data_7HCT
# 
_entry.id   7HCT 
# 
_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   7HCT         pdb_00007hct 10.2210/pdb7hct/pdb 
WWPDB D_1001407311 ?            ?                   
# 
_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                        7HCT 
_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 '(3R)-3-ethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-3-ol' 232.282   1   ?                      ? ? ? 
3 water       nat water                                                             18.015    410 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3R)-3-ethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-3-ol' A1A6N 
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 
A1A6N non-polymer         . '(3R)-3-ethyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-3-ol' ? 'C12 H16 N4 O'   232.282 
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 A1A6N 1   201 201  A1A6N LA1 A . 
D 3 HOH   1   301 40   HOH   HOH A . 
D 3 HOH   2   302 229  HOH   HOH A . 
D 3 HOH   3   303 196  HOH   HOH A . 
D 3 HOH   4   304 292  HOH   HOH A . 
D 3 HOH   5   305 36   HOH   HOH A . 
D 3 HOH   6   306 625  HOH   HOH A . 
D 3 HOH   7   307 209  HOH   HOH A . 
D 3 HOH   8   308 93   HOH   HOH A . 
D 3 HOH   9   309 393  HOH   HOH A . 
D 3 HOH   10  310 109  HOH   HOH A . 
D 3 HOH   11  311 247  HOH   HOH A . 
D 3 HOH   12  312 124  HOH   HOH A . 
D 3 HOH   13  313 409  HOH   HOH A . 
D 3 HOH   14  314 1295 HOH   HOH A . 
D 3 HOH   15  315 76   HOH   HOH A . 
D 3 HOH   16  316 136  HOH   HOH A . 
D 3 HOH   17  317 199  HOH   HOH A . 
D 3 HOH   18  318 39   HOH   HOH A . 
D 3 HOH   19  319 96   HOH   HOH A . 
D 3 HOH   20  320 1290 HOH   HOH A . 
D 3 HOH   21  321 661  HOH   HOH A . 
D 3 HOH   22  322 105  HOH   HOH A . 
D 3 HOH   23  323 192  HOH   HOH A . 
D 3 HOH   24  324 281  HOH   HOH A . 
D 3 HOH   25  325 151  HOH   HOH A . 
D 3 HOH   26  326 153  HOH   HOH A . 
D 3 HOH   27  327 164  HOH   HOH A . 
D 3 HOH   28  328 469  HOH   HOH A . 
D 3 HOH   29  329 1301 HOH   HOH A . 
D 3 HOH   30  330 964  HOH   HOH A . 
D 3 HOH   31  331 155  HOH   HOH A . 
D 3 HOH   32  332 2    HOH   HOH A . 
D 3 HOH   33  333 115  HOH   HOH A . 
D 3 HOH   34  334 630  HOH   HOH A . 
D 3 HOH   35  335 15   HOH   HOH A . 
D 3 HOH   36  336 1313 HOH   HOH A . 
D 3 HOH   37  337 461  HOH   HOH A . 
D 3 HOH   38  338 26   HOH   HOH A . 
D 3 HOH   39  339 225  HOH   HOH A . 
D 3 HOH   40  340 86   HOH   HOH A . 
D 3 HOH   41  341 42   HOH   HOH A . 
D 3 HOH   42  342 337  HOH   HOH A . 
D 3 HOH   43  343 102  HOH   HOH A . 
D 3 HOH   44  344 236  HOH   HOH A . 
D 3 HOH   45  345 140  HOH   HOH A . 
D 3 HOH   46  346 1310 HOH   HOH A . 
D 3 HOH   47  347 21   HOH   HOH A . 
D 3 HOH   48  348 169  HOH   HOH A . 
D 3 HOH   49  349 33   HOH   HOH A . 
D 3 HOH   50  350 17   HOH   HOH A . 
D 3 HOH   51  351 320  HOH   HOH A . 
D 3 HOH   52  352 165  HOH   HOH A . 
D 3 HOH   53  353 396  HOH   HOH A . 
D 3 HOH   54  354 241  HOH   HOH A . 
D 3 HOH   55  355 1300 HOH   HOH A . 
D 3 HOH   56  356 66   HOH   HOH A . 
D 3 HOH   57  357 2    HOH   HOH A . 
D 3 HOH   58  358 1283 HOH   HOH A . 
D 3 HOH   59  359 218  HOH   HOH A . 
D 3 HOH   60  360 92   HOH   HOH A . 
D 3 HOH   61  361 354  HOH   HOH A . 
D 3 HOH   62  362 56   HOH   HOH A . 
D 3 HOH   63  363 81   HOH   HOH A . 
D 3 HOH   64  364 18   HOH   HOH A . 
D 3 HOH   65  365 366  HOH   HOH A . 
D 3 HOH   66  366 195  HOH   HOH A . 
D 3 HOH   67  367 19   HOH   HOH A . 
D 3 HOH   68  368 57   HOH   HOH A . 
D 3 HOH   69  369 139  HOH   HOH A . 
D 3 HOH   70  370 5    HOH   HOH A . 
D 3 HOH   71  371 162  HOH   HOH A . 
D 3 HOH   72  372 662  HOH   HOH A . 
D 3 HOH   73  373 132  HOH   HOH A . 
D 3 HOH   74  374 939  HOH   HOH A . 
D 3 HOH   75  375 27   HOH   HOH A . 
D 3 HOH   76  376 6    HOH   HOH A . 
D 3 HOH   77  377 85   HOH   HOH A . 
D 3 HOH   78  378 1134 HOH   HOH A . 
D 3 HOH   79  379 493  HOH   HOH A . 
D 3 HOH   80  380 35   HOH   HOH A . 
D 3 HOH   81  381 8    HOH   HOH A . 
D 3 HOH   82  382 46   HOH   HOH A . 
D 3 HOH   83  383 296  HOH   HOH A . 
D 3 HOH   84  384 138  HOH   HOH A . 
D 3 HOH   85  385 49   HOH   HOH A . 
D 3 HOH   86  386 1309 HOH   HOH A . 
D 3 HOH   87  387 45   HOH   HOH A . 
D 3 HOH   88  388 12   HOH   HOH A . 
D 3 HOH   89  389 159  HOH   HOH A . 
D 3 HOH   90  390 154  HOH   HOH A . 
D 3 HOH   91  391 148  HOH   HOH A . 
D 3 HOH   92  392 186  HOH   HOH A . 
D 3 HOH   93  393 134  HOH   HOH A . 
D 3 HOH   94  394 121  HOH   HOH A . 
D 3 HOH   95  395 116  HOH   HOH A . 
D 3 HOH   96  396 278  HOH   HOH A . 
D 3 HOH   97  397 24   HOH   HOH A . 
D 3 HOH   98  398 58   HOH   HOH A . 
D 3 HOH   99  399 3    HOH   HOH A . 
D 3 HOH   100 400 83   HOH   HOH A . 
D 3 HOH   101 401 78   HOH   HOH A . 
D 3 HOH   102 402 25   HOH   HOH A . 
D 3 HOH   103 403 7    HOH   HOH A . 
D 3 HOH   104 404 4    HOH   HOH A . 
D 3 HOH   105 405 67   HOH   HOH A . 
D 3 HOH   106 406 74   HOH   HOH A . 
D 3 HOH   107 407 351  HOH   HOH A . 
D 3 HOH   108 408 53   HOH   HOH A . 
D 3 HOH   109 409 1068 HOH   HOH A . 
D 3 HOH   110 410 34   HOH   HOH A . 
D 3 HOH   111 411 1315 HOH   HOH A . 
D 3 HOH   112 412 1308 HOH   HOH A . 
D 3 HOH   113 413 123  HOH   HOH A . 
D 3 HOH   114 414 303  HOH   HOH A . 
D 3 HOH   115 415 1289 HOH   HOH A . 
D 3 HOH   116 416 95   HOH   HOH A . 
D 3 HOH   117 417 1279 HOH   HOH A . 
D 3 HOH   118 418 68   HOH   HOH A . 
D 3 HOH   119 419 122  HOH   HOH A . 
D 3 HOH   120 420 125  HOH   HOH A . 
D 3 HOH   121 421 405  HOH   HOH A . 
D 3 HOH   122 422 397  HOH   HOH A . 
D 3 HOH   123 423 1222 HOH   HOH A . 
D 3 HOH   124 424 333  HOH   HOH A . 
D 3 HOH   125 425 212  HOH   HOH A . 
D 3 HOH   126 426 51   HOH   HOH A . 
D 3 HOH   127 427 582  HOH   HOH A . 
D 3 HOH   128 428 16   HOH   HOH A . 
D 3 HOH   129 429 381  HOH   HOH A . 
D 3 HOH   130 430 1275 HOH   HOH A . 
D 3 HOH   131 431 70   HOH   HOH A . 
D 3 HOH   132 432 71   HOH   HOH A . 
D 3 HOH   133 433 3    HOH   HOH A . 
D 3 HOH   134 434 1238 HOH   HOH A . 
D 3 HOH   135 435 80   HOH   HOH A . 
D 3 HOH   136 436 156  HOH   HOH A . 
D 3 HOH   137 437 73   HOH   HOH A . 
D 3 HOH   138 438 1286 HOH   HOH A . 
D 3 HOH   139 439 952  HOH   HOH A . 
D 3 HOH   140 440 576  HOH   HOH A . 
D 3 HOH   141 441 104  HOH   HOH A . 
D 3 HOH   142 442 94   HOH   HOH A . 
D 3 HOH   143 443 944  HOH   HOH A . 
D 3 HOH   144 444 1296 HOH   HOH A . 
D 3 HOH   145 445 188  HOH   HOH A . 
D 3 HOH   146 446 97   HOH   HOH A . 
D 3 HOH   147 447 1189 HOH   HOH A . 
D 3 HOH   148 448 79   HOH   HOH A . 
D 3 HOH   149 449 1094 HOH   HOH A . 
D 3 HOH   150 450 509  HOH   HOH A . 
D 3 HOH   151 451 330  HOH   HOH A . 
D 3 HOH   152 452 107  HOH   HOH A . 
D 3 HOH   153 453 726  HOH   HOH A . 
D 3 HOH   154 454 163  HOH   HOH A . 
D 3 HOH   155 455 1119 HOH   HOH A . 
D 3 HOH   156 456 408  HOH   HOH A . 
D 3 HOH   157 457 342  HOH   HOH A . 
D 3 HOH   158 458 711  HOH   HOH A . 
D 3 HOH   159 459 756  HOH   HOH A . 
D 3 HOH   160 460 361  HOH   HOH A . 
D 3 HOH   161 461 126  HOH   HOH A . 
D 3 HOH   162 462 319  HOH   HOH A . 
D 3 HOH   163 463 370  HOH   HOH A . 
D 3 HOH   164 464 521  HOH   HOH A . 
D 3 HOH   165 465 801  HOH   HOH A . 
D 3 HOH   166 466 556  HOH   HOH A . 
D 3 HOH   167 467 1307 HOH   HOH A . 
D 3 HOH   168 468 250  HOH   HOH A . 
D 3 HOH   169 469 63   HOH   HOH A . 
D 3 HOH   170 470 280  HOH   HOH A . 
D 3 HOH   171 471 1276 HOH   HOH A . 
D 3 HOH   172 472 1287 HOH   HOH A . 
D 3 HOH   173 473 135  HOH   HOH A . 
D 3 HOH   174 474 674  HOH   HOH A . 
D 3 HOH   175 475 1306 HOH   HOH A . 
D 3 HOH   176 476 224  HOH   HOH A . 
D 3 HOH   177 477 318  HOH   HOH A . 
D 3 HOH   178 478 695  HOH   HOH A . 
D 3 HOH   179 479 202  HOH   HOH A . 
D 3 HOH   180 480 981  HOH   HOH A . 
D 3 HOH   181 481 919  HOH   HOH A . 
D 3 HOH   182 482 309  HOH   HOH A . 
D 3 HOH   183 483 1314 HOH   HOH A . 
D 3 HOH   184 484 267  HOH   HOH A . 
D 3 HOH   185 485 315  HOH   HOH A . 
D 3 HOH   186 486 331  HOH   HOH A . 
D 3 HOH   187 487 1299 HOH   HOH A . 
D 3 HOH   188 488 805  HOH   HOH A . 
D 3 HOH   189 489 941  HOH   HOH A . 
D 3 HOH   190 490 263  HOH   HOH A . 
D 3 HOH   191 491 152  HOH   HOH A . 
D 3 HOH   192 492 356  HOH   HOH A . 
D 3 HOH   193 493 326  HOH   HOH A . 
D 3 HOH   194 494 208  HOH   HOH A . 
D 3 HOH   195 495 1071 HOH   HOH A . 
D 3 HOH   196 496 180  HOH   HOH A . 
D 3 HOH   197 497 363  HOH   HOH A . 
D 3 HOH   198 498 371  HOH   HOH A . 
D 3 HOH   199 499 313  HOH   HOH A . 
D 3 HOH   200 500 1284 HOH   HOH A . 
D 3 HOH   201 501 1    HOH   HOH A . 
D 3 HOH   202 502 772  HOH   HOH A . 
D 3 HOH   203 503 185  HOH   HOH A . 
D 3 HOH   204 504 429  HOH   HOH A . 
D 3 HOH   205 505 376  HOH   HOH A . 
D 3 HOH   206 506 1074 HOH   HOH A . 
D 3 HOH   207 507 1292 HOH   HOH A . 
D 3 HOH   208 508 346  HOH   HOH A . 
D 3 HOH   209 509 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 1249 HOH   HOH B . 
E 3 HOH   3   203 205  HOH   HOH B . 
E 3 HOH   4   204 549  HOH   HOH B . 
E 3 HOH   5   205 240  HOH   HOH B . 
E 3 HOH   6   206 120  HOH   HOH B . 
E 3 HOH   7   207 531  HOH   HOH B . 
E 3 HOH   8   208 264  HOH   HOH B . 
E 3 HOH   9   209 50   HOH   HOH B . 
E 3 HOH   10  210 364  HOH   HOH B . 
E 3 HOH   11  211 358  HOH   HOH B . 
E 3 HOH   12  212 398  HOH   HOH B . 
E 3 HOH   13  213 758  HOH   HOH B . 
E 3 HOH   14  214 900  HOH   HOH B . 
E 3 HOH   15  215 743  HOH   HOH B . 
E 3 HOH   16  216 353  HOH   HOH B . 
E 3 HOH   17  217 1278 HOH   HOH B . 
E 3 HOH   18  218 75   HOH   HOH B . 
E 3 HOH   19  219 444  HOH   HOH B . 
E 3 HOH   20  220 232  HOH   HOH B . 
E 3 HOH   21  221 452  HOH   HOH B . 
E 3 HOH   22  222 131  HOH   HOH B . 
E 3 HOH   23  223 343  HOH   HOH B . 
E 3 HOH   24  224 332  HOH   HOH B . 
E 3 HOH   25  225 69   HOH   HOH B . 
E 3 HOH   26  226 1312 HOH   HOH B . 
E 3 HOH   27  227 172  HOH   HOH B . 
E 3 HOH   28  228 82   HOH   HOH B . 
E 3 HOH   29  229 54   HOH   HOH B . 
E 3 HOH   30  230 300  HOH   HOH B . 
E 3 HOH   31  231 1140 HOH   HOH B . 
E 3 HOH   32  232 127  HOH   HOH B . 
E 3 HOH   33  233 1    HOH   HOH B . 
E 3 HOH   34  234 52   HOH   HOH B . 
E 3 HOH   35  235 60   HOH   HOH B . 
E 3 HOH   36  236 325  HOH   HOH B . 
E 3 HOH   37  237 128  HOH   HOH B . 
E 3 HOH   38  238 110  HOH   HOH B . 
E 3 HOH   39  239 272  HOH   HOH B . 
E 3 HOH   40  240 129  HOH   HOH B . 
E 3 HOH   41  241 9    HOH   HOH B . 
E 3 HOH   42  242 133  HOH   HOH B . 
E 3 HOH   43  243 166  HOH   HOH B . 
E 3 HOH   44  244 723  HOH   HOH B . 
E 3 HOH   45  245 144  HOH   HOH B . 
E 3 HOH   46  246 181  HOH   HOH B . 
E 3 HOH   47  247 14   HOH   HOH B . 
E 3 HOH   48  248 221  HOH   HOH B . 
E 3 HOH   49  249 143  HOH   HOH B . 
E 3 HOH   50  250 654  HOH   HOH B . 
E 3 HOH   51  251 391  HOH   HOH B . 
E 3 HOH   52  252 276  HOH   HOH B . 
E 3 HOH   53  253 231  HOH   HOH B . 
E 3 HOH   54  254 41   HOH   HOH B . 
E 3 HOH   55  255 30   HOH   HOH B . 
E 3 HOH   56  256 243  HOH   HOH B . 
E 3 HOH   57  257 150  HOH   HOH B . 
E 3 HOH   58  258 47   HOH   HOH B . 
E 3 HOH   59  259 1277 HOH   HOH B . 
E 3 HOH   60  260 10   HOH   HOH B . 
E 3 HOH   61  261 31   HOH   HOH B . 
E 3 HOH   62  262 62   HOH   HOH B . 
E 3 HOH   63  263 347  HOH   HOH B . 
E 3 HOH   64  264 72   HOH   HOH B . 
E 3 HOH   65  265 103  HOH   HOH B . 
E 3 HOH   66  266 271  HOH   HOH B . 
E 3 HOH   67  267 117  HOH   HOH B . 
E 3 HOH   68  268 242  HOH   HOH B . 
E 3 HOH   69  269 287  HOH   HOH B . 
E 3 HOH   70  270 11   HOH   HOH B . 
E 3 HOH   71  271 147  HOH   HOH B . 
E 3 HOH   72  272 1285 HOH   HOH B . 
E 3 HOH   73  273 20   HOH   HOH B . 
E 3 HOH   74  274 175  HOH   HOH B . 
E 3 HOH   75  275 84   HOH   HOH B . 
E 3 HOH   76  276 43   HOH   HOH B . 
E 3 HOH   77  277 302  HOH   HOH B . 
E 3 HOH   78  278 59   HOH   HOH B . 
E 3 HOH   79  279 77   HOH   HOH B . 
E 3 HOH   80  280 61   HOH   HOH B . 
E 3 HOH   81  281 22   HOH   HOH B . 
E 3 HOH   82  282 416  HOH   HOH B . 
E 3 HOH   83  283 235  HOH   HOH B . 
E 3 HOH   84  284 1106 HOH   HOH B . 
E 3 HOH   85  285 114  HOH   HOH B . 
E 3 HOH   86  286 13   HOH   HOH B . 
E 3 HOH   87  287 106  HOH   HOH B . 
E 3 HOH   88  288 89   HOH   HOH B . 
E 3 HOH   89  289 1305 HOH   HOH B . 
E 3 HOH   90  290 960  HOH   HOH B . 
E 3 HOH   91  291 99   HOH   HOH B . 
E 3 HOH   92  292 252  HOH   HOH B . 
E 3 HOH   93  293 88   HOH   HOH B . 
E 3 HOH   94  294 635  HOH   HOH B . 
E 3 HOH   95  295 297  HOH   HOH B . 
E 3 HOH   96  296 137  HOH   HOH B . 
E 3 HOH   97  297 282  HOH   HOH B . 
E 3 HOH   98  298 55   HOH   HOH B . 
E 3 HOH   99  299 112  HOH   HOH B . 
E 3 HOH   100 300 100  HOH   HOH B . 
E 3 HOH   101 301 220  HOH   HOH B . 
E 3 HOH   102 302 1066 HOH   HOH B . 
E 3 HOH   103 303 316  HOH   HOH B . 
E 3 HOH   104 304 38   HOH   HOH B . 
E 3 HOH   105 305 160  HOH   HOH B . 
E 3 HOH   106 306 32   HOH   HOH B . 
E 3 HOH   107 307 341  HOH   HOH B . 
E 3 HOH   108 308 182  HOH   HOH B . 
E 3 HOH   109 309 44   HOH   HOH B . 
E 3 HOH   110 310 216  HOH   HOH B . 
E 3 HOH   111 311 197  HOH   HOH B . 
E 3 HOH   112 312 101  HOH   HOH B . 
E 3 HOH   113 313 170  HOH   HOH B . 
E 3 HOH   114 314 1291 HOH   HOH B . 
E 3 HOH   115 315 23   HOH   HOH B . 
E 3 HOH   116 316 299  HOH   HOH B . 
E 3 HOH   117 317 37   HOH   HOH B . 
E 3 HOH   118 318 142  HOH   HOH B . 
E 3 HOH   119 319 311  HOH   HOH B . 
E 3 HOH   120 320 118  HOH   HOH B . 
E 3 HOH   121 321 717  HOH   HOH B . 
E 3 HOH   122 322 141  HOH   HOH B . 
E 3 HOH   123 323 215  HOH   HOH B . 
E 3 HOH   124 324 48   HOH   HOH B . 
E 3 HOH   125 325 91   HOH   HOH B . 
E 3 HOH   126 326 1294 HOH   HOH B . 
E 3 HOH   127 327 28   HOH   HOH B . 
E 3 HOH   128 328 207  HOH   HOH B . 
E 3 HOH   129 329 387  HOH   HOH B . 
E 3 HOH   130 330 177  HOH   HOH B . 
E 3 HOH   131 331 704  HOH   HOH B . 
E 3 HOH   132 332 1274 HOH   HOH B . 
E 3 HOH   133 333 29   HOH   HOH B . 
E 3 HOH   134 334 98   HOH   HOH B . 
E 3 HOH   135 335 161  HOH   HOH B . 
E 3 HOH   136 336 334  HOH   HOH B . 
E 3 HOH   137 337 87   HOH   HOH B . 
E 3 HOH   138 338 234  HOH   HOH B . 
E 3 HOH   139 339 65   HOH   HOH B . 
E 3 HOH   140 340 445  HOH   HOH B . 
E 3 HOH   141 341 619  HOH   HOH B . 
E 3 HOH   142 342 178  HOH   HOH B . 
E 3 HOH   143 343 1293 HOH   HOH B . 
E 3 HOH   144 344 362  HOH   HOH B . 
E 3 HOH   145 345 1126 HOH   HOH B . 
E 3 HOH   146 346 463  HOH   HOH B . 
E 3 HOH   147 347 90   HOH   HOH B . 
E 3 HOH   148 348 623  HOH   HOH B . 
E 3 HOH   149 349 1304 HOH   HOH B . 
E 3 HOH   150 350 1046 HOH   HOH B . 
E 3 HOH   151 351 191  HOH   HOH B . 
E 3 HOH   152 352 1280 HOH   HOH B . 
E 3 HOH   153 353 339  HOH   HOH B . 
E 3 HOH   154 354 335  HOH   HOH B . 
E 3 HOH   155 355 304  HOH   HOH B . 
E 3 HOH   156 356 203  HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 479  HOH   HOH B . 
E 3 HOH   159 359 1077 HOH   HOH B . 
E 3 HOH   160 360 541  HOH   HOH B . 
E 3 HOH   161 361 718  HOH   HOH B . 
E 3 HOH   162 362 389  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 283  HOH   HOH B . 
E 3 HOH   165 365 615  HOH   HOH B . 
E 3 HOH   166 366 291  HOH   HOH B . 
E 3 HOH   167 367 373  HOH   HOH B . 
E 3 HOH   168 368 340  HOH   HOH B . 
E 3 HOH   169 369 898  HOH   HOH B . 
E 3 HOH   170 370 1316 HOH   HOH B . 
E 3 HOH   171 371 310  HOH   HOH B . 
E 3 HOH   172 372 667  HOH   HOH B . 
E 3 HOH   173 373 1303 HOH   HOH B . 
E 3 HOH   174 374 1000 HOH   HOH B . 
E 3 HOH   175 375 431  HOH   HOH B . 
E 3 HOH   176 376 183  HOH   HOH B . 
E 3 HOH   177 377 190  HOH   HOH B . 
E 3 HOH   178 378 149  HOH   HOH B . 
E 3 HOH   179 379 418  HOH   HOH B . 
E 3 HOH   180 380 1173 HOH   HOH B . 
E 3 HOH   181 381 1311 HOH   HOH B . 
E 3 HOH   182 382 1163 HOH   HOH B . 
E 3 HOH   183 383 176  HOH   HOH B . 
E 3 HOH   184 384 424  HOH   HOH B . 
E 3 HOH   185 385 491  HOH   HOH B . 
E 3 HOH   186 386 1298 HOH   HOH B . 
E 3 HOH   187 387 350  HOH   HOH B . 
E 3 HOH   188 388 470  HOH   HOH B . 
E 3 HOH   189 389 265  HOH   HOH B . 
E 3 HOH   190 390 248  HOH   HOH B . 
E 3 HOH   191 391 184  HOH   HOH B . 
E 3 HOH   192 392 360  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 355  HOH   HOH B . 
E 3 HOH   195 395 274  HOH   HOH B . 
E 3 HOH   196 396 314  HOH   HOH B . 
E 3 HOH   197 397 157  HOH   HOH B . 
E 3 HOH   198 398 566  HOH   HOH B . 
E 3 HOH   199 399 792  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCT 
_cell.length_a           88.782 
_cell.length_b           88.782 
_cell.length_c           39.417 
_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                         7HCT 
_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          7HCT 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.53 
_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   2023-03-04 
_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                     7HCT 
_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            1.010 
_reflns.number_obs                   160152 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.085 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.500 
_reflns.B_iso_Wilson_estimate        12.830 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.093 
_reflns.pdbx_Rpim_I_all              0.036 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1019642 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.010 1.030  ? 36569 7328 ? 3.030 ? ? ? 5.000 ? 0.300  ? ? ? ? ? ? 92.900 3.377 1.458 0.293 ? 
1 2 5.530 44.390 ? 7234  1066 ? 0.040 ? ? ? 6.800 ? 30.200 ? ? ? ? ? ? 99.900 0.043 0.016 0.999 ? 
# 
_refine.entry_id                                 7HCT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0100 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.6500 
_refine.ls_number_reflns_obs                     158242 
_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                          0.1598 
_refine.ls_R_factor_R_work                       0.1590 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1754 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7623 
_refine.ls_number_reflns_R_work                  150619 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.3665 
_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                            0.1700 
_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                                87.520 
_refine.B_iso_min                                7.970 
_refine.pdbx_overall_phase_error                 22.5600 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0100 
_refine_hist.d_res_low                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.number_atoms_solvent             410 
_refine_hist.number_atoms_total               2985 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           23.55 
_refine_hist.pdbx_B_iso_mean_solvent          32.02 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0100 1.0200  30 62.0000  3170 . 0.5666 0.5995 . 127 0.0000 3297 . 'X-RAY DIFFRACTION' . 
1.0200 1.0300  30 99.0000  5020 . 0.5062 0.4753 . 233 0.0000 5253 . 'X-RAY DIFFRACTION' . 
1.0300 1.0500  30 100.0000 5006 . 0.4595 0.4341 . 273 0.0000 5279 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5028 . 0.3977 0.4064 . 312 0.0000 5340 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 5025 . 0.3575 0.3636 . 249 0.0000 5274 . 'X-RAY DIFFRACTION' . 
1.0700 1.0900  30 100.0000 5117 . 0.3291 0.3550 . 256 0.0000 5373 . 'X-RAY DIFFRACTION' . 
1.0900 1.1000  30 100.0000 5040 . 0.2918 0.3045 . 243 0.0000 5283 . 'X-RAY DIFFRACTION' . 
1.1000 1.1200  30 100.0000 5044 . 0.2714 0.3018 . 270 0.0000 5314 . 'X-RAY DIFFRACTION' . 
1.1200 1.1400  30 100.0000 5095 . 0.2423 0.3016 . 220 0.0000 5315 . 'X-RAY DIFFRACTION' . 
1.1400 1.1600  30 100.0000 5106 . 0.2269 0.2573 . 258 0.0000 5364 . 'X-RAY DIFFRACTION' . 
1.1600 1.1800  30 100.0000 5010 . 0.2009 0.2206 . 264 0.0000 5274 . 'X-RAY DIFFRACTION' . 
1.1800 1.2000  30 100.0000 5130 . 0.1865 0.2283 . 249 0.0000 5379 . 'X-RAY DIFFRACTION' . 
1.2000 1.2200  30 100.0000 4999 . 0.1685 0.2095 . 279 0.0000 5278 . 'X-RAY DIFFRACTION' . 
1.2200 1.2500  30 100.0000 5038 . 0.1647 0.2035 . 245 0.0000 5283 . 'X-RAY DIFFRACTION' . 
1.2500 1.2700  30 100.0000 5154 . 0.1633 0.1836 . 242 0.0000 5396 . 'X-RAY DIFFRACTION' . 
1.2700 1.3000  30 100.0000 5066 . 0.1515 0.1745 . 243 0.0000 5309 . 'X-RAY DIFFRACTION' . 
1.3000 1.3400  30 100.0000 5024 . 0.1523 0.1930 . 288 0.0000 5312 . 'X-RAY DIFFRACTION' . 
1.3400 1.3700  30 100.0000 5078 . 0.1458 0.1795 . 265 0.0000 5343 . 'X-RAY DIFFRACTION' . 
1.3700 1.4100  30 100.0000 5135 . 0.1360 0.1769 . 220 0.0000 5355 . 'X-RAY DIFFRACTION' . 
1.4100 1.4600  30 100.0000 5070 . 0.1324 0.1462 . 280 0.0000 5350 . 'X-RAY DIFFRACTION' . 
1.4600 1.5100  30 100.0000 5093 . 0.1248 0.1242 . 245 0.0000 5338 . 'X-RAY DIFFRACTION' . 
1.5100 1.5700  30 100.0000 5091 . 0.1232 0.1570 . 265 0.0000 5356 . 'X-RAY DIFFRACTION' . 
1.5700 1.6400  30 100.0000 5092 . 0.1278 0.1446 . 274 0.0000 5366 . 'X-RAY DIFFRACTION' . 
1.6400 1.7300  30 100.0000 5098 . 0.1344 0.1647 . 220 0.0000 5318 . 'X-RAY DIFFRACTION' . 
1.7300 1.8400  30 100.0000 5089 . 0.1375 0.1521 . 267 0.0000 5356 . 'X-RAY DIFFRACTION' . 
1.8400 1.9800  30 100.0000 5130 . 0.1346 0.1313 . 280 0.0000 5410 . 'X-RAY DIFFRACTION' . 
1.9800 2.1800  30 100.0000 5097 . 0.1392 0.1570 . 277 0.0000 5374 . 'X-RAY DIFFRACTION' . 
2.1800 2.4900  30 100.0000 5120 . 0.1353 0.1390 . 260 0.0000 5380 . 'X-RAY DIFFRACTION' . 
2.4900 3.1400  30 100.0000 5170 . 0.1499 0.1657 . 261 0.0000 5431 . 'X-RAY DIFFRACTION' . 
3.1400 44.3900 30 100.0000 5284 . 0.1523 0.1713 . 258 0.0000 5542 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCT 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000612' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCT 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HCT A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCT 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 7HCT SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCT MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCT SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCT MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCT 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HD1 A HIS 91  ? ? O A HOH 306 ? ? 1.56 
2 1 O   A HOH 419 ? ? O A HOH 470 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.11 -133.40 
2 1 SER A 128 ? B 67.67 -1.86   
3 1 HIS B 86  ? ? 57.48 -127.52 
# 
_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 507 ? 5.90 . 
2 1 O ? A HOH 508 ? 6.02 . 
3 1 O ? A HOH 509 ? 7.70 . 
4 1 O ? B HOH 401 ? 6.33 . 
# 
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 
A1A6N N2   N Y N 1   
A1A6N C3   C N R 2   
A1A6N C6   C Y N 3   
A1A6N C9   C Y N 4   
A1A6N C12  C N N 5   
A1A6N C1   C N N 6   
A1A6N C10  C Y N 7   
A1A6N C11  C Y N 8   
A1A6N C2   C N N 9   
A1A6N C4   C N N 10  
A1A6N C5   C N N 11  
A1A6N C7   C Y N 12  
A1A6N C8   C Y N 13  
A1A6N N1   N N N 14  
A1A6N N3   N Y N 15  
A1A6N N4   N Y N 16  
A1A6N O1   O N N 17  
A1A6N H15  H N N 18  
A1A6N H16  H N N 19  
A1A6N H3   H N N 20  
A1A6N H2   H N N 21  
A1A6N H1   H N N 22  
A1A6N H12  H N N 23  
A1A6N H13  H N N 24  
A1A6N H4   H N N 25  
A1A6N H5   H N N 26  
A1A6N H8   H N N 27  
A1A6N H7   H N N 28  
A1A6N H9   H N N 29  
A1A6N H10  H N N 30  
A1A6N H11  H N N 31  
A1A6N H14  H N N 32  
A1A6N H6   H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H N N 106 
CYS   N    N N N 107 
CYS   CA   C N R 108 
CYS   C    C N N 109 
CYS   O    O N N 110 
CYS   CB   C N N 111 
CYS   SG   S N N 112 
CYS   OXT  O N N 113 
CYS   H    H N N 114 
CYS   H2   H N N 115 
CYS   HA   H N N 116 
CYS   HB2  H N N 117 
CYS   HB3  H N N 118 
CYS   HG   H N N 119 
CYS   HXT  H N N 120 
GLN   N    N N N 121 
GLN   CA   C N S 122 
GLN   C    C N N 123 
GLN   O    O N N 124 
GLN   CB   C N N 125 
GLN   CG   C N N 126 
GLN   CD   C N N 127 
GLN   OE1  O N N 128 
GLN   NE2  N N N 129 
GLN   OXT  O N N 130 
GLN   H    H N N 131 
GLN   H2   H N N 132 
GLN   HA   H N N 133 
GLN   HB2  H N N 134 
GLN   HB3  H N N 135 
GLN   HG2  H N N 136 
GLN   HG3  H N N 137 
GLN   HE21 H N N 138 
GLN   HE22 H N N 139 
GLN   HXT  H N N 140 
GLU   N    N N N 141 
GLU   CA   C N S 142 
GLU   C    C N N 143 
GLU   O    O N N 144 
GLU   CB   C N N 145 
GLU   CG   C N N 146 
GLU   CD   C N N 147 
GLU   OE1  O N N 148 
GLU   OE2  O N N 149 
GLU   OXT  O N N 150 
GLU   H    H N N 151 
GLU   H2   H N N 152 
GLU   HA   H N N 153 
GLU   HB2  H N N 154 
GLU   HB3  H N N 155 
GLU   HG2  H N N 156 
GLU   HG3  H N N 157 
GLU   HE2  H N N 158 
GLU   HXT  H N N 159 
GLY   N    N N N 160 
GLY   CA   C N N 161 
GLY   C    C N N 162 
GLY   O    O N N 163 
GLY   OXT  O N N 164 
GLY   H    H N N 165 
GLY   H2   H N N 166 
GLY   HA2  H N N 167 
GLY   HA3  H N N 168 
GLY   HXT  H N N 169 
HIS   N    N N N 170 
HIS   CA   C N S 171 
HIS   C    C N N 172 
HIS   O    O N N 173 
HIS   CB   C N N 174 
HIS   CG   C Y N 175 
HIS   ND1  N Y N 176 
HIS   CD2  C Y N 177 
HIS   CE1  C Y N 178 
HIS   NE2  N Y N 179 
HIS   OXT  O N N 180 
HIS   H    H N N 181 
HIS   H2   H N N 182 
HIS   HA   H N N 183 
HIS   HB2  H N N 184 
HIS   HB3  H N N 185 
HIS   HD1  H N N 186 
HIS   HD2  H N N 187 
HIS   HE1  H N N 188 
HIS   HE2  H N N 189 
HIS   HXT  H N N 190 
HOH   O    O N N 191 
HOH   H1   H N N 192 
HOH   H2   H N N 193 
ILE   N    N N N 194 
ILE   CA   C N S 195 
ILE   C    C N N 196 
ILE   O    O N N 197 
ILE   CB   C N S 198 
ILE   CG1  C N N 199 
ILE   CG2  C N N 200 
ILE   CD1  C N N 201 
ILE   OXT  O N N 202 
ILE   H    H N N 203 
ILE   H2   H N N 204 
ILE   HA   H N N 205 
ILE   HB   H N N 206 
ILE   HG12 H N N 207 
ILE   HG13 H N N 208 
ILE   HG21 H N N 209 
ILE   HG22 H N N 210 
ILE   HG23 H N N 211 
ILE   HD11 H N N 212 
ILE   HD12 H N N 213 
ILE   HD13 H N N 214 
ILE   HXT  H N N 215 
LEU   N    N N N 216 
LEU   CA   C N S 217 
LEU   C    C N N 218 
LEU   O    O N N 219 
LEU   CB   C N N 220 
LEU   CG   C N N 221 
LEU   CD1  C N N 222 
LEU   CD2  C N N 223 
LEU   OXT  O N N 224 
LEU   H    H N N 225 
LEU   H2   H N N 226 
LEU   HA   H N N 227 
LEU   HB2  H N N 228 
LEU   HB3  H N N 229 
LEU   HG   H N N 230 
LEU   HD11 H N N 231 
LEU   HD12 H N N 232 
LEU   HD13 H N N 233 
LEU   HD21 H N N 234 
LEU   HD22 H N N 235 
LEU   HD23 H N N 236 
LEU   HXT  H N N 237 
LYS   N    N N N 238 
LYS   CA   C N S 239 
LYS   C    C N N 240 
LYS   O    O N N 241 
LYS   CB   C N N 242 
LYS   CG   C N N 243 
LYS   CD   C N N 244 
LYS   CE   C N N 245 
LYS   NZ   N N N 246 
LYS   OXT  O N N 247 
LYS   H    H N N 248 
LYS   H2   H N N 249 
LYS   HA   H N N 250 
LYS   HB2  H N N 251 
LYS   HB3  H N N 252 
LYS   HG2  H N N 253 
LYS   HG3  H N N 254 
LYS   HD2  H N N 255 
LYS   HD3  H N N 256 
LYS   HE2  H N N 257 
LYS   HE3  H N N 258 
LYS   HZ1  H N N 259 
LYS   HZ2  H N N 260 
LYS   HZ3  H N N 261 
LYS   HXT  H N N 262 
MET   N    N N N 263 
MET   CA   C N S 264 
MET   C    C N N 265 
MET   O    O N N 266 
MET   CB   C N N 267 
MET   CG   C N N 268 
MET   SD   S N N 269 
MET   CE   C N N 270 
MET   OXT  O N N 271 
MET   H    H N N 272 
MET   H2   H N N 273 
MET   HA   H N N 274 
MET   HB2  H N N 275 
MET   HB3  H N N 276 
MET   HG2  H N N 277 
MET   HG3  H N N 278 
MET   HE1  H N N 279 
MET   HE2  H N N 280 
MET   HE3  H N N 281 
MET   HXT  H N N 282 
PHE   N    N N N 283 
PHE   CA   C N S 284 
PHE   C    C N N 285 
PHE   O    O N N 286 
PHE   CB   C N N 287 
PHE   CG   C Y N 288 
PHE   CD1  C Y N 289 
PHE   CD2  C Y N 290 
PHE   CE1  C Y N 291 
PHE   CE2  C Y N 292 
PHE   CZ   C Y N 293 
PHE   OXT  O N N 294 
PHE   H    H N N 295 
PHE   H2   H N N 296 
PHE   HA   H N N 297 
PHE   HB2  H N N 298 
PHE   HB3  H N N 299 
PHE   HD1  H N N 300 
PHE   HD2  H N N 301 
PHE   HE1  H N N 302 
PHE   HE2  H N N 303 
PHE   HZ   H N N 304 
PHE   HXT  H N N 305 
PRO   N    N N N 306 
PRO   CA   C N S 307 
PRO   C    C N N 308 
PRO   O    O N N 309 
PRO   CB   C N N 310 
PRO   CG   C N N 311 
PRO   CD   C N N 312 
PRO   OXT  O N N 313 
PRO   H    H N N 314 
PRO   HA   H N N 315 
PRO   HB2  H N N 316 
PRO   HB3  H N N 317 
PRO   HG2  H N N 318 
PRO   HG3  H N N 319 
PRO   HD2  H N N 320 
PRO   HD3  H N N 321 
PRO   HXT  H N N 322 
SER   N    N N N 323 
SER   CA   C N S 324 
SER   C    C N N 325 
SER   O    O N N 326 
SER   CB   C N N 327 
SER   OG   O N N 328 
SER   OXT  O N N 329 
SER   H    H N N 330 
SER   H2   H N N 331 
SER   HA   H N N 332 
SER   HB2  H N N 333 
SER   HB3  H N N 334 
SER   HG   H N N 335 
SER   HXT  H N N 336 
THR   N    N N N 337 
THR   CA   C N S 338 
THR   C    C N N 339 
THR   O    O N N 340 
THR   CB   C N R 341 
THR   OG1  O N N 342 
THR   CG2  C N N 343 
THR   OXT  O N N 344 
THR   H    H N N 345 
THR   H2   H N N 346 
THR   HA   H N N 347 
THR   HB   H N N 348 
THR   HG1  H N N 349 
THR   HG21 H N N 350 
THR   HG22 H N N 351 
THR   HG23 H N N 352 
THR   HXT  H N N 353 
TYR   N    N N N 354 
TYR   CA   C N S 355 
TYR   C    C N N 356 
TYR   O    O N N 357 
TYR   CB   C N N 358 
TYR   CG   C Y N 359 
TYR   CD1  C Y N 360 
TYR   CD2  C Y N 361 
TYR   CE1  C Y N 362 
TYR   CE2  C Y N 363 
TYR   CZ   C Y N 364 
TYR   OH   O N N 365 
TYR   OXT  O N N 366 
TYR   H    H N N 367 
TYR   H2   H N N 368 
TYR   HA   H N N 369 
TYR   HB2  H N N 370 
TYR   HB3  H N N 371 
TYR   HD1  H N N 372 
TYR   HD2  H N N 373 
TYR   HE1  H N N 374 
TYR   HE2  H N N 375 
TYR   HH   H N N 376 
TYR   HXT  H N N 377 
VAL   N    N N N 378 
VAL   CA   C N S 379 
VAL   C    C N N 380 
VAL   O    O N N 381 
VAL   CB   C N N 382 
VAL   CG1  C N N 383 
VAL   CG2  C N N 384 
VAL   OXT  O N N 385 
VAL   H    H N N 386 
VAL   H2   H N N 387 
VAL   HA   H N N 388 
VAL   HB   H N N 389 
VAL   HG11 H N N 390 
VAL   HG12 H N N 391 
VAL   HG13 H N N 392 
VAL   HG21 H N N 393 
VAL   HG22 H N N 394 
VAL   HG23 H N N 395 
VAL   HXT  H N N 396 
# 
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 
A1A6N O1  C3   sing N N 1   
A1A6N C2  C1   sing N N 2   
A1A6N C2  C3   sing N N 3   
A1A6N C3  C4   sing N N 4   
A1A6N C3  C12  sing N N 5   
A1A6N C4  C5   sing N N 6   
A1A6N C12 N1   sing N N 7   
A1A6N C5  N1   sing N N 8   
A1A6N N1  C6   sing N N 9   
A1A6N C6  C9   doub Y N 10  
A1A6N C6  N2   sing Y N 11  
A1A6N C10 C9   sing Y N 12  
A1A6N C10 C11  doub Y N 13  
A1A6N C9  C8   sing Y N 14  
A1A6N N2  C7   doub Y N 15  
A1A6N C11 N4   sing Y N 16  
A1A6N C7  N3   sing Y N 17  
A1A6N C8  N4   sing Y N 18  
A1A6N C8  N3   doub Y N 19  
A1A6N C12 H15  sing N N 20  
A1A6N C12 H16  sing N N 21  
A1A6N C1  H3   sing N N 22  
A1A6N C1  H2   sing N N 23  
A1A6N C1  H1   sing N N 24  
A1A6N C10 H12  sing N N 25  
A1A6N C11 H13  sing N N 26  
A1A6N C2  H4   sing N N 27  
A1A6N C2  H5   sing N N 28  
A1A6N C4  H8   sing N N 29  
A1A6N C4  H7   sing N N 30  
A1A6N C5  H9   sing N N 31  
A1A6N C5  H10  sing N N 32  
A1A6N C7  H11  sing N N 33  
A1A6N N4  H14  sing N N 34  
A1A6N O1  H6   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
THR   N   CA   sing N N 325 
THR   N   H    sing N N 326 
THR   N   H2   sing N N 327 
THR   CA  C    sing N N 328 
THR   CA  CB   sing N N 329 
THR   CA  HA   sing N N 330 
THR   C   O    doub N N 331 
THR   C   OXT  sing N N 332 
THR   CB  OG1  sing N N 333 
THR   CB  CG2  sing N N 334 
THR   CB  HB   sing N N 335 
THR   OG1 HG1  sing N N 336 
THR   CG2 HG21 sing N N 337 
THR   CG2 HG22 sing N N 338 
THR   CG2 HG23 sing N N 339 
THR   OXT HXT  sing N N 340 
TYR   N   CA   sing N N 341 
TYR   N   H    sing N N 342 
TYR   N   H2   sing N N 343 
TYR   CA  C    sing N N 344 
TYR   CA  CB   sing N N 345 
TYR   CA  HA   sing N N 346 
TYR   C   O    doub N N 347 
TYR   C   OXT  sing N N 348 
TYR   CB  CG   sing N N 349 
TYR   CB  HB2  sing N N 350 
TYR   CB  HB3  sing N N 351 
TYR   CG  CD1  doub Y N 352 
TYR   CG  CD2  sing Y N 353 
TYR   CD1 CE1  sing Y N 354 
TYR   CD1 HD1  sing N N 355 
TYR   CD2 CE2  doub Y N 356 
TYR   CD2 HD2  sing N N 357 
TYR   CE1 CZ   doub Y N 358 
TYR   CE1 HE1  sing N N 359 
TYR   CE2 CZ   sing Y N 360 
TYR   CE2 HE2  sing N N 361 
TYR   CZ  OH   sing N N 362 
TYR   OH  HH   sing N N 363 
TYR   OXT HXT  sing N N 364 
VAL   N   CA   sing N N 365 
VAL   N   H    sing N N 366 
VAL   N   H2   sing N N 367 
VAL   CA  C    sing N N 368 
VAL   CA  CB   sing N N 369 
VAL   CA  HA   sing N N 370 
VAL   C   O    doub N N 371 
VAL   C   OXT  sing N N 372 
VAL   CB  CG1  sing N N 373 
VAL   CB  CG2  sing N N 374 
VAL   CB  HB   sing N N 375 
VAL   CG1 HG11 sing N N 376 
VAL   CG1 HG12 sing N N 377 
VAL   CG1 HG13 sing N N 378 
VAL   CG2 HG21 sing N N 379 
VAL   CG2 HG22 sing N N 380 
VAL   CG2 HG23 sing N N 381 
VAL   OXT HXT  sing N N 382 
# 
_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                    7HCT 
_atom_sites.fract_transf_matrix[1][1]   0.011264 
_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]   0.011264 
_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]   0.025370 
