.30 16.93 ?  152 TYR   A OH   1 
ATOM   3175 H H    A TYR   A 1 152 ? 18.978 -9.813  10.284  0.70 16.52 ?  152 TYR   A H    1 
ATOM   3176 H H    B TYR   A 1 152 ? 19.047 -9.944  10.557  0.30 15.05 ?  152 TYR   A H    1 
ATOM   3177 H HA   A TYR   A 1 152 ? 16.301 -10.202 10.534  0.70 16.10 ?  152 TYR   A HA   1 
ATOM   3178 H HA   B TYR   A 1 152 ? 16.356 -10.180 10.816  0.30 14.42 ?  152 TYR   A HA   1 
ATOM   3179 H HB2  A TYR   A 1 152 ? 18.020 -8.599  12.096  0.70 16.39 ?  152 TYR   A HB2  1 
ATOM   3180 H HB2  B TYR   A 1 152 ? 18.241 -8.631  12.253  0.30 14.97 ?  152 TYR   A HB2  1 
ATOM   3181 H HB3  A TYR   A 1 152 ? 16.436 -8.483  12.197  0.70 16.39 ?  152 TYR   A HB3  1 
ATOM   3182 H HB3  B TYR   A 1 152 ? 16.680 -8.402  12.411  0.30 14.97 ?  152 TYR   A HB3  1 
ATOM   3183 H HD1  A TYR   A 1 152 ? 19.092 -10.759 12.790  0.70 17.60 ?  152 TYR   A HD1  1 
ATOM   3184 H HD1  B TYR   A 1 152 ? 19.273 -10.616 13.248  0.30 16.85 ?  152 TYR   A HD1  1 
ATOM   3185 H HD2  A TYR   A 1 152 ? 15.215 -10.089 13.478  0.70 16.38 ?  152 TYR   A HD2  1 
ATOM   3186 H HD2  B TYR   A 1 152 ? 15.372 -9.912  13.770  0.30 16.79 ?  152 TYR   A HD2  1 
ATOM   3187 H HE1  A TYR   A 1 152 ? 19.056 -12.539 14.259  0.70 17.94 ?  152 TYR   A HE1  1 
ATOM   3188 H HE1  B TYR   A 1 152 ? 19.217 -12.196 14.927  0.30 18.20 ?  152 TYR   A HE1  1 
ATOM   3189 H HE2  A TYR   A 1 152 ? 15.170 -11.871 14.951  0.70 16.98 ?  152 TYR   A HE2  1 
ATOM   3190 H HE2  B TYR   A 1 152 ? 15.309 -11.492 15.452  0.30 18.14 ?  152 TYR   A HE2  1 
ATOM   3191 H HH   A TYR   A 1 152 ? 16.309 -13.534 15.948  0.70 18.53 ?  152 TYR   A HH   1 
ATOM   3192 H HH   B TYR   A 1 152 ? 16.450 -12.999 16.667  0.30 20.32 ?  152 TYR   A HH   1 
ATOM   3193 N N    A LEU   A 1 153 ? 15.852 -8.691  8.671   0.70 12.76 ?  153 LEU   A N    1 
ATOM   3194 N N    B LEU   A 1 153 ? 15.889 -8.531  9.066   0.30 10.78 ?  153 LEU   A N    1 
ATOM   3195 C CA   A LEU   A 1 153 ? 15.574 -7.790  7.562   0.70 12.81 ?  153 LEU   A CA   1 
ATOM   3196 C CA   B LEU   A 1 153 ? 15.635 -7.569  8.008   0.30 10.83 ?  153 LEU   A CA   1 
ATOM   3197 C C    A LEU   A 1 153 ? 14.571 -6.719  7.969   0.70 12.82 ?  153 LEU   A C    1 
ATOM   3198 C C    B LEU   A 1 153 ? 14.664 -6.509  8.503   0.30 10.77 ?  153 LEU   A C    1 
ATOM   3199 O O    A LEU   A 1 153 ? 13.472 -7.030  8.438   0.70 13.53 ?  153 LEU   A O    1 
ATOM   3200 O O    B LEU   A 1 153 ? 13.585 -6.832  9.013   0.30 10.95 ?  153 LEU   A O    1 
ATOM   3201 C CB   A LEU   A 1 153 ? 15.011 -8.576  6.378   0.70 12.58 ?  153 LEU   A CB   1 
ATOM   3202 C CB   B LEU   A 1 153 ? 15.044 -8.265  6.785   0.30 11.22 ?  153 LEU   A CB   1 
ATOM   3203 C CG   A LEU   A 1 153 ? 15.968 -9.566  5.716   0.70 12.68 ?  153 LEU   A CG   1 
ATOM   3204 C CG   B LEU   A 1 153 ? 15.924 -9.289  6.070   0.30 11.63 ?  153 LEU   A CG   1 
ATOM   3205 C CD1  A LEU   A 1 153 ? 15.202 -10.464 4.768   0.70 13.37 ?  153 LEU   A CD1  1 
ATOM   3206 C CD1  B LEU   A 1 153 ? 15.101 -10.002 5.010   0.30 11.98 ?  153 LEU   A CD1  1 
ATOM   3207 C CD2  A LEU   A 1 153 ? 17.055 -8.812  4.974   0.70 12.86 ?  153 LEU   A CD2  1 
ATOM   3208 C CD2  B LEU   A 1 153 ? 17.158 -8.632  5.460   0.30 12.16 ?  153 LEU   A CD2  1 
ATOM   3209 H H    A LEU   A 1 153 ? 15.319 -9.379  8.699   0.70 15.32 ?  153 LEU   A H    1 
ATOM   3210 H H    B LEU   A 1 153 ? 15.273 -9.119  9.150   0.30 12.93 ?  153 LEU   A H    1 
ATOM   3211 H HA   A LEU   A 1 153 ? 16.397 -7.365  7.285   0.70 15.37 ?  153 LEU   A HA   1 
ATOM   3212 H HA   B LEU   A 1 153 ? 16.467 -7.136  7.758   0.30 12.99 ?  153 LEU   A HA   1 
ATOM   3213 H HB2  A LEU   A 1 153 ? 14.237 -9.082  6.683   0.70 15.10 ?  153 LEU   A HB2  1 
ATOM   3214 H HB2  B LEU   A 1 153 ? 14.240 -8.724  7.067   0.30 13.47 ?  153 LEU   A HB2  1 
ATOM   3215 H HB3  A LEU   A 1 153 ? 14.729 -7.946  5.696   0.70 15.10 ?  153 LEU   A HB3  1 
ATOM   3216 H HB3  B LEU   A 1 153 ? 14.814 -7.581  6.137   0.30 13.47 ?  153 LEU   A HB3  1 
ATOM   3217 H HG   A LEU   A 1 153 ? 16.386 -10.118 6.398   0.70 15.22 ?  153 LEU   A HG   1 
ATOM   3218 H HG   B LEU   A 1 153 ? 16.223 -9.950  6.713   0.30 13.96 ?  153 LEU   A HG   1 
ATOM   3219 H HD11 A LEU   A 1 153 ? 15.774 -11.204 4.510   0.70 16.05 ?  153 LEU   A HD11 1 
ATOM   3220 H HD11 B LEU   A 1 153 ? 15.663 -10.646 4.555   0.30 14.38 ?  153 LEU   A HD11 1 
ATOM   3221 H HD12 A LEU   A 1 153 ? 14.414 -10.795 5.219   0.70 16.05 ?  153 LEU   A HD12 1 
ATOM   3222 H HD12 B LEU   A 1 153 ? 14.357 -10.452 5.439   0.30 14.38 ?  153 LEU   A HD12 1 
ATOM   3223 H HD13 A LEU   A 1 153 ? 14.951 -9.949  3.988   0.70 16.05 ?  153 LEU   A HD13 1 
ATOM   3224 H HD13 B LEU   A 1 153 ? 14.768 -9.345  4.376   0.30 14.38 ?  153 LEU   A HD13 1 
ATOM   3225 H HD21 A LEU   A 1 153 ? 17.633 -9.449  4.534   0.70 15.43 ?  153 LEU   A HD21 1 
ATOM   3226 H HD21 B LEU   A 1 153 ? 17.664 -9.303  4.974   0.30 14.59 ?  153 LEU   A HD21 1 
ATOM   3227 H HD22 A LEU   A 1 153 ? 16.637 -8.231  4.321   0.70 15.43 ?  153 LEU   A HD22 1 
ATOM   3228 H HD22 B LEU   A 1 153 ? 16.876 -7.928  4.856   0.30 14.59 ?  153 LEU   A HD22 1 
ATOM   3229 H HD23 A LEU   A 1 153 ? 17.562 -8.286  5.611   0.70 15.43 ?  153 LEU   A HD23 1 
ATOM   3230 H HD23 B LEU   A 1 153 ? 17.703 -8.259  6.171   0.30 14.59 ?  153 LEU   A HD23 1 
ATOM   3231 N N    A ALA   A 1 154 ? 14.940 -5.460  7.755   0.70 12.24 ?  154 ALA   A N    1 
ATOM   3232 N N    B ALA   A 1 154 ? 15.051 -5.248  8.348   0.30 10.63 ?  154 ALA   A N    1 
ATOM   3233 C CA   A ALA   A 1 154 ? 14.071 -4.319  8.013   0.70 13.18 ?  154 ALA   A CA   1 
ATOM   3234 C CA   B ALA   A 1 154 ? 14.183 -4.112  8.617   0.30 11.09 ?  154 ALA   A CA   1 
ATOM   3235 C C    A ALA   A 1 154 ? 13.580 -3.777  6.677   0.70 13.11 ?  154 ALA   A C    1 
ATOM   3236 C C    B ALA   A 1 154 ? 13.751 -3.538  7.275   0.30 11.48 ?  154 ALA   A C    1 
ATOM   3237 O O    A ALA   A 1 154 ? 14.390 -3.396  5.822   0.70 13.67 ?  154 ALA   A O    1 
ATOM   3238 O O    B ALA   A 1 154 ? 14.597 -3.164  6.455   0.30 11.37 ?  154 ALA   A O    1 
ATOM   3239 C CB   A ALA   A 1 154 ? 14.821 -3.232  8.780   0.70 13.89 ?  154 ALA   A CB   1 
ATOM   3240 C CB   B ALA   A 1 154 ? 14.915 -3.055  9.444   0.30 11.33 ?  154 ALA   A CB   1 
ATOM   3241 H H    A ALA   A 1 154 ? 15.714 -5.243  7.444   0.70 14.69 ?  154 ALA   A H    1 
ATOM   3242 H H    B ALA   A 1 154 ? 15.839 -5.017  8.081   0.30 12.76 ?  154 ALA   A H    1 
ATOM   3243 H HA   A ALA   A 1 154 ? 13.307 -4.612  8.544   0.70 15.81 ?  154 ALA   A HA   1 
ATOM   3244 H HA   B ALA   A 1 154 ? 13.398 -4.402  9.107   0.30 13.31 ?  154 ALA   A HA   1 
ATOM   3245 H HB1  A ALA   A 1 154 ? 14.216 -2.495  8.938   0.70 16.66 ?  154 ALA   A HB1  1 
ATOM   3246 H HB1  B ALA   A 1 154 ? 14.302 -2.334  9.655   0.30 13.59 ?  154 ALA   A HB1  1 
ATOM   3247 H HB2  A ALA   A 1 154 ? 15.133 -3.597  9.623   0.70 16.66 ?  154 ALA   A HB2  1 
ATOM   3248 H HB2  B ALA   A 1 154 ? 15.239 -3.465  10.264  0.30 13.59 ?  154 ALA   A HB2  1 
ATOM   3249 H HB3  A ALA   A 1 154 ? 15.574 -2.942  8.244   0.70 16.66 ?  154 ALA   A HB3  1 
ATOM   3250 H HB3  B ALA   A 1 154 ? 15.665 -2.715  8.931   0.30 13.59 ?  154 ALA   A HB3  1 
ATOM   3251 N N    A VAL   A 1 155 ? 12.260 -3.747  6.505   0.70 13.89 ?  155 VAL   A N    1 
ATOM   3252 N N    B VAL   A 1 155 ? 12.441 -3.480  7.048   0.30 12.22 ?  155 VAL   A N    1 
ATOM   3253 C CA   A VAL   A 1 155 ? 11.608 -3.264  5.291   0.70 15.23 ?  155 VAL   A CA   1 
ATOM   3254 C CA   B VAL   A 1 155 ? 11.873 -2.964  5.808   0.30 13.15 ?  155 VAL   A CA   1 
ATOM   3255 C C    A VAL   A 1 155 ? 10.836 -2.000  5.653   0.70 16.93 ?  155 VAL   A C    1 
ATOM   3256 C C    B VAL   A 1 155 ? 11.035 -1.744  6.154   0.30 15.05 ?  155 VAL   A C    1 
ATOM   3257 O O    A VAL   A 1 155 ? 9.855  -2.059  6.404   0.70 17.41 ?  155 VAL   A O    1 
ATOM   3258 O O    B VAL   A 1 155 ? 10.050 -1.849  6.896   0.30 15.08 ?  155 VAL   A O    1 
ATOM   3259 C CB   A VAL   A 1 155 ? 10.679 -4.329  4.688   0.70 15.43 ?  155 VAL   A CB   1 
ATOM   3260 C CB   B VAL   A 1 155 ? 11.046 -4.024  5.064   0.30 13.01 ?  155 VAL   A CB   1 
ATOM   3261 C CG1  A VAL   A 1 155 ? 9.944  -3.777  3.477   0.70 16.31 ?  155 VAL   A CG1  1 
ATOM   3262 C CG1  B VAL   A 1 155 ? 10.386 -3.412  3.838   0.30 12.99 ?  155 VAL   A CG1  1 
ATOM   3263 C CG2  A VAL   A 1 155 ? 11.462 -5.581  4.303   0.70 16.10 ?  155 VAL   A CG2  1 
ATOM   3264 C CG2  B VAL   A 1 155 ? 11.939 -5.188  4.660   0.30 12.77 ?  155 VAL   A CG2  1 
ATOM   3265 H H    A VAL   A 1 155 ? 11.701 -4.038  7.101   0.70 16.66 ?  155 VAL   A H    1 
ATOM   3266 H H    B VAL   A 1 155 ? 11.850 -3.736  7.619   0.30 14.66 ?  155 VAL   A H    1 
ATOM   3267 H HA   A VAL   A 1 155 ? 12.284 -3.047  4.634   0.70 18.28 ?  155 VAL   A HA   1 
ATOM   3268 H HA   B VAL   A 1 155 ? 12.589 -2.679  5.223   0.30 15.78 ?  155 VAL   A HA   1 
ATOM   3269 H HB   A VAL   A 1 155 ? 10.016 -4.591  5.351   0.70 18.52 ?  155 VAL   A HB   1 
ATOM   3270 H HB   B VAL   A 1 155 ? 10.352 -4.361  5.652   0.30 15.61 ?  155 VAL   A HB   1 
ATOM   3271 H HG11 A VAL   A 1 155 ? 9.528  -4.510  2.996   0.70 19.57 ?  155 VAL   A HG11 1 
ATOM   3272 H HG11 B VAL   A 1 155 ? 10.045 -4.126  3.279   0.30 15.59 ?  155 VAL   A HG11 1 
ATOM   3273 H HG12 A VAL   A 1 155 ? 9.264  -3.153  3.776   0.70 19.57 ?  155 VAL   A HG12 1 
ATOM   3274 H HG12 B VAL   A 1 155 ? 9.660  -2.837  4.121   0.30 15.59 ?  155 VAL   A HG12 1 
ATOM   3275 H HG13 A VAL   A 1 155 ? 10.581 -3.325  2.903   0.70 19.57 ?  155 VAL   A HG13 1 
ATOM   3276 H HG13 B VAL   A 1 155 ? 11.047 -2.898  3.348   0.30 15.59 ?  155 VAL   A HG13 1 
ATOM   3277 H HG21 A VAL   A 1 155 ? 10.856 -6.221  3.891   0.70 19.32 ?  155 VAL   A HG21 1 
ATOM   3278 H HG21 B VAL   A 1 155 ? 11.408 -5.839  4.177   0.30 15.32 ?  155 VAL   A HG21 1 
ATOM   3279 H HG22 A VAL   A 1 155 ? 12.158 -5.336  3.674   0.70 19.32 ?  155 VAL   A HG22 1 
ATOM   3280 H HG22 B VAL   A 1 155 ? 12.654 -4.856  4.094   0.30 15.32 ?  155 VAL   A HG22 1 
ATOM   3281 H HG23 A VAL   A 1 155 ? 11.856 -5.969  5.100   0.70 19.32 ?  155 VAL   A HG23 1 
ATOM   3282 H HG23 B VAL   A 1 155 ? 12.312 -5.593  5.460   0.30 15.32 ?  155 VAL   A HG23 1 
ATOM   3283 N N    A PHE   A 1 156 ? 11.257 -0.862  5.090   0.70 18.63 ?  156 PHE   A N    1 
ATOM   3284 N N    B PHE   A 1 156 ? 11.432 -0.591  5.624   0.30 16.58 ?  156 PHE   A N    1 
ATOM   3285 C CA   A PHE   A 1 156 ? 10.724 0.435   5.509   0.70 20.37 ?  156 PHE   A CA   1 
ATOM   3286 C CA   B PHE   A 1 156 ? 10.786 0.681   5.942   0.30 18.82 ?  156 PHE   A CA   1 
ATOM   3287 C C    A PHE   A 1 156 ? 9.268  0.612   5.096   0.70 20.66 ?  156 PHE   A C    1 
ATOM   3288 C C    B PHE   A 1 156 ? 9.739  1.038   4.888   0.30 20.34 ?  156 PHE   A C    1 
ATOM   3289 O O    A PHE   A 1 156 ? 8.449  1.131   5.869   0.70 21.87 ?  156 PHE   A O    1 
ATOM   3290 O O    B PHE   A 1 156 ? 9.757  2.109   4.281   0.30 20.85 ?  156 PHE   A O    1 
ATOM   3291 C CB   A PHE   A 1 156 ? 11.596 1.545   4.916   0.70 21.64 ?  156 PHE   A CB   1 
ATOM   3292 C CB   B PHE   A 1 156 ? 11.838 1.778   6.070   0.30 19.58 ?  156 PHE   A CB   1 
ATOM   3293 C CG   A PHE   A 1 156 ? 11.108 2.938   5.214   0.70 23.29 ?  156 PHE   A CG   1 
ATOM   3294 C CG   B PHE   A 1 156 ? 11.326 3.051   6.675   0.30 20.30 ?  156 PHE   A CG   1 
ATOM   3295 C CD1  A PHE   A 1 156 ? 11.058 3.397   6.520   0.70 24.17 ?  156 PHE   A CD1  1 
ATOM   3296 C CD1  B PHE   A 1 156 ? 10.190 3.059   7.469   0.30 20.69 ?  156 PHE   A CD1  1 
ATOM   3297 C CD2  A PHE   A 1 156 ? 10.724 3.791   4.188   0.70 24.18 ?  156 PHE   A CD2  1 
ATOM   3298 C CD2  B PHE   A 1 156 ? 11.984 4.245   6.445   0.30 20.61 ?  156 PHE   A CD2  1 
ATOM   3299 C CE1  A PHE   A 1 156 ? 10.618 4.677   6.800   0.70 25.09 ?  156 PHE   A CE1  1 
ATOM   3300 C CE1  B PHE   A 1 156 ? 9.725  4.230   8.022   0.30 20.82 ?  156 PHE   A CE1  1 
ATOM   3301 C CE2  A PHE   A 1 156 ? 10.283 5.072   4.462   0.70 25.27 ?  156 PHE   A CE2  1 
ATOM   3302 C CE2  B PHE   A 1 156 ? 11.523 5.421   6.994   0.30 20.80 ?  156 PHE   A CE2  1 
ATOM   3303 C CZ   A PHE   A 1 156 ? 10.235 5.519   5.769   0.70 25.52 ?  156 PHE   A CZ   1 
ATOM   3304 C CZ   B PHE   A 1 156 ? 10.392 5.413   7.784   0.30 20.88 ?  156 PHE   A CZ   1 
ATOM   3305 H H    A PHE   A 1 156 ? 11.840 -0.838  4.459   0.70 22.36 ?  156 PHE   A H    1 
ATOM   3306 H H    B PHE   A 1 156 ? 12.093 -0.514  5.080   0.30 19.90 ?  156 PHE   A H    1 
ATOM   3307 H HA   A PHE   A 1 156 ? 10.777 0.484   6.473   0.70 24.45 ?  156 PHE   A HA   1 
ATOM   3308 H HA   B PHE   A 1 156 ? 10.334 0.579   6.789   0.30 22.59 ?  156 PHE   A HA   1 
ATOM   3309 H HB2  A PHE   A 1 156 ? 12.495 1.454   5.277   0.70 25.97 ?  156 PHE   A HB2  1 
ATOM   3310 H HB2  B PHE   A 1 156 ? 12.559 1.450   6.626   0.30 23.50 ?  156 PHE   A HB2  1 
ATOM   3311 H HB3  A PHE   A 1 156 ? 11.623 1.432   3.952   0.70 25.97 ?  156 PHE   A HB3  1 
ATOM   3312 H HB3  B PHE   A 1 156 ? 12.180 1.990   5.187   0.30 23.50 ?  156 PHE   A HB3  1 
ATOM   3313 H HD1  A PHE   A 1 156 ? 11.317 2.832   7.217   0.70 29.00 ?  156 PHE   A HD1  1 
ATOM   3314 H HD1  B PHE   A 1 156 ? 9.738  2.261   7.633   0.30 24.82 ?  156 PHE   A HD1  1 
ATOM   3315 H HD2  A PHE   A 1 156 ? 10.757 3.486   3.308   0.70 29.02 ?  156 PHE   A HD2  1 
ATOM   3316 H HD2  B PHE   A 1 156 ? 12.748 4.255   5.913   0.30 24.73 ?  156 PHE   A HD2  1 
ATOM   3317 H HE1  A PHE   A 1 156 ? 10.586 4.975   7.681   0.70 30.10 ?  156 PHE   A HE1  1 
ATOM   3318 H HE1  B PHE   A 1 156 ? 8.962  4.220   8.553   0.30 24.98 ?  156 PHE   A HE1  1 
ATOM   3319 H HE2  A PHE   A 1 156 ? 10.026 5.631   3.768   0.70 30.32 ?  156 PHE   A HE2  1 
ATOM   3320 H HE2  B PHE   A 1 156 ? 11.973 6.218   6.832   0.30 24.96 ?  156 PHE   A HE2  1 
ATOM   3321 H HZ   A PHE   A 1 156 ? 9.938  6.379   5.957   0.70 30.62 ?  156 PHE   A HZ   1 
ATOM   3322 H HZ   B PHE   A 1 156 ? 10.079 6.205   8.154   0.30 25.06 ?  156 PHE   A HZ   1 
ATOM   3323 N N    A ASP   A 1 157 ? 8.936  0.207   3.877   0.70 21.27 ?  157 ASP   A N    1 
ATOM   3324 N N    B ASP   A 1 157 ? 8.807  0.114   4.679   0.30 20.84 ?  157 ASP   A N    1 
ATOM   3325 C CA   A ASP   A 1 157 ? 7.612  0.442   3.320   0.70 22.77 ?  157 ASP   A CA   1 
ATOM   3326 C CA   B ASP   A 1 157 ? 7.698  0.361   3.762   0.30 21.55 ?  157 ASP   A CA   1 
ATOM   3327 C C    A ASP   A 1 157 ? 6.646  -0.612  3.846   0.70 23.04 ?  157 ASP   A C    1 
ATOM   3328 C C    B ASP   A 1 157 ? 6.588  -0.621  4.106   0.30 22.35 ?  157 ASP   A C    1 
ATOM   3329 O O    A ASP   A 1 157 ? 6.849  -1.810  3.617   0.70 22.32 ?  157 ASP   A O    1 
ATOM   3330 O O    B ASP   A 1 157 ? 6.744  -1.830  3.907   0.30 22.57 ?  157 ASP   A O    1 
ATOM   3331 C CB   A ASP   A 1 157 ? 7.698  0.364   1.802   0.70 24.39 ?  157 ASP   A CB   1 
ATOM   3332 C CB   B ASP   A 1 157 ? 8.143  0.215   2.314   0.30 21.30 ?  157 ASP   A CB   1 
ATOM   3333 C CG   A ASP   A 1 157 ? 6.457  0.876   1.129   0.70 25.85 ?  157 ASP   A CG   1 
ATOM   3334 C CG   B ASP   A 1 157 ? 7.071  0.684   1.329   0.30 20.99 ?  157 ASP   A CG   1 
ATOM   3335 O OD1  A ASP   A 1 157 ? 6.269  2.104   1.112   0.70 27.30 ?  157 ASP   A OD1  1 
ATOM   3336 O OD1  B ASP   A 1 157 ? 5.917  0.219   1.440   0.30 20.43 ?  157 ASP   A OD1  1 
ATOM   3337 O OD2  A ASP   A 1 157 ? 5.663  0.052   0.626   0.70 26.30 -1 157 ASP   A OD2  1 
ATOM   3338 O OD2  B ASP   A 1 157 ? 7.367  1.539   0.466   0.30 21.47 -1 157 ASP   A OD2  1 
ATOM   3339 H H    A ASP   A 1 157 ? 9.467  -0.209  3.341   0.70 25.52 ?  157 ASP   A H    1 
ATOM   3340 H H    B ASP   A 1 157 ? 8.790  -0.655  5.060   0.30 25.01 ?  157 ASP   A H    1 
ATOM   3341 H HA   A ASP   A 1 157 ? 7.290  1.319   3.579   0.70 27.33 ?  157 ASP   A HA   1 
ATOM   3342 H HA   B ASP   A 1 157 ? 7.363  1.261   3.885   0.30 25.86 ?  157 ASP   A HA   1 
ATOM   3343 H HB2  A ASP   A 1 157 ? 8.461  0.885   1.503   0.70 29.27 ?  157 ASP   A HB2  1 
ATOM   3344 H HB2  B ASP   A 1 157 ? 8.940  0.745   2.181   0.30 25.56 ?  157 ASP   A HB2  1 
ATOM   3345 H HB3  A ASP   A 1 157 ? 7.800  -0.558  1.534   0.70 29.27 ?  157 ASP   A HB3  1 
ATOM   3346 H HB3  B ASP   A 1 157 ? 8.361  -0.716  2.146   0.30 25.56 ?  157 ASP   A HB3  1 
ATOM   3347 N N    A LYS   A 1 158 ? 5.598  -0.170  4.552   0.70 24.29 ?  158 LYS   A N    1 
ATOM   3348 N N    B LYS   A 1 158 ? 5.478  -0.095  4.626   0.30 22.84 ?  158 LYS   A N    1 
ATOM   3349 C CA   A LYS   A 1 158 ? 4.652  -1.115  5.142   0.70 25.01 ?  158 LYS   A CA   1 
ATOM   3350 C CA   B LYS   A 1 158 ? 4.353  -0.938  5.013   0.30 23.07 ?  158 LYS   A CA   1 
ATOM   3351 C C    A LYS   A 1 158 ? 3.928  -1.912  4.064   0.70 24.69 ?  158 LYS   A C    1 
ATOM   3352 C C    B LYS   A 1 158 ? 3.852  -1.754  3.829   0.30 22.89 ?  158 LYS   A C    1 
ATOM   3353 O O    A LYS   A 1 158 ? 3.724  -3.123  4.205   0.70 24.76 ?  158 LYS   A O    1 
ATOM   3354 O O    B LYS   A 1 158 ? 3.697  -2.977  3.921   0.30 22.92 ?  158 LYS   A O    1 
ATOM   3355 C CB   A LYS   A 1 158 ? 3.661  -0.369  6.043   0.70 26.19 ?  158 LYS   A CB   1 
ATOM   3356 C CB   B LYS   A 1 158 ? 3.236  -0.054  5.568   0.30 23.59 ?  158 LYS   A CB   1 
ATOM   3357 C CG   A LYS   A 1 158 ? 2.445  -1.187  6.490   0.70 27.71 ?  158 LYS   A CG   1 
ATOM   3358 C CG   B LYS   A 1 158 ? 1.945  -0.783  5.895   0.30 23.96 ?  158 LYS   A CG   1 
ATOM   3359 C CD   A LYS   A 1 158 ? 2.824  -2.415  7.315   0.70 28.97 ?  158 LYS   A CD   1 
ATOM   3360 C CD   B LYS   A 1 158 ? 0.841  0.205   6.226   0.30 24.23 ?  158 LYS   A CD   1 
ATOM   3361 C CE   A LYS   A 1 158 ? 1.574  -3.142  7.814   0.70 29.88 ?  158 LYS   A CE   1 
ATOM   3362 C CE   B LYS   A 1 158 ? -0.298 -0.461  6.977   0.30 24.40 ?  158 LYS   A CE   1 
ATOM   3363 N NZ   A LYS   A 1 158 ? 1.879  -4.463  8.435   0.70 30.28 ?  158 LYS   A NZ   1 
ATOM   3364 N NZ   B LYS   A 1 158 ? -0.872 -1.612  6.230   0.30 24.52 ?  158 LYS   A NZ   1 
ATOM   3365 H H    A LYS   A 1 158 ? 5.420  0.655   4.701   0.70 29.14 ?  158 LYS   A H    1 
ATOM   3366 H H    B LYS   A 1 158 ? 5.356  0.741   4.759   0.30 27.40 ?  158 LYS   A H    1 
ATOM   3367 H HA   A LYS   A 1 158 ? 5.139  -1.740  5.704   0.70 30.01 ?  158 LYS   A HA   1 
ATOM   3368 H HA   B LYS   A 1 158 ? 4.631  -1.551  5.711   0.30 27.68 ?  158 LYS   A HA   1 
ATOM   3369 H HB2  A LYS   A 1 158 ? 4.126  -0.079  6.848   0.70 31.42 ?  158 LYS   A HB2  1 
ATOM   3370 H HB2  B LYS   A 1 158 ? 3.550  0.363   6.388   0.30 28.31 ?  158 LYS   A HB2  1 
ATOM   3371 H HB3  A LYS   A 1 158 ? 3.331  0.409   5.566   0.70 31.42 ?  158 LYS   A HB3  1 
ATOM   3372 H HB3  B LYS   A 1 158 ? 3.029  0.632   4.915   0.30 28.31 ?  158 LYS   A HB3  1 
ATOM   3373 H HG2  A LYS   A 1 158 ? 1.878  -0.625  7.041   0.70 33.25 ?  158 LYS   A HG2  1 
ATOM   3374 H HG2  B LYS   A 1 158 ? 1.658  -1.306  5.129   0.30 28.75 ?  158 LYS   A HG2  1 
ATOM   3375 H HG3  A LYS   A 1 158 ? 1.949  -1.484  5.711   0.70 33.25 ?  158 LYS   A HG3  1 
ATOM   3376 H HG3  B LYS   A 1 158 ? 2.086  -1.358  6.663   0.30 28.75 ?  158 LYS   A HG3  1 
ATOM   3377 H HD2  A LYS   A 1 158 ? 3.337  -3.026  6.765   0.70 34.76 ?  158 LYS   A HD2  1 
ATOM   3378 H HD2  B LYS   A 1 158 ? 1.201  0.912   6.784   0.30 29.07 ?  158 LYS   A HD2  1 
ATOM   3379 H HD3  A LYS   A 1 158 ? 3.345  -2.135  8.085   0.70 34.76 ?  158 LYS   A HD3  1 
ATOM   3380 H HD3  B LYS   A 1 158 ? 0.486  0.577   5.402   0.30 29.07 ?  158 LYS   A HD3  1 
ATOM   3381 H HE2  A LYS   A 1 158 ? 1.135  -2.592  8.481   0.70 35.85 ?  158 LYS   A HE2  1 
ATOM   3382 H HE2  B LYS   A 1 158 ? 0.032  -0.787  7.828   0.30 29.28 ?  158 LYS   A HE2  1 
ATOM   3383 H HE3  A LYS   A 1 158 ? 0.979  -3.293  7.064   0.70 35.85 ?  158 LYS   A HE3  1 
ATOM   3384 H HE3  B LYS   A 1 158 ? -1.005 0.188   7.120   0.30 29.28 ?  158 LYS   A HE3  1 
ATOM   3385 H HZ1  A LYS   A 1 158 ? 1.127  -4.851  8.709   0.70 36.34 ?  158 LYS   A HZ1  1 
ATOM   3386 H HZ1  B LYS   A 1 158 ? -1.547 -1.966  6.690   0.30 29.42 ?  158 LYS   A HZ1  1 
ATOM   3387 H HZ2  A LYS   A 1 158 ? 2.277  -4.994  7.840   0.70 36.34 ?  158 LYS   A HZ2  1 
ATOM   3388 H HZ2  B LYS   A 1 158 ? -1.173 -1.341  5.437   0.30 29.42 ?  158 LYS   A HZ2  1 
ATOM   3389 H HZ3  A LYS   A 1 158 ? 2.421  -4.355  9.132   0.70 36.34 ?  158 LYS   A HZ3  1 
ATOM   3390 H HZ3  B LYS   A 1 158 ? -0.249 -2.235  6.105   0.30 29.42 ?  158 LYS   A HZ3  1 
ATOM   3391 N N    A ASN   A 1 159 ? 3.531  -1.251  2.976   0.70 25.17 ?  159 ASN   A N    1 
ATOM   3392 N N    B ASN   A 1 159 ? 3.586  -1.088  2.703   0.30 22.82 ?  159 ASN   A N    1 
ATOM   3393 C CA   A ASN   A 1 159 ? 2.839  -1.957  1.904   0.70 25.03 ?  159 ASN   A CA   1 
ATOM   3394 C CA   B ASN   A 1 159 ? 3.081  -1.801  1.536   0.30 22.54 ?  159 ASN   A CA   1 
ATOM   3395 C C    A ASN   A 1 159 ? 3.726  -3.044  1.292   0.70 23.39 ?  159 ASN   A C    1 
ATOM   3396 C C    B ASN   A 1 159 ? 4.094  -2.815  1.032   0.30 21.31 ?  159 ASN   A C    1 
ATOM   3397 O O    A ASN   A 1 159 ? 3.273  -4.169  1.052   0.70 23.14 ?  159 ASN   A O    1 
ATOM   3398 O O    B ASN   A 1 159 ? 3.717  -3.901  0.578   0.30 21.11 ?  159 ASN   A O    1 
ATOM   3399 C CB   A ASN   A 1 159 ? 2.348  -0.950  0.860   0.70 26.81 ?  159 ASN   A CB   1 
ATOM   3400 C CB   B ASN   A 1 159 ? 2.708  -0.813  0.433   0.30 23.55 ?  159 ASN   A CB   1 
ATOM   3401 C CG   A ASN   A 1 159 ? 1.151  -0.142  1.348   0.70 28.85 ?  159 ASN   A CG   1 
ATOM   3402 C CG   B ASN   A 1 159 ? 1.595  0.122   0.849   0.30 24.59 ?  159 ASN   A CG   1 
ATOM   3403 O OD1  A ASN   A 1 159 ? 0.287  -0.667  2.049   0.70 29.74 ?  159 ASN   A OD1  1 
ATOM   3404 O OD1  B ASN   A 1 159 ? 1.590  1.302   0.493   0.30 25.10 ?  159 ASN   A OD1  1 
ATOM   3405 N ND2  A ASN   A 1 159 ? 1.095  1.135   0.981   0.70 29.74 ?  159 ASN   A ND2  1 
ATOM   3406 N ND2  B ASN   A 1 159 ? 0.644  -0.400  1.619   0.30 25.16 ?  159 ASN   A ND2  1 
ATOM   3407 H H    A ASN   A 1 159 ? 3.664  -0.416  2.839   0.70 30.20 ?  159 ASN   A H    1 
ATOM   3408 H H    B ASN   A 1 159 ? 3.692  -0.245  2.593   0.30 27.38 ?  159 ASN   A H    1 
ATOM   3409 H HA   A ASN   A 1 159 ? 2.059  -2.392  2.280   0.70 30.04 ?  159 ASN   A HA   1 
ATOM   3410 H HA   B ASN   A 1 159 ? 2.288  -2.299  1.786   0.30 27.05 ?  159 ASN   A HA   1 
ATOM   3411 H HB2  A ASN   A 1 159 ? 3.060  -0.325  0.658   0.70 32.18 ?  159 ASN   A HB2  1 
ATOM   3412 H HB2  B ASN   A 1 159 ? 3.484  -0.277  0.212   0.30 28.26 ?  159 ASN   A HB2  1 
ATOM   3413 H HB3  A ASN   A 1 159 ? 2.080  -1.426  0.062   0.70 32.18 ?  159 ASN   A HB3  1 
ATOM   3414 H HB3  B ASN   A 1 159 ? 2.411  -1.309  -0.348  0.30 28.26 ?  159 ASN   A HB3  1 
ATOM   3415 H HD21 A ASN   A 1 159 ? 0.439  1.627   1.237   0.70 35.68 ?  159 ASN   A HD21 1 
ATOM   3416 H HD21 B ASN   A 1 159 ? -0.005 0.090   1.882   0.30 30.20 ?  159 ASN   A HD21 1 
ATOM   3417 H HD22 A ASN   A 1 159 ? 1.722  1.467   0.497   0.70 35.68 ?  159 ASN   A HD22 1 
ATOM   3418 H HD22 B ASN   A 1 159 ? 0.677  -1.229  1.855   0.30 30.20 ?  159 ASN   A HD22 1 
ATOM   3419 N N    A LEU   A 1 160 ? 5.005  -2.743  1.068   0.70 22.15 ?  160 LEU   A N    1 
ATOM   3420 N N    B LEU   A 1 160 ? 5.383  -2.482  1.099   0.30 20.00 ?  160 LEU   A N    1 
ATOM   3421 C CA   A LEU   A 1 160 ? 5.907  -3.740  0.494   0.70 20.97 ?  160 LEU   A CA   1 
ATOM   3422 C CA   B LEU   A 1 160 ? 6.401  -3.460  0.733   0.30 18.33 ?  160 LEU   A CA   1 
ATOM   3423 C C    A LEU   A 1 160 ? 6.113  -4.914  1.443   0.70 20.12 ?  160 LEU   A C    1 
ATOM   3424 C C    B LEU   A 1 160 ? 6.471  -4.584  1.761   0.30 17.29 ?  160 LEU   A C    1 
ATOM   3425 O O    A LEU   A 1 160 ? 6.166  -6.072  1.011   0.70 20.79 ?  160 LEU   A O    1 
ATOM   3426 O O    B LEU   A 1 160 ? 6.481  -5.766  1.399   0.30 17.46 ?  160 LEU   A O    1 
ATOM   3427 C CB   A LEU   A 1 160 ? 7.249  -3.095  0.162   0.70 20.63 ?  160 LEU   A CB   1 
ATOM   3428 C CB   B LEU   A 1 160 ? 7.763  -2.787  0.566   0.30 18.27 ?  160 LEU   A CB   1 
ATOM   3429 C CG   A LEU   A 1 160 ? 8.335  -4.075  -0.276  0.70 20.90 ?  160 LEU   A CG   1 
ATOM   3430 C CG   B LEU   A 1 160 ? 8.912  -3.725  0.191   0.30 18.34 ?  160 LEU   A CG   1 
ATOM   3431 C CD1  A LEU   A 1 160 ? 7.871  -4.822  -1.505  0.70 21.57 ?  160 LEU   A CD1  1 
ATOM   3432 C CD1  B LEU   A 1 160 ? 8.593  -4.498  -1.080  0.30 18.30 ?  160 LEU   A CD1  1 
ATOM   3433 C CD2  A LEU   A 1 160 ? 9.651  -3.357  -0.541  0.70 20.82 ?  160 LEU   A CD2  1 
ATOM   3434 C CD2  B LEU   A 1 160 ? 10.214 -2.954  0.042   0.30 18.38 ?  160 LEU   A CD2  1 
ATOM   3435 H H    A LEU   A 1 160 ? 5.372  -1.988  1.252   0.70 26.57 ?  160 LEU   A H    1 
ATOM   3436 H H    B LEU   A 1 160 ? 5.684  -1.713  1.341   0.30 23.99 ?  160 LEU   A H    1 
ATOM   3437 H HA   A LEU   A 1 160 ? 5.514  -4.073  -0.328  0.70 25.17 ?  160 LEU   A HA   1 
ATOM   3438 H HA   B LEU   A 1 160 ? 6.160  -3.850  -0.118  0.30 22.00 ?  160 LEU   A HA   1 
ATOM   3439 H HB2  A LEU   A 1 160 ? 7.118  -2.456  -0.556  0.70 24.76 ?  160 LEU   A HB2  1 
ATOM   3440 H HB2  B LEU   A 1 160 ? 7.706  -2.078  -0.102  0.30 21.93 ?  160 LEU   A HB2  1 
ATOM   3441 H HB3  A LEU   A 1 160 ? 7.571  -2.639  0.953   0.70 24.76 ?  160 LEU   A HB3  1 
ATOM   3442 H HB3  B LEU   A 1 160 ? 7.998  -2.423  1.423   0.30 21.93 ?  160 LEU   A HB3  1 
ATOM   3443 H HG   A LEU   A 1 160 ? 8.492  -4.721  0.430   0.70 25.08 ?  160 LEU   A HG   1 
ATOM   3444 H HG   B LEU   A 1 160 ? 9.035  -4.367  0.909   0.30 22.01 ?  160 LEU   A HG   1 
ATOM   3445 H HD11 A LEU   A 1 160 ? 8.581  -5.406  -1.798  0.70 25.88 ?  160 LEU   A HD11 1 
ATOM   3446 H HD11 B LEU   A 1 160 ? 9.393  -4.962  -1.373  0.30 21.96 ?  160 LEU   A HD11 1 
ATOM   3447 H HD12 A LEU   A 1 160 ? 7.086  -5.349  -1.279  0.70 25.88 ?  160 LEU   A HD12 1 
ATOM   3448 H HD12 B LEU   A 1 160 ? 7.889  -5.137  -0.893  0.30 21.96 ?  160 LEU   A HD12 1 
ATOM   3449 H HD13 A LEU   A 1 160 ? 7.651  -4.182  -2.199  0.70 25.88 ?  160 LEU   A HD13 1 
ATOM   3450 H HD13 B LEU   A 1 160 ? 8.305  -3.873  -1.763  0.30 21.96 ?  160 LEU   A HD13 1 
ATOM   3451 H HD21 A LEU   A 1 160 ? 10.320 -4.011  -0.801  0.70 24.99 ?  160 LEU   A HD21 1 
ATOM   3452 H HD21 B LEU   A 1 160 ? 10.948 -3.585  -0.042  0.30 22.06 ?  160 LEU   A HD21 1 
ATOM   3453 H HD22 A LEU   A 1 160 ? 9.522  -2.713  -1.255  0.70 24.99 ?  160 LEU   A HD22 1 
ATOM   3454 H HD22 B LEU   A 1 160 ? 10.165 -2.397  -0.749  0.30 22.06 ?  160 LEU   A HD22 1 
ATOM   3455 H HD23 A LEU   A 1 160 ? 9.932  -2.902  0.268   0.70 24.99 ?  160 LEU   A HD23 1 
ATOM   3456 H HD23 B LEU   A 1 160 ? 10.346 -2.401  0.829   0.30 22.06 ?  160 LEU   A HD23 1 
ATOM   3457 N N    A TYR   A 1 161 ? 6.256  -4.628  2.735   0.70 19.51 ?  161 TYR   A N    1 
ATOM   3458 N N    B TYR   A 1 161 ? 6.520  -4.240  3.052   0.30 16.26 ?  161 TYR   A N    1 
ATOM   3459 C CA   A TYR   A 1 161 ? 6.420  -5.685  3.724   0.70 19.19 ?  161 TYR   A CA   1 
ATOM   3460 C CA   B TYR   A 1 161 ? 6.528  -5.278  4.080   0.30 15.97 ?  161 TYR   A CA   1 
ATOM   3461 C C    A TYR   A 1 161 ? 5.283  -6.691  3.646   0.70 19.70 ?  161 TYR   A C    1 
ATOM   3462 C C    B TYR   A 1 161 ? 5.313  -6.185  3.939   0.30 16.63 ?  161 TYR   A C    1 
ATOM   3463 O O    A TYR   A 1 161 ? 5.514  -7.904  3.609   0.70 19.52 ?  161 TYR   A O    1 
ATOM   3464 O O    B TYR   A 1 161 ? 5.427  -7.412  4.038   0.30 16.35 ?  161 TYR   A O    1 
ATOM   3465 C CB   A TYR   A 1 161 ? 6.494  -5.069  5.118   0.70 19.05 ?  161 TYR   A CB   1 
ATOM   3466 C CB   B TYR   A 1 161 ? 6.576  -4.652  5.476   0.30 15.65 ?  161 TYR   A CB   1 
ATOM   3467 C CG   A TYR   A 1 161 ? 6.395  -6.076  6.233   0.70 18.99 ?  161 TYR   A CG   1 
ATOM   3468 C CG   B TYR   A 1 161 ? 6.453  -5.662  6.600   0.30 15.28 ?  161 TYR   A CG   1 
ATOM   3469 C CD1  A TYR   A 1 161 ? 7.512  -6.779  6.651   0.70 18.44 ?  161 TYR   A CD1  1 
ATOM   3470 C CD1  B TYR   A 1 161 ? 7.576  -6.295  7.124   0.30 15.11 ?  161 TYR   A CD1  1 
ATOM   3471 C CD2  A TYR   A 1 161 ? 5.184  -6.326  6.869   0.70 19.42 ?  161 TYR   A CD2  1 
ATOM   3472 C CD2  B TYR   A 1 161 ? 5.213  -5.977  7.144   0.30 15.40 ?  161 TYR   A CD2  1 
ATOM   3473 C CE1  A TYR   A 1 161 ? 7.431  -7.707  7.665   0.70 18.11 ?  161 TYR   A CE1  1 
ATOM   3474 C CE1  B TYR   A 1 161 ? 7.466  -7.218  8.149   0.30 15.47 ?  161 TYR   A CE1  1 
ATOM   3475 C CE2  A TYR   A 1 161 ? 5.092  -7.252  7.887   0.70 19.09 ?  161 TYR   A CE2  1 
ATOM   3476 C CE2  B TYR   A 1 161 ? 5.094  -6.897  8.169   0.30 15.57 ?  161 TYR   A CE2  1 
ATOM   3477 C CZ   A TYR   A 1 161 ? 6.222  -7.940  8.280   0.70 18.72 ?  161 TYR   A CZ   1 
ATOM   3478 C CZ   B TYR   A 1 161 ? 6.223  -7.511  8.669   0.30 15.91 ?  161 TYR   A CZ   1 
ATOM   3479 O OH   A TYR   A 1 161 ? 6.145  -8.867  9.292   0.70 19.33 ?  161 TYR   A OH   1 
ATOM   3480 O OH   B TYR   A 1 161 ? 6.107  -8.427  9.690   0.30 17.01 ?  161 TYR   A OH   1 
ATOM   3481 H H    A TYR   A 1 161 ? 6.249  -3.842  3.061   0.70 23.41 ?  161 TYR   A H    1 
ATOM   3482 H H    B TYR   A 1 161 ? 6.541  -3.433  3.351   0.30 19.51 ?  161 TYR   A H    1 
ATOM   3483 H HA   A TYR   A 1 161 ? 7.239  -6.167  3.552   0.70 23.03 ?  161 TYR   A HA   1 
ATOM   3484 H HA   B TYR   A 1 161 ? 7.322  -5.821  3.970   0.30 19.17 ?  161 TYR   A HA   1 
ATOM   3485 H HB2  A TYR   A 1 161 ? 7.344  -4.617  5.204   0.70 22.86 ?  161 TYR   A HB2  1 
ATOM   3486 H HB2  B TYR   A 1 161 ? 7.423  -4.190  5.584   0.30 18.78 ?  161 TYR   A HB2  1 
ATOM   3487 H HB3  A TYR   A 1 161 ? 5.766  -4.440  5.222   0.70 22.86 ?  161 TYR   A HB3  1 
ATOM   3488 H HB3  B TYR   A 1 161 ? 5.845  -4.019  5.564   0.30 18.78 ?  161 TYR   A HB3  1 
ATOM   3489 H HD1  A TYR   A 1 161 ? 8.328  -6.631  6.236   0.70 22.13 ?  161 TYR   A HD1  1 
ATOM   3490 H HD1  B TYR   A 1 161 ? 8.415  -6.095  6.779   0.30 18.13 ?  161 TYR   A HD1  1 
ATOM   3491 H HD2  A TYR   A 1 161 ? 4.419  -5.867  6.605   0.70 23.31 ?  161 TYR   A HD2  1 
ATOM   3492 H HD2  B TYR   A 1 161 ? 4.448  -5.566  6.811   0.30 18.48 ?  161 TYR   A HD2  1 
ATOM   3493 H HE1  A TYR   A 1 161 ? 8.188  -8.176  7.937   0.70 21.73 ?  161 TYR   A HE1  1 
ATOM   3494 H HE1  B TYR   A 1 161 ? 8.227  -7.633  8.491   0.30 18.57 ?  161 TYR   A HE1  1 
ATOM   3495 H HE2  A TYR   A 1 161 ? 4.271  -7.414  8.310   0.70 22.91 ?  161 TYR   A HE2  1 
ATOM   3496 H HE2  B TYR   A 1 161 ? 4.254  -7.101  8.522   0.30 18.68 ?  161 TYR   A HE2  1 
ATOM   3497 H HH   A TYR   A 1 161 ? 6.892  -9.213  9.438   0.70 23.19 ?  161 TYR   A HH   1 
ATOM   3498 H HH   B TYR   A 1 161 ? 6.860  -8.730  9.900   0.30 20.41 ?  161 TYR   A HH   1 
ATOM   3499 N N    A ASP   A 1 162 ? 4.040  -6.204  3.624   0.70 20.55 ?  162 ASP   A N    1 
ATOM   3500 N N    B ASP   A 1 162 ? 4.141  -5.592  3.700   0.30 17.66 ?  162 ASP   A N    1 
ATOM   3501 C CA   A ASP   A 1 162 ? 2.894  -7.107  3.574   0.70 21.16 ?  162 ASP   A CA   1 
ATOM   3502 C CA   B ASP   A 1 162 ? 2.933  -6.373  3.452   0.30 18.92 ?  162 ASP   A CA   1 
ATOM   3503 C C    A ASP   A 1 162 ? 2.928  -7.965  2.313   0.70 21.27 ?  162 ASP   A C    1 
ATOM   3504 C C    B ASP   A 1 162 ? 3.085  -7.239  2.210   0.30 18.92 ?  162 ASP   A C    1 
ATOM   3505 O O    A ASP   A 1 162 ? 2.583  -9.149  2.352   0.70 21.31 ?  162 ASP   A O    1 
ATOM   3506 O O    B ASP   A 1 162 ? 2.769  -8.435  2.227   0.30 19.04 ?  162 ASP   A O    1 
ATOM   3507 C CB   A ASP   A 1 162 ? 1.581  -6.314  3.645   0.70 22.36 ?  162 ASP   A CB   1 
ATOM   3508 C CB   B ASP   A 1 162 ? 1.739  -5.430  3.292   0.30 20.49 ?  162 ASP   A CB   1 
ATOM   3509 C CG   A ASP   A 1 162 ? 1.321  -5.678  5.006   0.70 23.60 ?  162 ASP   A CG   1 
ATOM   3510 C CG   B ASP   A 1 162 ? 1.060  -5.120  4.611   0.30 21.75 ?  162 ASP   A CG   1 
ATOM   3511 O OD1  A ASP   A 1 162 ? 1.983  -6.034  5.996   0.70 24.29 ?  162 ASP   A OD1  1 
ATOM   3512 O OD1  B ASP   A 1 162 ? 1.052  -5.997  5.500   0.30 22.50 ?  162 ASP   A OD1  1 
ATOM   3513 O OD2  A ASP   A 1 162 ? 0.392  -4.840  5.092   0.70 24.48 -1 162 ASP   A OD2  1 
ATOM   3514 O OD2  B ASP   A 1 162 ? 0.541  -3.993  4.761   0.30 22.17 -1 162 ASP   A OD2  1 
ATOM   3515 H H    A ASP   A 1 162 ? 3.825  -5.381  3.636   0.70 24.66 ?  162 ASP   A H    1 
ATOM   3516 H H    B ASP   A 1 162 ? 4.023  -4.742  3.676   0.30 21.19 ?  162 ASP   A H    1 
ATOM   3517 H HA   A ASP   A 1 162 ? 2.913  -7.711  4.338   0.70 25.39 ?  162 ASP   A HA   1 
ATOM   3518 H HA   B ASP   A 1 162 ? 2.761  -6.955  4.207   0.30 22.71 ?  162 ASP   A HA   1 
ATOM   3519 H HB2  A ASP   A 1 162 ? 1.594  -5.617  2.984   0.70 26.83 ?  162 ASP   A HB2  1 
ATOM   3520 H HB2  B ASP   A 1 162 ? 2.046  -4.579  2.938   0.30 24.58 ?  162 ASP   A HB2  1 
ATOM   3521 H HB3  A ASP   A 1 162 ? 0.831  -6.913  3.494   0.70 26.83 ?  162 ASP   A HB3  1 
ATOM   3522 H HB3  B ASP   A 1 162 ? 1.100  -5.827  2.673   0.30 24.58 ?  162 ASP   A HB3  1 
ATOM   3523 N N    A LYS   A 1 163 ? 3.360  -7.396  1.188   0.70 21.58 ?  163 LYS   A N    1 
ATOM   3524 N N    B LYS   A 1 163 ? 3.550  -6.642  1.110   0.30 19.19 ?  163 LYS   A N    1 
ATOM   3525 C CA   A LYS   A 1 163 ? 3.442  -8.167  -0.050  0.70 21.89 ?  163 LYS   A CA   1 
ATOM   3526 C CA   B LYS   A 1 163 ? 3.754  -7.403  -0.119  0.30 19.67 ?  163 LYS   A CA   1 
ATOM   3527 C C    A LYS   A 1 163 ? 4.551  -9.212  0.015   0.70 21.33 ?  163 LYS   A C    1 
ATOM   3528 C C    B LYS   A 1 163 ? 4.719  -8.557  0.114   0.30 18.51 ?  163 LYS   A C    1 
ATOM   3529 O O    A LYS   A 1 163 ? 4.397  -10.326 -0.499  0.70 22.31 ?  163 LYS   A O    1 
ATOM   3530 O O    B LYS   A 1 163 ? 4.470  -9.688  -0.319  0.30 17.61 ?  163 LYS   A O    1 
ATOM   3531 C CB   A LYS   A 1 163 ? 3.669  -7.218  -1.223  0.70 23.96 ?  163 LYS   A CB   1 
ATOM   3532 C CB   B LYS   A 1 163 ? 4.292  -6.481  -1.217  0.30 21.33 ?  163 LYS   A CB   1 
ATOM   3533 C CG   A LYS   A 1 163 ? 3.686  -7.891  -2.575  0.70 26.38 ?  163 LYS   A CG   1 
ATOM   3534 C CG   B LYS   A 1 163 ? 4.304  -7.097  -2.614  0.30 23.18 ?  163 LYS   A CG   1 
ATOM   3535 C CD   A LYS   A 1 163 ? 4.053  -6.901  -3.663  0.70 28.66 ?  163 LYS   A CD   1 
ATOM   3536 C CD   B LYS   A 1 163 ? 5.139  -6.260  -3.579  0.30 24.87 ?  163 LYS   A CD   1 
ATOM   3537 C CE   A LYS   A 1 163 ? 3.944  -7.532  -5.038  0.70 30.28 ?  163 LYS   A CE   1 
ATOM   3538 C CE   B LYS   A 1 163 ? 4.611  -6.342  -5.006  0.30 26.21 ?  163 LYS   A CE   1 
ATOM   3539 N NZ   A LYS   A 1 163 ? 4.613  -6.709  -6.080  0.70 31.26 ?  163 LYS   A NZ   1 
ATOM   3540 N NZ   B LYS   A 1 163 ? 5.442  -5.541  -5.950  0.30 27.02 ?  163 LYS   A NZ   1 
ATOM   3541 H H    A LYS   A 1 163 ? 3.601  -6.584  1.121   0.70 25.90 ?  163 LYS   A H    1 
ATOM   3542 H H    B LYS   A 1 163 ? 3.747  -5.806  1.050   0.30 23.03 ?  163 LYS   A H    1 
ATOM   3543 H HA   A LYS   A 1 163 ? 2.596  -8.632  -0.195  0.70 26.26 ?  163 LYS   A HA   1 
ATOM   3544 H HA   B LYS   A 1 163 ? 2.907  -7.766  -0.418  0.30 23.61 ?  163 LYS   A HA   1 
ATOM   3545 H HB2  A LYS   A 1 163 ? 2.956  -6.560  -1.228  0.70 28.75 ?  163 LYS   A HB2  1 
ATOM   3546 H HB2  B LYS   A 1 163 ? 3.741  -5.685  -1.255  0.30 25.60 ?  163 LYS   A HB2  1 
ATOM   3547 H HB3  A LYS   A 1 163 ? 4.522  -6.779  -1.099  0.70 28.75 ?  163 LYS   A HB3  1 
ATOM   3548 H HB3  B LYS   A 1 163 ? 5.205  -6.237  -0.999  0.30 25.60 ?  163 LYS   A HB3  1 
ATOM   3549 H HG2  A LYS   A 1 163 ? 4.345  -8.603  -2.575  0.70 31.66 ?  163 LYS   A HG2  1 
ATOM   3550 H HG2  B LYS   A 1 163 ? 4.689  -7.986  -2.573  0.30 27.81 ?  163 LYS   A HG2  1 
ATOM   3551 H HG3  A LYS   A 1 163 ? 2.804  -8.248  -2.767  0.70 31.66 ?  163 LYS   A HG3  1 
ATOM   3552 H HG3  B LYS   A 1 163 ? 3.398  -7.139  -2.956  0.30 27.81 ?  163 LYS   A HG3  1 
ATOM   3553 H HD2  A LYS   A 1 163 ? 3.444  -6.145  -3.625  0.70 34.40 ?  163 LYS   A HD2  1 
ATOM   3554 H HD2  B LYS   A 1 163 ? 5.117  -5.332  -3.301  0.30 29.85 ?  163 LYS   A HD2  1 
ATOM   3555 H HD3  A LYS   A 1 163 ? 4.966  -6.603  -3.529  0.70 34.40 ?  163 LYS   A HD3  1 
ATOM   3556 H HD3  B LYS   A 1 163 ? 6.054  -6.587  -3.578  0.30 29.85 ?  163 LYS   A HD3  1 
ATOM   3557 H HE2  A LYS   A 1 163 ? 4.343  -8.415  -5.031  0.70 36.34 ?  163 LYS   A HE2  1 
ATOM   3558 H HE2  B LYS   A 1 163 ? 4.623  -7.265  -5.302  0.30 31.45 ?  163 LYS   A HE2  1 
ATOM   3559 H HE3  A LYS   A 1 163 ? 3.010  -7.602  -5.270  0.70 36.34 ?  163 LYS   A HE3  1 
ATOM   3560 H HE3  B LYS   A 1 163 ? 3.705  -5.994  -5.032  0.30 31.45 ?  163 LYS   A HE3  1 
ATOM   3561 H HZ1  A LYS   A 1 163 ? 4.536  -7.104  -6.873  0.70 37.51 ?  163 LYS   A HZ1  1 
ATOM   3562 H HZ1  B LYS   A 1 163 ? 5.143  -5.642  -6.783  0.30 32.42 ?  163 LYS   A HZ1  1 
ATOM   3563 H HZ2  A LYS   A 1 163 ? 4.234  -5.905  -6.118  0.70 37.51 ?  163 LYS   A HZ2  1 
ATOM   3564 H HZ2  B LYS   A 1 163 ? 5.403  -4.678  -5.734  0.30 32.42 ?  163 LYS   A HZ2  1 
ATOM   3565 H HZ3  A LYS   A 1 163 ? 5.476  -6.612  -5.886  0.70 37.51 ?  163 LYS   A HZ3  1 
ATOM   3566 H HZ3  B LYS   A 1 163 ? 6.289  -5.810  -5.913  0.30 32.42 ?  163 LYS   A HZ3  1 
ATOM   3567 N N    A LEU   A 1 164 ? 5.691  -8.857  0.613   0.70 19.68 ?  164 LEU   A N    1 
ATOM   3568 N N    B LEU   A 1 164 ? 5.829  -8.289  0.805   0.30 18.33 ?  164 LEU   A N    1 
ATOM   3569 C CA   A LEU   A 1 164 ? 6.785  -9.811  0.777   0.70 18.82 ?  164 LEU   A CA   1 
ATOM   3570 C CA   B LEU   A 1 164 ? 6.864  -9.306  0.969   0.30 18.34 ?  164 LEU   A CA   1 
ATOM   3571 C C    A LEU   A 1 164 ? 6.358  -10.986 1.643   0.70 18.71 ?  164 LEU   A C    1 
ATOM   3572 C C    B LEU   A 1 164 ? 6.403  -10.439 1.878   0.30 18.05 ?  164 LEU   A C    1 
ATOM   3573 O O    A LEU   A 1 164 ? 6.667  -12.142 1.334   0.70 19.26 ?  164 LEU   A O    1 
ATOM   3574 O O    B LEU   A 1 164 ? 6.645  -11.615 1.582   0.30 17.70 ?  164 LEU   A O    1 
ATOM   3575 C CB   A LEU   A 1 164 ? 7.978  -9.113  1.424   0.70 18.27 ?  164 LEU   A CB   1 
ATOM   3576 C CB   B LEU   A 1 164 ? 8.141  -8.669  1.515   0.30 18.77 ?  164 LEU   A CB   1 
ATOM   3577 C CG   A LEU   A 1 164 ? 8.703  -8.042  0.604   0.70 18.42 ?  164 LEU   A CG   1 
ATOM   3578 C CG   B LEU   A 1 164 ? 9.037  -7.924  0.521   0.30 19.31 ?  164 LEU   A CG   1 
ATOM   3579 C CD1  A LEU   A 1 164 ? 9.604  -7.173  1.481   0.70 18.10 ?  164 LEU   A CD1  1 
ATOM   3580 C CD1  B LEU   A 1 164 ? 10.229 -7.323  1.245   0.30 19.50 ?  164 LEU   A CD1  1 
ATOM   3581 C CD2  A LEU   A 1 164 ? 9.514  -8.690  -0.498  0.70 19.08 ?  164 LEU   A CD2  1 
ATOM   3582 C CD2  B LEU   A 1 164 ? 9.505  -8.835  -0.612  0.30 19.56 ?  164 LEU   A CD2  1 
ATOM   3583 H H    A LEU   A 1 164 ? 5.856  -8.078  0.919   0.70 23.62 ?  164 LEU   A H    1 
ATOM   3584 H H    B LEU   A 1 164 ? 6.002  -7.534  1.178   0.30 21.99 ?  164 LEU   A H    1 
ATOM   3585 H HA   A LEU   A 1 164 ? 7.052  -10.157 -0.090  0.70 22.59 ?  164 LEU   A HA   1 
ATOM   3586 H HA   B LEU   A 1 164 ? 7.062  -9.686  0.103   0.30 22.00 ?  164 LEU   A HA   1 
ATOM   3587 H HB2  A LEU   A 1 164 ? 7.670  -8.692  2.237   0.70 21.92 ?  164 LEU   A HB2  1 
ATOM   3588 H HB2  B LEU   A 1 164 ? 7.888  -8.031  2.201   0.30 22.52 ?  164 LEU   A HB2  1 
ATOM   3589 H HB3  A LEU   A 1 164 ? 8.635  -9.793  1.645   0.70 21.92 ?  164 LEU   A HB3  1 
ATOM   3590 H HB3  B LEU   A 1 164 ? 8.677  -9.370  1.913   0.30 22.52 ?  164 LEU   A HB3  1 
ATOM   3591 H HG   A LEU   A 1 164 ? 8.041  -7.465  0.190   0.70 22.10 ?  164 LEU   A HG   1 
ATOM   3592 H HG   B LEU   A 1 164 ? 8.533  -7.197  0.128   0.30 23.18 ?  164 LEU   A HG   1 
ATOM   3593 H HD11 A LEU   A 1 164 ? 10.040 -6.512  0.925   0.70 21.72 ?  164 LEU   A HD11 1 
ATOM   3594 H HD11 B LEU   A 1 164 ? 10.718 -6.757  0.628   0.30 23.40 ?  164 LEU   A HD11 1 
ATOM   3595 H HD12 A LEU   A 1 164 ? 9.057  -6.734  2.154   0.70 21.72 ?  164 LEU   A HD12 1 
ATOM   3596 H HD12 B LEU   A 1 164 ? 9.911  -6.798  1.995   0.30 23.40 ?  164 LEU   A HD12 1 
ATOM   3597 H HD13 A LEU   A 1 164 ? 10.264 -7.738  1.910   0.70 21.72 ?  164 LEU   A HD13 1 
ATOM   3598 H HD13 B LEU   A 1 164 ? 10.802 -8.041  1.562   0.30 23.40 ?  164 LEU   A HD13 1 
ATOM   3599 H HD21 A LEU   A 1 164 ? 9.949  -7.995  -1.015  0.70 22.90 ?  164 LEU   A HD21 1 
ATOM   3600 H HD21 B LEU   A 1 164 ? 10.213 -8.389  -1.105  0.30 23.47 ?  164 LEU   A HD21 1 
ATOM   3601 H HD22 A LEU   A 1 164 ? 10.176 -9.274  -0.100  0.70 22.90 ?  164 LEU   A HD22 1 
ATOM   3602 H HD22 B LEU   A 1 164 ? 9.839  -9.665  -0.236  0.30 23.47 ?  164 LEU   A HD22 1 
ATOM   3603 H HD23 A LEU   A 1 164 ? 8.918  -9.202  -1.067  0.70 22.90 ?  164 LEU   A HD23 1 
ATOM   3604 H HD23 B LEU   A 1 164 ? 8.758  -9.018  -1.204  0.30 23.47 ?  164 LEU   A HD23 1 
ATOM   3605 N N    A VAL   A 1 165 ? 5.665  -10.703 2.746   0.70 17.93 ?  165 VAL   A N    1 
ATOM   3606 N N    B VAL   A 1 165 ? 5.742  -10.109 2.987   0.30 18.28 ?  165 VAL   A N    1 
ATOM   3607 C CA   A VAL   A 1 165 ? 5.176  -11.760 3.623   0.70 17.61 ?  165 VAL   A CA   1 
ATOM   3608 C CA   B VAL   A 1 165 ? 5.347  -11.137 3.946   0.30 18.86 ?  165 VAL   A CA   1 
ATOM   3609 C C    A VAL   A 1 165 ? 4.140  -12.609 2.900   0.70 17.82 ?  165 VAL   A C    1 
ATOM   3610 C C    B VAL   A 1 165 ? 4.225  -11.995 3.374   0.30 18.71 ?  165 VAL   A C    1 
ATOM   3611 O O    A VAL   A 1 165 ? 4.245  -13.839 2.846   0.70 17.63 ?  165 VAL   A O    1 
ATOM   3612 O O    B VAL   A 1 165 ? 4.264  -13.229 3.444   0.30 18.75 ?  165 VAL   A O    1 
ATOM   3613 C CB   A VAL   A 1 165 ? 4.615  -11.143 4.919   0.70 17.70 ?  165 VAL   A CB   1 
ATOM   3614 C CB   B VAL   A 1 165 ? 4.967  -10.493 5.292   0.30 19.59 ?  165 VAL   A CB   1 
ATOM   3615 C CG1  A VAL   A 1 165 ? 3.845  -12.178 5.733   0.70 17.96 ?  165 VAL   A CG1  1 
ATOM   3616 C CG1  B VAL   A 1 165 ? 4.297  -11.505 6.207   0.30 19.92 ?  165 VAL   A CG1  1 
ATOM   3617 C CG2  A VAL   A 1 165 ? 5.736  -10.525 5.745   0.70 17.79 ?  165 VAL   A CG2  1 
ATOM   3618 C CG2  B VAL   A 1 165 ? 6.208  -9.909  5.959   0.30 19.78 ?  165 VAL   A CG2  1 
ATOM   3619 H H    A VAL   A 1 165 ? 5.469  -9.917  3.008   0.70 21.51 ?  165 VAL   A H    1 
ATOM   3620 H H    B VAL   A 1 165 ? 5.508  -9.309  3.200   0.30 21.93 ?  165 VAL   A H    1 
ATOM   3621 H HA   A VAL   A 1 165 ? 5.909  -12.344 3.872   0.70 21.14 ?  165 VAL   A HA   1 
ATOM   3622 H HA   B VAL   A 1 165 ? 6.108  -11.714 4.107   0.30 22.63 ?  165 VAL   A HA   1 
ATOM   3623 H HB   A VAL   A 1 165 ? 3.994  -10.433 4.686   0.70 21.24 ?  165 VAL   A HB   1 
ATOM   3624 H HB   B VAL   A 1 165 ? 4.343  -9.764  5.137   0.30 23.50 ?  165 VAL   A HB   1 
ATOM   3625 H HG11 A VAL   A 1 165 ? 3.741  -11.849 6.641   0.70 21.55 ?  165 VAL   A HG11 1 
ATOM   3626 H HG11 B VAL   A 1 165 ? 4.310  -11.164 7.117   0.30 23.90 ?  165 VAL   A HG11 1 
ATOM   3627 H HG12 A VAL   A 1 165 ? 2.970  -12.309 5.332   0.70 21.55 ?  165 VAL   A HG12 1 
ATOM   3628 H HG12 B VAL   A 1 165 ? 3.381  -11.635 5.919   0.30 23.90 ?  165 VAL   A HG12 1 
ATOM   3629 H HG13 A VAL   A 1 165 ? 4.340  -13.008 5.736   0.70 21.55 ?  165 VAL   A HG13 1 
ATOM   3630 H HG13 B VAL   A 1 165 ? 4.785  -12.340 6.162   0.30 23.90 ?  165 VAL   A HG13 1 
ATOM   3631 H HG21 A VAL   A 1 165 ? 5.362  -10.141 6.554   0.70 21.35 ?  165 VAL   A HG21 1 
ATOM   3632 H HG21 B VAL   A 1 165 ? 5.967  -9.558  6.830   0.30 23.74 ?  165 VAL   A HG21 1 
ATOM   3633 H HG22 A VAL   A 1 165 ? 6.378  -11.215 5.974   0.70 21.35 ?  165 VAL   A HG22 1 
ATOM   3634 H HG22 B VAL   A 1 165 ? 6.872  -10.610 6.058   0.30 23.74 ?  165 VAL   A HG22 1 
ATOM   3635 H HG23 A VAL   A 1 165 ? 6.169  -9.832  5.221   0.70 21.35 ?  165 VAL   A HG23 1 
ATOM   3636 H HG23 B VAL   A 1 165 ? 6.562  -9.197  5.402   0.30 23.74 ?  165 VAL   A HG23 1 
ATOM   3637 N N    A SER   A 1 166 ? 3.132  -11.959 2.318   0.70 18.21 ?  166 SER   A N    1 
ATOM   3638 N N    B SER   A 1 166 ? 3.216  -11.356 2.783   0.30 18.68 ?  166 SER   A N    1 
ATOM   3639 C CA   A SER   A 1 166 ? 2.008  -12.692 1.746   0.70 19.44 ?  166 SER   A CA   1 
ATOM   3640 C CA   B SER   A 1 166 ? 2.074  -12.094 2.260   0.30 18.99 ?  166 SER   A CA   1 
ATOM   3641 C C    A SER   A 1 166 ? 2.422  -13.542 0.554   0.70 20.15 ?  166 SER   A C    1 
ATOM   3642 C C    B SER   A 1 166 ? 2.409  -12.882 0.999   0.30 18.32 ?  166 SER   A C    1 
ATOM   3643 O O    A SER   A 1 166 ? 1.774  -14.559 0.269   0.70 21.73 ?  166 SER   A O    1 
ATOM   3644 O O    B SER   A 1 166 ? 1.638  -13.771 0.621   0.30 18.66 ?  166 SER   A O    1 
ATOM   3645 C CB   A SER   A 1 166 ? 0.897  -11.720 1.332   0.70 20.92 ?  166 SER   A CB   1 
ATOM   3646 C CB   B SER   A 1 166 ? 0.923  -11.129 1.983   0.30 20.25 ?  166 SER   A CB   1 
ATOM   3647 O OG   A SER   A 1 166 ? 0.298  -11.105 2.463   0.70 22.83 ?  166 SER   A OG   1 
ATOM   3648 O OG   B SER   A 1 166 ? 0.612  -10.375 3.142   0.30 21.59 ?  166 SER   A OG   1 
ATOM   3649 H H    A SER   A 1 166 ? 3.063  -11.112 2.254   0.70 21.86 ?  166 SER   A H    1 
ATOM   3650 H H    B SER   A 1 166 ? 3.167  -10.504 2.684   0.30 22.42 ?  166 SER   A H    1 
ATOM   3651 H HA   A SER   A 1 166 ? 1.626  -13.288 2.415   0.70 23.32 ?  166 SER   A HA   1 
ATOM   3652 H HA   B SER   A 1 166 ? 1.773  -12.721 2.935   0.30 22.79 ?  166 SER   A HA   1 
ATOM   3653 H HB2  A SER   A 1 166 ? 1.269  -11.034 0.758   0.70 25.11 ?  166 SER   A HB2  1 
ATOM   3654 H HB2  B SER   A 1 166 ? 1.181  -10.517 1.278   0.30 24.31 ?  166 SER   A HB2  1 
ATOM   3655 H HB3  A SER   A 1 166 ? 0.202  -12.205 0.850   0.70 25.11 ?  166 SER   A HB3  1 
ATOM   3656 H HB3  B SER   A 1 166 ? 0.140  -11.638 1.712   0.30 24.31 ?  166 SER   A HB3  1 
ATOM   3657 H HG   A SER   A 1 166 ? 0.877  -10.659 2.885   0.70 27.40 ?  166 SER   A HG   1 
ATOM   3658 H HG   B SER   A 1 166 ? -0.032 -9.857  2.989   0.30 25.91 ?  166 SER   A HG   1 
ATOM   3659 N N    A SER   A 1 167 ? 3.477  -13.148 -0.158  0.70 20.26 ?  167 SER   A N    1 
ATOM   3660 N N    B SER   A 1 167 ? 3.524  -12.576 0.336   0.30 17.92 ?  167 SER   A N    1 
ATOM   3661 C CA   A SER   A 1 167 ? 3.916  -13.878 -1.335  0.70 21.02 ?  167 SER   A CA   1 
ATOM   3662 C CA   B SER   A 1 167 ? 3.940  -13.304 -0.855  0.30 17.94 ?  167 SER   A CA   1 
ATOM   3663 C C    A SER   A 1 167 ? 5.088  -14.803 -1.051  0.70 20.78 ?  167 SER   A C    1 
ATOM   3664 C C    B SER   A 1 167 ? 5.132  -14.218 -0.608  0.30 18.34 ?  167 SER   A C    1 
ATOM   3665 O O    A SER   A 1 167 ? 5.604  -15.427 -1.983  0.70 21.33 ?  167 SER   A O    1 
ATOM   3666 O O    B SER   A 1 167 ? 5.602  -14.866 -1.550  0.30 18.11 ?  167 SER   A O    1 
ATOM   3667 C CB   A SER   A 1 167 ? 4.286  -12.908 -2.464  0.70 21.93 ?  167 SER   A CB   1 
ATOM   3668 C CB   B SER   A 1 167 ? 4.261  -12.328 -1.995  0.30 17.85 ?  167 SER   A CB   1 
ATOM   3669 O OG   A SER   A 1 167 ? 5.432  -12.144 -2.130  0.70 22.54 ?  167 SER   A OG   1 
ATOM   3670 O OG   B SER   A 1 167 ? 5.413  -11.556 -1.700  0.30 17.64 ?  167 SER   A OG   1 
ATOM   3671 H H    A SER   A 1 167 ? 3.943  -12.449 0.025   0.70 24.32 ?  167 SER   A H    1 
ATOM   3672 H H    B SER   A 1 167 ? 4.057  -11.937 0.559   0.30 21.51 ?  167 SER   A H    1 
ATOM   3673 H HA   A SER   A 1 167 ? 3.181  -14.426 -1.651  0.70 25.23 ?  167 SER   A HA   1 
ATOM   3674 H HA   B SER   A 1 167 ? 3.204  -13.860 -1.149  0.30 21.52 ?  167 SER   A HA   1 
ATOM   3675 H HB2  A SER   A 1 167 ? 4.467  -13.421 -3.267  0.70 26.31 ?  167 SER   A HB2  1 
ATOM   3676 H HB2  B SER   A 1 167 ? 4.419  -12.837 -2.807  0.30 21.42 ?  167 SER   A HB2  1 
ATOM   3677 H HB3  A SER   A 1 167 ? 3.534  -12.310 -2.622  0.70 26.31 ?  167 SER   A HB3  1 
ATOM   3678 H HB3  B SER   A 1 167 ? 3.501  -11.736 -2.124  0.30 21.42 ?  167 SER   A HB3  1 
ATOM   3679 H HG   A SER   A 1 167 ? 5.275  -11.692 -1.439  0.70 27.05 ?  167 SER   A HG   1 
ATOM   3680 H HG   B SER   A 1 167 ? 5.285  -11.106 -1.003  0.30 21.17 ?  167 SER   A HG   1 
ATOM   3681 N N    A PHE   A 1 168 ? 5.518  -14.915 0.204   0.70 20.05 ?  168 PHE   A N    1 
ATOM   3682 N N    B PHE   A 1 168 ? 5.628  -14.296 0.625   0.30 19.15 ?  168 PHE   A N    1 
ATOM   3683 C CA   A PHE   A 1 168 ? 6.703  -15.707 0.500   0.70 20.14 ?  168 PHE   A CA   1 
ATOM   3684 C CA   B PHE   A 1 168 ? 6.808  -15.101 0.905   0.30 20.44 ?  168 PHE   A CA   1 
ATOM   3685 C C    A PHE   A 1 168 ? 6.392  -17.191 0.393   0.70 22.29 ?  168 PHE   A C    1 
ATOM   3686 C C    B PHE   A 1 168 ? 6.496  -16.579 0.722   0.30 22.05 ?  168 PHE   A C    1 
ATOM   3687 O O    A PHE   A 1 168 ? 5.426  -17.683 0.986   0.70 23.42 ?  168 PHE   A O    1 
ATOM   3688 O O    B PHE   A 1 168 ? 5.458  -17.074 1.169   0.30 22.33 ?  168 PHE   A O    1 
ATOM   3689 C CB   A PHE   A 1 168 ? 7.232  -15.409 1.898   0.70 19.00 ?  168 PHE   A CB   1 
ATOM   3690 C CB   B PHE   A 1 168 ? 7.295  -14.855 2.331   0.30 20.21 ?  168 PHE   A CB   1 
ATOM   3691 C CG   A PHE   A 1 168 ? 8.499  -16.149 2.215   0.70 17.46 ?  168 PHE   A CG   1 
ATOM   3692 C CG   B PHE   A 1 168 ? 8.543  -15.616 2.681   0.30 20.02 ?  168 PHE   A CG   1 
ATOM   3693 C CD1  A PHE   A 1 168 ? 9.687  -15.785 1.611   0.70 17.43 ?  168 PHE   A CD1  1 
ATOM   3694 C CD1  B PHE   A 1 168 ? 9.767  -15.230 2.167   0.30 20.03 ?  168 PHE   A CD1  1 
ATOM   3695 C CD2  A PHE   A 1 168 ? 8.505  -17.227 3.086   0.70 16.70 ?  168 PHE   A CD2  1 
ATOM   3696 C CD2  B PHE   A 1 168 ? 8.494  -16.715 3.524   0.30 20.06 ?  168 PHE   A CD2  1 
ATOM   3697 C CE1  A PHE   A 1 168 ? 10.856 -16.465 1.879   0.70 16.94 ?  168 PHE   A CE1  1 
ATOM   3698 C CE1  B PHE   A 1 168 ? 10.917 -15.923 2.482   0.30 20.01 ?  168 PHE   A CE1  1 
ATOM   3699 C CE2  A PHE   A 1 168 ? 9.681  -17.908 3.357   0.70 16.82 ?  168 PHE   A CE2  1 
ATOM   3700 C CE2  B PHE   A 1 168 ? 9.646  -17.414 3.844   0.30 20.08 ?  168 PHE   A CE2  1 
ATOM   3701 C CZ   A PHE   A 1 168 ? 10.855 -17.523 2.751   0.70 16.90 ?  168 PHE   A CZ   1 
ATOM   3702 C CZ   B PHE   A 1 168 ? 10.858 -17.016 3.322   0.30 20.05 ?  168 PHE   A CZ   1 
ATOM   3703 H H    A PHE   A 1 168 ? 5.150  -14.548 0.890   0.70 24.06 ?  168 PHE   A H    1 
ATOM   3704 H H    B PHE   A 1 168 ? 5.300  -13.895 1.311   0.30 22.98 ?  168 PHE   A H    1 
ATOM   3705 H HA   A PHE   A 1 168 ? 7.399  -15.491 -0.142  0.70 24.16 ?  168 PHE   A HA   1 
ATOM   3706 H HA   B PHE   A 1 168 ? 7.518  -14.858 0.289   0.30 24.53 ?  168 PHE   A HA   1 
ATOM   3707 H HB2  A PHE   A 1 168 ? 7.417  -14.462 1.970   0.70 22.80 ?  168 PHE   A HB2  1 
ATOM   3708 H HB2  B PHE   A 1 168 ? 7.483  -13.909 2.438   0.30 24.25 ?  168 PHE   A HB2  1 
ATOM   3709 H HB3  A PHE   A 1 168 ? 6.563  -15.670 2.549   0.70 22.80 ?  168 PHE   A HB3  1 
ATOM   3710 H HB3  B PHE   A 1 168 ? 6.599  -15.123 2.947   0.30 24.25 ?  168 PHE   A HB3  1 
ATOM   3711 H HD1  A PHE   A 1 168 ? 9.702  -15.071 1.019   0.70 20.91 ?  168 PHE   A HD1  1 
ATOM   3712 H HD1  B PHE   A 1 168 ? 9.815  -14.496 1.600   0.30 24.04 ?  168 PHE   A HD1  1 
ATOM   3713 H HD2  A PHE   A 1 168 ? 7.711  -17.494 3.497   0.70 20.04 ?  168 PHE   A HD2  1 
ATOM   3714 H HD2  B PHE   A 1 168 ? 7.678  -16.986 3.879   0.30 24.08 ?  168 PHE   A HD2  1 
ATOM   3715 H HE1  A PHE   A 1 168 ? 11.653 -16.208 1.472   0.70 20.33 ?  168 PHE   A HE1  1 
ATOM   3716 H HE1  B PHE   A 1 168 ? 11.734 -15.652 2.129   0.30 24.01 ?  168 PHE   A HE1  1 
ATOM   3717 H HE2  A PHE   A 1 168 ? 9.669  -18.631 3.949   0.70 20.18 ?  168 PHE   A HE2  1 
ATOM   3718 H HE2  B PHE   A 1 168 ? 9.601  -18.150 4.412   0.30 24.10 ?  168 PHE   A HE2  1 
ATOM   3719 H HZ   A PHE   A 1 168 ? 11.640 -17.986 2.936   0.70 20.28 ?  168 PHE   A HZ   1 
ATOM   3720 H HZ   B PHE   A 1 168 ? 11.633 -17.483 3.536   0.30 24.06 ?  168 PHE   A HZ   1 
ATOM   3721 N N    A LEU   A 1 169 ? 7.236  -17.906 -0.345  0.70 24.78 ?  169 LEU   A N    1 
ATOM   3722 N N    B LEU   A 1 169 ? 7.411  -17.285 0.069   0.30 23.72 ?  169 LEU   A N    1 
ATOM   3723 C CA   A LEU   A 1 169 ? 7.074  -19.341 -0.485  0.70 28.43 ?  169 LEU   A CA   1 
ATOM   3724 C CA   B LEU   A 1 169 ? 7.201  -18.686 -0.246  0.30 25.41 ?  169 LEU   A CA   1 
ATOM   3725 C C    A LEU   A 1 169 ? 7.994  -20.055 0.494   0.70 29.63 ?  169 LEU   A C    1 
ATOM   3726 C C    B LEU   A 1 169 ? 7.868  -19.588 0.788   0.30 25.71 ?  169 LEU   A C    1 
ATOM   3727 O O    A LEU   A 1 169 ? 7.570  -20.440 1.584   0.70 30.38 ?  169 LEU   A O    1 
ATOM   3728 O O    B LEU   A 1 169 ? 7.207  -20.405 1.431   0.30 25.72 ?  169 LEU   A O    1 
ATOM   3729 C CB   A LEU   A 1 169 ? 7.374  -19.778 -1.920  0.70 30.34 ?  169 LEU   A CB   1 
ATOM   3730 C CB   B LEU   A 1 169 ? 7.742  -18.991 -1.646  0.30 26.66 ?  169 LEU   A CB   1 
ATOM   3731 C CG   A LEU   A 1 169 ? 7.043  -21.235 -2.249  0.70 31.61 ?  169 LEU   A CG   1 
ATOM   3732 C CG   B LEU   A 1 169 ? 7.145  -20.199 -2.365  0.30 27.74 ?  169 LEU   A CG   1 
ATOM   3733 C CD1  A LEU   A 1 169 ? 5.620  -21.569 -1.829  0.70 32.23 ?  169 LEU   A CD1  1 
ATOM   3734 C CD1  B LEU   A 1 169 ? 5.638  -20.234 -2.179  0.30 28.19 ?  169 LEU   A CD1  1 
ATOM   3735 C CD2  A LEU   A 1 169 ? 7.238  -21.503 -3.734  0.70 31.97 ?  169 LEU   A CD2  1 
ATOM   3736 C CD2  B LEU   A 1 169 ? 7.497  -20.150 -3.843  0.30 28.06 ?  169 LEU   A CD2  1 
ATOM   3737 O OXT  A LEU   A 1 169 ? 9.180  -20.249 0.225   0.70 29.69 -1 169 LEU   A OXT  1 
ATOM   3738 O OXT  B LEU   A 1 169 ? 9.078  -19.518 1.008   0.30 25.83 -1 169 LEU   A OXT  1 
ATOM   3739 H H    A LEU   A 1 169 ? 7.912  -17.582 -0.775  0.70 29.74 ?  169 LEU   A H    1 
ATOM   3740 H H    B LEU   A 1 169 ? 8.162  -16.970 -0.206  0.30 28.47 ?  169 LEU   A H    1 
ATOM   3741 H HA   A LEU   A 1 169 ? 6.159  -19.574 -0.272  0.70 34.12 ?  169 LEU   A HA   1 
ATOM   3742 H HA   B LEU   A 1 169 ? 6.248  -18.852 -0.227  0.30 30.50 ?  169 LEU   A HA   1 
ATOM   3743 H HB2  A LEU   A 1 169 ? 6.860  -19.222 -2.524  0.70 36.41 ?  169 LEU   A HB2  1 
ATOM   3744 H HB2  B LEU   A 1 169 ? 7.588  -18.216 -2.209  0.30 32.00 ?  169 LEU   A HB2  1 
ATOM   3745 H HB3  A LEU   A 1 169 ? 8.321  -19.652 -2.088  0.70 36.41 ?  169 LEU   A HB3  1 
ATOM   3746 H HB3  B LEU   A 1 169 ? 8.698  -19.145 -1.573  0.30 32.00 ?  169 LEU   A HB3  1 
ATOM   3747 H HG   A LEU   A 1 169 ? 7.645  -21.818 -1.759  0.70 37.93 ?  169 LEU   A HG   1 
ATOM   3748 H HG   B LEU   A 1 169 ? 7.520  -21.012 -1.990  0.30 33.28 ?  169 LEU   A HG   1 
ATOM   3749 H HD11 A LEU   A 1 169 ? 5.349  -22.394 -2.260  0.70 38.68 ?  169 LEU   A HD11 1 
ATOM   3750 H HD11 B LEU   A 1 169 ? 5.249  -20.787 -2.867  0.30 33.82 ?  169 LEU   A HD11 1 
ATOM   3751 H HD12 A LEU   A 1 169 ? 5.590  -21.674 -0.865  0.70 38.68 ?  169 LEU   A HD12 1 
ATOM   3752 H HD12 B LEU   A 1 169 ? 5.437  -20.602 -1.302  0.30 33.82 ?  169 LEU   A HD12 1 
ATOM   3753 H HD13 A LEU   A 1 169 ? 5.034  -20.846 -2.103  0.70 38.68 ?  169 LEU   A HD13 1 
ATOM   3754 H HD13 B LEU   A 1 169 ? 5.293  -19.328 -2.245  0.30 33.82 ?  169 LEU   A HD13 1 
ATOM   3755 H HD21 A LEU   A 1 169 ? 7.030  -22.433 -3.917  0.70 38.36 ?  169 LEU   A HD21 1 
ATOM   3756 H HD21 B LEU   A 1 169 ? 7.128  -20.932 -4.281  0.30 33.67 ?  169 LEU   A HD21 1 
ATOM   3757 H HD22 A LEU   A 1 169 ? 6.642  -20.926 -4.238  0.70 38.36 ?  169 LEU   A HD22 1 
ATOM   3758 H HD22 B LEU   A 1 169 ? 7.119  -19.344 -4.230  0.30 33.67 ?  169 LEU   A HD22 1 
ATOM   3759 H HD23 A LEU   A 1 169 ? 8.159  -21.316 -3.970  0.70 38.36 ?  169 LEU   A HD23 1 
ATOM   3760 H HD23 B LEU   A 1 169 ? 8.462  -20.140 -3.938  0.30 33.67 ?  169 LEU   A HD23 1 
ATOM   3761 N N    A SER   B 1 1   ? 50.754 -9.182  -23.685 0.70 31.24 ?  1   SER   B N    1 
ATOM   3762 N N    B SER   B 1 1   ? 50.768 -9.283  -23.752 0.30 28.60 ?  1   SER   B N    1 
ATOM   3763 C CA   A SER   B 1 1   ? 51.269 -10.262 -22.820 0.70 30.73 ?  1   SER   B CA   1 
ATOM   3764 C CA   B SER   B 1 1   ? 51.239 -10.276 -22.764 0.30 28.44 ?  1   SER   B CA   1 
ATOM   3765 C C    A SER   B 1 1   ? 50.201 -11.317 -22.571 0.70 29.21 ?  1   SER   B C    1 
ATOM   3766 C C    B SER   B 1 1   ? 50.176 -11.343 -22.537 0.30 27.93 ?  1   SER   B C    1 
ATOM   3767 O O    A SER   B 1 1   ? 49.007 -11.112 -22.831 0.70 28.97 ?  1   SER   B O    1 
ATOM   3768 O O    B SER   B 1 1   ? 49.016 -11.183 -22.927 0.30 27.73 ?  1   SER   B O    1 
ATOM   3769 C CB   A SER   B 1 1   ? 51.759 -9.700  -21.487 0.70 31.75 ?  1   SER   B CB   1 
ATOM   3770 C CB   B SER   B 1 1   ? 51.578 -9.597  -21.441 0.30 28.86 ?  1   SER   B CB   1 
ATOM   3771 O OG   A SER   B 1 1   ? 50.670 -9.335  -20.661 0.70 32.94 ?  1   SER   B OG   1 
ATOM   3772 O OG   B SER   B 1 1   ? 50.424 -9.473  -20.631 0.30 29.29 ?  1   SER   B OG   1 
ATOM   3773 H H1   A SER   B 1 1   ? 50.559 -9.520  -24.482 0.70 37.49 ?  1   SER   B H1   1 
ATOM   3774 H H1   B SER   B 1 1   ? 51.473 -8.897  -24.132 0.30 34.32 ?  1   SER   B H1   1 
ATOM   3775 H H2   A SER   B 1 1   ? 50.028 -8.837  -23.314 0.70 37.49 ?  1   SER   B H2   1 
ATOM   3776 H H2   B SER   B 1 1   ? 50.282 -9.695  -24.370 0.30 34.32 ?  1   SER   B H2   1 
ATOM   3777 H H3   A SER   B 1 1   ? 51.381 -8.558  -23.768 0.70 37.49 ?  1   SER   B H3   1 
ATOM   3778 H H3   B SER   B 1 1   ? 50.277 -8.673  -23.337 0.30 34.32 ?  1   SER   B H3   1 
ATOM   3779 H HA   A SER   B 1 1   ? 52.019 -10.676 -23.269 0.70 36.87 ?  1   SER   B HA   1 
ATOM   3780 H HA   B SER   B 1 1   ? 52.038 -10.696 -23.112 0.30 34.12 ?  1   SER   B HA   1 
ATOM   3781 H HB2  A SER   B 1 1   ? 52.281 -10.382 -21.040 0.70 38.10 ?  1   SER   B HB2  1 
ATOM   3782 H HB2  B SER   B 1 1   ? 52.240 -10.135 -20.981 0.30 34.64 ?  1   SER   B HB2  1 
ATOM   3783 H HB3  A SER   B 1 1   ? 52.305 -8.918  -21.654 0.70 38.10 ?  1   SER   B HB3  1 
ATOM   3784 H HB3  B SER   B 1 1   ? 51.933 -8.712  -21.618 0.30 34.64 ?  1   SER   B HB3  1 
ATOM   3785 H HG   A SER   B 1 1   ? 50.936 -8.814  -20.058 0.70 39.53 ?  1   SER   B HG   1 
ATOM   3786 H HG   B SER   B 1 1   ? 50.570 -8.925  -20.013 0.30 35.15 ?  1   SER   B HG   1 
ATOM   3787 N N    A MET   B 1 2   ? 50.652 -12.448 -22.046 0.70 28.13 ?  2   MET   B N    1 
ATOM   3788 N N    B MET   B 1 2   ? 50.583 -12.427 -21.886 0.30 27.61 ?  2   MET   B N    1 
ATOM   3789 C CA   A MET   B 1 2   ? 49.832 -13.639 -21.883 0.70 27.65 ?  2   MET   B CA   1 
ATOM   3790 C CA   B MET   B 1 2   ? 49.762 -13.626 -21.737 0.30 27.20 ?  2   MET   B CA   1 
ATOM   3791 C C    A MET   B 1 2   ? 49.593 -13.840 -20.393 0.70 24.68 ?  2   MET   B C    1 
ATOM   3792 C C    B MET   B 1 2   ? 49.483 -13.851 -20.255 0.30 25.19 ?  2   MET   B C    1 
ATOM   3793 O O    A MET   B 1 2   ? 50.535 -14.101 -19.639 0.70 24.49 ?  2   MET   B O    1 
ATOM   3794 O O    B MET   B 1 2   ? 50.348 -14.334 -19.519 0.30 25.41 ?  2   MET   B O    1 
ATOM   3795 C CB   A MET   B 1 2   ? 50.559 -14.832 -22.493 0.70 31.21 ?  2   MET   B CB   1 
ATOM   3796 C CB   B MET   B 1 2   ? 50.497 -14.812 -22.340 0.30 28.99 ?  2   MET   B CB   1 
ATOM   3797 C CG   A MET   B 1 2   ? 49.716 -16.084 -22.651 0.70 34.48 ?  2   MET   B CG   1 
ATOM   3798 C CG   B MET   B 1 2   ? 49.611 -15.972 -22.756 0.30 30.47 ?  2   MET   B CG   1 
ATOM   3799 S SD   A MET   B 1 2   ? 50.565 -17.319 -23.653 0.70 37.40 ?  2   MET   B SD   1 
ATOM   3800 S SD   B MET   B 1 2   ? 50.481 -17.094 -23.861 0.30 31.72 ?  2   MET   B SD   1 
ATOM   3801 C CE   A MET   B 1 2   ? 51.085 -16.295 -25.024 0.70 37.67 ?  2   MET   B CE   1 
ATOM   3802 C CE   B MET   B 1 2   ? 51.289 -15.915 -24.933 0.30 31.86 ?  2   MET   B CE   1 
ATOM   3803 H H    A MET   B 1 2   ? 51.459 -12.555 -21.762 0.70 33.75 ?  2   MET   B H    1 
ATOM   3804 H H    B MET   B 1 2   ? 51.359 -12.497 -21.522 0.30 33.14 ?  2   MET   B H    1 
ATOM   3805 H HA   A MET   B 1 2   ? 48.988 -13.530 -22.341 0.70 33.18 ?  2   MET   B HA   1 
ATOM   3806 H HA   B MET   B 1 2   ? 48.930 -13.512 -22.220 0.30 32.64 ?  2   MET   B HA   1 
ATOM   3807 H HB2  A MET   B 1 2   ? 50.872 -14.551 -23.363 0.70 37.45 ?  2   MET   B HB2  1 
ATOM   3808 H HB2  B MET   B 1 2   ? 50.977 -14.471 -23.105 0.30 34.79 ?  2   MET   B HB2  1 
ATOM   3809 H HB3  A MET   B 1 2   ? 51.315 -15.069 -21.937 0.70 37.45 ?  2   MET   B HB3  1 
ATOM   3810 H HB3  B MET   B 1 2   ? 51.127 -15.164 -21.699 0.30 34.79 ?  2   MET   B HB3  1 
ATOM   3811 H HG2  A MET   B 1 2   ? 49.540 -16.464 -21.773 0.70 41.38 ?  2   MET   B HG2  1 
ATOM   3812 H HG2  B MET   B 1 2   ? 49.342 -16.467 -21.963 0.30 36.57 ?  2   MET   B HG2  1 
ATOM   3813 H HG3  A MET   B 1 2   ? 48.884 -15.864 -23.096 0.70 41.38 ?  2   MET   B HG3  1 
ATOM   3814 H HG3  B MET   B 1 2   ? 48.831 -15.643 -23.223 0.30 36.57 ?  2   MET   B HG3  1 
ATOM   3815 H HE1  A MET   B 1 2   ? 51.239 -16.859 -25.787 0.70 45.20 ?  2   MET   B HE1  1 
ATOM   3816 H HE1  B MET   B 1 2   ? 51.484 -16.353 -25.759 0.30 38.24 ?  2   MET   B HE1  1 
ATOM   3817 H HE2  A MET   B 1 2   ? 50.376 -15.657 -25.215 0.70 45.20 ?  2   MET   B HE2  1 
ATOM   3818 H HE2  B MET   B 1 2   ? 50.687 -15.165 -25.085 0.30 38.24 ?  2   MET   B HE2  1 
ATOM   3819 H HE3  A MET   B 1 2   ? 51.900 -15.818 -24.787 0.70 45.20 ?  2   MET   B HE3  1 
ATOM   3820 H HE3  B MET   B 1 2   ? 52.110 -15.601 -24.510 0.30 38.24 ?  2   MET   B HE3  1 
ATOM   3821 N N    A VAL   B 1 3   ? 48.341 -13.687 -19.971 0.70 21.87 ?  3   VAL   B N    1 
ATOM   3822 N N    B VAL   B 1 3   ? 48.275 -13.504 -19.821 0.30 22.90 ?  3   VAL   B N    1 
ATOM   3823 C CA   A VAL   B 1 3   ? 47.931 -13.932 -18.595 0.70 20.65 ?  3   VAL   B CA   1 
ATOM   3824 C CA   B VAL   B 1 3   ? 47.832 -13.761 -18.456 0.30 20.97 ?  3   VAL   B CA   1 
ATOM   3825 C C    A VAL   B 1 3   ? 46.694 -14.820 -18.613 0.70 18.80 ?  3   VAL   B C    1 
ATOM   3826 C C    B VAL   B 1 3   ? 46.584 -14.630 -18.497 0.30 18.92 ?  3   VAL   B C    1 
ATOM   3827 O O    A VAL   B 1 3   ? 45.978 -14.913 -19.613 0.70 19.32 ?  3   VAL   B O    1 
ATOM   3828 O O    B VAL   B 1 3   ? 45.757 -14.529 -19.409 0.30 18.79 ?  3   VAL   B O    1 
ATOM   3829 C CB   A VAL   B 1 3   ? 47.654 -12.622 -17.822 0.70 22.27 ?  3   VAL   B CB   1 
ATOM   3830 C CB   B VAL   B 1 3   ? 47.566 -12.468 -17.654 0.30 21.31 ?  3   VAL   B CB   1 
ATOM   3831 C CG1  A VAL   B 1 3   ? 48.920 -11.764 -17.744 0.70 22.72 ?  3   VAL   B CG1  1 
ATOM   3832 C CG1  B VAL   B 1 3   ? 48.834 -11.632 -17.546 0.30 21.50 ?  3   VAL   B CG1  1 
ATOM   3833 C CG2  A VAL   B 1 3   ? 46.513 -11.852 -18.471 0.70 23.01 ?  3   VAL   B CG2  1 
ATOM   3834 C CG2  B VAL   B 1 3   ? 46.435 -11.672 -18.283 0.30 21.44 ?  3   VAL   B CG2  1 
ATOM   3835 H H    A VAL   B 1 3   ? 47.696 -13.438 -20.478 0.70 26.25 ?  3   VAL   B H    1 
ATOM   3836 H H    B VAL   B 1 3   ? 47.688 -13.113 -20.313 0.30 27.48 ?  3   VAL   B H    1 
ATOM   3837 H HA   A VAL   B 1 3   ? 48.639 -14.410 -18.130 0.70 24.78 ?  3   VAL   B HA   1 
ATOM   3838 H HA   B VAL   B 1 3   ? 48.525 -14.257 -17.996 0.30 25.16 ?  3   VAL   B HA   1 
ATOM   3839 H HB   A VAL   B 1 3   ? 47.393 -12.843 -16.914 0.70 26.72 ?  3   VAL   B HB   1 
ATOM   3840 H HB   B VAL   B 1 3   ? 47.296 -12.713 -16.755 0.30 25.58 ?  3   VAL   B HB   1 
ATOM   3841 H HG11 A VAL   B 1 3   ? 48.724 -10.959 -17.242 0.70 27.26 ?  3   VAL   B HG11 1 
ATOM   3842 H HG11 B VAL   B 1 3   ? 48.642 -10.838 -17.022 0.30 25.80 ?  3   VAL   B HG11 1 
ATOM   3843 H HG12 A VAL   B 1 3   ? 49.618 -12.271 -17.298 0.70 27.26 ?  3   VAL   B HG12 1 
ATOM   3844 H HG12 B VAL   B 1 3   ? 49.523 -12.158 -17.111 0.30 25.80 ?  3   VAL   B HG12 1 
ATOM   3845 H HG13 A VAL   B 1 3   ? 49.200 -11.537 -18.644 0.70 27.26 ?  3   VAL   B HG13 1 
ATOM   3846 H HG13 B VAL   B 1 3   ? 49.121 -11.380 -18.437 0.30 25.80 ?  3   VAL   B HG13 1 
ATOM   3847 H HG21 A VAL   B 1 3   ? 46.464 -10.971 -18.073 0.70 27.61 ?  3   VAL   B HG21 1 
ATOM   3848 H HG21 B VAL   B 1 3   ? 46.392 -10.801 -17.862 0.30 25.72 ?  3   VAL   B HG21 1 
ATOM   3849 H HG22 A VAL   B 1 3   ? 46.684 -11.780 -19.422 0.70 27.61 ?  3   VAL   B HG22 1 
ATOM   3850 H HG22 B VAL   B 1 3   ? 46.608 -11.574 -19.232 0.30 25.72 ?  3   VAL   B HG22 1 
ATOM   3851 H HG23 A VAL   B 1 3   ? 45.684 -12.332 -18.318 0.70 27.61 ?  3   VAL   B HG23 1 
ATOM   3852 H HG23 B VAL   B 1 3   ? 45.600 -12.148 -18.147 0.30 25.72 ?  3   VAL   B HG23 1 
ATOM   3853 N N    . ASN   B 1 4   ? 46.450 -15.483 -17.484 1.00 17.32 ?  4   ASN   B N    1 
ATOM   3854 C CA   . ASN   B 1 4   ? 45.318 -16.406 -17.369 1.00 16.12 ?  4   ASN   B CA   1 
ATOM   3855 C C    . ASN   B 1 4   ? 45.269 -17.370 -18.552 1.00 16.58 ?  4   ASN   B C    1 
ATOM   3856 O O    . ASN   B 1 4   ? 44.208 -17.632 -19.119 1.00 17.42 ?  4   ASN   B O    1 
ATOM   3857 C CB   . ASN   B 1 4   ? 43.990 -15.659 -17.203 1.00 15.57 ?  4   ASN   B CB   1 
ATOM   3858 C CG   . ASN   B 1 4   ? 43.943 -14.836 -15.930 1.00 14.80 ?  4   ASN   B CG   1 
ATOM   3859 O OD1  . ASN   B 1 4   ? 44.230 -15.340 -14.847 1.00 14.55 ?  4   ASN   B OD1  1 
ATOM   3860 N ND2  . ASN   B 1 4   ? 43.585 -13.560 -16.054 1.00 15.95 ?  4   ASN   B ND2  1 
ATOM   3861 H H    A ASN   B 1 4   ? 46.928 -15.421 -16.772 0.70 20.78 ?  4   ASN   B H    1 
ATOM   3862 H H    B ASN   B 1 4   ? 47.012 -15.545 -16.836 0.30 20.78 ?  4   ASN   B H    1 
ATOM   3863 H HA   . ASN   B 1 4   ? 45.451 -16.939 -16.568 1.00 19.34 ?  4   ASN   B HA   1 
ATOM   3864 H HB2  . ASN   B 1 4   ? 43.867 -15.061 -17.954 1.00 18.68 ?  4   ASN   B HB2  1 
ATOM   3865 H HB3  . ASN   B 1 4   ? 43.269 -16.309 -17.172 1.00 18.68 ?  4   ASN   B HB3  1 
ATOM   3866 H HD21 . ASN   B 1 4   ? 43.546 -13.054 -15.358 1.00 19.15 ?  4   ASN   B HD21 1 
ATOM   3867 H HD22 . ASN   B 1 4   ? 43.393 -13.238 -16.828 1.00 19.15 ?  4   ASN   B HD22 1 
ATOM   3868 N N    . SER   B 1 5   ? 46.433 -17.898 -18.933 1.00 17.56 ?  5   SER   B N    1 
ATOM   3869 C CA   . SER   B 1 5   ? 46.529 -18.821 -20.063 1.00 20.21 ?  5   SER   B CA   1 
ATOM   3870 C C    . SER   B 1 5   ? 46.527 -20.255 -19.542 1.00 21.46 ?  5   SER   B C    1 
ATOM   3871 O O    . SER   B 1 5   ? 47.542 -20.947 -19.513 1.00 23.21 ?  5   SER   B O    1 
ATOM   3872 C CB   . SER   B 1 5   ? 47.775 -18.524 -20.891 1.00 21.99 ?  5   SER   B CB   1 
ATOM   3873 O OG   . SER   B 1 5   ? 48.959 -18.749 -20.142 1.00 24.81 ?  5   SER   B OG   1 
ATOM   3874 H H    . SER   B 1 5   ? 47.190 -17.741 -18.549 1.00 21.08 ?  5   SER   B H    1 
ATOM   3875 H HA   . SER   B 1 5   ? 45.755 -18.711 -20.631 1.00 24.25 ?  5   SER   B HA   1 
ATOM   3876 H HB2  . SER   B 1 5   ? 47.771 -19.096 -21.675 1.00 26.39 ?  5   SER   B HB2  1 
ATOM   3877 H HB3  . SER   B 1 5   ? 47.735 -17.596 -21.160 1.00 26.39 ?  5   SER   B HB3  1 
ATOM   3878 H HG   . SER   B 1 5   ? 49.021 -19.561 -19.939 1.00 29.77 ?  5   SER   B HG   1 
ATOM   3879 N N    . PHE   B 1 6   ? 45.347 -20.678 -19.105 1.00 21.52 ?  6   PHE   B N    1 
ATOM   3880 C CA   . PHE   B 1 6   ? 45.156 -22.026 -18.596 1.00 20.79 ?  6   PHE   B CA   1 
ATOM   3881 C C    . PHE   B 1 6   ? 45.079 -23.004 -19.757 1.00 23.79 ?  6   PHE   B C    1 
ATOM   3882 O O    . PHE   B 1 6   ? 44.419 -22.737 -20.764 1.00 25.63 ?  6   PHE   B O    1 
ATOM   3883 C CB   . PHE   B 1 6   ? 43.866 -22.092 -17.778 1.00 18.95 ?  6   PHE   B CB   1 
ATOM   3884 C CG   . PHE   B 1 6   ? 43.879 -21.222 -16.552 1.00 17.13 ?  6   PHE   B CG   1 
ATOM   3885 C CD1  . PHE   B 1 6   ? 44.394 -21.697 -15.362 1.00 16.12 ?  6   PHE   B CD1  1 
ATOM   3886 C CD2  . PHE   B 1 6   ? 43.380 -19.926 -16.595 1.00 16.64 ?  6   PHE   B CD2  1 
ATOM   3887 C CE1  . PHE   B 1 6   ? 44.404 -20.901 -14.227 1.00 15.59 ?  6   PHE   B CE1  1 
ATOM   3888 C CE2  . PHE   B 1 6   ? 43.397 -19.120 -15.468 1.00 16.84 ?  6   PHE   B CE2  1 
ATOM   3889 C CZ   . PHE   B 1 6   ? 43.912 -19.602 -14.285 1.00 15.93 ?  6   PHE   B CZ   1 
ATOM   3890 H H    . PHE   B 1 6   ? 44.634 -20.202 -19.095 1.00 25.82 ?  6   PHE   B H    1 
ATOM   3891 H HA   . PHE   B 1 6   ? 45.897 -22.278 -18.028 1.00 24.94 ?  6   PHE   B HA   1 
ATOM   3892 H HB2  . PHE   B 1 6   ? 43.124 -21.806 -18.335 1.00 22.74 ?  6   PHE   B HB2  1 
ATOM   3893 H HB3  . PHE   B 1 6   ? 43.722 -23.008 -17.488 1.00 22.74 ?  6   PHE   B HB3  1 
ATOM   3894 H HD1  . PHE   B 1 6   ? 44.736 -22.560 -15.317 1.00 19.35 ?  6   PHE   B HD1  1 
ATOM   3895 H HD2  . PHE   B 1 6   ? 43.029 -19.597 -17.390 1.00 19.97 ?  6   PHE   B HD2  1 
ATOM   3896 H HE1  . PHE   B 1 6   ? 44.764 -21.223 -13.430 1.00 18.70 ?  6   PHE   B HE1  1 
ATOM   3897 H HE2  . PHE   B 1 6   ? 43.054 -18.255 -15.510 1.00 20.21 ?  6   PHE   B HE2  1 
ATOM   3898 H HZ   . PHE   B 1 6   ? 43.921 -19.066 -13.526 1.00 19.12 ?  6   PHE   B HZ   1 
ATOM   3899 N N    . SER   B 1 7   ? 45.766 -24.137 -19.614 1.00 24.33 ?  7   SER   B N    1 
ATOM   3900 C CA   . SER   B 1 7   ? 45.851 -25.125 -20.679 1.00 26.41 ?  7   SER   B CA   1 
ATOM   3901 C C    . SER   B 1 7   ? 45.815 -26.532 -20.099 1.00 25.52 ?  7   SER   B C    1 
ATOM   3902 O O    . SER   B 1 7   ? 46.408 -26.801 -19.050 1.00 26.53 ?  7   SER   B O    1 
ATOM   3903 C CB   . SER   B 1 7   ? 47.139 -24.935 -21.494 1.00 28.91 ?  7   SER   B CB   1 
ATOM   3904 O OG   . SER   B 1 7   ? 47.172 -25.814 -22.603 1.00 31.05 ?  7   SER   B OG   1 
ATOM   3905 H H    . SER   B 1 7   ? 46.200 -24.354 -18.900 1.00 29.20 ?  7   SER   B H    1 
ATOM   3906 H HA   . SER   B 1 7   ? 45.095 -25.023 -21.275 1.00 31.70 ?  7   SER   B HA   1 
ATOM   3907 H HB2  . SER   B 1 7   ? 47.176 -24.019 -21.817 1.00 34.70 ?  7   SER   B HB2  1 
ATOM   3908 H HB3  . SER   B 1 7   ? 47.904 -25.113 -20.923 1.00 34.70 ?  7   SER   B HB3  1 
ATOM   3909 H HG   . SER   B 1 7   ? 47.881 -25.702 -23.038 1.00 37.26 ?  7   SER   B HG   1 
ATOM   3910 N N    A GLY   B 1 8   ? 45.109 -27.426 -20.789 0.70 25.22 ?  8   GLY   B N    1 
ATOM   3911 N N    B GLY   B 1 8   ? 45.115 -27.426 -20.792 0.30 25.03 ?  8   GLY   B N    1 
ATOM   3912 C CA   A GLY   B 1 8   ? 45.076 -28.820 -20.400 0.70 24.60 ?  8   GLY   B CA   1 
ATOM   3913 C CA   B GLY   B 1 8   ? 45.078 -28.817 -20.397 0.30 24.39 ?  8   GLY   B CA   1 
ATOM   3914 C C    A GLY   B 1 8   ? 44.118 -29.155 -19.283 0.70 23.76 ?  8   GLY   B C    1 
ATOM   3915 C C    B GLY   B 1 8   ? 44.145 -29.132 -19.253 0.30 23.67 ?  8   GLY   B C    1 
ATOM   3916 O O    A GLY   B 1 8   ? 44.239 -30.229 -18.683 0.70 24.75 ?  8   GLY   B O    1 
ATOM   3917 O O    B GLY   B 1 8   ? 44.321 -30.164 -18.596 0.30 24.19 ?  8   GLY   B O    1 
ATOM   3918 H H    A GLY   B 1 8   ? 44.646 -27.240 -21.488 0.70 30.26 ?  8   GLY   B H    1 
ATOM   3919 H H    B GLY   B 1 8   ? 44.656 -27.243 -21.494 0.30 30.03 ?  8   GLY   B H    1 
ATOM   3920 H HA2  A GLY   B 1 8   ? 44.830 -29.352 -21.171 0.70 29.52 ?  8   GLY   B HA2  1 
ATOM   3921 H HA2  B GLY   B 1 8   ? 44.808 -29.350 -21.160 0.30 29.27 ?  8   GLY   B HA2  1 
ATOM   3922 H HA3  A GLY   B 1 8   ? 45.962 -29.088 -20.118 0.70 29.52 ?  8   GLY   B HA3  1 
ATOM   3923 H HA3  B GLY   B 1 8   ? 45.968 -29.094 -20.135 0.30 29.27 ?  8   GLY   B HA3  1 
ATOM   3924 N N    . TYR   B 1 9   ? 43.154 -28.286 -18.995 1.00 22.57 ?  9   TYR   B N    1 
ATOM   3925 C CA   . TYR   B 1 9   ? 42.194 -28.546 -17.935 1.00 20.35 ?  9   TYR   B CA   1 
ATOM   3926 C C    . TYR   B 1 9   ? 41.005 -29.329 -18.464 1.00 19.73 ?  9   TYR   B C    1 
ATOM   3927 O O    . TYR   B 1 9   ? 40.593 -29.182 -19.619 1.00 21.43 ?  9   TYR   B O    1 
ATOM   3928 C CB   . TYR   B 1 9   ? 41.698 -27.250 -17.299 1.00 19.83 ?  9   TYR   B CB   1 
ATOM   3929 C CG   . TYR   B 1 9   ? 42.715 -26.635 -16.369 1.00 19.13 ?  9   TYR   B CG   1 
ATOM   3930 C CD1  . TYR   B 1 9   ? 43.830 -25.983 -16.872 1.00 19.57 ?  9   TYR   B CD1  1 
ATOM   3931 C CD2  . TYR   B 1 9   ? 42.574 -26.722 -14.992 1.00 18.41 ?  9   TYR   B CD2  1 
ATOM   3932 C CE1  . TYR   B 1 9   ? 44.779 -25.431 -16.031 1.00 19.72 ?  9   TYR   B CE1  1 
ATOM   3933 C CE2  . TYR   B 1 9   ? 43.516 -26.173 -14.141 1.00 18.62 ?  9   TYR   B CE2  1 
ATOM   3934 C CZ   . TYR   B 1 9   ? 44.617 -25.523 -14.668 1.00 19.53 ?  9   TYR   B CZ   1 
ATOM   3935 O OH   . TYR   B 1 9   ? 45.564 -24.979 -13.835 1.00 20.13 ?  9   TYR   B OH   1 
ATOM   3936 H H    A TYR   B 1 9   ? 43.023 -27.544 -19.411 0.70 27.08 ?  9   TYR   B H    1 
ATOM   3937 H H    B TYR   B 1 9   ? 43.006 -27.558 -19.429 0.30 27.08 ?  9   TYR   B H    1 
ATOM   3938 H HA   . TYR   B 1 9   ? 42.612 -29.075 -17.242 1.00 24.42 ?  9   TYR   B HA   1 
ATOM   3939 H HB2  . TYR   B 1 9   ? 41.495 -26.601 -17.995 1.00 23.80 ?  9   TYR   B HB2  1 
ATOM   3940 H HB3  . TYR   B 1 9   ? 40.905 -27.443 -16.782 1.00 23.80 ?  9   TYR   B HB3  1 
ATOM   3941 H HD1  . TYR   B 1 9   ? 43.945 -25.919 -17.794 1.00 23.48 ?  9   TYR   B HD1  1 
ATOM   3942 H HD2  . TYR   B 1 9   ? 41.831 -27.161 -14.635 1.00 22.10 ?  9   TYR   B HD2  1 
ATOM   3943 H HE1  . TYR   B 1 9   ? 45.517 -25.000 -16.386 1.00 23.67 ?  9   TYR   B HE1  1 
ATOM   3944 H HE2  . TYR   B 1 9   ? 43.402 -26.243 -13.219 1.00 22.34 ?  9   TYR   B HE2  1 
ATOM   3945 H HH   . TYR   B 1 9   ? 46.166 -24.624 -14.292 1.00 24.15 ?  9   TYR   B HH   1 
ATOM   3946 N N    . LEU   B 1 10  ? 40.462 -30.172 -17.595 1.00 17.77 ?  10  LEU   B N    1 
ATOM   3947 C CA   . LEU   B 1 10  ? 39.255 -30.928 -17.879 1.00 17.68 ?  10  LEU   B CA   1 
ATOM   3948 C C    . LEU   B 1 10  ? 38.064 -30.161 -17.317 1.00 17.30 ?  10  LEU   B C    1 
ATOM   3949 O O    . LEU   B 1 10  ? 38.075 -29.748 -16.154 1.00 17.01 ?  10  LEU   B O    1 
ATOM   3950 C CB   . LEU   B 1 10  ? 39.359 -32.303 -17.218 1.00 18.60 ?  10  LEU   B CB   1 
ATOM   3951 C CG   . LEU   B 1 10  ? 38.220 -33.260 -17.546 1.00 20.27 ?  10  LEU   B CG   1 
ATOM   3952 C CD1  . LEU   B 1 10  ? 38.335 -33.754 -18.981 1.00 21.48 ?  10  LEU   B CD1  1 
ATOM   3953 C CD2  . LEU   B 1 10  ? 38.187 -34.417 -16.565 1.00 21.34 ?  10  LEU   B CD2  1 
ATOM   3954 H H    . LEU   B 1 10  ? 40.782 -30.327 -16.808 1.00 21.32 ?  10  LEU   B H    1 
ATOM   3955 H HA   . LEU   B 1 10  ? 39.143 -31.039 -18.833 1.00 21.22 ?  10  LEU   B HA   1 
ATOM   3956 H HB2  . LEU   B 1 10  ? 40.186 -32.723 -17.506 1.00 22.32 ?  10  LEU   B HB2  1 
ATOM   3957 H HB3  . LEU   B 1 10  ? 39.374 -32.186 -16.254 1.00 22.32 ?  10  LEU   B HB3  1 
ATOM   3958 H HG   . LEU   B 1 10  ? 37.380 -32.784 -17.465 1.00 24.33 ?  10  LEU   B HG   1 
ATOM   3959 H HD11 . LEU   B 1 10  ? 37.633 -34.401 -19.146 1.00 25.78 ?  10  LEU   B HD11 1 
ATOM   3960 H HD12 . LEU   B 1 10  ? 38.236 -32.998 -19.582 1.00 25.78 ?  10  LEU   B HD12 1 
ATOM   3961 H HD13 . LEU   B 1 10  ? 39.203 -34.165 -19.104 1.00 25.78 ?  10  LEU   B HD13 1 
ATOM   3962 H HD21 . LEU   B 1 10  ? 37.456 -35.006 -16.805 1.00 25.60 ?  10  LEU   B HD21 1 
ATOM   3963 H HD22 . LEU   B 1 10  ? 39.029 -34.890 -16.612 1.00 25.60 ?  10  LEU   B HD22 1 
ATOM   3964 H HD23 . LEU   B 1 10  ? 38.051 -34.063 -15.672 1.00 25.60 ?  10  LEU   B HD23 1 
ATOM   3965 N N    . LYS   B 1 11  ? 37.045 -29.970 -18.145 1.00 18.20 ?  11  LYS   B N    1 
ATOM   3966 C CA   . LYS   B 1 11  ? 35.847 -29.255 -17.732 1.00 20.12 ?  11  LYS   B CA   1 
ATOM   3967 C C    . LYS   B 1 11  ? 34.961 -30.184 -16.910 1.00 19.48 ?  11  LYS   B C    1 
ATOM   3968 O O    . LYS   B 1 11  ? 34.580 -31.263 -17.378 1.00 21.14 ?  11  LYS   B O    1 
ATOM   3969 C CB   . LYS   B 1 11  ? 35.108 -28.764 -18.974 1.00 23.83 ?  11  LYS   B CB   1 
ATOM   3970 C CG   . LYS   B 1 11  ? 33.943 -27.827 -18.706 1.00 27.25 ?  11  LYS   B CG   1 
ATOM   3971 C CD   . LYS   B 1 11  ? 33.170 -27.556 -19.993 1.00 30.07 ?  11  LYS   B CD   1 
ATOM   3972 C CE   . LYS   B 1 11  ? 32.149 -26.446 -19.816 1.00 32.17 ?  11  LYS   B CE   1 
ATOM   3973 N NZ   . LYS   B 1 11  ? 32.802 -25.125 -19.610 1.00 33.53 ?  11  LYS   B NZ   1 
ATOM   3974 H H    . LYS   B 1 11  ? 37.018 -30.256 -18.955 1.00 21.84 ?  11  LYS   B H    1 
ATOM   3975 H HA   . LYS   B 1 11  ? 36.090 -28.492 -17.186 1.00 24.15 ?  11  LYS   B HA   1 
ATOM   3976 H HB2  . LYS   B 1 11  ? 35.739 -28.289 -19.538 1.00 28.60 ?  11  LYS   B HB2  1 
ATOM   3977 H HB3  . LYS   B 1 11  ? 34.761 -29.533 -19.452 1.00 28.60 ?  11  LYS   B HB3  1 
ATOM   3978 H HG2  . LYS   B 1 11  ? 33.338 -28.237 -18.068 1.00 32.70 ?  11  LYS   B HG2  1 
ATOM   3979 H HG3  . LYS   B 1 11  ? 34.277 -26.984 -18.365 1.00 32.70 ?  11  LYS   B HG3  1 
ATOM   3980 H HD2  . LYS   B 1 11  ? 33.792 -27.288 -20.689 1.00 36.08 ?  11  LYS   B HD2  1 
ATOM   3981 H HD3  . LYS   B 1 11  ? 32.699 -28.362 -20.259 1.00 36.08 ?  11  LYS   B HD3  1 
ATOM   3982 H HE2  . LYS   B 1 11  ? 31.595 -26.391 -20.611 1.00 38.61 ?  11  LYS   B HE2  1 
ATOM   3983 H HE3  . LYS   B 1 11  ? 31.601 -26.642 -19.040 1.00 38.61 ?  11  LYS   B HE3  1 
ATOM   3984 H HZ1  . LYS   B 1 11  ? 32.184 -24.488 -19.538 1.00 40.23 ?  11  LYS   B HZ1  1 
ATOM   3985 H HZ2  . LYS   B 1 11  ? 33.292 -25.140 -18.868 1.00 40.23 ?  11  LYS   B HZ2  1 
ATOM   3986 H HZ3  . LYS   B 1 11  ? 33.330 -24.937 -20.302 1.00 40.23 ?  11  LYS   B HZ3  1 
ATOM   3987 N N    . LEU   B 1 12  ? 34.627 -29.767 -15.689 1.00 18.15 ?  12  LEU   B N    1 
ATOM   3988 C CA   . LEU   B 1 12  ? 33.667 -30.473 -14.849 1.00 17.65 ?  12  LEU   B CA   1 
ATOM   3989 C C    . LEU   B 1 12  ? 32.275 -29.867 -14.933 1.00 17.69 ?  12  LEU   B C    1 
ATOM   3990 O O    . LEU   B 1 12  ? 31.291 -30.584 -15.105 1.00 18.19 ?  12  LEU   B O    1 
ATOM   3991 C CB   . LEU   B 1 12  ? 34.127 -30.485 -13.389 1.00 17.08 ?  12  LEU   B CB   1 
ATOM   3992 C CG   . LEU   B 1 12  ? 35.463 -31.163 -13.113 1.00 17.26 ?  12  LEU   B CG   1 
ATOM   3993 C CD1  . LEU   B 1 12  ? 35.767 -31.106 -11.632 1.00 17.29 ?  12  LEU   B CD1  1 
ATOM   3994 C CD2  . LEU   B 1 12  ? 35.462 -32.603 -13.612 1.00 17.89 ?  12  LEU   B CD2  1 
ATOM   3995 H H    . LEU   B 1 12  ? 34.947 -29.061 -15.321 1.00 21.78 ?  12  LEU   B H    1 
ATOM   3996 H HA   . LEU   B 1 12  ? 33.597 -31.392 -15.154 1.00 21.18 ?  12  LEU   B HA   1 
ATOM   3997 H HB2  . LEU   B 1 12  ? 34.195 -29.569 -13.087 1.00 20.49 ?  12  LEU   B HB2  1 
ATOM   3998 H HB3  . LEU   B 1 12  ? 33.451 -30.949 -12.865 1.00 20.49 ?  12  LEU   B HB3  1 
ATOM   3999 H HG   . LEU   B 1 12  ? 36.160 -30.684 -13.586 1.00 20.71 ?  12  LEU   B HG   1 
ATOM   4000 H HD11 . LEU   B 1 12  ? 36.620 -31.540 -11.470 1.00 20.75 ?  12  LEU   B HD11 1 
ATOM   4001 H HD12 . LEU   B 1 12  ? 35.807 -30.180 -11.353 1.00 20.75 ?  12  LEU   B HD12 1 
ATOM   4002 H HD13 . LEU   B 1 12  ? 35.065 -31.569 -11.147 1.00 20.75 ?  12  LEU   B HD13 1 
ATOM   4003 H HD21 . LEU   B 1 12  ? 36.263 -33.045 -13.296 1.00 21.46 ?  12  LEU   B HD21 1 
ATOM   4004 H HD22 . LEU   B 1 12  ? 34.675 -33.055 -13.270 1.00 21.46 ?  12  LEU   B HD22 1 
ATOM   4005 H HD23 . LEU   B 1 12  ? 35.445 -32.602 -14.584 1.00 21.46 ?  12  LEU   B HD23 1 
ATOM   4006 N N    . THR   B 1 13  ? 32.180 -28.551 -14.800 1.00 17.52 ?  13  THR   B N    1 
ATOM   4007 C CA   . THR   B 1 13  ? 30.951 -27.803 -15.002 1.00 17.55 ?  13  THR   B CA   1 
ATOM   4008 C C    . THR   B 1 13  ? 31.285 -26.601 -15.880 1.00 19.33 ?  13  THR   B C    1 
ATOM   4009 O O    . THR   B 1 13  ? 32.432 -26.406 -16.300 1.00 20.37 ?  13  THR   B O    1 
ATOM   4010 C CB   . THR   B 1 13  ? 30.357 -27.335 -13.670 1.00 17.33 ?  13  THR   B CB   1 
ATOM   4011 O OG1  . THR   B 1 13  ? 31.203 -26.313 -13.121 1.00 17.06 ?  13  THR   B OG1  1 
ATOM   4012 C CG2  . THR   B 1 13  ? 30.242 -28.496 -12.682 1.00 17.95 ?  13  THR   B CG2  1 
ATOM   4013 H H    . THR   B 1 13  ? 32.843 -28.049 -14.581 1.00 21.03 ?  13  THR   B H    1 
ATOM   4014 H HA   . THR   B 1 13  ? 30.294 -28.359 -15.451 1.00 21.06 ?  13  THR   B HA   1 
ATOM   4015 H HB   . THR   B 1 13  ? 29.466 -26.973 -13.819 1.00 20.80 ?  13  THR   B HB   1 
ATOM   4016 H HG1  . THR   B 1 13  ? 30.901 -25.551 -13.323 1.00 20.48 ?  13  THR   B HG1  1 
ATOM   4017 H HG21 . THR   B 1 13  ? 29.720 -28.227 -11.910 1.00 21.54 ?  13  THR   B HG21 1 
ATOM   4018 H HG22 . THR   B 1 13  ? 29.804 -29.251 -13.108 1.00 21.54 ?  13  THR   B HG22 1 
ATOM   4019 H HG23 . THR   B 1 13  ? 31.124 -28.770 -12.387 1.00 21.54 ?  13  THR   B HG23 1 
ATOM   4020 N N    A ASP   B 1 14  ? 30.272 -25.778 -16.146 0.70 20.42 ?  14  ASP   B N    1 
ATOM   4021 N N    B ASP   B 1 14  ? 30.275 -25.766 -16.138 0.30 20.14 ?  14  ASP   B N    1 
ATOM   4022 C CA   A ASP   B 1 14  ? 30.486 -24.614 -16.999 0.70 22.02 ?  14  ASP   B CA   1 
ATOM   4023 C CA   B ASP   B 1 14  ? 30.478 -24.608 -17.003 0.30 20.92 ?  14  ASP   B CA   1 
ATOM   4024 C C    A ASP   B 1 14  ? 31.589 -23.708 -16.463 0.70 20.14 ?  14  ASP   B C    1 
ATOM   4025 C C    B ASP   B 1 14  ? 31.485 -23.615 -16.441 0.30 19.32 ?  14  ASP   B C    1 
ATOM   4026 O O    A ASP   B 1 14  ? 32.257 -23.021 -17.246 0.70 21.38 ?  14  ASP   B O    1 
ATOM   4027 O O    B ASP   B 1 14  ? 31.955 -22.745 -17.184 0.30 19.66 ?  14  ASP   B O    1 
ATOM   4028 C CB   A ASP   B 1 14  ? 29.183 -23.829 -17.153 0.70 25.35 ?  14  ASP   B CB   1 
ATOM   4029 C CB   B ASP   B 1 14  ? 29.155 -23.882 -17.246 0.30 23.10 ?  14  ASP   B CB   1 
ATOM   4030 C CG   A ASP   B 1 14  ? 28.209 -24.490 -18.103 0.70 28.68 ?  14  ASP   B CG   1 
ATOM   4031 C CG   B ASP   B 1 14  ? 28.278 -24.595 -18.256 0.30 25.06 ?  14  ASP   B CG   1 
ATOM   4032 O OD1  A ASP   B 1 14  ? 28.583 -25.482 -18.769 0.70 30.00 ?  14  ASP   B OD1  1 
ATOM   4033 O OD1  B ASP   B 1 14  ? 28.831 -25.231 -19.177 0.30 25.68 ?  14  ASP   B OD1  1 
ATOM   4034 O OD2  A ASP   B 1 14  ? 27.058 -24.015 -18.176 0.70 29.97 -1 14  ASP   B OD2  1 
ATOM   4035 O OD2  B ASP   B 1 14  ? 27.038 -24.525 -18.129 0.30 25.85 -1 14  ASP   B OD2  1 
ATOM   4036 H H    A ASP   B 1 14  ? 29.471 -25.860 -15.839 0.70 24.50 ?  14  ASP   B H    1 
ATOM   4037 H H    B ASP   B 1 14  ? 29.477 -25.844 -15.826 0.30 24.16 ?  14  ASP   B H    1 
ATOM   4038 H HA   A ASP   B 1 14  ? 30.758 -24.913 -17.876 0.70 26.42 ?  14  ASP   B HA   1 
ATOM   4039 H HA   B ASP   B 1 14  ? 30.808 -24.919 -17.860 0.30 25.10 ?  14  ASP   B HA   1 
ATOM   4040 H HB2  A ASP   B 1 14  ? 28.740 -23.767 -16.294 0.70 30.41 ?  14  ASP   B HB2  1 
ATOM   4041 H HB2  B ASP   B 1 14  ? 28.669 -23.824 -16.408 0.30 27.72 ?  14  ASP   B HB2  1 
ATOM   4042 H HB3  A ASP   B 1 14  ? 29.381 -22.942 -17.492 0.70 30.41 ?  14  ASP   B HB3  1 
ATOM   4043 H HB3  B ASP   B 1 14  ? 29.348 -22.986 -17.576 0.30 27.72 ?  14  ASP   B HB3  1 
ATOM   4044 N N    . ASN   B 1 15  ? 31.804 -23.696 -15.147 1.00 17.61 ?  15  ASN   B N    1 
ATOM   4045 C CA   . ASN   B 1 15  ? 32.763 -22.776 -14.541 1.00 15.70 ?  15  ASN   B CA   1 
ATOM   4046 C C    . ASN   B 1 15  ? 33.858 -23.430 -13.707 1.00 14.43 ?  15  ASN   B C    1 
ATOM   4047 O O    . ASN   B 1 15  ? 34.706 -22.703 -13.179 1.00 14.72 ?  15  ASN   B O    1 
ATOM   4048 C CB   . ASN   B 1 15  ? 32.048 -21.722 -13.679 1.00 15.69 ?  15  ASN   B CB   1 
ATOM   4049 C CG   . ASN   B 1 15  ? 31.428 -22.321 -12.438 1.00 15.64 ?  15  ASN   B CG   1 
ATOM   4050 O OD1  . ASN   B 1 15  ? 30.483 -23.121 -12.525 1.00 16.98 ?  15  ASN   B OD1  1 
ATOM   4051 N ND2  . ASN   B 1 15  ? 31.954 -21.970 -11.279 1.00 14.68 ?  15  ASN   B ND2  1 
ATOM   4052 H H    A ASN   B 1 15  ? 31.405 -24.212 -14.584 0.70 21.13 ?  15  ASN   B H    1 
ATOM   4053 H H    B ASN   B 1 15  ? 31.451 -24.254 -14.594 0.30 21.13 ?  15  ASN   B H    1 
ATOM   4054 H HA   . ASN   B 1 15  ? 33.209 -22.293 -15.247 1.00 18.84 ?  15  ASN   B HA   1 
ATOM   4055 H HB2  . ASN   B 1 15  ? 32.692 -21.044 -13.403 1.00 18.83 ?  15  ASN   B HB2  1 
ATOM   4056 H HB3  . ASN   B 1 15  ? 31.340 -21.304 -14.199 1.00 18.83 ?  15  ASN   B HB3  1 
ATOM   4057 H HD21 . ASN   B 1 15  ? 31.638 -22.282 -10.542 1.00 17.62 ?  15  ASN   B HD21 1 
ATOM   4058 H HD22 . ASN   B 1 15  ? 32.622 -21.419 -11.252 1.00 17.62 ?  15  ASN   B HD22 1 
ATOM   4059 N N    . VAL   B 1 16  ? 33.877 -24.755 -13.569 1.00 14.21 ?  16  VAL   B N    1 
ATOM   4060 C CA   . VAL   B 1 16  ? 34.874 -25.445 -12.757 1.00 14.02 ?  16  VAL   B CA   1 
ATOM   4061 C C    . VAL   B 1 16  ? 35.671 -26.382 -13.651 1.00 14.05 ?  16  VAL   B C    1 
ATOM   4062 O O    . VAL   B 1 16  ? 35.094 -27.256 -14.316 1.00 15.11 ?  16  VAL   B O    1 
ATOM   4063 C CB   . VAL   B 1 16  ? 34.239 -26.215 -11.584 1.00 14.79 ?  16  VAL   B CB   1 
ATOM   4064 C CG1  . VAL   B 1 16  ? 35.313 -26.947 -10.780 1.00 14.89 ?  16  VAL   B CG1  1 
ATOM   4065 C CG2  . VAL   B 1 16  ? 33.436 -25.267 -10.696 1.00 15.31 ?  16  VAL   B CG2  1 
ATOM   4066 H H    . VAL   B 1 16  ? 33.310 -25.286 -13.940 1.00 17.05 ?  16  VAL   B H    1 
ATOM   4067 H HA   . VAL   B 1 16  ? 35.487 -24.790 -12.382 1.00 16.82 ?  16  VAL   B HA   1 
ATOM   4068 H HB   . VAL   B 1 16  ? 33.627 -26.880 -11.942 1.00 17.74 ?  16  VAL   B HB   1 
ATOM   4069 H HG11 . VAL   B 1 16  ? 34.921 -27.255 -9.946  1.00 17.87 ?  16  VAL   B HG11 1 
ATOM   4070 H HG12 . VAL   B 1 16  ? 35.634 -27.703 -11.292 1.00 17.87 ?  16  VAL   B HG12 1 
ATOM   4071 H HG13 . VAL   B 1 16  ? 36.039 -26.333 -10.595 1.00 17.87 ?  16  VAL   B HG13 1 
ATOM   4072 H HG21 . VAL   B 1 16  ? 33.085 -25.766 -9.941  1.00 18.37 ?  16  VAL   B HG21 1 
ATOM   4073 H HG22 . VAL   B 1 16  ? 34.014 -24.558 -10.386 1.00 18.37 ?  16  VAL   B HG22 1 
ATOM   4074 H HG23 . VAL   B 1 16  ? 32.701 -24.896 -11.213 1.00 18.37 ?  16  VAL   B HG23 1 
ATOM   4075 N N    . TYR   B 1 17  ? 36.997 -26.222 -13.619 1.00 14.39 ?  17  TYR   B N    1 
ATOM   4076 C CA   . TYR   B 1 17  ? 37.946 -26.970 -14.429 1.00 14.78 ?  17  TYR   B CA   1 
ATOM   4077 C C    . TYR   B 1 17  ? 38.995 -27.586 -13.514 1.00 13.92 ?  17  TYR   B C    1 
ATOM   4078 O O    . TYR   B 1 17  ? 39.272 -27.055 -12.435 1.00 14.44 ?  17  TYR   B O    1 
ATOM   4079 C CB   . TYR   B 1 17  ? 38.654 -26.036 -15.422 1.00 17.19 ?  17  TYR   B CB   1 
ATOM   4080 C CG   . TYR   B 1 17  ? 37.727 -25.266 -16.328 1.00 20.26 ?  17  TYR   B CG   1 
ATOM   4081 C CD1  . TYR   B 1 17  ? 37.136 -24.077 -15.912 1.00 21.40 ?  17  TYR   B CD1  1 
ATOM   4082 C CD2  . TYR   B 1 17  ? 37.445 -25.724 -17.606 1.00 22.26 ?  17  TYR   B CD2  1 
ATOM   4083 C CE1  . TYR   B 1 17  ? 36.284 -23.372 -16.744 1.00 22.92 ?  17  TYR   B CE1  1 
ATOM   4084 C CE2  . TYR   B 1 17  ? 36.601 -25.027 -18.446 1.00 23.52 ?  17  TYR   B CE2  1 
ATOM   4085 C CZ   . TYR   B 1 17  ? 36.022 -23.854 -18.010 1.00 23.79 ?  17  TYR   B CZ   1 
ATOM   4086 O OH   . TYR   B 1 17  ? 35.180 -23.159 -18.845 1.00 25.21 ?  17  TYR   B OH   1 
ATOM   4087 H H    . TYR   B 1 17  ? 37.392 -25.643 -13.108 1.00 17.27 ?  17  TYR   B H    1 
ATOM   4088 H HA   . TYR   B 1 17  ? 37.490 -27.672 -14.919 1.00 17.73 ?  17  TYR   B HA   1 
ATOM   4089 H HB2  . TYR   B 1 17  ? 39.186 -25.394 -14.929 1.00 20.63 ?  17  TYR   B HB2  1 
ATOM   4090 H HB3  . TYR   B 1 17  ? 39.226 -26.569 -15.991 1.00 20.63 ?  17  TYR   B HB3  1 
ATOM   4091 H HD1  . TYR   B 1 17  ? 37.311 -23.751 -15.060 1.00 25.68 ?  17  TYR   B HD1  1 
ATOM   4092 H HD2  . TYR   B 1 17  ? 37.827 -26.514 -17.905 1.00 26.71 ?  17  TYR   B HD2  1 
ATOM   4093 H HE1  . TYR   B 1 17  ? 35.892 -22.577 -16.455 1.00 27.51 ?  17  TYR   B HE1  1 
ATOM   4094 H HE2  . TYR   B 1 17  ? 36.413 -25.348 -19.302 1.00 28.23 ?  17  TYR   B HE2  1 
ATOM   4095 H HH   . TYR   B 1 17  ? 35.099 -23.555 -19.581 1.00 30.25 ?  17  TYR   B HH   1 
ATOM   4096 N N    . ILE   B 1 18  ? 39.607 -28.691 -13.948 1.00 13.78 ?  18  ILE   B N    1 