_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   ? 19.673 -16.173 22.214  0.66 61.18 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.607 -15.964 22.350  0.34 58.88 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.697 -15.103 22.386  0.66 60.71 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.631 -14.900 22.546  0.34 58.43 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.342 -13.750 22.110  0.66 58.63 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.263 -13.543 22.256  0.34 56.45 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.447 -13.474 22.580  0.66 59.25 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.330 -13.224 22.783  0.34 56.94 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.060 -15.146 23.792  0.66 61.86 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.037 -14.941 23.968  0.34 59.55 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.029 -14.035 23.949  0.66 62.22 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.015 -13.827 24.147  0.34 59.92 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.426 -16.506 24.048  0.66 62.19 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.409 -16.300 24.246  0.34 59.88 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.986 -15.224 21.742  0.66 72.82 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.901 -15.025 21.923  0.34 70.09 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.751 -15.010 24.459  0.66 74.20 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.747 -14.803 24.613  0.34 71.43 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.522 -14.188 24.762  0.66 74.63 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.524 -13.980 24.969  0.34 71.87 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.487 -13.182 24.002  0.66 74.63 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.478 -12.976 24.193  0.34 71.87 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.434 -14.046 23.183  0.66 74.63 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.405 -13.834 23.393  0.34 71.87 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.971 -16.486 24.905  0.66 74.60 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.977 -16.276 25.114  0.34 71.83 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.789 -16.694 23.341  0.66 74.60 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.755 -16.492 23.556  0.34 71.83 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.120 -17.183 24.057  0.66 74.60 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.104 -16.977 24.241  0.34 71.83 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.651 -12.912 21.339  0.66 55.48 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.602 -12.748 21.417  0.34 53.59 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.099 -11.555 21.048  0.66 51.90 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.055 -11.401 21.091  0.34 50.40 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.947 -10.582 21.292  0.66 48.53 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.927 -10.409 21.363  0.34 47.37 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.833 -10.979 21.647  0.66 48.56 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.829 -10.783 21.789  0.34 47.44 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.681 -11.440 19.631  0.66 51.33 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.586 -11.306 19.653  0.34 50.00 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.705 -11.871 18.557  0.66 50.75 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.566 -11.732 18.618  0.34 49.59 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.545 -11.460 18.553  0.66 50.58 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.406 -11.323 18.663  0.34 49.45 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.174 -12.709 17.637  0.66 50.57 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.998 -12.562 17.674  0.34 49.47 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.901 -13.115 20.967  0.66 66.55 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.871 -12.974 21.022  0.34 64.28 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.806 -11.329 21.665  0.66 62.25 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.788 -11.177 21.677  0.34 60.45 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.923 -10.514 19.463  0.66 61.57 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.836 -10.386 19.468  0.34 59.97 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.468 -12.004 19.566  0.66 61.57 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.361 -11.882 19.563  0.34 59.97 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.662 -12.984 17.003  0.66 60.66 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.462 -12.833 17.059  0.34 59.33 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.991 -12.977 17.675  0.66 60.66 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.817 -12.829 17.678  0.34 59.33 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.225 -9.293  21.100  0.66 44.81 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.205 -9.130  21.113  0.34 44.08 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.308 -8.224  21.478  0.66 41.10 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.312 -8.044  21.495  0.34 40.79 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.453 -7.722  20.319  0.66 36.42 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.427 -7.561  20.351  0.34 36.78 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.801 -6.681  20.455  0.66 36.39 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.778 -6.518  20.486  0.34 36.74 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.080 -7.057  22.095  0.66 42.15 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.112 -6.871  22.067  0.34 41.53 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.041 -6.545  21.188  0.66 42.86 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.993 -6.331  21.098  0.34 42.01 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.954 -9.011  20.744  0.66 53.74 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.918 -8.867  20.712  0.34 52.86 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.710 -8.566  22.160  0.66 49.29 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.729 -8.364  22.198  0.34 48.92 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.453 -6.351  22.324  0.66 50.55 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.493 -6.180  22.355  0.34 49.81 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.534 -7.366  22.894  0.66 50.55 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.631 -7.185  22.824  0.34 49.81 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.454 -5.903  21.540  0.66 51.41 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.421 -5.687  21.427  0.34 50.38 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.439 -8.422  19.188  0.66 31.60 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.384 -8.282  19.235  0.34 32.78 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.525 -8.061  18.113  0.66 27.11 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.452 -7.933  18.171  0.34 28.96 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.100 -8.432  18.507  0.66 26.73 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.034 -8.294  18.594  0.34 28.00 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.856 -9.508  19.056  0.66 28.01 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.805 -9.321  19.239  0.34 28.59 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.915 -8.777  16.822  0.66 24.01 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.823 -8.663  16.881  0.34 26.57 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.190 -8.265  16.207  0.66 21.91 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.107 -8.183  16.261  0.34 24.69 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.200 -7.087  15.482  0.66 20.86 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.139 -7.013  15.521  0.34 23.84 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.373 -8.969  16.351  0.66 22.18 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.279 -8.904  16.415  0.34 24.27 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.370 -6.616  14.915  0.66 20.28 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.317 -6.569  14.949  0.34 23.35 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.543 -8.509  15.786  0.66 21.61 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.459 -8.467  15.846  0.34 23.76 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.542 -7.329  15.067  0.66 20.93 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.478 -7.297  15.111  0.34 23.45 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.941 -9.101  19.020  0.66 37.89 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.875 -8.969  19.071  0.34 39.30 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.559 -7.109  17.963  0.66 32.50 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.489 -6.981  18.008  0.34 34.73 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.032 -9.724  17.013  0.66 28.79 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.923 -9.609  17.072  0.34 31.85 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.202 -8.663  16.174  0.66 28.79 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.115 -8.532  16.231  0.34 31.85 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.409 -6.607  15.379  0.66 25.00 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.358 -6.519  15.409  0.34 28.58 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.376 -9.766  16.836  0.66 26.58 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.272 -9.692  16.909  0.34 29.09 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.366 -5.821  14.430  0.66 24.31 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.328 -5.780  14.454  0.34 27.99 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.334 -8.990  15.892  0.66 25.90 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.241 -8.959  15.957  0.34 28.49 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.330 -7.013  14.687  0.66 25.08 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.272 -6.999  14.727  0.34 28.12 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.155 -7.536  18.223  0.66 24.93 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.077 -7.438  18.239  0.34 26.45 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.781 -7.679  18.688  0.66 24.76 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.705 -7.592  18.705  0.34 25.56 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.797 -7.393  17.560  0.66 21.89 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.724 -7.331  17.571  0.34 23.17 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.034 -6.525  16.717  0.66 21.64 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.937 -6.442  16.744  0.34 22.96 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.518 -6.716  19.854  0.66 27.26 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.415 -6.625  19.859  0.34 27.10 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.155 -6.726  20.231  0.66 29.32 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.099 -6.803  20.353  0.34 28.41 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.292 -6.832  17.754  0.66 29.88 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.201 -6.758  17.726  0.34 31.71 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.634 -8.585  19.002  0.66 29.68 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.572 -8.497  19.023  0.34 30.64 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.058 -6.990  20.615  0.66 32.68 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.046 -6.792  20.577  0.34 32.49 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.769 -5.819  19.581  0.66 32.68 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.515 -5.714  19.538  0.34 32.49 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.032 -6.190  20.867  0.66 35.15 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 9.956  -6.263  20.980  0.34 34.06 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.688  -8.134  17.548  0.66 20.59 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.645  -8.113  17.544  0.34 21.51 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.615  -7.863  16.612  0.66 19.70 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.571  -7.883  16.600  0.34 20.21 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.808  -8.397  15.213  0.66 18.47 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.802  -8.402  15.201  0.34 18.81 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.089  -7.974  14.302  0.66 19.04 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.106  -7.971  14.276  0.34 19.11 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.540  -8.794  18.076  0.66 24.68 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.515  -8.781  18.068  0.34 25.78 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.796  -8.243  16.962  0.66 23.61 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.764  -8.298  16.940  0.34 24.22 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.495  -6.902  16.547  0.66 23.61 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.412  -6.928  16.536  0.34 24.22 ?  8   GLY   A HA3  1 
ATOM   157  N N    . TYR   A 1 9   ? 9.751  -9.315  15.009  1.00 17.66 ?  9   TYR   A N    1 
ATOM   158  C CA   . TYR   A 1 9   ? 10.032 -9.859  13.686  1.00 15.76 ?  9   TYR   A CA   1 
ATOM   159  C C    . TYR   A 1 9   ? 9.171  -11.083 13.398  1.00 15.06 ?  9   TYR   A C    1 
ATOM   160  O O    . TYR   A 1 9   ? 8.891  -11.896 14.285  1.00 16.61 ?  9   TYR   A O    1 
ATOM   161  C CB   . TYR   A 1 9   ? 11.514 -10.238 13.543  1.00 16.17 ?  9   TYR   A CB   1 
ATOM   162  C CG   . TYR   A 1 9   ? 12.431 -9.044  13.374  1.00 16.07 ?  9   TYR   A CG   1 
ATOM   163  C CD1  . TYR   A 1 9   ? 12.749 -8.247  14.460  1.00 16.76 ?  9   TYR   A CD1  1 
ATOM   164  C CD2  . TYR   A 1 9   ? 12.944 -8.701  12.130  1.00 15.61 ?  9   TYR   A CD2  1 
ATOM   165  C CE1  . TYR   A 1 9   ? 13.566 -7.140  14.318  1.00 17.26 ?  9   TYR   A CE1  1 
ATOM   166  C CE2  . TYR   A 1 9   ? 13.755 -7.594  11.975  1.00 16.62 ?  9   TYR   A CE2  1 
ATOM   167  C CZ   . TYR   A 1 9   ? 14.062 -6.813  13.068  1.00 17.43 ?  9   TYR   A CZ   1 
ATOM   168  O OH   . TYR   A 1 9   ? 14.864 -5.710  12.901  1.00 18.91 ?  9   TYR   A OH   1 
ATOM   169  H H    A TYR   A 1 9   ? 10.251 -9.640  15.629  0.66 21.17 ?  9   TYR   A H    1 
ATOM   170  H H    B TYR   A 1 9   ? 10.254 -9.632  15.631  0.34 21.17 ?  9   TYR   A H    1 
ATOM   171  H HA   . TYR   A 1 9   ? 9.829  -9.185  13.018  1.00 18.89 ?  9   TYR   A HA   1 
ATOM   172  H HB2  . TYR   A 1 9   ? 11.786 -10.732 14.333  1.00 19.38 ?  9   TYR   A HB2  1 
ATOM   173  H HB3  . TYR   A 1 9   ? 11.599 -10.802 12.758  1.00 19.38 ?  9   TYR   A HB3  1 
ATOM   174  H HD1  . TYR   A 1 9   ? 12.401 -8.469  15.301  1.00 20.09 ?  9   TYR   A HD1  1 
ATOM   175  H HD2  . TYR   A 1 9   ? 12.729 -9.221  11.388  1.00 18.70 ?  9   TYR   A HD2  1 
ATOM   176  H HE1  . TYR   A 1 9   ? 13.768 -6.618  15.059  1.00 20.68 ?  9   TYR   A HE1  1 
ATOM   177  H HE2  . TYR   A 1 9   ? 14.093 -7.375  11.138  1.00 19.91 ?  9   TYR   A HE2  1 
ATOM   178  H HH   . TYR   A 1 9   ? 14.986 -5.335  13.645  1.00 22.66 ?  9   TYR   A HH   1 
ATOM   179  N N    . LEU   A 1 10  ? 8.748  -11.194 12.146  1.00 14.84 ?  10  LEU   A N    1 
ATOM   180  C CA   . LEU   A 1 10  ? 8.158  -12.418 11.628  1.00 14.61 ?  10  LEU   A CA   1 
ATOM   181  C C    . LEU   A 1 10  ? 9.290  -13.340 11.186  1.00 14.18 ?  10  LEU   A C    1 
ATOM   182  O O    . LEU   A 1 10  ? 10.252 -12.903 10.548  1.00 14.33 ?  10  LEU   A O    1 
ATOM   183  C CB   . LEU   A 1 10  ? 7.266  -12.081 10.431  1.00 16.38 ?  10  LEU   A CB   1 
ATOM   184  C CG   . LEU   A 1 10  ? 6.613  -13.258 9.699   1.00 18.67 ?  10  LEU   A CG   1 
ATOM   185  C CD1  . LEU   A 1 10  ? 5.544  -13.897 10.559  1.00 20.74 ?  10  LEU   A CD1  1 
ATOM   186  C CD2  . LEU   A 1 10  ? 6.049  -12.838 8.352   1.00 21.32 ?  10  LEU   A CD2  1 
ATOM   187  H H    . LEU   A 1 10  ? 8.798  -10.563 11.564  1.00 17.78 ?  10  LEU   A H    1 
ATOM   188  H HA   . LEU   A 1 10  ? 7.624  -12.855 12.315  1.00 17.50 ?  10  LEU   A HA   1 
ATOM   189  H HB2  . LEU   A 1 10  ? 6.547  -11.506 10.741  1.00 19.63 ?  10  LEU   A HB2  1 
ATOM   190  H HB3  . LEU   A 1 10  ? 7.801  -11.603 9.783   1.00 19.63 ?  10  LEU   A HB3  1 
ATOM   191  H HG   . LEU   A 1 10  ? 7.293  -13.931 9.533   1.00 22.37 ?  10  LEU   A HG   1 
ATOM   192  H HD11 . LEU   A 1 10  ? 5.154  -14.640 10.076  1.00 24.86 ?  10  LEU   A HD11 1 
ATOM   193  H HD12 . LEU   A 1 10  ? 5.948  -14.213 11.384  1.00 24.86 ?  10  LEU   A HD12 1 
ATOM   194  H HD13 . LEU   A 1 10  ? 4.865  -13.235 10.758  1.00 24.86 ?  10  LEU   A HD13 1 
ATOM   195  H HD21 . LEU   A 1 10  ? 5.651  -13.613 7.927   1.00 25.55 ?  10  LEU   A HD21 1 
ATOM   196  H HD22 . LEU   A 1 10  ? 5.381  -12.153 8.492   1.00 25.55 ?  10  LEU   A HD22 1 
ATOM   197  H HD23 . LEU   A 1 10  ? 6.772  -12.494 7.804   1.00 25.55 ?  10  LEU   A HD23 1 
ATOM   198  N N    . LYS   A 1 11  ? 9.178  -14.620 11.537  1.00 14.51 ?  11  LYS   A N    1 
ATOM   199  C CA   . LYS   A 1 11  ? 10.187 -15.612 11.187  1.00 14.31 ?  11  LYS   A CA   1 
ATOM   200  C C    . LYS   A 1 11  ? 9.837  -16.176 9.817   1.00 14.60 ?  11  LYS   A C    1 
ATOM   201  O O    . LYS   A 1 11  ? 8.744  -16.720 9.636   1.00 16.86 ?  11  LYS   A O    1 
ATOM   202  C CB   . LYS   A 1 11  ? 10.211 -16.715 12.247  1.00 14.00 ?  11  LYS   A CB   1 
ATOM   203  C CG   . LYS   A 1 11  ? 11.249 -17.807 12.051  1.00 14.14 ?  11  LYS   A CG   1 
ATOM   204  C CD   . LYS   A 1 11  ? 11.316 -18.668 13.306  1.00 14.62 ?  11  LYS   A CD   1 
ATOM   205  C CE   . LYS   A 1 11  ? 12.321 -19.806 13.189  1.00 15.17 ?  11  LYS   A CE   1 
ATOM   206  N NZ   . LYS   A 1 11  ? 13.708 -19.331 12.960  1.00 15.74 ?  11  LYS   A NZ   1 
ATOM   207  H H    . LYS   A 1 11  ? 8.513  -14.943 11.977  1.00 17.38 ?  11  LYS   A H    1 
ATOM   208  H HA   . LYS   A 1 11  ? 11.062 -15.189 11.139  1.00 17.15 ?  11  LYS   A HA   1 
ATOM   209  H HB2  . LYS   A 1 11  ? 10.388 -16.298 13.107  1.00 16.77 ?  11  LYS   A HB2  1 
ATOM   210  H HB3  . LYS   A 1 11  ? 9.343  -17.137 12.264  1.00 16.77 ?  11  LYS   A HB3  1 
ATOM   211  H HG2  . LYS   A 1 11  ? 10.997 -18.365 11.300  1.00 16.94 ?  11  LYS   A HG2  1 
ATOM   212  H HG3  . LYS   A 1 11  ? 12.122 -17.407 11.903  1.00 16.94 ?  11  LYS   A HG3  1 
ATOM   213  H HD2  . LYS   A 1 11  ? 11.569 -18.114 14.061  1.00 17.52 ?  11  LYS   A HD2  1 
ATOM   214  H HD3  . LYS   A 1 11  ? 10.437 -19.059 13.467  1.00 17.52 ?  11  LYS   A HD3  1 
ATOM   215  H HE2  . LYS   A 1 11  ? 12.313 -20.320 14.012  1.00 18.17 ?  11  LYS   A HE2  1 
ATOM   216  H HE3  . LYS   A 1 11  ? 12.071 -20.371 12.443  1.00 18.17 ?  11  LYS   A HE3  1 
ATOM   217  H HZ1  . LYS   A 1 11  ? 14.239 -20.025 12.777  1.00 18.86 ?  11  LYS   A HZ1  1 
ATOM   218  H HZ2  . LYS   A 1 11  ? 13.730 -18.765 12.277  1.00 18.86 ?  11  LYS   A HZ2  1 
ATOM   219  H HZ3  . LYS   A 1 11  ? 14.016 -18.921 13.688  1.00 18.86 ?  11  LYS   A HZ3  1 
ATOM   220  N N    . LEU   A 1 12  ? 10.745 -16.046 8.851   1.00 13.65 ?  12  LEU   A N    1 
ATOM   221  C CA   . LEU   A 1 12  ? 10.506 -16.615 7.527   1.00 14.11 ?  12  LEU   A CA   1 
ATOM   222  C C    . LEU   A 1 12  ? 11.094 -18.013 7.381   1.00 14.02 ?  12  LEU   A C    1 
ATOM   223  O O    . LEU   A 1 12  ? 10.471 -18.885 6.764   1.00 14.86 ?  12  LEU   A O    1 
ATOM   224  C CB   . LEU   A 1 12  ? 11.089 -15.718 6.431   1.00 15.21 ?  12  LEU   A CB   1 
ATOM   225  C CG   . LEU   A 1 12  ? 10.426 -14.353 6.252   1.00 16.11 ?  12  LEU   A CG   1 
ATOM   226  C CD1  . LEU   A 1 12  ? 11.180 -13.547 5.206   1.00 16.66 ?  12  LEU   A CD1  1 
ATOM   227  C CD2  . LEU   A 1 12  ? 8.956  -14.514 5.872   1.00 17.09 ?  12  LEU   A CD2  1 
ATOM   228  H H    . LEU   A 1 12  ? 11.509 -15.644 8.930   1.00 16.35 ?  12  LEU   A H    1 
ATOM   229  H HA   . LEU   A 1 12  ? 9.552  -16.685 7.382   1.00 16.90 ?  12  LEU   A HA   1 
ATOM   230  H HB2  . LEU   A 1 12  ? 12.024 -15.564 6.632   1.00 18.23 ?  12  LEU   A HB2  1 
ATOM   231  H HB3  . LEU   A 1 12  ? 11.016 -16.191 5.585   1.00 18.23 ?  12  LEU   A HB3  1 
ATOM   232  H HG   . LEU   A 1 12  ? 10.468 -13.874 7.091   1.00 19.30 ?  12  LEU   A HG   1 
ATOM   233  H HD11 . LEU   A 1 12  ? 10.754 -12.684 5.100   1.00 19.96 ?  12  LEU   A HD11 1 
ATOM   234  H HD12 . LEU   A 1 12  ? 12.101 -13.424 5.504   1.00 19.96 ?  12  LEU   A HD12 1 
ATOM   235  H HD13 . LEU   A 1 12  ? 11.174 -14.027 4.363   1.00 19.96 ?  12  LEU   A HD13 1 
ATOM   236  H HD21 . LEU   A 1 12  ? 8.605  -13.649 5.609   1.00 20.47 ?  12  LEU   A HD21 1 
ATOM   237  H HD22 . LEU   A 1 12  ? 8.888  -15.138 5.131   1.00 20.47 ?  12  LEU   A HD22 1 
ATOM   238  H HD23 . LEU   A 1 12  ? 8.466  -14.852 6.636   1.00 20.47 ?  12  LEU   A HD23 1 
ATOM   239  N N    . THR   A 1 13  ? 12.298 -18.227 7.907   1.00 14.10 ?  13  THR   A N    1 
ATOM   240  C CA   . THR   A 1 13  ? 12.992 -19.508 7.829   1.00 14.15 ?  13  THR   A CA   1 
ATOM   241  C C    . THR   A 1 13  ? 13.740 -19.732 9.137   1.00 14.19 ?  13  THR   A C    1 
ATOM   242  O O    . THR   A 1 13  ? 13.641 -18.948 10.087  1.00 14.61 ?  13  THR   A O    1 
ATOM   243  C CB   . THR   A 1 13  ? 13.977 -19.563 6.651   1.00 15.36 ?  13  THR   A CB   1 
ATOM   244  O OG1  . THR   A 1 13  ? 15.034 -18.633 6.890   1.00 15.79 ?  13  THR   A OG1  1 
ATOM   245  C CG2  . THR   A 1 13  ? 13.303 -19.224 5.329   1.00 16.43 ?  13  THR   A CG2  1 
ATOM   246  H H    . THR   A 1 13  ? 12.753 -17.623 8.312   1.00 16.89 ?  13  THR   A H    1 
ATOM   247  H HA   . THR   A 1 13  ? 12.345 -20.222 7.715   1.00 16.95 ?  13  THR   A HA   1 
ATOM   248  H HB   . THR   A 1 13  ? 14.344 -20.461 6.578   1.00 18.40 ?  13  THR   A HB   1 
ATOM   249  H HG1  . THR   A 1 13  ? 15.593 -18.665 6.249   1.00 18.92 ?  13  THR   A HG1  1 
ATOM   250  H HG21 . THR   A 1 13  ? 13.922 -19.378 4.593   1.00 19.69 ?  13  THR   A HG21 1 
ATOM   251  H HG22 . THR   A 1 13  ? 12.524 -19.787 5.202   1.00 19.69 ?  13  THR   A HG22 1 
ATOM   252  H HG23 . THR   A 1 13  ? 13.031 -18.297 5.323   1.00 19.69 ?  13  THR   A HG23 1 
ATOM   253  N N    . ASP   A 1 14  ? 14.540 -20.796 9.156   1.00 15.55 ?  14  ASP   A N    1 
ATOM   254  C CA   . ASP   A 1 14  ? 15.378 -21.079 10.308  1.00 16.37 ?  14  ASP   A CA   1 
ATOM   255  C C    . ASP   A 1 14  ? 16.213 -19.873 10.709  1.00 15.40 ?  14  ASP   A C    1 
ATOM   256  O O    . ASP   A 1 14  ? 16.439 -19.640 11.902  1.00 17.16 ?  14  ASP   A O    1 
ATOM   257  C CB   . ASP   A 1 14  ? 16.306 -22.246 9.991   1.00 19.64 ?  14  ASP   A CB   1 
ATOM   258  C CG   . ASP   A 1 14  ? 17.250 -22.532 11.119  1.00 23.31 ?  14  ASP   A CG   1 
ATOM   259  O OD1  . ASP   A 1 14  ? 16.767 -22.900 12.215  1.00 24.97 ?  14  ASP   A OD1  1 
ATOM   260  O OD2  . ASP   A 1 14  ? 18.470 -22.377 10.912  1.00 26.33 -1 14  ASP   A OD2  1 
ATOM   261  H H    . ASP   A 1 14  ? 14.618 -21.362 8.514   1.00 18.64 ?  14  ASP   A H    1 
ATOM   262  H HA   . ASP   A 1 14  ? 14.821 -21.331 11.062  1.00 19.62 ?  14  ASP   A HA   1 
ATOM   263  H HB2  . ASP   A 1 14  ? 15.771 -23.045 9.819   1.00 23.54 ?  14  ASP   A HB2  1 
ATOM   264  H HB3  . ASP   A 1 14  ? 16.829 -22.035 9.197   1.00 23.54 ?  14  ASP   A HB3  1 
ATOM   265  N N    . ASN   A 1 15  ? 16.680 -19.083 9.730   1.00 14.46 ?  15  ASN   A N    1 
ATOM   266  C CA   . ASN   A 1 15  ? 17.669 -18.045 10.000  1.00 14.72 ?  15  ASN   A CA   1 
ATOM   267  C C    . ASN   A 1 15  ? 17.312 -16.654 9.491   1.00 14.90 ?  15  ASN   A C    1 
ATOM   268  O O    . ASN   A 1 15  ? 18.090 -15.726 9.730   1.00 16.17 ?  15  ASN   A O    1 
ATOM   269  C CB   . ASN   A 1 15  ? 19.044 -18.455 9.444   1.00 14.66 ?  15  ASN   A CB   1 
ATOM   270  C CG   . ASN   A 1 15  ? 19.054 -18.547 7.940   1.00 15.02 ?  15  ASN   A CG   1 
ATOM   271  O OD1  . ASN   A 1 15  ? 18.345 -19.376 7.358   1.00 16.29 ?  15  ASN   A OD1  1 
ATOM   272  N ND2  . ASN   A 1 15  ? 19.850 -17.694 7.295   1.00 14.98 ?  15  ASN   A ND2  1 
ATOM   273  H H    . ASN   A 1 15  ? 16.418 -19.114 8.912   1.00 17.32 ?  15  ASN   A H    1 
ATOM   274  H HA   . ASN   A 1 15  ? 17.771 -17.966 10.958  1.00 17.64 ?  15  ASN   A HA   1 
ATOM   275  H HB2  . ASN   A 1 15  ? 19.708 -17.790 9.712   1.00 17.56 ?  15  ASN   A HB2  1 
ATOM   276  H HB3  . ASN   A 1 15  ? 19.288 -19.321 9.801   1.00 17.56 ?  15  ASN   A HB3  1 
ATOM   277  H HD21 . ASN   A 1 15  ? 19.891 -17.706 6.438   1.00 17.95 ?  15  ASN   A HD21 1 
ATOM   278  H HD22 . ASN   A 1 15  ? 20.330 -17.124 7.737   1.00 17.95 ?  15  ASN   A HD22 1 
ATOM   279  N N    . VAL   A 1 16  ? 16.173 -16.466 8.820   1.00 14.71 ?  16  VAL   A N    1 
ATOM   280  C CA   . VAL   A 1 16  ? 15.791 -15.176 8.250   1.00 14.68 ?  16  VAL   A CA   1 
ATOM   281  C C    . VAL   A 1 16  ? 14.513 -14.688 8.916   1.00 14.08 ?  16  VAL   A C    1 
ATOM   282  O O    . VAL   A 1 16  ? 13.517 -15.420 8.986   1.00 13.90 ?  16  VAL   A O    1 
ATOM   283  C CB   . VAL   A 1 16  ? 15.624 -15.251 6.723   1.00 15.58 ?  16  VAL   A CB   1 
ATOM   284  C CG1  . VAL   A 1 16  ? 15.192 -13.884 6.166   1.00 16.55 ?  16  VAL   A CG1  1 
ATOM   285  C CG2  . VAL   A 1 16  ? 16.910 -15.726 6.064   1.00 15.97 ?  16  VAL   A CG2  1 
ATOM   286  H H    . VAL   A 1 16  ? 15.596 -17.086 8.684   1.00 17.62 ?  16  VAL   A H    1 
ATOM   287  H HA   . VAL   A 1 16  ? 16.493 -14.530 8.437   1.00 17.59 ?  16  VAL   A HA   1 
ATOM   288  H HB   . VAL   A 1 16  ? 14.929 -15.890 6.516   1.00 18.67 ?  16  VAL   A HB   1 
ATOM   289  H HG11 . VAL   A 1 16  ? 15.283 -13.894 5.201   1.00 19.84 ?  16  VAL   A HG11 1 
ATOM   290  H HG12 . VAL   A 1 16  ? 14.263 -13.723 6.405   1.00 19.84 ?  16  VAL   A HG12 1 
ATOM   291  H HG13 . VAL   A 1 16  ? 15.755 -13.192 6.544   1.00 19.84 ?  16  VAL   A HG13 1 
ATOM   292  H HG21 . VAL   A 1 16  ? 16.814 -15.665 5.101   1.00 19.14 ?  16  VAL   A HG21 1 
ATOM   293  H HG22 . VAL   A 1 16  ? 17.646 -15.166 6.359   1.00 19.14 ?  16  VAL   A HG22 1 
ATOM   294  H HG23 . VAL   A 1 16  ? 17.075 -16.647 6.322   1.00 19.14 ?  16  VAL   A HG23 1 
ATOM   295  N N    . TYR   A 1 17  ? 14.539 -13.430 9.354   1.00 13.66 ?  17  TYR   A N    1 
ATOM   296  C CA   . TYR   A 1 17  ? 13.440 -12.745 10.024  1.00 13.84 ?  17  TYR   A CA   1 
ATOM   297  C C    . TYR   A 1 17  ? 13.175 -11.421 9.310   1.00 13.96 ?  17  TYR   A C    1 
ATOM   298  O O    . TYR   A 1 17  ? 14.080 -10.869 8.685   1.00 13.95 ?  17  TYR   A O    1 
ATOM   299  C CB   . TYR   A 1 17  ? 13.828 -12.469 11.477  1.00 14.73 ?  17  TYR   A CB   1 
ATOM   300  C CG   . TYR   A 1 17  ? 14.036 -13.730 12.285  1.00 15.20 ?  17  TYR   A CG   1 
ATOM   301  C CD1  . TYR   A 1 17  ? 15.223 -14.457 12.204  1.00 16.60 ?  17  TYR   A CD1  1 
ATOM   302  C CD2  . TYR   A 1 17  ? 13.034 -14.206 13.117  1.00 15.92 ?  17  TYR   A CD2  1 
ATOM   303  C CE1  . TYR   A 1 17  ? 15.401 -15.631 12.937  1.00 17.31 ?  17  TYR   A CE1  1 
ATOM   304  C CE2  . TYR   A 1 17  ? 13.203 -15.375 13.856  1.00 16.88 ?  17  TYR   A CE2  1 
ATOM   305  C CZ   . TYR   A 1 17  ? 14.389 -16.080 13.767  1.00 17.23 ?  17  TYR   A CZ   1 
ATOM   306  O OH   . TYR   A 1 17  ? 14.552 -17.236 14.501  1.00 18.78 ?  17  TYR   A OH   1 
ATOM   307  H H    . TYR   A 1 17  ? 15.231 -12.917 9.254   1.00 16.37 ?  17  TYR   A H    1 
ATOM   308  H HA   . TYR   A 1 17  ? 12.641 -13.294 9.996   1.00 16.58 ?  17  TYR   A HA   1 
ATOM   309  H HB2  . TYR   A 1 17  ? 14.656 -11.963 11.486  1.00 17.65 ?  17  TYR   A HB2  1 
ATOM   310  H HB3  . TYR   A 1 17  ? 13.123 -11.958 11.893  1.00 17.65 ?  17  TYR   A HB3  1 
ATOM   311  H HD1  . TYR   A 1 17  ? 15.908 -14.161 11.644  1.00 19.89 ?  17  TYR   A HD1  1 
ATOM   312  H HD2  . TYR   A 1 17  ? 12.235 -13.739 13.184  1.00 19.07 ?  17  TYR   A HD2  1 
ATOM   313  H HE1  . TYR   A 1 17  ? 16.202 -16.109 12.877  1.00 20.75 ?  17  TYR   A HE1  1 
ATOM   314  H HE2  . TYR   A 1 17  ? 12.524 -15.675 14.411  1.00 20.23 ?  17  TYR   A HE2  1 
ATOM   315  H HH   . TYR   A 1 17  ? 13.819 -17.462 14.842  1.00 22.51 ?  17  TYR   A HH   1 
ATOM   316  N N    A ILE   A 1 18  ? 11.948 -10.901 9.413   0.66 14.00 ?  18  ILE   A N    1 
ATOM   317  N N    B ILE   A 1 18  ? 11.946 -10.905 9.414   0.34 14.04 ?  18  ILE   A N    1 
ATOM   318  C CA   A ILE   A 1 18  ? 11.563 -9.706  8.653   0.66 14.19 ?  18  ILE   A CA   1 
ATOM   319  C CA   B ILE   A 1 18  ? 11.553 -9.700  8.685   0.34 14.26 ?  18  ILE   A CA   1 
ATOM   320  C C    A ILE   A 1 18  ? 10.585 -8.853  9.459   0.66 14.61 ?  18  ILE   A C    1 
ATOM   321  C C    B ILE   A 1 18  ? 10.630 -8.833  9.536   0.34 14.45 ?  18  ILE   A C    1 
ATOM   322  O O    A ILE   A 1 18  ? 9.715  -9.373  10.161  0.66 15.10 ?  18  ILE   A O    1 
ATOM   323  O O    B ILE   A 1 18  ? 9.901  -9.329  10.400  0.34 14.52 ?  18  ILE   A O    1 
ATOM   324  C CB   A ILE   A 1 18  ? 11.020 -10.101 7.261   0.66 14.17 ?  18  ILE   A CB   1 
ATOM   325  C CB   B ILE   A 1 18  ? 10.919 -10.061 7.319   0.34 14.52 ?  18  ILE   A CB   1 
ATOM   326  C CG1  A ILE   A 1 18  ? 10.914 -8.884  6.343   0.66 15.35 ?  18  ILE   A CG1  1 
ATOM   327  C CG1  B ILE   A 1 18  ? 10.890 -8.848  6.387   0.34 15.23 ?  18  ILE   A CG1  1 
ATOM   328  C CG2  A ILE   A 1 18  ? 9.691  -10.857 7.382   0.66 14.52 ?  18  ILE   A CG2  1 
ATOM   329  C CG2  B ILE   A 1 18  ? 9.525  -10.653 7.506   0.34 14.86 ?  18  ILE   A CG2  1 
ATOM   330  C CD1  A ILE   A 1 18  ? 10.731 -9.258  4.895   0.66 17.02 ?  18  ILE   A CD1  1 
ATOM   331  C CD1  B ILE   A 1 18  ? 10.624 -9.211  4.943   0.34 16.26 ?  18  ILE   A CD1  1 
ATOM   332  H H    A ILE   A 1 18  ? 11.325 -11.229 9.903   0.66 16.77 ?  18  ILE   A H    1 
ATOM   333  H H    B ILE   A 1 18  ? 11.325 -11.244 9.899   0.34 16.82 ?  18  ILE   A H    1 
ATOM   334  H HA   A ILE   A 1 18  ? 12.363 -9.176  8.506   0.66 17.00 ?  18  ILE   A HA   1 
ATOM   335  H HA   B ILE   A 1 18  ? 12.351 -9.183  8.503   0.34 17.09 ?  18  ILE   A HA   1 
ATOM   336  H HB   A ILE   A 1 18  ? 11.660 -10.706 6.860   0.66 16.97 ?  18  ILE   A HB   1 
ATOM   337  H HB   B ILE   A 1 18  ? 11.472 -10.737 6.902   0.34 17.40 ?  18  ILE   A HB   1 
ATOM   338  H HG12 A ILE   A 1 18  ? 10.155 -8.345  6.609   0.66 18.39 ?  18  ILE   A HG12 1 
ATOM   339  H HG12 B ILE   A 1 18  ? 10.192 -8.241  6.673   0.34 18.24 ?  18  ILE   A HG12 1 
ATOM   340  H HG13 A ILE   A 1 18  ? 11.731 -8.361  6.411   0.66 18.39 ?  18  ILE   A HG13 1 
ATOM   341  H HG13 B ILE   A 1 18  ? 11.752 -8.401  6.422   0.34 18.24 ?  18  ILE   A HG13 1 
ATOM   342  H HG21 A ILE   A 1 18  ? 9.440  -11.199 6.507   0.66 17.39 ?  18  ILE   A HG21 1 
ATOM   343  H HG21 B ILE   A 1 18  ? 9.204  -10.978 6.650   0.34 17.81 ?  18  ILE   A HG21 1 
ATOM   344  H HG22 A ILE   A 1 18  ? 9.802  -11.595 8.001   0.66 17.39 ?  18  ILE   A HG22 1 
ATOM   345  H HG22 B ILE   A 1 18  ? 9.580  -11.385 8.138   0.34 17.81 ?  18  ILE   A HG22 1 
ATOM   346  H HG23 A ILE   A 1 18  ? 9.006  -10.253 7.707   0.66 17.39 ?  18  ILE   A HG23 1 
ATOM   347  H HG23 B ILE   A 1 18  ? 8.927  -9.970  7.843   0.34 17.81 ?  18  ILE   A HG23 1 
ATOM   348  H HD11 A ILE   A 1 18  ? 10.729 -8.450  4.356   0.66 20.39 ?  18  ILE   A HD11 1 
ATOM   349  H HD11 B ILE   A 1 18  ? 10.667 -8.407  4.400   0.34 19.49 ?  18  ILE   A HD11 1 
ATOM   350  H HD12 A ILE   A 1 18  ? 11.460 -9.835  4.622   0.66 20.39 ?  18  ILE   A HD12 1 
ATOM   351  H HD12 B ILE   A 1 18  ? 11.296 -9.845  4.646   0.34 19.49 ?  18  ILE   A HD12 1 
ATOM   352  H HD13 A ILE   A 1 18  ? 9.885  -9.722  4.794   0.66 20.39 ?  18  ILE   A HD13 1 
ATOM   353  H HD13 B ILE   A 1 18  ? 9.742  -9.608  4.874   0.34 19.49 ?  18  ILE   A HD13 1 
ATOM   354  N N    A LYS   A 1 19  ? 10.729 -7.529  9.331   0.66 14.79 ?  19  LYS   A N    1 
ATOM   355  N N    B LYS   A 1 19  ? 10.665 -7.521  9.280   0.34 14.89 ?  19  LYS   A N    1 
ATOM   356  C CA   A LYS   A 1 19  ? 9.914  -6.563  10.062  0.66 16.29 ?  19  LYS   A CA   1 
ATOM   357  C CA   B LYS   A 1 19  ? 9.869  -6.564  10.042  0.34 15.86 ?  19  LYS   A CA   1 
ATOM   358  C C    A LYS   A 1 19  ? 9.689  -5.341  9.182   0.66 16.12 ?  19  LYS   A C    1 
ATOM   359  C C    B LYS   A 1 19  ? 9.704  -5.274  9.244   0.34 15.27 ?  19  LYS   A C    1 
ATOM   360  O O    A LYS   A 1 19  ? 10.545 -4.985  8.367   0.66 15.89 ?  19  LYS   A O    1 
ATOM   361  O O    B LYS   A 1 19  ? 10.667 -4.782  8.651   0.34 14.88 ?  19  LYS   A O    1 
ATOM   362  C CB   A LYS   A 1 19  ? 10.653 -6.135  11.339  0.66 16.83 ?  19  LYS   A CB   1 
ATOM   363  C CB   B LYS   A 1 19  ? 10.551 -6.257  11.381  0.34 16.93 ?  19  LYS   A CB   1 
ATOM   364  C CG   A LYS   A 1 19  ? 9.904  -5.232  12.308  0.66 18.37 ?  19  LYS   A CG   1 
ATOM   365  C CG   B LYS   A 1 19  ? 9.813  -5.268  12.268  0.34 18.07 ?  19  LYS   A CG   1 
ATOM   366  C CD   A LYS   A 1 19  ? 10.815 -4.949  13.499  0.66 19.99 ?  19  LYS   A CD   1 
ATOM   367  C CD   B LYS   A 1 19  ? 10.613 -4.995  13.529  0.34 19.29 ?  19  LYS   A CD   1 
ATOM   368  C CE   A LYS   A 1 19  ? 10.187 -4.056  14.549  0.66 21.08 ?  19  LYS   A CE   1 
ATOM   369  C CE   B LYS   A 1 19  ? 9.920  -3.996  14.438  0.34 20.10 ?  19  LYS   A CE   1 
ATOM   370  N NZ   A LYS   A 1 19  ? 11.120 -3.905  15.703  0.66 21.42 ?  19  LYS   A NZ   1 
ATOM   371  N NZ   B LYS   A 1 19  ? 10.747 -3.687  15.636  0.34 20.37 ?  19  LYS   A NZ   1 
ATOM   372  H H    A LYS   A 1 19  ? 11.315 -7.161  8.815   0.66 17.72 ?  19  LYS   A H    1 
ATOM   373  H H    B LYS   A 1 19  ? 11.151 -7.162  8.666   0.34 17.84 ?  19  LYS   A H    1 
ATOM   374  H HA   A LYS   A 1 19  ? 9.062  -6.958  10.298  0.66 19.51 ?  19  LYS   A HA   1 
ATOM   375  H HA   B LYS   A 1 19  ? 8.994  -6.939  10.217  0.34 19.00 ?  19  LYS   A HA   1 
ATOM   376  H HB2  A LYS   A 1 19  ? 10.892 -6.934  11.829  0.66 20.16 ?  19  LYS   A HB2  1 
ATOM   377  H HB2  B LYS   A 1 19  ? 10.639 -7.084  11.879  0.34 20.29 ?  19  LYS   A HB2  1 
ATOM   378  H HB3  A LYS   A 1 19  ? 11.460 -5.665  11.077  0.66 20.16 ?  19  LYS   A HB3  1 
ATOM   379  H HB3  B LYS   A 1 19  ? 11.431 -5.890  11.203  0.34 20.29 ?  19  LYS   A HB3  1 
ATOM   380  H HG2  A LYS   A 1 19  ? 9.683  -4.390  11.877  0.66 22.01 ?  19  LYS   A HG2  1 
ATOM   381  H HG2  B LYS   A 1 19  ? 9.694  -4.429  11.794  0.34 21.66 ?  19  LYS   A HG2  1 
ATOM   382  H HG3  A LYS   A 1 19  ? 9.101  -5.677  12.625  0.66 22.01 ?  19  LYS   A HG3  1 
ATOM   383  H HG3  B LYS   A 1 19  ? 8.953  -5.638  12.522  0.34 21.66 ?  19  LYS   A HG3  1 
ATOM   384  H HD2  A LYS   A 1 19  ? 11.042 -5.792  13.924  0.66 23.96 ?  19  LYS   A HD2  1 
ATOM   385  H HD2  B LYS   A 1 19  ? 10.726 -5.824  14.020  0.34 23.12 ?  19  LYS   A HD2  1 
ATOM   386  H HD3  A LYS   A 1 19  ? 11.621 -4.514  13.180  0.66 23.96 ?  19  LYS   A HD3  1 
ATOM   387  H HD3  B LYS   A 1 19  ? 11.480 -4.632  13.284  0.34 23.12 ?  19  LYS   A HD3  1 
ATOM   388  H HE2  A LYS   A 1 19  ? 10.017 -3.178  14.171  0.66 25.27 ?  19  LYS   A HE2  1 
ATOM   389  H HE2  B LYS   A 1 19  ? 9.771  -3.171  13.950  0.34 24.09 ?  19  LYS   A HE2  1 
ATOM   390  H HE3  A LYS   A 1 19  ? 9.363  -4.455  14.868  0.66 25.27 ?  19  LYS   A HE3  1 
ATOM   391  H HE3  B LYS   A 1 19  ? 9.077  -4.368  14.737  0.34 24.09 ?  19  LYS   A HE3  1 
ATOM   392  H HZ1  A LYS   A 1 19  ? 10.728 -3.438  16.350  0.66 25.68 ?  19  LYS   A HZ1  1 
ATOM   393  H HZ1  B LYS   A 1 19  ? 10.326 -3.098  16.152  0.34 24.42 ?  19  LYS   A HZ1  1 
ATOM   394  H HZ2  A LYS   A 1 19  ? 11.346 -4.705  16.016  0.66 25.68 ?  19  LYS   A HZ2  1 
ATOM   395  H HZ2  B LYS   A 1 19  ? 10.895 -4.430  16.103  0.34 24.42 ?  19  LYS   A HZ2  1 
ATOM   396  H HZ3  A LYS   A 1 19  ? 11.856 -3.478  15.443  0.66 25.68 ?  19  LYS   A HZ3  1 
ATOM   397  H HZ3  B LYS   A 1 19  ? 11.529 -3.344  15.385  0.34 24.42 ?  19  LYS   A HZ3  1 
ATOM   398  N N    A ASN   A 1 20  ? 8.529  -4.699  9.347   0.66 16.83 ?  20  ASN   A N    1 
ATOM   399  N N    B ASN   A 1 20  ? 8.483  -4.731  9.242   0.34 15.37 ?  20  ASN   A N    1 
ATOM   400  C CA   A ASN   A 1 20  ? 8.306  -3.375  8.773   0.66 17.76 ?  20  ASN   A CA   1 
ATOM   401  C CA   B ASN   A 1 20  ? 8.179  -3.447  8.600   0.34 15.70 ?  20  ASN   A CA   1 
ATOM   402  C C    A ASN   A 1 20  ? 8.931  -2.370  9.728   0.66 17.56 ?  20  ASN   A C    1 
ATOM   403  C C    B ASN   A 1 20  ? 8.705  -2.320  9.487   0.34 16.27 ?  20  ASN   A C    1 
ATOM   404  O O    A ASN   A 1 20  ? 8.436  -2.170  10.842  0.66 17.60 ?  20  ASN   A O    1 
ATOM   405  O O    B ASN   A 1 20  ? 8.017  -1.840  10.390  0.34 16.75 ?  20  ASN   A O    1 
ATOM   406  C CB   A ASN   A 1 20  ? 6.813  -3.117  8.576   0.66 18.48 ?  20  ASN   A CB   1 
ATOM   407  C CB   B ASN   A 1 20  ? 6.672  -3.320  8.382   0.34 15.28 ?  20  ASN   A CB   1 
ATOM   408  C CG   A ASN   A 1 20  ? 6.498  -1.662  8.230   0.66 19.80 ?  20  ASN   A CG   1 
ATOM   409  C CG   B ASN   A 1 20  ? 6.265  -1.996  7.728   0.34 15.27 ?  20  ASN   A CG   1 