ATOM   4097 C CA   . ILE   B 1 18  ? 40.540 -29.414 -13.088 1.00 13.88 ?  18  ILE   B CA   1 
ATOM   4098 C C    . ILE   B 1 18  ? 41.708 -29.960 -13.903 1.00 14.14 ?  18  ILE   B C    1 
ATOM   4099 O O    . ILE   B 1 18  ? 41.554 -30.355 -15.063 1.00 15.40 ?  18  ILE   B O    1 
ATOM   4100 C CB   . ILE   B 1 18  ? 39.785 -30.513 -12.294 1.00 14.38 ?  18  ILE   B CB   1 
ATOM   4101 C CG1  . ILE   B 1 18  ? 40.633 -31.054 -11.142 1.00 14.43 ?  18  ILE   B CG1  1 
ATOM   4102 C CG2  . ILE   B 1 18  ? 39.300 -31.632 -13.222 1.00 14.86 ?  18  ILE   B CG2  1 
ATOM   4103 C CD1  . ILE   B 1 18  ? 39.820 -31.845 -10.127 1.00 15.82 ?  18  ILE   B CD1  1 
ATOM   4104 H H    . ILE   B 1 18  ? 39.509 -29.033 -14.732 1.00 16.54 ?  18  ILE   B H    1 
ATOM   4105 H HA   . ILE   B 1 18  ? 40.902 -28.792 -12.437 1.00 16.66 ?  18  ILE   B HA   1 
ATOM   4106 H HB   . ILE   B 1 18  ? 38.996 -30.105 -11.904 1.00 17.25 ?  18  ILE   B HB   1 
ATOM   4107 H HG12 . ILE   B 1 18  ? 41.318 -31.632 -11.497 1.00 17.31 ?  18  ILE   B HG12 1 
ATOM   4108 H HG13 . ILE   B 1 18  ? 41.038 -30.301 -10.676 1.00 17.31 ?  18  ILE   B HG13 1 
ATOM   4109 H HG21 . ILE   B 1 18  ? 38.707 -32.215 -12.725 1.00 17.83 ?  18  ILE   B HG21 1 
ATOM   4110 H HG22 . ILE   B 1 18  ? 38.827 -31.233 -13.967 1.00 17.83 ?  18  ILE   B HG22 1 
ATOM   4111 H HG23 . ILE   B 1 18  ? 40.067 -32.129 -13.541 1.00 17.83 ?  18  ILE   B HG23 1 
ATOM   4112 H HD11 . ILE   B 1 18  ? 40.401 -32.121 -9.402  1.00 18.98 ?  18  ILE   B HD11 1 
ATOM   4113 H HD12 . ILE   B 1 18  ? 39.106 -31.283 -9.782  1.00 18.98 ?  18  ILE   B HD12 1 
ATOM   4114 H HD13 . ILE   B 1 18  ? 39.442 -32.625 -10.564 1.00 18.98 ?  18  ILE   B HD13 1 
ATOM   4115 N N    . LYS   B 1 19  ? 42.887 -29.993 -13.277 1.00 14.73 ?  19  LYS   B N    1 
ATOM   4116 C CA   . LYS   B 1 19  ? 44.099 -30.471 -13.929 1.00 15.39 ?  19  LYS   B CA   1 
ATOM   4117 C C    . LYS   B 1 19  ? 44.994 -31.149 -12.903 1.00 15.11 ?  19  LYS   B C    1 
ATOM   4118 O O    . LYS   B 1 19  ? 45.077 -30.712 -11.753 1.00 14.81 ?  19  LYS   B O    1 
ATOM   4119 C CB   . LYS   B 1 19  ? 44.872 -29.311 -14.571 1.00 16.66 ?  19  LYS   B CB   1 
ATOM   4120 C CG   . LYS   B 1 19  ? 46.086 -29.717 -15.390 1.00 18.22 ?  19  LYS   B CG   1 
ATOM   4121 C CD   . LYS   B 1 19  ? 46.800 -28.481 -15.927 1.00 20.23 ?  19  LYS   B CD   1 
ATOM   4122 C CE   . LYS   B 1 19  ? 47.953 -28.848 -16.841 1.00 21.93 ?  19  LYS   B CE   1 
ATOM   4123 N NZ   . LYS   B 1 19  ? 48.720 -27.657 -17.291 1.00 23.12 ?  19  LYS   B NZ   1 
ATOM   4124 H H    . LYS   B 1 19  ? 43.002 -29.732 -12.463 1.00 17.68 ?  19  LYS   B H    1 
ATOM   4125 H HA   . LYS   B 1 19  ? 43.860 -31.114 -14.617 1.00 18.46 ?  19  LYS   B HA   1 
ATOM   4126 H HB2  . LYS   B 1 19  ? 44.268 -28.832 -15.161 1.00 19.99 ?  19  LYS   B HB2  1 
ATOM   4127 H HB3  . LYS   B 1 19  ? 45.173 -28.717 -13.865 1.00 19.99 ?  19  LYS   B HB3  1 
ATOM   4128 H HG2  . LYS   B 1 19  ? 46.699 -30.215 -14.829 1.00 21.86 ?  19  LYS   B HG2  1 
ATOM   4129 H HG3  . LYS   B 1 19  ? 45.795 -30.262 -16.141 1.00 21.86 ?  19  LYS   B HG3  1 
ATOM   4130 H HD2  . LYS   B 1 19  ? 46.167 -27.944 -16.430 1.00 24.27 ?  19  LYS   B HD2  1 
ATOM   4131 H HD3  . LYS   B 1 19  ? 47.151 -27.971 -15.180 1.00 24.27 ?  19  LYS   B HD3  1 
ATOM   4132 H HE2  . LYS   B 1 19  ? 48.556 -29.439 -16.365 1.00 26.31 ?  19  LYS   B HE2  1 
ATOM   4133 H HE3  . LYS   B 1 19  ? 47.599 -29.298 -17.626 1.00 26.31 ?  19  LYS   B HE3  1 
ATOM   4134 H HZ1  . LYS   B 1 19  ? 49.366 -27.907 -17.849 1.00 27.74 ?  19  LYS   B HZ1  1 
ATOM   4135 H HZ2  . LYS   B 1 19  ? 48.179 -27.088 -17.710 1.00 27.74 ?  19  LYS   B HZ2  1 
ATOM   4136 H HZ3  . LYS   B 1 19  ? 49.083 -27.249 -16.590 1.00 27.74 ?  19  LYS   B HZ3  1 
ATOM   4137 N N    . ASN   B 1 20  ? 45.673 -32.209 -13.330 1.00 16.32 ?  20  ASN   B N    1 
ATOM   4138 C CA   . ASN   B 1 20  ? 46.712 -32.838 -12.517 1.00 17.32 ?  20  ASN   B CA   1 
ATOM   4139 C C    . ASN   B 1 20  ? 47.979 -32.010 -12.711 1.00 17.64 ?  20  ASN   B C    1 
ATOM   4140 O O    . ASN   B 1 20  ? 48.618 -32.075 -13.765 1.00 19.60 ?  20  ASN   B O    1 
ATOM   4141 C CB   . ASN   B 1 20  ? 46.892 -34.291 -12.953 1.00 18.65 ?  20  ASN   B CB   1 
ATOM   4142 C CG   . ASN   B 1 20  ? 48.056 -34.990 -12.269 1.00 20.04 ?  20  ASN   B CG   1 
ATOM   4143 O OD1  . ASN   B 1 20  ? 48.724 -35.836 -12.876 1.00 22.22 ?  20  ASN   B OD1  1 
ATOM   4144 N ND2  . ASN   B 1 20  ? 48.290 -34.671 -11.004 1.00 19.77 ?  20  ASN   B ND2  1 
ATOM   4145 H H    . ASN   B 1 20  ? 45.551 -32.585 -14.093 1.00 19.59 ?  20  ASN   B H    1 
ATOM   4146 H HA   . ASN   B 1 20  ? 46.442 -32.817 -11.583 1.00 20.79 ?  20  ASN   B HA   1 
ATOM   4147 H HB2  . ASN   B 1 20  ? 46.084 -34.785 -12.739 1.00 22.38 ?  20  ASN   B HB2  1 
ATOM   4148 H HB3  . ASN   B 1 20  ? 47.048 -34.310 -13.908 1.00 22.38 ?  20  ASN   B HB3  1 
ATOM   4149 H HD21 . ASN   B 1 20  ? 48.942 -35.035 -10.583 1.00 23.72 ?  20  ASN   B HD21 1 
ATOM   4150 H HD22 . ASN   B 1 20  ? 47.797 -34.085 -10.605 1.00 23.72 ?  20  ASN   B HD22 1 
ATOM   4151 N N    . ALA   B 1 21  ? 48.334 -31.207 -11.704 1.00 17.18 ?  21  ALA   B N    1 
ATOM   4152 C CA   . ALA   B 1 21  ? 49.436 -30.267 -11.852 1.00 17.96 ?  21  ALA   B CA   1 
ATOM   4153 C C    . ALA   B 1 21  ? 49.896 -29.781 -10.487 1.00 17.09 ?  21  ALA   B C    1 
ATOM   4154 O O    . ALA   B 1 21  ? 49.148 -29.816 -9.504  1.00 16.95 ?  21  ALA   B O    1 
ATOM   4155 C CB   . ALA   B 1 21  ? 49.029 -29.080 -12.726 1.00 19.16 ?  21  ALA   B CB   1 
ATOM   4156 H H    . ALA   B 1 21  ? 47.948 -31.190 -10.929 1.00 20.62 ?  21  ALA   B H    1 
ATOM   4157 H HA   . ALA   B 1 21  ? 50.175 -30.722 -12.278 1.00 21.55 ?  21  ALA   B HA   1 
ATOM   4158 H HB1  . ALA   B 1 21  ? 49.808 -28.529 -12.873 1.00 22.99 ?  21  ALA   B HB1  1 
ATOM   4159 H HB2  . ALA   B 1 21  ? 48.693 -29.418 -13.570 1.00 22.99 ?  21  ALA   B HB2  1 
ATOM   4160 H HB3  . ALA   B 1 21  ? 48.336 -28.577 -12.271 1.00 22.99 ?  21  ALA   B HB3  1 
ATOM   4161 N N    . ASP   B 1 22  ? 51.155 -29.334 -10.460 1.00 16.41 ?  22  ASP   B N    1 
ATOM   4162 C CA   . ASP   B 1 22  ? 51.767 -28.644 -9.330  1.00 15.86 ?  22  ASP   B CA   1 
ATOM   4163 C C    . ASP   B 1 22  ? 51.365 -27.172 -9.414  1.00 14.52 ?  22  ASP   B C    1 
ATOM   4164 O O    . ASP   B 1 22  ? 51.682 -26.499 -10.400 1.00 14.60 ?  22  ASP   B O    1 
ATOM   4165 C CB   . ASP   B 1 22  ? 53.285 -28.817 -9.482  1.00 17.23 ?  22  ASP   B CB   1 
ATOM   4166 C CG   . ASP   B 1 22  ? 54.112 -28.059 -8.447  1.00 18.91 ?  22  ASP   B CG   1 
ATOM   4167 O OD1  . ASP   B 1 22  ? 53.749 -26.943 -8.042  1.00 19.10 ?  22  ASP   B OD1  1 
ATOM   4168 O OD2  . ASP   B 1 22  ? 55.185 -28.579 -8.067  1.00 21.07 -1 22  ASP   B OD2  1 
ATOM   4169 H H    . ASP   B 1 22  ? 51.699 -29.428 -11.126 1.00 19.69 ?  22  ASP   B H    1 
ATOM   4170 H HA   . ASP   B 1 22  ? 51.474 -29.032 -8.488  1.00 19.03 ?  22  ASP   B HA   1 
ATOM   4171 H HB2  . ASP   B 1 22  ? 53.510 -29.755 -9.406  1.00 20.68 ?  22  ASP   B HB2  1 
ATOM   4172 H HB3  . ASP   B 1 22  ? 53.552 -28.482 -10.352 1.00 20.68 ?  22  ASP   B HB3  1 
ATOM   4173 N N    . ILE   B 1 23  ? 50.651 -26.678 -8.396  1.00 13.93 ?  23  ILE   B N    1 
ATOM   4174 C CA   . ILE   B 1 23  ? 50.058 -25.341 -8.472  1.00 13.06 ?  23  ILE   B CA   1 
ATOM   4175 C C    . ILE   B 1 23  ? 51.112 -24.248 -8.606  1.00 12.95 ?  23  ILE   B C    1 
ATOM   4176 O O    . ILE   B 1 23  ? 50.843 -23.204 -9.208  1.00 12.54 ?  23  ILE   B O    1 
ATOM   4177 C CB   . ILE   B 1 23  ? 49.113 -25.102 -7.279  1.00 13.48 ?  23  ILE   B CB   1 
ATOM   4178 C CG1  . ILE   B 1 23  ? 48.277 -23.835 -7.486  1.00 14.38 ?  23  ILE   B CG1  1 
ATOM   4179 C CG2  . ILE   B 1 23  ? 49.879 -25.055 -5.977  1.00 14.64 ?  23  ILE   B CG2  1 
ATOM   4180 C CD1  . ILE   B 1 23  ? 47.155 -23.674 -6.472  1.00 15.09 ?  23  ILE   B CD1  1 
ATOM   4181 H H    . ILE   B 1 23  ? 50.503 -27.097 -7.660  1.00 16.72 ?  23  ILE   B H    1 
ATOM   4182 H HA   . ILE   B 1 23  ? 49.517 -25.306 -9.273  1.00 15.68 ?  23  ILE   B HA   1 
ATOM   4183 H HB   . ILE   B 1 23  ? 48.499 -25.855 -7.237  1.00 16.18 ?  23  ILE   B HB   1 
ATOM   4184 H HG12 . ILE   B 1 23  ? 48.860 -23.061 -7.415  1.00 17.26 ?  23  ILE   B HG12 1 
ATOM   4185 H HG13 . ILE   B 1 23  ? 47.880 -23.861 -8.375  1.00 17.26 ?  23  ILE   B HG13 1 
ATOM   4186 H HG21 . ILE   B 1 23  ? 49.249 -25.061 -5.240  1.00 17.56 ?  23  ILE   B HG21 1 
ATOM   4187 H HG22 . ILE   B 1 23  ? 50.460 -25.829 -5.923  1.00 17.56 ?  23  ILE   B HG22 1 
ATOM   4188 H HG23 . ILE   B 1 23  ? 50.409 -24.242 -5.953  1.00 17.56 ?  23  ILE   B HG23 1 
ATOM   4189 H HD11 . ILE   B 1 23  ? 46.624 -22.900 -6.711  1.00 18.11 ?  23  ILE   B HD11 1 
ATOM   4190 H HD12 . ILE   B 1 23  ? 46.603 -24.473 -6.490  1.00 18.11 ?  23  ILE   B HD12 1 
ATOM   4191 H HD13 . ILE   B 1 23  ? 47.542 -23.557 -5.593  1.00 18.11 ?  23  ILE   B HD13 1 
ATOM   4192 N N    . VAL   B 1 24  ? 52.305 -24.449 -8.041  1.00 13.27 ?  24  VAL   B N    1 
ATOM   4193 C CA   . VAL   B 1 24  ? 53.384 -23.473 -8.210  1.00 13.84 ?  24  VAL   B CA   1 
ATOM   4194 C C    . VAL   B 1 24  ? 53.839 -23.428 -9.663  1.00 14.21 ?  24  VAL   B C    1 
ATOM   4195 O O    . VAL   B 1 24  ? 53.981 -22.352 -10.258 1.00 14.64 ?  24  VAL   B O    1 
ATOM   4196 C CB   . VAL   B 1 24  ? 54.558 -23.787 -7.261  1.00 14.87 ?  24  VAL   B CB   1 
ATOM   4197 C CG1  . VAL   B 1 24  ? 55.771 -22.909 -7.588  1.00 15.65 ?  24  VAL   B CG1  1 
ATOM   4198 C CG2  . VAL   B 1 24  ? 54.137 -23.599 -5.825  1.00 16.05 ?  24  VAL   B CG2  1 
ATOM   4199 H H    . VAL   B 1 24  ? 52.515 -25.133 -7.562  1.00 15.93 ?  24  VAL   B H    1 
ATOM   4200 H HA   . VAL   B 1 24  ? 53.051 -22.596 -7.979  1.00 16.61 ?  24  VAL   B HA   1 
ATOM   4201 H HB   . VAL   B 1 24  ? 54.823 -24.715 -7.372  1.00 17.84 ?  24  VAL   B HB   1 
ATOM   4202 H HG11 . VAL   B 1 24  ? 56.364 -22.891 -6.819  1.00 18.78 ?  24  VAL   B HG11 1 
ATOM   4203 H HG12 . VAL   B 1 24  ? 56.234 -23.285 -8.351  1.00 18.78 ?  24  VAL   B HG12 1 
ATOM   4204 H HG13 . VAL   B 1 24  ? 55.464 -22.011 -7.789  1.00 18.78 ?  24  VAL   B HG13 1 
ATOM   4205 H HG21 . VAL   B 1 24  ? 54.861 -23.871 -5.241  1.00 19.26 ?  24  VAL   B HG21 1 
ATOM   4206 H HG22 . VAL   B 1 24  ? 53.929 -22.662 -5.679  1.00 19.26 ?  24  VAL   B HG22 1 
ATOM   4207 H HG23 . VAL   B 1 24  ? 53.350 -24.142 -5.652  1.00 19.26 ?  24  VAL   B HG23 1 
ATOM   4208 N N    . GLU   B 1 25  ? 54.094 -24.600 -10.251 1.00 15.13 ?  25  GLU   B N    1 
ATOM   4209 C CA   . GLU   B 1 25  ? 54.491 -24.638 -11.652 1.00 16.67 ?  25  GLU   B CA   1 
ATOM   4210 C C    . GLU   B 1 25  ? 53.386 -24.093 -12.542 1.00 15.44 ?  25  GLU   B C    1 
ATOM   4211 O O    . GLU   B 1 25  ? 53.655 -23.379 -13.517 1.00 16.25 ?  25  GLU   B O    1 
ATOM   4212 C CB   . GLU   B 1 25  ? 54.884 -26.062 -12.047 1.00 20.54 ?  25  GLU   B CB   1 
ATOM   4213 C CG   . GLU   B 1 25  ? 56.185 -26.508 -11.399 1.00 25.63 ?  25  GLU   B CG   1 
ATOM   4214 C CD   . GLU   B 1 25  ? 57.287 -25.460 -11.484 1.00 30.25 ?  25  GLU   B CD   1 
ATOM   4215 O OE1  . GLU   B 1 25  ? 57.664 -25.071 -12.611 1.00 31.97 ?  25  GLU   B OE1  1 
ATOM   4216 O OE2  . GLU   B 1 25  ? 57.769 -25.007 -10.419 1.00 31.63 -1 25  GLU   B OE2  1 
ATOM   4217 H H    . GLU   B 1 25  ? 54.043 -25.370 -9.868  1.00 18.16 ?  25  GLU   B H    1 
ATOM   4218 H HA   . GLU   B 1 25  ? 55.249 -24.053 -11.778 1.00 20.00 ?  25  GLU   B HA   1 
ATOM   4219 H HB2  . GLU   B 1 25  ? 54.184 -26.674 -11.763 1.00 24.65 ?  25  GLU   B HB2  1 
ATOM   4220 H HB3  . GLU   B 1 25  ? 54.991 -26.106 -13.010 1.00 24.65 ?  25  GLU   B HB3  1 
ATOM   4221 H HG2  . GLU   B 1 25  ? 56.033 -26.673 -10.462 1.00 30.76 ?  25  GLU   B HG2  1 
ATOM   4222 H HG3  . GLU   B 1 25  ? 56.497 -27.311 -11.843 1.00 30.76 ?  25  GLU   B HG3  1 
ATOM   4223 N N    . GLU   B 1 26  ? 52.132 -24.398 -12.206 1.00 14.61 ?  26  GLU   B N    1 
ATOM   4224 C CA   . GLU   B 1 26  ? 51.006 -23.868 -12.968 1.00 14.97 ?  26  GLU   B CA   1 
ATOM   4225 C C    . GLU   B 1 26  ? 50.959 -22.350 -12.889 1.00 14.16 ?  26  GLU   B C    1 
ATOM   4226 O O    . GLU   B 1 26  ? 50.766 -21.673 -13.903 1.00 15.44 ?  26  GLU   B O    1 
ATOM   4227 C CB   . GLU   B 1 26  ? 49.692 -24.453 -12.446 1.00 16.87 ?  26  GLU   B CB   1 
ATOM   4228 C CG   . GLU   B 1 26  ? 49.240 -25.728 -13.129 1.00 20.28 ?  26  GLU   B CG   1 
ATOM   4229 C CD   . GLU   B 1 26  ? 48.989 -25.570 -14.625 1.00 21.99 ?  26  GLU   B CD   1 
ATOM   4230 O OE1  . GLU   B 1 26  ? 48.014 -24.909 -15.039 1.00 22.47 ?  26  GLU   B OE1  1 
ATOM   4231 O OE2  . GLU   B 1 26  ? 49.771 -26.143 -15.392 1.00 23.95 -1 26  GLU   B OE2  1 
ATOM   4232 H H    . GLU   B 1 26  ? 51.905 -24.911 -11.546 1.00 17.53 ?  26  GLU   B H    1 
ATOM   4233 H HA   . GLU   B 1 26  ? 51.102 -24.122 -13.896 1.00 17.96 ?  26  GLU   B HA   1 
ATOM   4234 H HB2  . GLU   B 1 26  ? 49.791 -24.652 -11.499 1.00 20.24 ?  26  GLU   B HB2  1 
ATOM   4235 H HB3  . GLU   B 1 26  ? 48.989 -23.792 -12.562 1.00 20.24 ?  26  GLU   B HB3  1 
ATOM   4236 H HG2  . GLU   B 1 26  ? 49.932 -26.388 -13.027 1.00 24.34 ?  26  GLU   B HG2  1 
ATOM   4237 H HG3  . GLU   B 1 26  ? 48.416 -26.030 -12.715 1.00 24.34 ?  26  GLU   B HG3  1 
ATOM   4238 N N    . ALA   B 1 27  ? 51.107 -21.799 -11.684 1.00 13.67 ?  27  ALA   B N    1 
ATOM   4239 C CA   . ALA   B 1 27  ? 51.070 -20.348 -11.538 1.00 14.08 ?  27  ALA   B CA   1 
ATOM   4240 C C    . ALA   B 1 27  ? 52.143 -19.682 -12.390 1.00 14.82 ?  27  ALA   B C    1 
ATOM   4241 O O    . ALA   B 1 27  ? 51.886 -18.669 -13.057 1.00 15.83 ?  27  ALA   B O    1 
ATOM   4242 C CB   . ALA   B 1 27  ? 51.222 -19.967 -10.068 1.00 14.14 ?  27  ALA   B CB   1 
ATOM   4243 H H    . ALA   B 1 27  ? 51.223 -22.235 -10.949 1.00 16.41 ?  27  ALA   B H    1 
ATOM   4244 H HA   . ALA   B 1 27  ? 50.212 -20.024 -11.839 1.00 16.90 ?  27  ALA   B HA   1 
ATOM   4245 H HB1  . ALA   B 1 27  ? 51.192 -19.002 -9.985  1.00 16.97 ?  27  ALA   B HB1  1 
ATOM   4246 H HB2  . ALA   B 1 27  ? 50.490 -20.363 -9.563  1.00 16.97 ?  27  ALA   B HB2  1 
ATOM   4247 H HB3  . ALA   B 1 27  ? 52.068 -20.303 -9.735  1.00 16.97 ?  27  ALA   B HB3  1 
ATOM   4248 N N    . LYS   B 1 28  ? 53.358 -20.232 -12.381 1.00 16.24 ?  28  LYS   B N    1 
ATOM   4249 C CA   . LYS   B 1 28  ? 54.436 -19.617 -13.145 1.00 18.20 ?  28  LYS   B CA   1 
ATOM   4250 C C    . LYS   B 1 28  ? 54.184 -19.699 -14.644 1.00 19.12 ?  28  LYS   B C    1 
ATOM   4251 O O    . LYS   B 1 28  ? 54.594 -18.800 -15.389 1.00 20.37 ?  28  LYS   B O    1 
ATOM   4252 C CB   . LYS   B 1 28  ? 55.789 -20.223 -12.754 1.00 20.57 ?  28  LYS   B CB   1 
ATOM   4253 C CG   . LYS   B 1 28  ? 56.184 -19.888 -11.320 1.00 23.58 ?  28  LYS   B CG   1 
ATOM   4254 C CD   . LYS   B 1 28  ? 57.614 -20.282 -10.984 1.00 27.07 ?  28  LYS   B CD   1 
ATOM   4255 C CE   . LYS   B 1 28  ? 57.720 -21.743 -10.616 1.00 29.47 ?  28  LYS   B CE   1 
ATOM   4256 N NZ   . LYS   B 1 28  ? 59.076 -22.084 -10.094 1.00 31.74 ?  28  LYS   B NZ   1 
ATOM   4257 H H    . LYS   B 1 28  ? 53.583 -20.940 -11.948 1.00 19.49 ?  28  LYS   B H    1 
ATOM   4258 H HA   . LYS   B 1 28  ? 54.473 -18.674 -12.923 1.00 21.84 ?  28  LYS   B HA   1 
ATOM   4259 H HB2  . LYS   B 1 28  ? 55.744 -21.186 -12.833 1.00 24.69 ?  28  LYS   B HB2  1 
ATOM   4260 H HB3  . LYS   B 1 28  ? 56.479 -19.872 -13.342 1.00 24.69 ?  28  LYS   B HB3  1 
ATOM   4261 H HG2  . LYS   B 1 28  ? 56.095 -18.928 -11.190 1.00 28.30 ?  28  LYS   B HG2  1 
ATOM   4262 H HG3  . LYS   B 1 28  ? 55.589 -20.357 -10.717 1.00 28.30 ?  28  LYS   B HG3  1 
ATOM   4263 H HD2  . LYS   B 1 28  ? 58.177 -20.117 -11.756 1.00 32.48 ?  28  LYS   B HD2  1 
ATOM   4264 H HD3  . LYS   B 1 28  ? 57.916 -19.752 -10.230 1.00 32.48 ?  28  LYS   B HD3  1 
ATOM   4265 H HE2  . LYS   B 1 28  ? 57.069 -21.947 -9.925  1.00 35.37 ?  28  LYS   B HE2  1 
ATOM   4266 H HE3  . LYS   B 1 28  ? 57.552 -22.285 -11.402 1.00 35.37 ?  28  LYS   B HE3  1 
ATOM   4267 H HZ1  . LYS   B 1 28  ? 59.113 -22.948 -9.884  1.00 38.09 ?  28  LYS   B HZ1  1 
ATOM   4268 H HZ2  . LYS   B 1 28  ? 59.692 -21.909 -10.711 1.00 38.09 ?  28  LYS   B HZ2  1 
ATOM   4269 H HZ3  . LYS   B 1 28  ? 59.251 -21.602 -9.366  1.00 38.09 ?  28  LYS   B HZ3  1 
ATOM   4270 N N    . LYS   B 1 29  ? 53.478 -20.734 -15.100 1.00 20.24 ?  29  LYS   B N    1 
ATOM   4271 C CA   . LYS   B 1 29  ? 53.194 -20.871 -16.524 1.00 22.69 ?  29  LYS   B CA   1 
ATOM   4272 C C    . LYS   B 1 29  ? 51.942 -20.113 -16.959 1.00 21.61 ?  29  LYS   B C    1 
ATOM   4273 O O    . LYS   B 1 29  ? 51.937 -19.502 -18.032 1.00 23.03 ?  29  LYS   B O    1 
ATOM   4274 C CB   . LYS   B 1 29  ? 53.069 -22.351 -16.893 1.00 27.11 ?  29  LYS   B CB   1 
ATOM   4275 C CG   . LYS   B 1 29  ? 52.924 -22.611 -18.380 1.00 31.19 ?  29  LYS   B CG   1 
ATOM   4276 C CD   . LYS   B 1 29  ? 53.166 -24.079 -18.707 1.00 34.36 ?  29  LYS   B CD   1 
ATOM   4277 C CE   . LYS   B 1 29  ? 52.119 -24.985 -18.074 1.00 36.37 ?  29  LYS   B CE   1 
ATOM   4278 N NZ   . LYS   B 1 29  ? 52.366 -26.421 -18.392 1.00 37.45 ?  29  LYS   B NZ   1 
ATOM   4279 H H    . LYS   B 1 29  ? 53.146 -21.364 -14.602 1.00 24.29 ?  29  LYS   B H    1 
ATOM   4280 H HA   . LYS   B 1 29  ? 53.938 -20.507 -17.016 1.00 27.23 ?  29  LYS   B HA   1 
ATOM   4281 H HB2  . LYS   B 1 29  ? 53.869 -22.812 -16.593 1.00 32.53 ?  29  LYS   B HB2  1 
ATOM   4282 H HB3  . LYS   B 1 29  ? 52.291 -22.719 -16.453 1.00 32.53 ?  29  LYS   B HB3  1 
ATOM   4283 H HG2  . LYS   B 1 29  ? 52.024 -22.380 -18.659 1.00 37.43 ?  29  LYS   B HG2  1 
ATOM   4284 H HG3  . LYS   B 1 29  ? 53.574 -22.078 -18.865 1.00 37.43 ?  29  LYS   B HG3  1 
ATOM   4285 H HD2  . LYS   B 1 29  ? 53.130 -24.202 -19.668 1.00 41.23 ?  29  LYS   B HD2  1 
ATOM   4286 H HD3  . LYS   B 1 29  ? 54.037 -24.341 -18.368 1.00 41.23 ?  29  LYS   B HD3  1 
ATOM   4287 H HE2  . LYS   B 1 29  ? 52.145 -24.884 -17.109 1.00 43.64 ?  29  LYS   B HE2  1 
ATOM   4288 H HE3  . LYS   B 1 29  ? 51.242 -24.745 -18.412 1.00 43.64 ?  29  LYS   B HE3  1 
ATOM   4289 H HZ1  . LYS   B 1 29  ? 51.742 -26.929 -18.011 1.00 44.94 ?  29  LYS   B HZ1  1 
ATOM   4290 H HZ2  . LYS   B 1 29  ? 52.342 -26.545 -19.273 1.00 44.94 ?  29  LYS   B HZ2  1 
ATOM   4291 H HZ3  . LYS   B 1 29  ? 53.165 -26.667 -18.087 1.00 44.94 ?  29  LYS   B HZ3  1 
ATOM   4292 N N    . VAL   B 1 30  ? 50.880 -20.151 -16.147 1.00 19.93 ?  30  VAL   B N    1 
ATOM   4293 C CA   . VAL   B 1 30  ? 49.587 -19.569 -16.521 1.00 20.27 ?  30  VAL   B CA   1 
ATOM   4294 C C    . VAL   B 1 30  ? 49.575 -18.055 -16.369 1.00 19.29 ?  30  VAL   B C    1 
ATOM   4295 O O    . VAL   B 1 30  ? 48.827 -17.355 -17.069 1.00 19.99 ?  30  VAL   B O    1 
ATOM   4296 C CB   . VAL   B 1 30  ? 48.479 -20.199 -15.653 1.00 21.28 ?  30  VAL   B CB   1 
ATOM   4297 C CG1  . VAL   B 1 30  ? 47.190 -19.387 -15.728 1.00 21.55 ?  30  VAL   B CG1  1 
ATOM   4298 C CG2  . VAL   B 1 30  ? 48.243 -21.645 -16.054 1.00 21.96 ?  30  VAL   B CG2  1 
ATOM   4299 H H    . VAL   B 1 30  ? 50.872 -20.537 -15.367 1.00 23.91 ?  30  VAL   B H    1 
ATOM   4300 H HA   . VAL   B 1 30  ? 49.401 -19.797 -17.443 1.00 24.33 ?  30  VAL   B HA   1 
ATOM   4301 H HB   . VAL   B 1 30  ? 48.768 -20.202 -14.728 1.00 25.54 ?  30  VAL   B HB   1 
ATOM   4302 H HG11 . VAL   B 1 30  ? 46.447 -19.969 -15.506 1.00 25.85 ?  30  VAL   B HG11 1 
ATOM   4303 H HG12 . VAL   B 1 30  ? 47.234 -18.658 -15.092 1.00 25.85 ?  30  VAL   B HG12 1 
ATOM   4304 H HG13 . VAL   B 1 30  ? 47.075 -19.050 -16.626 1.00 25.85 ?  30  VAL   B HG13 1 
ATOM   4305 H HG21 . VAL   B 1 30  ? 47.551 -22.022 -15.486 1.00 26.35 ?  30  VAL   B HG21 1 
ATOM   4306 H HG22 . VAL   B 1 30  ? 47.959 -21.673 -16.982 1.00 26.35 ?  30  VAL   B HG22 1 
ATOM   4307 H HG23 . VAL   B 1 30  ? 49.067 -22.141 -15.944 1.00 26.35 ?  30  VAL   B HG23 1 
ATOM   4308 N N    . LYS   B 1 31  ? 50.349 -17.545 -15.431 1.00 18.84 ?  31  LYS   B N    1 
ATOM   4309 C CA   . LYS   B 1 31  ? 50.383 -16.138 -15.076 1.00 19.17 ?  31  LYS   B CA   1 
ATOM   4310 C C    . LYS   B 1 31  ? 48.982 -15.671 -14.684 1.00 17.09 ?  31  LYS   B C    1 
ATOM   4311 O O    . LYS   B 1 31  ? 48.432 -14.760 -15.316 1.00 18.25 ?  31  LYS   B O    1 
ATOM   4312 C CB   . LYS   B 1 31  ? 51.011 -15.328 -16.219 1.00 22.32 ?  31  LYS   B CB   1 
ATOM   4313 C CG   . LYS   B 1 31  ? 52.444 -15.761 -16.542 1.00 25.77 ?  31  LYS   B CG   1 
ATOM   4314 C CD   . LYS   B 1 31  ? 53.016 -14.985 -17.720 1.00 28.55 ?  31  LYS   B CD   1 
ATOM   4315 C CE   . LYS   B 1 31  ? 54.498 -15.253 -17.896 1.00 30.46 ?  31  LYS   B CE   1 
ATOM   4316 N NZ   . LYS   B 1 31  ? 55.250 -14.869 -16.674 1.00 31.92 ?  31  LYS   B NZ   1 
ATOM   4317 H H    . LYS   B 1 31  ? 50.875 -18.030 -14.967 1.00 22.61 ?  31  LYS   B H    1 
ATOM   4318 H HA   . LYS   B 1 31  ? 50.941 -16.048 -14.302 1.00 23.00 ?  31  LYS   B HA   1 
ATOM   4319 H HB2  . LYS   B 1 31  ? 50.481 -15.442 -17.025 1.00 26.78 ?  31  LYS   B HB2  1 
ATOM   4320 H HB3  . LYS   B 1 31  ? 51.033 -14.397 -15.964 1.00 26.78 ?  31  LYS   B HB3  1 
ATOM   4321 H HG2  . LYS   B 1 31  ? 52.999 -15.603 -15.762 1.00 30.92 ?  31  LYS   B HG2  1 
ATOM   4322 H HG3  . LYS   B 1 31  ? 52.447 -16.708 -16.765 1.00 30.92 ?  31  LYS   B HG3  1 
ATOM   4323 H HD2  . LYS   B 1 31  ? 52.557 -15.257 -18.530 1.00 34.26 ?  31  LYS   B HD2  1 
ATOM   4324 H HD3  . LYS   B 1 31  ? 52.891 -14.037 -17.564 1.00 34.26 ?  31  LYS   B HD3  1 
ATOM   4325 H HE2  . LYS   B 1 31  ? 54.643 -16.199 -18.058 1.00 36.55 ?  31  LYS   B HE2  1 
ATOM   4326 H HE3  . LYS   B 1 31  ? 54.837 -14.728 -18.639 1.00 36.55 ?  31  LYS   B HE3  1 
ATOM   4327 H HZ1  . LYS   B 1 31  ? 56.124 -14.897 -16.833 1.00 38.30 ?  31  LYS   B HZ1  1 
ATOM   4328 H HZ2  . LYS   B 1 31  ? 55.026 -14.043 -16.428 1.00 38.30 ?  31  LYS   B HZ2  1 
ATOM   4329 H HZ3  . LYS   B 1 31  ? 55.058 -15.430 -16.010 1.00 38.30 ?  31  LYS   B HZ3  1 
ATOM   4330 N N    . PRO   B 1 32  ? 48.377 -16.268 -13.650 1.00 14.84 ?  32  PRO   B N    1 
ATOM   4331 C CA   . PRO   B 1 32  ? 46.995 -15.919 -13.298 1.00 13.94 ?  32  PRO   B CA   1 
ATOM   4332 C C    . PRO   B 1 32  ? 46.910 -14.575 -12.594 1.00 14.05 ?  32  PRO   B C    1 
ATOM   4333 O O    . PRO   B 1 32  ? 47.836 -14.145 -11.898 1.00 15.27 ?  32  PRO   B O    1 
ATOM   4334 C CB   . PRO   B 1 32  ? 46.597 -17.038 -12.328 1.00 13.97 ?  32  PRO   B CB   1 
ATOM   4335 C CG   . PRO   B 1 32  ? 47.891 -17.372 -11.647 1.00 14.12 ?  32  PRO   B CG   1 
ATOM   4336 C CD   . PRO   B 1 32  ? 48.950 -17.252 -12.706 1.00 14.49 ?  32  PRO   B CD   1 
ATOM   4337 H HA   . PRO   B 1 32  ? 46.411 -15.935 -14.079 1.00 16.73 ?  32  PRO   B HA   1 
ATOM   4338 H HB2  . PRO   B 1 32  ? 45.939 -16.712 -11.691 1.00 16.76 ?  32  PRO   B HB2  1 
ATOM   4339 H HB3  . PRO   B 1 32  ? 46.254 -17.803 -12.818 1.00 16.76 ?  32  PRO   B HB3  1 
ATOM   4340 H HG2  . PRO   B 1 32  ? 48.052 -16.739 -10.925 1.00 16.94 ?  32  PRO   B HG2  1 
ATOM   4341 H HG3  . PRO   B 1 32  ? 47.857 -18.278 -11.300 1.00 16.94 ?  32  PRO   B HG3  1 
ATOM   4342 H HD2  . PRO   B 1 32  ? 49.768 -16.901 -12.321 1.00 17.38 ?  32  PRO   B HD2  1 
ATOM   4343 H HD3  . PRO   B 1 32  ? 49.086 -18.100 -13.140 1.00 17.38 ?  32  PRO   B HD3  1 
ATOM   4344 N N    . THR   B 1 33  ? 45.758 -13.922 -12.768 1.00 13.25 ?  33  THR   B N    1 
ATOM   4345 C CA   . THR   B 1 33  ? 45.457 -12.747 -11.960 1.00 13.45 ?  33  THR   B CA   1 
ATOM   4346 C C    . THR   B 1 33  ? 45.414 -13.098 -10.480 1.00 13.19 ?  33  THR   B C    1 
ATOM   4347 O O    . THR   B 1 33  ? 45.887 -12.319 -9.639  1.00 14.07 ?  33  THR   B O    1 
ATOM   4348 C CB   . THR   B 1 33  ? 44.139 -12.116 -12.413 1.00 14.49 ?  33  THR   B CB   1 
ATOM   4349 O OG1  . THR   B 1 33  ? 44.195 -11.859 -13.817 1.00 14.43 ?  33  THR   B OG1  1 
ATOM   4350 C CG2  . THR   B 1 33  ? 43.885 -10.811 -11.672 1.00 15.75 ?  33  THR   B CG2  1 
ATOM   4351 H H    . THR   B 1 33  ? 45.139 -14.143 -13.328 1.00 15.90 ?  33  THR   B H    1 
ATOM   4352 H HA   . THR   B 1 33  ? 46.157 -12.093 -12.089 1.00 16.14 ?  33  THR   B HA   1 
ATOM   4353 H HB   . THR   B 1 33  ? 43.403 -12.725 -12.223 1.00 17.39 ?  33  THR   B HB   1 
ATOM   4354 H HG1  . THR   B 1 33  ? 43.474 -11.500 -14.074 1.00 17.32 ?  33  THR   B HG1  1 
ATOM   4355 H HG21 . THR   B 1 33  ? 43.125 -10.354 -12.058 1.00 18.90 ?  33  THR   B HG21 1 
ATOM   4356 H HG22 . THR   B 1 33  ? 43.704 -10.990 -10.735 1.00 18.90 ?  33  THR   B HG22 1 
ATOM   4357 H HG23 . THR   B 1 33  ? 44.667 -10.240 -11.738 1.00 18.90 ?  33  THR   B HG23 1 
ATOM   4358 N N    . VAL   B 1 34  ? 44.860 -14.266 -10.139 1.00 12.44 ?  34  VAL   B N    1 
ATOM   4359 C CA   . VAL   B 1 34  ? 44.668 -14.663 -8.747  1.00 12.15 ?  34  VAL   B CA   1 
ATOM   4360 C C    . VAL   B 1 34  ? 45.103 -16.110 -8.576  1.00 11.21 ?  34  VAL   B C    1 
ATOM   4361 O O    . VAL   B 1 34  ? 44.587 -17.005 -9.258  1.00 11.74 ?  34  VAL   B O    1 
ATOM   4362 C CB   . VAL   B 1 34  ? 43.196 -14.526 -8.305  1.00 13.33 ?  34  VAL   B CB   1 
ATOM   4363 C CG1  . VAL   B 1 34  ? 43.029 -14.977 -6.860  1.00 13.71 ?  34  VAL   B CG1  1 
ATOM   4364 C CG2  . VAL   B 1 34  ? 42.689 -13.106 -8.507  1.00 14.14 ?  34  VAL   B CG2  1 
ATOM   4365 H H    . VAL   B 1 34  ? 44.596 -14.861 -10.702 1.00 14.93 ?  34  VAL   B H    1 
ATOM   4366 H HA   . VAL   B 1 34  ? 45.217 -14.109 -8.167  1.00 14.58 ?  34  VAL   B HA   1 
ATOM   4367 H HB   . VAL   B 1 34  ? 42.655 -15.111 -8.857  1.00 16.00 ?  34  VAL   B HB   1 
ATOM   4368 H HG11 . VAL   B 1 34  ? 42.169 -14.664 -6.530  1.00 16.45 ?  34  VAL   B HG11 1 
ATOM   4369 H HG12 . VAL   B 1 34  ? 43.058 -15.947 -6.820  1.00 16.45 ?  34  VAL   B HG12 1 
ATOM   4370 H HG13 . VAL   B 1 34  ? 43.742 -14.600 -6.323  1.00 16.45 ?  34  VAL   B HG13 1 
ATOM   4371 H HG21 . VAL   B 1 34  ? 41.771 -13.048 -8.194  1.00 16.97 ?  34  VAL   B HG21 1 
ATOM   4372 H HG22 . VAL   B 1 34  ? 43.248 -12.493 -8.006  1.00 16.97 ?  34  VAL   B HG22 1 
ATOM   4373 H HG23 . VAL   B 1 34  ? 42.726 -12.888 -9.454  1.00 16.97 ?  34  VAL   B HG23 1 
ATOM   4374 N N    . VAL   B 1 35  ? 46.007 -16.357 -7.633  1.00 10.80 ?  35  VAL   B N    1 
ATOM   4375 C CA   . VAL   B 1 35  ? 46.243 -17.702 -7.118  1.00 10.77 ?  35  VAL   B CA   1 
ATOM   4376 C C    . VAL   B 1 35  ? 45.701 -17.761 -5.699  1.00 10.52 ?  35  VAL   B C    1 
ATOM   4377 O O    . VAL   B 1 35  ? 45.920 -16.838 -4.905  1.00 10.46 ?  35  VAL   B O    1 
ATOM   4378 C CB   . VAL   B 1 35  ? 47.728 -18.125 -7.194  1.00 11.60 ?  35  VAL   B CB   1 
ATOM   4379 C CG1  . VAL   B 1 35  ? 48.627 -17.281 -6.274  1.00 12.07 ?  35  VAL   B CG1  1 
ATOM   4380 C CG2  . VAL   B 1 35  ? 47.876 -19.625 -6.881  1.00 11.97 ?  35  VAL   B CG2  1 
ATOM   4381 H H    . VAL   B 1 35  ? 46.508 -15.755 -7.273  1.00 12.96 ?  35  VAL   B H    1 
ATOM   4382 H HA   . VAL   B 1 35  ? 45.735 -18.334 -7.649  1.00 12.92 ?  35  VAL   B HA   1 
ATOM   4383 H HB   . VAL   B 1 35  ? 48.038 -17.994 -8.103  1.00 13.91 ?  35  VAL   B HB   1 
ATOM   4384 H HG11 . VAL   B 1 35  ? 49.553 -17.514 -6.443  1.00 14.48 ?  35  VAL   B HG11 1 
ATOM   4385 H HG12 . VAL   B 1 35  ? 48.474 -16.347 -6.461  1.00 14.48 ?  35  VAL   B HG12 1 
ATOM   4386 H HG13 . VAL   B 1 35  ? 48.401 -17.480 -5.349  1.00 14.48 ?  35  VAL   B HG13 1 
ATOM   4387 H HG21 . VAL   B 1 35  ? 48.803 -19.889 -6.976  1.00 14.36 ?  35  VAL   B HG21 1 
ATOM   4388 H HG22 . VAL   B 1 35  ? 47.578 -19.797 -5.969  1.00 14.36 ?  35  VAL   B HG22 1 
ATOM   4389 H HG23 . VAL   B 1 35  ? 47.325 -20.141 -7.500  1.00 14.36 ?  35  VAL   B HG23 1 
ATOM   4390 N N    . VAL   B 1 36  ? 44.982 -18.845 -5.386  1.00 10.53 ?  36  VAL   B N    1 
ATOM   4391 C CA   . VAL   B 1 36  ? 44.438 -19.050 -4.054  1.00 10.36 ?  36  VAL   B CA   1 
ATOM   4392 C C    . VAL   B 1 36  ? 45.447 -19.812 -3.203  1.00 9.95  ?  36  VAL   B C    1 
ATOM   4393 O O    . VAL   B 1 36  ? 45.986 -20.844 -3.626  1.00 10.83 ?  36  VAL   B O    1 
ATOM   4394 C CB   . VAL   B 1 36  ? 43.102 -19.811 -4.132  1.00 10.64 ?  36  VAL   B CB   1 
ATOM   4395 C CG1  . VAL   B 1 36  ? 42.604 -20.175 -2.743  1.00 11.44 ?  36  VAL   B CG1  1 
ATOM   4396 C CG2  . VAL   B 1 36  ? 42.076 -18.977 -4.878  1.00 11.46 ?  36  VAL   B CG2  1 
ATOM   4397 H H    . VAL   B 1 36  ? 44.813 -19.485 -5.935  1.00 12.63 ?  36  VAL   B H    1 
ATOM   4398 H HA   . VAL   B 1 36  ? 44.273 -18.188 -3.640  1.00 12.43 ?  36  VAL   B HA   1 
ATOM   4399 H HB   . VAL   B 1 36  ? 43.235 -20.632 -4.631  1.00 12.77 ?  36  VAL   B HB   1 
ATOM   4400 H HG11 . VAL   B 1 36  ? 41.663 -20.404 -2.798  1.00 13.73 ?  36  VAL   B HG11 1 
ATOM   4401 H HG12 . VAL   B 1 36  ? 43.111 -20.927 -2.410  1.00 13.73 ?  36  VAL   B HG12 1 
ATOM   4402 H HG13 . VAL   B 1 36  ? 42.719 -19.406 -2.159  1.00 13.73 ?  36  VAL   B HG13 1 
ATOM   4403 H HG21 . VAL   B 1 36  ? 41.234 -19.452 -4.899  1.00 13.75 ?  36  VAL   B HG21 1 
ATOM   4404 H HG22 . VAL   B 1 36  ? 41.969 -18.126 -4.422  1.00 13.75 ?  36  VAL   B HG22 1 
ATOM   4405 H HG23 . VAL   B 1 36  ? 42.392 -18.823 -5.786  1.00 13.75 ?  36  VAL   B HG23 1 
ATOM   4406 N N    . ASN   B 1 37  ? 45.670 -19.320 -1.985  1.00 10.32 ?  37  ASN   B N    1 
ATOM   4407 C CA   . ASN   B 1 37  ? 46.424 -20.046 -0.978  1.00 10.81 ?  37  ASN   B CA   1 
ATOM   4408 C C    . ASN   B 1 37  ? 45.474 -20.721 0.002   1.00 10.69 ?  37  ASN   B C    1 
ATOM   4409 O O    . ASN   B 1 37  ? 44.465 -20.140 0.415   1.00 10.97 ?  37  ASN   B O    1 
ATOM   4410 C CB   . ASN   B 1 37  ? 47.349 -19.098 -0.215  1.00 10.87 ?  37  ASN   B CB   1 
ATOM   4411 C CG   . ASN   B 1 37  ? 48.201 -19.817 0.801   1.00 10.97 ?  37  ASN   B CG   1 
ATOM   4412 O OD1  . ASN   B 1 37  ? 48.543 -20.992 0.622   1.00 11.54 ?  37  ASN   B OD1  1 
ATOM   4413 N ND2  . ASN   B 1 37  ? 48.548 -19.119 1.878   1.00 11.20 ?  37  ASN   B ND2  1 
ATOM   4414 H H    . ASN   B 1 37  ? 45.386 -18.551 -1.710  1.00 12.39 ?  37  ASN   B H    1 
ATOM   4415 H HA   . ASN   B 1 37  ? 46.961 -20.733 -1.400  1.00 12.98 ?  37  ASN   B HA   1 
ATOM   4416 H HB2  . ASN   B 1 37  ? 47.942 -18.668 -0.847  1.00 13.04 ?  37  ASN   B HB2  1 
ATOM   4417 H HB3  . ASN   B 1 37  ? 46.817 -18.441 0.253   1.00 13.04 ?  37  ASN   B HB3  1 
ATOM   4418 H HD21 . ASN   B 1 37  ? 49.036 -19.484 2.487   1.00 13.44 ?  37  ASN   B HD21 1 
ATOM   4419 H HD22 . ASN   B 1 37  ? 48.288 -18.311 1.971   1.00 13.44 ?  37  ASN   B HD22 1 
ATOM   4420 N N    . ALA   B 1 38  ? 45.821 -21.952 0.377   1.00 10.80 ?  38  ALA   B N    1 
ATOM   4421 C CA   . ALA   B 1 38  ? 45.166 -22.695 1.454   1.00 11.36 ?  38  ALA   B CA   1 
ATOM   4422 C C    . ALA   B 1 38  ? 45.750 -22.214 2.781   1.00 11.21 ?  38  ALA   B C    1 
ATOM   4423 O O    . ALA   B 1 38  ? 46.653 -22.825 3.364   1.00 11.68 ?  38  ALA   B O    1 
ATOM   4424 C CB   . ALA   B 1 38  ? 45.381 -24.189 1.258   1.00 12.42 ?  38  ALA   B CB   1 
ATOM   4425 H H    . ALA   B 1 38  ? 46.469 -22.391 0.021   1.00 12.96 ?  38  ALA   B H    1 
ATOM   4426 H HA   . ALA   B 1 38  ? 44.213 -22.513 1.448   1.00 13.63 ?  38  ALA   B HA   1 
ATOM   4427 H HB1  . ALA   B 1 38  ? 44.933 -24.674 1.980   1.00 14.91 ?  38  ALA   B HB1  1 
ATOM   4428 H HB2  . ALA   B 1 38  ? 44.994 -24.459 0.407   1.00 14.91 ?  38  ALA   B HB2  1 
ATOM   4429 H HB3  . ALA   B 1 38  ? 46.325 -24.387 1.271   1.00 14.91 ?  38  ALA   B HB3  1 
ATOM   4430 N N    . ALA   B 1 39  ? 45.233 -21.075 3.244   1.00 10.87 ?  39  ALA   B N    1 
ATOM   4431 C CA   . ALA   B 1 39  ? 45.786 -20.346 4.374   1.00 11.37 ?  39  ALA   B CA   1 
ATOM   4432 C C    . ALA   B 1 39  ? 45.163 -20.792 5.696   1.00 11.08 ?  39  ALA   B C    1 
ATOM   4433 O O    . ALA   B 1 39  ? 44.135 -21.467 5.739   1.00 12.05 ?  39  ALA   B O    1 
ATOM   4434 C CB   . ALA   B 1 39  ? 45.554 -18.843 4.183   1.00 11.98 ?  39  ALA   B CB   1 
ATOM   4435 H H    . ALA   B 1 39  ? 44.538 -20.698 2.901   1.00 13.04 ?  39  ALA   B H    1 
ATOM   4436 H HA   . ALA   B 1 39  ? 46.739 -20.505 4.416   1.00 13.65 ?  39  ALA   B HA   1 
ATOM   4437 H HB1  . ALA   B 1 39  ? 45.929 -18.369 4.942   1.00 14.38 ?  39  ALA   B HB1  1 
ATOM   4438 H HB2  . ALA   B 1 39  ? 45.996 -18.556 3.366   1.00 14.38 ?  39  ALA   B HB2  1 
ATOM   4439 H HB3  . ALA   B 1 39  ? 44.603 -18.672 4.121   1.00 14.38 ?  39  ALA   B HB3  1 
ATOM   4440 N N    . ASN   B 1 40  ? 45.805 -20.374 6.785   1.00 11.98 ?  40  ASN   B N    1 
ATOM   4441 C CA   . ASN   B 1 40  ? 45.242 -20.426 8.123   1.00 12.69 ?  40  ASN   B CA   1 
ATOM   4442 C C    . ASN   B 1 40  ? 45.061 -19.001 8.650   1.00 12.32 ?  40  ASN   B C    1 
ATOM   4443 O O    . ASN   B 1 40  ? 45.470 -18.018 8.021   1.00 12.34 ?  40  ASN   B O    1 
ATOM   4444 C CB   . ASN   B 1 40  ? 46.090 -21.302 9.061   1.00 13.72 ?  40  ASN   B CB   1 
ATOM   4445 C CG   . ASN   B 1 40  ? 47.546 -20.897 9.093   1.00 14.79 ?  40  ASN   B CG   1 
ATOM   4446 O OD1  . ASN   B 1 40  ? 47.865 -19.714 9.157   1.00 16.51 ?  40  ASN   B OD1  1 
ATOM   4447 N ND2  . ASN   B 1 40  ? 48.440 -21.876 9.048   1.00 14.87 ?  40  ASN   B ND2  1 
ATOM   4448 H H    . ASN   B 1 40  ? 46.598 -20.041 6.760   1.00 14.38 ?  40  ASN   B H    1 
ATOM   4449 H HA   . ASN   B 1 40  ? 44.360 -20.826 8.071   1.00 15.23 ?  40  ASN   B HA   1 
ATOM   4450 H HB2  . ASN   B 1 40  ? 45.738 -21.231 9.962   1.00 16.47 ?  40  ASN   B HB2  1 
ATOM   4451 H HB3  . ASN   B 1 40  ? 46.042 -22.224 8.760   1.00 16.47 ?  40  ASN   B HB3  1 
ATOM   4452 H HD21 . ASN   B 1 40  ? 49.281 -21.694 9.065   1.00 17.84 ?  40  ASN   B HD21 1 
ATOM   4453 H HD22 . ASN   B 1 40  ? 48.180 -22.695 9.004   1.00 17.84 ?  40  ASN   B HD22 1 
ATOM   4454 N N    . VAL   B 1 41  ? 44.412 -18.879 9.810   1.00 12.96 ?  41  VAL   B N    1 
ATOM   4455 C CA   . VAL   B 1 41  ? 43.955 -17.559 10.255  1.00 13.66 ?  41  VAL   B CA   1 
ATOM   4456 C C    . VAL   B 1 41  ? 45.105 -16.609 10.560  1.00 13.56 ?  41  VAL   B C    1 
ATOM   4457 O O    . VAL   B 1 41  ? 44.926 -15.387 10.491  1.00 13.64 ?  41  VAL   B O    1 
ATOM   4458 C CB   . VAL   B 1 41  ? 42.972 -17.632 11.439  1.00 14.82 ?  41  VAL   B CB   1 
ATOM   4459 C CG1  . VAL   B 1 41  ? 41.674 -18.307 11.027  1.00 15.40 ?  41  VAL   B CG1  1 
ATOM   4460 C CG2  . VAL   B 1 41  ? 43.605 -18.321 12.635  1.00 16.06 ?  41  VAL   B CG2  1 
ATOM   4461 H H    . VAL   B 1 41  ? 44.233 -19.524 10.341  1.00 15.55 ?  41  VAL   B H    1 
ATOM   4462 H HA   . VAL   B 1 41  ? 43.464 -17.162 9.521   1.00 16.39 ?  41  VAL   B HA   1 
ATOM   4463 H HB   . VAL   B 1 41  ? 42.751 -16.728 11.711  1.00 17.78 ?  41  VAL   B HB   1 
ATOM   4464 H HG11 . VAL   B 1 41  ? 41.066 -18.311 11.782  1.00 18.48 ?  41  VAL   B HG11 1 
ATOM   4465 H HG12 . VAL   B 1 41  ? 41.284 -17.816 10.288  1.00 18.48 ?  41  VAL   B HG12 1 
ATOM   4466 H HG13 . VAL   B 1 41  ? 41.868 -19.218 10.753  1.00 18.48 ?  41  VAL   B HG13 1 
ATOM   4467 H HG21 . VAL   B 1 41  ? 42.962 -18.352 13.359  1.00 19.27 ?  41  VAL   B HG21 1 
ATOM   4468 H HG22 . VAL   B 1 41  ? 43.861 -19.223 12.383  1.00 19.27 ?  41  VAL   B HG22 1 
ATOM   4469 H HG23 . VAL   B 1 41  ? 44.389 -17.821 12.911  1.00 19.27 ?  41  VAL   B HG23 1 
ATOM   4470 N N    . TYR   B 1 42  ? 46.274 -17.127 10.934  1.00 13.96 ?  42  TYR   B N    1 
ATOM   4471 C CA   . TYR   B 1 42  ? 47.427 -16.280 11.213  1.00 14.37 ?  42  TYR   B CA   1 
ATOM   4472 C C    . TYR   B 1 42  ? 48.392 -16.196 10.036  1.00 13.54 ?  42  TYR   B C    1 
ATOM   4473 O O    . TYR   B 1 42  ? 49.481 -15.625 10.177  1.00 14.66 ?  42  TYR   B O    1 
ATOM   4474 C CB   . TYR   B 1 42  ? 48.119 -16.690 12.521  1.00 16.23 ?  42  TYR   B CB   1 
ATOM   4475 C CG   . TYR   B 1 42  ? 47.519 -15.998 13.742  1.00 16.99 ?  42  TYR   B CG   1 
ATOM   4476 C CD1  . TYR   B 1 42  ? 47.753 -14.645 13.979  1.00 16.27 ?  42  TYR   B CD1  1 
ATOM   4477 C CD2  . TYR   B 1 42  ? 46.721 -16.686 14.645  1.00 18.67 ?  42  TYR   B CD2  1 
ATOM   4478 C CE1  . TYR   B 1 42  ? 47.210 -13.999 15.079  1.00 17.16 ?  42  TYR   B CE1  1 
ATOM   4479 C CE2  . TYR   B 1 42  ? 46.177 -16.049 15.750  1.00 18.82 ?  42  TYR   B CE2  1 
ATOM   4480 C CZ   . TYR   B 1 42  ? 46.422 -14.703 15.962  1.00 18.93 ?  42  TYR   B CZ   1 
ATOM   4481 O OH   . TYR   B 1 42  ? 45.887 -14.061 17.061  1.00 21.71 ?  42  TYR   B OH   1 
ATOM   4482 H H    . TYR   B 1 42  ? 46.423 -17.973 11.028  1.00 16.75 ?  42  TYR   B H    1 
ATOM   4483 H HA   . TYR   B 1 42  ? 47.097 -15.384 11.352  1.00 17.25 ?  42  TYR   B HA   1 
ATOM   4484 H HB2  . TYR   B 1 42  ? 48.029 -17.645 12.645  1.00 19.48 ?  42  TYR   B HB2  1 
ATOM   4485 H HB3  . TYR   B 1 42  ? 49.058 -16.446 12.468  1.00 19.48 ?  42  TYR   B HB3  1 
ATOM   4486 H HD1  . TYR   B 1 42  ? 48.288 -14.162 13.381  1.00 19.52 ?  42  TYR   B HD1  1 
ATOM   4487 H HD2  . TYR   B 1 42  ? 46.552 -17.589 14.502  1.00 22.40 ?  42  TYR   B HD2  1 
ATOM   4488 H HE1  . TYR   B 1 42  ? 47.382 -13.095 15.217  1.00 20.59 ?  42  TYR   B HE1  1 
ATOM   4489 H HE2  . TYR   B 1 42  ? 45.644 -16.525 16.342  1.00 22.58 ?  42  TYR   B HE2  1 
ATOM   4490 H HH   . TYR   B 1 42  ? 46.120 -13.258 17.058  1.00 26.05 ?  42  TYR   B HH   1 
ATOM   4491 N N    . LEU   B 1 43  ? 47.998 -16.706 8.871   1.00 12.82 ?  43  LEU   B N    1 
ATOM   4492 C CA   . LEU   B 1 43  ? 48.809 -16.630 7.662   1.00 12.44 ?  43  LEU   B CA   1 
ATOM   4493 C C    . LEU   B 1 43  ? 50.223 -17.137 7.918   1.00 12.66 ?  43  LEU   B C    1 
ATOM   4494 O O    . LEU   B 1 43  ? 51.203 -16.540 7.475   1.00 13.17 ?  43  LEU   B O    1 
ATOM   4495 C CB   . LEU   B 1 43  ? 48.819 -15.226 7.057   1.00 12.69 ?  43  LEU   B CB   1 
ATOM   4496 C CG   . LEU   B 1 43  ? 47.461 -14.617 6.684   1.00 12.78 ?  43  LEU   B CG   1 
ATOM   4497 C CD1  . LEU   B 1 43  ? 47.666 -13.214 6.114   1.00 14.11 ?  43  LEU   B CD1  1 
ATOM   4498 C CD2  . LEU   B 1 43  ? 46.711 -15.507 5.698   1.00 12.82 ?  43  LEU   B CD2  1 
ATOM   4499 H H    . LEU   B 1 43  ? 47.254 -17.121 8.756   1.00 15.39 ?  43  LEU   B H    1 
ATOM   4500 H HA   . LEU   B 1 43  ? 48.412 -17.219 6.996   1.00 14.93 ?  43  LEU   B HA   1 
ATOM   4501 H HB2  . LEU   B 1 43  ? 49.235 -14.626 7.693   1.00 15.23 ?  43  LEU   B HB2  1 
ATOM   4502 H HB3  . LEU   B 1 43  ? 49.350 -15.251 6.245   1.00 15.23 ?  43  LEU   B HB3  1 
ATOM   4503 H HG   . LEU   B 1 43  ? 46.922 -14.539 7.482   1.00 15.33 ?  43  LEU   B HG   1 
ATOM   4504 H HD11 . LEU   B 1 43  ? 46.802 -12.836 5.882   1.00 16.93 ?  43  LEU   B HD11 1 
ATOM   4505 H HD12 . LEU   B 1 43  ? 48.095 -12.660 6.788   1.00 16.93 ?  43  LEU   B HD12 1 
ATOM   4506 H HD13 . LEU   B 1 43  ? 48.227 -13.267 5.325   1.00 16.93 ?  43  LEU   B HD13 1 
ATOM   4507 H HD21 . LEU   B 1 43  ? 45.907 -15.048 5.404   1.00 15.38 ?  43  LEU   B HD21 1 
ATOM   4508 H HD22 . LEU   B 1 43  ? 47.282 -15.693 4.936   1.00 15.38 ?  43  LEU   B HD22 1 
ATOM   4509 H HD23 . LEU   B 1 43  ? 46.471 -16.338 6.140   1.00 15.38 ?  43  LEU   B HD23 1 
ATOM   4510 N N    . LYS   B 1 44  ? 50.325 -18.262 8.629   1.00 12.52 ?  44  LYS   B N    1 
ATOM   4511 C CA   . LYS   B 1 44  ? 51.594 -18.938 8.863   1.00 13.19 ?  44  LYS   B CA   1 
ATOM   4512 C C    . LYS   B 1 44  ? 51.711 -20.054 7.835   1.00 12.74 ?  44  LYS   B C    1 
ATOM   4513 O O    . LYS   B 1 44  ? 51.013 -21.071 7.922   1.00 14.20 ?  44  LYS   B O    1 
ATOM   4514 C CB   . LYS   B 1 44  ? 51.653 -19.454 10.299  1.00 15.00 ?  44  LYS   B CB   1 
ATOM   4515 C CG   . LYS   B 1 44  ? 51.848 -18.349 11.323  1.00 17.70 ?  44  LYS   B CG   1 
ATOM   4516 C CD   . LYS   B 1 44  ? 53.054 -17.490 10.940  1.00 20.85 ?  44  LYS   B CD   1 
ATOM   4517 C CE   . LYS   B 1 44  ? 53.513 -16.588 12.056  1.00 23.41 ?  44  LYS   B CE   1 
ATOM   4518 N NZ   . LYS   B 1 44  ? 54.707 -15.790 11.676  1.00 24.79 ?  44  LYS   B NZ   1 
ATOM   4519 H H    . LYS   B 1 44  ? 49.652 -18.652 8.995   1.00 15.02 ?  44  LYS   B H    1 
ATOM   4520 H HA   . LYS   B 1 44  ? 52.322 -18.316 8.700   1.00 15.82 ?  44  LYS   B HA   1 
ATOM   4521 H HB2  . LYS   B 1 44  ? 50.814 -19.903 10.504  1.00 18.00 ?  44  LYS   B HB2  1 
ATOM   4522 H HB3  . LYS   B 1 44  ? 52.388 -20.074 10.380  1.00 18.00 ?  44  LYS   B HB3  1 
ATOM   4523 H HG2  . LYS   B 1 44  ? 51.061 -17.787 11.352  1.00 21.24 ?  44  LYS   B HG2  1 
ATOM   4524 H HG3  . LYS   B 1 44  ? 52.018 -18.747 12.194  1.00 21.24 ?  44  LYS   B HG3  1 
ATOM   4525 H HD2  . LYS   B 1 44  ? 53.789 -18.077 10.683  1.00 25.02 ?  44  LYS   B HD2  1 
ATOM   4526 H HD3  . LYS   B 1 44  ? 52.808 -16.925 10.189  1.00 25.02 ?  44  LYS   B HD3  1 
ATOM   4527 H HE2  . LYS   B 1 44  ? 52.802 -15.968 12.258  1.00 28.09 ?  44  LYS   B HE2  1 
ATOM   4528 H HE3  . LYS   B 1 44  ? 53.734 -17.126 12.830  1.00 28.09 ?  44  LYS   B HE3  1 
ATOM   4529 H HZ1  . LYS   B 1 44  ? 54.946 -15.264 12.353  1.00 29.74 ?  44  LYS   B HZ1  1 
ATOM   4530 H HZ2  . LYS   B 1 44  ? 55.385 -16.327 11.473  1.00 29.74 ?  44  LYS   B HZ2  1 
ATOM   4531 H HZ3  . LYS   B 1 44  ? 54.521 -15.280 10.968  1.00 29.74 ?  44  LYS   B HZ3  1 
ATOM   4532 N N    . HIS   B 1 45  ? 52.567 -19.839 6.837   1.00 12.65 ?  45  HIS   B N    1 
ATOM   4533 C CA   . HIS   B 1 45  ? 52.588 -20.667 5.633   1.00 12.80 ?  45  HIS   B CA   1 
ATOM   4534 C C    . HIS   B 1 45  ? 53.607 -21.790 5.793   1.00 14.76 ?  45  HIS   B C    1 
ATOM   4535 O O    . HIS   B 1 45  ? 54.666 -21.804 5.178   1.00 16.68 ?  45  HIS   B O    1 
ATOM   4536 C CB   . HIS   B 1 45  ? 52.900 -19.808 4.419   1.00 12.59 ?  45  HIS   B CB   1 
ATOM   4537 C CG   . HIS   B 1 45  ? 52.025 -18.606 4.310   1.00 12.42 ?  45  HIS   B CG   1 
ATOM   4538 N ND1  . HIS   B 1 45  ? 50.649 -18.686 4.256   1.00 12.65 ?  45  HIS   B ND1  1 
ATOM   4539 C CD2  . HIS   B 1 45  ? 52.339 -17.292 4.257   1.00 13.24 ?  45  HIS   B CD2  1 
ATOM   4540 C CE1  . HIS   B 1 45  ? 50.158 -17.463 4.156   1.00 12.45 ?  45  HIS   B CE1  1 
ATOM   4541 N NE2  . HIS   B 1 45  ? 51.159 -16.600 4.154   1.00 13.11 ?  45  HIS   B NE2  1 
ATOM   4542 H H    . HIS   B 1 45  ? 53.148 -19.201 6.828   1.00 15.18 ?  45  HIS   B H    1 
ATOM   4543 H HA   . HIS   B 1 45  ? 51.710 -21.062 5.504   1.00 15.36 ?  45  HIS   B HA   1 
ATOM   4544 H HB2  . HIS   B 1 45  ? 53.817 -19.509 4.468   1.00 15.10 ?  45  HIS   B HB2  1 
ATOM   4545 H HB3  . HIS   B 1 45  ? 52.772 -20.346 3.614   1.00 15.10 ?  45  HIS   B HB3  1 
ATOM   4546 H HD2  . HIS   B 1 45  ? 53.191 -16.925 4.280   1.00 15.89 ?  45  HIS   B HD2  1 
ATOM   4547 H HE1  . HIS   B 1 45  ? 49.255 -17.246 4.085   1.00 14.94 ?  45  HIS   B HE1  1 
ATOM   4548 H HE2  . HIS   B 1 45  ? 51.080 -15.745 4.106   1.00 15.73 ?  45  HIS   B HE2  1 
ATOM   4549 N N    A GLY   B 1 46  ? 53.244 -22.760 6.628   0.70 15.56 ?  46  GLY   B N    1 
ATOM   4550 N N    B GLY   B 1 46  ? 53.254 -22.746 6.643   0.30 15.60 ?  46  GLY   B N    1 
ATOM   4551 C CA   A GLY   B 1 46  ? 54.165 -23.818 6.998   0.70 17.05 ?  46  GLY   B CA   1 
ATOM   4552 C CA   B GLY   B 1 46  ? 54.171 -23.815 6.973   0.30 16.65 ?  46  GLY   B CA   1 
ATOM   4553 C C    A GLY   B 1 46  ? 54.208 -25.035 6.096   0.70 18.42 ?  46  GLY   B C    1 
ATOM   4554 C C    B GLY   B 1 46  ? 54.191 -24.957 5.977   0.30 17.60 ?  46  GLY   B C    1 
ATOM   4555 O O    A GLY   B 1 46  ? 55.287 -25.472 5.683   0.70 21.15 ?  46  GLY   B O    1 
ATOM   4556 O O    B GLY   B 1 46  ? 55.220 -25.233 5.353   0.30 18.32 ?  46  GLY   B O    1 
ATOM   4557 H H    A GLY   B 1 46  ? 52.473 -22.807 7.012   0.70 18.67 ?  46  GLY   B H    1 
ATOM   4558 H H    B GLY   B 1 46  ? 52.493 -22.785 7.046   0.30 18.72 ?  46  GLY   B H    1 
ATOM   4559 H HA2  A GLY   B 1 46  ? 55.060 -23.446 7.042   0.70 20.46 ?  46  GLY   B HA2  1 
ATOM   4560 H HA2  B GLY   B 1 46  ? 55.067 -23.450 7.032   0.30 19.97 ?  46  GLY   B HA2  1 
ATOM   4561 H HA3  A GLY   B 1 46  ? 53.931 -24.132 7.885   0.70 20.46 ?  46  GLY   B HA3  1 
ATOM   4562 H HA3  B GLY   B 1 46  ? 53.934 -24.170 7.844   0.30 19.97 ?  46  GLY   B HA3  1 
ATOM   4563 N N    . GLY   B 1 47  ? 53.050 -25.622 5.803   1.00 18.13 ?  47  GLY   B N    1 
ATOM   4564 C CA   . GLY   B 1 47  ? 52.990 -26.891 5.107   1.00 16.06 ?  47  GLY   B CA   1 
ATOM   4565 C C    . GLY   B 1 47  ? 52.075 -26.873 3.897   1.00 14.04 ?  47  GLY   B C    1 
ATOM   4566 O O    . GLY   B 1 47  ? 51.428 -25.872 3.600   1.00 14.17 ?  47  GLY   B O    1 
ATOM   4567 H H    A GLY   B 1 47  ? 52.279 -25.312 6.027   0.70 21.75 ?  47  GLY   B H    1 
ATOM   4568 H H    B GLY   B 1 47  ? 52.285 -25.349 6.090   0.30 21.75 ?  47  GLY   B H    1 
ATOM   4569 H HA2  . GLY   B 1 47  ? 53.878 -27.144 4.809   1.00 19.27 ?  47  GLY   B HA2  1 
ATOM   4570 H HA3  . GLY   B 1 47  ? 52.674 -27.576 5.720   1.00 19.27 ?  47  GLY   B HA3  1 
ATOM   4571 N N    . GLY   B 1 48  ? 52.032 -28.010 3.207   1.00 13.35 ?  48  GLY   B N    1 
ATOM   4572 C CA   . GLY   B 1 48  ? 51.110 -28.152 2.098   1.00 13.21 ?  48  GLY   B CA   1 
ATOM   4573 C C    . GLY   B 1 48  ? 51.250 -27.042 1.081   1.00 12.56 ?  48  GLY   B C    1 
ATOM   4574 O O    . GLY   B 1 48  ? 52.356 -26.581 0.768   1.00 13.27 ?  48  GLY   B O    1 
ATOM   4575 H H    . GLY   B 1 48  ? 52.527 -28.692 3.358   1.00 16.02 ?  48  GLY   B H    1 
ATOM   4576 H HA2  . GLY   B 1 48  ? 51.269 -28.998 1.655   1.00 15.86 ?  48  GLY   B HA2  1 
ATOM   4577 H HA3  . GLY   B 1 48  ? 50.199 -28.147 2.433   1.00 15.86 ?  48  GLY   B HA3  1 
ATOM   4578 N N    . VAL   B 1 49  ? 50.104 -26.606 0.550   1.00 12.46 ?  49  VAL   B N    1 
ATOM   4579 C CA   . VAL   B 1 49  ? 50.089 -25.582 -0.494  1.00 12.60 ?  49  VAL   B CA   1 
ATOM   4580 C C    . VAL   B 1 49  ? 50.747 -24.295 -0.007  1.00 11.80 ?  49  VAL   B C    1 
ATOM   4581 O O    . VAL   B 1 49  ? 51.536 -23.671 -0.728  1.00 12.51 ?  49  VAL   B O    1 
ATOM   4582 C CB   . VAL   B 1 49  ? 48.646 -25.331 -0.974  1.00 13.64 ?  49  VAL   B CB   1 
ATOM   4583 C CG1  . VAL   B 1 49  ? 48.574 -24.070 -1.827  1.00 13.78 ?  49  VAL   B CG1  1 
ATOM   4584 C CG2  . VAL   B 1 49  ? 48.116 -26.534 -1.743  1.00 15.18 ?  49  VAL   B CG2  1 
ATOM   4585 H H    . VAL   B 1 49  ? 49.316 -26.885 0.777   1.00 14.95 ?  49  VAL   B H    1 
ATOM   4586 H HA   . VAL   B 1 49  ? 50.595 -25.905 -1.253  1.00 15.11 ?  49  VAL   B HA   1 
ATOM   4587 H HB   . VAL   B 1 49  ? 48.075 -25.198 -0.203  1.00 16.37 ?  49  VAL   B HB   1 
ATOM   4588 H HG11 . VAL   B 1 49  ? 47.750 -24.082 -2.339  1.00 16.54 ?  49  VAL   B HG11 1 
ATOM   4589 H HG12 . VAL   B 1 49  ? 48.585 -23.291 -1.245  1.00 16.54 ?  49  VAL   B HG12 1 
ATOM   4590 H HG13 . VAL   B 1 49  ? 49.334 -24.048 -2.427  1.00 16.54 ?  49  VAL   B HG13 1 
ATOM   4591 H HG21 . VAL   B 1 49  ? 47.208 -26.351 -2.031  1.00 18.22 ?  49  VAL   B HG21 1 
ATOM   4592 H HG22 . VAL   B 1 49  ? 48.683 -26.687 -2.518  1.00 18.22 ?  49  VAL   B HG22 1 
ATOM   4593 H HG23 . VAL   B 1 49  ? 48.132 -27.309 -1.164  1.00 18.22 ?  49  VAL   B HG23 1 
ATOM   4594 N N    . ALA   B 1 50  ? 50.405 -23.854 1.206   1.00 11.69 ?  50  ALA   B N    1 
ATOM   4595 C CA   . ALA   B 1 50  ? 50.922 -22.577 1.688   1.00 11.83 ?  50  ALA   B CA   1 
ATOM   4596 C C    . ALA   B 1 50  ? 52.440 -22.606 1.795   1.00 11.96 ?  50  ALA   B C    1 
ATOM   4597 O O    . ALA   B 1 50  ? 53.116 -21.633 1.437   1.00 11.83 ?  50  ALA   B O    1 
ATOM   4598 C CB   . ALA   B 1 50  ? 50.300 -22.225 3.037   1.00 11.90 ?  50  ALA   B CB   1 
ATOM   4599 H H    . ALA   B 1 50  ? 49.888 -24.265 1.756   1.00 14.03 ?  50  ALA   B H    1 
ATOM   4600 H HA   . ALA   B 1 50  ? 50.693 -21.883 1.060   1.00 14.20 ?  50  ALA   B HA   1 
ATOM   4601 H HB1  . ALA   B 1 50  ? 50.659 -21.372 3.339   1.00 14.28 ?  50  ALA   B HB1  1 
ATOM   4602 H HB2  . ALA   B 1 50  ? 49.338 -22.156 2.931   1.00 14.28 ?  50  ALA   B HB2  1 
ATOM   4603 H HB3  . ALA   B 1 50  ? 50.514 -22.917 3.681   1.00 14.28 ?  50  ALA   B HB3  1 
ATOM   4604 N N    . GLY   B 1 51  ? 52.993 -23.702 2.310   1.00 12.26 ?  51  GLY   B N    1 
ATOM   4605 C CA   . GLY   B 1 51  ? 54.439 -23.806 2.380   1.00 12.88 ?  51  GLY   B CA   1 
ATOM   4606 C C    . GLY   B 1 51  ? 55.086 -23.749 1.011   1.00 12.76 ?  51  GLY   B C    1 
ATOM   4607 O O    . GLY   B 1 51  ? 56.125 -23.107 0.828   1.00 13.80 ?  51  GLY   B O    1 
ATOM   4608 H H    . GLY   B 1 51  ? 52.566 -24.385 2.618   1.00 14.71 ?  51  GLY   B H    1 
ATOM   4609 H HA2  . GLY   B 1 51  ? 54.791 -23.078 2.917   1.00 15.45 ?  51  GLY   B HA2  1 
ATOM   4610 H HA3  . GLY   B 1 51  ? 54.686 -24.645 2.804   1.00 15.45 ?  51  GLY   B HA3  1 
ATOM   4611 N N    . ALA   B 1 52  ? 54.480 -24.412 0.028   1.00 12.25 ?  52  ALA   B N    1 
ATOM   4612 C CA   . ALA   B 1 52  ? 55.041 -24.414 -1.315  1.00 12.65 ?  52  ALA   B CA   1 
ATOM   4613 C C    . ALA   B 1 52  ? 54.959 -23.035 -1.961  1.00 12.21 ?  52  ALA   B C    1 
ATOM   4614 O O    . ALA   B 1 52  ? 55.934 -22.581 -2.582  1.00 12.95 ?  52  ALA   B O    1 
ATOM   4615 C CB   . ALA   B 1 52  ? 54.348 -25.467 -2.175  1.00 13.47 ?  52  ALA   B CB   1 
ATOM   4616 H H    . ALA   B 1 52  ? 53.741 -24.851 0.111   1.00 14.70 ?  52  ALA   B H    1 
ATOM   4617 H HA   . ALA   B 1 52  ? 55.976 -24.652 -1.252  1.00 15.18 ?  52  ALA   B HA   1 
ATOM   4618 H HB1  . ALA   B 1 52  ? 54.742 -25.455 -3.062  1.00 16.16 ?  52  ALA   B HB1  1 
ATOM   4619 H HB2  . ALA   B 1 52  ? 54.481 -26.340 -1.769  1.00 16.16 ?  52  ALA   B HB2  1 
ATOM   4620 H HB3  . ALA   B 1 52  ? 53.404 -25.266 -2.227  1.00 16.16 ?  52  ALA   B HB3  1 
ATOM   4621 N N    . LEU   B 1 53  ? 53.813 -22.358 -1.839  1.00 11.82 ?  53  LEU   B N    1 
ATOM   4622 C CA   . LEU   B 1 53  ? 53.701 -21.018 -2.407  1.00 12.19 ?  53  LEU   B CA   1 
ATOM   4623 C C    . LEU   B 1 53  ? 54.706 -20.076 -1.756  1.00 11.96 ?  53  LEU   B C    1 
ATOM   4624 O O    . LEU   B 1 53  ? 55.411 -19.326 -2.441  1.00 12.46 ?  53  LEU   B O    1 
ATOM   4625 C CB   . LEU   B 1 53  ? 52.276 -20.482 -2.246  1.00 12.58 ?  53  LEU   B CB   1 
ATOM   4626 C CG   . LEU   B 1 53  ? 51.141 -21.200 -2.984  1.00 12.75 ?  53  LEU   B CG   1 
ATOM   4627 C CD1  . LEU   B 1 53  ? 49.800 -20.580 -2.630  1.00 14.27 ?  53  LEU   B CD1  1 
ATOM   4628 C CD2  . LEU   B 1 53  ? 51.345 -21.191 -4.489  1.00 14.65 ?  53  LEU   B CD2  1 
ATOM   4629 H H    . LEU   B 1 53  ? 53.109 -22.645 -1.439  1.00 14.19 ?  53  LEU   B H    1 
ATOM   4630 H HA   . LEU   B 1 53  ? 53.903 -21.064 -3.357  1.00 14.62 ?  53  LEU   B HA   1 
ATOM   4631 H HB2  . LEU   B 1 53  ? 52.055 -20.508 -1.305  1.00 15.10 ?  53  LEU   B HB2  1 
ATOM   4632 H HB3  . LEU   B 1 53  ? 52.268 -19.566 -2.553  1.00 15.10 ?  53  LEU   B HB3  1 
ATOM   4633 H HG   . LEU   B 1 53  ? 51.115 -22.126 -2.696  1.00 15.30 ?  53  LEU   B HG   1 
ATOM   4634 H HD11 . LEU   B 1 53  ? 49.095 -21.053 -3.105  1.00 17.13 ?  53  LEU   B HD11 1 
ATOM   4635 H HD12 . LEU   B 1 53  ? 49.656 -20.660 -1.671  1.00 17.13 ?  53  LEU   B HD12 1 
ATOM   4636 H HD13 . LEU   B 1 53  ? 49.802 -19.647 -2.886  1.00 17.13 ?  53  LEU   B HD13 1 
ATOM   4637 H HD21 . LEU   B 1 53  ? 50.626 -21.689 -4.912  1.00 17.58 ?  53  LEU   B HD21 1 
ATOM   4638 H HD22 . LEU   B 1 53  ? 51.338 -20.275 -4.806  1.00 17.58 ?  53  LEU   B HD22 1 
ATOM   4639 H HD23 . LEU   B 1 53  ? 52.196 -21.608 -4.697  1.00 17.58 ?  53  LEU   B HD23 1 
ATOM   4640 N N    . ASN   B 1 54  ? 54.799 -20.110 -0.429  1.00 11.85 ?  54  ASN   B N    1 
ATOM   4641 C CA   . ASN   B 1 54  ? 55.714 -19.200 0.243   1.00 12.41 ?  54  ASN   B CA   1 
ATOM   4642 C C    . ASN   B 1 54  ? 57.158 -19.477 -0.155  1.00 12.92 ?  54  ASN   B C    1 
ATOM   4643 O O    . ASN   B 1 54  ? 57.932 -18.540 -0.383  1.00 13.21 ?  54  ASN   B O    1 
ATOM   4644 C CB   . ASN   B 1 54  ? 55.548 -19.273 1.754   1.00 13.14 ?  54  ASN   B CB   1 
ATOM   4645 C CG   . ASN   B 1 54  ? 56.531 -18.366 2.466   1.00 13.52 ?  54  ASN   B CG   1 
ATOM   4646 O OD1  . ASN   B 1 54  ? 56.544 -17.155 2.232   1.00 13.52 ?  54  ASN   B OD1  1 
ATOM   4647 N ND2  . ASN   B 1 54  ? 57.383 -18.947 3.306   1.00 14.88 ?  54  ASN   B ND2  1 
ATOM   4648 H H    . ASN   B 1 54  ? 54.356 -20.634 0.087   1.00 14.22 ?  54  ASN   B H    1 
ATOM   4649 H HA   . ASN   B 1 54  ? 55.503 -18.294 -0.031  1.00 14.89 ?  54  ASN   B HA   1 
ATOM   4650 H HB2  . ASN   B 1 54  ? 54.649 -18.987 1.993   1.00 15.77 ?  54  ASN   B HB2  1 
ATOM   4651 H HB3  . ASN   B 1 54  ? 55.700 -20.181 2.053   1.00 15.77 ?  54  ASN   B HB3  1 
ATOM   4652 H HD21 . ASN   B 1 54  ? 57.967 -18.475 3.727   1.00 17.85 ?  54  ASN   B HD21 1 
ATOM   4653 H HD22 . ASN   B 1 54  ? 57.353 -19.799 3.431   1.00 17.85 ?  54  ASN   B HD22 1 
ATOM   4654 N N    . LYS   B 1 55  ? 57.544 -20.755 -0.226  1.00 13.50 ?  55  LYS   B N    1 
ATOM   4655 C CA   . LYS   B 1 55  ? 58.900 -21.094 -0.644  1.00 14.39 ?  55  LYS   B CA   1 
ATOM   4656 C C    . LYS   B 1 55  ? 59.198 -20.546 -2.033  1.00 14.01 ?  55  LYS   B C    1 
ATOM   4657 O O    . LYS   B 1 55  ? 60.295 -20.035 -2.282  1.00 14.62 ?  55  LYS   B O    1 
ATOM   4658 C CB   . LYS   B 1 55  ? 59.093 -22.609 -0.604  1.00 15.62 ?  55  LYS   B CB   1 
ATOM   4659 C CG   . LYS   B 1 55  ? 60.477 -23.073 -1.010  1.00 19.43 ?  55  LYS   B CG   1 
ATOM   4660 C CD   . LYS   B 1 55  ? 60.636 -24.573 -0.844  1.00 22.85 ?  55  LYS   B CD   1 
ATOM   4661 C CE   . LYS   B 1 55  ? 60.695 -24.976 0.627   1.00 25.53 ?  55  LYS   B CE   1 
ATOM   4662 N NZ   . LYS   B 1 55  ? 61.035 -26.409 0.799   1.00 26.96 ?  55  LYS   B NZ   1 
ATOM   4663 H H    . LYS   B 1 55  ? 57.043 -21.429 -0.038  1.00 16.20 ?  55  LYS   B H    1 
ATOM   4664 H HA   . LYS   B 1 55  ? 59.530 -20.696 -0.025  1.00 17.27 ?  55  LYS   B HA   1 
ATOM   4665 H HB2  . LYS   B 1 55  ? 58.930 -22.916 0.301   1.00 18.74 ?  55  LYS   B HB2  1 
ATOM   4666 H HB3  . LYS   B 1 55  ? 58.457 -23.021 -1.209  1.00 18.74 ?  55  LYS   B HB3  1 
ATOM   4667 H HG2  . LYS   B 1 55  ? 60.630 -22.855 -1.943  1.00 23.32 ?  55  LYS   B HG2  1 
ATOM   4668 H HG3  . LYS   B 1 55  ? 61.139 -22.633 -0.452  1.00 23.32 ?  55  LYS   B HG3  1 
ATOM   4669 H HD2  . LYS   B 1 55  ? 59.881 -25.025 -1.250  1.00 27.42 ?  55  LYS   B HD2  1 
ATOM   4670 H HD3  . LYS   B 1 55  ? 61.464 -24.860 -1.265  1.00 27.42 ?  55  LYS   B HD3  1 
ATOM   4671 H HE2  . LYS   B 1 55  ? 61.372 -24.440 1.073   1.00 30.63 ?  55  LYS   B HE2  1 
ATOM   4672 H HE3  . LYS   B 1 55  ? 59.826 -24.815 1.033   1.00 30.63 ?  55  LYS   B HE3  1 
ATOM   4673 H HZ1  . LYS   B 1 55  ? 61.021 -26.620 1.664   1.00 32.35 ?  55  LYS   B HZ1  1 
ATOM   4674 H HZ2  . LYS   B 1 55  ? 60.441 -26.913 0.369   1.00 32.35 ?  55  LYS   B HZ2  1 
ATOM   4675 H HZ3  . LYS   B 1 55  ? 61.844 -26.569 0.472   1.00 32.35 ?  55  LYS   B HZ3  1 
ATOM   4676 N N    . ALA   B 1 56  ? 58.230 -20.631 -2.950  1.00 13.61 ?  56  ALA   B N    1 
ATOM   4677 C CA   . ALA   B 1 56  ? 58.443 -20.122 -4.300  1.00 14.44 ?  56  ALA   B CA   1 
ATOM   4678 C C    . ALA   B 1 56  ? 58.721 -18.627 -4.294  1.00 14.04 ?  56  ALA   B C    1 
ATOM   4679 O O    . ALA   B 1 56  ? 59.456 -18.128 -5.156  1.00 15.22 ?  56  ALA   B O    1 
ATOM   4680 C CB   . ALA   B 1 56  ? 57.242 -20.451 -5.187  1.00 15.33 ?  56  ALA   B CB   1 
ATOM   4681 H H    . ALA   B 1 56  ? 57.445 -20.964 -2.812  1.00 16.34 ?  56  ALA   B H    1 
ATOM   4682 H HA   . ALA   B 1 56  ? 59.219 -20.559 -4.676  1.00 17.33 ?  56  ALA   B HA   1 
ATOM   4683 H HB1  . ALA   B 1 56  ? 57.409 -20.111 -6.082  1.00 18.40 ?  56  ALA   B HB1  1 
ATOM   4684 H HB2  . ALA   B 1 56  ? 57.129 -21.414 -5.217  1.00 18.40 ?  56  ALA   B HB2  1 
ATOM   4685 H HB3  . ALA   B 1 56  ? 56.450 -20.034 -4.818  1.00 18.40 ?  56  ALA   B HB3  1 
ATOM   4686 N N    . THR   B 1 57  ? 58.156 -17.897 -3.331  1.00 14.05 ?  57  THR   B N    1 
ATOM   4687 C CA   . THR   B 1 57  ? 58.392 -16.463 -3.206  1.00 13.82 ?  57  THR   B CA   1 
ATOM   4688 C C    . THR   B 1 57  ? 59.642 -16.140 -2.393  1.00 14.71 ?  57  THR   B C    1 
ATOM   4689 O O    . THR   B 1 57  ? 59.874 -14.966 -2.080  1.00 15.29 ?  57  THR   B O    1 
ATOM   4690 C CB   . THR   B 1 57  ? 57.192 -15.736 -2.571  1.00 13.35 ?  57  THR   B CB   1 
ATOM   4691 O OG1  . THR   B 1 57  ? 57.167 -15.954 -1.153  1.00 13.43 ?  57  THR   B OG1  1 
ATOM   4692 C CG2  . THR   B 1 57  ? 55.870 -16.149 -3.215  1.00 13.47 ?  57  THR   B CG2  1 
ATOM   4693 H H    . THR   B 1 57  ? 57.615 -18.210 -2.737  1.00 16.86 ?  57  THR   B H    1 
ATOM   4694 H HA   . THR   B 1 57  ? 58.517 -16.093 -4.095  1.00 16.58 ?  57  THR   B HA   1 
ATOM   4695 H HB   . THR   B 1 57  ? 57.299 -14.784 -2.733  1.00 16.02 ?  57  THR   B HB   1 
ATOM   4696 H HG1  . THR   B 1 57  ? 57.100 -16.773 -0.992  1.00 16.12 ?  57  THR   B HG1  1 
ATOM   4697 H HG21 . THR   B 1 57  ? 55.144 -15.622 -2.853  1.00 16.16 ?  57  THR   B HG21 1 
ATOM   4698 H HG22 . THR   B 1 57  ? 55.910 -16.014 -4.176  1.00 16.16 ?  57  THR   B HG22 1 
ATOM   4699 H HG23 . THR   B 1 57  ? 55.695 -17.088 -3.041  1.00 16.16 ?  57  THR   B HG23 1 
ATOM   4700 N N    . ASN   B 1 58  ? 60.441 -17.142 -2.031  1.00 15.28 ?  58  ASN   B N    1 
ATOM   4701 C CA   . ASN   B 1 58  ? 61.639 -16.911 -1.229  1.00 17.92 ?  58  ASN   B CA   1 
ATOM   4702 C C    . ASN   B 1 58  ? 61.297 -16.203 0.083   1.00 16.01 ?  58  ASN   B C    1 
ATOM   4703 O O    . ASN   B 1 58  ? 62.037 -15.336 0.557   1.00 16.60 ?  58  ASN   B O    1 
ATOM   4704 C CB   . ASN   B 1 58  ? 62.713 -16.150 -2.015  1.00 24.16 ?  58  ASN   B CB   1 
ATOM   4705 C CG   . ASN   B 1 58  ? 64.086 -16.260 -1.382  1.00 31.57 ?  58  ASN   B CG   1 
ATOM   4706 O OD1  . ASN   B 1 58  ? 64.401 -17.256 -0.730  1.00 35.24 ?  58  ASN   B OD1  1 
ATOM   4707 N ND2  . ASN   B 1 58  ? 64.910 -15.234 -1.567  1.00 36.63 ?  58  ASN   B ND2  1 
ATOM   4708 H H    . ASN   B 1 58  ? 60.307 -17.971 -2.231  1.00 18.33 ?  58  ASN   B H    1 
ATOM   4709 H HA   . ASN   B 1 58  ? 62.016 -17.775 -0.999  1.00 21.51 ?  58  ASN   B HA   1 
ATOM   4710 H HB2  . ASN   B 1 58  ? 62.765 -16.515 -2.916  1.00 28.99 ?  58  ASN   B HB2  1 
ATOM   4711 H HB3  . ASN   B 1 58  ? 62.475 -15.212 -2.053  1.00 28.99 ?  58  ASN   B HB3  1 
ATOM   4712 H HD21 . ASN   B 1 58  ? 65.701 -15.250 -1.229  1.00 43.96 ?  58  ASN   B HD21 1 
ATOM   4713 H HD22 . ASN   B 1 58  ? 64.653 -14.554 -2.027  1.00 43.96 ?  58  ASN   B HD22 1 
ATOM   4714 N N    . ASN   B 1 59  ? 60.171 -16.590 0.684   1.00 15.07 ?  59  ASN   B N    1 
ATOM   4715 C CA   . ASN   B 1 59  ? 59.694 -16.126 1.988   1.00 14.97 ?  59  ASN   B CA   1 
ATOM   4716 C C    . ASN   B 1 59  ? 59.094 -14.722 1.936   1.00 14.32 ?  59  ASN   B C    1 
ATOM   4717 O O    . ASN   B 1 59  ? 58.657 -14.222 2.981   1.00 14.49 ?  59  ASN   B O    1 
ATOM   4718 C CB   . ASN   B 1 59  ? 60.765 -16.183 3.093   1.00 16.37 ?  59  ASN   B CB   1 
ATOM   4719 C CG   . ASN   B 1 59  ? 60.175 -16.371 4.471   1.00 17.40 ?  59  ASN   B CG   1 
ATOM   4720 O OD1  . ASN   B 1 59  ? 59.348 -17.259 4.686   1.00 17.76 ?  59  ASN   B OD1  1 
ATOM   4721 N ND2  . ASN   B 1 59  ? 60.592 -15.536 5.415   1.00 18.19 ?  59  ASN   B ND2  1 
ATOM   4722 H H    . ASN   B 1 59  ? 59.636 -17.167 0.337   1.00 18.08 ?  59  ASN   B H    1 
ATOM   4723 H HA   . ASN   B 1 59  ? 58.986 -16.725 2.267   1.00 17.96 ?  59  ASN   B HA   1 
ATOM   4724 H HB2  . ASN   B 1 59  ? 61.362 -16.929 2.928   1.00 19.65 ?  59  ASN   B HB2  1 
ATOM   4725 H HB3  . ASN   B 1 59  ? 61.264 -15.352 3.101   1.00 19.65 ?  59  ASN   B HB3  1 
ATOM   4726 H HD21 . ASN   B 1 59  ? 60.283 -15.601 6.217   1.00 21.83 ?  59  ASN   B HD21 1 
ATOM   4727 H HD22 . ASN   B 1 59  ? 61.169 -14.928 5.227   1.00 21.83 ?  59  ASN   B HD22 1 
ATOM   4728 N N    . ALA   B 1 60  ? 59.037 -14.074 0.769   1.00 14.16 ?  60  ALA   B N    1 
ATOM   4729 C CA   . ALA   B 1 60  ? 58.437 -12.742 0.699   1.00 14.02 ?  60  ALA   B CA   1 
ATOM   4730 C C    . ALA   B 1 60  ? 56.969 -12.773 1.102   1.00 13.33 ?  60  ALA   B C    1 
ATOM   4731 O O    . ALA   B 1 60  ? 56.461 -11.825 1.716   1.00 13.89 ?  60  ALA   B O    1 
ATOM   4732 C CB   . ALA   B 1 60  ? 58.597 -12.161 -0.705  1.00 14.90 ?  60  ALA   B CB   1 
ATOM   4733 H H    . ALA   B 1 60  ? 59.334 -14.379 0.024   1.00 16.99 ?  60  ALA   B H    1 
ATOM   4734 H HA   . ALA   B 1 60  ? 58.901 -12.159 1.319   1.00 16.83 ?  60  ALA   B HA   1 
ATOM   4735 H HB1  . ALA   B 1 60  ? 58.195 -11.281 -0.728  1.00 17.88 ?  60  ALA   B HB1  1 
ATOM   4736 H HB2  . ALA   B 1 60  ? 59.544 -12.100 -0.915  1.00 17.88 ?  60  ALA   B HB2  1 
ATOM   4737 H HB3  . ALA   B 1 60  ? 58.156 -12.747 -1.340  1.00 17.88 ?  60  ALA   B HB3  1 
ATOM   4738 N N    . MET   B 1 61  ? 56.265 -13.852 0.752   1.00 12.82 ?  61  MET   B N    1 
ATOM   4739 C CA   . MET   B 1 61  ? 54.871 -13.975 1.144   1.00 12.61 ?  61  MET   B CA   1 
ATOM   4740 C C    . MET   B 1 61  ? 54.732 -13.986 2.665   1.00 13.00 ?  61  MET   B C    1 
ATOM   4741 O O    . MET   B 1 61  ? 53.828 -13.344 3.217   1.00 12.49 ?  61  MET   B O    1 
ATOM   4742 C CB   . MET   B 1 61  ? 54.290 -15.240 0.511   1.00 12.55 ?  61  MET   B CB   1 
ATOM   4743 C CG   . MET   B 1 61  ? 52.850 -15.534 0.923   1.00 12.36 ?  61  MET   B CG   1 
ATOM   4744 S SD   . MET   B 1 61  ? 52.203 -17.046 0.167   1.00 12.85 ?  61  MET   B SD   1 
ATOM   4745 C CE   . MET   B 1 61  ? 51.954 -16.469 -1.511  1.00 14.25 ?  61  MET   B CE   1 
ATOM   4746 H H    . MET   B 1 61  ? 56.573 -14.514 0.291   1.00 15.38 ?  61  MET   B H    1 
ATOM   4747 H HA   . MET   B 1 61  ? 54.379 -13.218 0.786   1.00 15.14 ?  61  MET   B HA   1 
ATOM   4748 H HB2  . MET   B 1 61  ? 54.301 -15.143 -0.458  1.00 15.06 ?  61  MET   B HB2  1 
ATOM   4749 H HB3  . MET   B 1 61  ? 54.831 -16.000 0.767   1.00 15.06 ?  61  MET   B HB3  1 
ATOM   4750 H HG2  . MET   B 1 61  ? 52.809 -15.651 1.885   1.00 14.83 ?  61  MET   B HG2  1 
ATOM   4751 H HG3  . MET   B 1 61  ? 52.282 -14.797 0.653   1.00 14.83 ?  61  MET   B HG3  1 
ATOM   4752 H HE1  . MET   B 1 61  ? 51.573 -17.190 -2.038  1.00 17.10 ?  61  MET   B HE1  1 
ATOM   4753 H HE2  . MET   B 1 61  ? 51.353 -15.710 -1.502  1.00 17.10 ?  61  MET   B HE2  1 
ATOM   4754 H HE3  . MET   B 1 61  ? 52.813 -16.208 -1.884  1.00 17.10 ?  61  MET   B HE3  1 
ATOM   4755 N N    . GLN   B 1 62  ? 55.616 -14.705 3.363   1.00 12.50 ?  62  GLN   B N    1 
ATOM   4756 C CA   . GLN   B 1 62  ? 55.512 -14.768 4.817   1.00 12.79 ?  62  GLN   B CA   1 
ATOM   4757 C C    . GLN   B 1 62  ? 55.794 -13.416 5.458   1.00 13.26 ?  62  GLN   B C    1 
ATOM   4758 O O    . GLN   B 1 62  ? 55.113 -13.025 6.413   1.00 13.74 ?  62  GLN   B O    1 
ATOM   4759 C CB   . GLN   B 1 62  ? 56.460 -15.828 5.376   1.00 12.93 ?  62  GLN   B CB   1 
ATOM   4760 C CG   . GLN   B 1 62  ? 56.241 -16.103 6.852   1.00 13.34 ?  62  GLN   B CG   1 
ATOM   4761 C CD   . GLN   B 1 62  ? 54.866 -16.691 7.101   1.00 13.20 ?  62  GLN   B CD   1 
ATOM   4762 O OE1  . GLN   B 1 62  ? 54.608 -17.845 6.753   1.00 13.56 ?  62  GLN   B OE1  1 
ATOM   4763 N NE2  . GLN   B 1 62  ? 53.959 -15.893 7.662   1.00 13.67 ?  62  GLN   B NE2  1 
ATOM   4764 H H    . GLN   B 1 62  ? 56.262 -15.159 3.021   1.00 15.00 ?  62  GLN   B H    1 
ATOM   4765 H HA   . GLN   B 1 62  ? 54.607 -15.024 5.051   1.00 15.35 ?  62  GLN   B HA   1 
ATOM   4766 H HB2  . GLN   B 1 62  ? 56.331 -16.660 4.894   1.00 15.51 ?  62  GLN   B HB2  1 
ATOM   4767 H HB3  . GLN   B 1 62  ? 57.378 -15.524 5.263   1.00 15.51 ?  62  GLN   B HB3  1 
ATOM   4768 H HG2  . GLN   B 1 62  ? 56.906 -16.744 7.159   1.00 16.01 ?  62  GLN   B HG2  1 
ATOM   4769 H HG3  . GLN   B 1 62  ? 56.318 -15.278 7.351   1.00 16.01 ?  62  GLN   B HG3  1 
ATOM   4770 H HE21 . GLN   B 1 62  ? 54.173 -15.088 7.879   1.00 16.40 ?  62  GLN   B HE21 1 
ATOM   4771 H HE22 . GLN   B 1 62  ? 53.166 -16.184 7.814   1.00 16.40 ?  62  GLN   B HE22 1 
ATOM   4772 N N    . VAL   B 1 63  ? 56.805 -12.696 4.966   1.00 13.82 ?  63  VAL   B N    1 
ATOM   4773 C CA   . VAL   B 1 63  ? 57.108 -11.380 5.525   1.00 14.74 ?  63  VAL   B CA   1 
ATOM   4774 C C    . VAL   B 1 63  ? 55.916 -10.449 5.348   1.00 13.83 ?  63  VAL   B C    1 
ATOM   4775 O O    . VAL   B 1 63  ? 55.505 -9.745  6.281   1.00 14.59 ?  63  VAL   B O    1 
ATOM   4776 C CB   . VAL   B 1 63  ? 58.393 -10.813 4.899   1.00 15.96 ?  63  VAL   B CB   1 
ATOM   4777 C CG1  . VAL   B 1 63  ? 58.618 -9.375  5.351   1.00 16.67 ?  63  VAL   B CG1  1 
ATOM   4778 C CG2  . VAL   B 1 63  ? 59.582 -11.685 5.283   1.00 16.46 ?  63  VAL   B CG2  1 
ATOM   4779 H H    . VAL   B 1 63  ? 57.317 -12.942 4.316   1.00 16.59 ?  63  VAL   B H    1 
ATOM   4780 H HA   . VAL   B 1 63  ? 57.268 -11.480 6.474   1.00 17.69 ?  63  VAL   B HA   1 
ATOM   4781 H HB   . VAL   B 1 63  ? 58.318 -10.823 3.932   1.00 19.16 ?  63  VAL   B HB   1 
ATOM   4782 H HG11 . VAL   B 1 63  ? 59.535 -9.126  5.163   1.00 20.01 ?  63  VAL   B HG11 1 
ATOM   4783 H HG12 . VAL   B 1 63  ? 58.010 -8.796  4.870   1.00 20.01 ?  63  VAL   B HG12 1 
ATOM   4784 H HG13 . VAL   B 1 63  ? 58.450 -9.319  6.306   1.00 20.01 ?  63  VAL   B HG13 1 
ATOM   4785 H HG21 . VAL   B 1 63  ? 60.393 -11.306 4.903   1.00 19.75 ?  63  VAL   B HG21 1 
ATOM   4786 H HG22 . VAL   B 1 63  ? 59.658 -11.708 6.253   1.00 19.75 ?  63  VAL   B HG22 1 
ATOM   4787 H HG23 . VAL   B 1 63  ? 59.446 -12.581 4.943   1.00 19.75 ?  63  VAL   B HG23 1 
ATOM   4788 N N    . GLU   B 1 64  ? 55.344 -10.435 4.143   1.00 13.48 ?  64  GLU   B N    1 
ATOM   4789 C CA   . GLU   B 1 64  ? 54.175 -9.601  3.872   1.00 13.10 ?  64  GLU   B CA   1 
ATOM   4790 C C    . GLU   B 1 64  ? 52.996 -10.004 4.750   1.00 12.86 ?  64  GLU   B C    1 
ATOM   4791 O O    . GLU   B 1 64  ? 52.252 -9.142  5.250   1.00 13.23 ?  64  GLU   B O    1 
ATOM   4792 C CB   . GLU   B 1 64  ? 53.813 -9.743  2.395   1.00 13.40 ?  64  GLU   B CB   1 
ATOM   4793 C CG   . GLU   B 1 64  ? 52.542 -9.014  1.970   1.00 13.69 ?  64  GLU   B CG   1 
ATOM   4794 C CD   . GLU   B 1 64  ? 52.007 -9.506  0.632   1.00 14.37 ?  64  GLU   B CD   1 
ATOM   4795 O OE1  . GLU   B 1 64  ? 52.195 -10.710 0.305   1.00 15.02 ?  64  GLU   B OE1  1 
ATOM   4796 O OE2  . GLU   B 1 64  ? 51.383 -8.687  -0.086  1.00 15.12 -1 64  GLU   B OE2  1 
ATOM   4797 H H    . GLU   B 1 64  ? 55.620 -10.893 3.465   1.00 16.18 ?  64  GLU   B H    1 
ATOM   4798 H HA   . GLU   B 1 64  ? 54.389 -8.674  4.050   1.00 15.72 ?  64  GLU   B HA   1 
ATOM   4799 H HB2  . GLU   B 1 64  ? 54.539 -9.381  1.859   1.00 16.07 ?  64  GLU   B HB2  1 
ATOM   4800 H HB3  . GLU   B 1 64  ? 53.693 -10.680 2.191   1.00 16.07 ?  64  GLU   B HB3  1 
ATOM   4801 H HG2  . GLU   B 1 64  ? 51.845 -9.154  2.634   1.00 16.42 ?  64  GLU   B HG2  1 
ATOM   4802 H HG3  . GLU   B 1 64  ? 52.731 -8.067  1.889   1.00 16.42 ?  64  GLU   B HG3  1 
ATOM   4803 N N    . SER   B 1 65  ? 52.811 -11.312 4.937   1.00 12.57 ?  65  SER   B N    1 
ATOM   4804 C CA   . SER   B 1 65  ? 51.707 -11.821 5.739   1.00 12.58 ?  65  SER   B CA   1 
ATOM   4805 C C    . SER   B 1 65  ? 51.845 -11.426 7.203   1.00 12.59 ?  65  SER   B C    1 
ATOM   4806 O O    . SER   B 1 65  ? 50.848 -11.066 7.846   1.00 13.08 ?  65  SER   B O    1 
ATOM   4807 C CB   . SER   B 1 65  ? 51.626 -13.343 5.603   1.00 12.74 ?  65  SER   B CB   1 
ATOM   4808 O OG   . SER   B 1 65  ? 51.279 -13.732 4.281   1.00 12.92 ?  65  SER   B OG   1 
ATOM   4809 H H    . SER   B 1 65  ? 53.321 -11.934 4.612   1.00 15.08 ?  65  SER   B H    1 
ATOM   4810 H HA   . SER   B 1 65  ? 50.876 -11.454 5.403   1.00 15.10 ?  65  SER   B HA   1 
ATOM   4811 H HB2  . SER   B 1 65  ? 52.486 -13.731 5.824   1.00 15.29 ?  65  SER   B HB2  1 
ATOM   4812 H HB3  . SER   B 1 65  ? 50.947 -13.681 6.212   1.00 15.29 ?  65  SER   B HB3  1 
ATOM   4813 H HG   . SER   B 1 65  ? 51.857 -13.444 3.735   1.00 15.51 ?  65  SER   B HG   1 
ATOM   4814 N N    . ASP   B 1 66  ? 53.054 -11.529 7.764   1.00 13.24 ?  66  ASP   B N    1 
ATOM   4815 C CA   . ASP   B 1 66  ? 53.239 -11.144 9.160   1.00 13.60 ?  66  ASP   B CA   1 
ATOM   4816 C C    . ASP   B 1 66  ? 52.922 -9.666  9.368   1.00 13.85 ?  66  ASP   B C    1 
ATOM   4817 O O    . ASP   B 1 66  ? 52.346 -9.281  10.393  1.00 14.22 ?  66  ASP   B O    1 
ATOM   4818 C CB   . ASP   B 1 66  ? 54.669 -11.448 9.609   1.00 14.83 ?  66  ASP   B CB   1 
ATOM   4819 C CG   . ASP   B 1 66  ? 54.939 -12.937 9.766   1.00 16.59 ?  66  ASP   B CG   1 
ATOM   4820 O OD1  . ASP   B 1 66  ? 53.995 -13.760 9.691   1.00 17.32 ?  66  ASP   B OD1  1 
ATOM   4821 O OD2  . ASP   B 1 66  ? 56.119 -13.292 9.981   1.00 19.27 -1 66  ASP   B OD2  1 
ATOM   4822 H H    . ASP   B 1 66  ? 53.757 -11.825 7.372   1.00 15.89 ?  66  ASP   B H    1 
ATOM   4823 H HA   . ASP   B 1 66  ? 52.640 -11.657 9.723   1.00 16.32 ?  66  ASP   B HA   1 
ATOM   4824 H HB2  . ASP   B 1 66  ? 55.292 -11.104 8.948   1.00 17.79 ?  66  ASP   B HB2  1 
ATOM   4825 H HB3  . ASP   B 1 66  ? 54.834 -11.019 10.468  1.00 17.79 ?  66  ASP   B HB3  1 
ATOM   4826 N N    . ASP   B 1 67  ? 53.301 -8.817  8.410   1.00 13.44 ?  67  ASP   B N    1 
ATOM   4827 C CA   . ASP   B 1 67  ? 52.955 -7.406  8.505   1.00 13.91 ?  67  ASP   B CA   1 
ATOM   4828 C C    . ASP   B 1 67  ? 51.442 -7.200  8.421   1.00 14.08 ?  67  ASP   B C    1 
ATOM   4829 O O    . ASP   B 1 67  ? 50.878 -6.394  9.170   1.00 14.58 ?  67  ASP   B O    1 
ATOM   4830 C CB   . ASP   B 1 67  ? 53.675 -6.628  7.411   1.00 15.08 ?  67  ASP   B CB   1 
ATOM   4831 C CG   . ASP   B 1 67  ? 53.250 -5.185  7.375   1.00 16.37 ?  67  ASP   B CG   1 
ATOM   4832 O OD1  . ASP   B 1 67  ? 53.751 -4.376  8.193   1.00 17.63 ?  67  ASP   B OD1  1 
ATOM   4833 O OD2  . ASP   B 1 67  ? 52.375 -4.882  6.546   1.00 17.53 -1 67  ASP   B OD2  1 
ATOM   4834 H H    . ASP   B 1 67  ? 53.751 -9.035  7.708   1.00 16.13 ?  67  ASP   B H    1 
ATOM   4835 H HA   . ASP   B 1 67  ? 53.255 -7.065  9.359   1.00 16.70 ?  67  ASP   B HA   1 
ATOM   4836 H HB2  . ASP   B 1 67  ? 54.632 -6.656  7.576   1.00 18.09 ?  67  ASP   B HB2  1 
ATOM   4837 H HB3  . ASP   B 1 67  ? 53.479 -7.034  6.547   1.00 18.09 ?  67  ASP   B HB3  1 
ATOM   4838 N N    . TYR   B 1 68  ? 50.765 -7.929  7.528   1.00 14.12 ?  68  TYR   B N    1 
ATOM   4839 C CA   . TYR   B 1 68  ? 49.305 -7.857  7.457   1.00 14.45 ?  68  TYR   B CA   1 
ATOM   4840 C C    . TYR   B 1 68  ? 48.670 -8.202  8.800   1.00 13.82 ?  68  TYR   B C    1 
ATOM   4841 O O    . TYR   B 1 68  ? 47.738 -7.526  9.253   1.00 14.67 ?  68  TYR   B O    1 
ATOM   4842 C CB   . TYR   B 1 68  ? 48.772 -8.790  6.363   1.00 15.42 ?  68  TYR   B CB   1 
ATOM   4843 C CG   . TYR   B 1 68  ? 47.265 -8.941  6.422   1.00 16.44 ?  68  TYR   B CG   1 
ATOM   4844 C CD1  . TYR   B 1 68  ? 46.670 -9.904  7.236   1.00 17.17 ?  68  TYR   B CD1  1 
ATOM   4845 C CD2  . TYR   B 1 68  ? 46.439 -8.099  5.701   1.00 17.35 ?  68  TYR   B CD2  1 
ATOM   4846 C CE1  . TYR   B 1 68  ? 45.304 -10.026 7.321   1.00 18.39 ?  68  TYR   B CE1  1 
ATOM   4847 C CE2  . TYR   B 1 68  ? 45.057 -8.223  5.774   1.00 18.02 ?  68  TYR   B CE2  1 
ATOM   4848 C CZ   . TYR   B 1 68  ? 44.509 -9.184  6.587   1.00 18.28 ?  68  TYR   B CZ   1 
ATOM   4849 O OH   . TYR   B 1 68  ? 43.142 -9.301  6.676   1.00 19.24 ?  68  TYR   B OH   1 
ATOM   4850 H H    . TYR   B 1 68  ? 51.123 -8.477  6.960   1.00 16.95 ?  68  TYR   B H    1 
ATOM   4851 H HA   . TYR   B 1 68  ? 49.051 -6.951  7.230   1.00 17.33 ?  68  TYR   B HA   1 
ATOM   4852 H HB2  . TYR   B 1 68  ? 48.998 -8.425  5.496   1.00 18.51 ?  68  TYR   B HB2  1 
ATOM   4853 H HB3  . TYR   B 1 68  ? 49.164 -9.668  6.473   1.00 18.51 ?  68  TYR   B HB3  1 
ATOM   4854 H HD1  . TYR   B 1 68  ? 47.207 -10.478 7.736   1.00 20.60 ?  68  TYR   B HD1  1 
ATOM   4855 H HD2  . TYR   B 1 68  ? 46.810 -7.443  5.164   1.00 20.82 ?  68  TYR   B HD2  1 
ATOM   4856 H HE1  . TYR   B 1 68  ? 44.919 -10.686 7.860   1.00 22.06 ?  68  TYR   B HE1  1 
ATOM   4857 H HE2  . TYR   B 1 68  ? 44.505 -7.654  5.288   1.00 21.62 ?  68  TYR   B HE2  1 
ATOM   4858 H HH   . TYR   B 1 68  ? 42.754 -8.742  6.173   1.00 23.09 ?  68  TYR   B HH   1 
ATOM   4859 N N    . ILE   B 1 69  ? 49.148 -9.273  9.441   1.00 13.94 ?  69  ILE   B N    1 
ATOM   4860 C CA   . ILE   B 1 69  ? 48.593 -9.702  10.722  1.00 14.50 ?  69  ILE   B CA   1 
ATOM   4861 C C    . ILE   B 1 69  ? 48.850 -8.659  11.802  1.00 14.07 ?  69  ILE   B C    1 
ATOM   4862 O O    . ILE   B 1 69  ? 47.982 -8.386  12.637  1.00 14.68 ?  69  ILE   B O    1 
ATOM   4863 C CB   . ILE   B 1 69  ? 49.162 -11.083 11.107  1.00 15.53 ?  69  ILE   B CB   1 
ATOM   4864 C CG1  . ILE   B 1 69  ? 48.632 -12.176 10.169  1.00 15.57 ?  69  ILE   B CG1  1 
ATOM   4865 C CG2  . ILE   B 1 69  ? 48.881 -11.404 12.570  1.00 16.78 ?  69  ILE   B CG2  1 
ATOM   4866 C CD1  . ILE   B 1 69  ? 47.161 -12.505 10.335  1.00 15.95 ?  69  ILE   B CD1  1 
ATOM   4867 H H    . ILE   B 1 69  ? 49.794 -9.765  9.158   1.00 16.73 ?  69  ILE   B H    1 
ATOM   4868 H HA   . ILE   B 1 69  ? 47.635 -9.794  10.628  1.00 17.39 ?  69  ILE   B HA   1 
ATOM   4869 H HB   . ILE   B 1 69  ? 50.126 -11.044 10.997  1.00 18.63 ?  69  ILE   B HB   1 
ATOM   4870 H HG12 . ILE   B 1 69  ? 48.767 -11.884 9.253   1.00 18.69 ?  69  ILE   B HG12 1 
ATOM   4871 H HG13 . ILE   B 1 69  ? 49.137 -12.988 10.328  1.00 18.69 ?  69  ILE   B HG13 1 
ATOM   4872 H HG21 . ILE   B 1 69  ? 49.028 -12.354 12.713  1.00 20.14 ?  69  ILE   B HG21 1 
ATOM   4873 H HG22 . ILE   B 1 69  ? 49.483 -10.893 13.132  1.00 20.14 ?  69  ILE   B HG22 1 
ATOM   4874 H HG23 . ILE   B 1 69  ? 47.961 -11.180 12.773  1.00 20.14 ?  69  ILE   B HG23 1 
ATOM   4875 H HD11 . ILE   B 1 69  ? 46.924 -13.198 9.700   1.00 19.15 ?  69  ILE   B HD11 1 
ATOM   4876 H HD12 . ILE   B 1 69  ? 47.008 -12.821 11.240  1.00 19.15 ?  69  ILE   B HD12 1 
ATOM   4877 H HD13 . ILE   B 1 69  ? 46.636 -11.709 10.168  1.00 19.15 ?  69  ILE   B HD13 1 
ATOM   4878 N N    . ALA   B 1 70  ? 50.046 -8.069  11.819  1.00 14.09 ?  70  ALA   B N    1 
ATOM   4879 C CA   . ALA   B 1 70  ? 50.331 -7.033  12.807  1.00 13.98 ?  70  ALA   B CA   1 
ATOM   4880 C C    . ALA   B 1 70  ? 49.334 -5.888  12.700  1.00 14.20 ?  70  ALA   B C    1 
ATOM   4881 O O    . ALA   B 1 70  ? 48.892 -5.345  13.717  1.00 14.51 ?  70  ALA   B O    1 
ATOM   4882 C CB   . ALA   B 1 70  ? 51.760 -6.522  12.632  1.00 14.66 ?  70  ALA   B CB   1 
ATOM   4883 H H    . ALA   B 1 70  ? 50.689 -8.247  11.284  1.00 16.91 ?  70  ALA   B H    1 
ATOM   4884 H HA   . ALA   B 1 70  ? 50.259 -7.413  13.697  1.00 16.77 ?  70  ALA   B HA   1 
ATOM   4885 H HB1  . ALA   B 1 70  ? 51.951 -5.867  13.322  1.00 17.59 ?  70  ALA   B HB1  1 
ATOM   4886 H HB2  . ALA   B 1 70  ? 52.377 -7.269  12.711  1.00 17.59 ?  70  ALA   B HB2  1 
ATOM   4887 H HB3  . ALA   B 1 70  ? 51.849 -6.116  11.755  1.00 17.59 ?  70  ALA   B HB3  1 
ATOM   4888 N N    . THR   B 1 71  ? 48.958 -5.519  11.478  1.00 14.71 ?  71  THR   B N    1 
ATOM   4889 C CA   . THR   B 1 71  ? 48.063 -4.386  11.272  1.00 15.79 ?  71  THR   B CA   1 
ATOM   4890 C C    . THR   B 1 71  ? 46.596 -4.754  11.478  1.00 16.18 ?  71  THR   B C    1 
ATOM   4891 O O    . THR   B 1 71  ? 45.816 -3.938  11.989  1.00 17.77 ?  71  THR   B O    1 
ATOM   4892 C CB   . THR   B 1 71  ? 48.280 -3.817  9.868   1.00 17.49 ?  71  THR   B CB   1 
ATOM   4893 O OG1  . THR   B 1 71  ? 49.603 -3.279  9.777   1.00 19.36 ?  71  THR   B OG1  1 
ATOM   4894 C CG2  . THR   B 1 71  ? 47.261 -2.731  9.545   1.00 18.50 ?  71  THR   B CG2  1 
ATOM   4895 H H    . THR   B 1 71  ? 49.209 -5.909  10.755  1.00 17.65 ?  71  THR   B H    1 
ATOM   4896 H HA   . THR   B 1 71  ? 48.287 -3.690  11.909  1.00 18.95 ?  71  THR   B HA   1 
ATOM   4897 H HB   . THR   B 1 71  ? 48.187 -4.528  9.215   1.00 20.99 ?  71  THR   B HB   1 
ATOM   4898 H HG1  . THR   B 1 71  ? 49.737 -2.956  9.010   1.00 23.23 ?  71  THR   B HG1  1 
ATOM   4899 H HG21 . THR   B 1 71  ? 47.567 -2.207  8.787   1.00 22.20 ?  71  THR   B HG21 1 
ATOM   4900 H HG22 . THR   B 1 71  ? 46.406 -3.129  9.327   1.00 22.20 ?  71  THR   B HG22 1 
ATOM   4901 H HG23 . THR   B 1 71  ? 47.154 -2.141  10.308  1.00 22.20 ?  71  THR   B HG23 1 
ATOM   4902 N N    . ASN   B 1 72  ? 46.199 -5.969  11.084  1.00 15.83 ?  72  ASN   B N    1 
ATOM   4903 C CA   . ASN   B 1 72  ? 44.795 -6.326  10.959  1.00 16.29 ?  72  ASN   B CA   1 
ATOM   4904 C C    . ASN   B 1 72  ? 44.326 -7.431  11.895  1.00 16.72 ?  72  ASN   B C    1 
ATOM   4905 O O    . ASN   B 1 72  ? 43.111 -7.594  12.062  1.00 17.68 ?  72  ASN   B O    1 
ATOM   4906 C CB   . ASN   B 1 72  ? 44.486 -6.746  9.512   1.00 17.05 ?  72  ASN   B CB   1 
ATOM   4907 C CG   . ASN   B 1 72  ? 44.774 -5.643  8.518   1.00 18.09 ?  72  ASN   B CG   1 
ATOM   4908 O OD1  . ASN   B 1 72  ? 45.792 -5.656  7.822   1.00 19.05 ?  72  ASN   B OD1  1 
ATOM   4909 N ND2  . ASN   B 1 72  ? 43.900 -4.661  8.474   1.00 19.40 ?  72  ASN   B ND2  1 
ATOM   4910 H H    . ASN   B 1 72  ? 46.743 -6.610  10.882  1.00 19.00 ?  72  ASN   B H    1 
ATOM   4911 H HA   . ASN   B 1 72  ? 44.264 -5.541  11.149  1.00 19.55 ?  72  ASN   B HA   1 
ATOM   4912 H HB2  . ASN   B 1 72  ? 45.037 -7.513  9.281   1.00 20.46 ?  72  ASN   B HB2  1 
ATOM   4913 H HB3  . ASN   B 1 72  ? 43.549 -6.976  9.444   1.00 20.46 ?  72  ASN   B HB3  1 
ATOM   4914 H HD21 . ASN   B 1 72  ? 44.014 -4.008  7.924   1.00 23.28 ?  72  ASN   B HD21 1 
ATOM   4915 H HD22 . ASN   B 1 72  ? 43.200 -4.683  8.974   1.00 23.28 ?  72  ASN   B HD22 1 
ATOM   4916 N N    . GLY   B 1 73  ? 45.230 -8.183  12.513  1.00 16.50 ?  73  GLY   B N    1 
ATOM   4917 C CA   . GLY   B 1 73  ? 44.831 -9.323  13.302  1.00 15.76 ?  73  GLY   B CA   1 
ATOM   4918 C C    . GLY   B 1 73  ? 44.461 -10.504 12.429  1.00 14.50 ?  73  GLY   B C    1 
ATOM   4919 O O    . GLY   B 1 73  ? 44.448 -10.416 11.197  1.00 14.32 ?  73  GLY   B O    1 
ATOM   4920 H H    . GLY   B 1 73  ? 46.081 -8.045  12.491  1.00 19.80 ?  73  GLY   B H    1 
ATOM   4921 H HA2  . GLY   B 1 73  ? 45.562 -9.581  13.889  1.00 18.91 ?  73  GLY   B HA2  1 
ATOM   4922 H HA3  . GLY   B 1 73  ? 44.065 -9.089  13.849  1.00 18.91 ?  73  GLY   B HA3  1 
ATOM   4923 N N    . PRO   B 1 74  ? 44.155 -11.635 13.060  1.00 14.63 ?  74  PRO   B N    1 
ATOM   4924 C CA   . PRO   B 1 74  ? 43.913 -12.867 12.306  1.00 14.37 ?  74  PRO   B CA   1 
ATOM   4925 C C    . PRO   B 1 74  ? 42.612 -12.810 11.517  1.00 13.49 ?  74  PRO   B C    1 
ATOM   4926 O O    . PRO   B 1 74  ? 41.673 -12.069 11.834  1.00 14.91 ?  74  PRO   B O    1 
ATOM   4927 C CB   . PRO   B 1 74  ? 43.843 -13.939 13.400  1.00 15.62 ?  74  PRO   B CB   1 
ATOM   4928 C CG   . PRO   B 1 74  ? 43.392 -13.202 14.617  1.00 17.04 ?  74  PRO   B CG   1 
ATOM   4929 C CD   . PRO   B 1 74  ? 44.043 -11.846 14.513  1.00 16.43 ?  74  PRO   B CD   1 
ATOM   4930 H HA   . PRO   B 1 74  ? 44.657 -13.052 11.708  1.00 17.24 ?  74  PRO   B HA   1 
ATOM   4931 H HB2  . PRO   B 1 74  ? 43.200 -14.620 13.148  1.00 18.75 ?  74  PRO   B HB2  1 
ATOM   4932 H HB3  . PRO   B 1 74  ? 44.722 -14.328 13.535  1.00 18.75 ?  74  PRO   B HB3  1 
ATOM   4933 H HG2  . PRO   B 1 74  ? 42.426 -13.122 14.610  1.00 20.45 ?  74  PRO   B HG2  1 
ATOM   4934 H HG3  . PRO   B 1 74  ? 43.695 -13.669 15.411  1.00 20.45 ?  74  PRO   B HG3  1 
ATOM   4935 H HD2  . PRO   B 1 74  ? 43.474 -11.167 14.916  1.00 19.72 ?  74  PRO   B HD2  1 
ATOM   4936 H HD3  . PRO   B 1 74  ? 44.922 -11.858 14.923  1.00 19.72 ?  74  PRO   B HD3  1 
ATOM   4937 N N    . LEU   B 1 75  ? 42.577 -13.623 10.465  1.00 12.93 ?  75  LEU   B N    1 
ATOM   4938 C CA   . LEU   B 1 75  ? 41.364 -13.835 9.698   1.00 13.19 ?  75  LEU   B CA   1 
ATOM   4939 C C    . LEU   B 1 75  ? 40.394 -14.701 10.498  1.00 13.58 ?  75  LEU   B C    1 
ATOM   4940 O O    . LEU   B 1 75  ? 40.734 -15.252 11.546  1.00 14.73 ?  75  LEU   B O    1 
ATOM   4941 C CB   . LEU   B 1 75  ? 41.691 -14.542 8.383   1.00 13.14 ?  75  LEU   B CB   1 
ATOM   4942 C CG   . LEU   B 1 75  ? 42.537 -13.793 7.348   1.00 15.07 ?  75  LEU   B CG   1 
ATOM   4943 C CD1  . LEU   B 1 75  ? 42.735 -14.633 6.088   1.00 16.41 ?  75  LEU   B CD1  1 
ATOM   4944 C CD2  . LEU   B 1 75  ? 41.952 -12.452 6.999   1.00 18.01 ?  75  LEU   B CD2  1 
ATOM   4945 H H    . LEU   B 1 75  ? 43.252 -14.072 10.174  1.00 15.52 ?  75  LEU   B H    1 
ATOM   4946 H HA   . LEU   B 1 75  ? 40.939 -12.986 9.506   1.00 15.83 ?  75  LEU   B HA   1 
ATOM   4947 H HB2  . LEU   B 1 75  ? 42.166 -15.360 8.595   1.00 15.77 ?  75  LEU   B HB2  1 
ATOM   4948 H HB3  . LEU   B 1 75  ? 40.853 -14.768 7.949   1.00 15.77 ?  75  LEU   B HB3  1 
ATOM   4949 H HG   . LEU   B 1 75  ? 43.415 -13.636 7.727   1.00 18.08 ?  75  LEU   B HG   1 
ATOM   4950 H HD11 . LEU   B 1 75  ? 43.280 -14.131 5.455   1.00 19.69 ?  75  LEU   B HD11 1 
ATOM   4951 H HD12 . LEU   B 1 75  ? 43.189 -15.459 6.324   1.00 19.69 ?  75  LEU   B HD12 1 
ATOM   4952 H HD13 . LEU   B 1 75  ? 41.873 -14.829 5.695   1.00 19.69 ?  75  LEU   B HD13 1 
ATOM   4953 H HD21 . LEU   B 1 75  ? 42.476 -12.051 6.291   1.00 21.61 ?  75  LEU   B HD21 1 
ATOM   4954 H HD22 . LEU   B 1 75  ? 41.035 -12.574 6.707   1.00 21.61 ?  75  LEU   B HD22 1 
ATOM   4955 H HD23 . LEU   B 1 75  ? 41.973 -11.885 7.788   1.00 21.61 ?  75  LEU   B HD23 1 
ATOM   4956 N N    . LYS   B 1 76  ? 39.168 -14.813 9.983   1.00 14.67 ?  76  LYS   B N    1 
ATOM   4957 C CA   . LYS   B 1 76  ? 38.178 -15.773 10.456  1.00 15.95 ?  76  LYS   B CA   1 
ATOM   4958 C C    . LYS   B 1 76  ? 38.266 -17.040 9.610   1.00 14.43 ?  76  LYS   B C    1 
ATOM   4959 O O    . LYS   B 1 76  ? 38.535 -16.974 8.411   1.00 13.96 ?  76  LYS   B O    1 
ATOM   4960 C CB   . LYS   B 1 76  ? 36.762 -15.198 10.280  1.00 18.77 ?  76  LYS   B CB   1 
ATOM   4961 C CG   . LYS   B 1 76  ? 36.494 -13.812 10.891  1.00 21.02 ?  76  LYS   B CG   1 
ATOM   4962 C CD   . LYS   B 1 76  ? 35.089 -13.277 10.535  1.00 22.78 ?  76  LYS   B CD   1 
ATOM   4963 C CE   . LYS   B 1 76  ? 34.817 -11.920 11.172  1.00 24.78 ?  76  LYS   B CE   1 
ATOM   4964 N NZ   . LYS   B 1 76  ? 33.526 -11.320 10.722  1.00 25.76 ?  76  LYS   B NZ   1 
ATOM   4965 H H    . LYS   B 1 76  ? 38.881 -14.332 9.332   1.00 17.60 ?  76  LYS   B H    1 
ATOM   4966 H HA   . LYS   B 1 76  ? 38.327 -15.995 11.391  1.00 19.14 ?  76  LYS   B HA   1 
ATOM   4967 H HB2  . LYS   B 1 76  ? 36.580 -15.128 9.328   1.00 22.53 ?  76  LYS   B HB2  1 
ATOM   4968 H HB3  . LYS   B 1 76  ? 36.129 -15.812 10.682  1.00 22.53 ?  76  LYS   B HB3  1 
ATOM   4969 H HG2  . LYS   B 1 76  ? 36.562 -13.872 11.857  1.00 25.22 ?  76  LYS   B HG2  1 
ATOM   4970 H HG3  . LYS   B 1 76  ? 37.154 -13.183 10.552  1.00 25.22 ?  76  LYS   B HG3  1 
ATOM   4971 H HD2  . LYS   B 1 76  ? 35.020 -13.177 9.572   1.00 27.34 ?  76  LYS   B HD2  1 
ATOM   4972 H HD3  . LYS   B 1 76  ? 34.420 -13.901 10.855  1.00 27.34 ?  76  LYS   B HD3  1 
ATOM   4973 H HE2  . LYS   B 1 76  ? 34.780 -12.024 12.136  1.00 29.74 ?  76  LYS   B HE2  1 
ATOM   4974 H HE3  . LYS   B 1 76  ? 35.531 -11.308 10.932  1.00 29.74 ?  76  LYS   B HE3  1 
ATOM   4975 H HZ1  . LYS   B 1 76  ? 33.402 -10.529 11.116  1.00 30.92 ?  76  LYS   B HZ1  1 
ATOM   4976 H HZ2  . LYS   B 1 76  ? 33.533 -11.203 9.840   1.00 30.92 ?  76  LYS   B HZ2  1 
ATOM   4977 H HZ3  . LYS   B 1 76  ? 32.848 -11.856 10.936  1.00 30.92 ?  76  LYS   B HZ3  1 
ATOM   4978 N N    . VAL   B 1 77  ? 38.017 -18.201 10.232  1.00 14.98 ?  77  VAL   B N    1 
ATOM   4979 C CA   . VAL   B 1 77  ? 37.801 -19.408 9.440   1.00 15.10 ?  77  VAL   B CA   1 
ATOM   4980 C C    . VAL   B 1 77  ? 36.610 -19.164 8.524   1.00 13.95 ?  77  VAL   B C    1 
ATOM   4981 O O    . VAL   B 1 77  ? 35.545 -18.714 8.970   1.00 13.99 ?  77  VAL   B O    1 
ATOM   4982 C CB   . VAL   B 1 77  ? 37.598 -20.640 10.337  1.00 16.41 ?  77  VAL   B CB   1 
ATOM   4983 C CG1  . VAL   B 1 77  ? 37.297 -21.869 9.483   1.00 17.05 ?  77  VAL   B CG1  1 
ATOM   4984 C CG2  . VAL   B 1 77  ? 38.835 -20.893 11.201  1.00 18.12 ?  77  VAL   B CG2  1 
ATOM   4985 H H    . VAL   B 1 77  ? 37.975 -18.310 11.082  1.00 17.97 ?  77  VAL   B H    1 
ATOM   4986 H HA   . VAL   B 1 77  ? 38.574 -19.566 8.882   1.00 18.12 ?  77  VAL   B HA   1 
ATOM   4987 H HB   . VAL   B 1 77  ? 36.840 -20.486 10.926  1.00 19.69 ?  77  VAL   B HB   1 
ATOM   4988 H HG11 . VAL   B 1 77  ? 37.345 -22.660 10.044  1.00 20.46 ?  77  VAL   B HG11 1 
ATOM   4989 H HG12 . VAL   B 1 77  ? 36.402 -21.788 9.111   1.00 20.46 ?  77  VAL   B HG12 1 
ATOM   4990 H HG13 . VAL   B 1 77  ? 37.948 -21.926 8.771   1.00 20.46 ?  77  VAL   B HG13 1 
ATOM   4991 H HG21 . VAL   B 1 77  ? 38.684 -21.688 11.734  1.00 21.74 ?  77  VAL   B HG21 1 
ATOM   4992 H HG22 . VAL   B 1 77  ? 39.598 -21.018 10.622  1.00 21.74 ?  77  VAL   B HG22 1 
ATOM   4993 H HG23 . VAL   B 1 77  ? 38.973 -20.127 11.779  1.00 21.74 ?  77  VAL   B HG23 1 
ATOM   4994 N N    . GLY   B 1 78  ? 36.791 -19.444 7.234   1.00 13.21 ?  78  GLY   B N    1 
ATOM   4995 C CA   . GLY   B 1 78  ? 35.820 -19.114 6.219   1.00 12.92 ?  78  GLY   B CA   1 
ATOM   4996 C C    . GLY   B 1 78  ? 36.064 -17.793 5.524   1.00 12.52 ?  78  GLY   B C    1 
ATOM   4997 O O    . GLY   B 1 78  ? 35.388 -17.506 4.529   1.00 13.10 ?  78  GLY   B O    1 
ATOM   4998 H H    . GLY   B 1 78  ? 37.490 -19.834 6.922   1.00 15.85 ?  78  GLY   B H    1 
ATOM   4999 H HA2  . GLY   B 1 78  ? 35.815 -19.806 5.544   1.00 15.50 ?  78  GLY   B HA2  1 
ATOM   5000 H HA3  . GLY   B 1 78  ? 34.938 -19.074 6.620   1.00 15.50 ?  78  GLY   B HA3  1 
ATOM   5001 N N    . GLY   B 1 79  ? 37.016 -16.990 6.011   1.00 12.54 ?  79  GLY   B N    1 
ATOM   5002 C CA   . GLY   B 1 79  ? 37.315 -15.691 5.443   1.00 12.31 ?  79  GLY   B CA   1 
ATOM   5003 C C    . GLY   B 1 79  ? 38.554 -15.708 4.558   1.00 12.17 ?  79  GLY   B C    1 
ATOM   5004 O O    . GLY   B 1 79  ? 39.167 -16.744 4.305   1.00 12.60 ?  79  GLY   B O    1 
ATOM   5005 H H    . GLY   B 1 79  ? 37.519 -17.188 6.676   1.00 15.05 ?  79  GLY   B H    1 
ATOM   5006 H HA2  . GLY   B 1 79  ? 36.563 -15.385 4.908   1.00 14.77 ?  79  GLY   B HA2  1 
ATOM   5007 H HA3  . GLY   B 1 79  ? 37.463 -15.050 6.156   1.00 14.77 ?  79  GLY   B HA3  1 
ATOM   5008 N N    . SER   B 1 80  ? 38.922 -14.512 4.091   1.00 12.30 ?  80  SER   B N    1 
ATOM   5009 C CA   . SER   B 1 80  ? 40.023 -14.373 3.149   1.00 11.75 ?  80  SER   B CA   1 
ATOM   5010 C C    . SER   B 1 80  ? 40.602 -12.965 3.216   1.00 11.89 ?  80  SER   B C    1 
ATOM   5011 O O    . SER   B 1 80  ? 39.983 -12.035 3.739   1.00 13.46 ?  80  SER   B O    1 
ATOM   5012 C CB   . SER   B 1 80  ? 39.573 -14.660 1.711   1.00 12.46 ?  80  SER   B CB   1 
ATOM   5013 O OG   . SER   B 1 80  ? 38.738 -13.631 1.208   1.00 13.57 ?  80  SER   B OG   1 
ATOM   5014 H H    . SER   B 1 80  ? 38.553 -13.766 4.307   1.00 14.76 ?  80  SER   B H    1 
ATOM   5015 H HA   . SER   B 1 80  ? 40.718 -15.001 3.387   1.00 14.10 ?  80  SER   B HA   1 
ATOM   5016 H HB2  . SER   B 1 80  ? 40.353 -14.733 1.141   1.00 14.96 ?  80  SER   B HB2  1 
ATOM   5017 H HB3  . SER   B 1 80  ? 39.078 -15.497 1.698   1.00 14.96 ?  80  SER   B HB3  1 
ATOM   5018 H HG   . SER   B 1 80  ? 38.049 -13.559 1.689   1.00 16.28 ?  80  SER   B HG   1 
ATOM   5019 N N    . CYS   B 1 81  ? 41.786 -12.814 2.625   1.00 11.79 ?  81  CYS   B N    1 