ATOM   410  O OD1  A ASN   A 1 20  ? 5.558  -1.080  8.772   0.66 21.81 ?  20  ASN   A OD1  1 
ATOM   411  O OD1  B ASN   A 1 20  ? 5.142  -1.506  7.926   0.34 15.03 ?  20  ASN   A OD1  1 
ATOM   412  N ND2  A ASN   A 1 20  ? 7.277  -1.075  7.329   0.66 20.07 ?  20  ASN   A ND2  1 
ATOM   413  N ND2  B ASN   A 1 20  ? 7.167  -1.418  6.943   0.34 16.25 ?  20  ASN   A ND2  1 
ATOM   414  H H    A ASN   A 1 20  ? 7.867  -5.006  9.796   0.66 20.17 ?  20  ASN   A H    1 
ATOM   415  H H    B ASN   A 1 20  ? 7.796  -5.111  9.595   0.34 18.42 ?  20  ASN   A H    1 
ATOM   416  H HA   A ASN   A 1 20  ? 8.747  -3.310  7.915   0.66 21.29 ?  20  ASN   A HA   1 
ATOM   417  H HA   B ASN   A 1 20  ? 8.629  -3.408  7.740   0.34 18.81 ?  20  ASN   A HA   1 
ATOM   418  H HB2  A ASN   A 1 20  ? 6.491  -3.673  7.847   0.66 22.15 ?  20  ASN   A HB2  1 
ATOM   419  H HB2  B ASN   A 1 20  ? 6.371  -4.040  7.811   0.34 18.30 ?  20  ASN   A HB2  1 
ATOM   420  H HB3  A ASN   A 1 20  ? 6.341  -3.338  9.391   0.66 22.15 ?  20  ASN   A HB3  1 
ATOM   421  H HB3  B ASN   A 1 20  ? 6.229  -3.380  9.245   0.34 18.30 ?  20  ASN   A HB3  1 
ATOM   422  H HD21 A ASN   A 1 20  ? 7.132  -0.260  7.103   0.66 24.06 ?  20  ASN   A HD21 1 
ATOM   423  H HD21 B ASN   A 1 20  ? 6.982  -0.674  6.564   0.34 19.47 ?  20  ASN   A HD21 1 
ATOM   424  H HD22 A ASN   A 1 20  ? 7.930  -1.511  6.974   0.66 24.06 ?  20  ASN   A HD22 1 
ATOM   425  H HD22 B ASN   A 1 20  ? 7.938  -1.782  6.819   0.34 19.47 ?  20  ASN   A HD22 1 
ATOM   426  N N    A ALA   A 1 21  ? 10.050 -1.775  9.322   0.66 18.11 ?  21  ALA   A N    1 
ATOM   427  N N    B ALA   A 1 21  ? 9.931  -1.869  9.215   0.34 16.77 ?  21  ALA   A N    1 
ATOM   428  C CA   A ALA   A 1 21  ? 10.759 -0.882  10.223  0.66 17.87 ?  21  ALA   A CA   1 
ATOM   429  C CA   B ALA   A 1 21  ? 10.568 -0.878  10.075  0.34 16.92 ?  21  ALA   A CA   1 
ATOM   430  C C    A ALA   A 1 21  ? 11.712 -0.008  9.432   0.66 17.72 ?  21  ALA   A C    1 
ATOM   431  C C    B ALA   A 1 21  ? 11.694 -0.178  9.327   0.34 15.95 ?  21  ALA   A C    1 
ATOM   432  O O    A ALA   A 1 21  ? 12.160 -0.375  8.341   0.66 18.14 ?  21  ALA   A O    1 
ATOM   433  O O    B ALA   A 1 21  ? 12.207 -0.681  8.323   0.34 15.52 ?  21  ALA   A O    1 
ATOM   434  C CB   A ALA   A 1 21  ? 11.532 -1.668  11.286  0.66 18.68 ?  21  ALA   A CB   1 
ATOM   435  C CB   B ALA   A 1 21  ? 11.101 -1.514  11.365  0.34 18.05 ?  21  ALA   A CB   1 
ATOM   436  H H    A ALA   A 1 21  ? 10.417 -1.879  8.550   0.66 21.71 ?  21  ALA   A H    1 
ATOM   437  H H    B ALA   A 1 21  ? 10.403 -2.111  8.538   0.34 20.10 ?  21  ALA   A H    1 
ATOM   438  H HA   A ALA   A 1 21  ? 10.114 -0.310  10.672  0.66 21.41 ?  21  ALA   A HA   1 
ATOM   439  H HA   B ALA   A 1 21  ? 9.909  -0.214  10.323  0.34 20.27 ?  21  ALA   A HA   1 
ATOM   440  H HB1  A ALA   A 1 21  ? 11.931 -1.040  11.904  0.66 22.39 ?  21  ALA   A HB1  1 
ATOM   441  H HB1  B ALA   A 1 21  ? 11.516 -0.825  11.908  0.34 21.63 ?  21  ALA   A HB1  1 
ATOM   442  H HB2  A ALA   A 1 21  ? 10.910 -2.248  11.762  0.66 22.39 ?  21  ALA   A HB2  1 
ATOM   443  H HB2  B ALA   A 1 21  ? 10.364 -1.918  11.849  0.34 21.63 ?  21  ALA   A HB2  1 
ATOM   444  H HB3  A ALA   A 1 21  ? 12.213 -2.201  10.853  0.66 22.39 ?  21  ALA   A HB3  1 
ATOM   445  H HB3  B ALA   A 1 21  ? 11.757 -2.193  11.137  0.34 21.63 ?  21  ALA   A HB3  1 
ATOM   446  N N    A ASP   A 1 22  ? 11.988 1.163   9.999   0.66 17.65 ?  22  ASP   A N    1 
ATOM   447  N N    B ASP   A 1 22  ? 12.063 1.000   9.838   0.34 15.85 ?  22  ASP   A N    1 
ATOM   448  C CA   A ASP   A 1 22  ? 13.035 2.058   9.524   0.66 16.73 ?  22  ASP   A CA   1 
ATOM   449  C CA   B ASP   A 1 22  ? 13.198 1.765   9.333   0.34 15.84 ?  22  ASP   A CA   1 
ATOM   450  C C    A ASP   A 1 22  ? 14.355 1.560   10.097  0.66 15.65 ?  22  ASP   A C    1 
ATOM   451  C C    B ASP   A 1 22  ? 14.478 1.202   9.947   0.34 14.72 ?  22  ASP   A C    1 
ATOM   452  O O    A ASP   A 1 22  ? 14.560 1.595   11.313  0.66 16.53 ?  22  ASP   A O    1 
ATOM   453  O O    B ASP   A 1 22  ? 14.612 1.148   11.174  0.34 15.05 ?  22  ASP   A O    1 
ATOM   454  C CB   A ASP   A 1 22  ? 12.728 3.466   10.021  0.66 18.25 ?  22  ASP   A CB   1 
ATOM   455  C CB   B ASP   A 1 22  ? 13.024 3.238   9.713   0.34 16.96 ?  22  ASP   A CB   1 
ATOM   456  C CG   A ASP   A 1 22  ? 13.734 4.491   9.549   0.66 19.65 ?  22  ASP   A CG   1 
ATOM   457  C CG   B ASP   A 1 22  ? 14.113 4.137   9.136   0.34 17.64 ?  22  ASP   A CG   1 
ATOM   458  O OD1  A ASP   A 1 22  ? 14.857 4.122   9.166   0.66 19.33 ?  22  ASP   A OD1  1 
ATOM   459  O OD1  B ASP   A 1 22  ? 15.057 3.618   8.506   0.34 17.00 ?  22  ASP   A OD1  1 
ATOM   460  O OD2  A ASP   A 1 22  ? 13.392 5.692   9.563   0.66 21.33 -1 22  ASP   A OD2  1 
ATOM   461  O OD2  B ASP   A 1 22  ? 14.024 5.373   9.312   0.34 19.50 -1 22  ASP   A OD2  1 
ATOM   462  H H    A ASP   A 1 22  ? 11.546 1.472   10.675  0.66 21.15 ?  22  ASP   A H    1 
ATOM   463  H H    B ASP   A 1 22  ? 11.648 1.385   10.491  0.34 19.00 ?  22  ASP   A H    1 
ATOM   464  H HA   A ASP   A 1 22  ? 13.072 2.040   8.555   0.66 20.05 ?  22  ASP   A HA   1 
ATOM   465  H HA   B ASP   A 1 22  ? 13.242 1.689   8.365   0.34 18.98 ?  22  ASP   A HA   1 
ATOM   466  H HB2  A ASP   A 1 22  ? 11.855 3.727   9.694   0.66 21.88 ?  22  ASP   A HB2  1 
ATOM   467  H HB2  B ASP   A 1 22  ? 12.166 3.551   9.385   0.34 20.32 ?  22  ASP   A HB2  1 
ATOM   468  H HB3  A ASP   A 1 22  ? 12.724 3.452   10.994  0.66 21.88 ?  22  ASP   A HB3  1 
ATOM   469  H HB3  B ASP   A 1 22  ? 13.055 3.317   10.680  0.34 20.32 ?  22  ASP   A HB3  1 
ATOM   470  N N    A ILE   A 1 23  ? 15.253 1.099   9.220   0.66 15.10 ?  23  ILE   A N    1 
ATOM   471  N N    B ILE   A 1 23  ? 15.411 0.767   9.095   0.34 14.07 ?  23  ILE   A N    1 
ATOM   472  C CA   A ILE   A 1 23  ? 16.511 0.498   9.660   0.66 14.41 ?  23  ILE   A CA   1 
ATOM   473  C CA   B ILE   A 1 23  ? 16.663 0.184   9.575   0.34 14.04 ?  23  ILE   A CA   1 
ATOM   474  C C    A ILE   A 1 23  ? 17.316 1.456   10.529  0.66 14.66 ?  23  ILE   A C    1 
ATOM   475  C C    B ILE   A 1 23  ? 17.412 1.157   10.474  0.34 14.54 ?  23  ILE   A C    1 
ATOM   476  O O    A ILE   A 1 23  ? 18.042 1.021   11.431  0.66 15.31 ?  23  ILE   A O    1 
ATOM   477  O O    B ILE   A 1 23  ? 18.112 0.740   11.405  0.34 13.91 ?  23  ILE   A O    1 
ATOM   478  C CB   A ILE   A 1 23  ? 17.309 -0.013  8.439   0.66 14.10 ?  23  ILE   A CB   1 
ATOM   479  C CB   B ILE   A 1 23  ? 17.534 -0.316  8.399   0.34 13.36 ?  23  ILE   A CB   1 
ATOM   480  C CG1  A ILE   A 1 23  ? 18.484 -0.886  8.885   0.66 13.92 ?  23  ILE   A CG1  1 
ATOM   481  C CG1  B ILE   A 1 23  ? 18.609 -1.283  8.907   0.34 13.46 ?  23  ILE   A CG1  1 
ATOM   482  C CG2  A ILE   A 1 23  ? 17.764 1.146   7.561   0.66 14.36 ?  23  ILE   A CG2  1 
ATOM   483  C CG2  B ILE   A 1 23  ? 18.181 0.846   7.656   0.34 12.77 ?  23  ILE   A CG2  1 
ATOM   484  C CD1  A ILE   A 1 23  ? 19.193 -1.579  7.734   0.66 14.11 ?  23  ILE   A CD1  1 
ATOM   485  C CD1  B ILE   A 1 23  ? 19.465 -1.896  7.807   0.34 13.37 ?  23  ILE   A CD1  1 
ATOM   486  H H    A ILE   A 1 23  ? 15.149 1.119   8.373   0.66 18.10 ?  23  ILE   A H    1 
ATOM   487  H H    B ILE   A 1 23  ? 15.336 0.788   8.251   0.34 16.85 ?  23  ILE   A H    1 
ATOM   488  H HA   A ILE   A 1 23  ? 16.303 -0.276  10.210  0.66 17.26 ?  23  ILE   A HA   1 
ATOM   489  H HA   B ILE   A 1 23  ? 16.440 -0.590  10.110  0.34 16.81 ?  23  ILE   A HA   1 
ATOM   490  H HB   A ILE   A 1 23  ? 16.716 -0.570  7.913   0.66 16.89 ?  23  ILE   A HB   1 
ATOM   491  H HB   B ILE   A 1 23  ? 16.967 -0.798  7.777   0.34 16.01 ?  23  ILE   A HB   1 
ATOM   492  H HG12 A ILE   A 1 23  ? 19.136 -0.333  9.342   0.66 16.68 ?  23  ILE   A HG12 1 
ATOM   493  H HG12 B ILE   A 1 23  ? 19.203 -0.807  9.509   0.34 16.13 ?  23  ILE   A HG12 1 
ATOM   494  H HG13 A ILE   A 1 23  ? 18.158 -1.575  9.487   0.66 16.68 ?  23  ILE   A HG13 1 
ATOM   495  H HG13 B ILE   A 1 23  ? 18.179 -2.012  9.382   0.34 16.13 ?  23  ILE   A HG13 1 
ATOM   496  H HG21 A ILE   A 1 23  ? 18.121 0.791   6.732   0.66 17.20 ?  23  ILE   A HG21 1 
ATOM   497  H HG21 B ILE   A 1 23  ? 18.518 0.527   6.802   0.34 15.30 ?  23  ILE   A HG21 1 
ATOM   498  H HG22 A ILE   A 1 23  ? 17.000 1.715   7.374   0.66 17.20 ?  23  ILE   A HG22 1 
ATOM   499  H HG22 B ILE   A 1 23  ? 17.517 1.535   7.512   0.34 15.30 ?  23  ILE   A HG22 1 
ATOM   500  H HG23 A ILE   A 1 23  ? 18.445 1.651   8.029   0.66 17.20 ?  23  ILE   A HG23 1 
ATOM   501  H HG23 B ILE   A 1 23  ? 18.914 1.195   8.188   0.34 15.30 ?  23  ILE   A HG23 1 
ATOM   502  H HD11 A ILE   A 1 23  ? 19.865 -2.180  8.092   0.66 16.90 ?  23  ILE   A HD11 1 
ATOM   503  H HD11 B ILE   A 1 23  ? 20.044 -2.572  8.195   0.34 16.02 ?  23  ILE   A HD11 1 
ATOM   504  H HD12 A ILE   A 1 23  ? 18.541 -2.080  7.219   0.66 16.90 ?  23  ILE   A HD12 1 
ATOM   505  H HD12 B ILE   A 1 23  ? 18.884 -2.299  7.144   0.34 16.02 ?  23  ILE   A HD12 1 
ATOM   506  H HD13 A ILE   A 1 23  ? 19.614 -0.909  7.173   0.66 16.90 ?  23  ILE   A HD13 1 
ATOM   507  H HD13 B ILE   A 1 23  ? 20.001 -1.198  7.397   0.34 16.02 ?  23  ILE   A HD13 1 
ATOM   508  N N    A VAL   A 1 24  ? 17.191 2.765   10.295  0.66 15.70 ?  24  VAL   A N    1 
ATOM   509  N N    B VAL   A 1 24  ? 17.266 2.460   10.228  0.34 16.15 ?  24  VAL   A N    1 
ATOM   510  C CA   A VAL   A 1 24  ? 17.874 3.740   11.143  0.66 16.58 ?  24  VAL   A CA   1 
ATOM   511  C CA   B VAL   A 1 24  ? 17.936 3.456   11.058  0.34 17.28 ?  24  VAL   A CA   1 
ATOM   512  C C    A VAL   A 1 24  ? 17.355 3.654   12.572  0.66 17.25 ?  24  VAL   A C    1 
ATOM   513  C C    B VAL   A 1 24  ? 17.377 3.431   12.474  0.34 18.10 ?  24  VAL   A C    1 
ATOM   514  O O    A VAL   A 1 24  ? 18.129 3.581   13.534  0.66 17.96 ?  24  VAL   A O    1 
ATOM   515  O O    B VAL   A 1 24  ? 18.128 3.450   13.457  0.34 18.56 ?  24  VAL   A O    1 
ATOM   516  C CB   A VAL   A 1 24  ? 17.709 5.157   10.567  0.66 17.76 ?  24  VAL   A CB   1 
ATOM   517  C CB   B VAL   A 1 24  ? 17.810 4.850   10.419  0.34 18.17 ?  24  VAL   A CB   1 
ATOM   518  C CG1  A VAL   A 1 24  ? 18.181 6.209   11.569  0.66 18.43 ?  24  VAL   A CG1  1 
ATOM   519  C CG1  B VAL   A 1 24  ? 18.493 5.895   11.283  0.34 19.13 ?  24  VAL   A CG1  1 
ATOM   520  C CG2  A VAL   A 1 24  ? 18.453 5.278   9.253   0.66 18.73 ?  24  VAL   A CG2  1 
ATOM   521  C CG2  B VAL   A 1 24  ? 18.387 4.837   9.013   0.34 18.12 ?  24  VAL   A CG2  1 
ATOM   522  H H    A VAL   A 1 24  ? 16.721 3.108   9.664   0.66 18.81 ?  24  VAL   A H    1 
ATOM   523  H H    B VAL   A 1 24  ? 16.785 2.789   9.599   0.34 19.35 ?  24  VAL   A H    1 
ATOM   524  H HA   A VAL   A 1 24  ? 18.820 3.536   11.161  0.66 19.87 ?  24  VAL   A HA   1 
ATOM   525  H HA   B VAL   A 1 24  ? 18.880 3.239   11.109  0.34 20.71 ?  24  VAL   A HA   1 
ATOM   526  H HB   A VAL   A 1 24  ? 16.769 5.318   10.388  0.66 21.28 ?  24  VAL   A HB   1 
ATOM   527  H HB   B VAL   A 1 24  ? 16.871 5.082   10.352  0.34 21.77 ?  24  VAL   A HB   1 
ATOM   528  H HG11 A VAL   A 1 24  ? 18.339 7.041   11.098  0.66 22.09 ?  24  VAL   A HG11 1 
ATOM   529  H HG11 B VAL   A 1 24  ? 18.574 6.716   10.776  0.34 22.92 ?  24  VAL   A HG11 1 
ATOM   530  H HG12 A VAL   A 1 24  ? 17.495 6.334   12.242  0.66 22.09 ?  24  VAL   A HG12 1 
ATOM   531  H HG12 B VAL   A 1 24  ? 17.955 6.048   12.076  0.34 22.92 ?  24  VAL   A HG12 1 
ATOM   532  H HG13 A VAL   A 1 24  ? 19.003 5.901   11.981  0.66 22.09 ?  24  VAL   A HG13 1 
ATOM   533  H HG13 B VAL   A 1 24  ? 19.371 5.570   11.533  0.34 22.92 ?  24  VAL   A HG13 1 
ATOM   534  H HG21 A VAL   A 1 24  ? 18.220 6.121   8.833   0.66 22.44 ?  24  VAL   A HG21 1 
ATOM   535  H HG21 B VAL   A 1 24  ? 18.434 5.747   8.684   0.34 21.71 ?  24  VAL   A HG21 1 
ATOM   536  H HG22 A VAL   A 1 24  ? 19.408 5.251   9.427   0.66 22.44 ?  24  VAL   A HG22 1 
ATOM   537  H HG22 B VAL   A 1 24  ? 19.276 4.449   9.042   0.34 21.71 ?  24  VAL   A HG22 1 
ATOM   538  H HG23 A VAL   A 1 24  ? 18.201 4.541   8.674   0.66 22.44 ?  24  VAL   A HG23 1 
ATOM   539  H HG23 B VAL   A 1 24  ? 17.813 4.304   8.440   0.34 21.71 ?  24  VAL   A HG23 1 
ATOM   540  N N    A GLU   A 1 25  ? 16.029 3.672   12.731  0.66 17.96 ?  25  GLU   A N    1 
ATOM   541  N N    B GLU   A 1 25  ? 16.049 3.386   12.601  0.34 18.76 ?  25  GLU   A N    1 
ATOM   542  C CA   A GLU   A 1 25  ? 15.444 3.604   14.065  0.66 19.31 ?  25  GLU   A CA   1 
ATOM   543  C CA   B GLU   A 1 25  ? 15.438 3.349   13.925  0.34 20.00 ?  25  GLU   A CA   1 
ATOM   544  C C    A GLU   A 1 25  ? 15.681 2.240   14.703  0.66 17.95 ?  25  GLU   A C    1 
ATOM   545  C C    B GLU   A 1 25  ? 15.658 2.000   14.597  0.34 19.06 ?  25  GLU   A C    1 
ATOM   546  O O    A GLU   A 1 25  ? 15.927 2.152   15.912  0.66 18.66 ?  25  GLU   A O    1 
ATOM   547  O O    B GLU   A 1 25  ? 15.842 1.931   15.818  0.34 19.79 ?  25  GLU   A O    1 
ATOM   548  C CB   A GLU   A 1 25  ? 13.955 3.952   14.007  0.66 22.02 ?  25  GLU   A CB   1 
ATOM   549  C CB   B GLU   A 1 25  ? 13.949 3.690   13.833  0.34 22.01 ?  25  GLU   A CB   1 
ATOM   550  C CG   A GLU   A 1 25  ? 13.686 5.400   13.609  0.66 25.87 ?  25  GLU   A CG   1 
ATOM   551  C CG   B GLU   A 1 25  ? 13.682 5.120   13.393  0.34 24.59 ?  25  GLU   A CG   1 
ATOM   552  C CD   A GLU   A 1 25  ? 14.447 6.402   14.466  0.66 29.26 ?  25  GLU   A CD   1 
ATOM   553  C CD   B GLU   A 1 25  ? 14.369 6.134   14.280  0.34 26.81 ?  25  GLU   A CD   1 
ATOM   554  O OE1  A GLU   A 1 25  ? 14.524 6.208   15.699  0.66 30.49 ?  25  GLU   A OE1  1 
ATOM   555  O OE1  B GLU   A 1 25  ? 14.484 5.876   15.498  0.34 27.88 ?  25  GLU   A OE1  1 
ATOM   556  O OE2  A GLU   A 1 25  ? 14.984 7.376   13.901  0.66 30.71 -1 25  GLU   A OE2  1 
ATOM   557  O OE2  B GLU   A 1 25  ? 14.805 7.180   13.759  0.34 27.50 -1 25  GLU   A OE2  1 
ATOM   558  H H    A GLU   A 1 25  ? 15.457 3.733   12.091  0.66 21.53 ?  25  GLU   A H    1 
ATOM   559  H H    B GLU   A 1 25  ? 15.492 3.381   11.945  0.34 22.48 ?  25  GLU   A H    1 
ATOM   560  H HA   A GLU   A 1 25  ? 15.878 4.259   14.630  0.66 23.15 ?  25  GLU   A HA   1 
ATOM   561  H HA   B GLU   A 1 25  ? 15.863 4.017   14.479  0.34 23.97 ?  25  GLU   A HA   1 
ATOM   562  H HB2  A GLU   A 1 25  ? 13.517 3.382   13.351  0.66 26.40 ?  25  GLU   A HB2  1 
ATOM   563  H HB2  B GLU   A 1 25  ? 13.527 3.102   13.189  0.34 26.39 ?  25  GLU   A HB2  1 
ATOM   564  H HB3  A GLU   A 1 25  ? 13.556 3.810   14.880  0.66 26.40 ?  25  GLU   A HB3  1 
ATOM   565  H HB3  B GLU   A 1 25  ? 13.545 3.570   14.707  0.34 26.39 ?  25  GLU   A HB3  1 
ATOM   566  H HG2  A GLU   A 1 25  ? 13.966 5.530   12.690  0.66 31.01 ?  25  GLU   A HG2  1 
ATOM   567  H HG2  B GLU   A 1 25  ? 14.008 5.241   12.488  0.34 29.48 ?  25  GLU   A HG2  1 
ATOM   568  H HG3  A GLU   A 1 25  ? 12.736 5.581   13.696  0.66 31.01 ?  25  GLU   A HG3  1 
ATOM   569  H HG3  B GLU   A 1 25  ? 12.730 5.294   13.432  0.34 29.48 ?  25  GLU   A HG3  1 
ATOM   570  N N    A GLU   A 1 26  ? 15.631 1.167   13.906  0.66 17.49 ?  26  GLU   A N    1 
ATOM   571  N N    B GLU   A 1 26  ? 15.649 0.915   13.819  0.34 18.13 ?  26  GLU   A N    1 
ATOM   572  C CA   A GLU   A 1 26  ? 15.950 -0.160  14.430  0.66 17.56 ?  26  GLU   A CA   1 
ATOM   573  C CA   B GLU   A 1 26  ? 15.992 -0.388  14.377  0.34 17.84 ?  26  GLU   A CA   1 
ATOM   574  C C    A GLU   A 1 26  ? 17.369 -0.195  14.982  0.66 16.69 ?  26  GLU   A C    1 
ATOM   575  C C    B GLU   A 1 26  ? 17.430 -0.421  14.870  0.34 17.07 ?  26  GLU   A C    1 
ATOM   576  O O    A GLU   A 1 26  ? 17.603 -0.663  16.104  0.66 17.03 ?  26  GLU   A O    1 
ATOM   577  O O    B GLU   A 1 26  ? 17.729 -1.091  15.865  0.34 17.16 ?  26  GLU   A O    1 
ATOM   578  C CB   A GLU   A 1 26  ? 15.796 -1.219  13.334  0.66 19.51 ?  26  GLU   A CB   1 
ATOM   579  C CB   B GLU   A 1 26  ? 15.768 -1.483  13.334  0.34 19.05 ?  26  GLU   A CB   1 
ATOM   580  C CG   A GLU   A 1 26  ? 14.420 -1.846  13.192  0.66 22.22 ?  26  GLU   A CG   1 
ATOM   581  C CG   B GLU   A 1 26  ? 14.310 -1.807  13.087  0.34 20.39 ?  26  GLU   A CG   1 
ATOM   582  C CD   A GLU   A 1 26  ? 13.995 -2.657  14.413  0.66 22.79 ?  26  GLU   A CD   1 
ATOM   583  C CD   B GLU   A 1 26  ? 13.614 -2.339  14.318  0.34 20.60 ?  26  GLU   A CD   1 
ATOM   584  O OE1  A GLU   A 1 26  ? 14.403 -3.833  14.580  0.66 22.71 ?  26  GLU   A OE1  1 
ATOM   585  O OE1  B GLU   A 1 26  ? 14.230 -3.134  15.058  0.34 20.70 ?  26  GLU   A OE1  1 
ATOM   586  O OE2  A GLU   A 1 26  ? 13.230 -2.104  15.215  0.66 23.69 -1 26  GLU   A OE2  1 
ATOM   587  O OE2  B GLU   A 1 26  ? 12.457 -1.939  14.551  0.34 20.64 -1 26  GLU   A OE2  1 
ATOM   588  H H    A GLU   A 1 26  ? 15.416 1.187   13.072  0.66 20.96 ?  26  GLU   A H    1 
ATOM   589  H H    B GLU   A 1 26  ? 15.440 0.907   12.986  0.34 21.73 ?  26  GLU   A H    1 
ATOM   590  H HA   A GLU   A 1 26  ? 15.337 -0.371  15.149  0.66 21.04 ?  26  GLU   A HA   1 
ATOM   591  H HA   B GLU   A 1 26  ? 15.417 -0.569  15.134  0.34 21.38 ?  26  GLU   A HA   1 
ATOM   592  H HB2  A GLU   A 1 26  ? 16.019 -0.808  12.483  0.66 23.39 ?  26  GLU   A HB2  1 
ATOM   593  H HB2  B GLU   A 1 26  ? 16.154 -1.193  12.490  0.34 22.83 ?  26  GLU   A HB2  1 
ATOM   594  H HB3  A GLU   A 1 26  ? 16.424 -1.933  13.520  0.66 23.39 ?  26  GLU   A HB3  1 
ATOM   595  H HB3  B GLU   A 1 26  ? 16.211 -2.293  13.632  0.34 22.83 ?  26  GLU   A HB3  1 
ATOM   596  H HG2  A GLU   A 1 26  ? 13.771 -1.135  13.053  0.66 26.64 ?  26  GLU   A HG2  1 
ATOM   597  H HG2  B GLU   A 1 26  ? 13.843 -1.000  12.831  0.34 24.44 ?  26  GLU   A HG2  1 
ATOM   598  H HG3  A GLU   A 1 26  ? 14.421 -2.442  12.428  0.66 26.64 ?  26  GLU   A HG3  1 
ATOM   599  H HG3  B GLU   A 1 26  ? 14.246 -2.472  12.386  0.34 24.44 ?  26  GLU   A HG3  1 
ATOM   600  N N    . ALA   A 1 27  ? 18.333 0.291   14.195  1.00 16.27 ?  27  ALA   A N    1 
ATOM   601  C CA   . ALA   A 1 27  ? 19.726 0.286   14.631  1.00 16.73 ?  27  ALA   A CA   1 
ATOM   602  C C    . ALA   A 1 27  ? 19.900 1.092   15.912  1.00 18.43 ?  27  ALA   A C    1 
ATOM   603  O O    . ALA   A 1 27  ? 20.577 0.647   16.845  1.00 18.60 ?  27  ALA   A O    1 
ATOM   604  C CB   . ALA   A 1 27  ? 20.638 0.812   13.518  1.00 15.94 ?  27  ALA   A CB   1 
ATOM   605  H H    A ALA   A 1 27  ? 18.205 0.631   13.412  0.66 19.50 ?  27  ALA   A H    1 
ATOM   606  H H    B ALA   A 1 27  ? 18.168 0.777   13.499  0.34 19.50 ?  27  ALA   A H    1 
ATOM   607  H HA   . ALA   A 1 27  ? 19.985 -0.624  14.817  1.00 20.04 ?  27  ALA   A HA   1 
ATOM   608  H HB1  . ALA   A 1 27  ? 21.559 0.798   13.831  1.00 19.10 ?  27  ALA   A HB1  1 
ATOM   609  H HB2  . ALA   A 1 27  ? 20.550 0.242   12.737  1.00 19.10 ?  27  ALA   A HB2  1 
ATOM   610  H HB3  . ALA   A 1 27  ? 20.383 1.721   13.294  1.00 19.10 ?  27  ALA   A HB3  1 
ATOM   611  N N    A LYS   A 1 28  ? 19.282 2.273   15.987  0.66 19.82 ?  28  LYS   A N    1 
ATOM   612  N N    B LYS   A 1 28  ? 19.282 2.274   15.984  0.34 20.71 ?  28  LYS   A N    1 
ATOM   613  C CA   A LYS   A 1 28  ? 19.427 3.095   17.184  0.66 22.81 ?  28  LYS   A CA   1 
ATOM   614  C CA   B LYS   A 1 28  ? 19.399 3.099   17.183  0.34 23.76 ?  28  LYS   A CA   1 
ATOM   615  C C    A LYS   A 1 28  ? 18.856 2.407   18.417  0.66 24.01 ?  28  LYS   A C    1 
ATOM   616  C C    B LYS   A 1 28  ? 18.809 2.405   18.403  0.34 25.24 ?  28  LYS   A C    1 
ATOM   617  O O    A LYS   A 1 28  ? 19.341 2.635   19.531  0.66 25.79 ?  28  LYS   A O    1 
ATOM   618  O O    B LYS   A 1 28  ? 19.320 2.570   19.517  0.34 25.99 ?  28  LYS   A O    1 
ATOM   619  C CB   A LYS   A 1 28  ? 18.791 4.470   16.971  0.66 25.55 ?  28  LYS   A CB   1 
ATOM   620  C CB   B LYS   A 1 28  ? 18.734 4.459   16.957  0.34 25.65 ?  28  LYS   A CB   1 
ATOM   621  C CG   A LYS   A 1 28  ? 19.626 5.370   16.077  0.66 27.85 ?  28  LYS   A CG   1 
ATOM   622  C CG   B LYS   A 1 28  ? 19.496 5.357   15.994  0.34 27.40 ?  28  LYS   A CG   1 
ATOM   623  C CD   A LYS   A 1 28  ? 19.185 6.820   16.134  0.66 30.52 ?  28  LYS   A CD   1 
ATOM   624  C CD   B LYS   A 1 28  ? 19.062 6.812   16.091  0.34 29.38 ?  28  LYS   A CD   1 
ATOM   625  C CE   A LYS   A 1 28  ? 17.883 7.028   15.397  0.66 32.27 ?  28  LYS   A CE   1 
ATOM   626  C CE   B LYS   A 1 28  ? 17.753 7.061   15.367  0.34 30.74 ?  28  LYS   A CE   1 
ATOM   627  N NZ   A LYS   A 1 28  ? 17.539 8.474   15.308  0.66 33.40 ?  28  LYS   A NZ   1 
ATOM   628  N NZ   B LYS   A 1 28  ? 17.451 8.518   15.270  0.34 31.58 ?  28  LYS   A NZ   1 
ATOM   629  H H    A LYS   A 1 28  ? 18.790 2.614   15.373  0.66 23.76 ?  28  LYS   A H    1 
ATOM   630  H H    B LYS   A 1 28  ? 18.796 2.613   15.364  0.34 24.82 ?  28  LYS   A H    1 
ATOM   631  H HA   A LYS   A 1 28  ? 20.370 3.237   17.351  0.66 27.34 ?  28  LYS   A HA   1 
ATOM   632  H HA   B LYS   A 1 28  ? 20.337 3.259   17.364  0.34 28.48 ?  28  LYS   A HA   1 
ATOM   633  H HB2  A LYS   A 1 28  ? 17.923 4.359   16.555  0.66 30.63 ?  28  LYS   A HB2  1 
ATOM   634  H HB2  B LYS   A 1 28  ? 17.847 4.320   16.591  0.34 30.76 ?  28  LYS   A HB2  1 
ATOM   635  H HB3  A LYS   A 1 28  ? 18.693 4.913   17.830  0.66 30.63 ?  28  LYS   A HB3  1 
ATOM   636  H HB3  B LYS   A 1 28  ? 18.671 4.924   17.806  0.34 30.76 ?  28  LYS   A HB3  1 
ATOM   637  H HG2  A LYS   A 1 28  ? 20.553 5.327   16.360  0.66 33.39 ?  28  LYS   A HG2  1 
ATOM   638  H HG2  B LYS   A 1 28  ? 20.442 5.312   16.199  0.34 32.86 ?  28  LYS   A HG2  1 
ATOM   639  H HG3  A LYS   A 1 28  ? 19.544 5.068   15.159  0.66 33.39 ?  28  LYS   A HG3  1 
ATOM   640  H HG3  B LYS   A 1 28  ? 19.336 5.056   15.086  0.34 32.86 ?  28  LYS   A HG3  1 
ATOM   641  H HD2  A LYS   A 1 28  ? 19.056 7.081   17.060  0.66 36.59 ?  28  LYS   A HD2  1 
ATOM   642  H HD2  B LYS   A 1 28  ? 18.942 7.050   17.024  0.34 35.23 ?  28  LYS   A HD2  1 
ATOM   643  H HD3  A LYS   A 1 28  ? 19.863 7.378   15.720  0.66 36.59 ?  28  LYS   A HD3  1 
ATOM   644  H HD3  B LYS   A 1 28  ? 19.742 7.375   15.688  0.34 35.23 ?  28  LYS   A HD3  1 
ATOM   645  H HE2  A LYS   A 1 28  ? 17.966 6.677   14.496  0.66 38.69 ?  28  LYS   A HE2  1 
ATOM   646  H HE2  B LYS   A 1 28  ? 17.811 6.702   14.468  0.34 36.86 ?  28  LYS   A HE2  1 
ATOM   647  H HE3  A LYS   A 1 28  ? 17.170 6.572   15.871  0.66 38.69 ?  28  LYS   A HE3  1 
ATOM   648  H HE3  B LYS   A 1 28  ? 17.031 6.633   15.854  0.34 36.86 ?  28  LYS   A HE3  1 
ATOM   649  H HZ1  A LYS   A 1 28  ? 16.772 8.577   14.871  0.66 40.05 ?  28  LYS   A HZ1  1 
ATOM   650  H HZ1  B LYS   A 1 28  ? 16.681 8.642   14.842  0.34 37.87 ?  28  LYS   A HZ1  1 
ATOM   651  H HZ2  A LYS   A 1 28  ? 17.457 8.817   16.125  0.66 40.05 ?  28  LYS   A HZ2  1 
ATOM   652  H HZ2  B LYS   A 1 28  ? 17.391 8.872   16.084  0.34 37.87 ?  28  LYS   A HZ2  1 
ATOM   653  H HZ3  A LYS   A 1 28  ? 18.181 8.913   14.874  0.66 40.05 ?  28  LYS   A HZ3  1 
ATOM   654  H HZ3  B LYS   A 1 28  ? 18.100 8.934   14.822  0.34 37.87 ?  28  LYS   A HZ3  1 
ATOM   655  N N    A LYS   A 1 29  ? 17.847 1.554   18.242  0.66 24.58 ?  29  LYS   A N    1 
ATOM   656  N N    B LYS   A 1 29  ? 17.748 1.620   18.217  0.34 26.37 ?  29  LYS   A N    1 
ATOM   657  C CA   A LYS   A 1 29  ? 17.252 0.853   19.376  0.66 26.55 ?  29  LYS   A CA   1 
ATOM   658  C CA   B LYS   A 1 29  ? 17.117 0.936   19.341  0.34 27.74 ?  29  LYS   A CA   1 
ATOM   659  C C    A LYS   A 1 29  ? 18.074 -0.370  19.767  0.66 26.08 ?  29  LYS   A C    1 
ATOM   660  C C    B LYS   A 1 29  ? 17.894 -0.307  19.753  0.34 26.74 ?  29  LYS   A C    1 
ATOM   661  O O    A LYS   A 1 29  ? 18.404 -0.558  20.944  0.66 27.52 ?  29  LYS   A O    1 
ATOM   662  O O    B LYS   A 1 29  ? 18.072 -0.561  20.950  0.34 26.90 ?  29  LYS   A O    1 
ATOM   663  C CB   A LYS   A 1 29  ? 15.822 0.431   19.032  0.66 29.54 ?  29  LYS   A CB   1 
ATOM   664  C CB   B LYS   A 1 29  ? 15.688 0.539   18.973  0.34 30.17 ?  29  LYS   A CB   1 
ATOM   665  C CG   A LYS   A 1 29  ? 15.092 -0.288  20.160  0.66 32.82 ?  29  LYS   A CG   1 
ATOM   666  C CG   B LYS   A 1 29  ? 14.909 -0.118  20.103  0.34 32.55 ?  29  LYS   A CG   1 
ATOM   667  C CD   A LYS   A 1 29  ? 14.769 0.665   21.299  0.66 35.89 ?  29  LYS   A CD   1 
ATOM   668  C CD   B LYS   A 1 29  ? 14.645 0.860   21.236  0.34 34.67 ?  29  LYS   A CD   1 
ATOM   669  C CE   A LYS   A 1 29  ? 13.891 0.003   22.350  0.66 37.85 ?  29  LYS   A CE   1 
ATOM   670  C CE   B LYS   A 1 29  ? 13.810 0.223   22.332  0.34 36.08 ?  29  LYS   A CE   1 
ATOM   671  N NZ   A LYS   A 1 29  ? 13.469 0.967   23.404  0.66 38.93 ?  29  LYS   A NZ   1 
ATOM   672  N NZ   B LYS   A 1 29  ? 13.503 1.192   23.418  0.34 36.86 ?  29  LYS   A NZ   1 
ATOM   673  H H    A LYS   A 1 29  ? 17.491 1.365   17.483  0.66 29.47 ?  29  LYS   A H    1 
ATOM   674  H H    B LYS   A 1 29  ? 17.377 1.472   17.457  0.34 31.62 ?  29  LYS   A H    1 
ATOM   675  H HA   A LYS   A 1 29  ? 17.216 1.449   20.139  0.66 31.83 ?  29  LYS   A HA   1 
ATOM   676  H HA   B LYS   A 1 29  ? 17.084 1.537   20.102  0.34 33.26 ?  29  LYS   A HA   1 
ATOM   677  H HB2  A LYS   A 1 29  ? 15.309 1.224   18.812  0.66 35.42 ?  29  LYS   A HB2  1 
ATOM   678  H HB2  B LYS   A 1 29  ? 15.205 1.333   18.706  0.34 36.17 ?  29  LYS   A HB2  1 
ATOM   679  H HB3  A LYS   A 1 29  ? 15.847 -0.166  18.270  0.66 35.42 ?  29  LYS   A HB3  1 
ATOM   680  H HB3  B LYS   A 1 29  ? 15.722 -0.091  18.235  0.34 36.17 ?  29  LYS   A HB3  1 
ATOM   681  H HG2  A LYS   A 1 29  ? 14.259 -0.648  19.820  0.66 39.36 ?  29  LYS   A HG2  1 
ATOM   682  H HG2  B LYS   A 1 29  ? 14.055 -0.426  19.764  0.34 39.03 ?  29  LYS   A HG2  1 
ATOM   683  H HG3  A LYS   A 1 29  ? 15.647 -1.005  20.509  0.66 39.36 ?  29  LYS   A HG3  1 
ATOM   684  H HG3  B LYS   A 1 29  ? 15.415 -0.867  20.459  0.34 39.03 ?  29  LYS   A HG3  1 
ATOM   685  H HD2  A LYS   A 1 29  ? 15.593 0.948   21.725  0.66 43.04 ?  29  LYS   A HD2  1 
ATOM   686  H HD2  B LYS   A 1 29  ? 15.489 1.140   21.623  0.34 41.57 ?  29  LYS   A HD2  1 
ATOM   687  H HD3  A LYS   A 1 29  ? 14.293 1.434   20.945  0.66 43.04 ?  29  LYS   A HD3  1 
ATOM   688  H HD3  B LYS   A 1 29  ? 14.162 1.627   20.890  0.34 41.57 ?  29  LYS   A HD3  1 
ATOM   689  H HE2  A LYS   A 1 29  ? 13.094 -0.350  21.925  0.66 45.39 ?  29  LYS   A HE2  1 
ATOM   690  H HE2  B LYS   A 1 29  ? 12.972 -0.089  21.956  0.34 43.27 ?  29  LYS   A HE2  1 
ATOM   691  H HE3  A LYS   A 1 29  ? 14.388 -0.714  22.776  0.66 45.39 ?  29  LYS   A HE3  1 
ATOM   692  H HE3  B LYS   A 1 29  ? 14.301 -0.521  22.717  0.34 43.27 ?  29  LYS   A HE3  1 
ATOM   693  H HZ1  A LYS   A 1 29  ? 12.958 0.556   24.006  0.66 46.69 ?  29  LYS   A HZ1  1 
ATOM   694  H HZ1  B LYS   A 1 29  ? 13.013 0.798   24.048  0.34 44.21 ?  29  LYS   A HZ1  1 
ATOM   695  H HZ2  A LYS   A 1 29  ? 14.185 1.302   23.813  0.66 46.69 ?  29  LYS   A HZ2  1 
ATOM   696  H HZ2  B LYS   A 1 29  ? 14.259 1.489   23.782  0.34 44.21 ?  29  LYS   A HZ2  1 
ATOM   697  H HZ3  A LYS   A 1 29  ? 13.006 1.633   23.038  0.66 46.69 ?  29  LYS   A HZ3  1 
ATOM   698  H HZ3  B LYS   A 1 29  ? 13.049 1.883   23.089  0.34 44.21 ?  29  LYS   A HZ3  1 
ATOM   699  N N    A VAL   A 1 30  ? 18.391 -1.224  18.794  0.66 23.96 ?  30  VAL   A N    1 
ATOM   700  N N    B VAL   A 1 30  ? 18.344 -1.098  18.784  0.34 25.61 ?  30  VAL   A N    1 
ATOM   701  C CA   A VAL   A 1 30  ? 19.053 -2.489  19.093  0.66 23.09 ?  30  VAL   A CA   1 
ATOM   702  C CA   B VAL   A 1 30  ? 18.976 -2.373  19.096  0.34 24.82 ?  30  VAL   A CA   1 
ATOM   703  C C    A VAL   A 1 30  ? 20.550 -2.306  19.314  0.66 21.24 ?  30  VAL   A C    1 
ATOM   704  C C    B VAL   A 1 30  ? 20.479 -2.232  19.310  0.34 23.93 ?  30  VAL   A C    1 
ATOM   705  O O    A VAL   A 1 30  ? 21.152 -3.028  20.115  0.66 22.04 ?  30  VAL   A O    1 
ATOM   706  O O    B VAL   A 1 30  ? 21.056 -2.952  20.131  0.34 24.06 ?  30  VAL   A O    1 
ATOM   707  C CB   A VAL   A 1 30  ? 18.772 -3.497  17.965  0.66 24.24 ?  30  VAL   A CB   1 
ATOM   708  C CB   B VAL   A 1 30  ? 18.671 -3.390  17.983  0.34 25.09 ?  30  VAL   A CB   1 
ATOM   709  C CG1  A VAL   A 1 30  ? 19.582 -4.772  18.166  0.66 24.87 ?  30  VAL   A CG1  1 
ATOM   710  C CG1  B VAL   A 1 30  ? 19.429 -4.686  18.222  0.34 25.33 ?  30  VAL   A CG1  1 
ATOM   711  C CG2  A VAL   A 1 30  ? 17.285 -3.810  17.890  0.66 24.95 ?  30  VAL   A CG2  1 
ATOM   712  C CG2  B VAL   A 1 30  ? 17.175 -3.644  17.899  0.34 25.42 ?  30  VAL   A CG2  1 
ATOM   713  H H    A VAL   A 1 30  ? 18.217 -1.104  17.962  0.66 28.72 ?  30  VAL   A H    1 
ATOM   714  H H    B VAL   A 1 30  ? 18.295 -0.922  17.940  0.34 30.71 ?  30  VAL   A H    1 
ATOM   715  H HA   A VAL   A 1 30  ? 18.673 -2.854  19.907  0.66 27.68 ?  30  VAL   A HA   1 
ATOM   716  H HA   B VAL   A 1 30  ? 18.583 -2.714  19.917  0.34 29.75 ?  30  VAL   A HA   1 
ATOM   717  H HB   A VAL   A 1 30  ? 19.042 -3.107  17.119  0.66 29.05 ?  30  VAL   A HB   1 
ATOM   718  H HB   B VAL   A 1 30  ? 18.966 -3.029  17.132  0.34 30.08 ?  30  VAL   A HB   1 
ATOM   719  H HG11 A VAL   A 1 30  ? 19.216 -5.468  17.595  0.66 29.82 ?  30  VAL   A HG11 1 
ATOM   720  H HG11 B VAL   A 1 30  ? 19.037 -5.384  17.674  0.34 30.37 ?  30  VAL   A HG11 1 
ATOM   721  H HG12 A VAL   A 1 30  ? 20.507 -4.606  17.928  0.66 29.82 ?  30  VAL   A HG12 1 
ATOM   722  H HG12 B VAL   A 1 30  ? 20.360 -4.561  17.979  0.34 30.37 ?  30  VAL   A HG12 1 
ATOM   723  H HG13 A VAL   A 1 30  ? 19.518 -5.043  19.095  0.66 29.82 ?  30  VAL   A HG13 1 
ATOM   724  H HG13 B VAL   A 1 30  ? 19.358 -4.923  19.158  0.34 30.37 ?  30  VAL   A HG13 1 
ATOM   725  H HG21 A VAL   A 1 30  ? 17.138 -4.473  17.197  0.66 29.91 ?  30  VAL   A HG21 1 
ATOM   726  H HG21 B VAL   A 1 30  ? 17.006 -4.317  17.222  0.34 30.47 ?  30  VAL   A HG21 1 
ATOM   727  H HG22 A VAL   A 1 30  ? 16.994 -4.156  18.748  0.66 29.91 ?  30  VAL   A HG22 1 
ATOM   728  H HG22 B VAL   A 1 30  ? 16.860 -3.955  18.762  0.34 30.47 ?  30  VAL   A HG22 1 
ATOM   729  H HG23 A VAL   A 1 30  ? 16.804 -2.996  17.679  0.66 29.91 ?  30  VAL   A HG23 1 
ATOM   730  H HG23 B VAL   A 1 30  ? 16.730 -2.816  17.662  0.34 30.47 ?  30  VAL   A HG23 1 
ATOM   731  N N    A LYS   A 1 31  ? 21.170 -1.353  18.625  0.66 19.89 ?  31  LYS   A N    1 
ATOM   732  N N    B LYS   A 1 31  ? 21.120 -1.316  18.595  0.34 23.28 ?  31  LYS   A N    1 
ATOM   733  C CA   A LYS   A 1 31  ? 22.622 -1.227  18.575  0.66 20.56 ?  31  LYS   A CA   1 
ATOM   734  C CA   B LYS   A 1 31  ? 22.573 -1.217  18.543  0.34 23.27 ?  31  LYS   A CA   1 
ATOM   735  C C    A LYS   A 1 31  ? 23.252 -2.581  18.238  0.66 18.27 ?  31  LYS   A C    1 
ATOM   736  C C    B LYS   A 1 31  ? 23.197 -2.586  18.253  0.34 20.43 ?  31  LYS   A C    1 
ATOM   737  O O    A LYS   A 1 31  ? 24.047 -3.115  19.019  0.66 19.46 ?  31  LYS   A O    1 
ATOM   738  O O    B LYS   A 1 31  ? 23.934 -3.129  19.080  0.34 21.19 ?  31  LYS   A O    1 
ATOM   739  C CB   A LYS   A 1 31  ? 23.194 -0.670  19.871  0.66 25.16 ?  31  LYS   A CB   1 
ATOM   740  C CB   B LYS   A 1 31  ? 23.152 -0.606  19.811  0.34 26.60 ?  31  LYS   A CB   1 
ATOM   741  C CG   A LYS   A 1 31  ? 22.516 0.593   20.367  0.66 30.35 ?  31  LYS   A CG   1 
ATOM   742  C CG   B LYS   A 1 31  ? 22.444 0.655   20.274  0.34 29.98 ?  31  LYS   A CG   1 
ATOM   743  C CD   A LYS   A 1 31  ? 23.532 1.668   20.725  0.66 34.48 ?  31  LYS   A CD   1 
ATOM   744  C CD   B LYS   A 1 31  ? 23.434 1.708   20.741  0.34 32.74 ?  31  LYS   A CD   1 
ATOM   745  C CE   A LYS   A 1 31  ? 22.925 2.719   21.641  0.66 37.11 ?  31  LYS   A CE   1 
ATOM   746  C CE   B LYS   A 1 31  ? 22.774 2.741   21.638  0.34 34.61 ?  31  LYS   A CE   1 
ATOM   747  N NZ   A LYS   A 1 31  ? 21.680 3.310   21.079  0.66 38.30 ?  31  LYS   A NZ   1 
ATOM   748  N NZ   B LYS   A 1 31  ? 21.523 3.294   21.050  0.34 35.64 ?  31  LYS   A NZ   1 
ATOM   749  H H    A LYS   A 1 31  ? 20.758 -0.752  18.168  0.66 23.84 ?  31  LYS   A H    1 
ATOM   750  H H    B LYS   A 1 31  ? 20.717 -0.728  18.116  0.34 27.91 ?  31  LYS   A H    1 
ATOM   751  H HA   A LYS   A 1 31  ? 22.848 -0.606  17.867  0.66 24.65 ?  31  LYS   A HA   1 
ATOM   752  H HA   B LYS   A 1 31  ? 22.800 -0.632  17.815  0.34 27.89 ?  31  LYS   A HA   1 
ATOM   753  H HB2  A LYS   A 1 31  ? 23.108 -1.345  20.558  0.66 30.16 ?  31  LYS   A HB2  1 
ATOM   754  H HB2  B LYS   A 1 31  ? 23.070 -1.254  20.514  0.34 31.89 ?  31  LYS   A HB2  1 
ATOM   755  H HB3  A LYS   A 1 31  ? 24.133 -0.465  19.729  0.66 30.16 ?  31  LYS   A HB3  1 
ATOM   756  H HB3  B LYS   A 1 31  ? 24.089 -0.392  19.660  0.34 31.89 ?  31  LYS   A HB3  1 
ATOM   757  H HG2  A LYS   A 1 31  ? 21.937 0.942   19.672  0.66 36.39 ?  31  LYS   A HG2  1 
ATOM   758  H HG2  B LYS   A 1 31  ? 21.930 1.023   19.539  0.34 35.95 ?  31  LYS   A HG2  1 
ATOM   759  H HG3  A LYS   A 1 31  ? 22.000 0.387   21.163  0.66 36.39 ?  31  LYS   A HG3  1 
ATOM   760  H HG3  B LYS   A 1 31  ? 21.858 0.436   21.017  0.34 35.95 ?  31  LYS   A HG3  1 
ATOM   761  H HD2  A LYS   A 1 31  ? 24.283 1.261   21.186  0.66 41.35 ?  31  LYS   A HD2  1 
ATOM   762  H HD2  B LYS   A 1 31  ? 24.143 1.280   21.244  0.34 39.26 ?  31  LYS   A HD2  1 
ATOM   763  H HD3  A LYS   A 1 31  ? 23.834 2.107   19.914  0.66 41.35 ?  31  LYS   A HD3  1 
ATOM   764  H HD3  B LYS   A 1 31  ? 23.799 2.166   19.968  0.34 39.26 ?  31  LYS   A HD3  1 
ATOM   765  H HE2  A LYS   A 1 31  ? 22.708 2.309   22.493  0.66 44.50 ?  31  LYS   A HE2  1 
ATOM   766  H HE2  B LYS   A 1 31  ? 22.555 2.327   22.486  0.34 41.51 ?  31  LYS   A HE2  1 
ATOM   767  H HE3  A LYS   A 1 31  ? 23.567 3.435   21.770  0.66 44.50 ?  31  LYS   A HE3  1 
ATOM   768  H HE3  B LYS   A 1 31  ? 23.390 3.477   21.778  0.34 41.51 ?  31  LYS   A HE3  1 
ATOM   769  H HZ1  A LYS   A 1 31  ? 21.370 3.942   21.624  0.66 45.93 ?  31  LYS   A HZ1  1 
ATOM   770  H HZ1  B LYS   A 1 31  ? 21.193 3.929   21.579  0.34 42.74 ?  31  LYS   A HZ1  1 
ATOM   771  H HZ2  A LYS   A 1 31  ? 21.846 3.671   20.283  0.66 45.93 ?  31  LYS   A HZ2  1 
ATOM   772  H HZ2  B LYS   A 1 31  ? 21.693 3.644   20.250  0.34 42.74 ?  31  LYS   A HZ2  1 
ATOM   773  H HZ3  A LYS   A 1 31  ? 21.058 2.679   20.986  0.66 45.93 ?  31  LYS   A HZ3  1 
ATOM   774  H HZ3  B LYS   A 1 31  ? 20.917 2.648   20.961  0.34 42.74 ?  31  LYS   A HZ3  1 
ATOM   775  N N    . PRO   A 1 32  ? 22.919 -3.156  17.085  1.00 17.57 ?  32  PRO   A N    1 
ATOM   776  C CA   . PRO   A 1 32  ? 23.408 -4.497  16.768  1.00 17.82 ?  32  PRO   A CA   1 
ATOM   777  C C    . PRO   A 1 32  ? 24.909 -4.505  16.550  1.00 17.55 ?  32  PRO   A C    1 
ATOM   778  O O    . PRO   A 1 32  ? 25.545 -3.470  16.340  1.00 17.66 ?  32  PRO   A O    1 
ATOM   779  C CB   . PRO   A 1 32  ? 22.683 -4.819  15.458  1.00 17.95 ?  32  PRO   A CB   1 
ATOM   780  C CG   . PRO   A 1 32  ? 22.516 -3.479  14.812  1.00 17.05 ?  32  PRO   A CG   1 
ATOM   781  C CD   . PRO   A 1 32  ? 22.192 -2.559  15.954  1.00 16.62 ?  32  PRO   A CD   1 
ATOM   782  H HA   . PRO   A 1 32  ? 23.156 -5.133  17.456  1.00 21.35 ?  32  PRO   A HA   1 
ATOM   783  H HB2  . PRO   A 1 32  ? 23.231 -5.408  14.911  1.00 21.51 ?  32  PRO   A HB2  1 
ATOM   784  H HB3  . PRO   A 1 32  ? 21.821 -5.228  15.644  1.00 21.51 ?  32  PRO   A HB3  1 
ATOM   785  H HG2  . PRO   A 1 32  ? 23.344 -3.226  14.376  1.00 20.44 ?  32  PRO   A HG2  1 
ATOM   786  H HG3  . PRO   A 1 32  ? 21.787 -3.519  14.170  1.00 20.44 ?  32  PRO   A HG3  1 
ATOM   787  H HD2  . PRO   A 1 32  ? 22.522 -1.669  15.756  1.00 19.92 ?  32  PRO   A HD2  1 
ATOM   788  H HD3  . PRO   A 1 32  ? 21.238 -2.560  16.117  1.00 19.92 ?  32  PRO   A HD3  1 
ATOM   789  N N    . THR   A 1 33  ? 25.471 -5.712  16.572  1.00 17.67 ?  33  THR   A N    1 
ATOM   790  C CA   . THR   A 1 33  ? 26.884 -5.863  16.253  1.00 17.89 ?  33  THR   A CA   1 
ATOM   791  C C    . THR   A 1 33  ? 27.179 -5.402  14.831  1.00 16.22 ?  33  THR   A C    1 
ATOM   792  O O    . THR   A 1 33  ? 28.208 -4.760  14.581  1.00 16.38 ?  33  THR   A O    1 
ATOM   793  C CB   . THR   A 1 33  ? 27.313 -7.317  16.450  1.00 19.54 ?  33  THR   A CB   1 
ATOM   794  O OG1  . THR   A 1 33  ? 27.023 -7.726  17.790  1.00 21.60 ?  33  THR   A OG1  1 
ATOM   795  C CG2  . THR   A 1 33  ? 28.801 -7.467  16.194  1.00 20.40 ?  33  THR   A CG2  1 
ATOM   796  H H    . THR   A 1 33  ? 25.060 -6.448  16.759  1.00 21.17 ?  33  THR   A H    1 
ATOM   797  H HA   . THR   A 1 33  ? 27.402 -5.315  16.861  1.00 21.44 ?  33  THR   A HA   1 
ATOM   798  H HB   . THR   A 1 33  ? 26.832 -7.887  15.825  1.00 23.42 ?  33  THR   A HB   1 
ATOM   799  H HG1  . THR   A 1 33  ? 27.451 -7.245  18.336  1.00 25.89 ?  33  THR   A HG1  1 
ATOM   800  H HG21 . THR   A 1 33  ? 29.100 -8.341  16.486  1.00 24.46 ?  33  THR   A HG21 1 
ATOM   801  H HG22 . THR   A 1 33  ? 28.990 -7.371  15.247  1.00 24.46 ?  33  THR   A HG22 1 
ATOM   802  H HG23 . THR   A 1 33  ? 29.290 -6.787  16.683  1.00 24.46 ?  33  THR   A HG23 1 
ATOM   803  N N    . VAL   A 1 34  ? 26.291 -5.720  13.886  1.00 14.58 ?  34  VAL   A N    1 
ATOM   804  C CA   . VAL   A 1 34  ? 26.483 -5.394  12.475  1.00 13.24 ?  34  VAL   A CA   1 
ATOM   805  C C    . VAL   A 1 34  ? 25.182 -4.848  11.908  1.00 12.87 ?  34  VAL   A C    1 
ATOM   806  O O    . VAL   A 1 34  ? 24.148 -5.524  11.960  1.00 13.65 ?  34  VAL   A O    1 
ATOM   807  C CB   . VAL   A 1 34  ? 26.930 -6.612  11.642  1.00 13.96 ?  34  VAL   A CB   1 
ATOM   808  C CG1  . VAL   A 1 34  ? 27.079 -6.225  10.184  1.00 14.27 ?  34  VAL   A CG1  1 
ATOM   809  C CG2  . VAL   A 1 34  ? 28.225 -7.220  12.194  1.00 15.35 ?  34  VAL   A CG2  1 
ATOM   810  H H    . VAL   A 1 34  ? 25.550 -6.134  14.046  1.00 17.47 ?  34  VAL   A H    1 
ATOM   811  H HA   . VAL   A 1 34  ? 27.156 -4.704  12.395  1.00 15.86 ?  34  VAL   A HA   1 
ATOM   812  H HB   . VAL   A 1 34  ? 26.239 -7.292  11.702  1.00 16.72 ?  34  VAL   A HB   1 
ATOM   813  H HG11 . VAL   A 1 34  ? 27.592 -6.911  9.730   1.00 17.09 ?  34  VAL   A HG11 1 
ATOM   814  H HG12 . VAL   A 1 34  ? 26.201 -6.148  9.781   1.00 17.09 ?  34  VAL   A HG12 1 
ATOM   815  H HG13 . VAL   A 1 34  ? 27.546 -5.375  10.129  1.00 17.09 ?  34  VAL   A HG13 1 
ATOM   816  H HG21 . VAL   A 1 34  ? 28.484 -7.965  11.631  1.00 18.40 ?  34  VAL   A HG21 1 
ATOM   817  H HG22 . VAL   A 1 34  ? 28.918 -6.542  12.189  1.00 18.40 ?  34  VAL   A HG22 1 
ATOM   818  H HG23 . VAL   A 1 34  ? 28.070 -7.529  13.102  1.00 18.40 ?  34  VAL   A HG23 1 
ATOM   819  N N    . VAL   A 1 35  ? 25.233 -3.638  11.356  1.00 11.92 ?  35  VAL   A N    1 
ATOM   820  C CA   . VAL   A 1 35  ? 24.197 -3.133  10.463  1.00 11.27 ?  35  VAL   A CA   1 
ATOM   821  C C    . VAL   A 1 35  ? 24.750 -3.136  9.045   1.00 10.45 ?  35  VAL   A C    1 
ATOM   822  O O    . VAL   A 1 35  ? 25.894 -2.723  8.817   1.00 12.03 ?  35  VAL   A O    1 
ATOM   823  C CB   . VAL   A 1 35  ? 23.675 -1.736  10.868  1.00 12.77 ?  35  VAL   A CB   1 
ATOM   824  C CG1  . VAL   A 1 35  ? 24.757 -0.652  10.734  1.00 12.86 ?  35  VAL   A CG1  1 
ATOM   825  C CG2  . VAL   A 1 35  ? 22.437 -1.368  10.047  1.00 13.60 ?  35  VAL   A CG2  1 
ATOM   826  H H    . VAL   A 1 35  ? 25.869 -3.076  11.481  1.00 14.27 ?  35  VAL   A H    1 
ATOM   827  H HA   . VAL   A 1 35  ? 23.437 -3.743  10.486  1.00 13.49 ?  35  VAL   A HA   1 
ATOM   828  H HB   . VAL   A 1 35  ? 23.401 -1.767  11.794  1.00 15.29 ?  35  VAL   A HB   1 
ATOM   829  H HG11 . VAL   A 1 35  ? 24.418 0.179   11.101  1.00 15.41 ?  35  VAL   A HG11 1 
ATOM   830  H HG12 . VAL   A 1 35  ? 25.544 -0.935  11.225  1.00 15.41 ?  35  VAL   A HG12 1 
ATOM   831  H HG13 . VAL   A 1 35  ? 24.977 -0.533  9.796   1.00 15.41 ?  35  VAL   A HG13 1 
ATOM   832  H HG21 . VAL   A 1 35  ? 22.098 -0.516  10.357  1.00 16.29 ?  35  VAL   A HG21 1 
ATOM   833  H HG22 . VAL   A 1 35  ? 22.687 -1.305  9.110   1.00 16.29 ?  35  VAL   A HG22 1 
ATOM   834  H HG23 . VAL   A 1 35  ? 21.766 -2.057  10.164  1.00 16.29 ?  35  VAL   A HG23 1 
ATOM   835  N N    . VAL   A 1 36  ? 23.944 -3.606  8.093   1.00 9.83  ?  36  VAL   A N    1 
ATOM   836  C CA   . VAL   A 1 36  ? 24.319 -3.624  6.687   1.00 10.11 ?  36  VAL   A CA   1 
ATOM   837  C C    . VAL   A 1 36  ? 23.863 -2.331  6.028   1.00 10.82 ?  36  VAL   A C    1 
ATOM   838  O O    . VAL   A 1 36  ? 22.701 -1.924  6.168   1.00 11.22 ?  36  VAL   A O    1 
ATOM   839  C CB   . VAL   A 1 36  ? 23.715 -4.843  5.970   1.00 10.28 ?  36  VAL   A CB   1 
ATOM   840  C CG1  . VAL   A 1 36  ? 23.979 -4.780  4.482   1.00 11.15 ?  36  VAL   A CG1  1 
ATOM   841  C CG2  . VAL   A 1 36  ? 24.267 -6.141  6.553   1.00 11.57 ?  36  VAL   A CG2  1 
ATOM   842  H H    . VAL   A 1 36  ? 23.148 -3.922  8.237   1.00 11.76 ?  36  VAL   A H    1 
ATOM   843  H HA   . VAL   A 1 36  ? 25.287 -3.685  6.613   1.00 12.10 ?  36  VAL   A HA   1 
ATOM   844  H HB   . VAL   A 1 36  ? 22.752 -4.840  6.100   1.00 12.30 ?  36  VAL   A HB   1 
ATOM   845  H HG11 . VAL   A 1 36  ? 23.818 -5.657  4.099   1.00 13.36 ?  36  VAL   A HG11 1 
ATOM   846  H HG12 . VAL   A 1 36  ? 23.380 -4.132  4.079   1.00 13.36 ?  36  VAL   A HG12 1 
ATOM   847  H HG13 . VAL   A 1 36  ? 24.900 -4.521  4.339   1.00 13.36 ?  36  VAL   A HG13 1 
ATOM   848  H HG21 . VAL   A 1 36  ? 23.872 -6.896  6.082   1.00 13.86 ?  36  VAL   A HG21 1 
ATOM   849  H HG22 . VAL   A 1 36  ? 25.230 -6.154  6.443   1.00 13.86 ?  36  VAL   A HG22 1 
ATOM   850  H HG23 . VAL   A 1 36  ? 24.040 -6.190  7.495   1.00 13.86 ?  36  VAL   A HG23 1 
ATOM   851  N N    . ASN   A 1 37  ? 24.774 -1.700  5.287   1.00 9.96  ?  37  ASN   A N    1 
ATOM   852  C CA   . ASN   A 1 37  ? 24.442 -0.584  4.415   1.00 9.82  ?  37  ASN   A CA   1 
ATOM   853  C C    . ASN   A 1 37  ? 24.308 -1.060  2.976   1.00 9.64  ?  37  ASN   A C    1 
ATOM   854  O O    . ASN   A 1 37  ? 25.101 -1.889  2.501   1.00 10.42 ?  37  ASN   A O    1 
ATOM   855  C CB   . ASN   A 1 37  ? 25.525 0.495   4.488   1.00 10.23 ?  37  ASN   A CB   1 
ATOM   856  C CG   . ASN   A 1 37  ? 25.197 1.689   3.640   1.00 10.56 ?  37  ASN   A CG   1 
ATOM   857  O OD1  . ASN   A 1 37  ? 24.024 2.022   3.457   1.00 11.25 ?  37  ASN   A OD1  1 
ATOM   858  N ND2  . ASN   A 1 37  ? 26.226 2.360   3.129   1.00 10.68 ?  37  ASN   A ND2  1 
ATOM   859  H H    . ASN   A 1 37  ? 25.612 -1.906  5.275   1.00 11.92 ?  37  ASN   A H    1 
ATOM   860  H HA   . ASN   A 1 37  ? 23.604 -0.186  4.697   1.00 11.76 ?  37  ASN   A HA   1 
ATOM   861  H HB2  . ASN   A 1 37  ? 25.622 0.795   5.407   1.00 12.24 ?  37  ASN   A HB2  1 
ATOM   862  H HB3  . ASN   A 1 37  ? 26.370 0.122   4.175   1.00 12.24 ?  37  ASN   A HB3  1 
ATOM   863  H HD21 . ASN   A 1 37  ? 26.084 3.052   2.635   1.00 12.79 ?  37  ASN   A HD21 1 
ATOM   864  H HD22 . ASN   A 1 37  ? 27.027 2.106   3.279   1.00 12.79 ?  37  ASN   A HD22 1 
ATOM   865  N N    A ALA   A 1 38  ? 23.299 -0.509  2.289   0.66 10.28 ?  38  ALA   A N    1 
ATOM   866  N N    B ALA   A 1 38  ? 23.301 -0.547  2.275   0.34 10.24 ?  38  ALA   A N    1 
ATOM   867  C CA   A ALA   A 1 38  ? 23.109 -0.631  0.845   0.66 10.26 ?  38  ALA   A CA   1 
ATOM   868  C CA   B ALA   A 1 38  ? 23.143 -0.835  0.850   0.34 10.82 ?  38  ALA   A CA   1 
ATOM   869  C C    A ALA   A 1 38  ? 24.053 0.352   0.152   0.66 10.49 ?  38  ALA   A C    1 
ATOM   870  C C    B ALA   A 1 38  ? 23.930 0.220   0.080   0.34 10.92 ?  38  ALA   A C    1 
ATOM   871  O O    A ALA   A 1 38  ? 23.664 1.443   -0.276  0.66 10.35 ?  38  ALA   A O    1 
ATOM   872  O O    B ALA   A 1 38  ? 23.404 1.266   -0.306  0.34 10.89 ?  38  ALA   A O    1 
ATOM   873  C CB   A ALA   A 1 38  ? 21.655 -0.340  0.484   0.66 10.97 ?  38  ALA   A CB   1 
ATOM   874  C CB   B ALA   A 1 38  ? 21.670 -0.855  0.468   0.34 11.58 ?  38  ALA   A CB   1 
ATOM   875  H H    A ALA   A 1 38  ? 22.694 -0.023  2.663   0.66 12.30 ?  38  ALA   A H    1 
ATOM   876  H H    B ALA   A 1 38  ? 22.698 -0.023  2.603   0.34 12.26 ?  38  ALA   A H    1 
ATOM   877  H HA   A ALA   A 1 38  ? 23.331 -1.528  0.560   0.66 12.29 ?  38  ALA   A HA   1 
ATOM   878  H HA   B ALA   A 1 38  ? 23.525 -1.708  0.658   0.34 12.95 ?  38  ALA   A HA   1 
ATOM   879  H HB1  A ALA   A 1 38  ? 21.542 -0.429  -0.475  0.66 13.14 ?  38  ALA   A HB1  1 
ATOM   880  H HB1  B ALA   A 1 38  ? 21.604 -0.914  -0.495  0.34 13.86 ?  38  ALA   A HB1  1 
ATOM   881  H HB2  A ALA   A 1 38  ? 21.084 -0.974  0.945   0.66 13.14 ?  38  ALA   A HB2  1 
ATOM   882  H HB2  B ALA   A 1 38  ? 21.246 -1.623  0.882   0.34 13.86 ?  38  ALA   A HB2  1 
ATOM   883  H HB3  A ALA   A 1 38  ? 21.434 0.565   0.760   0.66 13.14 ?  38  ALA   A HB3  1 
ATOM   884  H HB3  B ALA   A 1 38  ? 21.257 -0.035  0.777   0.34 13.86 ?  38  ALA   A HB3  1 
ATOM   885  N N    A ALA   A 1 39  ? 25.321 -0.046  0.047   0.66 10.15 ?  39  ALA   A N    1 
ATOM   886  N N    B ALA   A 1 39  ? 25.212 -0.057  -0.142  0.34 11.12 ?  39  ALA   A N    1 
ATOM   887  C CA   A ALA   A 1 39  ? 26.378 0.824   -0.440  0.66 9.79  ?  39  ALA   A CA   1 
ATOM   888  C CA   B ALA   A 1 39  ? 26.152 0.931   -0.645  0.34 10.50 ?  39  ALA   A CA   1 
ATOM   889  C C    A ALA   A 1 39  ? 26.497 0.770   -1.960  0.66 9.77  ?  39  ALA   A C    1 
ATOM   890  C C    B ALA   A 1 39  ? 26.346 0.802   -2.153  0.34 10.54 ?  39  ALA   A C    1 
ATOM   891  O O    A ALA   A 1 39  ? 25.986 -0.136  -2.624  0.66 10.99 ?  39  ALA   A O    1 
ATOM   892  O O    B ALA   A 1 39  ? 25.961 -0.185  -2.785  0.34 11.09 ?  39  ALA   A O    1 
ATOM   893  C CB   A ALA   A 1 39  ? 27.707 0.417   0.199   0.66 10.24 ?  39  ALA   A CB   1 
ATOM   894  C CB   B ALA   A 1 39  ? 27.497 0.778   0.070   0.34 10.92 ?  39  ALA   A CB   1 
ATOM   895  H H    A ALA   A 1 39  ? 25.592 -0.839  0.255   0.66 12.16 ?  39  ALA   A H    1 
ATOM   896  H H    B ALA   A 1 39  ? 25.566 -0.832  0.004   0.34 13.31 ?  39  ALA   A H    1 
ATOM   897  H HA   A ALA   A 1 39  ? 26.184 1.738   -0.182  0.66 11.72 ?  39  ALA   A HA   1 
ATOM   898  H HA   B ALA   A 1 39  ? 25.808 1.817   -0.447  0.34 12.57 ?  39  ALA   A HA   1 
ATOM   899  H HB1  A ALA   A 1 39  ? 28.408 1.006   -0.128  0.66 12.26 ?  39  ALA   A HB1  1 
ATOM   900  H HB1  B ALA   A 1 39  ? 28.113 1.445   -0.274  0.34 13.08 ?  39  ALA   A HB1  1 
ATOM   901  H HB2  A ALA   A 1 39  ? 27.633 0.504   1.164   0.66 12.26 ?  39  ALA   A HB2  1 
ATOM   902  H HB2  B ALA   A 1 39  ? 27.369 0.910   1.024   0.34 13.08 ?  39  ALA   A HB2  1 
ATOM   903  H HB3  A ALA   A 1 39  ? 27.908 -0.499  -0.037  0.66 12.26 ?  39  ALA   A HB3  1 
ATOM   904  H HB3  B ALA   A 1 39  ? 27.845 -0.111  -0.096  0.34 13.08 ?  39  ALA   A HB3  1 
ATOM   905  N N    A ASN   A 1 40  ? 27.193 1.766   -2.509  0.66 10.34 ?  40  ASN   A N    1 
ATOM   906  N N    B ASN   A 1 40  ? 26.950 1.837   -2.730  0.34 10.40 ?  40  ASN   A N    1 
ATOM   907  C CA   A ASN   A 1 40  ? 27.723 1.710   -3.865  0.66 10.85 ?  40  ASN   A CA   1 
ATOM   908  C CA   B ASN   A 1 40  ? 27.516 1.766   -4.068  0.34 10.61 ?  40  ASN   A CA   1 
ATOM   909  C C    A ASN   A 1 40  ? 29.250 1.602   -3.804  0.66 10.22 ?  40  ASN   A C    1 
ATOM   910  C C    B ASN   A 1 40  ? 29.032 1.591   -3.965  0.34 11.14 ?  40  ASN   A C    1 
ATOM   911  O O    A ASN   A 1 40  ? 29.855 1.718   -2.735  0.66 10.43 ?  40  ASN   A O    1 
ATOM   912  O O    B ASN   A 1 40  ? 29.616 1.650   -2.881  0.34 11.19 ?  40  ASN   A O    1 
ATOM   913  C CB   A ASN   A 1 40  ? 27.229 2.891   -4.727  0.66 12.25 ?  40  ASN   A CB   1 
ATOM   914  C CB   B ASN   A 1 40  ? 27.148 3.010   -4.891  0.34 10.93 ?  40  ASN   A CB   1 
ATOM   915  C CG   A ASN   A 1 40  ? 27.599 4.247   -4.156  0.66 13.49 ?  40  ASN   A CG   1 
ATOM   916  C CG   B ASN   A 1 40  ? 27.536 4.305   -4.207  0.34 11.32 ?  40  ASN   A CG   1 
ATOM   917  O OD1  A ASN   A 1 40  ? 28.763 4.509   -3.842  0.66 13.53 ?  40  ASN   A OD1  1 
ATOM   918  O OD1  B ASN   A 1 40  ? 28.714 4.555   -3.945  0.34 11.41 ?  40  ASN   A OD1  1 
ATOM   919  N ND2  A ASN   A 1 40  ? 26.601 5.125   -4.030  0.66 14.65 ?  40  ASN   A ND2  1 
ATOM   920  N ND2  B ASN   A 1 40  ? 26.543 5.146   -3.928  0.34 12.32 ?  40  ASN   A ND2  1 
ATOM   921  H H    A ASN   A 1 40  ? 27.381 2.503   -2.104  0.66 12.38 ?  40  ASN   A H    1 
ATOM   922  H H    B ASN   A 1 40  ? 27.048 2.603   -2.352  0.34 12.45 ?  40  ASN   A H    1 
ATOM   923  H HA   A ASN   A 1 40  ? 27.398 0.902   -4.287  0.66 12.99 ?  40  ASN   A HA   1 
ATOM   924  H HA   B ASN   A 1 40  ? 27.151 0.986   -4.521  0.34 12.70 ?  40  ASN   A HA   1 
ATOM   925  H HB2  A ASN   A 1 40  ? 27.619 2.821   -5.617  0.66 14.68 ?  40  ASN   A HB2  1 
ATOM   926  H HB2  B ASN   A 1 40  ? 27.610 2.969   -5.740  0.34 13.09 ?  40  ASN   A HB2  1 
ATOM   927  H HB3  A ASN   A 1 40  ? 26.261 2.852   -4.795  0.66 14.68 ?  40  ASN   A HB3  1 
ATOM   928  H HB3  B ASN   A 1 40  ? 26.189 3.018   -5.035  0.34 13.09 ?  40  ASN   A HB3  1 
ATOM   929  H HD21 A ASN   A 1 40  ? 26.756 5.913   -3.717  0.66 17.55 ?  40  ASN   A HD21 1 
ATOM   930  H HD21 B ASN   A 1 40  ? 26.713 5.895   -3.540  0.34 14.76 ?  40  ASN   A HD21 1 
ATOM   931  H HD22 A ASN   A 1 40  ? 25.800 4.904   -4.252  0.66 17.55 ?  40  ASN   A HD22 1 
ATOM   932  H HD22 B ASN   A 1 40  ? 25.734 4.940   -4.130  0.34 14.76 ?  40  ASN   A HD22 1 
ATOM   933  N N    A VAL   A 1 41  ? 29.867 1.339   -4.961  0.66 10.35 ?  41  VAL   A N    1 
ATOM   934  N N    B VAL   A 1 41  ? 29.671 1.362   -5.115  0.34 11.21 ?  41  VAL   A N    1 
ATOM   935  C CA   A VAL   A 1 41  ? 31.297 1.027   -4.994  0.66 11.21 ?  41  VAL   A CA   1 
ATOM   936  C CA   B VAL   A 1 41  ? 31.095 1.030   -5.109  0.34 11.40 ?  41  VAL   A CA   1 
ATOM   937  C C    A VAL   A 1 41  ? 32.154 2.187   -4.525  0.66 11.48 ?  41  VAL   A C    1 
ATOM   938  C C    B VAL   A 1 41  ? 31.966 2.163   -4.584  0.34 11.23 ?  41  VAL   A C    1 
ATOM   939  O O    A VAL   A 1 41  ? 33.300 1.975   -4.113  0.66 12.09 ?  41  VAL   A O    1 
ATOM   940  O O    B VAL   A 1 41  ? 33.089 1.913   -4.130  0.34 11.37 ?  41  VAL   A O    1 
ATOM   941  C CB   A VAL   A 1 41  ? 31.785 0.548   -6.382  0.66 12.05 ?  41  VAL   A CB   1 
ATOM   942  C CB   B VAL   A 1 41  ? 31.580 0.558   -6.497  0.34 12.17 ?  41  VAL   A CB   1 
ATOM   943  C CG1  A VAL   A 1 41  ? 31.080 -0.737  -6.800  0.66 12.89 ?  41  VAL   A CG1  1 
ATOM   944  C CG1  B VAL   A 1 41  ? 30.865 -0.723  -6.909  0.34 13.12 ?  41  VAL   A CG1  1 
ATOM   945  C CG2  A VAL   A 1 41  ? 31.650 1.635   -7.445  0.66 12.67 ?  41  VAL   A CG2  1 
ATOM   946  C CG2  B VAL   A 1 41  ? 31.408 1.651   -7.543  0.34 12.77 ?  41  VAL   A CG2  1 
ATOM   947  H H    A VAL   A 1 41  ? 29.486 1.320   -5.731  0.66 12.39 ?  41  VAL   A H    1 
ATOM   948  H H    B VAL   A 1 41  ? 29.300 1.373   -5.892  0.34 13.42 ?  41  VAL   A H    1 
ATOM   949  H HA   A VAL   A 1 41  ? 31.460 0.292   -4.382  0.66 13.43 ?  41  VAL   A HA   1 
ATOM   950  H HA   B VAL   A 1 41  ? 31.217 0.283   -4.505  0.34 13.65 ?  41  VAL   A HA   1 
ATOM   951  H HB   A VAL   A 1 41  ? 32.733 0.339   -6.316  0.66 14.43 ?  41  VAL   A HB   1 
ATOM   952  H HB   B VAL   A 1 41  ? 32.526 0.352   -6.436  0.34 14.57 ?  41  VAL   A HB   1 
ATOM   953  H HG11 A VAL   A 1 41  ? 31.415 -1.019  -7.668  0.66 15.43 ?  41  VAL   A HG11 1 
ATOM   954  H HG11 B VAL   A 1 41  ? 31.198 -1.008  -7.774  0.34 15.72 ?  41  VAL   A HG11 1 
ATOM   955  H HG12 A VAL   A 1 41  ? 31.258 -1.427  -6.141  0.66 15.43 ?  41  VAL   A HG12 1 
ATOM   956  H HG12 B VAL   A 1 41  ? 31.039 -1.411  -6.245  0.34 15.72 ?  41  VAL   A HG12 1 
ATOM   957  H HG13 A VAL   A 1 41  ? 30.125 -0.571  -6.855  0.66 15.43 ?  41  VAL   A HG13 1 
ATOM   958  H HG13 B VAL   A 1 41  ? 29.912 -0.552  -6.961  0.34 15.72 ?  41  VAL   A HG13 1 
ATOM   959  H HG21 A VAL   A 1 41  ? 31.865 1.255   -8.316  0.66 15.17 ?  41  VAL   A HG21 1 
ATOM   960  H HG21 B VAL   A 1 41  ? 31.675 1.300   -8.409  0.34 15.29 ?  41  VAL   A HG21 1 
ATOM   961  H HG22 A VAL   A 1 41  ? 30.740 1.964   -7.447  0.66 15.17 ?  41  VAL   A HG22 1 
ATOM   962  H HG22 B VAL   A 1 41  ? 30.481 1.924   -7.567  0.34 15.29 ?  41  VAL   A HG22 1 
ATOM   963  H HG23 A VAL   A 1 41  ? 32.266 2.357   -7.244  0.66 15.17 ?  41  VAL   A HG23 1 
ATOM   964  H HG23 B VAL   A 1 41  ? 31.973 2.403   -7.306  0.34 15.29 ?  41  VAL   A HG23 1 
ATOM   965  N N    A TYR   A 1 42  ? 31.639 3.412   -4.608  0.66 11.25 ?  42  TYR   A N    1 
ATOM   966  N N    B TYR   A 1 42  ? 31.488 3.407   -4.643  0.34 11.18 ?  42  TYR   A N    1 
ATOM   967  C CA   A TYR   A 1 42  ? 32.357 4.607   -4.186  0.66 11.27 ?  42  TYR   A CA   1 
ATOM   968  C CA   B TYR   A 1 42  ? 32.270 4.572   -4.237  0.34 11.24 ?  42  TYR   A CA   1 
ATOM   969  C C    A TYR   A 1 42  ? 32.062 4.983   -2.746  0.66 10.72 ?  42  TYR   A C    1 
ATOM   970  C C    B TYR   A 1 42  ? 32.071 4.943   -2.772  0.34 10.87 ?  42  TYR   A C    1 
ATOM   971  O O    A TYR   A 1 42  ? 32.601 5.987   -2.259  0.66 11.82 ?  42  TYR   A O    1 
ATOM   972  O O    B TYR   A 1 42  ? 32.704 5.890   -2.292  0.34 11.61 ?  42  TYR   A O    1 
ATOM   973  C CB   A TYR   A 1 42  ? 32.026 5.789   -5.112  0.66 12.56 ?  42  TYR   A CB   1 
ATOM   974  C CB   B TYR   A 1 42  ? 31.914 5.776   -5.118  0.34 12.24 ?  42  TYR   A CB   1 
ATOM   975  C CG   A TYR   A 1 42  ? 32.235 5.469   -6.575  0.66 12.79 ?  42  TYR   A CG   1 
ATOM   976  C CG   B TYR   A 1 42  ? 32.012 5.488   -6.601  0.34 12.67 ?  42  TYR   A CG   1 
ATOM   977  C CD1  A TYR   A 1 42  ? 33.507 5.268   -7.087  0.66 13.32 ?  42  TYR   A CD1  1 
ATOM   978  C CD1  B TYR   A 1 42  ? 33.243 5.284   -7.208  0.34 12.92 ?  42  TYR   A CD1  1 
ATOM   979  C CD2  A TYR   A 1 42  ? 31.153 5.331   -7.439  0.66 14.62 ?  42  TYR   A CD2  1 
ATOM   980  C CD2  B TYR   A 1 42  ? 30.871 5.413   -7.394  0.34 13.45 ?  42  TYR   A CD2  1 
ATOM   981  C CE1  A TYR   A 1 42  ? 33.700 4.952   -8.418  0.66 13.64 ?  42  TYR   A CE1  1 
ATOM   982  C CE1  B TYR   A 1 42  ? 33.341 5.014   -8.559  0.34 13.10 ?  42  TYR   A CE1  1 
ATOM   983  C CE2  A TYR   A 1 42  ? 31.340 5.026   -8.776  0.66 15.03 ?  42  TYR   A CE2  1 
ATOM   984  C CE2  B TYR   A 1 42  ? 30.959 5.148   -8.749  0.34 13.86 ?  42  TYR   A CE2  1 
ATOM   985  C CZ   A TYR   A 1 42  ? 32.617 4.835   -9.260  0.66 14.49 ?  42  TYR   A CZ   1 
ATOM   986  C CZ   B TYR   A 1 42  ? 32.197 4.948   -9.325  0.34 13.46 ?  42  TYR   A CZ   1 
ATOM   987  O OH   A TYR   A 1 42  ? 32.808 4.522   -10.583 0.66 15.71 ?  42  TYR   A OH   1 
ATOM   988  O OH   B TYR   A 1 42  ? 32.303 4.683   -10.670 0.34 13.85 ?  42  TYR   A OH   1 
ATOM   989  H H    A TYR   A 1 42  ? 30.852 3.574   -4.914  0.66 13.48 ?  42  TYR   A H    1 
ATOM   990  H H    B TYR   A 1 42  ? 30.696 3.604   -4.924  0.34 13.39 ?  42  TYR   A H    1 
ATOM   991  H HA   A TYR   A 1 42  ? 33.310 4.439   -4.255  0.66 13.50 ?  42  TYR   A HA   1 
ATOM   992  H HA   B TYR   A 1 42  ? 33.209 4.374   -4.377  0.34 13.46 ?  42  TYR   A HA   1 
ATOM   993  H HB2  A TYR   A 1 42  ? 31.093 6.034   -4.989  0.66 15.04 ?  42  TYR   A HB2  1 
ATOM   994  H HB2  B TYR   A 1 42  ? 31.001 6.047   -4.925  0.34 14.66 ?  42  TYR   A HB2  1 
ATOM   995  H HB3  A TYR   A 1 42  ? 32.596 6.539   -4.884  0.66 15.04 ?  42  TYR   A HB3  1 
ATOM   996  H HB3  B TYR   A 1 42  ? 32.522 6.504   -4.913  0.34 14.66 ?  42  TYR   A HB3  1 
ATOM   997  H HD1  A TYR   A 1 42  ? 34.243 5.344   -6.521  0.66 15.95 ?  42  TYR   A HD1  1 
ATOM   998  H HD1  B TYR   A 1 42  ? 34.016 5.324   -6.694  0.34 15.47 ?  42  TYR   A HD1  1 
ATOM   999  H HD2  A TYR   A 1 42  ? 30.290 5.465   -7.116  0.66 17.51 ?  42  TYR   A HD2  1 
ATOM   1000 H HD2  B TYR   A 1 42  ? 30.036 5.550   -7.009  0.34 16.12 ?  42  TYR   A HD2  1 
ATOM   1001 H HE1  A TYR   A 1 42  ? 34.561 4.826   -8.746  0.66 16.34 ?  42  TYR   A HE1  1 
ATOM   1002 H HE1  B TYR   A 1 42  ? 34.175 4.877   -8.950  0.34 15.69 ?  42  TYR   A HE1  1 
ATOM   1003 H HE2  A TYR   A 1 42  ? 30.606 4.947   -9.345  0.66 18.01 ?  42  TYR   A HE2  1 
ATOM   1004 H HE2  B TYR   A 1 42  ? 30.190 5.102   -9.270  0.34 16.60 ?  42  TYR   A HE2  1 
ATOM   1005 H HH   A TYR   A 1 42  ? 33.624 4.390   -10.731 0.66 18.82 ?  42  TYR   A HH   1 
ATOM   1006 H HH   B TYR   A 1 42  ? 31.542 4.668   -11.024 0.34 16.59 ?  42  TYR   A HH   1 
ATOM   1007 N N    . LEU   A 1 43  ? 31.203 4.223   -2.066  1.00 10.77 ?  43  LEU   A N    1 
ATOM   1008 C CA   . LEU   A 1 43  ? 30.771 4.564   -0.714  1.00 10.32 ?  43  LEU   A CA   1 
ATOM   1009 C C    . LEU   A 1 43  ? 30.291 6.012   -0.618  1.00 10.53 ?  43  LEU   A C    1 
ATOM   1010 O O    . LEU   A 1 43  ? 30.551 6.711   0.363   1.00 12.19 ?  43  LEU   A O    1 
ATOM   1011 C CB   . LEU   A 1 43  ? 31.820 4.243   0.350   1.00 11.84 ?  43  LEU   A CB   1 
ATOM   1012 C CG   . LEU   A 1 43  ? 32.318 2.797   0.424   1.00 11.92 ?  43  LEU   A CG   1 
ATOM   1013 C CD1  . LEU   A 1 43  ? 33.357 2.684   1.515   1.00 12.62 ?  43  LEU   A CD1  1 
ATOM   1014 C CD2  . LEU   A 1 43  ? 31.175 1.812   0.662   1.00 11.71 ?  43  LEU   A CD2  1 
ATOM   1015 H H    A LEU   A 1 43  ? 30.863 3.488   -2.365  0.66 12.89 ?  43  LEU   A H    1 
ATOM   1016 H H    B LEU   A 1 43  ? 30.828 3.505   -2.365  0.34 12.89 ?  43  LEU   A H    1 
ATOM   1017 H HA   . LEU   A 1 43  ? 29.999 4.006   -0.508  1.00 12.35 ?  43  LEU   A HA   1 
ATOM   1018 H HB2  . LEU   A 1 43  ? 32.594 4.806   0.191   1.00 14.18 ?  43  LEU   A HB2  1 
ATOM   1019 H HB3  . LEU   A 1 43  ? 31.445 4.457   1.220   1.00 14.18 ?  43  LEU   A HB3  1 
ATOM   1020 H HG   . LEU   A 1 43  ? 32.745 2.566   -0.419  1.00 14.28 ?  43  LEU   A HG   1 
ATOM   1021 H HD11 . LEU   A 1 43  ? 33.672 1.765   1.554   1.00 15.12 ?  43  LEU   A HD11 1 
ATOM   1022 H HD12 . LEU   A 1 43  ? 34.096 3.277   1.310   1.00 15.12 ?  43  LEU   A HD12 1 
ATOM   1023 H HD13 . LEU   A 1 43  ? 32.953 2.932   2.359   1.00 15.12 ?  43  LEU   A HD13 1 
ATOM   1024 H HD21 . LEU   A 1 43  ? 31.545 0.927   0.795   1.00 14.02 ?  43  LEU   A HD21 1 
ATOM   1025 H HD22 . LEU   A 1 43  ? 30.685 2.090   1.451   1.00 14.02 ?  43  LEU   A HD22 1 
ATOM   1026 H HD23 . LEU   A 1 43  ? 30.592 1.817   -0.111  1.00 14.02 ?  43  LEU   A HD23 1 
ATOM   1027 N N    A LYS   A 1 44  ? 29.576 6.457   -1.654  0.66 10.82 ?  44  LYS   A N    1 
ATOM   1028 N N    B LYS   A 1 44  ? 29.564 6.459   -1.639  0.34 11.64 ?  44  LYS   A N    1 
ATOM   1029 C CA   A LYS   A 1 44  ? 28.937 7.772   -1.665  0.66 10.83 ?  44  LYS   A CA   1 
ATOM   1030 C CA   B LYS   A 1 44  ? 28.905 7.759   -1.609  0.34 12.70 ?  44  LYS   A CA   1 
ATOM   1031 C C    A LYS   A 1 44  ? 27.507 7.592   -1.171  0.66 9.95  ?  44  LYS   A C    1 
ATOM   1032 C C    B LYS   A 1 44  ? 27.474 7.552   -1.130  0.34 12.18 ?  44  LYS   A C    1 
ATOM   1033 O O    A LYS   A 1 44  ? 26.648 7.071   -1.886  0.66 11.61 ?  44  LYS   A O    1 
ATOM   1034 O O    B LYS   A 1 44  ? 26.630 7.029   -1.866  0.34 12.72 ?  44  LYS   A O    1 
ATOM   1035 C CB   A LYS   A 1 44  ? 28.981 8.374   -3.062  0.66 13.17 ?  44  LYS   A CB   1 
ATOM   1036 C CB   B LYS   A 1 44  ? 28.955 8.421   -2.983  0.34 14.63 ?  44  LYS   A CB   1 
ATOM   1037 C CG   A LYS   A 1 44  ? 30.362 8.838   -3.500  0.66 16.66 ?  44  LYS   A CG   1 
ATOM   1038 C CG   B LYS   A 1 44  ? 30.334 8.954   -3.358  0.34 16.84 ?  44  LYS   A CG   1 
ATOM   1039 C CD   A LYS   A 1 44  ? 30.996 9.778   -2.486  0.66 20.74 ?  44  LYS   A CD   1 
ATOM   1040 C CD   B LYS   A 1 44  ? 30.898 9.872   -2.275  0.34 19.63 ?  44  LYS   A CD   1 
ATOM   1041 C CE   A LYS   A 1 44  ? 32.294 10.362  -3.005  0.66 23.05 ?  44  LYS   A CE   1 
ATOM   1042 C CE   B LYS   A 1 44  ? 32.241 10.450  -2.675  0.34 21.60 ?  44  LYS   A CE   1 
ATOM   1043 N NZ   A LYS   A 1 44  ? 33.162 10.827  -1.888  0.66 24.28 ?  44  LYS   A NZ   1 
ATOM   1044 N NZ   B LYS   A 1 44  ? 32.911 11.144  -1.541  0.34 22.78 ?  44  LYS   A NZ   1 
ATOM   1045 H H    A LYS   A 1 44  ? 29.449 6.004   -2.375  0.66 12.96 ?  44  LYS   A H    1 
ATOM   1046 H H    B LYS   A 1 44  ? 29.440 6.021   -2.369  0.34 13.94 ?  44  LYS   A H    1 
ATOM   1047 H HA   A LYS   A 1 44  ? 29.391 8.358   -1.042  0.66 12.96 ?  44  LYS   A HA   1 
ATOM   1048 H HA   B LYS   A 1 44  ? 29.340 8.328   -0.958  0.34 15.21 ?  44  LYS   A HA   1 
ATOM   1049 H HB2  A LYS   A 1 44  ? 28.677 7.712   -3.699  0.66 15.77 ?  44  LYS   A HB2  1 
ATOM   1050 H HB2  B LYS   A 1 44  ? 28.696 7.771   -3.655  0.34 17.53 ?  44  LYS   A HB2  1 
ATOM   1051 H HB3  A LYS   A 1 44  ? 28.392 9.147   -3.085  0.66 15.77 ?  44  LYS   A HB3  1 
ATOM   1052 H HB3  B LYS   A 1 44  ? 28.337 9.170   -2.995  0.34 17.53 ?  44  LYS   A HB3  1 
ATOM   1053 H HG2  A LYS   A 1 44  ? 30.943 8.068   -3.604  0.66 19.96 ?  44  LYS   A HG2  1 
ATOM   1054 H HG2  B LYS   A 1 44  ? 30.944 8.209   -3.476  0.34 20.18 ?  44  LYS   A HG2  1 
ATOM   1055 H HG3  A LYS   A 1 44  ? 30.290 9.315   -4.345  0.66 19.96 ?  44  LYS   A HG3  1 
ATOM   1056 H HG3  B LYS   A 1 44  ? 30.268 9.465   -4.183  0.34 20.18 ?  44  LYS   A HG3  1 
ATOM   1057 H HD2  A LYS   A 1 44  ? 30.382 10.503  -2.294  0.66 24.86 ?  44  LYS   A HD2  1 
ATOM   1058 H HD2  B LYS   A 1 44  ? 30.274 10.598  -2.116  0.34 23.53 ?  44  LYS   A HD2  1 
ATOM   1059 H HD3  A LYS   A 1 44  ? 31.198 9.283   -1.675  0.66 24.86 ?  44  LYS   A HD3  1 
ATOM   1060 H HD3  B LYS   A 1 44  ? 31.036 9.362   -1.460  0.34 23.53 ?  44  LYS   A HD3  1 
ATOM   1061 H HE2  A LYS   A 1 44  ? 32.778 9.682   -3.500  0.66 27.63 ?  44  LYS   A HE2  1 
ATOM   1062 H HE2  B LYS   A 1 44  ? 32.819 9.729   -2.974  0.34 25.89 ?  44  LYS   A HE2  1 
ATOM   1063 H HE3  A LYS   A 1 44  ? 32.099 11.120  -3.576  0.66 27.63 ?  44  LYS   A HE3  1 
ATOM   1064 H HE3  B LYS   A 1 44  ? 32.110 11.090  -3.388  0.34 25.89 ?  44  LYS   A HE3  1 
ATOM   1065 H HZ1  A LYS   A 1 44  ? 33.916 11.168  -2.210  0.66 29.11 ?  44  LYS   A HZ1  1 
ATOM   1066 H HZ1  B LYS   A 1 44  ? 33.696 11.469  -1.807  0.34 27.31 ?  44  LYS   A HZ1  1 
ATOM   1067 H HZ2  A LYS   A 1 44  ? 32.738 11.456  -1.418  0.66 29.11 ?  44  LYS   A HZ2  1 
ATOM   1068 H HZ2  B LYS   A 1 44  ? 32.403 11.812  -1.250  0.34 27.31 ?  44  LYS   A HZ2  1 
ATOM   1069 H HZ3  A LYS   A 1 44  ? 33.356 10.147  -1.349  0.66 29.11 ?  44  LYS   A HZ3  1 
ATOM   1070 H HZ3  B LYS   A 1 44  ? 33.049 10.571  -0.872  0.34 27.31 ?  44  LYS   A HZ3  1 
ATOM   1071 N N    A HIS   A 1 45  ? 27.266 7.988   0.076   0.66 9.87  ?  45  HIS   A N    1 
ATOM   1072 N N    B HIS   A 1 45  ? 27.209 7.947   0.113   0.34 12.06 ?  45  HIS   A N    1 
ATOM   1073 C CA   A HIS   A 1 45  ? 26.032 7.641   0.784   0.66 10.22 ?  45  HIS   A CA   1 
ATOM   1074 C CA   B HIS   A 1 45  ? 25.940 7.657   0.778   0.34 12.06 ?  45  HIS   A CA   1 
ATOM   1075 C C    A HIS   A 1 45  ? 24.997 8.761   0.621   0.66 10.90 ?  45  HIS   A C    1 
ATOM   1076 C C    B HIS   A 1 45  ? 25.006 8.836   0.547   0.34 12.61 ?  45  HIS   A C    1 
ATOM   1077 O O    A HIS   A 1 45  ? 24.625 9.468   1.561   0.66 11.28 ?  45  HIS   A O    1 
ATOM   1078 O O    B HIS   A 1 45  ? 24.987 9.803   1.310   0.34 13.30 ?  45  HIS   A O    1 
ATOM   1079 C CB   A HIS   A 1 45  ? 26.347 7.374   2.245   0.66 10.24 ?  45  HIS   A CB   1 
ATOM   1080 C CB   B HIS   A 1 45  ? 26.176 7.410   2.259   0.34 11.53 ?  45  HIS   A CB   1 
ATOM   1081 C CG   A HIS   A 1 45  ? 27.459 6.389   2.451   0.66 10.20 ?  45  HIS   A CG   1 
ATOM   1082 C CG   B HIS   A 1 45  ? 27.316 6.480   2.533   0.34 10.52 ?  45  HIS   A CG   1 
ATOM   1083 N ND1  A HIS   A 1 45  ? 27.432 5.101   1.949   0.66 10.68 ?  45  HIS   A ND1  1 
ATOM   1084 N ND1  B HIS   A 1 45  ? 27.370 5.199   2.025   0.34 10.89 ?  45  HIS   A ND1  1 
ATOM   1085 C CD2  A HIS   A 1 45  ? 28.642 6.519   3.098   0.66 10.75 ?  45  HIS   A CD2  1 
ATOM   1086 C CD2  B HIS   A 1 45  ? 28.456 6.656   3.243   0.34 9.72  ?  45  HIS   A CD2  1 
ATOM   1087 C CE1  A HIS   A 1 45  ? 28.547 4.482   2.292   0.66 11.37 ?  45  HIS   A CE1  1 
ATOM   1088 C CE1  B HIS   A 1 45  ? 28.490 4.623   2.422   0.34 9.73  ?  45  HIS   A CE1  1 
ATOM   1089 N NE2  A HIS   A 1 45  ? 29.300 5.320   2.984   0.66 11.49 ?  45  HIS   A NE2  1 
ATOM   1090 N NE2  B HIS   A 1 45  ? 29.165 5.483   3.164   0.34 9.05  ?  45  HIS   A NE2  1 
ATOM   1091 H H    A HIS   A 1 45  ? 27.806 8.469   0.543   0.66 11.82 ?  45  HIS   A H    1 
ATOM   1092 H H    B HIS   A 1 45  ? 27.756 8.402   0.599   0.34 14.44 ?  45  HIS   A H    1 
ATOM   1093 H HA   A HIS   A 1 45  ? 25.662 6.833   0.400   0.66 12.24 ?  45  HIS   A HA   1 
ATOM   1094 H HA   B HIS   A 1 45  ? 25.545 6.862   0.390   0.34 14.44 ?  45  HIS   A HA   1 
ATOM   1095 H HB2  A HIS   A 1 45  ? 26.600 8.208   2.671   0.66 12.26 ?  45  HIS   A HB2  1 
ATOM   1096 H HB2  B HIS   A 1 45  ? 26.371 8.257   2.691   0.34 13.80 ?  45  HIS   A HB2  1 
ATOM   1097 H HB3  A HIS   A 1 45  ? 25.551 7.017   2.675   0.66 12.26 ?  45  HIS   A HB3  1 
ATOM   1098 H HB3  B HIS   A 1 45  ? 25.375 7.022   2.644   0.34 13.80 ?  45  HIS   A HB3  1 
ATOM   1099 H HD2  A HIS   A 1 45  ? 28.953 7.284   3.533   0.66 12.87 ?  45  HIS   A HD2  1 
ATOM   1100 H HD2  B HIS   A 1 45  ? 28.707 7.426   3.703   0.34 11.64 ?  45  HIS   A HD2  1 
ATOM   1101 H HE1  A HIS   A 1 45  ? 28.767 3.604   2.086   0.66 13.61 ?  45  HIS   A HE1  1 
ATOM   1102 H HE1  B HIS   A 1 45  ? 28.758 3.759   2.218   0.34 11.65 ?  45  HIS   A HE1  1 
ATOM   1103 H HE2  A HIS   A 1 45  ? 30.075 5.144   3.314   0.66 13.76 ?  45  HIS   A HE2  1 
ATOM   1104 H HE2  B HIS   A 1 45  ? 29.929 5.337   3.532   0.34 10.83 ?  45  HIS   A HE2  1 
ATOM   1105 N N    A GLY   A 1 46  ? 24.528 8.914   -0.615  0.66 12.40 ?  46  GLY   A N    1 
ATOM   1106 N N    B GLY   A 1 46  ? 24.223 8.759   -0.523  0.34 12.74 ?  46  GLY   A N    1 
ATOM   1107 C CA   A GLY   A 1 46  ? 23.721 10.074  -0.956  0.66 13.26 ?  46  GLY   A CA   1 
ATOM   1108 C CA   B GLY   A 1 46  ? 23.371 9.872   -0.891  0.34 12.07 ?  46  GLY   A CA   1 
ATOM   1109 C C    A GLY   A 1 46  ? 22.226 9.945   -0.728  0.66 13.23 ?  46  GLY   A C    1 
ATOM   1110 C C    B GLY   A 1 46  ? 21.922 9.729   -0.474  0.34 11.43 ?  46  GLY   A C    1 
ATOM   1111 O O    A GLY   A 1 46  ? 21.550 10.938  -0.434  0.66 13.93 ?  46  GLY   A O    1 
ATOM   1112 O O    B GLY   A 1 46  ? 21.315 10.692  0.007   0.34 11.46 ?  46  GLY   A O    1 
ATOM   1113 H H    A GLY   A 1 46  ? 24.655 8.361   -1.262  0.66 14.85 ?  46  GLY   A H    1 
ATOM   1114 H H    B GLY   A 1 46  ? 24.177 8.080   -1.052  0.34 15.26 ?  46  GLY   A H    1 
ATOM   1115 H HA2  A GLY   A 1 46  ? 24.034 10.832  -0.436  0.66 15.88 ?  46  GLY   A HA2  1 
ATOM   1116 H HA2  B GLY   A 1 46  ? 23.712 10.682  -0.482  0.34 14.46 ?  46  GLY   A HA2  1 
ATOM   1117 H HA3  A GLY   A 1 46  ? 23.855 10.280  -1.892  0.66 15.88 ?  46  GLY   A HA3  1 
ATOM   1118 H HA3  B GLY   A 1 46  ? 23.400 9.984   -1.851  0.34 14.46 ?  46  GLY   A HA3  1 
ATOM   1119 N N    A GLY   A 1 47  ? 21.696 8.738   -0.886  0.66 12.74 ?  47  GLY   A N    1 
ATOM   1120 N N    B GLY   A 1 47  ? 21.349 8.539   -0.655  0.34 11.37 ?  47  GLY   A N    1 
ATOM   1121 C CA   A GLY   A 1 47  ? 20.263 8.528   -0.845  0.66 12.96 ?  47  GLY   A CA   1 
ATOM   1122 C CA   B GLY   A 1 47  ? 19.930 8.353   -0.440  0.34 11.78 ?  47  GLY   A CA   1 
ATOM   1123 C C    A GLY   A 1 47  ? 19.947 7.089   -0.500  0.66 12.15 ?  47  GLY   A C    1 
ATOM   1124 C C    B GLY   A 1 47  ? 19.605 6.925   -0.062  0.34 10.57 ?  47  GLY   A C    1 
ATOM   1125 O O    A GLY   A 1 47  ? 20.836 6.274   -0.244  0.66 12.35 ?  47  GLY   A O    1 
ATOM   1126 O O    B GLY   A 1 47  ? 20.490 6.076   0.068   0.34 9.70  ?  47  GLY   A O    1 
ATOM   1127 H H    A GLY   A 1 47  ? 22.149 8.022   -1.008  0.66 15.26 ?  47  GLY   A H    1 
ATOM   1128 H H    B GLY   A 1 47  ? 21.769 7.820   -0.892  0.34 13.61 ?  47  GLY   A H    1 
ATOM   1129 H HA2  A GLY   A 1 47  ? 19.857 9.120   -0.185  0.66 15.52 ?  47  GLY   A HA2  1 
ATOM   1130 H HA2  B GLY   A 1 47  ? 19.630 8.938   0.274   0.34 14.10 ?  47  GLY   A HA2  1 
ATOM   1131 H HA3  A GLY   A 1 47  ? 19.879 8.727   -1.714  0.66 15.52 ?  47  GLY   A HA3  1 
ATOM   1132 H HA3  B GLY   A 1 47  ? 19.446 8.582   -1.250  0.34 14.10 ?  47  GLY   A HA3  1 
ATOM   1133 N N    A GLY   A 1 48  ? 18.656 6.774   -0.504  0.66 11.97 ?  48  GLY   A N    1 
ATOM   1134 N N    B GLY   A 1 48  ? 18.310 6.663   0.111   0.34 10.51 ?  48  GLY   A N    1 
ATOM   1135 C CA   A GLY   A 1 48  ? 18.220 5.453   -0.125  0.66 11.36 ?  48  GLY   A CA   1 
ATOM   1136 C CA   B GLY   A 1 48  ? 17.883 5.344   0.546   0.34 10.13 ?  48  GLY   A CA   1 
ATOM   1137 C C    A GLY   A 1 48  ? 18.589 5.145   1.311   0.66 10.82 ?  48  GLY   A C    1 
ATOM   1138 C C    B GLY   A 1 48  ? 18.483 4.993   1.892   0.34 10.41 ?  48  GLY   A C    1 
ATOM   1139 O O    A GLY   A 1 48  ? 18.730 6.036   2.161   0.66 10.97 ?  48  GLY   A O    1 
ATOM   1140 O O    B GLY   A 1 48  ? 18.651 5.847   2.772   0.34 10.58 ?  48  GLY   A O    1 
ATOM   1141 H H    A GLY   A 1 48  ? 18.024 7.303   -0.730  0.66 14.34 ?  48  GLY   A H    1 
ATOM   1142 H H    B GLY   A 1 48  ? 17.663 7.226   -0.010  0.34 12.59 ?  48  GLY   A H    1 
ATOM   1143 H HA2  A GLY   A 1 48  ? 17.265 5.380   -0.220  0.66 13.61 ?  48  GLY   A HA2  1 
ATOM   1144 H HA2  B GLY   A 1 48  ? 16.912 5.314   0.616   0.34 12.13 ?  48  GLY   A HA2  1 
ATOM   1145 H HA3  A GLY   A 1 48  ? 18.647 4.790   -0.695  0.66 13.61 ?  48  GLY   A HA3  1 
ATOM   1146 H HA3  B GLY   A 1 48  ? 18.163 4.677   -0.103  0.34 12.13 ?  48  GLY   A HA3  1 
ATOM   1147 N N    A VAL   A 1 49  ? 18.782 3.851   1.578   0.66 11.18 ?  49  VAL   A N    1 
ATOM   1148 N N    B VAL   A 1 49  ? 18.822 3.712   2.053   0.34 10.15 ?  49  VAL   A N    1 
ATOM   1149 C CA   A VAL   A 1 49  ? 19.230 3.415   2.895   0.66 11.25 ?  49  VAL   A CA   1 
ATOM   1150 C CA   B VAL   A 1 49  ? 19.439 3.242   3.291   0.34 10.14 ?  49  VAL   A CA   1 
ATOM   1151 C C    A VAL   A 1 49  ? 20.548 4.084   3.269   0.66 10.57 ?  49  VAL   A C    1 
ATOM   1152 C C    B VAL   A 1 49  ? 20.731 3.998   3.578   0.34 9.13  ?  49  VAL   A C    1 
ATOM   1153 O O    A VAL   A 1 49  ? 20.729 4.513   4.410   0.66 11.05 ?  49  VAL   A O    1 