ATOM   5020 C CA   . CYS   B 1 81  ? 42.333 -11.502 2.321   1.00 11.99 ?  81  CYS   B CA   1 
ATOM   5021 C C    . CYS   B 1 81  ? 43.107 -11.582 1.014   1.00 11.15 ?  81  CYS   B C    1 
ATOM   5022 O O    . CYS   B 1 81  ? 43.621 -12.643 0.641   1.00 12.22 ?  81  CYS   B O    1 
ATOM   5023 C CB   . CYS   B 1 81  ? 43.222 -10.949 3.450   1.00 12.50 ?  81  CYS   B CB   1 
ATOM   5024 S SG   . CYS   B 1 81  ? 44.746 -11.883 3.700   1.00 12.97 ?  81  CYS   B SG   1 
ATOM   5025 H H    . CYS   B 1 81  ? 42.296 -13.467 2.374   1.00 14.14 ?  81  CYS   B H    1 
ATOM   5026 H HA   . CYS   B 1 81  ? 41.602 -10.877 2.196   1.00 14.39 ?  81  CYS   B HA   1 
ATOM   5027 H HB2  . CYS   B 1 81  ? 43.465 -10.035 3.241   1.00 15.00 ?  81  CYS   B HB2  1 
ATOM   5028 H HB3  . CYS   B 1 81  ? 42.716 -10.970 4.282   1.00 15.00 ?  81  CYS   B HB3  1 
ATOM   5029 H HG   . CYS   B 1 81  ? 45.367 -11.388 4.603   1.00 15.57 ?  81  CYS   B HG   1 
ATOM   5030 N N    . VAL   B 1 82  ? 43.206 -10.439 0.341   1.00 11.53 ?  82  VAL   B N    1 
ATOM   5031 C CA   . VAL   B 1 82  ? 43.969 -10.311 -0.897  1.00 11.86 ?  82  VAL   B CA   1 
ATOM   5032 C C    . VAL   B 1 82  ? 45.307 -9.665  -0.572  1.00 12.15 ?  82  VAL   B C    1 
ATOM   5033 O O    . VAL   B 1 82  ? 45.353 -8.547  -0.034  1.00 13.09 ?  82  VAL   B O    1 
ATOM   5034 C CB   . VAL   B 1 82  ? 43.224 -9.468  -1.942  1.00 13.09 ?  82  VAL   B CB   1 
ATOM   5035 C CG1  . VAL   B 1 82  ? 44.076 -9.312  -3.198  1.00 14.54 ?  82  VAL   B CG1  1 
ATOM   5036 C CG2  . VAL   B 1 82  ? 41.867 -10.070 -2.261  1.00 13.98 ?  82  VAL   B CG2  1 
ATOM   5037 H H    . VAL   B 1 82  ? 42.828 -9.700  0.583   1.00 13.83 ?  82  VAL   B H    1 
ATOM   5038 H HA   . VAL   B 1 82  ? 44.131 -11.189 -1.271  1.00 14.23 ?  82  VAL   B HA   1 
ATOM   5039 H HB   . VAL   B 1 82  ? 43.072 -8.584  -1.582  1.00 15.71 ?  82  VAL   B HB   1 
ATOM   5040 H HG11 . VAL   B 1 82  ? 43.514 -9.006  -3.927  1.00 17.45 ?  82  VAL   B HG11 1 
ATOM   5041 H HG12 . VAL   B 1 82  ? 44.774 -8.656  -3.028  1.00 17.45 ?  82  VAL   B HG12 1 
ATOM   5042 H HG13 . VAL   B 1 82  ? 44.473 -10.166 -3.423  1.00 17.45 ?  82  VAL   B HG13 1 
ATOM   5043 H HG21 . VAL   B 1 82  ? 41.433 -9.538  -2.952  1.00 16.77 ?  82  VAL   B HG21 1 
ATOM   5044 H HG22 . VAL   B 1 82  ? 41.984 -10.981 -2.579  1.00 16.77 ?  82  VAL   B HG22 1 
ATOM   5045 H HG23 . VAL   B 1 82  ? 41.320 -10.071 -1.459  1.00 16.77 ?  82  VAL   B HG23 1 
ATOM   5046 N N    . LEU   B 1 83  ? 46.391 -10.349 -0.938  1.00 11.74 ?  83  LEU   B N    1 
ATOM   5047 C CA   . LEU   B 1 83  ? 47.746 -9.831  -0.820  1.00 11.69 ?  83  LEU   B CA   1 
ATOM   5048 C C    . LEU   B 1 83  ? 48.449 -9.972  -2.170  1.00 11.33 ?  83  LEU   B C    1 
ATOM   5049 O O    . LEU   B 1 83  ? 47.848 -10.385 -3.167  1.00 11.49 ?  83  LEU   B O    1 
ATOM   5050 C CB   . LEU   B 1 83  ? 48.500 -10.509 0.331   1.00 12.15 ?  83  LEU   B CB   1 
ATOM   5051 C CG   . LEU   B 1 83  ? 47.985 -10.151 1.729   1.00 13.38 ?  83  LEU   B CG   1 
ATOM   5052 C CD1  . LEU   B 1 83  ? 48.605 -11.025 2.807   1.00 13.99 ?  83  LEU   B CD1  1 
ATOM   5053 C CD2  . LEU   B 1 83  ? 48.201 -8.666  2.053   1.00 14.48 ?  83  LEU   B CD2  1 
ATOM   5054 H H    . LEU   B 1 83  ? 46.359 -11.144 -1.274  1.00 14.09 ?  83  LEU   B H    1 
ATOM   5055 H HA   . LEU   B 1 83  ? 47.695 -8.885  -0.625  1.00 14.03 ?  83  LEU   B HA   1 
ATOM   5056 H HB2  . LEU   B 1 83  ? 48.429 -11.468 0.226   1.00 14.58 ?  83  LEU   B HB2  1 
ATOM   5057 H HB3  . LEU   B 1 83  ? 49.434 -10.244 0.282   1.00 14.58 ?  83  LEU   B HB3  1 
ATOM   5058 H HG   . LEU   B 1 83  ? 47.031 -10.307 1.745   1.00 16.05 ?  83  LEU   B HG   1 
ATOM   5059 H HD11 . LEU   B 1 83  ? 48.241 -10.766 3.669   1.00 16.78 ?  83  LEU   B HD11 1 
ATOM   5060 H HD12 . LEU   B 1 83  ? 48.383 -11.953 2.622   1.00 16.78 ?  83  LEU   B HD12 1 
ATOM   5061 H HD13 . LEU   B 1 83  ? 49.565 -10.906 2.801   1.00 16.78 ?  83  LEU   B HD13 1 
ATOM   5062 H HD21 . LEU   B 1 83  ? 47.995 -8.517  2.988   1.00 17.38 ?  83  LEU   B HD21 1 
ATOM   5063 H HD22 . LEU   B 1 83  ? 49.125 -8.435  1.874   1.00 17.38 ?  83  LEU   B HD22 1 
ATOM   5064 H HD23 . LEU   B 1 83  ? 47.612 -8.133  1.495   1.00 17.38 ?  83  LEU   B HD23 1 
ATOM   5065 N N    . SER   B 1 84  ? 49.723 -9.588  -2.223  1.00 12.55 ?  84  SER   B N    1 
ATOM   5066 C CA   . SER   B 1 84  ? 50.460 -9.705  -3.472  1.00 12.64 ?  84  SER   B CA   1 
ATOM   5067 C C    . SER   B 1 84  ? 50.615 -11.165 -3.885  1.00 11.94 ?  84  SER   B C    1 
ATOM   5068 O O    . SER   B 1 84  ? 50.729 -12.066 -3.052  1.00 11.71 ?  84  SER   B O    1 
ATOM   5069 C CB   . SER   B 1 84  ? 51.855 -9.099  -3.320  1.00 14.80 ?  84  SER   B CB   1 
ATOM   5070 O OG   . SER   B 1 84  ? 52.606 -9.305  -4.501  1.00 16.50 ?  84  SER   B OG   1 
ATOM   5071 H H    . SER   B 1 84  ? 50.168 -9.250  -1.566  1.00 15.06 ?  84  SER   B H    1 
ATOM   5072 H HA   . SER   B 1 84  ? 49.995 -9.231  -4.175  1.00 15.17 ?  84  SER   B HA   1 
ATOM   5073 H HB2  . SER   B 1 84  ? 51.771 -8.141  -3.156  1.00 17.76 ?  84  SER   B HB2  1 
ATOM   5074 H HB3  . SER   B 1 84  ? 52.312 -9.520  -2.577  1.00 17.76 ?  84  SER   B HB3  1 
ATOM   5075 H HG   . SER   B 1 84  ? 53.372 -8.962  -4.422  1.00 19.80 ?  84  SER   B HG   1 
ATOM   5076 N N    . GLY   B 1 85  ? 50.679 -11.386 -5.192  1.00 13.15 ?  85  GLY   B N    1 
ATOM   5077 C CA   . GLY   B 1 85  ? 51.031 -12.675 -5.736  1.00 13.55 ?  85  GLY   B CA   1 
ATOM   5078 C C    . GLY   B 1 85  ? 52.501 -12.864 -6.040  1.00 12.95 ?  85  GLY   B C    1 
ATOM   5079 O O    . GLY   B 1 85  ? 52.878 -13.941 -6.503  1.00 13.25 ?  85  GLY   B O    1 
ATOM   5080 H H    . GLY   B 1 85  ? 50.528 -10.794 -5.788  1.00 15.78 ?  85  GLY   B H    1 
ATOM   5081 H HA2  . GLY   B 1 85  ? 50.767 -13.369 -5.106  1.00 16.26 ?  85  GLY   B HA2  1 
ATOM   5082 H HA3  . GLY   B 1 85  ? 50.542 -12.818 -6.556  1.00 16.26 ?  85  GLY   B HA3  1 
ATOM   5083 N N    . HIS   B 1 86  ? 53.352 -11.864 -5.817  1.00 13.02 ?  86  HIS   B N    1 
ATOM   5084 C CA   . HIS   B 1 86  ? 54.814 -12.034 -5.901  1.00 12.95 ?  86  HIS   B CA   1 
ATOM   5085 C C    . HIS   B 1 86  ? 55.189 -12.539 -7.294  1.00 13.13 ?  86  HIS   B C    1 
ATOM   5086 O O    . HIS   B 1 86  ? 54.799 -11.921 -8.297  1.00 13.97 ?  86  HIS   B O    1 
ATOM   5087 C CB   . HIS   B 1 86  ? 55.308 -12.877 -4.724  1.00 13.04 ?  86  HIS   B CB   1 
ATOM   5088 C CG   . HIS   B 1 86  ? 54.994 -12.275 -3.395  1.00 13.41 ?  86  HIS   B CG   1 
ATOM   5089 N ND1  . HIS   B 1 86  ? 55.819 -11.363 -2.772  1.00 14.86 ?  86  HIS   B ND1  1 
ATOM   5090 C CD2  . HIS   B 1 86  ? 53.917 -12.426 -2.587  1.00 13.92 ?  86  HIS   B CD2  1 
ATOM   5091 C CE1  . HIS   B 1 86  ? 55.260 -10.981 -1.637  1.00 14.64 ?  86  HIS   B CE1  1 
ATOM   5092 N NE2  . HIS   B 1 86  ? 54.104 -11.607 -1.503  1.00 14.17 ?  86  HIS   B NE2  1 
ATOM   5093 H H    . HIS   B 1 86  ? 53.110 -11.067 -5.621  1.00 15.62 ?  86  HIS   B H    1 
ATOM   5094 H HA   . HIS   B 1 86  ? 55.221 -11.162 -5.804  1.00 15.54 ?  86  HIS   B HA   1 
ATOM   5095 H HB2  . HIS   B 1 86  ? 54.895 -13.753 -4.763  1.00 15.65 ?  86  HIS   B HB2  1 
ATOM   5096 H HB3  . HIS   B 1 86  ? 56.276 -12.968 -4.784  1.00 15.65 ?  86  HIS   B HB3  1 
ATOM   5097 H HD2  . HIS   B 1 86  ? 53.175 -12.971 -2.750  1.00 16.71 ?  86  HIS   B HD2  1 
ATOM   5098 H HE1  . HIS   B 1 86  ? 55.626 -10.387 -1.023  1.00 17.57 ?  86  HIS   B HE1  1 
ATOM   5099 H HE2  . HIS   B 1 86  ? 53.563 -11.532 -0.836  1.00 17.00 ?  86  HIS   B HE2  1 
ATOM   5100 N N    . ASN   B 1 87  ? 55.957 -13.622 -7.407  1.00 13.56 ?  87  ASN   B N    1 
ATOM   5101 C CA   . ASN   B 1 87  ? 56.350 -14.195 -8.686  1.00 14.35 ?  87  ASN   B CA   1 
ATOM   5102 C C    . ASN   B 1 87  ? 55.368 -15.241 -9.185  1.00 14.02 ?  87  ASN   B C    1 
ATOM   5103 O O    . ASN   B 1 87  ? 55.684 -15.961 -10.137 1.00 15.51 ?  87  ASN   B O    1 
ATOM   5104 C CB   . ASN   B 1 87  ? 57.747 -14.823 -8.572  1.00 16.15 ?  87  ASN   B CB   1 
ATOM   5105 C CG   . ASN   B 1 87  ? 57.809 -15.935 -7.528  1.00 16.94 ?  87  ASN   B CG   1 
ATOM   5106 O OD1  . ASN   B 1 87  ? 57.164 -15.864 -6.476  1.00 16.06 ?  87  ASN   B OD1  1 
ATOM   5107 N ND2  . ASN   B 1 87  ? 58.562 -16.992 -7.837  1.00 19.04 ?  87  ASN   B ND2  1 
ATOM   5108 H H    . ASN   B 1 87  ? 56.270 -14.059 -6.734  1.00 16.28 ?  87  ASN   B H    1 
ATOM   5109 H HA   . ASN   B 1 87  ? 56.393 -13.491 -9.347  1.00 17.22 ?  87  ASN   B HA   1 
ATOM   5110 H HB2  . ASN   B 1 87  ? 57.995 -15.202 -9.435  1.00 19.38 ?  87  ASN   B HB2  1 
ATOM   5111 H HB3  . ASN   B 1 87  ? 58.382 -14.137 -8.320  1.00 19.38 ?  87  ASN   B HB3  1 
ATOM   5112 H HD21 . ASN   B 1 87  ? 58.633 -17.645 -7.285  1.00 22.85 ?  87  ASN   B HD21 1 
ATOM   5113 H HD22 . ASN   B 1 87  ? 58.991 -17.015 -8.586  1.00 22.85 ?  87  ASN   B HD22 1 
ATOM   5114 N N    . LEU   B 1 88  ? 54.189 -15.335 -8.569  1.00 12.93 ?  88  LEU   B N    1 
ATOM   5115 C CA   . LEU   B 1 88  ? 53.209 -16.367 -8.889  1.00 13.13 ?  88  LEU   B CA   1 
ATOM   5116 C C    . LEU   B 1 88  ? 51.972 -15.851 -9.608  1.00 12.85 ?  88  LEU   B C    1 
ATOM   5117 O O    . LEU   B 1 88  ? 51.368 -16.598 -10.389 1.00 14.85 ?  88  LEU   B O    1 
ATOM   5118 C CB   . LEU   B 1 88  ? 52.746 -17.050 -7.599  1.00 13.97 ?  88  LEU   B CB   1 
ATOM   5119 C CG   . LEU   B 1 88  ? 53.862 -17.721 -6.809  1.00 16.15 ?  88  LEU   B CG   1 
ATOM   5120 C CD1  . LEU   B 1 88  ? 53.366 -18.070 -5.415  1.00 17.69 ?  88  LEU   B CD1  1 
ATOM   5121 C CD2  . LEU   B 1 88  ? 54.334 -18.959 -7.542  1.00 18.78 ?  88  LEU   B CD2  1 
ATOM   5122 H H    . LEU   B 1 88  ? 53.929 -14.799 -7.942  1.00 15.52 ?  88  LEU   B H    1 
ATOM   5123 H HA   . LEU   B 1 88  ? 53.622 -17.032 -9.450  1.00 15.76 ?  88  LEU   B HA   1 
ATOM   5124 H HB2  . LEU   B 1 88  ? 52.334 -16.388 -7.021  1.00 16.76 ?  88  LEU   B HB2  1 
ATOM   5125 H HB3  . LEU   B 1 88  ? 52.095 -17.733 -7.826  1.00 16.76 ?  88  LEU   B HB3  1 
ATOM   5126 H HG   . LEU   B 1 88  ? 54.610 -17.110 -6.722  1.00 19.37 ?  88  LEU   B HG   1 
ATOM   5127 H HD11 . LEU   B 1 88  ? 54.023 -18.634 -4.979  1.00 21.23 ?  88  LEU   B HD11 1 
ATOM   5128 H HD12 . LEU   B 1 88  ? 53.243 -17.251 -4.910  1.00 21.23 ?  88  LEU   B HD12 1 
ATOM   5129 H HD13 . LEU   B 1 88  ? 52.523 -18.542 -5.493  1.00 21.23 ?  88  LEU   B HD13 1 
ATOM   5130 H HD21 . LEU   B 1 88  ? 54.987 -19.421 -6.993  1.00 22.54 ?  88  LEU   B HD21 1 
ATOM   5131 H HD22 . LEU   B 1 88  ? 53.573 -19.537 -7.708  1.00 22.54 ?  88  LEU   B HD22 1 
ATOM   5132 H HD23 . LEU   B 1 88  ? 54.738 -18.694 -8.383  1.00 22.54 ?  88  LEU   B HD23 1 
ATOM   5133 N N    . ALA   B 1 89  ? 51.568 -14.614 -9.344  1.00 12.25 ?  89  ALA   B N    1 
ATOM   5134 C CA   . ALA   B 1 89  ? 50.277 -14.124 -9.798  1.00 11.79 ?  89  ALA   B CA   1 
ATOM   5135 C C    . ALA   B 1 89  ? 50.248 -12.634 -9.513  1.00 12.03 ?  89  ALA   B C    1 
ATOM   5136 O O    . ALA   B 1 89  ? 51.089 -12.116 -8.777  1.00 12.87 ?  89  ALA   B O    1 
ATOM   5137 C CB   . ALA   B 1 89  ? 49.134 -14.810 -9.052  1.00 11.93 ?  89  ALA   B CB   1 
ATOM   5138 H H    . ALA   B 1 89  ? 52.016 -14.033 -8.888  1.00 14.70 ?  89  ALA   B H    1 
ATOM   5139 H HA   . ALA   B 1 89  ? 50.173 -14.269 -10.753 1.00 14.15 ?  89  ALA   B HA   1 
ATOM   5140 H HB1  . ALA   B 1 89  ? 48.286 -14.481 -9.401  1.00 14.32 ?  89  ALA   B HB1  1 
ATOM   5141 H HB2  . ALA   B 1 89  ? 49.195 -15.768 -9.200  1.00 14.32 ?  89  ALA   B HB2  1 
ATOM   5142 H HB3  . ALA   B 1 89  ? 49.206 -14.612 -8.112  1.00 14.32 ?  89  ALA   B HB3  1 
ATOM   5143 N N    . LYS   B 1 90  ? 49.252 -11.945 -10.070 1.00 12.98 ?  90  LYS   B N    1 
ATOM   5144 C CA   . LYS   B 1 90  ? 49.061 -10.558 -9.667  1.00 13.29 ?  90  LYS   B CA   1 
ATOM   5145 C C    . LYS   B 1 90  ? 48.741 -10.484 -8.179  1.00 13.03 ?  90  LYS   B C    1 
ATOM   5146 O O    . LYS   B 1 90  ? 49.380 -9.731  -7.428  1.00 14.56 ?  90  LYS   B O    1 
ATOM   5147 C CB   . LYS   B 1 90  ? 47.980 -9.902  -10.523 1.00 14.96 ?  90  LYS   B CB   1 
ATOM   5148 C CG   . LYS   B 1 90  ? 47.680 -8.465  -10.145 1.00 15.85 ?  90  LYS   B CG   1 
ATOM   5149 C CD   . LYS   B 1 90  ? 48.885 -7.564  -10.237 1.00 18.47 ?  90  LYS   B CD   1 
ATOM   5150 C CE   . LYS   B 1 90  ? 48.445 -6.143  -9.984  1.00 20.49 ?  90  LYS   B CE   1 
ATOM   5151 N NZ   . LYS   B 1 90  ? 49.587 -5.201  -9.931  1.00 20.58 ?  90  LYS   B NZ   1 
ATOM   5152 H H    . LYS   B 1 90  ? 48.695 -12.247 -10.655 1.00 15.58 ?  90  LYS   B H    1 
ATOM   5153 H HA   . LYS   B 1 90  ? 49.885 -10.079 -9.816  1.00 15.95 ?  90  LYS   B HA   1 
ATOM   5154 H HB2  . LYS   B 1 90  ? 48.270 -9.907  -11.451 1.00 17.95 ?  90  LYS   B HB2  1 
ATOM   5155 H HB3  . LYS   B 1 90  ? 47.158 -10.411 -10.439 1.00 17.95 ?  90  LYS   B HB3  1 
ATOM   5156 H HG2  . LYS   B 1 90  ? 47.000 -8.119  -10.744 1.00 19.02 ?  90  LYS   B HG2  1 
ATOM   5157 H HG3  . LYS   B 1 90  ? 47.351 -8.440  -9.230  1.00 19.02 ?  90  LYS   B HG3  1 
ATOM   5158 H HD2  . LYS   B 1 90  ? 49.536 -7.813  -9.561  1.00 22.16 ?  90  LYS   B HD2  1 
ATOM   5159 H HD3  . LYS   B 1 90  ? 49.270 -7.620  -11.124 1.00 22.16 ?  90  LYS   B HD3  1 
ATOM   5160 H HE2  . LYS   B 1 90  ? 47.856 -5.855  -10.701 1.00 24.59 ?  90  LYS   B HE2  1 
ATOM   5161 H HE3  . LYS   B 1 90  ? 47.980 -6.093  -9.134  1.00 24.59 ?  90  LYS   B HE3  1 
ATOM   5162 H HZ1  . LYS   B 1 90  ? 49.298 -4.371  -9.783  1.00 24.69 ?  90  LYS   B HZ1  1 
ATOM   5163 H HZ2  . LYS   B 1 90  ? 50.145 -5.433  -9.277  1.00 24.69 ?  90  LYS   B HZ2  1 
ATOM   5164 H HZ3  . LYS   B 1 90  ? 50.032 -5.215  -10.705 1.00 24.69 ?  90  LYS   B HZ3  1 
ATOM   5165 N N    . HIS   B 1 91  ? 47.780 -11.304 -7.732  1.00 11.54 ?  91  HIS   B N    1 
ATOM   5166 C CA   . HIS   B 1 91  ? 47.321 -11.328 -6.358  1.00 11.73 ?  91  HIS   B CA   1 
ATOM   5167 C C    . HIS   B 1 91  ? 47.325 -12.757 -5.842  1.00 11.19 ?  91  HIS   B C    1 
ATOM   5168 O O    . HIS   B 1 91  ? 47.093 -13.708 -6.597  1.00 11.60 ?  91  HIS   B O    1 
ATOM   5169 C CB   . HIS   B 1 91  ? 45.867 -10.849 -6.240  1.00 13.48 ?  91  HIS   B CB   1 
ATOM   5170 C CG   . HIS   B 1 91  ? 45.651 -9.446  -6.686  1.00 16.87 ?  91  HIS   B CG   1 
ATOM   5171 N ND1  . HIS   B 1 91  ? 46.241 -8.366  -6.065  1.00 19.21 ?  91  HIS   B ND1  1 
ATOM   5172 C CD2  . HIS   B 1 91  ? 44.872 -8.938  -7.666  1.00 19.17 ?  91  HIS   B CD2  1 
ATOM   5173 C CE1  . HIS   B 1 91  ? 45.856 -7.250  -6.661  1.00 20.05 ?  91  HIS   B CE1  1 
ATOM   5174 N NE2  . HIS   B 1 91  ? 45.018 -7.571  -7.632  1.00 20.16 ?  91  HIS   B NE2  1 
ATOM   5175 H H    . HIS   B 1 91  ? 47.370 -11.874 -8.229  1.00 13.84 ?  91  HIS   B H    1 
ATOM   5176 H HA   . HIS   B 1 91  ? 47.891 -10.773 -5.795  1.00 14.07 ?  91  HIS   B HA   1 
ATOM   5177 H HB2  . HIS   B 1 91  ? 45.302 -11.417 -6.781  1.00 16.17 ?  91  HIS   B HB2  1 
ATOM   5178 H HB3  . HIS   B 1 91  ? 45.591 -10.905 -5.307  1.00 16.17 ?  91  HIS   B HB3  1 
ATOM   5179 H HD1  . HIS   B 1 91  ? 46.783 -8.408  -5.396  1.00 23.05 ?  91  HIS   B HD1  1 
ATOM   5180 H HD2  . HIS   B 1 91  ? 44.346 -9.411  -8.261  1.00 23.00 ?  91  HIS   B HD2  1 
ATOM   5181 H HE1  . HIS   B 1 91  ? 46.125 -6.385  -6.427  1.00 24.05 ?  91  HIS   B HE1  1 
ATOM   5182 N N    . CYS   B 1 92  ? 47.524 -12.895 -4.540  1.00 10.94 ?  92  CYS   B N    1 
ATOM   5183 C CA   . CYS   B 1 92  ? 47.222 -14.128 -3.828  1.00 10.59 ?  92  CYS   B CA   1 
ATOM   5184 C C    . CYS   B 1 92  ? 46.003 -13.893 -2.943  1.00 10.32 ?  92  CYS   B C    1 
ATOM   5185 O O    . CYS   B 1 92  ? 46.001 -12.991 -2.091  1.00 11.11 ?  92  CYS   B O    1 
ATOM   5186 C CB   . CYS   B 1 92  ? 48.404 -14.594 -2.983  1.00 11.14 ?  92  CYS   B CB   1 
ATOM   5187 S SG   . CYS   B 1 92  ? 48.047 -16.127 -2.086  1.00 11.40 ?  92  CYS   B SG   1 
ATOM   5188 H H    . CYS   B 1 92  ? 47.858 -12.278 -4.033  1.00 13.13 ?  92  CYS   B H    1 
ATOM   5189 H HA   . CYS   B 1 92  ? 47.018 -14.824 -4.474  1.00 12.70 ?  92  CYS   B HA   1 
ATOM   5190 H HB2  . CYS   B 1 92  ? 49.165 -14.749 -3.555  1.00 13.36 ?  92  CYS   B HB2  1 
ATOM   5191 H HB3  . CYS   B 1 92  ? 48.607 -13.907 -2.328  1.00 13.36 ?  92  CYS   B HB3  1 
ATOM   5192 H HG   . CYS   B 1 92  ? 49.016 -16.447 -1.464  1.00 13.68 ?  92  CYS   B HG   1 
ATOM   5193 N N    . LEU   B 1 93  ? 44.964 -14.700 -3.160  1.00 10.17 ?  93  LEU   B N    1 
ATOM   5194 C CA   . LEU   B 1 93  ? 43.789 -14.725 -2.300  1.00 10.62 ?  93  LEU   B CA   1 
ATOM   5195 C C    . LEU   B 1 93  ? 44.016 -15.793 -1.237  1.00 9.98  ?  93  LEU   B C    1 
ATOM   5196 O O    . LEU   B 1 93  ? 43.964 -16.993 -1.532  1.00 10.55 ?  93  LEU   B O    1 
ATOM   5197 C CB   . LEU   B 1 93  ? 42.529 -15.019 -3.110  1.00 11.19 ?  93  LEU   B CB   1 
ATOM   5198 C CG   . LEU   B 1 93  ? 41.234 -15.037 -2.296  1.00 11.65 ?  93  LEU   B CG   1 
ATOM   5199 C CD1  . LEU   B 1 93  ? 40.877 -13.646 -1.814  1.00 12.13 ?  93  LEU   B CD1  1 
ATOM   5200 C CD2  . LEU   B 1 93  ? 40.100 -15.632 -3.112  1.00 11.86 ?  93  LEU   B CD2  1 
ATOM   5201 H H    . LEU   B 1 93  ? 44.923 -15.267 -3.821  1.00 12.21 ?  93  LEU   B H    1 
ATOM   5202 H HA   . LEU   B 1 93  ? 43.692 -13.866 -1.869  1.00 12.75 ?  93  LEU   B HA   1 
ATOM   5203 H HB2  . LEU   B 1 93  ? 42.434 -14.333 -3.793  1.00 13.43 ?  93  LEU   B HB2  1 
ATOM   5204 H HB3  . LEU   B 1 93  ? 42.622 -15.885 -3.532  1.00 13.43 ?  93  LEU   B HB3  1 
ATOM   5205 H HG   . LEU   B 1 93  ? 41.360 -15.594 -1.512  1.00 13.97 ?  93  LEU   B HG   1 
ATOM   5206 H HD11 . LEU   B 1 93  ? 40.024 -13.677 -1.361  1.00 14.56 ?  93  LEU   B HD11 1 
ATOM   5207 H HD12 . LEU   B 1 93  ? 41.568 -13.335 -1.208  1.00 14.56 ?  93  LEU   B HD12 1 
ATOM   5208 H HD13 . LEU   B 1 93  ? 40.824 -13.053 -2.584  1.00 14.56 ?  93  LEU   B HD13 1 
ATOM   5209 H HD21 . LEU   B 1 93  ? 39.291 -15.630 -2.576  1.00 14.23 ?  93  LEU   B HD21 1 
ATOM   5210 H HD22 . LEU   B 1 93  ? 39.971 -15.098 -3.910  1.00 14.23 ?  93  LEU   B HD22 1 
ATOM   5211 H HD23 . LEU   B 1 93  ? 40.332 -16.542 -3.356  1.00 14.23 ?  93  LEU   B HD23 1 
ATOM   5212 N N    . HIS   B 1 94  ? 44.293 -15.358 -0.011  1.00 10.03 ?  94  HIS   B N    1 
ATOM   5213 C CA   . HIS   B 1 94  ? 44.512 -16.268 1.107   1.00 10.46 ?  94  HIS   B CA   1 
ATOM   5214 C C    . HIS   B 1 94  ? 43.149 -16.628 1.681   1.00 10.89 ?  94  HIS   B C    1 
ATOM   5215 O O    . HIS   B 1 94  ? 42.474 -15.758 2.234   1.00 12.16 ?  94  HIS   B O    1 
ATOM   5216 C CB   . HIS   B 1 94  ? 45.384 -15.593 2.165   1.00 10.85 ?  94  HIS   B CB   1 
ATOM   5217 C CG   . HIS   B 1 94  ? 46.766 -15.286 1.693   1.00 10.68 ?  94  HIS   B CG   1 
ATOM   5218 N ND1  . HIS   B 1 94  ? 47.793 -16.201 1.771   1.00 10.84 ?  94  HIS   B ND1  1 
ATOM   5219 C CD2  . HIS   B 1 94  ? 47.271 -14.176 1.103   1.00 10.81 ?  94  HIS   B CD2  1 
ATOM   5220 C CE1  . HIS   B 1 94  ? 48.881 -15.646 1.263   1.00 10.83 ?  94  HIS   B CE1  1 
ATOM   5221 N NE2  . HIS   B 1 94  ? 48.593 -14.422 0.850   1.00 11.14 ?  94  HIS   B NE2  1 
ATOM   5222 H H    . HIS   B 1 94  ? 44.355 -14.522 0.198   1.00 12.04 ?  94  HIS   B H    1 
ATOM   5223 H HA   . HIS   B 1 94  ? 44.948 -17.074 0.795   1.00 12.55 ?  94  HIS   B HA   1 
ATOM   5224 H HB2  . HIS   B 1 94  ? 44.969 -14.758 2.424   1.00 13.02 ?  94  HIS   B HB2  1 
ATOM   5225 H HB3  . HIS   B 1 94  ? 45.457 -16.183 2.926   1.00 13.02 ?  94  HIS   B HB3  1 
ATOM   5226 H HD2  . HIS   B 1 94  ? 46.814 -13.391 0.908   1.00 12.97 ?  94  HIS   B HD2  1 
ATOM   5227 H HE1  . HIS   B 1 94  ? 49.717 -16.058 1.195   1.00 13.00 ?  94  HIS   B HE1  1 
ATOM   5228 H HE2  . HIS   B 1 94  ? 49.150 -13.877 0.480   1.00 13.37 ?  94  HIS   B HE2  1 
ATOM   5229 N N    . VAL   B 1 95  ? 42.715 -17.882 1.523   1.00 10.48 ?  95  VAL   B N    1 
ATOM   5230 C CA   . VAL   B 1 95  ? 41.390 -18.321 1.959   1.00 10.78 ?  95  VAL   B CA   1 
ATOM   5231 C C    . VAL   B 1 95  ? 41.560 -19.360 3.053   1.00 10.78 ?  95  VAL   B C    1 
ATOM   5232 O O    . VAL   B 1 95  ? 42.332 -20.311 2.892   1.00 11.38 ?  95  VAL   B O    1 
ATOM   5233 C CB   . VAL   B 1 95  ? 40.571 -18.919 0.799   1.00 11.10 ?  95  VAL   B CB   1 
ATOM   5234 C CG1  . VAL   B 1 95  ? 39.199 -19.383 1.284   1.00 12.12 ?  95  VAL   B CG1  1 
ATOM   5235 C CG2  . VAL   B 1 95  ? 40.437 -17.932 -0.334  1.00 11.17 ?  95  VAL   B CG2  1 
ATOM   5236 H H    . VAL   B 1 95  ? 43.178 -18.506 1.154   1.00 12.57 ?  95  VAL   B H    1 
ATOM   5237 H HA   . VAL   B 1 95  ? 40.898 -17.570 2.324   1.00 12.94 ?  95  VAL   B HA   1 
ATOM   5238 H HB   . VAL   B 1 95  ? 41.035 -19.697 0.458   1.00 13.32 ?  95  VAL   B HB   1 
ATOM   5239 H HG11 . VAL   B 1 95  ? 38.638 -19.580 0.512   1.00 14.54 ?  95  VAL   B HG11 1 
ATOM   5240 H HG12 . VAL   B 1 95  ? 39.301 -20.187 1.821   1.00 14.54 ?  95  VAL   B HG12 1 
ATOM   5241 H HG13 . VAL   B 1 95  ? 38.789 -18.682 1.812   1.00 14.54 ?  95  VAL   B HG13 1 
ATOM   5242 H HG21 . VAL   B 1 95  ? 39.860 -18.313 -1.016  1.00 13.41 ?  95  VAL   B HG21 1 
ATOM   5243 H HG22 . VAL   B 1 95  ? 40.045 -17.113 0.009   1.00 13.41 ?  95  VAL   B HG22 1 
ATOM   5244 H HG23 . VAL   B 1 95  ? 41.314 -17.756 -0.700  1.00 13.41 ?  95  VAL   B HG23 1 
ATOM   5245 N N    . VAL   B 1 96  ? 40.825 -19.196 4.149   1.00 11.41 ?  96  VAL   B N    1 
ATOM   5246 C CA   . VAL   B 1 96  ? 40.907 -20.114 5.286   1.00 11.60 ?  96  VAL   B CA   1 
ATOM   5247 C C    . VAL   B 1 96  ? 39.718 -21.073 5.238   1.00 12.32 ?  96  VAL   B C    1 
ATOM   5248 O O    . VAL   B 1 96  ? 38.600 -20.718 5.623   1.00 12.76 ?  96  VAL   B O    1 
ATOM   5249 C CB   . VAL   B 1 96  ? 40.958 -19.372 6.625   1.00 12.51 ?  96  VAL   B CB   1 
ATOM   5250 C CG1  . VAL   B 1 96  ? 41.138 -20.368 7.768   1.00 13.13 ?  96  VAL   B CG1  1 
ATOM   5251 C CG2  . VAL   B 1 96  ? 42.073 -18.334 6.633   1.00 13.25 ?  96  VAL   B CG2  1 
ATOM   5252 H H    . VAL   B 1 96  ? 40.259 -18.560 4.261   1.00 13.69 ?  96  VAL   B H    1 
ATOM   5253 H HA   . VAL   B 1 96  ? 41.719 -20.642 5.209   1.00 13.92 ?  96  VAL   B HA   1 
ATOM   5254 H HB   . VAL   B 1 96  ? 40.116 -18.910 6.761   1.00 15.02 ?  96  VAL   B HB   1 
ATOM   5255 H HG11 . VAL   B 1 96  ? 41.320 -19.877 8.587   1.00 15.76 ?  96  VAL   B HG11 1 
ATOM   5256 H HG12 . VAL   B 1 96  ? 40.330 -20.891 7.870   1.00 15.76 ?  96  VAL   B HG12 1 
ATOM   5257 H HG13 . VAL   B 1 96  ? 41.889 -20.951 7.565   1.00 15.76 ?  96  VAL   B HG13 1 
ATOM   5258 H HG21 . VAL   B 1 96  ? 42.123 -17.927 7.514   1.00 15.90 ?  96  VAL   B HG21 1 
ATOM   5259 H HG22 . VAL   B 1 96  ? 42.914 -18.767 6.422   1.00 15.90 ?  96  VAL   B HG22 1 
ATOM   5260 H HG23 . VAL   B 1 96  ? 41.878 -17.651 5.969   1.00 15.90 ?  96  VAL   B HG23 1 
ATOM   5261 N N    . GLY   B 1 97  ? 39.949 -22.306 4.794   1.00 12.13 ?  97  GLY   B N    1 
ATOM   5262 C CA   . GLY   B 1 97  ? 38.975 -23.363 4.956   1.00 12.72 ?  97  GLY   B CA   1 
ATOM   5263 C C    . GLY   B 1 97  ? 39.092 -23.974 6.334   1.00 13.33 ?  97  GLY   B C    1 
ATOM   5264 O O    . GLY   B 1 97  ? 40.126 -23.850 7.000   1.00 13.73 ?  97  GLY   B O    1 
ATOM   5265 H H    . GLY   B 1 97  ? 40.677 -22.549 4.397   1.00 14.56 ?  97  GLY   B H    1 
ATOM   5266 H HA2  . GLY   B 1 97  ? 38.084 -22.992 4.838   1.00 15.27 ?  97  GLY   B HA2  1 
ATOM   5267 H HA3  . GLY   B 1 97  ? 39.120 -24.045 4.284   1.00 15.27 ?  97  GLY   B HA3  1 
ATOM   5268 N N    . PRO   B 1 98  ? 38.044 -24.660 6.787   1.00 14.07 ?  98  PRO   B N    1 
ATOM   5269 C CA   . PRO   B 1 98  ? 38.128 -25.358 8.072   1.00 14.60 ?  98  PRO   B CA   1 
ATOM   5270 C C    . PRO   B 1 98  ? 39.161 -26.473 8.031   1.00 14.18 ?  98  PRO   B C    1 
ATOM   5271 O O    . PRO   B 1 98  ? 39.278 -27.204 7.047   1.00 14.60 ?  98  PRO   B O    1 
ATOM   5272 C CB   . PRO   B 1 98  ? 36.713 -25.915 8.262   1.00 14.84 ?  98  PRO   B CB   1 
ATOM   5273 C CG   . PRO   B 1 98  ? 36.163 -26.030 6.883   1.00 14.56 ?  98  PRO   B CG   1 
ATOM   5274 C CD   . PRO   B 1 98  ? 36.732 -24.845 6.145   1.00 14.06 ?  98  PRO   B CD   1 
ATOM   5275 H HA   . PRO   B 1 98  ? 38.343 -24.741 8.783   1.00 17.52 ?  98  PRO   B HA   1 
ATOM   5276 H HB2  . PRO   B 1 98  ? 36.761 -26.791 8.685   1.00 17.81 ?  98  PRO   B HB2  1 
ATOM   5277 H HB3  . PRO   B 1 98  ? 36.189 -25.303 8.793   1.00 17.81 ?  98  PRO   B HB3  1 
ATOM   5278 H HG2  . PRO   B 1 98  ? 36.462 -26.862 6.479   1.00 17.48 ?  98  PRO   B HG2  1 
ATOM   5279 H HG3  . PRO   B 1 98  ? 35.198 -25.987 6.912   1.00 17.48 ?  98  PRO   B HG3  1 
ATOM   5280 H HD2  . PRO   B 1 98  ? 36.835 -25.053 5.199   1.00 16.87 ?  98  PRO   B HD2  1 
ATOM   5281 H HD3  . PRO   B 1 98  ? 36.180 -24.062 6.278   1.00 16.87 ?  98  PRO   B HD3  1 
ATOM   5282 N N    . ASN   B 1 99  ? 39.900 -26.603 9.124   1.00 15.27 ?  99  ASN   B N    1 
ATOM   5283 C CA   . ASN   B 1 99  ? 40.880 -27.674 9.288   1.00 16.19 ?  99  ASN   B CA   1 
ATOM   5284 C C    . ASN   B 1 99  ? 40.247 -28.763 10.153  1.00 18.23 ?  99  ASN   B C    1 
ATOM   5285 O O    . ASN   B 1 99  ? 40.155 -28.623 11.375  1.00 18.76 ?  99  ASN   B O    1 
ATOM   5286 C CB   . ASN   B 1 99  ? 42.149 -27.119 9.920   1.00 16.64 ?  99  ASN   B CB   1 
ATOM   5287 C CG   . ASN   B 1 99  ? 43.282 -28.123 9.922   1.00 17.55 ?  99  ASN   B CG   1 
ATOM   5288 O OD1  . ASN   B 1 99  ? 43.058 -29.319 10.075  1.00 18.17 ?  99  ASN   B OD1  1 
ATOM   5289 N ND2  . ASN   B 1 99  ? 44.504 -27.641 9.745   1.00 17.97 ?  99  ASN   B ND2  1 
ATOM   5290 H H    . ASN   B 1 99  ? 39.854 -26.073 9.797   1.00 18.32 ?  99  ASN   B H    1 
ATOM   5291 H HA   . ASN   B 1 99  ? 41.102 -28.058 8.428   1.00 19.42 ?  99  ASN   B HA   1 
ATOM   5292 H HB2  . ASN   B 1 99  ? 42.436 -26.344 9.424   1.00 19.97 ?  99  ASN   B HB2  1 
ATOM   5293 H HB3  . ASN   B 1 99  ? 41.960 -26.876 10.844  1.00 19.97 ?  99  ASN   B HB3  1 
ATOM   5294 H HD21 . ASN   B 1 99  ? 45.180 -28.171 9.740   1.00 21.56 ?  99  ASN   B HD21 1 
ATOM   5295 H HD22 . ASN   B 1 99  ? 44.617 -26.795 9.639   1.00 21.56 ?  99  ASN   B HD22 1 
ATOM   5296 N N    A VAL   B 1 100 ? 39.787 -29.840 9.509   0.70 19.95 ?  100 VAL   B N    1 
ATOM   5297 N N    B VAL   B 1 100 ? 39.807 -29.847 9.507   0.30 20.11 ?  100 VAL   B N    1 
ATOM   5298 C CA   A VAL   B 1 100 ? 39.173 -30.948 10.241  0.70 22.65 ?  100 VAL   B CA   1 
ATOM   5299 C CA   B VAL   B 1 100 ? 39.182 -30.956 10.226  0.30 22.33 ?  100 VAL   B CA   1 
ATOM   5300 C C    A VAL   B 1 100 ? 40.173 -31.613 11.180  0.70 23.02 ?  100 VAL   B C    1 
ATOM   5301 C C    B VAL   B 1 100 ? 40.173 -31.619 11.172  0.30 22.95 ?  100 VAL   B C    1 
ATOM   5302 O O    A VAL   B 1 100 ? 39.791 -32.134 12.236  0.70 23.38 ?  100 VAL   B O    1 
ATOM   5303 O O    B VAL   B 1 100 ? 39.787 -32.131 12.230  0.30 23.19 ?  100 VAL   B O    1 
ATOM   5304 C CB   A VAL   B 1 100 ? 38.540 -31.959 9.262   0.70 25.25 ?  100 VAL   B CB   1 
ATOM   5305 C CB   B VAL   B 1 100 ? 38.570 -31.962 9.229   0.30 23.90 ?  100 VAL   B CB   1 
ATOM   5306 C CG1  A VAL   B 1 100 ? 38.062 -33.200 10.004  0.70 26.10 ?  100 VAL   B CG1  1 
ATOM   5307 C CG1  B VAL   B 1 100 ? 38.041 -33.192 9.956   0.30 24.44 ?  100 VAL   B CG1  1 
ATOM   5308 C CG2  A VAL   B 1 100 ? 37.387 -31.317 8.503   0.70 25.96 ?  100 VAL   B CG2  1 
ATOM   5309 C CG2  B VAL   B 1 100 ? 37.462 -31.300 8.428   0.30 24.32 ?  100 VAL   B CG2  1 
ATOM   5310 H H    A VAL   B 1 100 ? 39.803 -29.946 8.653   0.70 23.94 ?  100 VAL   B H    1 
ATOM   5311 H H    B VAL   B 1 100 ? 39.856 -29.962 8.657   0.30 24.13 ?  100 VAL   B H    1 
ATOM   5312 H HA   A VAL   B 1 100 ? 38.453 -30.594 10.785  0.70 27.18 ?  100 VAL   B HA   1 
ATOM   5313 H HA   B VAL   B 1 100 ? 38.456 -30.606 10.763  0.30 26.79 ?  100 VAL   B HA   1 
ATOM   5314 H HB   A VAL   B 1 100 ? 39.209 -32.238 8.620   0.70 30.30 ?  100 VAL   B HB   1 
ATOM   5315 H HB   B VAL   B 1 100 ? 39.256 -32.256 8.610   0.30 28.68 ?  100 VAL   B HB   1 
ATOM   5316 H HG11 A VAL   B 1 100 ? 37.477 -33.710 9.419   0.70 31.32 ?  100 VAL   B HG11 1 
ATOM   5317 H HG11 B VAL   B 1 100 ? 37.477 -33.699 9.349   0.30 29.32 ?  100 VAL   B HG11 1 
ATOM   5318 H HG12 A VAL   B 1 100 ? 38.828 -33.742 10.252  0.70 31.32 ?  100 VAL   B HG12 1 
ATOM   5319 H HG12 B VAL   B 1 100 ? 38.788 -33.741 10.243  0.30 29.32 ?  100 VAL   B HG12 1 
ATOM   5320 H HG13 A VAL   B 1 100 ? 37.575 -32.930 10.798  0.70 31.32 ?  100 VAL   B HG13 1 
ATOM   5321 H HG13 B VAL   B 1 100 ? 37.522 -32.907 10.724  0.30 29.32 ?  100 VAL   B HG13 1 
ATOM   5322 H HG21 A VAL   B 1 100 ? 37.005 -31.974 7.897   0.70 31.15 ?  100 VAL   B HG21 1 
ATOM   5323 H HG21 B VAL   B 1 100 ? 37.070 -31.955 7.830   0.30 29.18 ?  100 VAL   B HG21 1 
ATOM   5324 H HG22 A VAL   B 1 100 ? 36.713 -31.027 9.139   0.70 31.15 ?  100 VAL   B HG22 1 
ATOM   5325 H HG22 B VAL   B 1 100 ? 36.788 -30.966 9.041   0.30 29.18 ?  100 VAL   B HG22 1 
ATOM   5326 H HG23 A VAL   B 1 100 ? 37.721 -30.560 8.003   0.70 31.15 ?  100 VAL   B HG23 1 
ATOM   5327 H HG23 B VAL   B 1 100 ? 37.838 -30.568 7.917   0.30 29.18 ?  100 VAL   B HG23 1 
ATOM   5328 N N    . ASN   B 1 101 ? 41.457 -31.634 10.808  1.00 23.35 ?  101 ASN   B N    1 
ATOM   5329 C CA   . ASN   B 1 101 ? 42.481 -32.170 11.704  1.00 25.95 ?  101 ASN   B CA   1 
ATOM   5330 C C    . ASN   B 1 101 ? 42.635 -31.334 12.970  1.00 28.59 ?  101 ASN   B C    1 
ATOM   5331 O O    . ASN   B 1 101 ? 43.217 -31.817 13.949  1.00 29.48 ?  101 ASN   B O    1 
ATOM   5332 C CB   . ASN   B 1 101 ? 43.823 -32.299 10.976  1.00 26.12 ?  101 ASN   B CB   1 
ATOM   5333 C CG   . ASN   B 1 101 ? 43.824 -33.422 9.956   1.00 25.92 ?  101 ASN   B CG   1 
ATOM   5334 O OD1  . ASN   B 1 101 ? 43.166 -34.441 10.144  1.00 26.98 ?  101 ASN   B OD1  1 
ATOM   5335 N ND2  . ASN   B 1 101 ? 44.561 -33.237 8.868   1.00 25.62 ?  101 ASN   B ND2  1 
ATOM   5336 H H    A ASN   B 1 101 ? 41.750 -31.366 10.046  0.70 28.02 ?  101 ASN   B H    1 
ATOM   5337 H H    B ASN   B 1 101 ? 41.753 -31.351 10.053  0.30 28.02 ?  101 ASN   B H    1 
ATOM   5338 H HA   . ASN   B 1 101 ? 42.215 -33.056 11.977  1.00 31.14 ?  101 ASN   B HA   1 
ATOM   5339 H HB2  . ASN   B 1 101 ? 44.019 -31.472 10.508  1.00 31.34 ?  101 ASN   B HB2  1 
ATOM   5340 H HB3  . ASN   B 1 101 ? 44.519 -32.484 11.625  1.00 31.34 ?  101 ASN   B HB3  1 
ATOM   5341 H HD21 . ASN   B 1 101 ? 44.592 -33.846 8.261   1.00 30.74 ?  101 ASN   B HD21 1 
ATOM   5342 H HD22 . ASN   B 1 101 ? 45.006 -32.508 8.768   1.00 30.74 ?  101 ASN   B HD22 1 
ATOM   5343 N N    A LYS   B 1 102 ? 42.146 -30.093 12.965  0.70 29.93 ?  102 LYS   B N    1 
ATOM   5344 N N    B LYS   B 1 102 ? 42.126 -30.101 12.973  0.30 29.90 ?  102 LYS   B N    1 
ATOM   5345 C CA   A LYS   B 1 102 ? 42.135 -29.236 14.143  0.70 31.88 ?  102 LYS   B CA   1 
ATOM   5346 C CA   B LYS   B 1 102 ? 42.056 -29.278 14.174  0.30 31.41 ?  102 LYS   B CA   1 
ATOM   5347 C C    A LYS   B 1 102 ? 40.766 -29.186 14.809  0.70 31.24 ?  102 LYS   B C    1 
ATOM   5348 C C    B LYS   B 1 102 ? 40.673 -29.283 14.811  0.30 30.99 ?  102 LYS   B C    1 
ATOM   5349 O O    A LYS   B 1 102 ? 40.552 -28.360 15.702  0.70 31.52 ?  102 LYS   B O    1 
ATOM   5350 O O    B LYS   B 1 102 ? 40.456 -28.565 15.792  0.30 31.13 ?  102 LYS   B O    1 
ATOM   5351 C CB   A LYS   B 1 102 ? 42.560 -27.813 13.773  0.70 34.58 ?  102 LYS   B CB   1 
ATOM   5352 C CB   B LYS   B 1 102 ? 42.461 -27.833 13.860  0.30 33.22 ?  102 LYS   B CB   1 
ATOM   5353 C CG   A LYS   B 1 102 ? 44.031 -27.637 13.438  0.70 37.24 ?  102 LYS   B CG   1 
ATOM   5354 C CG   B LYS   B 1 102 ? 43.914 -27.654 13.455  0.30 34.95 ?  102 LYS   B CG   1 
ATOM   5355 C CD   A LYS   B 1 102 ? 44.320 -26.184 13.080  0.70 39.47 ?  102 LYS   B CD   1 
ATOM   5356 C CD   B LYS   B 1 102 ? 44.185 -26.214 13.046  0.30 36.37 ?  102 LYS   B CD   1 
ATOM   5357 C CE   A LYS   B 1 102 ? 45.796 -25.945 12.802  0.70 41.14 ?  102 LYS   B CE   1 
ATOM   5358 C CE   B LYS   B 1 102 ? 45.658 -25.979 12.759  0.30 37.42 ?  102 LYS   B CE   1 
ATOM   5359 N NZ   A LYS   B 1 102 ? 46.062 -24.529 12.410  0.70 42.12 ?  102 LYS   B NZ   1 
ATOM   5360 N NZ   B LYS   B 1 102 ? 45.914 -24.578 12.322  0.30 38.02 ?  102 LYS   B NZ   1 
ATOM   5361 H H    A LYS   B 1 102 ? 41.803 -29.717 12.271  0.70 35.91 ?  102 LYS   B H    1 
ATOM   5362 H H    B LYS   B 1 102 ? 41.809 -29.711 12.274  0.30 35.88 ?  102 LYS   B H    1 
ATOM   5363 H HA   A LYS   B 1 102 ? 42.780 -29.578 14.783  0.70 38.26 ?  102 LYS   B HA   1 
ATOM   5364 H HA   B LYS   B 1 102 ? 42.682 -29.625 14.826  0.30 37.70 ?  102 LYS   B HA   1 
ATOM   5365 H HB2  A LYS   B 1 102 ? 42.048 -27.531 13.000  0.70 41.49 ?  102 LYS   B HB2  1 
ATOM   5366 H HB2  B LYS   B 1 102 ? 41.912 -27.505 13.132  0.30 39.87 ?  102 LYS   B HB2  1 
ATOM   5367 H HB3  A LYS   B 1 102 ? 42.362 -27.228 14.523  0.70 41.49 ?  102 LYS   B HB3  1 
ATOM   5368 H HB3  B LYS   B 1 102 ? 42.310 -27.290 14.652  0.30 39.87 ?  102 LYS   B HB3  1 
ATOM   5369 H HG2  A LYS   B 1 102 ? 44.571 -27.876 14.208  0.70 44.69 ?  102 LYS   B HG2  1 
ATOM   5370 H HG2  B LYS   B 1 102 ? 44.490 -27.870 14.206  0.30 41.94 ?  102 LYS   B HG2  1 
ATOM   5371 H HG3  A LYS   B 1 102 ? 44.259 -28.192 12.676  0.70 44.69 ?  102 LYS   B HG3  1 
ATOM   5372 H HG3  B LYS   B 1 102 ? 44.113 -28.229 12.700  0.30 41.94 ?  102 LYS   B HG3  1 
ATOM   5373 H HD2  A LYS   B 1 102 ? 43.820 -25.947 12.283  0.70 47.37 ?  102 LYS   B HD2  1 
ATOM   5374 H HD2  B LYS   B 1 102 ? 43.683 -26.012 12.240  0.30 43.64 ?  102 LYS   B HD2  1 
ATOM   5375 H HD3  A LYS   B 1 102 ? 44.056 -25.615 13.820  0.70 47.37 ?  102 LYS   B HD3  1 
ATOM   5376 H HD3  B LYS   B 1 102 ? 43.917 -25.621 13.765  0.30 43.64 ?  102 LYS   B HD3  1 
ATOM   5377 H HE2  A LYS   B 1 102 ? 46.307 -26.139 13.603  0.70 49.37 ?  102 LYS   B HE2  1 
ATOM   5378 H HE2  B LYS   B 1 102 ? 46.171 -26.144 13.566  0.30 44.90 ?  102 LYS   B HE2  1 
ATOM   5379 H HE3  A LYS   B 1 102 ? 46.081 -26.520 12.075  0.70 49.37 ?  102 LYS   B HE3  1 
ATOM   5380 H HE3  B LYS   B 1 102 ? 45.945 -26.576 12.050  0.30 44.90 ?  102 LYS   B HE3  1 
ATOM   5381 H HZ1  A LYS   B 1 102 ? 46.931 -24.415 12.253  0.70 50.55 ?  102 LYS   B HZ1  1 
ATOM   5382 H HZ1  B LYS   B 1 102 ? 46.782 -24.464 12.160  0.30 45.62 ?  102 LYS   B HZ1  1 
ATOM   5383 H HZ2  A LYS   B 1 102 ? 45.606 -24.327 11.673  0.70 50.55 ?  102 LYS   B HZ2  1 
ATOM   5384 H HZ2  B LYS   B 1 102 ? 45.456 -24.403 11.579  0.30 45.62 ?  102 LYS   B HZ2  1 
ATOM   5385 H HZ3  A LYS   B 1 102 ? 45.812 -23.980 13.065  0.70 50.55 ?  102 LYS   B HZ3  1 
ATOM   5386 H HZ3  B LYS   B 1 102 ? 45.661 -24.010 12.959  0.30 45.62 ?  102 LYS   B HZ3  1 
ATOM   5387 N N    A GLY   B 1 103 ? 39.831 -30.032 14.384  0.70 30.32 ?  103 GLY   B N    1 
ATOM   5388 N N    B GLY   B 1 103 ? 39.733 -30.063 14.280  0.30 30.37 ?  103 GLY   B N    1 
ATOM   5389 C CA   A GLY   B 1 103 ? 38.503 -30.062 14.963  0.70 30.08 ?  103 GLY   B CA   1 
ATOM   5390 C CA   B GLY   B 1 103 ? 38.406 -30.128 14.858  0.30 29.81 ?  103 GLY   B CA   1 
ATOM   5391 C C    A GLY   B 1 103 ? 37.559 -28.991 14.465  0.70 29.27 ?  103 GLY   B C    1 
ATOM   5392 C C    B GLY   B 1 103 ? 37.469 -29.024 14.433  0.30 29.06 ?  103 GLY   B C    1 
ATOM   5393 O O    A GLY   B 1 103 ? 36.439 -28.888 14.981  0.70 30.03 ?  103 GLY   B O    1 
ATOM   5394 O O    B GLY   B 1 103 ? 36.427 -28.834 15.069  0.30 29.36 ?  103 GLY   B O    1 
ATOM   5395 H H    A GLY   B 1 103 ? 39.948 -30.602 13.754  0.70 36.39 ?  103 GLY   B H    1 
ATOM   5396 H H    B GLY   B 1 103 ? 39.842 -30.564 13.588  0.30 36.45 ?  103 GLY   B H    1 
ATOM   5397 H HA2  A GLY   B 1 103 ? 38.102 -30.924 14.774  0.70 36.10 ?  103 GLY   B HA2  1 
ATOM   5398 H HA2  B GLY   B 1 103 ? 38.000 -30.973 14.617  0.30 35.78 ?  103 GLY   B HA2  1 
ATOM   5399 H HA3  A GLY   B 1 103 ? 38.580 -29.974 15.927  0.70 36.10 ?  103 GLY   B HA3  1 
ATOM   5400 H HA3  B GLY   B 1 103 ? 38.486 -30.098 15.825  0.30 35.78 ?  103 GLY   B HA3  1 
ATOM   5401 N N    A GLU   B 1 104 ? 37.964 -28.195 13.480  0.70 27.59 ?  104 GLU   B N    1 
ATOM   5402 N N    B GLU   B 1 104 ? 37.799 -28.291 13.375  0.30 27.87 ?  104 GLU   B N    1 
ATOM   5403 C CA   A GLU   B 1 104 ? 37.122 -27.109 13.004  0.70 25.96 ?  104 GLU   B CA   1 
ATOM   5404 C CA   B GLU   B 1 104 ? 36.970 -27.179 12.936  0.30 26.69 ?  104 GLU   B CA   1 
ATOM   5405 C C    A GLU   B 1 104 ? 35.948 -27.651 12.187  0.70 26.46 ?  104 GLU   B C    1 
ATOM   5406 C C    B GLU   B 1 104 ? 35.811 -27.677 12.078  0.30 26.49 ?  104 GLU   B C    1 
ATOM   5407 O O    A GLU   B 1 104 ? 35.994 -28.750 11.626  0.70 27.08 ?  104 GLU   B O    1 
ATOM   5408 O O    B GLU   B 1 104 ? 35.899 -28.714 11.414  0.30 26.52 ?  104 GLU   B O    1 
ATOM   5409 C CB   A GLU   B 1 104 ? 37.958 -26.109 12.203  0.70 24.41 ?  104 GLU   B CB   1 
ATOM   5410 C CB   B GLU   B 1 104 ? 37.818 -26.162 12.173  0.30 25.83 ?  104 GLU   B CB   1 
ATOM   5411 C CG   A GLU   B 1 104 ? 39.058 -25.477 13.048  0.70 23.06 ?  104 GLU   B CG   1 
ATOM   5412 C CG   B GLU   B 1 104 ? 38.920 -25.557 13.036  0.30 25.05 ?  104 GLU   B CG   1 
ATOM   5413 C CD   A GLU   B 1 104 ? 39.998 -24.585 12.267  0.70 21.60 ?  104 GLU   B CD   1 
ATOM   5414 C CD   B GLU   B 1 104 ? 39.864 -24.654 12.266  0.30 24.39 ?  104 GLU   B CD   1 
ATOM   5415 O OE1  A GLU   B 1 104 ? 40.006 -24.635 11.018  0.70 19.63 ?  104 GLU   B OE1  1 
ATOM   5416 O OE1  B GLU   B 1 104 ? 39.808 -24.634 11.018  0.30 23.96 ?  104 GLU   B OE1  1 
ATOM   5417 O OE2  A GLU   B 1 104 ? 40.737 -23.823 12.924  0.70 22.23 -1 104 GLU   B OE2  1 
ATOM   5418 O OE2  B GLU   B 1 104 ? 40.669 -23.959 12.922  0.30 24.31 -1 104 GLU   B OE2  1 
ATOM   5419 H H    A GLU   B 1 104 ? 38.723 -28.259 13.080  0.70 33.10 ?  104 GLU   B H    1 
ATOM   5420 H H    B GLU   B 1 104 ? 38.502 -28.416 12.897  0.30 33.44 ?  104 GLU   B H    1 
ATOM   5421 H HA   A GLU   B 1 104 ? 36.762 -26.638 13.772  0.70 31.15 ?  104 GLU   B HA   1 
ATOM   5422 H HA   B GLU   B 1 104 ? 36.599 -26.736 13.714  0.30 32.02 ?  104 GLU   B HA   1 
ATOM   5423 H HB2  A GLU   B 1 104 ? 38.377 -26.566 11.458  0.70 29.29 ?  104 GLU   B HB2  1 
ATOM   5424 H HB2  B GLU   B 1 104 ? 38.235 -26.600 11.415  0.30 30.99 ?  104 GLU   B HB2  1 
ATOM   5425 H HB3  A GLU   B 1 104 ? 37.382 -25.399 11.880  0.70 29.29 ?  104 GLU   B HB3  1 
ATOM   5426 H HB3  B GLU   B 1 104 ? 37.247 -25.440 11.867  0.30 30.99 ?  104 GLU   B HB3  1 
ATOM   5427 H HG2  A GLU   B 1 104 ? 38.652 -24.930 13.739  0.70 27.68 ?  104 GLU   B HG2  1 
ATOM   5428 H HG2  B GLU   B 1 104 ? 38.514 -25.027 13.740  0.30 30.07 ?  104 GLU   B HG2  1 
ATOM   5429 H HG3  A GLU   B 1 104 ? 39.591 -26.177 13.455  0.70 27.68 ?  104 GLU   B HG3  1 
ATOM   5430 H HG3  B GLU   B 1 104 ? 39.445 -26.274 13.426  0.30 30.07 ?  104 GLU   B HG3  1 
ATOM   5431 N N    A ASP   B 1 105 ? 34.881 -26.856 12.133  0.70 26.74 ?  105 ASP   B N    1 
ATOM   5432 N N    B ASP   B 1 105 ? 34.717 -26.920 12.100  0.30 26.44 ?  105 ASP   B N    1 
ATOM   5433 C CA   A ASP   B 1 105 ? 33.598 -27.311 11.607  0.70 27.42 ?  105 ASP   B CA   1 
ATOM   5434 C CA   B ASP   B 1 105 ? 33.460 -27.376 11.518  0.30 26.56 ?  105 ASP   B CA   1 
ATOM   5435 C C    A ASP   B 1 105 ? 33.630 -27.355 10.082  0.70 25.35 ?  105 ASP   B C    1 
ATOM   5436 C C    B ASP   B 1 105 ? 33.553 -27.397 9.996   0.30 25.57 ?  105 ASP   B C    1 
ATOM   5437 O O    A ASP   B 1 105 ? 33.770 -26.318 9.426   0.70 24.53 ?  105 ASP   B O    1 
ATOM   5438 O O    B ASP   B 1 105 ? 33.760 -26.358 9.361   0.30 25.08 ?  105 ASP   B O    1 
ATOM   5439 C CB   A ASP   B 1 105 ? 32.490 -26.378 12.092  0.70 30.50 ?  105 ASP   B CB   1 
ATOM   5440 C CB   B ASP   B 1 105 ? 32.321 -26.467 11.972  0.30 27.65 ?  105 ASP   B CB   1 
ATOM   5441 C CG   A ASP   B 1 105 ? 31.113 -26.816 11.632  0.70 32.75 ?  105 ASP   B CG   1 
ATOM   5442 C CG   B ASP   B 1 105 ? 30.952 -27.054 11.671  0.30 28.35 ?  105 ASP   B CG   1 
ATOM   5443 O OD1  A ASP   B 1 105 ? 30.991 -27.924 11.069  0.70 33.07 ?  105 ASP   B OD1  1 
ATOM   5444 O OD1  B ASP   B 1 105 ? 30.878 -28.020 10.883  0.30 28.53 ?  105 ASP   B OD1  1 
ATOM   5445 O OD2  A ASP   B 1 105 ? 30.150 -26.044 11.829  0.70 34.25 -1 105 ASP   B OD2  1 
ATOM   5446 O OD2  B ASP   B 1 105 ? 29.952 -26.558 12.232  0.30 28.48 -1 105 ASP   B OD2  1 
ATOM   5447 H H    A ASP   B 1 105 ? 34.881 -26.037 12.394  0.70 32.08 ?  105 ASP   B H    1 
ATOM   5448 H H    B ASP   B 1 105 ? 34.677 -26.135 12.446  0.30 31.73 ?  105 ASP   B H    1 
ATOM   5449 H HA   A ASP   B 1 105 ? 33.415 -28.205 11.939  0.70 32.90 ?  105 ASP   B HA   1 
ATOM   5450 H HA   B ASP   B 1 105 ? 33.270 -28.277 11.822  0.30 31.88 ?  105 ASP   B HA   1 
ATOM   5451 H HB2  A ASP   B 1 105 ? 32.509 -26.345 13.065  0.70 36.60 ?  105 ASP   B HB2  1 
ATOM   5452 H HB2  B ASP   B 1 105 ? 32.387 -26.333 12.932  0.30 33.18 ?  105 ASP   B HB2  1 
ATOM   5453 H HB3  A ASP   B 1 105 ? 32.641 -25.493 11.730  0.70 36.60 ?  105 ASP   B HB3  1 
ATOM   5454 H HB3  B ASP   B 1 105 ? 32.395 -25.613 11.514  0.30 33.18 ?  105 ASP   B HB3  1 
ATOM   5455 N N    A ILE   B 1 106 ? 33.469 -28.557 9.523   0.70 24.77 ?  106 ILE   B N    1 
ATOM   5456 N N    B ILE   B 1 106 ? 33.387 -28.588 9.413   0.30 25.18 ?  106 ILE   B N    1 
ATOM   5457 C CA   A ILE   B 1 106 ? 33.458 -28.736 8.075   0.70 23.81 ?  106 ILE   B CA   1 
ATOM   5458 C CA   B ILE   B 1 106 ? 33.403 -28.741 7.964   0.30 24.85 ?  106 ILE   B CA   1 
ATOM   5459 C C    A ILE   B 1 106 ? 32.363 -27.910 7.403   0.70 22.36 ?  106 ILE   B C    1 
ATOM   5460 C C    B ILE   B 1 106 ? 32.310 -27.914 7.299   0.30 24.29 ?  106 ILE   B C    1 
ATOM   5461 O O    A ILE   B 1 106 ? 32.469 -27.589 6.214   0.70 21.50 ?  106 ILE   B O    1 
ATOM   5462 O O    B ILE   B 1 106 ? 32.402 -27.610 6.105   0.30 23.96 ?  106 ILE   B O    1 
ATOM   5463 C CB   A ILE   B 1 106 ? 33.350 -30.244 7.746   0.70 24.84 ?  106 ILE   B CB   1 
ATOM   5464 C CB   B ILE   B 1 106 ? 33.299 -30.240 7.600   0.30 25.20 ?  106 ILE   B CB   1 
ATOM   5465 C CG1  A ILE   B 1 106 ? 33.588 -30.500 6.257   0.70 25.44 ?  106 ILE   B CG1  1 
ATOM   5466 C CG1  B ILE   B 1 106 ? 33.588 -30.465 6.114   0.30 25.38 ?  106 ILE   B CG1  1 
ATOM   5467 C CG2  A ILE   B 1 106 ? 31.995 -30.795 8.178   0.70 25.59 ?  106 ILE   B CG2  1 
ATOM   5468 C CG2  B ILE   B 1 106 ? 31.925 -30.786 7.961   0.30 25.49 ?  106 ILE   B CG2  1 
ATOM   5469 C CD1  A ILE   B 1 106 ? 34.954 -30.061 5.781   0.70 25.71 ?  106 ILE   B CD1  1 
ATOM   5470 C CD1  B ILE   B 1 106 ? 34.967 -30.015 5.689   0.30 25.49 ?  106 ILE   B CD1  1 
ATOM   5471 H H    A ILE   B 1 106 ? 33.371 -29.284 9.970   0.70 29.72 ?  106 ILE   B H    1 
ATOM   5472 H H    B ILE   B 1 106 ? 33.270 -29.321 9.841   0.30 30.22 ?  106 ILE   B H    1 
ATOM   5473 H HA   A ILE   B 1 106 ? 34.307 -28.424 7.734   0.70 28.57 ?  106 ILE   B HA   1 
ATOM   5474 H HA   B ILE   B 1 106 ? 34.251 -28.414 7.635   0.30 29.82 ?  106 ILE   B HA   1 
ATOM   5475 H HB   A ILE   B 1 106 ? 34.036 -30.715 8.247   0.70 29.81 ?  106 ILE   B HB   1 
ATOM   5476 H HB   B ILE   B 1 106 ? 33.962 -30.725 8.115   0.30 30.24 ?  106 ILE   B HB   1 
ATOM   5477 H HG12 A ILE   B 1 106 ? 33.510 -31.453 6.087   0.70 30.52 ?  106 ILE   B HG12 1 
ATOM   5478 H HG12 B ILE   B 1 106 ? 33.517 -31.415 5.923   0.30 30.45 ?  106 ILE   B HG12 1 
ATOM   5479 H HG13 A ILE   B 1 106 ? 32.925 -30.019 5.743   0.70 30.52 ?  106 ILE   B HG13 1 
ATOM   5480 H HG13 B ILE   B 1 106 ? 32.939 -29.976 5.587   0.30 30.45 ?  106 ILE   B HG13 1 
ATOM   5481 H HG21 A ILE   B 1 106 ? 31.999 -31.760 8.073   0.70 30.70 ?  106 ILE   B HG21 1 
ATOM   5482 H HG21 B ILE   B 1 106 ? 31.940 -31.753 7.883   0.30 30.59 ?  106 ILE   B HG21 1 
ATOM   5483 H HG22 A ILE   B 1 106 ? 31.843 -30.566 9.109   0.70 30.70 ?  106 ILE   B HG22 1 
ATOM   5484 H HG22 B ILE   B 1 106 ? 31.714 -30.531 8.873   0.30 30.59 ?  106 ILE   B HG22 1 
ATOM   5485 H HG23 A ILE   B 1 106 ? 31.302 -30.406 7.624   0.70 30.70 ?  106 ILE   B HG23 1 
ATOM   5486 H HG23 B ILE   B 1 106 ? 31.266 -30.416 7.353   0.30 30.59 ?  106 ILE   B HG23 1 
ATOM   5487 H HD11 A ILE   B 1 106 ? 35.131 -30.463 4.917   0.70 30.85 ?  106 ILE   B HD11 1 
ATOM   5488 H HD11 B ILE   B 1 106 ? 35.175 -30.411 4.830   0.30 30.59 ?  106 ILE   B HD11 1 
ATOM   5489 H HD12 A ILE   B 1 106 ? 34.968 -29.093 5.704   0.70 30.85 ?  106 ILE   B HD12 1 
ATOM   5490 H HD12 B ILE   B 1 106 ? 34.975 -29.048 5.618   0.30 30.59 ?  106 ILE   B HD12 1 
ATOM   5491 H HD13 A ILE   B 1 106 ? 35.622 -30.351 6.423   0.70 30.85 ?  106 ILE   B HD13 1 
ATOM   5492 H HD13 B ILE   B 1 106 ? 35.612 -30.306 6.353   0.30 30.59 ?  106 ILE   B HD13 1 
ATOM   5493 N N    A GLN   B 1 107 ? 31.317 -27.537 8.142   0.70 23.16 ?  107 GLN   B N    1 
ATOM   5494 N N    B GLN   B 1 107 ? 31.270 -27.538 8.048   0.30 24.40 ?  107 GLN   B N    1 
ATOM   5495 C CA   A GLN   B 1 107 ? 30.238 -26.744 7.559   0.70 23.97 ?  107 GLN   B CA   1 
ATOM   5496 C CA   B GLN   B 1 107 ? 30.203 -26.716 7.489   0.30 24.54 ?  107 GLN   B CA   1 
ATOM   5497 C C    A GLN   B 1 107 ? 30.725 -25.397 7.032   0.70 22.19 ?  107 GLN   B C    1 
ATOM   5498 C C    B GLN   B 1 107 ? 30.704 -25.351 7.030   0.30 22.44 ?  107 GLN   B C    1 
ATOM   5499 O O    A GLN   B 1 107 ? 30.094 -24.832 6.135   0.70 22.75 ?  107 GLN   B O    1 
ATOM   5500 O O    B GLN   B 1 107 ? 30.057 -24.721 6.187   0.30 22.72 ?  107 GLN   B O    1 
ATOM   5501 C CB   A GLN   B 1 107 ? 29.128 -26.547 8.595   0.70 27.53 ?  107 GLN   B CB   1 
ATOM   5502 C CB   B GLN   B 1 107 ? 29.082 -26.556 8.520   0.30 26.95 ?  107 GLN   B CB   1 
ATOM   5503 C CG   A GLN   B 1 107 ? 27.804 -26.052 8.026   0.70 31.33 ?  107 GLN   B CG   1 
ATOM   5504 C CG   B GLN   B 1 107 ? 27.748 -26.100 7.942   0.30 29.28 ?  107 GLN   B CG   1 
ATOM   5505 C CD   A GLN   B 1 107 ? 27.736 -24.539 7.914   0.70 34.07 ?  107 GLN   B CD   1 
ATOM   5506 C CD   B GLN   B 1 107 ? 27.615 -24.591 7.880   0.30 31.07 ?  107 GLN   B CD   1 
ATOM   5507 O OE1  A GLN   B 1 107 ? 28.573 -23.824 8.468   0.70 35.15 ?  107 GLN   B OE1  1 
ATOM   5508 O OE1  B GLN   B 1 107 ? 28.423 -23.858 8.452   0.30 31.78 ?  107 GLN   B OE1  1 
ATOM   5509 N NE2  A GLN   B 1 107 ? 26.732 -24.043 7.194   0.70 35.14 ?  107 GLN   B NE2  1 
ATOM   5510 N NE2  B GLN   B 1 107 ? 26.587 -24.118 7.184   0.30 31.69 ?  107 GLN   B NE2  1 
ATOM   5511 H H    A GLN   B 1 107 ? 31.216 -27.720 8.972   0.70 27.79 ?  107 GLN   B H    1 
ATOM   5512 H H    B GLN   B 1 107 ? 31.157 -27.749 8.872   0.30 29.28 ?  107 GLN   B H    1 
ATOM   5513 H HA   A GLN   B 1 107 ? 29.862 -27.237 6.814   0.70 28.77 ?  107 GLN   B HA   1 
ATOM   5514 H HA   B GLN   B 1 107 ? 29.828 -27.173 6.718   0.30 29.44 ?  107 GLN   B HA   1 
ATOM   5515 H HB2  A GLN   B 1 107 ? 28.961 -27.396 9.028   0.70 33.03 ?  107 GLN   B HB2  1 
ATOM   5516 H HB2  B GLN   B 1 107 ? 28.933 -27.411 8.951   0.30 32.34 ?  107 GLN   B HB2  1 
ATOM   5517 H HB3  A GLN   B 1 107 ? 29.430 -25.900 9.251   0.70 33.03 ?  107 GLN   B HB3  1 
ATOM   5518 H HB3  B GLN   B 1 107 ? 29.357 -25.902 9.182   0.30 32.34 ?  107 GLN   B HB3  1 
ATOM   5519 H HG2  A GLN   B 1 107 ? 27.679 -26.422 7.139   0.70 37.60 ?  107 GLN   B HG2  1 
ATOM   5520 H HG2  B GLN   B 1 107 ? 27.659 -26.445 7.040   0.30 35.14 ?  107 GLN   B HG2  1 
ATOM   5521 H HG3  A GLN   B 1 107 ? 27.083 -26.345 8.610   0.70 37.60 ?  107 GLN   B HG3  1 
ATOM   5522 H HG3  B GLN   B 1 107 ? 27.029 -26.444 8.499   0.30 35.14 ?  107 GLN   B HG3  1 
ATOM   5523 H HE21 A GLN   B 1 107 ? 26.166 -24.573 6.819   0.70 42.17 ?  107 GLN   B HE21 1 
ATOM   5524 H HE21 B GLN   B 1 107 ? 26.043 -24.660 6.796   0.30 38.03 ?  107 GLN   B HE21 1 
ATOM   5525 H HE22 A GLN   B 1 107 ? 26.645 -23.192 7.104   0.70 42.17 ?  107 GLN   B HE22 1 
ATOM   5526 H HE22 B GLN   B 1 107 ? 26.464 -23.269 7.121   0.30 38.03 ?  107 GLN   B HE22 1 
ATOM   5527 N N    . LEU   B 1 108 ? 31.840 -24.882 7.550   1.00 20.21 ?  108 LEU   B N    1 
ATOM   5528 C CA   . LEU   B 1 108 ? 32.388 -23.588 7.141   1.00 18.18 ?  108 LEU   B CA   1 
ATOM   5529 C C    . LEU   B 1 108 ? 33.042 -23.615 5.767   1.00 15.93 ?  108 LEU   B C    1 
ATOM   5530 O O    . LEU   B 1 108 ? 33.470 -22.558 5.279   1.00 15.77 ?  108 LEU   B O    1 
ATOM   5531 C CB   . LEU   B 1 108 ? 33.393 -23.101 8.181   1.00 18.81 ?  108 LEU   B CB   1 
ATOM   5532 C CG   . LEU   B 1 108 ? 32.773 -22.630 9.496   1.00 20.08 ?  108 LEU   B CG   1 
ATOM   5533 C CD1  . LEU   B 1 108 ? 33.802 -22.581 10.613  1.00 20.39 ?  108 LEU   B CD1  1 
ATOM   5534 C CD2  . LEU   B 1 108 ? 32.145 -21.261 9.305   1.00 21.12 ?  108 LEU   B CD2  1 
ATOM   5535 H H    A LEU   B 1 108 ? 32.300 -25.270 8.161   0.70 24.25 ?  108 LEU   B H    1 
ATOM   5536 H H    B LEU   B 1 108 ? 32.304 -25.290 8.144   0.30 24.25 ?  108 LEU   B H    1 
ATOM   5537 H HA   . LEU   B 1 108 ? 31.662 -22.946 7.106   1.00 21.81 ?  108 LEU   B HA   1 
ATOM   5538 H HB2  . LEU   B 1 108 ? 33.996 -23.826 8.393   1.00 22.57 ?  108 LEU   B HB2  1 
ATOM   5539 H HB3  . LEU   B 1 108 ? 33.886 -22.356 7.811   1.00 22.57 ?  108 LEU   B HB3  1 
ATOM   5540 H HG   . LEU   B 1 108 ? 32.069 -23.245 9.763   1.00 24.09 ?  108 LEU   B HG   1 
ATOM   5541 H HD11 . LEU   B 1 108 ? 33.363 -22.316 11.439  1.00 24.46 ?  108 LEU   B HD11 1 
ATOM   5542 H HD12 . LEU   B 1 108 ? 34.196 -23.459 10.717  1.00 24.46 ?  108 LEU   B HD12 1 
ATOM   5543 H HD13 . LEU   B 1 108 ? 34.486 -21.933 10.383  1.00 24.46 ?  108 LEU   B HD13 1 
ATOM   5544 H HD21 . LEU   B 1 108 ? 31.806 -20.944 10.157  1.00 25.34 ?  108 LEU   B HD21 1 
ATOM   5545 H HD22 . LEU   B 1 108 ? 32.819 -20.649 8.970   1.00 25.34 ?  108 LEU   B HD22 1 
ATOM   5546 H HD23 . LEU   B 1 108 ? 31.417 -21.332 8.667   1.00 25.34 ?  108 LEU   B HD23 1 
ATOM   5547 N N    . LEU   B 1 109 ? 33.114 -24.783 5.133   1.00 15.17 ?  109 LEU   B N    1 
ATOM   5548 C CA   . LEU   B 1 109 ? 33.747 -24.886 3.826   1.00 14.22 ?  109 LEU   B CA   1 
ATOM   5549 C C    . LEU   B 1 109 ? 32.986 -24.093 2.771   1.00 13.54 ?  109 LEU   B C    1 
ATOM   5550 O O    . LEU   B 1 109 ? 33.600 -23.502 1.878   1.00 13.40 ?  109 LEU   B O    1 
ATOM   5551 C CB   . LEU   B 1 109 ? 33.852 -26.357 3.432   1.00 14.17 ?  109 LEU   B CB   1 
ATOM   5552 C CG   . LEU   B 1 109 ? 34.651 -26.694 2.174   1.00 13.90 ?  109 LEU   B CG   1 
ATOM   5553 C CD1  . LEU   B 1 109 ? 36.034 -26.054 2.211   1.00 14.16 ?  109 LEU   B CD1  1 
ATOM   5554 C CD2  . LEU   B 1 109 ? 34.763 -28.207 2.010   1.00 14.83 ?  109 LEU   B CD2  1 
ATOM   5555 H H    . LEU   B 1 109 ? 32.811 -25.524 5.434   1.00 18.20 ?  109 LEU   B H    1 
ATOM   5556 H HA   . LEU   B 1 109 ? 34.644 -24.524 3.879   1.00 17.07 ?  109 LEU   B HA   1 
ATOM   5557 H HB2  . LEU   B 1 109 ? 34.268 -26.836 4.165   1.00 17.00 ?  109 LEU   B HB2  1 
ATOM   5558 H HB3  . LEU   B 1 109 ? 32.954 -26.700 3.298   1.00 17.00 ?  109 LEU   B HB3  1 
ATOM   5559 H HG   . LEU   B 1 109 ? 34.178 -26.354 1.397   1.00 16.68 ?  109 LEU   B HG   1 
ATOM   5560 H HD11 . LEU   B 1 109 ? 36.573 -26.419 1.491   1.00 16.99 ?  109 LEU   B HD11 1 
ATOM   5561 H HD12 . LEU   B 1 109 ? 35.939 -25.096 2.100   1.00 16.99 ?  109 LEU   B HD12 1 
ATOM   5562 H HD13 . LEU   B 1 109 ? 36.449 -26.252 3.065   1.00 16.99 ?  109 LEU   B HD13 1 
ATOM   5563 H HD21 . LEU   B 1 109 ? 35.355 -28.402 1.265   1.00 17.79 ?  109 LEU   B HD21 1 
ATOM   5564 H HD22 . LEU   B 1 109 ? 35.119 -28.588 2.825   1.00 17.79 ?  109 LEU   B HD22 1 
ATOM   5565 H HD23 . LEU   B 1 109 ? 33.880 -28.575 1.831   1.00 17.79 ?  109 LEU   B HD23 1 
ATOM   5566 N N    . LYS   B 1 110 ? 31.651 -24.072 2.844   1.00 13.43 ?  110 LYS   B N    1 
ATOM   5567 C CA   . LYS   B 1 110 ? 30.892 -23.306 1.858   1.00 13.29 ?  110 LYS   B CA   1 
ATOM   5568 C C    . LYS   B 1 110 ? 31.228 -21.816 1.950   1.00 13.07 ?  110 LYS   B C    1 
ATOM   5569 O O    . LYS   B 1 110 ? 31.489 -21.166 0.933   1.00 12.68 ?  110 LYS   B O    1 
ATOM   5570 C CB   . LYS   B 1 110 ? 29.388 -23.559 2.005   1.00 14.10 ?  110 LYS   B CB   1 
ATOM   5571 C CG   . LYS   B 1 110 ? 28.574 -22.921 0.882   1.00 14.37 ?  110 LYS   B CG   1 
ATOM   5572 C CD   . LYS   B 1 110 ? 27.117 -23.360 0.902   1.00 14.93 ?  110 LYS   B CD   1 
ATOM   5573 C CE   . LYS   B 1 110 ? 26.350 -22.826 -0.308  1.00 15.39 ?  110 LYS   B CE   1 
ATOM   5574 N NZ   . LYS   B 1 110 ? 26.684 -23.530 -1.575  1.00 15.59 ?  110 LYS   B NZ   1 
ATOM   5575 H H    . LYS   B 1 110 ? 31.179 -24.485 3.430   1.00 16.11 ?  110 LYS   B H    1 
ATOM   5576 H HA   . LYS   B 1 110 ? 31.151 -23.608 0.970   1.00 15.95 ?  110 LYS   B HA   1 
ATOM   5577 H HB2  . LYS   B 1 110 ? 29.225 -24.518 1.983   1.00 16.92 ?  110 LYS   B HB2  1 
ATOM   5578 H HB3  . LYS   B 1 110 ? 29.085 -23.191 2.845   1.00 16.92 ?  110 LYS   B HB3  1 
ATOM   5579 H HG2  . LYS   B 1 110 ? 28.592 -21.956 0.983   1.00 17.24 ?  110 LYS   B HG2  1 
ATOM   5580 H HG3  . LYS   B 1 110 ? 28.948 -23.174 0.025   1.00 17.24 ?  110 LYS   B HG3  1 
ATOM   5581 H HD2  . LYS   B 1 110 ? 27.071 -24.333 0.885   1.00 17.91 ?  110 LYS   B HD2  1 
ATOM   5582 H HD3  . LYS   B 1 110 ? 26.686 -23.025 1.706   1.00 17.91 ?  110 LYS   B HD3  1 
ATOM   5583 H HE2  . LYS   B 1 110 ? 25.399 -22.931 -0.154  1.00 18.47 ?  110 LYS   B HE2  1 
ATOM   5584 H HE3  . LYS   B 1 110 ? 26.566 -21.888 -0.424  1.00 18.47 ?  110 LYS   B HE3  1 
ATOM   5585 H HZ1  . LYS   B 1 110 ? 26.221 -23.183 -2.248  1.00 18.70 ?  110 LYS   B HZ1  1 
ATOM   5586 H HZ2  . LYS   B 1 110 ? 27.555 -23.443 -1.748  1.00 18.70 ?  110 LYS   B HZ2  1 
ATOM   5587 H HZ3  . LYS   B 1 110 ? 26.491 -24.395 -1.502  1.00 18.70 ?  110 LYS   B HZ3  1 
ATOM   5588 N N    . SER   B 1 111 ? 31.247 -21.266 3.168   1.00 13.41 ?  111 SER   B N    1 
ATOM   5589 C CA   . SER   B 1 111 ? 31.638 -19.868 3.348   1.00 13.26 ?  111 SER   B CA   1 
ATOM   5590 C C    . SER   B 1 111 ? 33.019 -19.605 2.763   1.00 12.91 ?  111 SER   B C    1 
ATOM   5591 O O    . SER   B 1 111 ? 33.247 -18.566 2.123   1.00 13.06 ?  111 SER   B O    1 
ATOM   5592 C CB   . SER   B 1 111 ? 31.627 -19.513 4.833   1.00 14.47 ?  111 SER   B CB   1 
ATOM   5593 O OG   . SER   B 1 111 ? 30.318 -19.526 5.360   1.00 16.36 ?  111 SER   B OG   1 
ATOM   5594 H H    . SER   B 1 111 ? 31.046 -21.682 3.892   1.00 16.09 ?  111 SER   B H    1 
ATOM   5595 H HA   . SER   B 1 111 ? 31.004 -19.299 2.892   1.00 15.91 ?  111 SER   B HA   1 
ATOM   5596 H HB2  . SER   B 1 111 ? 32.165 -20.162 5.317   1.00 17.37 ?  111 SER   B HB2  1 
ATOM   5597 H HB3  . SER   B 1 111 ? 31.993 -18.628 4.949   1.00 17.37 ?  111 SER   B HB3  1 
ATOM   5598 H HG   . SER   B 1 111 ? 30.331 -19.338 6.183   1.00 19.64 ?  111 SER   B HG   1 
ATOM   5599 N N    . ALA   B 1 112 ? 33.962 -20.523 2.986   1.00 12.95 ?  112 ALA   B N    1 
ATOM   5600 C CA   . ALA   B 1 112 ? 35.307 -20.348 2.445   1.00 12.63 ?  112 ALA   B CA   1 
ATOM   5601 C C    . ALA   B 1 112 ? 35.278 -20.251 0.923   1.00 11.88 ?  112 ALA   B C    1 
ATOM   5602 O O    . ALA   B 1 112 ? 35.904 -19.362 0.332   1.00 12.35 ?  112 ALA   B O    1 
ATOM   5603 C CB   . ALA   B 1 112 ? 36.215 -21.493 2.911   1.00 13.47 ?  112 ALA   B CB   1 
ATOM   5604 H H    . ALA   B 1 112 ? 33.852 -21.247 3.449   1.00 15.53 ?  112 ALA   B H    1 
ATOM   5605 H HA   . ALA   B 1 112 ? 35.675 -19.520 2.793   1.00 15.16 ?  112 ALA   B HA   1 
ATOM   5606 H HB1  . ALA   B 1 112 ? 37.107 -21.351 2.551   1.00 16.17 ?  112 ALA   B HB1  1 
ATOM   5607 H HB2  . ALA   B 1 112 ? 36.253 -21.491 3.883   1.00 16.17 ?  112 ALA   B HB2  1 
ATOM   5608 H HB3  . ALA   B 1 112 ? 35.857 -22.332 2.595   1.00 16.17 ?  112 ALA   B HB3  1 
ATOM   5609 N N    . TYR   B 1 113 ? 34.552 -21.158 0.264   1.00 11.91 ?  113 TYR   B N    1 
ATOM   5610 C CA   . TYR   B 1 113 ? 34.471 -21.105 -1.190  1.00 11.75 ?  113 TYR   B CA   1 
ATOM   5611 C C    . TYR   B 1 113 ? 33.763 -19.851 -1.703  1.00 11.78 ?  113 TYR   B C    1 
ATOM   5612 O O    . TYR   B 1 113 ? 34.034 -19.417 -2.827  1.00 11.65 ?  113 TYR   B O    1 
ATOM   5613 C CB   . TYR   B 1 113 ? 33.796 -22.367 -1.737  1.00 11.98 ?  113 TYR   B CB   1 
ATOM   5614 C CG   . TYR   B 1 113 ? 34.757 -23.512 -2.003  1.00 12.15 ?  113 TYR   B CG   1 
ATOM   5615 C CD1  . TYR   B 1 113 ? 35.744 -23.408 -2.977  1.00 12.43 ?  113 TYR   B CD1  1 
ATOM   5616 C CD2  . TYR   B 1 113 ? 34.664 -24.706 -1.298  1.00 12.46 ?  113 TYR   B CD2  1 
ATOM   5617 C CE1  . TYR   B 1 113 ? 36.623 -24.442 -3.226  1.00 12.77 ?  113 TYR   B CE1  1 
ATOM   5618 C CE2  . TYR   B 1 113 ? 35.533 -25.757 -1.549  1.00 12.72 ?  113 TYR   B CE2  1 
ATOM   5619 C CZ   . TYR   B 1 113 ? 36.507 -25.622 -2.518  1.00 12.54 ?  113 TYR   B CZ   1 
ATOM   5620 O OH   . TYR   B 1 113 ? 37.387 -26.644 -2.792  1.00 13.39 ?  113 TYR   B OH   1 
ATOM   5621 H H    . TYR   B 1 113 ? 34.105 -21.798 0.637   1.00 14.29 ?  113 TYR   B H    1 
ATOM   5622 H HA   . TYR   B 1 113 ? 35.370 -21.089 -1.533  1.00 14.10 ?  113 TYR   B HA   1 
ATOM   5623 H HB2  . TYR   B 1 113 ? 33.139 -22.683 -1.094  1.00 14.38 ?  113 TYR   B HB2  1 
ATOM   5624 H HB3  . TYR   B 1 113 ? 33.356 -22.150 -2.573  1.00 14.38 ?  113 TYR   B HB3  1 
ATOM   5625 H HD1  . TYR   B 1 113 ? 35.823 -22.617 -3.463  1.00 14.92 ?  113 TYR   B HD1  1 
ATOM   5626 H HD2  . TYR   B 1 113 ? 34.002 -24.801 -0.654  1.00 14.95 ?  113 TYR   B HD2  1 
ATOM   5627 H HE1  . TYR   B 1 113 ? 37.274 -24.355 -3.890  1.00 15.33 ?  113 TYR   B HE1  1 
ATOM   5628 H HE2  . TYR   B 1 113 ? 35.453 -26.550 -1.076  1.00 15.26 ?  113 TYR   B HE2  1 
ATOM   5629 H HH   . TYR   B 1 113 ? 37.211 -27.309 -2.308  1.00 16.06 ?  113 TYR   B HH   1 
ATOM   5630 N N    . GLU   B 1 114 ? 32.840 -19.272 -0.924  1.00 11.78 ?  114 GLU   B N    1 
ATOM   5631 C CA   . GLU   B 1 114 ? 32.152 -18.067 -1.377  1.00 11.74 ?  114 GLU   B CA   1 
ATOM   5632 C C    . GLU   B 1 114 ? 33.135 -16.942 -1.670  1.00 11.74 ?  114 GLU   B C    1 
ATOM   5633 O O    . GLU   B 1 114 ? 32.861 -16.088 -2.513  1.00 12.05 ?  114 GLU   B O    1 
ATOM   5634 C CB   . GLU   B 1 114 ? 31.092 -17.648 -0.360  1.00 12.10 ?  114 GLU   B CB   1 
ATOM   5635 C CG   . GLU   B 1 114 ? 29.878 -18.569 -0.432  1.00 12.29 ?  114 GLU   B CG   1 
ATOM   5636 C CD   . GLU   B 1 114 ? 28.853 -18.378 0.675   1.00 12.55 ?  114 GLU   B CD   1 
ATOM   5637 O OE1  . GLU   B 1 114 ? 29.148 -17.768 1.724   1.00 12.99 ?  114 GLU   B OE1  1 
ATOM   5638 O OE2  . GLU   B 1 114 ? 27.730 -18.910 0.509   1.00 13.34 -1 114 GLU   B OE2  1 
ATOM   5639 H H    . GLU   B 1 114 ? 32.595 -19.560 -0.147  1.00 14.14 ?  114 GLU   B H    1 
ATOM   5640 H HA   . GLU   B 1 114 ? 31.699 -18.266 -2.202  1.00 14.09 ?  114 GLU   B HA   1 
ATOM   5641 H HB2  . GLU   B 1 114 ? 31.463 -17.702 0.537   1.00 14.52 ?  114 GLU   B HB2  1 
ATOM   5642 H HB3  . GLU   B 1 114 ? 30.800 -16.746 -0.551  1.00 14.52 ?  114 GLU   B HB3  1 
ATOM   5643 H HG2  . GLU   B 1 114 ? 29.433 -18.421 -1.278  1.00 14.74 ?  114 GLU   B HG2  1 
ATOM   5644 H HG3  . GLU   B 1 114 ? 30.193 -19.491 -0.390  1.00 14.74 ?  114 GLU   B HG3  1 
ATOM   5645 N N    . ASN   B 1 115 ? 34.302 -16.937 -1.020  1.00 11.46 ?  115 ASN   B N    1 
ATOM   5646 C CA   . ASN   B 1 115 ? 35.296 -15.904 -1.319  1.00 11.37 ?  115 ASN   B CA   1 
ATOM   5647 C C    . ASN   B 1 115 ? 35.710 -15.926 -2.784  1.00 11.11 ?  115 ASN   B C    1 
ATOM   5648 O O    . ASN   B 1 115 ? 36.098 -14.889 -3.339  1.00 11.74 ?  115 ASN   B O    1 
ATOM   5649 C CB   . ASN   B 1 115 ? 36.536 -16.077 -0.436  1.00 12.10 ?  115 ASN   B CB   1 
ATOM   5650 C CG   . ASN   B 1 115 ? 36.268 -15.819 1.027   1.00 12.49 ?  115 ASN   B CG   1 
ATOM   5651 O OD1  . ASN   B 1 115 ? 36.266 -14.673 1.469   1.00 14.48 ?  115 ASN   B OD1  1 
ATOM   5652 N ND2  . ASN   B 1 115 ? 36.104 -16.888 1.803   1.00 12.61 ?  115 ASN   B ND2  1 
ATOM   5653 H H    . ASN   B 1 115 ? 34.536 -17.500 -0.409  1.00 13.76 ?  115 ASN   B H    1 
ATOM   5654 H HA   . ASN   B 1 115 ? 34.916 -15.034 -1.128  1.00 13.65 ?  115 ASN   B HA   1 
ATOM   5655 H HB2  . ASN   B 1 115 ? 36.868 -16.983 -0.525  1.00 14.52 ?  115 ASN   B HB2  1 
ATOM   5656 H HB3  . ASN   B 1 115 ? 37.217 -15.446 -0.722  1.00 14.52 ?  115 ASN   B HB3  1 
ATOM   5657 H HD21 . ASN   B 1 115 ? 35.957 -16.790 2.647   1.00 15.13 ?  115 ASN   B HD21 1 
ATOM   5658 H HD22 . ASN   B 1 115 ? 36.126 -17.677 1.462   1.00 15.13 ?  115 ASN   B HD22 1 
ATOM   5659 N N    . PHE   B 1 116 ? 35.681 -17.104 -3.422  1.00 10.93 ?  116 PHE   B N    1 
ATOM   5660 C CA   . PHE   B 1 116 ? 36.116 -17.192 -4.813  1.00 11.29 ?  116 PHE   B CA   1 
ATOM   5661 C C    . PHE   B 1 116 ? 35.211 -16.368 -5.724  1.00 11.18 ?  116 PHE   B C    1 
ATOM   5662 O O    . PHE   B 1 116 ? 35.645 -15.937 -6.796  1.00 11.58 ?  116 PHE   B O    1 
ATOM   5663 C CB   . PHE   B 1 116 ? 36.087 -18.637 -5.339  1.00 11.22 ?  116 PHE   B CB   1 
ATOM   5664 C CG   . PHE   B 1 116 ? 37.156 -19.590 -4.787  1.00 11.17 ?  116 PHE   B CG   1 
ATOM   5665 C CD1  . PHE   B 1 116 ? 37.813 -19.405 -3.582  1.00 11.87 ?  116 PHE   B CD1  1 
ATOM   5666 C CD2  . PHE   B 1 116 ? 37.458 -20.727 -5.520  1.00 11.39 ?  116 PHE   B CD2  1 
ATOM   5667 C CE1  . PHE   B 1 116 ? 38.745 -20.348 -3.130  1.00 12.13 ?  116 PHE   B CE1  1 
ATOM   5668 C CE2  . PHE   B 1 116 ? 38.382 -21.668 -5.074  1.00 11.54 ?  116 PHE   B CE2  1 
ATOM   5669 C CZ   . PHE   B 1 116 ? 39.025 -21.477 -3.883  1.00 11.63 ?  116 PHE   B CZ   1 
ATOM   5670 H H    . PHE   B 1 116 ? 35.413 -17.851 -3.079  1.00 13.11 ?  116 PHE   B H    1 
ATOM   5671 H HA   . PHE   B 1 116 ? 37.020 -16.857 -4.891  1.00 13.55 ?  116 PHE   B HA   1 
ATOM   5672 H HB2  . PHE   B 1 116 ? 35.215 -19.019 -5.128  1.00 13.47 ?  116 PHE   B HB2  1 
ATOM   5673 H HB3  . PHE   B 1 116 ? 36.190 -18.609 -6.305  1.00 13.47 ?  116 PHE   B HB3  1 
ATOM   5674 H HD1  . PHE   B 1 116 ? 37.621 -18.653 -3.066  1.00 14.25 ?  116 PHE   B HD1  1 
ATOM   5675 H HD2  . PHE   B 1 116 ? 37.014 -20.882 -6.326  1.00 13.67 ?  116 PHE   B HD2  1 
ATOM   5676 H HE1  . PHE   B 1 116 ? 39.186 -20.204 -2.325  1.00 14.56 ?  116 PHE   B HE1  1 
ATOM   5677 H HE2  . PHE   B 1 116 ? 38.568 -22.420 -5.588  1.00 13.85 ?  116 PHE   B HE2  1 
ATOM   5678 H HZ   . PHE   B 1 116 ? 39.659 -22.086 -3.585  1.00 13.96 ?  116 PHE   B HZ   1 
ATOM   5679 N N    . ASN   B 1 117 ? 33.939 -16.175 -5.342  1.00 11.52 ?  117 ASN   B N    1 
ATOM   5680 C CA   . ASN   B 1 117 ? 32.994 -15.465 -6.206  1.00 11.86 ?  117 ASN   B CA   1 
ATOM   5681 C C    . ASN   B 1 117 ? 33.311 -13.983 -6.353  1.00 12.11 ?  117 ASN   B C    1 
ATOM   5682 O O    . ASN   B 1 117 ? 32.721 -13.328 -7.214  1.00 13.16 ?  117 ASN   B O    1 
ATOM   5683 C CB   . ASN   B 1 117 ? 31.571 -15.685 -5.715  1.00 12.07 ?  117 ASN   B CB   1 
ATOM   5684 C CG   . ASN   B 1 117 ? 31.118 -17.096 -5.964  1.00 12.38 ?  117 ASN   B CG   1 
ATOM   5685 O OD1  . ASN   B 1 117 ? 31.466 -17.684 -6.988  1.00 13.18 ?  117 ASN   B OD1  1 
ATOM   5686 N ND2  . ASN   B 1 117 ? 30.381 -17.669 -5.023  1.00 12.30 ?  117 ASN   B ND2  1 
ATOM   5687 H H    . ASN   B 1 117 ? 33.609 -16.443 -4.590  1.00 13.83 ?  117 ASN   B H    1 
ATOM   5688 H HA   . ASN   B 1 117 ? 33.055 -15.857 -7.087  1.00 14.23 ?  117 ASN   B HA   1 
ATOM   5689 H HB2  . ASN   B 1 117 ? 31.526 -15.512 -4.760  1.00 14.49 ?  117 ASN   B HB2  1 
ATOM   5690 H HB3  . ASN   B 1 117 ? 30.974 -15.077 -6.188  1.00 14.49 ?  117 ASN   B HB3  1 
ATOM   5691 H HD21 . ASN   B 1 117 ? 30.101 -18.474 -5.126  1.00 14.76 ?  117 ASN   B HD21 1 
ATOM   5692 H HD22 . ASN   B 1 117 ? 30.160 -17.225 -4.317  1.00 14.76 ?  117 ASN   B HD22 1 
ATOM   5693 N N    . GLN   B 1 118 ? 34.248 -13.457 -5.572  1.00 11.93 ?  118 GLN   B N    1 
ATOM   5694 C CA   . GLN   B 1 118 ? 34.678 -12.067 -5.703  1.00 12.22 ?  118 GLN   B CA   1 
ATOM   5695 C C    . GLN   B 1 118 ? 35.741 -11.873 -6.778  1.00 12.60 ?  118 GLN   B C    1 
ATOM   5696 O O    . GLN   B 1 118 ? 36.216 -10.746 -6.957  1.00 13.95 ?  118 GLN   B O    1 
ATOM   5697 C CB   . GLN   B 1 118 ? 35.156 -11.542 -4.347  1.00 12.99 ?  118 GLN   B CB   1 
ATOM   5698 C CG   . GLN   B 1 118 ? 34.069 -11.582 -3.279  1.00 13.09 ?  118 GLN   B CG   1 
ATOM   5699 C CD   . GLN   B 1 118 ? 32.894 -10.672 -3.609  1.00 12.99 ?  118 GLN   B CD   1 
ATOM   5700 O OE1  . GLN   B 1 118 ? 33.080 -9.530  -4.056  1.00 13.80 ?  118 GLN   B OE1  1 
ATOM   5701 N NE2  . GLN   B 1 118 ? 31.680 -11.167 -3.397  1.00 13.50 ?  118 GLN   B NE2  1 
ATOM   5702 H H    . GLN   B 1 118 ? 34.665 -13.887 -4.947  1.00 14.31 ?  118 GLN   B H    1 
ATOM   5703 H HA   . GLN   B 1 118 ? 33.909 -11.538 -5.965  1.00 14.67 ?  118 GLN   B HA   1 
ATOM   5704 H HB2  . GLN   B 1 118 ? 35.899 -12.079 -4.040  1.00 15.59 ?  118 GLN   B HB2  1 
ATOM   5705 H HB3  . GLN   B 1 118 ? 35.436 -10.614 -4.449  1.00 15.59 ?  118 GLN   B HB3  1 
ATOM   5706 H HG2  . GLN   B 1 118 ? 33.738 -12.490 -3.202  1.00 15.71 ?  118 GLN   B HG2  1 
ATOM   5707 H HG3  . GLN   B 1 118 ? 34.446 -11.291 -2.434  1.00 15.71 ?  118 GLN   B HG3  1 
ATOM   5708 H HE21 . GLN   B 1 118 ? 31.591 -11.964 -3.085  1.00 16.20 ?  118 GLN   B HE21 1 
ATOM   5709 H HE22 . GLN   B 1 118 ? 30.992 -10.691 -3.574  1.00 16.20 ?  118 GLN   B HE22 1 
ATOM   5710 N N    . HIS   B 1 119 ? 36.099 -12.932 -7.507  1.00 11.61 ?  119 HIS   B N    1 
ATOM   5711 C CA   . HIS   B 1 119 ? 37.141 -12.887 -8.525  1.00 12.13 ?  119 HIS   B CA   1 
ATOM   5712 C C    . HIS   B 1 119 ? 36.665 -13.622 -9.766  1.00 12.47 ?  119 HIS   B C    1 
ATOM   5713 O O    . HIS   B 1 119 ? 36.159 -14.741 -9.665  1.00 13.01 ?  119 HIS   B O    1 
ATOM   5714 C CB   . HIS   B 1 119 ? 38.425 -13.514 -7.979  1.00 12.83 ?  119 HIS   B CB   1 
ATOM   5715 C CG   . HIS   B 1 119 ? 38.904 -12.823 -6.747  1.00 14.25 ?  119 HIS   B CG   1 
ATOM   5716 N ND1  . HIS   B 1 119 ? 39.702 -11.699 -6.790  1.00 15.78 ?  119 HIS   B ND1  1 
ATOM   5717 C CD2  . HIS   B 1 119 ? 38.612 -13.034 -5.443  1.00 15.24 ?  119 HIS   B CD2  1 
ATOM   5718 C CE1  . HIS   B 1 119 ? 39.911 -11.274 -5.557  1.00 16.67 ?  119 HIS   B CE1  1 
ATOM   5719 N NE2  . HIS   B 1 119 ? 39.253 -12.058 -4.723  1.00 16.74 ?  119 HIS   B NE2  1 
ATOM   5720 H H    . HIS   B 1 119 ? 35.734 -13.709 -7.432  1.00 13.93 ?  119 HIS   B H    1 
ATOM   5721 H HA   . HIS   B 1 119 ? 37.321 -11.960 -8.762  1.00 14.56 ?  119 HIS   B HA   1 
ATOM   5722 H HB2  . HIS   B 1 119 ? 38.257 -14.443 -7.767  1.00 15.40 ?  119 HIS   B HB2  1 
ATOM   5723 H HB3  . HIS   B 1 119 ? 39.120 -13.445 -8.655  1.00 15.40 ?  119 HIS   B HB3  1 
ATOM   5724 H HD2  . HIS   B 1 119 ? 38.076 -13.718 -5.102  1.00 18.29 ?  119 HIS   B HD2  1 
ATOM   5725 H HE1  . HIS   B 1 119 ? 40.441 -10.552 -5.312  1.00 20.00 ?  119 HIS   B HE1  1 
ATOM   5726 H HE2  . HIS   B 1 119 ? 39.255 -11.995 -3.864  1.00 20.09 ?  119 HIS   B HE2  1 
ATOM   5727 N N    . GLU   B 1 120 ? 36.821 -13.005 -10.938 1.00 12.91 ?  120 GLU   B N    1 
ATOM   5728 C CA   . GLU   B 1 120 ? 36.226 -13.590 -12.135 1.00 14.43 ?  120 GLU   B CA   1 
ATOM   5729 C C    . GLU   B 1 120 ? 36.906 -14.889 -12.554 1.00 13.13 ?  120 GLU   B C    1 
ATOM   5730 O O    . GLU   B 1 120 ? 36.248 -15.763 -13.130 1.00 13.30 ?  120 GLU   B O    1 
ATOM   5731 C CB   . GLU   B 1 120 ? 36.212 -12.581 -13.280 1.00 18.53 ?  120 GLU   B CB   1 
ATOM   5732 C CG   . GLU   B 1 120 ? 35.245 -11.435 -13.045 1.00 24.08 ?  120 GLU   B CG   1 
ATOM   5733 C CD   . GLU   B 1 120 ? 35.051 -10.558 -14.264 1.00 29.25 ?  120 GLU   B CD   1 
ATOM   5734 O OE1  . GLU   B 1 120 ? 36.016 -10.384 -15.039 1.00 31.65 ?  120 GLU   B OE1  1 
ATOM   5735 O OE2  . GLU   B 1 120 ? 33.928 -10.041 -14.443 1.00 32.24 -1 120 GLU   B OE2  1 
ATOM   5736 H H    . GLU   B 1 120 ? 37.252 -12.268 -11.064 1.00 15.49 ?  120 GLU   B H    1 
ATOM   5737 H HA   . GLU   B 1 120 ? 35.307 -13.810 -11.936 1.00 17.32 ?  120 GLU   B HA   1 
ATOM   5738 H HB2  . GLU   B 1 120 ? 37.095 -12.205 -13.386 1.00 22.23 ?  120 GLU   B HB2  1 
ATOM   5739 H HB3  . GLU   B 1 120 ? 35.940 -13.033 -14.095 1.00 22.23 ?  120 GLU   B HB3  1 
ATOM   5740 H HG2  . GLU   B 1 120 ? 34.376 -11.796 -12.803 1.00 28.89 ?  120 GLU   B HG2  1 
ATOM   5741 H HG3  . GLU   B 1 120 ? 35.582 -10.877 -12.328 1.00 28.89 ?  120 GLU   B HG3  1 
ATOM   5742 N N    . VAL   B 1 121 ? 38.205 -15.027 -12.289 1.00 12.52 ?  121 VAL   B N    1 
ATOM   5743 C CA   . VAL   B 1 121 ? 38.954 -16.234 -12.637 1.00 12.21 ?  121 VAL   B CA   1 
ATOM   5744 C C    . VAL   B 1 121 ? 40.065 -16.436 -11.615 1.00 11.92 ?  121 VAL   B C    1 
ATOM   5745 O O    . VAL   B 1 121 ? 40.742 -15.478 -11.224 1.00 12.68 ?  121 VAL   B O    1 
ATOM   5746 C CB   . VAL   B 1 121 ? 39.471 -16.197 -14.094 1.00 13.79 ?  121 VAL   B CB   1 
ATOM   5747 C CG1  . VAL   B 1 121 ? 40.344 -14.970 -14.351 1.00 15.33 ?  121 VAL   B CG1  1 
ATOM   5748 C CG2  . VAL   B 1 121 ? 40.206 -17.481 -14.442 1.00 15.66 ?  121 VAL   B CG2  1 
ATOM   5749 H H    . VAL   B 1 121 ? 38.690 -14.421 -11.911 1.00 15.02 ?  121 VAL   B H    1 
ATOM   5750 H HA   . VAL   B 1 121 ? 38.350 -16.987 -12.569 1.00 14.65 ?  121 VAL   B HA   1 
ATOM   5751 H HB   . VAL   B 1 121 ? 38.704 -16.132 -14.689 1.00 16.55 ?  121 VAL   B HB   1 
ATOM   5752 H HG11 . VAL   B 1 121 ? 40.648 -14.984 -15.272 1.00 18.39 ?  121 VAL   B HG11 1 
ATOM   5753 H HG12 . VAL   B 1 121 ? 39.821 -14.168 -14.189 1.00 18.39 ?  121 VAL   B HG12 1 
ATOM   5754 H HG13 . VAL   B 1 121 ? 41.106 -14.993 -13.751 1.00 18.39 ?  121 VAL   B HG13 1 
ATOM   5755 H HG21 . VAL   B 1 121 ? 40.405 -17.480 -15.393 1.00 18.79 ?  121 VAL   B HG21 1 
ATOM   5756 H HG22 . VAL   B 1 121 ? 41.030 -17.520 -13.934 1.00 18.79 ?  121 VAL   B HG22 1 
ATOM   5757 H HG23 . VAL   B 1 121 ? 39.641 -18.236 -14.224 1.00 18.79 ?  121 VAL   B HG23 1 
ATOM   5758 N N    . LEU   B 1 122 ? 40.249 -17.690 -11.183 1.00 11.57 ?  122 LEU   B N    1 
ATOM   5759 C CA   . LEU   B 1 122 ? 41.231 -18.041 -10.162 1.00 11.37 ?  122 LEU   B CA   1 
ATOM   5760 C C    . LEU   B 1 122 ? 41.889 -19.371 -10.492 1.00 11.41 ?  122 LEU   B C    1 
ATOM   5761 O O    . LEU   B 1 122 ? 41.228 -20.294 -10.989 1.00 12.56 ?  122 LEU   B O    1 
ATOM   5762 C CB   . LEU   B 1 122 ? 40.579 -18.274 -8.786  1.00 13.00 ?  122 LEU   B CB   1 
ATOM   5763 C CG   . LEU   B 1 122 ? 39.543 -17.255 -8.294  1.00 12.91 ?  122 LEU   B CG   1 
ATOM   5764 C CD1  . LEU   B 1 122 ? 38.143 -17.608 -8.776  1.00 13.92 ?  122 LEU   B CD1  1 
ATOM   5765 C CD2  . LEU   B 1 122 ? 39.587 -17.149 -6.780  1.00 12.62 ?  122 LEU   B CD2  1 
ATOM   5766 H H    . LEU   B 1 122 ? 39.810 -18.369 -11.478 1.00 13.88 ?  122 LEU   B H    1 
ATOM   5767 H HA   . LEU   B 1 122 ? 41.906 -17.346 -10.085 1.00 13.65 ?  122 LEU   B HA   1 
ATOM   5768 H HB2  . LEU   B 1 122 ? 40.137 -19.132 -8.810  1.00 15.60 ?  122 LEU   B HB2  1 
ATOM   5769 H HB3  . LEU   B 1 122 ? 41.287 -18.296 -8.124  1.00 15.60 ?  122 LEU   B HB3  1 
ATOM   5770 H HG   . LEU   B 1 122 ? 39.770 -16.382 -8.651  1.00 15.49 ?  122 LEU   B HG   1 
ATOM   5771 H HD11 . LEU   B 1 122 ? 37.515 -16.967 -8.405  1.00 16.70 ?  122 LEU   B HD11 1 
ATOM   5772 H HD12 . LEU   B 1 122 ? 38.126 -17.562 -9.745  1.00 16.70 ?  122 LEU   B HD12 1 
ATOM   5773 H HD13 . LEU   B 1 122 ? 37.924 -18.500 -8.478  1.00 16.70 ?  122 LEU   B HD13 1 
ATOM   5774 H HD21 . LEU   B 1 122 ? 38.911 -16.521 -6.482  1.00 15.14 ?  122 LEU   B HD21 1 
ATOM   5775 H HD22 . LEU   B 1 122 ? 39.422 -18.022 -6.392  1.00 15.14 ?  122 LEU   B HD22 1 
ATOM   5776 H HD23 . LEU   B 1 122 ? 40.468 -16.832 -6.507  1.00 15.14 ?  122 LEU   B HD23 1 
ATOM   5777 N N    . LEU   B 1 123 ? 43.177 -19.478 -10.136 1.00 10.94 ?  123 LEU   B N    1 
ATOM   5778 C CA   . LEU   B 1 123 ? 43.893 -20.749 -10.013 1.00 11.19 ?  123 LEU   B CA   1 
ATOM   5779 C C    . LEU   B 1 123 ? 43.858 -21.150 -8.542  1.00 10.93 ?  123 LEU   B C    1 
ATOM   5780 O O    . LEU   B 1 123 ? 44.203 -20.325 -7.683  1.00 11.29 ?  123 LEU   B O    1 
ATOM   5781 C CB   . LEU   B 1 123 ? 45.343 -20.570 -10.471 1.00 11.52 ?  123 LEU   B CB   1 
ATOM   5782 C CG   . LEU   B 1 123 ? 46.282 -21.755 -10.222 1.00 11.93 ?  123 LEU   B CG   1 
ATOM   5783 C CD1  . LEU   B 1 123 ? 45.862 -23.000 -11.001 1.00 12.38 ?  123 LEU   B CD1  1 
ATOM   5784 C CD2  . LEU   B 1 123 ? 47.704 -21.360 -10.576 1.00 12.66 ?  123 LEU   B CD2  1 
ATOM   5785 H H    . LEU   B 1 123 ? 43.668 -18.798 -9.946  1.00 13.13 ?  123 LEU   B H    1 
ATOM   5786 H HA   . LEU   B 1 123 ? 43.457 -21.435 -10.543 1.00 13.43 ?  123 LEU   B HA   1 
ATOM   5787 H HB2  . LEU   B 1 123 ? 45.335 -20.407 -11.428 1.00 13.82 ?  123 LEU   B HB2  1 
ATOM   5788 H HB3  . LEU   B 1 123 ? 45.715 -19.806 -10.014 1.00 13.82 ?  123 LEU   B HB3  1 
ATOM   5789 H HG   . LEU   B 1 123 ? 46.265 -21.983 -9.278  1.00 14.32 ?  123 LEU   B HG   1 
ATOM   5790 H HD11 . LEU   B 1 123 ? 46.494 -23.712 -10.819 1.00 14.85 ?  123 LEU   B HD11 1 
ATOM   5791 H HD12 . LEU   B 1 123 ? 44.973 -23.265 -10.715 1.00 14.85 ?  123 LEU   B HD12 1 
ATOM   5792 H HD13 . LEU   B 1 123 ? 45.859 -22.791 -11.946 1.00 14.85 ?  123 LEU   B HD13 1 
ATOM   5793 H HD21 . LEU   B 1 123 ? 48.293 -22.113 -10.416 1.00 15.19 ?  123 LEU   B HD21 1 
ATOM   5794 H HD22 . LEU   B 1 123 ? 47.737 -21.104 -11.510 1.00 15.19 ?  123 LEU   B HD22 1 
ATOM   5795 H HD23 . LEU   B 1 123 ? 47.968 -20.610 -10.018 1.00 15.19 ?  123 LEU   B HD23 1 
ATOM   5796 N N    . ALA   B 1 124 ? 43.425 -22.381 -8.237  1.00 10.65 ?  124 ALA   B N    1 
ATOM   5797 C CA   . ALA   B 1 124 ? 43.169 -22.698 -6.839  1.00 10.98 ?  124 ALA   B CA   1 
ATOM   5798 C C    . ALA   B 1 124 ? 43.441 -24.159 -6.517  1.00 10.86 ?  124 ALA   B C    1 
ATOM   5799 O O    . ALA   B 1 124 ? 43.308 -25.034 -7.383  1.00 11.39 ?  124 ALA   B O    1 
ATOM   5800 C CB   . ALA   B 1 124 ? 41.721 -22.377 -6.460  1.00 11.76 ?  124 ALA   B CB   1 
ATOM   5801 H H    . ALA   B 1 124 ? 43.246 -23.015 -8.803  1.00 12.77 ?  124 ALA   B H    1 
ATOM   5802 H HA   . ALA   B 1 124 ? 43.752 -22.152 -6.298  1.00 13.18 ?  124 ALA   B HA   1 
ATOM   5803 H HB1  . ALA   B 1 124 ? 41.578 -22.597 -5.527  1.00 14.11 ?  124 ALA   B HB1  1 
ATOM   5804 H HB2  . ALA   B 1 124 ? 41.563 -21.429 -6.604  1.00 14.11 ?  124 ALA   B HB2  1 
ATOM   5805 H HB3  . ALA   B 1 124 ? 41.122 -22.898 -7.019  1.00 14.11 ?  124 ALA   B HB3  1 
ATOM   5806 N N    . PRO   B 1 125 ? 43.734 -24.455 -5.251  1.00 11.01 ?  125 PRO   B N    1 
ATOM   5807 C CA   . PRO   B 1 125 ? 43.673 -25.820 -4.728  1.00 11.49 ?  125 PRO   B CA   1 
ATOM   5808 C C    . PRO   B 1 125 ? 42.272 -26.095 -4.183  1.00 11.77 ?  125 PRO   B C    1 
ATOM   5809 O O    . PRO   B 1 125 ? 41.479 -25.180 -3.965  1.00 12.21 ?  125 PRO   B O    1 
ATOM   5810 C CB   . PRO   B 1 125 ? 44.658 -25.742 -3.555  1.00 12.61 ?  125 PRO   B CB   1 
ATOM   5811 C CG   . PRO   B 1 125 ? 44.406 -24.358 -2.984  1.00 12.87 ?  125 PRO   B CG   1 
ATOM   5812 C CD   . PRO   B 1 125 ? 44.064 -23.485 -4.188  1.00 11.76 ?  125 PRO   B CD   1 
ATOM   5813 H HA   . PRO   B 1 125 ? 43.952 -26.489 -5.373  1.00 13.79 ?  125 PRO   B HA   1 
ATOM   5814 H HB2  . PRO   B 1 125 ? 44.454 -26.429 -2.896  1.00 15.13 ?  125 PRO   B HB2  1 
ATOM   5815 H HB3  . PRO   B 1 125 ? 45.569 -25.826 -3.873  1.00 15.13 ?  125 PRO   B HB3  1 
ATOM   5816 H HG2  . PRO   B 1 125 ? 43.658 -24.380 -2.362  1.00 15.44 ?  125 PRO   B HG2  1 
ATOM   5817 H HG3  . PRO   B 1 125 ? 45.205 -24.028 -2.536  1.00 15.44 ?  125 PRO   B HG3  1 
ATOM   5818 H HD2  . PRO   B 1 125 ? 43.305 -22.915 -3.993  1.00 14.11 ?  125 PRO   B HD2  1 
ATOM   5819 H HD3  . PRO   B 1 125 ? 44.843 -22.951 -4.444  1.00 14.11 ?  125 PRO   B HD3  1 
ATOM   5820 N N    . LEU   B 1 126 ? 41.996 -27.376 -3.915  1.00 12.13 ?  126 LEU   B N    1 
ATOM   5821 C CA   . LEU   B 1 126 ? 40.775 -27.742 -3.204  1.00 12.78 ?  126 LEU   B CA   1 
ATOM   5822 C C    . LEU   B 1 126 ? 40.888 -27.343 -1.741  1.00 12.76 ?  126 LEU   B C    1 
ATOM   5823 O O    . LEU   B 1 126 ? 41.777 -27.804 -1.021  1.00 14.47 ?  126 LEU   B O    1 
ATOM   5824 C CB   . LEU   B 1 126 ? 40.513 -29.238 -3.321  1.00 13.89 ?  126 LEU   B CB   1 
ATOM   5825 C CG   . LEU   B 1 126 ? 39.988 -29.724 -4.672  1.00 14.66 ?  126 LEU   B CG   1 
ATOM   5826 C CD1  . LEU   B 1 126 ? 40.028 -31.238 -4.749  1.00 16.31 ?  126 LEU   B CD1  1 
ATOM   5827 C CD2  . LEU   B 1 126 ? 38.576 -29.223 -4.918  1.00 15.34 ?  126 LEU   B CD2  1 
ATOM   5828 H H    . LEU   B 1 126 ? 42.502 -28.042 -4.125  1.00 14.56 ?  126 LEU   B H    1 
ATOM   5829 H HA   . LEU   B 1 126 ? 40.030 -27.262 -3.595  1.00 15.34 ?  126 LEU   B HA   1 
ATOM   5830 H HB2  . LEU   B 1 126 ? 41.340 -29.706 -3.145  1.00 16.67 ?  126 LEU   B HB2  1 
ATOM   5831 H HB3  . LEU   B 1 126 ? 39.853 -29.479 -2.653  1.00 16.67 ?  126 LEU   B HB3  1 
ATOM   5832 H HG   . LEU   B 1 126 ? 40.558 -29.376 -5.377  1.00 17.60 ?  126 LEU   B HG   1 
ATOM   5833 H HD11 . LEU   B 1 126 ? 39.689 -31.522 -5.614  1.00 19.58 ?  126 LEU   B HD11 1 
ATOM   5834 H HD12 . LEU   B 1 126 ? 40.939 -31.541 -4.634  1.00 19.58 ?  126 LEU   B HD12 1 
ATOM   5835 H HD13 . LEU   B 1 126 ? 39.466 -31.605 -4.043  1.00 19.58 ?  126 LEU   B HD13 1 
ATOM   5836 H HD21 . LEU   B 1 126 ? 38.229 -29.635 -5.723  1.00 18.41 ?  126 LEU   B HD21 1 
ATOM   5837 H HD22 . LEU   B 1 126 ? 38.021 -29.456 -4.158  1.00 18.41 ?  126 LEU   B HD22 1 
ATOM   5838 H HD23 . LEU   B 1 126 ? 38.597 -28.256 -5.025  1.00 18.41 ?  126 LEU   B HD23 1 
ATOM   5839 N N    . LEU   B 1 127 ? 39.961 -26.507 -1.286  1.00 12.70 ?  127 LEU   B N    1 
ATOM   5840 C CA   . LEU   B 1 127 ? 40.008 -26.023 0.083   1.00 12.78 ?  127 LEU   B CA   1 
ATOM   5841 C C    . LEU   B 1 127 ? 39.736 -27.147 1.075   1.00 12.81 ?  127 LEU   B C    1 
ATOM   5842 O O    . LEU   B 1 127 ? 38.917 -28.045 0.841   1.00 13.08 ?  127 LEU   B O    1 
ATOM   5843 C CB   . LEU   B 1 127 ? 38.990 -24.899 0.293   1.00 13.86 ?  127 LEU   B CB   1 
ATOM   5844 C CG   . LEU   B 1 127 ? 39.168 -23.632 -0.542  1.00 14.42 ?  127 LEU   B CG   1 
ATOM   5845 C CD1  . LEU   B 1 127 ? 38.049 -22.661 -0.195  1.00 14.33 ?  127 LEU   B CD1  1 
ATOM   5846 C CD2  . LEU   B 1 127 ? 40.531 -22.986 -0.322  1.00 14.81 ?  127 LEU   B CD2  1 
ATOM   5847 H H    . LEU   B 1 127 ? 39.293 -26.200 -1.746  1.00 15.25 ?  127 LEU   B H    1 
ATOM   5848 H HA   . LEU   B 1 127 ? 40.893 -25.661 0.264   1.00 15.34 ?  127 LEU   B HA   1 
ATOM   5849 H HB2  . LEU   B 1 127 ? 38.108 -25.249 0.097   1.00 16.63 ?  127 LEU   B HB2  1 
ATOM   5850 H HB3  . LEU   B 1 127 ? 39.024 -24.628 1.226   1.00 16.63 ?  127 LEU   B HB3  1 
ATOM   5851 H HG   . LEU   B 1 127 ? 39.076 -23.850 -1.480  1.00 17.30 ?  127 LEU   B HG   1 
ATOM   5852 H HD11 . LEU   B 1 127 ? 38.153 -21.849 -0.721  1.00 17.19 ?  127 LEU   B HD11 1 
ATOM   5853 H HD12 . LEU   B 1 127 ? 37.192 -23.070 -0.388  1.00 17.19 ?  127 LEU   B HD12 1 
ATOM   5854 H HD13 . LEU   B 1 127 ? 38.101 -22.440 0.753   1.00 17.19 ?  127 LEU   B HD13 1 
ATOM   5855 H HD21 . LEU   B 1 127 ? 40.564 -22.139 -0.800  1.00 17.77 ?  127 LEU   B HD21 1 
ATOM   5856 H HD22 . LEU   B 1 127 ? 40.661 -22.830 0.627   1.00 17.77 ?  127 LEU   B HD22 1 
ATOM   5857 H HD23 . LEU   B 1 127 ? 41.217 -23.580 -0.658  1.00 17.77 ?  127 LEU   B HD23 1 
ATOM   5858 N N    . SER   B 1 128 ? 40.419 -27.064 2.207   1.00 12.94 ?  128 SER   B N    1 
ATOM   5859 C CA   . SER   B 1 128 ? 40.312 -27.986 3.326   1.00 13.30 ?  128 SER   B CA   1 
ATOM   5860 C C    . SER   B 1 128 ? 40.807 -29.392 2.997   1.00 14.32 ?  128 SER   B C    1 
ATOM   5861 O O    . SER   B 1 128 ? 40.725 -30.273 3.851   1.00 15.50 ?  128 SER   B O    1 
ATOM   5862 C CB   . SER   B 1 128 ? 38.911 -27.993 3.953   1.00 13.55 ?  128 SER   B CB   1 
ATOM   5863 O OG   . SER   B 1 128 ? 38.595 -26.721 4.507   1.00 14.25 ?  128 SER   B OG   1 
ATOM   5864 H H    . SER   B 1 128 ? 40.992 -26.438 2.357   1.00 15.53 ?  128 SER   B H    1 
ATOM   5865 H HA   . SER   B 1 128 ? 40.899 -27.651 4.015   1.00 15.96 ?  128 SER   B HA   1 
ATOM   5866 H HB2  . SER   B 1 128 ? 38.254 -28.227 3.276   1.00 16.26 ?  128 SER   B HB2  1 
ATOM   5867 H HB3  . SER   B 1 128 ? 38.889 -28.668 4.666   1.00 16.26 ?  128 SER   B HB3  1 
ATOM   5868 H HG   . SER   B 1 128 ? 39.162 -26.526 5.092   1.00 17.09 ?  128 SER   B HG   1 
ATOM   5869 N N    . ALA   B 1 129 ? 41.375 -29.613 1.809   1.00 14.89 ?  129 ALA   B N    1 
ATOM   5870 C CA   . ALA   B 1 129 ? 41.926 -30.909 1.450   1.00 15.92 ?  129 ALA   B CA   1 
ATOM   5871 C C    . ALA   B 1 129 ? 43.317 -31.082 2.050   1.00 15.06 ?  129 ALA   B C    1 
ATOM   5872 O O    . ALA   B 1 129 ? 43.880 -30.176 2.683   1.00 15.21 ?  129 ALA   B O    1 
ATOM   5873 C CB   . ALA   B 1 129 ? 41.974 -31.066 -0.067  1.00 17.91 ?  129 ALA   B CB   1 
ATOM   5874 H H    . ALA   B 1 129 ? 41.448 -29.021 1.189   1.00 17.87 ?  129 ALA   B H    1 
ATOM   5875 H HA   . ALA   B 1 129 ? 41.354 -31.605 1.806   1.00 19.10 ?  129 ALA   B HA   1 
ATOM   5876 H HB1  . ALA   B 1 129 ? 42.338 -31.940 -0.283  1.00 21.49 ?  129 ALA   B HB1  1 
ATOM   5877 H HB2  . ALA   B 1 129 ? 41.075 -30.986 -0.422  1.00 21.49 ?  129 ALA   B HB2  1 
ATOM   5878 H HB3  . ALA   B 1 129 ? 42.540 -30.372 -0.440  1.00 21.49 ?  129 ALA   B HB3  1 
ATOM   5879 N N    . GLY   B 1 130 ? 43.875 -32.273 1.840   1.00 14.82 ?  130 GLY   B N    1 
ATOM   5880 C CA   . GLY   B 1 130 ? 45.263 -32.507 2.190   1.00 15.89 ?  130 GLY   B CA   1 
ATOM   5881 C C    . GLY   B 1 130 ? 45.478 -32.414 3.682   1.00 15.65 ?  130 GLY   B C    1 
ATOM   5882 O O    . GLY   B 1 130 ? 44.783 -33.060 4.479   1.00 16.69 ?  130 GLY   B O    1 
ATOM   5883 H H    . GLY   B 1 130 ? 43.476 -32.953 1.491   1.00 17.79 ?  130 GLY   B H    1 
ATOM   5884 H HA2  . GLY   B 1 130 ? 45.532 -33.393 1.894   1.00 19.07 ?  130 GLY   B HA2  1 
ATOM   5885 H HA3  . GLY   B 1 130 ? 45.828 -31.851 1.750   1.00 19.07 ?  130 GLY   B HA3  1 
ATOM   5886 N N    . ILE   B 1 131 ? 46.452 -31.585 4.071   1.00 15.77 ?  131 ILE   B N    1 
ATOM   5887 C CA   . ILE   B 1 131 ? 46.809 -31.447 5.471   1.00 16.80 ?  131 ILE   B CA   1 
ATOM   5888 C C    . ILE   B 1 131 ? 45.691 -30.849 6.307   1.00 16.19 ?  131 ILE   B C    1 
ATOM   5889 O O    . ILE   B 1 131 ? 45.765 -30.914 7.536   1.00 17.66 ?  131 ILE   B O    1 
ATOM   5890 C CB   . ILE   B 1 131 ? 48.132 -30.664 5.654   1.00 18.78 ?  131 ILE   B CB   1 
ATOM   5891 C CG1  . ILE   B 1 131 ? 47.965 -29.190 5.260   1.00 19.64 ?  131 ILE   B CG1  1 
ATOM   5892 C CG2  . ILE   B 1 131 ? 49.251 -31.319 4.848   1.00 19.79 ?  131 ILE   B CG2  1 
ATOM   5893 C CD1  . ILE   B 1 131 ? 49.170 -28.321 5.594   1.00 20.80 ?  131 ILE   B CD1  1 
ATOM   5894 H H    . ILE   B 1 131 ? 46.920 -31.095 3.539   1.00 18.92 ?  131 ILE   B H    1 
ATOM   5895 H HA   . ILE   B 1 131 ? 46.960 -32.333 5.825   1.00 20.16 ?  131 ILE   B HA   1 
ATOM   5896 H HB   . ILE   B 1 131 ? 48.372 -30.698 6.594   1.00 22.54 ?  131 ILE   B HB   1 
ATOM   5897 H HG12 . ILE   B 1 131 ? 47.814 -29.140 4.303   1.00 23.57 ?  131 ILE   B HG12 1 
ATOM   5898 H HG13 . ILE   B 1 131 ? 47.198 -28.817 5.730   1.00 23.57 ?  131 ILE   B HG13 1 
ATOM   5899 H HG21 . ILE   B 1 131 ? 50.092 -30.909 5.093   1.00 23.75 ?  131 ILE   B HG21 1 
ATOM   5900 H HG22 . ILE   B 1 131 ? 49.266 -32.265 5.050   1.00 23.75 ?  131 ILE   B HG22 1 
ATOM   5901 H HG23 . ILE   B 1 131 ? 49.073 -31.182 3.904   1.00 23.75 ?  131 ILE   B HG23 1 
ATOM   5902 H HD11 . ILE   B 1 131 ? 48.955 -27.397 5.394   1.00 24.96 ?  131 ILE   B HD11 1 
ATOM   5903 H HD12 . ILE   B 1 131 ? 49.374 -28.417 6.537   1.00 24.96 ?  131 ILE   B HD12 1 
ATOM   5904 H HD13 . ILE   B 1 131 ? 49.923 -28.611 5.059   1.00 24.96 ?  131 ILE   B HD13 1 
ATOM   5905 N N    . PHE   B 1 132 ? 44.659 -30.270 5.675   1.00 15.00 ?  132 PHE   B N    1 
ATOM   5906 C CA   . PHE   B 1 132 ? 43.494 -29.767 6.399   1.00 15.43 ?  132 PHE   B CA   1 
ATOM   5907 C C    . PHE   B 1 132 ? 42.469 -30.857 6.721   1.00 16.73 ?  132 PHE   B C    1 
ATOM   5908 O O    . PHE   B 1 132 ? 41.558 -30.610 7.518   1.00 18.37 ?  132 PHE   B O    1 
ATOM   5909 C CB   . PHE   B 1 132 ? 42.823 -28.627 5.617   1.00 14.48 ?  132 PHE   B CB   1 
ATOM   5910 C CG   . PHE   B 1 132 ? 43.524 -27.286 5.736   1.00 14.74 ?  132 PHE   B CG   1 
ATOM   5911 C CD1  . PHE   B 1 132 ? 44.820 -27.102 5.267   1.00 15.65 ?  132 PHE   B CD1  1 
ATOM   5912 C CD2  . PHE   B 1 132 ? 42.852 -26.192 6.262   1.00 14.40 ?  132 PHE   B CD2  1 
ATOM   5913 C CE1  . PHE   B 1 132 ? 45.442 -25.863 5.365   1.00 16.24 ?  132 PHE   B CE1  1 
ATOM   5914 C CE2  . PHE   B 1 132 ? 43.462 -24.952 6.357   1.00 14.87 ?  132 PHE   B CE2  1 
ATOM   5915 C CZ   . PHE   B 1 132 ? 44.756 -24.788 5.906   1.00 16.15 ?  132 PHE   B CZ   1 
ATOM   5916 H H    . PHE   B 1 132 ? 44.614 -30.153 4.821   1.00 17.99 ?  132 PHE   B H    1 
ATOM   5917 H HA   . PHE   B 1 132 ? 43.799 -29.391 7.238   1.00 18.52 ?  132 PHE   B HA   1 
ATOM   5918 H HB2  . PHE   B 1 132 ? 42.810 -28.866 4.678   1.00 17.38 ?  132 PHE   B HB2  1 
ATOM   5919 H HB3  . PHE   B 1 132 ? 41.917 -28.517 5.942   1.00 17.38 ?  132 PHE   B HB3  1 
ATOM   5920 H HD1  . PHE   B 1 132 ? 45.285 -27.826 4.906   1.00 18.78 ?  132 PHE   B HD1  1 
ATOM   5921 H HD2  . PHE   B 1 132 ? 41.979 -26.299 6.567   1.00 17.28 ?  132 PHE   B HD2  1 
ATOM   5922 H HE1  . PHE   B 1 132 ? 46.316 -25.757 5.062   1.00 19.48 ?  132 PHE   B HE1  1 
ATOM   5923 H HE2  . PHE   B 1 132 ? 43.000 -24.230 6.726   1.00 17.85 ?  132 PHE   B HE2  1 
ATOM   5924 H HZ   . PHE   B 1 132 ? 45.171 -23.953 5.976   1.00 19.38 ?  132 PHE   B HZ   1 
ATOM   5925 N N    . GLY   B 1 133 ? 42.577 -32.049 6.122   1.00 16.47 ?  133 GLY   B N    1 
ATOM   5926 C CA   . GLY   B 1 133 ? 41.869 -33.220 6.608   1.00 17.06 ?  133 GLY   B CA   1 
ATOM   5927 C C    . GLY   B 1 133 ? 40.472 -33.479 6.074   1.00 17.12 ?  133 GLY   B C    1 
ATOM   5928 O O    . GLY   B 1 133 ? 39.884 -34.501 6.439   1.00 19.17 ?  133 GLY   B O    1 
ATOM   5929 H H    . GLY   B 1 133 ? 43.066 -32.194 5.429   1.00 19.76 ?  133 GLY   B H    1 
ATOM   5930 H HA2  . GLY   B 1 133 ? 42.402 -33.999 6.401   1.00 20.47 ?  133 GLY   B HA2  1 
ATOM   5931 H HA3  . GLY   B 1 133 ? 41.806 -33.152 7.573   1.00 20.47 ?  133 GLY   B HA3  1 
ATOM   5932 N N    . ALA   B 1 134 ? 39.910 -32.609 5.241   1.00 16.42 ?  134 ALA   B N    1 
ATOM   5933 C CA   . ALA   B 1 134 ? 38.584 -32.886 4.704   1.00 16.61 ?  134 ALA   B CA   1 
ATOM   5934 C C    . ALA   B 1 134 ? 38.668 -33.881 3.551   1.00 16.61 ?  134 ALA   B C    1 
ATOM   5935 O O    . ALA   B 1 134 ? 39.722 -34.075 2.938   1.00 17.89 ?  134 ALA   B O    1 
ATOM   5936 C CB   . ALA   B 1 134 ? 37.911 -31.599 4.228   1.00 17.27 ?  134 ALA   B CB   1 
ATOM   5937 H H    . ALA   B 1 134 ? 40.262 -31.863 4.979   1.00 19.70 ?  134 ALA   B H    1 
ATOM   5938 H HA   . ALA   B 1 134 ? 38.032 -33.268 5.404   1.00 19.94 ?  134 ALA   B HA   1 
ATOM   5939 H HB1  . ALA   B 1 134 ? 37.026 -31.813 3.889   1.00 20.72 ?  134 ALA   B HB1  1 
ATOM   5940 H HB2  . ALA   B 1 134 ? 37.837 -30.981 4.973   1.00 20.72 ?  134 ALA   B HB2  1 
ATOM   5941 H HB3  . ALA   B 1 134 ? 38.446 -31.203 3.522   1.00 20.72 ?  134 ALA   B HB3  1 
ATOM   5942 N N    . ASP   B 1 135 ? 37.532 -34.504 3.258   1.00 16.86 ?  135 ASP   B N    1 