ATOM   1154 O O    B VAL   A 1 49  ? 20.992 4.390   4.721   0.34 8.83  ?  49  VAL   A O    1 
ATOM   1155 C CB   A VAL   A 1 49  ? 19.330 1.878   2.936   0.66 12.67 ?  49  VAL   A CB   1 
ATOM   1156 C CB   B VAL   A 1 49  ? 19.675 1.721   3.219   0.34 10.71 ?  49  VAL   A CB   1 
ATOM   1157 C CG1  A VAL   A 1 49  ? 20.064 1.406   4.186   0.66 13.22 ?  49  VAL   A CG1  1 
ATOM   1158 C CG1  B VAL   A 1 49  ? 20.592 1.272   4.344   0.34 10.29 ?  49  VAL   A CG1  1 
ATOM   1159 C CG2  A VAL   A 1 49  ? 17.931 1.271   2.867   0.66 14.89 ?  49  VAL   A CG2  1 
ATOM   1160 C CG2  B VAL   A 1 49  ? 18.356 0.967   3.273   0.34 12.15 ?  49  VAL   A CG2  1 
ATOM   1161 H H    A VAL   A 1 49  ? 18.654 3.203   1.023   0.66 13.38 ?  49  VAL   A H    1 
ATOM   1162 H H    B VAL   A 1 49  ? 18.703 3.099   1.463   0.34 12.15 ?  49  VAL   A H    1 
ATOM   1163 H HA   A VAL   A 1 49  ? 18.577 3.676   3.558   0.66 13.47 ?  49  VAL   A HA   1 
ATOM   1164 H HA   B VAL   A 1 49  ? 18.835 3.408   4.028   0.34 12.14 ?  49  VAL   A HA   1 
ATOM   1165 H HB   A VAL   A 1 49  ? 19.834 1.569   2.167   0.66 15.17 ?  49  VAL   A HB   1 
ATOM   1166 H HB   B VAL   A 1 49  ? 20.111 1.505   2.379   0.34 12.82 ?  49  VAL   A HB   1 
ATOM   1167 H HG11 A VAL   A 1 49  ? 19.883 0.462   4.318   0.66 15.83 ?  49  VAL   A HG11 1 
ATOM   1168 H HG11 B VAL   A 1 49  ? 20.491 0.316   4.466   0.34 12.31 ?  49  VAL   A HG11 1 
ATOM   1169 H HG12 A VAL   A 1 49  ? 21.017 1.545   4.069   0.66 15.83 ?  49  VAL   A HG12 1 
ATOM   1170 H HG12 B VAL   A 1 49  ? 21.510 1.479   4.107   0.34 12.31 ?  49  VAL   A HG12 1 
ATOM   1171 H HG13 A VAL   A 1 49  ? 19.744 1.913   4.949   0.66 15.83 ?  49  VAL   A HG13 1 
ATOM   1172 H HG13 B VAL   A 1 49  ? 20.343 1.737   5.156   0.34 12.31 ?  49  VAL   A HG13 1 
ATOM   1173 H HG21 A VAL   A 1 49  ? 18.005 0.303   2.900   0.66 17.84 ?  49  VAL   A HG21 1 
ATOM   1174 H HG21 B VAL   A 1 49  ? 18.529 0.016   3.195   0.34 14.56 ?  49  VAL   A HG21 1 
ATOM   1175 H HG22 A VAL   A 1 49  ? 17.413 1.588   3.623   0.66 17.84 ?  49  VAL   A HG22 1 
ATOM   1176 H HG22 B VAL   A 1 49  ? 17.919 1.155   4.120   0.34 14.56 ?  49  VAL   A HG22 1 
ATOM   1177 H HG23 A VAL   A 1 49  ? 17.513 1.544   2.037   0.66 17.84 ?  49  VAL   A HG23 1 
ATOM   1178 H HG23 B VAL   A 1 49  ? 17.795 1.263   2.540   0.34 14.56 ?  49  VAL   A HG23 1 
ATOM   1179 N N    A ALA   A 1 50  ? 21.503 4.127   2.332   0.66 10.51 ?  50  ALA   A N    1 
ATOM   1180 N N    B ALA   A 1 50  ? 21.571 4.183   2.555   0.34 9.09  ?  50  ALA   A N    1 
ATOM   1181 C CA   A ALA   A 1 50  ? 22.829 4.664   2.636   0.66 10.44 ?  50  ALA   A CA   1 
ATOM   1182 C CA   B ALA   A 1 50  ? 22.883 4.785   2.773   0.34 8.70  ?  50  ALA   A CA   1 
ATOM   1183 C C    A ALA   A 1 50  ? 22.758 6.131   3.030   0.66 10.50 ?  50  ALA   A C    1 
ATOM   1184 C C    B ALA   A 1 50  ? 22.751 6.223   3.254   0.34 7.97  ?  50  ALA   A C    1 
ATOM   1185 O O    A ALA   A 1 50  ? 23.413 6.555   3.987   0.66 11.32 ?  50  ALA   A O    1 
ATOM   1186 O O    B ALA   A 1 50  ? 23.347 6.610   4.265   0.34 8.32  ?  50  ALA   A O    1 
ATOM   1187 C CB   A ALA   A 1 50  ? 23.742 4.494   1.426   0.66 10.85 ?  50  ALA   A CB   1 
ATOM   1188 C CB   B ALA   A 1 50  ? 23.710 4.715   1.489   0.34 8.88  ?  50  ALA   A CB   1 
ATOM   1189 H H    A ALA   A 1 50  ? 21.407 3.858   1.528   0.66 12.58 ?  50  ALA   A H    1 
ATOM   1190 H H    B ALA   A 1 50  ? 21.398 3.980   1.736   0.34 10.88 ?  50  ALA   A H    1 
ATOM   1191 H HA   A ALA   A 1 50  ? 23.211 4.178   3.384   0.66 12.50 ?  50  ALA   A HA   1 
ATOM   1192 H HA   B ALA   A 1 50  ? 23.349 4.289   3.460   0.34 10.42 ?  50  ALA   A HA   1 
ATOM   1193 H HB1  A ALA   A 1 50  ? 24.616 4.855   1.639   0.66 12.99 ?  50  ALA   A HB1  1 
ATOM   1194 H HB1  B ALA   A 1 50  ? 24.583 5.105   1.654   0.34 10.63 ?  50  ALA   A HB1  1 
ATOM   1195 H HB2  A ALA   A 1 50  ? 23.811 3.551   1.220   0.66 12.99 ?  50  ALA   A HB2  1 
ATOM   1196 H HB2  B ALA   A 1 50  ? 23.808 3.786   1.228   0.34 10.63 ?  50  ALA   A HB2  1 
ATOM   1197 H HB3  A ALA   A 1 50  ? 23.358 4.973   0.677   0.66 12.99 ?  50  ALA   A HB3  1 
ATOM   1198 H HB3  B ALA   A 1 50  ? 23.254 5.209   0.790   0.34 10.63 ?  50  ALA   A HB3  1 
ATOM   1199 N N    A GLY   A 1 51  ? 21.978 6.921   2.299   0.66 10.12 ?  51  GLY   A N    1 
ATOM   1200 N N    B GLY   A 1 51  ? 21.959 7.027   2.544   0.34 9.51  ?  51  GLY   A N    1 
ATOM   1201 C CA   A GLY   A 1 51  ? 21.839 8.325   2.655   0.66 10.91 ?  51  GLY   A CA   1 
ATOM   1202 C CA   B GLY   A 1 51  ? 21.775 8.408   2.957   0.34 9.16  ?  51  GLY   A CA   1 
ATOM   1203 C C    A GLY   A 1 51  ? 21.219 8.506   4.025   0.66 10.32 ?  51  GLY   A C    1 
ATOM   1204 C C    B GLY   A 1 51  ? 21.196 8.514   4.354   0.34 9.51  ?  51  GLY   A C    1 
ATOM   1205 O O    A GLY   A 1 51  ? 21.607 9.401   4.778   0.66 11.04 ?  51  GLY   A O    1 
ATOM   1206 O O    B GLY   A 1 51  ? 21.604 9.368   5.144   0.34 9.55  ?  51  GLY   A O    1 
ATOM   1207 H H    A GLY   A 1 51  ? 21.537 6.684   1.608   0.66 12.12 ?  51  GLY   A H    1 
ATOM   1208 H H    B GLY   A 1 51  ? 21.522 6.801   1.839   0.34 11.38 ?  51  GLY   A H    1 
ATOM   1209 H HA2  A GLY   A 1 51  ? 22.709 8.756   2.666   0.66 13.06 ?  51  GLY   A HA2  1 
ATOM   1210 H HA2  B GLY   A 1 51  ? 22.629 8.870   2.941   0.34 10.97 ?  51  GLY   A HA2  1 
ATOM   1211 H HA3  A GLY   A 1 51  ? 21.279 8.781   2.008   0.66 13.06 ?  51  GLY   A HA3  1 
ATOM   1212 H HA3  B GLY   A 1 51  ? 21.178 8.857   2.331   0.34 10.97 ?  51  GLY   A HA3  1 
ATOM   1213 N N    A ALA   A 1 52  ? 20.257 7.644   4.372   0.66 10.67 ?  52  ALA   A N    1 
ATOM   1214 N N    B ALA   A 1 52  ? 20.246 7.635   4.682   0.34 9.52  ?  52  ALA   A N    1 
ATOM   1215 C CA   A ALA   A 1 52  ? 19.602 7.728   5.674   0.66 11.24 ?  52  ALA   A CA   1 
ATOM   1216 C CA   B ALA   A 1 52  ? 19.603 7.688   5.990   0.34 10.08 ?  52  ALA   A CA   1 
ATOM   1217 C C    A ALA   A 1 52  ? 20.538 7.307   6.803   0.66 11.25 ?  52  ALA   A C    1 
ATOM   1218 C C    B ALA   A 1 52  ? 20.559 7.251   7.097   0.34 9.52  ?  52  ALA   A C    1 
ATOM   1219 O O    A ALA   A 1 52  ? 20.608 7.975   7.841   0.66 12.36 ?  52  ALA   A O    1 
ATOM   1220 O O    B ALA   A 1 52  ? 20.642 7.895   8.150   0.34 9.75  ?  52  ALA   A O    1 
ATOM   1221 C CB   A ALA   A 1 52  ? 18.329 6.881   5.670   0.66 12.56 ?  52  ALA   A CB   1 
ATOM   1222 C CB   B ALA   A 1 52  ? 18.338 6.833   5.981   0.34 11.57 ?  52  ALA   A CB   1 
ATOM   1223 H H    A ALA   A 1 52  ? 19.985 7.003   3.881   0.66 12.78 ?  52  ALA   A H    1 
ATOM   1224 H H    B ALA   A 1 52  ? 19.966 7.007   4.165   0.34 11.40 ?  52  ALA   A H    1 
ATOM   1225 H HA   A ALA   A 1 52  ? 19.340 8.646   5.835   0.66 13.46 ?  52  ALA   A HA   1 
ATOM   1226 H HA   B ALA   A 1 52  ? 19.342 8.605   6.166   0.34 12.07 ?  52  ALA   A HA   1 
ATOM   1227 H HB1  A ALA   A 1 52  ? 17.899 6.946   6.540   0.66 15.05 ?  52  ALA   A HB1  1 
ATOM   1228 H HB1  B ALA   A 1 52  ? 17.898 6.917   6.840   0.34 13.86 ?  52  ALA   A HB1  1 
ATOM   1229 H HB2  A ALA   A 1 52  ? 17.728 7.214   4.983   0.66 15.05 ?  52  ALA   A HB2  1 
ATOM   1230 H HB2  B ALA   A 1 52  ? 17.749 7.151   5.277   0.34 13.86 ?  52  ALA   A HB2  1 
ATOM   1231 H HB3  A ALA   A 1 52  ? 18.559 5.957   5.486   0.66 15.05 ?  52  ALA   A HB3  1 
ATOM   1232 H HB3  B ALA   A 1 52  ? 18.581 5.910   5.816   0.34 13.86 ?  52  ALA   A HB3  1 
ATOM   1233 N N    A LEU   A 1 53  ? 21.268 6.203   6.630   0.66 10.90 ?  53  LEU   A N    1 
ATOM   1234 N N    B LEU   A 1 53  ? 21.289 6.154   6.884   0.34 9.79  ?  53  LEU   A N    1 
ATOM   1235 C CA   A LEU   A 1 53  ? 22.215 5.789   7.664   0.66 11.30 ?  53  LEU   A CA   1 
ATOM   1236 C CA   B LEU   A 1 53  ? 22.302 5.754   7.857   0.34 9.69  ?  53  LEU   A CA   1 
ATOM   1237 C C    A LEU   A 1 53  ? 23.287 6.849   7.869   0.66 10.14 ?  53  LEU   A C    1 
ATOM   1238 C C    B LEU   A 1 53  ? 23.328 6.861   8.046   0.34 9.94  ?  53  LEU   A C    1 
ATOM   1239 O O    A LEU   A 1 53  ? 23.634 7.183   9.006   0.66 11.88 ?  53  LEU   A O    1 
ATOM   1240 O O    B LEU   A 1 53  ? 23.628 7.262   9.176   0.34 10.96 ?  53  LEU   A O    1 
ATOM   1241 C CB   A LEU   A 1 53  ? 22.858 4.446   7.306   0.66 12.70 ?  53  LEU   A CB   1 
ATOM   1242 C CB   B LEU   A 1 53  ? 22.993 4.458   7.420   0.34 9.62  ?  53  LEU   A CB   1 
ATOM   1243 C CG   A LEU   A 1 53  ? 21.949 3.211   7.323   0.66 12.71 ?  53  LEU   A CG   1 
ATOM   1244 C CG   B LEU   A 1 53  ? 22.245 3.125   7.539   0.34 9.46  ?  53  LEU   A CG   1 
ATOM   1245 C CD1  A LEU   A 1 53  ? 22.673 2.005   6.738   0.66 12.66 ?  53  LEU   A CD1  1 
ATOM   1246 C CD1  B LEU   A 1 53  ? 23.085 2.010   6.931   0.34 10.19 ?  53  LEU   A CD1  1 
ATOM   1247 C CD2  A LEU   A 1 53  ? 21.457 2.899   8.728   0.66 13.38 ?  53  LEU   A CD2  1 
ATOM   1248 C CD2  B LEU   A 1 53  ? 21.909 2.799   8.980   0.34 9.96  ?  53  LEU   A CD2  1 
ATOM   1249 H H    A LEU   A 1 53  ? 21.238 5.691   5.942   0.66 13.05 ?  53  LEU   A H    1 
ATOM   1250 H H    B LEU   A 1 53  ? 21.221 5.636   6.200   0.34 11.71 ?  53  LEU   A H    1 
ATOM   1251 H HA   A LEU   A 1 53  ? 21.739 5.677   8.502   0.66 13.53 ?  53  LEU   A HA   1 
ATOM   1252 H HA   B LEU   A 1 53  ? 21.874 5.597   8.708   0.34 11.60 ?  53  LEU   A HA   1 
ATOM   1253 H HB2  A LEU   A 1 53  ? 23.231 4.517   6.413   0.66 15.21 ?  53  LEU   A HB2  1 
ATOM   1254 H HB2  B LEU   A 1 53  ? 23.236 4.554   6.487   0.34 11.52 ?  53  LEU   A HB2  1 
ATOM   1255 H HB3  A LEU   A 1 53  ? 23.578 4.277   7.938   0.66 15.21 ?  53  LEU   A HB3  1 
ATOM   1256 H HB3  B LEU   A 1 53  ? 23.801 4.365   7.946   0.34 11.52 ?  53  LEU   A HB3  1 
ATOM   1257 H HG   A LEU   A 1 53  ? 21.174 3.388   6.766   0.66 15.22 ?  53  LEU   A HG   1 
ATOM   1258 H HG   B LEU   A 1 53  ? 21.418 3.175   7.036   0.34 11.33 ?  53  LEU   A HG   1 
ATOM   1259 H HD11 A LEU   A 1 53  ? 22.077 1.240   6.759   0.66 15.16 ?  53  LEU   A HD11 1 
ATOM   1260 H HD11 B LEU   A 1 53  ? 22.602 1.171   7.013   0.34 12.20 ?  53  LEU   A HD11 1 
ATOM   1261 H HD12 A LEU   A 1 53  ? 22.929 2.201   5.824   0.66 15.16 ?  53  LEU   A HD12 1 
ATOM   1262 H HD12 B LEU   A 1 53  ? 23.245 2.209   5.996   0.34 12.20 ?  53  LEU   A HD12 1 
ATOM   1263 H HD13 A LEU   A 1 53  ? 23.463 1.824   7.272   0.66 15.16 ?  53  LEU   A HD13 1 
ATOM   1264 H HD13 B LEU   A 1 53  ? 23.927 1.954   7.408   0.34 12.20 ?  53  LEU   A HD13 1 
ATOM   1265 H HD21 A LEU   A 1 53  ? 20.932 2.084   8.705   0.66 16.03 ?  53  LEU   A HD21 1 
ATOM   1266 H HD21 B LEU   A 1 53  ? 21.435 1.952   9.011   0.34 11.92 ?  53  LEU   A HD21 1 
ATOM   1267 H HD22 A LEU   A 1 53  ? 22.223 2.783   9.311   0.66 16.03 ?  53  LEU   A HD22 1 
ATOM   1268 H HD22 B LEU   A 1 53  ? 22.729 2.739   9.490   0.34 11.92 ?  53  LEU   A HD22 1 
ATOM   1269 H HD23 A LEU   A 1 53  ? 20.910 3.635   9.043   0.66 16.03 ?  53  LEU   A HD23 1 
ATOM   1270 H HD23 B LEU   A 1 53  ? 21.345 3.503   9.337   0.34 11.92 ?  53  LEU   A HD23 1 
ATOM   1271 N N    A ASN   A 1 54  ? 23.813 7.403   6.781   0.66 10.00 ?  54  ASN   A N    1 
ATOM   1272 N N    B ASN   A 1 54  ? 23.863 7.385   6.943   0.34 10.82 ?  54  ASN   A N    1 
ATOM   1273 C CA   A ASN   A 1 54  ? 24.872 8.391   6.931   0.66 10.26 ?  54  ASN   A CA   1 
ATOM   1274 C CA   B ASN   A 1 54  ? 24.908 8.393   7.061   0.34 10.52 ?  54  ASN   A CA   1 
ATOM   1275 C C    A ASN   A 1 54  ? 24.374 9.623   7.687   0.66 10.57 ?  54  ASN   A C    1 
ATOM   1276 C C    B ASN   A 1 54  ? 24.384 9.668   7.712   0.34 10.69 ?  54  ASN   A C    1 
ATOM   1277 O O    A ASN   A 1 54  ? 25.069 10.149  8.567   0.66 11.60 ?  54  ASN   A O    1 
ATOM   1278 O O    B ASN   A 1 54  ? 25.079 10.284  8.531   0.34 10.94 ?  54  ASN   A O    1 
ATOM   1279 C CB   A ASN   A 1 54  ? 25.427 8.775   5.571   0.66 10.88 ?  54  ASN   A CB   1 
ATOM   1280 C CB   B ASN   A 1 54  ? 25.520 8.698   5.703   0.34 10.11 ?  54  ASN   A CB   1 
ATOM   1281 C CG   A ASN   A 1 54  ? 26.474 9.845   5.683   0.66 12.19 ?  54  ASN   A CG   1 
ATOM   1282 C CG   B ASN   A 1 54  ? 26.492 9.849   5.777   0.34 9.69  ?  54  ASN   A CG   1 
ATOM   1283 O OD1  A ASN   A 1 54  ? 27.481 9.666   6.378   0.66 13.03 ?  54  ASN   A OD1  1 
ATOM   1284 O OD1  B ASN   A 1 54  ? 27.509 9.768   6.469   0.34 9.02  ?  54  ASN   A OD1  1 
ATOM   1285 N ND2  A ASN   A 1 54  ? 26.243 10.974  5.029   0.66 12.99 ?  54  ASN   A ND2  1 
ATOM   1286 N ND2  B ASN   A 1 54  ? 26.178 10.938  5.092   0.34 10.39 ?  54  ASN   A ND2  1 
ATOM   1287 H H    A ASN   A 1 54  ? 23.575 7.233   5.976   0.66 11.97 ?  54  ASN   A H    1 
ATOM   1288 H H    B ASN   A 1 54  ? 23.640 7.185   6.137   0.34 12.96 ?  54  ASN   A H    1 
ATOM   1289 H HA   A ASN   A 1 54  ? 25.587 8.003   7.450   0.66 12.29 ?  54  ASN   A HA   1 
ATOM   1290 H HA   B ASN   A 1 54  ? 25.610 8.049   7.628   0.34 12.59 ?  54  ASN   A HA   1 
ATOM   1291 H HB2  A ASN   A 1 54  ? 25.834 7.996   5.164   0.66 13.03 ?  54  ASN   A HB2  1 
ATOM   1292 H HB2  B ASN   A 1 54  ? 26.001 7.913   5.387   0.34 12.11 ?  54  ASN   A HB2  1 
ATOM   1293 H HB3  A ASN   A 1 54  ? 24.708 9.111   5.013   0.66 13.03 ?  54  ASN   A HB3  1 
ATOM   1294 H HB3  B ASN   A 1 54  ? 24.820 8.933   5.075   0.34 12.11 ?  54  ASN   A HB3  1 
ATOM   1295 H HD21 A ASN   A 1 54  ? 26.810 11.620  5.070   0.66 15.56 ?  54  ASN   A HD21 1 
ATOM   1296 H HD21 B ASN   A 1 54  ? 26.702 11.622  5.109   0.34 12.44 ?  54  ASN   A HD21 1 
ATOM   1297 H HD22 A ASN   A 1 54  ? 25.529 11.059  4.560   0.66 15.56 ?  54  ASN   A HD22 1 
ATOM   1298 H HD22 B ASN   A 1 54  ? 25.456 10.962  4.630   0.34 12.44 ?  54  ASN   A HD22 1 
ATOM   1299 N N    . LYS   A 1 55  ? 23.168 10.095  7.357   1.00 10.97 ?  55  LYS   A N    1 
ATOM   1300 C CA   . LYS   A 1 55  ? 22.591 11.255  8.025   1.00 11.68 ?  55  LYS   A CA   1 
ATOM   1301 C C    . LYS   A 1 55  ? 22.494 11.026  9.530   1.00 11.46 ?  55  LYS   A C    1 
ATOM   1302 O O    . LYS   A 1 55  ? 22.777 11.927  10.332  1.00 12.56 ?  55  LYS   A O    1 
ATOM   1303 C CB   . LYS   A 1 55  ? 21.219 11.544  7.418   1.00 12.66 ?  55  LYS   A CB   1 
ATOM   1304 C CG   . LYS   A 1 55  ? 20.469 12.697  8.054   1.00 14.42 ?  55  LYS   A CG   1 
ATOM   1305 C CD   . LYS   A 1 55  ? 19.139 12.931  7.336   1.00 16.33 ?  55  LYS   A CD   1 
ATOM   1306 C CE   . LYS   A 1 55  ? 18.320 14.048  7.968   1.00 18.86 ?  55  LYS   A CE   1 
ATOM   1307 N NZ   . LYS   A 1 55  ? 16.979 14.191  7.319   1.00 20.54 ?  55  LYS   A NZ   1 
ATOM   1308 H H    A LYS   A 1 55  ? 22.656 9.750   6.757   0.66 13.14 ?  55  LYS   A H    1 
ATOM   1309 H H    B LYS   A 1 55  ? 22.662 9.730   6.762   0.34 13.14 ?  55  LYS   A H    1 
ATOM   1310 H HA   . LYS   A 1 55  ? 23.157 12.029  7.869   1.00 13.99 ?  55  LYS   A HA   1 
ATOM   1311 H HB2  . LYS   A 1 55  ? 21.331 11.757  6.478   1.00 15.16 ?  55  LYS   A HB2  1 
ATOM   1312 H HB3  . LYS   A 1 55  ? 20.665 10.753  7.509   1.00 15.16 ?  55  LYS   A HB3  1 
ATOM   1313 H HG2  . LYS   A 1 55  ? 20.276 12.491  8.983   1.00 17.28 ?  55  LYS   A HG2  1 
ATOM   1314 H HG3  . LYS   A 1 55  ? 20.996 13.507  7.987   1.00 17.28 ?  55  LYS   A HG3  1 
ATOM   1315 H HD2  . LYS   A 1 55  ? 19.316 13.169  6.412   1.00 19.57 ?  55  LYS   A HD2  1 
ATOM   1316 H HD3  . LYS   A 1 55  ? 18.613 12.114  7.371   1.00 19.57 ?  55  LYS   A HD3  1 
ATOM   1317 H HE2  . LYS   A 1 55  ? 18.183 13.851  8.907   1.00 22.61 ?  55  LYS   A HE2  1 
ATOM   1318 H HE3  . LYS   A 1 55  ? 18.796 14.887  7.867   1.00 22.61 ?  55  LYS   A HE3  1 
ATOM   1319 H HZ1  . LYS   A 1 55  ? 16.406 14.577  7.885   1.00 24.62 ?  55  LYS   A HZ1  1 
ATOM   1320 H HZ2  . LYS   A 1 55  ? 17.041 14.700  6.590   1.00 24.62 ?  55  LYS   A HZ2  1 
ATOM   1321 H HZ3  . LYS   A 1 55  ? 16.659 13.393  7.090   1.00 24.62 ?  55  LYS   A HZ3  1 
ATOM   1322 N N    . ALA   A 1 56  ? 22.106 9.816   9.933   1.00 12.43 ?  56  ALA   A N    1 
ATOM   1323 C CA   . ALA   A 1 56  ? 21.979 9.498   11.346  1.00 13.09 ?  56  ALA   A CA   1 
ATOM   1324 C C    . ALA   A 1 56  ? 23.321 9.523   12.069  1.00 12.04 ?  56  ALA   A C    1 
ATOM   1325 O O    . ALA   A 1 56  ? 23.339 9.717   13.285  1.00 13.44 ?  56  ALA   A O    1 
ATOM   1326 C CB   . ALA   A 1 56  ? 21.277 8.148   11.529  1.00 14.22 ?  56  ALA   A CB   1 
ATOM   1327 H H    . ALA   A 1 56  ? 21.916 9.174   9.405   1.00 14.88 ?  56  ALA   A H    1 
ATOM   1328 H HA   . ALA   A 1 56  ? 21.430 10.168  11.767  1.00 15.68 ?  56  ALA   A HA   1 
ATOM   1329 H HB1  . ALA   A 1 56  ? 21.208 7.953   12.479  1.00 17.04 ?  56  ALA   A HB1  1 
ATOM   1330 H HB2  . ALA   A 1 56  ? 20.391 8.204   11.139  1.00 17.04 ?  56  ALA   A HB2  1 
ATOM   1331 H HB3  . ALA   A 1 56  ? 21.793 7.457   11.087  1.00 17.04 ?  56  ALA   A HB3  1 
ATOM   1332 N N    . THR   A 1 57  ? 24.439 9.336   11.353  1.00 12.00 ?  57  THR   A N    1 
ATOM   1333 C CA   . THR   A 1 57  ? 25.780 9.467   11.930  1.00 12.00 ?  57  THR   A CA   1 
ATOM   1334 C C    . THR   A 1 57  ? 26.331 10.886  11.840  1.00 12.26 ?  57  THR   A C    1 
ATOM   1335 O O    . THR   A 1 57  ? 27.518 11.094  12.118  1.00 12.91 ?  57  THR   A O    1 
ATOM   1336 C CB   . THR   A 1 57  ? 26.792 8.511   11.267  1.00 11.68 ?  57  THR   A CB   1 
ATOM   1337 O OG1  . THR   A 1 57  ? 27.173 9.002   9.969   1.00 11.47 ?  57  THR   A OG1  1 
ATOM   1338 C CG2  . THR   A 1 57  ? 26.255 7.092   11.172  1.00 11.96 ?  57  THR   A CG2  1 
ATOM   1339 H H    . THR   A 1 57  ? 24.447 9.107   10.525  1.00 14.37 ?  57  THR   A H    1 
ATOM   1340 H HA   . THR   A 1 57  ? 25.738 9.222   12.871  1.00 14.38 ?  57  THR   A HA   1 
ATOM   1341 H HB   . THR   A 1 57  ? 27.590 8.476   11.825  1.00 13.98 ?  57  THR   A HB   1 
ATOM   1342 H HG1  . THR   A 1 57  ? 26.494 9.066   9.480   1.00 13.73 ?  57  THR   A HG1  1 
ATOM   1343 H HG21 . THR   A 1 57  ? 26.961 6.479   10.914  1.00 14.32 ?  57  THR   A HG21 1 
ATOM   1344 H HG22 . THR   A 1 57  ? 25.896 6.811   12.031  1.00 14.32 ?  57  THR   A HG22 1 
ATOM   1345 H HG23 . THR   A 1 57  ? 25.546 7.047   10.511  1.00 14.32 ?  57  THR   A HG23 1 
ATOM   1346 N N    . ASN   A 1 58  ? 25.516 11.860  11.438  1.00 12.73 ?  58  ASN   A N    1 
ATOM   1347 C CA   . ASN   A 1 58  ? 25.984 13.242  11.350  1.00 13.91 ?  58  ASN   A CA   1 
ATOM   1348 C C    . ASN   A 1 58  ? 27.127 13.372  10.335  1.00 12.50 ?  58  ASN   A C    1 
ATOM   1349 O O    . ASN   A 1 58  ? 28.014 14.214  10.478  1.00 13.52 ?  58  ASN   A O    1 
ATOM   1350 C CB   . ASN   A 1 58  ? 26.372 13.765  12.749  1.00 15.85 ?  58  ASN   A CB   1 
ATOM   1351 C CG   . ASN   A 1 58  ? 26.795 15.224  12.761  1.00 19.31 ?  58  ASN   A CG   1 
ATOM   1352 O OD1  . ASN   A 1 58  ? 26.150 16.066  12.151  1.00 20.94 ?  58  ASN   A OD1  1 
ATOM   1353 N ND2  . ASN   A 1 58  ? 27.872 15.531  13.497  1.00 19.98 ?  58  ASN   A ND2  1 
ATOM   1354 H H    . ASN   A 1 58  ? 24.694 11.741  11.206  1.00 15.25 ?  58  ASN   A H    1 
ATOM   1355 H HA   . ASN   A 1 58  ? 25.248 13.782  11.037  1.00 16.66 ?  58  ASN   A HA   1 
ATOM   1356 H HB2  . ASN   A 1 58  ? 25.602 13.674  13.347  1.00 18.99 ?  58  ASN   A HB2  1 
ATOM   1357 H HB3  . ASN   A 1 58  ? 27.108 13.242  13.099  1.00 18.99 ?  58  ASN   A HB3  1 
ATOM   1358 H HD21 . ASN   A 1 58  ? 28.149 16.347  13.541  1.00 23.94 ?  58  ASN   A HD21 1 
ATOM   1359 H HD22 . ASN   A 1 58  ? 28.292 14.914  13.921  1.00 23.94 ?  58  ASN   A HD22 1 
ATOM   1360 N N    . ASN   A 1 59  ? 27.103 12.553  9.283   1.00 11.52 ?  59  ASN   A N    1 
ATOM   1361 C CA   . ASN   A 1 59  ? 28.084 12.518  8.188   1.00 11.24 ?  59  ASN   A CA   1 
ATOM   1362 C C    . ASN   A 1 59  ? 29.398 11.828  8.573   1.00 11.06 ?  59  ASN   A C    1 
ATOM   1363 O O    . ASN   A 1 59  ? 30.319 11.789  7.746   1.00 11.44 ?  59  ASN   A O    1 
ATOM   1364 C CB   . ASN   A 1 59  ? 28.375 13.904  7.574   1.00 11.35 ?  59  ASN   A CB   1 
ATOM   1365 C CG   . ASN   A 1 59  ? 28.729 13.831  6.104   1.00 11.71 ?  59  ASN   A CG   1 
ATOM   1366 O OD1  . ASN   A 1 59  ? 28.027 13.199  5.315   1.00 12.02 ?  59  ASN   A OD1  1 
ATOM   1367 N ND2  . ASN   A 1 59  ? 29.826 14.486  5.722   1.00 12.83 ?  59  ASN   A ND2  1 
ATOM   1368 H H    . ASN   A 1 59  ? 26.484 11.964  9.170   1.00 13.79 ?  59  ASN   A H    1 
ATOM   1369 H HA   . ASN   A 1 59  ? 27.704 11.991  7.480   1.00 13.46 ?  59  ASN   A HA   1 
ATOM   1370 H HB2  . ASN   A 1 59  ? 27.592 14.465  7.654   1.00 13.59 ?  59  ASN   A HB2  1 
ATOM   1371 H HB3  . ASN   A 1 59  ? 29.127 14.313  8.035   1.00 13.59 ?  59  ASN   A HB3  1 
ATOM   1372 H HD21 . ASN   A 1 59  ? 30.071 14.481  4.894   1.00 15.36 ?  59  ASN   A HD21 1 
ATOM   1373 H HD22 . ASN   A 1 59  ? 30.294 14.925  6.298   1.00 15.36 ?  59  ASN   A HD22 1 
ATOM   1374 N N    . ALA   A 1 60  ? 29.525 11.287  9.784   1.00 11.37 ?  60  ALA   A N    1 
ATOM   1375 C CA   . ALA   A 1 60  ? 30.770 10.624  10.145  1.00 11.41 ?  60  ALA   A CA   1 
ATOM   1376 C C    . ALA   A 1 60  ? 31.001 9.379   9.295   1.00 11.50 ?  60  ALA   A C    1 
ATOM   1377 O O    . ALA   A 1 60  ? 32.146 9.053   8.964   1.00 12.13 ?  60  ALA   A O    1 
ATOM   1378 C CB   . ALA   A 1 60  ? 30.768 10.272  11.628  1.00 11.70 ?  60  ALA   A CB   1 
ATOM   1379 H H    . ALA   A 1 60  ? 28.921 11.283  10.395  1.00 13.61 ?  60  ALA   A H    1 
ATOM   1380 H HA   . ALA   A 1 60  ? 31.511 11.236  9.988   1.00 13.66 ?  60  ALA   A HA   1 
ATOM   1381 H HB1  . ALA   A 1 60  ? 31.599 9.836   11.855  1.00 14.01 ?  60  ALA   A HB1  1 
ATOM   1382 H HB2  . ALA   A 1 60  ? 30.669 11.091  12.145  1.00 14.01 ?  60  ALA   A HB2  1 
ATOM   1383 H HB3  . ALA   A 1 60  ? 30.018 9.681   11.808  1.00 14.01 ?  60  ALA   A HB3  1 
ATOM   1384 N N    . MET   A 1 61  ? 29.933 8.674   8.919   1.00 11.04 ?  61  MET   A N    1 
ATOM   1385 C CA   . MET   A 1 61  ? 30.075 7.532   8.021   1.00 10.61 ?  61  MET   A CA   1 
ATOM   1386 C C    . MET   A 1 61  ? 30.703 7.953   6.693   1.00 10.76 ?  61  MET   A C    1 
ATOM   1387 O O    . MET   A 1 61  ? 31.592 7.273   6.174   1.00 11.13 ?  61  MET   A O    1 
ATOM   1388 C CB   . MET   A 1 61  ? 28.707 6.879   7.810   1.00 10.75 ?  61  MET   A CB   1 
ATOM   1389 C CG   . MET   A 1 61  ? 28.713 5.707   6.842   1.00 11.59 ?  61  MET   A CG   1 
ATOM   1390 S SD   . MET   A 1 61  ? 27.083 4.959   6.626   1.00 12.21 ?  61  MET   A SD   1 
ATOM   1391 C CE   . MET   A 1 61  ? 26.927 4.100   8.194   1.00 14.00 ?  61  MET   A CE   1 
ATOM   1392 H H    . MET   A 1 61  ? 29.131 8.838   9.164   1.00 13.22 ?  61  MET   A H    1 
ATOM   1393 H HA   . MET   A 1 61  ? 30.649 6.874   8.440   1.00 12.70 ?  61  MET   A HA   1 
ATOM   1394 H HB2  . MET   A 1 61  ? 28.379 6.554   8.661   1.00 12.87 ?  61  MET   A HB2  1 
ATOM   1395 H HB3  . MET   A 1 61  ? 28.093 7.544   7.456   1.00 12.87 ?  61  MET   A HB3  1 
ATOM   1396 H HG2  . MET   A 1 61  ? 29.006 6.009   5.969   1.00 13.88 ?  61  MET   A HG2  1 
ATOM   1397 H HG3  . MET   A 1 61  ? 29.312 5.022   7.175   1.00 13.88 ?  61  MET   A HG3  1 
ATOM   1398 H HE1  . MET   A 1 61  ? 26.083 3.621   8.208   1.00 16.77 ?  61  MET   A HE1  1 
ATOM   1399 H HE2  . MET   A 1 61  ? 27.664 3.485   8.297   1.00 16.77 ?  61  MET   A HE2  1 
ATOM   1400 H HE3  . MET   A 1 61  ? 26.940 4.757   8.916   1.00 16.77 ?  61  MET   A HE3  1 
ATOM   1401 N N    . GLN   A 1 62  ? 30.260 9.079   6.132   1.00 10.88 ?  62  GLN   A N    1 
ATOM   1402 C CA   . GLN   A 1 62  ? 30.821 9.547   4.869   1.00 11.04 ?  62  GLN   A CA   1 
ATOM   1403 C C    . GLN   A 1 62  ? 32.292 9.928   5.012   1.00 10.77 ?  62  GLN   A C    1 
ATOM   1404 O O    . GLN   A 1 62  ? 33.099 9.610   4.132   1.00 11.70 ?  62  GLN   A O    1 
ATOM   1405 C CB   . GLN   A 1 62  ? 30.017 10.728  4.333   1.00 11.39 ?  62  GLN   A CB   1 
ATOM   1406 C CG   . GLN   A 1 62  ? 30.390 11.089  2.905   1.00 11.51 ?  62  GLN   A CG   1 
ATOM   1407 C CD   . GLN   A 1 62  ? 30.068 9.960   1.955   1.00 11.49 ?  62  GLN   A CD   1 
ATOM   1408 O OE1  . GLN   A 1 62  ? 28.892 9.646   1.740   1.00 11.78 ?  62  GLN   A OE1  1 
ATOM   1409 N NE2  . GLN   A 1 62  ? 31.098 9.282   1.441   1.00 11.80 ?  62  GLN   A NE2  1 
ATOM   1410 H H    . GLN   A 1 62  ? 29.644 9.577   6.460   1.00 13.03 ?  62  GLN   A H    1 
ATOM   1411 H HA   . GLN   A 1 62  ? 30.769 8.829   4.225   1.00 13.22 ?  62  GLN   A HA   1 
ATOM   1412 H HB2  . GLN   A 1 62  ? 29.076 10.508  4.356   1.00 13.64 ?  62  GLN   A HB2  1 
ATOM   1413 H HB3  . GLN   A 1 62  ? 30.191 11.508  4.888   1.00 13.64 ?  62  GLN   A HB3  1 
ATOM   1414 H HG2  . GLN   A 1 62  ? 29.875 11.860  2.625   1.00 13.79 ?  62  GLN   A HG2  1 
ATOM   1415 H HG3  . GLN   A 1 62  ? 31.336 11.270  2.849   1.00 13.79 ?  62  GLN   A HG3  1 
ATOM   1416 H HE21 . GLN   A 1 62  ? 31.904 9.520   1.629   1.00 14.13 ?  62  GLN   A HE21 1 
ATOM   1417 H HE22 . GLN   A 1 62  ? 30.962 8.622   0.905   1.00 14.13 ?  62  GLN   A HE22 1 
ATOM   1418 N N    . VAL   A 1 63  ? 32.655 10.615  6.098   1.00 11.38 ?  63  VAL   A N    1 
ATOM   1419 C CA   . VAL   A 1 63  ? 34.049 11.011  6.301   1.00 12.24 ?  63  VAL   A CA   1 
ATOM   1420 C C    . VAL   A 1 63  ? 34.945 9.775   6.378   1.00 11.86 ?  63  VAL   A C    1 
ATOM   1421 O O    . VAL   A 1 63  ? 35.994 9.693   5.722   1.00 12.45 ?  63  VAL   A O    1 
ATOM   1422 C CB   . VAL   A 1 63  ? 34.164 11.898  7.554   1.00 14.60 ?  63  VAL   A CB   1 
ATOM   1423 C CG1  . VAL   A 1 63  ? 35.610 12.141  7.908   1.00 16.56 ?  63  VAL   A CG1  1 
ATOM   1424 C CG2  . VAL   A 1 63  ? 33.448 13.228  7.323   1.00 14.61 ?  63  VAL   A CG2  1 
ATOM   1425 H H    . VAL   A 1 63  ? 32.118 10.864  6.725   1.00 13.62 ?  63  VAL   A H    1 
ATOM   1426 H HA   . VAL   A 1 63  ? 34.339 11.540  5.544   1.00 14.66 ?  63  VAL   A HA   1 
ATOM   1427 H HB   . VAL   A 1 63  ? 33.740 11.456  8.306   1.00 17.49 ?  63  VAL   A HB   1 
ATOM   1428 H HG11 . VAL   A 1 63  ? 35.662 12.890  8.523   1.00 19.84 ?  63  VAL   A HG11 1 
ATOM   1429 H HG12 . VAL   A 1 63  ? 35.971 11.345  8.328   1.00 19.84 ?  63  VAL   A HG12 1 
ATOM   1430 H HG13 . VAL   A 1 63  ? 36.102 12.344  7.099   1.00 19.84 ?  63  VAL   A HG13 1 
ATOM   1431 H HG21 . VAL   A 1 63  ? 33.536 13.782  8.117   1.00 17.50 ?  63  VAL   A HG21 1 
ATOM   1432 H HG22 . VAL   A 1 63  ? 33.851 13.678  6.563   1.00 17.50 ?  63  VAL   A HG22 1 
ATOM   1433 H HG23 . VAL   A 1 63  ? 32.510 13.056  7.145   1.00 17.50 ?  63  VAL   A HG23 1 
ATOM   1434 N N    . GLU   A 1 64  ? 34.522 8.776   7.158   1.00 11.95 ?  64  GLU   A N    1 
ATOM   1435 C CA   . GLU   A 1 64  ? 35.284 7.536   7.260   1.00 11.54 ?  64  GLU   A CA   1 
ATOM   1436 C C    . GLU   A 1 64  ? 35.372 6.845   5.908   1.00 11.12 ?  64  GLU   A C    1 
ATOM   1437 O O    . GLU   A 1 64  ? 36.424 6.298   5.535   1.00 11.80 ?  64  GLU   A O    1 
ATOM   1438 C CB   . GLU   A 1 64  ? 34.600 6.629   8.283   1.00 12.33 ?  64  GLU   A CB   1 
ATOM   1439 C CG   . GLU   A 1 64  ? 35.248 5.281   8.438   1.00 12.79 ?  64  GLU   A CG   1 
ATOM   1440 C CD   . GLU   A 1 64  ? 34.367 4.289   9.172   1.00 13.90 ?  64  GLU   A CD   1 
ATOM   1441 O OE1  . GLU   A 1 64  ? 33.130 4.376   9.035   1.00 14.25 ?  64  GLU   A OE1  1 
ATOM   1442 O OE2  . GLU   A 1 64  ? 34.920 3.402   9.865   1.00 14.02 -1 64  GLU   A OE2  1 
ATOM   1443 H H    . GLU   A 1 64  ? 33.794 8.793   7.625   1.00 14.31 ?  64  GLU   A H    1 
ATOM   1444 H HA   . GLU   A 1 64  ? 36.180 7.741   7.575   1.00 13.83 ?  64  GLU   A HA   1 
ATOM   1445 H HB2  . GLU   A 1 64  ? 34.625 7.070   9.154   1.00 14.77 ?  64  GLU   A HB2  1 
ATOM   1446 H HB3  . GLU   A 1 64  ? 33.680 6.500   8.014   1.00 14.77 ?  64  GLU   A HB3  1 
ATOM   1447 H HG2  . GLU   A 1 64  ? 35.442 4.910   7.559   1.00 15.32 ?  64  GLU   A HG2  1 
ATOM   1448 H HG3  . GLU   A 1 64  ? 36.067 5.378   8.941   1.00 15.32 ?  64  GLU   A HG3  1 
ATOM   1449 N N    . SER   A 1 65  ? 34.252 6.826   5.177   1.00 10.99 ?  65  SER   A N    1 
ATOM   1450 C CA   . SER   A 1 65  ? 34.200 6.162   3.880   1.00 10.72 ?  65  SER   A CA   1 
ATOM   1451 C C    . SER   A 1 65  ? 35.126 6.821   2.863   1.00 11.17 ?  65  SER   A C    1 
ATOM   1452 O O    . SER   A 1 65  ? 35.775 6.132   2.069   1.00 12.04 ?  65  SER   A O    1 
ATOM   1453 C CB   . SER   A 1 65  ? 32.763 6.176   3.356   1.00 10.99 ?  65  SER   A CB   1 
ATOM   1454 O OG   . SER   A 1 65  ? 31.905 5.350   4.145   1.00 11.52 ?  65  SER   A OG   1 
ATOM   1455 H H    . SER   A 1 65  ? 33.511 7.197   5.416   1.00 13.16 ?  65  SER   A H    1 
ATOM   1456 H HA   . SER   A 1 65  ? 34.474 5.240   3.986   1.00 12.84 ?  65  SER   A HA   1 
ATOM   1457 H HB2  . SER   A 1 65  ? 32.431 7.088   3.373   1.00 13.16 ?  65  SER   A HB2  1 
ATOM   1458 H HB3  . SER   A 1 65  ? 32.762 5.844   2.444   1.00 13.16 ?  65  SER   A HB3  1 
ATOM   1459 H HG   . SER   A 1 65  ? 31.899 5.635   4.943   1.00 13.80 ?  65  SER   A HG   1 
ATOM   1460 N N    . ASP   A 1 66  ? 35.195 8.156   2.859   1.00 11.37 ?  66  ASP   A N    1 
ATOM   1461 C CA   . ASP   A 1 66  ? 36.069 8.844   1.913   1.00 12.01 ?  66  ASP   A CA   1 
ATOM   1462 C C    . ASP   A 1 66  ? 37.531 8.497   2.166   1.00 12.14 ?  66  ASP   A C    1 
ATOM   1463 O O    . ASP   A 1 66  ? 38.304 8.312   1.220   1.00 13.23 ?  66  ASP   A O    1 
ATOM   1464 C CB   . ASP   A 1 66  ? 35.857 10.353  1.987   1.00 13.89 ?  66  ASP   A CB   1 
ATOM   1465 C CG   . ASP   A 1 66  ? 34.525 10.804  1.389   1.00 15.35 ?  66  ASP   A CG   1 
ATOM   1466 O OD1  . ASP   A 1 66  ? 33.818 9.999   0.743   1.00 15.84 ?  66  ASP   A OD1  1 
ATOM   1467 O OD2  . ASP   A 1 66  ? 34.208 11.997  1.549   1.00 18.03 -1 66  ASP   A OD2  1 
ATOM   1468 H H    . ASP   A 1 66  ? 34.744 8.677   3.376   1.00 13.62 ?  66  ASP   A H    1 
ATOM   1469 H HA   . ASP   A 1 66  ? 35.844 8.554   1.013   1.00 14.39 ?  66  ASP   A HA   1 
ATOM   1470 H HB2  . ASP   A 1 66  ? 35.870 10.625  2.917   1.00 16.64 ?  66  ASP   A HB2  1 
ATOM   1471 H HB3  . ASP   A 1 66  ? 36.570 10.794  1.501   1.00 16.64 ?  66  ASP   A HB3  1 
ATOM   1472 N N    . ASP   A 1 67  ? 37.923 8.381   3.438   1.00 12.39 ?  67  ASP   A N    1 
ATOM   1473 C CA   . ASP   A 1 67  ? 39.274 7.930   3.748   1.00 13.71 ?  67  ASP   A CA   1 
ATOM   1474 C C    . ASP   A 1 67  ? 39.498 6.492   3.281   1.00 13.34 ?  67  ASP   A C    1 
ATOM   1475 O O    . ASP   A 1 67  ? 40.559 6.167   2.734   1.00 13.76 ?  67  ASP   A O    1 
ATOM   1476 C CB   . ASP   A 1 67  ? 39.535 8.070   5.246   1.00 14.68 ?  67  ASP   A CB   1 
ATOM   1477 C CG   . ASP   A 1 67  ? 40.835 7.419   5.674   1.00 16.28 ?  67  ASP   A CG   1 
ATOM   1478 O OD1  . ASP   A 1 67  ? 41.905 8.066   5.550   1.00 19.36 ?  67  ASP   A OD1  1 
ATOM   1479 O OD2  . ASP   A 1 67  ? 40.785 6.257   6.135   1.00 16.01 -1 67  ASP   A OD2  1 
ATOM   1480 H H    . ASP   A 1 67  ? 37.439 8.563   4.122   1.00 14.84 ?  67  ASP   A H    1 
ATOM   1481 H HA   . ASP   A 1 67  ? 39.912 8.495   3.282   1.00 16.43 ?  67  ASP   A HA   1 
ATOM   1482 H HB2  . ASP   A 1 67  ? 39.583 9.010   5.468   1.00 17.59 ?  67  ASP   A HB2  1 
ATOM   1483 H HB3  . ASP   A 1 67  ? 38.808 7.647   5.731   1.00 17.59 ?  67  ASP   A HB3  1 
ATOM   1484 N N    . TYR   A 1 68  ? 38.510 5.612   3.477   1.00 13.12 ?  68  TYR   A N    1 
ATOM   1485 C CA   . TYR   A 1 68  ? 38.637 4.229   3.011   1.00 13.30 ?  68  TYR   A CA   1 
ATOM   1486 C C    . TYR   A 1 68  ? 38.881 4.173   1.503   1.00 12.74 ?  68  TYR   A C    1 
ATOM   1487 O O    . TYR   A 1 68  ? 39.765 3.442   1.031   1.00 13.60 ?  68  TYR   A O    1 
ATOM   1488 C CB   . TYR   A 1 68  ? 37.392 3.406   3.385   1.00 13.61 ?  68  TYR   A CB   1 
ATOM   1489 C CG   . TYR   A 1 68  ? 37.428 2.013   2.766   1.00 15.10 ?  68  TYR   A CG   1 
ATOM   1490 C CD1  . TYR   A 1 68  ? 36.966 1.804   1.469   1.00 16.83 ?  68  TYR   A CD1  1 
ATOM   1491 C CD2  . TYR   A 1 68  ? 37.968 0.936   3.445   1.00 17.11 ?  68  TYR   A CD2  1 
ATOM   1492 C CE1  . TYR   A 1 68  ? 37.034 0.582   0.868   1.00 18.28 ?  68  TYR   A CE1  1 
ATOM   1493 C CE2  . TYR   A 1 68  ? 38.033 -0.326  2.842   1.00 18.00 ?  68  TYR   A CE2  1 
ATOM   1494 C CZ   . TYR   A 1 68  ? 37.566 -0.477  1.558   1.00 18.76 ?  68  TYR   A CZ   1 
ATOM   1495 O OH   . TYR   A 1 68  ? 37.645 -1.692  0.934   1.00 21.00 ?  68  TYR   A OH   1 
ATOM   1496 H H    . TYR   A 1 68  ? 37.763 5.790   3.869   1.00 15.72 ?  68  TYR   A H    1 
ATOM   1497 H HA   . TYR   A 1 68  ? 39.399 3.824   3.448   1.00 15.93 ?  68  TYR   A HA   1 
ATOM   1498 H HB2  . TYR   A 1 68  ? 37.349 3.306   4.346   1.00 16.30 ?  68  TYR   A HB2  1 
ATOM   1499 H HB3  . TYR   A 1 68  ? 36.597 3.861   3.058   1.00 16.30 ?  68  TYR   A HB3  1 
ATOM   1500 H HD1  . TYR   A 1 68  ? 36.611 2.523   0.993   1.00 20.17 ?  68  TYR   A HD1  1 
ATOM   1501 H HD2  . TYR   A 1 68  ? 38.302 1.046   4.301   1.00 20.50 ?  68  TYR   A HD2  1 
ATOM   1502 H HE1  . TYR   A 1 68  ? 36.715 0.466   -0.000  1.00 21.91 ?  68  TYR   A HE1  1 
ATOM   1503 H HE2  . TYR   A 1 68  ? 38.406 -1.055  3.286   1.00 21.57 ?  68  TYR   A HE2  1 
ATOM   1504 H HH   . TYR   A 1 68  ? 37.982 -2.264  1.445   1.00 25.17 ?  68  TYR   A HH   1 
ATOM   1505 N N    . ILE   A 1 69  ? 38.096 4.930   0.729   1.00 12.22 ?  69  ILE   A N    1 
ATOM   1506 C CA   . ILE   A 1 69  ? 38.229 4.913   -0.726  1.00 12.44 ?  69  ILE   A CA   1 
ATOM   1507 C C    . ILE   A 1 69  ? 39.554 5.532   -1.163  1.00 12.46 ?  69  ILE   A C    1 
ATOM   1508 O O    . ILE   A 1 69  ? 40.192 5.051   -2.104  1.00 12.56 ?  69  ILE   A O    1 
ATOM   1509 C CB   . ILE   A 1 69  ? 37.024 5.614   -1.388  1.00 13.21 ?  69  ILE   A CB   1 
ATOM   1510 C CG1  . ILE   A 1 69  ? 35.716 4.871   -1.098  1.00 13.52 ?  69  ILE   A CG1  1 
ATOM   1511 C CG2  . ILE   A 1 69  ? 37.265 5.780   -2.892  1.00 14.60 ?  69  ILE   A CG2  1 
ATOM   1512 C CD1  . ILE   A 1 69  ? 35.549 3.589   -1.872  1.00 14.44 ?  69  ILE   A CD1  1 
ATOM   1513 H H    . ILE   A 1 69  ? 37.484 5.463   1.021   1.00 14.64 ?  69  ILE   A H    1 
ATOM   1514 H HA   . ILE   A 1 69  ? 38.230 3.991   -1.023  1.00 14.90 ?  69  ILE   A HA   1 
ATOM   1515 H HB   . ILE   A 1 69  ? 36.952 6.497   -1.008  1.00 15.82 ?  69  ILE   A HB   1 
ATOM   1516 H HG12 . ILE   A 1 69  ? 35.689 4.652   -0.151  1.00 16.20 ?  69  ILE   A HG12 1 
ATOM   1517 H HG13 . ILE   A 1 69  ? 34.974 5.455   -1.317  1.00 16.20 ?  69  ILE   A HG13 1 
ATOM   1518 H HG21 . ILE   A 1 69  ? 36.416 5.965   -3.329  1.00 17.49 ?  69  ILE   A HG21 1 
ATOM   1519 H HG22 . ILE   A 1 69  ? 37.873 6.525   -3.038  1.00 17.49 ?  69  ILE   A HG22 1 
ATOM   1520 H HG23 . ILE   A 1 69  ? 37.646 4.965   -3.249  1.00 17.49 ?  69  ILE   A HG23 1 
ATOM   1521 H HD11 . ILE   A 1 69  ? 34.770 3.122   -1.533  1.00 17.30 ?  69  ILE   A HD11 1 
ATOM   1522 H HD12 . ILE   A 1 69  ? 35.420 3.805   -2.810  1.00 17.30 ?  69  ILE   A HD12 1 
ATOM   1523 H HD13 . ILE   A 1 69  ? 36.339 3.045   -1.760  1.00 17.30 ?  69  ILE   A HD13 1 
ATOM   1524 N N    . ALA   A 1 70  ? 39.971 6.614   -0.508  1.00 13.06 ?  70  ALA   A N    1 
ATOM   1525 C CA   . ALA   A 1 70  ? 41.253 7.227   -0.846  1.00 13.68 ?  70  ALA   A CA   1 
ATOM   1526 C C    . ALA   A 1 70  ? 42.410 6.248   -0.667  1.00 14.02 ?  70  ALA   A C    1 
ATOM   1527 O O    . ALA   A 1 70  ? 43.396 6.306   -1.407  1.00 15.90 ?  70  ALA   A O    1 
ATOM   1528 C CB   . ALA   A 1 70  ? 41.472 8.473   0.012   1.00 14.94 ?  70  ALA   A CB   1 
ATOM   1529 H H    . ALA   A 1 70  ? 39.535 7.008   0.120   1.00 15.65 ?  70  ALA   A H    1 
ATOM   1530 H HA   . ALA   A 1 70  ? 41.230 7.511   -1.777  1.00 16.39 ?  70  ALA   A HA   1 
ATOM   1531 H HB1  . ALA   A 1 70  ? 42.331 8.867   -0.223  1.00 17.90 ?  70  ALA   A HB1  1 
ATOM   1532 H HB2  . ALA   A 1 70  ? 40.762 9.106   -0.152  1.00 17.90 ?  70  ALA   A HB2  1 
ATOM   1533 H HB3  . ALA   A 1 70  ? 41.480 8.211   0.947   1.00 17.90 ?  70  ALA   A HB3  1 
ATOM   1534 N N    . THR   A 1 71  ? 42.304 5.339   0.295   1.00 14.00 ?  71  THR   A N    1 
ATOM   1535 C CA   . THR   A 1 71  ? 43.354 4.361   0.551   1.00 15.75 ?  71  THR   A CA   1 
ATOM   1536 C C    . THR   A 1 71  ? 43.237 3.129   -0.334  1.00 16.05 ?  71  THR   A C    1 
ATOM   1537 O O    . THR   A 1 71  ? 44.251 2.605   -0.813  1.00 18.05 ?  71  THR   A O    1 
ATOM   1538 C CB   . THR   A 1 71  ? 43.275 3.923   2.010   1.00 17.80 ?  71  THR   A CB   1 
ATOM   1539 O OG1  . THR   A 1 71  ? 43.530 5.055   2.850   1.00 19.98 ?  71  THR   A OG1  1 
ATOM   1540 C CG2  . THR   A 1 71  ? 44.278 2.817   2.310   1.00 19.69 ?  71  THR   A CG2  1 
ATOM   1541 H H    . THR   A 1 71  ? 41.615 5.253   0.802   1.00 16.77 ?  71  THR   A H    1 
ATOM   1542 H HA   . THR   A 1 71  ? 44.216 4.769   0.391   1.00 18.87 ?  71  THR   A HA   1 
ATOM   1543 H HB   . THR   A 1 71  ? 42.381 3.575   2.186   1.00 21.33 ?  71  THR   A HB   1 
ATOM   1544 H HG1  . THR   A 1 71  ? 42.945 5.642   2.712   1.00 23.95 ?  71  THR   A HG1  1 
ATOM   1545 H HG21 . THR   A 1 71  ? 44.410 2.747   3.267   1.00 23.59 ?  71  THR   A HG21 1 
ATOM   1546 H HG22 . THR   A 1 71  ? 43.955 1.966   1.974   1.00 23.59 ?  71  THR   A HG22 1 
ATOM   1547 H HG23 . THR   A 1 71  ? 45.128 3.021   1.890   1.00 23.59 ?  71  THR   A HG23 1 
ATOM   1548 N N    . ASN   A 1 72  ? 42.018 2.634   -0.546  1.00 14.95 ?  72  ASN   A N    1 
ATOM   1549 C CA   . ASN   A 1 72  ? 41.802 1.308   -1.112  1.00 15.32 ?  72  ASN   A CA   1 
ATOM   1550 C C    . ASN   A 1 72  ? 41.184 1.300   -2.500  1.00 15.33 ?  72  ASN   A C    1 
ATOM   1551 O O    . ASN   A 1 72  ? 41.188 0.244   -3.150  1.00 16.25 ?  72  ASN   A O    1 
ATOM   1552 C CB   . ASN   A 1 72  ? 40.911 0.484   -0.175  1.00 16.24 ?  72  ASN   A CB   1 
ATOM   1553 C CG   . ASN   A 1 72  ? 41.521 0.320   1.191   1.00 17.17 ?  72  ASN   A CG   1 
ATOM   1554 O OD1  . ASN   A 1 72  ? 41.069 0.913   2.168   1.00 18.66 ?  72  ASN   A OD1  1 
ATOM   1555 N ND2  . ASN   A 1 72  ? 42.571 -0.470  1.265   1.00 17.35 ?  72  ASN   A ND2  1 
ATOM   1556 H H    . ASN   A 1 72  ? 41.285 3.052   -0.363  1.00 17.91 ?  72  ASN   A H    1 
ATOM   1557 H HA   . ASN   A 1 72  ? 42.656 0.860   -1.178  1.00 18.35 ?  72  ASN   A HA   1 
ATOM   1558 H HB2  . ASN   A 1 72  ? 40.057 0.928   -0.075  1.00 19.45 ?  72  ASN   A HB2  1 
ATOM   1559 H HB3  . ASN   A 1 72  ? 40.787 -0.401  -0.554  1.00 19.45 ?  72  ASN   A HB3  1 
ATOM   1560 H HD21 . ASN   A 1 72  ? 42.963 -0.593  2.022   1.00 20.79 ?  72  ASN   A HD21 1 
ATOM   1561 H HD22 . ASN   A 1 72  ? 42.860 -0.870  0.562   1.00 20.79 ?  72  ASN   A HD22 1 
ATOM   1562 N N    . GLY   A 1 73  ? 40.637 2.414   -2.965  1.00 14.30 ?  73  GLY   A N    1 
ATOM   1563 C CA   . GLY   A 1 73  ? 39.905 2.413   -4.205  1.00 13.69 ?  73  GLY   A CA   1 
ATOM   1564 C C    . GLY   A 1 73  ? 38.515 1.833   -4.023  1.00 12.99 ?  73  GLY   A C    1 
ATOM   1565 O O    . GLY   A 1 73  ? 38.132 1.391   -2.935  1.00 13.92 ?  73  GLY   A O    1 
ATOM   1566 H H    . GLY   A 1 73  ? 40.683 3.190   -2.585  1.00 17.13 ?  73  GLY   A H    1 
ATOM   1567 H HA2  . GLY   A 1 73  ? 39.826 3.328   -4.534  1.00 16.39 ?  73  GLY   A HA2  1 
ATOM   1568 H HA3  . GLY   A 1 73  ? 40.377 1.888   -4.867  1.00 16.39 ?  73  GLY   A HA3  1 
ATOM   1569 N N    . PRO   A 1 74  ? 37.735 1.836   -5.099  1.00 13.85 ?  74  PRO   A N    1 
ATOM   1570 C CA   . PRO   A 1 74  ? 36.333 1.416   -5.008  1.00 13.75 ?  74  PRO   A CA   1 
ATOM   1571 C C    . PRO   A 1 74  ? 36.182 -0.066  -4.684  1.00 13.22 ?  74  PRO   A C    1 
ATOM   1572 O O    . PRO   A 1 74  ? 37.053 -0.899  -4.959  1.00 14.04 ?  74  PRO   A O    1 
ATOM   1573 C CB   . PRO   A 1 74  ? 35.786 1.708   -6.410  1.00 15.68 ?  74  PRO   A CB   1 
ATOM   1574 C CG   . PRO   A 1 74  ? 36.743 2.677   -7.022  1.00 19.03 ?  74  PRO   A CG   1 
ATOM   1575 C CD   . PRO   A 1 74  ? 38.077 2.341   -6.436  1.00 15.84 ?  74  PRO   A CD   1 
ATOM   1576 H HA   . PRO   A 1 74  ? 35.855 1.948   -4.348  1.00 16.47 ?  74  PRO   A HA   1 
ATOM   1577 H HB2  . PRO   A 1 74  ? 35.756 0.881   -6.919  1.00 18.79 ?  74  PRO   A HB2  1 
ATOM   1578 H HB3  . PRO   A 1 74  ? 34.900 2.095   -6.336  1.00 18.79 ?  74  PRO   A HB3  1 
ATOM   1579 H HG2  . PRO   A 1 74  ? 36.759 2.565   -7.985  1.00 22.81 ?  74  PRO   A HG2  1 
ATOM   1580 H HG3  . PRO   A 1 74  ? 36.491 3.584   -6.787  1.00 22.81 ?  74  PRO   A HG3  1 
ATOM   1581 H HD2  . PRO   A 1 74  ? 38.518 1.646   -6.955  1.00 18.97 ?  74  PRO   A HD2  1 
ATOM   1582 H HD3  . PRO   A 1 74  ? 38.632 3.139   -6.381  1.00 18.97 ?  74  PRO   A HD3  1 
ATOM   1583 N N    . LEU   A 1 75  ? 35.027 -0.392  -4.108  1.00 12.52 ?  75  LEU   A N    1 
ATOM   1584 C CA   . LEU   A 1 75  ? 34.642 -1.786  -3.949  1.00 11.96 ?  75  LEU   A CA   1 
ATOM   1585 C C    . LEU   A 1 75  ? 34.260 -2.368  -5.307  1.00 12.45 ?  75  LEU   A C    1 
ATOM   1586 O O    . LEU   A 1 75  ? 34.128 -1.655  -6.305  1.00 13.67 ?  75  LEU   A O    1 
ATOM   1587 C CB   . LEU   A 1 75  ? 33.451 -1.910  -2.996  1.00 11.86 ?  75  LEU   A CB   1 
ATOM   1588 C CG   . LEU   A 1 75  ? 33.665 -1.506  -1.544  1.00 13.81 ?  75  LEU   A CG   1 
ATOM   1589 C CD1  . LEU   A 1 75  ? 32.398 -1.741  -0.742  1.00 16.04 ?  75  LEU   A CD1  1 
ATOM   1590 C CD2  . LEU   A 1 75  ? 34.817 -2.237  -0.926  1.00 17.20 ?  75  LEU   A CD2  1 
ATOM   1591 H H    . LEU   A 1 75  ? 34.449 0.175   -3.814  1.00 14.99 ?  75  LEU   A H    1 
ATOM   1592 H HA   . LEU   A 1 75  ? 35.388 -2.287  -3.599  1.00 14.32 ?  75  LEU   A HA   1 
ATOM   1593 H HB2  . LEU   A 1 75  ? 32.731 -1.366  -3.341  1.00 14.20 ?  75  LEU   A HB2  1 
ATOM   1594 H HB3  . LEU   A 1 75  ? 33.175 -2.842  -2.992  1.00 14.20 ?  75  LEU   A HB3  1 
ATOM   1595 H HG   . LEU   A 1 75  ? 33.874 -0.557  -1.512  1.00 16.55 ?  75  LEU   A HG   1 
ATOM   1596 H HD11 . LEU   A 1 75  ? 32.553 -1.474  0.177   1.00 19.21 ?  75  LEU   A HD11 1 
ATOM   1597 H HD12 . LEU   A 1 75  ? 31.683 -1.212  -1.127  1.00 19.21 ?  75  LEU   A HD12 1 
ATOM   1598 H HD13 . LEU   A 1 75  ? 32.174 -2.683  -0.781  1.00 19.21 ?  75  LEU   A HD13 1 
ATOM   1599 H HD21 . LEU   A 1 75  ? 34.861 -2.020  0.017   1.00 20.61 ?  75  LEU   A HD21 1 
ATOM   1600 H HD22 . LEU   A 1 75  ? 34.684 -3.191  -1.041  1.00 20.61 ?  75  LEU   A HD22 1 
ATOM   1601 H HD23 . LEU   A 1 75  ? 35.643 -1.966  -1.364  1.00 20.61 ?  75  LEU   A HD23 1 
ATOM   1602 N N    . LYS   A 1 76  ? 34.086 -3.690  -5.329  1.00 12.76 ?  76  LYS   A N    1 
ATOM   1603 C CA   . LYS   A 1 76  ? 33.496 -4.412  -6.450  1.00 13.10 ?  76  LYS   A CA   1 
ATOM   1604 C C    . LYS   A 1 76  ? 31.983 -4.489  -6.265  1.00 11.85 ?  76  LYS   A C    1 
ATOM   1605 O O    . LYS   A 1 76  ? 31.495 -4.589  -5.141  1.00 12.10 ?  76  LYS   A O    1 
ATOM   1606 C CB   . LYS   A 1 76  ? 34.043 -5.850  -6.502  1.00 14.86 ?  76  LYS   A CB   1 
ATOM   1607 C CG   . LYS   A 1 76  ? 35.547 -5.953  -6.722  1.00 16.03 ?  76  LYS   A CG   1 
ATOM   1608 C CD   . LYS   A 1 76  ? 36.056 -7.366  -6.522  1.00 17.35 ?  76  LYS   A CD   1 
ATOM   1609 C CE   . LYS   A 1 76  ? 37.563 -7.417  -6.679  1.00 19.85 ?  76  LYS   A CE   1 
ATOM   1610 N NZ   . LYS   A 1 76  ? 38.094 -8.765  -6.438  1.00 20.74 ?  76  LYS   A NZ   1 
ATOM   1611 H H    . LYS   A 1 76  ? 34.316 -4.210  -4.678  1.00 15.29 ?  76  LYS   A H    1 
ATOM   1612 H HA   . LYS   A 1 76  ? 33.696 -3.959  -7.284  1.00 15.69 ?  76  LYS   A HA   1 
ATOM   1613 H HB2  . LYS   A 1 76  ? 33.836 -6.285  -5.662  1.00 17.80 ?  76  LYS   A HB2  1 
ATOM   1614 H HB3  . LYS   A 1 76  ? 33.604 -6.314  -7.230  1.00 17.80 ?  76  LYS   A HB3  1 
ATOM   1615 H HG2  . LYS   A 1 76  ? 35.752 -5.677  -7.630  1.00 19.21 ?  76  LYS   A HG2  1 
ATOM   1616 H HG3  . LYS   A 1 76  ? 35.999 -5.370  -6.089  1.00 19.21 ?  76  LYS   A HG3  1 
ATOM   1617 H HD2  . LYS   A 1 76  ? 35.825 -7.666  -5.627  1.00 20.79 ?  76  LYS   A HD2  1 
ATOM   1618 H HD3  . LYS   A 1 76  ? 35.653 -7.948  -7.186  1.00 20.79 ?  76  LYS   A HD3  1 
ATOM   1619 H HE2  . LYS   A 1 76  ? 37.794 -7.152  -7.581  1.00 23.79 ?  76  LYS   A HE2  1 
ATOM   1620 H HE3  . LYS   A 1 76  ? 37.966 -6.812  -6.037  1.00 23.79 ?  76  LYS   A HE3  1 
ATOM   1621 H HZ1  . LYS   A 1 76  ? 38.979 -8.773  -6.538  1.00 24.86 ?  76  LYS   A HZ1  1 
ATOM   1622 H HZ2  . LYS   A 1 76  ? 37.895 -9.037  -5.613  1.00 24.86 ?  76  LYS   A HZ2  1 
ATOM   1623 H HZ3  . LYS   A 1 76  ? 37.738 -9.346  -7.019  1.00 24.86 ?  76  LYS   A HZ3  1 
ATOM   1624 N N    . VAL   A 1 77  ? 31.241 -4.447  -7.375  1.00 12.68 ?  77  VAL   A N    1 
ATOM   1625 C CA   . VAL   A 1 77  ? 29.828 -4.825  -7.301  1.00 12.54 ?  77  VAL   A CA   1 
ATOM   1626 C C    . VAL   A 1 77  ? 29.756 -6.279  -6.857  1.00 12.47 ?  77  VAL   A C    1 
ATOM   1627 O O    . VAL   A 1 77  ? 30.407 -7.152  -7.440  1.00 13.15 ?  77  VAL   A O    1 
ATOM   1628 C CB   . VAL   A 1 77  ? 29.127 -4.617  -8.651  1.00 14.21 ?  77  VAL   A CB   1 
ATOM   1629 C CG1  . VAL   A 1 77  ? 27.662 -5.032  -8.557  1.00 14.77 ?  77  VAL   A CG1  1 
ATOM   1630 C CG2  . VAL   A 1 77  ? 29.241 -3.173  -9.098  1.00 15.66 ?  77  VAL   A CG2  1 
ATOM   1631 H H    . VAL   A 1 77  ? 31.517 -4.200  -8.151  1.00 15.19 ?  77  VAL   A H    1 
ATOM   1632 H HA   . VAL   A 1 77  ? 29.380 -4.279  -6.636  1.00 15.02 ?  77  VAL   A HA   1 
ATOM   1633 H HB   . VAL   A 1 77  ? 29.556 -5.171  -9.320  1.00 17.03 ?  77  VAL   A HB   1 
ATOM   1634 H HG11 . VAL   A 1 77  ? 27.205 -4.742  -9.360  1.00 17.69 ?  77  VAL   A HG11 1 
ATOM   1635 H HG12 . VAL   A 1 77  ? 27.614 -5.997  -8.477  1.00 17.69 ?  77  VAL   A HG12 1 
ATOM   1636 H HG13 . VAL   A 1 77  ? 27.268 -4.612  -7.778  1.00 17.69 ?  77  VAL   A HG13 1 
ATOM   1637 H HG21 . VAL   A 1 77  ? 28.734 -3.055  -9.915  1.00 18.77 ?  77  VAL   A HG21 1 
ATOM   1638 H HG22 . VAL   A 1 77  ? 28.887 -2.599  -8.401  1.00 18.77 ?  77  VAL   A HG22 1 
ATOM   1639 H HG23 . VAL   A 1 77  ? 30.176 -2.963  -9.255  1.00 18.77 ?  77  VAL   A HG23 1 
ATOM   1640 N N    . GLY   A 1 78  ? 28.972 -6.547  -5.815  1.00 11.80 ?  78  GLY   A N    1 
ATOM   1641 C CA   . GLY   A 1 78  ? 28.952 -7.839  -5.164  1.00 12.33 ?  78  GLY   A CA   1 
ATOM   1642 C C    . GLY   A 1 78  ? 29.859 -7.929  -3.959  1.00 11.85 ?  78  GLY   A C    1 
ATOM   1643 O O    . GLY   A 1 78  ? 29.789 -8.923  -3.218  1.00 12.60 ?  78  GLY   A O    1 
ATOM   1644 H H    . GLY   A 1 78  ? 28.423 -5.976  -5.472  1.00 14.13 ?  78  GLY   A H    1 
ATOM   1645 H HA2  . GLY   A 1 78  ? 28.044 -8.035  -4.883  1.00 14.77 ?  78  GLY   A HA2  1 
ATOM   1646 H HA3  . GLY   A 1 78  ? 29.223 -8.518  -5.803  1.00 14.77 ?  78  GLY   A HA3  1 
ATOM   1647 N N    . GLY   A 1 79  ? 30.703 -6.917  -3.733  1.00 12.03 ?  79  GLY   A N    1 
ATOM   1648 C CA   . GLY   A 1 79  ? 31.661 -6.935  -2.652  1.00 12.23 ?  79  GLY   A CA   1 
ATOM   1649 C C    . GLY   A 1 79  ? 31.208 -6.137  -1.440  1.00 11.13 ?  79  GLY   A C    1 
ATOM   1650 O O    . GLY   A 1 79  ? 30.088 -5.626  -1.366  1.00 12.17 ?  79  GLY   A O    1 
ATOM   1651 H H    . GLY   A 1 79  ? 30.736 -6.195  -4.209  1.00 14.41 ?  79  GLY   A H    1 
ATOM   1652 H HA2  . GLY   A 1 79  ? 31.811 -7.856  -2.379  1.00 14.65 ?  79  GLY   A HA2  1 
ATOM   1653 H HA3  . GLY   A 1 79  ? 32.503 -6.571  -2.965  1.00 14.65 ?  79  GLY   A HA3  1 
ATOM   1654 N N    . SER   A 1 80  ? 32.111 -6.045  -0.465  1.00 11.85 ?  80  SER   A N    1 
ATOM   1655 C CA   . SER   A 1 80  ? 31.786 -5.406  0.802   1.00 11.51 ?  80  SER   A CA   1 
ATOM   1656 C C    . SER   A 1 80  ? 33.055 -4.951  1.505   1.00 11.37 ?  80  SER   A C    1 
ATOM   1657 O O    . SER   A 1 80  ? 34.170 -5.384  1.182   1.00 13.13 ?  80  SER   A O    1 
ATOM   1658 C CB   . SER   A 1 80  ? 31.016 -6.367  1.723   1.00 12.40 ?  80  SER   A CB   1 
ATOM   1659 O OG   . SER   A 1 80  ? 31.850 -7.417  2.199   1.00 13.91 ?  80  SER   A OG   1 
ATOM   1660 H H    . SER   A 1 80  ? 32.920 -6.331  -0.522  1.00 14.19 ?  80  SER   A H    1 
ATOM   1661 H HA   . SER   A 1 80  ? 31.232 -4.627  0.620   1.00 13.79 ?  80  SER   A HA   1 
ATOM   1662 H HB2  . SER   A 1 80  ? 30.672 -5.864  2.478   1.00 14.85 ?  80  SER   A HB2  1 
ATOM   1663 H HB3  . SER   A 1 80  ? 30.277 -6.753  1.223   1.00 14.85 ?  80  SER   A HB3  1 
ATOM   1664 H HG   . SER   A 1 80  ? 32.159 -7.847  1.545   1.00 16.67 ?  80  SER   A HG   1 
ATOM   1665 N N    . CYS   A 1 81  ? 32.862 -4.108  2.515   1.00 11.02 ?  81  CYS   A N    1 
ATOM   1666 C CA   . CYS   A 1 81  ? 33.913 -3.813  3.477   1.00 11.26 ?  81  CYS   A CA   1 
ATOM   1667 C C    . CYS   A 1 81  ? 33.273 -3.571  4.835   1.00 10.98 ?  81  CYS   A C    1 
ATOM   1668 O O    . CYS   A 1 81  ? 32.107 -3.164  4.923   1.00 12.33 ?  81  CYS   A O    1 
ATOM   1669 C CB   . CYS   A 1 81  ? 34.775 -2.621  3.051   1.00 12.05 ?  81  CYS   A CB   1 
ATOM   1670 S SG   . CYS   A 1 81  ? 33.891 -1.047  3.073   1.00 12.23 ?  81  CYS   A SG   1 
ATOM   1671 H H    . CYS   A 1 81  ? 32.123 -3.691  2.664   1.00 13.19 ?  81  CYS   A H    1 
ATOM   1672 H HA   . CYS   A 1 81  ? 34.494 -4.587  3.550   1.00 13.48 ?  81  CYS   A HA   1 
ATOM   1673 H HB2  . CYS   A 1 81  ? 35.534 -2.554  3.655   1.00 14.43 ?  81  CYS   A HB2  1 
ATOM   1674 H HB3  . CYS   A 1 81  ? 35.097 -2.774  2.145   1.00 14.43 ?  81  CYS   A HB3  1 
ATOM   1675 H HG   . CYS   A 1 81  ? 34.638 -0.170  2.733   1.00 14.64 ?  81  CYS   A HG   1 
ATOM   1676 N N    . VAL   A 1 82  ? 34.036 -3.842  5.892   1.00 11.34 ?  82  VAL   A N    1 
ATOM   1677 C CA   . VAL   A 1 82  ? 33.612 -3.597  7.265   1.00 11.88 ?  82  VAL   A CA   1 
ATOM   1678 C C    . VAL   A 1 82  ? 34.212 -2.282  7.734   1.00 12.12 ?  82  VAL   A C    1 
ATOM   1679 O O    . VAL   A 1 82  ? 35.437 -2.111  7.732   1.00 13.41 ?  82  VAL   A O    1 
ATOM   1680 C CB   . VAL   A 1 82  ? 34.039 -4.737  8.200   1.00 13.73 ?  82  VAL   A CB   1 
ATOM   1681 C CG1  . VAL   A 1 82  ? 33.610 -4.443  9.625   1.00 14.96 ?  82  VAL   A CG1  1 
ATOM   1682 C CG2  . VAL   A 1 82  ? 33.471 -6.066  7.726   1.00 14.63 ?  82  VAL   A CG2  1 
ATOM   1683 H H    . VAL   A 1 82  ? 34.827 -4.193  5.834   1.00 13.57 ?  82  VAL   A H    1 
ATOM   1684 H HA   . VAL   A 1 82  ? 32.644 -3.521  7.287   1.00 14.23 ?  82  VAL   A HA   1 
ATOM   1685 H HB   . VAL   A 1 82  ? 35.005 -4.803  8.186   1.00 16.45 ?  82  VAL   A HB   1 
ATOM   1686 H HG11 . VAL   A 1 82  ? 33.702 -5.251  10.153  1.00 17.92 ?  82  VAL   A HG11 1 
ATOM   1687 H HG12 . VAL   A 1 82  ? 34.178 -3.745  9.992   1.00 17.92 ?  82  VAL   A HG12 1 
ATOM   1688 H HG13 . VAL   A 1 82  ? 32.685 -4.152  9.625   1.00 17.92 ?  82  VAL   A HG13 1 
ATOM   1689 H HG21 . VAL   A 1 82  ? 33.720 -6.759  8.359   1.00 17.53 ?  82  VAL   A HG21 1 
ATOM   1690 H HG22 . VAL   A 1 82  ? 32.503 -5.999  7.677   1.00 17.53 ?  82  VAL   A HG22 1 
ATOM   1691 H HG23 . VAL   A 1 82  ? 33.831 -6.274  6.850   1.00 17.53 ?  82  VAL   A HG23 1 
ATOM   1692 N N    . LEU   A 1 83  ? 33.351 -1.353  8.133   1.00 12.18 ?  83  LEU   A N    1 
ATOM   1693 C CA   . LEU   A 1 83  ? 33.768 -0.085  8.713   1.00 11.71 ?  83  LEU   A CA   1 
ATOM   1694 C C    . LEU   A 1 83  ? 33.056 0.105   10.048  1.00 11.89 ?  83  LEU   A C    1 
ATOM   1695 O O    . LEU   A 1 83  ? 32.319 -0.775  10.515  1.00 12.59 ?  83  LEU   A O    1 
ATOM   1696 C CB   . LEU   A 1 83  ? 33.529 1.080   7.746   1.00 12.42 ?  83  LEU   A CB   1 
ATOM   1697 C CG   . LEU   A 1 83  ? 34.421 1.080   6.501   1.00 13.04 ?  83  LEU   A CG   1 
ATOM   1698 C CD1  . LEU   A 1 83  ? 33.979 2.143   5.505   1.00 13.17 ?  83  LEU   A CD1  1 
ATOM   1699 C CD2  . LEU   A 1 83  ? 35.905 1.276   6.864   1.00 14.17 ?  83  LEU   A CD2  1 
ATOM   1700 H H    . LEU   A 1 83  ? 32.494 -1.428  8.072   1.00 14.58 ?  83  LEU   A H    1 
ATOM   1701 H HA   . LEU   A 1 83  ? 34.720 -0.117  8.896   1.00 14.02 ?  83  LEU   A HA   1 
ATOM   1702 H HB2  . LEU   A 1 83  ? 32.610 1.055   7.443   1.00 14.88 ?  83  LEU   A HB2  1 
ATOM   1703 H HB3  . LEU   A 1 83  ? 33.691 1.918   8.213   1.00 14.88 ?  83  LEU   A HB3  1 
ATOM   1704 H HG   . LEU   A 1 83  ? 34.340 0.221   6.061   1.00 15.63 ?  83  LEU   A HG   1 
ATOM   1705 H HD11 . LEU   A 1 83  ? 34.565 2.110   4.727   1.00 15.77 ?  83  LEU   A HD11 1 
ATOM   1706 H HD12 . LEU   A 1 83  ? 33.067 1.964   5.234   1.00 15.77 ?  83  LEU   A HD12 1 
ATOM   1707 H HD13 . LEU   A 1 83  ? 34.039 3.015   5.922   1.00 15.77 ?  83  LEU   A HD13 1 
ATOM   1708 H HD21 . LEU   A 1 83  ? 36.420 1.408   6.050   1.00 16.98 ?  83  LEU   A HD21 1 
ATOM   1709 H HD22 . LEU   A 1 83  ? 35.993 2.055   7.437   1.00 16.98 ?  83  LEU   A HD22 1 
ATOM   1710 H HD23 . LEU   A 1 83  ? 36.226 0.487   7.330   1.00 16.98 ?  83  LEU   A HD23 1 
ATOM   1711 N N    . SER   A 1 84  ? 33.269 1.257   10.679  1.00 12.32 ?  84  SER   A N    1 
ATOM   1712 C CA   . SER   A 1 84  ? 32.619 1.512   11.954  1.00 12.30 ?  84  SER   A CA   1 
ATOM   1713 C C    . SER   A 1 84  ? 31.099 1.613   11.801  1.00 12.42 ?  84  SER   A C    1 
ATOM   1714 O O    . SER   A 1 84  ? 30.579 2.080   10.787  1.00 12.61 ?  84  SER   A O    1 
ATOM   1715 C CB   . SER   A 1 84  ? 33.134 2.821   12.541  1.00 13.60 ?  84  SER   A CB   1 
ATOM   1716 O OG   . SER   A 1 84  ? 32.495 3.121   13.762  1.00 14.74 ?  84  SER   A OG   1 
ATOM   1717 H H    . SER   A 1 84  ? 33.771 1.895   10.391  1.00 14.75 ?  84  SER   A H    1 
ATOM   1718 H HA   . SER   A 1 84  ? 32.827 0.787   12.568  1.00 14.73 ?  84  SER   A HA   1 
ATOM   1719 H HB2  . SER   A 1 84  ? 34.095 2.741   12.681  1.00 16.29 ?  84  SER   A HB2  1 
ATOM   1720 H HB3  . SER   A 1 84  ? 32.952 3.535   11.915  1.00 16.29 ?  84  SER   A HB3  1 
ATOM   1721 H HG   . SER   A 1 84  ? 32.809 3.832   14.082  1.00 17.65 ?  84  SER   A HG   1 
ATOM   1722 N N    . GLY   A 1 85  ? 30.388 1.209   12.851  1.00 13.62 ?  85  GLY   A N    1 
ATOM   1723 C CA   . GLY   A 1 85  ? 28.962 1.442   12.937  1.00 14.58 ?  85  GLY   A CA   1 
ATOM   1724 C C    . GLY   A 1 85  ? 28.587 2.759   13.582  1.00 13.83 ?  85  GLY   A C    1 
ATOM   1725 O O    . GLY   A 1 85  ? 27.396 3.068   13.701  1.00 14.75 ?  85  GLY   A O    1 
ATOM   1726 H H    . GLY   A 1 85  ? 30.717 0.785   13.530  1.00 16.32 ?  85  GLY   A H    1 
ATOM   1727 H HA2  . GLY   A 1 85  ? 28.588 1.422   12.044  1.00 17.47 ?  85  GLY   A HA2  1 
ATOM   1728 H HA3  . GLY   A 1 85  ? 28.554 0.731   13.451  1.00 17.47 ?  85  GLY   A HA3  1 
ATOM   1729 N N    . HIS   A 1 86  ? 29.570 3.540   14.024  1.00 13.13 ?  86  HIS   A N    1 
ATOM   1730 C CA   . HIS   A 1 86  ? 29.337 4.882   14.577  1.00 14.02 ?  86  HIS   A CA   1 
ATOM   1731 C C    . HIS   A 1 86  ? 28.351 4.766   15.733  1.00 14.54 ?  86  HIS   A C    1 
ATOM   1732 O O    . HIS   A 1 86  ? 28.545 3.903   16.603  1.00 15.90 ?  86  HIS   A O    1 
ATOM   1733 C CB   . HIS   A 1 86  ? 28.966 5.857   13.463  1.00 13.84 ?  86  HIS   A CB   1 
ATOM   1734 C CG   . HIS   A 1 86  ? 30.035 5.963   12.433  1.00 13.75 ?  86  HIS   A CG   1 
ATOM   1735 N ND1  . HIS   A 1 86  ? 31.125 6.798   12.579  1.00 15.01 ?  86  HIS   A ND1  1 
ATOM   1736 C CD2  . HIS   A 1 86  ? 30.235 5.270   11.289  1.00 13.50 ?  86  HIS   A CD2  1 
ATOM   1737 C CE1  . HIS   A 1 86  ? 31.931 6.633   11.546  1.00 14.41 ?  86  HIS   A CE1  1 
ATOM   1738 N NE2  . HIS   A 1 86  ? 31.419 5.709   10.754  1.00 14.41 ?  86  HIS   A NE2  1 
ATOM   1739 H H    . HIS   A 1 86  ? 30.395 3.316   14.023  1.00 15.73 ?  86  HIS   A H    1 
ATOM   1740 H HA   . HIS   A 1 86  ? 30.170 5.203   14.948  1.00 16.80 ?  86  HIS   A HA   1 
ATOM   1741 H HB2  . HIS   A 1 86  ? 28.153 5.553   13.022  1.00 16.57 ?  86  HIS   A HB2  1 
ATOM   1742 H HB3  . HIS   A 1 86  ? 28.826 6.743   13.834  1.00 16.57 ?  86  HIS   A HB3  1 
ATOM   1743 H HD2  . HIS   A 1 86  ? 29.677 4.614   10.926  1.00 16.17 ?  86  HIS   A HD2  1 
ATOM   1744 H HE1  . HIS   A 1 86  ? 32.723 7.093   11.393  1.00 17.26 ?  86  HIS   A HE1  1 
ATOM   1745 H HE2  . HIS   A 1 86  ? 31.765 5.437   10.005  1.00 17.26 ?  86  HIS   A HE2  1 
ATOM   1746 N N    . ASN   A 1 87  ? 27.330 5.617   15.799  1.00 15.91 ?  87  ASN   A N    1 
ATOM   1747 C CA   . ASN   A 1 87  ? 26.345 5.603   16.865  1.00 16.34 ?  87  ASN   A CA   1 
ATOM   1748 C C    . ASN   A 1 87  ? 25.235 4.593   16.634  1.00 17.68 ?  87  ASN   A C    1 
ATOM   1749 O O    . ASN   A 1 87  ? 24.324 4.518   17.459  1.00 19.88 ?  87  ASN   A O    1 
ATOM   1750 C CB   . ASN   A 1 87  ? 25.731 7.003   17.012  1.00 17.48 ?  87  ASN   A CB   1 
ATOM   1751 C CG   . ASN   A 1 87  ? 25.222 7.561   15.691  1.00 17.13 ?  87  ASN   A CG   1 
ATOM   1752 O OD1  . ASN   A 1 87  ? 25.878 7.450   14.663  1.00 17.79 ?  87  ASN   A OD1  1 
ATOM   1753 N ND2  . ASN   A 1 87  ? 24.048 8.166   15.720  1.00 18.79 ?  87  ASN   A ND2  1 
ATOM   1754 H H    . ASN   A 1 87  ? 27.187 6.235   15.217  1.00 19.07 ?  87  ASN   A H    1 
ATOM   1755 H HA   . ASN   A 1 87  ? 26.781 5.380   17.707  1.00 19.58 ?  87  ASN   A HA   1 
ATOM   1756 H HB2  . ASN   A 1 87  ? 24.981 6.956   17.630  1.00 20.95 ?  87  ASN   A HB2  1 
ATOM   1757 H HB3  . ASN   A 1 87  ? 26.404 7.609   17.358  1.00 20.95 ?  87  ASN   A HB3  1 
ATOM   1758 H HD21 . ASN   A 1 87  ? 23.721 8.492   14.996  1.00 22.52 ?  87  ASN   A HD21 1 
ATOM   1759 H HD22 . ASN   A 1 87  ? 23.617 8.234   16.459  1.00 22.52 ?  87  ASN   A HD22 1 
ATOM   1760 N N    . LEU   A 1 88  ? 25.290 3.817   15.556  1.00 16.81 ?  88  LEU   A N    1 
ATOM   1761 C CA   . LEU   A 1 88  ? 24.180 2.950   15.170  1.00 16.44 ?  88  LEU   A CA   1 
ATOM   1762 C C    . LEU   A 1 88  ? 24.404 1.474   15.477  1.00 16.26 ?  88  LEU   A C    1 
ATOM   1763 O O    . LEU   A 1 88  ? 23.430 0.734   15.653  1.00 17.22 ?  88  LEU   A O    1 
ATOM   1764 C CB   . LEU   A 1 88  ? 23.922 3.093   13.671  1.00 16.72 ?  88  LEU   A CB   1 
ATOM   1765 C CG   . LEU   A 1 88  ? 23.635 4.513   13.175  1.00 17.81 ?  88  LEU   A CG   1 
ATOM   1766 C CD1  . LEU   A 1 88  ? 23.507 4.514   11.668  1.00 18.28 ?  88  LEU   A CD1  1 
ATOM   1767 C CD2  . LEU   A 1 88  ? 22.375 5.079   13.826  1.00 19.72 ?  88  LEU   A CD2  1 
ATOM   1768 H H    . LEU   A 1 88  ? 25.976 3.766   15.041  1.00 20.14 ?  88  LEU   A H    1 
ATOM   1769 H HA   . LEU   A 1 88  ? 23.384 3.236   15.642  1.00 19.70 ?  88  LEU   A HA   1 
ATOM   1770 H HB2  . LEU   A 1 88  ? 24.700 2.778   13.193  1.00 20.03 ?  88  LEU   A HB2  1 
ATOM   1771 H HB3  . LEU   A 1 88  ? 23.153 2.553   13.443  1.00 20.03 ?  88  LEU   A HB3  1 
ATOM   1772 H HG   . LEU   A 1 88  ? 24.377 5.091   13.413  1.00 21.34 ?  88  LEU   A HG   1 
ATOM   1773 H HD11 . LEU   A 1 88  ? 23.377 5.426   11.362  1.00 21.91 ?  88  LEU   A HD11 1 
ATOM   1774 H HD12 . LEU   A 1 88  ? 24.317 4.147   11.283  1.00 21.91 ?  88  LEU   A HD12 1 
ATOM   1775 H HD13 . LEU   A 1 88  ? 22.744 3.970   11.417  1.00 21.91 ?  88  LEU   A HD13 1 
ATOM   1776 H HD21 . LEU   A 1 88  ? 22.174 5.939   13.423  1.00 23.63 ?  88  LEU   A HD21 1 
ATOM   1777 H HD22 . LEU   A 1 88  ? 21.644 4.463   13.679  1.00 23.63 ?  88  LEU   A HD22 1 
ATOM   1778 H HD23 . LEU   A 1 88  ? 22.535 5.189   14.776  1.00 23.63 ?  88  LEU   A HD23 1 
ATOM   1779 N N    . ALA   A 1 89  ? 25.655 1.031   15.518  1.00 15.53 ?  89  ALA   A N    1 
ATOM   1780 C CA   . ALA   A 1 89  ? 26.003 -0.379  15.617  1.00 15.11 ?  89  ALA   A CA   1 
ATOM   1781 C C    . ALA   A 1 89  ? 27.488 -0.437  15.931  1.00 15.34 ?  89  ALA   A C    1 
ATOM   1782 O O    . ALA   A 1 89  ? 28.197 0.560   15.800  1.00 16.27 ?  89  ALA   A O    1 
ATOM   1783 C CB   . ALA   A 1 89  ? 25.727 -1.092  14.296  1.00 14.63 ?  89  ALA   A CB   1 
ATOM   1784 H H    . ALA   A 1 89  ? 26.338 1.551   15.489  1.00 18.61 ?  89  ALA   A H    1 
ATOM   1785 H HA   . ALA   A 1 89  ? 25.499 -0.801  16.331  1.00 18.11 ?  89  ALA   A HA   1 
ATOM   1786 H HB1  . ALA   A 1 89  ? 25.975 -2.024  14.383  1.00 17.53 ?  89  ALA   A HB1  1 
ATOM   1787 H HB2  . ALA   A 1 89  ? 24.782 -1.019  14.085  1.00 17.53 ?  89  ALA   A HB2  1 
ATOM   1788 H HB3  . ALA   A 1 89  ? 26.253 -0.673  13.595  1.00 17.53 ?  89  ALA   A HB3  1 
ATOM   1789 N N    . LYS   A 1 90  ? 27.970 -1.612  16.324  1.00 16.06 ?  90  LYS   A N    1 
ATOM   1790 C CA   . LYS   A 1 90  ? 29.415 -1.756  16.466  1.00 16.36 ?  90  LYS   A CA   1 
ATOM   1791 C C    . LYS   A 1 90  ? 30.111 -1.570  15.121  1.00 14.98 ?  90  LYS   A C    1 
ATOM   1792 O O    . LYS   A 1 90  ? 31.040 -0.753  14.988  1.00 16.34 ?  90  LYS   A O    1 
ATOM   1793 C CB   . LYS   A 1 90  ? 29.767 -3.109  17.080  1.00 19.41 ?  90  LYS   A CB   1 
ATOM   1794 C CG   . LYS   A 1 90  ? 31.260 -3.261  17.375  1.00 24.57 ?  90  LYS   A CG   1 
ATOM   1795 C CD   . LYS   A 1 90  ? 31.531 -4.474  18.252  1.00 30.35 ?  90  LYS   A CD   1 
ATOM   1796 C CE   . LYS   A 1 90  ? 32.943 -4.456  18.819  1.00 34.62 ?  90  LYS   A CE   1 
ATOM   1797 N NZ   . LYS   A 1 90  ? 33.932 -5.122  17.927  1.00 37.60 ?  90  LYS   A NZ   1 
ATOM   1798 H H    . LYS   A 1 90  ? 27.501 -2.304  16.513  1.00 19.24 ?  90  LYS   A H    1 
ATOM   1799 H HA   . LYS   A 1 90  ? 29.742 -1.066  17.060  1.00 19.60 ?  90  LYS   A HA   1 
ATOM   1800 H HB2  . LYS   A 1 90  ? 29.285 -3.210  17.919  1.00 23.27 ?  90  LYS   A HB2  1 
ATOM   1801 H HB3  . LYS   A 1 90  ? 29.510 -3.816  16.468  1.00 23.27 ?  90  LYS   A HB3  1 
ATOM   1802 H HG2  . LYS   A 1 90  ? 31.742 -3.373  16.542  1.00 29.45 ?  90  LYS   A HG2  1 
ATOM   1803 H HG3  . LYS   A 1 90  ? 31.574 -2.470  17.843  1.00 29.45 ?  90  LYS   A HG3  1 
ATOM   1804 H HD2  . LYS   A 1 90  ? 30.904 -4.479  18.994  1.00 36.39 ?  90  LYS   A HD2  1 
ATOM   1805 H HD3  . LYS   A 1 90  ? 31.426 -5.281  17.722  1.00 36.39 ?  90  LYS   A HD3  1 
ATOM   1806 H HE2  . LYS   A 1 90  ? 33.223 -3.535  18.942  1.00 41.51 ?  90  LYS   A HE2  1 
ATOM   1807 H HE3  . LYS   A 1 90  ? 32.946 -4.919  19.671  1.00 41.51 ?  90  LYS   A HE3  1 
ATOM   1808 H HZ1  . LYS   A 1 90  ? 34.734 -5.125  18.313  1.00 45.10 ?  90  LYS   A HZ1  1 
ATOM   1809 H HZ2  . LYS   A 1 90  ? 33.683 -5.963  17.773  1.00 45.10 ?  90  LYS   A HZ2  1 
ATOM   1810 H HZ3  . LYS   A 1 90  ? 33.984 -4.689  17.153  1.00 45.10 ?  90  LYS   A HZ3  1 
ATOM   1811 N N    . HIS   A 1 91  ? 29.654 -2.303  14.106  1.00 12.55 ?  91  HIS   A N    1 
ATOM   1812 C CA   . HIS   A 1 91  ? 30.216 -2.286  12.771  1.00 13.01 ?  91  HIS   A CA   1 
ATOM   1813 C C    . HIS   A 1 91  ? 29.129 -2.020  11.744  1.00 10.46 ?  91  HIS   A C    1 
ATOM   1814 O O    . HIS   A 1 91  ? 27.958 -2.373  11.942  1.00 13.18 ?  91  HIS   A O    1 
ATOM   1815 C CB   . HIS   A 1 91  ? 30.835 -3.648  12.404  1.00 16.16 ?  91  HIS   A CB   1 
ATOM   1816 C CG   . HIS   A 1 91  ? 31.858 -4.136  13.378  1.00 20.41 ?  91  HIS   A CG   1 
ATOM   1817 N ND1  . HIS   A 1 91  ? 33.125 -3.600  13.460  1.00 22.45 ?  91  HIS   A ND1  1 
ATOM   1818 C CD2  . HIS   A 1 91  ? 31.810 -5.130  14.295  1.00 22.69 ?  91  HIS   A CD2  1 
ATOM   1819 C CE1  . HIS   A 1 91  ? 33.811 -4.235  14.396  1.00 23.49 ?  91  HIS   A CE1  1 
ATOM   1820 N NE2  . HIS   A 1 91  ? 33.035 -5.171  14.916  1.00 23.91 ?  91  HIS   A NE2  1 
ATOM   1821 H H    . HIS   A 1 91  ? 28.983 -2.854  14.178  1.00 15.03 ?  91  HIS   A H    1 
ATOM   1822 H HA   . HIS   A 1 91  ? 30.900 -1.608  12.702  1.00 15.59 ?  91  HIS   A HA   1 
ATOM   1823 H HB2  . HIS   A 1 91  ? 30.134 -4.316  12.363  1.00 19.36 ?  91  HIS   A HB2  1 
ATOM   1824 H HB3  . HIS   A 1 91  ? 31.268 -3.575  11.538  1.00 19.36 ?  91  HIS   A HB3  1 
ATOM   1825 H HD1  . HIS   A 1 91  ? 33.426 -2.952  12.979  1.00 26.91 ?  91  HIS   A HD1  1 
ATOM   1826 H HD2  . HIS   A 1 91  ? 31.090 -5.681  14.478  1.00 27.21 ?  91  HIS   A HD2  1 
ATOM   1827 H HE1  . HIS   A 1 91  ? 34.694 -4.053  14.644  1.00 28.16 ?  91  HIS   A HE1  1 
ATOM   1828 N N    . CYS   A 1 92  ? 29.532 -1.428  10.630  1.00 11.13 ?  92  CYS   A N    1 
ATOM   1829 C CA   . CYS   A 1 92  ? 28.704 -1.367  9.438   1.00 10.81 ?  92  CYS   A CA   1 
ATOM   1830 C C    . CYS   A 1 92  ? 29.361 -2.188  8.341   1.00 11.34 ?  92  CYS   A C    1 
ATOM   1831 O O    . CYS   A 1 92  ? 30.518 -1.936  7.979   1.00 12.21 ?  92  CYS   A O    1 
ATOM   1832 C CB   . CYS   A 1 92  ? 28.487 0.072   8.969   1.00 11.71 ?  92  CYS   A CB   1 
ATOM   1833 S SG   . CYS   A 1 92  ? 27.486 0.191   7.459   1.00 11.74 ?  92  CYS   A SG   1 
ATOM   1834 H H    . CYS   A 1 92  ? 30.299 -1.042  10.542  1.00 13.33 ?  92  CYS   A H    1 
ATOM   1835 H HA   . CYS   A 1 92  ? 27.840 -1.754  9.631   1.00 12.95 ?  92  CYS   A HA   1 
ATOM   1836 H HB2  . CYS   A 1 92  ? 28.029 0.568   9.668   1.00 14.02 ?  92  CYS   A HB2  1 
ATOM   1837 H HB3  . CYS   A 1 92  ? 29.348 0.482   8.787   1.00 14.02 ?  92  CYS   A HB3  1 
ATOM   1838 H HG   . CYS   A 1 92  ? 27.351 1.348   7.173   1.00 14.06 ?  92  CYS   A HG   1 
ATOM   1839 N N    . LEU   A 1 93  ? 28.622 -3.169  7.827   1.00 11.20 ?  93  LEU   A N    1 
ATOM   1840 C CA   . LEU   A 1 93  ? 29.035 -3.923  6.653   1.00 10.61 ?  93  LEU   A CA   1 
ATOM   1841 C C    . LEU   A 1 93  ? 28.434 -3.233  5.435   1.00 10.51 ?  93  LEU   A C    1 
ATOM   1842 O O    . LEU   A 1 93  ? 27.221 -3.304  5.207   1.00 10.67 ?  93  LEU   A O    1 
ATOM   1843 C CB   . LEU   A 1 93  ? 28.570 -5.374  6.768   1.00 11.56 ?  93  LEU   A CB   1 
ATOM   1844 C CG   . LEU   A 1 93  ? 28.959 -6.282  5.604   1.00 11.83 ?  93  LEU   A CG   1 
ATOM   1845 C CD1  . LEU   A 1 93  ? 30.463 -6.555  5.595   1.00 12.49 ?  93  LEU   A CD1  1 
ATOM   1846 C CD2  . LEU   A 1 93  ? 28.171 -7.586  5.671   1.00 12.66 ?  93  LEU   A CD2  1 
ATOM   1847 H H    . LEU   A 1 93  ? 27.865 -3.420  8.155   1.00 13.42 ?  93  LEU   A H    1 
ATOM   1848 H HA   . LEU   A 1 93  ? 30.003 -3.907  6.583   1.00 12.71 ?  93  LEU   A HA   1 
ATOM   1849 H HB2  . LEU   A 1 93  ? 28.956 -5.758  7.576   1.00 13.84 ?  93  LEU   A HB2  1 
ATOM   1850 H HB3  . LEU   A 1 93  ? 27.606 -5.386  6.835   1.00 13.84 ?  93  LEU   A HB3  1 
ATOM   1851 H HG   . LEU   A 1 93  ? 28.738 -5.842  4.773   1.00 14.17 ?  93  LEU   A HG   1 
ATOM   1852 H HD11 . LEU   A 1 93  ? 30.676 -7.156  4.865   1.00 14.97 ?  93  LEU   A HD11 1 
ATOM   1853 H HD12 . LEU   A 1 93  ? 30.940 -5.716  5.482   1.00 14.97 ?  93  LEU   A HD12 1 
ATOM   1854 H HD13 . LEU   A 1 93  ? 30.719 -6.962  6.442   1.00 14.97 ?  93  LEU   A HD13 1 
ATOM   1855 H HD21 . LEU   A 1 93  ? 28.435 -8.150  4.929   1.00 15.17 ?  93  LEU   A HD21 1 
ATOM   1856 H HD22 . LEU   A 1 93  ? 28.365 -8.028  6.511   1.00 15.17 ?  93  LEU   A HD22 1 
ATOM   1857 H HD23 . LEU   A 1 93  ? 27.225 -7.381  5.613   1.00 15.17 ?  93  LEU   A HD23 1 
ATOM   1858 N N    . HIS   A 1 94  ? 29.278 -2.544  4.672   1.00 10.02 ?  94  HIS   A N    1 
ATOM   1859 C CA   . HIS   A 1 94  ? 28.856 -1.879  3.442   1.00 10.20 ?  94  HIS   A CA   1 
ATOM   1860 C C    . HIS   A 1 94  ? 28.875 -2.919  2.337   1.00 10.23 ?  94  HIS   A C    1 
ATOM   1861 O O    . HIS   A 1 94  ? 29.942 -3.433  1.988   1.00 11.89 ?  94  HIS   A O    1 
ATOM   1862 C CB   . HIS   A 1 94  ? 29.815 -0.735  3.105   1.00 10.41 ?  94  HIS   A CB   1 
ATOM   1863 C CG   . HIS   A 1 94  ? 29.810 0.362   4.117   1.00 10.44 ?  94  HIS   A CG   1 
ATOM   1864 N ND1  . HIS   A 1 94  ? 28.923 1.422   4.072   1.00 10.56 ?  94  HIS   A ND1  1 
ATOM   1865 C CD2  . HIS   A 1 94  ? 30.553 0.534   5.232   1.00 11.41 ?  94  HIS   A CD2  1 
ATOM   1866 C CE1  . HIS   A 1 94  ? 29.139 2.206   5.114   1.00 10.59 ?  94  HIS   A CE1  1 
ATOM   1867 N NE2  . HIS   A 1 94  ? 30.120 1.687   5.833   1.00 10.85 ?  94  HIS   A NE2  1 
ATOM   1868 H H    . HIS   A 1 94  ? 30.116 -2.435  4.848   1.00 12.00 ?  94  HIS   A H    1 
ATOM   1869 H HA   . HIS   A 1 94  ? 27.953 -1.525  3.540   1.00 12.21 ?  94  HIS   A HA   1 
ATOM   1870 H HB2  . HIS   A 1 94  ? 30.713 -1.081  3.054   1.00 12.46 ?  94  HIS   A HB2  1 
ATOM   1871 H HB3  . HIS   A 1 94  ? 29.555 -0.346  2.253   1.00 12.46 ?  94  HIS   A HB3  1 
ATOM   1872 H HD2  . HIS   A 1 94  ? 31.234 -0.016  5.532   1.00 13.66 ?  94  HIS   A HD2  1 
ATOM   1873 H HE1  . HIS   A 1 94  ? 28.671 2.990   5.305   1.00 12.68 ?  94  HIS   A HE1  1 
ATOM   1874 H HE2  . HIS   A 1 94  ? 30.440 2.034   6.552   1.00 12.99 ?  94  HIS   A HE2  1 
ATOM   1875 N N    . VAL   A 1 95  ? 27.704 -3.250  1.796   1.00 9.76  ?  95  VAL   A N    1 
ATOM   1876 C CA   . VAL   A 1 95  ? 27.564 -4.286  0.780   1.00 9.58  ?  95  VAL   A CA   1 
ATOM   1877 C C    . VAL   A 1 95  ? 27.026 -3.658  -0.490  1.00 9.61  ?  95  VAL   A C    1 
ATOM   1878 O O    . VAL   A 1 95  ? 26.024 -2.926  -0.445  1.00 10.73 ?  95  VAL   A O    1 
ATOM   1879 C CB   . VAL   A 1 95  ? 26.632 -5.422  1.235   1.00 10.87 ?  95  VAL   A CB   1 
ATOM   1880 C CG1  . VAL   A 1 95  ? 26.531 -6.465  0.126   1.00 11.61 ?  95  VAL   A CG1  1 
ATOM   1881 C CG2  . VAL   A 1 95  ? 27.135 -6.035  2.526   1.00 10.88 ?  95  VAL   A CG2  1 
ATOM   1882 H H    . VAL   A 1 95  ? 26.955 -2.887  2.012   1.00 11.69 ?  95  VAL   A H    1 
ATOM   1883 H HA   . VAL   A 1 95  ? 28.433 -4.670  0.584   1.00 11.47 ?  95  VAL   A HA   1 
ATOM   1884 H HB   . VAL   A 1 95  ? 25.744 -5.073  1.389   1.00 13.01 ?  95  VAL   A HB   1 
ATOM   1885 H HG11 . VAL   A 1 95  ? 26.171 -7.287  0.490   1.00 13.91 ?  95  VAL   A HG11 1 
ATOM   1886 H HG12 . VAL   A 1 95  ? 25.951 -6.131  -0.577  1.00 13.91 ?  95  VAL   A HG12 1 
ATOM   1887 H HG13 . VAL   A 1 95  ? 27.422 -6.630  -0.235  1.00 13.91 ?  95  VAL   A HG13 1 
ATOM   1888 H HG21 . VAL   A 1 95  ? 26.573 -6.795  2.753   1.00 13.03 ?  95  VAL   A HG21 1 
ATOM   1889 H HG22 . VAL   A 1 95  ? 28.049 -6.325  2.403   1.00 13.03 ?  95  VAL   A HG22 1 
ATOM   1890 H HG23 . VAL   A 1 95  ? 27.084 -5.367  3.225   1.00 13.03 ?  95  VAL   A HG23 1 
ATOM   1891 N N    . VAL   A 1 96  ? 27.660 -3.960  -1.622  1.00 9.13  ?  96  VAL   A N    1 
ATOM   1892 C CA   . VAL   A 1 96  ? 27.257 -3.416  -2.912  1.00 10.44 ?  96  VAL   A CA   1 
ATOM   1893 C C    . VAL   A 1 96  ? 26.459 -4.464  -3.684  1.00 11.18 ?  96  VAL   A C    1 
ATOM   1894 O O    . VAL   A 1 96  ? 27.026 -5.413  -4.229  1.00 12.08 ?  96  VAL   A O    1 
ATOM   1895 C CB   . VAL   A 1 96  ? 28.459 -2.934  -3.728  1.00 10.55 ?  96  VAL   A CB   1 
ATOM   1896 C CG1  . VAL   A 1 96  ? 27.968 -2.301  -4.997  1.00 11.09 ?  96  VAL   A CG1  1 
ATOM   1897 C CG2  . VAL   A 1 96  ? 29.312 -1.960  -2.928  1.00 11.36 ?  96  VAL   A CG2  1 
ATOM   1898 H H    . VAL   A 1 96  ? 28.351 -4.487  -1.667  1.00 10.93 ?  96  VAL   A H    1 