ATOM   5943 C CA   . ASP   B 1 135 ? 37.430 -35.400 2.115   1.00 17.53 ?  135 ASP   B CA   1 
ATOM   5944 C C    . ASP   B 1 135 ? 37.536 -34.567 0.844   1.00 16.45 ?  135 ASP   B C    1 
ATOM   5945 O O    . ASP   B 1 135 ? 36.687 -33.693 0.618   1.00 16.33 ?  135 ASP   B O    1 
ATOM   5946 C CB   . ASP   B 1 135 ? 36.081 -36.117 2.166   1.00 19.18 ?  135 ASP   B CB   1 
ATOM   5947 C CG   . ASP   B 1 135 ? 35.896 -37.114 1.036   1.00 20.83 ?  135 ASP   B CG   1 
ATOM   5948 O OD1  . ASP   B 1 135 ? 36.763 -37.178 0.138   1.00 20.89 ?  135 ASP   B OD1  1 
ATOM   5949 O OD2  . ASP   B 1 135 ? 34.892 -37.865 1.068   1.00 23.99 -1 135 ASP   B OD2  1 
ATOM   5950 H H    . ASP   B 1 135 ? 36.803 -34.420 3.709   1.00 20.23 ?  135 ASP   B H    1 
ATOM   5951 H HA   . ASP   B 1 135 ? 38.143 -36.056 2.150   1.00 21.03 ?  135 ASP   B HA   1 
ATOM   5952 H HB2  . ASP   B 1 135 ? 36.019 -36.602 3.000   1.00 23.02 ?  135 ASP   B HB2  1 
ATOM   5953 H HB3  . ASP   B 1 135 ? 35.377 -35.454 2.109   1.00 23.02 ?  135 ASP   B HB3  1 
ATOM   5954 N N    . PRO   B 1 136 ? 38.550 -34.775 0.002   1.00 16.69 ?  136 PRO   B N    1 
ATOM   5955 C CA   . PRO   B 1 136 ? 38.652 -33.954 -1.215  1.00 16.08 ?  136 PRO   B CA   1 
ATOM   5956 C C    . PRO   B 1 136 ? 37.465 -34.102 -2.145  1.00 15.43 ?  136 PRO   B C    1 
ATOM   5957 O O    . PRO   B 1 136 ? 37.145 -33.152 -2.867  1.00 14.83 ?  136 PRO   B O    1 
ATOM   5958 C CB   . PRO   B 1 136 ? 39.961 -34.434 -1.858  1.00 16.95 ?  136 PRO   B CB   1 
ATOM   5959 C CG   . PRO   B 1 136 ? 40.169 -35.815 -1.308  1.00 18.10 ?  136 PRO   B CG   1 
ATOM   5960 C CD   . PRO   B 1 136 ? 39.625 -35.777 0.088   1.00 17.83 ?  136 PRO   B CD   1 
ATOM   5961 H HA   . PRO   B 1 136 ? 38.746 -33.017 -0.983  1.00 19.29 ?  136 PRO   B HA   1 
ATOM   5962 H HB2  . PRO   B 1 136 ? 39.863 -34.464 -2.825  1.00 20.34 ?  136 PRO   B HB2  1 
ATOM   5963 H HB3  . PRO   B 1 136 ? 40.688 -33.848 -1.604  1.00 20.34 ?  136 PRO   B HB3  1 
ATOM   5964 H HG2  . PRO   B 1 136 ? 39.685 -36.464 -1.843  1.00 21.72 ?  136 PRO   B HG2  1 
ATOM   5965 H HG3  . PRO   B 1 136 ? 41.118 -36.026 -1.294  1.00 21.72 ?  136 PRO   B HG3  1 
ATOM   5966 H HD2  . PRO   B 1 136 ? 39.257 -36.640 0.337   1.00 21.40 ?  136 PRO   B HD2  1 
ATOM   5967 H HD3  . PRO   B 1 136 ? 40.305 -35.487 0.718   1.00 21.40 ?  136 PRO   B HD3  1 
ATOM   5968 N N    . ILE   B 1 137 ? 36.808 -35.268 -2.158  1.00 15.66 ?  137 ILE   B N    1 
ATOM   5969 C CA   . ILE   B 1 137 ? 35.591 -35.434 -2.951  1.00 16.20 ?  137 ILE   B CA   1 
ATOM   5970 C C    . ILE   B 1 137 ? 34.515 -34.466 -2.473  1.00 15.87 ?  137 ILE   B C    1 
ATOM   5971 O O    . ILE   B 1 137 ? 33.795 -33.858 -3.275  1.00 15.32 ?  137 ILE   B O    1 
ATOM   5972 C CB   . ILE   B 1 137 ? 35.120 -36.904 -2.896  1.00 18.26 ?  137 ILE   B CB   1 
ATOM   5973 C CG1  . ILE   B 1 137 ? 36.104 -37.808 -3.645  1.00 20.62 ?  137 ILE   B CG1  1 
ATOM   5974 C CG2  . ILE   B 1 137 ? 33.707 -37.044 -3.468  1.00 18.94 ?  137 ILE   B CG2  1 
ATOM   5975 C CD1  . ILE   B 1 137 ? 35.792 -39.292 -3.530  1.00 23.00 ?  137 ILE   B CD1  1 
ATOM   5976 H H    . ILE   B 1 137 ? 37.040 -35.973 -1.722  1.00 18.79 ?  137 ILE   B H    1 
ATOM   5977 H HA   . ILE   B 1 137 ? 35.785 -35.224 -3.879  1.00 19.44 ?  137 ILE   B HA   1 
ATOM   5978 H HB   . ILE   B 1 137 ? 35.094 -37.180 -1.972  1.00 21.92 ?  137 ILE   B HB   1 
ATOM   5979 H HG12 . ILE   B 1 137 ? 36.089 -37.581 -4.588  1.00 24.75 ?  137 ILE   B HG12 1 
ATOM   5980 H HG13 . ILE   B 1 137 ? 36.991 -37.668 -3.286  1.00 24.75 ?  137 ILE   B HG13 1 
ATOM   5981 H HG21 . ILE   B 1 137 ? 33.462 -37.982 -3.507  1.00 22.73 ?  137 ILE   B HG21 1 
ATOM   5982 H HG22 . ILE   B 1 137 ? 33.079 -36.579 -2.894  1.00 22.73 ?  137 ILE   B HG22 1 
ATOM   5983 H HG23 . ILE   B 1 137 ? 33.685 -36.664 -4.360  1.00 22.73 ?  137 ILE   B HG23 1 
ATOM   5984 H HD11 . ILE   B 1 137 ? 36.441 -39.778 -4.057  1.00 27.59 ?  137 ILE   B HD11 1 
ATOM   5985 H HD12 . ILE   B 1 137 ? 35.850 -39.559 -2.598  1.00 27.59 ?  137 ILE   B HD12 1 
ATOM   5986 H HD13 . ILE   B 1 137 ? 34.902 -39.470 -3.871  1.00 27.59 ?  137 ILE   B HD13 1 
ATOM   5987 N N    . HIS   B 1 138 ? 34.387 -34.317 -1.157  1.00 15.76 ?  138 HIS   B N    1 
ATOM   5988 C CA   . HIS   B 1 138 ? 33.435 -33.356 -0.619  1.00 16.08 ?  138 HIS   B CA   1 
ATOM   5989 C C    . HIS   B 1 138 ? 33.853 -31.925 -0.930  1.00 15.44 ?  138 HIS   B C    1 
ATOM   5990 O O    . HIS   B 1 138 ? 33.003 -31.083 -1.234  1.00 15.90 ?  138 HIS   B O    1 
ATOM   5991 C CB   . HIS   B 1 138 ? 33.295 -33.542 0.885   1.00 17.39 ?  138 HIS   B CB   1 
ATOM   5992 C CG   . HIS   B 1 138 ? 32.359 -32.561 1.512   1.00 18.39 ?  138 HIS   B CG   1 
ATOM   5993 N ND1  . HIS   B 1 138 ? 31.021 -32.498 1.185   1.00 19.51 ?  138 HIS   B ND1  1 
ATOM   5994 C CD2  . HIS   B 1 138 ? 32.570 -31.581 2.422   1.00 18.86 ?  138 HIS   B CD2  1 
ATOM   5995 C CE1  . HIS   B 1 138 ? 30.445 -31.534 1.879   1.00 19.59 ?  138 HIS   B CE1  1 
ATOM   5996 N NE2  . HIS   B 1 138 ? 31.363 -30.963 2.639   1.00 19.06 ?  138 HIS   B NE2  1 
ATOM   5997 H H    . HIS   B 1 138 ? 34.837 -34.750 -0.569  1.00 18.91 ?  138 HIS   B H    1 
ATOM   5998 H HA   . HIS   B 1 138 ? 32.567 -33.515 -1.024  1.00 19.30 ?  138 HIS   B HA   1 
ATOM   5999 H HB2  . HIS   B 1 138 ? 32.951 -34.432 1.062   1.00 20.86 ?  138 HIS   B HB2  1 
ATOM   6000 H HB3  . HIS   B 1 138 ? 34.162 -33.432 1.298   1.00 20.86 ?  138 HIS   B HB3  1 
ATOM   6001 H HD1  . HIS   B 1 138 ? 30.622 -33.014 0.621   1.00 23.41 ?  138 HIS   B HD1  1 
ATOM   6002 H HD2  . HIS   B 1 138 ? 33.372 -31.371 2.836   1.00 22.63 ?  138 HIS   B HD2  1 
ATOM   6003 H HE1  . HIS   B 1 138 ? 29.542 -31.303 1.841   1.00 23.50 ?  138 HIS   B HE1  1 
ATOM   6004 N N    . SER   B 1 139 ? 35.147 -31.620 -0.850  1.00 14.84 ?  139 SER   B N    1 
ATOM   6005 C CA   . SER   B 1 139 ? 35.583 -30.268 -1.169  1.00 13.97 ?  139 SER   B CA   1 
ATOM   6006 C C    . SER   B 1 139 ? 35.246 -29.917 -2.609  1.00 13.16 ?  139 SER   B C    1 
ATOM   6007 O O    . SER   B 1 139 ? 34.799 -28.801 -2.891  1.00 13.63 ?  139 SER   B O    1 
ATOM   6008 C CB   . SER   B 1 139 ? 37.078 -30.131 -0.903  1.00 14.44 ?  139 SER   B CB   1 
ATOM   6009 O OG   . SER   B 1 139 ? 37.492 -28.798 -1.152  1.00 14.76 ?  139 SER   B OG   1 
ATOM   6010 H H    . SER   B 1 139 ? 35.766 -32.165 -0.627  1.00 17.81 ?  139 SER   B H    1 
ATOM   6011 H HA   . SER   B 1 139 ? 35.113 -29.645 -0.597  1.00 16.76 ?  139 SER   B HA   1 
ATOM   6012 H HB2  . SER   B 1 139 ? 37.257 -30.350 0.025   1.00 17.33 ?  139 SER   B HB2  1 
ATOM   6013 H HB3  . SER   B 1 139 ? 37.565 -30.731 -1.488  1.00 17.33 ?  139 SER   B HB3  1 
ATOM   6014 H HG   . SER   B 1 139 ? 38.322 -28.724 -1.004  1.00 17.72 ?  139 SER   B HG   1 
ATOM   6015 N N    . LEU   B 1 140 ? 35.437 -30.862 -3.533  1.00 13.17 ?  140 LEU   B N    1 
ATOM   6016 C CA   . LEU   B 1 140 ? 35.078 -30.615 -4.923  1.00 13.10 ?  140 LEU   B CA   1 
ATOM   6017 C C    . LEU   B 1 140 ? 33.575 -30.388 -5.063  1.00 13.52 ?  140 LEU   B C    1 
ATOM   6018 O O    . LEU   B 1 140 ? 33.140 -29.498 -5.800  1.00 13.85 ?  140 LEU   B O    1 
ATOM   6019 C CB   . LEU   B 1 140 ? 35.554 -31.772 -5.802  1.00 13.42 ?  140 LEU   B CB   1 
ATOM   6020 C CG   . LEU   B 1 140 ? 35.189 -31.667 -7.277  1.00 13.74 ?  140 LEU   B CG   1 
ATOM   6021 C CD1  . LEU   B 1 140 ? 35.761 -30.394 -7.893  1.00 14.66 ?  140 LEU   B CD1  1 
ATOM   6022 C CD2  . LEU   B 1 140 ? 35.661 -32.895 -8.021  1.00 14.83 ?  140 LEU   B CD2  1 
ATOM   6023 H H    . LEU   B 1 140 ? 35.771 -31.639 -3.383  1.00 15.81 ?  140 LEU   B H    1 
ATOM   6024 H HA   . LEU   B 1 140 ? 35.532 -29.810 -5.225  1.00 15.72 ?  140 LEU   B HA   1 
ATOM   6025 H HB2  . LEU   B 1 140 ? 36.523 -31.825 -5.747  1.00 16.10 ?  140 LEU   B HB2  1 
ATOM   6026 H HB3  . LEU   B 1 140 ? 35.166 -32.595 -5.466  1.00 16.10 ?  140 LEU   B HB3  1 
ATOM   6027 H HG   . LEU   B 1 140 ? 34.222 -31.621 -7.357  1.00 16.48 ?  140 LEU   B HG   1 
ATOM   6028 H HD11 . LEU   B 1 140 ? 35.611 -30.415 -8.852  1.00 17.59 ?  140 LEU   B HD11 1 
ATOM   6029 H HD12 . LEU   B 1 140 ? 35.309 -29.623 -7.509  1.00 17.59 ?  140 LEU   B HD12 1 
ATOM   6030 H HD13 . LEU   B 1 140 ? 36.709 -30.349 -7.705  1.00 17.59 ?  140 LEU   B HD13 1 
ATOM   6031 H HD21 . LEU   B 1 140 ? 35.410 -32.805 -8.956  1.00 17.79 ?  140 LEU   B HD21 1 
ATOM   6032 H HD22 . LEU   B 1 140 ? 36.616 -32.968 -7.935  1.00 17.79 ?  140 LEU   B HD22 1 
ATOM   6033 H HD23 . LEU   B 1 140 ? 35.224 -33.673 -7.639  1.00 17.79 ?  140 LEU   B HD23 1 
ATOM   6034 N N    . ARG   B 1 141 ? 32.771 -31.179 -4.348  1.00 13.76 ?  141 ARG   B N    1 
ATOM   6035 C CA   . ARG   B 1 141 ? 31.321 -31.001 -4.335  1.00 14.88 ?  141 ARG   B CA   1 
ATOM   6036 C C    . ARG   B 1 141 ? 30.939 -29.591 -3.899  1.00 14.41 ?  141 ARG   B C    1 
ATOM   6037 O O    . ARG   B 1 141 ? 30.140 -28.911 -4.558  1.00 14.78 ?  141 ARG   B O    1 
ATOM   6038 C CB   . ARG   B 1 141 ? 30.729 -32.037 -3.370  1.00 16.47 ?  141 ARG   B CB   1 
ATOM   6039 C CG   . ARG   B 1 141 ? 29.269 -31.912 -3.027  1.00 18.83 ?  141 ARG   B CG   1 
ATOM   6040 C CD   . ARG   B 1 141 ? 28.453 -32.548 -4.079  1.00 20.68 ?  141 ARG   B CD   1 
ATOM   6041 N NE   . ARG   B 1 141 ? 28.195 -31.639 -5.184  1.00 21.28 ?  141 ARG   B NE   1 
ATOM   6042 C CZ   . ARG   B 1 141 ? 28.193 -31.989 -6.463  1.00 20.90 ?  141 ARG   B CZ   1 
ATOM   6043 N NH1  . ARG   B 1 141 ? 28.639 -33.171 -6.859  1.00 20.79 ?  141 ARG   B NH1  1 
ATOM   6044 N NH2  . ARG   B 1 141 ? 27.727 -31.129 -7.366  1.00 21.51 ?  141 ARG   B NH2  1 
ATOM   6045 H H    . ARG   B 1 141 ? 33.049 -31.826 -3.857  1.00 16.52 ?  141 ARG   B H    1 
ATOM   6046 H HA   . ARG   B 1 141 ? 30.964 -31.160 -5.220  1.00 17.86 ?  141 ARG   B HA   1 
ATOM   6047 H HB2  . ARG   B 1 141 ? 30.871 -32.919 -3.755  1.00 19.76 ?  141 ARG   B HB2  1 
ATOM   6048 H HB3  . ARG   B 1 141 ? 31.223 -31.984 -2.537  1.00 19.76 ?  141 ARG   B HB3  1 
ATOM   6049 H HG2  . ARG   B 1 141 ? 29.103 -32.355 -2.185  1.00 22.59 ?  141 ARG   B HG2  1 
ATOM   6050 H HG3  . ARG   B 1 141 ? 29.021 -30.972 -2.966  1.00 22.59 ?  141 ARG   B HG3  1 
ATOM   6051 H HD2  . ARG   B 1 141 ? 28.919 -33.334 -4.416  1.00 24.82 ?  141 ARG   B HD2  1 
ATOM   6052 H HD3  . ARG   B 1 141 ? 27.608 -32.819 -3.695  1.00 24.82 ?  141 ARG   B HD3  1 
ATOM   6053 H HE   . ARG   B 1 141 ? 27.990 -30.828 -4.991  1.00 25.54 ?  141 ARG   B HE   1 
ATOM   6054 H HH11 . ARG   B 1 141 ? 28.929 -33.743 -6.287  1.00 24.95 ?  141 ARG   B HH11 1 
ATOM   6055 H HH12 . ARG   B 1 141 ? 28.637 -33.369 -7.694  1.00 24.95 ?  141 ARG   B HH12 1 
ATOM   6056 H HH21 . ARG   B 1 141 ? 27.437 -30.357 -7.120  1.00 25.81 ?  141 ARG   B HH21 1 
ATOM   6057 H HH22 . ARG   B 1 141 ? 27.739 -31.334 -8.203  1.00 25.81 ?  141 ARG   B HH22 1 
ATOM   6058 N N    . VAL   B 1 142 ? 31.488 -29.144 -2.772  1.00 13.95 ?  142 VAL   B N    1 
ATOM   6059 C CA   . VAL   B 1 142 ? 31.153 -27.812 -2.286  1.00 13.92 ?  142 VAL   B CA   1 
ATOM   6060 C C    . VAL   B 1 142 ? 31.629 -26.753 -3.274  1.00 13.79 ?  142 VAL   B C    1 
ATOM   6061 O O    . VAL   B 1 142 ? 30.929 -25.766 -3.531  1.00 14.36 ?  142 VAL   B O    1 
ATOM   6062 C CB   . VAL   B 1 142 ? 31.700 -27.586 -0.864  1.00 14.47 ?  142 VAL   B CB   1 
ATOM   6063 C CG1  . VAL   B 1 142 ? 31.375 -26.166 -0.383  1.00 14.25 ?  142 VAL   B CG1  1 
ATOM   6064 C CG2  . VAL   B 1 142 ? 31.129 -28.618 0.101   1.00 15.26 ?  142 VAL   B CG2  1 
ATOM   6065 H H    . VAL   B 1 142 ? 32.051 -29.578 -2.285  1.00 16.75 ?  142 VAL   B H    1 
ATOM   6066 H HA   . VAL   B 1 142 ? 30.192 -27.742 -2.234  1.00 16.70 ?  142 VAL   B HA   1 
ATOM   6067 H HB   . VAL   B 1 142 ? 32.666 -27.686 -0.872  1.00 17.37 ?  142 VAL   B HB   1 
ATOM   6068 H HG11 . VAL   B 1 142 ? 31.562 -26.104 0.566   1.00 17.10 ?  142 VAL   B HG11 1 
ATOM   6069 H HG12 . VAL   B 1 142 ? 31.929 -25.532 -0.869  1.00 17.10 ?  142 VAL   B HG12 1 
ATOM   6070 H HG13 . VAL   B 1 142 ? 30.439 -25.983 -0.549  1.00 17.10 ?  142 VAL   B HG13 1 
ATOM   6071 H HG21 . VAL   B 1 142 ? 31.457 -28.432 0.994   1.00 18.31 ?  142 VAL   B HG21 1 
ATOM   6072 H HG22 . VAL   B 1 142 ? 30.161 -28.561 0.084   1.00 18.31 ?  142 VAL   B HG22 1 
ATOM   6073 H HG23 . VAL   B 1 142 ? 31.413 -29.502 -0.179  1.00 18.31 ?  142 VAL   B HG23 1 
ATOM   6074 N N    . CYS   B 1 143 ? 32.814 -26.948 -3.858  1.00 13.37 ?  143 CYS   B N    1 
ATOM   6075 C CA   . CYS   B 1 143 ? 33.305 -26.007 -4.859  1.00 13.35 ?  143 CYS   B CA   1 
ATOM   6076 C C    . CYS   B 1 143 ? 32.302 -25.860 -5.997  1.00 13.19 ?  143 CYS   B C    1 
ATOM   6077 O O    . CYS   B 1 143 ? 31.904 -24.748 -6.355  1.00 13.33 ?  143 CYS   B O    1 
ATOM   6078 C CB   . CYS   B 1 143 ? 34.656 -26.495 -5.392  1.00 13.77 ?  143 CYS   B CB   1 
ATOM   6079 S SG   . CYS   B 1 143 ? 35.414 -25.385 -6.602  1.00 13.73 ?  143 CYS   B SG   1 
ATOM   6080 H H    . CYS   B 1 143 ? 33.345 -27.604 -3.695  1.00 16.04 ?  143 CYS   B H    1 
ATOM   6081 H HA   . CYS   B 1 143 ? 33.435 -25.137 -4.455  1.00 16.02 ?  143 CYS   B HA   1 
ATOM   6082 H HB2  . CYS   B 1 143 ? 35.278 -26.581 -4.653  1.00 16.52 ?  143 CYS   B HB2  1 
ATOM   6083 H HB3  . CYS   B 1 143 ? 34.536 -27.351 -5.819  1.00 16.52 ?  143 CYS   B HB3  1 
ATOM   6084 H HG   . CYS   B 1 143 ? 36.478 -25.829 -6.930  1.00 16.48 ?  143 CYS   B HG   1 
ATOM   6085 N N    . VAL   B 1 144 ? 31.894 -26.981 -6.590  1.00 13.61 ?  144 VAL   B N    1 
ATOM   6086 C CA   . VAL   B 1 144 ? 30.991 -26.915 -7.734  1.00 14.63 ?  144 VAL   B CA   1 
ATOM   6087 C C    . VAL   B 1 144 ? 29.649 -26.305 -7.359  1.00 14.71 ?  144 VAL   B C    1 
ATOM   6088 O O    . VAL   B 1 144 ? 29.033 -25.598 -8.167  1.00 16.15 ?  144 VAL   B O    1 
ATOM   6089 C CB   . VAL   B 1 144 ? 30.835 -28.316 -8.331  1.00 17.21 ?  144 VAL   B CB   1 
ATOM   6090 C CG1  . VAL   B 1 144 ? 29.568 -28.426 -9.177  1.00 19.70 ?  144 VAL   B CG1  1 
ATOM   6091 C CG2  . VAL   B 1 144 ? 32.085 -28.702 -9.120  1.00 17.45 ?  144 VAL   B CG2  1 
ATOM   6092 H H    . VAL   B 1 144 ? 32.121 -27.776 -6.353  1.00 16.33 ?  144 VAL   B H    1 
ATOM   6093 H HA   . VAL   B 1 144 ? 31.386 -26.352 -8.413  1.00 17.55 ?  144 VAL   B HA   1 
ATOM   6094 H HB   . VAL   B 1 144 ? 30.752 -28.957 -7.606  1.00 20.65 ?  144 VAL   B HB   1 
ATOM   6095 H HG11 . VAL   B 1 144 ? 29.647 -29.203 -9.758  1.00 23.64 ?  144 VAL   B HG11 1 
ATOM   6096 H HG12 . VAL   B 1 144 ? 28.806 -28.537 -8.589  1.00 23.64 ?  144 VAL   B HG12 1 
ATOM   6097 H HG13 . VAL   B 1 144 ? 29.473 -27.626 -9.711  1.00 23.64 ?  144 VAL   B HG13 1 
ATOM   6098 H HG21 . VAL   B 1 144 ? 31.969 -29.593 -9.483  1.00 20.94 ?  144 VAL   B HG21 1 
ATOM   6099 H HG22 . VAL   B 1 144 ? 32.206 -28.063 -9.842  1.00 20.94 ?  144 VAL   B HG22 1 
ATOM   6100 H HG23 . VAL   B 1 144 ? 32.849 -28.679 -8.527  1.00 20.94 ?  144 VAL   B HG23 1 
ATOM   6101 N N    . ASP   B 1 145 ? 29.179 -26.555 -6.141  1.00 14.83 ?  145 ASP   B N    1 
ATOM   6102 C CA   . ASP   B 1 145 ? 27.870 -26.086 -5.717  1.00 15.42 ?  145 ASP   B CA   1 
ATOM   6103 C C    . ASP   B 1 145 ? 27.901 -24.667 -5.167  1.00 15.06 ?  145 ASP   B C    1 
ATOM   6104 O O    . ASP   B 1 145 ? 26.839 -24.125 -4.835  1.00 16.88 ?  145 ASP   B O    1 
ATOM   6105 C CB   . ASP   B 1 145 ? 27.271 -27.006 -4.643  1.00 17.19 ?  145 ASP   B CB   1 
ATOM   6106 C CG   . ASP   B 1 145 ? 26.923 -28.385 -5.157  1.00 18.77 ?  145 ASP   B CG   1 
ATOM   6107 O OD1  . ASP   B 1 145 ? 26.826 -28.569 -6.385  1.00 19.10 ?  145 ASP   B OD1  1 
ATOM   6108 O OD2  . ASP   B 1 145 ? 26.735 -29.277 -4.308  1.00 21.08 -1 145 ASP   B OD2  1 
ATOM   6109 H H    . ASP   B 1 145 ? 29.609 -26.992 -5.536  1.00 17.80 ?  145 ASP   B H    1 
ATOM   6110 H HA   . ASP   B 1 145 ? 27.281 -26.070 -6.485  1.00 18.50 ?  145 ASP   B HA   1 
ATOM   6111 H HB2  . ASP   B 1 145 ? 27.906 -27.109 -3.931  1.00 20.63 ?  145 ASP   B HB2  1 
ATOM   6112 H HB3  . ASP   B 1 145 ? 26.453 -26.593 -4.312  1.00 20.63 ?  145 ASP   B HB3  1 
ATOM   6113 N N    . THR   B 1 146 ? 29.079 -24.051 -5.054  1.00 13.59 ?  146 THR   B N    1 
ATOM   6114 C CA   . THR   B 1 146 ? 29.212 -22.730 -4.444  1.00 13.35 ?  146 THR   B CA   1 
ATOM   6115 C C    . THR   B 1 146 ? 29.843 -21.695 -5.361  1.00 13.09 ?  146 THR   B C    1 
ATOM   6116 O O    . THR   B 1 146 ? 29.389 -20.535 -5.404  1.00 13.41 ?  146 THR   B O    1 
ATOM   6117 C CB   . THR   B 1 146 ? 30.039 -22.834 -3.155  1.00 13.56 ?  146 THR   B CB   1 
ATOM   6118 O OG1  . THR   B 1 146 ? 29.467 -23.833 -2.298  1.00 13.56 ?  146 THR   B OG1  1 
ATOM   6119 C CG2  . THR   B 1 146 ? 30.112 -21.495 -2.430  1.00 13.75 ?  146 THR   B CG2  1 
ATOM   6120 H H    . THR   B 1 146 ? 29.830 -24.380 -5.325  1.00 16.31 ?  146 THR   B H    1 
ATOM   6121 H HA   . THR   B 1 146 ? 28.338 -22.405 -4.202  1.00 16.02 ?  146 THR   B HA   1 
ATOM   6122 H HB   . THR   B 1 146 ? 30.949 -23.096 -3.379  1.00 16.27 ?  146 THR   B HB   1 
ATOM   6123 H HG1  . THR   B 1 146 ? 29.504 -24.589 -2.678  1.00 16.28 ?  146 THR   B HG1  1 
ATOM   6124 H HG21 . THR   B 1 146 ? 30.467 -21.617 -1.537  1.00 16.50 ?  146 THR   B HG21 1 
ATOM   6125 H HG22 . THR   B 1 146 ? 30.693 -20.884 -2.916  1.00 16.50 ?  146 THR   B HG22 1 
ATOM   6126 H HG23 . THR   B 1 146 ? 29.228 -21.104 -2.368  1.00 16.50 ?  146 THR   B HG23 1 
ATOM   6127 N N    . VAL   B 1 147 ? 30.915 -22.062 -6.055  1.00 12.93 ?  147 VAL   B N    1 
ATOM   6128 C CA   . VAL   B 1 147 ? 31.641 -21.119 -6.891  1.00 12.78 ?  147 VAL   B CA   1 
ATOM   6129 C C    . VAL   B 1 147 ? 30.907 -20.986 -8.211  1.00 12.94 ?  147 VAL   B C    1 
ATOM   6130 O O    . VAL   B 1 147 ? 30.543 -21.988 -8.841  1.00 13.68 ?  147 VAL   B O    1 
ATOM   6131 C CB   . VAL   B 1 147 ? 33.094 -21.580 -7.098  1.00 12.92 ?  147 VAL   B CB   1 
ATOM   6132 C CG1  . VAL   B 1 147 ? 33.855 -20.559 -7.925  1.00 13.09 ?  147 VAL   B CG1  1 
ATOM   6133 C CG2  . VAL   B 1 147 ? 33.769 -21.787 -5.755  1.00 12.94 ?  147 VAL   B CG2  1 
ATOM   6134 H H    . VAL   B 1 147 ? 31.248 -22.860 -6.062  1.00 15.51 ?  147 VAL   B H    1 
ATOM   6135 H HA   . VAL   B 1 147 ? 31.660 -20.252 -6.462  1.00 15.34 ?  147 VAL   B HA   1 
ATOM   6136 H HB   . VAL   B 1 147 ? 33.102 -22.429 -7.575  1.00 15.50 ?  147 VAL   B HB   1 
ATOM   6137 H HG11 . VAL   B 1 147 ? 34.801 -20.782 -7.913  1.00 15.71 ?  147 VAL   B HG11 1 
ATOM   6138 H HG12 . VAL   B 1 147 ? 33.526 -20.578 -8.838  1.00 15.71 ?  147 VAL   B HG12 1 
ATOM   6139 H HG13 . VAL   B 1 147 ? 33.721 -19.679 -7.541  1.00 15.71 ?  147 VAL   B HG13 1 
ATOM   6140 H HG21 . VAL   B 1 147 ? 34.711 -21.979 -5.899  1.00 15.53 ?  147 VAL   B HG21 1 
ATOM   6141 H HG22 . VAL   B 1 147 ? 33.675 -20.979 -5.227  1.00 15.53 ?  147 VAL   B HG22 1 
ATOM   6142 H HG23 . VAL   B 1 147 ? 33.349 -22.532 -5.297  1.00 15.53 ?  147 VAL   B HG23 1 
ATOM   6143 N N    . ARG   B 1 148 ? 30.695 -19.738 -8.627  1.00 13.09 ?  148 ARG   B N    1 
ATOM   6144 C CA   . ARG   B 1 148 ? 30.072 -19.416 -9.899  1.00 13.36 ?  148 ARG   B CA   1 
ATOM   6145 C C    . ARG   B 1 148 ? 31.029 -18.747 -10.872 1.00 13.41 ?  148 ARG   B C    1 
ATOM   6146 O O    . ARG   B 1 148 ? 30.745 -18.725 -12.072 1.00 14.71 ?  148 ARG   B O    1 
ATOM   6147 C CB   . ARG   B 1 148 ? 28.840 -18.525 -9.675  1.00 13.81 ?  148 ARG   B CB   1 
ATOM   6148 C CG   . ARG   B 1 148 ? 27.761 -19.222 -8.857  1.00 14.76 ?  148 ARG   B CG   1 
ATOM   6149 C CD   . ARG   B 1 148 ? 26.557 -18.330 -8.557  1.00 15.48 ?  148 ARG   B CD   1 
ATOM   6150 N NE   . ARG   B 1 148 ? 26.943 -17.134 -7.821  1.00 15.15 ?  148 ARG   B NE   1 
ATOM   6151 C CZ   . ARG   B 1 148 ? 27.241 -17.106 -6.529  1.00 14.17 ?  148 ARG   B CZ   1 
ATOM   6152 N NH1  . ARG   B 1 148 ? 27.166 -18.193 -5.775  1.00 14.08 ?  148 ARG   B NH1  1 
ATOM   6153 N NH2  . ARG   B 1 148 ? 27.631 -15.958 -5.980  1.00 14.27 ?  148 ARG   B NH2  1 
ATOM   6154 H H    . ARG   B 1 148 ? 30.919 -19.039 -8.169  1.00 15.70 ?  148 ARG   B H    1 
ATOM   6155 H HA   . ARG   B 1 148 ? 29.768 -20.238 -10.307 1.00 16.03 ?  148 ARG   B HA   1 
ATOM   6156 H HB2  . ARG   B 1 148 ? 29.111 -17.724 -9.195  1.00 16.57 ?  148 ARG   B HB2  1 
ATOM   6157 H HB3  . ARG   B 1 148 ? 28.462 -18.286 -10.534 1.00 16.57 ?  148 ARG   B HB3  1 
ATOM   6158 H HG2  . ARG   B 1 148 ? 27.441 -19.994 -9.352  1.00 17.71 ?  148 ARG   B HG2  1 
ATOM   6159 H HG3  . ARG   B 1 148 ? 28.138 -19.508 -8.011  1.00 17.71 ?  148 ARG   B HG3  1 
ATOM   6160 H HD2  . ARG   B 1 148 ? 26.150 -18.054 -9.391  1.00 18.57 ?  148 ARG   B HD2  1 
ATOM   6161 H HD3  . ARG   B 1 148 ? 25.919 -18.827 -8.020  1.00 18.57 ?  148 ARG   B HD3  1 
ATOM   6162 H HE   . ARG   B 1 148 ? 26.989 -16.397 -8.254  1.00 18.18 ?  148 ARG   B HE   1 
ATOM   6163 H HH11 . ARG   B 1 148 ? 26.906 -18.942 -6.112  1.00 16.90 ?  148 ARG   B HH11 1 
ATOM   6164 H HH12 . ARG   B 1 148 ? 27.352 -18.151 -4.933  1.00 16.90 ?  148 ARG   B HH12 1 
ATOM   6165 H HH21 . ARG   B 1 148 ? 27.687 -15.250 -6.461  1.00 17.13 ?  148 ARG   B HH21 1 
ATOM   6166 H HH22 . ARG   B 1 148 ? 27.824 -15.924 -5.142  1.00 17.13 ?  148 ARG   B HH22 1 
ATOM   6167 N N    . THR   B 1 149 ? 32.139 -18.196 -10.384 1.00 13.19 ?  149 THR   B N    1 
ATOM   6168 C CA   . THR   B 1 149 ? 33.182 -17.636 -11.229 1.00 13.33 ?  149 THR   B CA   1 
ATOM   6169 C C    . THR   B 1 149 ? 34.073 -18.772 -11.736 1.00 12.90 ?  149 THR   B C    1 
ATOM   6170 O O    . THR   B 1 149 ? 33.878 -19.941 -11.398 1.00 13.26 ?  149 THR   B O    1 
ATOM   6171 C CB   . THR   B 1 149 ? 33.953 -16.582 -10.444 1.00 13.31 ?  149 THR   B CB   1 
ATOM   6172 O OG1  . THR   B 1 149 ? 34.409 -17.180 -9.229  1.00 13.29 ?  149 THR   B OG1  1 
ATOM   6173 C CG2  . THR   B 1 149 ? 33.063 -15.377 -10.146 1.00 13.94 ?  149 THR   B CG2  1 
ATOM   6174 H H    . THR   B 1 149 ? 32.307 -18.130 -9.544  1.00 15.83 ?  149 THR   B H    1 
ATOM   6175 H HA   . THR   B 1 149 ? 32.777 -17.204 -11.995 1.00 15.99 ?  149 THR   B HA   1 
ATOM   6176 H HB   . THR   B 1 149 ? 34.715 -16.286 -10.959 1.00 15.98 ?  149 THR   B HB   1 
ATOM   6177 H HG1  . THR   B 1 149 ? 34.830 -16.609 -8.765  1.00 15.95 ?  149 THR   B HG1  1 
ATOM   6178 H HG21 . THR   B 1 149 ? 33.567 -14.706 -9.661  1.00 16.72 ?  149 THR   B HG21 1 
ATOM   6179 H HG22 . THR   B 1 149 ? 32.743 -14.991 -10.977 1.00 16.72 ?  149 THR   B HG22 1 
ATOM   6180 H HG23 . THR   B 1 149 ? 32.301 -15.649 -9.611  1.00 16.72 ?  149 THR   B HG23 1 
ATOM   6181 N N    . ASN   B 1 150 ? 35.039 -18.451 -12.586 1.00 12.83 ?  150 ASN   B N    1 
ATOM   6182 C CA   . ASN   B 1 150 ? 35.805 -19.478 -13.284 1.00 13.40 ?  150 ASN   B CA   1 
ATOM   6183 C C    . ASN   B 1 150 ? 36.969 -19.931 -12.413 1.00 13.10 ?  150 ASN   B C    1 
ATOM   6184 O O    . ASN   B 1 150 ? 37.899 -19.163 -12.157 1.00 13.84 ?  150 ASN   B O    1 
ATOM   6185 C CB   . ASN   B 1 150 ? 36.279 -18.944 -14.628 1.00 15.35 ?  150 ASN   B CB   1 
ATOM   6186 C CG   . ASN   B 1 150 ? 35.135 -18.725 -15.576 1.00 17.89 ?  150 ASN   B CG   1 
ATOM   6187 O OD1  . ASN   B 1 150 ? 34.244 -19.559 -15.674 1.00 19.05 ?  150 ASN   B OD1  1 
ATOM   6188 N ND2  . ASN   B 1 150 ? 35.128 -17.590 -16.255 1.00 19.28 ?  150 ASN   B ND2  1 
ATOM   6189 H H    . ASN   B 1 150 ? 35.281 -17.643 -12.768 1.00 15.40 ?  150 ASN   B H    1 
ATOM   6190 H HA   . ASN   B 1 150 ? 35.226 -20.243 -13.450 1.00 16.08 ?  150 ASN   B HA   1 
ATOM   6191 H HB2  . ASN   B 1 150 ? 36.725 -18.093 -14.493 1.00 18.42 ?  150 ASN   B HB2  1 
ATOM   6192 H HB3  . ASN   B 1 150 ? 36.885 -19.582 -15.030 1.00 18.42 ?  150 ASN   B HB3  1 
ATOM   6193 H HD21 . ASN   B 1 150 ? 34.492 -17.418 -16.814 1.00 23.14 ?  150 ASN   B HD21 1 
ATOM   6194 H HD22 . ASN   B 1 150 ? 35.767 -17.020 -16.155 1.00 23.14 ?  150 ASN   B HD22 1 
ATOM   6195 N N    . VAL   B 1 151 ? 36.924 -21.177 -11.959 1.00 12.76 ?  151 VAL   B N    1 
ATOM   6196 C CA   . VAL   B 1 151 ? 37.945 -21.705 -11.067 1.00 12.82 ?  151 VAL   B CA   1 
ATOM   6197 C C    . VAL   B 1 151 ? 38.653 -22.871 -11.744 1.00 12.62 ?  151 VAL   B C    1 
ATOM   6198 O O    . VAL   B 1 151 ? 38.012 -23.805 -12.248 1.00 13.54 ?  151 VAL   B O    1 
ATOM   6199 C CB   . VAL   B 1 151 ? 37.384 -22.042 -9.671  1.00 14.04 ?  151 VAL   B CB   1 
ATOM   6200 C CG1  . VAL   B 1 151 ? 36.236 -23.046 -9.752  1.00 15.01 ?  151 VAL   B CG1  1 
ATOM   6201 C CG2  . VAL   B 1 151 ? 38.493 -22.531 -8.747  1.00 14.55 ?  151 VAL   B CG2  1 
ATOM   6202 H H    . VAL   B 1 151 ? 36.302 -21.743 -12.155 1.00 15.31 ?  151 VAL   B H    1 
ATOM   6203 H HA   . VAL   B 1 151 ? 38.609 -21.011 -10.934 1.00 15.38 ?  151 VAL   B HA   1 
ATOM   6204 H HB   . VAL   B 1 151 ? 37.023 -21.228 -9.282  1.00 16.85 ?  151 VAL   B HB   1 
ATOM   6205 H HG11 . VAL   B 1 151 ? 35.910 -23.234 -8.856  1.00 18.01 ?  151 VAL   B HG11 1 
ATOM   6206 H HG12 . VAL   B 1 151 ? 35.519 -22.674 -10.290 1.00 18.01 ?  151 VAL   B HG12 1 
ATOM   6207 H HG13 . VAL   B 1 151 ? 36.559 -23.869 -10.160 1.00 18.01 ?  151 VAL   B HG13 1 
ATOM   6208 H HG21 . VAL   B 1 151 ? 38.138 -22.613 -7.847  1.00 17.46 ?  151 VAL   B HG21 1 
ATOM   6209 H HG22 . VAL   B 1 151 ? 38.809 -23.391 -9.058  1.00 17.46 ?  151 VAL   B HG22 1 
ATOM   6210 H HG23 . VAL   B 1 151 ? 39.217 -21.885 -8.756  1.00 17.46 ?  151 VAL   B HG23 1 
ATOM   6211 N N    . TYR   B 1 152 ? 39.982 -22.785 -11.767 1.00 12.11 ?  152 TYR   B N    1 
ATOM   6212 C CA   . TYR   B 1 152 ? 40.886 -23.768 -12.346 1.00 12.56 ?  152 TYR   B CA   1 
ATOM   6213 C C    . TYR   B 1 152 ? 41.604 -24.446 -11.184 1.00 11.87 ?  152 TYR   B C    1 
ATOM   6214 O O    . TYR   B 1 152 ? 42.454 -23.833 -10.531 1.00 12.11 ?  152 TYR   B O    1 
ATOM   6215 C CB   . TYR   B 1 152 ? 41.861 -23.059 -13.292 1.00 12.95 ?  152 TYR   B CB   1 
ATOM   6216 C CG   . TYR   B 1 152 ? 41.184 -22.599 -14.561 1.00 13.56 ?  152 TYR   B CG   1 
ATOM   6217 C CD1  . TYR   B 1 152 ? 40.514 -21.381 -14.627 1.00 13.96 ?  152 TYR   B CD1  1 
ATOM   6218 C CD2  . TYR   B 1 152 ? 41.193 -23.400 -15.689 1.00 14.57 ?  152 TYR   B CD2  1 
ATOM   6219 C CE1  . TYR   B 1 152 ? 39.875 -20.980 -15.790 1.00 15.15 ?  152 TYR   B CE1  1 
ATOM   6220 C CE2  . TYR   B 1 152 ? 40.560 -23.014 -16.850 1.00 15.61 ?  152 TYR   B CE2  1 
ATOM   6221 C CZ   . TYR   B 1 152 ? 39.904 -21.803 -16.901 1.00 15.82 ?  152 TYR   B CZ   1 
ATOM   6222 O OH   . TYR   B 1 152 ? 39.279 -21.434 -18.069 1.00 18.25 ?  152 TYR   B OH   1 
ATOM   6223 H H    . TYR   B 1 152 ? 40.413 -22.118 -11.422 1.00 14.53 ?  152 TYR   B H    1 
ATOM   6224 H HA   . TYR   B 1 152 ? 40.381 -24.434 -12.843 1.00 15.07 ?  152 TYR   B HA   1 
ATOM   6225 H HB2  . TYR   B 1 152 ? 42.225 -22.281 -12.840 1.00 15.54 ?  152 TYR   B HB2  1 
ATOM   6226 H HB3  . TYR   B 1 152 ? 42.575 -23.670 -13.529 1.00 15.54 ?  152 TYR   B HB3  1 
ATOM   6227 H HD1  . TYR   B 1 152 ? 40.486 -20.831 -13.876 1.00 16.76 ?  152 TYR   B HD1  1 
ATOM   6228 H HD2  . TYR   B 1 152 ? 41.632 -24.223 -15.661 1.00 17.48 ?  152 TYR   B HD2  1 
ATOM   6229 H HE1  . TYR   B 1 152 ? 39.431 -20.165 -15.825 1.00 18.18 ?  152 TYR   B HE1  1 
ATOM   6230 H HE2  . TYR   B 1 152 ? 40.585 -23.564 -17.599 1.00 18.73 ?  152 TYR   B HE2  1 
ATOM   6231 H HH   . TYR   B 1 152 ? 38.922 -20.681 -17.973 1.00 21.90 ?  152 TYR   B HH   1 
ATOM   6232 N N    . LEU   B 1 153 ? 41.236 -25.701 -10.913 1.00 12.07 ?  153 LEU   B N    1 
ATOM   6233 C CA   . LEU   B 1 153 ? 41.745 -26.449 -9.773  1.00 11.64 ?  153 LEU   B CA   1 
ATOM   6234 C C    . LEU   B 1 153 ? 42.980 -27.248 -10.165 1.00 12.00 ?  153 LEU   B C    1 
ATOM   6235 O O    . LEU   B 1 153 ? 42.965 -27.980 -11.158 1.00 13.13 ?  153 LEU   B O    1 
ATOM   6236 C CB   . LEU   B 1 153 ? 40.668 -27.405 -9.253  1.00 12.20 ?  153 LEU   B CB   1 
ATOM   6237 C CG   . LEU   B 1 153 ? 39.407 -26.751 -8.691  1.00 12.95 ?  153 LEU   B CG   1 
ATOM   6238 C CD1  . LEU   B 1 153 ? 38.317 -27.806 -8.544  1.00 13.52 ?  153 LEU   B CD1  1 
ATOM   6239 C CD2  . LEU   B 1 153 ? 39.694 -26.085 -7.352  1.00 13.29 ?  153 LEU   B CD2  1 
ATOM   6240 H H    . LEU   B 1 153 ? 40.669 -26.150 -11.390 1.00 14.48 ?  153 LEU   B H    1 
ATOM   6241 H HA   . LEU   B 1 153 ? 41.976 -25.829 -9.066  1.00 13.96 ?  153 LEU   B HA   1 
ATOM   6242 H HB2  . LEU   B 1 153 ? 40.393 -27.982 -9.980  1.00 14.64 ?  153 LEU   B HB2  1 
ATOM   6243 H HB3  . LEU   B 1 153 ? 41.053 -27.939 -8.541  1.00 14.64 ?  153 LEU   B HB3  1 
ATOM   6244 H HG   . LEU   B 1 153 ? 39.088 -26.067 -9.307  1.00 15.54 ?  153 LEU   B HG   1 
ATOM   6245 H HD11 . LEU   B 1 153 ? 37.511 -27.378 -8.211  1.00 16.22 ?  153 LEU   B HD11 1 
ATOM   6246 H HD12 . LEU   B 1 153 ? 38.150 -28.201 -9.409  1.00 16.22 ?  153 LEU   B HD12 1 
ATOM   6247 H HD13 . LEU   B 1 153 ? 38.621 -28.476 -7.917  1.00 16.22 ?  153 LEU   B HD13 1 
ATOM   6248 H HD21 . LEU   B 1 153 ? 38.874 -25.705 -7.001  1.00 15.95 ?  153 LEU   B HD21 1 
ATOM   6249 H HD22 . LEU   B 1 153 ? 40.041 -26.752 -6.739  1.00 15.95 ?  153 LEU   B HD22 1 
ATOM   6250 H HD23 . LEU   B 1 153 ? 40.353 -25.384 -7.484  1.00 15.95 ?  153 LEU   B HD23 1 
ATOM   6251 N N    . ALA   B 1 154 ? 44.031 -27.137 -9.362  1.00 11.87 ?  154 ALA   B N    1 
ATOM   6252 C CA   . ALA   B 1 154 ? 45.259 -27.898 -9.545  1.00 12.99 ?  154 ALA   B CA   1 
ATOM   6253 C C    . ALA   B 1 154 ? 45.326 -28.979 -8.474  1.00 13.36 ?  154 ALA   B C    1 
ATOM   6254 O O    . ALA   B 1 154 ? 45.246 -28.683 -7.275  1.00 14.99 ?  154 ALA   B O    1 
ATOM   6255 C CB   . ALA   B 1 154 ? 46.478 -26.980 -9.479  1.00 13.78 ?  154 ALA   B CB   1 
ATOM   6256 H H    . ALA   B 1 154 ? 44.049 -26.611 -8.676  1.00 14.25 ?  154 ALA   B H    1 
ATOM   6257 H HA   . ALA   B 1 154 ? 45.247 -28.324 -10.411 1.00 15.59 ?  154 ALA   B HA   1 
ATOM   6258 H HB1  . ALA   B 1 154 ? 47.283 -27.507 -9.602  1.00 16.53 ?  154 ALA   B HB1  1 
ATOM   6259 H HB2  . ALA   B 1 154 ? 46.412 -26.310 -10.181 1.00 16.53 ?  154 ALA   B HB2  1 
ATOM   6260 H HB3  . ALA   B 1 154 ? 46.503 -26.540 -8.612  1.00 16.53 ?  154 ALA   B HB3  1 
ATOM   6261 N N    . VAL   B 1 155 ? 45.450 -30.227 -8.911  1.00 12.64 ?  155 VAL   B N    1 
ATOM   6262 C CA   . VAL   B 1 155 ? 45.557 -31.376 -8.021  1.00 13.05 ?  155 VAL   B CA   1 
ATOM   6263 C C    . VAL   B 1 155 ? 46.900 -32.047 -8.297  1.00 12.83 ?  155 VAL   B C    1 
ATOM   6264 O O    . VAL   B 1 155 ? 47.137 -32.544 -9.407  1.00 14.73 ?  155 VAL   B O    1 
ATOM   6265 C CB   . VAL   B 1 155 ? 44.400 -32.371 -8.216  1.00 14.53 ?  155 VAL   B CB   1 
ATOM   6266 C CG1  . VAL   B 1 155 ? 44.580 -33.569 -7.299  1.00 14.45 ?  155 VAL   B CG1  1 
ATOM   6267 C CG2  . VAL   B 1 155 ? 43.055 -31.684 -7.965  1.00 15.67 ?  155 VAL   B CG2  1 
ATOM   6268 H H    . VAL   B 1 155 ? 45.478 -30.440 -9.744  1.00 15.17 ?  155 VAL   B H    1 
ATOM   6269 H HA   . VAL   B 1 155 ? 45.544 -31.079 -7.099  1.00 15.66 ?  155 VAL   B HA   1 
ATOM   6270 H HB   . VAL   B 1 155 ? 44.403 -32.688 -9.132  1.00 17.43 ?  155 VAL   B HB   1 
ATOM   6271 H HG11 . VAL   B 1 155 ? 43.753 -34.072 -7.263  1.00 17.33 ?  155 VAL   B HG11 1 
ATOM   6272 H HG12 . VAL   B 1 155 ? 45.292 -34.134 -7.648  1.00 17.33 ?  155 VAL   B HG12 1 
ATOM   6273 H HG13 . VAL   B 1 155 ? 44.815 -33.258 -6.410  1.00 17.33 ?  155 VAL   B HG13 1 
ATOM   6274 H HG21 . VAL   B 1 155 ? 42.344 -32.338 -8.055  1.00 18.80 ?  155 VAL   B HG21 1 
ATOM   6275 H HG22 . VAL   B 1 155 ? 43.052 -31.316 -7.067  1.00 18.80 ?  155 VAL   B HG22 1 
ATOM   6276 H HG23 . VAL   B 1 155 ? 42.935 -30.973 -8.614  1.00 18.80 ?  155 VAL   B HG23 1 
ATOM   6277 N N    . PHE   B 1 156 ? 47.765 -32.080 -7.280  1.00 13.42 ?  156 PHE   B N    1 
ATOM   6278 C CA   . PHE   B 1 156 ? 49.143 -32.542 -7.471  1.00 14.79 ?  156 PHE   B CA   1 
ATOM   6279 C C    . PHE   B 1 156 ? 49.240 -34.043 -7.758  1.00 15.66 ?  156 PHE   B C    1 
ATOM   6280 O O    . PHE   B 1 156 ? 49.972 -34.466 -8.664  1.00 17.31 ?  156 PHE   B O    1 
ATOM   6281 C CB   . PHE   B 1 156 ? 49.966 -32.175 -6.238  1.00 14.78 ?  156 PHE   B CB   1 
ATOM   6282 C CG   . PHE   B 1 156 ? 51.389 -32.636 -6.293  1.00 15.63 ?  156 PHE   B CG   1 
ATOM   6283 C CD1  . PHE   B 1 156 ? 52.276 -32.085 -7.198  1.00 17.05 ?  156 PHE   B CD1  1 
ATOM   6284 C CD2  . PHE   B 1 156 ? 51.842 -33.609 -5.429  1.00 15.76 ?  156 PHE   B CD2  1 
ATOM   6285 C CE1  . PHE   B 1 156 ? 53.598 -32.496 -7.242  1.00 17.86 ?  156 PHE   B CE1  1 
ATOM   6286 C CE2  . PHE   B 1 156 ? 53.162 -34.028 -5.469  1.00 17.32 ?  156 PHE   B CE2  1 
ATOM   6287 C CZ   . PHE   B 1 156 ? 54.034 -33.473 -6.381  1.00 17.69 ?  156 PHE   B CZ   1 
ATOM   6288 H H    . PHE   B 1 156 ? 47.578 -31.844 -6.473  1.00 16.10 ?  156 PHE   B H    1 
ATOM   6289 H HA   . PHE   B 1 156 ? 49.520 -32.072 -8.227  1.00 17.74 ?  156 PHE   B HA   1 
ATOM   6290 H HB2  . PHE   B 1 156 ? 49.972 -31.208 -6.147  1.00 17.74 ?  156 PHE   B HB2  1 
ATOM   6291 H HB3  . PHE   B 1 156 ? 49.556 -32.574 -5.456  1.00 17.74 ?  156 PHE   B HB3  1 
ATOM   6292 H HD1  . PHE   B 1 156 ? 51.987 -31.418 -7.783  1.00 20.46 ?  156 PHE   B HD1  1 
ATOM   6293 H HD2  . PHE   B 1 156 ? 51.254 -33.990 -4.816  1.00 18.91 ?  156 PHE   B HD2  1 
ATOM   6294 H HE1  . PHE   B 1 156 ? 54.185 -32.118 -7.859  1.00 21.44 ?  156 PHE   B HE1  1 
ATOM   6295 H HE2  . PHE   B 1 156 ? 53.453 -34.695 -4.886  1.00 20.78 ?  156 PHE   B HE2  1 
ATOM   6296 H HZ   . PHE   B 1 156 ? 54.919 -33.759 -6.408  1.00 21.23 ?  156 PHE   B HZ   1 
ATOM   6297 N N    . ASP   B 1 157 ? 48.569 -34.867 -6.963  1.00 16.03 ?  157 ASP   B N    1 
ATOM   6298 C CA   . ASP   B 1 157 ? 48.715 -36.315 -7.064  1.00 16.97 ?  157 ASP   B CA   1 
ATOM   6299 C C    . ASP   B 1 157 ? 47.802 -36.857 -8.158  1.00 17.27 ?  157 ASP   B C    1 
ATOM   6300 O O    . ASP   B 1 157 ? 46.575 -36.745 -8.057  1.00 16.89 ?  157 ASP   B O    1 
ATOM   6301 C CB   . ASP   B 1 157 ? 48.357 -36.930 -5.718  1.00 18.56 ?  157 ASP   B CB   1 
ATOM   6302 C CG   . ASP   B 1 157 ? 48.489 -38.438 -5.706  1.00 20.42 ?  157 ASP   B CG   1 
ATOM   6303 O OD1  . ASP   B 1 157 ? 48.820 -39.039 -6.756  1.00 21.04 ?  157 ASP   B OD1  1 
ATOM   6304 O OD2  . ASP   B 1 157 ? 48.270 -39.023 -4.626  1.00 22.58 -1 157 ASP   B OD2  1 
ATOM   6305 H H    . ASP   B 1 157 ? 48.016 -34.615 -6.358  1.00 19.23 ?  157 ASP   B H    1 
ATOM   6306 H HA   . ASP   B 1 157 ? 49.636 -36.542 -7.281  1.00 20.36 ?  157 ASP   B HA   1 
ATOM   6307 H HB2  . ASP   B 1 157 ? 48.935 -36.553 -5.041  1.00 22.27 ?  157 ASP   B HB2  1 
ATOM   6308 H HB3  . ASP   B 1 157 ? 47.430 -36.712 -5.517  1.00 22.27 ?  157 ASP   B HB3  1 
ATOM   6309 N N    . LYS   B 1 158 ? 48.400 -37.470 -9.189  1.00 18.11 ?  158 LYS   B N    1 
ATOM   6310 C CA   . LYS   B 1 158 ? 47.623 -38.087 -10.266 1.00 19.24 ?  158 LYS   B CA   1 
ATOM   6311 C C    . LYS   B 1 158 ? 46.564 -39.052 -9.732  1.00 19.09 ?  158 LYS   B C    1 
ATOM   6312 O O    . LYS   B 1 158 ? 45.461 -39.148 -10.287 1.00 19.23 ?  158 LYS   B O    1 
ATOM   6313 C CB   . LYS   B 1 158 ? 48.571 -38.807 -11.235 1.00 21.10 ?  158 LYS   B CB   1 
ATOM   6314 C CG   . LYS   B 1 158 ? 47.894 -39.698 -12.268 1.00 23.25 ?  158 LYS   B CG   1 
ATOM   6315 C CD   . LYS   B 1 158 ? 47.053 -38.905 -13.246 1.00 25.40 ?  158 LYS   B CD   1 
ATOM   6316 C CE   . LYS   B 1 158 ? 46.450 -39.817 -14.301 1.00 27.03 ?  158 LYS   B CE   1 
ATOM   6317 N NZ   . LYS   B 1 158 ? 45.410 -39.122 -15.113 1.00 26.96 ?  158 LYS   B NZ   1 
ATOM   6318 H H    . LYS   B 1 158 ? 49.256 -37.550 -9.286  1.00 21.73 ?  158 LYS   B H    1 
ATOM   6319 H HA   . LYS   B 1 158 ? 47.172 -37.392 -10.768 1.00 23.09 ?  158 LYS   B HA   1 
ATOM   6320 H HB2  . LYS   B 1 158 ? 49.083 -38.142 -11.726 1.00 25.32 ?  158 LYS   B HB2  1 
ATOM   6321 H HB3  . LYS   B 1 158 ? 49.176 -39.366 -10.725 1.00 25.32 ?  158 LYS   B HB3  1 
ATOM   6322 H HG2  . LYS   B 1 158 ? 48.577 -40.164 -12.778 1.00 27.91 ?  158 LYS   B HG2  1 
ATOM   6323 H HG3  . LYS   B 1 158 ? 47.322 -40.348 -11.828 1.00 27.91 ?  158 LYS   B HG3  1 
ATOM   6324 H HD2  . LYS   B 1 158 ? 46.330 -38.466 -12.771 1.00 30.48 ?  158 LYS   B HD2  1 
ATOM   6325 H HD3  . LYS   B 1 158 ? 47.610 -38.250 -13.695 1.00 30.48 ?  158 LYS   B HD3  1 
ATOM   6326 H HE2  . LYS   B 1 158 ? 47.146 -40.120 -14.902 1.00 32.44 ?  158 LYS   B HE2  1 
ATOM   6327 H HE3  . LYS   B 1 158 ? 46.030 -40.577 -13.866 1.00 32.44 ?  158 LYS   B HE3  1 
ATOM   6328 H HZ1  . LYS   B 1 158 ? 45.072 -39.677 -15.720 1.00 32.35 ?  158 LYS   B HZ1  1 
ATOM   6329 H HZ2  . LYS   B 1 158 ? 44.751 -38.835 -14.585 1.00 32.35 ?  158 LYS   B HZ2  1 
ATOM   6330 H HZ3  . LYS   B 1 158 ? 45.769 -38.421 -15.530 1.00 32.35 ?  158 LYS   B HZ3  1 
ATOM   6331 N N    . ASN   B 1 159 ? 46.887 -39.807 -8.679  1.00 19.36 ?  159 ASN   B N    1 
ATOM   6332 C CA   . ASN   B 1 159 ? 45.932 -40.790 -8.173  1.00 20.04 ?  159 ASN   B CA   1 
ATOM   6333 C C    . ASN   B 1 159 ? 44.730 -40.120 -7.506  1.00 18.95 ?  159 ASN   B C    1 
ATOM   6334 O O    . ASN   B 1 159 ? 43.597 -40.609 -7.621  1.00 19.25 ?  159 ASN   B O    1 
ATOM   6335 C CB   . ASN   B 1 159 ? 46.634 -41.764 -7.234  1.00 22.01 ?  159 ASN   B CB   1 
ATOM   6336 C CG   . ASN   B 1 159 ? 47.668 -42.609 -7.948  1.00 24.10 ?  159 ASN   B CG   1 
ATOM   6337 O OD1  . ASN   B 1 159 ? 47.423 -43.117 -9.051  1.00 25.10 ?  159 ASN   B OD1  1 
ATOM   6338 N ND2  . ASN   B 1 159 ? 48.828 -42.775 -7.324  1.00 25.08 ?  159 ASN   B ND2  1 
ATOM   6339 H H    . ASN   B 1 159 ? 47.630 -39.758 -8.254  1.00 23.24 ?  159 ASN   B H    1 
ATOM   6340 H HA   . ASN   B 1 159 ? 45.597 -41.298 -8.928  1.00 24.05 ?  159 ASN   B HA   1 
ATOM   6341 H HB2  . ASN   B 1 159 ? 47.082 -41.267 -6.535  1.00 26.42 ?  159 ASN   B HB2  1 
ATOM   6342 H HB3  . ASN   B 1 159 ? 45.976 -42.364 -6.855  1.00 26.42 ?  159 ASN   B HB3  1 
ATOM   6343 H HD21 . ASN   B 1 159 ? 49.453 -43.245 -7.689  1.00 30.09 ?  159 ASN   B HD21 1 
ATOM   6344 H HD22 . ASN   B 1 159 ? 48.957 -42.423 -6.550  1.00 30.09 ?  159 ASN   B HD22 1 
ATOM   6345 N N    . LEU   B 1 160 ? 44.941 -38.988 -6.824  1.00 17.96 ?  160 LEU   B N    1 
ATOM   6346 C CA   . LEU   B 1 160 ? 43.806 -38.250 -6.280  1.00 16.95 ?  160 LEU   B CA   1 
ATOM   6347 C C    . LEU   B 1 160 ? 43.019 -37.581 -7.394  1.00 16.22 ?  160 LEU   B C    1 
ATOM   6348 O O    . LEU   B 1 160 ? 41.782 -37.590 -7.381  1.00 16.00 ?  160 LEU   B O    1 
ATOM   6349 C CB   . LEU   B 1 160 ? 44.266 -37.217 -5.251  1.00 16.61 ?  160 LEU   B CB   1 
ATOM   6350 C CG   . LEU   B 1 160 ? 43.140 -36.321 -4.715  1.00 16.38 ?  160 LEU   B CG   1 
ATOM   6351 C CD1  . LEU   B 1 160 ? 42.021 -37.153 -4.094  1.00 17.25 ?  160 LEU   B CD1  1 
ATOM   6352 C CD2  . LEU   B 1 160 ? 43.679 -35.319 -3.709  1.00 16.89 ?  160 LEU   B CD2  1 
ATOM   6353 H H    . LEU   B 1 160 ? 45.715 -38.631 -6.675  1.00 21.55 ?  160 LEU   B H    1 
ATOM   6354 H HA   . LEU   B 1 160 ? 43.220 -38.876 -5.837  1.00 20.34 ?  160 LEU   B HA   1 
ATOM   6355 H HB2  . LEU   B 1 160 ? 44.662 -37.687 -4.498  1.00 19.93 ?  160 LEU   B HB2  1 
ATOM   6356 H HB3  . LEU   B 1 160 ? 44.936 -36.643 -5.661  1.00 19.93 ?  160 LEU   B HB3  1 
ATOM   6357 H HG   . LEU   B 1 160 ? 42.762 -35.821 -5.452  1.00 19.65 ?  160 LEU   B HG   1 
ATOM   6358 H HD11 . LEU   B 1 160 ? 41.387 -36.557 -3.669  1.00 20.71 ?  160 LEU   B HD11 1 
ATOM   6359 H HD12 . LEU   B 1 160 ? 41.578 -37.664 -4.791  1.00 20.71 ?  160 LEU   B HD12 1 
ATOM   6360 H HD13 . LEU   B 1 160 ? 42.402 -37.756 -3.435  1.00 20.71 ?  160 LEU   B HD13 1 
ATOM   6361 H HD21 . LEU   B 1 160 ? 42.948 -34.752 -3.414  1.00 20.27 ?  160 LEU   B HD21 1 
ATOM   6362 H HD22 . LEU   B 1 160 ? 44.052 -35.798 -2.954  1.00 20.27 ?  160 LEU   B HD22 1 
ATOM   6363 H HD23 . LEU   B 1 160 ? 44.363 -34.781 -4.136  1.00 20.27 ?  160 LEU   B HD23 1 
ATOM   6364 N N    . TYR   B 1 161 ? 43.721 -37.012 -8.378  1.00 16.19 ?  161 TYR   B N    1 
ATOM   6365 C CA   . TYR   B 1 161 ? 43.049 -36.447 -9.542  1.00 16.09 ?  161 TYR   B CA   1 
ATOM   6366 C C    . TYR   B 1 161 ? 42.105 -37.467 -10.165 1.00 15.90 ?  161 TYR   B C    1 
ATOM   6367 O O    . TYR   B 1 161 ? 40.934 -37.172 -10.423 1.00 16.02 ?  161 TYR   B O    1 
ATOM   6368 C CB   . TYR   B 1 161 ? 44.092 -35.964 -10.559 1.00 16.93 ?  161 TYR   B CB   1 
ATOM   6369 C CG   . TYR   B 1 161 ? 43.517 -35.494 -11.874 1.00 17.24 ?  161 TYR   B CG   1 
ATOM   6370 C CD1  . TYR   B 1 161 ? 43.124 -34.171 -12.045 1.00 17.13 ?  161 TYR   B CD1  1 
ATOM   6371 C CD2  . TYR   B 1 161 ? 43.346 -36.372 -12.939 1.00 18.02 ?  161 TYR   B CD2  1 
ATOM   6372 C CE1  . TYR   B 1 161 ? 42.593 -33.736 -13.235 1.00 18.30 ?  161 TYR   B CE1  1 
ATOM   6373 C CE2  . TYR   B 1 161 ? 42.813 -35.944 -14.134 1.00 19.00 ?  161 TYR   B CE2  1 
ATOM   6374 C CZ   . TYR   B 1 161 ? 42.438 -34.624 -14.277 1.00 18.81 ?  161 TYR   B CZ   1 
ATOM   6375 O OH   . TYR   B 1 161 ? 41.904 -34.182 -15.463 1.00 20.82 ?  161 TYR   B OH   1 
ATOM   6376 H H    . TYR   B 1 161 ? 44.576 -36.950 -8.402  1.00 19.42 ?  161 TYR   B H    1 
ATOM   6377 H HA   . TYR   B 1 161 ? 42.522 -35.682 -9.269  1.00 19.31 ?  161 TYR   B HA   1 
ATOM   6378 H HB2  . TYR   B 1 161 ? 44.581 -35.219 -10.173 1.00 20.31 ?  161 TYR   B HB2  1 
ATOM   6379 H HB3  . TYR   B 1 161 ? 44.703 -36.690 -10.753 1.00 20.31 ?  161 TYR   B HB3  1 
ATOM   6380 H HD1  . TYR   B 1 161 ? 43.233 -33.563 -11.347 1.00 20.55 ?  161 TYR   B HD1  1 
ATOM   6381 H HD2  . TYR   B 1 161 ? 43.592 -37.262 -12.846 1.00 21.63 ?  161 TYR   B HD2  1 
ATOM   6382 H HE1  . TYR   B 1 161 ? 42.344 -32.841 -13.337 1.00 21.97 ?  161 TYR   B HE1  1 
ATOM   6383 H HE2  . TYR   B 1 161 ? 42.701 -36.537 -14.841 1.00 22.80 ?  161 TYR   B HE2  1 
ATOM   6384 H HH   . TYR   B 1 161 ? 41.859 -34.820 -16.012 1.00 24.98 ?  161 TYR   B HH   1 
ATOM   6385 N N    . ASP   B 1 162 ? 42.601 -38.687 -10.392 1.00 16.48 ?  162 ASP   B N    1 
ATOM   6386 C CA   . ASP   B 1 162 ? 41.778 -39.726 -11.007 1.00 17.15 ?  162 ASP   B CA   1 
ATOM   6387 C C    . ASP   B 1 162 ? 40.569 -40.064 -10.143 1.00 16.48 ?  162 ASP   B C    1 
ATOM   6388 O O    . ASP   B 1 162 ? 39.466 -40.277 -10.662 1.00 17.02 ?  162 ASP   B O    1 
ATOM   6389 C CB   . ASP   B 1 162 ? 42.614 -40.984 -11.253 1.00 18.71 ?  162 ASP   B CB   1 
ATOM   6390 C CG   . ASP   B 1 162 ? 43.603 -40.826 -12.397 1.00 20.15 ?  162 ASP   B CG   1 
ATOM   6391 O OD1  . ASP   B 1 162 ? 43.478 -39.876 -13.193 1.00 20.33 ?  162 ASP   B OD1  1 
ATOM   6392 O OD2  . ASP   B 1 162 ? 44.499 -41.685 -12.512 1.00 21.87 -1 162 ASP   B OD2  1 
ATOM   6393 H H    . ASP   B 1 162 ? 43.399 -38.934 -10.201 1.00 19.77 ?  162 ASP   B H    1 
ATOM   6394 H HA   . ASP   B 1 162 ? 41.452 -39.408 -11.863 1.00 20.58 ?  162 ASP   B HA   1 
ATOM   6395 H HB2  . ASP   B 1 162 ? 43.123 -41.185 -10.451 1.00 22.45 ?  162 ASP   B HB2  1 
ATOM   6396 H HB3  . ASP   B 1 162 ? 42.023 -41.720 -11.466 1.00 22.45 ?  162 ASP   B HB3  1 
ATOM   6397 N N    A LYS   B 1 163 ? 40.757 -40.138 -8.823  0.70 15.72 ?  163 LYS   B N    1 
ATOM   6398 N N    B LYS   B 1 163 ? 40.751 -40.122 -8.821  0.30 16.62 ?  163 LYS   B N    1 
ATOM   6399 C CA   A LYS   B 1 163 ? 39.630 -40.414 -7.938  0.70 15.96 ?  163 LYS   B CA   1 
ATOM   6400 C CA   B LYS   B 1 163 ? 39.627 -40.416 -7.937  0.30 17.04 ?  163 LYS   B CA   1 
ATOM   6401 C C    A LYS   B 1 163 ? 38.587 -39.305 -8.008  0.70 15.20 ?  163 LYS   B C    1 
ATOM   6402 C C    B LYS   B 1 163 ? 38.586 -39.302 -7.974  0.30 15.78 ?  163 LYS   B C    1 
ATOM   6403 O O    A LYS   B 1 163 ? 37.378 -39.577 -8.032  0.70 16.11 ?  163 LYS   B O    1 
ATOM   6404 O O    B LYS   B 1 163 ? 37.379 -39.568 -7.937  0.30 16.14 ?  163 LYS   B O    1 
ATOM   6405 C CB   A LYS   B 1 163 ? 40.115 -40.602 -6.502  0.70 18.75 ?  163 LYS   B CB   1 
ATOM   6406 C CB   B LYS   B 1 163 ? 40.124 -40.635 -6.509  0.30 19.31 ?  163 LYS   B CB   1 
ATOM   6407 C CG   A LYS   B 1 163 ? 39.031 -41.136 -5.587  0.70 23.00 ?  163 LYS   B CG   1 
ATOM   6408 C CG   B LYS   B 1 163 ? 39.044 -41.136 -5.569  0.30 22.14 ?  163 LYS   B CG   1 
ATOM   6409 C CD   A LYS   B 1 163 ? 39.445 -41.164 -4.128  0.70 26.27 ?  163 LYS   B CD   1 
ATOM   6410 C CD   B LYS   B 1 163 ? 39.545 -41.289 -4.145  0.30 24.62 ?  163 LYS   B CD   1 
ATOM   6411 C CE   A LYS   B 1 163 ? 38.369 -41.843 -3.288  0.70 28.42 ?  163 LYS   B CE   1 
ATOM   6412 C CE   B LYS   B 1 163 ? 38.490 -41.967 -3.284  0.30 26.12 ?  163 LYS   B CE   1 
ATOM   6413 N NZ   A LYS   B 1 163 ? 38.506 -41.554 -1.835  0.70 29.85 ?  163 LYS   B NZ   1 
ATOM   6414 N NZ   B LYS   B 1 163 ? 38.709 -41.739 -1.830  0.30 26.99 ?  163 LYS   B NZ   1 
ATOM   6415 H H    A LYS   B 1 163 ? 41.513 -40.031 -8.425  0.70 18.86 ?  163 LYS   B H    1 
ATOM   6416 H H    B LYS   B 1 163 ? 41.503 -39.999 -8.421  0.30 19.94 ?  163 LYS   B H    1 
ATOM   6417 H HA   A LYS   B 1 163 ? 39.209 -41.239 -8.220  0.70 19.15 ?  163 LYS   B HA   1 
ATOM   6418 H HA   B LYS   B 1 163 ? 39.200 -41.234 -8.233  0.30 20.45 ?  163 LYS   B HA   1 
ATOM   6419 H HB2  A LYS   B 1 163 ? 40.851 -41.237 -6.496  0.70 22.50 ?  163 LYS   B HB2  1 
ATOM   6420 H HB2  B LYS   B 1 163 ? 40.836 -41.296 -6.521  0.30 23.17 ?  163 LYS   B HB2  1 
ATOM   6421 H HB3  A LYS   B 1 163 ? 40.411 -39.749 -6.152  0.70 22.50 ?  163 LYS   B HB3  1 
ATOM   6422 H HB3  B LYS   B 1 163 ? 40.458 -39.796 -6.158  0.30 23.17 ?  163 LYS   B HB3  1 
ATOM   6423 H HG2  A LYS   B 1 163 ? 38.246 -40.573 -5.662  0.70 27.60 ?  163 LYS   B HG2  1 
ATOM   6424 H HG2  B LYS   B 1 163 ? 38.309 -40.503 -5.561  0.30 26.57 ?  163 LYS   B HG2  1 
ATOM   6425 H HG3  A LYS   B 1 163 ? 38.813 -42.044 -5.854  0.70 27.60 ?  163 LYS   B HG3  1 
ATOM   6426 H HG3  B LYS   B 1 163 ? 38.734 -42.003 -5.874  0.30 26.57 ?  163 LYS   B HG3  1 
ATOM   6427 H HD2  A LYS   B 1 163 ? 40.270 -41.668 -4.034  0.70 31.53 ?  163 LYS   B HD2  1 
ATOM   6428 H HD2  B LYS   B 1 163 ? 40.346 -41.838 -4.140  0.30 29.55 ?  163 LYS   B HD2  1 
ATOM   6429 H HD3  A LYS   B 1 163 ? 39.562 -40.257 -3.806  0.70 31.53 ?  163 LYS   B HD3  1 
ATOM   6430 H HD3  B LYS   B 1 163 ? 39.732 -40.414 -3.771  0.30 29.55 ?  163 LYS   B HD3  1 
ATOM   6431 H HE2  A LYS   B 1 163 ? 37.495 -41.540 -3.579  0.70 34.10 ?  163 LYS   B HE2  1 
ATOM   6432 H HE2  B LYS   B 1 163 ? 37.617 -41.616 -3.518  0.30 31.34 ?  163 LYS   B HE2  1 
ATOM   6433 H HE3  A LYS   B 1 163 ? 38.438 -42.802 -3.409  0.70 34.10 ?  163 LYS   B HE3  1 
ATOM   6434 H HE3  B LYS   B 1 163 ? 38.517 -42.923 -3.446  0.30 31.34 ?  163 LYS   B HE3  1 
ATOM   6435 H HZ1  A LYS   B 1 163 ? 37.860 -41.966 -1.381  0.70 35.82 ?  163 LYS   B HZ1  1 
ATOM   6436 H HZ1  B LYS   B 1 163 ? 38.073 -42.149 -1.361  0.30 32.38 ?  163 LYS   B HZ1  1 
ATOM   6437 H HZ2  A LYS   B 1 163 ? 39.295 -41.843 -1.542  0.70 35.82 ?  163 LYS   B HZ2  1 
ATOM   6438 H HZ2  B LYS   B 1 163 ? 39.501 -42.061 -1.588  0.30 32.38 ?  163 LYS   B HZ2  1 
ATOM   6439 H HZ3  A LYS   B 1 163 ? 38.447 -40.678 -1.692  0.70 35.82 ?  163 LYS   B HZ3  1 
ATOM   6440 H HZ3  B LYS   B 1 163 ? 38.683 -40.867 -1.653  0.30 32.38 ?  163 LYS   B HZ3  1 
ATOM   6441 N N    . LEU   B 1 164 ? 39.039 -38.049 -8.043  1.00 14.55 ?  164 LEU   B N    1 
ATOM   6442 C CA   . LEU   B 1 164 ? 38.126 -36.912 -8.105  1.00 14.24 ?  164 LEU   B CA   1 
ATOM   6443 C C    . LEU   B 1 164 ? 37.349 -36.895 -9.417  1.00 14.55 ?  164 LEU   B C    1 
ATOM   6444 O O    . LEU   B 1 164 ? 36.127 -36.697 -9.425  1.00 15.51 ?  164 LEU   B O    1 
ATOM   6445 C CB   . LEU   B 1 164 ? 38.932 -35.621 -7.948  1.00 13.72 ?  164 LEU   B CB   1 
ATOM   6446 C CG   . LEU   B 1 164 ? 39.455 -35.349 -6.544  1.00 14.65 ?  164 LEU   B CG   1 
ATOM   6447 C CD1  . LEU   B 1 164 ? 40.558 -34.290 -6.577  1.00 14.77 ?  164 LEU   B CD1  1 
ATOM   6448 C CD2  . LEU   B 1 164 ? 38.332 -34.924 -5.621  1.00 16.52 ?  164 LEU   B CD2  1 
ATOM   6449 H H    A LEU   B 1 164 ? 39.873 -37.830 -8.030  0.70 17.45 ?  164 LEU   B H    1 
ATOM   6450 H H    B LEU   B 1 164 ? 39.873 -37.832 -8.057  0.30 17.45 ?  164 LEU   B H    1 
ATOM   6451 H HA   . LEU   B 1 164 ? 37.492 -36.968 -7.380  1.00 17.09 ?  164 LEU   B HA   1 
ATOM   6452 H HB2  . LEU   B 1 164 ? 39.701 -35.663 -8.545  1.00 16.46 ?  164 LEU   B HB2  1 
ATOM   6453 H HB3  . LEU   B 1 164 ? 38.370 -34.874 -8.204  1.00 16.46 ?  164 LEU   B HB3  1 
ATOM   6454 H HG   . LEU   B 1 164 ? 39.843 -36.160 -6.193  1.00 17.58 ?  164 LEU   B HG   1 
ATOM   6455 H HD11 . LEU   B 1 164 ? 40.876 -34.130 -5.671  1.00 17.73 ?  164 LEU   B HD11 1 
ATOM   6456 H HD12 . LEU   B 1 164 ? 41.297 -34.611 -7.126  1.00 17.73 ?  164 LEU   B HD12 1 
ATOM   6457 H HD13 . LEU   B 1 164 ? 40.209 -33.467 -6.952  1.00 17.73 ?  164 LEU   B HD13 1 
ATOM   6458 H HD21 . LEU   B 1 164 ? 38.703 -34.682 -4.759  1.00 19.82 ?  164 LEU   B HD21 1 
ATOM   6459 H HD22 . LEU   B 1 164 ? 37.871 -34.163 -6.008  1.00 19.82 ?  164 LEU   B HD22 1 
ATOM   6460 H HD23 . LEU   B 1 164 ? 37.713 -35.666 -5.519  1.00 19.82 ?  164 LEU   B HD23 1 
ATOM   6461 N N    . VAL   B 1 165 ? 38.045 -37.075 -10.541 1.00 15.85 ?  165 VAL   B N    1 
ATOM   6462 C CA   . VAL   B 1 165 ? 37.395 -37.004 -11.845 1.00 16.95 ?  165 VAL   B CA   1 
ATOM   6463 C C    . VAL   B 1 165 ? 36.470 -38.198 -12.036 1.00 18.61 ?  165 VAL   B C    1 
ATOM   6464 O O    . VAL   B 1 165 ? 35.313 -38.056 -12.452 1.00 19.62 ?  165 VAL   B O    1 
ATOM   6465 C CB   . VAL   B 1 165 ? 38.444 -36.915 -12.969 1.00 17.98 ?  165 VAL   B CB   1 
ATOM   6466 C CG1  . VAL   B 1 165 ? 37.780 -37.008 -14.322 1.00 19.18 ?  165 VAL   B CG1  1 
ATOM   6467 C CG2  . VAL   B 1 165 ? 39.231 -35.625 -12.856 1.00 17.92 ?  165 VAL   B CG2  1 
ATOM   6468 H H    . VAL   B 1 165 ? 38.895 -37.230 -10.573 1.00 19.02 ?  165 VAL   B H    1 
ATOM   6469 H HA   . VAL   B 1 165 ? 36.856 -36.206 -11.884 1.00 20.34 ?  165 VAL   B HA   1 
ATOM   6470 H HB   . VAL   B 1 165 ? 39.073 -37.650 -12.885 1.00 21.58 ?  165 VAL   B HB   1 
ATOM   6471 H HG11 . VAL   B 1 165 ? 38.401 -36.707 -15.000 1.00 23.02 ?  165 VAL   B HG11 1 
ATOM   6472 H HG12 . VAL   B 1 165 ? 37.540 -37.936 -14.487 1.00 23.02 ?  165 VAL   B HG12 1 
ATOM   6473 H HG13 . VAL   B 1 165 ? 36.987 -36.455 -14.322 1.00 23.02 ?  165 VAL   B HG13 1 
ATOM   6474 H HG21 . VAL   B 1 165 ? 39.869 -35.574 -13.588 1.00 21.50 ?  165 VAL   B HG21 1 
ATOM   6475 H HG22 . VAL   B 1 165 ? 38.617 -34.873 -12.905 1.00 21.50 ?  165 VAL   B HG22 1 
ATOM   6476 H HG23 . VAL   B 1 165 ? 39.702 -35.609 -12.008 1.00 21.50 ?  165 VAL   B HG23 1 
ATOM   6477 N N    . SER   B 1 166 ? 36.973 -39.398 -11.730 1.00 19.45 ?  166 SER   B N    1 
ATOM   6478 C CA   . SER   B 1 166 ? 36.214 -40.608 -12.012 1.00 20.53 ?  166 SER   B CA   1 
ATOM   6479 C C    . SER   B 1 166 ? 34.961 -40.695 -11.156 1.00 20.61 ?  166 SER   B C    1 
ATOM   6480 O O    . SER   B 1 166 ? 33.990 -41.322 -11.575 1.00 21.93 ?  166 SER   B O    1 
ATOM   6481 C CB   . SER   B 1 166 ? 37.079 -41.865 -11.849 1.00 21.76 ?  166 SER   B CB   1 
ATOM   6482 O OG   . SER   B 1 166 ? 37.456 -42.071 -10.499 1.00 21.81 ?  166 SER   B OG   1 
ATOM   6483 H H    . SER   B 1 166 ? 37.747 -39.536 -11.372 1.00 23.33 ?  166 SER   B H    1 
ATOM   6484 H HA   . SER   B 1 166 ? 35.929 -40.581 -12.938 1.00 24.64 ?  166 SER   B HA   1 
ATOM   6485 H HB2  . SER   B 1 166 ? 36.570 -42.637 -12.153 1.00 26.12 ?  166 SER   B HB2  1 
ATOM   6486 H HB3  . SER   B 1 166 ? 37.878 -41.770 -12.392 1.00 26.12 ?  166 SER   B HB3  1 
ATOM   6487 H HG   . SER   B 1 166 ? 37.908 -41.419 -10.228 1.00 26.17 ?  166 SER   B HG   1 
ATOM   6488 N N    . SER   B 1 167 ? 34.942 -40.078 -9.976  1.00 19.35 ?  167 SER   B N    1 
ATOM   6489 C CA   . SER   B 1 167 ? 33.786 -40.140 -9.090  1.00 18.83 ?  167 SER   B CA   1 
ATOM   6490 C C    . SER   B 1 167 ? 32.866 -38.924 -9.188  1.00 18.69 ?  167 SER   B C    1 
ATOM   6491 O O    . SER   B 1 167 ? 31.794 -38.924 -8.571  1.00 18.88 ?  167 SER   B O    1 
ATOM   6492 C CB   . SER   B 1 167 ? 34.226 -40.323 -7.633  1.00 18.92 ?  167 SER   B CB   1 
ATOM   6493 O OG   . SER   B 1 167 ? 34.905 -39.167 -7.159  1.00 18.61 ?  167 SER   B OG   1 
ATOM   6494 H H    . SER   B 1 167 ? 35.591 -39.608 -9.669  1.00 23.22 ?  167 SER   B H    1 
ATOM   6495 H HA   . SER   B 1 167 ? 33.258 -40.917 -9.332  1.00 22.59 ?  167 SER   B HA   1 
ATOM   6496 H HB2  . SER   B 1 167 ? 33.440 -40.477 -7.085  1.00 22.70 ?  167 SER   B HB2  1 
ATOM   6497 H HB3  . SER   B 1 167 ? 34.816 -41.096 -7.582  1.00 22.70 ?  167 SER   B HB3  1 
ATOM   6498 H HG   . SER   B 1 167 ? 35.595 -39.043 -7.628  1.00 22.33 ?  167 SER   B HG   1 
ATOM   6499 N N    . PHE   B 1 168 ? 33.234 -37.895 -9.953  1.00 18.60 ?  168 PHE   B N    1 
ATOM   6500 C CA   . PHE   B 1 168 ? 32.407 -36.689 -10.009 1.00 18.10 ?  168 PHE   B CA   1 
ATOM   6501 C C    . PHE   B 1 168 ? 31.087 -36.944 -10.731 1.00 15.88 ?  168 PHE   B C    1 
ATOM   6502 O O    . PHE   B 1 168 ? 30.048 -36.347 -10.385 1.00 16.62 ?  168 PHE   B O    1 
ATOM   6503 C CB   . PHE   B 1 168 ? 33.169 -35.558 -10.695 1.00 18.92 ?  168 PHE   B CB   1 
ATOM   6504 C CG   . PHE   B 1 168 ? 32.369 -34.305 -10.824 1.00 19.07 ?  168 PHE   B CG   1 
ATOM   6505 C CD1  . PHE   B 1 168 ? 32.054 -33.560 -9.696  1.00 20.29 ?  168 PHE   B CD1  1 
ATOM   6506 C CD2  . PHE   B 1 168 ? 31.910 -33.877 -12.054 1.00 18.59 ?  168 PHE   B CD2  1 
ATOM   6507 C CE1  . PHE   B 1 168 ? 31.298 -32.409 -9.790  1.00 20.85 ?  168 PHE   B CE1  1 
ATOM   6508 C CE2  . PHE   B 1 168 ? 31.163 -32.709 -12.163 1.00 19.62 ?  168 PHE   B CE2  1 
ATOM   6509 C CZ   . PHE   B 1 168 ? 30.854 -31.974 -11.026 1.00 20.05 ?  168 PHE   B CZ   1 
ATOM   6510 H H    . PHE   B 1 168 ? 33.949 -37.864 -10.431 1.00 22.32 ?  168 PHE   B H    1 
ATOM   6511 H HA   . PHE   B 1 168 ? 32.198 -36.406 -9.109  1.00 21.73 ?  168 PHE   B HA   1 
ATOM   6512 H HB2  . PHE   B 1 168 ? 33.960 -35.352 -10.173 1.00 22.71 ?  168 PHE   B HB2  1 
ATOM   6513 H HB3  . PHE   B 1 168 ? 33.422 -35.839 -11.586 1.00 22.71 ?  168 PHE   B HB3  1 
ATOM   6514 H HD1  . PHE   B 1 168 ? 32.346 -33.852 -8.864  1.00 24.35 ?  168 PHE   B HD1  1 
ATOM   6515 H HD2  . PHE   B 1 168 ? 32.115 -34.360 -12.819 1.00 22.31 ?  168 PHE   B HD2  1 
ATOM   6516 H HE1  . PHE   B 1 168 ? 31.092 -31.922 -9.026  1.00 25.02 ?  168 PHE   B HE1  1 
ATOM   6517 H HE2  . PHE   B 1 168 ? 30.857 -32.426 -12.998 1.00 23.54 ?  168 PHE   B HE2  1 
ATOM   6518 H HZ   . PHE   B 1 168 ? 30.341 -31.199 -11.099 1.00 24.06 ?  168 PHE   B HZ   1 
ATOM   6519 N N    . LEU   B 1 169 ? 31.111 -37.828 -11.726 1.00 16.23 ?  169 LEU   B N    1 
ATOM   6520 C CA   . LEU   B 1 169 ? 29.933 -38.133 -12.521 1.00 18.42 ?  169 LEU   B CA   1 
ATOM   6521 C C    . LEU   B 1 169 ? 29.933 -39.570 -13.019 1.00 20.97 ?  169 LEU   B C    1 
ATOM   6522 O O    . LEU   B 1 169 ? 29.022 -39.984 -13.737 1.00 23.48 ?  169 LEU   B O    1 
ATOM   6523 C CB   . LEU   B 1 169 ? 29.857 -37.186 -13.717 1.00 20.27 ?  169 LEU   B CB   1 
ATOM   6524 C CG   . LEU   B 1 169 ? 28.599 -36.323 -13.808 1.00 23.39 ?  169 LEU   B CG   1 
ATOM   6525 C CD1  . LEU   B 1 169 ? 28.566 -35.590 -15.136 1.00 24.61 ?  169 LEU   B CD1  1 
ATOM   6526 C CD2  . LEU   B 1 169 ? 27.343 -37.153 -13.620 1.00 23.56 ?  169 LEU   B CD2  1 
ATOM   6527 O OXT  . LEU   B 1 169 ? 30.851 -40.332 -12.728 1.00 21.86 -1 169 LEU   B OXT  1 
ATOM   6528 H H    . LEU   B 1 169 ? 31.814 -38.266 -11.972 1.00 19.48 ?  169 LEU   B H    1 
ATOM   6529 H HA   . LEU   B 1 169 ? 29.147 -38.001 -11.973 1.00 22.11 ?  169 LEU   B HA   1 
ATOM   6530 H HB2  . LEU   B 1 169 ? 30.618 -36.584 -13.682 1.00 24.33 ?  169 LEU   B HB2  1 
ATOM   6531 H HB3  . LEU   B 1 169 ? 29.901 -37.712 -14.532 1.00 24.33 ?  169 LEU   B HB3  1 
ATOM   6532 H HG   . LEU   B 1 169 ? 28.624 -35.655 -13.104 1.00 28.07 ?  169 LEU   B HG   1 
ATOM   6533 H HD11 . LEU   B 1 169 ? 27.774 -35.030 -15.167 1.00 29.53 ?  169 LEU   B HD11 1 
ATOM   6534 H HD12 . LEU   B 1 169 ? 29.362 -35.042 -15.213 1.00 29.53 ?  169 LEU   B HD12 1 
ATOM   6535 H HD13 . LEU   B 1 169 ? 28.539 -36.241 -15.853 1.00 29.53 ?  169 LEU   B HD13 1 
ATOM   6536 H HD21 . LEU   B 1 169 ? 26.594 -36.694 -14.026 1.00 28.27 ?  169 LEU   B HD21 1 
ATOM   6537 H HD22 . LEU   B 1 169 ? 27.472 -38.018 -14.044 1.00 28.27 ?  169 LEU   B HD22 1 
ATOM   6538 H HD23 . LEU   B 1 169 ? 27.185 -37.273 -12.672 1.00 28.27 ?  169 LEU   B HD23 1 
HETATM 6539 O O1   B A1BAA C 2 .   ? 14.973 -2.743  3.137   0.15 13.10 ?  201 A1BAA A O1   1 
HETATM 6540 C C1   B A1BAA C 2 .   ? 15.702 -0.317  -0.500  0.15 14.51 ?  201 A1BAA A C1   1 
HETATM 6541 C C2   B A1BAA C 2 .   ? 14.292 -0.568  0.058   0.15 14.36 ?  201 A1BAA A C2   1 
HETATM 6542 C C3   B A1BAA C 2 .   ? 14.303 -0.811  1.607   0.15 13.94 ?  201 A1BAA A C3   1 
HETATM 6543 C C4   B A1BAA C 2 .   ? 12.847 -1.205  2.105   0.15 14.11 ?  201 A1BAA A C4   1 
HETATM 6544 C C5   B A1BAA C 2 .   ? 11.863 -0.014  2.093   0.15 14.46 ?  201 A1BAA A C5   1 
HETATM 6545 C C6   B A1BAA C 2 .   ? 15.341 -2.005  1.970   0.15 13.15 ?  201 A1BAA A C6   1 
HETATM 6546 C C7   B A1BAA C 2 .   ? 14.890 0.776   3.646   0.15 13.04 ?  201 A1BAA A C7   1 
HETATM 6547 C C8   B A1BAA C 2 .   ? 14.794 -0.069  5.887   0.15 12.94 ?  201 A1BAA A C8   1 
HETATM 6548 C C10  B A1BAA C 2 .   ? 15.187 2.099   4.222   0.15 12.78 ?  201 A1BAA A C10  1 
HETATM 6549 C C11  B A1BAA C 2 .   ? 15.468 3.489   3.830   0.15 12.71 ?  201 A1BAA A C11  1 
HETATM 6550 C C12  B A1BAA C 2 .   ? 15.666 4.248   4.978   0.15 12.50 ?  201 A1BAA A C12  1 
HETATM 6551 C C9   B A1BAA C 2 .   ? 15.247 2.138   5.664   0.15 12.67 ?  201 A1BAA A C9   1 
HETATM 6552 N N1   B A1BAA C 2 .   ? 14.786 0.508   2.261   0.15 14.02 ?  201 A1BAA A N1   1 
HETATM 6553 N N2   B A1BAA C 2 .   ? 14.700 -0.277  4.531   0.15 13.00 ?  201 A1BAA A N2   1 
HETATM 6554 N N3   B A1BAA C 2 .   ? 15.057 1.090   6.493   0.15 12.76 ?  201 A1BAA A N3   1 
HETATM 6555 N N4   B A1BAA C 2 .   ? 15.532 3.418   6.029   0.15 12.71 ?  201 A1BAA A N4   1 
HETATM 6556 H H13  B A1BAA C 2 .   ? 14.176 -3.283  2.967   0.15 15.72 ?  201 A1BAA A H13  1 
HETATM 6557 H H2   B A1BAA C 2 .   ? 16.474 -0.297  0.289   0.15 17.41 ?  201 A1BAA A H2   1 
HETATM 6558 H H1   B A1BAA C 2 .   ? 15.811 0.651   -1.033  0.15 17.41 ?  201 A1BAA A H1   1 
HETATM 6559 H H3   B A1BAA C 2 .   ? 16.001 -1.096  -1.217  0.15 17.41 ?  201 A1BAA A H3   1 
HETATM 6560 H H4   B A1BAA C 2 .   ? 13.634 0.314   -0.189  0.15 17.23 ?  201 A1BAA A H4   1 
HETATM 6561 H H5   B A1BAA C 2 .   ? 13.806 -1.430  -0.467  0.15 17.23 ?  201 A1BAA A H5   1 
HETATM 6562 H H6   B A1BAA C 2 .   ? 12.447 -2.034  1.449   0.15 16.93 ?  201 A1BAA A H6   1 
HETATM 6563 H H7   B A1BAA C 2 .   ? 12.875 -1.652  3.122   0.15 16.93 ?  201 A1BAA A H7   1 
HETATM 6564 H H8   B A1BAA C 2 .   ? 10.863 -0.285  1.703   0.15 17.35 ?  201 A1BAA A H8   1 
HETATM 6565 H H10  B A1BAA C 2 .   ? 11.709 0.386   3.112   0.15 17.35 ?  201 A1BAA A H10  1 
HETATM 6566 H H9   B A1BAA C 2 .   ? 12.200 0.847   1.477   0.15 17.35 ?  201 A1BAA A H9   1 
HETATM 6567 H H12  B A1BAA C 2 .   ? 16.353 -1.579  2.092   0.15 15.79 ?  201 A1BAA A H12  1 
HETATM 6568 H H11  B A1BAA C 2 .   ? 15.390 -2.701  1.097   0.15 15.79 ?  201 A1BAA A H11  1 
HETATM 6569 H H15  B A1BAA C 2 .   ? 14.633 -0.951  6.558   0.15 15.52 ?  201 A1BAA A H15  1 
HETATM 6570 H H16  B A1BAA C 2 .   ? 15.524 3.935   2.879   0.15 15.25 ?  201 A1BAA A H16  1 
HETATM 6571 H H17  B A1BAA C 2 .   ? 15.891 5.302   5.183   0.15 15.00 ?  201 A1BAA A H17  1 
HETATM 6572 H H14  B A1BAA C 2 .   ? 15.050 1.246   1.587   0.15 16.82 ?  201 A1BAA A H14  1 
HETATM 6573 H H18  B A1BAA C 2 .   ? 15.638 3.758   7.030   0.15 15.25 ?  201 A1BAA A H18  1 
HETATM 6574 O O1   C A1BAA D 2 .   ? 14.812 -1.353  -0.342  0.15 16.14 ?  202 A1BAA A O1   1 
HETATM 6575 C C1   C A1BAA D 2 .   ? 13.392 2.300   0.046   0.15 14.62 ?  202 A1BAA A C1   1 
HETATM 6576 C C2   C A1BAA D 2 .   ? 13.203 0.781   0.002   0.15 14.53 ?  202 A1BAA A C2   1 
HETATM 6577 C C3   C A1BAA D 2 .   ? 13.651 0.052   1.336   0.15 14.44 ?  202 A1BAA A C3   1 
HETATM 6578 C C4   C A1BAA D 2 .   ? 12.365 -0.375  2.189   0.15 14.20 ?  202 A1BAA A C4   1 
HETATM 6579 C C5   C A1BAA D 2 .   ? 11.495 0.796   2.681   0.15 14.08 ?  202 A1BAA A C5   1 
HETATM 6580 C C6   C A1BAA D 2 .   ? 14.447 -1.299  1.020   0.15 15.38 ?  202 A1BAA A C6   1 
HETATM 6581 C C7   C A1BAA D 2 .   ? 14.790 1.041   3.545   0.15 12.79 ?  202 A1BAA A C7   1 
HETATM 6582 C C8   C A1BAA D 2 .   ? 14.856 -0.102  5.684   0.15 12.15 ?  202 A1BAA A C8   1 
HETATM 6583 C C10  C A1BAA D 2 .   ? 15.131 2.262   4.264   0.15 12.41 ?  202 A1BAA A C10  1 
HETATM 6584 C C11  C A1BAA D 2 .   ? 15.380 3.686   4.000   0.15 12.41 ?  202 A1BAA A C11  1 
HETATM 6585 C C12  C A1BAA D 2 .   ? 15.661 4.302   5.218   0.15 11.92 ?  202 A1BAA A C12  1 
HETATM 6586 C C9   C A1BAA D 2 .   ? 15.294 2.116   5.702   0.15 12.09 ?  202 A1BAA A C9   1 
HETATM 6587 N N1   C A1BAA D 2 .   ? 14.598 0.989   2.130   0.15 13.88 ?  202 A1BAA A N1   1 
HETATM 6588 N N2   C A1BAA D 2 .   ? 14.667 -0.117  4.308   0.15 12.74 ?  202 A1BAA A N2   1 
HETATM 6589 N N3   C A1BAA D 2 .   ? 15.171 0.961   6.445   0.15 11.94 ?  202 A1BAA A N3   1 
HETATM 6590 N N4   C A1BAA D 2 .   ? 15.605 3.350   6.174   0.15 12.05 ?  202 A1BAA A N4   1 
HETATM 6591 H H13  C A1BAA D 2 .   ? 15.334 -2.127  -0.540  0.15 19.36 ?  202 A1BAA A H13  1 
HETATM 6592 H H2   C A1BAA D 2 .   ? 12.734 2.813   -0.662  0.15 17.54 ?  202 A1BAA A H2   1 
HETATM 6593 H H1   C A1BAA D 2 .   ? 14.430 2.624   -0.214  0.15 17.54 ?  202 A1BAA A H1   1 
HETATM 6594 H H3   C A1BAA D 2 .   ? 13.195 2.717   1.047   0.15 17.54 ?  202 A1BAA A H3   1 
HETATM 6595 H H4   C A1BAA D 2 .   ? 13.765 0.391   -0.880  0.15 17.43 ?  202 A1BAA A H4   1 
HETATM 6596 H H5   C A1BAA D 2 .   ? 12.146 0.509   -0.226  0.15 17.43 ?  202 A1BAA A H5   1 
HETATM 6597 H H6   C A1BAA D 2 .   ? 12.687 -0.997  3.071   0.15 17.04 ?  202 A1BAA A H6   1 
HETATM 6598 H H7   C A1BAA D 2 .   ? 11.720 -1.088  1.602   0.15 17.04 ?  202 A1BAA A H7   1 
HETATM 6599 H H8   C A1BAA D 2 .   ? 11.752 1.117   3.710   0.15 16.89 ?  202 A1BAA A H8   1 
HETATM 6600 H H10  C A1BAA D 2 .   ? 10.421 0.523   2.695   0.15 16.89 ?  202 A1BAA A H10  1 
HETATM 6601 H H9   C A1BAA D 2 .   ? 11.565 1.706   2.056   0.15 16.89 ?  202 A1BAA A H9   1 
HETATM 6602 H H12  C A1BAA D 2 .   ? 15.350 -1.352  1.649   0.15 18.46 ?  202 A1BAA A H12  1 
HETATM 6603 H H11  C A1BAA D 2 .   ? 13.796 -2.181  1.287   0.15 18.46 ?  202 A1BAA A H11  1 
HETATM 6604 H H15  C A1BAA D 2 .   ? 14.735 -1.077  6.221   0.15 14.58 ?  202 A1BAA A H15  1 
HETATM 6605 H H16  C A1BAA D 2 .   ? 15.363 4.241   3.063   0.15 14.89 ?  202 A1BAA A H16  1 
HETATM 6606 H H17  C A1BAA D 2 .   ? 15.904 5.323   5.530   0.15 14.31 ?  202 A1BAA A H17  1 
HETATM 6607 H H14  C A1BAA D 2 .   ? 15.147 1.616   1.536   0.15 16.66 ?  202 A1BAA A H14  1 
HETATM 6608 H H18  C A1BAA D 2 .   ? 15.779 3.563   7.198   0.15 14.46 ?  202 A1BAA A H18  1 
HETATM 6609 O O    B HOH   E 3 .   ? 18.864 -0.508  -3.826  0.30 30.64 ?  301 HOH   A O    1 
HETATM 6610 O O    . HOH   E 3 .   ? 4.859  3.814   0.723   1.00 26.80 ?  302 HOH   A O    1 
HETATM 6611 O O    . HOH   E 3 .   ? 8.887  -12.069 17.255  1.00 43.35 ?  303 HOH   A O    1 
HETATM 6612 O O    . HOH   E 3 .   ? 17.137 -18.090 15.081  1.00 27.26 ?  304 HOH   A O    1 
HETATM 6613 O O    . HOH   E 3 .   ? 15.156 -12.235 18.755  1.00 35.04 ?  305 HOH   A O    1 
HETATM 6614 O O    . HOH   E 3 .   ? 6.961  -8.194  11.898  1.00 23.10 ?  306 HOH   A O    1 
HETATM 6615 O O    . HOH   E 3 .   ? 14.123 -4.500  -11.865 1.00 33.96 ?  307 HOH   A O    1 
HETATM 6616 O O    . HOH   E 3 .   ? 34.383 -1.890  12.504  1.00 38.51 ?  308 HOH   A O    1 
HETATM 6617 O O    . HOH   E 3 .   ? 28.915 0.464   -9.691  1.00 22.70 ?  309 HOH   A O    1 
HETATM 6618 O O    . HOH   E 3 .   ? 15.236 -21.613 14.235  1.00 18.30 ?  310 HOH   A O    1 
HETATM 6619 O O    . HOH   E 3 .   ? 7.683  -6.399  -6.647  1.00 40.53 ?  311 HOH   A O    1 
HETATM 6620 O O    A HOH   E 3 .   ? 14.804 -4.657  20.458  0.70 37.74 ?  312 HOH   A O    1 
HETATM 6621 O O    . HOH   E 3 .   ? 19.869 -12.403 -9.044  1.00 27.40 ?  313 HOH   A O    1 
HETATM 6622 O O    . HOH   E 3 .   ? 7.994  -12.519 -0.812  1.00 23.31 ?  314 HOH   A O    1 
HETATM 6623 O O    . HOH   E 3 .   ? 26.830 11.406  1.708   1.00 17.10 ?  315 HOH   A O    1 
HETATM 6624 O O    . HOH   E 3 .   ? -0.676 -8.325  2.266   1.00 48.59 ?  316 HOH   A O    1 
HETATM 6625 O O    . HOH   E 3 .   ? 20.077 4.579   -7.564  1.00 19.91 ?  317 HOH   A O    1 
HETATM 6626 O O    . HOH   E 3 .   ? 15.181 -8.030  -9.723  1.00 23.47 ?  318 HOH   A O    1 
HETATM 6627 O O    . HOH   E 3 .   ? 42.441 10.550  5.200   1.00 20.27 ?  319 HOH   A O    1 
HETATM 6628 O O    . HOH   E 3 .   ? 13.971 -4.967  17.490  1.00 26.49 ?  320 HOH   A O    1 
HETATM 6629 O O    . HOH   E 3 .   ? 0.815  -4.482  0.234   1.00 32.88 ?  321 HOH   A O    1 
HETATM 6630 O O    . HOH   E 3 .   ? 14.772 -14.003 16.748  1.00 23.12 ?  322 HOH   A O    1 
HETATM 6631 O O    . HOH   E 3 .   ? 14.952 3.756   17.756  1.00 39.65 ?  323 HOH   A O    1 
HETATM 6632 O O    . HOH   E 3 .   ? 36.173 -5.094  -0.544  1.00 28.72 ?  324 HOH   A O    1 
HETATM 6633 O O    B HOH   E 3 .   ? 14.823 7.219   7.331   0.30 19.12 ?  325 HOH   A O    1 
HETATM 6634 O O    . HOH   E 3 .   ? 30.250 -13.299 -8.561  1.00 20.48 ?  326 HOH   A O    1 
HETATM 6635 O O    . HOH   E 3 .   ? 28.245 -6.293  19.639  1.00 42.91 ?  327 HOH   A O    1 
HETATM 6636 O O    . HOH   E 3 .   ? 33.974 -0.978  -8.890  1.00 26.87 ?  328 HOH   A O    1 
HETATM 6637 O O    . HOH   E 3 .   ? 37.544 2.795   10.211  1.00 28.38 ?  329 HOH   A O    1 
HETATM 6638 O O    . HOH   E 3 .   ? 27.269 13.776  2.950   1.00 27.78 ?  330 HOH   A O    1 
HETATM 6639 O O    . HOH   E 3 .   ? 31.027 -18.168 7.776   1.00 20.75 ?  331 HOH   A O    1 
HETATM 6640 O O    . HOH   E 3 .   ? 22.410 5.307   19.057  1.00 44.15 ?  332 HOH   A O    1 
HETATM 6641 O O    . HOH   E 3 .   ? 18.860 -22.009 6.912   1.00 32.64 ?  333 HOH   A O    1 
HETATM 6642 O O    A HOH   E 3 .   ? 17.499 -1.721  0.485   0.70 20.83 ?  334 HOH   A O    1 
HETATM 6643 O O    . HOH   E 3 .   ? 11.669 -10.918 -10.085 1.00 42.54 ?  335 HOH   A O    1 
HETATM 6644 O O    . HOH   E 3 .   ? 8.068  -21.533 3.988   1.00 44.18 ?  336 HOH   A O    1 
HETATM 6645 O O    . HOH   E 3 .   ? 9.840  -21.364 5.712   1.00 20.16 ?  337 HOH   A O    1 
HETATM 6646 O O    . HOH   E 3 .   ? 10.425 -22.161 -1.201  1.00 46.38 ?  338 HOH   A O    1 
HETATM 6647 O O    . HOH   E 3 .   ? 28.294 -0.136  -13.371 1.00 36.43 ?  339 HOH   A O    1 
HETATM 6648 O O    . HOH   E 3 .   ? 22.291 -19.312 11.333  1.00 32.98 ?  340 HOH   A O    1 
HETATM 6649 O O    . HOH   E 3 .   ? 12.047 0.343   14.930  1.00 37.88 ?  341 HOH   A O    1 
HETATM 6650 O O    . HOH   E 3 .   ? 20.601 -19.706 -5.074  1.00 30.62 ?  342 HOH   A O    1 
HETATM 6651 O O    . HOH   E 3 .   ? 38.300 10.090  7.183   1.00 42.51 ?  343 HOH   A O    1 
HETATM 6652 O O    . HOH   E 3 .   ? 9.080  -10.225 19.407  1.00 42.78 ?  344 HOH   A O    1 
HETATM 6653 O O    . HOH   E 3 .   ? 38.572 4.952   6.969   1.00 15.77 ?  345 HOH   A O    1 
HETATM 6654 O O    A HOH   E 3 .   ? 14.640 -3.668  3.137   0.85 24.00 ?  346 HOH   A O    1 
HETATM 6655 O O    B HOH   E 3 .   ? 19.204 -2.091  0.328   0.30 27.20 ?  347 HOH   A O    1 
HETATM 6656 O O    . HOH   E 3 .   ? 17.144 -17.852 -5.021  1.00 27.92 ?  348 HOH   A O    1 
HETATM 6657 O O    . HOH   E 3 .   ? 37.183 -2.830  9.722   1.00 40.03 ?  349 HOH   A O    1 
HETATM 6658 O O    . HOH   E 3 .   ? 31.793 -9.319  -6.680  1.00 22.01 ?  350 HOH   A O    1 
HETATM 6659 O O    . HOH   E 3 .   ? 42.585 4.285   5.408   1.00 30.63 ?  351 HOH   A O    1 
HETATM 6660 O O    . HOH   E 3 .   ? 39.744 -1.009  -5.184  1.00 19.46 ?  352 HOH   A O    1 
HETATM 6661 O O    . HOH   E 3 .   ? 18.692 -19.439 13.581  1.00 35.99 ?  353 HOH   A O    1 
HETATM 6662 O O    . HOH   E 3 .   ? 35.776 -12.703 6.825   1.00 16.40 ?  354 HOH   A O    1 
HETATM 6663 O O    . HOH   E 3 .   ? 44.316 7.100   6.495   1.00 27.21 ?  355 HOH   A O    1 
HETATM 6664 O O    . HOH   E 3 .   ? 24.025 -2.104  -2.044  1.00 11.14 ?  356 HOH   A O    1 
HETATM 6665 O O    A HOH   E 3 .   ? 14.282 0.550   6.850   0.70 27.46 ?  357 HOH   A O    1 
HETATM 6666 O O    . HOH   E 3 .   ? 25.684 -0.774  -7.342  1.00 16.64 ?  358 HOH   A O    1 
HETATM 6667 O O    A HOH   E 3 .   ? -0.473 -3.108  3.150   0.70 32.67 ?  359 HOH   A O    1 
HETATM 6668 O O    . HOH   E 3 .   ? 21.886 -21.926 8.439   1.00 28.38 ?  360 HOH   A O    1 
HETATM 6669 O O    . HOH   E 3 .   ? 30.810 3.058   8.305   1.00 12.51 ?  361 HOH   A O    1 
HETATM 6670 O O    . HOH   E 3 .   ? 13.285 -1.403  -6.623  1.00 19.82 ?  362 HOH   A O    1 
HETATM 6671 O O    . HOH   E 3 .   ? 31.069 -13.945 -2.500  1.00 14.01 ?  363 HOH   A O    1 
HETATM 6672 O O    . HOH   E 3 .   ? 6.471  -5.624  11.241  1.00 22.38 ?  364 HOH   A O    1 
HETATM 6673 O O    . HOH   E 3 .   ? 31.693 8.172   14.910  1.00 23.77 ?  365 HOH   A O    1 
HETATM 6674 O O    . HOH   E 3 .   ? 14.345 -21.198 -4.299  1.00 30.87 ?  366 HOH   A O    1 
HETATM 6675 O O    . HOH   E 3 .   ? 16.484 -22.039 0.970   1.00 29.08 ?  367 HOH   A O    1 
HETATM 6676 O O    . HOH   E 3 .   ? 33.670 -7.162  4.291   1.00 16.80 ?  368 HOH   A O    1 
HETATM 6677 O O    . HOH   E 3 .   ? 13.579 -15.232 -7.527  1.00 28.03 ?  369 HOH   A O    1 
HETATM 6678 O O    . HOH   E 3 .   ? 23.989 3.930   -4.784  1.00 22.59 ?  370 HOH   A O    1 
HETATM 6679 O O    . HOH   E 3 .   ? 37.377 11.945  4.994   1.00 31.05 ?  371 HOH   A O    1 
HETATM 6680 O O    . HOH   E 3 .   ? 43.908 8.468   -3.074  1.00 26.25 ?  372 HOH   A O    1 
HETATM 6681 O O    B HOH   E 3 .   ? 21.169 2.691   -0.005  0.30 16.75 ?  373 HOH   A O    1 
HETATM 6682 O O    A HOH   E 3 .   ? 21.248 -2.397  -2.012  0.70 13.53 ?  374 HOH   A O    1 
HETATM 6683 O O    . HOH   E 3 .   ? 18.912 -0.684  -1.668  1.00 15.08 ?  375 HOH   A O    1 
HETATM 6684 O O    . HOH   E 3 .   ? 14.061 -23.057 7.440   1.00 18.87 ?  376 HOH   A O    1 
HETATM 6685 O O    . HOH   E 3 .   ? 17.010 -19.288 4.909   1.00 16.18 ?  377 HOH   A O    1 
HETATM 6686 O O    . HOH   E 3 .   ? 43.361 7.821   2.728   1.00 24.82 ?  378 HOH   A O    1 
HETATM 6687 O O    . HOH   E 3 .   ? 18.513 9.392   9.033   1.00 22.75 ?  379 HOH   A O    1 
HETATM 6688 O O    . HOH   E 3 .   ? 27.539 -10.679 14.076  1.00 17.95 ?  380 HOH   A O    1 
HETATM 6689 O O    . HOH   E 3 .   ? 27.910 0.842   -7.142  1.00 14.33 ?  381 HOH   A O    1 
HETATM 6690 O O    . HOH   E 3 .   ? 3.454  -9.294  9.902   1.00 35.06 ?  382 HOH   A O    1 
HETATM 6691 O O    . HOH   E 3 .   ? 24.737 -17.587 12.742  1.00 24.95 ?  383 HOH   A O    1 
HETATM 6692 O O    . HOH   E 3 .   ? 24.398 3.572   -1.786  1.00 15.80 ?  384 HOH   A O    1 
HETATM 6693 O O    . HOH   E 3 .   ? 22.748 12.511  1.688   1.00 15.49 ?  385 HOH   A O    1 
HETATM 6694 O O    B HOH   E 3 .   ? 21.286 -2.057  -2.567  0.30 13.91 ?  386 HOH   A O    1 
HETATM 6695 O O    . HOH   E 3 .   ? 31.741 -7.293  -9.866  1.00 22.11 ?  387 HOH   A O    1 
HETATM 6696 O O    . HOH   E 3 .   ? 22.690 -12.010 21.884  1.00 43.58 ?  388 HOH   A O    1 
HETATM 6697 O O    . HOH   E 3 .   ? 21.223 10.237  15.102  1.00 35.38 ?  389 HOH   A O    1 
HETATM 6698 O O    . HOH   E 3 .   ? 15.494 11.905  7.950   1.00 36.71 ?  390 HOH   A O    1 
HETATM 6699 O O    . HOH   E 3 .   ? 14.413 -24.711 11.636  1.00 32.33 ?  391 HOH   A O    1 
HETATM 6700 O O    . HOH   E 3 .   ? 24.336 -7.839  14.502  1.00 18.09 ?  392 HOH   A O    1 
HETATM 6701 O O    . HOH   E 3 .   ? 26.943 4.151   -0.613  1.00 12.94 ?  393 HOH   A O    1 
HETATM 6702 O O    A HOH   E 3 .   ? 15.880 2.138   24.840  0.70 37.53 ?  394 HOH   A O    1 
HETATM 6703 O O    . HOH   E 3 .   ? 27.387 2.292   18.750  1.00 31.63 ?  395 HOH   A O    1 
HETATM 6704 O O    . HOH   E 3 .   ? 32.777 -9.267  5.933   1.00 20.30 ?  396 HOH   A O    1 
HETATM 6705 O O    . HOH   E 3 .   ? 14.482 -0.471  -12.134 1.00 26.31 ?  397 HOH   A O    1 
HETATM 6706 O O    . HOH   E 3 .   ? 27.529 -6.220  -14.066 1.00 39.40 ?  398 HOH   A O    1 
HETATM 6707 O O    . HOH   E 3 .   ? 37.546 -2.016  5.746   1.00 26.48 ?  399 HOH   A O    1 
HETATM 6708 O O    . HOH   E 3 .   ? 18.439 4.911   -15.120 1.00 50.23 ?  400 HOH   A O    1 
HETATM 6709 O O    A HOH   E 3 .   ? 24.580 2.052   -6.939  0.70 16.42 ?  401 HOH   A O    1 
HETATM 6710 O O    . HOH   E 3 .   ? 41.592 1.513   4.923   1.00 34.95 ?  402 HOH   A O    1 
HETATM 6711 O O    A HOH   E 3 .   ? 15.806 -0.965  5.316   0.70 35.73 ?  403 HOH   A O    1 
HETATM 6712 O O    . HOH   E 3 .   ? 11.697 -10.813 17.279  1.00 28.38 ?  404 HOH   A O    1 
HETATM 6713 O O    . HOH   E 3 .   ? 16.004 6.936   2.915   1.00 19.38 ?  405 HOH   A O    1 
HETATM 6714 O O    . HOH   E 3 .   ? 30.754 1.810   16.726  1.00 22.72 ?  406 HOH   A O    1 
HETATM 6715 O O    . HOH   E 3 .   ? 23.453 11.366  4.155   1.00 13.13 ?  407 HOH   A O    1 
HETATM 6716 O O    A HOH   E 3 .   ? 21.350 3.151   -0.296  0.70 11.94 ?  408 HOH   A O    1 
HETATM 6717 O O    . HOH   E 3 .   ? 23.931 -15.679 -9.154  1.00 33.43 ?  409 HOH   A O    1 
HETATM 6718 O O    . HOH   E 3 .   ? 40.906 -8.289  -6.722  1.00 36.81 ?  410 HOH   A O    1 
HETATM 6719 O O    . HOH   E 3 .   ? 20.563 -20.037 2.740   1.00 18.21 ?  411 HOH   A O    1 
HETATM 6720 O O    . HOH   E 3 .   ? 38.101 -1.351  -1.954  1.00 19.23 ?  412 HOH   A O    1 
HETATM 6721 O O    . HOH   E 3 .   ? 21.691 -13.823 -8.211  1.00 41.75 ?  413 HOH   A O    1 
HETATM 6722 O O    . HOH   E 3 .   ? 30.942 6.202   -12.287 1.00 29.71 ?  414 HOH   A O    1 
HETATM 6723 O O    . HOH   E 3 .   ? 16.281 16.706  8.697   1.00 31.26 ?  415 HOH   A O    1 
HETATM 6724 O O    . HOH   E 3 .   ? 30.101 -10.165 13.020  1.00 21.79 ?  416 HOH   A O    1 
HETATM 6725 O O    . HOH   E 3 .   ? 23.919 -20.283 -1.377  1.00 16.77 ?  417 HOH   A O    1 
HETATM 6726 O O    A HOH   E 3 .   ? 11.045 1.513   12.806  0.70 22.85 ?  418 HOH   A O    1 
HETATM 6727 O O    . HOH   E 3 .   ? 35.002 -5.217  -3.093  1.00 17.98 ?  419 HOH   A O    1 
HETATM 6728 O O    . HOH   E 3 .   ? 28.539 -10.591 -14.018 1.00 46.28 ?  420 HOH   A O    1 
HETATM 6729 O O    A HOH   E 3 .   ? 11.071 -0.392  1.984   0.70 30.37 ?  421 HOH   A O    1 
HETATM 6730 O O    . HOH   E 3 .   ? 10.423 -13.739 -1.669  1.00 19.33 ?  422 HOH   A O    1 
HETATM 6731 O O    . HOH   E 3 .   ? 30.394 -12.985 13.478  1.00 20.51 ?  423 HOH   A O    1 
HETATM 6732 O O    . HOH   E 3 .   ? 32.549 -10.627 3.175   1.00 31.45 ?  424 HOH   A O    1 
HETATM 6733 O O    . HOH   E 3 .   ? 44.950 -0.634  3.005   1.00 39.94 ?  425 HOH   A O    1 
HETATM 6734 O O    . HOH   E 3 .   ? 6.700  -3.352  13.013  1.00 30.79 ?  426 HOH   A O    1 
HETATM 6735 O O    . HOH   E 3 .   ? 5.233  2.769   5.162   1.00 33.65 ?  427 HOH   A O    1 
HETATM 6736 O O    . HOH   E 3 .   ? 16.244 -14.271 20.297  1.00 45.53 ?  428 HOH   A O    1 
HETATM 6737 O O    . HOH   E 3 .   ? 36.736 -4.985  5.386   1.00 24.69 ?  429 HOH   A O    1 
HETATM 6738 O O    . HOH   E 3 .   ? 27.137 -3.277  19.398  1.00 36.59 ?  430 HOH   A O    1 
HETATM 6739 O O    . HOH   E 3 .   ? 32.656 -4.297  -9.909  1.00 28.72 ?  431 HOH   A O    1 
HETATM 6740 O O    B HOH   E 3 .   ? 11.891 -1.950  -3.646  0.30 14.74 ?  432 HOH   A O    1 
HETATM 6741 O O    A HOH   E 3 .   ? 18.565 -2.429  -16.298 0.70 35.25 ?  433 HOH   A O    1 
HETATM 6742 O O    . HOH   E 3 .   ? 22.673 8.049   18.436  1.00 45.35 ?  434 HOH   A O    1 
HETATM 6743 O O    B HOH   E 3 .   ? 10.822 2.419   12.278  0.30 23.58 ?  435 HOH   A O    1 
HETATM 6744 O O    B HOH   E 3 .   ? 12.096 6.795   10.381  0.30 26.02 ?  436 HOH   A O    1 
HETATM 6745 O O    . HOH   E 3 .   ? 18.434 -16.042 16.391  1.00 37.67 ?  437 HOH   A O    1 
HETATM 6746 O O    . HOH   E 3 .   ? 21.489 -14.781 18.040  1.00 52.06 ?  438 HOH   A O    1 
HETATM 6747 O O    . HOH   E 3 .   ? 37.732 -8.838  -3.503  1.00 24.89 ?  439 HOH   A O    1 
HETATM 6748 O O    A HOH   E 3 .   ? 16.259 2.945   -1.386  0.70 14.31 ?  440 HOH   A O    1 
HETATM 6749 O O    A HOH   E 3 .   ? 18.865 2.029   -0.700  0.70 12.41 ?  441 HOH   A O    1 
HETATM 6750 O O    . HOH   E 3 .   ? 23.604 -8.112  17.099  1.00 22.61 ?  442 HOH   A O    1 
HETATM 6751 O O    . HOH   E 3 .   ? 23.297 -20.970 1.289   1.00 18.39 ?  443 HOH   A O    1 
HETATM 6752 O O    . HOH   E 3 .   ? 20.577 -17.807 24.829  1.00 48.51 ?  444 HOH   A O    1 
HETATM 6753 O O    . HOH   E 3 .   ? 34.408 -8.088  -0.554  1.00 27.23 ?  445 HOH   A O    1 
HETATM 6754 O O    . HOH   E 3 .   ? 9.471  -16.237 -2.022  1.00 38.00 ?  446 HOH   A O    1 
HETATM 6755 O O    . HOH   E 3 .   ? 23.213 7.590   -3.185  1.00 31.63 ?  447 HOH   A O    1 
HETATM 6756 O O    . HOH   E 3 .   ? 30.579 14.757  2.856   1.00 18.77 ?  448 HOH   A O    1 
HETATM 6757 O O    . HOH   E 3 .   ? 31.328 -12.798 -0.007  1.00 19.54 ?  449 HOH   A O    1 
HETATM 6758 O O    . HOH   E 3 .   ? 29.850 -16.068 10.645  1.00 37.57 ?  450 HOH   A O    1 
HETATM 6759 O O    A HOH   E 3 .   ? 14.032 -0.354  3.510   0.70 30.88 ?  451 HOH   A O    1 
HETATM 6760 O O    . HOH   E 3 .   ? 27.779 6.980   -6.386  1.00 35.86 ?  452 HOH   A O    1 
HETATM 6761 O O    . HOH   E 3 .   ? -1.467 -4.961  7.755   1.00 45.45 ?  453 HOH   A O    1 
HETATM 6762 O O    A HOH   E 3 .   ? 19.331 -11.104 24.172  0.70 45.20 ?  454 HOH   A O    1 
HETATM 6763 O O    B HOH   E 3 .   ? 7.338  1.714   7.457   0.30 29.40 ?  455 HOH   A O    1 
HETATM 6764 O O    B HOH   E 3 .   ? 18.525 1.459   -0.466  0.30 19.71 ?  456 HOH   A O    1 
HETATM 6765 O O    . HOH   E 3 .   ? 25.435 8.252   -4.758  1.00 25.55 ?  457 HOH   A O    1 
HETATM 6766 O O    . HOH   E 3 .   ? 32.498 -15.959 10.844  1.00 36.49 ?  458 HOH   A O    1 
HETATM 6767 O O    . HOH   E 3 .   ? 29.884 -1.938  -12.679 1.00 44.79 ?  459 HOH   A O    1 
HETATM 6768 O O    . HOH   E 3 .   ? 19.908 -17.331 -5.101  1.00 25.07 ?  460 HOH   A O    1 
HETATM 6769 O O    . HOH   E 3 .   ? 21.704 -9.126  21.507  1.00 52.19 ?  461 HOH   A O    1 
HETATM 6770 O O    B HOH   E 3 .   ? 15.821 3.279   -1.559  0.30 14.14 ?  462 HOH   A O    1 
HETATM 6771 O O    . HOH   E 3 .   ? 24.911 5.616   20.809  1.00 54.35 ?  463 HOH   A O    1 
HETATM 6772 O O    . HOH   E 3 .   ? 23.209 -22.365 -3.347  1.00 35.21 ?  464 HOH   A O    1 
HETATM 6773 O O    . HOH   E 3 .   ? 24.602 14.554  7.882   1.00 35.74 ?  465 HOH   A O    1 
HETATM 6774 O O    . HOH   E 3 .   ? 11.031 -14.939 -6.081  1.00 35.23 ?  466 HOH   A O    1 
HETATM 6775 O O    . HOH   E 3 .   ? 26.898 11.621  -1.293  1.00 29.93 ?  467 HOH   A O    1 
HETATM 6776 O O    B HOH   E 3 .   ? 15.273 3.947   0.986   0.30 30.77 ?  468 HOH   A O    1 
HETATM 6777 O O    . HOH   E 3 .   ? 21.940 5.233   -5.862  1.00 29.08 ?  469 HOH   A O    1 
HETATM 6778 O O    . HOH   E 3 .   ? 39.613 -7.046  -3.530  1.00 46.45 ?  470 HOH   A O    1 
HETATM 6779 O O    . HOH   E 3 .   ? 27.495 -11.412 16.573  1.00 39.38 ?  471 HOH   A O    1 
HETATM 6780 O O    . HOH   E 3 .   ? 15.719 -21.504 3.692   1.00 23.35 ?  472 HOH   A O    1 
HETATM 6781 O O    . HOH   E 3 .   ? 8.208  -2.963  -5.749  1.00 48.35 ?  473 HOH   A O    1 
HETATM 6782 O O    . HOH   E 3 .   ? 18.746 10.782  11.383  1.00 34.17 ?  474 HOH   A O    1 
HETATM 6783 O O    . HOH   E 3 .   ? 11.953 -13.463 16.363  1.00 48.60 ?  475 HOH   A O    1 
HETATM 6784 O O    . HOH   E 3 .   ? 18.107 -16.252 -8.772  1.00 42.52 ?  476 HOH   A O    1 
HETATM 6785 O O    . HOH   E 3 .   ? 12.403 1.562   17.396  1.00 42.20 ?  477 HOH   A O    1 
HETATM 6786 O O    . HOH   E 3 .   ? 25.853 10.789  -3.679  1.00 24.97 ?  478 HOH   A O    1 
HETATM 6787 O O    . HOH   E 3 .   ? 23.486 13.708  5.552   1.00 19.72 ?  479 HOH   A O    1 
HETATM 6788 O O    . HOH   E 3 .   ? 35.193 7.387   12.268  1.00 51.22 ?  480 HOH   A O    1 
HETATM 6789 O O    . HOH   E 3 .   ? 16.866 -20.614 16.148  1.00 30.26 ?  481 HOH   A O    1 
HETATM 6790 O O    . HOH   E 3 .   ? 16.013 -6.678  -11.831 1.00 44.68 ?  482 HOH   A O    1 
HETATM 6791 O O    . HOH   E 3 .   ? 28.935 8.937   17.526  1.00 35.54 ?  483 HOH   A O    1 
HETATM 6792 O O    . HOH   E 3 .   ? 23.122 11.801  -4.052  1.00 19.91 ?  484 HOH   A O    1 
HETATM 6793 O O    . HOH   E 3 .   ? 17.342 -18.696 19.813  1.00 50.01 ?  485 HOH   A O    1 
HETATM 6794 O O    . HOH   E 3 .   ? 15.736 -17.136 -6.965  1.00 32.78 ?  486 HOH   A O    1 
HETATM 6795 O O    B HOH   E 3 .   ? 10.755 -1.684  -6.073  0.30 20.38 ?  487 HOH   A O    1 
HETATM 6796 O O    . HOH   E 3 .   ? 30.873 0.667   19.201  1.00 40.08 ?  488 HOH   A O    1 
HETATM 6797 O O    . HOH   E 3 .   ? 14.018 -10.310 -10.902 1.00 32.97 ?  489 HOH   A O    1 
HETATM 6798 O O    . HOH   E 3 .   ? 40.964 -3.987  -0.377  1.00 37.62 ?  490 HOH   A O    1 
HETATM 6799 O O    . HOH   E 3 .   ? 28.563 -4.667  -12.237 1.00 41.19 ?  491 HOH   A O    1 
HETATM 6800 O O    . HOH   E 3 .   ? 23.315 -12.900 19.388  1.00 44.35 ?  492 HOH   A O    1 
HETATM 6801 O O    . HOH   E 3 .   ? 44.498 10.440  -1.601  1.00 32.35 ?  493 HOH   A O    1 
HETATM 6802 O O    . HOH   E 3 .   ? 31.443 -0.581  -10.547 1.00 27.10 ?  494 HOH   A O    1 
HETATM 6803 O O    . HOH   E 3 .   ? 41.662 9.288   -4.096  1.00 31.40 ?  495 HOH   A O    1 
HETATM 6804 O O    . HOH   E 3 .   ? 28.729 -7.936  -15.263 1.00 48.17 ?  496 HOH   A O    1 
HETATM 6805 O O    . HOH   E 3 .   ? 39.195 2.381   7.506   1.00 31.83 ?  497 HOH   A O    1 
HETATM 6806 O O    . HOH   E 3 .   ? 18.530 -23.225 1.848   1.00 43.21 ?  498 HOH   A O    1 
HETATM 6807 O O    . HOH   E 3 .   ? 14.029 -25.307 8.926   1.00 29.00 ?  499 HOH   A O    1 
HETATM 6808 O O    . HOH   E 3 .   ? 40.493 -0.237  -7.815  1.00 34.74 ?  500 HOH   A O    1 
HETATM 6809 O O    . HOH   E 3 .   ? 16.146 -23.377 5.752   1.00 29.38 ?  501 HOH   A O    1 
HETATM 6810 O O    . HOH   E 3 .   ? 19.995 -22.348 4.179   1.00 29.40 ?  502 HOH   A O    1 
HETATM 6811 O O    B HOH   E 3 .   ? 14.712 7.643   4.693   0.30 24.48 ?  503 HOH   A O    1 
HETATM 6812 O O    . HOH   E 3 .   ? 30.664 -5.758  -11.813 1.00 50.80 ?  504 HOH   A O    1 
HETATM 6813 O O    . HOH   E 3 .   ? 23.191 -23.792 1.691   1.00 31.00 ?  505 HOH   A O    1 
HETATM 6814 O O    . HOH   E 3 .   ? 37.423 -6.641  7.536   1.00 24.17 ?  506 HOH   A O    1 
HETATM 6815 O O    . HOH   E 3 .   ? 30.750 5.797   -14.717 1.00 37.81 ?  507 HOH   A O    1 
HETATM 6816 O O    . HOH   E 3 .   ? 20.506 -16.019 -7.398  1.00 29.76 ?  508 HOH   A O    1 
HETATM 6817 O O    . HOH   E 3 .   ? 39.573 -0.002  6.604   1.00 30.80 ?  509 HOH   A O    1 
HETATM 6818 O O    . HOH   E 3 .   ? 38.025 13.876  6.767   1.00 43.52 ?  510 HOH   A O    1 
HETATM 6819 O O    . HOH   E 3 .   ? 28.997 14.410  0.948   1.00 50.21 ?  511 HOH   A O    1 
HETATM 6820 O O    . HOH   E 3 .   ? 22.015 -24.057 4.464   1.00 26.17 ?  512 HOH   A O    1 
HETATM 6821 O O    . HOH   E 3 .   ? 36.483 -6.534  10.145  1.00 42.47 ?  513 HOH   A O    1 
HETATM 6822 O O    . HOH   E 3 .   ? 17.242 -6.640  -14.265 1.00 41.50 ?  514 HOH   A O    1 
HETATM 6823 O O    A HOH   E 3 .   ? 14.854 8.632   4.959   0.70 36.79 ?  515 HOH   A O    1 
HETATM 6824 O O    . HOH   E 3 .   ? 15.890 -12.306 27.426  1.00 43.53 ?  516 HOH   A O    1 
HETATM 6825 O O    . HOH   E 3 .   ? 24.033 8.957   -7.195  1.00 36.42 ?  517 HOH   A O    1 
HETATM 6826 O O    . HOH   E 3 .   ? 16.375 -21.146 18.724  1.00 35.26 ?  518 HOH   A O    1 
HETATM 6827 O O    . HOH   E 3 .   ? 14.665 -22.791 19.817  1.00 36.63 ?  519 HOH   A O    1 
HETATM 6828 O O    . HOH   F 3 .   ? 29.836 -22.441 5.432   1.00 21.05 ?  201 HOH   B O    1 
HETATM 6829 O O    . HOH   F 3 .   ? 48.119 -6.897  15.576  1.00 37.25 ?  202 HOH   B O    1 
HETATM 6830 O O    . HOH   F 3 .   ? 47.412 -7.473  -3.982  1.00 40.18 ?  203 HOH   B O    1 
HETATM 6831 O O    . HOH   F 3 .   ? 41.880 -35.933 -17.341 1.00 30.08 ?  204 HOH   B O    1 
HETATM 6832 O O    . HOH   F 3 .   ? 49.461 -22.648 -19.756 1.00 48.11 ?  205 HOH   B O    1 
HETATM 6833 O O    . HOH   F 3 .   ? 27.838 -41.784 -15.170 1.00 35.53 ?  206 HOH   B O    1 
HETATM 6834 O O    . HOH   F 3 .   ? 59.167 -18.744 6.798   1.00 38.62 ?  207 HOH   B O    1 
HETATM 6835 O O    . HOH   F 3 .   ? 27.751 -29.206 -1.900  1.00 35.59 ?  208 HOH   B O    1 
HETATM 6836 O O    . HOH   F 3 .   ? 52.955 -13.448 -20.392 1.00 39.05 ?  209 HOH   B O    1 
HETATM 6837 O O    . HOH   F 3 .   ? 38.012 -39.458 -0.200  1.00 40.27 ?  210 HOH   B O    1 
HETATM 6838 O O    . HOH   F 3 .   ? 41.413 -7.740  5.467   1.00 39.74 ?  211 HOH   B O    1 
HETATM 6839 O O    . HOH   F 3 .   ? 56.363 -19.723 7.285   1.00 33.65 ?  212 HOH   B O    1 
HETATM 6840 O O    . HOH   F 3 .   ? 29.886 -26.325 3.983   1.00 28.53 ?  213 HOH   B O    1 
HETATM 6841 O O    . HOH   F 3 .   ? 54.493 -9.339  -8.787  1.00 19.00 ?  214 HOH   B O    1 
HETATM 6842 O O    . HOH   F 3 .   ? 58.216 -12.961 8.395   1.00 33.00 ?  215 HOH   B O    1 
HETATM 6843 O O    . HOH   F 3 .   ? 30.224 -41.025 -8.180  1.00 16.53 ?  216 HOH   B O    1 
HETATM 6844 O O    . HOH   F 3 .   ? 50.250 -3.363  7.205   1.00 33.68 ?  217 HOH   B O    1 
HETATM 6845 O O    . HOH   F 3 .   ? 26.475 -19.347 -1.798  1.00 14.50 ?  218 HOH   B O    1 
HETATM 6846 O O    . HOH   F 3 .   ? 57.743 -24.438 5.047   1.00 34.98 ?  219 HOH   B O    1 
HETATM 6847 O O    . HOH   F 3 .   ? 29.783 -34.178 -0.491  1.00 35.34 ?  220 HOH   B O    1 
HETATM 6848 O O    . HOH   F 3 .   ? 56.711 -30.761 -7.777  1.00 30.38 ?  221 HOH   B O    1 
HETATM 6849 O O    . HOH   F 3 .   ? 44.464 -7.252  2.142   1.00 32.48 ?  222 HOH   B O    1 
HETATM 6850 O O    . HOH   F 3 .   ? 50.691 -6.107  0.234   1.00 27.09 ?  223 HOH   B O    1 
HETATM 6851 O O    . HOH   F 3 .   ? 57.221 -26.862 -7.666  1.00 40.90 ?  224 HOH   B O    1 
HETATM 6852 O O    . HOH   F 3 .   ? 37.184 -19.737 -18.091 1.00 39.08 ?  225 HOH   B O    1 
HETATM 6853 O O    . HOH   F 3 .   ? 57.427 -16.231 -12.180 1.00 19.35 ?  226 HOH   B O    1 
HETATM 6854 O O    . HOH   F 3 .   ? 35.970 -43.221 -8.553  1.00 30.20 ?  227 HOH   B O    1 
HETATM 6855 O O    . HOH   F 3 .   ? 55.423 -16.459 -14.312 1.00 35.94 ?  228 HOH   B O    1 
HETATM 6856 O O    . HOH   F 3 .   ? 45.165 -34.912 6.828   1.00 39.54 ?  229 HOH   B O    1 
HETATM 6857 O O    . HOH   F 3 .   ? 39.320 -10.910 6.112   1.00 26.17 ?  230 HOH   B O    1 
HETATM 6858 O O    . HOH   F 3 .   ? 30.826 -28.778 4.234   1.00 24.63 ?  231 HOH   B O    1 
HETATM 6859 O O    . HOH   F 3 .   ? 48.560 -36.462 -15.515 1.00 41.02 ?  232 HOH   B O    1 
HETATM 6860 O O    . HOH   F 3 .   ? 34.548 -36.365 -7.235  1.00 17.90 ?  233 HOH   B O    1 
HETATM 6861 O O    . HOH   F 3 .   ? 35.091 -7.999  -3.046  1.00 18.74 ?  234 HOH   B O    1 
HETATM 6862 O O    . HOH   F 3 .   ? 28.395 -19.626 -13.115 1.00 24.29 ?  235 HOH   B O    1 
HETATM 6863 O O    . HOH   F 3 .   ? 41.359 -9.663  13.087  1.00 22.25 ?  236 HOH   B O    1 
HETATM 6864 O O    . HOH   F 3 .   ? 40.639 -16.044 14.160  1.00 25.13 ?  237 HOH   B O    1 
HETATM 6865 O O    . HOH   F 3 .   ? 50.734 -12.966 -0.470  1.00 12.54 ?  238 HOH   B O    1 