ATOM   1899 H HA   . VAL   A 1 96  ? 26.679 -2.656  -2.758  1.00 12.50 ?  96  VAL   A HA   1 
ATOM   1900 H HB   . VAL   A 1 96  ? 29.009 -3.692  -3.966  1.00 12.64 ?  96  VAL   A HB   1 
ATOM   1901 H HG11 . VAL   A 1 96  ? 28.701 -1.814  -5.411  1.00 13.28 ?  96  VAL   A HG11 1 
ATOM   1902 H HG12 . VAL   A 1 96  ? 27.652 -2.989  -5.601  1.00 13.28 ?  96  VAL   A HG12 1 
ATOM   1903 H HG13 . VAL   A 1 96  ? 27.246 -1.684  -4.790  1.00 13.28 ?  96  VAL   A HG13 1 
ATOM   1904 H HG21 . VAL   A 1 96  ? 30.021 -1.617  -3.495  1.00 13.60 ?  96  VAL   A HG21 1 
ATOM   1905 H HG22 . VAL   A 1 96  ? 28.755 -1.227  -2.619  1.00 13.60 ?  96  VAL   A HG22 1 
ATOM   1906 H HG23 . VAL   A 1 96  ? 29.695 -2.425  -2.166  1.00 13.60 ?  96  VAL   A HG23 1 
ATOM   1907 N N    A GLY   A 1 97  ? 25.140 -4.315  -3.700  0.66 11.12 ?  97  GLY   A N    1 
ATOM   1908 N N    B GLY   A 1 97  ? 25.146 -4.278  -3.778  0.34 11.07 ?  97  GLY   A N    1 
ATOM   1909 C CA   A GLY   A 1 97  ? 24.319 -5.062  -4.614  0.66 11.70 ?  97  GLY   A CA   1 
ATOM   1910 C CA   B GLY   A 1 97  ? 24.347 -5.072  -4.680  0.34 11.52 ?  97  GLY   A CA   1 
ATOM   1911 C C    A GLY   A 1 97  ? 24.301 -4.369  -5.962  0.66 11.60 ?  97  GLY   A C    1 
ATOM   1912 C C    B GLY   A 1 97  ? 24.445 -4.545  -6.102  0.34 11.74 ?  97  GLY   A C    1 
ATOM   1913 O O    A GLY   A 1 97  ? 24.558 -3.166  -6.064  0.66 12.36 ?  97  GLY   A O    1 
ATOM   1914 O O    B GLY   A 1 97  ? 24.849 -3.400  -6.332  0.34 11.81 ?  97  GLY   A O    1 
ATOM   1915 H H    A GLY   A 1 97  ? 24.704 -3.782  -3.180  0.66 13.32 ?  97  GLY   A H    1 
ATOM   1916 H H    B GLY   A 1 97  ? 24.700 -3.699  -3.321  0.34 13.25 ?  97  GLY   A H    1 
ATOM   1917 H HA2  A GLY   A 1 97  ? 24.680 -5.952  -4.716  0.66 14.01 ?  97  GLY   A HA2  1 
ATOM   1918 H HA2  B GLY   A 1 97  ? 24.659 -5.990  -4.656  0.34 13.80 ?  97  GLY   A HA2  1 
ATOM   1919 H HA3  A GLY   A 1 97  ? 23.414 -5.122  -4.267  0.66 14.01 ?  97  GLY   A HA3  1 
ATOM   1920 H HA3  B GLY   A 1 97  ? 23.420 -5.050  -4.399  0.34 13.80 ?  97  GLY   A HA3  1 
ATOM   1921 N N    A PRO   A 1 98  ? 23.997 -5.111  -7.025  0.66 11.46 ?  98  PRO   A N    1 
ATOM   1922 N N    B PRO   A 1 98  ? 24.084 -5.367  -7.086  0.34 12.42 ?  98  PRO   A N    1 
ATOM   1923 C CA   A PRO   A 1 98  ? 23.878 -4.490  -8.348  0.66 12.16 ?  98  PRO   A CA   1 
ATOM   1924 C CA   B PRO   A 1 98  ? 24.092 -4.895  -8.477  0.34 13.47 ?  98  PRO   A CA   1 
ATOM   1925 C C    A PRO   A 1 98  ? 22.758 -3.459  -8.380  0.66 12.07 ?  98  PRO   A C    1 
ATOM   1926 C C    B PRO   A 1 98  ? 23.018 -3.845  -8.725  0.34 13.84 ?  98  PRO   A C    1 
ATOM   1927 O O    A PRO   A 1 98  ? 21.692 -3.647  -7.788  0.66 11.95 ?  98  PRO   A O    1 
ATOM   1928 O O    B PRO   A 1 98  ? 21.890 -3.947  -8.235  0.34 14.33 ?  98  PRO   A O    1 
ATOM   1929 C CB   A PRO   A 1 98  ? 23.580 -5.679  -9.269  0.66 12.61 ?  98  PRO   A CB   1 
ATOM   1930 C CB   B PRO   A 1 98  ? 23.820 -6.169  -9.286  0.34 13.36 ?  98  PRO   A CB   1 
ATOM   1931 C CG   A PRO   A 1 98  ? 22.957 -6.704  -8.366  0.66 12.66 ?  98  PRO   A CG   1 
ATOM   1932 C CG   B PRO   A 1 98  ? 23.135 -7.094  -8.330  0.34 13.03 ?  98  PRO   A CG   1 
ATOM   1933 C CD   A PRO   A 1 98  ? 23.683 -6.551  -7.053  0.66 12.17 ?  98  PRO   A CD   1 
ATOM   1934 C CD   B PRO   A 1 98  ? 23.738 -6.796  -6.985  0.34 11.96 ?  98  PRO   A CD   1 
ATOM   1935 H HA   A PRO   A 1 98  ? 24.720 -4.081  -8.601  0.66 14.56 ?  98  PRO   A HA   1 
ATOM   1936 H HA   B PRO   A 1 98  ? 24.964 -4.539  -8.711  0.34 16.14 ?  98  PRO   A HA   1 
ATOM   1937 H HB2  A PRO   A 1 98  ? 22.959 -5.411  -9.958  0.66 15.10 ?  98  PRO   A HB2  1 
ATOM   1938 H HB2  B PRO   A 1 98  ? 23.243 -5.961  -10.036 0.34 16.01 ?  98  PRO   A HB2  1 
ATOM   1939 H HB3  A PRO   A 1 98  ? 24.405 -6.019  -9.649  0.66 15.10 ?  98  PRO   A HB3  1 
ATOM   1940 H HB3  B PRO   A 1 98  ? 24.658 -6.551  -9.590  0.34 16.01 ?  98  PRO   A HB3  1 
ATOM   1941 H HG2  A PRO   A 1 98  ? 22.010 -6.520  -8.256  0.66 15.17 ?  98  PRO   A HG2  1 
ATOM   1942 H HG2  B PRO   A 1 98  ? 22.182 -6.910  -8.327  0.34 15.61 ?  98  PRO   A HG2  1 
ATOM   1943 H HG3  A PRO   A 1 98  ? 23.093 -7.595  -8.728  0.66 15.17 ?  98  PRO   A HG3  1 
ATOM   1944 H HG3  B PRO   A 1 98  ? 23.304 -8.014  -8.588  0.34 15.61 ?  98  PRO   A HG3  1 
ATOM   1945 H HD2  A PRO   A 1 98  ? 23.102 -6.796  -6.308  0.66 14.58 ?  98  PRO   A HD2  1 
ATOM   1946 H HD2  B PRO   A 1 98  ? 23.085 -6.939  -6.279  0.34 14.32 ?  98  PRO   A HD2  1 
ATOM   1947 H HD3  A PRO   A 1 98  ? 24.500 -7.077  -7.046  0.66 14.58 ?  98  PRO   A HD3  1 
ATOM   1948 H HD3  B PRO   A 1 98  ? 24.535 -7.334  -6.841  0.34 14.32 ?  98  PRO   A HD3  1 
ATOM   1949 N N    A ASN   A 1 99  ? 23.020 -2.354  -9.068  0.66 12.67 ?  99  ASN   A N    1 
ATOM   1950 N N    B ASN   A 1 99  ? 23.381 -2.825  -9.498  0.34 13.77 ?  99  ASN   A N    1 
ATOM   1951 C CA   A ASN   A 1 99  ? 22.036 -1.299  -9.276  0.66 14.00 ?  99  ASN   A CA   1 
ATOM   1952 C CA   B ASN   A 1 99  ? 22.460 -1.764  -9.904  0.34 14.37 ?  99  ASN   A CA   1 
ATOM   1953 C C    A ASN   A 1 99  ? 21.468 -1.465  -10.681 0.66 15.81 ?  99  ASN   A C    1 
ATOM   1954 C C    B ASN   A 1 99  ? 21.928 -2.130  -11.284 0.34 14.84 ?  99  ASN   A C    1 
ATOM   1955 O O    A ASN   A 1 99  ? 22.145 -1.171  -11.674 0.66 17.48 ?  99  ASN   A O    1 
ATOM   1956 O O    B ASN   A 1 99  ? 22.614 -1.952  -12.293 0.34 14.10 ?  99  ASN   A O    1 
ATOM   1957 C CB   A ASN   A 1 99  ? 22.675 0.076   -9.091  0.66 13.99 ?  99  ASN   A CB   1 
ATOM   1958 C CB   B ASN   A 1 99  ? 23.176 -0.418  -9.936  0.34 15.25 ?  99  ASN   A CB   1 
ATOM   1959 C CG   A ASN   A 1 99  ? 21.652 1.211   -9.094  0.66 14.86 ?  99  ASN   A CG   1 
ATOM   1960 C CG   B ASN   A 1 99  ? 22.234 0.742   -10.223 0.34 15.96 ?  99  ASN   A CG   1 
ATOM   1961 O OD1  A ASN   A 1 99  ? 20.671 1.182   -9.840  0.66 15.90 ?  99  ASN   A OD1  1 
ATOM   1962 O OD1  B ASN   A 1 99  ? 21.130 0.555   -10.730 0.34 15.56 ?  99  ASN   A OD1  1 
ATOM   1963 N ND2  A ASN   A 1 99  ? 21.891 2.220   -8.263  0.66 15.70 ?  99  ASN   A ND2  1 
ATOM   1964 N ND2  B ASN   A 1 99  ? 22.673 1.951   -9.901  0.34 17.43 ?  99  ASN   A ND2  1 
ATOM   1965 H H    A ASN   A 1 99  ? 23.789 -2.185  -9.411  0.66 15.18 ?  99  ASN   A H    1 
ATOM   1966 H H    B ASN   A 1 99  ? 24.179 -2.724  -9.799  0.34 16.50 ?  99  ASN   A H    1 
ATOM   1967 H HA   A ASN   A 1 99  ? 21.315 -1.400  -8.629  0.66 16.77 ?  99  ASN   A HA   1 
ATOM   1968 H HA   B ASN   A 1 99  ? 21.716 -1.716  -9.283  0.34 17.22 ?  99  ASN   A HA   1 
ATOM   1969 H HB2  A ASN   A 1 99  ? 23.149 0.092   -8.244  0.66 16.76 ?  99  ASN   A HB2  1 
ATOM   1970 H HB2  B ASN   A 1 99  ? 23.589 -0.264  -9.076  0.34 18.27 ?  99  ASN   A HB2  1 
ATOM   1971 H HB3  A ASN   A 1 99  ? 23.293 0.230   -9.820  0.66 16.76 ?  99  ASN   A HB3  1 
ATOM   1972 H HB3  B ASN   A 1 99  ? 23.853 -0.444  -10.628 0.34 18.27 ?  99  ASN   A HB3  1 
ATOM   1973 H HD21 A ASN   A 1 99  ? 21.345 2.881   -8.220  0.66 18.81 ?  99  ASN   A HD21 1 
ATOM   1974 H HD21 B ASN   A 1 99  ? 22.175 2.639   -10.040 0.34 20.89 ?  99  ASN   A HD21 1 
ATOM   1975 H HD22 A ASN   A 1 99  ? 22.594 2.209   -7.765  0.66 18.81 ?  99  ASN   A HD22 1 
ATOM   1976 H HD22 B ASN   A 1 99  ? 23.453 2.045   -9.556  0.34 20.89 ?  99  ASN   A HD22 1 
ATOM   1977 N N    A VAL   A 1 100 ? 20.221 -1.941  -10.758 0.66 16.23 ?  100 VAL   A N    1 
ATOM   1978 N N    B VAL   A 1 100 ? 20.697 -2.646  -11.322 0.34 17.85 ?  100 VAL   A N    1 
ATOM   1979 C CA   A VAL   A 1 100 ? 19.585 -2.193  -12.048 0.66 18.27 ?  100 VAL   A CA   1 
ATOM   1980 C CA   B VAL   A 1 100 ? 20.111 -3.093  -12.583 0.34 20.41 ?  100 VAL   A CA   1 
ATOM   1981 C C    A VAL   A 1 100 ? 19.453 -0.906  -12.849 0.66 19.90 ?  100 VAL   A C    1 
ATOM   1982 C C    B VAL   A 1 100 ? 19.924 -1.932  -13.551 0.34 21.78 ?  100 VAL   A C    1 
ATOM   1983 O O    A VAL   A 1 100 ? 19.499 -0.926  -14.085 0.66 21.34 ?  100 VAL   A O    1 
ATOM   1984 O O    B VAL   A 1 100 ? 19.946 -2.122  -14.774 0.34 21.83 ?  100 VAL   A O    1 
ATOM   1985 C CB   A VAL   A 1 100 ? 18.227 -2.905  -11.844 0.66 19.30 ?  100 VAL   A CB   1 
ATOM   1986 C CB   B VAL   A 1 100 ? 18.801 -3.860  -12.312 0.34 21.73 ?  100 VAL   A CB   1 
ATOM   1987 C CG1  A VAL   A 1 100 ? 17.492 -3.079  -13.165 0.66 20.57 ?  100 VAL   A CG1  1 
ATOM   1988 C CG1  B VAL   A 1 100 ? 17.839 -3.747  -13.489 0.34 22.15 ?  100 VAL   A CG1  1 
ATOM   1989 C CG2  A VAL   A 1 100 ? 18.443 -4.259  -11.177 0.66 19.13 ?  100 VAL   A CG2  1 
ATOM   1990 C CG2  B VAL   A 1 100 ? 19.105 -5.317  -12.008 0.34 22.59 ?  100 VAL   A CG2  1 
ATOM   1991 H H    A VAL   A 1 100 ? 19.724 -2.128  -10.076 0.66 19.44 ?  100 VAL   A H    1 
ATOM   1992 H H    B VAL   A 1 100 ? 20.187 -2.751  -10.636 0.34 21.39 ?  100 VAL   A H    1 
ATOM   1993 H HA   A VAL   A 1 100 ? 20.146 -2.798  -12.555 0.66 21.89 ?  100 VAL   A HA   1 
ATOM   1994 H HA   B VAL   A 1 100 ? 20.726 -3.719  -12.996 0.34 24.46 ?  100 VAL   A HA   1 
ATOM   1995 H HB   A VAL   A 1 100 ? 17.670 -2.371  -11.258 0.66 23.14 ?  100 VAL   A HB   1 
ATOM   1996 H HB   B VAL   A 1 100 ? 18.365 -3.475  -11.536 0.34 26.05 ?  100 VAL   A HB   1 
ATOM   1997 H HG11 A VAL   A 1 100 ? 16.746 -3.689  -13.035 0.66 24.65 ?  100 VAL   A HG11 1 
ATOM   1998 H HG11 B VAL   A 1 100 ? 17.126 -4.394  -13.370 0.34 26.55 ?  100 VAL   A HG11 1 
ATOM   1999 H HG12 A VAL   A 1 100 ? 17.162 -2.218  -13.462 0.66 24.65 ?  100 VAL   A HG12 1 
ATOM   2000 H HG12 B VAL   A 1 100 ? 17.465 -2.851  -13.513 0.34 26.55 ?  100 VAL   A HG12 1 
ATOM   2001 H HG13 A VAL   A 1 100 ? 18.103 -3.447  -13.823 0.66 24.65 ?  100 VAL   A HG13 1 
ATOM   2002 H HG13 B VAL   A 1 100 ? 18.317 -3.933  -14.311 0.34 26.55 ?  100 VAL   A HG13 1 
ATOM   2003 H HG21 A VAL   A 1 100 ? 17.589 -4.713  -11.098 0.66 22.93 ?  100 VAL   A HG21 1 
ATOM   2004 H HG21 B VAL   A 1 100 ? 18.276 -5.776  -11.805 0.34 27.08 ?  100 VAL   A HG21 1 
ATOM   2005 H HG22 A VAL   A 1 100 ? 19.048 -4.787  -11.722 0.66 22.93 ?  100 VAL   A HG22 1 
ATOM   2006 H HG22 B VAL   A 1 100 ? 19.525 -5.719  -12.785 0.34 27.08 ?  100 VAL   A HG22 1 
ATOM   2007 H HG23 A VAL   A 1 100 ? 18.827 -4.121  -10.297 0.66 22.93 ?  100 VAL   A HG23 1 
ATOM   2008 H HG23 B VAL   A 1 100 ? 19.704 -5.360  -11.247 0.34 27.08 ?  100 VAL   A HG23 1 
ATOM   2009 N N    A ASN   A 1 101 ? 19.281 0.228   -12.171 0.66 20.80 ?  101 ASN   A N    1 
ATOM   2010 N N    B ASN   A 1 101 ? 19.729 -0.720  -13.036 0.34 22.99 ?  101 ASN   A N    1 
ATOM   2011 C CA   A ASN   A 1 101 ? 19.216 1.508   -12.867 0.66 22.64 ?  101 ASN   A CA   1 
ATOM   2012 C CA   B ASN   A 1 101 ? 19.634 0.449   -13.901 0.34 24.26 ?  101 ASN   A CA   1 
ATOM   2013 C C    A ASN   A 1 101 ? 20.570 1.961   -13.408 0.66 24.41 ?  101 ASN   A C    1 
ATOM   2014 C C    B ASN   A 1 101 ? 20.994 0.940   -14.384 0.34 24.67 ?  101 ASN   A C    1 
ATOM   2015 O O    A ASN   A 1 101 ? 20.636 3.029   -14.032 0.66 26.39 ?  101 ASN   A O    1 
ATOM   2016 O O    B ASN   A 1 101 ? 21.043 1.841   -15.229 0.34 24.62 ?  101 ASN   A O    1 
ATOM   2017 C CB   A ASN   A 1 101 ? 18.602 2.568   -11.949 0.66 21.95 ?  101 ASN   A CB   1 
ATOM   2018 C CB   B ASN   A 1 101 ? 18.859 1.565   -13.195 0.34 25.19 ?  101 ASN   A CB   1 
ATOM   2019 C CG   A ASN   A 1 101 ? 17.219 2.172   -11.452 0.66 22.10 ?  101 ASN   A CG   1 
ATOM   2020 C CG   B ASN   A 1 101 ? 17.485 1.112   -12.736 0.34 25.91 ?  101 ASN   A CG   1 
ATOM   2021 O OD1  A ASN   A 1 101 ? 16.394 1.656   -12.212 0.66 22.77 ?  101 ASN   A OD1  1 
ATOM   2022 O OD1  B ASN   A 1 101 ? 16.886 0.213   -13.326 0.34 26.18 ?  101 ASN   A OD1  1 
ATOM   2023 N ND2  A ASN   A 1 101 ? 16.964 2.395   -10.169 0.66 22.36 ?  101 ASN   A ND2  1 
ATOM   2024 N ND2  B ASN   A 1 101 ? 16.980 1.729   -11.679 0.34 26.28 ?  101 ASN   A ND2  1 
ATOM   2025 H H    A ASN   A 1 101 ? 19.180 0.277   -11.321 0.66 24.94 ?  101 ASN   A H    1 
ATOM   2026 H H    B ASN   A 1 101 ? 19.633 -0.556  -12.200 0.34 27.56 ?  101 ASN   A H    1 
ATOM   2027 H HA   A ASN   A 1 101 ? 18.621 1.410   -13.625 0.66 27.14 ?  101 ASN   A HA   1 
ATOM   2028 H HA   B ASN   A 1 101 ? 19.129 0.204   -14.688 0.34 29.09 ?  101 ASN   A HA   1 
ATOM   2029 H HB2  A ASN   A 1 101 ? 19.176 2.695   -11.180 0.66 26.31 ?  101 ASN   A HB2  1 
ATOM   2030 H HB2  B ASN   A 1 101 ? 19.357 1.855   -12.416 0.34 30.20 ?  101 ASN   A HB2  1 
ATOM   2031 H HB3  A ASN   A 1 101 ? 18.519 3.402   -12.444 0.66 26.31 ?  101 ASN   A HB3  1 
ATOM   2032 H HB3  B ASN   A 1 101 ? 18.738 2.303   -13.811 0.34 30.20 ?  101 ASN   A HB3  1 
ATOM   2033 H HD21 A ASN   A 1 101 ? 16.195 2.191   -9.843  0.66 26.80 ?  101 ASN   A HD21 1 
ATOM   2034 H HD21 B ASN   A 1 101 ? 16.206 1.502   -11.380 0.34 31.51 ?  101 ASN   A HD21 1 
ATOM   2035 H HD22 A ASN   A 1 101 ? 17.563 2.753   -9.666  0.66 26.80 ?  101 ASN   A HD22 1 
ATOM   2036 H HD22 B ASN   A 1 101 ? 17.425 2.354   -11.296 0.34 31.51 ?  101 ASN   A HD22 1 
ATOM   2037 N N    A LYS   A 1 102 ? 21.635 1.184   -13.187 0.66 25.88 ?  102 LYS   A N    1 
ATOM   2038 N N    B LYS   A 1 102 ? 22.089 0.370   -13.877 0.34 25.36 ?  102 LYS   A N    1 
ATOM   2039 C CA   A LYS   A 1 102 ? 22.924 1.390   -13.838 0.66 27.30 ?  102 LYS   A CA   1 
ATOM   2040 C CA   B LYS   A 1 102 ? 23.425 0.577   -14.421 0.34 25.53 ?  102 LYS   A CA   1 
ATOM   2041 C C    A LYS   A 1 102 ? 23.266 0.283   -14.827 0.66 27.94 ?  102 LYS   A C    1 
ATOM   2042 C C    B LYS   A 1 102 ? 23.832 -0.535  -15.383 0.34 24.20 ?  102 LYS   A C    1 
ATOM   2043 O O    A LYS   A 1 102 ? 24.363 0.301   -15.396 0.66 28.90 ?  102 LYS   A O    1 
ATOM   2044 O O    B LYS   A 1 102 ? 24.997 -0.600  -15.788 0.34 24.19 ?  102 LYS   A O    1 
ATOM   2045 C CB   A LYS   A 1 102 ? 24.047 1.482   -12.796 0.66 29.04 ?  102 LYS   A CB   1 
ATOM   2046 C CB   B LYS   A 1 102 ? 24.460 0.661   -13.296 0.34 27.03 ?  102 LYS   A CB   1 
ATOM   2047 C CG   A LYS   A 1 102 ? 23.898 2.605   -11.788 0.66 30.39 ?  102 LYS   A CG   1 
ATOM   2048 C CG   B LYS   A 1 102 ? 24.561 2.001   -12.585 0.34 28.54 ?  102 LYS   A CG   1 
ATOM   2049 C CD   A LYS   A 1 102 ? 25.081 2.620   -10.828 0.66 31.95 ?  102 LYS   A CD   1 
ATOM   2050 C CD   B LYS   A 1 102 ? 25.593 1.924   -11.461 0.34 30.16 ?  102 LYS   A CD   1 
ATOM   2051 C CE   A LYS   A 1 102 ? 24.939 3.709   -9.779  0.66 33.30 ?  102 LYS   A CE   1 
ATOM   2052 C CE   B LYS   A 1 102 ? 25.573 3.157   -10.571 0.34 31.44 ?  102 LYS   A CE   1 
ATOM   2053 N NZ   A LYS   A 1 102 ? 26.040 3.660   -8.773  0.66 33.98 ?  102 LYS   A NZ   1 
ATOM   2054 N NZ   B LYS   A 1 102 ? 25.935 2.812   -9.164  0.34 32.28 ?  102 LYS   A NZ   1 
ATOM   2055 H H    A LYS   A 1 102 ? 21.633 0.511   -12.650 0.66 31.03 ?  102 LYS   A H    1 
ATOM   2056 H H    B LYS   A 1 102 ? 22.078 -0.160  -13.198 0.34 30.41 ?  102 LYS   A H    1 
ATOM   2057 H HA   A LYS   A 1 102 ? 22.900 2.225   -14.328 0.66 32.73 ?  102 LYS   A HA   1 
ATOM   2058 H HA   B LYS   A 1 102 ? 23.442 1.426   -14.893 0.34 30.61 ?  102 LYS   A HA   1 
ATOM   2059 H HB2  A LYS   A 1 102 ? 24.080 0.646   -12.303 0.66 34.82 ?  102 LYS   A HB2  1 
ATOM   2060 H HB2  B LYS   A 1 102 ? 24.242 -0.008  -12.631 0.34 32.41 ?  102 LYS   A HB2  1 
ATOM   2061 H HB3  A LYS   A 1 102 ? 24.889 1.615   -13.260 0.66 34.82 ?  102 LYS   A HB3  1 
ATOM   2062 H HB3  B LYS   A 1 102 ? 25.335 0.471   -13.666 0.34 32.41 ?  102 LYS   A HB3  1 
ATOM   2063 H HG2  A LYS   A 1 102 ? 23.867 3.455   -12.253 0.66 36.44 ?  102 LYS   A HG2  1 
ATOM   2064 H HG2  B LYS   A 1 102 ? 24.846 2.682   -13.215 0.34 34.22 ?  102 LYS   A HG2  1 
ATOM   2065 H HG3  A LYS   A 1 102 ? 23.086 2.470   -11.273 0.66 36.44 ?  102 LYS   A HG3  1 
ATOM   2066 H HG3  B LYS   A 1 102 ? 23.702 2.234   -12.201 0.34 34.22 ?  102 LYS   A HG3  1 
ATOM   2067 H HD2  A LYS   A 1 102 ? 25.134 1.764   -10.373 0.66 38.32 ?  102 LYS   A HD2  1 
ATOM   2068 H HD2  B LYS   A 1 102 ? 25.407 1.150   -10.908 0.34 36.16 ?  102 LYS   A HD2  1 
ATOM   2069 H HD3  A LYS   A 1 102 ? 25.896 2.784   -11.329 0.66 38.32 ?  102 LYS   A HD3  1 
ATOM   2070 H HD3  B LYS   A 1 102 ? 26.480 1.848   -11.850 0.34 36.16 ?  102 LYS   A HD3  1 
ATOM   2071 H HE2  A LYS   A 1 102 ? 24.964 4.575   -10.216 0.66 39.93 ?  102 LYS   A HE2  1 
ATOM   2072 H HE2  B LYS   A 1 102 ? 26.220 3.803   -10.901 0.34 37.70 ?  102 LYS   A HE2  1 
ATOM   2073 H HE3  A LYS   A 1 102 ? 24.096 3.593   -9.314  0.66 39.93 ?  102 LYS   A HE3  1 
ATOM   2074 H HE3  B LYS   A 1 102 ? 24.683 3.542   -10.573 0.34 37.70 ?  102 LYS   A HE3  1 
ATOM   2075 H HZ1  A LYS   A 1 102 ? 25.932 4.307   -8.173  0.66 40.75 ?  102 LYS   A HZ1  1 
ATOM   2076 H HZ1  B LYS   A 1 102 ? 25.915 3.542   -8.656  0.34 38.71 ?  102 LYS   A HZ1  1 
ATOM   2077 H HZ2  A LYS   A 1 102 ? 26.035 2.873   -8.356  0.66 40.75 ?  102 LYS   A HZ2  1 
ATOM   2078 H HZ2  B LYS   A 1 102 ? 25.355 2.218   -8.839  0.34 38.71 ?  102 LYS   A HZ2  1 
ATOM   2079 H HZ3  A LYS   A 1 102 ? 26.826 3.767   -9.178  0.66 40.75 ?  102 LYS   A HZ3  1 
ATOM   2080 H HZ3  B LYS   A 1 102 ? 26.752 2.461   -9.137  0.34 38.71 ?  102 LYS   A HZ3  1 
ATOM   2081 N N    A GLY   A 1 103 ? 22.375 -0.685  -15.034 0.66 28.48 ?  103 GLY   A N    1 
ATOM   2082 N N    B GLY   A 1 103 ? 22.906 -1.422  -15.741 0.34 23.07 ?  103 GLY   A N    1 
ATOM   2083 C CA   A GLY   A 1 103 ? 22.633 -1.778  -15.953 0.66 28.79 ?  103 GLY   A CA   1 
ATOM   2084 C CA   B GLY   A 1 103 ? 23.228 -2.539  -16.610 0.34 22.45 ?  103 GLY   A CA   1 
ATOM   2085 C C    A GLY   A 1 103 ? 23.461 -2.913  -15.391 0.66 28.93 ?  103 GLY   A C    1 
ATOM   2086 C C    B GLY   A 1 103 ? 23.978 -3.672  -15.947 0.34 21.90 ?  103 GLY   A C    1 
ATOM   2087 O O    A GLY   A 1 103 ? 23.975 -3.728  -16.163 0.66 30.36 ?  103 GLY   A O    1 
ATOM   2088 O O    B GLY   A 1 103 ? 24.581 -4.495  -16.644 0.34 22.50 ?  103 GLY   A O    1 
ATOM   2089 H H    A GLY   A 1 103 ? 21.608 -0.729  -14.657 0.66 34.14 ?  103 GLY   A H    1 
ATOM   2090 H H    B GLY   A 1 103 ? 22.083 -1.381  -15.496 0.34 27.65 ?  103 GLY   A H    1 
ATOM   2091 H HA2  A GLY   A 1 103 ? 21.784 -2.136  -16.267 0.66 34.52 ?  103 GLY   A HA2  1 
ATOM   2092 H HA2  B GLY   A 1 103 ? 22.405 -2.889  -16.992 0.34 26.92 ?  103 GLY   A HA2  1 
ATOM   2093 H HA3  A GLY   A 1 103 ? 23.110 -1.433  -16.724 0.66 34.52 ?  103 GLY   A HA3  1 
ATOM   2094 H HA3  B GLY   A 1 103 ? 23.780 -2.206  -17.336 0.34 26.92 ?  103 GLY   A HA3  1 
ATOM   2095 N N    A GLU   A 1 104 ? 23.601 -3.003  -14.072 0.66 27.00 ?  104 GLU   A N    1 
ATOM   2096 N N    B GLU   A 1 104 ? 23.949 -3.754  -14.623 0.34 20.06 ?  104 GLU   A N    1 
ATOM   2097 C CA   A GLU   A 1 104 ? 24.488 -3.988  -13.469 0.66 25.56 ?  104 GLU   A CA   1 
ATOM   2098 C CA   B GLU   A 1 104 ? 24.785 -4.696  -13.896 0.34 18.52 ?  104 GLU   A CA   1 
ATOM   2099 C C    A GLU   A 1 104 ? 23.813 -5.353  -13.350 0.66 25.77 ?  104 GLU   A C    1 
ATOM   2100 C C    B GLU   A 1 104 ? 24.072 -6.028  -13.687 0.34 17.37 ?  104 GLU   A C    1 
ATOM   2101 O O    A GLU   A 1 104 ? 22.599 -5.463  -13.152 0.66 25.92 ?  104 GLU   A O    1 
ATOM   2102 O O    B GLU   A 1 104 ? 22.841 -6.104  -13.643 0.34 17.55 ?  104 GLU   A O    1 
ATOM   2103 C CB   A GLU   A 1 104 ? 24.986 -3.480  -12.112 0.66 23.50 ?  104 GLU   A CB   1 
ATOM   2104 C CB   B GLU   A 1 104 ? 25.225 -4.100  -12.560 0.34 18.29 ?  104 GLU   A CB   1 
ATOM   2105 C CG   A GLU   A 1 104 ? 25.833 -2.209  -12.268 0.66 22.37 ?  104 GLU   A CG   1 
ATOM   2106 C CG   B GLU   A 1 104 ? 26.129 -2.883  -12.743 0.34 18.50 ?  104 GLU   A CG   1 
ATOM   2107 C CD   A GLU   A 1 104 ? 26.205 -1.507  -10.964 0.66 20.69 ?  104 GLU   A CD   1 
ATOM   2108 C CD   B GLU   A 1 104 ? 26.504 -2.181  -11.448 0.34 18.62 ?  104 GLU   A CD   1 
ATOM   2109 O OE1  A GLU   A 1 104 ? 25.670 -1.857  -9.895  0.66 18.53 ?  104 GLU   A OE1  1 
ATOM   2110 O OE1  B GLU   A 1 104 ? 25.946 -2.522  -10.387 0.34 19.48 ?  104 GLU   A OE1  1 
ATOM   2111 O OE2  A GLU   A 1 104 ? 27.036 -0.571  -11.023 0.66 21.77 -1 104 GLU   A OE2  1 
ATOM   2112 O OE2  B GLU   A 1 104 ? 27.360 -1.270  -11.502 0.34 18.19 -1 104 GLU   A OE2  1 
ATOM   2113 H H    A GLU   A 1 104 ? 23.200 -2.500  -13.507 0.66 32.37 ?  104 GLU   A H    1 
ATOM   2114 H H    B GLU   A 1 104 ? 23.444 -3.264  -14.131 0.34 24.05 ?  104 GLU   A H    1 
ATOM   2115 H HA   A GLU   A 1 104 ? 25.260 -4.096  -14.043 0.66 30.64 ?  104 GLU   A HA   1 
ATOM   2116 H HA   B GLU   A 1 104 ? 25.578 -4.862  -14.427 0.34 22.19 ?  104 GLU   A HA   1 
ATOM   2117 H HB2  A GLU   A 1 104 ? 24.222 -3.277  -11.551 0.66 28.18 ?  104 GLU   A HB2  1 
ATOM   2118 H HB2  B GLU   A 1 104 ? 24.440 -3.827  -12.065 0.34 21.92 ?  104 GLU   A HB2  1 
ATOM   2119 H HB3  A GLU   A 1 104 ? 25.533 -4.168  -11.700 0.66 28.18 ?  104 GLU   A HB3  1 
ATOM   2120 H HB3  B GLU   A 1 104 ? 25.716 -4.776  -12.072 0.34 21.92 ?  104 GLU   A HB3  1 
ATOM   2121 H HG2  A GLU   A 1 104 ? 26.652 -2.447  -12.728 0.66 26.82 ?  104 GLU   A HG2  1 
ATOM   2122 H HG2  B GLU   A 1 104 ? 26.946 -3.166  -13.182 0.34 22.17 ?  104 GLU   A HG2  1 
ATOM   2123 H HG3  A GLU   A 1 104 ? 25.331 -1.574  -12.801 0.66 26.82 ?  104 GLU   A HG3  1 
ATOM   2124 H HG3  B GLU   A 1 104 ? 25.667 -2.232  -13.294 0.34 22.17 ?  104 GLU   A HG3  1 
ATOM   2125 N N    A ASP   A 1 105 ? 24.629 -6.399  -13.470 0.66 26.23 ?  105 ASP   A N    1 
ATOM   2126 N N    B ASP   A 1 105 ? 24.877 -7.074  -13.527 0.34 17.16 ?  105 ASP   A N    1 
ATOM   2127 C CA   A ASP   A 1 105 ? 24.139 -7.768  -13.591 0.66 27.20 ?  105 ASP   A CA   1 
ATOM   2128 C CA   B ASP   A 1 105 ? 24.413 -8.453  -13.618 0.34 17.67 ?  105 ASP   A CA   1 
ATOM   2129 C C    A ASP   A 1 105 ? 23.462 -8.209  -12.296 0.66 25.27 ?  105 ASP   A C    1 
ATOM   2130 C C    B ASP   A 1 105 ? 23.620 -8.836  -12.373 0.34 16.44 ?  105 ASP   A C    1 
ATOM   2131 O O    A ASP   A 1 105 ? 24.091 -8.225  -11.234 0.66 24.48 ?  105 ASP   A O    1 
ATOM   2132 O O    B ASP   A 1 105 ? 24.138 -8.776  -11.254 0.34 13.74 ?  105 ASP   A O    1 
ATOM   2133 C CB   A ASP   A 1 105 ? 25.320 -8.681  -13.914 0.66 29.62 ?  105 ASP   A CB   1 
ATOM   2134 C CB   B ASP   A 1 105 ? 25.632 -9.360  -13.775 0.34 19.33 ?  105 ASP   A CB   1 
ATOM   2135 C CG   A ASP   A 1 105 ? 24.907 -10.115 -14.138 0.66 31.80 ?  105 ASP   A CG   1 
ATOM   2136 C CG   B ASP   A 1 105 ? 25.267 -10.819 -13.931 0.34 21.10 ?  105 ASP   A CG   1 
ATOM   2137 O OD1  A ASP   A 1 105 ? 23.690 -10.376 -14.243 0.66 32.39 ?  105 ASP   A OD1  1 
ATOM   2138 O OD1  B ASP   A 1 105 ? 24.062 -11.144 -13.977 0.34 21.08 ?  105 ASP   A OD1  1 
ATOM   2139 O OD2  A ASP   A 1 105 ? 25.808 -10.981 -14.205 0.66 33.29 -1 105 ASP   A OD2  1 
ATOM   2140 O OD2  B ASP   A 1 105 ? 26.202 -11.645 -13.998 0.34 22.10 -1 105 ASP   A OD2  1 
ATOM   2141 H H    A ASP   A 1 105 ? 25.487 -6.342  -13.484 0.66 31.45 ?  105 ASP   A H    1 
ATOM   2142 H H    B ASP   A 1 105 ? 25.708 -7.002  -13.348 0.34 20.56 ?  105 ASP   A H    1 
ATOM   2143 H HA   A ASP   A 1 105 ? 23.495 -7.831  -14.313 0.66 32.62 ?  105 ASP   A HA   1 
ATOM   2144 H HA   B ASP   A 1 105 ? 23.844 -8.565  -14.395 0.34 21.18 ?  105 ASP   A HA   1 
ATOM   2145 H HB2  A ASP   A 1 105 ? 25.757 -8.363  -14.722 0.66 35.51 ?  105 ASP   A HB2  1 
ATOM   2146 H HB2  B ASP   A 1 105 ? 26.145 -9.068  -14.551 0.34 23.17 ?  105 ASP   A HB2  1 
ATOM   2147 H HB3  A ASP   A 1 105 ? 25.946 -8.672  -13.175 0.66 35.51 ?  105 ASP   A HB3  1 
ATOM   2148 H HB3  B ASP   A 1 105 ? 26.182 -9.299  -12.982 0.34 23.17 ?  105 ASP   A HB3  1 
ATOM   2149 N N    A ILE   A 1 106 ? 22.183 -8.589  -12.391 0.66 24.21 ?  106 ILE   A N    1 
ATOM   2150 N N    B ILE   A 1 106 ? 22.367 -9.259  -12.576 0.34 18.39 ?  106 ILE   A N    1 
ATOM   2151 C CA   A ILE   A 1 106 ? 21.424 -9.007  -11.216 0.66 22.89 ?  106 ILE   A CA   1 
ATOM   2152 C CA   B ILE   A 1 106 ? 21.522 -9.671  -11.459 0.34 19.97 ?  106 ILE   A CA   1 
ATOM   2153 C C    A ILE   A 1 106 ? 21.954 -10.307 -10.632 0.66 21.78 ?  106 ILE   A C    1 
ATOM   2154 C C    B ILE   A 1 106 ? 22.153 -10.822 -10.691 0.34 20.16 ?  106 ILE   A C    1 
ATOM   2155 O O    A ILE   A 1 106 ? 21.741 -10.577 -9.445  0.66 21.30 ?  106 ILE   A O    1 
ATOM   2156 O O    B ILE   A 1 106 ? 21.922 -10.972 -9.485  0.34 20.40 ?  106 ILE   A O    1 
ATOM   2157 C CB   A ILE   A 1 106 ? 19.919 -9.107  -11.544 0.66 24.06 ?  106 ILE   A CB   1 
ATOM   2158 C CB   B ILE   A 1 106 ? 20.105 -10.025 -11.956 0.34 21.43 ?  106 ILE   A CB   1 
ATOM   2159 C CG1  A ILE   A 1 106 ? 19.083 -9.149  -10.261 0.66 24.84 ?  106 ILE   A CG1  1 
ATOM   2160 C CG1  B ILE   A 1 106 ? 19.095 -9.949  -10.810 0.34 22.13 ?  106 ILE   A CG1  1 
ATOM   2161 C CG2  A ILE   A 1 106 ? 19.631 -10.346 -12.372 0.66 24.90 ?  106 ILE   A CG2  1 
ATOM   2162 C CG2  B ILE   A 1 106 ? 20.074 -11.427 -12.551 0.34 21.84 ?  106 ILE   A CG2  1 
ATOM   2163 C CD1  A ILE   A 1 106 ? 19.216 -7.910  -9.398  0.66 25.07 ?  106 ILE   A CD1  1 
ATOM   2164 C CD1  B ILE   A 1 106 ? 18.930 -8.564  -10.234 0.34 22.73 ?  106 ILE   A CD1  1 
ATOM   2165 H H    A ILE   A 1 106 ? 21.740 -8.610  -13.121 0.66 29.03 ?  106 ILE   A H    1 
ATOM   2166 H H    B ILE   A 1 106 ? 21.992 -9.317  -13.344 0.34 22.04 ?  106 ILE   A H    1 
ATOM   2167 H HA   A ILE   A 1 106 ? 21.537 -8.332  -10.534 0.66 27.43 ?  106 ILE   A HA   1 
ATOM   2168 H HA   B ILE   A 1 106 ? 21.448 -8.933  -10.845 0.34 23.94 ?  106 ILE   A HA   1 
ATOM   2169 H HB   A ILE   A 1 106 ? 19.662 -8.323  -12.055 0.66 28.85 ?  106 ILE   A HB   1 
ATOM   2170 H HB   B ILE   A 1 106 ? 19.848 -9.393  -12.645 0.34 25.69 ?  106 ILE   A HB   1 
ATOM   2171 H HG12 A ILE   A 1 106 ? 18.148 -9.239  -10.501 0.66 29.78 ?  106 ILE   A HG12 1 
ATOM   2172 H HG12 B ILE   A 1 106 ? 18.228 -10.241 -11.138 0.34 26.53 ?  106 ILE   A HG12 1 
ATOM   2173 H HG13 A ILE   A 1 106 ? 19.360 -9.910  -9.729  0.66 29.78 ?  106 ILE   A HG13 1 
ATOM   2174 H HG13 B ILE   A 1 106 ? 19.389 -10.538 -10.097 0.34 26.53 ?  106 ILE   A HG13 1 
ATOM   2175 H HG21 A ILE   A 1 106 ? 18.756 -10.254 -12.776 0.66 29.85 ?  106 ILE   A HG21 1 
ATOM   2176 H HG21 B ILE   A 1 106 ? 19.277 -11.522 -13.097 0.34 26.18 ?  106 ILE   A HG21 1 
ATOM   2177 H HG22 A ILE   A 1 106 ? 20.310 -10.425 -13.058 0.66 29.85 ?  106 ILE   A HG22 1 
ATOM   2178 H HG22 B ILE   A 1 106 ? 20.865 -11.558 -13.096 0.34 26.18 ?  106 ILE   A HG22 1 
ATOM   2179 H HG23 A ILE   A 1 106 ? 19.651 -11.123 -11.792 0.66 29.85 ?  106 ILE   A HG23 1 
ATOM   2180 H HG23 B ILE   A 1 106 ? 20.057 -12.079 -11.831 0.34 26.18 ?  106 ILE   A HG23 1 
ATOM   2181 H HD11 A ILE   A 1 106 ? 18.479 -7.885  -8.768  0.66 30.06 ?  106 ILE   A HD11 1 
ATOM   2182 H HD11 B ILE   A 1 106 ? 18.095 -8.528  -9.747  0.34 27.25 ?  106 ILE   A HD11 1 
ATOM   2183 H HD12 A ILE   A 1 106 ? 20.058 -7.947  -8.916  0.66 30.06 ?  106 ILE   A HD12 1 
ATOM   2184 H HD12 B ILE   A 1 106 ? 19.672 -8.381  -9.638  0.34 27.25 ?  106 ILE   A HD12 1 
ATOM   2185 H HD13 A ILE   A 1 106 ? 19.193 -7.124  -9.966  0.66 30.06 ?  106 ILE   A HD13 1 
ATOM   2186 H HD13 B ILE   A 1 106 ? 18.920 -7.923  -10.961 0.34 27.25 ?  106 ILE   A HD13 1 
ATOM   2187 N N    A GLN   A 1 107 ? 22.661 -11.112 -11.432 0.66 22.55 ?  107 GLN   A N    1 
ATOM   2188 N N    B GLN   A 1 107 ? 22.958 -11.650 -11.366 0.34 20.37 ?  107 GLN   A N    1 
ATOM   2189 C CA   A GLN   A 1 107 ? 23.270 -12.334 -10.920 0.66 24.86 ?  107 GLN   A CA   1 
ATOM   2190 C CA   B GLN   A 1 107 ? 23.612 -12.766 -10.691 0.34 21.67 ?  107 GLN   A CA   1 
ATOM   2191 C C    A GLN   A 1 107 ? 24.261 -12.047 -9.798  0.66 22.43 ?  107 GLN   A C    1 
ATOM   2192 C C    B GLN   A 1 107 ? 24.491 -12.287 -9.545  0.34 19.35 ?  107 GLN   A C    1 
ATOM   2193 O O    A GLN   A 1 107 ? 24.508 -12.918 -8.959  0.66 24.37 ?  107 GLN   A O    1 
ATOM   2194 O O    B GLN   A 1 107 ? 24.722 -13.028 -8.581  0.34 19.28 ?  107 GLN   A O    1 
ATOM   2195 C CB   A GLN   A 1 107 ? 23.954 -13.088 -12.067 0.66 29.37 ?  107 GLN   A CB   1 
ATOM   2196 C CB   B GLN   A 1 107 ? 24.436 -13.576 -11.698 0.34 25.18 ?  107 GLN   A CB   1 
ATOM   2197 C CG   A GLN   A 1 107 ? 23.048 -13.330 -13.273 0.66 34.40 ?  107 GLN   A CG   1 
ATOM   2198 C CG   B GLN   A 1 107 ? 23.619 -14.152 -12.846 0.34 28.74 ?  107 GLN   A CG   1 
ATOM   2199 C CD   A GLN   A 1 107 ? 21.793 -14.103 -12.916 0.66 38.46 ?  107 GLN   A CD   1 
ATOM   2200 C CD   B GLN   A 1 107 ? 22.543 -15.108 -12.371 0.34 31.45 ?  107 GLN   A CD   1 
ATOM   2201 O OE1  A GLN   A 1 107 ? 21.855 -15.135 -12.247 0.66 40.09 ?  107 GLN   A OE1  1 
ATOM   2202 O OE1  B GLN   A 1 107 ? 22.763 -15.905 -11.457 0.34 32.35 ?  107 GLN   A OE1  1 
ATOM   2203 N NE2  A GLN   A 1 107 ? 20.643 -13.602 -13.357 0.66 39.78 ?  107 GLN   A NE2  1 
ATOM   2204 N NE2  B GLN   A 1 107 ? 21.368 -15.027 -12.985 0.34 32.18 ?  107 GLN   A NE2  1 
ATOM   2205 H H    A GLN   A 1 107 ? 22.809 -10.964 -12.265 0.66 27.04 ?  107 GLN   A H    1 
ATOM   2206 H H    B GLN   A 1 107 ? 23.144 -11.586 -12.203 0.34 24.42 ?  107 GLN   A H    1 
ATOM   2207 H HA   A GLN   A 1 107 ? 22.577 -12.908 -10.566 0.66 29.80 ?  107 GLN   A HA   1 
ATOM   2208 H HA   B GLN   A 1 107 ? 22.940 -13.354 -10.321 0.34 25.97 ?  107 GLN   A HA   1 
ATOM   2209 H HB2  A GLN   A 1 107 ? 24.718 -12.576 -12.375 0.66 35.22 ?  107 GLN   A HB2  1 
ATOM   2210 H HB2  B GLN   A 1 107 ? 25.118 -13.005 -12.084 0.34 30.19 ?  107 GLN   A HB2  1 
ATOM   2211 H HB3  A GLN   A 1 107 ? 24.247 -13.956 -11.748 0.66 35.22 ?  107 GLN   A HB3  1 
ATOM   2212 H HB3  B GLN   A 1 107 ? 24.856 -14.321 -11.238 0.34 30.19 ?  107 GLN   A HB3  1 
ATOM   2213 H HG2  A GLN   A 1 107 ? 22.777 -12.477 -13.649 0.66 41.25 ?  107 GLN   A HG2  1 
ATOM   2214 H HG2  B GLN   A 1 107 ? 23.187 -13.427 -13.324 0.34 34.46 ?  107 GLN   A HG2  1 
ATOM   2215 H HG3  A GLN   A 1 107 ? 23.536 -13.841 -13.940 0.66 41.25 ?  107 GLN   A HG3  1 
ATOM   2216 H HG3  B GLN   A 1 107 ? 24.209 -14.639 -13.445 0.34 34.46 ?  107 GLN   A HG3  1 
ATOM   2217 H HE21 A GLN   A 1 107 ? 20.637 -12.878 -13.820 0.66 47.71 ?  107 GLN   A HE21 1 
ATOM   2218 H HE21 B GLN   A 1 107 ? 21.253 -14.456 -13.617 0.34 38.59 ?  107 GLN   A HE21 1 
ATOM   2219 H HE22 A GLN   A 1 107 ? 19.904 -14.006 -13.180 0.66 47.71 ?  107 GLN   A HE22 1 
ATOM   2220 H HE22 B GLN   A 1 107 ? 20.725 -15.546 -12.750 0.34 38.59 ?  107 GLN   A HE22 1 
ATOM   2221 N N    A LEU   A 1 108 ? 24.809 -10.832 -9.743  0.66 18.44 ?  108 LEU   A N    1 
ATOM   2222 N N    B LEU   A 1 108 ? 24.986 -11.052 -9.625  0.34 17.60 ?  108 LEU   A N    1 
ATOM   2223 C CA   A LEU   A 1 108 ? 25.733 -10.453 -8.682  0.66 16.44 ?  108 LEU   A CA   1 
ATOM   2224 C CA   B LEU   A 1 108 ? 25.817 -10.504 -8.565  0.34 16.33 ?  108 LEU   A CA   1 
ATOM   2225 C C    A LEU   A 1 108 ? 25.039 -10.286 -7.336  0.66 14.35 ?  108 LEU   A C    1 
ATOM   2226 C C    B LEU   A 1 108 ? 25.039 -10.247 -7.283  0.34 14.82 ?  108 LEU   A C    1 
ATOM   2227 O O    A LEU   A 1 108 ? 25.722 -10.137 -6.320  0.66 14.53 ?  108 LEU   A O    1 
ATOM   2228 O O    B LEU   A 1 108 ? 25.665 -9.978  -6.253  0.34 15.10 ?  108 LEU   A O    1 
ATOM   2229 C CB   A LEU   A 1 108 ? 26.475 -9.169  -9.070  0.66 16.82 ?  108 LEU   A CB   1 
ATOM   2230 C CB   B LEU   A 1 108 ? 26.508 -9.222  -9.042  0.34 16.56 ?  108 LEU   A CB   1 
ATOM   2231 C CG   A LEU   A 1 108 ? 27.481 -9.345  -10.209 0.66 18.52 ?  108 LEU   A CG   1 
ATOM   2232 C CG   B LEU   A 1 108 ? 27.482 -9.416  -10.207 0.34 17.23 ?  108 LEU   A CG   1 
ATOM   2233 C CD1  A LEU   A 1 108 ? 27.874 -8.007  -10.820 0.66 19.26 ?  108 LEU   A CD1  1 
ATOM   2234 C CD1  B LEU   A 1 108 ? 28.147 -8.103  -10.589 0.34 17.61 ?  108 LEU   A CD1  1 
ATOM   2235 C CD2  A LEU   A 1 108 ? 28.719 -10.077 -9.716  0.66 19.94 ?  108 LEU   A CD2  1 
ATOM   2236 C CD2  B LEU   A 1 108 ? 28.530 -10.467 -9.872  0.34 17.64 ?  108 LEU   A CD2  1 
ATOM   2237 H H    A LEU   A 1 108 ? 24.656 -10.214 -10.311 0.66 22.10 ?  108 LEU   A H    1 
ATOM   2238 H H    B LEU   A 1 108 ? 24.854 -10.519 -10.280 0.34 21.09 ?  108 LEU   A H    1 
ATOM   2239 H HA   A LEU   A 1 108 ? 26.392 -11.156 -8.578  0.66 19.70 ?  108 LEU   A HA   1 
ATOM   2240 H HA   B LEU   A 1 108 ? 26.507 -11.148 -8.349  0.34 19.57 ?  108 LEU   A HA   1 
ATOM   2241 H HB2  A LEU   A 1 108 ? 25.823 -8.511  -9.355  0.66 20.16 ?  108 LEU   A HB2  1 
ATOM   2242 H HB2  B LEU   A 1 108 ? 25.830 -8.592  -9.329  0.34 19.84 ?  108 LEU   A HB2  1 
ATOM   2243 H HB3  A LEU   A 1 108 ? 26.957 -8.844  -8.297  0.66 20.16 ?  108 LEU   A HB3  1 
ATOM   2244 H HB3  B LEU   A 1 108 ? 27.010 -8.847  -8.302  0.34 19.84 ?  108 LEU   A HB3  1 
ATOM   2245 H HG   A LEU   A 1 108 ? 27.080 -9.884  -10.909 0.66 22.20 ?  108 LEU   A HG   1 
ATOM   2246 H HG   B LEU   A 1 108 ? 26.987 -9.731  -10.979 0.34 20.65 ?  108 LEU   A HG   1 
ATOM   2247 H HD11 A LEU   A 1 108 ? 28.491 -8.162  -11.556 0.66 23.08 ?  108 LEU   A HD11 1 
ATOM   2248 H HD11 B LEU   A 1 108 ? 28.748 -8.257  -11.335 0.34 21.10 ?  108 LEU   A HD11 1 
ATOM   2249 H HD12 A LEU   A 1 108 ? 27.078 -7.562  -11.146 0.66 23.08 ?  108 LEU   A HD12 1 
ATOM   2250 H HD12 B LEU   A 1 108 ? 27.462 -7.464  -10.844 0.34 21.10 ?  108 LEU   A HD12 1 
ATOM   2251 H HD13 A LEU   A 1 108 ? 28.305 -7.463  -10.141 0.66 23.08 ?  108 LEU   A HD13 1 
ATOM   2252 H HD13 B LEU   A 1 108 ? 28.645 -7.767  -9.828  0.34 21.10 ?  108 LEU   A HD13 1 
ATOM   2253 H HD21 A LEU   A 1 108 ? 29.374 -10.108 -10.431 0.66 23.90 ?  108 LEU   A HD21 1 
ATOM   2254 H HD21 B LEU   A 1 108 ? 29.253 -10.409 -10.514 0.34 21.14 ?  108 LEU   A HD21 1 
ATOM   2255 H HD22 A LEU   A 1 108 ? 29.083 -9.602  -8.953  0.66 23.90 ?  108 LEU   A HD22 1 
ATOM   2256 H HD22 B LEU   A 1 108 ? 28.866 -10.299 -8.977  0.34 21.14 ?  108 LEU   A HD22 1 
ATOM   2257 H HD23 A LEU   A 1 108 ? 28.471 -10.979 -9.457  0.66 23.90 ?  108 LEU   A HD23 1 
ATOM   2258 H HD23 B LEU   A 1 108 ? 28.120 -11.344 -9.911  0.34 21.14 ?  108 LEU   A HD23 1 
ATOM   2259 N N    . LEU   A 1 109 ? 23.704 -10.332 -7.302  1.00 13.77 ?  109 LEU   A N    1 
ATOM   2260 C CA   . LEU   A 1 109 ? 22.978 -10.194 -6.045  1.00 13.16 ?  109 LEU   A CA   1 
ATOM   2261 C C    . LEU   A 1 109 ? 23.306 -11.344 -5.096  1.00 12.41 ?  109 LEU   A C    1 
ATOM   2262 O O    . LEU   A 1 109 ? 23.439 -11.142 -3.886  1.00 13.08 ?  109 LEU   A O    1 
ATOM   2263 C CB   . LEU   A 1 109 ? 21.474 -10.108 -6.313  1.00 14.07 ?  109 LEU   A CB   1 
ATOM   2264 C CG   . LEU   A 1 109 ? 20.568 -9.808  -5.114  1.00 14.77 ?  109 LEU   A CG   1 
ATOM   2265 C CD1  . LEU   A 1 109 ? 21.017 -8.534  -4.418  1.00 14.72 ?  109 LEU   A CD1  1 
ATOM   2266 C CD2  . LEU   A 1 109 ? 19.104 -9.700  -5.550  1.00 16.02 ?  109 LEU   A CD2  1 
ATOM   2267 H H    A LEU   A 1 109 ? 23.198 -10.445 -7.988  0.66 16.50 ?  109 LEU   A H    1 
ATOM   2268 H H    B LEU   A 1 109 ? 23.215 -10.466 -7.996  0.34 16.50 ?  109 LEU   A H    1 
ATOM   2269 H HA   . LEU   A 1 109 ? 23.254 -9.368  -5.619  1.00 15.76 ?  109 LEU   A HA   1 
ATOM   2270 H HB2  . LEU   A 1 109 ? 21.323 -9.404  -6.963  1.00 16.86 ?  109 LEU   A HB2  1 