HETATM 6866 O O    . HOH   F 3 .   ? 44.985 -43.537 -10.552 1.00 27.73 ?  239 HOH   B O    1 
HETATM 6867 O O    . HOH   F 3 .   ? 41.504 -39.161 -14.957 1.00 21.98 ?  240 HOH   B O    1 
HETATM 6868 O O    . HOH   F 3 .   ? 51.672 -6.510  4.453   1.00 19.41 ?  241 HOH   B O    1 
HETATM 6869 O O    . HOH   F 3 .   ? 48.085 -24.525 -17.756 1.00 30.61 ?  242 HOH   B O    1 
HETATM 6870 O O    . HOH   F 3 .   ? 32.841 -43.807 -11.374 1.00 19.77 ?  243 HOH   B O    1 
HETATM 6871 O O    . HOH   F 3 .   ? 39.505 -11.146 0.327   1.00 17.51 ?  244 HOH   B O    1 
HETATM 6872 O O    . HOH   F 3 .   ? 46.414 -1.597  13.298  1.00 27.52 ?  245 HOH   B O    1 
HETATM 6873 O O    . HOH   F 3 .   ? 25.429 -25.970 -1.391  1.00 32.14 ?  246 HOH   B O    1 
HETATM 6874 O O    . HOH   F 3 .   ? 42.638 -22.882 3.838   1.00 12.05 ?  247 HOH   B O    1 
HETATM 6875 O O    . HOH   F 3 .   ? 43.119 -43.240 -8.298  1.00 29.71 ?  248 HOH   B O    1 
HETATM 6876 O O    . HOH   F 3 .   ? 51.540 -13.858 10.971  1.00 28.00 ?  249 HOH   B O    1 
HETATM 6877 O O    . HOH   F 3 .   ? 41.870 -23.545 9.282   1.00 16.75 ?  250 HOH   B O    1 
HETATM 6878 O O    . HOH   F 3 .   ? 57.650 -24.380 -3.808  1.00 22.16 ?  251 HOH   B O    1 
HETATM 6879 O O    . HOH   F 3 .   ? 42.582 -25.381 2.625   1.00 15.60 ?  252 HOH   B O    1 
HETATM 6880 O O    . HOH   F 3 .   ? 43.232 -32.378 -17.101 1.00 23.13 ?  253 HOH   B O    1 
HETATM 6881 O O    . HOH   F 3 .   ? 40.345 -12.745 -11.548 1.00 15.54 ?  254 HOH   B O    1 
HETATM 6882 O O    . HOH   F 3 .   ? 34.206 -18.567 11.405  1.00 23.54 ?  255 HOH   B O    1 
HETATM 6883 O O    . HOH   F 3 .   ? 38.473 -11.043 -2.247  1.00 19.45 ?  256 HOH   B O    1 
HETATM 6884 O O    . HOH   F 3 .   ? 44.551 -27.778 -0.744  1.00 22.78 ?  257 HOH   B O    1 
HETATM 6885 O O    . HOH   F 3 .   ? 29.729 -25.229 -10.852 1.00 16.77 ?  258 HOH   B O    1 
HETATM 6886 O O    . HOH   F 3 .   ? 27.149 -31.832 -10.009 1.00 21.69 ?  259 HOH   B O    1 
HETATM 6887 O O    . HOH   F 3 .   ? 34.863 -24.643 13.846  1.00 27.50 ?  260 HOH   B O    1 
HETATM 6888 O O    . HOH   F 3 .   ? 50.976 -39.984 -8.270  1.00 31.50 ?  261 HOH   B O    1 
HETATM 6889 O O    . HOH   F 3 .   ? 30.860 -15.741 2.626   1.00 14.12 ?  262 HOH   B O    1 
HETATM 6890 O O    . HOH   F 3 .   ? 33.521 -17.008 8.046   1.00 19.98 ?  263 HOH   B O    1 
HETATM 6891 O O    . HOH   F 3 .   ? 58.191 -10.595 -4.055  1.00 20.66 ?  264 HOH   B O    1 
HETATM 6892 O O    . HOH   F 3 .   ? 56.944 -8.646  8.422   1.00 20.36 ?  265 HOH   B O    1 
HETATM 6893 O O    . HOH   F 3 .   ? 31.815 -17.924 -14.540 1.00 29.55 ?  266 HOH   B O    1 
HETATM 6894 O O    . HOH   F 3 .   ? 46.636 -31.275 -4.839  1.00 18.49 ?  267 HOH   B O    1 
HETATM 6895 O O    . HOH   F 3 .   ? 42.364 -9.916  9.379   1.00 20.96 ?  268 HOH   B O    1 
HETATM 6896 O O    . HOH   F 3 .   ? 48.009 -22.767 5.827   1.00 17.58 ?  269 HOH   B O    1 
HETATM 6897 O O    . HOH   F 3 .   ? 57.482 -9.220  1.413   1.00 20.14 ?  270 HOH   B O    1 
HETATM 6898 O O    . HOH   F 3 .   ? 49.334 -28.714 -6.921  1.00 15.87 ?  271 HOH   B O    1 
HETATM 6899 O O    . HOH   F 3 .   ? 28.268 -34.361 -9.460  1.00 20.89 ?  272 HOH   B O    1 
HETATM 6900 O O    . HOH   F 3 .   ? 56.204 -23.505 -14.727 1.00 27.08 ?  273 HOH   B O    1 
HETATM 6901 O O    . HOH   F 3 .   ? 43.386 -15.784 -12.181 1.00 14.47 ?  274 HOH   B O    1 
HETATM 6902 O O    . HOH   F 3 .   ? 34.938 -33.355 -19.253 1.00 28.79 ?  275 HOH   B O    1 
HETATM 6903 O O    . HOH   F 3 .   ? 30.653 -42.251 -10.654 1.00 29.01 ?  276 HOH   B O    1 
HETATM 6904 O O    . HOH   F 3 .   ? 49.823 -0.495  10.263  1.00 30.39 ?  277 HOH   B O    1 
HETATM 6905 O O    . HOH   F 3 .   ? 41.166 -5.589  11.566  1.00 45.82 ?  278 HOH   B O    1 
HETATM 6906 O O    . HOH   F 3 .   ? 38.890 -12.046 12.394  1.00 33.57 ?  279 HOH   B O    1 
HETATM 6907 O O    . HOH   F 3 .   ? 34.470 -12.793 2.620   1.00 25.41 ?  280 HOH   B O    1 
HETATM 6908 O O    . HOH   F 3 .   ? 27.967 -22.882 -8.022  1.00 17.77 ?  281 HOH   B O    1 
HETATM 6909 O O    . HOH   F 3 .   ? 42.891 -20.333 -20.779 1.00 38.68 ?  282 HOH   B O    1 
HETATM 6910 O O    . HOH   F 3 .   ? 28.468 -30.792 -14.776 1.00 29.34 ?  283 HOH   B O    1 
HETATM 6911 O O    . HOH   F 3 .   ? 57.126 -12.073 12.358  1.00 35.86 ?  284 HOH   B O    1 
HETATM 6912 O O    . HOH   F 3 .   ? 46.871 -29.585 9.816   1.00 32.47 ?  285 HOH   B O    1 
HETATM 6913 O O    . HOH   F 3 .   ? 42.395 -34.714 3.750   1.00 25.68 ?  286 HOH   B O    1 
HETATM 6914 O O    . HOH   F 3 .   ? 48.428 -25.062 3.082   1.00 13.44 ?  287 HOH   B O    1 
HETATM 6915 O O    . HOH   F 3 .   ? 33.548 -15.314 -13.997 1.00 21.37 ?  288 HOH   B O    1 
HETATM 6916 O O    . HOH   F 3 .   ? 36.827 -12.775 -1.515  1.00 26.75 ?  289 HOH   B O    1 
HETATM 6917 O O    . HOH   F 3 .   ? 48.729 -20.047 5.927   1.00 14.15 ?  290 HOH   B O    1 
HETATM 6918 O O    . HOH   F 3 .   ? 47.096 -33.988 -4.641  1.00 17.09 ?  291 HOH   B O    1 
HETATM 6919 O O    . HOH   F 3 .   ? 27.584 -26.759 -15.730 1.00 32.28 ?  292 HOH   B O    1 
HETATM 6920 O O    . HOH   F 3 .   ? 48.164 -32.596 -16.574 1.00 42.49 ?  293 HOH   B O    1 
HETATM 6921 O O    . HOH   F 3 .   ? 45.922 -40.399 -3.645  1.00 28.62 ?  294 HOH   B O    1 
HETATM 6922 O O    . HOH   F 3 .   ? 45.412 -33.393 -15.959 1.00 23.27 ?  295 HOH   B O    1 
HETATM 6923 O O    . HOH   F 3 .   ? 52.549 -10.453 13.036  1.00 22.70 ?  296 HOH   B O    1 
HETATM 6924 O O    . HOH   F 3 .   ? 37.530 -18.236 13.089  1.00 28.77 ?  297 HOH   B O    1 
HETATM 6925 O O    . HOH   F 3 .   ? 44.627 -27.467 1.970   1.00 15.80 ?  298 HOH   B O    1 
HETATM 6926 O O    . HOH   F 3 .   ? 49.912 -24.725 5.790   1.00 34.21 ?  299 HOH   B O    1 
HETATM 6927 O O    . HOH   F 3 .   ? 52.604 -35.681 -8.553  1.00 29.04 ?  300 HOH   B O    1 
HETATM 6928 O O    . HOH   F 3 .   ? 42.278 -10.000 -14.952 1.00 33.77 ?  301 HOH   B O    1 
HETATM 6929 O O    . HOH   F 3 .   ? 51.269 -37.635 -9.598  1.00 25.63 ?  302 HOH   B O    1 
HETATM 6930 O O    . HOH   F 3 .   ? 59.776 -15.340 8.201   1.00 32.54 ?  303 HOH   B O    1 
HETATM 6931 O O    . HOH   F 3 .   ? 37.320 -35.699 7.137   1.00 34.58 ?  304 HOH   B O    1 
HETATM 6932 O O    . HOH   F 3 .   ? 53.101 -16.032 -12.747 1.00 28.19 ?  305 HOH   B O    1 
HETATM 6933 O O    . HOH   F 3 .   ? 42.735 -12.271 -18.534 1.00 29.24 ?  306 HOH   B O    1 
HETATM 6934 O O    . HOH   F 3 .   ? 41.192 -24.454 15.760  1.00 43.31 ?  307 HOH   B O    1 
HETATM 6935 O O    . HOH   F 3 .   ? 52.606 -29.278 -13.009 1.00 23.83 ?  308 HOH   B O    1 
HETATM 6936 O O    . HOH   F 3 .   ? 37.836 -10.252 -10.778 1.00 17.43 ?  309 HOH   B O    1 
HETATM 6937 O O    . HOH   F 3 .   ? 53.465 -30.222 4.510   1.00 19.04 ?  310 HOH   B O    1 
HETATM 6938 O O    . HOH   F 3 .   ? 32.813 -34.610 -5.944  1.00 17.14 ?  311 HOH   B O    1 
HETATM 6939 O O    . HOH   F 3 .   ? 25.950 -21.483 -3.558  1.00 16.50 ?  312 HOH   B O    1 
HETATM 6940 O O    . HOH   F 3 .   ? 43.535 -15.384 18.239  1.00 34.23 ?  313 HOH   B O    1 
HETATM 6941 O O    . HOH   F 3 .   ? 44.058 -29.354 -4.665  1.00 23.01 ?  314 HOH   B O    1 
HETATM 6942 O O    . HOH   F 3 .   ? 35.027 -33.583 4.505   1.00 26.84 ?  315 HOH   B O    1 
HETATM 6943 O O    . HOH   F 3 .   ? 41.743 -8.098  1.382   1.00 25.51 ?  316 HOH   B O    1 
HETATM 6944 O O    . HOH   F 3 .   ? 62.845 -20.198 -0.806  1.00 39.15 ?  317 HOH   B O    1 
HETATM 6945 O O    . HOH   F 3 .   ? 40.248 -10.825 -9.556  1.00 17.33 ?  318 HOH   B O    1 
HETATM 6946 O O    . HOH   F 3 .   ? 62.686 -13.552 4.781   1.00 27.67 ?  319 HOH   B O    1 
HETATM 6947 O O    . HOH   F 3 .   ? 57.662 -22.098 3.148   1.00 27.40 ?  320 HOH   B O    1 
HETATM 6948 O O    . HOH   F 3 .   ? 43.209 -21.457 10.660  1.00 16.23 ?  321 HOH   B O    1 
HETATM 6949 O O    . HOH   F 3 .   ? 44.582 -24.663 9.553   1.00 19.47 ?  322 HOH   B O    1 
HETATM 6950 O O    . HOH   F 3 .   ? 38.354 -12.816 7.918   1.00 19.22 ?  323 HOH   B O    1 
HETATM 6951 O O    . HOH   F 3 .   ? 26.330 -21.024 -6.289  1.00 17.19 ?  324 HOH   B O    1 
HETATM 6952 O O    . HOH   F 3 .   ? 37.234 -30.591 -21.081 1.00 31.43 ?  325 HOH   B O    1 
HETATM 6953 O O    . HOH   F 3 .   ? 59.940 -17.189 -10.507 1.00 34.08 ?  326 HOH   B O    1 
HETATM 6954 O O    . HOH   F 3 .   ? 53.660 -12.539 -22.298 1.00 37.66 ?  327 HOH   B O    1 
HETATM 6955 O O    . HOH   F 3 .   ? 51.412 -32.912 -10.834 1.00 38.65 ?  328 HOH   B O    1 
HETATM 6956 O O    . HOH   F 3 .   ? 36.721 -12.429 4.298   1.00 18.48 ?  329 HOH   B O    1 
HETATM 6957 O O    . HOH   F 3 .   ? 27.937 -14.749 -9.425  1.00 33.96 ?  330 HOH   B O    1 
HETATM 6958 O O    . HOH   F 3 .   ? 39.553 -23.446 -20.336 1.00 35.61 ?  331 HOH   B O    1 
HETATM 6959 O O    . HOH   F 3 .   ? 51.730 -5.970  -7.909  1.00 48.41 ?  332 HOH   B O    1 
HETATM 6960 O O    . HOH   F 3 .   ? 33.624 -31.207 11.053  1.00 34.34 ?  333 HOH   B O    1 
HETATM 6961 O O    . HOH   F 3 .   ? 47.169 -24.515 8.144   1.00 25.98 ?  334 HOH   B O    1 
HETATM 6962 O O    . HOH   F 3 .   ? 44.164 -1.749  7.553   1.00 46.16 ?  335 HOH   B O    1 
HETATM 6963 O O    . HOH   F 3 .   ? 43.124 -34.644 0.046   1.00 20.97 ?  336 HOH   B O    1 
HETATM 6964 O O    . HOH   F 3 .   ? 45.778 -36.240 -16.148 1.00 33.82 ?  337 HOH   B O    1 
HETATM 6965 O O    . HOH   F 3 .   ? 42.910 -43.508 -14.443 1.00 43.47 ?  338 HOH   B O    1 
HETATM 6966 O O    . HOH   F 3 .   ? 38.347 -9.364  -13.269 1.00 27.52 ?  339 HOH   B O    1 
HETATM 6967 O O    . HOH   F 3 .   ? 47.491 -27.453 2.004   1.00 14.89 ?  340 HOH   B O    1 
HETATM 6968 O O    . HOH   F 3 .   ? 48.598 -11.908 -13.919 1.00 27.34 ?  341 HOH   B O    1 
HETATM 6969 O O    . HOH   F 3 .   ? 46.829 -19.904 12.296  1.00 31.55 ?  342 HOH   B O    1 
HETATM 6970 O O    . HOH   F 3 .   ? 37.057 -15.077 -16.477 1.00 37.99 ?  343 HOH   B O    1 
HETATM 6971 O O    . HOH   F 3 .   ? 28.898 -42.948 -12.380 1.00 39.59 ?  344 HOH   B O    1 
HETATM 6972 O O    . HOH   F 3 .   ? 38.432 -12.266 -16.245 1.00 41.95 ?  345 HOH   B O    1 
HETATM 6973 O O    . HOH   F 3 .   ? 37.103 -45.274 -9.773  1.00 37.73 ?  346 HOH   B O    1 
HETATM 6974 O O    . HOH   F 3 .   ? 32.987 -14.692 1.017   1.00 18.61 ?  347 HOH   B O    1 
HETATM 6975 O O    . HOH   F 3 .   ? 39.790 -44.296 -11.247 1.00 37.39 ?  348 HOH   B O    1 
HETATM 6976 O O    . HOH   F 3 .   ? 40.391 -43.485 -9.142  1.00 26.61 ?  349 HOH   B O    1 
HETATM 6977 O O    . HOH   F 3 .   ? 38.528 -22.361 15.061  1.00 39.45 ?  350 HOH   B O    1 
HETATM 6978 O O    . HOH   F 3 .   ? 23.226 -23.735 6.765   1.00 35.21 ?  351 HOH   B O    1 
HETATM 6979 O O    . HOH   F 3 .   ? 33.782 -9.205  -8.784  1.00 29.92 ?  352 HOH   B O    1 
HETATM 6980 O O    . HOH   F 3 .   ? 62.506 -20.167 -4.884  1.00 44.40 ?  353 HOH   B O    1 
HETATM 6981 O O    . HOH   F 3 .   ? 44.246 -37.369 -17.810 1.00 33.06 ?  354 HOH   B O    1 
HETATM 6982 O O    . HOH   F 3 .   ? 27.767 -26.632 -0.621  1.00 31.18 ?  355 HOH   B O    1 
HETATM 6983 O O    . HOH   F 3 .   ? 55.644 -8.253  10.840  1.00 24.35 ?  356 HOH   B O    1 
HETATM 6984 O O    . HOH   F 3 .   ? 34.627 -10.326 7.533   1.00 24.16 ?  357 HOH   B O    1 
HETATM 6985 O O    . HOH   F 3 .   ? 56.567 -7.281  3.135   1.00 28.33 ?  358 HOH   B O    1 
HETATM 6986 O O    . HOH   F 3 .   ? 36.149 -8.536  -9.719  1.00 34.94 ?  359 HOH   B O    1 
HETATM 6987 O O    . HOH   F 3 .   ? 34.074 -7.814  11.484  1.00 42.32 ?  360 HOH   B O    1 
HETATM 6988 O O    . HOH   F 3 .   ? 61.494 -19.888 1.634   1.00 32.68 ?  361 HOH   B O    1 
HETATM 6989 O O    . HOH   F 3 .   ? 43.142 -12.689 -21.242 1.00 39.49 ?  362 HOH   B O    1 
HETATM 6990 O O    . HOH   F 3 .   ? 40.266 -8.754  9.934   1.00 38.97 ?  363 HOH   B O    1 
HETATM 6991 O O    . HOH   F 3 .   ? 56.923 -21.538 -16.446 1.00 41.25 ?  364 HOH   B O    1 
HETATM 6992 O O    . HOH   F 3 .   ? 27.117 -25.958 -11.516 1.00 33.15 ?  365 HOH   B O    1 
HETATM 6993 O O    . HOH   F 3 .   ? 32.489 -23.659 14.064  1.00 39.84 ?  366 HOH   B O    1 
HETATM 6994 O O    . HOH   F 3 .   ? 54.185 -5.725  3.033   1.00 35.80 ?  367 HOH   B O    1 
HETATM 6995 O O    . HOH   F 3 .   ? 36.244 -8.762  8.964   1.00 37.56 ?  368 HOH   B O    1 
HETATM 6996 O O    . HOH   F 3 .   ? 40.079 -11.374 -13.985 1.00 33.97 ?  369 HOH   B O    1 
HETATM 6997 O O    . HOH   F 3 .   ? 59.030 -10.447 9.174   1.00 38.62 ?  370 HOH   B O    1 
HETATM 6998 O O    . HOH   F 3 .   ? 39.853 -7.055  7.857   1.00 43.34 ?  371 HOH   B O    1 
HETATM 6999 O O    . HOH   F 3 .   ? 41.839 -10.030 -17.407 1.00 52.74 ?  372 HOH   B O    1 
HETATM 7000 O O    . HOH   F 3 .   ? 48.421 -26.537 8.764   1.00 39.06 ?  373 HOH   B O    1 
HETATM 7001 O O    . HOH   F 3 .   ? 56.053 -7.779  -0.566  1.00 35.40 ?  374 HOH   B O    1 
HETATM 7002 O O    . HOH   F 3 .   ? 52.054 -12.953 13.378  1.00 30.28 ?  375 HOH   B O    1 
HETATM 7003 O O    . HOH   F 3 .   ? 63.050 -12.415 6.957   1.00 37.17 ?  376 HOH   B O    1 
HETATM 7004 O O    . HOH   F 3 .   ? 38.051 -10.623 10.086  1.00 29.97 ?  377 HOH   B O    1 
HETATM 7005 O O    . HOH   F 3 .   ? 36.560 -22.833 13.314  1.00 27.84 ?  378 HOH   B O    1 
HETATM 7006 O O    . HOH   F 3 .   ? 44.121 -5.622  -3.469  1.00 42.84 ?  379 HOH   B O    1 
HETATM 7007 O O    . HOH   F 3 .   ? 41.864 -6.679  -4.784  1.00 48.45 ?  380 HOH   B O    1 
HETATM 7008 O O    . HOH   F 3 .   ? 40.143 -7.691  3.245   1.00 37.41 ?  381 HOH   B O    1 
HETATM 7009 O O    . HOH   F 3 .   ? 39.665 -14.063 15.717  1.00 49.86 ?  382 HOH   B O    1 
HETATM 7010 O O    . HOH   F 3 .   ? 42.629 -17.083 -23.275 1.00 40.66 ?  383 HOH   B O    1 
HETATM 7011 O O    . HOH   F 3 .   ? 52.868 -29.915 7.176   1.00 24.38 ?  384 HOH   B O    1 
HETATM 7012 O O    . HOH   F 3 .   ? 60.477 -22.296 2.809   1.00 45.60 ?  385 HOH   B O    1 
HETATM 7013 O O    . HOH   F 3 .   ? 46.747 -5.386  2.962   1.00 41.51 ?  386 HOH   B O    1 
HETATM 7014 O O    . HOH   F 3 .   ? 35.361 -33.758 7.255   1.00 41.08 ?  387 HOH   B O    1 
HETATM 7015 O O    . HOH   F 3 .   ? 23.918 -20.844 -7.710  1.00 28.36 ?  388 HOH   B O    1 
HETATM 7016 O O    . HOH   F 3 .   ? 35.333 -20.325 13.343  1.00 30.19 ?  389 HOH   B O    1 
HETATM 7017 O O    . HOH   F 3 .   ? 40.886 -9.847  15.834  1.00 44.30 ?  390 HOH   B O    1 
HETATM 7018 O O    . HOH   F 3 .   ? 25.755 -18.908 -11.977 1.00 38.63 ?  391 HOH   B O    1 
HETATM 7019 O O    . HOH   F 3 .   ? 40.696 -6.630  -0.859  1.00 25.19 ?  392 HOH   B O    1 
HETATM 7020 O O    . HOH   F 3 .   ? 44.037 -31.743 -3.803  1.00 32.53 ?  393 HOH   B O    1 
HETATM 7021 O O    . HOH   F 3 .   ? 27.914 -27.086 2.171   1.00 33.36 ?  394 HOH   B O    1 
HETATM 7022 O O    . HOH   F 3 .   ? 26.650 -28.005 -13.583 1.00 35.21 ?  395 HOH   B O    1 
HETATM 7023 O O    . HOH   F 3 .   ? 34.382 -33.472 9.557   1.00 33.65 ?  396 HOH   B O    1 
HETATM 7024 O O    . HOH   F 3 .   ? 24.595 -20.666 -10.466 1.00 37.34 ?  397 HOH   B O    1 
HETATM 7025 O O    . HOH   F 3 .   ? 50.637 -30.816 8.675   1.00 27.88 ?  398 HOH   B O    1 
HETATM 7026 O O    . HOH   F 3 .   ? 45.705 -20.313 15.185  1.00 50.89 ?  399 HOH   B O    1 
HETATM 7027 O O    . HOH   F 3 .   ? 26.847 -30.655 -12.672 1.00 30.35 ?  400 HOH   B O    1 
HETATM 7028 O O    . HOH   F 3 .   ? 57.630 -6.435  -2.315  1.00 34.60 ?  401 HOH   B O    1 
HETATM 7029 O O    . HOH   F 3 .   ? 40.947 -11.803 -22.353 1.00 43.26 ?  402 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   ? 0.4779 0.4689 0.5723 0.0311  -0.0171 0.0905  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.4968 0.4601 0.5365 0.0118  0.0056  0.0043  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.4746 0.4665 0.5633 0.0297  -0.0165 0.0886  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.4946 0.4588 0.5286 0.0112  0.0044  0.0047  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.4598 0.4555 0.5155 0.0196  -0.0192 0.0877  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.4850 0.4503 0.4965 0.0088  0.0034  0.0023  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.4638 0.4566 0.5173 0.0235  -0.0196 0.0910  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.4873 0.4525 0.5001 0.0087  0.0043  0.0002  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.4839 0.4731 0.5933 0.0359  -0.0117 0.0892  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5001 0.4642 0.5461 0.0126  0.0052  0.0058  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.4869 0.4748 0.6052 0.0376  -0.0096 0.0897  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5032 0.4664 0.5525 0.0126  0.0061  0.0060  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.4872 0.4761 0.6050 0.0380  -0.0100 0.0895  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5007 0.4657 0.5531 0.0136  0.0058  0.0069  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.4382 0.4417 0.4574 0.0057  -0.0197 0.0817  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.4715 0.4376 0.4560 0.0061  0.0024  0.0029  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.4182 0.4279 0.3988 -0.0113 -0.0168 0.0714  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.4575 0.4242 0.4153 0.0025  0.0006  0.0039  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.3952 0.4105 0.3592 -0.0296 -0.0061 0.0491  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.4404 0.4086 0.4016 -0.0033 0.0111  0.0056  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.3987 0.4111 0.3475 -0.0309 -0.0089 0.0522  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.4416 0.4091 0.3987 -0.0041 0.0126  0.0064  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.4216 0.4312 0.3779 -0.0110 -0.0239 0.0792  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.4598 0.4257 0.3895 0.0031  -0.0108 0.0027  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.4251 0.4318 0.3560 -0.0124 -0.0284 0.0898  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.4621 0.4277 0.3678 0.0029  -0.0210 0.0026  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.4274 0.4298 0.3445 -0.0109 -0.0278 0.0938  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.4650 0.4288 0.3600 0.0029  -0.0253 0.0027  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.4252 0.4329 0.3491 -0.0139 -0.0327 0.0967  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.4610 0.4279 0.3589 0.0027  -0.0240 0.0032  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.3679 0.3888 0.3334 -0.0467 0.0054  0.0236  5   SER   A N   
60   N N   B SER   A 5   ? 0.4213 0.3919 0.3912 -0.0094 0.0204  0.0066  5   SER   A N   
61   C CA  A SER   A 5   ? 0.3425 0.3703 0.3145 -0.0583 0.0194  -0.0019 5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4000 0.3742 0.3824 -0.0172 0.0293  0.0072  5   SER   A CA  
63   C C   A SER   A 5   ? 0.3151 0.3465 0.2742 -0.0608 0.0342  -0.0173 5   SER   A C   
64   C C   B SER   A 5   ? 0.3755 0.3549 0.3560 -0.0252 0.0374  0.0071  5   SER   A C   
65   O O   A SER   A 5   ? 0.3173 0.3517 0.2755 -0.0543 0.0347  -0.0297 5   SER   A O   
66   O O   B SER   A 5   ? 0.3759 0.3531 0.3579 -0.0284 0.0383  0.0068  5   SER   A O   
67   C CB  A SER   A 5   ? 0.3481 0.3755 0.3310 -0.0637 0.0199  -0.0078 5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4024 0.3749 0.3985 -0.0168 0.0298  0.0075  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.3531 0.3771 0.3407 -0.0661 0.0259  -0.0077 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4039 0.3752 0.4095 -0.0166 0.0286  0.0079  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.2815 0.3125 0.2359 -0.0680 0.0523  -0.0177 6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3508 0.3366 0.3287 -0.0313 0.0436  0.0076  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2579 0.2830 0.2077 -0.0680 0.0621  -0.0056 6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3253 0.3174 0.3001 -0.0367 0.0471  0.0099  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2550 0.2831 0.2121 -0.0721 0.0768  -0.0006 6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3178 0.3126 0.3039 -0.0398 0.0516  0.0017  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2563 0.2900 0.2315 -0.0798 0.0649  0.0020  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3169 0.3122 0.3040 -0.0401 0.0541  0.0031  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2470 0.2612 0.1857 -0.0532 0.0613  0.0068  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.3101 0.3046 0.2719 -0.0371 0.0434  0.0193  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2372 0.2446 0.1782 -0.0443 0.0592  0.0179  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2983 0.2957 0.2477 -0.0350 0.0384  0.0226  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2352 0.2354 0.1828 -0.0369 0.0523  0.0225  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2934 0.2913 0.2374 -0.0326 0.0359  0.0260  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2374 0.2402 0.1880 -0.0337 0.0584  0.0129  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2949 0.2943 0.2459 -0.0331 0.0350  0.0227  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2338 0.2332 0.1928 -0.0338 0.0550  0.0203  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2908 0.2890 0.2329 -0.0318 0.0329  0.0249  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2362 0.2357 0.2086 -0.0320 0.0570  0.0098  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2920 0.2919 0.2416 -0.0318 0.0342  0.0216  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2365 0.2316 0.2024 -0.0342 0.0535  0.0104  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2909 0.2894 0.2371 -0.0319 0.0325  0.0217  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2534 0.2802 0.2094 -0.0645 0.0919  0.0004  7   SER   A N   
122  N N   B SER   A 7   ? 0.3106 0.3069 0.3071 -0.0400 0.0524  -0.0097 7   SER   A N   
123  C CA  A SER   A 7   ? 0.2590 0.2865 0.2261 -0.0524 0.0940  -0.0175 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.3036 0.3020 0.3121 -0.0364 0.0475  -0.0218 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2380 0.2603 0.2201 -0.0508 0.1090  -0.0138 7   SER   A C   
126  C C   B SER   A 7   ? 0.2908 0.2951 0.2932 -0.0350 0.0516  -0.0217 7   SER   A C   
127  O O   A SER   A 7   ? 0.2453 0.2490 0.2290 -0.0513 0.1086  -0.0086 7   SER   A O   
128  O O   B SER   A 7   ? 0.2938 0.2981 0.2961 -0.0359 0.0524  -0.0194 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2824 0.3172 0.2531 -0.0404 0.0843  -0.0278 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3080 0.3022 0.3327 -0.0363 0.0387  -0.0309 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2988 0.3364 0.2733 -0.0320 0.0824  -0.0327 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3114 0.3046 0.3460 -0.0351 0.0325  -0.0368 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2250 0.2477 0.2309 -0.0502 0.0974  -0.0173 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2755 0.2856 0.2733 -0.0308 0.0573  -0.0220 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2152 0.2388 0.2295 -0.0370 0.0888  -0.0135 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2618 0.2742 0.2546 -0.0262 0.0555  -0.0210 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1982 0.2294 0.2190 -0.0277 0.0697  -0.0089 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2467 0.2637 0.2365 -0.0218 0.0535  -0.0136 8   GLY   A C   
149  O O   A GLY   A 8   ? 0.2011 0.2389 0.2385 -0.0104 0.0628  -0.0262 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2469 0.2650 0.2375 -0.0199 0.0563  -0.0216 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1793 0.2123 0.2005 -0.0270 0.0621  0.0052  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.2314 0.2528 0.2286 -0.0169 0.0460  0.0003  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1702 0.1884 0.1868 -0.0307 0.0512  0.0185  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.2188 0.2412 0.2232 -0.0122 0.0394  0.0102  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1777 0.1724 0.1842 -0.0256 0.0478  0.0345  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.2117 0.2283 0.2117 -0.0087 0.0404  0.0128  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.2072 0.1858 0.1964 -0.0334 0.0499  0.0273  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.2131 0.2282 0.2141 -0.0106 0.0436  0.0135  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1625 0.1985 0.1863 -0.0208 0.0453  0.0155  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.2146 0.2439 0.2350 -0.0112 0.0302  0.0133  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1611 0.2049 0.2092 -0.0134 0.0519  0.0152  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.2117 0.2440 0.2414 -0.0109 0.0289  0.0199  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1555 0.2107 0.2265 -0.0255 0.0599  0.0068  9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.2100 0.2459 0.2465 -0.0157 0.0305  0.0222  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1608 0.1951 0.2060 -0.0113 0.0470  0.0364  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.2130 0.2412 0.2406 -0.0118 0.0249  0.0246  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1622 0.2125 0.2270 -0.0277 0.0705  0.0042  9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.2099 0.2448 0.2514 -0.0195 0.0267  0.0216  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1625 0.1986 0.2180 -0.0135 0.0559  0.0212  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.2153 0.2422 0.2480 -0.0154 0.0265  0.0222  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1602 0.2097 0.2232 -0.0225 0.0722  0.0038  9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.2154 0.2435 0.2540 -0.0217 0.0311  0.0229  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1718 0.2206 0.2304 -0.0329 0.0881  -0.0108 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.2214 0.2442 0.2583 -0.0271 0.0375  0.0226  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1594 0.1568 0.1909 -0.0205 0.0316  0.0375  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.2052 0.2202 0.2050 -0.0063 0.0336  0.0165  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1495 0.1557 0.2009 -0.0242 0.0258  0.0375  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1998 0.2189 0.2040 -0.0073 0.0241  0.0200  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1441 0.1505 0.1994 -0.0213 0.0283  0.0388  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1939 0.1976 0.1928 -0.0132 0.0223  0.0208  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1480 0.1431 0.2010 -0.0203 0.0437  0.0371  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1988 0.1913 0.1821 -0.0166 0.0309  0.0221  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1529 0.1667 0.2271 -0.0281 0.0172  0.0472  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1992 0.2326 0.2166 -0.0098 0.0117  0.0305  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1772 0.1848 0.2660 -0.0217 0.0035  0.0550  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.2007 0.2449 0.2279 -0.0107 0.0019  0.0394  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1892 0.1975 0.2900 -0.0275 0.0054  0.0502  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.2045 0.2541 0.2324 -0.0091 -0.0047 0.0388  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1989 0.2066 0.2814 -0.0159 0.0034  0.0435  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1995 0.2462 0.2300 -0.0129 0.0050  0.0479  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1443 0.1486 0.1980 -0.0156 0.0369  0.0368  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1883 0.1849 0.1962 -0.0179 0.0141  0.0198  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1459 0.1486 0.2018 -0.0220 0.0250  0.0339  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1816 0.1734 0.1927 -0.0243 0.0170  0.0240  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1397 0.1534 0.1924 -0.0240 0.0280  0.0229  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1708 0.1654 0.1949 -0.0329 0.0134  0.0196  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1500 0.1820 0.2332 -0.0473 0.0305  0.0100  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1665 0.1610 0.2088 -0.0376 0.0172  0.0052  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1546 0.1427 0.1916 -0.0130 0.0288  0.0251  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1879 0.1692 0.1896 -0.0214 0.0203  0.0227  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1638 0.1426 0.1932 -0.0145 0.0366  0.0317  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1898 0.1715 0.1803 -0.0171 0.0302  0.0224  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1723 0.1523 0.1996 -0.0131 0.0331  0.0351  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1874 0.1751 0.1714 -0.0136 0.0379  0.0250  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1771 0.1490 0.2013 -0.0062 0.0311  0.0389  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1839 0.1742 0.1665 -0.0102 0.0323  0.0249  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1742 0.1492 0.2011 0.0048  0.0281  0.0265  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1829 0.1758 0.1641 -0.0026 0.0268  0.0222  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1328 0.1453 0.1788 -0.0248 0.0213  0.0153  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1673 0.1722 0.1942 -0.0196 0.0080  0.0143  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1356 0.1557 0.1834 -0.0247 0.0120  0.0290  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1709 0.1720 0.2016 -0.0141 0.0075  0.0160  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1386 0.1497 0.1821 -0.0256 0.0177  0.0280  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1673 0.1700 0.1844 -0.0080 0.0182  0.0148  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1469 0.1485 0.1853 -0.0192 0.0210  0.0191  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1746 0.1725 0.1781 0.0001  0.0103  0.0100  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1452 0.1577 0.2038 -0.0281 0.0030  0.0414  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1864 0.1761 0.2283 -0.0179 0.0066  0.0206  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1569 0.1686 0.2305 -0.0188 0.0150  0.0547  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1944 0.1764 0.2518 -0.0244 0.0013  0.0263  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1680 0.1763 0.2289 -0.0101 0.0087  0.0620  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.2029 0.1807 0.2670 -0.0262 0.0026  0.0272  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1568 0.1732 0.2652 -0.0212 0.0076  0.0569  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1983 0.1756 0.2583 -0.0301 -0.0060 0.0295  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1294 0.1407 0.1939 -0.0243 0.0125  0.0211  13  THR   A N   
320  N N   B THR   A 13  ? 0.1615 0.1666 0.1831 -0.0092 0.0229  0.0127  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1370 0.1403 0.1996 -0.0174 0.0245  0.0115  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1585 0.1677 0.1839 -0.0162 0.0286  0.0091  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1408 0.1384 0.1994 -0.0171 0.0228  0.0200  13  THR   A C   
324  C C   B THR   A 13  ? 0.1632 0.1727 0.1882 -0.0212 0.0332  0.0158  13  THR   A C   
325  O O   A THR   A 13  ? 0.1464 0.1440 0.1942 -0.0091 0.0201  0.0219  13  THR   A O   
326  O O   B THR   A 13  ? 0.1612 0.1708 0.1897 -0.0213 0.0324  0.0164  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1503 0.1500 0.2146 -0.0108 0.0314  0.0180  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1508 0.1720 0.1866 -0.0081 0.0237  0.0046  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1598 0.1398 0.2199 -0.0167 0.0263  0.0172  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1315 0.1754 0.1887 -0.0077 0.0298  0.0142  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1604 0.1668 0.2336 -0.0077 0.0305  0.0065  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1529 0.1727 0.1822 -0.0066 0.0180  -0.0020 13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1461 0.1386 0.2149 -0.0190 0.0179  0.0275  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1695 0.1796 0.1942 -0.0232 0.0304  0.0285  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1497 0.1494 0.2238 -0.0181 0.0113  0.0424  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1792 0.1873 0.2081 -0.0206 0.0137  0.0376  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1539 0.1513 0.2062 -0.0187 0.0054  0.0400  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1703 0.1776 0.1933 -0.0211 0.0031  0.0507  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1760 0.1603 0.2181 -0.0273 -0.0023 0.0372  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1779 0.1748 0.1933 -0.0234 -0.0028 0.0578  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1665 0.1720 0.2794 -0.0235 0.0133  0.0546  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.1973 0.2049 0.2495 -0.0180 -0.0021 0.0322  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1928 0.2158 0.3562 -0.0249 0.0052  0.0452  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2094 0.2300 0.2881 -0.0147 -0.0131 0.0220  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.2066 0.2148 0.3711 -0.0131 -0.0097 0.0509  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2176 0.2359 0.3026 -0.0081 -0.0261 0.0217  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.2197 0.2583 0.4026 -0.0249 -0.0082 0.0286  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2156 0.2484 0.3040 -0.0141 -0.0220 0.0144  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1463 0.1472 0.2075 -0.0219 0.0150  0.0422  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1575 0.1690 0.1997 -0.0204 0.0060  0.0541  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1499 0.1560 0.2290 -0.0231 -0.0001 0.0352  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1507 0.1653 0.2066 -0.0226 0.0043  0.0424  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1451 0.1547 0.2302 -0.0254 0.0051  0.0363  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1480 0.1646 0.2125 -0.0209 0.0141  0.0388  15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1349 0.1593 0.2473 -0.0201 0.0078  0.0418  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1423 0.1671 0.2301 -0.0155 0.0277  0.0331  15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1488 0.1585 0.2338 -0.0184 0.0015  0.0364  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1435 0.1602 0.2049 -0.0254 0.0022  0.0373  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1495 0.1652 0.2489 -0.0143 0.0111  0.0299  15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1442 0.1606 0.2113 -0.0184 0.0027  0.0310  15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1653 0.1767 0.2634 -0.0294 0.0106  0.0341  15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1511 0.1672 0.2156 -0.0268 0.0045  0.0318  15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1425 0.1672 0.2276 -0.0117 0.0338  0.0171  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1372 0.1516 0.2006 -0.0070 0.0052  0.0242  15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1453 0.1429 0.1998 -0.0181 0.0120  0.0278  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1475 0.1599 0.1927 -0.0173 0.0100  0.0391  16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1435 0.1444 0.1903 -0.0181 0.0162  0.0164  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1490 0.1547 0.1689 -0.0130 0.0108  0.0353  16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1366 0.1417 0.1777 -0.0170 0.0117  0.0174  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1475 0.1609 0.1551 -0.0121 0.0179  0.0388  16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1324 0.1423 0.1862 -0.0221 0.0201  0.0120  16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1479 0.1653 0.1620 -0.0097 0.0246  0.0325  16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1541 0.1565 0.1871 -0.0002 0.0303  0.0148  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1549 0.1450 0.1590 -0.0028 0.0057  0.0294  16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1701 0.1635 0.1935 0.0028  0.0178  0.0099  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1614 0.1317 0.1540 -0.0028 0.0040  0.0261  16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1637 0.1722 0.1892 0.0003  0.0442  0.0114  16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1588 0.1602 0.1714 0.0061  0.0180  0.0261  16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1375 0.1358 0.1775 -0.0128 0.0226  0.0191  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1519 0.1611 0.1469 -0.0169 0.0153  0.0369  17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1431 0.1448 0.1692 -0.0178 0.0172  0.0252  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1539 0.1651 0.1429 -0.0191 0.0094  0.0331  17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1448 0.1358 0.1810 -0.0174 0.0196  0.0176  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1524 0.1670 0.1383 -0.0212 0.0154  0.0338  17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1403 0.1351 0.1813 -0.0199 0.0212  0.0230  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1478 0.1684 0.1311 -0.0249 0.0106  0.0316  17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1603 0.1531 0.1705 -0.0211 0.0060  0.0218  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.1705 0.1695 0.1502 -0.0167 -0.0014 0.0277  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.1783 0.1612 0.1785 -0.0304 -0.0096 0.0202  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.1876 0.1792 0.1624 -0.0144 -0.0179 0.0206  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.1852 0.1621 0.1940 -0.0277 -0.0210 0.0143  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.1953 0.1834 0.1727 -0.0096 -0.0246 0.0218  17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.1922 0.1719 0.1737 -0.0431 -0.0081 0.0361  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.1953 0.1903 0.1725 -0.0145 -0.0136 0.0162  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.1899 0.1622 0.1993 -0.0365 -0.0336 0.0199  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.2017 0.1917 0.1876 -0.0050 -0.0257 0.0219  17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.2009 0.1737 0.1914 -0.0419 -0.0171 0.0255  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.2021 0.1966 0.1823 -0.0096 -0.0148 0.0124  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.1970 0.1676 0.1992 -0.0448 -0.0349 0.0333  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.2018 0.1979 0.1919 -0.0062 -0.0213 0.0196  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.2089 0.1711 0.2080 -0.0461 -0.0356 0.0365  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.2013 0.2031 0.2012 -0.0022 -0.0215 0.0232  17  TYR   A OH  
473  N N   A ILE   A 18  ? 0.1495 0.1417 0.1836 -0.0182 0.0245  0.0263  18  ILE   A N   
474  N N   B ILE   A 18  ? 0.1507 0.1634 0.1380 -0.0233 0.0213  0.0316  18  ILE   A N   
475  C CA  A ILE   A 18  ? 0.1562 0.1428 0.1956 -0.0155 0.0282  0.0177  18  ILE   A CA  
476  C CA  B ILE   A 18  ? 0.1496 0.1662 0.1336 -0.0192 0.0276  0.0252  18  ILE   A CA  
477  C C   A ILE   A 18  ? 0.1539 0.1489 0.2095 -0.0205 0.0297  0.0188  18  ILE   A C   
478  C C   B ILE   A 18  ? 0.1479 0.1774 0.1313 -0.0185 0.0258  0.0192  18  ILE   A C   
479  O O   A ILE   A 18  ? 0.1493 0.1587 0.2159 -0.0219 0.0468  0.0296  18  ILE   A O   
480  O O   B ILE   A 18  ? 0.1423 0.1842 0.1338 -0.0185 0.0334  0.0181  18  ILE   A O   
481  C CB  A ILE   A 18  ? 0.1692 0.1502 0.1834 -0.0052 0.0280  0.0352  18  ILE   A CB  
482  C CB  B ILE   A 18  ? 0.1510 0.1612 0.1235 -0.0162 0.0254  0.0244  18  ILE   A CB  
483  C CG1 A ILE   A 18  ? 0.1803 0.1565 0.1824 0.0095  0.0276  0.0361  18  ILE   A CG1 
484  C CG1 B ILE   A 18  ? 0.1615 0.1655 0.1310 -0.0187 0.0293  0.0284  18  ILE   A CG1 
485  C CG2 A ILE   A 18  ? 0.1724 0.1542 0.1895 -0.0060 0.0224  0.0284  18  ILE   A CG2 
486  C CG2 B ILE   A 18  ? 0.1551 0.1687 0.1133 -0.0173 0.0162  0.0235  18  ILE   A CG2 
487  C CD1 A ILE   A 18  ? 0.1985 0.1749 0.2040 0.0156  0.0242  0.0313  18  ILE   A CD1 
488  C CD1 B ILE   A 18  ? 0.1687 0.1695 0.1429 -0.0202 0.0326  0.0206  18  ILE   A CD1 
511  N N   A LYS   A 19  ? 0.1599 0.1521 0.2113 -0.0147 0.0467  0.0229  19  LYS   A N   
512  N N   B LYS   A 19  ? 0.1548 0.1817 0.1419 -0.0171 0.0318  0.0150  19  LYS   A N   
513  C CA  A LYS   A 19  ? 0.1681 0.1638 0.2292 -0.0092 0.0539  0.0279  19  LYS   A CA  
514  C CA  B LYS   A 19  ? 0.1675 0.1899 0.1563 -0.0132 0.0378  0.0099  19  LYS   A CA  
515  C C   A LYS   A 19  ? 0.1607 0.1619 0.2528 -0.0012 0.0582  0.0457  19  LYS   A C   
516  C C   B LYS   A 19  ? 0.1709 0.1929 0.1740 -0.0054 0.0353  0.0094  19  LYS   A C   
517  O O   A LYS   A 19  ? 0.1570 0.1587 0.2557 -0.0009 0.0477  0.0450  19  LYS   A O   
518  O O   B LYS   A 19  ? 0.1726 0.1913 0.1754 -0.0098 0.0333  0.0098  19  LYS   A O   
519  C CB  A LYS   A 19  ? 0.1837 0.1802 0.2407 -0.0155 0.0600  0.0208  19  LYS   A CB  
520  C CB  B LYS   A 19  ? 0.1770 0.2005 0.1645 -0.0125 0.0407  -0.0016 19  LYS   A CB  
521  C CG  A LYS   A 19  ? 0.2123 0.1971 0.2444 -0.0135 0.0616  0.0043  19  LYS   A CG  
522  C CG  B LYS   A 19  ? 0.1918 0.2132 0.1717 -0.0117 0.0391  -0.0106 19  LYS   A CG  
523  C CD  A LYS   A 19  ? 0.2322 0.2126 0.2488 -0.0110 0.0759  0.0010  19  LYS   A CD  
524  C CD  B LYS   A 19  ? 0.2064 0.2197 0.1780 -0.0151 0.0404  -0.0174 19  LYS   A CD  
525  C CE  A LYS   A 19  ? 0.2460 0.2162 0.2497 -0.0101 0.0787  -0.0076 19  LYS   A CE  
526  C CE  B LYS   A 19  ? 0.2166 0.2270 0.1872 -0.0161 0.0389  -0.0215 19  LYS   A CE  
527  N NZ  A LYS   A 19  ? 0.2543 0.2186 0.2486 -0.0140 0.0920  -0.0160 19  LYS   A NZ  
528  N NZ  B LYS   A 19  ? 0.2264 0.2304 0.1965 -0.0187 0.0384  -0.0257 19  LYS   A NZ  
555  N N   A ASN   A 20  ? 0.1693 0.1727 0.2899 0.0042  0.0674  0.0613  20  ASN   A N   
556  N N   B ASN   A 20  ? 0.1781 0.1992 0.2024 0.0039  0.0440  0.0072  20  ASN   A N   
557  C CA  A ASN   A 20  ? 0.1862 0.1889 0.3204 0.0216  0.0866  0.0638  20  ASN   A CA  
558  C CA  B ASN   A 20  ? 0.1858 0.2129 0.2365 0.0128  0.0481  0.0063  20  ASN   A CA  
559  C C   A ASN   A 20  ? 0.2014 0.1881 0.3210 0.0173  0.0980  0.0583  20  ASN   A C   
560  C C   B ASN   A 20  ? 0.1952 0.2148 0.2479 0.0166  0.0589  0.0091  20  ASN   A C   
561  O O   A ASN   A 20  ? 0.2180 0.1868 0.3293 0.0079  0.0927  0.0530  20  ASN   A O   
562  O O   B ASN   A 20  ? 0.1985 0.2179 0.2646 0.0214  0.0606  0.0079  20  ASN   A O   
563  C CB  A ASN   A 20  ? 0.1914 0.1989 0.3544 0.0316  0.0834  0.0794  20  ASN   A CB  
564  C CB  B ASN   A 20  ? 0.1831 0.2208 0.2580 0.0160  0.0416  0.0011  20  ASN   A CB  
565  C CG  A ASN   A 20  ? 0.2012 0.1984 0.3913 0.0453  0.0798  0.0861  20  ASN   A CG  
566  C CG  B ASN   A 20  ? 0.1805 0.2230 0.2795 0.0188  0.0359  -0.0082 20  ASN   A CG  
567  O OD1 A ASN   A 20  ? 0.2249 0.2105 0.4215 0.0453  0.0826  0.0704  20  ASN   A OD1 
568  O OD1 B ASN   A 20  ? 0.1747 0.2202 0.2857 0.0181  0.0406  -0.0216 20  ASN   A OD1 
569  N ND2 A ASN   A 20  ? 0.2056 0.1909 0.3992 0.0476  0.0733  0.0940  20  ASN   A ND2 
570  N ND2 B ASN   A 20  ? 0.1911 0.2254 0.2940 0.0135  0.0267  -0.0017 20  ASN   A ND2 
583  N N   A ALA   A 21  ? 0.2045 0.1934 0.3271 0.0126  0.0937  0.0427  21  ALA   A N   
584  N N   B ALA   A 21  ? 0.2027 0.2138 0.2487 0.0138  0.0548  0.0099  21  ALA   A N   
585  C CA  A ALA   A 21  ? 0.2088 0.1909 0.3252 0.0077  0.0837  0.0446  21  ALA   A CA  
586  C CA  B ALA   A 21  ? 0.2093 0.2105 0.2441 0.0084  0.0513  0.0155  21  ALA   A CA  
587  C C   A ALA   A 21  ? 0.2002 0.1890 0.3202 0.0023  0.0744  0.0507  21  ALA   A C   
588  C C   B ALA   A 21  ? 0.2052 0.2038 0.2328 0.0084  0.0581  0.0215  21  ALA   A C   
589  O O   A ALA   A 21  ? 0.1921 0.1903 0.3273 0.0092  0.0668  0.0593  21  ALA   A O   
590  O O   B ALA   A 21  ? 0.2102 0.1990 0.2321 0.0133  0.0600  0.0189  21  ALA   A O   
591  C CB  A ALA   A 21  ? 0.2180 0.1966 0.3361 0.0017  0.0747  0.0521  21  ALA   A CB  
592  C CB  B ALA   A 21  ? 0.2141 0.2105 0.2530 0.0071  0.0457  0.0134  21  ALA   A CB  
603  N N   A ASP   A 22  ? 0.2022 0.1927 0.3198 -0.0018 0.0668  0.0454  22  ASP   A N   
604  N N   B ASP   A 22  ? 0.1980 0.2031 0.2290 0.0043  0.0615  0.0284  22  ASP   A N   
605  C CA  A ASP   A 22  ? 0.2054 0.1956 0.3075 -0.0026 0.0558  0.0401  22  ASP   A CA  
606  C CA  B ASP   A 22  ? 0.1913 0.2037 0.2288 0.0032  0.0565  0.0270  22  ASP   A CA  
607  C C   A ASP   A 22  ? 0.1888 0.1956 0.2725 -0.0079 0.0575  0.0367  22  ASP   A C   
608  C C   B ASP   A 22  ? 0.1759 0.1943 0.2062 -0.0038 0.0608  0.0216  22  ASP   A C   
609  O O   A ASP   A 22  ? 0.1950 0.2017 0.2715 -0.0141 0.0623  0.0396  22  ASP   A O   
610  O O   B ASP   A 22  ? 0.1747 0.1905 0.2052 -0.0066 0.0658  0.0158  22  ASP   A O   
611  C CB  A ASP   A 22  ? 0.2282 0.1975 0.3475 -0.0013 0.0471  0.0271  22  ASP   A CB  
612  C CB  B ASP   A 22  ? 0.1986 0.2122 0.2549 0.0098  0.0540  0.0203  22  ASP   A CB  
613  C CG  A ASP   A 22  ? 0.2470 0.1977 0.3852 -0.0036 0.0261  0.0269  22  ASP   A CG  
614  C CG  B ASP   A 22  ? 0.2077 0.2155 0.2705 0.0104  0.0515  0.0252  22  ASP   A CG  
615  O OD1 A ASP   A 22  ? 0.2455 0.1945 0.3886 -0.0252 0.0088  0.0419  22  ASP   A OD1 
616  O OD1 B ASP   A 22  ? 0.2114 0.2118 0.2669 0.0112  0.0529  0.0314  22  ASP   A OD1 
617  O OD2 A ASP   A 22  ? 0.2667 0.2078 0.4132 0.0092  0.0228  0.0175  22  ASP   A OD2 
618  O OD2 B ASP   A 22  ? 0.2090 0.2230 0.2771 0.0096  0.0509  0.0254  22  ASP   A OD2 
627  N N   A ILE   A 23  ? 0.1876 0.1906 0.2491 -0.0056 0.0599  0.0276  23  ILE   A N   
628  N N   B ILE   A 23  ? 0.1685 0.1899 0.1941 -0.0030 0.0537  0.0181  23  ILE   A N   
629  C CA  A ILE   A 23  ? 0.1858 0.1793 0.2219 -0.0072 0.0547  0.0265  23  ILE   A CA  
630  C CA  B ILE   A 23  ? 0.1648 0.1862 0.1780 -0.0072 0.0377  0.0173  23  ILE   A CA  
631  C C   A ILE   A 23  ? 0.1895 0.1888 0.2138 -0.0076 0.0668  0.0188  23  ILE   A C   
632  C C   B ILE   A 23  ? 0.1728 0.1908 0.1846 -0.0157 0.0399  0.0053  23  ILE   A C   
633  O O   A ILE   A 23  ? 0.1958 0.1920 0.2201 -0.0009 0.0626  0.0090  23  ILE   A O   
634  O O   B ILE   A 23  ? 0.1733 0.1854 0.1889 -0.0125 0.0357  0.0016  23  ILE   A O   
635  C CB  A ILE   A 23  ? 0.1974 0.1699 0.2005 -0.0083 0.0432  0.0198  23  ILE   A CB  
636  C CB  B ILE   A 23  ? 0.1569 0.1752 0.1591 0.0003  0.0226  0.0257  23  ILE   A CB  
637  C CG1 A ILE   A 23  ? 0.1982 0.1725 0.1988 -0.0028 0.0367  0.0091  23  ILE   A CG1 
638  C CG1 B ILE   A 23  ? 0.1585 0.1748 0.1495 0.0019  0.0066  0.0200  23  ILE   A CG1 
639  C CG2 A ILE   A 23  ? 0.2054 0.1690 0.1989 -0.0116 0.0453  0.0207  23  ILE   A CG2 
640  C CG2 B ILE   A 23  ? 0.1547 0.1694 0.1544 0.0103  0.0185  0.0296  23  ILE   A CG2 
641  C CD1 A ILE   A 23  ? 0.2002 0.1679 0.2008 -0.0027 0.0330  0.0034  23  ILE   A CD1 
642  C CD1 B ILE   A 23  ? 0.1549 0.1746 0.1509 0.0082  -0.0050 0.0212  23  ILE   A CD1 
665  N N   A VAL   A 24  ? 0.1982 0.1966 0.2201 -0.0132 0.0630  0.0189  24  VAL   A N   
666  N N   B VAL   A 24  ? 0.1882 0.2045 0.1992 -0.0239 0.0425  -0.0010 24  VAL   A N   
667  C CA  A VAL   A 24  ? 0.2156 0.2067 0.2401 -0.0196 0.0615  0.0101  24  VAL   A CA  
668  C CA  B VAL   A 24  ? 0.2031 0.2171 0.2137 -0.0240 0.0455  -0.0032 24  VAL   A CA  
669  C C   A VAL   A 24  ? 0.2270 0.2227 0.2459 -0.0251 0.0616  0.0022  24  VAL   A C   
670  C C   B VAL   A 24  ? 0.2129 0.2303 0.2213 -0.0261 0.0531  -0.0121 24  VAL   A C   
671  O O   A VAL   A 24  ? 0.2362 0.2219 0.2526 -0.0209 0.0586  0.0016  24  VAL   A O   
672  O O   B VAL   A 24  ? 0.2157 0.2330 0.2245 -0.0213 0.0514  -0.0104 24  VAL   A O   
673  C CB  A VAL   A 24  ? 0.2185 0.2108 0.2586 -0.0187 0.0632  0.0123  24  VAL   A CB  
674  C CB  B VAL   A 24  ? 0.2059 0.2185 0.2312 -0.0220 0.0390  0.0042  24  VAL   A CB  
675  C CG1 A VAL   A 24  ? 0.2246 0.2140 0.2706 -0.0162 0.0596  0.0066  24  VAL   A CG1 
676  C CG1 B VAL   A 24  ? 0.2122 0.2218 0.2400 -0.0170 0.0302  0.0048  24  VAL   A CG1 
677  C CG2 A VAL   A 24  ? 0.2262 0.2194 0.2628 -0.0199 0.0709  0.0190  24  VAL   A CG2 
678  C CG2 B VAL   A 24  ? 0.2048 0.2157 0.2293 -0.0250 0.0432  0.0047  24  VAL   A CG2 
697  N N   A GLU   A 25  ? 0.2349 0.2516 0.2473 -0.0304 0.0725  -0.0211 25  GLU   A N   
698  N N   B GLU   A 25  ? 0.2198 0.2409 0.2277 -0.0317 0.0665  -0.0225 25  GLU   A N   
699  C CA  A GLU   A 25  ? 0.2530 0.2807 0.2495 -0.0300 0.0833  -0.0297 25  GLU   A CA  
700  C CA  B GLU   A 25  ? 0.2321 0.2523 0.2367 -0.0413 0.0704  -0.0265 25  GLU   A CA  
701  C C   A GLU   A 25  ? 0.2433 0.2866 0.2179 -0.0413 0.0952  -0.0270 25  GLU   A C   
702  C C   B GLU   A 25  ? 0.2317 0.2516 0.2243 -0.0484 0.0794  -0.0260 25  GLU   A C   
703  O O   A GLU   A 25  ? 0.2508 0.2955 0.2247 -0.0390 0.0939  -0.0287 25  GLU   A O   
704  O O   B GLU   A 25  ? 0.2357 0.2527 0.2222 -0.0490 0.0812  -0.0289 25  GLU   A O   
705  C CB  A GLU   A 25  ? 0.2759 0.3017 0.2913 -0.0248 0.0786  -0.0272 25  GLU   A CB  
706  C CB  B GLU   A 25  ? 0.2411 0.2608 0.2607 -0.0442 0.0673  -0.0238 25  GLU   A CB  
707  C CG  A GLU   A 25  ? 0.2994 0.3212 0.3403 -0.0250 0.0610  -0.0283 25  GLU   A CG  
708  C CG  B GLU   A 25  ? 0.2522 0.2704 0.2920 -0.0455 0.0580  -0.0209 25  GLU   A CG  
709  C CD  A GLU   A 25  ? 0.3169 0.3375 0.3843 -0.0269 0.0505  -0.0291 25  GLU   A CD  
710  C CD  B GLU   A 25  ? 0.2573 0.2766 0.3229 -0.0490 0.0492  -0.0167 25  GLU   A CD  
711  O OE1 A GLU   A 25  ? 0.3247 0.3437 0.3925 -0.0259 0.0410  -0.0386 25  GLU   A OE1 
712  O OE1 B GLU   A 25  ? 0.2598 0.2754 0.3363 -0.0509 0.0449  -0.0127 25  GLU   A OE1 
713  O OE2 A GLU   A 25  ? 0.3211 0.3445 0.4141 -0.0289 0.0479  -0.0341 25  GLU   A OE2 
714  O OE2 B GLU   A 25  ? 0.2613 0.2826 0.3373 -0.0489 0.0479  -0.0126 25  GLU   A OE2 
727  N N   A GLU   A 26  ? 0.2329 0.2796 0.2194 -0.0593 0.0934  -0.0282 26  GLU   A N   
728  N N   B GLU   A 26  ? 0.2319 0.2477 0.2218 -0.0561 0.0839  -0.0275 26  GLU   A N   
729  C CA  A GLU   A 26  ? 0.2422 0.2781 0.2129 -0.0716 0.0865  -0.0159 26  GLU   A CA  
730  C CA  B GLU   A 26  ? 0.2379 0.2435 0.2192 -0.0593 0.0885  -0.0247 26  GLU   A CA  
731  C C   A GLU   A 26  ? 0.2419 0.2607 0.1892 -0.0699 0.0837  -0.0139 26  GLU   A C   
732  C C   B GLU   A 26  ? 0.2376 0.2462 0.2043 -0.0582 0.0837  -0.0206 26  GLU   A C   
733  O O   A GLU   A 26  ? 0.2467 0.2537 0.1681 -0.0757 0.0817  -0.0172 26  GLU   A O   
734  O O   B GLU   A 26  ? 0.2417 0.2460 0.2051 -0.0533 0.0828  -0.0221 26  GLU   A O   
735  C CB  A GLU   A 26  ? 0.2596 0.2902 0.2496 -0.0804 0.0727  -0.0048 26  GLU   A CB  
736  C CB  B GLU   A 26  ? 0.2462 0.2371 0.2354 -0.0637 0.0869  -0.0293 26  GLU   A CB  
737  C CG  A GLU   A 26  ? 0.2774 0.3092 0.2961 -0.0834 0.0712  -0.0016 26  GLU   A CG  
738  C CG  B GLU   A 26  ? 0.2524 0.2261 0.2384 -0.0729 0.0961  -0.0317 26  GLU   A CG  
739  C CD  A GLU   A 26  ? 0.2855 0.3262 0.3305 -0.0913 0.0757  0.0019  26  GLU   A CD  
740  C CD  B GLU   A 26  ? 0.2546 0.2146 0.2331 -0.0839 0.1102  -0.0399 26  GLU   A CD  
741  O OE1 A GLU   A 26  ? 0.2794 0.3517 0.3352 -0.0830 0.0880  -0.0176 26  GLU   A OE1 
742  O OE1 B GLU   A 26  ? 0.2548 0.2188 0.2476 -0.0838 0.1212  -0.0545 26  GLU   A OE1 
743  O OE2 A GLU   A 26  ? 0.3053 0.3306 0.3457 -0.0890 0.0638  0.0088  26  GLU   A OE2 
744  O OE2 B GLU   A 26  ? 0.2582 0.2104 0.2064 -0.0848 0.1162  -0.0447 26  GLU   A OE2 
757  N N   . ALA   A 27  ? 0.2321 0.2490 0.1906 -0.0651 0.0773  -0.0111 27  ALA   A N   
758  C CA  . ALA   A 27  ? 0.2400 0.2547 0.1842 -0.0607 0.0715  -0.0069 27  ALA   A CA  
759  C C   . ALA   A 27  ? 0.2736 0.2807 0.2044 -0.0645 0.0767  -0.0288 27  ALA   A C   
760  O O   . ALA   A 27  ? 0.2725 0.2712 0.2071 -0.0739 0.0633  -0.0292 27  ALA   A O   
761  C CB  . ALA   A 27  ? 0.2255 0.2408 0.1861 -0.0601 0.0574  0.0066  27  ALA   A CB  
768  N N   A LYS   A 28  ? 0.2996 0.2999 0.2165 -0.0574 0.0729  -0.0521 28  LYS   A N   
769  N N   B LYS   A 28  ? 0.2972 0.3052 0.2263 -0.0585 0.0753  -0.0329 28  LYS   A N   
770  C CA  A LYS   A 28  ? 0.3306 0.3287 0.2559 -0.0460 0.0691  -0.0636 28  LYS   A CA  
771  C CA  B LYS   A 28  ? 0.3232 0.3330 0.2612 -0.0500 0.0726  -0.0353 28  LYS   A CA  
772  C C   A LYS   A 28  ? 0.3425 0.3509 0.2538 -0.0491 0.0802  -0.0509 28  LYS   A C   
773  C C   B LYS   A 28  ? 0.3371 0.3521 0.2550 -0.0519 0.0853  -0.0340 28  LYS   A C   
774  O O   A LYS   A 28  ? 0.3491 0.3591 0.2861 -0.0460 0.0601  -0.0448 28  LYS   A O   
775  O O   B LYS   A 28  ? 0.3412 0.3565 0.2729 -0.0499 0.0743  -0.0301 28  LYS   A O   
776  C CB  A LYS   A 28  ? 0.3495 0.3409 0.3078 -0.0306 0.0578  -0.0775 28  LYS   A CB  
777  C CB  B LYS   A 28  ? 0.3351 0.3426 0.3034 -0.0397 0.0584  -0.0368 28  LYS   A CB  
778  C CG  A LYS   A 28  ? 0.3654 0.3523 0.3628 -0.0197 0.0488  -0.0821 28  LYS   A CG  
779  C CG  B LYS   A 28  ? 0.3451 0.3508 0.3438 -0.0319 0.0473  -0.0360 28  LYS   A CG  
780  C CD  A LYS   A 28  ? 0.3774 0.3660 0.4210 -0.0119 0.0398  -0.0833 28  LYS   A CD  
781  C CD  B LYS   A 28  ? 0.3524 0.3592 0.3812 -0.0261 0.0377  -0.0348 28  LYS   A CD  
782  C CE  A LYS   A 28  ? 0.3834 0.3733 0.4652 -0.0071 0.0323  -0.0820 28  LYS   A CE  
783  C CE  B LYS   A 28  ? 0.3563 0.3638 0.4106 -0.0233 0.0302  -0.0333 28  LYS   A CE  
784  N NZ  A LYS   A 28  ? 0.3886 0.3774 0.4894 -0.0031 0.0281  -0.0771 28  LYS   A NZ  
785  N NZ  B LYS   A 28  ? 0.3588 0.3665 0.4252 -0.0207 0.0261  -0.0312 28  LYS   A NZ  
812  N N   . LYS   A 29  ? 0.3452 0.3659 0.2413 -0.0570 0.1070  -0.0329 29  LYS   A N   
813  C CA  . LYS   A 29  ? 0.3692 0.3981 0.2586 -0.0631 0.1214  -0.0118 29  LYS   A CA  
814  C C   . LYS   A 29  ? 0.3732 0.3931 0.2317 -0.0728 0.1113  -0.0056 29  LYS   A C   
815  O O   . LYS   A 29  ? 0.3848 0.3990 0.2469 -0.0644 0.1064  -0.0103 29  LYS   A O   
816  C CB  . LYS   A 29  ? 0.3875 0.4314 0.3267 -0.0551 0.1321  -0.0015 29  LYS   A CB  
817  C CG  . LYS   A 29  ? 0.4068 0.4564 0.3971 -0.0451 0.1337  -0.0000 29  LYS   A CG  
818  C CD  . LYS   A 29  ? 0.4222 0.4774 0.4659 -0.0363 0.1329  -0.0028 29  LYS   A CD  
819  C CE  . LYS   A 29  ? 0.4323 0.4909 0.5167 -0.0297 0.1325  -0.0014 29  LYS   A CE  
820  N NZ  . LYS   A 29  ? 0.4363 0.4991 0.5441 -0.0266 0.1323  0.0002  29  LYS   A NZ  
835  N N   . VAL   A 30  ? 0.3607 0.3782 0.2120 -0.0912 0.1044  0.0028  30  VAL   A N   
836  C CA  . VAL   A 30  ? 0.3595 0.3652 0.1923 -0.1028 0.0796  0.0205  30  VAL   A CA  
837  C C   . VAL   A 30  ? 0.3636 0.3501 0.1535 -0.1049 0.0620  0.0240  30  VAL   A C   
838  O O   . VAL   A 30  ? 0.3715 0.3517 0.1629 -0.1046 0.0533  0.0258  30  VAL   A O   
839  C CB  . VAL   A 30  ? 0.3567 0.3639 0.2360 -0.1110 0.0564  0.0251  30  VAL   A CB  
840  C CG1 . VAL   A 30  ? 0.3588 0.3641 0.2519 -0.1120 0.0443  0.0281  30  VAL   A CG1 
841  C CG2 . VAL   A 30  ? 0.3559 0.3656 0.2663 -0.1131 0.0553  0.0240  30  VAL   A CG2 
851  N N   . LYS   A 31  ? 0.3548 0.3302 0.1412 -0.1088 0.0505  0.0170  31  LYS   A N   
852  C CA  . LYS   A 31  ? 0.3668 0.3238 0.1669 -0.0992 0.0254  0.0131  31  LYS   A CA  
853  C C   . LYS   A 31  ? 0.3449 0.2993 0.1258 -0.0820 0.0188  0.0388  31  LYS   A C   
854  O O   . LYS   A 31  ? 0.3457 0.3050 0.1406 -0.0769 0.0060  0.0515  31  LYS   A O   
855  C CB  . LYS   A 31  ? 0.4059 0.3469 0.2811 -0.0942 0.0033  -0.0076 31  LYS   A CB  
856  C CG  . LYS   A 31  ? 0.4456 0.3719 0.4124 -0.0854 -0.0168 -0.0191 31  LYS   A CG  
857  C CD  . LYS   A 31  ? 0.4759 0.3923 0.5181 -0.0790 -0.0360 -0.0280 31  LYS   A CD  
858  C CE  . LYS   A 31  ? 0.4950 0.4051 0.5875 -0.0748 -0.0512 -0.0347 31  LYS   A CE  
859  N NZ  . LYS   A 31  ? 0.5043 0.4135 0.6206 -0.0737 -0.0576 -0.0366 31  LYS   A NZ  
873  N N   . PRO   A 32  ? 0.3128 0.2693 0.1080 -0.0779 0.0186  0.0314  32  PRO   A N   
874  C CA  . PRO   A 32  ? 0.3033 0.2523 0.1352 -0.0717 0.0076  0.0416  32  PRO   A CA  
875  C C   . PRO   A 32  ? 0.2956 0.2422 0.1556 -0.0606 -0.0029 0.0487  32  PRO   A C   
876  O O   . PRO   A 32  ? 0.2918 0.2320 0.1606 -0.0631 -0.0182 0.0465  32  PRO   A O   
877  C CB  . PRO   A 32  ? 0.2963 0.2596 0.1383 -0.0703 0.0080  0.0348  32  PRO   A CB  
878  C CG  . PRO   A 32  ? 0.2937 0.2636 0.1131 -0.0689 0.0040  0.0217  32  PRO   A CG  
879  C CD  . PRO   A 32  ? 0.2995 0.2616 0.1006 -0.0732 0.0114  0.0270  32  PRO   A CD  
887  N N   . THR   A 33  ? 0.2958 0.2403 0.1507 -0.0526 -0.0037 0.0552  33  THR   A N   
888  C CA  . THR   A 33  ? 0.2869 0.2408 0.1592 -0.0382 -0.0212 0.0576  33  THR   A CA  
889  C C   . THR   A 33  ? 0.2485 0.2242 0.1524 -0.0384 -0.0228 0.0506  33  THR   A C   
890  O O   . THR   A 33  ? 0.2401 0.2279 0.1539 -0.0358 -0.0369 0.0508  33  THR   A O   
891  C CB  . THR   A 33  ? 0.3103 0.2580 0.1687 -0.0253 -0.0306 0.0738  33  THR   A CB  
892  O OG1 . THR   A 33  ? 0.3298 0.2674 0.1993 -0.0149 -0.0231 0.0833  33  THR   A OG1 
893  C CG2 . THR   A 33  ? 0.3138 0.2718 0.1864 -0.0183 -0.0337 0.0706  33  THR   A CG2 
901  N N   . VAL   A 34  ? 0.2203 0.2104 0.1305 -0.0362 -0.0138 0.0478  34  VAL   A N   
902  C CA  . VAL   A 34  ? 0.2013 0.1891 0.1344 -0.0314 -0.0055 0.0400  34  VAL   A CA  
903  C C   . VAL   A 34  ? 0.1881 0.1815 0.1283 -0.0306 0.0041  0.0306  34  VAL   A C   
904  O O   . VAL   A 34  ? 0.1866 0.1799 0.1415 -0.0375 0.0068  0.0372  34  VAL   A O   
905  C CB  . VAL   A 34  ? 0.2016 0.1834 0.1573 -0.0297 -0.0039 0.0316  34  VAL   A CB  
906  C CG1 . VAL   A 34  ? 0.2044 0.1856 0.1611 -0.0286 0.0096  0.0173  34  VAL   A CG1 
907  C CG2 . VAL   A 34  ? 0.2052 0.1989 0.1788 -0.0236 -0.0184 0.0258  34  VAL   A CG2 
917  N N   . VAL   A 35  ? 0.1714 0.1708 0.1237 -0.0288 -0.0026 0.0243  35  VAL   A N   
918  C CA  . VAL   A 35  ? 0.1645 0.1649 0.1219 -0.0237 0.0072  0.0194  35  VAL   A CA  
919  C C   . VAL   A 35  ? 0.1502 0.1515 0.1246 -0.0170 0.0069  0.0173  35  VAL   A C   
920  O O   . VAL   A 35  ? 0.1439 0.1605 0.1386 -0.0242 0.0136  0.0151  35  VAL   A O   
921  C CB  . VAL   A 35  ? 0.1708 0.1719 0.1353 -0.0174 0.0169  0.0085  35  VAL   A CB  
922  C CG1 . VAL   A 35  ? 0.1875 0.1722 0.1470 -0.0073 0.0114  0.0027  35  VAL   A CG1 
923  C CG2 . VAL   A 35  ? 0.1683 0.1707 0.1570 -0.0123 0.0249  0.0016  35  VAL   A CG2 
933  N N   . VAL   A 36  ? 0.1392 0.1515 0.1191 -0.0210 0.0080  0.0190  36  VAL   A N   
934  C CA  . VAL   A 36  ? 0.1348 0.1389 0.1178 -0.0128 0.0058  0.0150  36  VAL   A CA  
935  C C   . VAL   A 36  ? 0.1307 0.1435 0.1315 -0.0172 0.0137  0.0081  36  VAL   A C   
936  O O   . VAL   A 36  ? 0.1358 0.1407 0.1497 -0.0046 0.0247  0.0136  36  VAL   A O   
937  C CB  . VAL   A 36  ? 0.1365 0.1342 0.1284 -0.0103 0.0070  0.0139  36  VAL   A CB  
938  C CG1 . VAL   A 36  ? 0.1436 0.1413 0.1403 -0.0183 0.0070  0.0101  36  VAL   A CG1 
939  C CG2 . VAL   A 36  ? 0.1449 0.1335 0.1538 -0.0123 0.0002  0.0222  36  VAL   A CG2 
949  N N   . ASN   A 37  ? 0.1265 0.1339 0.1153 -0.0055 0.0075  0.0151  37  ASN   A N   
950  C CA  . ASN   A 37  ? 0.1203 0.1269 0.1120 0.0003  0.0115  0.0180  37  ASN   A CA  
951  C C   . ASN   A 37  ? 0.1246 0.1292 0.1153 -0.0052 0.0181  0.0203  37  ASN   A C   
952  O O   . ASN   A 37  ? 0.1374 0.1407 0.1139 0.0043  0.0139  0.0091  37  ASN   A O   
953  C CB  . ASN   A 37  ? 0.1278 0.1288 0.1276 0.0005  0.0056  0.0120  37  ASN   A CB  
954  C CG  . ASN   A 37  ? 0.1285 0.1294 0.1375 -0.0011 0.0042  0.0084  37  ASN   A CG  
955  O OD1 . ASN   A 37  ? 0.1277 0.1329 0.1450 0.0003  0.0076  0.0154  37  ASN   A OD1 
956  N ND2 . ASN   A 37  ? 0.1293 0.1311 0.1457 -0.0025 -0.0001 0.0232  37  ASN   A ND2 
963  N N   A ALA   A 38  ? 0.1262 0.1383 0.1346 -0.0049 0.0148  0.0067  38  ALA   A N   
964  N N   B ALA   A 38  ? 0.1259 0.1375 0.1293 -0.0075 0.0104  0.0156  38  ALA   A N   
965  C CA  A ALA   A 38  ? 0.1315 0.1461 0.1313 -0.0033 0.0054  -0.0011 38  ALA   A CA  
966  C CA  B ALA   A 38  ? 0.1278 0.1453 0.1330 -0.0089 0.0006  0.0131  38  ALA   A CA  
967  C C   A ALA   A 38  ? 0.1317 0.1413 0.1299 0.0003  -0.0034 -0.0022 38  ALA   A C   
968  C C   B ALA   A 38  ? 0.1278 0.1431 0.1279 -0.0060 -0.0082 0.0160  38  ALA   A C   
969  O O   A ALA   A 38  ? 0.1350 0.1297 0.1250 0.0026  -0.0122 -0.0094 38  ALA   A O   
970  O O   B ALA   A 38  ? 0.1248 0.1393 0.1265 -0.0042 -0.0168 0.0174  38  ALA   A O   
971  C CB  A ALA   A 38  ? 0.1386 0.1696 0.1459 -0.0083 -0.0001 -0.0004 38  ALA   A CB  
972  C CB  B ALA   A 38  ? 0.1296 0.1555 0.1483 -0.0114 -0.0047 0.0052  38  ALA   A CB  
983  N N   A ALA   A 39  ? 0.1304 0.1326 0.1342 0.0043  0.0060  0.0043  39  ALA   A N   
984  N N   B ALA   A 39  ? 0.1329 0.1412 0.1295 -0.0061 -0.0042 0.0232  39  ALA   A N   
985  C CA  A ALA   A 39  ? 0.1310 0.1252 0.1204 0.0049  0.0077  -0.0001 39  ALA   A CA  
986  C CA  B ALA   A 39  ? 0.1400 0.1443 0.1279 -0.0068 -0.0058 0.0210  39  ALA   A CA  
987  C C   A ALA   A 39  ? 0.1365 0.1278 0.1212 0.0021  0.0048  -0.0030 39  ALA   A C   
988  C C   B ALA   A 39  ? 0.1419 0.1359 0.1272 -0.0046 -0.0067 0.0171  39  ALA   A C   
989  O O   A ALA   A 39  ? 0.1504 0.1326 0.1258 -0.0032 0.0138  -0.0005 39  ALA   A O   
990  O O   B ALA   A 39  ? 0.1493 0.1367 0.1301 -0.0060 -0.0017 0.0107  39  ALA   A O   
991  C CB  A ALA   A 39  ? 0.1324 0.1281 0.1295 0.0012  -0.0040 0.0031  39  ALA   A CB  
992  C CB  B ALA   A 39  ? 0.1463 0.1527 0.1307 -0.0081 -0.0119 0.0229  39  ALA   A CB  
1003 N N   A ASN   A 40  ? 0.1422 0.1307 0.1211 -0.0049 0.0193  0.0001  40  ASN   A N   
1004 N N   B ASN   A 40  ? 0.1463 0.1306 0.1236 -0.0046 -0.0012 0.0226  40  ASN   A N   
1005 C CA  A ASN   A 40  ? 0.1480 0.1284 0.1273 -0.0018 0.0088  -0.0004 40  ASN   A CA  
1006 C CA  B ASN   A 40  ? 0.1501 0.1275 0.1312 -0.0016 -0.0073 0.0213  40  ASN   A CA  
1007 C C   A ASN   A 40  ? 0.1463 0.1213 0.1235 -0.0051 0.0204  0.0104  40  ASN   A C   
1008 C C   B ASN   A 40  ? 0.1510 0.1218 0.1212 -0.0028 0.0029  0.0269  40  ASN   A C   
1009 O O   A ASN   A 40  ? 0.1415 0.1264 0.1293 -0.0106 0.0178  0.0048  40  ASN   A O   
1010 O O   B ASN   A 40  ? 0.1458 0.1198 0.1194 -0.0047 0.0010  0.0267  40  ASN   A O   
1011 C CB  A ASN   A 40  ? 0.1529 0.1363 0.1403 0.0028  -0.0019 -0.0011 40  ASN   A CB  
1012 C CB  B ASN   A 40  ? 0.1510 0.1285 0.1466 -0.0036 -0.0098 0.0125  40  ASN   A CB  
1013 C CG  A ASN   A 40  ? 0.1534 0.1397 0.1744 0.0041  -0.0012 0.0077  40  ASN   A CG  
1014 C CG  B ASN   A 40  ? 0.1481 0.1301 0.1590 -0.0058 -0.0119 0.0034  40  ASN   A CG  
1015 O OD1 A ASN   A 40  ? 0.1604 0.1459 0.1930 0.0065  -0.0062 0.0140  40  ASN   A OD1 
1016 O OD1 B ASN   A 40  ? 0.1537 0.1333 0.1851 -0.0004 -0.0062 0.0006  40  ASN   A OD1 
1017 N ND2 A ASN   A 40  ? 0.1558 0.1494 0.1936 -0.0001 0.0087  0.0007  40  ASN   A ND2 
1018 N ND2 B ASN   A 40  ? 0.1449 0.1330 0.1637 -0.0145 0.0005  -0.0122 40  ASN   A ND2 
1031 N N   A VAL   A 41  ? 0.1565 0.1258 0.1301 0.0012  0.0217  0.0146  41  VAL   A N   
1032 N N   B VAL   A 41  ? 0.1572 0.1230 0.1194 0.0025  0.0120  0.0280  41  VAL   A N   
1033 C CA  A VAL   A 41  ? 0.1564 0.1344 0.1433 -0.0037 0.0273  0.0108  41  VAL   A CA  
1034 C CA  B VAL   A 41  ? 0.1584 0.1259 0.1234 -0.0011 0.0246  0.0259  41  VAL   A CA  
1035 C C   A VAL   A 41  ? 0.1553 0.1355 0.1537 -0.0030 0.0285  0.0081  41  VAL   A C   
1036 C C   B VAL   A 41  ? 0.1567 0.1231 0.1343 -0.0019 0.0302  0.0183  41  VAL   A C   
1037 O O   A VAL   A 41  ? 0.1586 0.1312 0.1731 0.0010  0.0249  -0.0062 41  VAL   A O   
1038 O O   B VAL   A 41  ? 0.1604 0.1091 0.1295 -0.0024 0.0287  0.0143  41  VAL   A O   
1039 C CB  A VAL   A 41  ? 0.1611 0.1450 0.1345 -0.0079 0.0277  0.0056  41  VAL   A CB  
1040 C CB  B VAL   A 41  ? 0.1630 0.1336 0.1253 -0.0004 0.0335  0.0244  41  VAL   A CB  
1041 C CG1 A VAL   A 41  ? 0.1742 0.1540 0.1589 0.0001  0.0182  -0.0043 41  VAL   A CG1 
1042 C CG1 B VAL   A 41  ? 0.1747 0.1408 0.1408 -0.0037 0.0414  0.0151  41  VAL   A CG1 
1043 C CG2 A VAL   A 41  ? 0.1639 0.1537 0.1308 -0.0080 0.0357  0.0054  41  VAL   A CG2 
1044 C CG2 B VAL   A 41  ? 0.1616 0.1404 0.1259 0.0018  0.0294  0.0250  41  VAL   A CG2 
1063 N N   . TYR   A 42  ? 0.1471 0.1264 0.1533 -0.0013 0.0335  0.0206  42  TYR   A N   
1064 C CA  . TYR   A 42  ? 0.1516 0.1279 0.1522 -0.0015 0.0355  0.0236  42  TYR   A CA  
1065 C C   . TYR   A 42  ? 0.1413 0.1263 0.1615 0.0012  0.0243  0.0233  42  TYR   A C   
1066 O O   . TYR   A 42  ? 0.1404 0.1256 0.1811 -0.0117 0.0234  0.0077  42  TYR   A O   
1067 C CB  . TYR   A 42  ? 0.1713 0.1392 0.1541 0.0001  0.0339  0.0244  42  TYR   A CB  
1068 C CG  . TYR   A 42  ? 0.1940 0.1508 0.1525 -0.0039 0.0295  0.0354  42  TYR   A CG  
1069 C CD1 . TYR   A 42  ? 0.2042 0.1664 0.1605 -0.0123 0.0445  0.0346  42  TYR   A CD1 
1070 C CD2 . TYR   A 42  ? 0.2057 0.1731 0.1722 -0.0013 0.0235  0.0196  42  TYR   A CD2 
1071 C CE1 . TYR   A 42  ? 0.2142 0.1794 0.1563 -0.0138 0.0464  0.0282  42  TYR   A CE1 
1072 C CE2 . TYR   A 42  ? 0.2212 0.1865 0.1752 -0.0159 0.0249  0.0242  42  TYR   A CE2 
1073 C CZ  . TYR   A 42  ? 0.2294 0.1901 0.1570 -0.0198 0.0414  0.0271  42  TYR   A CZ  
1074 O OH  . TYR   A 42  ? 0.2448 0.2143 0.1895 -0.0340 0.0363  0.0209  42  TYR   A OH  
1085 N N   . LEU   A 43  ? 0.1381 0.1262 0.1414 -0.0064 0.0161  0.0090  43  LEU   A N   
1086 C CA  . LEU   A 43  ? 0.1326 0.1254 0.1452 -0.0077 0.0111  0.0099  43  LEU   A CA  
1087 C C   . LEU   A 43  ? 0.1294 0.1307 0.1521 -0.0028 0.0127  0.0047  43  LEU   A C   
1088 O O   . LEU   A 43  ? 0.1480 0.1353 0.1723 0.0031  -0.0036 0.0028  43  LEU   A O   
1089 C CB  . LEU   A 43  ? 0.1399 0.1282 0.1606 -0.0057 0.0139  0.0087  43  LEU   A CB  
1090 C CG  . LEU   A 43  ? 0.1394 0.1283 0.1637 -0.0025 0.0107  0.0096  43  LEU   A CG  
1091 C CD1 . LEU   A 43  ? 0.1481 0.1368 0.1822 -0.0022 -0.0049 0.0183  43  LEU   A CD1 
1092 C CD2 . LEU   A 43  ? 0.1587 0.1335 0.1562 -0.0028 0.0094  0.0159  43  LEU   A CD2 
1104 N N   A LYS   A 44  ? 0.1336 0.1280 0.1429 0.0039  0.0145  0.0106  44  LYS   A N   
1105 N N   B LYS   A 44  ? 0.1421 0.1424 0.1554 -0.0044 0.0066  0.0053  44  LYS   A N   
1106 C CA  A LYS   A 44  ? 0.1444 0.1260 0.1452 -0.0009 0.0163  0.0189  44  LYS   A CA  
1107 C CA  B LYS   A 44  ? 0.1586 0.1533 0.1695 -0.0102 0.0017  0.0084  44  LYS   A CA  
1108 C C   A LYS   A 44  ? 0.1322 0.1255 0.1313 0.0091  0.0056  0.0103  44  LYS   A C   
1109 C C   B LYS   A 44  ? 0.1508 0.1496 0.1524 -0.0093 -0.0059 0.0097  44  LYS   A C   
1110 O O   A LYS   A 44  ? 0.1437 0.1410 0.1532 0.0036  0.0093  -0.0059 44  LYS   A O   
1111 O O   B LYS   A 44  ? 0.1533 0.1542 0.1523 -0.0115 -0.0093 0.0047  44  LYS   A O   
1112 C CB  A LYS   A 44  ? 0.1730 0.1383 0.1935 -0.0003 0.0266  0.0359  44  LYS   A CB  
1113 C CB  B LYS   A 44  ? 0.1831 0.1723 0.2117 -0.0101 0.0130  0.0125  44  LYS   A CB  
1114 C CG  A LYS   A 44  ? 0.2071 0.1688 0.2682 -0.0108 0.0528  0.0461  44  LYS   A CG  
1115 C CG  B LYS   A 44  ? 0.2071 0.1957 0.2650 -0.0112 0.0240  0.0182  44  LYS   A CG  
1116 C CD  A LYS   A 44  ? 0.2469 0.2242 0.3709 -0.0160 0.0433  0.0349  44  LYS   A CD  
1117 C CD  B LYS   A 44  ? 0.2327 0.2275 0.3246 -0.0124 0.0165  0.0152  44  LYS   A CD  
1118 C CE  A LYS   A 44  ? 0.2670 0.2578 0.4430 -0.0199 0.0425  0.0288  44  LYS   A CE  
1119 C CE  B LYS   A 44  ? 0.2462 0.2493 0.3663 -0.0152 0.0138  0.0165  44  LYS   A CE  
1120 N NZ  A LYS   A 44  ? 0.2765 0.2764 0.4794 -0.0184 0.0458  0.0276  44  LYS   A NZ  
1121 N NZ  B LYS   A 44  ? 0.2537 0.2638 0.3893 -0.0183 0.0149  0.0185  44  LYS   A NZ  
1148 N N   A HIS   A 45  ? 0.1197 0.1203 0.1387 0.0051  0.0033  0.0163  45  HIS   A N   
1149 N N   B HIS   A 45  ? 0.1470 0.1427 0.1506 -0.0098 -0.0099 0.0103  45  HIS   A N   
1150 C CA  A HIS   A 45  ? 0.1224 0.1268 0.1475 0.0052  0.0008  0.0136  45  HIS   A CA  
1151 C CA  B HIS   A 45  ? 0.1447 0.1423 0.1504 -0.0066 -0.0118 0.0095  45  HIS   A CA  
1152 C C   A HIS   A 45  ? 0.1300 0.1383 0.1664 0.0103  0.0068  0.0208  45  HIS   A C   
1153 C C   B HIS   A 45  ? 0.1455 0.1389 0.1566 -0.0092 -0.0078 0.0172  45  HIS   A C   
1154 O O   A HIS   A 45  ? 0.1379 0.1313 0.1870 0.0104  0.0120  0.0097  45  HIS   A O   
1155 O O   B HIS   A 45  ? 0.1487 0.1427 0.1667 -0.0008 0.0023  0.0181  45  HIS   A O   
1156 C CB  A HIS   A 45  ? 0.1214 0.1269 0.1317 -0.0007 0.0050  0.0065  45  HIS   A CB  
1157 C CB  B HIS   A 45  ? 0.1399 0.1444 0.1475 -0.0021 -0.0133 0.0014  45  HIS   A CB  
1158 C CG  A HIS   A 45  ? 0.1255 0.1198 0.1285 0.0002  0.0102  0.0075  45  HIS   A CG  
1159 C CG  B HIS   A 45  ? 0.1287 0.1402 0.1286 -0.0062 0.0061  -0.0045 45  HIS   A CG  
1160 N ND1 A HIS   A 45  ? 0.1221 0.1298 0.1414 -0.0005 0.0029  0.0125  45  HIS   A ND1 
1161 N ND1 B HIS   A 45  ? 0.1251 0.1426 0.1455 -0.0044 0.0000  0.0010  45  HIS   A ND1 
1162 C CD2 A HIS   A 45  ? 0.1308 0.1174 0.1351 -0.0049 0.0017  0.0163  45  HIS   A CD2 
1163 C CD2 B HIS   A 45  ? 0.1183 0.1286 0.1094 -0.0056 0.0107  -0.0183 45  HIS   A CD2 
1164 C CE1 A HIS   A 45  ? 0.1281 0.1306 0.1350 -0.0072 0.0041  0.0269  45  HIS   A CE1 
1165 C CE1 B HIS   A 45  ? 0.1191 0.1299 0.1171 -0.0080 0.0030  -0.0138 45  HIS   A CE1 
1166 N NE2 A HIS   A 45  ? 0.1342 0.1286 0.1381 0.0024  0.0043  0.0250  45  HIS   A NE2 
1167 N NE2 B HIS   A 45  ? 0.1154 0.1243 0.0954 -0.0091 0.0028  -0.0281 45  HIS   A NE2 
1182 N N   A GLY   A 46  ? 0.1335 0.1543 0.1836 0.0151  -0.0086 0.0291  46  GLY   A N   
1183 N N   B GLY   A 46  ? 0.1449 0.1301 0.1553 -0.0229 -0.0160 0.0161  46  GLY   A N   
1184 C CA  A GLY   A 46  ? 0.1392 0.1569 0.2003 0.0106  -0.0145 0.0383  46  GLY   A CA  
1185 C CA  B GLY   A 46  ? 0.1407 0.1345 0.1603 -0.0193 -0.0163 0.0120  46  GLY   A CA  
1186 C C   A GLY   A 46  ? 0.1437 0.1483 0.1959 0.0166  -0.0161 0.0441  46  GLY   A C   
1187 C C   B GLY   A 46  ? 0.1413 0.1380 0.1587 -0.0046 -0.0050 0.0243  46  GLY   A C   
1188 O O   A GLY   A 46  ? 0.1553 0.1505 0.2213 0.0138  -0.0200 0.0479  46  GLY   A O   
1189 O O   B GLY   A 46  ? 0.1472 0.1444 0.1622 -0.0000 -0.0029 0.0170  46  GLY   A O   
1196 N N   A GLY   A 47  ? 0.1420 0.1517 0.1872 0.0132  -0.0210 0.0374  47  GLY   A N   
1197 N N   B GLY   A 47  ? 0.1413 0.1397 0.1617 -0.0006 -0.0005 0.0188  47  GLY   A N   
1198 C CA  A GLY   A 47  ? 0.1449 0.1548 0.1768 0.0137  -0.0199 0.0276  47  GLY   A CA  
1199 C CA  B GLY   A 47  ? 0.1359 0.1411 0.1541 0.0012  -0.0011 0.0162  47  GLY   A CA  
1200 C C   A GLY   A 47  ? 0.1418 0.1497 0.1606 0.0143  -0.0164 0.0166  47  GLY   A C   
1201 C C   B GLY   A 47  ? 0.1314 0.1317 0.1437 -0.0001 0.0011  0.0173  47  GLY   A C   
1202 O O   A GLY   A 47  ? 0.1395 0.1453 0.1719 0.0207  -0.0146 0.0217  47  GLY   A O   
1203 O O   B GLY   A 47  ? 0.1297 0.1285 0.1380 -0.0071 0.0016  0.0220  47  GLY   A O   
1210 N N   A GLY   A 48  ? 0.1421 0.1541 0.1613 0.0157  -0.0143 0.0134  48  GLY   A N   
1211 N N   B GLY   A 48  ? 0.1344 0.1363 0.1414 0.0013  0.0017  0.0170  48  GLY   A N   
1212 C CA  A GLY   A 48  ? 0.1381 0.1529 0.1665 0.0113  -0.0078 0.0064  48  GLY   A CA  
1213 C CA  B GLY   A 48  ? 0.1285 0.1270 0.1352 -0.0034 0.0047  0.0062  48  GLY   A CA  
1214 C C   A GLY   A 48  ? 0.1354 0.1470 0.1557 0.0040  0.0065  0.0061  48  GLY   A C   
1215 C C   B GLY   A 48  ? 0.1308 0.1231 0.1385 -0.0104 0.0076  0.0084  48  GLY   A C   
1216 O O   A GLY   A 48  ? 0.1458 0.1399 0.1511 0.0011  0.0052  0.0072  48  GLY   A O   
1217 O O   B GLY   A 48  ? 0.1409 0.1228 0.1278 -0.0168 0.0176  0.0080  48  GLY   A O   
1224 N N   A VAL   A 49  ? 0.1319 0.1404 0.1713 0.0039  -0.0087 -0.0006 49  VAL   A N   
1225 N N   B VAL   A 49  ? 0.1237 0.1194 0.1494 -0.0093 -0.0011 0.0073  49  VAL   A N   
1226 C CA  A VAL   A 49  ? 0.1419 0.1368 0.1647 0.0010  0.0091  -0.0006 49  VAL   A CA  
1227 C CA  B VAL   A 49  ? 0.1200 0.1250 0.1525 -0.0066 0.0005  0.0078  49  VAL   A CA  
1228 C C   A VAL   A 49  ? 0.1368 0.1253 0.1437 0.0014  0.0043  -0.0029 49  VAL   A C   
1229 C C   B VAL   A 49  ? 0.1202 0.1229 0.1373 0.0019  0.0010  0.0003  49  VAL   A C   
1230 O O   A VAL   A 49  ? 0.1401 0.1291 0.1541 -0.0089 0.0102  0.0015  49  VAL   A O   
1231 O O   B VAL   A 49  ? 0.1149 0.1168 0.1264 0.0071  0.0126  0.0001  49  VAL   A O   
1232 C CB  A VAL   A 49  ? 0.1586 0.1413 0.1894 0.0008  0.0082  0.0031  49  VAL   A CB  
1233 C CB  B VAL   A 49  ? 0.1192 0.1227 0.1681 0.0014  -0.0082 0.0064  49  VAL   A CB  
1234 C CG1 A VAL   A 49  ? 0.1664 0.1334 0.2085 0.0068  0.0211  0.0013  49  VAL   A CG1 
1235 C CG1 B VAL   A 49  ? 0.1045 0.1173 0.1638 0.0128  -0.0018 -0.0006 49  VAL   A CG1 
1236 C CG2 A VAL   A 49  ? 0.1720 0.1495 0.2277 -0.0151 -0.0061 0.0064  49  VAL   A CG2 
1237 C CG2 B VAL   A 49  ? 0.1207 0.1222 0.1899 0.0003  -0.0172 0.0106  49  VAL   A CG2 
1256 N N   . ALA   A 50  ? 0.1308 0.1276 0.1335 -0.0008 -0.0014 0.0048  50  ALA   A N   
1257 C CA  . ALA   A 50  ? 0.1290 0.1307 0.1352 -0.0050 -0.0016 0.0139  50  ALA   A CA  
1258 C C   . ALA   A 50  ? 0.1264 0.1288 0.1325 -0.0062 -0.0009 -0.0000 50  ALA   A C   
1259 O O   . ALA   A 50  ? 0.1253 0.1323 0.1411 -0.0021 -0.0038 0.0021  50  ALA   A O   
1260 C CB  . ALA   A 50  ? 0.1248 0.1274 0.1396 -0.0041 0.0009  0.0028  50  ALA   A CB  
1267 N N   . GLY   A 51  ? 0.1289 0.1253 0.1531 0.0050  -0.0110 0.0053  51  GLY   A N   
1268 C CA  . GLY   A 51  ? 0.1408 0.1231 0.1592 0.0068  -0.0162 0.0008  51  GLY   A CA  
1269 C C   . GLY   A 51  ? 0.1313 0.1352 0.1536 0.0039  -0.0026 -0.0117 51  GLY   A C   
1270 O O   . GLY   A 51  ? 0.1351 0.1379 0.1677 0.0015  -0.0075 -0.0139 51  GLY   A O   
1274 N N   . ALA   A 52  ? 0.1286 0.1486 0.1486 0.0035  0.0008  -0.0200 52  ALA   A N   
1275 C CA  . ALA   A 52  ? 0.1310 0.1598 0.1654 -0.0021 0.0052  -0.0190 52  ALA   A CA  
1276 C C   . ALA   A 52  ? 0.1303 0.1550 0.1385 -0.0083 0.0110  -0.0152 52  ALA   A C   
1277 O O   . ALA   A 52  ? 0.1406 0.1602 0.1605 -0.0060 0.0126  -0.0192 52  ALA   A O   
1278 C CB  . ALA   A 52  ? 0.1374 0.1832 0.1802 -0.0047 0.0038  -0.0194 52  ALA   A CB  
1284 N N   A LEU   A 53  ? 0.1280 0.1488 0.1337 -0.0093 0.0063  -0.0079 53  LEU   A N   
1285 N N   B LEU   A 53  ? 0.1292 0.1493 0.1313 -0.0080 0.0058  -0.0075 53  LEU   A N   
1286 C CA  A LEU   A 53  ? 0.1411 0.1524 0.1292 -0.0075 0.0084  0.0016  53  LEU   A CA  
1287 C CA  B LEU   A 53  ? 0.1354 0.1489 0.1271 -0.0058 0.0035  0.0015  53  LEU   A CA  
1288 C C   A LEU   A 53  ? 0.1382 0.1541 0.1121 0.0003  0.0050  -0.0059 53  LEU   A C   
1289 C C   B LEU   A 53  ? 0.1354 0.1500 0.1180 -0.0020 0.0025  -0.0017 53  LEU   A C   
1290 O O   A LEU   A 53  ? 0.1544 0.1681 0.1308 -0.0124 0.0033  -0.0032 53  LEU   A O   
1291 O O   B LEU   A 53  ? 0.1442 0.1568 0.1265 -0.0084 0.0024  -0.0015 53  LEU   A O   
1292 C CB  A LEU   A 53  ? 0.1494 0.1542 0.1401 -0.0103 0.0098  0.0083  53  LEU   A CB  
1293 C CB  B LEU   A 53  ? 0.1380 0.1463 0.1319 -0.0053 0.0016  0.0056  53  LEU   A CB  
1294 C CG  A LEU   A 53  ? 0.1555 0.1533 0.1511 -0.0105 0.0150  0.0094  53  LEU   A CG  
1295 C CG  B LEU   A 53  ? 0.1383 0.1422 0.1276 -0.0048 -0.0012 0.0021  53  LEU   A CG  
1296 C CD1 A LEU   A 53  ? 0.1528 0.1549 0.1560 -0.0005 0.0038  0.0061  53  LEU   A CD1 
1297 C CD1 B LEU   A 53  ? 0.1415 0.1461 0.1228 -0.0056 0.0021  -0.0101 53  LEU   A CD1 
1298 C CD2 A LEU   A 53  ? 0.1717 0.1697 0.1631 -0.0158 0.0089  0.0061  53  LEU   A CD2 
1299 C CD2 B LEU   A 53  ? 0.1317 0.1405 0.1307 -0.0043 -0.0010 0.0026  53  LEU   A CD2 
1322 N N   . ASN   A 54  ? 0.1317 0.1451 0.1130 -0.0018 0.0036  0.0029  54  ASN   A N   
1323 C CA  . ASN   A 54  ? 0.1217 0.1395 0.1386 -0.0034 -0.0001 -0.0046 54  ASN   A CA  
1324 C C   . ASN   A 54  ? 0.1328 0.1463 0.1490 -0.0116 0.0059  -0.0017 54  ASN   A C   
1325 O O   . ASN   A 54  ? 0.1364 0.1506 0.1488 -0.0049 -0.0012 -0.0174 54  ASN   A O   
1326 C CB  . ASN   A 54  ? 0.1211 0.1395 0.1496 -0.0054 -0.0028 -0.0092 54  ASN   A CB  
1327 C CG  . ASN   A 54  ? 0.1247 0.1387 0.1546 -0.0024 0.0005  -0.0092 54  ASN   A CG  
1328 O OD1 . ASN   A 54  ? 0.1255 0.1417 0.1441 -0.0010 -0.0053 0.0003  54  ASN   A OD1 
1329 N ND2 . ASN   A 54  ? 0.1314 0.1418 0.1580 -0.0061 -0.0143 0.0076  54  ASN   A ND2 
1337 N N   . LYS   A 55  ? 0.1329 0.1481 0.1534 -0.0006 0.0004  -0.0179 55  LYS   A N   
1338 C CA  . LYS   A 55  ? 0.1417 0.1537 0.1548 0.0029  -0.0019 -0.0234 55  LYS   A CA  
1339 C C   . LYS   A 55  ? 0.1431 0.1606 0.1463 -0.0013 0.0064  -0.0260 55  LYS   A C   
1340 O O   . LYS   A 55  ? 0.1510 0.1724 0.1546 0.0052  0.0021  -0.0311 55  LYS   A O   
1341 C CB  . LYS   A 55  ? 0.1514 0.1584 0.1849 0.0130  -0.0014 -0.0234 55  LYS   A CB  
1342 C CG  . LYS   A 55  ? 0.1630 0.1846 0.2050 0.0228  -0.0100 -0.0279 55  LYS   A CG  
1343 C CD  . LYS   A 55  ? 0.1751 0.2111 0.2157 0.0318  -0.0061 -0.0323 55  LYS   A CD  
1344 C CE  . LYS   A 55  ? 0.1930 0.2445 0.2364 0.0364  -0.0190 -0.0351 55  LYS   A CE  
1345 N NZ  . LYS   A 55  ? 0.1988 0.2618 0.2449 0.0467  -0.0241 -0.0289 55  LYS   A NZ  
1359 N N   . ALA   A 56  ? 0.1491 0.1720 0.1471 -0.0099 0.0136  -0.0295 56  ALA   A N   
1360 C CA  . ALA   A 56  ? 0.1587 0.1907 0.1509 -0.0152 0.0176  -0.0247 56  ALA   A CA  
1361 C C   . ALA   A 56  ? 0.1641 0.2031 0.1320 -0.0167 0.0185  -0.0295 56  ALA   A C   
1362 O O   . ALA   A 56  ? 0.1727 0.2320 0.1445 -0.0024 0.0210  -0.0192 56  ALA   A O   
1363 C CB  . ALA   A 56  ? 0.1683 0.2045 0.1621 -0.0191 0.0167  -0.0131 56  ALA   A CB  
1369 N N   . THR   A 57  ? 0.1483 0.1793 0.1355 -0.0106 0.0114  -0.0186 57  THR   A N   
1370 C CA  . THR   A 57  ? 0.1536 0.1731 0.1455 -0.0108 0.0052  -0.0125 57  THR   A CA  
1371 C C   . THR   A 57  ? 0.1516 0.1794 0.1471 -0.0061 0.0033  -0.0224 57  THR   A C   
1372 O O   . THR   A 57  ? 0.1475 0.1819 0.1711 -0.0088 -0.0049 -0.0333 57  THR   A O   
1373 C CB  . THR   A 57  ? 0.1510 0.1712 0.1369 -0.0065 0.0059  -0.0141 57  THR   A CB  
1374 O OG1 . THR   A 57  ? 0.1413 0.1644 0.1342 -0.0072 0.0022  -0.0154 57  THR   A OG1 
1375 C CG2 . THR   A 57  ? 0.1546 0.1775 0.1315 -0.0071 0.0022  -0.0071 57  THR   A CG2 
1383 N N   . ASN   A 58  ? 0.1551 0.1751 0.1665 -0.0108 0.0066  -0.0372 58  ASN   A N   
1384 C CA  . ASN   A 58  ? 0.1733 0.1708 0.1851 -0.0110 0.0142  -0.0400 58  ASN   A CA  
1385 C C   . ASN   A 58  ? 0.1525 0.1564 0.1708 -0.0028 0.0013  -0.0286 58  ASN   A C   
1386 O O   . ASN   A 58  ? 0.1530 0.1680 0.1883 -0.0113 -0.0039 -0.0319 58  ASN   A O   
1387 C CB  . ASN   A 58  ? 0.2188 0.1853 0.2152 -0.0188 0.0405  -0.0548 58  ASN   A CB  
1388 C CG  . ASN   A 58  ? 0.2620 0.2083 0.2903 -0.0130 0.0422  -0.0430 58  ASN   A CG  
1389 O OD1 . ASN   A 58  ? 0.2854 0.2010 0.3274 0.0185  0.0648  -0.0442 58  ASN   A OD1 
1390 N ND2 . ASN   A 58  ? 0.2766 0.2221 0.3173 -0.0153 0.0314  -0.0377 58  ASN   A ND2 
1397 N N   . ASN   A 59  ? 0.1385 0.1478 0.1638 -0.0050 -0.0098 -0.0204 59  ASN   A N   
1398 C CA  . ASN   A 59  ? 0.1379 0.1367 0.1603 0.0002  -0.0032 -0.0104 59  ASN   A CA  
1399 C C   . ASN   A 59  ? 0.1378 0.1403 0.1501 -0.0044 -0.0115 -0.0089 59  ASN   A C   
1400 O O   . ASN   A 59  ? 0.1353 0.1472 0.1476 -0.0041 -0.0001 -0.0007 59  ASN   A O   
1401 C CB  . ASN   A 59  ? 0.1405 0.1362 0.1699 0.0030  -0.0134 -0.0176 59  ASN   A CB  
1402 C CG  . ASN   A 59  ? 0.1480 0.1402 0.1794 -0.0013 -0.0237 -0.0006 59  ASN   A CG  
1403 O OD1 . ASN   A 59  ? 0.1561 0.1456 0.1633 -0.0096 -0.0248 0.0043  59  ASN   A OD1 
1404 N ND2 . ASN   A 59  ? 0.1590 0.1445 0.1782 -0.0087 -0.0186 0.0063  59  ASN   A ND2 
1411 N N   . ALA   A 60  ? 0.1313 0.1485 0.1456 0.0001  -0.0090 -0.0068 60  ALA   A N   
1412 C CA  . ALA   A 60  ? 0.1342 0.1472 0.1556 -0.0041 -0.0130 -0.0050 60  ALA   A CA  
1413 C C   . ALA   A 60  ? 0.1348 0.1404 0.1560 -0.0039 -0.0038 -0.0089 60  ALA   A C   
1414 O O   . ALA   A 60  ? 0.1334 0.1450 0.1716 -0.0057 -0.0071 -0.0150 60  ALA   A O   
1415 C CB  . ALA   A 60  ? 0.1471 0.1574 0.1581 -0.0070 -0.0199 -0.0181 60  ALA   A CB  
1421 N N   . MET   A 61  ? 0.1339 0.1375 0.1448 -0.0033 -0.0013 -0.0061 61  MET   A N   
1422 C CA  . MET   A 61  ? 0.1323 0.1290 0.1480 -0.0078 -0.0010 -0.0012 61  MET   A CA  
1423 C C   . MET   A 61  ? 0.1290 0.1273 0.1508 -0.0044 -0.0029 -0.0056 61  MET   A C   
1424 O O   . MET   A 61  ? 0.1333 0.1292 0.1511 -0.0043 0.0063  -0.0011 61  MET   A O   
1425 C CB  . MET   A 61  ? 0.1409 0.1358 0.1376 -0.0042 0.0047  -0.0014 61  MET   A CB  
1426 C CG  . MET   A 61  ? 0.1386 0.1424 0.1530 -0.0009 0.0008  -0.0018 61  MET   A CG  
1427 S SD  . MET   A 61  ? 0.1389 0.1432 0.1899 -0.0116 0.0007  -0.0197 61  MET   A SD  
1428 C CE  . MET   A 61  ? 0.1631 0.1598 0.2102 -0.0181 0.0140  -0.0153 61  MET   A CE  
1438 N N   . GLN   A 62  ? 0.1289 0.1299 0.1465 -0.0086 -0.0025 -0.0046 62  GLN   A N   
1439 C CA  . GLN   A 62  ? 0.1349 0.1273 0.1573 -0.0069 -0.0020 0.0004  62  GLN   A CA  
1440 C C   . GLN   A 62  ? 0.1365 0.1191 0.1636 -0.0045 0.0031  0.0026  62  GLN   A C   
1441 O O   . GLN   A 62  ? 0.1343 0.1372 0.1570 -0.0038 0.0028  -0.0009 62  GLN   A O   
1442 C CB  . GLN   A 62  ? 0.1349 0.1204 0.1531 -0.0008 -0.0008 -0.0004 62  GLN   A CB  
1443 C CG  . GLN   A 62  ? 0.1353 0.1218 0.1559 -0.0045 -0.0040 0.0088  62  GLN   A CG  
1444 C CD  . GLN   A 62  ? 0.1431 0.1291 0.1556 0.0037  0.0035  0.0072  62  GLN   A CD  
1445 O OE1 . GLN   A 62  ? 0.1453 0.1392 0.1605 -0.0013 -0.0002 0.0046  62  GLN   A OE1 
1446 N NE2 . GLN   A 62  ? 0.1483 0.1344 0.1699 0.0011  -0.0011 -0.0022 62  GLN   A NE2 
1455 N N   . VAL   A 63  ? 0.1295 0.1289 0.1688 -0.0057 0.0080  -0.0197 63  VAL   A N   
1456 C CA  . VAL   A 63  ? 0.1326 0.1366 0.1885 -0.0137 0.0010  -0.0189 63  VAL   A CA  
1457 C C   . VAL   A 63  ? 0.1216 0.1372 0.1768 -0.0129 -0.0075 -0.0169 63  VAL   A C   
1458 O O   . VAL   A 63  ? 0.1205 0.1407 0.1888 -0.0159 -0.0030 -0.0114 63  VAL   A O   
1459 C CB  . VAL   A 63  ? 0.1475 0.1552 0.2165 -0.0137 -0.0029 -0.0382 63  VAL   A CB  
1460 C CG1 . VAL   A 63  ? 0.1640 0.1732 0.2462 -0.0148 -0.0100 -0.0547 63  VAL   A CG1 
1461 C CG2 . VAL   A 63  ? 0.1551 0.1463 0.2376 -0.0166 0.0141  -0.0372 63  VAL   A CG2 
1471 N N   . GLU   A 64  ? 0.1276 0.1410 0.1712 -0.0052 -0.0053 -0.0093 64  GLU   A N   
1472 C CA  . GLU   A 64  ? 0.1291 0.1424 0.1720 -0.0090 -0.0080 -0.0037 64  GLU   A CA  
1473 C C   . GLU   A 64  ? 0.1206 0.1343 0.1706 -0.0124 -0.0002 0.0001  64  GLU   A C   
1474 O O   . GLU   A 64  ? 0.1281 0.1434 0.1706 -0.0036 0.0002  -0.0021 64  GLU   A O   
1475 C CB  . GLU   A 64  ? 0.1376 0.1523 0.1730 -0.0089 -0.0013 -0.0042 64  GLU   A CB  
1476 C CG  . GLU   A 64  ? 0.1458 0.1578 0.1803 -0.0099 0.0026  -0.0019 64  GLU   A CG  
1477 C CD  . GLU   A 64  ? 0.1555 0.1660 0.1895 -0.0158 0.0060  -0.0034 64  GLU   A CD  
1478 O OE1 . GLU   A 64  ? 0.1539 0.1768 0.2011 -0.0165 0.0129  -0.0039 64  GLU   A OE1 
1479 O OE2 . GLU   A 64  ? 0.1704 0.1655 0.1865 -0.0217 -0.0052 0.0034  64  GLU   A OE2 
1486 N N   . SER   A 65  ? 0.1202 0.1388 0.1534 -0.0009 0.0025  -0.0032 65  SER   A N   
1487 C CA  . SER   A 65  ? 0.1270 0.1306 0.1555 -0.0044 -0.0030 -0.0050 65  SER   A CA  
1488 C C   . SER   A 65  ? 0.1241 0.1390 0.1676 -0.0028 -0.0069 0.0023  65  SER   A C   
1489 O O   . SER   A 65  ? 0.1320 0.1423 0.1747 0.0031  0.0104  -0.0051 65  SER   A O   
1490 C CB  . SER   A 65  ? 0.1284 0.1313 0.1566 -0.0097 0.0034  0.0055  65  SER   A CB  
1491 O OG  . SER   A 65  ? 0.1268 0.1423 0.1611 -0.0091 -0.0030 0.0084  65  SER   A OG  
1497 N N   . ASP   A 66  ? 0.1317 0.1311 0.1751 -0.0049 0.0121  0.0086  66  ASP   A N   
1498 C CA  . ASP   A 66  ? 0.1403 0.1436 0.1845 -0.0050 0.0092  0.0199  66  ASP   A CA  
1499 C C   . ASP   A 66  ? 0.1350 0.1354 0.1818 -0.0091 0.0116  0.0172  66  ASP   A C   
1500 O O   . ASP   A 66  ? 0.1413 0.1534 0.1947 -0.0027 0.0227  0.0231  66  ASP   A O   
1501 C CB  . ASP   A 66  ? 0.1515 0.1530 0.2132 0.0031  0.0093  0.0278  66  ASP   A CB  
1502 C CG  . ASP   A 66  ? 0.1759 0.1699 0.2374 0.0051  -0.0010 0.0475  66  ASP   A CG  
1503 O OD1 . ASP   A 66  ? 0.1737 0.1978 0.2170 -0.0042 -0.0079 0.0499  66  ASP   A OD1 
1504 O OD2 . ASP   A 66  ? 0.1903 0.1819 0.3201 0.0266  -0.0231 0.0256  66  ASP   A OD2 
1509 N N   . ASP   A 67  ? 0.1320 0.1387 0.1933 -0.0062 0.0057  0.0148  67  ASP   A N   
1510 C CA  . ASP   A 67  ? 0.1332 0.1561 0.2070 -0.0040 -0.0021 0.0225  67  ASP   A CA  
1511 C C   . ASP   A 67  ? 0.1312 0.1582 0.1990 -0.0022 0.0031  0.0260  67  ASP   A C   
1512 O O   . ASP   A 67  ? 0.1299 0.1648 0.2203 0.0004  0.0193  0.0339  67  ASP   A O   
1513 C CB  . ASP   A 67  ? 0.1402 0.1662 0.2359 -0.0094 -0.0166 0.0267  67  ASP   A CB  
1514 C CG  . ASP   A 67  ? 0.1375 0.1806 0.2632 -0.0082 -0.0355 0.0340  67  ASP   A CG  
1515 O OD1 . ASP   A 67  ? 0.1483 0.2012 0.3334 -0.0159 -0.0394 0.0461  67  ASP   A OD1 
1516 O OD2 . ASP   A 67  ? 0.1404 0.1833 0.2572 -0.0020 -0.0210 0.0219  67  ASP   A OD2 
1521 N N   . TYR   A 68  ? 0.1327 0.1463 0.1824 0.0010  0.0170  0.0246  68  TYR   A N   
1522 C CA  . TYR   A 68  ? 0.1459 0.1403 0.1798 0.0019  0.0174  0.0282  68  TYR   A CA  
1523 C C   . TYR   A 68  ? 0.1417 0.1442 0.1856 0.0004  0.0249  0.0167  68  TYR   A C   
1524 O O   . TYR   A 68  ? 0.1480 0.1475 0.1929 0.0078  0.0309  0.0169  68  TYR   A O   
1525 C CB  . TYR   A 68  ? 0.1496 0.1400 0.1972 0.0094  0.0447  0.0276  68  TYR   A CB  
1526 C CG  . TYR   A 68  ? 0.1480 0.1585 0.2276 0.0077  0.0514  0.0308  68  TYR   A CG  
1527 C CD1 . TYR   A 68  ? 0.1649 0.1709 0.2561 -0.0178 0.0403  -0.0069 68  TYR   A CD1 
1528 C CD2 . TYR   A 68  ? 0.1756 0.1612 0.2624 0.0132  0.0541  0.0429  68  TYR   A CD2 
1529 C CE1 . TYR   A 68  ? 0.1726 0.1776 0.2831 -0.0167 0.0497  -0.0064 68  TYR   A CE1 
1530 C CE2 . TYR   A 68  ? 0.1721 0.1628 0.2806 0.0048  0.0601  0.0250  68  TYR   A CE2 
1531 C CZ  . TYR   A 68  ? 0.1753 0.1692 0.3005 -0.0184 0.0559  -0.0026 68  TYR   A CZ  
1532 O OH  . TYR   A 68  ? 0.1995 0.1649 0.3227 -0.0153 0.0331  -0.0317 68  TYR   A OH  
1542 N N   . ILE   A 69  ? 0.1345 0.1368 0.1839 -0.0026 0.0156  0.0234  69  ILE   A N   
1543 C CA  . ILE   A 69  ? 0.1409 0.1413 0.1818 0.0023  0.0133  0.0111  69  ILE   A CA  
1544 C C   . ILE   A 69  ? 0.1452 0.1456 0.1708 0.0046  0.0185  0.0220  69  ILE   A C   
1545 O O   . ILE   A 69  ? 0.1483 0.1540 0.1667 -0.0019 0.0211  0.0229  69  ILE   A O   
1546 C CB  . ILE   A 69  ? 0.1466 0.1634 0.1768 0.0020  0.0122  -0.0020 69  ILE   A CB  
1547 C CG1 . ILE   A 69  ? 0.1501 0.1749 0.1895 0.0086  0.0137  -0.0189 69  ILE   A CG1 
1548 C CG2 . ILE   A 69  ? 0.1687 0.1859 0.1897 0.0146  0.0022  -0.0096 69  ILE   A CG2 
1549 C CD1 . ILE   A 69  ? 0.1509 0.1845 0.2044 -0.0054 0.0147  -0.0263 69  ILE   A CD1 
1561 N N   . ALA   A 70  ? 0.1491 0.1423 0.1803 -0.0056 0.0211  0.0177  70  ALA   A N   
1562 C CA  . ALA   A 70  ? 0.1545 0.1521 0.1898 -0.0183 0.0295  0.0268  70  ALA   A CA  
1563 C C   . ALA   A 70  ? 0.1492 0.1698 0.1836 -0.0156 0.0248  0.0239  70  ALA   A C   
1564 O O   . ALA   A 70  ? 0.1668 0.2056 0.2115 0.0025  0.0419  0.0394  70  ALA   A O   
1565 C CB  . ALA   A 70  ? 0.1583 0.1452 0.2309 -0.0234 0.0264  0.0112  70  ALA   A CB  
1571 N N   . THR   A 71  ? 0.1406 0.1654 0.1780 -0.0044 0.0178  0.0237  71  THR   A N   
1572 C CA  . THR   A 71  ? 0.1483 0.1825 0.2088 0.0049  0.0221  0.0225  71  THR   A CA  
1573 C C   . THR   A 71  ? 0.1443 0.1778 0.2277 0.0118  0.0313  0.0130  71  THR   A C   
1574 O O   . THR   A 71  ? 0.1498 0.2034 0.2691 0.0078  0.0458  -0.0114 71  THR   A O   
1575 C CB  . THR   A 71  ? 0.1746 0.2028 0.2369 0.0147  -0.0095 0.0270  71  THR   A CB  
1576 O OG1 . THR   A 71  ? 0.2008 0.2200 0.2490 0.0086  -0.0339 0.0164  71  THR   A OG1 
1577 C CG2 . THR   A 71  ? 0.1878 0.2193 0.2664 0.0200  -0.0140 0.0321  71  THR   A CG2 
1585 N N   . ASN   A 72  ? 0.1442 0.1581 0.2058 0.0116  0.0310  0.0170  72  ASN   A N   
1586 C CA  . ASN   A 72  ? 0.1491 0.1595 0.2162 0.0153  0.0357  0.0168  72  ASN   A CA  
1587 C C   . ASN   A 72  ? 0.1639 0.1584 0.2052 0.0091  0.0448  0.0085  72  ASN   A C   
1588 O O   . ASN   A 72  ? 0.1785 0.1579 0.2287 0.0122  0.0386  -0.0027 72  ASN   A O   
1589 C CB  . ASN   A 72  ? 0.1690 0.1649 0.2153 0.0111  0.0404  0.0138  72  ASN   A CB  
1590 C CG  . ASN   A 72  ? 0.1933 0.1782 0.2157 0.0227  0.0309  0.0172  72  ASN   A CG  
1591 O OD1 . ASN   A 72  ? 0.2099 0.2127 0.2226 0.0222  0.0389  0.0212  72  ASN   A OD1 
1592 N ND2 . ASN   A 72  ? 0.2113 0.1793 0.2149 0.0458  0.0121  0.0111  72  ASN   A ND2 
1599 N N   . GLY   A 73  ? 0.1636 0.1569 0.1980 0.0051  0.0434  0.0109  73  GLY   A N   
1600 C CA  . GLY   A 73  ? 0.1670 0.1572 0.1869 -0.0035 0.0373  0.0094  73  GLY   A CA  
1601 C C   . GLY   A 73  ? 0.1672 0.1452 0.1749 0.0037  0.0438  0.0174  73  GLY   A C   
1602 O O   . GLY   A 73  ? 0.1635 0.1506 0.1877 0.0112  0.0375  0.0261  73  GLY   A O   
1606 N N   . PRO   A 74  ? 0.1764 0.1468 0.1691 -0.0091 0.0459  0.0151  74  PRO   A N   
1607 C CA  . PRO   A 74  ? 0.1729 0.1460 0.1806 0.0007  0.0378  0.0193  74  PRO   A CA  
1608 C C   . PRO   A 74  ? 0.1653 0.1352 0.1793 0.0047  0.0282  0.0050  74  PRO   A C   
1609 O O   . PRO   A 74  ? 0.1760 0.1383 0.1996 0.0047  0.0373  -0.0061 74  PRO   A O   
1610 C CB  . PRO   A 74  ? 0.1885 0.1766 0.2043 0.0040  0.0408  0.0263  74  PRO   A CB  
1611 C CG  . PRO   A 74  ? 0.2150 0.2090 0.2410 -0.0148 0.0314  0.0096  74  PRO   A CG  
1612 C CD  . PRO   A 74  ? 0.1964 0.1855 0.1938 -0.0209 0.0329  0.0002  74  PRO   A CD  
1620 N N   . LEU   A 75  ? 0.1582 0.1264 0.1618 0.0032  0.0276  0.0079  75  LEU   A N   
1621 C CA  . LEU   A 75  ? 0.1653 0.1263 0.1498 -0.0002 0.0079  0.0050  75  LEU   A CA  
1622 C C   . LEU   A 75  ? 0.1752 0.1375 0.1546 0.0082  0.0107  0.0140  75  LEU   A C   
1623 O O   . LEU   A 75  ? 0.2087 0.1533 0.1601 0.0097  0.0047  0.0103  75  LEU   A O   
1624 C CB  . LEU   A 75  ? 0.1650 0.1323 0.1484 -0.0074 0.0069  0.0164  75  LEU   A CB  
1625 C CG  . LEU   A 75  ? 0.1818 0.1654 0.1632 -0.0368 0.0047  0.0173  75  LEU   A CG  
1626 C CD1 . LEU   A 75  ? 0.1913 0.2186 0.1750 -0.0318 0.0005  0.0061  75  LEU   A CD1 
1627 C CD2 . LEU   A 75  ? 0.2095 0.2109 0.2138 -0.0153 0.0104  0.0278  75  LEU   A CD2 
1639 N N   . LYS   A 76  ? 0.1786 0.1339 0.1696 -0.0065 0.0072  0.0026  76  LYS   A N   
1640 C CA  . LYS   A 76  ? 0.1741 0.1577 0.1689 -0.0118 0.0094  -0.0110 76  LYS   A CA  
1641 C C   . LYS   A 76  ? 0.1698 0.1401 0.1403 -0.0001 0.0113  -0.0035 76  LYS   A C   
1642 O O   . LYS   A 76  ? 0.1755 0.1399 0.1356 -0.0027 0.0163  0.0057  76  LYS   A O   
1643 C CB  . LYS   A 76  ? 0.1772 0.1789 0.2079 -0.0000 0.0112  -0.0366 76  LYS   A CB  
1644 C CG  . LYS   A 76  ? 0.1896 0.1760 0.2651 0.0011  0.0126  -0.0299 76  LYS   A CG  
1645 C CD  . LYS   A 76  ? 0.1944 0.1768 0.3104 0.0038  0.0046  -0.0419 76  LYS   A CD  
1646 C CE  . LYS   A 76  ? 0.2112 0.1974 0.3617 -0.0031 0.0046  -0.0549 76  LYS   A CE  
1647 N NZ  . LYS   A 76  ? 0.2144 0.1944 0.3974 -0.0150 0.0038  -0.0656 76  LYS   A NZ  
1661 N N   . VAL   A 77  ? 0.1778 0.1518 0.1390 -0.0019 0.0223  0.0115  77  VAL   A N   
1662 C CA  . VAL   A 77  ? 0.1747 0.1517 0.1423 0.0040  0.0195  0.0099  77  VAL   A CA  
1663 C C   . VAL   A 77  ? 0.1726 0.1481 0.1425 0.0055  0.0153  -0.0000 77  VAL   A C   
1664 O O   . VAL   A 77  ? 0.1783 0.1500 0.1465 0.0094  0.0252  -0.0080 77  VAL   A O   
1665 C CB  . VAL   A 77  ? 0.1955 0.1718 0.1563 0.0006  0.0128  0.0159  77  VAL   A CB  
1666 C CG1 . VAL   A 77  ? 0.1909 0.1859 0.1793 0.0142  0.0092  0.0148  77  VAL   A CG1 
1667 C CG2 . VAL   A 77  ? 0.2206 0.1829 0.1761 -0.0035 -0.0007 0.0247  77  VAL   A CG2 
1677 N N   . GLY   A 78  ? 0.1703 0.1410 0.1401 0.0035  0.0239  0.0055  78  GLY   A N   
1678 C CA  . GLY   A 78  ? 0.1638 0.1373 0.1547 0.0039  0.0240  0.0082  78  GLY   A CA  
1679 C C   . GLY   A 78  ? 0.1500 0.1310 0.1539 0.0057  0.0199  0.0034  78  GLY   A C   
1680 O O   . GLY   A 78  ? 0.1516 0.1327 0.1777 0.0020  0.0185  0.0232  78  GLY   A O   
1684 N N   . GLY   A 79  ? 0.1499 0.1302 0.1516 0.0012  0.0185  0.0117  79  GLY   A N   
1685 C CA  . GLY   A 79  ? 0.1487 0.1340 0.1587 -0.0020 0.0217  0.0113  79  GLY   A CA  
1686 C C   . GLY   A 79  ? 0.1386 0.1298 0.1532 0.0014  0.0152  0.0033  79  GLY   A C   
1687 O O   . GLY   A 79  ? 0.1446 0.1401 0.1592 0.0183  0.0147  0.0020  79  GLY   A O   
1691 N N   . SER   A 80  ? 0.1335 0.1471 0.1714 -0.0000 0.0172  0.0018  80  SER   A N   
1692 C CA  . SER   A 80  ? 0.1317 0.1400 0.1581 -0.0022 0.0098  0.0043  80  SER   A CA  
1693 C C   . SER   A 80  ? 0.1342 0.1376 0.1575 -0.0056 0.0101  0.0094  80  SER   A C   
1694 O O   . SER   A 80  ? 0.1304 0.1616 0.1876 0.0052  0.0162  -0.0028 80  SER   A O   
1695 C CB  . SER   A 80  ? 0.1448 0.1379 0.1946 -0.0083 0.0090  0.0109  80  SER   A CB  
1696 O OG  . SER   A 80  ? 0.1693 0.1371 0.2253 0.0016  -0.0016 0.0212  80  SER   A OG  
1702 N N   . CYS   A 81  ? 0.1269 0.1364 0.1555 0.0028  0.0004  0.0101  81  CYS   A N   
1703 C CA  . CYS   A 81  ? 0.1300 0.1449 0.1515 -0.0061 -0.0032 0.0220  81  CYS   A CA  
1704 C C   . CYS   A 81  ? 0.1310 0.1400 0.1586 -0.0116 -0.0025 0.0267  81  CYS   A C   
1705 O O   . CYS   A 81  ? 0.1294 0.1663 0.1668 -0.0029 0.0024  0.0320  81  CYS   A O   
1706 C CB  . CYS   A 81  ? 0.1330 0.1504 0.1731 -0.0099 -0.0021 0.0208  81  CYS   A CB  
1707 S SG  . CYS   A 81  ? 0.1502 0.1383 0.1732 -0.0123 0.0025  0.0139  81  CYS   A SG  
1713 N N   . VAL   A 82  ? 0.1307 0.1502 0.1491 -0.0037 -0.0107 0.0197  82  VAL   A N   
1714 C CA  . VAL   A 82  ? 0.1472 0.1526 0.1565 -0.0017 -0.0075 0.0266  82  VAL   A CA  
1715 C C   . VAL   A 82  ? 0.1460 0.1575 0.1687 0.0005  -0.0113 0.0260  82  VAL   A C   
1716 O O   . VAL   A 82  ? 0.1360 0.1660 0.1876 -0.0021 -0.0065 0.0044  82  VAL   A O   
1717 C CB  . VAL   A 82  ? 0.1823 0.1657 0.1656 0.0009  0.0002  0.0279  82  VAL   A CB  
1718 C CG1 . VAL   A 82  ? 0.2018 0.1800 0.1814 0.0074  0.0001  0.0284  82  VAL   A CG1 
1719 C CG2 . VAL   A 82  ? 0.1892 0.1659 0.1952 -0.0080 -0.0000 0.0310  82  VAL   A CG2 
1729 N N   . LEU   A 83  ? 0.1415 0.1486 0.1456 -0.0080 -0.0099 0.0159  83  LEU   A N   
1730 C CA  . LEU   A 83  ? 0.1435 0.1540 0.1403 -0.0082 -0.0081 0.0149  83  LEU   A CA  
1731 C C   . LEU   A 83  ? 0.1469 0.1580 0.1416 -0.0131 -0.0049 0.0209  83  LEU   A C   
1732 O O   . LEU   A 83  ? 0.1610 0.1589 0.1512 -0.0139 -0.0016 0.0208  83  LEU   A O   
1733 C CB  . LEU   A 83  ? 0.1527 0.1593 0.1412 -0.0136 -0.0117 0.0148  83  LEU   A CB  
1734 C CG  . LEU   A 83  ? 0.1640 0.1658 0.1520 -0.0126 0.0021  0.0135  83  LEU   A CG  
1735 C CD1 . LEU   A 83  ? 0.1753 0.1716 0.1588 -0.0239 0.0020  0.0202  83  LEU   A CD1 
1736 C CD2 . LEU   A 83  ? 0.1631 0.1777 0.1717 -0.0103 0.0111  0.0122  83  LEU   A CD2 
1748 N N   . SER   A 84  ? 0.1601 0.1642 0.1384 -0.0173 -0.0023 0.0212  84  SER   A N   
1749 C CA  . SER   A 84  ? 0.1724 0.1686 0.1365 -0.0164 -0.0040 0.0198  84  SER   A CA  
1750 C C   . SER   A 84  ? 0.1743 0.1661 0.1359 -0.0167 0.0055  0.0124  84  SER   A C   
1751 O O   . SER   A 84  ? 0.1742 0.1769 0.1299 -0.0112 -0.0070 0.0101  84  SER   A O   
1752 C CB  . SER   A 84  ? 0.1769 0.1903 0.1469 -0.0120 -0.0068 0.0049  84  SER   A CB  
1753 O OG  . SER   A 84  ? 0.1841 0.2126 0.1546 -0.0119 -0.0161 -0.0088 84  SER   A OG  
1759 N N   . GLY   A 85  ? 0.1889 0.1800 0.1343 -0.0208 0.0094  0.0034  85  GLY   A N   
1760 C CA  . GLY   A 85  ? 0.1918 0.1907 0.1482 -0.0277 0.0128  -0.0027 85  GLY   A CA  
1761 C C   . GLY   A 85  ? 0.1899 0.1944 0.1318 -0.0230 0.0048  -0.0011 85  GLY   A C   
1762 O O   . GLY   A 85  ? 0.1873 0.2044 0.1400 -0.0263 0.0169  -0.0118 85  GLY   A O   
1766 N N   . HIS   A 86  ? 0.1971 0.1840 0.1190 -0.0216 0.0036  0.0047  86  HIS   A N   
1767 C CA  . HIS   A 86  ? 0.2108 0.1948 0.1134 -0.0242 0.0063  0.0048  86  HIS   A CA  
1768 C C   . HIS   A 86  ? 0.2333 0.2053 0.1217 -0.0232 -0.0013 -0.0008 86  HIS   A C   
1769 O O   . HIS   A 86  ? 0.2438 0.2273 0.1334 -0.0148 0.0095  0.0048  86  HIS   A O   
1770 C CB  . HIS   A 86  ? 0.2068 0.1891 0.1308 -0.0185 0.0095  0.0022  86  HIS   A CB  
1771 C CG  . HIS   A 86  ? 0.1962 0.1876 0.1484 -0.0104 0.0052  0.0077  86  HIS   A CG  
1772 N ND1 . HIS   A 86  ? 0.1972 0.1890 0.1772 -0.0203 0.0037  0.0107  86  HIS   A ND1 
1773 C CD2 . HIS   A 86  ? 0.1910 0.1823 0.1449 -0.0022 0.0077  0.0109  86  HIS   A CD2 
1774 C CE1 . HIS   A 86  ? 0.1864 0.1870 0.1689 -0.0151 0.0176  0.0166  86  HIS   A CE1 
1775 N NE2 . HIS   A 86  ? 0.1852 0.1788 0.1549 0.0015  0.0150  0.0259  86  HIS   A NE2 
1783 N N   . ASN   A 87  ? 0.2475 0.2116 0.1402 -0.0213 0.0253  -0.0104 87  ASN   A N   
1784 C CA  . ASN   A 87  ? 0.2664 0.2234 0.1438 -0.0171 0.0533  -0.0121 87  ASN   A CA  
1785 C C   . ASN   A 87  ? 0.2651 0.2427 0.1600 -0.0222 0.0741  -0.0020 87  ASN   A C   
1786 O O   . ASN   A 87  ? 0.2856 0.2619 0.2130 -0.0351 0.0935  -0.0048 87  ASN   A O   
1787 C CB  . ASN   A 87  ? 0.2850 0.2326 0.1624 -0.0047 0.0509  -0.0163 87  ASN   A CB  
1788 C CG  . ASN   A 87  ? 0.2945 0.2418 0.1706 0.0065  0.0639  -0.0074 87  ASN   A CG  
1789 O OD1 . ASN   A 87  ? 0.3101 0.2402 0.1746 0.0240  0.0641  -0.0012 87  ASN   A OD1 
1790 N ND2 . ASN   A 87  ? 0.2963 0.2625 0.1918 0.0079  0.0594  -0.0056 87  ASN   A ND2 
1797 N N   . LEU   A 88  ? 0.2394 0.2381 0.1644 -0.0262 0.0536  0.0068  88  LEU   A N   
1798 C CA  . LEU   A 88  ? 0.2157 0.2376 0.1856 -0.0306 0.0471  0.0174  88  LEU   A CA  
1799 C C   . LEU   A 88  ? 0.2106 0.2378 0.1850 -0.0314 0.0437  0.0304  88  LEU   A C   
1800 O O   . LEU   A 88  ? 0.2148 0.2472 0.2176 -0.0296 0.0497  0.0454  88  LEU   A O   
1801 C CB  . LEU   A 88  ? 0.2137 0.2453 0.2010 -0.0355 0.0123  0.0312  88  LEU   A CB  
1802 C CG  . LEU   A 88  ? 0.2312 0.2577 0.2286 -0.0327 -0.0068 0.0308  88  LEU   A CG  
1803 C CD1 . LEU   A 88  ? 0.2421 0.2651 0.2205 -0.0339 -0.0128 0.0134  88  LEU   A CD1 
1804 C CD2 . LEU   A 88  ? 0.2456 0.2674 0.2646 -0.0253 -0.0067 0.0262  88  LEU   A CD2 
1816 N N   . ALA   A 89  ? 0.2151 0.2263 0.1588 -0.0290 0.0342  0.0162  89  ALA   A N   
1817 C CA  . ALA   A 89  ? 0.2269 0.2222 0.1437 -0.0210 0.0175  0.0226  89  ALA   A CA  
1818 C C   . ALA   A 89  ? 0.2338 0.2222 0.1464 -0.0184 -0.0012 0.0183  89  ALA   A C   
1819 O O   . ALA   A 89  ? 0.2351 0.2185 0.1768 -0.0263 -0.0078 -0.0044 89  ALA   A O   
1820 C CB  . ALA   A 89  ? 0.2197 0.2203 0.1321 -0.0187 0.0149  0.0271  89  ALA   A CB  
1826 N N   . LYS   A 90  ? 0.2439 0.2355 0.1436 -0.0232 -0.0205 0.0274  90  LYS   A N   
1827 C CA  . LYS   A 90  ? 0.2473 0.2483 0.1489 -0.0200 -0.0267 0.0249  90  LYS   A CA  
1828 C C   . LYS   A 90  ? 0.2213 0.2335 0.1483 -0.0212 -0.0214 0.0100  90  LYS   A C   
1829 O O   . LYS   A 90  ? 0.2215 0.2474 0.1777 -0.0212 -0.0314 -0.0001 90  LYS   A O   
1830 C CB  . LYS   A 90  ? 0.2683 0.2801 0.1969 -0.0164 -0.0287 0.0365  90  LYS   A CB  
1831 C CG  . LYS   A 90  ? 0.2960 0.3079 0.2919 -0.0130 -0.0188 0.0400  90  LYS   A CG  
1832 C CD  . LYS   A 90  ? 0.3227 0.3305 0.3803 -0.0134 -0.0031 0.0473  90  LYS   A CD  
1833 C CE  . LYS   A 90  ? 0.3403 0.3479 0.4541 -0.0137 0.0078  0.0440  90  LYS   A CE  
1834 N NZ  . LYS   A 90  ? 0.3559 0.3639 0.4964 -0.0127 0.0143  0.0352  90  LYS   A NZ  
1848 N N   . HIS   A 91  ? 0.2060 0.2069 0.1155 -0.0218 -0.0254 0.0175  91  HIS   A N   
1849 C CA  . HIS   A 91  ? 0.1953 0.1877 0.1258 -0.0194 -0.0260 0.0280  91  HIS   A CA  
1850 C C   . HIS   A 91  ? 0.1735 0.1745 0.1237 -0.0197 -0.0124 0.0263  91  HIS   A C   
1851 O O   . HIS   A 91  ? 0.1702 0.1865 0.1336 -0.0209 0.0005  0.0256  91  HIS   A O   
1852 C CB  . HIS   A 91  ? 0.2128 0.2149 0.1697 0.0021  -0.0460 0.0284  91  HIS   A CB  
1853 C CG  . HIS   A 91  ? 0.2528 0.2644 0.2406 0.0150  -0.0635 0.0156  91  HIS   A CG  
1854 N ND1 . HIS   A 91  ? 0.2654 0.2928 0.2833 0.0210  -0.0666 -0.0079 91  HIS   A ND1 
1855 C CD2 . HIS   A 91  ? 0.2747 0.2829 0.2598 0.0238  -0.0728 0.0214  91  HIS   A CD2 
1856 C CE1 . HIS   A 91  ? 0.2765 0.2994 0.2948 0.0273  -0.0675 0.0005  91  HIS   A CE1 
1857 N NE2 . HIS   A 91  ? 0.2855 0.2974 0.2851 0.0335  -0.0727 0.0103  91  HIS   A NE2 
1865 N N   . CYS   A 92  ? 0.1614 0.1663 0.1206 -0.0200 -0.0089 0.0176  92  CYS   A N   
1866 C CA  . CYS   A 92  ? 0.1518 0.1590 0.1374 -0.0152 -0.0021 0.0131  92  CYS   A CA  
1867 C C   . CYS   A 92  ? 0.1432 0.1538 0.1295 -0.0105 0.0003  0.0157  92  CYS   A C   
1868 O O   . CYS   A 92  ? 0.1450 0.1601 0.1400 -0.0180 -0.0039 0.0105  92  CYS   A O   
1869 C CB  . CYS   A 92  ? 0.1473 0.1547 0.1549 -0.0060 -0.0051 0.0100  92  CYS   A CB  
1870 S SG  . CYS   A 92  ? 0.1484 0.1467 0.1418 -0.0109 -0.0010 0.0112  92  CYS   A SG  
1876 N N   . LEU   A 93  ? 0.1415 0.1378 0.1442 -0.0140 0.0058  0.0180  93  LEU   A N   
1877 C CA  . LEU   A 93  ? 0.1292 0.1374 0.1415 -0.0092 0.0049  0.0160  93  LEU   A CA  
1878 C C   . LEU   A 93  ? 0.1253 0.1286 0.1386 -0.0021 0.0072  0.0114  93  LEU   A C   
1879 O O   . LEU   A 93  ? 0.1282 0.1345 0.1294 -0.0039 0.0018  0.0151  93  LEU   A O   
1880 C CB  . LEU   A 93  ? 0.1380 0.1338 0.1519 -0.0081 -0.0066 0.0275  93  LEU   A CB  
1881 C CG  . LEU   A 93  ? 0.1437 0.1377 0.1494 -0.0041 0.0048  0.0235  93  LEU   A CG  
1882 C CD1 . LEU   A 93  ? 0.1543 0.1373 0.1778 0.0007  0.0113  0.0188  93  LEU   A CD1 
1883 C CD2 . LEU   A 93  ? 0.1587 0.1305 0.1710 -0.0087 -0.0036 0.0143  93  LEU   A CD2 
1895 N N   . HIS   A 94  ? 0.1221 0.1249 0.1245 0.0013  0.0098  0.0178  94  HIS   A N   
1896 C CA  . HIS   A 94  ? 0.1212 0.1239 0.1391 -0.0063 0.0050  0.0148  94  HIS   A CA  
1897 C C   . HIS   A 94  ? 0.1194 0.1205 0.1480 -0.0081 0.0045  0.0117  94  HIS   A C   
1898 O O   . HIS   A 94  ? 0.1231 0.1455 0.1701 -0.0000 0.0043  -0.0091 94  HIS   A O   
1899 C CB  . HIS   A 94  ? 0.1250 0.1247 0.1426 -0.0040 -0.0024 0.0163  94  HIS   A CB  
1900 C CG  . HIS   A 94  ? 0.1306 0.1261 0.1309 -0.0051 -0.0027 0.0158  94  HIS   A CG  
1901 N ND1 . HIS   A 94  ? 0.1262 0.1243 0.1383 -0.0026 0.0019  0.0150  94  HIS   A ND1 
1902 C CD2 . HIS   A 94  ? 0.1353 0.1345 0.1371 -0.0046 -0.0044 0.0093  94  HIS   A CD2 
1903 C CE1 . HIS   A 94  ? 0.1347 0.1335 0.1350 -0.0091 -0.0020 0.0036  94  HIS   A CE1 
1904 N NE2 . HIS   A 94  ? 0.1409 0.1358 0.1353 -0.0099 -0.0057 0.0045  94  HIS   A NE2 
1912 N N   . VAL   A 95  ? 0.1211 0.1173 0.1288 -0.0031 0.0129  0.0047  95  VAL   A N   
1913 C CA  . VAL   A 95  ? 0.1260 0.1226 0.1321 -0.0027 0.0189  0.0083  95  VAL   A CA  
1914 C C   . VAL   A 95  ? 0.1282 0.1222 0.1198 -0.0098 0.0037  0.0100  95  VAL   A C   
1915 O O   . VAL   A 95  ? 0.1309 0.1366 0.1230 0.0085  0.0059  0.0076  95  VAL   A O   
1916 C CB  . VAL   A 95  ? 0.1330 0.1228 0.1491 -0.0117 0.0092  0.0122  95  VAL   A CB  
1917 C CG1 . VAL   A 95  ? 0.1498 0.1279 0.1600 -0.0175 0.0073  0.0015  95  VAL   A CG1 
1918 C CG2 . VAL   A 95  ? 0.1319 0.1276 0.1507 -0.0135 0.0042  0.0213  95  VAL   A CG2 
1928 N N   . VAL   A 96  ? 0.1339 0.1232 0.1144 -0.0029 0.0042  0.0152  96  VAL   A N   
1929 C CA  . VAL   A 96  ? 0.1380 0.1243 0.1299 -0.0016 0.0091  0.0155  96  VAL   A CA  
1930 C C   . VAL   A 96  ? 0.1428 0.1324 0.1350 -0.0065 0.0069  0.0167  96  VAL   A C   
1931 O O   . VAL   A 96  ? 0.1534 0.1379 0.1492 -0.0054 0.0153  -0.0023 96  VAL   A O   
1932 C CB  . VAL   A 96  ? 0.1443 0.1307 0.1377 -0.0039 0.0196  0.0091  96  VAL   A CB  
1933 C CG1 . VAL   A 96  ? 0.1545 0.1399 0.1246 -0.0040 0.0125  0.0098  96  VAL   A CG1 
1934 C CG2 . VAL   A 96  ? 0.1424 0.1397 0.1589 -0.0122 0.0170  0.0147  96  VAL   A CG2 
1944 N N   A GLY   A 97  ? 0.1403 0.1391 0.1422 -0.0118 -0.0001 0.0129  97  GLY   A N   
1945 N N   B GLY   A 97  ? 0.1470 0.1377 0.1369 -0.0049 0.0037  0.0185  97  GLY   A N   
1946 C CA  A GLY   A 97  ? 0.1466 0.1534 0.1429 -0.0099 -0.0048 0.0130  97  GLY   A CA  
1947 C CA  B GLY   A 97  ? 0.1544 0.1443 0.1372 -0.0020 0.0016  0.0261  97  GLY   A CA  
1948 C C   A GLY   A 97  ? 0.1481 0.1607 0.1275 -0.0112 0.0007  0.0044  97  GLY   A C   
1949 C C   B GLY   A 97  ? 0.1606 0.1476 0.1375 -0.0003 0.0050  0.0297  97  GLY   A C   
1950 O O   A GLY   A 97  ? 0.1565 0.1607 0.1422 -0.0051 0.0007  0.0048  97  GLY   A O   
1951 O O   B GLY   A 97  ? 0.1610 0.1475 0.1435 0.0000  0.0109  0.0268  97  GLY   A O   
1958 N N   A PRO   A 98  ? 0.1534 0.1643 0.1128 -0.0077 -0.0062 0.0087  98  PRO   A N   
1959 N N   B PRO   A 98  ? 0.1752 0.1516 0.1428 0.0008  -0.0007 0.0345  98  PRO   A N   
1960 C CA  A PRO   A 98  ? 0.1663 0.1759 0.1118 -0.0060 -0.0077 -0.0015 98  PRO   A CA  
1961 C CA  B PRO   A 98  ? 0.1908 0.1598 0.1523 0.0021  -0.0066 0.0229  98  PRO   A CA  
1962 C C   A PRO   A 98  ? 0.1660 0.1811 0.0947 -0.0156 0.0009  0.0063  98  PRO   A C   
1963 C C   B PRO   A 98  ? 0.2110 0.1615 0.1580 -0.0004 -0.0093 0.0296  98  PRO   A C   
1964 O O   A PRO   A 98  ? 0.1613 0.1721 0.1138 -0.0127 0.0010  0.0065  98  PRO   A O   
1965 O O   B PRO   A 98  ? 0.2081 0.1574 0.1706 0.0021  -0.0097 0.0271  98  PRO   A O   
1966 C CB  A PRO   A 98  ? 0.1794 0.1840 0.1111 0.0010  -0.0057 -0.0097 98  PRO   A CB  
1967 C CB  B PRO   A 98  ? 0.1892 0.1563 0.1387 0.0074  -0.0067 0.0250  98  PRO   A CB  
1968 C CG  A PRO   A 98  ? 0.1767 0.1791 0.1369 0.0055  -0.0089 -0.0158 98  PRO   A CG  
1969 C CG  B PRO   A 98  ? 0.1895 0.1538 0.1446 0.0036  -0.0026 0.0289  98  PRO   A CG  
1970 C CD  A PRO   A 98  ? 0.1628 0.1680 0.1280 0.0004  -0.0067 -0.0047 98  PRO   A CD  
1971 C CD  B PRO   A 98  ? 0.1811 0.1482 0.1379 0.0037  -0.0004 0.0357  98  PRO   A CD  
1986 N N   A ASN   A 99  ? 0.1716 0.2029 0.0991 -0.0151 0.0091  0.0217  99  ASN   A N   
1987 N N   B ASN   A 99  ? 0.2352 0.1663 0.1535 0.0006  -0.0092 0.0359  99  ASN   A N   
1988 C CA  A ASN   A 99  ? 0.1886 0.2187 0.0980 -0.0150 0.0049  0.0348  99  ASN   A CA  
1989 C CA  B ASN   A 99  ? 0.2593 0.1722 0.1653 0.0089  -0.0132 0.0444  99  ASN   A CA  
1990 C C   A ASN   A 99  ? 0.2004 0.2542 0.0925 -0.0211 0.0085  0.0428  99  ASN   A C   
1991 C C   B ASN   A 99  ? 0.2718 0.1795 0.1758 0.0139  -0.0195 0.0455  99  ASN   A C   
1992 O O   A ASN   A 99  ? 0.2119 0.2824 0.1120 -0.0079 0.0078  0.0336  99  ASN   A O   
1993 O O   B ASN   A 99  ? 0.2717 0.1709 0.1681 0.0180  -0.0214 0.0501  99  ASN   A O   
1994 C CB  A ASN   A 99  ? 0.1914 0.2072 0.1207 -0.0160 -0.0099 0.0401  99  ASN   A CB  
1995 C CB  B ASN   A 99  ? 0.2713 0.1721 0.1769 0.0110  -0.0106 0.0462  99  ASN   A CB  
1996 C CG  A ASN   A 99  ? 0.1944 0.2014 0.1302 -0.0134 -0.0201 0.0391  99  ASN   A CG  
1997 C CG  B ASN   A 99  ? 0.2807 0.1779 0.1943 0.0116  -0.0073 0.0442  99  ASN   A CG  
1998 O OD1 A ASN   A 99  ? 0.2063 0.2085 0.1441 -0.0026 -0.0235 0.0275  99  ASN   A OD1 
1999 O OD1 B ASN   A 99  ? 0.2853 0.1854 0.1965 0.0173  -0.0081 0.0451  99  ASN   A OD1 
2000 N ND2 A ASN   A 99  ? 0.1949 0.2014 0.1566 -0.0134 -0.0265 0.0487  99  ASN   A ND2 
2001 N ND2 B ASN   A 99  ? 0.2836 0.1832 0.2180 0.0125  -0.0147 0.0381  99  ASN   A ND2 
2014 N N   A VAL   A 100 ? 0.2154 0.2605 0.0834 -0.0406 -0.0166 0.0293  100 VAL   A N   
2015 N N   B VAL   A 100 ? 0.2872 0.2038 0.2100 0.0143  -0.0194 0.0473  100 VAL   A N   
2016 C CA  A VAL   A 100 ? 0.2439 0.2842 0.1233 -0.0436 -0.0323 0.0335  100 VAL   A CA  
2017 C CA  B VAL   A 100 ? 0.3030 0.2235 0.2480 0.0115  -0.0180 0.0387  100 VAL   A CA  
2018 C C   A VAL   A 100 ? 0.2598 0.3009 0.1103 -0.0488 -0.0437 0.0580  100 VAL   A C   
2019 C C   B VAL   A 100 ? 0.3138 0.2326 0.2667 0.0119  -0.0207 0.0325  100 VAL   A C   
2020 O O   A VAL   A 100 ? 0.2737 0.3145 0.1423 -0.0473 -0.0276 0.0581  100 VAL   A O   
2021 O O   B VAL   A 100 ? 0.3156 0.2333 0.2734 0.0074  -0.0273 0.0294  100 VAL   A O   
2022 C CB  A VAL   A 100 ? 0.2609 0.2862 0.1694 -0.0524 -0.0330 0.0233  100 VAL   A CB  
2023 C CB  B VAL   A 100 ? 0.3076 0.2368 0.2669 0.0069  -0.0078 0.0345  100 VAL   A CB  
2024 C CG1 A VAL   A 100 ? 0.2630 0.2938 0.1898 -0.0540 -0.0271 0.0212  100 VAL   A CG1 
2025 C CG1 B VAL   A 100 ? 0.3105 0.2388 0.2783 0.0041  -0.0041 0.0373  100 VAL   A CG1 
2026 C CG2 A VAL   A 100 ? 0.2729 0.2896 0.1802 -0.0528 -0.0324 0.0199  100 VAL   A CG2 
2027 C CG2 B VAL   A 100 ? 0.3074 0.2437 0.2706 0.0083  -0.0074 0.0348  100 VAL   A CG2 
2046 N N   A ASN   A 101 ? 0.2708 0.3093 0.1329 -0.0541 -0.0491 0.0826  101 ASN   A N   
2047 N N   B ASN   A 101 ? 0.3253 0.2469 0.2780 0.0145  -0.0184 0.0269  101 ASN   A N   
2048 C CA  A ASN   A 101 ? 0.2969 0.3187 0.1590 -0.0607 -0.0474 0.0983  101 ASN   A CA  
2049 C CA  B ASN   A 101 ? 0.3360 0.2652 0.2904 0.0203  -0.0105 0.0258  101 ASN   A CA  
2050 C C   A ASN   A 101 ? 0.3207 0.3469 0.1836 -0.0702 -0.0151 0.1159  101 ASN   A C   
2051 C C   B ASN   A 101 ? 0.3431 0.2778 0.2979 0.0164  -0.0078 0.0224  101 ASN   A C   
2052 O O   A ASN   A 101 ? 0.3341 0.3498 0.2249 -0.0678 -0.0149 0.1113  101 ASN   A O   
2053 O O   B ASN   A 101 ? 0.3455 0.2776 0.2963 0.0152  -0.0098 0.0262  101 ASN   A O   
2054 C CB  A ASN   A 101 ? 0.2996 0.3000 0.1632 -0.0520 -0.0681 0.0853  101 ASN   A CB  
2055 C CB  B ASN   A 101 ? 0.3413 0.2721 0.2989 0.0242  -0.0037 0.0250  101 ASN   A CB  
2056 C CG  A ASN   A 101 ? 0.3034 0.2838 0.1714 -0.0495 -0.0765 0.0497  101 ASN   A CG  
2057 C CG  B ASN   A 101 ? 0.3474 0.2803 0.3077 0.0257  0.0032  0.0224  101 ASN   A CG  
2058 O OD1 A ASN   A 101 ? 0.2977 0.2893 0.1914 -0.0345 -0.0833 0.0132  101 ASN   A OD1 
2059 O OD1 B ASN   A 101 ? 0.3533 0.2862 0.3095 0.0246  0.0025  0.0251  101 ASN   A OD1 
2060 N ND2 A ASN   A 101 ? 0.3095 0.2709 0.1800 -0.0572 -0.0729 0.0551  101 ASN   A ND2 
2061 N ND2 B ASN   A 101 ? 0.3473 0.2804 0.3078 0.0299  0.0067  0.0207  101 ASN   A ND2 
2074 N N   A LYS   A 102 ? 0.3273 0.3771 0.2196 -0.0787 0.0000  0.1089  102 LYS   A N   
2075 N N   B LYS   A 102 ? 0.3470 0.2893 0.3019 0.0156  -0.0041 0.0177  102 LYS   A N   
2076 C CA  A LYS   A 102 ? 0.3411 0.4066 0.2412 -0.0737 -0.0002 0.0936  102 LYS   A CA  
2077 C CA  B LYS   A 102 ? 0.3505 0.3018 0.2991 0.0099  -0.0015 0.0132  102 LYS   A CA  
2078 C C   A LYS   A 102 ? 0.3449 0.4273 0.2261 -0.0594 0.0001  0.0857  102 LYS   A C   
2079 C C   B LYS   A 102 ? 0.3488 0.3037 0.2792 0.0096  -0.0010 0.0194  102 LYS   A C   
2080 O O   A LYS   A 102 ? 0.3481 0.4367 0.2348 -0.0534 0.0038  0.0796  102 LYS   A O   
2081 O O   B LYS   A 102 ? 0.3520 0.3054 0.2853 0.0113  0.0025  0.0215  102 LYS   A O   
2082 C CB  A LYS   A 102 ? 0.3521 0.4128 0.2794 -0.0791 -0.0051 0.0789  102 LYS   A CB  
2083 C CB  B LYS   A 102 ? 0.3544 0.3098 0.3143 0.0062  -0.0022 0.0033  102 LYS   A CB  
2084 C CG  A LYS   A 102 ? 0.3617 0.4165 0.3161 -0.0808 -0.0147 0.0531  102 LYS   A CG  
2085 C CG  B LYS   A 102 ? 0.3577 0.3180 0.3325 0.0021  -0.0034 -0.0060 102 LYS   A CG  
2086 C CD  A LYS   A 102 ? 0.3730 0.4202 0.3512 -0.0817 -0.0289 0.0254  102 LYS   A CD  
2087 C CD  B LYS   A 102 ? 0.3604 0.3258 0.3527 -0.0020 -0.0030 -0.0137 102 LYS   A CD  
2088 C CE  A LYS   A 102 ? 0.3822 0.4235 0.3759 -0.0823 -0.0370 0.0111  102 LYS   A CE  
2089 C CE  B LYS   A 102 ? 0.3621 0.3311 0.3680 -0.0053 -0.0051 -0.0179 102 LYS   A CE  
2090 N NZ  A LYS   A 102 ? 0.3874 0.4243 0.3914 -0.0874 -0.0356 0.0022  102 LYS   A NZ  
2091 N NZ  B LYS   A 102 ? 0.3630 0.3340 0.3806 -0.0068 -0.0068 -0.0222 102 LYS   A NZ  
2118 N N   A GLY   A 103 ? 0.3445 0.4400 0.2236 -0.0465 -0.0054 0.0674  103 GLY   A N   
2119 N N   B GLY   A 103 ? 0.3431 0.3051 0.2562 0.0118  -0.0075 0.0194  103 GLY   A N   
2120 C CA  A GLY   A 103 ? 0.3448 0.4491 0.2224 -0.0353 -0.0033 0.0521  103 GLY   A CA  
2121 C CA  B GLY   A 103 ? 0.3389 0.3038 0.2417 0.0153  -0.0146 0.0277  103 GLY   A CA  
2122 C C   A GLY   A 103 ? 0.3409 0.4572 0.2271 -0.0292 0.0043  0.0355  103 GLY   A C   
2123 C C   B GLY   A 103 ? 0.3360 0.3034 0.2308 0.0160  -0.0240 0.0340  103 GLY   A C   
2124 O O   A GLY   A 103 ? 0.3474 0.4625 0.2523 -0.0238 0.0027  0.0237  103 GLY   A O   
2125 O O   B GLY   A 103 ? 0.3391 0.3034 0.2249 0.0182  -0.0259 0.0374  103 GLY   A O   
2132 N N   A GLU   A 104 ? 0.3266 0.4568 0.2006 -0.0338 0.0176  0.0298  104 GLU   A N   
2133 N N   B GLU   A 104 ? 0.3282 0.3005 0.2196 0.0128  -0.0322 0.0410  104 GLU   A N   
2134 C CA  A GLU   A 104 ? 0.3081 0.4522 0.1855 -0.0459 0.0231  0.0216  104 GLU   A CA  
2135 C CA  B GLU   A 104 ? 0.3202 0.2962 0.2073 0.0061  -0.0385 0.0417  104 GLU   A CA  
2136 C C   A GLU   A 104 ? 0.3115 0.4640 0.1968 -0.0482 0.0289  -0.0038 104 GLU   A C   
2137 C C   B GLU   A 104 ? 0.3160 0.2943 0.2093 0.0054  -0.0340 0.0338  104 GLU   A C   
2138 O O   A GLU   A 104 ? 0.3075 0.4648 0.2169 -0.0474 0.0233  -0.0073 104 GLU   A O   
2139 O O   B GLU   A 104 ? 0.3156 0.2846 0.2083 0.0087  -0.0349 0.0415  104 GLU   A O   
2140 C CB  A GLU   A 104 ? 0.2835 0.4342 0.1755 -0.0562 0.0269  0.0467  104 GLU   A CB  
2141 C CB  B GLU   A 104 ? 0.3184 0.2954 0.2068 -0.0001 -0.0416 0.0444  104 GLU   A CB  
2142 C CG  A GLU   A 104 ? 0.2660 0.4169 0.1884 -0.0623 0.0183  0.0680  104 GLU   A CG  
2143 C CG  B GLU   A 104 ? 0.3188 0.2971 0.2190 -0.0036 -0.0463 0.0455  104 GLU   A CG  
2144 C CD  A GLU   A 104 ? 0.2449 0.3995 0.1831 -0.0696 0.0131  0.0888  104 GLU   A CD  
2145 C CD  B GLU   A 104 ? 0.3176 0.2996 0.2301 -0.0048 -0.0517 0.0429  104 GLU   A CD  
2146 O OE1 A GLU   A 104 ? 0.2270 0.3812 0.1462 -0.0659 0.0033  0.0931  104 GLU   A OE1 
2147 O OE1 B GLU   A 104 ? 0.3199 0.3037 0.2326 -0.0053 -0.0528 0.0415  104 GLU   A OE1 
2148 O OE2 A GLU   A 104 ? 0.2469 0.3911 0.2054 -0.0723 0.0180  0.1052  104 GLU   A OE2 
2149 O OE2 B GLU   A 104 ? 0.3162 0.2994 0.2393 -0.0047 -0.0570 0.0391  104 GLU   A OE2 
2162 N N   A ASP   A 105 ? 0.3189 0.4734 0.2067 -0.0478 0.0392  -0.0305 105 ASP   A N   
2163 N N   B ASP   A 105 ? 0.3171 0.3026 0.2295 -0.0012 -0.0284 0.0175  105 ASP   A N   
2164 C CA  A ASP   A 105 ? 0.3222 0.4803 0.2351 -0.0483 0.0464  -0.0593 105 ASP   A CA  
2165 C CA  B ASP   A 105 ? 0.3176 0.3093 0.2556 -0.0046 -0.0193 -0.0055 105 ASP   A CA  
2166 C C   A ASP   A 105 ? 0.2940 0.4672 0.2093 -0.0604 0.0321  -0.0787 105 ASP   A C   
2167 C C   B ASP   A 105 ? 0.3088 0.3070 0.2369 -0.0123 -0.0123 -0.0190 105 ASP   A C   
2168 O O   A ASP   A 105 ? 0.2802 0.4656 0.1623 -0.0656 0.0235  -0.1047 105 ASP   A O   
2169 O O   B ASP   A 105 ? 0.3030 0.3019 0.2023 -0.0131 -0.0122 -0.0230 105 ASP   A O   
2170 C CB  A ASP   A 105 ? 0.3499 0.4964 0.2950 -0.0377 0.0579  -0.0691 105 ASP   A CB  
2171 C CB  B ASP   A 105 ? 0.3276 0.3173 0.3014 -0.0012 -0.0186 -0.0116 105 ASP   A CB  
2172 C CG  A ASP   A 105 ? 0.3733 0.5079 0.3477 -0.0294 0.0644  -0.0773 105 ASP   A CG  
2173 C CG  B ASP   A 105 ? 0.3364 0.3231 0.3417 0.0038  -0.0181 -0.0172 105 ASP   A CG  
2174 O OD1 A ASP   A 105 ? 0.3799 0.5122 0.3500 -0.0301 0.0676  -0.0899 105 ASP   A OD1 
2175 O OD1 B ASP   A 105 ? 0.3433 0.3231 0.3628 0.0054  -0.0175 -0.0201 105 ASP   A OD1 
2176 O OD2 A ASP   A 105 ? 0.3862 0.5128 0.3806 -0.0246 0.0685  -0.0712 105 ASP   A OD2 
2177 O OD2 B ASP   A 105 ? 0.3377 0.3272 0.3592 0.0038  -0.0217 -0.0182 105 ASP   A OD2 
2186 N N   A ILE   A 106 ? 0.2783 0.4501 0.2406 -0.0693 0.0058  -0.0799 106 ILE   A N   
2187 N N   B ILE   A 106 ? 0.3050 0.3113 0.2590 -0.0182 -0.0105 -0.0266 106 ILE   A N   
2188 C CA  A ILE   A 106 ? 0.2533 0.4308 0.2646 -0.0819 -0.0190 -0.0878 106 ILE   A CA  
2189 C CA  B ILE   A 106 ? 0.3000 0.3181 0.2816 -0.0277 -0.0095 -0.0340 106 ILE   A CA  
2190 C C   A ILE   A 106 ? 0.2340 0.4020 0.2754 -0.1033 -0.0192 -0.1018 106 ILE   A C   
2191 C C   B ILE   A 106 ? 0.2948 0.3186 0.2903 -0.0368 0.0005  -0.0357 106 ILE   A C   
2192 O O   A ILE   A 106 ? 0.2129 0.3964 0.2728 -0.1122 -0.0020 -0.1074 106 ILE   A O   
2193 O O   B ILE   A 106 ? 0.2927 0.3224 0.2890 -0.0370 0.0026  -0.0372 106 ILE   A O   
2194 C CB  A ILE   A 106 ? 0.2577 0.4414 0.3040 -0.0672 -0.0321 -0.0651 106 ILE   A CB  
2195 C CB  B ILE   A 106 ? 0.3025 0.3262 0.3028 -0.0272 -0.0177 -0.0329 106 ILE   A CB  
2196 C CG1 A ILE   A 106 ? 0.2514 0.4447 0.3273 -0.0573 -0.0379 -0.0487 106 ILE   A CG1 
2197 C CG1 B ILE   A 106 ? 0.3014 0.3318 0.3136 -0.0258 -0.0217 -0.0284 106 ILE   A CG1 
2198 C CG2 A ILE   A 106 ? 0.2642 0.4440 0.3124 -0.0639 -0.0362 -0.0637 106 ILE   A CG2 
2199 C CG2 B ILE   A 106 ? 0.3046 0.3276 0.3062 -0.0273 -0.0204 -0.0363 106 ILE   A CG2 
2200 C CD1 A ILE   A 106 ? 0.2513 0.4446 0.3420 -0.0469 -0.0323 -0.0404 106 ILE   A CD1 
2201 C CD1 B ILE   A 106 ? 0.3008 0.3337 0.3198 -0.0234 -0.0206 -0.0274 106 ILE   A CD1 
2224 N N   A GLN   A 107 ? 0.2485 0.3790 0.3040 -0.1001 -0.0120 -0.1104 107 GLN   A N   
2225 N N   B GLN   A 107 ? 0.2925 0.3116 0.3079 -0.0433 0.0102  -0.0401 107 GLN   A N   
2226 C CA  A GLN   A 107 ? 0.2704 0.3553 0.3708 -0.0806 0.0139  -0.1001 107 GLN   A CA  
2227 C CA  B GLN   A 107 ? 0.2906 0.3067 0.3405 -0.0485 0.0217  -0.0471 107 GLN   A CA  
2228 C C   A GLN   A 107 ? 0.2467 0.3030 0.3459 -0.0689 0.0376  -0.0766 107 GLN   A C   
2229 C C   B GLN   A 107 ? 0.2591 0.2804 0.3143 -0.0560 0.0334  -0.0542 107 GLN   A C   
2230 O O   A GLN   A 107 ? 0.2499 0.2974 0.3899 -0.0567 0.0509  -0.0720 107 GLN   A O   
2231 O O   B GLN   A 107 ? 0.2625 0.2786 0.3301 -0.0556 0.0330  -0.0503 107 GLN   A O   
2232 C CB  A GLN   A 107 ? 0.3098 0.3812 0.4600 -0.0782 0.0045  -0.1004 107 GLN   A CB  
2233 C CB  B GLN   A 107 ? 0.3162 0.3270 0.3994 -0.0479 0.0159  -0.0448 107 GLN   A CB  
2234 C CG  A GLN   A 107 ? 0.3449 0.4084 0.5554 -0.0735 -0.0026 -0.0924 107 GLN   A CG  
2235 C CG  B GLN   A 107 ? 0.3388 0.3464 0.4590 -0.0464 0.0116  -0.0412 107 GLN   A CG  
2236 C CD  A GLN   A 107 ? 0.3691 0.4292 0.6354 -0.0720 -0.0049 -0.0822 107 GLN   A CD  
2237 C CD  B GLN   A 107 ? 0.3574 0.3640 0.5100 -0.0443 0.0103  -0.0372 107 GLN   A CD  
2238 O OE1 A GLN   A 107 ? 0.3795 0.4351 0.6675 -0.0709 -0.0051 -0.0800 107 GLN   A OE1 
2239 O OE1 B GLN   A 107 ? 0.3617 0.3704 0.5307 -0.0432 0.0111  -0.0366 107 GLN   A OE1 
2240 N NE2 A GLN   A 107 ? 0.3812 0.4391 0.6619 -0.0744 -0.0074 -0.0807 107 GLN   A NE2 
2241 N NE2 B GLN   A 107 ? 0.3664 0.3705 0.5273 -0.0454 0.0090  -0.0373 107 GLN   A NE2 
2258 N N   . LEU   A 108 ? 0.2231 0.2549 0.2811 -0.0627 0.0391  -0.0672 108 LEU   A N   
2259 C CA  . LEU   A 108 ? 0.1949 0.2003 0.2300 -0.0272 0.0330  -0.0266 108 LEU   A CA  
2260 C C   . LEU   A 108 ? 0.1708 0.1580 0.2251 -0.0089 0.0225  0.0087  108 LEU   A C   
2261 O O   . LEU   A 108 ? 0.1591 0.1561 0.2441 -0.0031 0.0263  0.0175  108 LEU   A O   
2262 C CB  . LEU   A 108 ? 0.1964 0.2053 0.2061 -0.0267 0.0343  -0.0210 108 LEU   A CB  
2263 C CG  . LEU   A 108 ? 0.2109 0.2306 0.2187 -0.0219 0.0401  -0.0203 108 LEU   A CG  
2264 C CD1 . LEU   A 108 ? 0.2277 0.2392 0.2172 -0.0303 0.0530  -0.0142 108 LEU   A CD1 
2265 C CD2 . LEU   A 108 ? 0.2119 0.2519 0.2624 -0.0131 0.0400  -0.0072 108 LEU   A CD2 
2278 N N   . LEU   A 109 ? 0.1589 0.1537 0.2218 -0.0018 0.0201  0.0262  109 LEU   A N   
2279 C CA  . LEU   A 109 ? 0.1561 0.1489 0.2051 -0.0040 0.0067  0.0241  109 LEU   A CA  
2280 C C   . LEU   A 109 ? 0.1409 0.1395 0.1892 -0.0124 0.0051  0.0160  109 LEU   A C   
2281 O O   . LEU   A 109 ? 0.1523 0.1373 0.2021 -0.0068 -0.0067 0.0076  109 LEU   A O   
2282 C CB  . LEU   A 109 ? 0.1579 0.1591 0.2138 0.0044  -0.0039 0.0381  109 LEU   A CB  
2283 C CG  . LEU   A 109 ? 0.1518 0.1672 0.2238 -0.0013 -0.0005 0.0399  109 LEU   A CG  
2284 C CD1 . LEU   A 109 ? 0.1579 0.1561 0.2396 -0.0015 0.0078  0.0178  109 LEU   A CD1 
2285 C CD2 . LEU   A 109 ? 0.1530 0.1842 0.2461 -0.0014 -0.0047 0.0439  109 LEU   A CD2 
2297 N N   . LYS   A 110 ? 0.1429 0.1369 0.1913 -0.0098 -0.0027 0.0100  110 LYS   A N   
2298 C CA  . LYS   A 110 ? 0.1420 0.1315 0.1920 -0.0085 -0.0045 0.0167  110 LYS   A CA  
2299 C C   . LYS   A 110 ? 0.1431 0.1282 0.1783 -0.0059 -0.0046 0.0085  110 LYS   A C   
2300 O O   . LYS   A 110 ? 0.1417 0.1325 0.1861 -0.0077 0.0032  0.0018  110 LYS   A O   
2301 C CB  . LYS   A 110 ? 0.1523 0.1357 0.2042 -0.0073 -0.0137 0.0005  110 LYS   A CB  
2302 C CG  . LYS   A 110 ? 0.1549 0.1371 0.2227 -0.0072 -0.0122 -0.0027 110 LYS   A CG  
2303 C CD  . LYS   A 110 ? 0.1581 0.1429 0.2266 -0.0142 -0.0100 -0.0034 110 LYS   A CD  
2304 C CE  . LYS   A 110 ? 0.1668 0.1469 0.2515 -0.0115 0.0107  0.0006  110 LYS   A CE  
2305 N NZ  . LYS   A 110 ? 0.1686 0.1466 0.2575 -0.0199 0.0133  0.0024  110 LYS   A NZ  
2319 N N   . SER   A 111 ? 0.1450 0.1328 0.1741 -0.0019 -0.0053 0.0105  111 SER   A N   
2320 C CA  . SER   A 111 ? 0.1363 0.1360 0.1817 -0.0010 0.0025  -0.0004 111 SER   A CA  
2321 C C   . SER   A 111 ? 0.1318 0.1300 0.1795 -0.0089 0.0070  0.0088  111 SER   A C   
2322 O O   . SER   A 111 ? 0.1480 0.1272 0.1901 -0.0073 0.0096  0.0064  111 SER   A O   
2323 C CB  . SER   A 111 ? 0.1531 0.1557 0.1956 -0.0075 0.0156  -0.0098 111 SER   A CB  
2324 O OG  . SER   A 111 ? 0.2028 0.1776 0.1959 0.0031  0.0170  -0.0108 111 SER   A OG  
2330 N N   . ALA   A 112 ? 0.1362 0.1244 0.1900 -0.0044 0.0139  0.0091  112 ALA   A N   
2331 C CA  . ALA   A 112 ? 0.1396 0.1238 0.1760 -0.0063 0.0145  0.0036  112 ALA   A CA  
2332 C C   . ALA   A 112 ? 0.1344 0.1218 0.1806 -0.0058 0.0096  0.0030  112 ALA   A C   
2333 O O   . ALA   A 112 ? 0.1365 0.1208 0.1936 -0.0122 0.0154  0.0120  112 ALA   A O   
2334 C CB  . ALA   A 112 ? 0.1528 0.1281 0.1847 -0.0048 0.0030  0.0065  112 ALA   A CB  
2340 N N   . TYR   A 113 ? 0.1260 0.1272 0.1869 -0.0047 0.0085  0.0125  113 TYR   A N   
2341 C CA  . TYR   A 113 ? 0.1263 0.1244 0.1876 -0.0056 0.0114  0.0150  113 TYR   A CA  
2342 C C   . TYR   A 113 ? 0.1233 0.1234 0.1709 -0.0133 0.0103  0.0097  113 TYR   A C   
2343 O O   . TYR   A 113 ? 0.1318 0.1283 0.1811 -0.0087 0.0163  0.0051  113 TYR   A O   
2344 C CB  . TYR   A 113 ? 0.1251 0.1359 0.2020 -0.0055 -0.0029 0.0253  113 TYR   A CB  
2345 C CG  . TYR   A 113 ? 0.1269 0.1411 0.1919 -0.0129 0.0082  0.0304  113 TYR   A CG  
2346 C CD1 . TYR   A 113 ? 0.1336 0.1459 0.1825 -0.0022 0.0066  0.0336  113 TYR   A CD1 
2347 C CD2 . TYR   A 113 ? 0.1339 0.1496 0.1882 -0.0129 0.0033  0.0305  113 TYR   A CD2 
2348 C CE1 . TYR   A 113 ? 0.1384 0.1597 0.1788 -0.0030 0.0115  0.0374  113 TYR   A CE1 
2349 C CE2 . TYR   A 113 ? 0.1300 0.1608 0.1768 -0.0091 -0.0027 0.0304  113 TYR   A CE2 
2350 C CZ  . TYR   A 113 ? 0.1346 0.1602 0.1749 0.0009  0.0093  0.0417  113 TYR   A CZ  
2351 O OH  . TYR   A 113 ? 0.1341 0.1761 0.2059 0.0098  0.0115  0.0420  113 TYR   A OH  
2361 N N   . GLU   A 114 ? 0.1264 0.1208 0.1825 -0.0070 0.0096  0.0083  114 GLU   A N   
2362 C CA  . GLU   A 114 ? 0.1303 0.1177 0.1874 0.0017  0.0050  0.0155  114 GLU   A CA  
2363 C C   . GLU   A 114 ? 0.1244 0.1250 0.1840 0.0006  0.0160  0.0119  114 GLU   A C   
2364 O O   . GLU   A 114 ? 0.1371 0.1263 0.1818 -0.0023 0.0073  0.0108  114 GLU   A O   
2365 C CB  . GLU   A 114 ? 0.1328 0.1247 0.1894 -0.0053 0.0079  0.0110  114 GLU   A CB  
2366 C CG  . GLU   A 114 ? 0.1447 0.1279 0.1944 0.0013  0.0043  0.0002  114 GLU   A CG  
2367 C CD  . GLU   A 114 ? 0.1518 0.1276 0.1977 -0.0029 0.0010  0.0024  114 GLU   A CD  
2368 O OE1 . GLU   A 114 ? 0.1500 0.1264 0.1990 -0.0092 0.0092  -0.0010 114 GLU   A OE1 
2369 O OE2 . GLU   A 114 ? 0.1653 0.1301 0.2188 -0.0101 0.0030  -0.0112 114 GLU   A OE2 
2376 N N   . ASN   A 115 ? 0.1262 0.1215 0.1756 -0.0036 0.0045  0.0091  115 ASN   A N   
2377 C CA  . ASN   A 115 ? 0.1252 0.1298 0.1847 -0.0089 0.0113  0.0104  115 ASN   A CA  
2378 C C   . ASN   A 115 ? 0.1324 0.1209 0.1762 -0.0115 0.0061  0.0062  115 ASN   A C   
2379 O O   . ASN   A 115 ? 0.1348 0.1393 0.1751 -0.0121 0.0112  0.0148  115 ASN   A O   
2380 C CB  . ASN   A 115 ? 0.1350 0.1331 0.1717 -0.0125 0.0148  0.0037  115 ASN   A CB  
2381 C CG  . ASN   A 115 ? 0.1356 0.1570 0.1828 -0.0145 0.0160  0.0039  115 ASN   A CG  
2382 O OD1 . ASN   A 115 ? 0.1436 0.2495 0.2075 -0.0165 0.0252  0.0242  115 ASN   A OD1 
2383 N ND2 . ASN   A 115 ? 0.1399 0.1403 0.1844 -0.0135 0.0289  0.0101  115 ASN   A ND2 
2390 N N   . PHE   A 116 ? 0.1266 0.1264 0.1852 -0.0042 0.0135  0.0152  116 PHE   A N   
2391 C CA  . PHE   A 116 ? 0.1311 0.1346 0.1716 -0.0053 0.0157  0.0189  116 PHE   A CA  
2392 C C   . PHE   A 116 ? 0.1310 0.1428 0.1750 -0.0106 0.0244  0.0225  116 PHE   A C   
2393 O O   . PHE   A 116 ? 0.1375 0.1503 0.1800 -0.0002 0.0179  0.0245  116 PHE   A O   
2394 C CB  . PHE   A 116 ? 0.1276 0.1273 0.1844 -0.0028 0.0208  0.0173  116 PHE   A CB  
2395 C CG  . PHE   A 116 ? 0.1322 0.1266 0.1780 -0.0071 0.0147  0.0158  116 PHE   A CG  
2396 C CD1 . PHE   A 116 ? 0.1369 0.1296 0.1760 -0.0065 0.0158  0.0141  116 PHE   A CD1 
2397 C CD2 . PHE   A 116 ? 0.1370 0.1335 0.1961 -0.0082 0.0206  0.0211  116 PHE   A CD2 
2398 C CE1 . PHE   A 116 ? 0.1389 0.1286 0.1873 -0.0149 0.0121  0.0109  116 PHE   A CE1 
2399 C CE2 . PHE   A 116 ? 0.1410 0.1343 0.1999 -0.0078 0.0203  0.0144  116 PHE   A CE2 
2400 C CZ  . PHE   A 116 ? 0.1426 0.1235 0.1949 -0.0037 0.0112  0.0171  116 PHE   A CZ  
2410 N N   . ASN   A 117 ? 0.1329 0.1341 0.1837 -0.0073 0.0137  0.0150  117 ASN   A N   
2411 C CA  . ASN   A 117 ? 0.1358 0.1332 0.1877 -0.0043 0.0166  0.0254  117 ASN   A CA  
2412 C C   . ASN   A 117 ? 0.1353 0.1419 0.1916 -0.0022 0.0154  0.0296  117 ASN   A C   
2413 O O   . ASN   A 117 ? 0.1451 0.1481 0.2175 -0.0078 -0.0051 0.0407  117 ASN   A O   
2414 C CB  . ASN   A 117 ? 0.1314 0.1374 0.1954 -0.0020 0.0106  0.0329  117 ASN   A CB  
2415 C CG  . ASN   A 117 ? 0.1308 0.1378 0.1940 -0.0037 0.0114  0.0320  117 ASN   A CG  
2416 O OD1 . ASN   A 117 ? 0.1321 0.1569 0.2052 -0.0121 0.0128  0.0179  117 ASN   A OD1 
2417 N ND2 . ASN   A 117 ? 0.1290 0.1399 0.1956 -0.0058 0.0066  0.0262  117 ASN   A ND2 
2424 N N   . GLN   A 118 ? 0.1307 0.1412 0.1986 -0.0054 0.0037  0.0301  118 GLN   A N   
2425 C CA  . GLN   A 118 ? 0.1431 0.1503 0.2016 -0.0086 0.0002  0.0183  118 GLN   A CA  
2426 C C   . GLN   A 118 ? 0.1444 0.1581 0.1891 -0.0109 -0.0011 0.0224  118 GLN   A C   
2427 O O   . GLN   A 118 ? 0.1469 0.1917 0.2108 0.0000  -0.0083 0.0042  118 GLN   A O   
2428 C CB  . GLN   A 118 ? 0.1395 0.1554 0.1996 -0.0077 0.0088  0.0228  118 GLN   A CB  
2429 C CG  . GLN   A 118 ? 0.1308 0.1570 0.2037 -0.0051 0.0063  0.0264  118 GLN   A CG  
2430 C CD  . GLN   A 118 ? 0.1271 0.1594 0.2145 -0.0003 0.0098  0.0214  118 GLN   A CD  
2431 O OE1 . GLN   A 118 ? 0.1336 0.1737 0.2295 0.0085  0.0022  0.0135  118 GLN   A OE1 
2432 N NE2 . GLN   A 118 ? 0.1431 0.1534 0.2164 0.0049  0.0022  0.0208  118 GLN   A NE2 
2441 N N   . HIS   A 119 ? 0.1476 0.1567 0.1817 -0.0103 0.0070  0.0223  119 HIS   A N   
2442 C CA  . HIS   A 119 ? 0.1571 0.1647 0.1861 -0.0079 0.0081  0.0328  119 HIS   A CA  
2443 C C   . HIS   A 119 ? 0.1620 0.1730 0.1785 -0.0080 0.0125  0.0370  119 HIS   A C   
2444 O O   . HIS   A 119 ? 0.1629 0.1832 0.1920 -0.0254 0.0035  0.0359  119 HIS   A O   
2445 C CB  . HIS   A 119 ? 0.1597 0.1637 0.2035 -0.0026 0.0234  0.0353  119 HIS   A CB  
2446 C CG  . HIS   A 119 ? 0.1651 0.1699 0.2397 0.0004  0.0228  0.0390  119 HIS   A CG  
2447 N ND1 . HIS   A 119 ? 0.1753 0.1913 0.2815 -0.0113 0.0193  0.0278  119 HIS   A ND1 
2448 C CD2 . HIS   A 119 ? 0.1708 0.1753 0.2563 0.0128  0.0393  0.0589  119 HIS   A CD2 
2449 C CE1 . HIS   A 119 ? 0.1700 0.1880 0.3029 -0.0164 0.0309  0.0512  119 HIS   A CE1 
2450 N NE2 . HIS   A 119 ? 0.1824 0.1764 0.2953 0.0027  0.0482  0.0649  119 HIS   A NE2 
2458 N N   . GLU   A 120 ? 0.1719 0.1990 0.1780 -0.0067 0.0048  0.0530  120 GLU   A N   
2459 C CA  . GLU   A 120 ? 0.1947 0.2279 0.2020 0.0015  0.0068  0.0856  120 GLU   A CA  
2460 C C   . GLU   A 120 ? 0.1771 0.2080 0.1898 -0.0133 0.0101  0.0789  120 GLU   A C   
2461 O O   . GLU   A 120 ? 0.1766 0.2037 0.1974 -0.0118 0.0097  0.0745  120 GLU   A O   
2462 C CB  . GLU   A 120 ? 0.2531 0.2883 0.2597 0.0213  0.0079  0.1372  120 GLU   A CB  
2463 C CG  . GLU   A 120 ? 0.3265 0.3483 0.3719 0.0344  0.0093  0.1329  120 GLU   A CG  
2464 C CD  . GLU   A 120 ? 0.3926 0.4048 0.4794 0.0447  0.0171  0.1225  120 GLU   A CD  
2465 O OE1 . GLU   A 120 ? 0.4128 0.4243 0.5113 0.0450  0.0201  0.1168  120 GLU   A OE1 
2466 O OE2 . GLU   A 120 ? 0.4590 0.4590 0.5298 0.0502  0.0180  0.1211  120 GLU   A OE2 
2473 N N   . VAL   A 121 ? 0.1726 0.2104 0.1734 -0.0145 0.0142  0.0668  121 VAL   A N   
2474 C CA  . VAL   A 121 ? 0.1818 0.2139 0.1626 -0.0138 0.0244  0.0622  121 VAL   A CA  
2475 C C   . VAL   A 121 ? 0.1704 0.1961 0.1488 -0.0229 0.0192  0.0466  121 VAL   A C   
2476 O O   . VAL   A 121 ? 0.1700 0.2019 0.1760 -0.0282 0.0030  0.0378  121 VAL   A O   
2477 C CB  . VAL   A 121 ? 0.2217 0.2454 0.1874 -0.0023 0.0372  0.0653  121 VAL   A CB  
2478 C CG1 . VAL   A 121 ? 0.2271 0.2619 0.1902 0.0033  0.0381  0.0634  121 VAL   A CG1 
2479 C CG2 . VAL   A 121 ? 0.2448 0.2647 0.2288 -0.0100 0.0320  0.0439  121 VAL   A CG2 
2489 N N   . LEU   A 122 ? 0.1650 0.1744 0.1633 -0.0234 0.0145  0.0437  122 LEU   A N   
2490 C CA  . LEU   A 122 ? 0.1665 0.1613 0.1652 -0.0237 0.0345  0.0387  122 LEU   A CA  
2491 C C   . LEU   A 122 ? 0.1587 0.1655 0.1674 -0.0239 0.0207  0.0367  122 LEU   A C   
2492 O O   . LEU   A 122 ? 0.1601 0.1709 0.2025 -0.0275 0.0183  0.0392  122 LEU   A O   
2493 C CB  . LEU   A 122 ? 0.1855 0.1660 0.1970 -0.0100 0.0234  0.0436  122 LEU   A CB  
2494 C CG  . LEU   A 122 ? 0.1885 0.1701 0.1844 -0.0113 0.0305  0.0269  122 LEU   A CG  
2495 C CD1 . LEU   A 122 ? 0.2077 0.1709 0.1901 -0.0242 0.0312  0.0286  122 LEU   A CD1 
2496 C CD2 . LEU   A 122 ? 0.1828 0.1617 0.1727 -0.0066 0.0332  0.0203  122 LEU   A CD2 
2508 N N   . LEU   A 123 ? 0.1570 0.1628 0.1533 -0.0212 0.0134  0.0331  123 LEU   A N   
2509 C CA  . LEU   A 123 ? 0.1570 0.1597 0.1490 -0.0202 0.0211  0.0300  123 LEU   A CA  
2510 C C   . LEU   A 123 ? 0.1490 0.1558 0.1483 -0.0129 0.0170  0.0325  123 LEU   A C   
2511 O O   . LEU   A 123 ? 0.1458 0.1687 0.1657 -0.0271 0.0137  0.0332  123 LEU   A O   
2512 C CB  . LEU   A 123 ? 0.1673 0.1727 0.1608 -0.0200 0.0336  0.0280  123 LEU   A CB  
2513 C CG  . LEU   A 123 ? 0.1751 0.1835 0.1674 -0.0211 0.0385  0.0214  123 LEU   A CG  
2514 C CD1 . LEU   A 123 ? 0.1811 0.1916 0.1823 -0.0112 0.0344  0.0195  123 LEU   A CD1 
2515 C CD2 . LEU   A 123 ? 0.1881 0.1932 0.1699 -0.0146 0.0259  0.0122  123 LEU   A CD2 
2527 N N   A ALA   A 124 ? 0.1469 0.1423 0.1482 -0.0147 0.0199  0.0271  124 ALA   A N   
2528 N N   B ALA   A 124 ? 0.1537 0.1471 0.1458 -0.0190 0.0107  0.0241  124 ALA   A N   
2529 C CA  A ALA   A 124 ? 0.1345 0.1370 0.1570 -0.0077 0.0141  0.0238  124 ALA   A CA  
2530 C CA  B ALA   A 124 ? 0.1550 0.1420 0.1513 -0.0269 0.0022  0.0265  124 ALA   A CA  
2531 C C   A ALA   A 124 ? 0.1314 0.1382 0.1684 -0.0071 0.0191  0.0246  124 ALA   A C   
2532 C C   B ALA   A 124 ? 0.1517 0.1397 0.1491 -0.0173 0.0024  0.0282  124 ALA   A C   
2533 O O   A ALA   A 124 ? 0.1294 0.1478 0.1914 -0.0078 0.0287  0.0334  124 ALA   A O   
2534 O O   B ALA   A 124 ? 0.1515 0.1323 0.1704 -0.0034 0.0116  0.0276  124 ALA   A O   
2535 C CB  A ALA   A 124 ? 0.1344 0.1256 0.1769 -0.0052 0.0085  0.0255  124 ALA   A CB  
2536 C CB  B ALA   A 124 ? 0.1622 0.1421 0.1619 -0.0329 0.0004  0.0230  124 ALA   A CB  
2547 N N   A PRO   A 125 ? 0.1281 0.1428 0.1703 -0.0080 0.0163  0.0300  125 PRO   A N   
2548 N N   B PRO   A 125 ? 0.1379 0.1396 0.1248 -0.0153 -0.0022 0.0381  125 PRO   A N   
2549 C CA  A PRO   A 125 ? 0.1344 0.1412 0.1826 -0.0118 0.0114  0.0295  125 PRO   A CA  
2550 C CA  B PRO   A 125 ? 0.1387 0.1430 0.1299 -0.0200 0.0011  0.0355  125 PRO   A CA  
2551 C C   A PRO   A 125 ? 0.1253 0.1397 0.1785 -0.0065 0.0081  0.0332  125 PRO   A C   
2552 C C   B PRO   A 125 ? 0.1477 0.1557 0.1379 -0.0100 0.0003  0.0302  125 PRO   A C   
2553 O O   A PRO   A 125 ? 0.1301 0.1425 0.1888 0.0009  0.0032  0.0267  125 PRO   A O   
2554 O O   B PRO   A 125 ? 0.1496 0.1584 0.1437 -0.0046 -0.0005 0.0300  125 PRO   A O   
2555 C CB  A PRO   A 125 ? 0.1485 0.1442 0.1829 -0.0160 0.0063  0.0192  125 PRO   A CB  
2556 C CB  B PRO   A 125 ? 0.1315 0.1393 0.1233 -0.0236 0.0000  0.0391  125 PRO   A CB  
2557 C CG  A PRO   A 125 ? 0.1501 0.1457 0.1930 -0.0159 0.0095  0.0305  125 PRO   A CG  
2558 C CG  B PRO   A 125 ? 0.1237 0.1359 0.1241 -0.0162 -0.0002 0.0400  125 PRO   A CG  
2559 C CD  A PRO   A 125 ? 0.1391 0.1464 0.1793 -0.0121 0.0165  0.0289  125 PRO   A CD  
2560 C CD  B PRO   A 125 ? 0.1278 0.1301 0.1218 -0.0152 0.0050  0.0392  125 PRO   A CD  
2575 N N   A LEU   A 126 ? 0.1195 0.1489 0.1820 -0.0038 0.0053  0.0314  126 LEU   A N   
2576 N N   B LEU   A 126 ? 0.1606 0.1670 0.1559 -0.0039 -0.0085 0.0239  126 LEU   A N   
2577 C CA  A LEU   A 126 ? 0.1260 0.1580 0.1795 -0.0068 0.0069  0.0312  126 LEU   A CA  
2578 C CA  B LEU   A 126 ? 0.1662 0.1762 0.1747 0.0003  -0.0092 0.0191  126 LEU   A CA  
2579 C C   A LEU   A 126 ? 0.1374 0.1559 0.1836 0.0057  -0.0007 0.0341  126 LEU   A C   
2580 C C   B LEU   A 126 ? 0.1657 0.1644 0.1660 0.0110  -0.0046 0.0149  126 LEU   A C   
2581 O O   A LEU   A 126 ? 0.1490 0.1553 0.2061 0.0152  0.0177  0.0409  126 LEU   A O   
2582 O O   B LEU   A 126 ? 0.1727 0.1657 0.1716 0.0127  -0.0145 0.0234  126 LEU   A O   
2583 C CB  A LEU   A 126 ? 0.1327 0.1767 0.1855 -0.0156 0.0044  0.0303  126 LEU   A CB  
2584 C CB  B LEU   A 126 ? 0.1770 0.1983 0.2137 -0.0020 -0.0195 0.0195  126 LEU   A CB  
2585 C CG  A LEU   A 126 ? 0.1333 0.2073 0.2088 -0.0170 0.0130  0.0295  126 LEU   A CG  
2586 C CG  B LEU   A 126 ? 0.1849 0.2149 0.2429 -0.0019 -0.0274 0.0170  126 LEU   A CG  
2587 C CD1 A LEU   A 126 ? 0.1414 0.2247 0.2272 -0.0181 0.0035  0.0267  126 LEU   A CD1 
2588 C CD1 B LEU   A 126 ? 0.1856 0.2214 0.2501 -0.0024 -0.0314 0.0152  126 LEU   A CD1 
2589 C CD2 A LEU   A 126 ? 0.1383 0.1995 0.2116 -0.0236 0.0125  0.0407  126 LEU   A CD2 
2590 C CD2 B LEU   A 126 ? 0.1876 0.2147 0.2525 -0.0031 -0.0278 0.0157  126 LEU   A CD2 
2613 N N   A LEU   A 127 ? 0.1381 0.1523 0.1743 0.0028  0.0061  0.0247  127 LEU   A N   
2614 N N   B LEU   A 127 ? 0.1605 0.1555 0.1583 0.0147  0.0002  0.0211  127 LEU   A N   
2615 C CA  A LEU   A 127 ? 0.1393 0.1516 0.1564 0.0002  -0.0007 0.0157  127 LEU   A CA  
2616 C CA  B LEU   A 127 ? 0.1585 0.1564 0.1519 0.0144  -0.0019 0.0276  127 LEU   A CA  
2617 C C   A LEU   A 127 ? 0.1336 0.1418 0.1488 -0.0028 -0.0034 0.0137  127 LEU   A C   
2618 C C   B LEU   A 127 ? 0.1620 0.1608 0.1552 0.0088  -0.0050 0.0231  127 LEU   A C   
2619 O O   A LEU   A 127 ? 0.1381 0.1374 0.1541 -0.0121 -0.0009 0.0126  127 LEU   A O   
2620 O O   B LEU   A 127 ? 0.1678 0.1644 0.1608 0.0104  -0.0024 0.0281  127 LEU   A O   
2621 C CB  A LEU   A 127 ? 0.1423 0.1589 0.1592 0.0070  0.0052  0.0145  127 LEU   A CB  
2622 C CB  B LEU   A 127 ? 0.1572 0.1613 0.1485 0.0110  0.0015  0.0237  127 LEU   A CB  
2623 C CG  A LEU   A 127 ? 0.1453 0.1577 0.1645 0.0071  -0.0064 0.0241  127 LEU   A CG  
2624 C CG  B LEU   A 127 ? 0.1535 0.1677 0.1454 0.0096  -0.0071 0.0262  127 LEU   A CG  
2625 C CD1 A LEU   A 127 ? 0.1535 0.1526 0.1768 0.0044  -0.0069 0.0218  127 LEU   A CD1 
2626 C CD1 B LEU   A 127 ? 0.1462 0.1675 0.1503 0.0118  -0.0000 0.0300  127 LEU   A CD1 
2627 C CD2 A LEU   A 127 ? 0.1582 0.1569 0.1818 0.0085  -0.0206 0.0258  127 LEU   A CD2 
2628 C CD2 B LEU   A 127 ? 0.1610 0.1738 0.1524 0.0057  -0.0169 0.0173  127 LEU   A CD2 
2651 N N   A SER   A 128 ? 0.1404 0.1473 0.1384 -0.0103 -0.0058 0.0208  128 SER   A N   
2652 N N   B SER   A 128 ? 0.1614 0.1619 0.1531 0.0012  -0.0118 0.0235  128 SER   A N   
2653 C CA  A SER   A 128 ? 0.1546 0.1464 0.1317 -0.0066 -0.0085 0.0208  128 SER   A CA  
2654 C CA  B SER   A 128 ? 0.1654 0.1603 0.1510 -0.0068 -0.0205 0.0220  128 SER   A CA  
2655 C C   A SER   A 128 ? 0.1588 0.1465 0.1460 -0.0004 -0.0088 0.0298  128 SER   A C   
2656 C C   B SER   A 128 ? 0.1646 0.1569 0.1545 -0.0151 -0.0343 0.0237  128 SER   A C   
2657 O O   A SER   A 128 ? 0.1753 0.1635 0.1736 0.0030  -0.0018 0.0252  128 SER   A O   
2658 O O   B SER   A 128 ? 0.1624 0.1550 0.1624 -0.0229 -0.0343 0.0166  128 SER   A O   
2659 C CB  A SER   A 128 ? 0.1498 0.1491 0.1456 -0.0096 -0.0079 0.0258  128 SER   A CB  
2660 C CB  B SER   A 128 ? 0.1663 0.1631 0.1552 -0.0079 -0.0139 0.0231  128 SER   A CB  
2661 O OG  A SER   A 128 ? 0.1506 0.1635 0.1592 -0.0075 -0.0047 0.0162  128 SER   A OG  
2662 O OG  B SER   A 128 ? 0.1678 0.1683 0.1607 -0.0101 -0.0076 0.0259  128 SER   A OG  
2673 N N   A ALA   A 129 ? 0.1484 0.1588 0.1717 -0.0026 -0.0074 0.0293  129 ALA   A N   
2674 N N   B ALA   A 129 ? 0.1684 0.1673 0.1671 -0.0136 -0.0424 0.0249  129 ALA   A N   
2675 C CA  A ALA   A 129 ? 0.1468 0.1631 0.1751 0.0015  -0.0048 0.0308  129 ALA   A CA  
2676 C CA  B ALA   A 129 ? 0.1764 0.1775 0.1735 -0.0108 -0.0426 0.0270  129 ALA   A CA  
2677 C C   A ALA   A 129 ? 0.1479 0.1587 0.1542 0.0010  -0.0134 0.0100  129 ALA   A C   
2678 C C   B ALA   A 129 ? 0.1871 0.1819 0.1698 -0.0069 -0.0453 0.0266  129 ALA   A C   
2679 O O   A ALA   A 129 ? 0.1529 0.1631 0.1604 -0.0074 -0.0020 0.0162  129 ALA   A O   
2680 O O   B ALA   A 129 ? 0.1876 0.1835 0.1689 -0.0032 -0.0434 0.0344  129 ALA   A O   
2681 C CB  A ALA   A 129 ? 0.1520 0.1826 0.1909 0.0151  0.0057  0.0426  129 ALA   A CB  
2682 C CB  B ALA   A 129 ? 0.1763 0.1888 0.1732 -0.0101 -0.0411 0.0259  129 ALA   A CB  
2693 N N   A GLY   A 130 ? 0.1510 0.1557 0.1653 0.0002  -0.0012 -0.0010 130 GLY   A N   
2694 N N   B GLY   A 130 ? 0.1985 0.1880 0.1666 -0.0109 -0.0447 0.0276  130 GLY   A N   
2695 C CA  A GLY   A 130 ? 0.1719 0.1565 0.1639 0.0050  0.0068  -0.0024 130 GLY   A CA  
2696 C CA  B GLY   A 130 ? 0.2155 0.1957 0.1822 -0.0148 -0.0422 0.0204  130 GLY   A CA  
2697 C C   A GLY   A 130 ? 0.1763 0.1467 0.1469 0.0085  -0.0018 -0.0040 130 GLY   A C   
2698 C C   B GLY   A 130 ? 0.2284 0.1999 0.1865 -0.0208 -0.0474 0.0196  130 GLY   A C   
2699 O O   A GLY   A 130 ? 0.1873 0.1451 0.1566 0.0096  -0.0290 -0.0040 130 GLY   A O   
2700 O O   B GLY   A 130 ? 0.2338 0.1980 0.1853 -0.0225 -0.0538 0.0208  130 GLY   A O   
2707 N N   A ILE   A 131 ? 0.1843 0.1400 0.1428 0.0001  -0.0049 0.0041  131 ILE   A N   
2708 N N   B ILE   A 131 ? 0.2366 0.2052 0.1956 -0.0257 -0.0403 0.0240  131 ILE   A N   
2709 C CA  A ILE   A 131 ? 0.2010 0.1392 0.1287 -0.0117 -0.0251 0.0038  131 ILE   A CA  
2710 C CA  B ILE   A 131 ? 0.2463 0.2110 0.2075 -0.0293 -0.0360 0.0240  131 ILE   A CA  
2711 C C   A ILE   A 131 ? 0.1873 0.1447 0.1130 -0.0153 -0.0196 0.0144  131 ILE   A C   
2712 C C   B ILE   A 131 ? 0.2487 0.2164 0.2129 -0.0266 -0.0315 0.0423  131 ILE   A C   
2713 O O   A ILE   A 131 ? 0.1975 0.1531 0.1379 -0.0133 -0.0161 0.0228  131 ILE   A O   
2714 O O   B ILE   A 131 ? 0.2479 0.2144 0.2120 -0.0257 -0.0269 0.0513  131 ILE   A O   
2715 C CB  A ILE   A 131 ? 0.2288 0.1547 0.1473 -0.0224 -0.0369 -0.0032 131 ILE   A CB  
2716 C CB  B ILE   A 131 ? 0.2532 0.2152 0.2184 -0.0346 -0.0359 0.0105  131 ILE   A CB  
2717 C CG1 A ILE   A 131 ? 0.2402 0.1820 0.1458 -0.0340 -0.0448 0.0064  131 ILE   A CG1 
2718 C CG1 B ILE   A 131 ? 0.2518 0.2164 0.2326 -0.0396 -0.0335 0.0132  131 ILE   A CG1 
2719 C CG2 A ILE   A 131 ? 0.2463 0.1438 0.1686 -0.0142 -0.0362 -0.0234 131 ILE   A CG2 
2720 C CG2 B ILE   A 131 ? 0.2595 0.2162 0.2159 -0.0315 -0.0392 -0.0006 131 ILE   A CG2 
2721 C CD1 A ILE   A 131 ? 0.2500 0.1948 0.1808 -0.0409 -0.0460 0.0046  131 ILE   A CD1 
2722 C CD1 B ILE   A 131 ? 0.2499 0.2152 0.2364 -0.0414 -0.0347 0.0177  131 ILE   A CD1 
2745 N N   A PHE   A 132 ? 0.1789 0.1419 0.1082 -0.0106 -0.0169 0.0171  132 PHE   A N   
2746 N N   B PHE   A 132 ? 0.2537 0.2243 0.2161 -0.0232 -0.0350 0.0488  132 PHE   A N   
2747 C CA  A PHE   A 132 ? 0.1816 0.1474 0.0968 -0.0094 -0.0054 0.0131  132 PHE   A CA  
2748 C CA  B PHE   A 132 ? 0.2605 0.2333 0.2259 -0.0230 -0.0401 0.0517  132 PHE   A CA  
2749 C C   A PHE   A 132 ? 0.1885 0.1682 0.0956 -0.0051 -0.0123 0.0184  132 PHE   A C   
2750 C C   B PHE   A 132 ? 0.2616 0.2399 0.2149 -0.0181 -0.0378 0.0477  132 PHE   A C   
2751 O O   A PHE   A 132 ? 0.1993 0.1892 0.1011 -0.0039 -0.0230 0.0266  132 PHE   A O   
2752 O O   B PHE   A 132 ? 0.2676 0.2478 0.2193 -0.0176 -0.0324 0.0506  132 PHE   A O   
2753 C CB  A PHE   A 132 ? 0.1715 0.1360 0.0961 -0.0059 -0.0099 0.0264  132 PHE   A CB  
2754 C CB  B PHE   A 132 ? 0.2659 0.2389 0.2521 -0.0265 -0.0442 0.0535  132 PHE   A CB  
2755 C CG  A PHE   A 132 ? 0.1662 0.1360 0.1016 0.0001  -0.0146 0.0163  132 PHE   A CG  
2756 C CG  B PHE   A 132 ? 0.2732 0.2480 0.2879 -0.0274 -0.0426 0.0504  132 PHE   A CG  
2757 C CD1 A PHE   A 132 ? 0.1584 0.1459 0.1322 0.0070  -0.0080 -0.0033 132 PHE   A CD1 
2758 C CD1 B PHE   A 132 ? 0.2770 0.2527 0.3058 -0.0274 -0.0396 0.0467  132 PHE   A CD1 
2759 C CD2 A PHE   A 132 ? 0.1716 0.1421 0.1228 0.0003  -0.0184 0.0018  132 PHE   A CD2 
2760 C CD2 B PHE   A 132 ? 0.2759 0.2514 0.2999 -0.0282 -0.0447 0.0501  132 PHE   A CD2 
2761 C CE1 A PHE   A 132 ? 0.1568 0.1490 0.1355 0.0045  -0.0194 -0.0157 132 PHE   A CE1 
2762 C CE1 B PHE   A 132 ? 0.2782 0.2542 0.3146 -0.0272 -0.0398 0.0434  132 PHE   A CE1 
2763 C CE2 A PHE   A 132 ? 0.1652 0.1496 0.1363 0.0046  -0.0208 -0.0017 132 PHE   A CE2 
2764 C CE2 B PHE   A 132 ? 0.2769 0.2521 0.3072 -0.0295 -0.0446 0.0478  132 PHE   A CE2 
2765 C CZ  A PHE   A 132 ? 0.1532 0.1467 0.1380 -0.0030 -0.0284 -0.0083 132 PHE   A CZ  
2766 C CZ  B PHE   A 132 ? 0.2764 0.2531 0.3122 -0.0291 -0.0440 0.0430  132 PHE   A CZ  
2785 N N   A GLY   A 133 ? 0.1958 0.1740 0.1166 -0.0057 -0.0399 0.0144  133 GLY   A N   
2786 N N   B GLY   A 133 ? 0.2553 0.2391 0.2035 -0.0153 -0.0403 0.0431  133 GLY   A N   
2787 C CA  A GLY   A 133 ? 0.2024 0.1822 0.1377 -0.0138 -0.0482 0.0026  133 GLY   A CA  
2788 C CA  B GLY   A 133 ? 0.2485 0.2407 0.1989 -0.0168 -0.0390 0.0310  133 GLY   A CA  
2789 C C   A GLY   A 133 ? 0.2089 0.1929 0.1327 -0.0156 -0.0503 -0.0094 133 GLY   A C   
2790 C C   B GLY   A 133 ? 0.2402 0.2422 0.1950 -0.0182 -0.0360 0.0203  133 GLY   A C   
2791 O O   A GLY   A 133 ? 0.2292 0.2072 0.1545 -0.0193 -0.0477 -0.0354 133 GLY   A O   
2792 O O   B GLY   A 133 ? 0.2465 0.2471 0.1923 -0.0198 -0.0341 0.0153  133 GLY   A O   
2799 N N   A ALA   A 134 ? 0.2034 0.1810 0.1306 -0.0197 -0.0334 -0.0083 134 ALA   A N   
2800 N N   B ALA   A 134 ? 0.2295 0.2392 0.1923 -0.0161 -0.0361 0.0120  134 ALA   A N   
2801 C CA  A ALA   A 134 ? 0.1966 0.1754 0.1499 -0.0167 -0.0238 -0.0137 134 ALA   A CA  
2802 C CA  B ALA   A 134 ? 0.2186 0.2384 0.1964 -0.0104 -0.0313 0.0114  134 ALA   A CA  
2803 C C   A ALA   A 134 ? 0.1960 0.1892 0.1533 -0.0131 -0.0219 -0.0018 134 ALA   A C   
2804 C C   B ALA   A 134 ? 0.2090 0.2406 0.1978 -0.0075 -0.0311 0.0136  134 ALA   A C   
2805 O O   A ALA   A 134 ? 0.2069 0.1967 0.1759 -0.0071 0.0060  0.0019  134 ALA   A O   
2806 O O   B ALA   A 134 ? 0.2153 0.2435 0.1953 -0.0080 -0.0363 0.0096  134 ALA   A O   
2807 C CB  A ALA   A 134 ? 0.2013 0.1690 0.1764 -0.0185 -0.0166 -0.0156 134 ALA   A CB  
2808 C CB  B ALA   A 134 ? 0.2212 0.2369 0.2001 -0.0080 -0.0276 0.0098  134 ALA   A CB  
2819 N N   A ASP   A 135 ? 0.1979 0.2007 0.1715 -0.0198 -0.0266 0.0138  135 ASP   A N   
2820 N N   B ASP   A 135 ? 0.2004 0.2394 0.2091 -0.0037 -0.0214 0.0213  135 ASP   A N   
2821 C CA  A ASP   A 135 ? 0.1916 0.2192 0.2057 -0.0263 -0.0417 0.0279  135 ASP   A CA  
2822 C CA  B ASP   A 135 ? 0.1953 0.2409 0.2237 -0.0033 -0.0182 0.0308  135 ASP   A CA  
2823 C C   A ASP   A 135 ? 0.1791 0.2011 0.1983 -0.0157 -0.0317 0.0324  135 ASP   A C   
2824 C C   B ASP   A 135 ? 0.1886 0.2302 0.1992 -0.0050 -0.0134 0.0300  135 ASP   A C   
2825 O O   A ASP   A 135 ? 0.1725 0.1903 0.1947 -0.0176 -0.0242 0.0361  135 ASP   A O   
2826 O O   B ASP   A 135 ? 0.1857 0.2263 0.1929 -0.0101 -0.0012 0.0322  135 ASP   A O   
2827 C CB  A ASP   A 135 ? 0.2051 0.2546 0.2596 -0.0421 -0.0645 0.0216  135 ASP   A CB  
2828 C CB  B ASP   A 135 ? 0.2024 0.2539 0.2744 -0.0043 -0.0182 0.0379  135 ASP   A CB  
2829 C CG  A ASP   A 135 ? 0.2119 0.2892 0.3024 -0.0523 -0.0849 0.0237  135 ASP   A CG  
2830 C CG  B ASP   A 135 ? 0.2075 0.2650 0.3190 -0.0027 -0.0230 0.0418  135 ASP   A CG  
2831 O OD1 A ASP   A 135 ? 0.2064 0.3021 0.3088 -0.0568 -0.0897 0.0514  135 ASP   A OD1 
2832 O OD1 B ASP   A 135 ? 0.2147 0.2705 0.3396 0.0014  -0.0132 0.0486  135 ASP   A OD1 
2833 O OD2 A ASP   A 135 ? 0.2412 0.3083 0.3560 -0.0500 -0.0677 0.0198  135 ASP   A OD2 
2834 O OD2 B ASP   A 135 ? 0.2070 0.2694 0.3356 -0.0019 -0.0338 0.0419  135 ASP   A OD2 
2843 N N   A PRO   A 136 ? 0.1701 0.1934 0.2021 -0.0039 -0.0252 0.0389  136 PRO   A N   
2844 N N   B PRO   A 136 ? 0.1801 0.2223 0.1862 0.0009  -0.0224 0.0252  136 PRO   A N   
2845 C CA  A PRO   A 136 ? 0.1650 0.1984 0.2044 -0.0066 -0.0178 0.0276  136 PRO   A CA  
2846 C CA  B PRO   A 136 ? 0.1709 0.2141 0.1794 0.0005  -0.0227 0.0189  136 PRO   A CA  
2847 C C   A PRO   A 136 ? 0.1433 0.1933 0.1918 -0.0026 -0.0085 0.0289  136 PRO   A C   
2848 C C   B PRO   A 136 ? 0.1564 0.2086 0.1756 0.0030  -0.0188 0.0135  136 PRO   A C   
2849 O O   A PRO   A 136 ? 0.1339 0.1887 0.1860 0.0013  0.0065  0.0243  136 PRO   A O   
2850 O O   B PRO   A 136 ? 0.1494 0.2098 0.1721 0.0058  -0.0154 0.0143  136 PRO   A O   
2851 C CB  A PRO   A 136 ? 0.1882 0.1992 0.2239 -0.0054 -0.0255 0.0188  136 PRO   A CB  
2852 C CB  B PRO   A 136 ? 0.1813 0.2133 0.1794 0.0016  -0.0248 0.0191  136 PRO   A CB  
2853 C CG  A PRO   A 136 ? 0.2026 0.2034 0.2417 0.0029  -0.0289 0.0175  136 PRO   A CG  
2854 C CG  B PRO   A 136 ? 0.1876 0.2174 0.1852 0.0032  -0.0293 0.0133  136 PRO   A CG  
2855 C CD  A PRO   A 136 ? 0.1831 0.1916 0.2240 0.0049  -0.0219 0.0383  136 PRO   A CD  
2856 C CD  B PRO   A 136 ? 0.1857 0.2201 0.1859 0.0040  -0.0256 0.0196  136 PRO   A CD  
2871 N N   A ILE   A 137 ? 0.1417 0.1930 0.2184 -0.0046 -0.0206 0.0295  137 ILE   A N   
2872 N N   B ILE   A 137 ? 0.1522 0.2087 0.1773 -0.0018 -0.0212 0.0107  137 ILE   A N   
2873 C CA  A ILE   A 137 ? 0.1453 0.2018 0.2230 -0.0138 -0.0276 0.0232  137 ILE   A CA  
2874 C CA  B ILE   A 137 ? 0.1554 0.2120 0.1840 -0.0102 -0.0179 0.0098  137 ILE   A CA  
2875 C C   A ILE   A 137 ? 0.1456 0.2014 0.2200 -0.0212 -0.0184 0.0324  137 ILE   A C   
2876 C C   B ILE   A 137 ? 0.1559 0.2113 0.1950 -0.0141 -0.0196 0.0145  137 ILE   A C   
2877 O O   A ILE   A 137 ? 0.1499 0.1999 0.2264 -0.0227 -0.0123 0.0308  137 ILE   A O   
2878 O O   B ILE   A 137 ? 0.1637 0.2068 0.2069 -0.0207 -0.0158 0.0063  137 ILE   A O   
2879 C CB  A ILE   A 137 ? 0.1545 0.2186 0.2430 -0.0083 -0.0379 0.0045  137 ILE   A CB  
2880 C CB  B ILE   A 137 ? 0.1601 0.2194 0.1887 -0.0101 -0.0170 -0.0036 137 ILE   A CB  
2881 C CG1 A ILE   A 137 ? 0.1670 0.2377 0.2636 0.0026  -0.0443 -0.0057 137 ILE   A CG1 
2882 C CG1 B ILE   A 137 ? 0.1641 0.2246 0.1941 -0.0066 -0.0207 -0.0120 137 ILE   A CG1 
2883 C CG2 A ILE   A 137 ? 0.1657 0.2202 0.2536 -0.0072 -0.0442 -0.0077 137 ILE   A CG2 
2884 C CG2 B ILE   A 137 ? 0.1649 0.2211 0.1869 -0.0112 -0.0144 -0.0111 137 ILE   A CG2 
2885 C CD1 A ILE   A 137 ? 0.1826 0.2504 0.2842 0.0093  -0.0388 -0.0117 137 ILE   A CD1 
2886 C CD1 B ILE   A 137 ? 0.1707 0.2285 0.2036 -0.0010 -0.0188 -0.0237 137 ILE   A CD1 
2909 N N   A HIS   A 138 ? 0.1436 0.2195 0.2320 -0.0193 -0.0020 0.0313  138 HIS   A N   
2910 N N   B HIS   A 138 ? 0.1507 0.2172 0.2054 -0.0099 -0.0169 0.0235  138 HIS   A N   
2911 C CA  A HIS   A 138 ? 0.1481 0.2206 0.2300 -0.0176 0.0004  0.0281  138 HIS   A CA  
2912 C CA  B HIS   A 138 ? 0.1473 0.2179 0.2086 -0.0114 -0.0158 0.0286  138 HIS   A CA  
2913 C C   A HIS   A 138 ? 0.1479 0.2103 0.2231 -0.0126 -0.0005 0.0407  138 HIS   A C   
2914 C C   B HIS   A 138 ? 0.1420 0.2113 0.2079 -0.0112 -0.0145 0.0406  138 HIS   A C   
2915 O O   A HIS   A 138 ? 0.1547 0.2047 0.2228 -0.0155 0.0048  0.0284  138 HIS   A O   
2916 O O   B HIS   A 138 ? 0.1403 0.2108 0.1986 -0.0147 -0.0128 0.0392  138 HIS   A O   
2917 C CB  A HIS   A 138 ? 0.1528 0.2307 0.2365 -0.0155 -0.0097 0.0089  138 HIS   A CB  
2918 C CB  B HIS   A 138 ? 0.1619 0.2287 0.2188 -0.0147 -0.0204 0.0197  138 HIS   A CB  
2919 C CG  A HIS   A 138 ? 0.1680 0.2360 0.2475 -0.0157 -0.0128 -0.0067 138 HIS   A CG  
2920 C CG  B HIS   A 138 ? 0.1783 0.2388 0.2335 -0.0176 -0.0140 0.0137  138 HIS   A CG  
2921 N ND1 A HIS   A 138 ? 0.1898 0.2442 0.2689 -0.0176 -0.0127 -0.0191 138 HIS   A ND1 
2922 N ND1 B HIS   A 138 ? 0.1894 0.2468 0.2467 -0.0210 -0.0093 0.0075  138 HIS   A ND1 
2923 C CD2 A HIS   A 138 ? 0.1698 0.2347 0.2454 -0.0078 -0.0168 -0.0107 138 HIS   A CD2 
2924 C CD2 B HIS   A 138 ? 0.1819 0.2445 0.2378 -0.0153 -0.0135 0.0125  138 HIS   A CD2 
2925 C CE1 A HIS   A 138 ? 0.1947 0.2438 0.2677 -0.0055 -0.0176 -0.0206 138 HIS   A CE1 
2926 C CE1 B HIS   A 138 ? 0.1920 0.2506 0.2484 -0.0169 -0.0115 0.0081  138 HIS   A CE1 
2927 N NE2 A HIS   A 138 ? 0.1852 0.2400 0.2540 -0.0029 -0.0102 -0.0191 138 HIS   A NE2 
2928 N NE2 B HIS   A 138 ? 0.1850 0.2487 0.2420 -0.0136 -0.0121 0.0108  138 HIS   A NE2 
2943 N N   . SER   A 139 ? 0.1396 0.2034 0.2171 -0.0098 -0.0086 0.0549  139 SER   A N   
2944 C CA  . SER   A 139 ? 0.1397 0.1927 0.2179 -0.0107 -0.0075 0.0623  139 SER   A CA  
2945 C C   . SER   A 139 ? 0.1328 0.1837 0.2139 -0.0117 -0.0040 0.0428  139 SER   A C   
2946 O O   . SER   A 139 ? 0.1304 0.1756 0.2225 -0.0129 0.0007  0.0471  139 SER   A O   
2947 C CB  . SER   A 139 ? 0.1411 0.1886 0.2268 -0.0172 -0.0115 0.0614  139 SER   A CB  
2948 O OG  . SER   A 139 ? 0.1420 0.1861 0.2290 -0.0192 -0.0168 0.0637  139 SER   A OG  
2955 N N   . LEU   A 140 ? 0.1289 0.1880 0.2180 -0.0084 -0.0029 0.0584  140 LEU   A N   
2956 C CA  . LEU   A 140 ? 0.1344 0.1819 0.2253 -0.0107 -0.0001 0.0610  140 LEU   A CA  
2957 C C   . LEU   A 140 ? 0.1254 0.1884 0.2208 -0.0148 0.0013  0.0560  140 LEU   A C   
2958 O O   . LEU   A 140 ? 0.1297 0.1869 0.2414 -0.0060 0.0008  0.0565  140 LEU   A O   
2959 C CB  . LEU   A 140 ? 0.1330 0.1913 0.2317 -0.0119 0.0037  0.0576  140 LEU   A CB  
2960 C CG  . LEU   A 140 ? 0.1352 0.2068 0.2377 -0.0181 0.0043  0.0619  140 LEU   A CG  
2961 C CD1 . LEU   A 140 ? 0.1455 0.2108 0.2428 -0.0119 0.0096  0.0620  140 LEU   A CD1 
2962 C CD2 . LEU   A 140 ? 0.1383 0.2181 0.2486 -0.0126 0.0135  0.0704  140 LEU   A CD2 
2974 N N   . ARG   A 141 ? 0.1327 0.1997 0.2277 -0.0155 -0.0064 0.0472  141 ARG   A N   
2975 C CA  . ARG   A 141 ? 0.1450 0.2093 0.2513 -0.0293 -0.0176 0.0243  141 ARG   A CA  
2976 C C   . ARG   A 141 ? 0.1446 0.1874 0.2340 -0.0209 -0.0126 0.0285  141 ARG   A C   
2977 O O   . ARG   A 141 ? 0.1438 0.1829 0.2398 -0.0227 -0.0004 0.0251  141 ARG   A O   
2978 C CB  . ARG   A 141 ? 0.1596 0.2338 0.2835 -0.0313 -0.0279 0.0034  141 ARG   A CB  
2979 C CG  . ARG   A 141 ? 0.1957 0.2653 0.3132 -0.0337 -0.0163 0.0002  141 ARG   A CG  
2980 C CD  . ARG   A 141 ? 0.2189 0.2851 0.3356 -0.0403 -0.0097 0.0062  141 ARG   A CD  
2981 N NE  . ARG   A 141 ? 0.2084 0.2974 0.3457 -0.0460 -0.0137 0.0092  141 ARG   A NE  
2982 C CZ  . ARG   A 141 ? 0.2124 0.3120 0.3591 -0.0587 -0.0099 0.0128  141 ARG   A CZ  
2983 N NH1 . ARG   A 141 ? 0.2024 0.3132 0.3588 -0.0669 -0.0018 -0.0011 141 ARG   A NH1 
2984 N NH2 . ARG   A 141 ? 0.2187 0.3230 0.3756 -0.0562 -0.0244 0.0177  141 ARG   A NH2 
2998 N N   . VAL   A 142 ? 0.1367 0.1790 0.2279 -0.0165 -0.0073 0.0196  142 VAL   A N   
2999 C CA  . VAL   A 142 ? 0.1424 0.1699 0.2204 -0.0132 0.0065  0.0172  142 VAL   A CA  
3000 C C   . VAL   A 142 ? 0.1272 0.1642 0.2095 -0.0165 0.0026  0.0243  142 VAL   A C   
3001 O O   . VAL   A 142 ? 0.1380 0.1626 0.2147 -0.0064 0.0073  0.0241  142 VAL   A O   
3002 C CB  . VAL   A 142 ? 0.1507 0.1781 0.2146 -0.0137 0.0070  0.0261  142 VAL   A CB  
3003 C CG1 . VAL   A 142 ? 0.1525 0.1737 0.2107 -0.0201 0.0101  0.0183  142 VAL   A CG1 
3004 C CG2 . VAL   A 142 ? 0.1647 0.1959 0.2234 -0.0042 0.0007  0.0331  142 VAL   A CG2 
3014 N N   . CYS   A 143 ? 0.1324 0.1634 0.1976 -0.0171 0.0011  0.0239  143 CYS   A N   
3015 C CA  . CYS   A 143 ? 0.1354 0.1582 0.2074 -0.0148 0.0068  0.0284  143 CYS   A CA  
3016 C C   . CYS   A 143 ? 0.1302 0.1566 0.2068 -0.0117 0.0050  0.0369  143 CYS   A C   
3017 O O   . CYS   A 143 ? 0.1307 0.1542 0.2095 -0.0074 0.0049  0.0369  143 CYS   A O   
3018 C CB  . CYS   A 143 ? 0.1457 0.1547 0.2140 -0.0128 0.0188  0.0443  143 CYS   A CB  
3019 S SG  . CYS   A 143 ? 0.1619 0.1675 0.2030 0.0012  0.0160  0.0281  143 CYS   A SG  
3025 N N   . VAL   A 144 ? 0.1278 0.1640 0.2345 -0.0079 0.0067  0.0490  144 VAL   A N   
3026 C CA  . VAL   A 144 ? 0.1369 0.1657 0.2710 -0.0157 0.0156  0.0454  144 VAL   A CA  
3027 C C   . VAL   A 144 ? 0.1407 0.1580 0.2659 -0.0247 -0.0088 0.0387  144 VAL   A C   
3028 O O   . VAL   A 144 ? 0.1514 0.1612 0.2678 -0.0116 -0.0086 0.0417  144 VAL   A O   
3029 C CB  . VAL   A 144 ? 0.1587 0.1956 0.3351 -0.0043 0.0287  0.0495  144 VAL   A CB  
3030 C CG1 . VAL   A 144 ? 0.1723 0.2115 0.3681 -0.0155 0.0112  0.0484  144 VAL   A CG1 
3031 C CG2 . VAL   A 144 ? 0.1423 0.2033 0.3347 -0.0031 0.0409  0.0612  144 VAL   A CG2 
3041 N N   . ASP   A 145 ? 0.1438 0.1566 0.2735 -0.0220 -0.0032 0.0229  145 ASP   A N   
3042 C CA  . ASP   A 145 ? 0.1555 0.1671 0.2732 -0.0259 -0.0085 0.0118  145 ASP   A CA  
3043 C C   . ASP   A 145 ? 0.1594 0.1548 0.2599 -0.0182 -0.0016 0.0081  145 ASP   A C   
3044 O O   . ASP   A 145 ? 0.1736 0.1630 0.3114 -0.0225 -0.0118 -0.0289 145 ASP   A O   
3045 C CB  . ASP   A 145 ? 0.1689 0.1950 0.2919 -0.0308 -0.0231 0.0116  145 ASP   A CB  
3046 C CG  . ASP   A 145 ? 0.1859 0.2329 0.3265 -0.0469 -0.0297 0.0241  145 ASP   A CG  
3047 O OD1 . ASP   A 145 ? 0.1808 0.2460 0.3386 -0.0595 -0.0183 0.0321  145 ASP   A OD1 
3048 O OD2 . ASP   A 145 ? 0.2046 0.2527 0.3355 -0.0555 -0.0471 0.0225  145 ASP   A OD2 
3053 N N   . THR   A 146 ? 0.1418 0.1445 0.2220 -0.0147 0.0004  0.0164  146 THR   A N   
3054 C CA  . THR   A 146 ? 0.1392 0.1414 0.2015 -0.0106 -0.0023 0.0097  146 THR   A CA  
3055 C C   . THR   A 146 ? 0.1346 0.1384 0.2103 -0.0069 0.0090  0.0171  146 THR   A C   
3056 O O   . THR   A 146 ? 0.1456 0.1543 0.2217 0.0020  0.0006  0.0133  146 THR   A O   
3057 C CB  . THR   A 146 ? 0.1369 0.1445 0.2002 -0.0064 -0.0024 0.0188  146 THR   A CB  
3058 O OG1 . THR   A 146 ? 0.1360 0.1634 0.2138 -0.0070 -0.0020 0.0132  146 THR   A OG1 
3059 C CG2 . THR   A 146 ? 0.1407 0.1492 0.2210 -0.0119 0.0033  0.0164  146 THR   A CG2 
3067 N N   . VAL   A 147 ? 0.1324 0.1432 0.2120 -0.0056 0.0056  0.0213  147 VAL   A N   
3068 C CA  . VAL   A 147 ? 0.1363 0.1428 0.2080 -0.0110 0.0169  0.0263  147 VAL   A CA  
3069 C C   . VAL   A 147 ? 0.1376 0.1443 0.2189 -0.0126 0.0140  0.0262  147 VAL   A C   
3070 O O   . VAL   A 147 ? 0.1404 0.1507 0.2364 -0.0173 0.0083  0.0330  147 VAL   A O   
3071 C CB  . VAL   A 147 ? 0.1510 0.1441 0.2038 -0.0132 0.0224  0.0305  147 VAL   A CB  
3072 C CG1 . VAL   A 147 ? 0.1795 0.1525 0.2036 -0.0102 0.0206  0.0381  147 VAL   A CG1 
3073 C CG2 . VAL   A 147 ? 0.1536 0.1455 0.2073 -0.0071 0.0147  0.0333  147 VAL   A CG2 
3083 N N   . ARG   A 148 ? 0.1351 0.1437 0.2263 -0.0122 0.0189  0.0449  148 ARG   A N   
3084 C CA  . ARG   A 148 ? 0.1441 0.1467 0.2223 -0.0116 0.0109  0.0454  148 ARG   A CA  
3085 C C   . ARG   A 148 ? 0.1578 0.1460 0.2232 -0.0165 0.0130  0.0567  148 ARG   A C   
3086 O O   . ARG   A 148 ? 0.1888 0.1613 0.2443 -0.0226 0.0224  0.0586  148 ARG   A O   
3087 C CB  . ARG   A 148 ? 0.1465 0.1491 0.2384 -0.0064 0.0190  0.0420  148 ARG   A CB  
3088 C CG  . ARG   A 148 ? 0.1664 0.1483 0.2584 -0.0076 0.0307  0.0282  148 ARG   A CG  
3089 C CD  . ARG   A 148 ? 0.1843 0.1485 0.2801 -0.0051 0.0428  0.0527  148 ARG   A CD  
3090 N NE  . ARG   A 148 ? 0.1787 0.1532 0.2818 0.0055  0.0498  0.0545  148 ARG   A NE  
3091 C CZ  . ARG   A 148 ? 0.1754 0.1440 0.2664 0.0054  0.0554  0.0463  148 ARG   A CZ  
3092 N NH1 . ARG   A 148 ? 0.1834 0.1440 0.2753 -0.0039 0.0439  0.0212  148 ARG   A NH1 
3093 N NH2 . ARG   A 148 ? 0.1687 0.1672 0.2706 0.0155  0.0578  0.0522  148 ARG   A NH2 
3107 N N   . THR   A 149 ? 0.1593 0.1558 0.2107 -0.0187 0.0026  0.0450  149 THR   A N   
3108 C CA  . THR   A 149 ? 0.1560 0.1635 0.2126 -0.0156 0.0105  0.0485  149 THR   A CA  
3109 C C   . THR   A 149 ? 0.1495 0.1625 0.2047 -0.0217 0.0174  0.0541  149 THR   A C   
3110 O O   . THR   A 149 ? 0.1470 0.1701 0.2231 -0.0212 0.0150  0.0471  149 THR   A O   
3111 C CB  . THR   A 149 ? 0.1562 0.1768 0.2118 -0.0146 0.0135  0.0426  149 THR   A CB  
3112 O OG1 . THR   A 149 ? 0.1583 0.1675 0.2245 -0.0275 0.0115  0.0351  149 THR   A OG1 
3113 C CG2 . THR   A 149 ? 0.1541 0.1875 0.2237 -0.0103 -0.0013 0.0351  149 THR   A CG2 
3121 N N   . ASN   A 150 ? 0.1551 0.1675 0.2174 -0.0106 0.0116  0.0544  150 ASN   A N   
3122 C CA  . ASN   A 150 ? 0.1689 0.1775 0.2054 -0.0148 0.0225  0.0480  150 ASN   A CA  
3123 C C   . ASN   A 150 ? 0.1506 0.1705 0.2058 -0.0204 0.0128  0.0416  150 ASN   A C   
3124 O O   . ASN   A 150 ? 0.1599 0.1776 0.2360 -0.0157 -0.0036 0.0364  150 ASN   A O   
3125 C CB  . ASN   A 150 ? 0.2148 0.2082 0.2308 -0.0232 0.0432  0.0680  150 ASN   A CB  
3126 C CG  . ASN   A 150 ? 0.2672 0.2394 0.2967 -0.0236 0.0173  0.0731  150 ASN   A CG  
3127 O OD1 . ASN   A 150 ? 0.2904 0.2472 0.3140 -0.0315 0.0117  0.0860  150 ASN   A OD1 
3128 N ND2 . ASN   A 150 ? 0.2944 0.2671 0.3349 -0.0164 0.0054  0.0626  150 ASN   A ND2 
3135 N N   . VAL   A 151 ? 0.1503 0.1570 0.2002 -0.0195 0.0075  0.0439  151 VAL   A N   
3136 C CA  . VAL   A 151 ? 0.1573 0.1592 0.2009 -0.0233 0.0117  0.0404  151 VAL   A CA  
3137 C C   . VAL   A 151 ? 0.1509 0.1549 0.2104 -0.0259 0.0151  0.0440  151 VAL   A C   
3138 O O   . VAL   A 151 ? 0.1587 0.1638 0.2453 -0.0220 0.0158  0.0401  151 VAL   A O   
3139 C CB  . VAL   A 151 ? 0.1864 0.1787 0.2000 -0.0101 0.0094  0.0365  151 VAL   A CB  
3140 C CG1 . VAL   A 151 ? 0.1802 0.2002 0.2190 -0.0091 0.0031  0.0273  151 VAL   A CG1 
3141 C CG2 . VAL   A 151 ? 0.2005 0.1768 0.2053 -0.0083 0.0167  0.0329  151 VAL   A CG2 
3151 N N   A TYR   A 152 ? 0.1548 0.1539 0.2143 -0.0213 0.0151  0.0388  152 TYR   A N   
3152 N N   B TYR   A 152 ? 0.1453 0.1581 0.1731 -0.0242 0.0055  0.0473  152 TYR   A N   
3153 C CA  A TYR   A 152 ? 0.1549 0.1595 0.1953 -0.0162 0.0249  0.0376  152 TYR   A CA  
3154 C CA  B TYR   A 152 ? 0.1424 0.1678 0.1464 -0.0202 -0.0014 0.0418  152 TYR   A CA  
3155 C C   A TYR   A 152 ? 0.1506 0.1527 0.1856 -0.0204 0.0316  0.0448  152 TYR   A C   
3156 C C   B TYR   A 152 ? 0.1324 0.1612 0.1254 -0.0152 -0.0043 0.0385  152 TYR   A C   
3157 O O   A TYR   A 152 ? 0.1528 0.1506 0.2077 -0.0244 0.0254  0.0473  152 TYR   A O   
3158 O O   B TYR   A 152 ? 0.1273 0.1579 0.1365 -0.0068 -0.0123 0.0390  152 TYR   A O   
3159 C CB  A TYR   A 152 ? 0.1696 0.1633 0.1861 -0.0131 0.0408  0.0356  152 TYR   A CB  
3160 C CB  B TYR   A 152 ? 0.1480 0.1780 0.1479 -0.0202 -0.0047 0.0442  152 TYR   A CB  
3161 C CG  A TYR   A 152 ? 0.1841 0.1727 0.1668 -0.0209 0.0336  0.0289  152 TYR   A CG  
3162 C CG  B TYR   A 152 ? 0.1581 0.1929 0.1621 -0.0269 0.0057  0.0399  152 TYR   A CG  
3163 C CD1 A TYR   A 152 ? 0.1953 0.1883 0.1738 -0.0138 0.0251  0.0327  152 TYR   A CD1 
3164 C CD1 B TYR   A 152 ? 0.1666 0.2055 0.1614 -0.0234 0.0047  0.0338  152 TYR   A CD1 
3165 C CD2 A TYR   A 152 ? 0.1884 0.1761 0.1541 -0.0389 0.0354  0.0193  152 TYR   A CD2 
3166 C CD2 B TYR   A 152 ? 0.1629 0.2021 0.1667 -0.0344 0.0081  0.0321  152 TYR   A CD2 
3167 C CE1 A TYR   A 152 ? 0.2155 0.1905 0.1621 -0.0151 0.0083  0.0271  152 TYR   A CE1 
3168 C CE1 B TYR   A 152 ? 0.1796 0.2165 0.1802 -0.0236 0.0008  0.0276  152 TYR   A CE1 
3169 C CE2 A TYR   A 152 ? 0.2055 0.1838 0.1483 -0.0435 0.0328  0.0169  152 TYR   A CE2 
3170 C CE2 B TYR   A 152 ? 0.1785 0.2145 0.1813 -0.0331 0.0082  0.0253  152 TYR   A CE2 
3171 C CZ  A TYR   A 152 ? 0.2244 0.1820 0.1363 -0.0332 0.0123  0.0299  152 TYR   A CZ  
3172 C CZ  B TYR   A 152 ? 0.1898 0.2227 0.1880 -0.0281 0.0056  0.0245  152 TYR   A CZ  
3173 O OH  A TYR   A 152 ? 0.2464 0.1937 0.1468 -0.0240 0.0073  0.0272  152 TYR   A OH  
3174 O OH  B TYR   A 152 ? 0.2062 0.2339 0.2033 -0.0270 0.0050  0.0167  152 TYR   A OH  
3193 N N   A LEU   A 153 ? 0.1489 0.1491 0.1869 -0.0244 0.0338  0.0347  153 LEU   A N   
3194 N N   B LEU   A 153 ? 0.1317 0.1564 0.1214 -0.0187 -0.0010 0.0350  153 LEU   A N   
3195 C CA  A LEU   A 153 ? 0.1485 0.1430 0.1952 -0.0171 0.0277  0.0302  153 LEU   A CA  
3196 C CA  B LEU   A 153 ? 0.1359 0.1531 0.1223 -0.0104 -0.0055 0.0134  153 LEU   A CA  
3197 C C   A LEU   A 153 ? 0.1498 0.1471 0.1901 -0.0197 0.0379  0.0228  153 LEU   A C   
3198 C C   B LEU   A 153 ? 0.1362 0.1578 0.1151 -0.0088 0.0043  0.0114  153 LEU   A C   
3199 O O   A LEU   A 153 ? 0.1536 0.1591 0.2015 -0.0172 0.0439  0.0212  153 LEU   A O   
3200 O O   B LEU   A 153 ? 0.1329 0.1637 0.1195 -0.0090 0.0032  0.0182  153 LEU   A O   
3201 C CB  A LEU   A 153 ? 0.1386 0.1365 0.2029 -0.0169 0.0204  0.0242  153 LEU   A CB  
3202 C CB  B LEU   A 153 ? 0.1399 0.1503 0.1362 -0.0044 -0.0058 0.0058  153 LEU   A CB  
3203 C CG  A LEU   A 153 ? 0.1389 0.1457 0.1973 -0.0142 0.0264  0.0164  153 LEU   A CG  
3204 C CG  B LEU   A 153 ? 0.1502 0.1538 0.1381 0.0042  0.0040  0.0027  153 LEU   A CG  
3205 C CD1 A LEU   A 153 ? 0.1457 0.1404 0.2219 -0.0094 0.0151  0.0154  153 LEU   A CD1 
3206 C CD1 B LEU   A 153 ? 0.1536 0.1515 0.1502 0.0153  0.0081  -0.0007 153 LEU   A CD1 
3207 C CD2 A LEU   A 153 ? 0.1506 0.1562 0.1817 -0.0202 0.0308  -0.0005 153 LEU   A CD2 
3208 C CD2 B LEU   A 153 ? 0.1566 0.1605 0.1450 0.0030  0.0013  0.0015  153 LEU   A CD2 
3231 N N   A ALA   A 154 ? 0.1490 0.1385 0.1776 -0.0143 0.0434  0.0206  154 ALA   A N   
3232 N N   B ALA   A 154 ? 0.1418 0.1590 0.1032 -0.0061 0.0103  0.0135  154 ALA   A N   
3233 C CA  A ALA   A 154 ? 0.1590 0.1476 0.1941 -0.0145 0.0434  0.0209  154 ALA   A CA  
3234 C CA  B ALA   A 154 ? 0.1499 0.1611 0.1104 -0.0052 0.0055  0.0147  154 ALA   A CA  
3235 C C   A ALA   A 154 ? 0.1555 0.1446 0.1979 -0.0038 0.0375  0.0312  154 ALA   A C   
3236 C C   B ALA   A 154 ? 0.1487 0.1668 0.1208 -0.0022 0.0047  0.0256  154 ALA   A C   
3237 O O   A ALA   A 154 ? 0.1603 0.1605 0.1984 -0.0055 0.0281  0.0307  154 ALA   A O   
3238 O O   B ALA   A 154 ? 0.1516 0.1698 0.1105 -0.0010 0.0029  0.0423  154 ALA   A O   
3239 C CB  A ALA   A 154 ? 0.1699 0.1589 0.1988 -0.0077 0.0357  0.0005  154 ALA   A CB  
3240 C CB  B ALA   A 154 ? 0.1566 0.1609 0.1129 -0.0061 -0.0053 0.0071  154 ALA   A CB  
3251 N N   A VAL   A 155 ? 0.1610 0.1481 0.2185 -0.0003 0.0389  0.0457  155 VAL   A N   
3252 N N   B VAL   A 155 ? 0.1516 0.1707 0.1419 -0.0021 -0.0053 0.0215  155 VAL   A N   
3253 C CA  A VAL   A 155 ? 0.1700 0.1584 0.2504 -0.0021 0.0309  0.0604  155 VAL   A CA  
3254 C CA  B VAL   A 155 ? 0.1637 0.1757 0.1603 0.0019  -0.0175 0.0231  155 VAL   A CA  
3255 C C   A VAL   A 155 ? 0.1798 0.1687 0.2950 0.0110  0.0377  0.0737  155 VAL   A C   
3256 C C   B VAL   A 155 ? 0.1804 0.1884 0.2029 0.0123  -0.0234 0.0179  155 VAL   A C   
3257 O O   A VAL   A 155 ? 0.1767 0.1748 0.3099 0.0165  0.0493  0.0593  155 VAL   A O   
3258 O O   B VAL   A 155 ? 0.1777 0.1931 0.2022 0.0146  -0.0365 0.0121  155 VAL   A O   
3259 C CB  A VAL   A 155 ? 0.1778 0.1645 0.2441 0.0009  -0.0009 0.0444  155 VAL   A CB  
3260 C CB  B VAL   A 155 ? 0.1608 0.1739 0.1595 -0.0056 -0.0271 0.0221  155 VAL   A CB  
3261 C CG1 A VAL   A 155 ? 0.1890 0.1786 0.2519 0.0008  -0.0095 0.0449  155 VAL   A CG1 
3262 C CG1 B VAL   A 155 ? 0.1602 0.1753 0.1582 -0.0115 -0.0437 0.0199  155 VAL   A CG1 
3263 C CG2 A VAL   A 155 ? 0.1880 0.1760 0.2478 0.0068  -0.0190 0.0352  155 VAL   A CG2 
3264 C CG2 B VAL   A 155 ? 0.1611 0.1717 0.1524 -0.0111 -0.0291 0.0220  155 VAL   A CG2 
3283 N N   A PHE   A 156 ? 0.1974 0.1748 0.3356 0.0137  0.0323  0.0996  156 PHE   A N   
3284 N N   B PHE   A 156 ? 0.1984 0.2017 0.2300 0.0191  -0.0145 0.0153  156 PHE   A N   
3285 C CA  A PHE   A 156 ? 0.2172 0.1828 0.3742 0.0263  0.0251  0.1045  156 PHE   A CA  
3286 C CA  B PHE   A 156 ? 0.2235 0.2251 0.2665 0.0258  0.0024  0.0098  156 PHE   A CA  
3287 C C   A PHE   A 156 ? 0.2132 0.1947 0.3769 0.0437  0.0376  0.1177  156 PHE   A C   
3288 C C   B PHE   A 156 ? 0.2398 0.2472 0.2859 0.0298  0.0105  0.0176  156 PHE   A C   
3289 O O   A PHE   A 156 ? 0.2271 0.2039 0.4000 0.0331  0.0384  0.0928  156 PHE   A O   
3290 O O   B PHE   A 156 ? 0.2442 0.2495 0.2983 0.0280  0.0097  0.0136  156 PHE   A O   
3291 C CB  A PHE   A 156 ? 0.2456 0.1897 0.3870 0.0178  0.0036  0.1028  156 PHE   A CB  
3292 C CB  B PHE   A 156 ? 0.2330 0.2328 0.2782 0.0236  0.0052  0.0009  156 PHE   A CB  
3293 C CG  A PHE   A 156 ? 0.2722 0.1995 0.4132 0.0270  -0.0197 0.0915  156 PHE   A CG  
3294 C CG  B PHE   A 156 ? 0.2435 0.2402 0.2875 0.0235  0.0022  -0.0075 156 PHE   A CG  
3295 C CD1 A PHE   A 156 ? 0.2842 0.2097 0.4243 0.0283  -0.0237 0.0772  156 PHE   A CD1 
3296 C CD1 B PHE   A 156 ? 0.2487 0.2442 0.2931 0.0246  0.0031  -0.0130 156 PHE   A CD1 
3297 C CD2 A PHE   A 156 ? 0.2873 0.2109 0.4206 0.0361  -0.0332 0.0929  156 PHE   A CD2 
3298 C CD2 B PHE   A 156 ? 0.2469 0.2436 0.2926 0.0197  0.0023  -0.0132 156 PHE   A CD2 
3299 C CE1 A PHE   A 156 ? 0.2952 0.2188 0.4392 0.0317  -0.0207 0.0666  156 PHE   A CE1 
3300 C CE1 B PHE   A 156 ? 0.2506 0.2465 0.2939 0.0246  0.0027  -0.0184 156 PHE   A CE1 
3301 C CE2 A PHE   A 156 ? 0.3009 0.2253 0.4338 0.0375  -0.0298 0.0745  156 PHE   A CE2 
3302 C CE2 B PHE   A 156 ? 0.2506 0.2458 0.2938 0.0213  0.0014  -0.0178 156 PHE   A CE2 
3303 C CZ  A PHE   A 156 ? 0.3014 0.2264 0.4418 0.0404  -0.0212 0.0601  156 PHE   A CZ  
3304 C CZ  B PHE   A 156 ? 0.2515 0.2479 0.2941 0.0240  0.0025  -0.0229 156 PHE   A CZ  
3323 N N   A ASP   A 157 ? 0.2278 0.2193 0.3609 0.0592  0.0496  0.1408  157 ASP   A N   
3324 N N   B ASP   A 157 ? 0.2435 0.2613 0.2871 0.0373  0.0104  0.0268  157 ASP   A N   
3325 C CA  A ASP   A 157 ? 0.2483 0.2477 0.3693 0.0719  0.0512  0.1456  157 ASP   A CA  
3326 C CA  B ASP   A 157 ? 0.2488 0.2786 0.2915 0.0356  0.0126  0.0402  157 ASP   A CA  
3327 C C   A ASP   A 157 ? 0.2309 0.2707 0.3737 0.0803  0.0694  0.1507  157 ASP   A C   
3328 C C   B ASP   A 157 ? 0.2521 0.2867 0.3105 0.0390  0.0158  0.0452  157 ASP   A C   
3329 O O   A ASP   A 157 ? 0.2193 0.2626 0.3662 0.0814  0.0831  0.1637  157 ASP   A O   
3330 O O   B ASP   A 157 ? 0.2510 0.2891 0.3174 0.0383  0.0163  0.0466  157 ASP   A O   
3331 C CB  A ASP   A 157 ? 0.2796 0.2542 0.3928 0.0801  0.0284  0.1346  157 ASP   A CB  
3332 C CB  B ASP   A 157 ? 0.2467 0.2839 0.2789 0.0285  0.0125  0.0461  157 ASP   A CB  
3333 C CG  A ASP   A 157 ? 0.3064 0.2603 0.4155 0.0783  0.0101  0.1317  157 ASP   A CG  
3334 C CG  B ASP   A 157 ? 0.2453 0.2859 0.2662 0.0184  0.0106  0.0513  157 ASP   A CG  
3335 O OD1 A ASP   A 157 ? 0.3284 0.2650 0.4437 0.0686  -0.0091 0.1260  157 ASP   A OD1 
3336 O OD1 B ASP   A 157 ? 0.2419 0.2791 0.2551 0.0160  0.0049  0.0661  157 ASP   A OD1 
3337 O OD2 A ASP   A 157 ? 0.3081 0.2631 0.4280 0.0756  0.0132  0.1302  157 ASP   A OD2 
3338 O OD2 B ASP   A 157 ? 0.2495 0.2928 0.2735 0.0105  0.0142  0.0379  157 ASP   A OD2 
3347 N N   A LYS   A 158 ? 0.2273 0.3001 0.3953 0.0850  0.0724  0.1341  158 LYS   A N   
3348 N N   B LYS   A 158 ? 0.2565 0.2893 0.3219 0.0407  0.0156  0.0486  158 LYS   A N   
3349 C CA  A LYS   A 158 ? 0.2227 0.3259 0.4017 0.0896  0.0798  0.1294  158 LYS   A CA  
3350 C CA  B LYS   A 158 ? 0.2601 0.2917 0.3247 0.0403  0.0139  0.0548  158 LYS   A CA  
3351 C C   A LYS   A 158 ? 0.2067 0.3371 0.3942 0.0900  0.0685  0.1477  158 LYS   A C   
3352 C C   B LYS   A 158 ? 0.2576 0.2902 0.3220 0.0422  0.0146  0.0723  158 LYS   A C   
3353 O O   A LYS   A 158 ? 0.2070 0.3416 0.3923 0.0845  0.0690  0.1554  158 LYS   A O   
3354 O O   B LYS   A 158 ? 0.2567 0.2958 0.3183 0.0456  0.0151  0.0758  158 LYS   A O   
3355 C CB  A LYS   A 158 ? 0.2347 0.3386 0.4216 0.0902  0.0929  0.1185  158 LYS   A CB  
3356 C CB  B LYS   A 158 ? 0.2667 0.2962 0.3334 0.0355  0.0104  0.0422  158 LYS   A CB  
3357 C CG  A LYS   A 158 ? 0.2521 0.3542 0.4467 0.0871  0.1011  0.1091  158 LYS   A CG  
3358 C CG  B LYS   A 158 ? 0.2731 0.2999 0.3374 0.0299  0.0030  0.0329  158 LYS   A CG  
3359 C CD  A LYS   A 158 ? 0.2660 0.3689 0.4657 0.0778  0.1134  0.1085  158 LYS   A CD  
3360 C CD  B LYS   A 158 ? 0.2778 0.3027 0.3400 0.0242  -0.0024 0.0268  158 LYS   A CD  
3361 C CE  A LYS   A 158 ? 0.2758 0.3785 0.4809 0.0661  0.1230  0.1114  158 LYS   A CE  
3362 C CE  B LYS   A 158 ? 0.2813 0.3048 0.3410 0.0200  -0.0049 0.0202  158 LYS   A CE  
3363 N NZ  A LYS   A 158 ? 0.2808 0.3830 0.4868 0.0576  0.1309  0.1142  158 LYS   A NZ  
3364 N NZ  B LYS   A 158 ? 0.2843 0.3056 0.3416 0.0187  -0.0063 0.0143  158 LYS   A NZ  
3391 N N   A ASN   A 159 ? 0.2069 0.3466 0.4029 0.0836  0.0511  0.1515  159 ASN   A N   
3392 N N   B ASN   A 159 ? 0.2571 0.2816 0.3284 0.0379  0.0119  0.0793  159 ASN   A N   
3393 C CA  A ASN   A 159 ? 0.2019 0.3504 0.3988 0.0777  0.0304  0.1666  159 ASN   A CA  
3394 C CA  B ASN   A 159 ? 0.2542 0.2739 0.3283 0.0260  0.0138  0.0812  159 ASN   A CA  
3395 C C   A ASN   A 159 ? 0.1793 0.3486 0.3609 0.0624  0.0279  0.1624  159 ASN   A C   
3396 C C   B ASN   A 159 ? 0.2399 0.2640 0.3059 0.0178  0.0090  0.0705  159 ASN   A C   
3397 O O   A ASN   A 159 ? 0.1663 0.3606 0.3525 0.0590  0.0173  0.1516  159 ASN   A O   
3398 O O   B ASN   A 159 ? 0.2328 0.2623 0.3068 0.0093  0.0108  0.0707  159 ASN   A O   
3399 C CB  A ASN   A 159 ? 0.2231 0.3556 0.4400 0.0792  0.0191  0.1802  159 ASN   A CB  
3400 C CB  B ASN   A 159 ? 0.2637 0.2767 0.3543 0.0226  0.0215  0.0872  159 ASN   A CB  
3401 C CG  A ASN   A 159 ? 0.2426 0.3640 0.4896 0.0717  0.0218  0.1741  159 ASN   A CG  
3402 C CG  B ASN   A 159 ? 0.2724 0.2821 0.3797 0.0182  0.0311  0.0871  159 ASN   A CG  
3403 O OD1 A ASN   A 159 ? 0.2529 0.3713 0.5059 0.0612  0.0341  0.1701  159 ASN   A OD1 
3404 O OD1 B ASN   A 159 ? 0.2781 0.2857 0.3898 0.0156  0.0321  0.0891  159 ASN   A OD1 
3405 N ND2 A ASN   A 159 ? 0.2501 0.3681 0.5116 0.0698  0.0251  0.1657  159 ASN   A ND2 
3406 N ND2 B ASN   A 159 ? 0.2758 0.2874 0.3929 0.0159  0.0397  0.0839  159 ASN   A ND2 
3419 N N   A LEU   A 160 ? 0.1659 0.3301 0.3455 0.0484  0.0165  0.1621  160 LEU   A N   
3420 N N   B LEU   A 160 ? 0.2282 0.2533 0.2782 0.0190  -0.0005 0.0602  160 LEU   A N   
3421 C CA  A LEU   A 160 ? 0.1638 0.3110 0.3220 0.0306  0.0184  0.1516  160 LEU   A CA  
3422 C CA  B LEU   A 160 ? 0.2147 0.2396 0.2422 0.0186  -0.0153 0.0531  160 LEU   A CA  
3423 C C   A LEU   A 160 ? 0.1504 0.3056 0.3085 0.0219  0.0272  0.1397  160 LEU   A C   
3424 C C   B LEU   A 160 ? 0.2046 0.2276 0.2245 0.0162  -0.0092 0.0515  160 LEU   A C   
3425 O O   A LEU   A 160 ? 0.1479 0.3187 0.3231 0.0137  0.0260  0.1271  160 LEU   A O   
3426 O O   B LEU   A 160 ? 0.2044 0.2318 0.2272 0.0125  -0.0138 0.0459  160 LEU   A O   
3427 C CB  A LEU   A 160 ? 0.1718 0.3042 0.3078 0.0181  0.0198  0.1451  160 LEU   A CB  
3428 C CB  B LEU   A 160 ? 0.2184 0.2402 0.2357 0.0117  -0.0213 0.0463  160 LEU   A CB  
3429 C CG  A LEU   A 160 ? 0.1779 0.3045 0.3117 0.0028  0.0299  0.1217  160 LEU   A CG  
3430 C CG  B LEU   A 160 ? 0.2227 0.2423 0.2319 0.0071  -0.0266 0.0353  160 LEU   A CG  
3431 C CD1 A LEU   A 160 ? 0.1923 0.3091 0.3180 0.0011  0.0215  0.1118  160 LEU   A CD1 
3432 C CD1 B LEU   A 160 ? 0.2227 0.2431 0.2295 0.0032  -0.0249 0.0326  160 LEU   A CD1 
3433 C CD2 A LEU   A 160 ? 0.1777 0.3044 0.3091 -0.0037 0.0386  0.1139  160 LEU   A CD2 
3434 C CD2 B LEU   A 160 ? 0.2238 0.2430 0.2315 0.0038  -0.0263 0.0318  160 LEU   A CD2 
3457 N N   A TYR   A 161 ? 0.1516 0.2892 0.3004 0.0217  0.0362  0.1352  161 TYR   A N   
3458 N N   B TYR   A 161 ? 0.1952 0.2109 0.2115 0.0194  0.0004  0.0537  161 TYR   A N   
3459 C CA  A TYR   A 161 ? 0.1606 0.2725 0.2962 0.0220  0.0400  0.1304  161 TYR   A CA  
3460 C CA  B TYR   A 161 ? 0.1939 0.2014 0.2115 0.0206  0.0176  0.0453  161 TYR   A CA  
3461 C C   A TYR   A 161 ? 0.1533 0.2803 0.3151 0.0236  0.0424  0.1277  161 TYR   A C   
3462 C C   B TYR   A 161 ? 0.2021 0.2023 0.2276 0.0152  0.0215  0.0351  161 TYR   A C   
3463 O O   A TYR   A 161 ? 0.1449 0.2839 0.3129 0.0229  0.0369  0.1160  161 TYR   A O   
3464 O O   B TYR   A 161 ? 0.1976 0.1973 0.2262 0.0125  0.0180  0.0315  161 TYR   A O   
3465 C CB  A TYR   A 161 ? 0.1729 0.2563 0.2947 0.0175  0.0429  0.1059  161 TYR   A CB  
3466 C CB  B TYR   A 161 ? 0.1853 0.1989 0.2104 0.0243  0.0281  0.0425  161 TYR   A CB  
3467 C CG  A TYR   A 161 ? 0.1860 0.2463 0.2893 0.0131  0.0388  0.0786  161 TYR   A CG  
3468 C CG  B TYR   A 161 ? 0.1746 0.1951 0.2109 0.0282  0.0336  0.0376  161 TYR   A CG  
3469 C CD1 A TYR   A 161 ? 0.1855 0.2329 0.2823 0.0126  0.0392  0.0714  161 TYR   A CD1 
3470 C CD1 B TYR   A 161 ? 0.1685 0.1940 0.2116 0.0264  0.0351  0.0387  161 TYR   A CD1 
3471 C CD2 A TYR   A 161 ? 0.1933 0.2527 0.2920 0.0083  0.0343  0.0638  161 TYR   A CD2 
3472 C CD2 B TYR   A 161 ? 0.1727 0.1963 0.2161 0.0287  0.0376  0.0376  161 TYR   A CD2 
3473 C CE1 A TYR   A 161 ? 0.1919 0.2236 0.2724 0.0104  0.0328  0.0713  161 TYR   A CE1 
3474 C CE1 B TYR   A 161 ? 0.1691 0.2000 0.2188 0.0248  0.0315  0.0405  161 TYR   A CE1 
3475 C CE2 A TYR   A 161 ? 0.1974 0.2436 0.2844 0.0034  0.0320  0.0652  161 TYR   A CE2 
3476 C CE2 B TYR   A 161 ? 0.1717 0.1972 0.2226 0.0245  0.0397  0.0445  161 TYR   A CE2 
3477 C CZ  A TYR   A 161 ? 0.2035 0.2308 0.2769 0.0012  0.0277  0.0720  161 TYR   A CZ  
3478 C CZ  B TYR   A 161 ? 0.1765 0.2013 0.2266 0.0235  0.0360  0.0454  161 TYR   A CZ  
3479 O OH  A TYR   A 161 ? 0.2190 0.2256 0.2898 -0.0069 0.0245  0.0691  161 TYR   A OH  
3480 O OH  B TYR   A 161 ? 0.1899 0.2088 0.2476 0.0214  0.0317  0.0500  161 TYR   A OH  
3499 N N   A ASP   A 162 ? 0.1543 0.2895 0.3372 0.0235  0.0496  0.1306  162 ASP   A N   
3500 N N   B ASP   A 162 ? 0.2125 0.2130 0.2456 0.0093  0.0286  0.0371  162 ASP   A N   
3501 C CA  A ASP   A 162 ? 0.1451 0.3090 0.3498 0.0202  0.0492  0.1306  162 ASP   A CA  
3502 C CA  B ASP   A 162 ? 0.2281 0.2249 0.2661 0.0073  0.0288  0.0266  162 ASP   A CA  
3503 C C   A ASP   A 162 ? 0.1430 0.3184 0.3467 0.0136  0.0382  0.1367  162 ASP   A C   
3504 C C   B ASP   A 162 ? 0.2348 0.2206 0.2632 0.0008  0.0219  0.0169  162 ASP   A C   
3505 O O   A ASP   A 162 ? 0.1440 0.3099 0.3559 -0.0025 0.0394  0.1470  162 ASP   A O   
3506 O O   B ASP   A 162 ? 0.2336 0.2202 0.2697 -0.0019 0.0245  0.0080  162 ASP   A O   
3507 C CB  A ASP   A 162 ? 0.1540 0.3270 0.3685 0.0204  0.0597  0.1199  162 ASP   A CB  
3508 C CB  B ASP   A 162 ? 0.2382 0.2412 0.2989 0.0110  0.0324  0.0267  162 ASP   A CB  
3509 C CG  A ASP   A 162 ? 0.1631 0.3433 0.3903 0.0273  0.0700  0.1047  162 ASP   A CG  
3510 C CG  B ASP   A 162 ? 0.2500 0.2547 0.3218 0.0119  0.0378  0.0297  162 ASP   A CG  
3511 O OD1 A ASP   A 162 ? 0.1715 0.3563 0.3952 0.0197  0.0665  0.0928  162 ASP   A OD1 
3512 O OD1 B ASP   A 162 ? 0.2573 0.2621 0.3354 0.0138  0.0406  0.0255  162 ASP   A OD1 
3513 O OD2 A ASP   A 162 ? 0.1744 0.3471 0.4086 0.0383  0.0691  0.0952  162 ASP   A OD2 
3514 O OD2 B ASP   A 162 ? 0.2523 0.2577 0.3323 0.0121  0.0385  0.0354  162 ASP   A OD2 
3523 N N   A LYS   A 163 ? 0.1473 0.3272 0.3455 0.0120  0.0027  0.1338  163 LYS   A N   
3524 N N   B LYS   A 163 ? 0.2460 0.2237 0.2597 -0.0055 0.0152  0.0229  163 LYS   A N   
3525 C CA  A LYS   A 163 ? 0.1599 0.3343 0.3373 -0.0030 -0.0050 0.1294  163 LYS   A CA  
3526 C CA  B LYS   A 163 ? 0.2571 0.2296 0.2607 -0.0123 0.0098  0.0188  163 LYS   A CA  
3527 C C   A LYS   A 163 ? 0.1526 0.3247 0.3330 -0.0098 0.0087  0.1210  163 LYS   A C   
3528 C C   B LYS   A 163 ? 0.2480 0.2120 0.2432 -0.0199 0.0038  0.0093  163 LYS   A C   
3529 O O   A LYS   A 163 ? 0.1508 0.3385 0.3584 -0.0157 0.0087  0.1127  163 LYS   A O   
3530 O O   B LYS   A 163 ? 0.2396 0.1937 0.2356 -0.0304 0.0003  -0.0067 163 LYS   A O   
3531 C CB  A LYS   A 163 ? 0.1939 0.3533 0.3630 -0.0029 -0.0205 0.1170  163 LYS   A CB  
3532 C CB  B LYS   A 163 ? 0.2761 0.2486 0.2859 -0.0140 0.0158  0.0238  163 LYS   A CB  
3533 C CG  A LYS   A 163 ? 0.2313 0.3710 0.4001 -0.0114 -0.0157 0.1032  163 LYS   A CG  
3534 C CG  B LYS   A 163 ? 0.2936 0.2663 0.3207 -0.0160 0.0161  0.0266  163 LYS   A CG  
3535 C CD  A LYS   A 163 ? 0.2646 0.3879 0.4366 -0.0162 -0.0197 0.0893  163 LYS   A CD  
3536 C CD  B LYS   A 163 ? 0.3088 0.2812 0.3550 -0.0170 0.0195  0.0280  163 LYS   A CD  
3537 C CE  A LYS   A 163 ? 0.2805 0.3995 0.4706 -0.0217 -0.0220 0.0788  163 LYS   A CE  
3538 C CE  B LYS   A 163 ? 0.3199 0.2931 0.3829 -0.0176 0.0225  0.0278  163 LYS   A CE  
3539 N NZ  A LYS   A 163 ? 0.2931 0.4067 0.4878 -0.0247 -0.0245 0.0731  163 LYS   A NZ  
3540 N NZ  B LYS   A 163 ? 0.3254 0.3001 0.4010 -0.0181 0.0244  0.0280  163 LYS   A NZ  
3567 N N   A LEU   A 164 ? 0.1342 0.2986 0.3149 -0.0169 0.0069  0.1156  164 LEU   A N   
3568 N N   B LEU   A 164 ? 0.2437 0.2164 0.2362 -0.0115 0.0012  0.0165  164 LEU   A N   
3569 C CA  A LEU   A 164 ? 0.1362 0.2796 0.2994 -0.0257 0.0196  0.1044  164 LEU   A CA  
3570 C CA  B LEU   A 164 ? 0.2414 0.2197 0.2356 -0.0102 0.0057  0.0201  164 LEU   A CA  
3571 C C   A LEU   A 164 ? 0.1418 0.2737 0.2954 -0.0239 0.0236  0.0961  164 LEU   A C   
3572 C C   B LEU   A 164 ? 0.2362 0.2137 0.2360 -0.0082 0.0047  0.0154  164 LEU   A C   
3573 O O   A LEU   A 164 ? 0.1524 0.2757 0.3036 -0.0249 0.0415  0.0736  164 LEU   A O   
3574 O O   B LEU   A 164 ? 0.2335 0.2064 0.2325 -0.0130 0.0128  0.0150  164 LEU   A O   
3575 C CB  A LEU   A 164 ? 0.1338 0.2701 0.2901 -0.0274 0.0264  0.1073  164 LEU   A CB  
3576 C CB  B LEU   A 164 ? 0.2439 0.2296 0.2397 -0.0090 0.0093  0.0234  164 LEU   A CB  
3577 C CG  A LEU   A 164 ? 0.1438 0.2654 0.2905 -0.0168 0.0263  0.0975  164 LEU   A CG  
3578 C CG  B LEU   A 164 ? 0.2476 0.2394 0.2468 -0.0096 0.0149  0.0294  164 LEU   A CG  
3579 C CD1 A LEU   A 164 ? 0.1454 0.2617 0.2807 -0.0013 0.0258  0.0847  164 LEU   A CD1 
3580 C CD1 B LEU   A 164 ? 0.2473 0.2438 0.2498 -0.0119 0.0200  0.0289  164 LEU   A CD1 
3581 C CD2 A LEU   A 164 ? 0.1629 0.2668 0.2954 -0.0183 0.0227  0.0858  164 LEU   A CD2 
3582 C CD2 B LEU   A 164 ? 0.2511 0.2406 0.2514 -0.0103 0.0163  0.0300  164 LEU   A CD2 
3605 N N   A VAL   A 165 ? 0.1360 0.2668 0.2784 -0.0208 0.0195  0.1074  165 VAL   A N   
3606 N N   B VAL   A 165 ? 0.2321 0.2196 0.2427 -0.0076 -0.0002 0.0132  165 VAL   A N   
3607 C CA  A VAL   A 165 ? 0.1435 0.2684 0.2574 -0.0182 0.0244  0.0955  165 VAL   A CA  
3608 C CA  B VAL   A 165 ? 0.2320 0.2282 0.2563 -0.0035 -0.0018 0.0083  165 VAL   A CA  
3609 C C   A VAL   A 165 ? 0.1397 0.2824 0.2550 -0.0096 0.0283  0.0835  165 VAL   A C   
3610 C C   B VAL   A 165 ? 0.2257 0.2249 0.2602 0.0024  0.0079  0.0109  165 VAL   A C   
3611 O O   A VAL   A 165 ? 0.1413 0.2838 0.2446 -0.0110 0.0332  0.0770  165 VAL   A O   
3612 O O   B VAL   A 165 ? 0.2248 0.2234 0.2643 0.0006  0.0138  0.0183  165 VAL   A O   
3613 C CB  A VAL   A 165 ? 0.1575 0.2594 0.2556 -0.0223 0.0285  0.0872  165 VAL   A CB  
3614 C CB  B VAL   A 165 ? 0.2382 0.2406 0.2653 -0.0061 -0.0109 0.0038  165 VAL   A CB  
3615 C CG1 A VAL   A 165 ? 0.1632 0.2594 0.2598 -0.0256 0.0361  0.0725  165 VAL   A CG1 
3616 C CG1 B VAL   A 165 ? 0.2407 0.2486 0.2676 -0.0072 -0.0190 0.0000  165 VAL   A CG1 
3617 C CG2 A VAL   A 165 ? 0.1658 0.2605 0.2497 -0.0203 0.0196  0.0917  165 VAL   A CG2 
3618 C CG2 B VAL   A 165 ? 0.2404 0.2420 0.2693 -0.0090 -0.0106 0.0008  165 VAL   A CG2 
3637 N N   A SER   A 166 ? 0.1276 0.2914 0.2730 -0.0085 0.0278  0.0732  166 SER   A N   
3638 N N   B SER   A 166 ? 0.2175 0.2262 0.2661 0.0089  0.0126  0.0057  166 SER   A N   
3639 C CA  A SER   A 166 ? 0.1357 0.3110 0.2918 -0.0139 0.0204  0.0540  166 SER   A CA  
3640 C CA  B SER   A 166 ? 0.2182 0.2296 0.2738 0.0139  0.0118  0.0016  166 SER   A CA  
3641 C C   A SER   A 166 ? 0.1371 0.3276 0.3008 -0.0149 0.0076  0.0381  166 SER   A C   
3642 C C   B SER   A 166 ? 0.2141 0.2269 0.2552 0.0221  -0.0047 0.0051  166 SER   A C   
3643 O O   A SER   A 166 ? 0.1566 0.3352 0.3340 -0.0230 0.0174  0.0226  166 SER   A O   
3644 O O   B SER   A 166 ? 0.2157 0.2289 0.2644 0.0286  -0.0012 0.0021  166 SER   A O   
3645 C CB  A SER   A 166 ? 0.1547 0.3189 0.3213 -0.0070 0.0120  0.0402  166 SER   A CB  
3646 C CB  B SER   A 166 ? 0.2252 0.2394 0.3050 0.0151  0.0230  -0.0058 166 SER   A CB  
3647 O OG  A SER   A 166 ? 0.1930 0.3249 0.3497 -0.0155 0.0086  0.0334  166 SER   A OG  
3648 O OG  B SER   A 166 ? 0.2394 0.2491 0.3321 0.0131  0.0275  -0.0148 166 SER   A OG  
3659 N N   A SER   A 167 ? 0.1518 0.3351 0.2830 -0.0021 0.0014  0.0331  167 SER   A N   
3660 N N   B SER   A 167 ? 0.2163 0.2290 0.2356 0.0220  -0.0193 0.0092  167 SER   A N   
3661 C CA  A SER   A 167 ? 0.1777 0.3419 0.2790 0.0037  -0.0016 0.0216  167 SER   A CA  
3662 C CA  B SER   A 167 ? 0.2235 0.2335 0.2245 0.0129  -0.0246 0.0087  167 SER   A CA  
3663 C C   A SER   A 167 ? 0.1797 0.3402 0.2697 0.0065  0.0051  0.0167  167 SER   A C   
3664 C C   B SER   A 167 ? 0.2291 0.2446 0.2229 0.0122  -0.0186 0.0173  167 SER   A C   
3665 O O   A SER   A 167 ? 0.1944 0.3432 0.2728 0.0078  -0.0051 0.0161  167 SER   A O   
3666 O O   B SER   A 167 ? 0.2304 0.2401 0.2175 0.0142  -0.0194 0.0182  167 SER   A O   
3667 C CB  A SER   A 167 ? 0.1982 0.3491 0.2858 0.0091  0.0076  0.0200  167 SER   A CB  
3668 C CB  B SER   A 167 ? 0.2284 0.2288 0.2209 0.0053  -0.0264 0.0005  167 SER   A CB  
3669 O OG  A SER   A 167 ? 0.2118 0.3531 0.2917 0.0089  0.0236  0.0226  167 SER   A OG  
3670 O OG  B SER   A 167 ? 0.2297 0.2241 0.2164 0.0009  -0.0245 -0.0117 167 SER   A OG  
3681 N N   A PHE   A 168 ? 0.1681 0.3333 0.2604 0.0112  0.0114  0.0140  168 PHE   A N   
3682 N N   B PHE   A 168 ? 0.2347 0.2596 0.2332 0.0127  -0.0139 0.0326  168 PHE   A N   
3683 C CA  A PHE   A 168 ? 0.1667 0.3258 0.2725 0.0064  0.0199  0.0076  168 PHE   A CA  
3684 C CA  B PHE   A 168 ? 0.2403 0.2780 0.2583 0.0103  -0.0065 0.0405  168 PHE   A CA  
3685 C C   A PHE   A 168 ? 0.1850 0.3425 0.3194 -0.0101 0.0533  -0.0094 168 PHE   A C   
3686 C C   B PHE   A 168 ? 0.2512 0.2939 0.2927 0.0069  0.0013  0.0324  168 PHE   A C   
3687 O O   A PHE   A 168 ? 0.1878 0.3448 0.3573 -0.0253 0.0579  -0.0025 168 PHE   A O   
3688 O O   B PHE   A 168 ? 0.2543 0.2917 0.3024 0.0066  0.0049  0.0313  168 PHE   A O   
3689 C CB  A PHE   A 168 ? 0.1661 0.3031 0.2526 0.0002  -0.0004 0.0182  168 PHE   A CB  
3690 C CB  B PHE   A 168 ? 0.2359 0.2796 0.2522 0.0131  0.0000  0.0542  168 PHE   A CB  
3691 C CG  A PHE   A 168 ? 0.1564 0.2817 0.2252 -0.0101 -0.0069 0.0217  168 PHE   A CG  
3692 C CG  B PHE   A 168 ? 0.2328 0.2812 0.2467 0.0119  0.0087  0.0692  168 PHE   A CG  
3693 C CD1 A PHE   A 168 ? 0.1582 0.2797 0.2242 -0.0171 -0.0127 0.0257  168 PHE   A CD1 
3694 C CD1 B PHE   A 168 ? 0.2336 0.2815 0.2459 0.0081  0.0169  0.0727  168 PHE   A CD1 
3695 C CD2 A PHE   A 168 ? 0.1503 0.2679 0.2165 -0.0068 0.0137  0.0190  168 PHE   A CD2 
3696 C CD2 B PHE   A 168 ? 0.2328 0.2831 0.2464 0.0120  0.0150  0.0744  168 PHE   A CD2 
3697 C CE1 A PHE   A 168 ? 0.1481 0.2760 0.2196 -0.0218 -0.0114 0.0233  168 PHE   A CE1 
3698 C CE1 B PHE   A 168 ? 0.2335 0.2808 0.2459 0.0076  0.0212  0.0774  168 PHE   A CE1 
3699 C CE2 A PHE   A 168 ? 0.1561 0.2641 0.2189 -0.0090 0.0143  0.0266  168 PHE   A CE2 
3700 C CE2 B PHE   A 168 ? 0.2343 0.2816 0.2470 0.0111  0.0169  0.0800  168 PHE   A CE2 
3701 C CZ  A PHE   A 168 ? 0.1545 0.2698 0.2180 -0.0179 0.0042  0.0278  168 PHE   A CZ  
3702 C CZ  B PHE   A 168 ? 0.2350 0.2809 0.2458 0.0075  0.0198  0.0800  168 PHE   A CZ  
3721 N N   A LEU   A 169 ? 0.2292 0.3552 0.3572 -0.0185 0.0504  -0.0325 169 LEU   A N   
3722 N N   B LEU   A 169 ? 0.2660 0.3135 0.3220 0.0012  0.0008  0.0270  169 LEU   A N   
3723 C CA  A LEU   A 169 ? 0.2942 0.3721 0.4140 -0.0188 0.0178  -0.0482 169 LEU   A CA  
3724 C CA  B LEU   A 169 ? 0.2816 0.3298 0.3542 -0.0049 -0.0044 0.0202  169 LEU   A CA  
3725 C C   A LEU   A 169 ? 0.3099 0.3751 0.4408 -0.0181 0.0108  -0.0452 169 LEU   A C   
3726 C C   B LEU   A 169 ? 0.2799 0.3318 0.3653 -0.0083 -0.0071 0.0272  169 LEU   A C   
3727 O O   A LEU   A 169 ? 0.3273 0.3750 0.4522 -0.0160 0.0109  -0.0446 169 LEU   A O   
3728 O O   B LEU   A 169 ? 0.2741 0.3330 0.3700 -0.0081 -0.0081 0.0282  169 LEU   A O   
3729 C CB  A LEU   A 169 ? 0.3340 0.3845 0.4344 -0.0189 -0.0033 -0.0611 169 LEU   A CB  
3730 C CB  B LEU   A 169 ? 0.2984 0.3415 0.3732 -0.0086 -0.0108 0.0065  169 LEU   A CB  
3731 C CG  A LEU   A 169 ? 0.3621 0.3925 0.4464 -0.0208 -0.0190 -0.0732 169 LEU   A CG  
3732 C CG  B LEU   A 169 ? 0.3137 0.3510 0.3892 -0.0109 -0.0149 -0.0034 169 LEU   A CG  
3733 C CD1 A LEU   A 169 ? 0.3738 0.3964 0.4545 -0.0199 -0.0235 -0.0742 169 LEU   A CD1 
3734 C CD1 B LEU   A 169 ? 0.3203 0.3537 0.3969 -0.0130 -0.0154 -0.0058 169 LEU   A CD1 
3735 C CD2 A LEU   A 169 ? 0.3733 0.3939 0.4473 -0.0228 -0.0223 -0.0785 169 LEU   A CD2 
3736 C CD2 B LEU   A 169 ? 0.3172 0.3537 0.3951 -0.0095 -0.0160 -0.0075 169 LEU   A CD2 
3737 O OXT A LEU   A 169 ? 0.3046 0.3777 0.4457 -0.0153 0.0109  -0.0474 169 LEU   A OXT 
3738 O OXT B LEU   A 169 ? 0.2811 0.3327 0.3675 -0.0108 -0.0103 0.0310  169 LEU   A OXT 
3761 N N   A SER   B 1   ? 0.3779 0.3863 0.4230 -0.1212 -0.0896 0.0475  1   SER   B N   
3762 N N   B SER   B 1   ? 0.3571 0.3523 0.3772 -0.0754 -0.0531 0.0232  1   SER   B N   
3763 C CA  A SER   B 1   ? 0.3676 0.3855 0.4144 -0.1225 -0.0951 0.0514  1   SER   B CA  
3764 C CA  B SER   B 1   ? 0.3532 0.3541 0.3732 -0.0745 -0.0540 0.0251  1   SER   B CA  
3765 C C   A SER   B 1   ? 0.3389 0.3789 0.3919 -0.1225 -0.1007 0.0679  1   SER   B C   
3766 C C   B SER   B 1   ? 0.3418 0.3547 0.3645 -0.0694 -0.0570 0.0351  1   SER   B C   
3767 O O   A SER   B 1   ? 0.3473 0.3787 0.3748 -0.1153 -0.0945 0.0684  1   SER   B O   
3768 O O   B SER   B 1   ? 0.3437 0.3539 0.3562 -0.0691 -0.0589 0.0343  1   SER   B O   
3769 C CB  A SER   B 1   ? 0.3813 0.3886 0.4366 -0.1198 -0.0886 0.0401  1   SER   B CB  
3770 C CB  B SER   B 1   ? 0.3584 0.3536 0.3847 -0.0765 -0.0494 0.0164  1   SER   B CB  
3771 O OG  A SER   B 1   ? 0.3932 0.3970 0.4613 -0.1169 -0.0765 0.0307  1   SER   B OG  
3772 O OG  B SER   B 1   ? 0.3626 0.3558 0.3946 -0.0782 -0.0447 0.0097  1   SER   B OG  
3787 N N   A MET   B 2   ? 0.3106 0.3706 0.3875 -0.1220 -0.1010 0.0973  2   MET   B N   
3788 N N   B MET   B 2   ? 0.3307 0.3550 0.3635 -0.0624 -0.0546 0.0504  2   MET   B N   
3789 C CA  A MET   B 2   ? 0.2932 0.3643 0.3930 -0.1025 -0.0974 0.1159  2   MET   B CA  
3790 C CA  B MET   B 2   ? 0.3196 0.3531 0.3609 -0.0510 -0.0513 0.0633  2   MET   B CA  
3791 C C   A MET   B 2   ? 0.2553 0.3333 0.3492 -0.0867 -0.1037 0.1462  2   MET   B C   
3792 C C   B MET   B 2   ? 0.2966 0.3320 0.3284 -0.0457 -0.0482 0.0732  2   MET   B C   
3793 O O   A MET   B 2   ? 0.2457 0.3418 0.3428 -0.0747 -0.1157 0.1541  2   MET   B O   
3794 O O   B MET   B 2   ? 0.2972 0.3371 0.3309 -0.0426 -0.0460 0.0731  2   MET   B O   
3795 C CB  A MET   B 2   ? 0.3231 0.3958 0.4670 -0.0812 -0.0788 0.0926  2   MET   B CB  
3796 C CB  B MET   B 2   ? 0.3321 0.3717 0.3978 -0.0408 -0.0506 0.0640  2   MET   B CB  
3797 C CG  A MET   B 2   ? 0.3491 0.4229 0.5382 -0.0602 -0.0610 0.0784  2   MET   B CG  
3798 C CG  B MET   B 2   ? 0.3415 0.3859 0.4305 -0.0313 -0.0507 0.0679  2   MET   B CG  
3799 S SD  A MET   B 2   ? 0.3745 0.4478 0.5985 -0.0419 -0.0450 0.0645  2   MET   B SD  
3800 S SD  B MET   B 2   ? 0.3495 0.3982 0.4575 -0.0227 -0.0520 0.0716  2   MET   B SD  
3801 C CE  A MET   B 2   ? 0.3766 0.4527 0.6020 -0.0403 -0.0368 0.0620  2   MET   B CE  
3802 C CE  B MET   B 2   ? 0.3489 0.3985 0.4633 -0.0232 -0.0483 0.0683  2   MET   B CE  
3821 N N   A VAL   B 3   ? 0.2279 0.2878 0.3154 -0.0948 -0.0934 0.1611  3   VAL   B N   
3822 N N   B VAL   B 3   ? 0.2720 0.3041 0.2940 -0.0462 -0.0480 0.0811  3   VAL   B N   
3823 C CA  A VAL   B 3   ? 0.2246 0.2532 0.3069 -0.0809 -0.0807 0.1415  3   VAL   B CA  
3824 C CA  B VAL   B 3   ? 0.2505 0.2765 0.2697 -0.0430 -0.0484 0.0797  3   VAL   B CA  
3825 C C   A VAL   B 3   ? 0.2078 0.2432 0.2632 -0.0674 -0.0772 0.1174  3   VAL   B C   
3826 C C   B VAL   B 3   ? 0.2245 0.2552 0.2391 -0.0429 -0.0556 0.0833  3   VAL   B C   
3827 O O   A VAL   B 3   ? 0.2081 0.2478 0.2781 -0.0673 -0.0782 0.1229  3   VAL   B O   
3828 O O   B VAL   B 3   ? 0.2229 0.2598 0.2314 -0.0311 -0.0556 0.0826  3   VAL   B O   
3829 C CB  A VAL   B 3   ? 0.2416 0.2465 0.3580 -0.0756 -0.0773 0.1191  3   VAL   B CB  
3830 C CB  B VAL   B 3   ? 0.2562 0.2731 0.2806 -0.0408 -0.0433 0.0726  3   VAL   B CB  
3831 C CG1 A VAL   B 3   ? 0.2453 0.2349 0.3829 -0.0805 -0.0764 0.1087  3   VAL   B CG1 
3832 C CG1 B VAL   B 3   ? 0.2578 0.2706 0.2886 -0.0419 -0.0421 0.0672  3   VAL   B CG1 
3833 C CG2 A VAL   B 3   ? 0.2466 0.2513 0.3763 -0.0731 -0.0669 0.1217  3   VAL   B CG2 
3834 C CG2 B VAL   B 3   ? 0.2585 0.2729 0.2831 -0.0397 -0.0401 0.0752  3   VAL   B CG2 
3853 N N   . ASN   B 4   ? 0.2018 0.2279 0.2283 -0.0531 -0.0652 0.0917  4   ASN   B N   
3854 C CA  . ASN   B 4   ? 0.1991 0.2199 0.1935 -0.0571 -0.0521 0.0484  4   ASN   B CA  
3855 C C   . ASN   B 4   ? 0.2066 0.2330 0.1905 -0.0580 -0.0383 0.0369  4   ASN   B C   
3856 O O   . ASN   B 4   ? 0.2095 0.2359 0.2166 -0.0549 -0.0337 0.0149  4   ASN   B O   
3857 C CB  . ASN   B 4   ? 0.1949 0.2122 0.1844 -0.0525 -0.0582 0.0388  4   ASN   B CB  
3858 C CG  . ASN   B 4   ? 0.1924 0.1936 0.1763 -0.0446 -0.0563 0.0337  4   ASN   B CG  
3859 O OD1 . ASN   B 4   ? 0.1982 0.1796 0.1749 -0.0463 -0.0551 0.0304  4   ASN   B OD1 
3860 N ND2 . ASN   B 4   ? 0.2121 0.1985 0.1956 -0.0221 -0.0419 0.0266  4   ASN   B ND2 
3868 N N   . SER   B 5   ? 0.2219 0.2484 0.1970 -0.0600 -0.0245 0.0348  5   SER   B N   
3869 C CA  . SER   B 5   ? 0.2508 0.2776 0.2394 -0.0500 0.0055  0.0402  5   SER   B CA  
3870 C C   . SER   B 5   ? 0.2680 0.2806 0.2668 -0.0651 0.0319  0.0433  5   SER   B C   
3871 O O   . SER   B 5   ? 0.2838 0.2810 0.3170 -0.0569 0.0592  0.0407  5   SER   B O   
3872 C CB  . SER   B 5   ? 0.2601 0.3000 0.2755 -0.0396 0.0082  0.0462  5   SER   B CB  
3873 O OG  . SER   B 5   ? 0.2846 0.3283 0.3298 -0.0220 0.0067  0.0512  5   SER   B OG  
3879 N N   . PHE   B 6   ? 0.2826 0.2960 0.2391 -0.0685 0.0383  0.0454  6   PHE   B N   
3880 C CA  . PHE   B 6   ? 0.2895 0.2983 0.2021 -0.0811 0.0392  0.0280  6   PHE   B CA  
3881 C C   . PHE   B 6   ? 0.3358 0.3224 0.2458 -0.0802 0.0517  -0.0007 6   PHE   B C   
3882 O O   . PHE   B 6   ? 0.3496 0.3501 0.2743 -0.0713 0.0349  -0.0165 6   PHE   B O   
3883 C CB  . PHE   B 6   ? 0.2603 0.2780 0.1818 -0.0774 0.0072  0.0221  6   PHE   B CB  
3884 C CG  . PHE   B 6   ? 0.2291 0.2480 0.1738 -0.0709 -0.0055 0.0132  6   PHE   B CG  
3885 C CD1 . PHE   B 6   ? 0.2266 0.2207 0.1652 -0.0650 -0.0233 0.0130  6   PHE   B CD1 
3886 C CD2 . PHE   B 6   ? 0.2077 0.2446 0.1799 -0.0582 0.0040  0.0314  6   PHE   B CD2 
3887 C CE1 . PHE   B 6   ? 0.2242 0.1995 0.1684 -0.0502 -0.0206 0.0042  6   PHE   B CE1 
3888 C CE2 . PHE   B 6   ? 0.2107 0.2263 0.2028 -0.0425 0.0083  0.0321  6   PHE   B CE2 
3889 C CZ  . PHE   B 6   ? 0.2132 0.2037 0.1885 -0.0458 -0.0023 0.0116  6   PHE   B CZ  
3899 N N   . SER   B 7   ? 0.3664 0.3071 0.2510 -0.0985 0.0736  -0.0277 7   SER   B N   
3900 C CA  . SER   B 7   ? 0.3939 0.3149 0.2949 -0.0986 0.0915  -0.0346 7   SER   B CA  
3901 C C   . SER   B 7   ? 0.3906 0.2963 0.2827 -0.0974 0.1109  -0.0472 7   SER   B C   
3902 O O   . SER   B 7   ? 0.4024 0.2980 0.3076 -0.1013 0.1148  -0.0390 7   SER   B O   
3903 C CB  . SER   B 7   ? 0.4152 0.3300 0.3534 -0.0942 0.1020  -0.0291 7   SER   B CB  
3904 O OG  . SER   B 7   ? 0.4305 0.3442 0.4049 -0.0915 0.1038  -0.0269 7   SER   B OG  
3910 N N   A GLY   B 8   ? 0.3876 0.2872 0.2833 -0.0857 0.1138  -0.0606 8   GLY   B N   
3911 N N   B GLY   B 8   ? 0.3846 0.2861 0.2801 -0.0891 0.1097  -0.0549 8   GLY   B N   
3912 C CA  A GLY   B 8   ? 0.3783 0.2720 0.2844 -0.0817 0.1179  -0.0662 8   GLY   B CA  
3913 C CA  B GLY   B 8   ? 0.3759 0.2732 0.2778 -0.0846 0.1078  -0.0580 8   GLY   B CA  
3914 C C   A GLY   B 8   ? 0.3686 0.2548 0.2794 -0.0820 0.1199  -0.0567 8   GLY   B C   
3915 C C   B GLY   B 8   ? 0.3673 0.2590 0.2729 -0.0817 0.1068  -0.0560 8   GLY   B C   
3916 O O   A GLY   B 8   ? 0.3778 0.2558 0.3069 -0.0745 0.1227  -0.0612 8   GLY   B O   
3917 O O   B GLY   B 8   ? 0.3723 0.2623 0.2846 -0.0768 0.1060  -0.0581 8   GLY   B O   
3924 N N   . TYR   B 9   ? 0.3572 0.2446 0.2556 -0.0766 0.1004  -0.0582 9   TYR   B N   
3925 C CA  . TYR   B 9   ? 0.3315 0.2132 0.2284 -0.0609 0.0728  -0.0467 9   TYR   B CA  
3926 C C   . TYR   B 9   ? 0.3198 0.2140 0.2159 -0.0535 0.0363  -0.0286 9   TYR   B C   
3927 O O   . TYR   B 9   ? 0.3309 0.2361 0.2471 -0.0534 0.0313  -0.0179 9   TYR   B O   
3928 C CB  . TYR   B 9   ? 0.3269 0.1956 0.2309 -0.0546 0.0669  -0.0336 9   TYR   B CB  
3929 C CG  . TYR   B 9   ? 0.3172 0.1785 0.2310 -0.0618 0.0619  -0.0327 9   TYR   B CG  
3930 C CD1 . TYR   B 9   ? 0.3190 0.1790 0.2455 -0.0734 0.0644  -0.0366 9   TYR   B CD1 
3931 C CD2 . TYR   B 9   ? 0.3020 0.1740 0.2237 -0.0568 0.0562  -0.0369 9   TYR   B CD2 
3932 C CE1 . TYR   B 9   ? 0.3113 0.1853 0.2529 -0.0802 0.0709  -0.0489 9   TYR   B CE1 
3933 C CE2 . TYR   B 9   ? 0.3015 0.1730 0.2329 -0.0575 0.0558  -0.0364 9   TYR   B CE2 
3934 C CZ  . TYR   B 9   ? 0.3034 0.1847 0.2538 -0.0716 0.0624  -0.0577 9   TYR   B CZ  
3935 O OH  . TYR   B 9   ? 0.2965 0.1987 0.2696 -0.0818 0.0617  -0.0719 9   TYR   B OH  
3946 N N   . LEU   B 10  ? 0.2977 0.1893 0.1882 -0.0495 0.0181  -0.0270 10  LEU   B N   
3947 C CA  . LEU   B 10  ? 0.2929 0.1869 0.1921 -0.0613 -0.0107 -0.0296 10  LEU   B CA  
3948 C C   . LEU   B 10  ? 0.2752 0.1878 0.1942 -0.0604 -0.0262 -0.0297 10  LEU   B C   
3949 O O   . LEU   B 10  ? 0.2614 0.1911 0.1939 -0.0439 -0.0178 -0.0298 10  LEU   B O   
3950 C CB  . LEU   B 10  ? 0.3079 0.1866 0.2124 -0.0636 -0.0284 -0.0174 10  LEU   B CB  
3951 C CG  . LEU   B 10  ? 0.3222 0.1938 0.2543 -0.0557 -0.0552 -0.0101 10  LEU   B CG  
3952 C CD1 . LEU   B 10  ? 0.3331 0.2070 0.2762 -0.0510 -0.0524 -0.0089 10  LEU   B CD1 
3953 C CD2 . LEU   B 10  ? 0.3308 0.2003 0.2796 -0.0557 -0.0507 0.0087  10  LEU   B CD2 
3965 N N   . LYS   B 11  ? 0.2861 0.2076 0.1979 -0.0549 -0.0306 -0.0195 11  LYS   B N   
3966 C CA  . LYS   B 11  ? 0.3023 0.2383 0.2240 -0.0431 -0.0461 -0.0233 11  LYS   B CA  
3967 C C   . LYS   B 11  ? 0.2846 0.2244 0.2313 -0.0620 -0.0494 -0.0352 11  LYS   B C   
3968 O O   . LYS   B 11  ? 0.2980 0.2416 0.2638 -0.0773 -0.0490 -0.0661 11  LYS   B O   
3969 C CB  . LYS   B 11  ? 0.3351 0.2871 0.2833 -0.0178 -0.0506 -0.0156 11  LYS   B CB  
3970 C CG  . LYS   B 11  ? 0.3645 0.3180 0.3527 -0.0029 -0.0550 -0.0181 11  LYS   B CG  
3971 C CD  . LYS   B 11  ? 0.3878 0.3425 0.4122 0.0072  -0.0571 -0.0251 11  LYS   B CD  
3972 C CE  . LYS   B 11  ? 0.4036 0.3604 0.4584 0.0116  -0.0542 -0.0283 11  LYS   B CE  
3973 N NZ  . LYS   B 11  ? 0.4147 0.3723 0.4868 0.0139  -0.0486 -0.0265 11  LYS   B NZ  
3987 N N   . LEU   B 12  ? 0.2540 0.2031 0.2326 -0.0547 -0.0423 -0.0422 12  LEU   B N   
3988 C CA  . LEU   B 12  ? 0.2396 0.1840 0.2471 -0.0519 -0.0324 -0.0340 12  LEU   B CA  
3989 C C   . LEU   B 12  ? 0.2291 0.1844 0.2585 -0.0514 -0.0461 -0.0312 12  LEU   B C   
3990 O O   . LEU   B 12  ? 0.2266 0.1868 0.2775 -0.0602 -0.0623 -0.0232 12  LEU   B O   
3991 C CB  . LEU   B 12  ? 0.2389 0.1627 0.2473 -0.0395 -0.0188 -0.0360 12  LEU   B CB  
3992 C CG  . LEU   B 12  ? 0.2409 0.1614 0.2535 -0.0382 -0.0131 -0.0260 12  LEU   B CG  
3993 C CD1 . LEU   B 12  ? 0.2486 0.1569 0.2516 -0.0261 -0.0114 -0.0148 12  LEU   B CD1 
3994 C CD2 . LEU   B 12  ? 0.2469 0.1690 0.2637 -0.0395 -0.0170 -0.0349 12  LEU   B CD2 
4006 N N   . THR   B 13  ? 0.2196 0.1881 0.2581 -0.0498 -0.0507 -0.0403 13  THR   B N   
4007 C CA  . THR   B 13  ? 0.2154 0.1952 0.2562 -0.0558 -0.0609 -0.0263 13  THR   B CA  
4008 C C   . THR   B 13  ? 0.2548 0.2094 0.2703 -0.0630 -0.0798 -0.0230 13  THR   B C   
4009 O O   . THR   B 13  ? 0.2710 0.2094 0.2936 -0.0645 -0.0441 -0.0199 13  THR   B O   
4010 C CB  . THR   B 13  ? 0.2005 0.1958 0.2623 -0.0511 -0.0560 -0.0201 13  THR   B CB  
4011 O OG1 . THR   B 13  ? 0.1916 0.1908 0.2660 -0.0431 -0.0432 -0.0236 13  THR   B OG1 
4012 C CG2 . THR   B 13  ? 0.2140 0.2032 0.2649 -0.0413 -0.0452 -0.0120 13  THR   B CG2 
4020 N N   A ASP   B 14  ? 0.2719 0.2189 0.2850 -0.0627 -0.1117 -0.0095 14  ASP   B N   
4021 N N   B ASP   B 14  ? 0.2655 0.2164 0.2833 -0.0596 -0.0874 -0.0108 14  ASP   B N   
4022 C CA  A ASP   B 14  ? 0.2825 0.2367 0.3175 -0.0603 -0.1115 0.0138  14  ASP   B CA  
4023 C CA  B ASP   B 14  ? 0.2695 0.2251 0.3002 -0.0563 -0.0848 0.0043  14  ASP   B CA  
4024 C C   A ASP   B 14  ? 0.2670 0.2210 0.2774 -0.0645 -0.0903 0.0195  14  ASP   B C   
4025 C C   B ASP   B 14  ? 0.2541 0.2103 0.2696 -0.0561 -0.0830 0.0105  14  ASP   B C   
4026 O O   A ASP   B 14  ? 0.2903 0.2389 0.2833 -0.0676 -0.0860 0.0292  14  ASP   B O   
4027 O O   B ASP   B 14  ? 0.2630 0.2130 0.2711 -0.0551 -0.0861 0.0098  14  ASP   B O   
4028 C CB  A ASP   B 14  ? 0.3036 0.2691 0.3903 -0.0543 -0.1224 0.0181  14  ASP   B CB  
4029 C CB  B ASP   B 14  ? 0.2851 0.2465 0.3460 -0.0523 -0.0807 0.0067  14  ASP   B CB  
4030 C CG  A ASP   B 14  ? 0.3271 0.2983 0.4644 -0.0479 -0.1192 0.0123  14  ASP   B CG  
4031 C CG  B ASP   B 14  ? 0.3002 0.2645 0.3875 -0.0475 -0.0724 0.0043  14  ASP   B CG  
4032 O OD1 A ASP   B 14  ? 0.3427 0.3110 0.4862 -0.0484 -0.1149 0.0037  14  ASP   B OD1 
4033 O OD1 B ASP   B 14  ? 0.3045 0.2716 0.3995 -0.0462 -0.0664 0.0018  14  ASP   B OD1 
4034 O OD2 A ASP   B 14  ? 0.3303 0.3105 0.4982 -0.0471 -0.1168 0.0164  14  ASP   B OD2 
4035 O OD2 B ASP   B 14  ? 0.3061 0.2716 0.4046 -0.0488 -0.0713 0.0064  14  ASP   B OD2 
4044 N N   . ASN   B 15  ? 0.2314 0.1934 0.2441 -0.0502 -0.0839 0.0148  15  ASN   B N   
4045 C CA  . ASN   B 15  ? 0.1912 0.1735 0.2319 -0.0343 -0.0581 0.0053  15  ASN   B CA  
4046 C C   . ASN   B 15  ? 0.1753 0.1596 0.2135 -0.0220 -0.0484 -0.0018 15  ASN   B C   
4047 O O   . ASN   B 15  ? 0.1729 0.1514 0.2351 -0.0212 -0.0532 -0.0134 15  ASN   B O   
4048 C CB  . ASN   B 15  ? 0.1821 0.1697 0.2446 -0.0181 -0.0591 0.0062  15  ASN   B CB  
4049 C CG  . ASN   B 15  ? 0.1720 0.1681 0.2540 -0.0227 -0.0386 0.0107  15  ASN   B CG  
4050 O OD1 . ASN   B 15  ? 0.1794 0.1961 0.2698 -0.0412 -0.0404 0.0149  15  ASN   B OD1 
4051 N ND2 . ASN   B 15  ? 0.1717 0.1461 0.2400 -0.0156 -0.0163 -0.0024 15  ASN   B ND2 
4059 N N   . VAL   B 16  ? 0.1820 0.1496 0.2082 -0.0283 -0.0531 -0.0007 16  VAL   B N   
4060 C CA  . VAL   B 16  ? 0.1813 0.1498 0.2016 -0.0325 -0.0438 -0.0201 16  VAL   B CA  
4061 C C   . VAL   B 16  ? 0.1785 0.1590 0.1964 -0.0372 -0.0459 -0.0133 16  VAL   B C   
4062 O O   . VAL   B 16  ? 0.1846 0.1721 0.2175 -0.0298 -0.0358 -0.0280 16  VAL   B O   
4063 C CB  . VAL   B 16  ? 0.1870 0.1503 0.2245 -0.0161 -0.0328 -0.0109 16  VAL   B CB  
4064 C CG1 . VAL   B 16  ? 0.1992 0.1485 0.2181 0.0008  -0.0287 -0.0031 16  VAL   B CG1 
4065 C CG2 . VAL   B 16  ? 0.1860 0.1570 0.2388 -0.0094 -0.0281 -0.0121 16  VAL   B CG2 
4075 N N   . TYR   B 17  ? 0.1838 0.1654 0.1976 -0.0296 -0.0403 -0.0158 17  TYR   B N   
4076 C CA  . TYR   B 17  ? 0.1946 0.1767 0.1901 -0.0364 -0.0410 -0.0009 17  TYR   B CA  
4077 C C   . TYR   B 17  ? 0.1842 0.1538 0.1909 -0.0400 -0.0304 -0.0047 17  TYR   B C   
4078 O O   . TYR   B 17  ? 0.1784 0.1594 0.2110 -0.0291 -0.0366 -0.0255 17  TYR   B O   
4079 C CB  . TYR   B 17  ? 0.2260 0.2151 0.2120 -0.0253 -0.0337 0.0360  17  TYR   B CB  
4080 C CG  . TYR   B 17  ? 0.2563 0.2641 0.2495 -0.0184 -0.0416 0.0384  17  TYR   B CG  
4081 C CD1 . TYR   B 17  ? 0.2720 0.2775 0.2636 -0.0142 -0.0478 0.0504  17  TYR   B CD1 
4082 C CD2 . TYR   B 17  ? 0.2769 0.2965 0.2723 -0.0083 -0.0457 0.0327  17  TYR   B CD2 
4083 C CE1 . TYR   B 17  ? 0.2877 0.3018 0.2814 -0.0064 -0.0604 0.0460  17  TYR   B CE1 
4084 C CE2 . TYR   B 17  ? 0.2907 0.3143 0.2889 0.0020  -0.0633 0.0380  17  TYR   B CE2 
4085 C CZ  . TYR   B 17  ? 0.2988 0.3164 0.2889 0.0040  -0.0725 0.0464  17  TYR   B CZ  
4086 O OH  . TYR   B 17  ? 0.3122 0.3347 0.3110 0.0126  -0.0847 0.0491  17  TYR   B OH  
4096 N N   . ILE   B 18  ? 0.1993 0.1557 0.1687 -0.0340 -0.0137 -0.0128 18  ILE   B N   
4097 C CA  . ILE   B 18  ? 0.2060 0.1525 0.1689 -0.0335 -0.0131 -0.0126 18  ILE   B CA  
4098 C C   . ILE   B 18  ? 0.2129 0.1562 0.1682 -0.0421 -0.0080 -0.0271 18  ILE   B C   
4099 O O   . ILE   B 18  ? 0.2291 0.1720 0.1840 -0.0354 -0.0001 -0.0327 18  ILE   B O   
4100 C CB  . ILE   B 18  ? 0.2081 0.1527 0.1855 -0.0388 -0.0181 -0.0109 18  ILE   B CB  
4101 C CG1 . ILE   B 18  ? 0.2003 0.1580 0.1898 -0.0394 -0.0079 0.0004  18  ILE   B CG1 
4102 C CG2 . ILE   B 18  ? 0.2112 0.1576 0.1957 -0.0441 -0.0167 -0.0083 18  ILE   B CG2 
4103 C CD1 . ILE   B 18  ? 0.2027 0.1874 0.2108 -0.0332 -0.0280 0.0201  18  ILE   B CD1 
4115 N N   . LYS   B 19  ? 0.2133 0.1609 0.1856 -0.0281 0.0200  -0.0311 19  LYS   B N   
4116 C CA  . LYS   B 19  ? 0.2206 0.1618 0.2022 -0.0290 0.0277  -0.0338 19  LYS   B CA  
4117 C C   . LYS   B 19  ? 0.2053 0.1603 0.2086 -0.0273 0.0270  -0.0448 19  LYS   B C   
4118 O O   . LYS   B 19  ? 0.1954 0.1632 0.2041 -0.0142 0.0167  -0.0403 19  LYS   B O   
4119 C CB  . LYS   B 19  ? 0.2436 0.1790 0.2104 -0.0313 0.0391  -0.0242 19  LYS   B CB  
4120 C CG  . LYS   B 19  ? 0.2668 0.2002 0.2252 -0.0392 0.0416  -0.0337 19  LYS   B CG  
4121 C CD  . LYS   B 19  ? 0.2937 0.2305 0.2443 -0.0463 0.0451  -0.0250 19  LYS   B CD  
4122 C CE  . LYS   B 19  ? 0.3169 0.2578 0.2586 -0.0460 0.0477  -0.0229 19  LYS   B CE  
4123 N NZ  . LYS   B 19  ? 0.3315 0.2742 0.2727 -0.0519 0.0512  -0.0181 19  LYS   B NZ  
4137 N N   . ASN   B 20  ? 0.2057 0.1730 0.2415 -0.0194 0.0337  -0.0503 20  ASN   B N   
4138 C CA  . ASN   B 20  ? 0.2036 0.1859 0.2687 -0.0118 0.0370  -0.0617 20  ASN   B CA  
4139 C C   . ASN   B 20  ? 0.1981 0.2041 0.2681 -0.0177 0.0472  -0.0715 20  ASN   B C   
4140 O O   . ASN   B 20  ? 0.2160 0.2370 0.2917 -0.0326 0.0494  -0.0722 20  ASN   B O   
4141 C CB  . ASN   B 20  ? 0.2240 0.1878 0.2969 0.0064  0.0289  -0.0641 20  ASN   B CB  
4142 C CG  . ASN   B 20  ? 0.2466 0.1938 0.3211 0.0333  0.0266  -0.0716 20  ASN   B CG  
4143 O OD1 . ASN   B 20  ? 0.2746 0.2212 0.3484 0.0488  0.0274  -0.0727 20  ASN   B OD1 
4144 N ND2 . ASN   B 20  ? 0.2351 0.1978 0.3182 0.0349  0.0180  -0.0726 20  ASN   B ND2 
4151 N N   . ALA   B 21  ? 0.1994 0.1873 0.2661 -0.0274 0.0429  -0.0573 21  ALA   B N   
4152 C CA  . ALA   B 21  ? 0.2066 0.1968 0.2789 -0.0313 0.0380  -0.0432 21  ALA   B CA  
4153 C C   . ALA   B 21  ? 0.2052 0.1731 0.2711 -0.0252 0.0376  -0.0321 21  ALA   B C   
4154 O O   . ALA   B 21  ? 0.2086 0.1602 0.2753 -0.0345 0.0311  -0.0264 21  ALA   B O   
4155 C CB  . ALA   B 21  ? 0.2190 0.2206 0.2885 -0.0459 0.0354  -0.0244 21  ALA   B CB  
4161 N N   . ASP   B 22  ? 0.1963 0.1665 0.2606 -0.0210 0.0276  -0.0222 22  ASP   B N   
4162 C CA  . ASP   B 22  ? 0.1934 0.1603 0.2487 -0.0092 0.0222  -0.0176 22  ASP   B CA  
4163 C C   . ASP   B 22  ? 0.1824 0.1561 0.2132 -0.0150 0.0160  -0.0091 22  ASP   B C   
4164 O O   . ASP   B 22  ? 0.1876 0.1535 0.2137 -0.0100 0.0050  -0.0054 22  ASP   B O   
4165 C CB  . ASP   B 22  ? 0.2004 0.1652 0.2892 -0.0059 0.0251  -0.0040 22  ASP   B CB  
4166 C CG  . ASP   B 22  ? 0.2030 0.1873 0.3281 -0.0011 -0.0026 -0.0086 22  ASP   B CG  
4167 O OD1 . ASP   B 22  ? 0.2176 0.1833 0.3250 0.0050  -0.0235 -0.0150 22  ASP   B OD1 
4168 O OD2 . ASP   B 22  ? 0.2092 0.2175 0.3739 0.0079  -0.0239 -0.0193 22  ASP   B OD2 
4173 N N   . ILE   B 23  ? 0.1862 0.1495 0.1936 -0.0114 0.0076  0.0147  23  ILE   B N   
4174 C CA  . ILE   B 23  ? 0.1759 0.1482 0.1722 -0.0091 -0.0004 0.0055  23  ILE   B CA  
4175 C C   . ILE   B 23  ? 0.1686 0.1497 0.1736 -0.0055 -0.0108 0.0001  23  ILE   B C   
4176 O O   . ILE   B 23  ? 0.1632 0.1470 0.1663 -0.0079 -0.0070 0.0023  23  ILE   B O   
4177 C CB  . ILE   B 23  ? 0.1723 0.1536 0.1863 -0.0180 -0.0012 0.0191  23  ILE   B CB  
4178 C CG1 . ILE   B 23  ? 0.1758 0.1616 0.2090 -0.0151 0.0008  0.0233  23  ILE   B CG1 
4179 C CG2 . ILE   B 23  ? 0.1824 0.1776 0.1962 -0.0188 0.0025  0.0084  23  ILE   B CG2 
4180 C CD1 . ILE   B 23  ? 0.1820 0.1733 0.2182 -0.0121 0.0021  0.0184  23  ILE   B CD1 
4192 N N   . VAL   B 24  ? 0.1700 0.1476 0.1868 -0.0079 -0.0094 0.0016  24  VAL   B N   
4193 C CA  . VAL   B 24  ? 0.1637 0.1532 0.2089 -0.0054 -0.0167 -0.0007 24  VAL   B CA  
4194 C C   . VAL   B 24  ? 0.1641 0.1538 0.2218 -0.0121 -0.0110 0.0061  24  VAL   B C   
4195 O O   . VAL   B 24  ? 0.1638 0.1620 0.2305 -0.0163 -0.0088 0.0166  24  VAL   B O   
4196 C CB  . VAL   B 24  ? 0.1739 0.1697 0.2212 0.0032  -0.0269 -0.0022 24  VAL   B CB  
4197 C CG1 . VAL   B 24  ? 0.1741 0.1749 0.2457 -0.0031 -0.0260 -0.0078 24  VAL   B CG1 
4198 C CG2 . VAL   B 24  ? 0.1842 0.1987 0.2270 0.0077  -0.0277 -0.0082 24  VAL   B CG2 
4208 N N   . GLU   B 25  ? 0.1874 0.1633 0.2243 -0.0117 -0.0047 0.0095  25  GLU   B N   
4209 C CA  . GLU   B 25  ? 0.1982 0.1950 0.2401 0.0002  0.0069  0.0026  25  GLU   B CA  
4210 C C   . GLU   B 25  ? 0.1941 0.1821 0.2105 -0.0059 0.0082  0.0068  25  GLU   B C   
4211 O O   . GLU   B 25  ? 0.1986 0.1954 0.2234 -0.0097 0.0157  0.0132  25  GLU   B O   
4212 C CB  . GLU   B 25  ? 0.2282 0.2419 0.3104 0.0231  0.0203  -0.0009 25  GLU   B CB  
4213 C CG  . GLU   B 25  ? 0.2663 0.2961 0.4114 0.0309  0.0185  -0.0095 25  GLU   B CG  
4214 C CD  . GLU   B 25  ? 0.3168 0.3412 0.4914 0.0215  0.0169  -0.0153 25  GLU   B CD  
4215 O OE1 . GLU   B 25  ? 0.3245 0.3637 0.5265 0.0215  0.0235  -0.0148 25  GLU   B OE1 
4216 O OE2 . GLU   B 25  ? 0.3167 0.3577 0.5273 0.0176  0.0118  -0.0222 25  GLU   B OE2 
4223 N N   . GLU   B 26  ? 0.1901 0.1777 0.1874 -0.0252 0.0071  0.0057  26  GLU   B N   
4224 C CA  . GLU   B 26  ? 0.1883 0.1888 0.1915 -0.0329 -0.0009 0.0037  26  GLU   B CA  
4225 C C   . GLU   B 26  ? 0.1743 0.1852 0.1784 -0.0248 0.0014  0.0184  26  GLU   B C   
4226 O O   . GLU   B 26  ? 0.1960 0.2048 0.1858 -0.0226 -0.0024 0.0302  26  GLU   B O   
4227 C CB  . GLU   B 26  ? 0.2185 0.2121 0.2102 -0.0456 0.0021  0.0123  26  GLU   B CB  
4228 C CG  . GLU   B 26  ? 0.2649 0.2500 0.2557 -0.0490 0.0103  -0.0081 26  GLU   B CG  
4229 C CD  . GLU   B 26  ? 0.2916 0.2725 0.2714 -0.0691 0.0242  -0.0354 26  GLU   B CD  
4230 O OE1 . GLU   B 26  ? 0.3148 0.2601 0.2787 -0.0815 0.0565  -0.0302 26  GLU   B OE1 
4231 O OE2 . GLU   B 26  ? 0.2890 0.3088 0.3122 -0.0603 0.0192  -0.0267 26  GLU   B OE2 
4238 N N   . ALA   B 27  ? 0.1600 0.1721 0.1874 -0.0223 0.0041  0.0201  27  ALA   B N   
4239 C CA  . ALA   B 27  ? 0.1642 0.1693 0.2015 -0.0127 0.0004  0.0301  27  ALA   B CA  
4240 C C   . ALA   B 27  ? 0.1664 0.1779 0.2189 -0.0118 0.0103  0.0378  27  ALA   B C   
4241 O O   . ALA   B 27  ? 0.1773 0.1832 0.2409 -0.0020 0.0082  0.0454  27  ALA   B O   
4242 C CB  . ALA   B 27  ? 0.1842 0.1495 0.2037 -0.0206 0.0036  0.0286  27  ALA   B CB  
4248 N N   . LYS   B 28  ? 0.1620 0.1937 0.2614 -0.0162 0.0198  0.0569  28  LYS   B N   
4249 C CA  . LYS   B 28  ? 0.1790 0.2257 0.2870 -0.0097 0.0479  0.0826  28  LYS   B CA  
4250 C C   . LYS   B 28  ? 0.2039 0.2411 0.2816 -0.0005 0.0581  0.0748  28  LYS   B C   
4251 O O   . LYS   B 28  ? 0.2293 0.2459 0.2987 -0.0056 0.0628  0.0736  28  LYS   B O   
4252 C CB  . LYS   B 28  ? 0.1999 0.2564 0.3255 -0.0007 0.0635  0.0984  28  LYS   B CB  
4253 C CG  . LYS   B 28  ? 0.2211 0.3024 0.3725 0.0073  0.0616  0.1044  28  LYS   B CG  
4254 C CD  . LYS   B 28  ? 0.2550 0.3502 0.4233 0.0154  0.0776  0.1002  28  LYS   B CD  
4255 C CE  . LYS   B 28  ? 0.2802 0.3774 0.4622 0.0252  0.0836  0.1000  28  LYS   B CE  
4256 N NZ  . LYS   B 28  ? 0.3131 0.4043 0.4887 0.0354  0.0844  0.1051  28  LYS   B NZ  
4270 N N   . LYS   B 29  ? 0.2211 0.2633 0.2847 0.0172  0.0619  0.0609  29  LYS   B N   
4271 C CA  . LYS   B 29  ? 0.2634 0.2939 0.3050 0.0180  0.0637  0.0577  29  LYS   B CA  
4272 C C   . LYS   B 29  ? 0.2569 0.2976 0.2665 0.0169  0.0502  0.0708  29  LYS   B C   
4273 O O   . LYS   B 29  ? 0.2745 0.3208 0.2799 0.0190  0.0414  0.0732  29  LYS   B O   
4274 C CB  . LYS   B 29  ? 0.3176 0.3281 0.3843 0.0155  0.0664  0.0433  29  LYS   B CB  
4275 C CG  . LYS   B 29  ? 0.3632 0.3580 0.4638 0.0102  0.0705  0.0363  29  LYS   B CG  
4276 C CD  . LYS   B 29  ? 0.3953 0.3789 0.5313 0.0038  0.0794  0.0267  29  LYS   B CD  
4277 C CE  . LYS   B 29  ? 0.4136 0.3898 0.5785 -0.0006 0.0887  0.0198  29  LYS   B CE  
4278 N NZ  . LYS   B 29  ? 0.4209 0.3985 0.6035 -0.0010 0.0927  0.0162  29  LYS   B NZ  
4292 N N   . VAL   B 30  ? 0.2275 0.2804 0.2492 0.0057  0.0420  0.0721  30  VAL   B N   
4293 C CA  . VAL   B 30  ? 0.2151 0.2713 0.2839 -0.0053 0.0069  0.0761  30  VAL   B CA  
4294 C C   . VAL   B 30  ? 0.1938 0.2673 0.2719 -0.0039 0.0140  0.0922  30  VAL   B C   
4295 O O   . VAL   B 30  ? 0.2088 0.2866 0.2642 0.0028  0.0236  0.1020  30  VAL   B O   
4296 C CB  . VAL   B 30  ? 0.2226 0.2662 0.3199 -0.0218 -0.0246 0.0697  30  VAL   B CB  
4297 C CG1 . VAL   B 30  ? 0.2247 0.2733 0.3206 -0.0248 -0.0259 0.0672  30  VAL   B CG1 
4298 C CG2 . VAL   B 30  ? 0.2348 0.2652 0.3343 -0.0307 -0.0367 0.0566  30  VAL   B CG2 
4308 N N   . LYS   B 31  ? 0.1804 0.2341 0.3013 -0.0146 0.0098  0.1015  31  LYS   B N   
4309 C CA  . LYS   B 31  ? 0.1710 0.2248 0.3325 -0.0287 -0.0068 0.1023  31  LYS   B CA  
4310 C C   . LYS   B 31  ? 0.1670 0.1894 0.2928 -0.0280 -0.0277 0.0827  31  LYS   B C   
4311 O O   . LYS   B 31  ? 0.1739 0.2053 0.3143 -0.0247 -0.0224 0.0955  31  LYS   B O   
4312 C CB  . LYS   B 31  ? 0.1852 0.2757 0.3871 -0.0266 0.0166  0.1138  31  LYS   B CB  
4313 C CG  . LYS   B 31  ? 0.2199 0.3242 0.4350 -0.0248 0.0324  0.1104  31  LYS   B CG  
4314 C CD  . LYS   B 31  ? 0.2488 0.3632 0.4727 -0.0166 0.0309  0.1029  31  LYS   B CD  
4315 C CE  . LYS   B 31  ? 0.2616 0.3892 0.5064 -0.0102 0.0196  0.0926  31  LYS   B CE  
4316 N NZ  . LYS   B 31  ? 0.2749 0.4121 0.5258 -0.0002 0.0046  0.0795  31  LYS   B NZ  
4330 N N   . PRO   B 32  ? 0.1741 0.1607 0.2289 -0.0312 -0.0414 0.0482  32  PRO   B N   
4331 C CA  . PRO   B 32  ? 0.1828 0.1600 0.1869 -0.0317 -0.0425 0.0355  32  PRO   B CA  
4332 C C   . PRO   B 32  ? 0.1945 0.1489 0.1905 -0.0310 -0.0548 0.0348  32  PRO   B C   
4333 O O   . PRO   B 32  ? 0.2078 0.1475 0.2247 -0.0396 -0.0739 0.0339  32  PRO   B O   
4334 C CB  . PRO   B 32  ? 0.1943 0.1482 0.1882 -0.0316 -0.0342 0.0193  32  PRO   B CB  
4335 C CG  . PRO   B 32  ? 0.2101 0.1402 0.1861 -0.0275 -0.0494 0.0225  32  PRO   B CG  
4336 C CD  . PRO   B 32  ? 0.1973 0.1478 0.2054 -0.0230 -0.0555 0.0282  32  PRO   B CD  
4344 N N   . THR   B 33  ? 0.1992 0.1378 0.1666 -0.0300 -0.0505 0.0218  33  THR   B N   
4345 C CA  . THR   B 33  ? 0.2024 0.1475 0.1612 -0.0341 -0.0502 0.0274  33  THR   B CA  
4346 C C   . THR   B 33  ? 0.2054 0.1375 0.1584 -0.0268 -0.0468 0.0154  33  THR   B C   
4347 O O   . THR   B 33  ? 0.2284 0.1398 0.1666 -0.0371 -0.0532 0.0120  33  THR   B O   
4348 C CB  . THR   B 33  ? 0.2127 0.1583 0.1797 -0.0166 -0.0567 0.0338  33  THR   B CB  
4349 O OG1 . THR   B 33  ? 0.2037 0.1651 0.1796 -0.0234 -0.0516 0.0373  33  THR   B OG1 
4350 C CG2 . THR   B 33  ? 0.2358 0.1613 0.2013 -0.0049 -0.0587 0.0246  33  THR   B CG2 
4358 N N   . VAL   B 34  ? 0.1909 0.1350 0.1469 -0.0324 -0.0438 0.0114  34  VAL   B N   
4359 C CA  . VAL   B 34  ? 0.1752 0.1354 0.1509 -0.0265 -0.0385 0.0082  34  VAL   B CA  
4360 C C   . VAL   B 34  ? 0.1569 0.1314 0.1377 -0.0276 -0.0234 0.0061  34  VAL   B C   
4361 O O   . VAL   B 34  ? 0.1768 0.1340 0.1352 -0.0244 -0.0323 0.0107  34  VAL   B O   
4362 C CB  . VAL   B 34  ? 0.1815 0.1436 0.1814 -0.0080 -0.0323 0.0032  34  VAL   B CB  
4363 C CG1 . VAL   B 34  ? 0.1747 0.1567 0.1895 -0.0060 -0.0225 -0.0107 34  VAL   B CG1 
4364 C CG2 . VAL   B 34  ? 0.1869 0.1493 0.2011 -0.0077 -0.0256 0.0052  34  VAL   B CG2 
4374 N N   . VAL   B 35  ? 0.1523 0.1292 0.1288 -0.0263 -0.0162 0.0056  35  VAL   B N   
4375 C CA  . VAL   B 35  ? 0.1478 0.1242 0.1372 -0.0209 -0.0107 0.0045  35  VAL   B CA  
4376 C C   . VAL   B 35  ? 0.1356 0.1240 0.1401 -0.0144 -0.0130 0.0044  35  VAL   B C   
4377 O O   . VAL   B 35  ? 0.1411 0.1311 0.1252 -0.0200 -0.0045 -0.0044 35  VAL   B O   
4378 C CB  . VAL   B 35  ? 0.1467 0.1450 0.1489 -0.0172 -0.0000 0.0096  35  VAL   B CB  
4379 C CG1 . VAL   B 35  ? 0.1414 0.1574 0.1596 -0.0237 -0.0022 0.0048  35  VAL   B CG1 
4380 C CG2 . VAL   B 35  ? 0.1486 0.1494 0.1569 -0.0087 0.0006  0.0053  35  VAL   B CG2 
4390 N N   . VAL   B 36  ? 0.1436 0.1224 0.1340 -0.0188 -0.0143 0.0126  36  VAL   B N   
4391 C CA  . VAL   B 36  ? 0.1396 0.1215 0.1324 -0.0126 -0.0075 0.0067  36  VAL   B CA  
4392 C C   . VAL   B 36  ? 0.1315 0.1226 0.1239 -0.0136 -0.0047 0.0082  36  VAL   B C   
4393 O O   . VAL   B 36  ? 0.1419 0.1310 0.1384 -0.0102 -0.0008 -0.0042 36  VAL   B O   
4394 C CB  . VAL   B 36  ? 0.1362 0.1300 0.1381 -0.0143 -0.0068 0.0040  36  VAL   B CB  
4395 C CG1 . VAL   B 36  ? 0.1388 0.1436 0.1522 -0.0209 -0.0101 0.0012  36  VAL   B CG1 
4396 C CG2 . VAL   B 36  ? 0.1427 0.1327 0.1600 -0.0131 -0.0115 0.0157  36  VAL   B CG2 
4406 N N   . ASN   B 37  ? 0.1345 0.1313 0.1265 -0.0078 -0.0074 0.0077  37  ASN   B N   
4407 C CA  . ASN   B 37  ? 0.1344 0.1328 0.1436 -0.0030 -0.0172 0.0106  37  ASN   B CA  
4408 C C   . ASN   B 37  ? 0.1279 0.1323 0.1460 0.0033  -0.0101 0.0004  37  ASN   B C   
4409 O O   . ASN   B 37  ? 0.1416 0.1388 0.1366 -0.0042 -0.0057 0.0063  37  ASN   B O   
4410 C CB  . ASN   B 37  ? 0.1385 0.1340 0.1404 -0.0041 -0.0173 0.0088  37  ASN   B CB  
4411 C CG  . ASN   B 37  ? 0.1422 0.1296 0.1452 -0.0046 -0.0123 0.0052  37  ASN   B CG  
4412 O OD1 . ASN   B 37  ? 0.1477 0.1363 0.1547 0.0060  -0.0148 0.0064  37  ASN   B OD1 
4413 N ND2 . ASN   B 37  ? 0.1433 0.1321 0.1501 -0.0003 -0.0137 0.0084  37  ASN   B ND2 
4420 N N   . ALA   B 38  ? 0.1459 0.1274 0.1371 0.0051  0.0001  0.0029  38  ALA   B N   
4421 C CA  . ALA   B 38  ? 0.1536 0.1330 0.1450 -0.0049 0.0032  0.0089  38  ALA   B CA  
4422 C C   . ALA   B 38  ? 0.1493 0.1290 0.1478 0.0007  0.0032  0.0083  38  ALA   B C   
4423 O O   . ALA   B 38  ? 0.1559 0.1399 0.1481 0.0050  -0.0030 0.0103  38  ALA   B O   
4424 C CB  . ALA   B 38  ? 0.1751 0.1384 0.1585 -0.0117 0.0114  0.0049  38  ALA   B CB  
4430 N N   . ALA   B 39  ? 0.1501 0.1334 0.1294 0.0067  -0.0042 0.0061  39  ALA   B N   
4431 C CA  . ALA   B 39  ? 0.1599 0.1414 0.1308 0.0029  -0.0033 0.0060  39  ALA   B CA  
4432 C C   . ALA   B 39  ? 0.1596 0.1437 0.1175 0.0024  -0.0065 -0.0023 39  ALA   B C   
4433 O O   . ALA   B 39  ? 0.1610 0.1526 0.1441 0.0004  -0.0029 0.0102  39  ALA   B O   
4434 C CB  . ALA   B 39  ? 0.1597 0.1438 0.1518 -0.0064 -0.0002 -0.0002 39  ALA   B CB  
4440 N N   . ASN   B 40  ? 0.1632 0.1674 0.1247 -0.0082 0.0008  0.0004  40  ASN   B N   
4441 C CA  . ASN   B 40  ? 0.1688 0.1738 0.1395 -0.0028 -0.0017 -0.0044 40  ASN   B CA  
4442 C C   . ASN   B 40  ? 0.1762 0.1721 0.1199 0.0029  -0.0097 -0.0011 40  ASN   B C   
4443 O O   . ASN   B 40  ? 0.1722 0.1657 0.1310 0.0086  -0.0111 -0.0015 40  ASN   B O   
4444 C CB  . ASN   B 40  ? 0.1857 0.1719 0.1639 0.0084  -0.0106 0.0122  40  ASN   B CB  
4445 C CG  . ASN   B 40  ? 0.1879 0.1792 0.1950 0.0036  -0.0234 0.0180  40  ASN   B CG  
4446 O OD1 . ASN   B 40  ? 0.1826 0.1771 0.2677 0.0042  -0.0334 0.0239  40  ASN   B OD1 
4447 N ND2 . ASN   B 40  ? 0.1896 0.1774 0.1980 0.0033  -0.0196 0.0164  40  ASN   B ND2 
4454 N N   . VAL   B 41  ? 0.1856 0.1773 0.1294 0.0082  0.0024  0.0024  41  VAL   B N   
4455 C CA  . VAL   B 41  ? 0.1909 0.1877 0.1403 0.0065  0.0004  -0.0108 41  VAL   B CA  
4456 C C   . VAL   B 41  ? 0.1860 0.1869 0.1423 0.0139  -0.0080 -0.0124 41  VAL   B C   
4457 O O   . VAL   B 41  ? 0.1864 0.1829 0.1492 0.0103  -0.0131 -0.0161 41  VAL   B O   
4458 C CB  . VAL   B 41  ? 0.2047 0.1968 0.1614 -0.0071 0.0198  -0.0246 41  VAL   B CB  
4459 C CG1 . VAL   B 41  ? 0.2057 0.1975 0.1819 -0.0115 0.0324  -0.0285 41  VAL   B CG1 
4460 C CG2 . VAL   B 41  ? 0.2154 0.2174 0.1773 -0.0095 0.0213  -0.0241 41  VAL   B CG2 
4470 N N   . TYR   B 42  ? 0.1924 0.1903 0.1476 0.0141  -0.0194 -0.0029 42  TYR   B N   
4471 C CA  . TYR   B 42  ? 0.1955 0.1936 0.1570 0.0182  -0.0255 -0.0110 42  TYR   B CA  
4472 C C   . TYR   B 42  ? 0.1790 0.1710 0.1644 0.0173  -0.0232 -0.0163 42  TYR   B C   
4473 O O   . TYR   B 42  ? 0.1853 0.1781 0.1934 0.0098  -0.0314 -0.0236 42  TYR   B O   
4474 C CB  . TYR   B 42  ? 0.2196 0.2238 0.1734 0.0085  -0.0304 0.0041  42  TYR   B CB  
4475 C CG  . TYR   B 42  ? 0.2233 0.2458 0.1766 0.0014  -0.0266 0.0117  42  TYR   B CG  
4476 C CD1 . TYR   B 42  ? 0.2210 0.2477 0.1494 -0.0030 -0.0191 0.0003  42  TYR   B CD1 
4477 C CD2 . TYR   B 42  ? 0.2383 0.2590 0.2119 0.0010  -0.0109 0.0179  42  TYR   B CD2 
4478 C CE1 . TYR   B 42  ? 0.2324 0.2603 0.1591 0.0007  -0.0149 0.0023  42  TYR   B CE1 
4479 C CE2 . TYR   B 42  ? 0.2421 0.2642 0.2086 0.0039  0.0102  0.0308  42  TYR   B CE2 
4480 C CZ  . TYR   B 42  ? 0.2527 0.2706 0.1960 0.0164  0.0119  0.0173  42  TYR   B CZ  
4481 O OH  . TYR   B 42  ? 0.2886 0.2933 0.2431 0.0329  0.0233  0.0274  42  TYR   B OH  
4491 N N   . LEU   B 43  ? 0.1696 0.1585 0.1592 0.0096  -0.0156 -0.0122 43  LEU   B N   
4492 C CA  . LEU   B 43  ? 0.1683 0.1576 0.1469 0.0037  -0.0140 -0.0052 43  LEU   B CA  
4493 C C   . LEU   B 43  ? 0.1737 0.1591 0.1483 0.0013  -0.0177 -0.0039 43  LEU   B C   
4494 O O   . LEU   B 43  ? 0.1686 0.1622 0.1696 0.0038  -0.0292 0.0053  43  LEU   B O   
4495 C CB  . LEU   B 43  ? 0.1690 0.1530 0.1603 -0.0036 -0.0243 -0.0104 43  LEU   B CB  
4496 C CG  . LEU   B 43  ? 0.1733 0.1524 0.1598 -0.0009 -0.0314 -0.0081 43  LEU   B CG  
4497 C CD1 . LEU   B 43  ? 0.1772 0.1595 0.1994 -0.0017 -0.0475 -0.0085 43  LEU   B CD1 
4498 C CD2 . LEU   B 43  ? 0.1713 0.1528 0.1629 0.0003  -0.0268 -0.0061 43  LEU   B CD2 
4510 N N   . LYS   B 44  ? 0.1695 0.1594 0.1467 0.0043  -0.0069 -0.0115 44  LYS   B N   
4511 C CA  . LYS   B 44  ? 0.1822 0.1708 0.1481 0.0063  -0.0152 0.0075  44  LYS   B CA  
4512 C C   . LYS   B 44  ? 0.1697 0.1635 0.1509 0.0122  -0.0157 -0.0004 44  LYS   B C   
4513 O O   . LYS   B 44  ? 0.1907 0.1626 0.1862 0.0013  -0.0123 -0.0011 44  LYS   B O   
4514 C CB  . LYS   B 44  ? 0.2099 0.1903 0.1696 0.0133  -0.0270 -0.0004 44  LYS   B CB  
4515 C CG  . LYS   B 44  ? 0.2497 0.2179 0.2048 0.0102  -0.0510 0.0050  44  LYS   B CG  
4516 C CD  . LYS   B 44  ? 0.2875 0.2415 0.2632 -0.0048 -0.0610 0.0073  44  LYS   B CD  
4517 C CE  . LYS   B 44  ? 0.3177 0.2677 0.3042 -0.0101 -0.0618 0.0113  44  LYS   B CE  
4518 N NZ  . LYS   B 44  ? 0.3320 0.2793 0.3304 -0.0051 -0.0644 0.0185  44  LYS   B NZ  
4532 N N   . HIS   B 45  ? 0.1684 0.1681 0.1442 0.0090  -0.0148 0.0082  45  HIS   B N   
4533 C CA  . HIS   B 45  ? 0.1720 0.1613 0.1531 0.0099  -0.0075 0.0017  45  HIS   B CA  
4534 C C   . HIS   B 45  ? 0.1938 0.1753 0.1918 0.0154  -0.0209 -0.0040 45  HIS   B C   
4535 O O   . HIS   B 45  ? 0.2011 0.2050 0.2275 0.0437  0.0099  -0.0006 45  HIS   B O   
4536 C CB  . HIS   B 45  ? 0.1612 0.1607 0.1562 -0.0013 -0.0106 0.0006  45  HIS   B CB  
4537 C CG  . HIS   B 45  ? 0.1611 0.1580 0.1530 -0.0064 -0.0126 0.0037  45  HIS   B CG  
4538 N ND1 . HIS   B 45  ? 0.1657 0.1532 0.1617 -0.0004 -0.0205 -0.0106 45  HIS   B ND1 
4539 C CD2 . HIS   B 45  ? 0.1754 0.1609 0.1667 -0.0108 -0.0200 -0.0007 45  HIS   B CD2 
4540 C CE1 . HIS   B 45  ? 0.1789 0.1419 0.1523 -0.0049 -0.0346 -0.0081 45  HIS   B CE1 
4541 N NE2 . HIS   B 45  ? 0.1852 0.1516 0.1612 -0.0033 -0.0248 -0.0048 45  HIS   B NE2 
4549 N N   A GLY   B 46  ? 0.2034 0.1697 0.2181 0.0129  -0.0402 -0.0005 46  GLY   B N   
4550 N N   B GLY   B 46  ? 0.2022 0.1817 0.2087 0.0143  -0.0285 0.0031  46  GLY   B N   
4551 C CA  A GLY   B 46  ? 0.2126 0.1793 0.2559 0.0139  -0.0480 0.0026  46  GLY   B CA  
4552 C CA  B GLY   B 46  ? 0.2100 0.1922 0.2303 0.0135  -0.0335 0.0100  46  GLY   B CA  
4553 C C   A GLY   B 46  ? 0.2108 0.1947 0.2945 0.0249  -0.0400 0.0027  46  GLY   B C   
4554 C C   B GLY   B 46  ? 0.2119 0.2028 0.2540 0.0161  -0.0300 0.0152  46  GLY   B C   
4555 O O   A GLY   B 46  ? 0.2174 0.2093 0.3770 0.0304  -0.0191 -0.0211 46  GLY   B O   
4556 O O   B GLY   B 46  ? 0.2153 0.2115 0.2692 0.0183  -0.0281 0.0269  46  GLY   B O   
4563 N N   . GLY   B 47  ? 0.2125 0.2088 0.2675 0.0081  -0.0177 0.0027  47  GLY   B N   
4564 C CA  . GLY   B 47  ? 0.2025 0.1843 0.2235 0.0004  -0.0125 0.0071  47  GLY   B CA  
4565 C C   . GLY   B 47  ? 0.1820 0.1619 0.1897 0.0012  -0.0037 0.0108  47  GLY   B C   
4566 O O   . GLY   B 47  ? 0.1932 0.1438 0.2013 0.0022  -0.0153 0.0119  47  GLY   B O   
4571 N N   . GLY   B 48  ? 0.1600 0.1532 0.1940 0.0050  -0.0125 0.0188  48  GLY   B N   
4572 C CA  . GLY   B 48  ? 0.1601 0.1493 0.1926 -0.0018 -0.0085 0.0122  48  GLY   B CA  
4573 C C   . GLY   B 48  ? 0.1563 0.1446 0.1765 -0.0011 -0.0009 0.0065  48  GLY   B C   
4574 O O   . GLY   B 48  ? 0.1528 0.1490 0.2024 0.0027  -0.0093 0.0099  48  GLY   B O   
4578 N N   . VAL   B 49  ? 0.1584 0.1531 0.1620 0.0082  -0.0020 0.0082  49  VAL   B N   
4579 C CA  . VAL   B 49  ? 0.1587 0.1592 0.1606 0.0082  -0.0176 -0.0026 49  VAL   B CA  
4580 C C   . VAL   B 49  ? 0.1523 0.1494 0.1465 0.0121  -0.0125 0.0038  49  VAL   B C   
4581 O O   . VAL   B 49  ? 0.1591 0.1533 0.1629 0.0032  -0.0055 0.0064  49  VAL   B O   
4582 C CB  . VAL   B 49  ? 0.1577 0.1785 0.1823 0.0004  -0.0267 0.0021  49  VAL   B CB  
4583 C CG1 . VAL   B 49  ? 0.1578 0.1874 0.1783 0.0079  -0.0273 0.0072  49  VAL   B CG1 
4584 C CG2 . VAL   B 49  ? 0.1761 0.1929 0.2079 -0.0053 -0.0435 0.0020  49  VAL   B CG2 
4594 N N   . ALA   B 50  ? 0.1489 0.1407 0.1546 0.0048  -0.0096 0.0029  50  ALA   B N   
4595 C CA  . ALA   B 50  ? 0.1485 0.1393 0.1618 0.0054  -0.0071 0.0072  50  ALA   B CA  
4596 C C   . ALA   B 50  ? 0.1544 0.1415 0.1585 0.0024  -0.0033 0.0076  50  ALA   B C   
4597 O O   . ALA   B 50  ? 0.1539 0.1464 0.1489 0.0063  -0.0024 0.0025  50  ALA   B O   
4598 C CB  . ALA   B 50  ? 0.1511 0.1389 0.1623 0.0016  -0.0089 0.0092  50  ALA   B CB  
4604 N N   . GLY   B 51  ? 0.1518 0.1556 0.1585 0.0072  -0.0132 0.0097  51  GLY   B N   
4605 C CA  . GLY   B 51  ? 0.1487 0.1607 0.1798 0.0198  -0.0141 0.0081  51  GLY   B CA  
4606 C C   . GLY   B 51  ? 0.1485 0.1546 0.1817 0.0202  -0.0107 0.0102  51  GLY   B C   
4607 O O   . GLY   B 51  ? 0.1524 0.1664 0.2055 0.0111  -0.0112 0.0021  51  GLY   B O   
4611 N N   . ALA   B 52  ? 0.1537 0.1469 0.1650 0.0136  -0.0111 0.0117  52  ALA   B N   
4612 C CA  . ALA   B 52  ? 0.1603 0.1552 0.1652 0.0160  0.0012  0.0039  52  ALA   B CA  
4613 C C   . ALA   B 52  ? 0.1471 0.1531 0.1637 0.0104  0.0026  0.0029  52  ALA   B C   
4614 O O   . ALA   B 52  ? 0.1530 0.1584 0.1808 0.0108  0.0053  0.0010  52  ALA   B O   
4615 C CB  . ALA   B 52  ? 0.1740 0.1613 0.1763 0.0059  0.0060  -0.0030 52  ALA   B CB  
4621 N N   . LEU   B 53  ? 0.1440 0.1502 0.1550 0.0172  0.0043  0.0024  53  LEU   B N   
4622 C CA  . LEU   B 53  ? 0.1442 0.1606 0.1582 0.0138  -0.0021 0.0043  53  LEU   B CA  
4623 C C   . LEU   B 53  ? 0.1517 0.1535 0.1492 0.0147  0.0016  0.0111  53  LEU   B C   
4624 O O   . LEU   B 53  ? 0.1549 0.1614 0.1570 0.0034  0.0059  0.0199  53  LEU   B O   
4625 C CB  . LEU   B 53  ? 0.1424 0.1654 0.1703 0.0093  -0.0020 0.0223  53  LEU   B CB  
4626 C CG  . LEU   B 53  ? 0.1420 0.1770 0.1655 0.0021  -0.0022 0.0253  53  LEU   B CG  
4627 C CD1 . LEU   B 53  ? 0.1518 0.1936 0.1969 0.0112  0.0009  0.0069  53  LEU   B CD1 
4628 C CD2 . LEU   B 53  ? 0.1584 0.2044 0.1938 -0.0101 -0.0103 -0.0114 53  LEU   B CD2 
4640 N N   . ASN   B 54  ? 0.1526 0.1460 0.1514 0.0049  -0.0052 0.0076  54  ASN   B N   
4641 C CA  . ASN   B 54  ? 0.1545 0.1562 0.1609 0.0008  -0.0096 0.0018  54  ASN   B CA  
4642 C C   . ASN   B 54  ? 0.1482 0.1581 0.1845 -0.0010 -0.0017 0.0136  54  ASN   B C   
4643 O O   . ASN   B 54  ? 0.1446 0.1637 0.1936 -0.0016 -0.0005 0.0099  54  ASN   B O   
4644 C CB  . ASN   B 54  ? 0.1613 0.1668 0.1713 0.0071  -0.0060 0.0061  54  ASN   B CB  
4645 C CG  . ASN   B 54  ? 0.1524 0.1774 0.1840 0.0060  -0.0067 0.0013  54  ASN   B CG  
4646 O OD1 . ASN   B 54  ? 0.1473 0.1767 0.1896 -0.0005 -0.0147 -0.0105 54  ASN   B OD1 
4647 N ND2 . ASN   B 54  ? 0.1606 0.1977 0.2069 0.0027  -0.0277 0.0110  54  ASN   B ND2 
4654 N N   . LYS   B 55  ? 0.1466 0.1672 0.1992 0.0115  0.0015  0.0108  55  LYS   B N   
4655 C CA  . LYS   B 55  ? 0.1541 0.1803 0.2125 0.0231  -0.0047 0.0162  55  LYS   B CA  
4656 C C   . LYS   B 55  ? 0.1483 0.1745 0.2096 0.0172  0.0005  0.0049  55  LYS   B C   
4657 O O   . LYS   B 55  ? 0.1463 0.1909 0.2184 0.0089  0.0035  0.0021  55  LYS   B O   
4658 C CB  . LYS   B 55  ? 0.1678 0.1913 0.2342 0.0260  0.0012  0.0272  55  LYS   B CB  
4659 C CG  . LYS   B 55  ? 0.2086 0.2143 0.3154 0.0274  0.0207  0.0324  55  LYS   B CG  
4660 C CD  . LYS   B 55  ? 0.2487 0.2330 0.3865 0.0391  0.0323  0.0371  55  LYS   B CD  
4661 C CE  . LYS   B 55  ? 0.2744 0.2488 0.4468 0.0402  0.0419  0.0379  55  LYS   B CE  
4662 N NZ  . LYS   B 55  ? 0.2826 0.2631 0.4786 0.0382  0.0325  0.0431  55  LYS   B NZ  
4676 N N   . ALA   B 56  ? 0.1487 0.1777 0.1908 0.0083  -0.0004 -0.0017 56  ALA   B N   
4677 C CA  . ALA   B 56  ? 0.1638 0.1945 0.1905 0.0024  0.0039  -0.0020 56  ALA   B CA  
4678 C C   . ALA   B 56  ? 0.1630 0.1920 0.1783 0.0045  0.0112  0.0087  56  ALA   B C   
4679 O O   . ALA   B 56  ? 0.1755 0.2019 0.2008 0.0037  0.0290  0.0112  56  ALA   B O   
4680 C CB  . ALA   B 56  ? 0.1763 0.2162 0.1901 -0.0131 -0.0060 -0.0086 56  ALA   B CB  
4686 N N   . THR   B 57  ? 0.1557 0.1856 0.1925 0.0072  0.0129  0.0132  57  THR   B N   
4687 C CA  . THR   B 57  ? 0.1588 0.1815 0.1846 -0.0005 0.0191  0.0123  57  THR   B CA  
4688 C C   . THR   B 57  ? 0.1646 0.1908 0.2037 -0.0001 0.0144  0.0119  57  THR   B C   
4689 O O   . THR   B 57  ? 0.1697 0.1954 0.2158 -0.0138 0.0129  0.0104  57  THR   B O   
4690 C CB  . THR   B 57  ? 0.1673 0.1690 0.1710 -0.0012 0.0135  0.0180  57  THR   B CB  
4691 O OG1 . THR   B 57  ? 0.1628 0.1632 0.1843 -0.0013 0.0102  0.0106  57  THR   B OG1 
4692 C CG2 . THR   B 57  ? 0.1624 0.1679 0.1813 0.0001  0.0115  0.0086  57  THR   B CG2 
4700 N N   . ASN   B 58  ? 0.1513 0.2075 0.2217 -0.0085 0.0032  -0.0039 58  ASN   B N   
4701 C CA  . ASN   B 58  ? 0.1647 0.2512 0.2651 -0.0184 0.0306  0.0021  58  ASN   B CA  
4702 C C   . ASN   B 58  ? 0.1484 0.2334 0.2267 -0.0144 -0.0055 0.0086  58  ASN   B C   
4703 O O   . ASN   B 58  ? 0.1551 0.2388 0.2367 -0.0197 -0.0070 -0.0010 58  ASN   B O   
4704 C CB  . ASN   B 58  ? 0.2276 0.3069 0.3833 -0.0320 0.0711  0.0061  58  ASN   B CB  
4705 C CG  . ASN   B 58  ? 0.3231 0.3527 0.5236 -0.0336 0.0842  0.0290  58  ASN   B CG  
4706 O OD1 . ASN   B 58  ? 0.3815 0.3815 0.5761 -0.0366 0.0865  0.0368  58  ASN   B OD1 
4707 N ND2 . ASN   B 58  ? 0.4097 0.4097 0.5724 -0.0367 0.0912  0.0378  58  ASN   B ND2 
4714 N N   . ASN   B 59  ? 0.1493 0.2142 0.2090 -0.0101 -0.0045 0.0163  59  ASN   B N   
4715 C CA  . ASN   B 59  ? 0.1513 0.2119 0.2054 -0.0115 -0.0140 0.0161  59  ASN   B CA  
4716 C C   . ASN   B 59  ? 0.1435 0.2018 0.1988 -0.0122 -0.0100 0.0058  59  ASN   B C   
4717 O O   . ASN   B 59  ? 0.1521 0.1992 0.1994 -0.0118 -0.0106 0.0018  59  ASN   B O   
4718 C CB  . ASN   B 59  ? 0.1641 0.2310 0.2270 -0.0099 -0.0242 0.0158  59  ASN   B CB  
4719 C CG  . ASN   B 59  ? 0.1771 0.2483 0.2357 -0.0036 -0.0381 0.0154  59  ASN   B CG  
4720 O OD1 . ASN   B 59  ? 0.1850 0.2548 0.2349 -0.0047 -0.0272 0.0257  59  ASN   B OD1 
4721 N ND2 . ASN   B 59  ? 0.1848 0.2574 0.2491 -0.0120 -0.0420 0.0179  59  ASN   B ND2 
4728 N N   . ALA   B 60  ? 0.1497 0.1894 0.1989 -0.0126 -0.0054 0.0066  60  ALA   B N   
4729 C CA  . ALA   B 60  ? 0.1615 0.1783 0.1929 -0.0212 -0.0055 0.0087  60  ALA   B CA  
4730 C C   . ALA   B 60  ? 0.1612 0.1680 0.1774 -0.0147 -0.0112 0.0130  60  ALA   B C   
4731 O O   . ALA   B 60  ? 0.1645 0.1685 0.1946 -0.0183 -0.0075 -0.0038 60  ALA   B O   
4732 C CB  . ALA   B 60  ? 0.1761 0.1741 0.2159 -0.0166 -0.0011 0.0101  60  ALA   B CB  
4738 N N   . MET   B 61  ? 0.1516 0.1645 0.1709 -0.0127 -0.0067 0.0114  61  MET   B N   
4739 C CA  . MET   B 61  ? 0.1457 0.1561 0.1775 -0.0076 -0.0118 0.0105  61  MET   B CA  
4740 C C   . MET   B 61  ? 0.1543 0.1556 0.1842 -0.0070 -0.0168 0.0121  61  MET   B C   
4741 O O   . MET   B 61  ? 0.1573 0.1536 0.1636 -0.0041 -0.0130 -0.0035 61  MET   B O   
4742 C CB  . MET   B 61  ? 0.1447 0.1607 0.1717 0.0033  -0.0055 0.0078  61  MET   B CB  
4743 C CG  . MET   B 61  ? 0.1469 0.1596 0.1632 -0.0012 -0.0025 0.0041  61  MET   B CG  
4744 S SD  . MET   B 61  ? 0.1481 0.1575 0.1826 -0.0039 -0.0082 -0.0088 61  MET   B SD  
4745 C CE  . MET   B 61  ? 0.1562 0.1821 0.2031 -0.0013 0.0016  -0.0195 61  MET   B CE  
4755 N N   . GLN   B 62  ? 0.1530 0.1590 0.1629 -0.0034 -0.0174 0.0127  62  GLN   B N   
4756 C CA  . GLN   B 62  ? 0.1554 0.1624 0.1681 -0.0027 -0.0178 0.0040  62  GLN   B CA  
4757 C C   . GLN   B 62  ? 0.1572 0.1705 0.1760 -0.0091 -0.0264 -0.0020 62  GLN   B C   
4758 O O   . GLN   B 62  ? 0.1709 0.1679 0.1831 -0.0041 -0.0331 -0.0078 62  GLN   B O   
4759 C CB  . GLN   B 62  ? 0.1554 0.1679 0.1680 0.0030  -0.0145 0.0072  62  GLN   B CB  
4760 C CG  . GLN   B 62  ? 0.1592 0.1742 0.1734 0.0038  -0.0229 0.0028  62  GLN   B CG  
4761 C CD  . GLN   B 62  ? 0.1632 0.1679 0.1705 0.0015  -0.0284 0.0116  62  GLN   B CD  
4762 O OE1 . GLN   B 62  ? 0.1656 0.1656 0.1842 0.0016  -0.0273 -0.0096 62  GLN   B OE1 
4763 N NE2 . GLN   B 62  ? 0.1648 0.1724 0.1822 -0.0000 -0.0255 -0.0005 62  GLN   B NE2 
4772 N N   . VAL   B 63  ? 0.1538 0.1751 0.1964 -0.0118 -0.0248 -0.0073 63  VAL   B N   
4773 C CA  . VAL   B 63  ? 0.1681 0.1791 0.2128 -0.0151 -0.0338 -0.0036 63  VAL   B CA  
4774 C C   . VAL   B 63  ? 0.1692 0.1636 0.1925 -0.0188 -0.0330 -0.0100 63  VAL   B C   
4775 O O   . VAL   B 63  ? 0.1777 0.1660 0.2107 -0.0098 -0.0472 -0.0123 63  VAL   B O   
4776 C CB  . VAL   B 63  ? 0.1724 0.1933 0.2408 -0.0215 -0.0339 -0.0045 63  VAL   B CB  
4777 C CG1 . VAL   B 63  ? 0.1801 0.1959 0.2575 -0.0331 -0.0263 -0.0050 63  VAL   B CG1 
4778 C CG2 . VAL   B 63  ? 0.1683 0.2143 0.2428 -0.0161 -0.0323 -0.0078 63  VAL   B CG2 
4788 N N   . GLU   B 64  ? 0.1688 0.1583 0.1852 -0.0115 -0.0280 -0.0082 64  GLU   B N   
4789 C CA  . GLU   B 64  ? 0.1650 0.1539 0.1789 -0.0118 -0.0376 -0.0081 64  GLU   B CA  
4790 C C   . GLU   B 64  ? 0.1587 0.1517 0.1782 -0.0067 -0.0315 -0.0123 64  GLU   B C   
4791 O O   . GLU   B 64  ? 0.1728 0.1604 0.1696 -0.0122 -0.0296 -0.0118 64  GLU   B O   
4792 C CB  . GLU   B 64  ? 0.1650 0.1604 0.1835 -0.0179 -0.0274 0.0017  64  GLU   B CB  
4793 C CG  . GLU   B 64  ? 0.1749 0.1620 0.1831 -0.0290 -0.0310 -0.0038 64  GLU   B CG  
4794 C CD  . GLU   B 64  ? 0.1784 0.1737 0.1938 -0.0307 -0.0283 -0.0032 64  GLU   B CD  
4795 O OE1 . GLU   B 64  ? 0.1802 0.1947 0.1958 -0.0341 -0.0242 -0.0209 64  GLU   B OE1 
4796 O OE2 . GLU   B 64  ? 0.1943 0.1807 0.1994 -0.0331 -0.0460 -0.0113 64  GLU   B OE2 
4803 N N   . SER   B 65  ? 0.1602 0.1498 0.1675 -0.0092 -0.0206 -0.0136 65  SER   B N   
4804 C CA  . SER   B 65  ? 0.1638 0.1498 0.1645 -0.0057 -0.0224 -0.0110 65  SER   B CA  
4805 C C   . SER   B 65  ? 0.1635 0.1546 0.1604 -0.0013 -0.0296 -0.0162 65  SER   B C   
4806 O O   . SER   B 65  ? 0.1635 0.1613 0.1720 -0.0004 -0.0279 -0.0286 65  SER   B O   
4807 C CB  . SER   B 65  ? 0.1682 0.1574 0.1586 -0.0108 -0.0154 -0.0083 65  SER   B CB  
4808 O OG  . SER   B 65  ? 0.1648 0.1560 0.1703 -0.0115 -0.0157 -0.0171 65  SER   B OG  
4814 N N   . ASP   B 66  ? 0.1754 0.1615 0.1663 -0.0025 -0.0350 -0.0156 66  ASP   B N   
4815 C CA  . ASP   B 66  ? 0.1817 0.1652 0.1699 0.0005  -0.0367 -0.0109 66  ASP   B CA  
4816 C C   . ASP   B 66  ? 0.1799 0.1706 0.1757 -0.0059 -0.0284 -0.0137 66  ASP   B C   
4817 O O   . ASP   B 66  ? 0.1816 0.1775 0.1811 0.0038  -0.0328 -0.0174 66  ASP   B O   
4818 C CB  . ASP   B 66  ? 0.2022 0.1748 0.1864 0.0075  -0.0430 -0.0134 66  ASP   B CB  
4819 C CG  . ASP   B 66  ? 0.2294 0.1898 0.2111 0.0161  -0.0527 0.0001  66  ASP   B CG  
4820 O OD1 . ASP   B 66  ? 0.2520 0.1864 0.2195 0.0095  -0.0521 0.0021  66  ASP   B OD1 
4821 O OD2 . ASP   B 66  ? 0.2469 0.2166 0.2685 0.0343  -0.0509 -0.0033 66  ASP   B OD2 
4826 N N   . ASP   B 67  ? 0.1769 0.1612 0.1727 -0.0102 -0.0270 -0.0194 67  ASP   B N   
4827 C CA  . ASP   B 67  ? 0.1917 0.1584 0.1786 -0.0112 -0.0254 -0.0124 67  ASP   B CA  
4828 C C   . ASP   B 67  ? 0.1901 0.1624 0.1824 0.0011  -0.0246 -0.0178 67  ASP   B C   
4829 O O   . ASP   B 67  ? 0.1939 0.1700 0.1899 0.0020  -0.0206 -0.0219 67  ASP   B O   
4830 C CB  . ASP   B 67  ? 0.2130 0.1678 0.1920 -0.0181 -0.0397 -0.0109 67  ASP   B CB  
4831 C CG  . ASP   B 67  ? 0.2498 0.1758 0.1965 -0.0130 -0.0622 -0.0146 67  ASP   B CG  
4832 O OD1 . ASP   B 67  ? 0.2724 0.1843 0.2132 -0.0172 -0.0675 -0.0064 67  ASP   B OD1 
4833 O OD2 . ASP   B 67  ? 0.2673 0.1856 0.2129 0.0050  -0.0733 -0.0130 67  ASP   B OD2 
4838 N N   . TYR   B 68  ? 0.1868 0.1634 0.1865 -0.0021 -0.0459 -0.0275 68  TYR   B N   
4839 C CA  . TYR   B 68  ? 0.1824 0.1761 0.1903 0.0080  -0.0433 -0.0320 68  TYR   B CA  
4840 C C   . TYR   B 68  ? 0.1767 0.1712 0.1771 0.0040  -0.0350 -0.0394 68  TYR   B C   
4841 O O   . TYR   B 68  ? 0.1822 0.1876 0.1875 0.0061  -0.0340 -0.0577 68  TYR   B O   
4842 C CB  . TYR   B 68  ? 0.1901 0.1982 0.1977 0.0086  -0.0540 -0.0435 68  TYR   B CB  
4843 C CG  . TYR   B 68  ? 0.2004 0.2122 0.2122 0.0122  -0.0402 -0.0636 68  TYR   B CG  
4844 C CD1 . TYR   B 68  ? 0.2022 0.2189 0.2311 -0.0060 -0.0391 -0.0731 68  TYR   B CD1 
4845 C CD2 . TYR   B 68  ? 0.2013 0.2290 0.2289 0.0219  -0.0495 -0.0563 68  TYR   B CD2 
4846 C CE1 . TYR   B 68  ? 0.2073 0.2348 0.2565 -0.0016 -0.0307 -0.0694 68  TYR   B CE1 
4847 C CE2 . TYR   B 68  ? 0.2041 0.2376 0.2428 0.0181  -0.0380 -0.0623 68  TYR   B CE2 
4848 C CZ  . TYR   B 68  ? 0.2036 0.2396 0.2515 0.0033  -0.0375 -0.0707 68  TYR   B CZ  
4849 O OH  . TYR   B 68  ? 0.2030 0.2549 0.2732 -0.0010 -0.0396 -0.0474 68  TYR   B OH  
4859 N N   . ILE   B 69  ? 0.1776 0.1679 0.1842 0.0068  -0.0335 -0.0345 69  ILE   B N   
4860 C CA  . ILE   B 69  ? 0.1814 0.1725 0.1969 -0.0023 -0.0224 -0.0409 69  ILE   B CA  
4861 C C   . ILE   B 69  ? 0.1822 0.1677 0.1845 0.0092  -0.0377 -0.0337 69  ILE   B C   
4862 O O   . ILE   B 69  ? 0.1899 0.1811 0.1867 0.0071  -0.0261 -0.0321 69  ILE   B O   
4863 C CB  . ILE   B 69  ? 0.1926 0.1825 0.2148 -0.0026 0.0002  -0.0382 69  ILE   B CB  
4864 C CG1 . ILE   B 69  ? 0.1904 0.1790 0.2222 -0.0052 0.0042  -0.0357 69  ILE   B CG1 
4865 C CG2 . ILE   B 69  ? 0.2088 0.1952 0.2336 -0.0010 -0.0113 -0.0350 69  ILE   B CG2 
4866 C CD1 . ILE   B 69  ? 0.1864 0.1829 0.2369 -0.0130 0.0044  -0.0316 69  ILE   B CD1 
4878 N N   . ALA   B 70  ? 0.1846 0.1711 0.1798 0.0103  -0.0433 -0.0286 70  ALA   B N   
4879 C CA  . ALA   B 70  ? 0.1894 0.1746 0.1671 0.0038  -0.0453 -0.0262 70  ALA   B CA  
4880 C C   . ALA   B 70  ? 0.1934 0.1716 0.1745 -0.0029 -0.0471 -0.0368 70  ALA   B C   
4881 O O   . ALA   B 70  ? 0.1995 0.1745 0.1775 0.0040  -0.0382 -0.0373 70  ALA   B O   
4882 C CB  . ALA   B 70  ? 0.1920 0.1900 0.1750 -0.0025 -0.0430 -0.0235 70  ALA   B CB  
4888 N N   . THR   B 71  ? 0.1968 0.1732 0.1888 0.0054  -0.0623 -0.0356 71  THR   B N   
4889 C CA  . THR   B 71  ? 0.2120 0.1780 0.2098 0.0104  -0.0689 -0.0411 71  THR   B CA  
4890 C C   . THR   B 71  ? 0.2061 0.1795 0.2291 0.0256  -0.0656 -0.0532 71  THR   B C   
4891 O O   . THR   B 71  ? 0.2169 0.1869 0.2713 0.0237  -0.0538 -0.0646 71  THR   B O   
4892 C CB  . THR   B 71  ? 0.2331 0.2031 0.2282 0.0005  -0.0761 -0.0156 71  THR   B CB  
4893 O OG1 . THR   B 71  ? 0.2456 0.2289 0.2612 -0.0160 -0.0730 0.0060  71  THR   B OG1 
4894 C CG2 . THR   B 71  ? 0.2502 0.2026 0.2501 0.0057  -0.0651 0.0036  71  THR   B CG2 
4902 N N   . ASN   B 72  ? 0.1945 0.1874 0.2196 0.0165  -0.0639 -0.0682 72  ASN   B N   
4903 C CA  . ASN   B 72  ? 0.1976 0.1984 0.2228 0.0196  -0.0487 -0.0701 72  ASN   B CA  
4904 C C   . ASN   B 72  ? 0.1971 0.2090 0.2289 0.0034  -0.0232 -0.0677 72  ASN   B C   
4905 O O   . ASN   B 72  ? 0.1974 0.2220 0.2525 0.0111  -0.0090 -0.0706 72  ASN   B O   
4906 C CB  . ASN   B 72  ? 0.2056 0.2077 0.2346 0.0127  -0.0618 -0.0582 72  ASN   B CB  
4907 C CG  . ASN   B 72  ? 0.2216 0.2239 0.2420 0.0302  -0.0626 -0.0338 72  ASN   B CG  
4908 O OD1 . ASN   B 72  ? 0.2448 0.2436 0.2354 0.0147  -0.0436 -0.0390 72  ASN   B OD1 
4909 N ND2 . ASN   B 72  ? 0.2307 0.2310 0.2755 0.0479  -0.0479 0.0014  72  ASN   B ND2 
4916 N N   . GLY   B 73  ? 0.2016 0.2099 0.2155 -0.0021 -0.0297 -0.0623 73  GLY   B N   
4917 C CA  . GLY   B 73  ? 0.1938 0.2143 0.1905 -0.0028 -0.0268 -0.0531 73  GLY   B CA  
4918 C C   . GLY   B 73  ? 0.1881 0.2124 0.1506 0.0066  -0.0201 -0.0497 73  GLY   B C   
4919 O O   . GLY   B 73  ? 0.1833 0.1981 0.1628 0.0090  -0.0211 -0.0371 73  GLY   B O   
4923 N N   . PRO   B 74  ? 0.1874 0.2198 0.1487 0.0080  -0.0284 -0.0362 74  PRO   B N   
4924 C CA  . PRO   B 74  ? 0.1820 0.2173 0.1466 0.0093  -0.0256 -0.0252 74  PRO   B CA  
4925 C C   . PRO   B 74  ? 0.1703 0.2023 0.1398 0.0086  -0.0220 -0.0229 74  PRO   B C   
4926 O O   . PRO   B 74  ? 0.1777 0.2053 0.1834 0.0087  -0.0151 -0.0366 74  PRO   B O   
4927 C CB  . PRO   B 74  ? 0.1980 0.2372 0.1584 0.0068  -0.0238 -0.0159 74  PRO   B CB  
4928 C CG  . PRO   B 74  ? 0.2156 0.2467 0.1853 0.0079  -0.0174 -0.0142 74  PRO   B CG  
4929 C CD  . PRO   B 74  ? 0.2131 0.2380 0.1733 0.0085  -0.0176 -0.0278 74  PRO   B CD  
4937 N N   . LEU   B 75  ? 0.1642 0.1872 0.1401 0.0129  -0.0206 -0.0216 75  LEU   B N   
4938 C CA  . LEU   B 75  ? 0.1670 0.1928 0.1413 0.0052  -0.0211 -0.0102 75  LEU   B CA  
4939 C C   . LEU   B 75  ? 0.1710 0.2000 0.1449 0.0055  -0.0100 -0.0072 75  LEU   B C   
4940 O O   . LEU   B 75  ? 0.1915 0.2125 0.1557 0.0010  -0.0093 -0.0060 75  LEU   B O   
4941 C CB  . LEU   B 75  ? 0.1762 0.1935 0.1294 -0.0061 -0.0221 0.0064  75  LEU   B CB  
4942 C CG  . LEU   B 75  ? 0.2109 0.2101 0.1516 -0.0327 -0.0165 -0.0006 75  LEU   B CG  
4943 C CD1 . LEU   B 75  ? 0.2407 0.2233 0.1595 -0.0398 0.0019  -0.0027 75  LEU   B CD1 
4944 C CD2 . LEU   B 75  ? 0.2493 0.2296 0.2054 -0.0279 -0.0093 -0.0006 75  LEU   B CD2 
4956 N N   . LYS   B 76  ? 0.1711 0.2229 0.1632 0.0010  -0.0050 -0.0036 76  LYS   B N   
4957 C CA  . LYS   B 76  ? 0.1849 0.2276 0.1935 -0.0060 0.0181  -0.0073 76  LYS   B CA  
4958 C C   . LYS   B 76  ? 0.1802 0.2118 0.1562 0.0043  0.0072  0.0130  76  LYS   B C   
4959 O O   . LYS   B 76  ? 0.1803 0.1947 0.1553 -0.0013 0.0035  0.0148  76  LYS   B O   
4960 C CB  . LYS   B 76  ? 0.2033 0.2403 0.2697 -0.0103 0.0417  -0.0338 76  LYS   B CB  
4961 C CG  . LYS   B 76  ? 0.2101 0.2620 0.3265 -0.0034 0.0321  -0.0431 76  LYS   B CG  
4962 C CD  . LYS   B 76  ? 0.2109 0.2731 0.3816 0.0041  0.0131  -0.0616 76  LYS   B CD  
4963 C CE  . LYS   B 76  ? 0.2210 0.2891 0.4314 0.0083  0.0019  -0.0718 76  LYS   B CE  
4964 N NZ  . LYS   B 76  ? 0.2225 0.2942 0.4621 0.0086  -0.0144 -0.0858 76  LYS   B NZ  
4978 N N   . VAL   B 77  ? 0.1915 0.2223 0.1552 0.0129  0.0087  0.0190  77  VAL   B N   
4979 C CA  . VAL   B 77  ? 0.1918 0.2145 0.1676 0.0202  0.0171  0.0404  77  VAL   B CA  
4980 C C   . VAL   B 77  ? 0.1738 0.1934 0.1629 0.0177  0.0219  0.0350  77  VAL   B C   
4981 O O   . VAL   B 77  ? 0.1762 0.1897 0.1658 0.0268  0.0290  0.0238  77  VAL   B O   
4982 C CB  . VAL   B 77  ? 0.1992 0.2259 0.1984 0.0215  0.0278  0.0548  77  VAL   B CB  
4983 C CG1 . VAL   B 77  ? 0.2027 0.2154 0.2297 0.0100  0.0264  0.0563  77  VAL   B CG1 
4984 C CG2 . VAL   B 77  ? 0.2116 0.2475 0.2292 0.0200  0.0196  0.0617  77  VAL   B CG2 
4994 N N   . GLY   B 78  ? 0.1652 0.1798 0.1568 0.0114  0.0143  0.0230  78  GLY   B N   
4995 C CA  . GLY   B 78  ? 0.1614 0.1769 0.1526 0.0120  0.0204  0.0154  78  GLY   B CA  
4996 C C   . GLY   B 78  ? 0.1608 0.1697 0.1451 0.0104  0.0164  0.0224  78  GLY   B C   
4997 O O   . GLY   B 78  ? 0.1666 0.1638 0.1672 0.0191  0.0176  0.0224  78  GLY   B O   
5001 N N   . GLY   B 79  ? 0.1532 0.1733 0.1500 0.0073  0.0162  0.0117  79  GLY   B N   
5002 C CA  . GLY   B 79  ? 0.1529 0.1607 0.1541 0.0082  0.0112  0.0086  79  GLY   B CA  
5003 C C   . GLY   B 79  ? 0.1462 0.1500 0.1664 0.0098  0.0054  0.0028  79  GLY   B C   
5004 O O   . GLY   B 79  ? 0.1556 0.1467 0.1763 0.0069  0.0164  0.0142  79  GLY   B O   
5008 N N   . SER   B 80  ? 0.1490 0.1469 0.1715 0.0058  0.0150  -0.0030 80  SER   B N   
5009 C CA  . SER   B 80  ? 0.1402 0.1443 0.1621 0.0041  -0.0020 0.0003  80  SER   B CA  
5010 C C   . SER   B 80  ? 0.1481 0.1405 0.1632 0.0092  -0.0083 -0.0020 80  SER   B C   
5011 O O   . SER   B 80  ? 0.1603 0.1469 0.2044 0.0100  0.0016  -0.0081 80  SER   B O   
5012 C CB  . SER   B 80  ? 0.1476 0.1497 0.1763 -0.0063 -0.0058 0.0083  80  SER   B CB  
5013 O OG  . SER   B 80  ? 0.1550 0.1658 0.1946 -0.0031 -0.0179 0.0109  80  SER   B OG  
5019 N N   . CYS   B 81  ? 0.1485 0.1296 0.1698 0.0000  -0.0069 -0.0044 81  CYS   B N   
5020 C CA  . CYS   B 81  ? 0.1504 0.1321 0.1730 0.0064  -0.0121 -0.0054 81  CYS   B CA  
5021 C C   . CYS   B 81  ? 0.1468 0.1266 0.1502 0.0042  -0.0133 -0.0058 81  CYS   B C   
5022 O O   . CYS   B 81  ? 0.1749 0.1304 0.1589 0.0065  -0.0055 -0.0047 81  CYS   B O   
5023 C CB  . CYS   B 81  ? 0.1632 0.1445 0.1673 -0.0004 -0.0130 -0.0060 81  CYS   B CB  
5024 S SG  . CYS   B 81  ? 0.1670 0.1618 0.1641 -0.0051 -0.0252 -0.0121 81  CYS   B SG  
5030 N N   . VAL   B 82  ? 0.1504 0.1267 0.1608 -0.0028 -0.0138 -0.0077 82  VAL   B N   
5031 C CA  . VAL   B 82  ? 0.1571 0.1322 0.1614 -0.0064 -0.0152 0.0033  82  VAL   B CA  
5032 C C   . VAL   B 82  ? 0.1651 0.1258 0.1707 0.0021  -0.0111 0.0002  82  VAL   B C   
5033 O O   . VAL   B 82  ? 0.1730 0.1277 0.1965 -0.0008 -0.0092 -0.0161 82  VAL   B O   
5034 C CB  . VAL   B 82  ? 0.1662 0.1518 0.1793 0.0020  -0.0143 0.0059  82  VAL   B CB  
5035 C CG1 . VAL   B 82  ? 0.1872 0.1734 0.1918 0.0073  -0.0132 0.0147  82  VAL   B CG1 
5036 C CG2 . VAL   B 82  ? 0.1746 0.1688 0.1876 -0.0048 -0.0261 0.0110  82  VAL   B CG2 
5046 N N   . LEU   B 83  ? 0.1528 0.1298 0.1634 -0.0152 -0.0226 -0.0069 83  LEU   B N   
5047 C CA  . LEU   B 83  ? 0.1564 0.1320 0.1558 -0.0117 -0.0208 -0.0041 83  LEU   B CA  
5048 C C   . LEU   B 83  ? 0.1524 0.1292 0.1489 -0.0182 -0.0191 0.0008  83  LEU   B C   
5049 O O   . LEU   B 83  ? 0.1553 0.1442 0.1372 -0.0225 -0.0171 0.0052  83  LEU   B O   
5050 C CB  . LEU   B 83  ? 0.1593 0.1478 0.1545 -0.0108 -0.0250 -0.0042 83  LEU   B CB  
5051 C CG  . LEU   B 83  ? 0.1775 0.1698 0.1610 -0.0134 -0.0160 -0.0069 83  LEU   B CG  
5052 C CD1 . LEU   B 83  ? 0.1897 0.1769 0.1649 -0.0095 -0.0263 -0.0009 83  LEU   B CD1 
5053 C CD2 . LEU   B 83  ? 0.1956 0.1731 0.1816 -0.0099 -0.0086 -0.0248 83  LEU   B CD2 
5065 N N   . SER   B 84  ? 0.1564 0.1424 0.1781 -0.0198 -0.0198 -0.0002 84  SER   B N   
5066 C CA  . SER   B 84  ? 0.1583 0.1570 0.1652 -0.0264 -0.0181 0.0179  84  SER   B CA  
5067 C C   . SER   B 84  ? 0.1526 0.1777 0.1232 -0.0270 -0.0241 0.0244  84  SER   B C   
5068 O O   . SER   B 84  ? 0.1624 0.1603 0.1221 -0.0209 -0.0149 0.0073  84  SER   B O   
5069 C CB  . SER   B 84  ? 0.1786 0.1675 0.2160 -0.0272 0.0034  0.0182  84  SER   B CB  
5070 O OG  . SER   B 84  ? 0.1813 0.1816 0.2640 -0.0349 0.0058  0.0250  84  SER   B OG  
5076 N N   . GLY   B 85  ? 0.1543 0.2033 0.1421 -0.0288 -0.0171 0.0289  85  GLY   B N   
5077 C CA  . GLY   B 85  ? 0.1577 0.2132 0.1440 -0.0383 -0.0023 -0.0012 85  GLY   B CA  
5078 C C   . GLY   B 85  ? 0.1544 0.1889 0.1486 -0.0424 -0.0072 0.0088  85  GLY   B C   
5079 O O   . GLY   B 85  ? 0.1663 0.1879 0.1492 -0.0536 0.0112  -0.0081 85  GLY   B O   
5083 N N   . HIS   B 86  ? 0.1549 0.1732 0.1665 -0.0315 -0.0256 0.0221  86  HIS   B N   
5084 C CA  . HIS   B 86  ? 0.1572 0.1656 0.1693 -0.0313 -0.0203 0.0173  86  HIS   B CA  
5085 C C   . HIS   B 86  ? 0.1593 0.1822 0.1575 -0.0409 -0.0098 0.0359  86  HIS   B C   
5086 O O   . HIS   B 86  ? 0.1734 0.1944 0.1631 -0.0343 0.0015  0.0364  86  HIS   B O   
5087 C CB  . HIS   B 86  ? 0.1622 0.1704 0.1628 -0.0229 -0.0302 0.0098  86  HIS   B CB  
5088 C CG  . HIS   B 86  ? 0.1668 0.1796 0.1632 -0.0149 -0.0242 0.0085  86  HIS   B CG  
5089 N ND1 . HIS   B 86  ? 0.1743 0.2036 0.1868 -0.0242 -0.0310 -0.0043 86  HIS   B ND1 
5090 C CD2 . HIS   B 86  ? 0.1684 0.1799 0.1808 -0.0135 -0.0254 0.0085  86  HIS   B CD2 
5091 C CE1 . HIS   B 86  ? 0.1812 0.2000 0.1752 -0.0164 -0.0156 -0.0215 86  HIS   B CE1 
5092 N NE2 . HIS   B 86  ? 0.1770 0.1919 0.1694 -0.0039 -0.0177 -0.0038 86  HIS   B NE2 
5100 N N   . ASN   B 87  ? 0.1595 0.1862 0.1696 -0.0338 -0.0092 0.0360  87  ASN   B N   
5101 C CA  . ASN   B 87  ? 0.1654 0.2054 0.1745 -0.0318 0.0190  0.0259  87  ASN   B CA  
5102 C C   . ASN   B 87  ? 0.1767 0.1904 0.1657 -0.0294 0.0268  0.0156  87  ASN   B C   
5103 O O   . ASN   B 87  ? 0.2051 0.1968 0.1872 -0.0230 0.0456  0.0139  87  ASN   B O   
5104 C CB  . ASN   B 87  ? 0.1672 0.2404 0.2059 -0.0305 0.0255  0.0210  87  ASN   B CB  
5105 C CG  . ASN   B 87  ? 0.1749 0.2564 0.2124 0.0032  0.0337  0.0323  87  ASN   B CG  
5106 O OD1 . ASN   B 87  ? 0.1745 0.2418 0.1937 0.0121  0.0428  0.0511  87  ASN   B OD1 
5107 N ND2 . ASN   B 87  ? 0.2098 0.2647 0.2489 0.0044  0.0388  0.0156  87  ASN   B ND2 
5114 N N   . LEU   B 88  ? 0.1652 0.1778 0.1485 -0.0319 0.0091  0.0115  88  LEU   B N   
5115 C CA  . LEU   B 88  ? 0.1772 0.1744 0.1474 -0.0308 0.0036  0.0025  88  LEU   B CA  
5116 C C   . LEU   B 88  ? 0.1777 0.1611 0.1495 -0.0363 0.0007  0.0061  88  LEU   B C   
5117 O O   . LEU   B 88  ? 0.2030 0.1697 0.1915 -0.0199 -0.0288 -0.0076 88  LEU   B O   
5118 C CB  . LEU   B 88  ? 0.1847 0.1809 0.1652 -0.0369 -0.0118 0.0180  88  LEU   B CB  
5119 C CG  . LEU   B 88  ? 0.2206 0.2108 0.1821 -0.0317 -0.0324 0.0384  88  LEU   B CG  
5120 C CD1 . LEU   B 88  ? 0.2340 0.2432 0.1950 -0.0442 -0.0207 0.0544  88  LEU   B CD1 
5121 C CD2 . LEU   B 88  ? 0.2537 0.2324 0.2275 0.0094  -0.0535 0.0188  88  LEU   B CD2 
5133 N N   . ALA   B 89  ? 0.1684 0.1570 0.1400 -0.0379 0.0145  0.0024  89  ALA   B N   
5134 C CA  . ALA   B 89  ? 0.1658 0.1572 0.1249 -0.0342 0.0024  0.0093  89  ALA   B CA  
5135 C C   . ALA   B 89  ? 0.1716 0.1601 0.1255 -0.0366 0.0152  0.0055  89  ALA   B C   
5136 O O   . ALA   B 89  ? 0.1567 0.1691 0.1633 -0.0397 0.0101  -0.0265 89  ALA   B O   
5137 C CB  . ALA   B 89  ? 0.1559 0.1573 0.1402 -0.0387 0.0016  0.0180  89  ALA   B CB  
5143 N N   . LYS   B 90  ? 0.2084 0.1478 0.1371 -0.0403 -0.0066 0.0115  90  LYS   B N   
5144 C CA  . LYS   B 90  ? 0.2226 0.1432 0.1393 -0.0382 -0.0068 0.0104  90  LYS   B CA  
5145 C C   . LYS   B 90  ? 0.2085 0.1363 0.1502 -0.0405 -0.0107 -0.0021 90  LYS   B C   
5146 O O   . LYS   B 90  ? 0.2178 0.1619 0.1734 -0.0607 -0.0030 0.0026  90  LYS   B O   
5147 C CB  . LYS   B 90  ? 0.2503 0.1463 0.1716 -0.0323 -0.0013 0.0201  90  LYS   B CB  
5148 C CG  . LYS   B 90  ? 0.2546 0.1674 0.1801 -0.0172 0.0333  0.0216  90  LYS   B CG  
5149 C CD  . LYS   B 90  ? 0.2784 0.1943 0.2289 -0.0080 0.0597  0.0015  90  LYS   B CD  
5150 C CE  . LYS   B 90  ? 0.2917 0.2138 0.2730 -0.0139 0.0704  -0.0143 90  LYS   B CE  
5151 N NZ  . LYS   B 90  ? 0.2952 0.2063 0.2803 -0.0260 0.0833  -0.0163 90  LYS   B NZ  
5165 N N   . HIS   B 91  ? 0.1826 0.1266 0.1291 -0.0290 -0.0150 0.0083  91  HIS   B N   
5166 C CA  . HIS   B 91  ? 0.1700 0.1324 0.1432 -0.0237 -0.0195 0.0044  91  HIS   B CA  
5167 C C   . HIS   B 91  ? 0.1615 0.1377 0.1258 -0.0258 -0.0161 0.0047  91  HIS   B C   
5168 O O   . HIS   B 91  ? 0.1754 0.1379 0.1274 -0.0246 -0.0236 0.0015  91  HIS   B O   
5169 C CB  . HIS   B 91  ? 0.1839 0.1330 0.1952 -0.0089 -0.0087 0.0195  91  HIS   B CB  
5170 C CG  . HIS   B 91  ? 0.2256 0.1513 0.2641 0.0059  0.0243  0.0259  91  HIS   B CG  
5171 N ND1 . HIS   B 91  ? 0.2587 0.1578 0.3132 0.0071  0.0318  0.0051  91  HIS   B ND1 
5172 C CD2 . HIS   B 91  ? 0.2396 0.1833 0.3055 0.0191  0.0057  0.0575  91  HIS   B CD2 
5173 C CE1 . HIS   B 91  ? 0.2604 0.1719 0.3294 0.0242  0.0287  0.0126  91  HIS   B CE1 
5174 N NE2 . HIS   B 91  ? 0.2504 0.1887 0.3267 0.0321  0.0188  0.0607  91  HIS   B NE2 
5182 N N   . CYS   B 92  ? 0.1518 0.1334 0.1306 -0.0223 -0.0184 0.0033  92  CYS   B N   
5183 C CA  . CYS   B 92  ? 0.1490 0.1284 0.1248 -0.0215 -0.0094 0.0025  92  CYS   B CA  
5184 C C   . CYS   B 92  ? 0.1422 0.1247 0.1252 -0.0144 -0.0112 0.0043  92  CYS   B C   
5185 O O   . CYS   B 92  ? 0.1518 0.1328 0.1374 -0.0168 -0.0065 -0.0015 92  CYS   B O   
5186 C CB  . CYS   B 92  ? 0.1531 0.1432 0.1267 -0.0128 -0.0076 0.0041  92  CYS   B CB  
5187 S SG  . CYS   B 92  ? 0.1481 0.1405 0.1445 -0.0122 -0.0135 0.0053  92  CYS   B SG  
5193 N N   . LEU   B 93  ? 0.1348 0.1271 0.1247 -0.0120 -0.0073 -0.0011 93  LEU   B N   
5194 C CA  . LEU   B 93  ? 0.1403 0.1299 0.1335 -0.0049 -0.0126 0.0018  93  LEU   B CA  
5195 C C   . LEU   B 93  ? 0.1329 0.1228 0.1233 -0.0043 -0.0082 0.0075  93  LEU   B C   
5196 O O   . LEU   B 93  ? 0.1367 0.1260 0.1383 -0.0048 -0.0060 0.0027  93  LEU   B O   
5197 C CB  . LEU   B 93  ? 0.1408 0.1298 0.1547 -0.0025 -0.0115 0.0092  93  LEU   B CB  
5198 C CG  . LEU   B 93  ? 0.1392 0.1413 0.1620 -0.0045 -0.0077 0.0130  93  LEU   B CG  
5199 C CD1 . LEU   B 93  ? 0.1476 0.1523 0.1610 0.0004  -0.0082 -0.0005 93  LEU   B CD1 
5200 C CD2 . LEU   B 93  ? 0.1380 0.1440 0.1686 -0.0046 -0.0158 0.0087  93  LEU   B CD2 
5212 N N   . HIS   B 94  ? 0.1347 0.1238 0.1227 -0.0099 -0.0124 0.0036  94  HIS   B N   
5213 C CA  . HIS   B 94  ? 0.1400 0.1267 0.1306 -0.0053 -0.0075 0.0093  94  HIS   B CA  
5214 C C   . HIS   B 94  ? 0.1408 0.1273 0.1456 -0.0026 -0.0031 0.0063  94  HIS   B C   
5215 O O   . HIS   B 94  ? 0.1421 0.1349 0.1848 -0.0058 0.0163  -0.0061 94  HIS   B O   
5216 C CB  . HIS   B 94  ? 0.1408 0.1339 0.1377 -0.0020 -0.0112 0.0051  94  HIS   B CB  
5217 C CG  . HIS   B 94  ? 0.1436 0.1311 0.1310 -0.0063 -0.0218 0.0042  94  HIS   B CG  
5218 N ND1 . HIS   B 94  ? 0.1458 0.1354 0.1306 -0.0076 -0.0219 -0.0003 94  HIS   B ND1 
5219 C CD2 . HIS   B 94  ? 0.1452 0.1324 0.1331 -0.0012 -0.0194 0.0078  94  HIS   B CD2 
5220 C CE1 . HIS   B 94  ? 0.1521 0.1354 0.1241 -0.0152 -0.0214 0.0040  94  HIS   B CE1 
5221 N NE2 . HIS   B 94  ? 0.1437 0.1402 0.1394 -0.0145 -0.0160 0.0063  94  HIS   B NE2 
5229 N N   . VAL   B 95  ? 0.1293 0.1242 0.1445 -0.0002 0.0001  0.0055  95  VAL   B N   
5230 C CA  . VAL   B 95  ? 0.1334 0.1344 0.1417 0.0011  -0.0004 0.0147  95  VAL   B CA  
5231 C C   . VAL   B 95  ? 0.1362 0.1307 0.1428 -0.0003 0.0064  0.0065  95  VAL   B C   
5232 O O   . VAL   B 95  ? 0.1452 0.1334 0.1538 0.0016  0.0008  0.0158  95  VAL   B O   
5233 C CB  . VAL   B 95  ? 0.1393 0.1343 0.1480 -0.0045 -0.0110 0.0045  95  VAL   B CB  
5234 C CG1 . VAL   B 95  ? 0.1483 0.1493 0.1629 -0.0100 0.0001  0.0113  95  VAL   B CG1 
5235 C CG2 . VAL   B 95  ? 0.1522 0.1291 0.1432 -0.0029 -0.0150 0.0077  95  VAL   B CG2 
5245 N N   . VAL   B 96  ? 0.1502 0.1378 0.1454 0.0094  0.0049  0.0142  96  VAL   B N   
5246 C CA  . VAL   B 96  ? 0.1563 0.1484 0.1361 0.0084  0.0051  0.0160  96  VAL   B CA  
5247 C C   . VAL   B 96  ? 0.1597 0.1562 0.1520 0.0066  0.0162  0.0185  96  VAL   B C   
5248 O O   . VAL   B 96  ? 0.1612 0.1577 0.1658 -0.0004 0.0176  0.0046  96  VAL   B O   
5249 C CB  . VAL   B 96  ? 0.1596 0.1673 0.1486 0.0062  0.0030  0.0037  96  VAL   B CB  
5250 C CG1 . VAL   B 96  ? 0.1641 0.1803 0.1545 0.0152  0.0012  0.0066  96  VAL   B CG1 
5251 C CG2 . VAL   B 96  ? 0.1723 0.1759 0.1551 0.0051  0.0040  -0.0005 96  VAL   B CG2 
5261 N N   . GLY   B 97  ? 0.1596 0.1527 0.1488 0.0056  0.0011  0.0187  97  GLY   B N   
5262 C CA  . GLY   B 97  ? 0.1723 0.1545 0.1567 -0.0007 0.0107  0.0208  97  GLY   B CA  
5263 C C   . GLY   B 97  ? 0.1894 0.1623 0.1546 0.0072  0.0061  0.0165  97  GLY   B C   
5264 O O   . GLY   B 97  ? 0.1974 0.1718 0.1527 0.0024  0.0029  0.0082  97  GLY   B O   
5268 N N   . PRO   B 98  ? 0.2022 0.1667 0.1657 0.0066  0.0234  0.0262  98  PRO   B N   
5269 C CA  . PRO   B 98  ? 0.2111 0.1798 0.1636 0.0094  0.0311  0.0212  98  PRO   B CA  
5270 C C   . PRO   B 98  ? 0.2201 0.1804 0.1383 0.0220  0.0325  0.0348  98  PRO   B C   
5271 O O   . PRO   B 98  ? 0.2152 0.1781 0.1615 0.0252  0.0351  0.0346  98  PRO   B O   
5272 C CB  . PRO   B 98  ? 0.1991 0.1826 0.1823 0.0013  0.0438  0.0162  98  PRO   B CB  
5273 C CG  . PRO   B 98  ? 0.1952 0.1750 0.1832 0.0037  0.0305  0.0281  98  PRO   B CG  
5274 C CD  . PRO   B 98  ? 0.1851 0.1677 0.1815 0.0080  0.0269  0.0306  98  PRO   B CD  
5282 N N   . ASN   B 99  ? 0.2310 0.1922 0.1571 0.0383  0.0307  0.0158  99  ASN   B N   
5283 C CA  . ASN   B 99  ? 0.2505 0.1950 0.1695 0.0403  0.0280  0.0354  99  ASN   B CA  
5284 C C   . ASN   B 99  ? 0.2737 0.2261 0.1927 0.0340  0.0432  0.0586  99  ASN   B C   
5285 O O   . ASN   B 99  ? 0.2845 0.2285 0.1998 0.0342  0.0302  0.0538  99  ASN   B O   
5286 C CB  . ASN   B 99  ? 0.2603 0.1930 0.1790 0.0405  0.0151  0.0364  99  ASN   B CB  
5287 C CG  . ASN   B 99  ? 0.2615 0.2032 0.2020 0.0359  -0.0044 0.0299  99  ASN   B CG  
5288 O OD1 . ASN   B 99  ? 0.2627 0.2073 0.2203 0.0393  -0.0178 0.0296  99  ASN   B OD1 
5289 N ND2 . ASN   B 99  ? 0.2607 0.2036 0.2185 0.0397  -0.0194 0.0293  99  ASN   B ND2 
5296 N N   A VAL   B 100 ? 0.2913 0.2396 0.2270 0.0212  0.0496  0.0807  100 VAL   B N   
5297 N N   B VAL   B 100 ? 0.2955 0.2408 0.2277 0.0271  0.0388  0.0739  100 VAL   B N   
5298 C CA  A VAL   B 100 ? 0.3185 0.2607 0.2812 0.0123  0.0496  0.0890  100 VAL   B CA  
5299 C CA  B VAL   B 100 ? 0.3202 0.2583 0.2698 0.0209  0.0338  0.0824  100 VAL   B CA  
5300 C C   A VAL   B 100 ? 0.3396 0.2680 0.2670 0.0213  0.0467  0.1052  100 VAL   B C   
5301 C C   B VAL   B 100 ? 0.3394 0.2666 0.2660 0.0259  0.0328  0.0994  100 VAL   B C   
5302 O O   A VAL   B 100 ? 0.3452 0.2777 0.2655 0.0205  0.0526  0.0978  100 VAL   B O   
5303 O O   B VAL   B 100 ? 0.3420 0.2715 0.2676 0.0246  0.0335  0.0954  100 VAL   B O   
5304 C CB  A VAL   B 100 ? 0.3281 0.2790 0.3522 -0.0077 0.0443  0.0899  100 VAL   B CB  
5305 C CB  B VAL   B 100 ? 0.3263 0.2693 0.3127 0.0083  0.0284  0.0781  100 VAL   B CB  
5306 C CG1 A VAL   B 100 ? 0.3318 0.2830 0.3770 -0.0142 0.0418  0.0901  100 VAL   B CG1 
5307 C CG1 B VAL   B 100 ? 0.3286 0.2723 0.3276 0.0047  0.0259  0.0774  100 VAL   B CG1 
5308 C CG2 A VAL   B 100 ? 0.3319 0.2860 0.3684 -0.0113 0.0474  0.0958  100 VAL   B CG2 
5309 C CG2 B VAL   B 100 ? 0.3281 0.2726 0.3234 0.0048  0.0288  0.0796  100 VAL   B CG2 
5328 N N   . ASN   B 101 ? 0.3550 0.2720 0.2603 0.0335  0.0291  0.1151  101 ASN   B N   
5329 C CA  . ASN   B 101 ? 0.3971 0.2938 0.2950 0.0411  0.0110  0.1216  101 ASN   B CA  
5330 C C   . ASN   B 101 ? 0.4392 0.3369 0.3102 0.0378  -0.0006 0.1151  101 ASN   B C   
5331 O O   . ASN   B 101 ? 0.4441 0.3503 0.3256 0.0438  -0.0062 0.0957  101 ASN   B O   
5332 C CB  . ASN   B 101 ? 0.3993 0.2829 0.3102 0.0411  0.0167  0.1087  101 ASN   B CB  
5333 C CG  . ASN   B 101 ? 0.3981 0.2710 0.3157 0.0419  0.0201  0.1124  101 ASN   B CG  
5334 O OD1 . ASN   B 101 ? 0.4038 0.2732 0.3483 0.0354  0.0322  0.1057  101 ASN   B OD1 
5335 N ND2 . ASN   B 101 ? 0.3919 0.2685 0.3129 0.0448  0.0161  0.1039  101 ASN   B ND2 
5343 N N   A LYS   B 102 ? 0.4652 0.3576 0.3143 0.0297  0.0057  0.1142  102 LYS   B N   
5344 N N   B LYS   B 102 ? 0.4481 0.3552 0.3328 0.0306  0.0010  0.0939  102 LYS   B N   
5345 C CA  A LYS   B 102 ? 0.4898 0.3847 0.3368 0.0203  0.0157  0.1017  102 LYS   B CA  
5346 C CA  B LYS   B 102 ? 0.4552 0.3746 0.3638 0.0228  0.0053  0.0697  102 LYS   B CA  
5347 C C   A LYS   B 102 ? 0.4891 0.3862 0.3117 0.0230  0.0269  0.1129  102 LYS   B C   
5348 C C   B LYS   B 102 ? 0.4488 0.3738 0.3547 0.0207  0.0091  0.0643  102 LYS   B C   
5349 O O   A LYS   B 102 ? 0.4959 0.3899 0.3118 0.0237  0.0207  0.1119  102 LYS   B O   
5350 O O   B LYS   B 102 ? 0.4517 0.3760 0.3552 0.0209  0.0079  0.0627  102 LYS   B O   
5351 C CB  A LYS   B 102 ? 0.5116 0.4086 0.3936 0.0106  0.0216  0.0698  102 LYS   B CB  
5352 C CB  B LYS   B 102 ? 0.4665 0.3928 0.4030 0.0177  0.0090  0.0485  102 LYS   B CB  
5353 C CG  A LYS   B 102 ? 0.5286 0.4286 0.4578 0.0039  0.0268  0.0348  102 LYS   B CG  
5354 C CG  B LYS   B 102 ? 0.4753 0.4081 0.4444 0.0138  0.0129  0.0273  102 LYS   B CG  
5355 C CD  A LYS   B 102 ? 0.5420 0.4439 0.5138 -0.0024 0.0310  0.0062  102 LYS   B CD  
5356 C CD  B LYS   B 102 ? 0.4821 0.4198 0.4799 0.0101  0.0157  0.0106  102 LYS   B CD  
5357 C CE  A LYS   B 102 ? 0.5499 0.4542 0.5592 -0.0081 0.0354  -0.0117 102 LYS   B CE  
5358 C CE  B LYS   B 102 ? 0.4862 0.4277 0.5079 0.0071  0.0184  -0.0004 102 LYS   B CE  
5359 N NZ  A LYS   B 102 ? 0.5544 0.4605 0.5855 -0.0115 0.0383  -0.0202 102 LYS   B NZ  
5360 N NZ  B LYS   B 102 ? 0.4883 0.4324 0.5238 0.0056  0.0202  -0.0057 102 LYS   B NZ  
5387 N N   A GLY   B 103 ? 0.4778 0.3823 0.2920 0.0238  0.0485  0.1196  103 GLY   B N   
5388 N N   B GLY   B 103 ? 0.4374 0.3688 0.3477 0.0177  0.0156  0.0604  103 GLY   B N   
5389 C CA  A GLY   B 103 ? 0.4642 0.3777 0.3011 0.0248  0.0705  0.1130  103 GLY   B CA  
5390 C CA  B GLY   B 103 ? 0.4251 0.3623 0.3454 0.0137  0.0219  0.0533  103 GLY   B CA  
5391 C C   A GLY   B 103 ? 0.4455 0.3682 0.2983 0.0218  0.0922  0.1016  103 GLY   B C   
5392 C C   B GLY   B 103 ? 0.4108 0.3538 0.3396 0.0075  0.0277  0.0442  103 GLY   B C   
5393 O O   A GLY   B 103 ? 0.4517 0.3764 0.3127 0.0186  0.0876  0.0977  103 GLY   B O   
5394 O O   B GLY   B 103 ? 0.4126 0.3569 0.3461 0.0079  0.0272  0.0428  103 GLY   B O   
5401 N N   A GLU   B 104 ? 0.4187 0.3473 0.2821 0.0224  0.1126  0.0847  104 GLU   B N   
5402 N N   B GLU   B 104 ? 0.3943 0.3405 0.3241 -0.0001 0.0309  0.0339  104 GLU   B N   
5403 C CA  A GLU   B 104 ? 0.3925 0.3280 0.2657 0.0259  0.1207  0.0613  104 GLU   B CA  
5404 C CA  B GLU   B 104 ? 0.3781 0.3282 0.3077 -0.0075 0.0314  0.0236  104 GLU   B CA  
5405 C C   A GLU   B 104 ? 0.3951 0.3279 0.2823 0.0116  0.1441  0.0499  104 GLU   B C   
5406 C C   B GLU   B 104 ? 0.3724 0.3247 0.3093 -0.0127 0.0454  0.0167  104 GLU   B C   
5407 O O   A GLU   B 104 ? 0.3944 0.3256 0.3087 0.0098  0.1410  0.0410  104 GLU   B O   
5408 O O   B GLU   B 104 ? 0.3711 0.3227 0.3138 -0.0128 0.0463  0.0133  104 GLU   B O   
5409 C CB  A GLU   B 104 ? 0.3679 0.3094 0.2501 0.0428  0.0895  0.0405  104 GLU   B CB  
5410 C CB  B GLU   B 104 ? 0.3691 0.3190 0.2931 -0.0111 0.0160  0.0179  104 GLU   B CB  
5411 C CG  A GLU   B 104 ? 0.3469 0.2956 0.2338 0.0567  0.0501  0.0095  104 GLU   B CG  
5412 C CG  B GLU   B 104 ? 0.3620 0.3107 0.2792 -0.0150 0.0000  0.0093  104 GLU   B CG  
5413 C CD  A GLU   B 104 ? 0.3279 0.2797 0.2131 0.0666  0.0178  -0.0052 104 GLU   B CD  
5414 C CD  B GLU   B 104 ? 0.3565 0.3020 0.2683 -0.0209 -0.0116 0.0050  104 GLU   B CD  
5415 O OE1 A GLU   B 104 ? 0.3026 0.2620 0.1813 0.0783  0.0270  -0.0010 104 GLU   B OE1 
5416 O OE1 B GLU   B 104 ? 0.3515 0.2960 0.2630 -0.0261 -0.0110 0.0062  104 GLU   B OE1 
5417 O OE2 A GLU   B 104 ? 0.3324 0.2900 0.2222 0.0622  -0.0130 -0.0215 104 GLU   B OE2 
5418 O OE2 B GLU   B 104 ? 0.3562 0.3025 0.2649 -0.0222 -0.0214 0.0008  104 GLU   B OE2 
5431 N N   A ASP   B 105 ? 0.3956 0.3331 0.2871 -0.0046 0.1659  0.0512  105 ASP   B N   
5432 N N   B ASP   B 105 ? 0.3676 0.3250 0.3120 -0.0189 0.0589  0.0149  105 ASP   B N   
5433 C CA  A ASP   B 105 ? 0.3979 0.3353 0.3086 -0.0178 0.1840  0.0364  105 ASP   B CA  
5434 C CA  B ASP   B 105 ? 0.3645 0.3248 0.3199 -0.0236 0.0699  0.0096  105 ASP   B CA  
5435 C C   A ASP   B 105 ? 0.3799 0.3028 0.2807 -0.0296 0.1820  0.0265  105 ASP   B C   
5436 C C   B ASP   B 105 ? 0.3555 0.3145 0.3015 -0.0247 0.0692  0.0020  105 ASP   B C   
5437 O O   A ASP   B 105 ? 0.3681 0.2935 0.2703 -0.0291 0.1787  0.0231  105 ASP   B O   
5438 O O   B ASP   B 105 ? 0.3517 0.3107 0.2906 -0.0259 0.0707  -0.0015 105 ASP   B O   
5439 C CB  A ASP   B 105 ? 0.4153 0.3636 0.3798 -0.0097 0.1887  0.0179  105 ASP   B CB  
5440 C CB  B ASP   B 105 ? 0.3679 0.3328 0.3499 -0.0239 0.0797  0.0097  105 ASP   B CB  
5441 C CG  A ASP   B 105 ? 0.4235 0.3800 0.4410 -0.0061 0.1943  0.0070  105 ASP   B CG  
5442 C CG  B ASP   B 105 ? 0.3684 0.3359 0.3727 -0.0259 0.0882  0.0128  105 ASP   B CG  
5443 O OD1 A ASP   B 105 ? 0.4223 0.3858 0.4484 -0.0124 0.2063  0.0134  105 ASP   B OD1 
5444 O OD1 B ASP   B 105 ? 0.3679 0.3369 0.3793 -0.0293 0.0914  0.0151  105 ASP   B OD1 
5445 O OD2 A ASP   B 105 ? 0.4292 0.3860 0.4864 0.0008  0.1799  -0.0060 105 ASP   B OD2 
5446 O OD2 B ASP   B 105 ? 0.3662 0.3369 0.3792 -0.0279 0.0951  0.0166  105 ASP   B OD2 
5455 N N   A ILE   B 106 ? 0.3706 0.2785 0.2919 -0.0333 0.1644  0.0228  106 ILE   B N   
5456 N N   B ILE   B 106 ? 0.3497 0.3078 0.2994 -0.0219 0.0638  -0.0012 106 ILE   B N   
5457 C CA  A ILE   B 106 ? 0.3516 0.2502 0.3028 -0.0450 0.1687  0.0171  106 ILE   B CA  
5458 C CA  B ILE   B 106 ? 0.3410 0.3012 0.3018 -0.0202 0.0642  -0.0058 106 ILE   B CA  
5459 C C   A ILE   B 106 ? 0.3160 0.2451 0.2885 -0.0454 0.1686  -0.0001 106 ILE   B C   
5460 C C   B ILE   B 106 ? 0.3242 0.2997 0.2992 -0.0180 0.0620  -0.0142 106 ILE   B C   
5461 O O   A ILE   B 106 ? 0.3079 0.2226 0.2864 -0.0464 0.1563  -0.0127 106 ILE   B O   
5462 O O   B ILE   B 106 ? 0.3215 0.2949 0.2940 -0.0196 0.0553  -0.0191 106 ILE   B O   
5463 C CB  A ILE   B 106 ? 0.3728 0.2412 0.3297 -0.0523 0.1563  0.0257  106 ILE   B CB  
5464 C CB  B ILE   B 106 ? 0.3499 0.3000 0.3076 -0.0208 0.0638  -0.0021 106 ILE   B CB  
5465 C CG1 A ILE   B 106 ? 0.3829 0.2418 0.3418 -0.0440 0.1448  0.0204  106 ILE   B CG1 
5466 C CG1 B ILE   B 106 ? 0.3542 0.2999 0.3101 -0.0177 0.0613  -0.0003 106 ILE   B CG1 
5467 C CG2 A ILE   B 106 ? 0.3776 0.2433 0.3512 -0.0600 0.1577  0.0293  106 ILE   B CG2 
5468 C CG2 B ILE   B 106 ? 0.3524 0.3016 0.3144 -0.0223 0.0651  -0.0019 106 ILE   B CG2 
5469 C CD1 A ILE   B 106 ? 0.3884 0.2466 0.3418 -0.0358 0.1433  0.0186  106 ILE   B CD1 
5470 C CD1 B ILE   B 106 ? 0.3567 0.3009 0.3109 -0.0148 0.0610  0.0014  106 ILE   B CD1 
5493 N N   A GLN   B 107 ? 0.3012 0.2724 0.3062 -0.0404 0.1522  -0.0048 107 GLN   B N   
5494 N N   B GLN   B 107 ? 0.3116 0.3050 0.3103 -0.0148 0.0622  -0.0162 107 GLN   B N   
5495 C CA  A GLN   B 107 ? 0.2848 0.2939 0.3321 -0.0343 0.1322  -0.0010 107 GLN   B CA  
5496 C CA  B GLN   B 107 ? 0.2982 0.3075 0.3265 -0.0106 0.0621  -0.0132 107 GLN   B CA  
5497 C C   A GLN   B 107 ? 0.2576 0.2751 0.3105 -0.0146 0.0956  -0.0108 107 GLN   B C   
5498 C C   B GLN   B 107 ? 0.2679 0.2851 0.2996 -0.0035 0.0655  -0.0160 107 GLN   B C   
5499 O O   A GLN   B 107 ? 0.2524 0.2731 0.3391 -0.0026 0.0730  -0.0204 107 GLN   B O   
5500 O O   B GLN   B 107 ? 0.2677 0.2874 0.3082 -0.0004 0.0570  -0.0213 107 GLN   B O   
5501 C CB  A GLN   B 107 ? 0.3091 0.3345 0.4023 -0.0377 0.1239  0.0073  107 GLN   B CB  
5502 C CB  B GLN   B 107 ? 0.3175 0.3302 0.3761 -0.0114 0.0538  -0.0084 107 GLN   B CB  
5503 C CG  A GLN   B 107 ? 0.3397 0.3708 0.4800 -0.0301 0.0902  0.0100  107 GLN   B CG  
5504 C CG  B GLN   B 107 ? 0.3360 0.3495 0.4269 -0.0090 0.0405  -0.0043 107 GLN   B CG  
5505 C CD  A GLN   B 107 ? 0.3615 0.3941 0.5391 -0.0245 0.0665  0.0144  107 GLN   B CD  
5506 C CD  B GLN   B 107 ? 0.3502 0.3632 0.4673 -0.0069 0.0301  -0.0003 107 GLN   B CD  
5507 O OE1 A GLN   B 107 ? 0.3683 0.4046 0.5627 -0.0164 0.0634  0.0136  107 GLN   B OE1 
5508 O OE1 B GLN   B 107 ? 0.3556 0.3685 0.4835 -0.0043 0.0295  0.0003  107 GLN   B OE1 
5509 N NE2 A GLN   B 107 ? 0.3716 0.4040 0.5597 -0.0230 0.0566  0.0197  107 GLN   B NE2 
5510 N NE2 B GLN   B 107 ? 0.3558 0.3674 0.4809 -0.0061 0.0259  0.0030  107 GLN   B NE2 
5527 N N   . LEU   B 108 ? 0.2373 0.2589 0.2716 0.0049  0.0769  -0.0132 108 LEU   B N   
5528 C CA  . LEU   B 108 ? 0.2219 0.2313 0.2373 0.0228  0.0531  0.0025  108 LEU   B CA  
5529 C C   . LEU   B 108 ? 0.1941 0.1916 0.2196 0.0243  0.0351  0.0202  108 LEU   B C   
5530 O O   . LEU   B 108 ? 0.1981 0.1815 0.2198 0.0221  0.0249  0.0180  108 LEU   B O   
5531 C CB  . LEU   B 108 ? 0.2417 0.2517 0.2210 0.0184  0.0476  0.0070  108 LEU   B CB  
5532 C CG  . LEU   B 108 ? 0.2609 0.2791 0.2229 0.0182  0.0414  -0.0135 108 LEU   B CG  
5533 C CD1 . LEU   B 108 ? 0.2688 0.2926 0.2131 0.0056  0.0439  -0.0097 108 LEU   B CD1 
5534 C CD2 . LEU   B 108 ? 0.2772 0.2898 0.2354 0.0275  0.0333  -0.0252 108 LEU   B CD2 
5547 N N   . LEU   B 109 ? 0.1848 0.1750 0.2166 0.0200  0.0355  0.0217  109 LEU   B N   
5548 C CA  . LEU   B 109 ? 0.1677 0.1498 0.2229 0.0138  0.0287  0.0273  109 LEU   B CA  
5549 C C   . LEU   B 109 ? 0.1530 0.1355 0.2260 0.0060  0.0334  0.0175  109 LEU   B C   
5550 O O   . LEU   B 109 ? 0.1503 0.1376 0.2210 0.0044  0.0264  0.0314  109 LEU   B O   
5551 C CB  . LEU   B 109 ? 0.1763 0.1420 0.2201 0.0058  0.0219  0.0322  109 LEU   B CB  
5552 C CG  . LEU   B 109 ? 0.1716 0.1385 0.2180 0.0073  0.0149  0.0150  109 LEU   B CG  
5553 C CD1 . LEU   B 109 ? 0.1674 0.1539 0.2166 0.0109  0.0193  0.0184  109 LEU   B CD1 
5554 C CD2 . LEU   B 109 ? 0.1838 0.1451 0.2344 0.0054  0.0073  0.0155  109 LEU   B CD2 
5566 N N   . LYS   B 110 ? 0.1508 0.1402 0.2192 -0.0032 0.0316  0.0275  110 LYS   B N   
5567 C CA  . LYS   B 110 ? 0.1510 0.1354 0.2186 -0.0002 0.0227  0.0183  110 LYS   B CA  
5568 C C   . LYS   B 110 ? 0.1485 0.1384 0.2098 -0.0009 0.0239  0.0105  110 LYS   B C   
5569 O O   . LYS   B 110 ? 0.1456 0.1405 0.1955 -0.0053 0.0165  0.0067  110 LYS   B O   
5570 C CB  . LYS   B 110 ? 0.1544 0.1360 0.2455 -0.0046 0.0263  0.0125  110 LYS   B CB  
5571 C CG  . LYS   B 110 ? 0.1541 0.1411 0.2508 -0.0073 0.0102  0.0152  110 LYS   B CG  
5572 C CD  . LYS   B 110 ? 0.1577 0.1442 0.2653 -0.0051 0.0125  0.0188  110 LYS   B CD  
5573 C CE  . LYS   B 110 ? 0.1536 0.1543 0.2770 -0.0021 0.0142  0.0092  110 LYS   B CE  
5574 N NZ  . LYS   B 110 ? 0.1515 0.1683 0.2724 0.0018  -0.0002 0.0030  110 LYS   B NZ  
5588 N N   . SER   B 111 ? 0.1484 0.1413 0.2198 -0.0040 0.0285  0.0183  111 SER   B N   
5589 C CA  . SER   B 111 ? 0.1529 0.1456 0.2052 0.0034  0.0197  0.0200  111 SER   B CA  
5590 C C   . SER   B 111 ? 0.1528 0.1389 0.1987 0.0031  0.0113  0.0118  111 SER   B C   
5591 O O   . SER   B 111 ? 0.1509 0.1419 0.2035 0.0001  0.0076  0.0109  111 SER   B O   
5592 C CB  . SER   B 111 ? 0.1685 0.1709 0.2106 0.0054  0.0300  0.0297  111 SER   B CB  
5593 O OG  . SER   B 111 ? 0.1884 0.2032 0.2301 0.0092  0.0442  0.0319  111 SER   B OG  
5599 N N   . ALA   B 112 ? 0.1449 0.1408 0.2062 0.0037  0.0163  0.0163  112 ALA   B N   
5600 C CA  . ALA   B 112 ? 0.1416 0.1451 0.1933 0.0000  0.0032  0.0060  112 ALA   B CA  
5601 C C   . ALA   B 112 ? 0.1337 0.1359 0.1817 -0.0002 0.0044  0.0064  112 ALA   B C   
5602 O O   . ALA   B 112 ? 0.1316 0.1357 0.2021 -0.0042 0.0093  0.0016  112 ALA   B O   
5603 C CB  . ALA   B 112 ? 0.1461 0.1497 0.2161 0.0050  0.0024  0.0125  112 ALA   B CB  
5609 N N   . TYR   B 113 ? 0.1361 0.1282 0.1881 -0.0020 -0.0008 0.0082  113 TYR   B N   
5610 C CA  . TYR   B 113 ? 0.1318 0.1264 0.1883 -0.0037 0.0018  0.0052  113 TYR   B CA  
5611 C C   . TYR   B 113 ? 0.1271 0.1240 0.1963 -0.0108 0.0028  0.0076  113 TYR   B C   
5612 O O   . TYR   B 113 ? 0.1333 0.1251 0.1841 -0.0069 -0.0021 -0.0035 113 TYR   B O   
5613 C CB  . TYR   B 113 ? 0.1377 0.1219 0.1957 -0.0027 0.0143  0.0157  113 TYR   B CB  
5614 C CG  . TYR   B 113 ? 0.1420 0.1271 0.1926 -0.0080 0.0071  0.0106  113 TYR   B CG  
5615 C CD1 . TYR   B 113 ? 0.1447 0.1220 0.2057 -0.0070 0.0103  0.0145  113 TYR   B CD1 
5616 C CD2 . TYR   B 113 ? 0.1500 0.1264 0.1970 -0.0036 0.0071  0.0104  113 TYR   B CD2 
5617 C CE1 . TYR   B 113 ? 0.1447 0.1353 0.2052 -0.0021 0.0123  0.0087  113 TYR   B CE1 
5618 C CE2 . TYR   B 113 ? 0.1524 0.1180 0.2128 -0.0024 0.0070  0.0135  113 TYR   B CE2 
5619 C CZ  . TYR   B 113 ? 0.1434 0.1260 0.2073 0.0065  0.0081  0.0066  113 TYR   B CZ  
5620 O OH  . TYR   B 113 ? 0.1501 0.1250 0.2335 0.0089  0.0115  0.0075  113 TYR   B OH  
5630 N N   . GLU   B 114 ? 0.1305 0.1188 0.1984 -0.0027 0.0069  0.0054  114 GLU   B N   
5631 C CA  . GLU   B 114 ? 0.1285 0.1187 0.1988 0.0030  0.0067  0.0051  114 GLU   B CA  
5632 C C   . GLU   B 114 ? 0.1272 0.1194 0.1994 0.0013  0.0059  0.0011  114 GLU   B C   
5633 O O   . GLU   B 114 ? 0.1268 0.1220 0.2089 0.0012  -0.0002 0.0099  114 GLU   B O   
5634 C CB  . GLU   B 114 ? 0.1287 0.1274 0.2037 0.0019  0.0053  0.0048  114 GLU   B CB  
5635 C CG  . GLU   B 114 ? 0.1384 0.1260 0.2024 -0.0017 0.0060  0.0079  114 GLU   B CG  
5636 C CD  . GLU   B 114 ? 0.1337 0.1318 0.2114 -0.0074 0.0063  0.0061  114 GLU   B CD  
5637 O OE1 . GLU   B 114 ? 0.1339 0.1502 0.2096 -0.0087 0.0173  0.0112  114 GLU   B OE1 
5638 O OE2 . GLU   B 114 ? 0.1336 0.1505 0.2229 -0.0187 0.0053  0.0079  114 GLU   B OE2 
5645 N N   . ASN   B 115 ? 0.1327 0.1174 0.1855 -0.0041 -0.0005 0.0055  115 ASN   B N   
5646 C CA  . ASN   B 115 ? 0.1311 0.1271 0.1739 -0.0085 0.0087  0.0043  115 ASN   B CA  
5647 C C   . ASN   B 115 ? 0.1238 0.1222 0.1762 -0.0103 -0.0004 0.0038  115 ASN   B C   
5648 O O   . ASN   B 115 ? 0.1373 0.1278 0.1811 -0.0133 0.0004  0.0055  115 ASN   B O   
5649 C CB  . ASN   B 115 ? 0.1413 0.1345 0.1838 -0.0078 0.0103  0.0027  115 ASN   B CB  
5650 C CG  . ASN   B 115 ? 0.1527 0.1420 0.1799 0.0040  0.0031  0.0003  115 ASN   B CG  
5651 O OD1 . ASN   B 115 ? 0.1978 0.1551 0.1971 0.0014  0.0143  -0.0112 115 ASN   B OD1 
5652 N ND2 . ASN   B 115 ? 0.1511 0.1506 0.1774 -0.0040 0.0022  0.0032  115 ASN   B ND2 
5659 N N   . PHE   B 116 ? 0.1279 0.1216 0.1657 -0.0051 -0.0012 0.0006  116 PHE   B N   
5660 C CA  . PHE   B 116 ? 0.1334 0.1245 0.1712 -0.0099 -0.0030 0.0042  116 PHE   B CA  
5661 C C   . PHE   B 116 ? 0.1334 0.1126 0.1786 -0.0124 -0.0019 0.0037  116 PHE   B C   
5662 O O   . PHE   B 116 ? 0.1374 0.1234 0.1792 -0.0027 -0.0035 0.0047  116 PHE   B O   
5663 C CB  . PHE   B 116 ? 0.1326 0.1223 0.1714 -0.0046 -0.0076 0.0081  116 PHE   B CB  
5664 C CG  . PHE   B 116 ? 0.1288 0.1244 0.1712 -0.0066 -0.0080 0.0016  116 PHE   B CG  
5665 C CD1 . PHE   B 116 ? 0.1370 0.1290 0.1851 -0.0047 -0.0042 0.0038  116 PHE   B CD1 
5666 C CD2 . PHE   B 116 ? 0.1334 0.1320 0.1675 -0.0045 -0.0031 -0.0025 116 PHE   B CD2 
5667 C CE1 . PHE   B 116 ? 0.1380 0.1347 0.1882 -0.0039 -0.0138 0.0051  116 PHE   B CE1 
5668 C CE2 . PHE   B 116 ? 0.1335 0.1303 0.1748 -0.0024 -0.0031 0.0043  116 PHE   B CE2 
5669 C CZ  . PHE   B 116 ? 0.1306 0.1318 0.1796 -0.0055 -0.0100 0.0076  116 PHE   B CZ  
5679 N N   . ASN   B 117 ? 0.1316 0.1181 0.1880 -0.0068 -0.0093 0.0046  117 ASN   B N   
5680 C CA  . ASN   B 117 ? 0.1387 0.1210 0.1908 -0.0004 -0.0074 -0.0019 117 ASN   B CA  
5681 C C   . ASN   B 117 ? 0.1392 0.1209 0.1999 0.0050  -0.0076 0.0004  117 ASN   B C   
5682 O O   . ASN   B 117 ? 0.1505 0.1315 0.2179 -0.0044 -0.0278 0.0079  117 ASN   B O   
5683 C CB  . ASN   B 117 ? 0.1397 0.1266 0.1925 0.0002  -0.0115 -0.0061 117 ASN   B CB  
5684 C CG  . ASN   B 117 ? 0.1344 0.1297 0.2061 0.0024  -0.0085 -0.0099 117 ASN   B CG  
5685 O OD1 . ASN   B 117 ? 0.1589 0.1302 0.2117 -0.0121 -0.0035 -0.0003 117 ASN   B OD1 
5686 N ND2 . ASN   B 117 ? 0.1388 0.1331 0.1953 -0.0030 -0.0006 -0.0072 117 ASN   B ND2 
5693 N N   . GLN   B 118 ? 0.1409 0.1193 0.1929 -0.0035 -0.0183 -0.0016 118 GLN   B N   
5694 C CA  . GLN   B 118 ? 0.1438 0.1221 0.1985 0.0019  -0.0153 0.0016  118 GLN   B CA  
5695 C C   . GLN   B 118 ? 0.1482 0.1242 0.2064 -0.0020 -0.0099 -0.0058 118 GLN   B C   
5696 O O   . GLN   B 118 ? 0.1685 0.1227 0.2388 -0.0095 0.0015  0.0035  118 GLN   B O   
5697 C CB  . GLN   B 118 ? 0.1555 0.1311 0.2069 0.0004  -0.0125 -0.0082 118 GLN   B CB  
5698 C CG  . GLN   B 118 ? 0.1627 0.1289 0.2058 0.0061  -0.0097 -0.0083 118 GLN   B CG  
5699 C CD  . GLN   B 118 ? 0.1634 0.1279 0.2022 0.0008  -0.0081 -0.0121 118 GLN   B CD  
5700 O OE1 . GLN   B 118 ? 0.1737 0.1265 0.2242 0.0038  0.0016  0.0028  118 GLN   B OE1 
5701 N NE2 . GLN   B 118 ? 0.1694 0.1250 0.2185 0.0024  -0.0095 0.0000  118 GLN   B NE2 
5710 N N   . HIS   B 119 ? 0.1514 0.1304 0.1593 -0.0091 -0.0061 0.0064  119 HIS   B N   
5711 C CA  . HIS   B 119 ? 0.1622 0.1386 0.1600 -0.0009 -0.0140 0.0082  119 HIS   B CA  
5712 C C   . HIS   B 119 ? 0.1669 0.1376 0.1693 -0.0050 -0.0267 0.0122  119 HIS   B C   
5713 O O   . HIS   B 119 ? 0.1708 0.1354 0.1880 -0.0208 -0.0205 0.0078  119 HIS   B O   
5714 C CB  . HIS   B 119 ? 0.1623 0.1520 0.1733 -0.0031 -0.0177 -0.0026 119 HIS   B CB  
5715 C CG  . HIS   B 119 ? 0.1697 0.1769 0.1950 0.0092  -0.0389 -0.0209 119 HIS   B CG  
5716 N ND1 . HIS   B 119 ? 0.1824 0.1897 0.2277 0.0010  -0.0494 -0.0404 119 HIS   B ND1 
5717 C CD2 . HIS   B 119 ? 0.1849 0.1936 0.2005 0.0363  -0.0493 -0.0276 119 HIS   B CD2 
5718 C CE1 . HIS   B 119 ? 0.2014 0.2010 0.2310 0.0158  -0.0535 -0.0548 119 HIS   B CE1 
5719 N NE2 . HIS   B 119 ? 0.2039 0.2144 0.2178 0.0318  -0.0513 -0.0450 119 HIS   B NE2 
5727 N N   . GLU   B 120 ? 0.1776 0.1383 0.1744 -0.0112 -0.0384 0.0136  120 GLU   B N   
5728 C CA  . GLU   B 120 ? 0.2048 0.1513 0.1922 -0.0057 -0.0469 0.0257  120 GLU   B CA  
5729 C C   . GLU   B 120 ? 0.1850 0.1446 0.1693 -0.0134 -0.0371 0.0294  120 GLU   B C   
5730 O O   . GLU   B 120 ? 0.1802 0.1550 0.1700 -0.0161 -0.0358 0.0167  120 GLU   B O   
5731 C CB  . GLU   B 120 ? 0.2660 0.1807 0.2573 0.0143  -0.0756 0.0413  120 GLU   B CB  
5732 C CG  . GLU   B 120 ? 0.3178 0.2446 0.3523 0.0249  -0.0953 0.0589  120 GLU   B CG  
5733 C CD  . GLU   B 120 ? 0.3574 0.3063 0.4478 0.0214  -0.0974 0.0731  120 GLU   B CD  
5734 O OE1 . GLU   B 120 ? 0.3818 0.3352 0.4856 0.0134  -0.0884 0.0854  120 GLU   B OE1 
5735 O OE2 . GLU   B 120 ? 0.3741 0.3490 0.5018 0.0183  -0.0980 0.0655  120 GLU   B OE2 
5742 N N   . VAL   B 121 ? 0.1738 0.1402 0.1618 -0.0164 -0.0230 0.0196  121 VAL   B N   
5743 C CA  . VAL   B 121 ? 0.1685 0.1474 0.1479 -0.0166 -0.0225 0.0161  121 VAL   B CA  
5744 C C   . VAL   B 121 ? 0.1613 0.1420 0.1496 -0.0232 -0.0183 0.0168  121 VAL   B C   
5745 O O   . VAL   B 121 ? 0.1720 0.1410 0.1687 -0.0316 -0.0277 0.0082  121 VAL   B O   
5746 C CB  . VAL   B 121 ? 0.1894 0.1867 0.1480 -0.0025 -0.0316 0.0223  121 VAL   B CB  
5747 C CG1 . VAL   B 121 ? 0.1940 0.1981 0.1902 -0.0121 -0.0121 0.0153  121 VAL   B CG1 
5748 C CG2 . VAL   B 121 ? 0.2137 0.2100 0.1711 0.0061  -0.0232 0.0077  121 VAL   B CG2 
5758 N N   . LEU   B 122 ? 0.1523 0.1357 0.1516 -0.0157 -0.0309 0.0089  122 LEU   B N   
5759 C CA  . LEU   B 122 ? 0.1454 0.1392 0.1475 -0.0222 -0.0208 0.0117  122 LEU   B CA  
5760 C C   . LEU   B 122 ? 0.1500 0.1295 0.1541 -0.0274 -0.0232 0.0108  122 LEU   B C   
5761 O O   . LEU   B 122 ? 0.1629 0.1358 0.1784 -0.0277 -0.0318 0.0032  122 LEU   B O   
5762 C CB  . LEU   B 122 ? 0.1670 0.1503 0.1765 -0.0035 -0.0236 0.0118  122 LEU   B CB  
5763 C CG  . LEU   B 122 ? 0.1608 0.1544 0.1753 -0.0155 -0.0121 0.0057  122 LEU   B CG  
5764 C CD1 . LEU   B 122 ? 0.1644 0.1743 0.1903 -0.0141 -0.0196 0.0045  122 LEU   B CD1 
5765 C CD2 . LEU   B 122 ? 0.1587 0.1614 0.1593 -0.0095 -0.0008 -0.0049 122 LEU   B CD2 
5777 N N   . LEU   B 123 ? 0.1491 0.1225 0.1441 -0.0237 -0.0144 0.0080  123 LEU   B N   
5778 C CA  . LEU   B 123 ? 0.1538 0.1293 0.1421 -0.0173 -0.0230 -0.0004 123 LEU   B CA  
5779 C C   . LEU   B 123 ? 0.1508 0.1284 0.1360 -0.0217 -0.0214 -0.0041 123 LEU   B C   
5780 O O   . LEU   B 123 ? 0.1614 0.1294 0.1383 -0.0281 -0.0196 0.0002  123 LEU   B O   
5781 C CB  . LEU   B 123 ? 0.1572 0.1322 0.1483 -0.0199 -0.0157 -0.0000 123 LEU   B CB  
5782 C CG  . LEU   B 123 ? 0.1533 0.1378 0.1623 -0.0103 -0.0031 0.0099  123 LEU   B CG  
5783 C CD1 . LEU   B 123 ? 0.1569 0.1413 0.1720 -0.0133 -0.0043 -0.0078 123 LEU   B CD1 
5784 C CD2 . LEU   B 123 ? 0.1636 0.1424 0.1749 -0.0114 0.0014  0.0134  123 LEU   B CD2 
5796 N N   . ALA   B 124 ? 0.1466 0.1254 0.1324 -0.0216 -0.0104 -0.0035 124 ALA   B N   
5797 C CA  . ALA   B 124 ? 0.1381 0.1267 0.1525 -0.0182 -0.0123 -0.0093 124 ALA   B CA  
5798 C C   . ALA   B 124 ? 0.1355 0.1257 0.1516 -0.0172 -0.0088 0.0011  124 ALA   B C   
5799 O O   . ALA   B 124 ? 0.1502 0.1286 0.1539 -0.0134 -0.0138 -0.0007 124 ALA   B O   
5800 C CB  . ALA   B 124 ? 0.1458 0.1294 0.1714 -0.0125 -0.0000 -0.0014 124 ALA   B CB  
5806 N N   . PRO   B 125 ? 0.1470 0.1271 0.1444 -0.0151 -0.0119 0.0086  125 PRO   B N   
5807 C CA  . PRO   B 125 ? 0.1530 0.1325 0.1511 -0.0138 -0.0141 0.0176  125 PRO   B CA  
5808 C C   . PRO   B 125 ? 0.1504 0.1241 0.1726 -0.0115 -0.0123 0.0076  125 PRO   B C   
5809 O O   . PRO   B 125 ? 0.1524 0.1193 0.1923 -0.0107 -0.0055 0.0063  125 PRO   B O   
5810 C CB  . PRO   B 125 ? 0.1563 0.1548 0.1679 -0.0231 -0.0210 0.0291  125 PRO   B CB  
5811 C CG  . PRO   B 125 ? 0.1636 0.1590 0.1663 -0.0330 -0.0209 0.0202  125 PRO   B CG  
5812 C CD  . PRO   B 125 ? 0.1593 0.1410 0.1466 -0.0298 -0.0129 0.0099  125 PRO   B CD  
5820 N N   . LEU   B 126 ? 0.1518 0.1215 0.1877 -0.0111 0.0047  0.0134  126 LEU   B N   
5821 C CA  . LEU   B 126 ? 0.1563 0.1330 0.1963 -0.0122 0.0144  0.0124  126 LEU   B CA  
5822 C C   . LEU   B 126 ? 0.1506 0.1367 0.1977 -0.0017 0.0165  0.0181  126 LEU   B C   
5823 O O   . LEU   B 126 ? 0.1709 0.1625 0.2164 0.0146  -0.0078 -0.0039 126 LEU   B O   
5824 C CB  . LEU   B 126 ? 0.1734 0.1333 0.2211 -0.0135 0.0198  0.0095  126 LEU   B CB  
5825 C CG  . LEU   B 126 ? 0.1902 0.1422 0.2247 -0.0184 0.0236  -0.0075 126 LEU   B CG  
5826 C CD1 . LEU   B 126 ? 0.2020 0.1528 0.2651 -0.0214 0.0174  -0.0165 126 LEU   B CD1 
5827 C CD2 . LEU   B 126 ? 0.1942 0.1505 0.2383 -0.0254 0.0184  -0.0109 126 LEU   B CD2 
5839 N N   . LEU   B 127 ? 0.1489 0.1298 0.2041 0.0028  0.0186  0.0119  127 LEU   B N   
5840 C CA  . LEU   B 127 ? 0.1455 0.1345 0.2057 -0.0049 0.0212  0.0202  127 LEU   B CA  
5841 C C   . LEU   B 127 ? 0.1464 0.1327 0.2078 0.0004  0.0088  0.0182  127 LEU   B C   
5842 O O   . LEU   B 127 ? 0.1480 0.1390 0.2099 -0.0111 0.0053  0.0193  127 LEU   B O   
5843 C CB  . LEU   B 127 ? 0.1614 0.1357 0.2296 -0.0039 0.0199  0.0261  127 LEU   B CB  
5844 C CG  . LEU   B 127 ? 0.1747 0.1375 0.2356 0.0029  0.0157  0.0228  127 LEU   B CG  
5845 C CD1 . LEU   B 127 ? 0.1762 0.1360 0.2321 0.0081  0.0137  0.0083  127 LEU   B CD1 
5846 C CD2 . LEU   B 127 ? 0.1776 0.1471 0.2381 -0.0065 0.0151  0.0343  127 LEU   B CD2 
5858 N N   . SER   B 128 ? 0.1473 0.1346 0.2099 0.0011  -0.0026 0.0152  128 SER   B N   
5859 C CA  . SER   B 128 ? 0.1616 0.1421 0.2016 0.0068  -0.0055 0.0227  128 SER   B CA  
5860 C C   . SER   B 128 ? 0.1768 0.1476 0.2199 0.0068  -0.0212 0.0157  128 SER   B C   
5861 O O   . SER   B 128 ? 0.1936 0.1511 0.2442 0.0087  -0.0129 0.0302  128 SER   B O   
5862 C CB  . SER   B 128 ? 0.1748 0.1398 0.2002 0.0046  -0.0010 0.0348  128 SER   B CB  
5863 O OG  . SER   B 128 ? 0.1830 0.1580 0.2003 0.0062  0.0080  0.0402  128 SER   B OG  
5869 N N   . ALA   B 129 ? 0.1870 0.1495 0.2293 0.0248  -0.0193 0.0048  129 ALA   B N   
5870 C CA  . ALA   B 129 ? 0.2019 0.1590 0.2439 0.0268  -0.0202 -0.0056 129 ALA   B CA  
5871 C C   . ALA   B 129 ? 0.1890 0.1540 0.2293 0.0201  -0.0000 0.0031  129 ALA   B C   
5872 O O   . ALA   B 129 ? 0.1798 0.1546 0.2437 0.0159  -0.0048 0.0105  129 ALA   B O   
5873 C CB  . ALA   B 129 ? 0.2225 0.1845 0.2734 0.0287  -0.0140 -0.0163 129 ALA   B CB  
5879 N N   . GLY   B 130 ? 0.1844 0.1491 0.2297 0.0255  0.0134  0.0008  130 GLY   B N   
5880 C CA  . GLY   B 130 ? 0.1930 0.1636 0.2473 0.0259  0.0407  -0.0028 130 GLY   B CA  
5881 C C   . GLY   B 130 ? 0.1960 0.1628 0.2357 0.0194  0.0230  0.0075  130 GLY   B C   
5882 O O   . GLY   B 130 ? 0.2139 0.1738 0.2465 0.0180  0.0109  0.0199  130 GLY   B O   
5886 N N   . ILE   B 131 ? 0.1857 0.1735 0.2400 0.0337  0.0154  0.0014  131 ILE   B N   
5887 C CA  . ILE   B 131 ? 0.2054 0.1905 0.2424 0.0269  -0.0038 0.0218  131 ILE   B CA  
5888 C C   . ILE   B 131 ? 0.2171 0.1807 0.2173 0.0176  -0.0069 0.0300  131 ILE   B C   
5889 O O   . ILE   B 131 ? 0.2443 0.1961 0.2307 0.0230  -0.0164 0.0317  131 ILE   B O   
5890 C CB  . ILE   B 131 ? 0.2082 0.2323 0.2733 0.0196  -0.0084 0.0267  131 ILE   B CB  
5891 C CG1 . ILE   B 131 ? 0.2120 0.2507 0.2836 0.0001  0.0003  0.0289  131 ILE   B CG1 
5892 C CG2 . ILE   B 131 ? 0.2073 0.2524 0.2922 0.0220  -0.0095 0.0172  131 ILE   B CG2 
5893 C CD1 . ILE   B 131 ? 0.2255 0.2681 0.2966 -0.0127 -0.0098 0.0307  131 ILE   B CD1 
5905 N N   . PHE   B 132 ? 0.2004 0.1607 0.2086 0.0133  0.0070  0.0271  132 PHE   B N   
5906 C CA  . PHE   B 132 ? 0.2104 0.1654 0.2106 0.0067  0.0268  0.0145  132 PHE   B CA  
5907 C C   . PHE   B 132 ? 0.2286 0.1778 0.2293 0.0097  0.0383  0.0162  132 PHE   B C   
5908 O O   . PHE   B 132 ? 0.2482 0.1985 0.2512 0.0084  0.0504  0.0220  132 PHE   B O   
5909 C CB  . PHE   B 132 ? 0.1938 0.1624 0.1940 0.0092  0.0233  0.0183  132 PHE   B CB  
5910 C CG  . PHE   B 132 ? 0.1919 0.1682 0.1998 0.0159  0.0211  0.0139  132 PHE   B CG  
5911 C CD1 . PHE   B 132 ? 0.1968 0.1688 0.2292 0.0094  0.0269  0.0195  132 PHE   B CD1 
5912 C CD2 . PHE   B 132 ? 0.1912 0.1714 0.1846 0.0248  0.0202  0.0296  132 PHE   B CD2 
5913 C CE1 . PHE   B 132 ? 0.2026 0.1761 0.2382 0.0060  0.0269  0.0238  132 PHE   B CE1 
5914 C CE2 . PHE   B 132 ? 0.2003 0.1764 0.1883 0.0170  0.0202  0.0190  132 PHE   B CE2 
5915 C CZ  . PHE   B 132 ? 0.2054 0.1792 0.2291 0.0102  0.0080  0.0340  132 PHE   B CZ  
5925 N N   . GLY   B 133 ? 0.2278 0.1683 0.2295 0.0091  0.0305  0.0304  133 GLY   B N   
5926 C CA  . GLY   B 133 ? 0.2343 0.1788 0.2350 -0.0148 0.0243  0.0372  133 GLY   B CA  
5927 C C   . GLY   B 133 ? 0.2358 0.1833 0.2312 -0.0250 0.0282  0.0372  133 GLY   B C   
5928 O O   . GLY   B 133 ? 0.2550 0.2009 0.2726 -0.0352 0.0256  0.0495  133 GLY   B O   
5932 N N   . ALA   B 134 ? 0.2224 0.1818 0.2195 -0.0287 0.0230  0.0240  134 ALA   B N   
5933 C CA  . ALA   B 134 ? 0.2185 0.1807 0.2320 -0.0201 0.0298  0.0098  134 ALA   B CA  
5934 C C   . ALA   B 134 ? 0.2233 0.1767 0.2312 -0.0148 0.0307  0.0237  134 ALA   B C   
5935 O O   . ALA   B 134 ? 0.2299 0.1992 0.2506 -0.0017 0.0245  0.0152  134 ALA   B O   
5936 C CB  . ALA   B 134 ? 0.2195 0.1797 0.2569 -0.0131 0.0212  0.0034  134 ALA   B CB  
5942 N N   . ASP   B 135 ? 0.2370 0.1683 0.2353 -0.0157 0.0191  0.0305  135 ASP   B N   
5943 C CA  . ASP   B 135 ? 0.2537 0.1618 0.2505 -0.0110 -0.0008 0.0342  135 ASP   B CA  
5944 C C   . ASP   B 135 ? 0.2313 0.1528 0.2409 -0.0030 -0.0000 0.0249  135 ASP   B C   
5945 O O   . ASP   B 135 ? 0.2235 0.1460 0.2510 -0.0055 0.0005  0.0294  135 ASP   B O   
5946 C CB  . ASP   B 135 ? 0.2847 0.1726 0.2715 -0.0284 -0.0050 0.0405  135 ASP   B CB  
5947 C CG  . ASP   B 135 ? 0.3131 0.1734 0.3050 -0.0439 -0.0042 0.0304  135 ASP   B CG  
5948 O OD1 . ASP   B 135 ? 0.3258 0.1600 0.3082 -0.0285 -0.0143 0.0221  135 ASP   B OD1 
5949 O OD2 . ASP   B 135 ? 0.3350 0.2091 0.3675 -0.0549 -0.0008 0.0124  135 ASP   B OD2 
5954 N N   . PRO   B 136 ? 0.2216 0.1582 0.2544 0.0151  -0.0107 0.0217  136 PRO   B N   
5955 C CA  . PRO   B 136 ? 0.2014 0.1515 0.2581 0.0118  -0.0063 0.0133  136 PRO   B CA  
5956 C C   . PRO   B 136 ? 0.1853 0.1395 0.2615 0.0132  -0.0024 0.0064  136 PRO   B C   
5957 O O   . PRO   B 136 ? 0.1698 0.1349 0.2586 0.0092  -0.0017 0.0104  136 PRO   B O   
5958 C CB  . PRO   B 136 ? 0.2058 0.1737 0.2647 0.0298  -0.0111 0.0028  136 PRO   B CB  
5959 C CG  . PRO   B 136 ? 0.2277 0.1799 0.2800 0.0335  -0.0110 0.0022  136 PRO   B CG  
5960 C CD  . PRO   B 136 ? 0.2296 0.1723 0.2756 0.0369  -0.0050 0.0111  136 PRO   B CD  
5968 N N   . ILE   B 137 ? 0.1982 0.1312 0.2657 0.0155  -0.0112 0.0063  137 ILE   B N   
5969 C CA  . ILE   B 137 ? 0.2062 0.1278 0.2814 -0.0041 -0.0034 0.0059  137 ILE   B CA  
5970 C C   . ILE   B 137 ? 0.1956 0.1376 0.2699 -0.0082 0.0016  0.0170  137 ILE   B C   
5971 O O   . ILE   B 137 ? 0.1835 0.1392 0.2596 -0.0126 0.0001  0.0110  137 ILE   B O   
5972 C CB  . ILE   B 137 ? 0.2347 0.1345 0.3248 -0.0042 -0.0040 0.0043  137 ILE   B CB  
5973 C CG1 . ILE   B 137 ? 0.2613 0.1493 0.3730 0.0043  0.0049  -0.0177 137 ILE   B CG1 
5974 C CG2 . ILE   B 137 ? 0.2407 0.1386 0.3405 -0.0296 -0.0038 0.0127  137 ILE   B CG2 
5975 C CD1 . ILE   B 137 ? 0.2838 0.1795 0.4104 0.0199  -0.0046 -0.0043 137 ILE   B CD1 
5987 N N   . HIS   B 138 ? 0.1978 0.1325 0.2685 -0.0048 0.0132  0.0115  138 HIS   B N   
5988 C CA  . HIS   B 138 ? 0.2072 0.1412 0.2627 -0.0025 0.0296  0.0143  138 HIS   B CA  
5989 C C   . HIS   B 138 ? 0.1907 0.1432 0.2527 -0.0039 0.0306  0.0227  138 HIS   B C   
5990 O O   . HIS   B 138 ? 0.1849 0.1473 0.2719 0.0000  0.0296  0.0334  138 HIS   B O   
5991 C CB  . HIS   B 138 ? 0.2298 0.1555 0.2753 -0.0062 0.0445  0.0097  138 HIS   B CB  
5992 C CG  . HIS   B 138 ? 0.2468 0.1722 0.2798 -0.0077 0.0546  0.0262  138 HIS   B CG  
5993 N ND1 . HIS   B 138 ? 0.2541 0.1909 0.2962 -0.0040 0.0626  0.0265  138 HIS   B ND1 
5994 C CD2 . HIS   B 138 ? 0.2583 0.1836 0.2746 -0.0111 0.0580  0.0177  138 HIS   B CD2 
5995 C CE1 . HIS   B 138 ? 0.2561 0.1933 0.2948 -0.0053 0.0590  0.0222  138 HIS   B CE1 
5996 N NE2 . HIS   B 138 ? 0.2630 0.1788 0.2824 -0.0027 0.0591  0.0096  138 HIS   B NE2 
6004 N N   . SER   B 139 ? 0.1858 0.1306 0.2474 0.0005  0.0241  0.0113  139 SER   B N   
6005 C CA  . SER   B 139 ? 0.1793 0.1225 0.2290 0.0003  0.0182  0.0052  139 SER   B CA  
6006 C C   . SER   B 139 ? 0.1539 0.1172 0.2290 -0.0046 0.0127  0.0045  139 SER   B C   
6007 O O   . SER   B 139 ? 0.1598 0.1228 0.2355 -0.0012 0.0007  0.0104  139 SER   B O   
6008 C CB  . SER   B 139 ? 0.1879 0.1258 0.2350 0.0062  0.0012  0.0095  139 SER   B CB  
6009 O OG  . SER   B 139 ? 0.1886 0.1280 0.2444 0.0022  -0.0129 0.0143  139 SER   B OG  
6015 N N   . LEU   B 140 ? 0.1601 0.1164 0.2241 -0.0058 0.0129  -0.0058 140 LEU   B N   
6016 C CA  . LEU   B 140 ? 0.1546 0.1214 0.2218 -0.0044 0.0096  0.0053  140 LEU   B CA  
6017 C C   . LEU   B 140 ? 0.1519 0.1220 0.2398 -0.0063 0.0026  -0.0007 140 LEU   B C   
6018 O O   . LEU   B 140 ? 0.1515 0.1314 0.2434 -0.0027 -0.0011 0.0033  140 LEU   B O   
6019 C CB  . LEU   B 140 ? 0.1528 0.1232 0.2338 -0.0102 0.0128  -0.0040 140 LEU   B CB  
6020 C CG  . LEU   B 140 ? 0.1651 0.1245 0.2323 -0.0097 -0.0004 0.0083  140 LEU   B CG  
6021 C CD1 . LEU   B 140 ? 0.1738 0.1401 0.2430 -0.0141 -0.0005 0.0055  140 LEU   B CD1 
6022 C CD2 . LEU   B 140 ? 0.1820 0.1324 0.2488 -0.0091 -0.0021 -0.0158 140 LEU   B CD2 
6034 N N   . ARG   B 141 ? 0.1451 0.1268 0.2511 -0.0088 0.0074  0.0010  141 ARG   B N   
6035 C CA  . ARG   B 141 ? 0.1493 0.1278 0.2885 -0.0121 0.0254  -0.0011 141 ARG   B CA  
6036 C C   . ARG   B 141 ? 0.1431 0.1298 0.2744 -0.0143 0.0110  0.0004  141 ARG   B C   
6037 O O   . ARG   B 141 ? 0.1519 0.1334 0.2764 -0.0150 -0.0024 -0.0132 141 ARG   B O   
6038 C CB  . ARG   B 141 ? 0.1622 0.1371 0.3264 -0.0152 0.0379  0.0005  141 ARG   B CB  
6039 C CG  . ARG   B 141 ? 0.2002 0.1614 0.3536 -0.0254 0.0402  0.0020  141 ARG   B CG  
6040 C CD  . ARG   B 141 ? 0.2441 0.1846 0.3571 -0.0166 0.0265  -0.0115 141 ARG   B CD  
6041 N NE  . ARG   B 141 ? 0.2662 0.1905 0.3518 -0.0327 0.0311  -0.0133 141 ARG   B NE  
6042 C CZ  . ARG   B 141 ? 0.2786 0.1725 0.3430 -0.0277 0.0450  -0.0243 141 ARG   B CZ  
6043 N NH1 . ARG   B 141 ? 0.2889 0.1603 0.3409 -0.0260 0.0457  -0.0324 141 ARG   B NH1 
6044 N NH2 . ARG   B 141 ? 0.2843 0.1847 0.3483 -0.0141 0.0401  -0.0150 141 ARG   B NH2 
6058 N N   . VAL   B 142 ? 0.1468 0.1259 0.2576 -0.0106 0.0110  -0.0041 142 VAL   B N   
6059 C CA  . VAL   B 142 ? 0.1476 0.1271 0.2541 -0.0070 0.0133  -0.0014 142 VAL   B CA  
6060 C C   . VAL   B 142 ? 0.1451 0.1249 0.2539 -0.0046 0.0076  -0.0026 142 VAL   B C   
6061 O O   . VAL   B 142 ? 0.1526 0.1199 0.2732 -0.0022 0.0136  -0.0050 142 VAL   B O   
6062 C CB  . VAL   B 142 ? 0.1608 0.1368 0.2523 -0.0008 0.0174  0.0085  142 VAL   B CB  
6063 C CG1 . VAL   B 142 ? 0.1595 0.1341 0.2479 0.0082  0.0175  0.0066  142 VAL   B CG1 
6064 C CG2 . VAL   B 142 ? 0.1831 0.1395 0.2571 -0.0005 0.0181  0.0118  142 VAL   B CG2 
6074 N N   . CYS   B 143 ? 0.1400 0.1269 0.2411 -0.0044 0.0028  0.0052  143 CYS   B N   
6075 C CA  . CYS   B 143 ? 0.1387 0.1245 0.2441 -0.0042 -0.0008 0.0026  143 CYS   B CA  
6076 C C   . CYS   B 143 ? 0.1356 0.1269 0.2386 -0.0054 0.0056  -0.0019 143 CYS   B C   
6077 O O   . CYS   B 143 ? 0.1409 0.1297 0.2359 -0.0054 -0.0059 -0.0020 143 CYS   B O   
6078 C CB  . CYS   B 143 ? 0.1510 0.1300 0.2420 -0.0117 -0.0016 0.0020  143 CYS   B CB  
6079 S SG  . CYS   B 143 ? 0.1472 0.1494 0.2251 -0.0063 0.0034  0.0061  143 CYS   B SG  
6085 N N   . VAL   B 144 ? 0.1429 0.1282 0.2460 -0.0050 0.0041  -0.0118 144 VAL   B N   
6086 C CA  . VAL   B 144 ? 0.1489 0.1332 0.2738 -0.0145 -0.0129 -0.0206 144 VAL   B CA  
6087 C C   . VAL   B 144 ? 0.1448 0.1379 0.2764 -0.0121 -0.0174 0.0002  144 VAL   B C   
6088 O O   . VAL   B 144 ? 0.1556 0.1609 0.2970 0.0014  -0.0151 0.0221  144 VAL   B O   
6089 C CB  . VAL   B 144 ? 0.1693 0.1519 0.3327 -0.0129 -0.0197 -0.0337 144 VAL   B CB  
6090 C CG1 . VAL   B 144 ? 0.1934 0.1950 0.3601 -0.0051 -0.0232 -0.0288 144 VAL   B CG1 
6091 C CG2 . VAL   B 144 ? 0.1876 0.1547 0.3207 -0.0028 -0.0329 -0.0442 144 VAL   B CG2 
6101 N N   . ASP   B 145 ? 0.1470 0.1318 0.2847 -0.0064 -0.0119 -0.0152 145 ASP   B N   
6102 C CA  . ASP   B 145 ? 0.1437 0.1399 0.3023 -0.0069 -0.0053 -0.0078 145 ASP   B CA  
6103 C C   . ASP   B 145 ? 0.1377 0.1451 0.2895 -0.0075 -0.0027 -0.0057 145 ASP   B C   
6104 O O   . ASP   B 145 ? 0.1418 0.1593 0.3404 -0.0105 0.0087  -0.0246 145 ASP   B O   
6105 C CB  . ASP   B 145 ? 0.1608 0.1488 0.3436 -0.0149 0.0134  0.0023  145 ASP   B CB  
6106 C CG  . ASP   B 145 ? 0.1752 0.1522 0.3857 -0.0279 0.0258  -0.0013 145 ASP   B CG  
6107 O OD1 . ASP   B 145 ? 0.1760 0.1566 0.3929 -0.0262 -0.0034 -0.0095 145 ASP   B OD1 
6108 O OD2 . ASP   B 145 ? 0.2047 0.1640 0.4323 -0.0315 0.0513  0.0011  145 ASP   B OD2 
6113 N N   . THR   B 146 ? 0.1325 0.1335 0.2503 -0.0059 -0.0043 0.0009  146 THR   B N   
6114 C CA  . THR   B 146 ? 0.1450 0.1295 0.2327 -0.0075 0.0064  -0.0011 146 THR   B CA  
6115 C C   . THR   B 146 ? 0.1432 0.1263 0.2278 -0.0084 0.0003  0.0022  146 THR   B C   
6116 O O   . THR   B 146 ? 0.1465 0.1266 0.2364 -0.0053 -0.0051 0.0013  146 THR   B O   
6117 C CB  . THR   B 146 ? 0.1500 0.1307 0.2344 -0.0048 0.0124  -0.0004 146 THR   B CB  
6118 O OG1 . THR   B 146 ? 0.1509 0.1284 0.2360 -0.0054 0.0120  0.0105  146 THR   B OG1 
6119 C CG2 . THR   B 146 ? 0.1557 0.1373 0.2295 -0.0016 0.0143  0.0020  146 THR   B CG2 
6127 N N   . VAL   B 147 ? 0.1482 0.1325 0.2105 -0.0067 0.0046  0.0004  147 VAL   B N   
6128 C CA  . VAL   B 147 ? 0.1489 0.1264 0.2103 -0.0130 -0.0069 -0.0033 147 VAL   B CA  
6129 C C   . VAL   B 147 ? 0.1419 0.1285 0.2214 -0.0189 -0.0139 -0.0081 147 VAL   B C   
6130 O O   . VAL   B 147 ? 0.1558 0.1427 0.2213 -0.0204 -0.0325 -0.0089 147 VAL   B O   
6131 C CB  . VAL   B 147 ? 0.1497 0.1404 0.2007 -0.0080 -0.0078 -0.0008 147 VAL   B CB  
6132 C CG1 . VAL   B 147 ? 0.1486 0.1550 0.1937 -0.0119 -0.0072 0.0039  147 VAL   B CG1 
6133 C CG2 . VAL   B 147 ? 0.1534 0.1395 0.1989 -0.0078 -0.0051 0.0069  147 VAL   B CG2 
6143 N N   . ARG   B 148 ? 0.1428 0.1306 0.2238 -0.0107 -0.0218 -0.0119 148 ARG   B N   
6144 C CA  . ARG   B 148 ? 0.1482 0.1414 0.2179 -0.0060 -0.0289 -0.0162 148 ARG   B CA  
6145 C C   . ARG   B 148 ? 0.1528 0.1529 0.2038 -0.0064 -0.0306 -0.0108 148 ARG   B C   
6146 O O   . ARG   B 148 ? 0.1733 0.1773 0.2083 -0.0221 -0.0397 -0.0035 148 ARG   B O   
6147 C CB  . ARG   B 148 ? 0.1508 0.1504 0.2235 0.0004  -0.0357 -0.0193 148 ARG   B CB  
6148 C CG  . ARG   B 148 ? 0.1533 0.1691 0.2384 -0.0111 -0.0340 -0.0333 148 ARG   B CG  
6149 C CD  . ARG   B 148 ? 0.1555 0.1816 0.2510 0.0057  -0.0356 -0.0345 148 ARG   B CD  
6150 N NE  . ARG   B 148 ? 0.1611 0.1720 0.2426 0.0193  -0.0415 -0.0383 148 ARG   B NE  
6151 C CZ  . ARG   B 148 ? 0.1546 0.1648 0.2192 0.0108  -0.0334 -0.0229 148 ARG   B CZ  
6152 N NH1 . ARG   B 148 ? 0.1539 0.1664 0.2148 -0.0009 -0.0155 -0.0197 148 ARG   B NH1 
6153 N NH2 . ARG   B 148 ? 0.1782 0.1520 0.2121 0.0150  -0.0214 -0.0091 148 ARG   B NH2 
6167 N N   . THR   B 149 ? 0.1570 0.1441 0.2001 -0.0101 -0.0235 -0.0022 149 THR   B N   
6168 C CA  . THR   B 149 ? 0.1640 0.1460 0.1963 -0.0124 -0.0286 0.0059  149 THR   B CA  
6169 C C   . THR   B 149 ? 0.1606 0.1400 0.1896 -0.0109 -0.0339 0.0080  149 THR   B C   
6170 O O   . THR   B 149 ? 0.1658 0.1421 0.1958 -0.0178 -0.0113 0.0026  149 THR   B O   
6171 C CB  . THR   B 149 ? 0.1670 0.1403 0.1986 -0.0165 -0.0283 -0.0027 149 THR   B CB  
6172 O OG1 . THR   B 149 ? 0.1662 0.1456 0.1932 -0.0231 -0.0335 -0.0021 149 THR   B OG1 
6173 C CG2 . THR   B 149 ? 0.1727 0.1423 0.2146 -0.0072 -0.0227 -0.0042 149 THR   B CG2 
6181 N N   . ASN   B 150 ? 0.1659 0.1389 0.1829 -0.0146 -0.0374 -0.0012 150 ASN   B N   
6182 C CA  . ASN   B 150 ? 0.1754 0.1512 0.1826 -0.0207 -0.0337 -0.0079 150 ASN   B CA  
6183 C C   . ASN   B 150 ? 0.1637 0.1444 0.1894 -0.0167 -0.0352 0.0015  150 ASN   B C   
6184 O O   . ASN   B 150 ? 0.1747 0.1440 0.2073 -0.0265 -0.0479 -0.0003 150 ASN   B O   
6185 C CB  . ASN   B 150 ? 0.1968 0.1908 0.1957 -0.0208 -0.0408 0.0128  150 ASN   B CB  
6186 C CG  . ASN   B 150 ? 0.2220 0.2328 0.2251 -0.0270 -0.0429 0.0292  150 ASN   B CG  
6187 O OD1 . ASN   B 150 ? 0.2327 0.2523 0.2389 -0.0370 -0.0590 0.0267  150 ASN   B OD1 
6188 N ND2 . ASN   B 150 ? 0.2340 0.2489 0.2497 -0.0171 -0.0527 0.0618  150 ASN   B ND2 
6195 N N   . VAL   B 151 ? 0.1574 0.1396 0.1876 -0.0160 -0.0340 0.0020  151 VAL   B N   
6196 C CA  . VAL   B 151 ? 0.1554 0.1453 0.1863 -0.0209 -0.0254 -0.0017 151 VAL   B CA  
6197 C C   . VAL   B 151 ? 0.1611 0.1382 0.1800 -0.0298 -0.0289 0.0002  151 VAL   B C   
6198 O O   . VAL   B 151 ? 0.1712 0.1478 0.1956 -0.0280 -0.0216 -0.0060 151 VAL   B O   
6199 C CB  . VAL   B 151 ? 0.1752 0.1588 0.1996 -0.0078 -0.0225 -0.0100 151 VAL   B CB  
6200 C CG1 . VAL   B 151 ? 0.1876 0.1578 0.2248 -0.0175 -0.0121 -0.0170 151 VAL   B CG1 
6201 C CG2 . VAL   B 151 ? 0.1906 0.1744 0.1879 0.0031  -0.0212 0.0053  151 VAL   B CG2 
6211 N N   . TYR   B 152 ? 0.1567 0.1291 0.1743 -0.0220 -0.0258 -0.0078 152 TYR   B N   
6212 C CA  . TYR   B 152 ? 0.1590 0.1451 0.1730 -0.0267 -0.0170 -0.0041 152 TYR   B CA  
6213 C C   . TYR   B 152 ? 0.1524 0.1332 0.1656 -0.0200 -0.0162 -0.0055 152 TYR   B C   
6214 O O   . TYR   B 152 ? 0.1615 0.1376 0.1610 -0.0239 -0.0122 -0.0008 152 TYR   B O   
6215 C CB  . TYR   B 152 ? 0.1719 0.1554 0.1648 -0.0226 -0.0200 0.0082  152 TYR   B CB  
6216 C CG  . TYR   B 152 ? 0.1879 0.1652 0.1620 -0.0386 -0.0186 0.0068  152 TYR   B CG  
6217 C CD1 . TYR   B 152 ? 0.1988 0.1783 0.1535 -0.0316 -0.0342 0.0064  152 TYR   B CD1 
6218 C CD2 . TYR   B 152 ? 0.2082 0.1831 0.1622 -0.0367 -0.0168 -0.0019 152 TYR   B CD2 
6219 C CE1 . TYR   B 152 ? 0.2138 0.1939 0.1680 -0.0326 -0.0392 0.0182  152 TYR   B CE1 
6220 C CE2 . TYR   B 152 ? 0.2230 0.2043 0.1658 -0.0377 -0.0190 -0.0019 152 TYR   B CE2 
6221 C CZ  . TYR   B 152 ? 0.2243 0.2157 0.1611 -0.0331 -0.0521 0.0164  152 TYR   B CZ  
6222 O OH  . TYR   B 152 ? 0.2453 0.2497 0.1985 -0.0179 -0.0474 0.0226  152 TYR   B OH  
6232 N N   . LEU   B 153 ? 0.1555 0.1314 0.1715 -0.0251 -0.0159 -0.0089 153 LEU   B N   
6233 C CA  . LEU   B 153 ? 0.1567 0.1274 0.1580 -0.0163 -0.0092 -0.0091 153 LEU   B CA  
6234 C C   . LEU   B 153 ? 0.1615 0.1243 0.1704 -0.0232 -0.0099 -0.0109 153 LEU   B C   
6235 O O   . LEU   B 153 ? 0.1704 0.1472 0.1814 -0.0149 -0.0121 -0.0277 153 LEU   B O   
6236 C CB  . LEU   B 153 ? 0.1581 0.1282 0.1773 -0.0218 -0.0126 -0.0048 153 LEU   B CB  
6237 C CG  . LEU   B 153 ? 0.1545 0.1397 0.1979 -0.0194 -0.0103 -0.0026 153 LEU   B CG  
6238 C CD1 . LEU   B 153 ? 0.1608 0.1469 0.2059 -0.0304 -0.0004 0.0049  153 LEU   B CD1 
6239 C CD2 . LEU   B 153 ? 0.1567 0.1488 0.1996 -0.0246 -0.0014 0.0029  153 LEU   B CD2 
6251 N N   . ALA   B 154 ? 0.1556 0.1307 0.1649 -0.0068 -0.0161 -0.0090 154 ALA   B N   
6252 C CA  . ALA   B 154 ? 0.1654 0.1424 0.1859 -0.0026 -0.0178 -0.0173 154 ALA   B CA  
6253 C C   . ALA   B 154 ? 0.1741 0.1441 0.1893 0.0008  -0.0276 -0.0229 154 ALA   B C   
6254 O O   . ALA   B 154 ? 0.2030 0.1463 0.2201 0.0061  -0.0121 -0.0049 154 ALA   B O   
6255 C CB  . ALA   B 154 ? 0.1607 0.1606 0.2022 -0.0027 -0.0142 -0.0222 154 ALA   B CB  
6261 N N   . VAL   B 155 ? 0.1484 0.1360 0.1959 -0.0036 -0.0093 -0.0127 155 VAL   B N   
6262 C CA  . VAL   B 155 ? 0.1445 0.1367 0.2146 -0.0059 -0.0155 -0.0051 155 VAL   B CA  
6263 C C   . VAL   B 155 ? 0.1437 0.1345 0.2093 -0.0032 -0.0150 -0.0186 155 VAL   B C   
6264 O O   . VAL   B 155 ? 0.1620 0.1551 0.2425 0.0051  -0.0110 -0.0361 155 VAL   B O   
6265 C CB  . VAL   B 155 ? 0.1496 0.1470 0.2553 -0.0081 -0.0145 0.0114  155 VAL   B CB  
6266 C CG1 . VAL   B 155 ? 0.1510 0.1394 0.2585 -0.0166 -0.0204 0.0012  155 VAL   B CG1 
6267 C CG2 . VAL   B 155 ? 0.1406 0.1644 0.2903 -0.0090 -0.0111 0.0365  155 VAL   B CG2 
6277 N N   . PHE   B 156 ? 0.1357 0.1443 0.2299 -0.0011 -0.0084 -0.0124 156 PHE   B N   
6278 C CA  . PHE   B 156 ? 0.1423 0.1548 0.2647 0.0062  -0.0082 -0.0157 156 PHE   B CA  
6279 C C   . PHE   B 156 ? 0.1408 0.1647 0.2897 0.0127  -0.0122 -0.0316 156 PHE   B C   
6280 O O   . PHE   B 156 ? 0.1630 0.1859 0.3089 0.0257  -0.0049 -0.0370 156 PHE   B O   
6281 C CB  . PHE   B 156 ? 0.1460 0.1495 0.2662 0.0028  -0.0205 -0.0070 156 PHE   B CB  
6282 C CG  . PHE   B 156 ? 0.1540 0.1599 0.2800 0.0000  -0.0172 0.0062  156 PHE   B CG  
6283 C CD1 . PHE   B 156 ? 0.1568 0.1855 0.3057 0.0072  -0.0055 0.0356  156 PHE   B CD1 
6284 C CD2 . PHE   B 156 ? 0.1561 0.1706 0.2719 0.0081  -0.0269 0.0109  156 PHE   B CD2 
6285 C CE1 . PHE   B 156 ? 0.1592 0.1988 0.3207 0.0103  -0.0007 0.0383  156 PHE   B CE1 
6286 C CE2 . PHE   B 156 ? 0.1662 0.1946 0.2973 0.0108  -0.0191 0.0153  156 PHE   B CE2 
6287 C CZ  . PHE   B 156 ? 0.1590 0.1991 0.3141 0.0173  -0.0178 0.0248  156 PHE   B CZ  
6297 N N   . ASP   B 157 ? 0.1444 0.1513 0.3133 0.0112  -0.0213 -0.0170 157 ASP   B N   
6298 C CA  . ASP   B 157 ? 0.1522 0.1514 0.3410 0.0079  -0.0257 -0.0205 157 ASP   B CA  
6299 C C   . ASP   B 157 ? 0.1553 0.1520 0.3489 0.0062  -0.0221 -0.0403 157 ASP   B C   
6300 O O   . ASP   B 157 ? 0.1467 0.1532 0.3418 0.0052  -0.0199 -0.0356 157 ASP   B O   
6301 C CB  . ASP   B 157 ? 0.1755 0.1719 0.3578 0.0011  -0.0412 -0.0115 157 ASP   B CB  
6302 C CG  . ASP   B 157 ? 0.2119 0.1820 0.3819 -0.0019 -0.0352 -0.0076 157 ASP   B CG  
6303 O OD1 . ASP   B 157 ? 0.2256 0.1765 0.3972 0.0094  -0.0327 0.0018  157 ASP   B OD1 
6304 O OD2 . ASP   B 157 ? 0.2476 0.2029 0.4073 -0.0039 -0.0130 -0.0075 157 ASP   B OD2 
6309 N N   . LYS   B 158 ? 0.1580 0.1764 0.3537 0.0035  -0.0062 -0.0553 158 LYS   B N   
6310 C CA  . LYS   B 158 ? 0.1724 0.1924 0.3663 0.0032  -0.0048 -0.0728 158 LYS   B CA  
6311 C C   . LYS   B 158 ? 0.1731 0.1770 0.3753 0.0056  -0.0118 -0.0713 158 LYS   B C   
6312 O O   . LYS   B 158 ? 0.1754 0.1721 0.3830 -0.0092 -0.0100 -0.0818 158 LYS   B O   
6313 C CB  . LYS   B 158 ? 0.1953 0.2343 0.3721 0.0068  0.0045  -0.0937 158 LYS   B CB  
6314 C CG  . LYS   B 158 ? 0.2281 0.2757 0.3797 0.0123  0.0116  -0.1054 158 LYS   B CG  
6315 C CD  . LYS   B 158 ? 0.2552 0.3177 0.3923 0.0108  0.0129  -0.1011 158 LYS   B CD  
6316 C CE  . LYS   B 158 ? 0.2765 0.3475 0.4030 0.0112  0.0107  -0.0974 158 LYS   B CE  
6317 N NZ  . LYS   B 158 ? 0.2712 0.3542 0.3990 0.0093  0.0144  -0.0985 158 LYS   B NZ  
6331 N N   . ASN   B 159 ? 0.1761 0.1682 0.3914 0.0084  -0.0159 -0.0625 159 ASN   B N   
6332 C CA  . ASN   B 159 ? 0.1878 0.1619 0.4117 0.0176  -0.0354 -0.0443 159 ASN   B CA  
6333 C C   . ASN   B 159 ? 0.1706 0.1530 0.3962 0.0152  -0.0426 -0.0340 159 ASN   B C   
6334 O O   . ASN   B 159 ? 0.1717 0.1477 0.4120 0.0003  -0.0469 -0.0279 159 ASN   B O   
6335 C CB  . ASN   B 159 ? 0.2061 0.1766 0.4537 0.0226  -0.0445 -0.0360 159 ASN   B CB  
6336 C CG  . ASN   B 159 ? 0.2306 0.1975 0.4877 0.0244  -0.0511 -0.0597 159 ASN   B CG  
6337 O OD1 . ASN   B 159 ? 0.2457 0.2068 0.5014 0.0312  -0.0483 -0.0717 159 ASN   B OD1 
6338 N ND2 . ASN   B 159 ? 0.2334 0.2106 0.5088 0.0292  -0.0558 -0.0557 159 ASN   B ND2 
6345 N N   . LEU   B 160 ? 0.1624 0.1501 0.3697 0.0070  -0.0398 -0.0319 160 LEU   B N   
6346 C CA  . LEU   B 160 ? 0.1593 0.1566 0.3283 0.0091  -0.0324 -0.0164 160 LEU   B CA  
6347 C C   . LEU   B 160 ? 0.1546 0.1463 0.3155 -0.0027 -0.0249 -0.0317 160 LEU   B C   
6348 O O   . LEU   B 160 ? 0.1500 0.1500 0.3079 -0.0056 -0.0274 -0.0211 160 LEU   B O   
6349 C CB  . LEU   B 160 ? 0.1565 0.1629 0.3118 0.0103  -0.0342 -0.0074 160 LEU   B CB  
6350 C CG  . LEU   B 160 ? 0.1566 0.1775 0.2880 0.0140  -0.0353 0.0012  160 LEU   B CG  
6351 C CD1 . LEU   B 160 ? 0.1736 0.1970 0.2850 0.0009  -0.0226 0.0078  160 LEU   B CD1 
6352 C CD2 . LEU   B 160 ? 0.1626 0.1816 0.2977 0.0216  -0.0276 -0.0163 160 LEU   B CD2 
6364 N N   . TYR   B 161 ? 0.1530 0.1510 0.3110 -0.0062 -0.0046 -0.0371 161 TYR   B N   
6365 C CA  . TYR   B 161 ? 0.1612 0.1522 0.2980 -0.0124 0.0074  -0.0399 161 TYR   B CA  
6366 C C   . TYR   B 161 ? 0.1669 0.1474 0.2897 -0.0130 0.0064  -0.0369 161 TYR   B C   
6367 O O   . TYR   B 161 ? 0.1713 0.1515 0.2859 -0.0135 -0.0047 -0.0303 161 TYR   B O   
6368 C CB  . TYR   B 161 ? 0.1759 0.1627 0.3045 -0.0194 0.0237  -0.0423 161 TYR   B CB  
6369 C CG  . TYR   B 161 ? 0.1976 0.1640 0.2935 -0.0263 0.0344  -0.0539 161 TYR   B CG  
6370 C CD1 . TYR   B 161 ? 0.2037 0.1611 0.2860 -0.0371 0.0339  -0.0518 161 TYR   B CD1 
6371 C CD2 . TYR   B 161 ? 0.2207 0.1713 0.2928 -0.0236 0.0328  -0.0501 161 TYR   B CD2 
6372 C CE1 . TYR   B 161 ? 0.2201 0.1804 0.2950 -0.0369 0.0316  -0.0513 161 TYR   B CE1 
6373 C CE2 . TYR   B 161 ? 0.2393 0.1878 0.2948 -0.0292 0.0324  -0.0419 161 TYR   B CE2 
6374 C CZ  . TYR   B 161 ? 0.2349 0.1900 0.2898 -0.0412 0.0292  -0.0344 161 TYR   B CZ  
6375 O OH  . TYR   B 161 ? 0.2619 0.2149 0.3142 -0.0425 0.0259  -0.0342 161 TYR   B OH  
6385 N N   . ASP   B 162 ? 0.1716 0.1474 0.3071 -0.0082 0.0007  -0.0482 162 ASP   B N   
6386 C CA  . ASP   B 162 ? 0.1830 0.1567 0.3117 -0.0083 -0.0095 -0.0494 162 ASP   B CA  
6387 C C   . ASP   B 162 ? 0.1769 0.1476 0.3019 -0.0107 -0.0123 -0.0444 162 ASP   B C   
6388 O O   . ASP   B 162 ? 0.1802 0.1566 0.3097 -0.0168 -0.0215 -0.0365 162 ASP   B O   
6389 C CB  . ASP   B 162 ? 0.2018 0.1742 0.3348 0.0023  -0.0130 -0.0642 162 ASP   B CB  
6390 C CG  . ASP   B 162 ? 0.2083 0.1987 0.3588 0.0099  -0.0095 -0.0746 162 ASP   B CG  
6391 O OD1 . ASP   B 162 ? 0.2084 0.2156 0.3484 0.0042  0.0039  -0.0752 162 ASP   B OD1 
6392 O OD2 . ASP   B 162 ? 0.2219 0.2141 0.3950 0.0242  -0.0061 -0.0731 162 ASP   B OD2 
6397 N N   A LYS   B 163 ? 0.1726 0.1335 0.2912 -0.0100 -0.0217 -0.0340 163 LYS   B N   
6398 N N   B LYS   B 163 ? 0.1799 0.1549 0.2964 -0.0096 -0.0180 -0.0290 163 LYS   B N   
6399 C CA  A LYS   B 163 ? 0.1764 0.1408 0.2893 -0.0198 -0.0262 -0.0132 163 LYS   B CA  
6400 C CA  B LYS   B 163 ? 0.1843 0.1665 0.2966 -0.0119 -0.0192 -0.0103 163 LYS   B CA  
6401 C C   A LYS   B 163 ? 0.1552 0.1404 0.2817 -0.0204 -0.0235 -0.0047 163 LYS   B C   
6402 C C   B LYS   B 163 ? 0.1635 0.1537 0.2823 -0.0139 -0.0193 -0.0022 163 LYS   B C   
6403 O O   A LYS   B 163 ? 0.1537 0.1506 0.3077 -0.0253 -0.0203 -0.0030 163 LYS   B O   
6404 O O   B LYS   B 163 ? 0.1622 0.1577 0.2933 -0.0155 -0.0180 0.0018  163 LYS   B O   
6405 C CB  A LYS   B 163 ? 0.2155 0.1727 0.3240 -0.0113 -0.0317 0.0096  163 LYS   B CB  
6406 C CB  B LYS   B 163 ? 0.2104 0.1964 0.3269 -0.0086 -0.0213 0.0006  163 LYS   B CB  
6407 C CG  A LYS   B 163 ? 0.2770 0.2289 0.3680 -0.0074 -0.0207 0.0163  163 LYS   B CG  
6408 C CG  B LYS   B 163 ? 0.2439 0.2365 0.3608 -0.0059 -0.0169 0.0050  163 LYS   B CG  
6409 C CD  A LYS   B 163 ? 0.3216 0.2669 0.4097 -0.0114 -0.0174 0.0063  163 LYS   B CD  
6410 C CD  B LYS   B 163 ? 0.2735 0.2682 0.3938 -0.0067 -0.0158 0.0018  163 LYS   B CD  
6411 C CE  A LYS   B 163 ? 0.3489 0.2914 0.4394 -0.0163 -0.0138 0.0060  163 LYS   B CE  
6412 C CE  B LYS   B 163 ? 0.2906 0.2825 0.4193 -0.0089 -0.0139 0.0026  163 LYS   B CE  
6413 N NZ  A LYS   B 163 ? 0.3693 0.3057 0.4592 -0.0193 -0.0109 0.0034  163 LYS   B NZ  
6414 N NZ  B LYS   B 163 ? 0.3003 0.2898 0.4352 -0.0099 -0.0125 0.0019  163 LYS   B NZ  
6441 N N   . LEU   B 164 ? 0.1482 0.1388 0.2657 -0.0128 -0.0195 0.0018  164 LEU   B N   
6442 C CA  . LEU   B 164 ? 0.1493 0.1343 0.2576 -0.0091 -0.0254 -0.0012 164 LEU   B CA  
6443 C C   . LEU   B 164 ? 0.1558 0.1336 0.2633 -0.0131 -0.0325 0.0018  164 LEU   B C   
6444 O O   . LEU   B 164 ? 0.1573 0.1549 0.2770 -0.0147 -0.0331 -0.0002 164 LEU   B O   
6445 C CB  . LEU   B 164 ? 0.1469 0.1319 0.2424 -0.0087 -0.0210 0.0012  164 LEU   B CB  
6446 C CG  . LEU   B 164 ? 0.1546 0.1514 0.2506 -0.0110 -0.0092 -0.0009 164 LEU   B CG  
6447 C CD1 . LEU   B 164 ? 0.1626 0.1514 0.2473 -0.0122 -0.0209 -0.0015 164 LEU   B CD1 
6448 C CD2 . LEU   B 164 ? 0.1751 0.1926 0.2600 -0.0107 0.0090  -0.0214 164 LEU   B CD2 
6461 N N   . VAL   B 165 ? 0.1857 0.1473 0.2693 -0.0221 -0.0338 -0.0130 165 VAL   B N   
6462 C CA  . VAL   B 165 ? 0.2187 0.1551 0.2702 -0.0291 -0.0489 -0.0107 165 VAL   B CA  
6463 C C   . VAL   B 165 ? 0.2452 0.1684 0.2936 -0.0370 -0.0773 -0.0100 165 VAL   B C   
6464 O O   . VAL   B 165 ? 0.2647 0.1839 0.2969 -0.0410 -0.0797 -0.0044 165 VAL   B O   
6465 C CB  . VAL   B 165 ? 0.2407 0.1738 0.2687 -0.0134 -0.0153 -0.0136 165 VAL   B CB  
6466 C CG1 . VAL   B 165 ? 0.2548 0.1790 0.2951 -0.0133 -0.0004 -0.0115 165 VAL   B CG1 
6467 C CG2 . VAL   B 165 ? 0.2372 0.1828 0.2609 -0.0048 -0.0039 -0.0113 165 VAL   B CG2 
6477 N N   . SER   B 166 ? 0.2506 0.1587 0.3295 -0.0346 -0.0802 -0.0258 166 SER   B N   
6478 C CA  . SER   B 166 ? 0.2434 0.1575 0.3793 -0.0395 -0.0689 -0.0364 166 SER   B CA  
6479 C C   . SER   B 166 ? 0.2302 0.1632 0.3896 -0.0349 -0.0760 -0.0131 166 SER   B C   
6480 O O   . SER   B 166 ? 0.2345 0.1827 0.4160 -0.0429 -0.0962 -0.0340 166 SER   B O   
6481 C CB  . SER   B 166 ? 0.2446 0.1695 0.4128 -0.0288 -0.0643 -0.0471 166 SER   B CB  
6482 O OG  . SER   B 166 ? 0.2309 0.1649 0.4328 -0.0238 -0.0672 -0.0263 166 SER   B OG  
6488 N N   . SER   B 167 ? 0.2124 0.1586 0.3640 -0.0343 -0.0770 0.0162  167 SER   B N   
6489 C CA  . SER   B 167 ? 0.2021 0.1638 0.3494 -0.0345 -0.0597 0.0147  167 SER   B CA  
6490 C C   . SER   B 167 ? 0.1979 0.1744 0.3379 -0.0419 -0.0591 0.0318  167 SER   B C   
6491 O O   . SER   B 167 ? 0.1972 0.1841 0.3361 -0.0467 -0.0540 0.0354  167 SER   B O   
6492 C CB  . SER   B 167 ? 0.1942 0.1763 0.3483 -0.0303 -0.0310 0.0228  167 SER   B CB  
6493 O OG  . SER   B 167 ? 0.1849 0.1859 0.3364 -0.0223 -0.0173 0.0240  167 SER   B OG  
6499 N N   . PHE   B 168 ? 0.2010 0.1737 0.3320 -0.0381 -0.0386 0.0437  168 PHE   B N   
6500 C CA  . PHE   B 168 ? 0.2062 0.1690 0.3127 -0.0436 -0.0356 0.0316  168 PHE   B CA  
6501 C C   . PHE   B 168 ? 0.1810 0.1595 0.2628 -0.0232 -0.0147 0.0134  168 PHE   B C   
6502 O O   . PHE   B 168 ? 0.2106 0.1540 0.2667 0.0016  -0.0151 -0.0032 168 PHE   B O   
6503 C CB  . PHE   B 168 ? 0.2243 0.1777 0.3170 -0.0498 -0.0554 0.0436  168 PHE   B CB  
6504 C CG  . PHE   B 168 ? 0.2527 0.1649 0.3069 -0.0554 -0.0609 0.0196  168 PHE   B CG  
6505 C CD1 . PHE   B 168 ? 0.2857 0.1648 0.3203 -0.0486 -0.0608 0.0161  168 PHE   B CD1 
6506 C CD2 . PHE   B 168 ? 0.2412 0.1625 0.3028 -0.0486 -0.0636 0.0247  168 PHE   B CD2 
6507 C CE1 . PHE   B 168 ? 0.2972 0.1797 0.3152 -0.0328 -0.0563 0.0155  168 PHE   B CE1 
6508 C CE2 . PHE   B 168 ? 0.2668 0.1699 0.3087 -0.0343 -0.0672 0.0139  168 PHE   B CE2 
6509 C CZ  . PHE   B 168 ? 0.2823 0.1672 0.3122 -0.0241 -0.0674 0.0242  168 PHE   B CZ  
6519 N N   . LEU   B 169 ? 0.1781 0.1779 0.2608 -0.0046 -0.0053 -0.0001 169 LEU   B N   
6520 C CA  . LEU   B 169 ? 0.1975 0.2068 0.2957 -0.0127 -0.0076 -0.0305 169 LEU   B CA  
6521 C C   . LEU   B 169 ? 0.2270 0.2288 0.3409 0.0031  -0.0089 -0.0582 169 LEU   B C   
6522 O O   . LEU   B 169 ? 0.2525 0.2474 0.3925 0.0010  -0.0143 -0.0771 169 LEU   B O   
6523 C CB  . LEU   B 169 ? 0.2118 0.2491 0.3095 -0.0195 -0.0120 -0.0068 169 LEU   B CB  
6524 C CG  . LEU   B 169 ? 0.2531 0.2876 0.3482 -0.0054 -0.0045 -0.0004 169 LEU   B CG  
6525 C CD1 . LEU   B 169 ? 0.2728 0.3080 0.3542 -0.0054 -0.0061 0.0116  169 LEU   B CD1 
6526 C CD2 . LEU   B 169 ? 0.2495 0.2938 0.3519 0.0118  0.0162  -0.0090 169 LEU   B CD2 
6527 O OXT . LEU   B 169 ? 0.2461 0.2488 0.3358 0.0310  -0.0009 -0.0586 169 LEU   B OXT 
6539 O O1  B A1BAA C .   ? 0.1534 0.1699 0.1744 0.0129  -0.0115 0.0065  201 A1BAA A O1  
6540 C C1  B A1BAA C .   ? 0.1761 0.1866 0.1885 0.0068  0.0138  -0.0040 201 A1BAA A C1  
6541 C C2  B A1BAA C .   ? 0.1745 0.1859 0.1850 0.0082  0.0089  -0.0012 201 A1BAA A C2  
6542 C C3  B A1BAA C .   ? 0.1680 0.1828 0.1790 0.0096  0.0059  0.0021  201 A1BAA A C3  
6543 C C4  B A1BAA C .   ? 0.1706 0.1891 0.1764 0.0077  0.0094  0.0057  201 A1BAA A C4  
6544 C C5  B A1BAA C .   ? 0.1778 0.1918 0.1798 0.0075  0.0067  0.0126  201 A1BAA A C5  
6545 C C6  B A1BAA C .   ? 0.1574 0.1722 0.1701 0.0119  0.0039  0.0054  201 A1BAA A C6  
6546 C C7  B A1BAA C .   ? 0.1529 0.1803 0.1622 -0.0103 0.0116  0.0184  201 A1BAA A C7  
6547 C C8  B A1BAA C .   ? 0.1518 0.1761 0.1636 -0.0127 0.0098  0.0186  201 A1BAA A C8  
6548 C C10 B A1BAA C .   ? 0.1426 0.1777 0.1655 -0.0101 0.0095  0.0263  201 A1BAA A C10 
6549 C C11 B A1BAA C .   ? 0.1361 0.1790 0.1678 -0.0090 0.0105  0.0326  201 A1BAA A C11 
6550 C C12 B A1BAA C .   ? 0.1292 0.1769 0.1688 -0.0151 0.0036  0.0369  201 A1BAA A C12 
6551 C C9  B A1BAA C .   ? 0.1416 0.1747 0.1651 -0.0136 0.0039  0.0275  201 A1BAA A C9  
6552 N N1  B A1BAA C .   ? 0.1658 0.1861 0.1805 0.0011  0.0090  0.0036  201 A1BAA A N1  
6553 N N2  B A1BAA C .   ? 0.1561 0.1769 0.1607 -0.0123 0.0124  0.0195  201 A1BAA A N2  
6554 N N3  B A1BAA C .   ? 0.1459 0.1747 0.1643 -0.0172 0.0087  0.0236  201 A1BAA A N3  
6555 N N4  B A1BAA C .   ? 0.1378 0.1753 0.1697 -0.0127 -0.0037 0.0334  201 A1BAA A N4  
6574 O O1  C A1BAA D .   ? 0.1904 0.2106 0.2120 0.0182  0.0056  0.0105  202 A1BAA A O1  
6575 C C1  C A1BAA D .   ? 0.1776 0.1934 0.1845 0.0282  0.0119  0.0173  202 A1BAA A C1  
6576 C C2  C A1BAA D .   ? 0.1762 0.1927 0.1829 0.0286  0.0158  0.0205  202 A1BAA A C2  
6577 C C3  C A1BAA D .   ? 0.1735 0.1898 0.1853 0.0305  0.0162  0.0188  202 A1BAA A C3  
6578 C C4  C A1BAA D .   ? 0.1703 0.1867 0.1827 0.0337  0.0283  0.0138  202 A1BAA A C4  
6579 C C5  C A1BAA D .   ? 0.1679 0.1862 0.1808 0.0276  0.0345  0.0121  202 A1BAA A C5  
6580 C C6  C A1BAA D .   ? 0.1830 0.2014 0.2000 0.0262  0.0100  0.0116  202 A1BAA A C6  
6581 C C7  C A1BAA D .   ? 0.1482 0.1742 0.1636 0.0202  0.0185  0.0183  202 A1BAA A C7  
6582 C C8  C A1BAA D .   ? 0.1402 0.1641 0.1574 0.0248  0.0271  0.0071  202 A1BAA A C8  
6583 C C10 C A1BAA D .   ? 0.1366 0.1696 0.1652 0.0165  0.0155  0.0206  202 A1BAA A C10 
6584 C C11 C A1BAA D .   ? 0.1326 0.1706 0.1682 0.0128  0.0113  0.0306  202 A1BAA A C11 
6585 C C12 C A1BAA D .   ? 0.1234 0.1647 0.1648 0.0067  0.0078  0.0380  202 A1BAA A C12 
6586 C C9  C A1BAA D .   ? 0.1338 0.1624 0.1631 0.0142  0.0121  0.0216  202 A1BAA A C9  
6587 N N1  C A1BAA D .   ? 0.1656 0.1821 0.1798 0.0268  0.0102  0.0242  202 A1BAA A N1  
6588 N N2  C A1BAA D .   ? 0.1498 0.1699 0.1644 0.0231  0.0255  0.0075  202 A1BAA A N2  
6589 N N3  C A1BAA D .   ? 0.1342 0.1597 0.1599 0.0173  0.0216  0.0143  202 A1BAA A N3  
6590 N N4  C A1BAA D .   ? 0.1302 0.1608 0.1667 0.0108  0.0017  0.0328  202 A1BAA A N4  
6609 O O   B HOH   E .   ? 0.4588 0.4028 0.3027 0.0215  -0.0042 0.0648  301 HOH   A O   
6610 O O   . HOH   E .   ? 0.4082 0.2584 0.3515 -0.0539 -0.0746 0.0657  302 HOH   A O   
6611 O O   . HOH   E .   ? 0.6527 0.4656 0.5287 -0.1482 -0.0032 0.1283  303 HOH   A O   
6612 O O   . HOH   E .   ? 0.2873 0.2476 0.5008 -0.0267 -0.1098 0.1161  304 HOH   A O   
6613 O O   . HOH   E .   ? 0.4928 0.3463 0.4923 -0.0374 0.1312  0.0938  305 HOH   A O   
6614 O O   . HOH   E .   ? 0.2653 0.2568 0.3555 -0.0333 0.0636  0.0836  306 HOH   A O   
6615 O O   . HOH   E .   ? 0.5283 0.3939 0.3682 -0.1378 -0.1284 -0.0286 307 HOH   A O   
6616 O O   . HOH   E .   ? 0.6372 0.4352 0.3908 0.1752  -0.1270 0.0834  308 HOH   A O   
6617 O O   . HOH   E .   ? 0.3152 0.3576 0.1895 -0.0343 0.0646  0.0654  309 HOH   A O   
6618 O O   . HOH   E .   ? 0.2119 0.2213 0.2621 -0.0169 -0.0156 0.0737  310 HOH   A O   
6619 O O   . HOH   E .   ? 0.3066 0.7197 0.5135 -0.0316 -0.0735 0.1755  311 HOH   A O   
6620 O O   A HOH   E .   ? 0.3964 0.6119 0.4258 -0.0932 0.0691  0.0297  312 HOH   A O   
6621 O O   . HOH   E .   ? 0.2012 0.3541 0.4857 -0.0395 0.0454  -0.1309 313 HOH   A O   
6622 O O   . HOH   E .   ? 0.1594 0.4166 0.3096 -0.0021 0.0205  0.1091  314 HOH   A O   
6623 O O   . HOH   E .   ? 0.2224 0.1774 0.2501 0.0218  -0.0323 -0.0002 315 HOH   A O   
6624 O O   . HOH   E .   ? 0.6172 0.6203 0.6088 0.0912  -0.0991 0.0694  316 HOH   A O   
6625 O O   . HOH   E .   ? 0.2624 0.2247 0.2692 -0.0035 -0.0082 0.0593  317 HOH   A O   
6626 O O   . HOH   E .   ? 0.2551 0.3124 0.3241 0.0057  -0.0160 -0.0438 318 HOH   A O   
6627 O O   . HOH   E .   ? 0.2224 0.1877 0.3599 -0.0420 0.0057  -0.0126 319 HOH   A O   
6628 O O   . HOH   E .   ? 0.3128 0.3094 0.3843 -0.0766 0.1075  0.0042  320 HOH   A O   
6629 O O   . HOH   E .   ? 0.2991 0.5441 0.4063 0.0370  -0.0673 0.0874  321 HOH   A O   
6630 O O   . HOH   E .   ? 0.3066 0.2839 0.2878 -0.0817 0.0150  0.0656  322 HOH   A O   
6631 O O   . HOH   E .   ? 0.4227 0.5433 0.5406 0.1354  0.0968  -0.0514 323 HOH   A O   
6632 O O   . HOH   E .   ? 0.3616 0.3301 0.3994 -0.0532 0.1609  0.0110  324 HOH   A O   
6633 O O   B HOH   E .   ? 0.2684 0.2569 0.2010 -0.0603 0.0116  -0.0164 325 HOH   A O   
6634 O O   . HOH   E .   ? 0.1855 0.2961 0.2964 0.0271  -0.0214 -0.0344 326 HOH   A O   
6635 O O   . HOH   E .   ? 0.7002 0.5882 0.3420 -0.0065 -0.0378 0.1275  327 HOH   A O   
6636 O O   . HOH   E .   ? 0.3204 0.4415 0.2590 0.0096  0.0465  0.0594  328 HOH   A O   
6637 O O   . HOH   E .   ? 0.2349 0.4605 0.3828 -0.0192 -0.0603 0.1699  329 HOH   A O   
6638 O O   . HOH   E .   ? 0.4273 0.2202 0.4080 0.0352  -0.1195 0.0598  330 HOH   A O   
6639 O O   . HOH   E .   ? 0.2488 0.2364 0.3033 0.0459  0.0302  0.0412  331 HOH   A O   
6640 O O   . HOH   E .   ? 0.6077 0.5015 0.5684 0.0939  0.2294  -0.1097 332 HOH   A O   
6641 O O   . HOH   E .   ? 0.5183 0.2124 0.5096 0.0508  0.0026  0.0147  333 HOH   A O   
6642 O O   A HOH   E .   ? 0.3948 0.1735 0.2231 0.0233  0.0455  0.0165  334 HOH   A O   
6643 O O   . HOH   E .   ? 0.5386 0.6279 0.4499 -0.1187 -0.1053 -0.0943 335 HOH   A O   
6644 O O   . HOH   E .   ? 0.8265 0.3256 0.5267 -0.0465 -0.1352 0.0627  336 HOH   A O   
6645 O O   . HOH   E .   ? 0.2711 0.2234 0.2714 -0.0262 0.0151  0.0002  337 HOH   A O   
6646 O O   . HOH   E .   ? 0.5928 0.6130 0.5564 -0.0926 0.1088  0.0687  338 HOH   A O   
6647 O O   . HOH   E .   ? 0.4935 0.5423 0.3482 -0.1351 0.1335  0.0598  339 HOH   A O   
6648 O O   . HOH   E .   ? 0.5544 0.3777 0.3210 -0.0051 0.0188  0.1196  340 HOH   A O   
6649 O O   . HOH   E .   ? 0.4409 0.3714 0.6271 -0.0179 0.1430  -0.0654 341 HOH   A O   
6650 O O   . HOH   E .   ? 0.3443 0.4179 0.4012 -0.1198 -0.1157 0.0010  342 HOH   A O   
6651 O O   . HOH   E .   ? 0.6426 0.5345 0.4382 0.0373  -0.0530 -0.1021 343 HOH   A O   
6652 O O   . HOH   E .   ? 0.7257 0.4913 0.4086 -0.1339 0.1429  0.1590  344 HOH   A O   
6653 O O   . HOH   E .   ? 0.1507 0.2267 0.2220 0.0008  -0.0092 0.0559  345 HOH   A O   
6654 O O   A HOH   E .   ? 0.2083 0.3931 0.3105 0.1211  0.0881  0.1634  346 HOH   A O   
6655 O O   B HOH   E .   ? 0.3877 0.3387 0.3071 0.0048  -0.0138 -0.0887 347 HOH   A O   
6656 O O   . HOH   E .   ? 0.2729 0.4516 0.3361 -0.0540 0.0447  -0.0005 348 HOH   A O   
6657 O O   . HOH   E .   ? 0.3720 0.6606 0.4884 0.0091  -0.1594 0.0206  349 HOH   A O   
6658 O O   . HOH   E .   ? 0.3813 0.2054 0.2495 0.1016  0.0503  0.0077  350 HOH   A O   
6659 O O   . HOH   E .   ? 0.3614 0.3787 0.4239 0.1678  0.0655  0.0337  351 HOH   A O   
6660 O O   . HOH   E .   ? 0.1920 0.2031 0.3442 0.0174  0.0690  0.0009  352 HOH   A O   
6661 O O   . HOH   E .   ? 0.5022 0.4458 0.4196 -0.1980 -0.0187 0.1901  353 HOH   A O   
6662 O O   . HOH   E .   ? 0.1554 0.1973 0.2705 0.0119  -0.0078 0.0134  354 HOH   A O   
6663 O O   . HOH   E .   ? 0.2475 0.4075 0.3789 0.1107  -0.0794 -0.0192 355 HOH   A O   
6664 O O   . HOH   E .   ? 0.1377 0.1379 0.1475 -0.0045 0.0091  0.0083  356 HOH   A O   
6665 O O   A HOH   E .   ? 0.2761 0.4565 0.3108 0.1340  -0.0208 -0.0588 357 HOH   A O   
6666 O O   . HOH   E .   ? 0.1886 0.2436 0.1999 -0.0263 -0.0091 0.0742  358 HOH   A O   
6667 O O   A HOH   E .   ? 0.2679 0.4930 0.4806 0.0856  0.0133  0.0814  359 HOH   A O   
6668 O O   . HOH   E .   ? 0.4072 0.2341 0.4369 -0.1128 0.0768  0.0320  360 HOH   A O   
6669 O O   . HOH   E .   ? 0.1520 0.1621 0.1610 -0.0058 -0.0149 -0.0006 361 HOH   A O   
6670 O O   . HOH   E .   ? 0.2405 0.1957 0.3167 -0.0080 -0.0772 -0.0176 362 HOH   A O   
6671 O O   . HOH   E .   ? 0.1598 0.1378 0.2349 -0.0058 0.0147  -0.0102 363 HOH   A O   
6672 O O   . HOH   E .   ? 0.1912 0.2964 0.3625 -0.0201 0.0789  0.0904  364 HOH   A O   
6673 O O   . HOH   E .   ? 0.3024 0.3730 0.2277 -0.0654 -0.0162 -0.0739 365 HOH   A O   
6674 O O   . HOH   E .   ? 0.3098 0.3549 0.5082 -0.0873 -0.1041 -0.0776 366 HOH   A O   
6675 O O   . HOH   E .   ? 0.3340 0.2292 0.5419 -0.0666 -0.0054 0.0156  367 HOH   A O   
6676 O O   . HOH   E .   ? 0.2013 0.1973 0.2398 -0.0324 0.0082  0.0319  368 HOH   A O   
6677 O O   . HOH   E .   ? 0.3495 0.3424 0.3730 -0.1206 -0.0191 -0.0154 369 HOH   A O   
6678 O O   . HOH   E .   ? 0.2196 0.2297 0.4091 0.0178  -0.0574 -0.0445 370 HOH   A O   
6679 O O   . HOH   E .   ? 0.4742 0.2621 0.4436 -0.1446 0.1905  -0.0816 371 HOH   A O   
6680 O O   . HOH   E .   ? 0.2814 0.4195 0.2965 0.0449  0.0710  0.1558  372 HOH   A O   
6681 O O   B HOH   E .   ? 0.1387 0.2143 0.2834 0.0086  -0.0381 -0.0851 373 HOH   A O   
6682 O O   A HOH   E .   ? 0.1497 0.1567 0.2076 0.0051  -0.0288 -0.0128 374 HOH   A O   
6683 O O   . HOH   E .   ? 0.1689 0.1993 0.2048 0.0055  -0.0252 -0.0117 375 HOH   A O   
6684 O O   . HOH   E .   ? 0.2442 0.1964 0.2765 -0.0106 0.0153  0.0298  376 HOH   A O   
6685 O O   . HOH   E .   ? 0.1799 0.1871 0.2479 -0.0237 0.0052  0.0487  377 HOH   A O   
6686 O O   . HOH   E .   ? 0.2256 0.3921 0.3253 -0.0300 -0.0049 0.0517  378 HOH   A O   
6687 O O   . HOH   E .   ? 0.2084 0.2772 0.3788 0.0366  0.0831  -0.0660 379 HOH   A O   
6688 O O   . HOH   E .   ? 0.2218 0.2385 0.2217 -0.0251 -0.0361 0.0473  380 HOH   A O   
6689 O O   . HOH   E .   ? 0.2123 0.1694 0.1627 -0.0019 0.0218  0.0152  381 HOH   A O   
6690 O O   . HOH   E .   ? 0.3327 0.4738 0.5255 0.0081  0.1713  0.2055  382 HOH   A O   
6691 O O   . HOH   E .   ? 0.3475 0.2433 0.3574 -0.0152 -0.0363 0.0995  383 HOH   A O   
6692 O O   . HOH   E .   ? 0.2013 0.1992 0.2000 0.0029  0.0019  0.0171  384 HOH   A O   
6693 O O   . HOH   E .   ? 0.1897 0.1747 0.2239 0.0128  -0.0225 0.0270  385 HOH   A O   
6694 O O   B HOH   E .   ? 0.2009 0.1810 0.1465 -0.0064 -0.0380 0.0317  386 HOH   A O   
6695 O O   . HOH   E .   ? 0.3124 0.3115 0.2162 0.0253  0.0638  -0.0057 387 HOH   A O   
6696 O O   . HOH   E .   ? 0.5683 0.4795 0.6079 -0.1027 -0.0269 0.1212  388 HOH   A O   
6697 O O   . HOH   E .   ? 0.3411 0.6150 0.3881 0.0958  0.0919  -0.0936 389 HOH   A O   
6698 O O   . HOH   E .   ? 0.3873 0.4954 0.5122 0.1683  -0.0310 0.0618  390 HOH   A O   
6699 O O   . HOH   E .   ? 0.4226 0.3204 0.4853 0.0448  0.1468  -0.0493 391 HOH   A O   
6700 O O   . HOH   E .   ? 0.2862 0.2098 0.1914 -0.0605 0.0320  0.0336  392 HOH   A O   
6701 O O   . HOH   E .   ? 0.1768 0.1454 0.1694 -0.0186 0.0103  0.0070  393 HOH   A O   
6702 O O   A HOH   E .   ? 0.3428 0.5974 0.4858 -0.0345 -0.1290 0.0628  394 HOH   A O   
6703 O O   . HOH   E .   ? 0.5236 0.4721 0.2061 -0.0092 0.1119  0.0763  395 HOH   A O   
6704 O O   . HOH   E .   ? 0.1959 0.2026 0.3730 0.0401  0.1005  0.1035  396 HOH   A O   
6705 O O   . HOH   E .   ? 0.3891 0.3451 0.2656 -0.0111 -0.1130 0.0399  397 HOH   A O   
6706 O O   . HOH   E .   ? 0.4515 0.6384 0.4070 -0.1178 -0.0503 0.1165  398 HOH   A O   
6707 O O   . HOH   E .   ? 0.2634 0.3990 0.3437 -0.0366 0.1009  -0.0747 399 HOH   A O   
6708 O O   . HOH   E .   ? 0.6510 0.8177 0.4399 0.2276  -0.1002 0.2105  400 HOH   A O   
6709 O O   A HOH   E .   ? 0.1910 0.1837 0.2493 0.0011  -0.0545 0.0273  401 HOH   A O   
6710 O O   . HOH   E .   ? 0.4428 0.5732 0.3118 -0.0733 -0.0337 0.1044  402 HOH   A O   
6711 O O   A HOH   E .   ? 0.4748 0.4474 0.4355 -0.1765 0.0845  0.0646  403 HOH   A O   
6712 O O   . HOH   E .   ? 0.4397 0.3106 0.3279 -0.0447 -0.0176 0.0498  404 HOH   A O   
6713 O O   . HOH   E .   ? 0.1846 0.1968 0.3549 0.0224  -0.0340 0.0473  405 HOH   A O   
6714 O O   . HOH   E .   ? 0.3415 0.2852 0.2364 -0.0844 -0.0928 0.0290  406 HOH   A O   
6715 O O   . HOH   E .   ? 0.1469 0.1499 0.2020 0.0022  -0.0186 0.0052  407 HOH   A O   
6716 O O   A HOH   E .   ? 0.1368 0.1550 0.1618 -0.0022 -0.0118 -0.0181 408 HOH   A O   
6717 O O   . HOH   E .   ? 0.5171 0.2576 0.4954 0.0515  0.0058  -0.0543 409 HOH   A O   
6718 O O   . HOH   E .   ? 0.2983 0.3778 0.7226 -0.0262 0.1210  -0.0394 410 HOH   A O   
6719 O O   . HOH   E .   ? 0.2246 0.1748 0.2924 -0.0038 -0.0352 0.0157  411 HOH   A O   
6720 O O   . HOH   E .   ? 0.2619 0.2199 0.2488 -0.0659 0.0027  0.0516  412 HOH   A O   
6721 O O   . HOH   E .   ? 0.3773 0.6778 0.5313 0.0766  0.0591  0.1211  413 HOH   A O   
6722 O O   . HOH   E .   ? 0.5349 0.3137 0.2803 -0.1155 0.0516  0.0543  414 HOH   A O   
6723 O O   . HOH   E .   ? 0.3641 0.4727 0.3510 0.1601  -0.0897 -0.1541 415 HOH   A O   
6724 O O   . HOH   E .   ? 0.2057 0.2782 0.3442 -0.0199 -0.0119 0.0262  416 HOH   A O   
6725 O O   . HOH   E .   ? 0.1555 0.1762 0.3055 -0.0059 -0.0029 0.0192  417 HOH   A O   
6726 O O   A HOH   E .   ? 0.2617 0.2921 0.3143 0.0176  0.0911  0.0244  418 HOH   A O   
6727 O O   . HOH   E .   ? 0.3291 0.1390 0.2151 0.0007  -0.0544 0.0021  419 HOH   A O   
6728 O O   . HOH   E .   ? 0.6439 0.6979 0.4164 0.2575  -0.0911 -0.0583 420 HOH   A O   
6729 O O   A HOH   E .   ? 0.5036 0.2718 0.3786 0.0583  0.0816  0.1216  421 HOH   A O   
6730 O O   . HOH   E .   ? 0.1700 0.2375 0.3269 -0.0161 -0.0028 0.0652  422 HOH   A O   
6731 O O   . HOH   E .   ? 0.2299 0.2778 0.2715 -0.0084 -0.0524 0.0474  423 HOH   A O   
6732 O O   . HOH   E .   ? 0.4309 0.2299 0.5341 -0.0801 -0.2321 0.0977  424 HOH   A O   
6733 O O   . HOH   E .   ? 0.6436 0.3935 0.4804 0.1652  -0.0592 0.1289  425 HOH   A O   
6734 O O   . HOH   E .   ? 0.3086 0.3855 0.4759 -0.0270 0.1474  0.0223  426 HOH   A O   
6735 O O   . HOH   E .   ? 0.4559 0.3328 0.4898 0.1300  0.0775  0.0346  427 HOH   A O   
6736 O O   . HOH   E .   ? 0.5705 0.5762 0.5834 -0.0819 -0.0394 -0.1140 428 HOH   A O   
6737 O O   . HOH   E .   ? 0.2362 0.4429 0.2589 0.1562  -0.0112 0.0109  429 HOH   A O   
6738 O O   . HOH   E .   ? 0.5562 0.4923 0.3417 0.0063  -0.1379 0.0161  430 HOH   A O   
6739 O O   . HOH   E .   ? 0.2940 0.6141 0.1831 -0.0565 0.0412  -0.0110 431 HOH   A O   
6740 O O   B HOH   E .   ? 0.1186 0.1659 0.2754 -0.0054 -0.0155 0.0503  432 HOH   A O   
6741 O O   A HOH   E .   ? 0.4979 0.5332 0.3082 -0.0983 -0.0064 0.1712  433 HOH   A O   
6742 O O   . HOH   E .   ? 0.5794 0.7239 0.4198 0.1096  0.2550  -0.0639 434 HOH   A O   
6743 O O   B HOH   E .   ? 0.2942 0.3953 0.2065 -0.0079 0.0432  0.0132  435 HOH   A O   
6744 O O   B HOH   E .   ? 0.3560 0.2964 0.3363 0.0271  0.0194  -0.0433 436 HOH   A O   
6745 O O   . HOH   E .   ? 0.4653 0.4378 0.5282 -0.1088 -0.1099 -0.1250 437 HOH   A O   
6746 O O   . HOH   E .   ? 0.6912 0.5284 0.7586 0.1206  -0.1303 0.1625  438 HOH   A O   
6747 O O   . HOH   E .   ? 0.1980 0.2299 0.5176 -0.0308 -0.0802 0.0733  439 HOH   A O   
6748 O O   A HOH   E .   ? 0.1686 0.1503 0.2248 0.0298  -0.0742 -0.0184 440 HOH   A O   
6749 O O   A HOH   E .   ? 0.1736 0.1434 0.1545 -0.0132 -0.0109 -0.0174 441 HOH   A O   
6750 O O   . HOH   E .   ? 0.3930 0.2819 0.1842 -0.0828 0.0374  0.0383  442 HOH   A O   
6751 O O   . HOH   E .   ? 0.2400 0.1787 0.2798 0.0038  -0.0032 0.0191  443 HOH   A O   
6752 O O   . HOH   E .   ? 0.6000 0.6976 0.5455 0.0209  -0.1267 0.0052  444 HOH   A O   
6753 O O   . HOH   E .   ? 0.3689 0.3208 0.3451 0.1829  -0.0303 -0.0332 445 HOH   A O   
6754 O O   . HOH   E .   ? 0.4951 0.3017 0.6471 0.0468  -0.0054 -0.0664 446 HOH   A O   
6755 O O   . HOH   E .   ? 0.3014 0.3250 0.5754 -0.0052 0.1267  -0.1078 447 HOH   A O   
6756 O O   . HOH   E .   ? 0.2446 0.2126 0.2559 0.0152  0.0314  0.0195  448 HOH   A O   
6757 O O   . HOH   E .   ? 0.2250 0.2674 0.2500 -0.0069 -0.0114 -0.0487 449 HOH   A O   
6758 O O   . HOH   E .   ? 0.6127 0.3356 0.4792 0.0181  -0.0436 0.1664  450 HOH   A O   
6759 O O   A HOH   E .   ? 0.4255 0.2837 0.4643 0.1436  0.1674  0.1545  451 HOH   A O   
6760 O O   . HOH   E .   ? 0.5051 0.4310 0.4266 -0.0075 0.0065  0.0664  452 HOH   A O   
6761 O O   . HOH   E .   ? 0.6802 0.5827 0.4640 -0.0284 0.0525  0.2188  453 HOH   A O   
6762 O O   A HOH   E .   ? 0.6942 0.5815 0.4417 -0.1478 -0.1273 -0.1449 454 HOH   A O   
6763 O O   B HOH   E .   ? 0.4948 0.3112 0.3111 -0.0193 -0.0049 0.0663  455 HOH   A O   
6764 O O   B HOH   E .   ? 0.2152 0.2919 0.2419 -0.1101 -0.0308 -0.0118 456 HOH   A O   
6765 O O   . HOH   E .   ? 0.2680 0.3128 0.3899 0.0497  -0.0331 0.0783  457 HOH   A O   
6766 O O   . HOH   E .   ? 0.5223 0.3548 0.5092 0.0492  0.1104  0.0568  458 HOH   A O   
6767 O O   . HOH   E .   ? 0.7181 0.5456 0.4380 -0.0864 0.1468  0.0522  459 HOH   A O   
6768 O O   . HOH   E .   ? 0.2914 0.2941 0.3670 -0.0724 0.0194  -0.0633 460 HOH   A O   
6769 O O   . HOH   E .   ? 0.7367 0.6103 0.6362 -0.0780 0.0681  -0.1190 461 HOH   A O   
6770 O O   B HOH   E .   ? 0.1706 0.1469 0.2199 0.0392  -0.0824 0.0076  462 HOH   A O   
6771 O O   . HOH   E .   ? 0.7355 0.8190 0.5105 0.0788  -0.1176 -0.0010 463 HOH   A O   
6772 O O   . HOH   E .   ? 0.2944 0.5425 0.5011 -0.1407 0.0494  -0.1259 464 HOH   A O   
6773 O O   . HOH   E .   ? 0.3331 0.5244 0.5005 0.0741  -0.0559 0.1503  465 HOH   A O   
6774 O O   . HOH   E .   ? 0.3785 0.5824 0.3776 0.0055  -0.0496 -0.0567 466 HOH   A O   
6775 O O   . HOH   E .   ? 0.2618 0.4554 0.4201 -0.0335 -0.0273 -0.0237 467 HOH   A O   
6776 O O   B HOH   E .   ? 0.2982 0.3719 0.4990 0.1209  -0.0659 -0.0173 468 HOH   A O   
6777 O O   . HOH   E .   ? 0.3013 0.2607 0.5428 0.0666  -0.1310 -0.0249 469 HOH   A O   
6778 O O   . HOH   E .   ? 0.6521 0.3521 0.7605 0.0824  0.0835  0.2345  470 HOH   A O   
6779 O O   . HOH   E .   ? 0.4217 0.6584 0.4163 -0.0949 -0.0492 0.2265  471 HOH   A O   
6780 O O   . HOH   E .   ? 0.2662 0.3062 0.3147 -0.0988 0.0337  -0.0212 472 HOH   A O   
6781 O O   . HOH   E .   ? 0.6979 0.6321 0.5073 0.1752  -0.1432 0.0448  473 HOH   A O   
6782 O O   . HOH   E .   ? 0.3080 0.4220 0.5685 0.0742  0.0140  -0.1844 474 HOH   A O   
6783 O O   . HOH   E .   ? 0.6827 0.5598 0.6042 0.1247  0.2258  0.2879  475 HOH   A O   
6784 O O   . HOH   E .   ? 0.5500 0.5278 0.5379 0.0712  -0.0770 -0.1176 476 HOH   A O   
6785 O O   . HOH   E .   ? 0.5540 0.5838 0.4658 -0.0019 0.1431  0.0717  477 HOH   A O   
6786 O O   . HOH   E .   ? 0.3125 0.2519 0.3846 0.0079  0.0607  0.0142  478 HOH   A O   
6787 O O   . HOH   E .   ? 0.3100 0.1885 0.2508 0.0384  -0.0938 -0.0250 479 HOH   A O   
6788 O O   . HOH   E .   ? 0.5735 0.7251 0.6476 -0.1513 -0.1237 0.0235  480 HOH   A O   
6789 O O   . HOH   E .   ? 0.5045 0.2981 0.3472 -0.1091 -0.1327 0.0873  481 HOH   A O   
6790 O O   . HOH   E .   ? 0.6007 0.5815 0.5154 -0.0469 -0.1178 -0.1000 482 HOH   A O   
6791 O O   . HOH   E .   ? 0.4543 0.4377 0.4586 -0.2149 0.0015  0.0136  483 HOH   A O   
6792 O O   . HOH   E .   ? 0.2564 0.2424 0.2577 0.0201  -0.0019 -0.0118 484 HOH   A O   
6793 O O   . HOH   E .   ? 0.6567 0.5179 0.7254 -0.0447 0.1224  -0.0615 485 HOH   A O   
6794 O O   . HOH   E .   ? 0.4094 0.5545 0.2818 -0.0355 -0.0162 0.0120  486 HOH   A O   
6795 O O   B HOH   E .   ? 0.1890 0.2013 0.3841 0.0560  0.0117  0.0903  487 HOH   A O   
6796 O O   . HOH   E .   ? 0.8174 0.3765 0.3291 -0.0388 -0.1241 -0.0110 488 HOH   A O   
6797 O O   . HOH   E .   ? 0.4344 0.4764 0.3419 -0.0562 -0.0303 0.0113  489 HOH   A O   
6798 O O   . HOH   E .   ? 0.5447 0.4453 0.4395 -0.0124 0.0080  -0.1204 490 HOH   A O   
6799 O O   . HOH   E .   ? 0.6709 0.4143 0.4799 0.0043  0.1670  -0.0035 491 HOH   A O   
6800 O O   . HOH   E .   ? 0.5799 0.6726 0.4326 -0.0698 0.1414  0.1064  492 HOH   A O   
6801 O O   . HOH   E .   ? 0.3053 0.4110 0.5131 0.0253  0.1277  0.1268  493 HOH   A O   
6802 O O   . HOH   E .   ? 0.4149 0.3600 0.2548 -0.0572 0.1059  -0.0191 494 HOH   A O   
6803 O O   . HOH   E .   ? 0.3075 0.5289 0.3566 0.1193  0.1040  0.2330  495 HOH   A O   
6804 O O   . HOH   E .   ? 0.5776 0.6195 0.6330 0.1039  0.1962  -0.1068 496 HOH   A O   
6805 O O   . HOH   E .   ? 0.2747 0.2584 0.6762 -0.0108 -0.1237 0.0227  497 HOH   A O   
6806 O O   . HOH   E .   ? 0.5502 0.5133 0.5783 -0.0776 -0.1275 0.0261  498 HOH   A O   
6807 O O   . HOH   E .   ? 0.3706 0.2873 0.4440 -0.0737 0.0336  0.0777  499 HOH   A O   
6808 O O   . HOH   E .   ? 0.4992 0.3339 0.4870 -0.0286 0.2778  -0.0082 500 HOH   A O   
6809 O O   . HOH   E .   ? 0.2612 0.3125 0.5428 -0.0229 0.0942  -0.0891 501 HOH   A O   
6810 O O   . HOH   E .   ? 0.3000 0.2222 0.5950 0.0070  0.0465  0.0963  502 HOH   A O   
6811 O O   B HOH   E .   ? 0.2026 0.4124 0.3149 0.0600  -0.0138 0.0986  503 HOH   A O   
6812 O O   . HOH   E .   ? 0.4626 0.8855 0.5821 -0.1100 -0.0713 0.2407  504 HOH   A O   
6813 O O   . HOH   E .   ? 0.4768 0.2632 0.4379 -0.1343 0.0085  0.0480  505 HOH   A O   
6814 O O   . HOH   E .   ? 0.2362 0.3144 0.3677 0.0386  -0.0425 0.0420  506 HOH   A O   
6815 O O   . HOH   E .   ? 0.6705 0.2762 0.4899 -0.0387 0.0804  0.0957  507 HOH   A O   
6816 O O   . HOH   E .   ? 0.3182 0.4582 0.3542 -0.0290 -0.0378 -0.0615 508 HOH   A O   
6817 O O   . HOH   E .   ? 0.3105 0.4193 0.4406 0.0862  0.0005  0.0689  509 HOH   A O   
6818 O O   . HOH   E .   ? 0.6680 0.4350 0.5505 0.1798  -0.0127 -0.0770 510 HOH   A O   
6819 O O   . HOH   E .   ? 0.5875 0.7881 0.5321 0.1598  -0.0866 0.0954  511 HOH   A O   
6820 O O   . HOH   E .   ? 0.3118 0.2392 0.4433 0.0112  0.0368  0.0451  512 HOH   A O   
6821 O O   . HOH   E .   ? 0.4831 0.6755 0.4550 0.2634  -0.0056 0.1427  513 HOH   A O   
6822 O O   . HOH   E .   ? 0.5406 0.5467 0.4896 -0.0485 -0.0344 -0.1262 514 HOH   A O   
6823 O O   A HOH   E .   ? 0.3617 0.7095 0.3265 0.1072  0.1051  -0.0885 515 HOH   A O   
6824 O O   . HOH   E .   ? 0.4575 0.6216 0.5748 -0.0101 -0.0952 0.0410  516 HOH   A O   
6825 O O   . HOH   E .   ? 0.3219 0.7082 0.3538 0.0856  -0.0172 -0.0313 517 HOH   A O   
6826 O O   . HOH   E .   ? 0.4663 0.4357 0.4376 0.1272  -0.0560 0.0535  518 HOH   A O   
6827 O O   . HOH   E .   ? 0.4071 0.3940 0.5908 0.0414  -0.1017 0.2093  519 HOH   A O   
6828 O O   . HOH   F .   ? 0.2459 0.2266 0.3273 0.0258  0.0937  0.0244  201 HOH   B O   
6829 O O   . HOH   F .   ? 0.5707 0.5587 0.2860 0.0960  -0.0528 -0.1387 202 HOH   B O   
6830 O O   . HOH   F .   ? 0.4929 0.4240 0.6096 0.0196  -0.1247 0.2665  203 HOH   B O   
6831 O O   . HOH   F .   ? 0.4681 0.3082 0.3665 -0.0361 -0.0143 -0.1135 204 HOH   B O   
6832 O O   . HOH   F .   ? 0.6295 0.6020 0.5963 0.1601  0.0093  0.0039  205 HOH   B O   
6833 O O   . HOH   F .   ? 0.2880 0.5766 0.4854 -0.0059 0.1449  -0.1938 206 HOH   B O   
6834 O O   . HOH   F .   ? 0.3312 0.7320 0.4041 0.1035  0.0221  0.2449  207 HOH   B O   
6835 O O   . HOH   F .   ? 0.3397 0.3721 0.6406 -0.0612 0.0656  -0.0696 208 HOH   B O   
6836 O O   . HOH   F .   ? 0.4695 0.4551 0.5591 -0.1363 -0.0219 -0.1495 209 HOH   B O   
6837 O O   . HOH   F .   ? 0.7520 0.2814 0.4965 0.1249  0.1354  0.0324  210 HOH   B O   
6838 O O   . HOH   F .   ? 0.4776 0.6274 0.4051 0.2901  -0.1012 0.0062  211 HOH   B O   
6839 O O   . HOH   F .   ? 0.2968 0.3020 0.6796 0.0809  -0.1105 0.0318  212 HOH   B O   
6840 O O   . HOH   F .   ? 0.3149 0.2135 0.5556 0.0162  0.1865  0.0907  213 HOH   B O   
6841 O O   . HOH   F .   ? 0.1937 0.2350 0.2933 0.0042  0.0072  -0.0229 214 HOH   B O   
6842 O O   . HOH   F .   ? 0.4757 0.4040 0.3743 -0.0005 -0.1216 0.0664  215 HOH   B O   
6843 O O   . HOH   F .   ? 0.1626 0.1943 0.2712 -0.0142 -0.0084 -0.0045 216 HOH   B O   
6844 O O   . HOH   F .   ? 0.4234 0.4931 0.3631 0.2193  -0.0384 0.0252  217 HOH   B O   
6845 O O   . HOH   F .   ? 0.1622 0.1545 0.2342 -0.0245 -0.0022 0.0118  218 HOH   B O   
6846 O O   . HOH   F .   ? 0.3637 0.5483 0.4170 0.2036  0.0231  -0.0554 219 HOH   B O   
6847 O O   . HOH   F .   ? 0.4084 0.3869 0.5475 -0.1589 -0.0037 0.0633  220 HOH   B O   
6848 O O   . HOH   F .   ? 0.3089 0.2939 0.5514 0.0218  -0.0803 0.0031  221 HOH   B O   
6849 O O   . HOH   F .   ? 0.3991 0.4456 0.3893 0.0015  0.0723  -0.1281 222 HOH   B O   
6850 O O   . HOH   F .   ? 0.4766 0.2104 0.3422 -0.0090 -0.0991 0.0156  223 HOH   B O   
6851 O O   . HOH   F .   ? 0.4476 0.4290 0.6773 -0.0766 -0.1540 -0.0974 224 HOH   B O   
6852 O O   . HOH   F .   ? 0.4482 0.6625 0.3742 0.2563  -0.0067 -0.0256 225 HOH   B O   
6853 O O   . HOH   F .   ? 0.2576 0.1853 0.2921 -0.0309 0.1031  -0.0009 226 HOH   B O   
6854 O O   . HOH   F .   ? 0.3174 0.2693 0.5608 0.0029  0.1012  0.0536  227 HOH   B O   
6855 O O   . HOH   F .   ? 0.6382 0.3130 0.4142 -0.2064 0.0943  0.0027  228 HOH   B O   
6856 O O   . HOH   F .   ? 0.5536 0.6249 0.3240 0.0239  -0.0222 0.0706  229 HOH   B O   
6857 O O   . HOH   F .   ? 0.2780 0.3540 0.3623 -0.0814 0.0533  -0.0319 230 HOH   B O   
6858 O O   . HOH   F .   ? 0.3022 0.2212 0.4125 -0.0005 0.1366  -0.0075 231 HOH   B O   
6859 O O   . HOH   F .   ? 0.6271 0.4441 0.4874 0.1161  0.0101  -0.1161 232 HOH   B O   
6860 O O   . HOH   F .   ? 0.1803 0.2044 0.2954 -0.0217 0.0049  -0.0095 233 HOH   B O   
6861 O O   . HOH   F .   ? 0.2219 0.1361 0.3539 0.0104  -0.0633 -0.0232 234 HOH   B O   
6862 O O   . HOH   F .   ? 0.2340 0.3629 0.3258 -0.0338 -0.0683 -0.0505 235 HOH   B O   
6863 O O   . HOH   F .   ? 0.2733 0.2575 0.3147 0.0334  0.0301  -0.0843 236 HOH   B O   
6864 O O   . HOH   F .   ? 0.3661 0.3348 0.2541 0.0353  0.0526  0.0392  237 HOH   B O   
6865 O O   . HOH   F .   ? 0.1546 0.1491 0.1728 -0.0126 -0.0071 0.0027  238 HOH   B O   
6866 O O   . HOH   F .   ? 0.4008 0.2573 0.3955 0.0815  -0.0468 -0.0606 239 HOH   B O   
6867 O O   . HOH   F .   ? 0.2255 0.2188 0.3906 -0.0369 -0.0113 -0.0593 240 HOH   B O   
6868 O O   . HOH   F .   ? 0.3359 0.1917 0.2101 0.0157  -0.0684 -0.0067 241 HOH   B O   
6869 O O   . HOH   F .   ? 0.4593 0.3524 0.3512 -0.0970 0.0625  -0.0580 242 HOH   B O   
6870 O O   . HOH   F .   ? 0.2238 0.2366 0.2908 -0.0533 0.0022  -0.0298 243 HOH   B O   
6871 O O   . HOH   F .   ? 0.2347 0.2032 0.2273 -0.0251 -0.0528 0.0000  244 HOH   B O   
6872 O O   . HOH   F .   ? 0.3861 0.2459 0.4135 0.0426  -0.0925 -0.1074 245 HOH   B O   
6873 O O   . HOH   F .   ? 0.4731 0.3205 0.4276 -0.2252 -0.0102 0.0128  246 HOH   B O   
6874 O O   . HOH   F .   ? 0.1543 0.1385 0.1650 -0.0007 -0.0035 0.0060  247 HOH   B O   
6875 O O   . HOH   F .   ? 0.3129 0.1795 0.6364 -0.0076 -0.1456 -0.0338 248 HOH   B O   
6876 O O   . HOH   F .   ? 0.2980 0.4324 0.3334 -0.0944 -0.0388 -0.0663 249 HOH   B O   
6877 O O   . HOH   F .   ? 0.2360 0.2127 0.1876 0.0042  0.0018  -0.0000 250 HOH   B O   
6878 O O   . HOH   F .   ? 0.3112 0.2312 0.2996 0.0845  0.0934  0.0102  251 HOH   B O   
6879 O O   . HOH   F .   ? 0.1670 0.1525 0.2733 -0.0055 0.0056  -0.0193 252 HOH   B O   
6880 O O   . HOH   F .   ? 0.3443 0.2511 0.2834 -0.0502 0.0203  -0.0434 253 HOH   B O   
6881 O O   . HOH   F .   ? 0.2159 0.1501 0.2246 -0.0235 -0.0326 0.0223  254 HOH   B O   
6882 O O   . HOH   F .   ? 0.3430 0.3340 0.2176 0.0521  0.0744  0.0273  255 HOH   B O   
6883 O O   . HOH   F .   ? 0.2460 0.2238 0.2693 0.0723  -0.0812 -0.0656 256 HOH   B O   
6884 O O   . HOH   F .   ? 0.2121 0.4074 0.2460 -0.0391 -0.0243 0.0689  257 HOH   B O   
6885 O O   . HOH   F .   ? 0.1683 0.1757 0.2931 -0.0208 -0.0228 0.0062  258 HOH   B O   
6886 O O   . HOH   F .   ? 0.2227 0.1975 0.4038 0.0038  -0.0607 -0.0368 259 HOH   B O   
6887 O O   . HOH   F .   ? 0.4881 0.3027 0.2539 0.0099  0.1027  -0.0241 260 HOH   B O   
6888 O O   . HOH   F .   ? 0.2594 0.4343 0.5031 0.1343  -0.0564 -0.0717 261 HOH   B O   
6889 O O   . HOH   F .   ? 0.1456 0.1702 0.2207 -0.0077 0.0068  0.0133  262 HOH   B O   
6890 O O   . HOH   F .   ? 0.1901 0.2846 0.2844 0.0503  0.0451  0.1014  263 HOH   B O   
6891 O O   . HOH   F .   ? 0.2343 0.3227 0.2278 -0.0414 0.0260  0.0650  264 HOH   B O   
6892 O O   . HOH   F .   ? 0.2605 0.2622 0.2511 -0.0480 -0.0807 -0.0378 265 HOH   B O   
6893 O O   . HOH   F .   ? 0.3391 0.4417 0.3420 -0.0401 -0.1060 0.1009  266 HOH   B O   
6894 O O   . HOH   F .   ? 0.2329 0.2308 0.2390 0.0432  -0.0060 -0.0071 267 HOH   B O   
6895 O O   . HOH   F .   ? 0.2661 0.2807 0.2498 -0.0325 -0.0786 0.0043  268 HOH   B O   
6896 O O   . HOH   F .   ? 0.2486 0.2154 0.2040 0.0113  -0.0061 0.0037  269 HOH   B O   
6897 O O   . HOH   F .   ? 0.2649 0.2014 0.2991 -0.0626 0.0141  0.0023  270 HOH   B O   
6898 O O   . HOH   F .   ? 0.2046 0.1588 0.2395 -0.0250 -0.0174 0.0163  271 HOH   B O   
6899 O O   . HOH   F .   ? 0.1810 0.1480 0.4646 -0.0125 -0.0396 0.0036  272 HOH   B O   
6900 O O   . HOH   F .   ? 0.2671 0.4074 0.3543 0.0358  0.0954  0.0285  273 HOH   B O   
6901 O O   . HOH   F .   ? 0.1860 0.1889 0.1749 -0.0387 -0.0403 0.0063  274 HOH   B O   
6902 O O   . HOH   F .   ? 0.2996 0.2897 0.5046 -0.0212 -0.0333 -0.1093 275 HOH   B O   
6903 O O   . HOH   F .   ? 0.4607 0.3711 0.2704 0.0518  -0.0077 -0.1028 276 HOH   B O   
6904 O O   . HOH   F .   ? 0.4205 0.3036 0.4305 -0.0319 -0.1119 -0.0789 277 HOH   B O   
6905 O O   . HOH   F .   ? 0.2654 0.7342 0.7416 0.1007  -0.1104 -0.1099 278 HOH   B O   
6906 O O   . HOH   F .   ? 0.2582 0.4496 0.5676 0.0351  -0.0102 -0.0997 279 HOH   B O   
6907 O O   . HOH   F .   ? 0.2480 0.3647 0.3527 -0.0625 0.0551  -0.1288 280 HOH   B O   
6908 O O   . HOH   F .   ? 0.1642 0.1658 0.3451 -0.0149 0.0083  -0.0017 281 HOH   B O   
6909 O O   . HOH   F .   ? 0.5288 0.6833 0.2577 0.0327  -0.0891 0.1110  282 HOH   B O   
6910 O O   . HOH   F .   ? 0.2223 0.4222 0.4701 -0.0369 -0.0242 -0.1673 283 HOH   B O   
6911 O O   . HOH   F .   ? 0.4279 0.4599 0.4746 0.0100  -0.1501 0.0025  284 HOH   B O   
6912 O O   . HOH   F .   ? 0.3584 0.3905 0.4847 0.1279  -0.0864 -0.0971 285 HOH   B O   
6913 O O   . HOH   F .   ? 0.2900 0.2182 0.4676 0.0161  0.0400  0.0365  286 HOH   B O   
6914 O O   . HOH   F .   ? 0.1686 0.1620 0.1800 -0.0028 0.0068  0.0008  287 HOH   B O   
6915 O O   . HOH   F .   ? 0.2596 0.2708 0.2814 0.0094  -0.0827 0.0221  288 HOH   B O   
6916 O O   . HOH   F .   ? 0.3814 0.2206 0.4144 -0.0916 -0.2083 0.0686  289 HOH   B O   
6917 O O   . HOH   F .   ? 0.1691 0.2104 0.1581 -0.0139 -0.0193 0.0062  290 HOH   B O   
6918 O O   . HOH   F .   ? 0.1726 0.1996 0.2773 0.0188  -0.0080 0.0088  291 HOH   B O   
6919 O O   . HOH   F .   ? 0.2828 0.4668 0.4770 -0.0976 -0.1122 0.1067  292 HOH   B O   
6920 O O   . HOH   F .   ? 0.6473 0.4031 0.5641 0.0932  0.0552  0.0053  293 HOH   B O   
6921 O O   . HOH   F .   ? 0.3008 0.2725 0.5140 -0.0182 -0.0678 0.1128  294 HOH   B O   
6922 O O   . HOH   F .   ? 0.3287 0.2830 0.2723 -0.0102 0.0094  -0.1117 295 HOH   B O   
6923 O O   . HOH   F .   ? 0.3788 0.2655 0.2182 0.0308  -0.0767 -0.0188 296 HOH   B O   
6924 O O   . HOH   F .   ? 0.4231 0.4490 0.2211 -0.0021 0.0461  0.0430  297 HOH   B O   
6925 O O   . HOH   F .   ? 0.1794 0.1716 0.2494 0.0055  0.0083  0.0228  298 HOH   B O   
6926 O O   . HOH   F .   ? 0.6063 0.3790 0.3146 0.2646  0.0907  0.0774  299 HOH   B O   
6927 O O   . HOH   F .   ? 0.2173 0.2798 0.6063 0.0459  -0.0620 -0.1027 300 HOH   B O   
6928 O O   . HOH   F .   ? 0.3272 0.6235 0.3324 0.1311  -0.0459 0.0798  301 HOH   B O   
6929 O O   . HOH   F .   ? 0.1739 0.3259 0.4740 0.0214  -0.0118 -0.1130 302 HOH   B O   
6930 O O   . HOH   F .   ? 0.2573 0.7241 0.2548 0.0588  -0.0282 -0.0671 303 HOH   B O   
6931 O O   . HOH   F .   ? 0.4613 0.3384 0.5144 -0.0796 0.0092  0.1393  304 HOH   B O   
6932 O O   . HOH   F .   ? 0.5132 0.2994 0.2585 -0.1819 0.1039  -0.0239 305 HOH   B O   
6933 O O   . HOH   F .   ? 0.4768 0.3812 0.2530 0.1198  -0.1002 0.0464  306 HOH   B O   
6934 O O   . HOH   F .   ? 0.5971 0.5740 0.4746 -0.1177 -0.0292 0.1477  307 HOH   B O   
6935 O O   . HOH   F .   ? 0.2675 0.3020 0.3360 -0.0304 0.0746  -0.0695 308 HOH   B O   
6936 O O   . HOH   F .   ? 0.2394 0.1582 0.2644 -0.0144 -0.0163 0.0244  309 HOH   B O   
6937 O O   . HOH   F .   ? 0.2170 0.1676 0.3390 0.0343  -0.1029 -0.0073 310 HOH   B O   
6938 O O   . HOH   F .   ? 0.1676 0.1955 0.2881 -0.0281 -0.0094 0.0106  311 HOH   B O   
6939 O O   . HOH   F .   ? 0.1663 0.1569 0.3038 0.0044  -0.0089 -0.0009 312 HOH   B O   
6940 O O   . HOH   F .   ? 0.5193 0.5206 0.2606 0.1964  -0.1070 -0.0590 313 HOH   B O   
6941 O O   . HOH   F .   ? 0.3461 0.1956 0.3327 0.0747  0.1185  0.0509  314 HOH   B O   
6942 O O   . HOH   F .   ? 0.3056 0.3315 0.3826 -0.1113 0.1071  -0.0591 315 HOH   B O   
6943 O O   . HOH   F .   ? 0.4333 0.2379 0.2980 0.1604  0.1088  0.0308  316 HOH   B O   
6944 O O   . HOH   F .   ? 0.4202 0.3998 0.6674 0.0422  -0.0510 0.0979  317 HOH   B O   
6945 O O   . HOH   F .   ? 0.2167 0.1643 0.2774 -0.0223 -0.0316 -0.0017 318 HOH   B O   
6946 O O   . HOH   F .   ? 0.2384 0.3052 0.5078 -0.0119 -0.0623 0.0013  319 HOH   B O   
6947 O O   . HOH   F .   ? 0.2680 0.3387 0.4344 -0.0462 -0.1295 0.1081  320 HOH   B O   
6948 O O   . HOH   F .   ? 0.2177 0.2029 0.1961 -0.0111 0.0136  0.0207  321 HOH   B O   
6949 O O   . HOH   F .   ? 0.2784 0.2258 0.2355 0.0224  -0.0217 0.0127  322 HOH   B O   
6950 O O   . HOH   F .   ? 0.1741 0.3022 0.2538 -0.0153 -0.0225 0.0805  323 HOH   B O   
6951 O O   . HOH   F .   ? 0.1706 0.1682 0.3143 -0.0154 -0.0143 -0.0152 324 HOH   B O   
6952 O O   . HOH   F .   ? 0.5042 0.4314 0.2586 0.0431  -0.0530 -0.0388 325 HOH   B O   
6953 O O   . HOH   F .   ? 0.4410 0.3300 0.5237 0.1170  0.2165  0.1834  326 HOH   B O   
6954 O O   . HOH   F .   ? 0.2384 0.6279 0.5644 -0.0734 -0.0321 0.0210  327 HOH   B O   
6955 O O   . HOH   F .   ? 0.3230 0.3679 0.7776 -0.0231 -0.0886 0.1913  328 HOH   B O   
6956 O O   . HOH   F .   ? 0.2050 0.2165 0.2806 0.0328  0.0463  0.0223  329 HOH   B O   
6957 O O   . HOH   F .   ? 0.7778 0.2132 0.2995 0.0003  -0.0818 0.0214  330 HOH   B O   
6958 O O   . HOH   F .   ? 0.4928 0.5441 0.3159 0.0201  -0.0886 0.0205  331 HOH   B O   
6959 O O   . HOH   F .   ? 0.6694 0.6308 0.5390 0.3229  0.0082  -0.0541 332 HOH   B O   
6960 O O   . HOH   F .   ? 0.6182 0.3419 0.3448 0.0158  0.1202  0.1070  333 HOH   B O   
6961 O O   . HOH   F .   ? 0.2667 0.2100 0.5104 0.0121  0.0036  0.0590  334 HOH   B O   
6962 O O   . HOH   F .   ? 0.5985 0.5502 0.6050 0.0845  -0.0667 0.2406  335 HOH   B O   
6963 O O   . HOH   F .   ? 0.1835 0.3016 0.3116 0.0281  -0.0258 -0.0740 336 HOH   B O   
6964 O O   . HOH   F .   ? 0.5391 0.3533 0.3926 0.0188  0.0635  -0.1510 337 HOH   B O   
6965 O O   . HOH   F .   ? 0.5809 0.4825 0.5884 -0.0653 -0.0793 -0.1210 338 HOH   B O   
6966 O O   . HOH   F .   ? 0.4491 0.2543 0.3421 0.0438  0.0333  0.0756  339 HOH   B O   
6967 O O   . HOH   F .   ? 0.1811 0.1547 0.2301 0.0036  -0.0242 0.0033  340 HOH   B O   
6968 O O   . HOH   F .   ? 0.2403 0.2354 0.5631 -0.0532 0.0082  0.1374  341 HOH   B O   
6969 O O   . HOH   F .   ? 0.5145 0.3890 0.2952 0.0766  -0.1137 -0.0588 342 HOH   B O   
6970 O O   . HOH   F .   ? 0.4293 0.6884 0.3256 0.0219  -0.0245 0.1510  343 HOH   B O   
6971 O O   . HOH   F .   ? 0.2305 0.6026 0.6711 0.0107  -0.0964 0.0565  344 HOH   B O   
6972 O O   . HOH   F .   ? 0.6351 0.6745 0.2843 -0.0210 -0.0643 0.1062  345 HOH   B O   
6973 O O   . HOH   F .   ? 0.4510 0.5913 0.3914 -0.1075 -0.1225 -0.0739 346 HOH   B O   
6974 O O   . HOH   F .   ? 0.2170 0.2038 0.2863 -0.0137 0.0593  -0.0101 347 HOH   B O   
6975 O O   . HOH   F .   ? 0.4325 0.5032 0.4849 0.0450  -0.0941 0.0138  348 HOH   B O   
6976 O O   . HOH   F .   ? 0.2950 0.2167 0.4994 -0.0244 -0.0891 -0.0528 349 HOH   B O   
6977 O O   . HOH   F .   ? 0.5082 0.5423 0.4486 -0.1077 0.0200  0.0736  350 HOH   B O   
6978 O O   . HOH   F .   ? 0.5097 0.2890 0.5393 -0.1080 0.1512  0.0533  351 HOH   B O   
6979 O O   . HOH   F .   ? 0.2376 0.5165 0.3827 0.1089  -0.0313 -0.1177 352 HOH   B O   
6980 O O   . HOH   F .   ? 0.4745 0.5680 0.6445 0.0125  0.0143  -0.1075 353 HOH   B O   
6981 O O   . HOH   F .   ? 0.3481 0.4430 0.4652 -0.1603 0.0099  -0.0116 354 HOH   B O   
6982 O O   . HOH   F .   ? 0.2235 0.4238 0.5374 0.0186  0.0256  0.0361  355 HOH   B O   
6983 O O   . HOH   F .   ? 0.3622 0.2315 0.3317 -0.0576 -0.0263 -0.0640 356 HOH   B O   
6984 O O   . HOH   F .   ? 0.3304 0.1979 0.3896 0.0465  -0.1207 -0.0614 357 HOH   B O   
6985 O O   . HOH   F .   ? 0.3855 0.2797 0.4113 -0.0741 -0.0370 -0.0432 358 HOH   B O   
6986 O O   . HOH   F .   ? 0.5235 0.3797 0.4245 0.0642  0.1320  -0.0204 359 HOH   B O   
6987 O O   . HOH   F .   ? 0.4749 0.6030 0.5299 0.1961  -0.1310 0.1400  360 HOH   B O   
6988 O O   . HOH   F .   ? 0.4496 0.3440 0.4479 0.0197  -0.1745 -0.0195 361 HOH   B O   
6989 O O   . HOH   F .   ? 0.5050 0.4860 0.5096 -0.0638 -0.0302 0.0345  362 HOH   B O   
6990 O O   . HOH   F .   ? 0.4757 0.6670 0.3381 0.2044  -0.0701 0.0442  363 HOH   B O   
6991 O O   . HOH   F .   ? 0.5343 0.3932 0.6397 0.0453  0.1003  0.1108  364 HOH   B O   
6992 O O   . HOH   F .   ? 0.2242 0.3880 0.6475 -0.0741 -0.0548 -0.0995 365 HOH   B O   
6993 O O   . HOH   F .   ? 0.6304 0.4461 0.4374 0.1191  0.1135  0.0842  366 HOH   B O   
6994 O O   . HOH   F .   ? 0.4991 0.3041 0.5569 -0.1316 -0.0534 0.0217  367 HOH   B O   
6995 O O   . HOH   F .   ? 0.5789 0.3600 0.4881 0.0452  -0.1642 0.0372  368 HOH   B O   
6996 O O   . HOH   F .   ? 0.6175 0.2342 0.4389 0.0181  0.0222  0.0659  369 HOH   B O   
6997 O O   . HOH   F .   ? 0.5737 0.5580 0.3355 0.1585  -0.1487 0.0348  370 HOH   B O   
6998 O O   . HOH   F .   ? 0.5052 0.5792 0.5622 0.2717  0.1014  0.1234  371 HOH   B O   
6999 O O   . HOH   F .   ? 0.7236 0.7667 0.5136 0.2551  -0.1252 0.1279  372 HOH   B O   
7000 O O   . HOH   F .   ? 0.5284 0.5168 0.4388 -0.0600 -0.0929 -0.1036 373 HOH   B O   
7001 O O   . HOH   F .   ? 0.6369 0.4146 0.2935 -0.0990 -0.0906 -0.0743 374 HOH   B O   
7002 O O   . HOH   F .   ? 0.3981 0.3313 0.4210 0.0379  -0.1299 -0.0173 375 HOH   B O   
7003 O O   . HOH   F .   ? 0.4573 0.4713 0.4837 -0.0899 -0.0522 0.0484  376 HOH   B O   
7004 O O   . HOH   F .   ? 0.2552 0.4540 0.4295 0.0568  -0.0765 -0.0742 377 HOH   B O   
7005 O O   . HOH   F .   ? 0.4049 0.4334 0.2196 0.0290  0.0599  0.0025  378 HOH   B O   
7006 O O   . HOH   F .   ? 0.7348 0.3486 0.5442 -0.1204 -0.0055 -0.0233 379 HOH   B O   
7007 O O   . HOH   F .   ? 0.4935 0.7455 0.6020 0.1816  0.0794  0.2890  380 HOH   B O   
7008 O O   . HOH   F .   ? 0.3625 0.5228 0.5360 0.0753  -0.0487 0.0729  381 HOH   B O   
7009 O O   . HOH   F .   ? 0.5907 0.7175 0.5863 0.0034  0.1976  0.1442  382 HOH   B O   
7010 O O   . HOH   F .   ? 0.5285 0.6328 0.3835 -0.1315 0.0400  -0.1472 383 HOH   B O   
7011 O O   . HOH   F .   ? 0.3244 0.2581 0.3439 0.0083  0.0046  0.0392  384 HOH   B O   
7012 O O   . HOH   F .   ? 0.3577 0.8097 0.5653 0.0819  0.1658  0.1626  385 HOH   B O   
7013 O O   . HOH   F .   ? 0.7119 0.4257 0.4397 0.1010  0.0879  -0.1028 386 HOH   B O   
7014 O O   . HOH   F .   ? 0.6263 0.4306 0.5040 -0.0850 0.0193  -0.0004 387 HOH   B O   
7015 O O   . HOH   F .   ? 0.2581 0.4232 0.3963 -0.0886 -0.1120 -0.0237 388 HOH   B O   
7016 O O   . HOH   F .   ? 0.4711 0.3661 0.3101 0.0277  0.0387  -0.0233 389 HOH   B O   
7017 O O   . HOH   F .   ? 0.7182 0.5560 0.4088 0.1784  -0.0005 0.1241  390 HOH   B O   
7018 O O   . HOH   F .   ? 0.5689 0.4555 0.4433 0.0022  -0.0802 -0.0694 391 HOH   B O   
7019 O O   . HOH   F .   ? 0.4004 0.2329 0.3238 0.0880  -0.0212 0.0154  392 HOH   B O   
7020 O O   . HOH   F .   ? 0.4016 0.4446 0.3897 -0.0033 0.0250  0.0309  393 HOH   B O   
7021 O O   . HOH   F .   ? 0.4695 0.2417 0.5562 -0.0528 0.0887  0.0466  394 HOH   B O   
7022 O O   . HOH   F .   ? 0.2464 0.4501 0.6412 -0.1284 -0.0845 0.0518  395 HOH   B O   
7023 O O   . HOH   F .   ? 0.4314 0.4069 0.4402 -0.0001 0.1066  0.0556  396 HOH   B O   
7024 O O   . HOH   F .   ? 0.4656 0.5952 0.3578 0.1848  -0.0687 -0.0924 397 HOH   B O   
7025 O O   . HOH   F .   ? 0.3136 0.3915 0.3541 0.0332  0.0122  -0.0638 398 HOH   B O   
7026 O O   . HOH   F .   ? 0.5502 0.6405 0.7429 0.1231  -0.1207 0.2034  399 HOH   B O   
7027 O O   . HOH   F .   ? 0.2252 0.3068 0.6211 -0.0519 -0.1027 0.0070  400 HOH   B O   
7028 O O   . HOH   F .   ? 0.5905 0.4140 0.3101 -0.2159 -0.0108 0.1025  401 HOH   B O   
7029 O O   . HOH   F .   ? 0.6152 0.6403 0.3882 0.1843  0.0097  0.0355  402 HOH   B O   
# 