ATOM   2271 H HB3  . LEU   A 1 109 ? 21.182 -10.953 -6.680  1.00 16.86 ?  109 LEU   A HB3  1 
ATOM   2272 H HG   . LEU   A 1 109 ? 20.634 -10.530 -4.474  1.00 17.69 ?  109 LEU   A HG   1 
ATOM   2273 H HD11 . LEU   A 1 109 ? 20.340 -8.254  -3.784  1.00 17.64 ?  109 LEU   A HD11 1 
ATOM   2274 H HD12 . LEU   A 1 109 ? 21.855 -8.699  -3.956  1.00 17.64 ?  109 LEU   A HD12 1 
ATOM   2275 H HD13 . LEU   A 1 109 ? 21.146 -7.834  -5.086  1.00 17.64 ?  109 LEU   A HD13 1 
ATOM   2276 H HD21 . LEU   A 1 109 ? 18.569 -9.378  -4.805  1.00 19.20 ?  109 LEU   A HD21 1 
ATOM   2277 H HD22 . LEU   A 1 109 ? 19.034 -9.082  -6.294  1.00 19.20 ?  109 LEU   A HD22 1 
ATOM   2278 H HD23 . LEU   A 1 109 ? 18.788 -10.579 -5.823  1.00 19.20 ?  109 LEU   A HD23 1 
ATOM   2279 N N    . LYS   A 1 110 ? 23.446 -12.561 -5.621  1.00 12.78 ?  110 LYS   A N    1 
ATOM   2280 C CA   . LYS   A 1 110 ? 23.822 -13.677 -4.755  1.00 13.06 ?  110 LYS   A CA   1 
ATOM   2281 C C    . LYS   A 1 110 ? 25.202 -13.450 -4.147  1.00 12.03 ?  110 LYS   A C    1 
ATOM   2282 O O    . LYS   A 1 110 ? 25.399 -13.651 -2.945  1.00 12.37 ?  110 LYS   A O    1 
ATOM   2283 C CB   . LYS   A 1 110 ? 23.744 -15.006 -5.509  1.00 14.12 ?  110 LYS   A CB   1 
ATOM   2284 C CG   . LYS   A 1 110 ? 23.918 -16.227 -4.600  1.00 14.22 ?  110 LYS   A CG   1 
ATOM   2285 C CD   . LYS   A 1 110 ? 23.688 -17.542 -5.334  1.00 14.90 ?  110 LYS   A CD   1 
ATOM   2286 C CE   . LYS   A 1 110 ? 23.820 -18.735 -4.405  1.00 15.52 ?  110 LYS   A CE   1 
ATOM   2287 N NZ   . LYS   A 1 110 ? 22.664 -18.842 -3.475  1.00 15.31 ?  110 LYS   A NZ   1 
ATOM   2288 H H    . LYS   A 1 110 ? 23.325 -12.763 -6.443  1.00 15.31 ?  110 LYS   A H    1 
ATOM   2289 H HA   . LYS   A 1 110 ? 23.187 -13.724 -4.019  1.00 15.64 ?  110 LYS   A HA   1 
ATOM   2290 H HB2  . LYS   A 1 110 ? 22.876 -15.072 -5.938  1.00 16.92 ?  110 LYS   A HB2  1 
ATOM   2291 H HB3  . LYS   A 1 110 ? 24.447 -15.030 -6.175  1.00 16.92 ?  110 LYS   A HB3  1 
ATOM   2292 H HG2  . LYS   A 1 110 ? 24.815 -16.229 -4.240  1.00 17.03 ?  110 LYS   A HG2  1 
ATOM   2293 H HG3  . LYS   A 1 110 ? 23.269 -16.169 -3.876  1.00 17.03 ?  110 LYS   A HG3  1 
ATOM   2294 H HD2  . LYS   A 1 110 ? 22.795 -17.546 -5.711  1.00 17.86 ?  110 LYS   A HD2  1 
ATOM   2295 H HD3  . LYS   A 1 110 ? 24.350 -17.627 -6.040  1.00 17.86 ?  110 LYS   A HD3  1 
ATOM   2296 H HE2  . LYS   A 1 110 ? 23.866 -19.548 -4.933  1.00 18.60 ?  110 LYS   A HE2  1 
ATOM   2297 H HE3  . LYS   A 1 110 ? 24.630 -18.638 -3.874  1.00 18.60 ?  110 LYS   A HE3  1 
ATOM   2298 H HZ1  . LYS   A 1 110 ? 22.762 -19.547 -2.943  1.00 18.35 ?  110 LYS   A HZ1  1 
ATOM   2299 H HZ2  . LYS   A 1 110 ? 22.604 -18.107 -2.976  1.00 18.35 ?  110 LYS   A HZ2  1 
ATOM   2300 H HZ3  . LYS   A 1 110 ? 21.909 -18.934 -3.941  1.00 18.35 ?  110 LYS   A HZ3  1 
ATOM   2301 N N    . SER   A 1 111 ? 26.162 -13.003 -4.961  1.00 12.36 ?  111 SER   A N    1 
ATOM   2302 C CA   . SER   A 1 111 ? 27.490 -12.693 -4.440  1.00 12.33 ?  111 SER   A CA   1 
ATOM   2303 C C    . SER   A 1 111 ? 27.421 -11.644 -3.337  1.00 11.98 ?  111 SER   A C    1 
ATOM   2304 O O    . SER   A 1 111 ? 28.115 -11.752 -2.321  1.00 13.12 ?  111 SER   A O    1 
ATOM   2305 C CB   . SER   A 1 111 ? 28.391 -12.202 -5.575  1.00 13.70 ?  111 SER   A CB   1 
ATOM   2306 O OG   . SER   A 1 111 ? 28.465 -13.174 -6.611  1.00 15.68 ?  111 SER   A OG   1 
ATOM   2307 H H    . SER   A 1 111 ? 26.067 -12.878 -5.804  1.00 14.81 ?  111 SER   A H    1 
ATOM   2308 H HA   . SER   A 1 111 ? 27.886 -13.502 -4.071  1.00 14.77 ?  111 SER   A HA   1 
ATOM   2309 H HB2  . SER   A 1 111 ? 28.019 -11.390 -5.948  1.00 16.42 ?  111 SER   A HB2  1 
ATOM   2310 H HB3  . SER   A 1 111 ? 29.280 -12.034 -5.228  1.00 16.42 ?  111 SER   A HB3  1 
ATOM   2311 H HG   . SER   A 1 111 ? 28.979 -12.897 -7.229  1.00 18.79 ?  111 SER   A HG   1 
ATOM   2312 N N    . ALA   A 1 112 ? 26.581 -10.622 -3.521  1.00 12.31 ?  112 ALA   A N    1 
ATOM   2313 C CA   . ALA   A 1 112 ? 26.433 -9.584  -2.503  1.00 11.86 ?  112 ALA   A CA   1 
ATOM   2314 C C    . ALA   A 1 112 ? 25.944 -10.177 -1.185  1.00 11.47 ?  112 ALA   A C    1 
ATOM   2315 O O    . ALA   A 1 112 ? 26.484 -9.884  -0.115  1.00 12.17 ?  112 ALA   A O    1 
ATOM   2316 C CB   . ALA   A 1 112 ? 25.474 -8.501  -2.998  1.00 12.45 ?  112 ALA   A CB   1 
ATOM   2317 H H    . ALA   A 1 112 ? 26.098 -10.507 -4.222  1.00 14.74 ?  112 ALA   A H    1 
ATOM   2318 H HA   . ALA   A 1 112 ? 27.296 -9.167  -2.347  1.00 14.20 ?  112 ALA   A HA   1 
ATOM   2319 H HB1  . ALA   A 1 112 ? 25.405 -7.804  -2.318  1.00 14.92 ?  112 ALA   A HB1  1 
ATOM   2320 H HB2  . ALA   A 1 112 ? 25.815 -8.118  -3.820  1.00 14.92 ?  112 ALA   A HB2  1 
ATOM   2321 H HB3  . ALA   A 1 112 ? 24.600 -8.892  -3.151  1.00 14.92 ?  112 ALA   A HB3  1 
ATOM   2322 N N    . TYR   A 1 113 ? 24.913 -11.022 -1.244  1.00 11.81 ?  113 TYR   A N    1 
ATOM   2323 C CA   . TYR   A 1 113 ? 24.392 -11.628 -0.022  1.00 11.53 ?  113 TYR   A CA   1 
ATOM   2324 C C    . TYR   A 1 113 ? 25.394 -12.578 0.635   1.00 11.38 ?  113 TYR   A C    1 
ATOM   2325 O O    . TYR   A 1 113 ? 25.353 -12.763 1.855   1.00 11.99 ?  113 TYR   A O    1 
ATOM   2326 C CB   . TYR   A 1 113 ? 23.081 -12.362 -0.311  1.00 12.10 ?  113 TYR   A CB   1 
ATOM   2327 C CG   . TYR   A 1 113 ? 21.859 -11.468 -0.251  1.00 11.42 ?  113 TYR   A CG   1 
ATOM   2328 C CD1  . TYR   A 1 113 ? 21.481 -10.859 0.941   1.00 12.03 ?  113 TYR   A CD1  1 
ATOM   2329 C CD2  . TYR   A 1 113 ? 21.063 -11.259 -1.369  1.00 12.13 ?  113 TYR   A CD2  1 
ATOM   2330 C CE1  . TYR   A 1 113 ? 20.353 -10.065 1.020   1.00 13.03 ?  113 TYR   A CE1  1 
ATOM   2331 C CE2  . TYR   A 1 113 ? 19.910 -10.456 -1.294  1.00 12.52 ?  113 TYR   A CE2  1 
ATOM   2332 C CZ   . TYR   A 1 113 ? 19.572 -9.870  -0.094  1.00 12.62 ?  113 TYR   A CZ   1 
ATOM   2333 O OH   . TYR   A 1 113 ? 18.448 -9.072  0.020   1.00 13.53 ?  113 TYR   A OH   1 
ATOM   2334 H H    . TYR   A 1 113 ? 24.516 -11.260 -1.968  1.00 14.14 ?  113 TYR   A H    1 
ATOM   2335 H HA   . TYR   A 1 113 ? 24.207 -10.927 0.612   1.00 13.81 ?  113 TYR   A HA   1 
ATOM   2336 H HB2  . TYR   A 1 113 ? 23.123 -12.746 -1.202  1.00 14.49 ?  113 TYR   A HB2  1 
ATOM   2337 H HB3  . TYR   A 1 113 ? 22.970 -13.073 0.343   1.00 14.49 ?  113 TYR   A HB3  1 
ATOM   2338 H HD1  . TYR   A 1 113 ? 22.002 -10.997 1.705   1.00 14.41 ?  113 TYR   A HD1  1 
ATOM   2339 H HD2  . TYR   A 1 113 ? 21.283 -11.670 -2.174  1.00 14.52 ?  113 TYR   A HD2  1 
ATOM   2340 H HE1  . TYR   A 1 113 ? 20.128 -9.670  1.828   1.00 15.61 ?  113 TYR   A HE1  1 
ATOM   2341 H HE2  . TYR   A 1 113 ? 19.381 -10.321 -2.047  1.00 14.99 ?  113 TYR   A HE2  1 
ATOM   2342 H HH   . TYR   A 1 113 ? 18.065 -9.033  -0.729  1.00 16.21 ?  113 TYR   A HH   1 
ATOM   2343 N N    . GLU   A 1 114 ? 26.301 -13.192 -0.142  1.00 11.60 ?  114 GLU   A N    1 
ATOM   2344 C CA   . GLU   A 1 114 ? 27.296 -14.085 0.456   1.00 12.05 ?  114 GLU   A CA   1 
ATOM   2345 C C    . GLU   A 1 114 ? 28.149 -13.375 1.501   1.00 11.59 ?  114 GLU   A C    1 
ATOM   2346 O O    . GLU   A 1 114 ? 28.630 -14.006 2.452   1.00 12.04 ?  114 GLU   A O    1 
ATOM   2347 C CB   . GLU   A 1 114 ? 28.167 -14.737 -0.625  1.00 11.97 ?  114 GLU   A CB   1 
ATOM   2348 C CG   . GLU   A 1 114 ? 27.423 -15.797 -1.405  1.00 12.85 ?  114 GLU   A CG   1 
ATOM   2349 C CD   . GLU   A 1 114 ? 28.140 -16.324 -2.637  1.00 13.53 ?  114 GLU   A CD   1 
ATOM   2350 O OE1  . GLU   A 1 114 ? 29.086 -15.683 -3.133  1.00 13.76 ?  114 GLU   A OE1  1 
ATOM   2351 O OE2  . GLU   A 1 114 ? 27.715 -17.381 -3.145  1.00 14.45 -1 114 GLU   A OE2  1 
ATOM   2352 H H    . GLU   A 1 114 ? 26.358 -13.106 -1.001  1.00 13.90 ?  114 GLU   A H    1 
ATOM   2353 H HA   . GLU   A 1 114 ? 26.827 -14.799 0.907   1.00 14.44 ?  114 GLU   A HA   1 
ATOM   2354 H HB2  . GLU   A 1 114 ? 28.463 -14.055 -1.256  1.00 14.34 ?  114 GLU   A HB2  1 
ATOM   2355 H HB3  . GLU   A 1 114 ? 28.938 -15.154 -0.210  1.00 14.34 ?  114 GLU   A HB3  1 
ATOM   2356 H HG2  . GLU   A 1 114 ? 27.270 -16.555 -0.822  1.00 15.39 ?  114 GLU   A HG2  1 
ATOM   2357 H HG3  . GLU   A 1 114 ? 26.573 -15.430 -1.692  1.00 15.39 ?  114 GLU   A HG3  1 
ATOM   2358 N N    . ASN   A 1 115 ? 28.338 -12.063 1.358   1.00 11.53 ?  115 ASN   A N    1 
ATOM   2359 C CA   . ASN   A 1 115 ? 29.095 -11.319 2.359   1.00 12.41 ?  115 ASN   A CA   1 
ATOM   2360 C C    . ASN   A 1 115 ? 28.477 -11.452 3.746   1.00 12.15 ?  115 ASN   A C    1 
ATOM   2361 O O    . ASN   A 1 115 ? 29.186 -11.376 4.755   1.00 12.42 ?  115 ASN   A O    1 
ATOM   2362 C CB   . ASN   A 1 115 ? 29.201 -9.841  1.969   1.00 12.38 ?  115 ASN   A CB   1 
ATOM   2363 C CG   . ASN   A 1 115 ? 29.995 -9.637  0.702   1.00 13.10 ?  115 ASN   A CG   1 
ATOM   2364 O OD1  . ASN   A 1 115 ? 31.217 -9.761  0.710   1.00 16.28 ?  115 ASN   A OD1  1 
ATOM   2365 N ND2  . ASN   A 1 115 ? 29.322 -9.333  -0.390  1.00 12.40 ?  115 ASN   A ND2  1 
ATOM   2366 H H    . ASN   A 1 115 ? 28.032 -11.580 0.713   1.00 13.81 ?  115 ASN   A H    1 
ATOM   2367 H HA   . ASN   A 1 115 ? 29.990 -11.682 2.404   1.00 14.86 ?  115 ASN   A HA   1 
ATOM   2368 H HB2  . ASN   A 1 115 ? 28.308 -9.485  1.839   1.00 14.83 ?  115 ASN   A HB2  1 
ATOM   2369 H HB3  . ASN   A 1 115 ? 29.646 -9.360  2.688   1.00 14.83 ?  115 ASN   A HB3  1 
ATOM   2370 H HD21 . ASN   A 1 115 ? 29.740 -9.211  -1.132  1.00 14.85 ?  115 ASN   A HD21 1 
ATOM   2371 H HD22 . ASN   A 1 115 ? 28.466 -9.269  -0.363  1.00 14.85 ?  115 ASN   A HD22 1 
ATOM   2372 N N    . PHE   A 1 116 ? 27.149 -11.619 3.822   1.00 12.03 ?  116 PHE   A N    1 
ATOM   2373 C CA   . PHE   A 1 116 ? 26.489 -11.715 5.124   1.00 11.88 ?  116 PHE   A CA   1 
ATOM   2374 C C    . PHE   A 1 116 ? 26.969 -12.940 5.902   1.00 11.89 ?  116 PHE   A C    1 
ATOM   2375 O O    . PHE   A 1 116 ? 26.903 -12.958 7.135   1.00 12.51 ?  116 PHE   A O    1 
ATOM   2376 C CB   . PHE   A 1 116 ? 24.959 -11.850 4.979   1.00 11.89 ?  116 PHE   A CB   1 
ATOM   2377 C CG   . PHE   A 1 116 ? 24.207 -10.607 4.519   1.00 11.82 ?  116 PHE   A CG   1 
ATOM   2378 C CD1  . PHE   A 1 116 ? 24.776 -9.589  3.769   1.00 11.88 ?  116 PHE   A CD1  1 
ATOM   2379 C CD2  . PHE   A 1 116 ? 22.851 -10.502 4.840   1.00 12.21 ?  116 PHE   A CD2  1 
ATOM   2380 C CE1  . PHE   A 1 116 ? 24.007 -8.509  3.357   1.00 12.68 ?  116 PHE   A CE1  1 
ATOM   2381 C CE2  . PHE   A 1 116 ? 22.089 -9.423  4.444   1.00 12.56 ?  116 PHE   A CE2  1 
ATOM   2382 C CZ   . PHE   A 1 116 ? 22.657 -8.434  3.698   1.00 12.48 ?  116 PHE   A CZ   1 
ATOM   2383 H H    . PHE   A 1 116 ? 26.616 -11.670 3.148   1.00 14.41 ?  116 PHE   A H    1 
ATOM   2384 H HA   . PHE   A 1 116 ? 26.678 -10.918 5.647   1.00 14.23 ?  116 PHE   A HA   1 
ATOM   2385 H HB2  . PHE   A 1 116 ? 24.777 -12.550 4.334   1.00 14.24 ?  116 PHE   A HB2  1 
ATOM   2386 H HB3  . PHE   A 1 116 ? 24.595 -12.107 5.842   1.00 14.24 ?  116 PHE   A HB3  1 
ATOM   2387 H HD1  . PHE   A 1 116 ? 25.672 -9.646  3.532   1.00 14.23 ?  116 PHE   A HD1  1 
ATOM   2388 H HD2  . PHE   A 1 116 ? 22.450 -11.182 5.343   1.00 14.63 ?  116 PHE   A HD2  1 
ATOM   2389 H HE1  . PHE   A 1 116 ? 24.402 -7.830  2.859   1.00 15.18 ?  116 PHE   A HE1  1 
ATOM   2390 H HE2  . PHE   A 1 116 ? 21.186 -9.380  4.678   1.00 15.04 ?  116 PHE   A HE2  1 
ATOM   2391 H HZ   . PHE   A 1 116 ? 22.152 -7.697  3.434   1.00 14.95 ?  116 PHE   A HZ   1 
ATOM   2392 N N    . ASN   A 1 117 ? 27.423 -13.980 5.201   1.00 12.01 ?  117 ASN   A N    1 
ATOM   2393 C CA   . ASN   A 1 117 ? 27.783 -15.224 5.873   1.00 12.48 ?  117 ASN   A CA   1 
ATOM   2394 C C    . ASN   A 1 117 ? 29.043 -15.111 6.713   1.00 13.20 ?  117 ASN   A C    1 
ATOM   2395 O O    . ASN   A 1 117 ? 29.330 -16.028 7.492   1.00 13.99 ?  117 ASN   A O    1 
ATOM   2396 C CB   . ASN   A 1 117 ? 27.911 -16.350 4.852   1.00 13.07 ?  117 ASN   A CB   1 
ATOM   2397 C CG   . ASN   A 1 117 ? 26.560 -16.756 4.308   1.00 13.52 ?  117 ASN   A CG   1 
ATOM   2398 O OD1  . ASN   A 1 117 ? 25.575 -16.777 5.047   1.00 14.14 ?  117 ASN   A OD1  1 
ATOM   2399 N ND2  . ASN   A 1 117 ? 26.493 -17.038 3.019   1.00 13.09 ?  117 ASN   A ND2  1 
ATOM   2400 H H    . ASN   A 1 117 ? 27.506 -13.994 4.343   1.00 14.38 ?  117 ASN   A H    1 
ATOM   2401 H HA   . ASN   A 1 117 ? 27.055 -15.459 6.471   1.00 14.94 ?  117 ASN   A HA   1 
ATOM   2402 H HB2  . ASN   A 1 117 ? 28.462 -16.048 4.111   1.00 15.65 ?  117 ASN   A HB2  1 
ATOM   2403 H HB3  . ASN   A 1 117 ? 28.310 -17.119 5.279   1.00 15.65 ?  117 ASN   A HB3  1 
ATOM   2404 H HD21 . ASN   A 1 117 ? 25.746 -17.267 2.672   1.00 15.68 ?  117 ASN   A HD21 1 
ATOM   2405 H HD22 . ASN   A 1 117 ? 27.205 -17.001 2.532   1.00 15.68 ?  117 ASN   A HD22 1 
ATOM   2406 N N    . GLN   A 1 118 ? 29.788 -14.012 6.592   1.00 13.46 ?  118 GLN   A N    1 
ATOM   2407 C CA   . GLN   A 1 118 ? 30.955 -13.780 7.432   1.00 13.85 ?  118 GLN   A CA   1 
ATOM   2408 C C    . GLN   A 1 118 ? 30.603 -13.210 8.799   1.00 13.40 ?  118 GLN   A C    1 
ATOM   2409 O O    . GLN   A 1 118 ? 31.516 -12.929 9.587   1.00 14.77 ?  118 GLN   A O    1 
ATOM   2410 C CB   . GLN   A 1 118 ? 31.955 -12.875 6.714   1.00 14.15 ?  118 GLN   A CB   1 
ATOM   2411 C CG   . GLN   A 1 118 ? 32.438 -13.440 5.394   1.00 13.88 ?  118 GLN   A CG   1 
ATOM   2412 C CD   . GLN   A 1 118 ? 33.288 -14.689 5.568   1.00 14.03 ?  118 GLN   A CD   1 
ATOM   2413 O OE1  . GLN   A 1 118 ? 34.144 -14.752 6.459   1.00 15.36 ?  118 GLN   A OE1  1 
ATOM   2414 N NE2  . GLN   A 1 118 ? 33.040 -15.698 4.731   1.00 14.60 ?  118 GLN   A NE2  1 
ATOM   2415 H H    . GLN   A 1 118 ? 29.626 -13.369 6.033   1.00 16.12 ?  118 GLN   A H    1 
ATOM   2416 H HA   . GLN   A 1 118 ? 31.383 -14.638 7.580   1.00 16.59 ?  118 GLN   A HA   1 
ATOM   2417 H HB2  . GLN   A 1 118 ? 31.531 -12.021 6.540   1.00 16.95 ?  118 GLN   A HB2  1 
ATOM   2418 H HB3  . GLN   A 1 118 ? 32.725 -12.751 7.291   1.00 16.95 ?  118 GLN   A HB3  1 
ATOM   2419 H HG2  . GLN   A 1 118 ? 31.675 -13.667 4.843   1.00 16.63 ?  118 GLN   A HG2  1 
ATOM   2420 H HG3  . GLN   A 1 118 ? 32.984 -12.772 4.948   1.00 16.63 ?  118 GLN   A HG3  1 
ATOM   2421 H HE21 . GLN   A 1 118 ? 32.427 -15.616 4.128   1.00 17.49 ?  118 GLN   A HE21 1 
ATOM   2422 H HE22 . GLN   A 1 118 ? 33.483 -16.428 4.794   1.00 17.49 ?  118 GLN   A HE22 1 
ATOM   2423 N N    . HIS   A 1 119 ? 29.311 -13.043 9.102   1.00 13.00 ?  119 HIS   A N    1 
ATOM   2424 C CA   . HIS   A 1 119 ? 28.856 -12.433 10.346  1.00 13.65 ?  119 HIS   A CA   1 
ATOM   2425 C C    . HIS   A 1 119 ? 27.715 -13.250 10.927  1.00 14.02 ?  119 HIS   A C    1 
ATOM   2426 O O    . HIS   A 1 119 ? 26.768 -13.588 10.211  1.00 14.52 ?  119 HIS   A O    1 
ATOM   2427 C CB   . HIS   A 1 119 ? 28.403 -10.997 10.078  1.00 14.04 ?  119 HIS   A CB   1 
ATOM   2428 C CG   . HIS   A 1 119 ? 29.495 -10.180 9.483   1.00 14.86 ?  119 HIS   A CG   1 
ATOM   2429 N ND1  . HIS   A 1 119 ? 30.460 -9.567  10.249  1.00 17.14 ?  119 HIS   A ND1  1 
ATOM   2430 C CD2  . HIS   A 1 119 ? 29.845 -9.979  8.194   1.00 15.60 ?  119 HIS   A CD2  1 
ATOM   2431 C CE1  . HIS   A 1 119 ? 31.333 -8.977  9.453   1.00 16.96 ?  119 HIS   A CE1  1 
ATOM   2432 N NE2  . HIS   A 1 119 ? 30.995 -9.227  8.201   1.00 16.85 ?  119 HIS   A NE2  1 
ATOM   2433 H H    . HIS   A 1 119 ? 28.658 -13.295 8.590   1.00 15.57 ?  119 HIS   A H    1 
ATOM   2434 H HA   . HIS   A 1 119 ? 29.581 -12.420 10.985  1.00 16.35 ?  119 HIS   A HA   1 
ATOM   2435 H HB2  . HIS   A 1 119 ? 27.653 -11.011 9.460   1.00 16.82 ?  119 HIS   A HB2  1 
ATOM   2436 H HB3  . HIS   A 1 119 ? 28.135 -10.591 10.918  1.00 16.82 ?  119 HIS   A HB3  1 
ATOM   2437 H HD1  . HIS   A 1 119 ? 30.473 -9.554  11.110  1.00 20.54 ?  119 HIS   A HD1  1 
ATOM   2438 H HD2  . HIS   A 1 119 ? 29.396 -10.297 7.441   1.00 18.69 ?  119 HIS   A HD2  1 
ATOM   2439 H HE1  . HIS   A 1 119 ? 32.063 -8.475  9.731   1.00 20.32 ?  119 HIS   A HE1  1 
ATOM   2440 N N    . GLU   A 1 120 ? 27.803 -13.546 12.227  1.00 15.17 ?  120 GLU   A N    1 
ATOM   2441 C CA   . GLU   A 1 120 ? 26.850 -14.464 12.849  1.00 17.15 ?  120 GLU   A CA   1 
ATOM   2442 C C    . GLU   A 1 120 ? 25.432 -13.902 12.871  1.00 15.49 ?  120 GLU   A C    1 
ATOM   2443 O O    . GLU   A 1 120 ? 24.459 -14.661 12.746  1.00 16.21 ?  120 GLU   A O    1 
ATOM   2444 C CB   . GLU   A 1 120 ? 27.310 -14.809 14.266  1.00 21.33 ?  120 GLU   A CB   1 
ATOM   2445 C CG   . GLU   A 1 120 ? 28.513 -15.731 14.321  1.00 27.81 ?  120 GLU   A CG   1 
ATOM   2446 C CD   . GLU   A 1 120 ? 28.578 -16.522 15.610  1.00 33.57 ?  120 GLU   A CD   1 
ATOM   2447 O OE1  . GLU   A 1 120 ? 28.266 -15.948 16.675  1.00 35.34 ?  120 GLU   A OE1  1 
ATOM   2448 O OE2  . GLU   A 1 120 ? 28.932 -17.720 15.559  1.00 36.02 -1 120 GLU   A OE2  1 
ATOM   2449 H H    . GLU   A 1 120 ? 28.411 -13.238 12.761  1.00 18.18 ?  120 GLU   A H    1 
ATOM   2450 H HA   . GLU   A 1 120 ? 26.838 -15.286 12.340  1.00 20.55 ?  120 GLU   A HA   1 
ATOM   2451 H HB2  . GLU   A 1 120 ? 27.545 -13.994 14.735  1.00 25.57 ?  120 GLU   A HB2  1 
ATOM   2452 H HB3  . GLU   A 1 120 ? 26.579 -15.253 14.733  1.00 25.57 ?  120 GLU   A HB3  1 
ATOM   2453 H HG2  . GLU   A 1 120 ? 28.475 -16.349 13.575  1.00 33.35 ?  120 GLU   A HG2  1 
ATOM   2454 H HG3  . GLU   A 1 120 ? 29.322 -15.203 14.280  1.00 33.35 ?  120 GLU   A HG3  1 
ATOM   2455 N N    . VAL   A 1 121 ? 25.295 -12.589 13.069  1.00 14.83 ?  121 VAL   A N    1 
ATOM   2456 C CA   . VAL   A 1 121 ? 23.995 -11.927 13.173  1.00 15.01 ?  121 VAL   A CA   1 
ATOM   2457 C C    . VAL   A 1 121 ? 24.099 -10.549 12.528  1.00 13.77 ?  121 VAL   A C    1 
ATOM   2458 O O    . VAL   A 1 121 ? 25.065 -9.818  12.769  1.00 14.43 ?  121 VAL   A O    1 
ATOM   2459 C CB   . VAL   A 1 121 ? 23.537 -11.779 14.642  1.00 18.17 ?  121 VAL   A CB   1 
ATOM   2460 C CG1  . VAL   A 1 121 ? 22.159 -11.141 14.708  1.00 18.64 ?  121 VAL   A CG1  1 
ATOM   2461 C CG2  . VAL   A 1 121 ? 23.526 -13.108 15.374  1.00 20.77 ?  121 VAL   A CG2  1 
ATOM   2462 H H    . VAL   A 1 121 ? 25.960 -12.047 13.156  1.00 17.77 ?  121 VAL   A H    1 
ATOM   2463 H HA   . VAL   A 1 121 ? 23.333 -12.452 12.699  1.00 17.98 ?  121 VAL   A HA   1 
ATOM   2464 H HB   . VAL   A 1 121 ? 24.153 -11.196 15.109  1.00 21.78 ?  121 VAL   A HB   1 
ATOM   2465 H HG11 . VAL   A 1 121 ? 21.814 -11.213 15.616  1.00 22.34 ?  121 VAL   A HG11 1 
ATOM   2466 H HG12 . VAL   A 1 121 ? 22.223 -10.207 14.458  1.00 22.34 ?  121 VAL   A HG12 1 
ATOM   2467 H HG13 . VAL   A 1 121 ? 21.561 -11.607 14.099  1.00 22.34 ?  121 VAL   A HG13 1 
ATOM   2468 H HG21 . VAL   A 1 121 ? 23.174 -12.974 16.273  1.00 24.90 ?  121 VAL   A HG21 1 
ATOM   2469 H HG22 . VAL   A 1 121 ? 22.956 -13.731 14.894  1.00 24.90 ?  121 VAL   A HG22 1 
ATOM   2470 H HG23 . VAL   A 1 121 ? 24.428 -13.454 15.424  1.00 24.90 ?  121 VAL   A HG23 1 
ATOM   2471 N N    . LEU   A 1 122 ? 23.092 -10.178 11.734  1.00 12.90 ?  122 LEU   A N    1 
ATOM   2472 C CA   . LEU   A 1 122 ? 23.089 -8.879  11.071  1.00 12.56 ?  122 LEU   A CA   1 
ATOM   2473 C C    . LEU   A 1 122 ? 21.692 -8.285  11.028  1.00 12.91 ?  122 LEU   A C    1 
ATOM   2474 O O    . LEU   A 1 122 ? 20.704 -9.006  10.888  1.00 13.72 ?  122 LEU   A O    1 
ATOM   2475 C CB   . LEU   A 1 122 ? 23.529 -8.983  9.609   1.00 14.22 ?  122 LEU   A CB   1 
ATOM   2476 C CG   . LEU   A 1 122 ? 24.742 -9.831  9.265   1.00 14.22 ?  122 LEU   A CG   1 
ATOM   2477 C CD1  . LEU   A 1 122 ? 24.335 -11.297 9.062   1.00 14.95 ?  122 LEU   A CD1  1 
ATOM   2478 C CD2  . LEU   A 1 122 ? 25.438 -9.267  8.031   1.00 13.54 ?  122 LEU   A CD2  1 
ATOM   2479 H H    . LEU   A 1 122 ? 22.403 -10.666 11.565  1.00 15.45 ?  122 LEU   A H    1 
ATOM   2480 H HA   . LEU   A 1 122 ? 23.686 -8.267  11.539  1.00 15.04 ?  122 LEU   A HA   1 
ATOM   2481 H HB2  . LEU   A 1 122 ? 22.796 -9.344  9.101   1.00 17.03 ?  122 LEU   A HB2  1 
ATOM   2482 H HB3  . LEU   A 1 122 ? 23.733 -8.090  9.295   1.00 17.03 ?  122 LEU   A HB3  1 
ATOM   2483 H HG   . LEU   A 1 122 ? 25.386 -9.805  9.996   1.00 17.04 ?  122 LEU   A HG   1 
ATOM   2484 H HD11 . LEU   A 1 122 ? 25.107 -11.806 8.762   1.00 17.92 ?  122 LEU   A HD11 1 
ATOM   2485 H HD12 . LEU   A 1 122 ? 24.013 -11.656 9.902   1.00 17.92 ?  122 LEU   A HD12 1 
ATOM   2486 H HD13 . LEU   A 1 122 ? 23.636 -11.338 8.392   1.00 17.92 ?  122 LEU   A HD13 1 
ATOM   2487 H HD21 . LEU   A 1 122 ? 26.185 -9.841  7.786   1.00 16.22 ?  122 LEU   A HD21 1 
ATOM   2488 H HD22 . LEU   A 1 122 ? 24.801 -9.231  7.299   1.00 16.22 ?  122 LEU   A HD22 1 
ATOM   2489 H HD23 . LEU   A 1 122 ? 25.763 -8.375  8.229   1.00 16.22 ?  122 LEU   A HD23 1 
ATOM   2490 N N    A LEU   A 1 123 ? 21.625 -6.958  11.133  0.66 12.26 ?  123 LEU   A N    1 
ATOM   2491 N N    B LEU   A 1 123 ? 21.637 -6.962  11.167  0.34 12.60 ?  123 LEU   A N    1 
ATOM   2492 C CA   A LEU   A 1 123 ? 20.455 -6.169  10.749  0.66 11.82 ?  123 LEU   A CA   1 
ATOM   2493 C CA   B LEU   A 1 123 ? 20.459 -6.163  10.857  0.34 12.57 ?  123 LEU   A CA   1 
ATOM   2494 C C    A LEU   A 1 123 ? 20.697 -5.656  9.336   0.66 11.23 ?  123 LEU   A C    1 
ATOM   2495 C C    B LEU   A 1 123 ? 20.680 -5.580  9.468   0.34 11.89 ?  123 LEU   A C    1 
ATOM   2496 O O    A LEU   A 1 123 ? 21.784 -5.143  9.052   0.66 11.44 ?  123 LEU   A O    1 
ATOM   2497 O O    B LEU   A 1 123 ? 21.608 -4.788  9.275   0.34 11.35 ?  123 LEU   A O    1 
ATOM   2498 C CB   A LEU   A 1 123 ? 20.302 -4.986  11.704  0.66 12.54 ?  123 LEU   A CB   1 
ATOM   2499 C CB   B LEU   A 1 123 ? 20.309 -5.041  11.884  0.34 13.43 ?  123 LEU   A CB   1 
ATOM   2500 C CG   A LEU   A 1 123 ? 19.259 -3.921  11.358  0.66 13.01 ?  123 LEU   A CG   1 
ATOM   2501 C CG   B LEU   A 1 123 ? 19.267 -3.966  11.566  0.34 14.16 ?  123 LEU   A CG   1 
ATOM   2502 C CD1  A LEU   A 1 123 ? 17.845 -4.492  11.375  0.66 13.66 ?  123 LEU   A CD1  1 
ATOM   2503 C CD1  B LEU   A 1 123 ? 17.863 -4.561  11.538  0.34 14.88 ?  123 LEU   A CD1  1 
ATOM   2504 C CD2  A LEU   A 1 123 ? 19.382 -2.740  12.316  0.66 13.20 ?  123 LEU   A CD2  1 
ATOM   2505 C CD2  B LEU   A 1 123 ? 19.359 -2.827  12.569  0.34 14.93 ?  123 LEU   A CD2  1 
ATOM   2506 H H    A LEU   A 1 123 ? 22.278 -6.475  11.436  0.66 14.68 ?  123 LEU   A H    1 
ATOM   2507 H H    B LEU   A 1 123 ? 22.303 -6.485  11.444  0.34 15.09 ?  123 LEU   A H    1 
ATOM   2508 H HA   A LEU   A 1 123 ? 19.660 -6.720  10.770  0.66 14.15 ?  123 LEU   A HA   1 
ATOM   2509 H HA   B LEU   A 1 123 ? 19.665 -6.712  10.858  0.34 15.05 ?  123 LEU   A HA   1 
ATOM   2510 H HB2  A LEU   A 1 123 ? 20.066 -5.335  12.578  0.66 15.01 ?  123 LEU   A HB2  1 
ATOM   2511 H HB2  B LEU   A 1 123 ? 20.063 -5.438  12.735  0.34 16.09 ?  123 LEU   A HB2  1 
ATOM   2512 H HB3  A LEU   A 1 123 ? 21.158 -4.535  11.764  0.66 15.01 ?  123 LEU   A HB3  1 
ATOM   2513 H HB3  B LEU   A 1 123 ? 21.166 -4.593  11.978  0.34 16.09 ?  123 LEU   A HB3  1 
ATOM   2514 H HG   A LEU   A 1 123 ? 19.433 -3.586  10.462  0.66 15.58 ?  123 LEU   A HG   1 
ATOM   2515 H HG   B LEU   A 1 123 ? 19.449 -3.595  10.689  0.34 16.97 ?  123 LEU   A HG   1 
ATOM   2516 H HD11 A LEU   A 1 123 ? 17.215 -3.787  11.161  0.66 16.36 ?  123 LEU   A HD11 1 
ATOM   2517 H HD11 B LEU   A 1 123 ? 17.223 -3.853  11.364  0.34 17.83 ?  123 LEU   A HD11 1 
ATOM   2518 H HD12 A LEU   A 1 123 ? 17.782 -5.202  10.717  0.66 16.36 ?  123 LEU   A HD12 1 
ATOM   2519 H HD12 B LEU   A 1 123 ? 17.816 -5.228  10.833  0.34 17.83 ?  123 LEU   A HD12 1 
ATOM   2520 H HD13 A LEU   A 1 123 ? 17.658 -4.845  12.260  0.66 16.36 ?  123 LEU   A HD13 1 
ATOM   2521 H HD13 B LEU   A 1 123 ? 17.676 -4.973  12.396  0.34 17.83 ?  123 LEU   A HD13 1 
ATOM   2522 H HD21 A LEU   A 1 123 ? 18.717 -2.075  12.087  0.66 15.82 ?  123 LEU   A HD21 1 
ATOM   2523 H HD21 B LEU   A 1 123 ? 18.692 -2.160  12.349  0.34 17.89 ?  123 LEU   A HD21 1 
ATOM   2524 H HD22 A LEU   A 1 123 ? 19.236 -3.058  13.223  0.66 15.82 ?  123 LEU   A HD22 1 
ATOM   2525 H HD22 B LEU   A 1 123 ? 19.199 -3.179  13.458  0.34 17.89 ?  123 LEU   A HD22 1 
ATOM   2526 H HD23 A LEU   A 1 123 ? 20.272 -2.363  12.240  0.66 15.82 ?  123 LEU   A HD23 1 
ATOM   2527 H HD23 B LEU   A 1 123 ? 20.247 -2.439  12.521  0.34 17.89 ?  123 LEU   A HD23 1 
ATOM   2528 N N    A ALA   A 1 124 ? 19.699 -5.766  8.453   0.66 10.06 ?  124 ALA   A N    1 
ATOM   2529 N N    B ALA   A 1 124 ? 19.854 -5.972  8.505   0.34 11.53 ?  124 ALA   A N    1 
ATOM   2530 C CA   A ALA   A 1 124 ? 19.984 -5.502  7.047   0.66 10.11 ?  124 ALA   A CA   1 
ATOM   2531 C CA   B ALA   A 1 124 ? 20.109 -5.672  7.105   0.34 12.06 ?  124 ALA   A CA   1 
ATOM   2532 C C    A ALA   A 1 124 ? 18.740 -5.075  6.274   0.66 10.46 ?  124 ALA   A C    1 
ATOM   2533 C C    B ALA   A 1 124 ? 18.880 -5.120  6.400   0.34 12.34 ?  124 ALA   A C    1 
ATOM   2534 O O    A ALA   A 1 124 ? 17.620 -5.489  6.604   0.66 10.60 ?  124 ALA   A O    1 
ATOM   2535 O O    B ALA   A 1 124 ? 17.745 -5.316  6.851   0.34 12.87 ?  124 ALA   A O    1 
ATOM   2536 C CB   A ALA   A 1 124 ? 20.599 -6.733  6.379   0.66 10.61 ?  124 ALA   A CB   1 
ATOM   2537 C CB   B ALA   A 1 124 ? 20.587 -6.921  6.352   0.34 12.47 ?  124 ALA   A CB   1 
ATOM   2538 H H    A ALA   A 1 124 ? 18.882 -5.965  8.645   0.66 12.04 ?  124 ALA   A H    1 
ATOM   2539 H H    B ALA   A 1 124 ? 19.127 -6.416  8.638   0.34 13.80 ?  124 ALA   A H    1 
ATOM   2540 H HA   A ALA   A 1 124 ? 20.632 -4.783  7.007   0.66 12.10 ?  124 ALA   A HA   1 
ATOM   2541 H HA   B ALA   A 1 124 ? 20.814 -5.011  7.057   0.34 14.44 ?  124 ALA   A HA   1 
ATOM   2542 H HB1  A ALA   A 1 124 ? 20.781 -6.529  5.449   0.66 12.70 ?  124 ALA   A HB1  1 
ATOM   2543 H HB1  B ALA   A 1 124 ? 20.753 -6.685  5.424   0.34 14.94 ?  124 ALA   A HB1  1 
ATOM   2544 H HB2  A ALA   A 1 124 ? 21.430 -6.957  6.835   0.66 12.70 ?  124 ALA   A HB2  1 
ATOM   2545 H HB2  B ALA   A 1 124 ? 21.405 -7.245  6.760   0.34 14.94 ?  124 ALA   A HB2  1 
ATOM   2546 H HB3  A ALA   A 1 124 ? 19.980 -7.473  6.445   0.66 12.70 ?  124 ALA   A HB3  1 
ATOM   2547 H HB3  B ALA   A 1 124 ? 19.899 -7.602  6.401   0.34 14.94 ?  124 ALA   A HB3  1 
ATOM   2548 N N    A PRO   A 1 125 ? 18.924 -4.313  5.201   0.66 10.68 ?  125 PRO   A N    1 
ATOM   2549 N N    B PRO   A 1 125 ? 19.083 -4.425  5.272   0.34 11.56 ?  125 PRO   A N    1 
ATOM   2550 C CA   A PRO   A 1 125 ? 17.874 -4.096  4.209   0.66 10.97 ?  125 PRO   A CA   1 
ATOM   2551 C CA   B PRO   A 1 125 ? 17.967 -4.059  4.397   0.34 11.49 ?  125 PRO   A CA   1 
ATOM   2552 C C    A PRO   A 1 125 ? 17.946 -5.188  3.145   0.66 11.48 ?  125 PRO   A C    1 
ATOM   2553 C C    B PRO   A 1 125 ? 17.895 -5.034  3.234   0.34 12.26 ?  125 PRO   A C    1 
ATOM   2554 O O    A PRO   A 1 125 ? 18.915 -5.945  3.064   0.66 11.52 ?  125 PRO   A O    1 
ATOM   2555 O O    B PRO   A 1 125 ? 18.774 -5.893  3.104   0.34 12.68 ?  125 PRO   A O    1 
ATOM   2556 C CB   A PRO   A 1 125 ? 18.313 -2.760  3.594   0.66 11.32 ?  125 PRO   A CB   1 
ATOM   2557 C CB   B PRO   A 1 125 ? 18.382 -2.668  3.911   0.34 11.74 ?  125 PRO   A CB   1 
ATOM   2558 C CG   A PRO   A 1 125 ? 19.809 -2.926  3.513   0.66 11.72 ?  125 PRO   A CG   1 
ATOM   2559 C CG   B PRO   A 1 125 ? 19.890 -2.804  3.760   0.34 11.96 ?  125 PRO   A CG   1 
ATOM   2560 C CD   A PRO   A 1 125 ? 20.180 -3.642  4.804   0.66 11.39 ?  125 PRO   A CD   1 
ATOM   2561 C CD   B PRO   A 1 125 ? 20.348 -3.830  4.797   0.34 11.61 ?  125 PRO   A CD   1 
ATOM   2562 H HA   A PRO   A 1 125 ? 16.986 -4.041  4.606   0.66 13.13 ?  125 PRO   A HA   1 
ATOM   2563 H HA   B PRO   A 1 125 ? 17.121 -4.025  4.874   0.34 13.76 ?  125 PRO   A HA   1 
ATOM   2564 H HB2  A PRO   A 1 125 ? 17.917 -2.654  2.717   0.66 13.56 ?  125 PRO   A HB2  1 
ATOM   2565 H HB2  B PRO   A 1 125 ? 17.959 -2.470  3.058   0.34 14.06 ?  125 PRO   A HB2  1 
ATOM   2566 H HB3  A PRO   A 1 125 ? 18.069 -2.031  4.185   0.66 13.56 ?  125 PRO   A HB3  1 
ATOM   2567 H HB3  B PRO   A 1 125 ? 18.152 -2.000  4.577   0.34 14.06 ?  125 PRO   A HB3  1 
ATOM   2568 H HG2  A PRO   A 1 125 ? 20.044 -3.468  2.740   0.66 14.04 ?  125 PRO   A HG2  1 
ATOM   2569 H HG2  B PRO   A 1 125 ? 20.097 -3.113  2.864   0.34 14.32 ?  125 PRO   A HG2  1 
ATOM   2570 H HG3  A PRO   A 1 125 ? 20.236 -2.057  3.464   0.66 14.04 ?  125 PRO   A HG3  1 
ATOM   2571 H HG3  B PRO   A 1 125 ? 20.309 -1.945  3.926   0.34 14.32 ?  125 PRO   A HG3  1 
ATOM   2572 H HD2  A PRO   A 1 125 ? 20.876 -4.297  4.650   0.66 13.64 ?  125 PRO   A HD2  1 
ATOM   2573 H HD2  B PRO   A 1 125 ? 20.910 -4.505  4.380   0.34 13.91 ?  125 PRO   A HD2  1 
ATOM   2574 H HD3  A PRO   A 1 125 ? 20.441 -3.000  5.487   0.66 13.64 ?  125 PRO   A HD3  1 
ATOM   2575 H HD3  B PRO   A 1 125 ? 20.810 -3.387  5.526   0.34 13.91 ?  125 PRO   A HD3  1 
ATOM   2576 N N    A LEU   A 1 126 ? 16.915 -5.235  2.306   0.66 11.66 ?  126 LEU   A N    1 
ATOM   2577 N N    B LEU   A 1 126 ? 16.889 -4.913  2.372   0.34 12.72 ?  126 LEU   A N    1 
ATOM   2578 C CA   A LEU   A 1 126 ? 16.952 -6.079  1.119   0.66 12.21 ?  126 LEU   A CA   1 
ATOM   2579 C CA   B LEU   A 1 126 ? 16.833 -5.726  1.163   0.34 12.74 ?  126 LEU   A CA   1 
ATOM   2580 C C    A LEU   A 1 126 ? 17.885 -5.473  0.079   0.66 12.04 ?  126 LEU   A C    1 
ATOM   2581 C C    B LEU   A 1 126 ? 17.788 -5.142  0.128   0.34 12.75 ?  126 LEU   A C    1 
ATOM   2582 O O    A LEU   A 1 126 ? 17.663 -4.358  -0.405  0.66 12.90 ?  126 LEU   A O    1 
ATOM   2583 O O    B LEU   A 1 126 ? 17.612 -4.001  -0.310  0.34 14.06 ?  126 LEU   A O    1 
ATOM   2584 C CB   A LEU   A 1 126 ? 15.552 -6.251  0.546   0.66 13.37 ?  126 LEU   A CB   1 
ATOM   2585 C CB   B LEU   A 1 126 ? 15.411 -5.753  0.609   0.34 13.98 ?  126 LEU   A CB   1 
ATOM   2586 C CG   A LEU   A 1 126 ? 14.650 -7.216  1.314   0.66 14.40 ?  126 LEU   A CG   1 
ATOM   2587 C CG   B LEU   A 1 126 ? 14.476 -6.826  1.158   0.34 14.90 ?  126 LEU   A CG   1 
ATOM   2588 C CD1  A LEU   A 1 126 ? 13.236 -7.116  0.788   0.66 14.88 ?  126 LEU   A CD1  1 
ATOM   2589 C CD1  B LEU   A 1 126 ? 13.081 -6.579  0.636   0.34 15.09 ?  126 LEU   A CD1  1 
ATOM   2590 C CD2  A LEU   A 1 126 ? 15.163 -8.645  1.210   0.66 13.63 ?  126 LEU   A CD2  1 
ATOM   2591 C CD2  B LEU   A 1 126 ? 14.948 -8.221  0.766   0.34 15.14 ?  126 LEU   A CD2  1 
ATOM   2592 H H    A LEU   A 1 126 ? 16.189 -4.785  2.396   0.66 13.96 ?  126 LEU   A H    1 
ATOM   2593 H H    B LEU   A 1 126 ? 16.229 -4.363  2.461   0.34 15.24 ?  126 LEU   A H    1 
ATOM   2594 H HA   A LEU   A 1 126 ? 17.296 -6.952  1.354   0.66 14.63 ?  126 LEU   A HA   1 
ATOM   2595 H HA   B LEU   A 1 126 ? 17.106 -6.635  1.368   0.34 15.27 ?  126 LEU   A HA   1 
ATOM   2596 H HB2  A LEU   A 1 126 ? 15.112 -5.384  0.541   0.66 16.02 ?  126 LEU   A HB2  1 
ATOM   2597 H HB2  B LEU   A 1 126 ? 14.997 -4.896  0.794   0.34 16.75 ?  126 LEU   A HB2  1 
ATOM   2598 H HB3  A LEU   A 1 126 ? 15.625 -6.579  -0.364  0.66 16.02 ?  126 LEU   A HB3  1 
ATOM   2599 H HB3  B LEU   A 1 126 ? 15.461 -5.885  -0.350  0.34 16.75 ?  126 LEU   A HB3  1 
ATOM   2600 H HG   A LEU   A 1 126 ? 14.642 -6.967  2.250   0.66 17.25 ?  126 LEU   A HG   1 
ATOM   2601 H HG   B LEU   A 1 126 ? 14.453 -6.776  2.127   0.34 17.85 ?  126 LEU   A HG   1 
ATOM   2602 H HD11 A LEU   A 1 126 ? 12.673 -7.736  1.278   0.66 17.82 ?  126 LEU   A HD11 1 
ATOM   2603 H HD11 B LEU   A 1 126 ? 12.489 -7.267  0.977   0.34 18.08 ?  126 LEU   A HD11 1 
ATOM   2604 H HD12 A LEU   A 1 126 ? 12.917 -6.209  0.911   0.66 17.82 ?  126 LEU   A HD12 1 
ATOM   2605 H HD12 B LEU   A 1 126 ? 12.785 -5.706  0.934   0.34 18.08 ?  126 LEU   A HD12 1 
ATOM   2606 H HD13 A LEU   A 1 126 ? 13.233 -7.344  -0.156  0.66 17.82 ?  126 LEU   A HD13 1 
ATOM   2607 H HD13 B LEU   A 1 126 ? 13.100 -6.610  -0.334  0.34 18.08 ?  126 LEU   A HD13 1 
ATOM   2608 H HD21 A LEU   A 1 126 ? 14.493 -9.250  1.559   0.66 16.32 ?  126 LEU   A HD21 1 
ATOM   2609 H HD21 B LEU   A 1 126 ? 14.261 -8.865  0.994   0.34 18.14 ?  126 LEU   A HD21 1 
ATOM   2610 H HD22 A LEU   A 1 126 ? 15.344 -8.851  0.278   0.66 16.32 ?  126 LEU   A HD22 1 
ATOM   2611 H HD22 B LEU   A 1 126 ? 15.113 -8.239  -0.191  0.34 18.14 ?  126 LEU   A HD22 1 
ATOM   2612 H HD23 A LEU   A 1 126 ? 15.983 -8.727  1.727   0.66 16.32 ?  126 LEU   A HD23 1 
ATOM   2613 H HD23 B LEU   A 1 126 ? 15.766 -8.426  1.245   0.34 18.14 ?  126 LEU   A HD23 1 
ATOM   2614 N N    A LEU   A 1 127 ? 18.933 -6.211  -0.269  0.66 12.12 ?  127 LEU   A N    1 
ATOM   2615 N N    B LEU   A 1 127 ? 18.799 -5.914  -0.265  0.34 12.42 ?  127 LEU   A N    1 
ATOM   2616 C CA   A LEU   A 1 127 ? 19.922 -5.710  -1.209  0.66 11.88 ?  127 LEU   A CA   1 
ATOM   2617 C CA   B LEU   A 1 127 ? 19.790 -5.397  -1.200  0.34 12.40 ?  127 LEU   A CA   1 
ATOM   2618 C C    A LEU   A 1 127 ? 19.302 -5.494  -2.583  0.66 11.30 ?  127 LEU   A C    1 
ATOM   2619 C C    B LEU   A 1 127 ? 19.220 -5.301  -2.613  0.34 12.64 ?  127 LEU   A C    1 
ATOM   2620 O O    A LEU   A 1 127 ? 18.472 -6.281  -3.051  0.66 11.87 ?  127 LEU   A O    1 
ATOM   2621 O O    B LEU   A 1 127 ? 18.423 -6.140  -3.046  0.34 13.06 ?  127 LEU   A O    1 
ATOM   2622 C CB   A LEU   A 1 127 ? 21.085 -6.699  -1.314  0.66 12.72 ?  127 LEU   A CB   1 
ATOM   2623 C CB   B LEU   A 1 127 ? 21.043 -6.276  -1.201  0.34 12.80 ?  127 LEU   A CB   1 
ATOM   2624 C CG   A LEU   A 1 127 ? 21.885 -6.944  -0.037  0.66 12.66 ?  127 LEU   A CG   1 
ATOM   2625 C CG   B LEU   A 1 127 ? 21.868 -6.299  0.092   0.34 13.18 ?  127 LEU   A CG   1 
ATOM   2626 C CD1  A LEU   A 1 127 ? 22.972 -7.962  -0.305  0.66 13.32 ?  127 LEU   A CD1  1 
ATOM   2627 C CD1  B LEU   A 1 127 ? 23.038 -7.274  -0.018  0.34 13.22 ?  127 LEU   A CD1  1 
ATOM   2628 C CD2  A LEU   A 1 127 ? 22.494 -5.654  0.479   0.66 13.67 ?  127 LEU   A CD2  1 
ATOM   2629 C CD2  B LEU   A 1 127 ? 22.364 -4.901  0.443   0.34 13.71 ?  127 LEU   A CD2  1 
ATOM   2630 H H    A LEU   A 1 127 ? 19.090 -7.001  0.029   0.66 14.51 ?  127 LEU   A H    1 
ATOM   2631 H H    B LEU   A 1 127 ? 18.937 -6.723  0.006   0.34 14.88 ?  127 LEU   A H    1 
ATOM   2632 H HA   A LEU   A 1 127 ? 20.267 -4.864  -0.894  0.66 14.23 ?  127 LEU   A HA   1 
ATOM   2633 H HA   B LEU   A 1 127 ? 20.045 -4.506  -0.915  0.34 14.85 ?  127 LEU   A HA   1 
ATOM   2634 H HB2  A LEU   A 1 127 ? 20.732 -7.554  -1.603  0.66 15.24 ?  127 LEU   A HB2  1 
ATOM   2635 H HB2  B LEU   A 1 127 ? 20.774 -7.188  -1.387  0.34 15.33 ?  127 LEU   A HB2  1 
ATOM   2636 H HB3  A LEU   A 1 127 ? 21.705 -6.365  -1.980  0.66 15.24 ?  127 LEU   A HB3  1 
ATOM   2637 H HB3  B LEU   A 1 127 ? 21.627 -5.963  -1.911  0.34 15.33 ?  127 LEU   A HB3  1 
ATOM   2638 H HG   A LEU   A 1 127 ? 21.298 -7.303  0.649   0.66 15.16 ?  127 LEU   A HG   1 
ATOM   2639 H HG   B LEU   A 1 127 ? 21.300 -6.599  0.817   0.34 15.78 ?  127 LEU   A HG   1 
ATOM   2640 H HD11 A LEU   A 1 127 ? 23.421 -8.173  0.530   0.66 15.96 ?  127 LEU   A HD11 1 
ATOM   2641 H HD11 B LEU   A 1 127 ? 23.543 -7.255  0.811   0.34 15.84 ?  127 LEU   A HD11 1 
ATOM   2642 H HD12 A LEU   A 1 127 ? 22.569 -8.765  -0.674  0.66 15.96 ?  127 LEU   A HD12 1 
ATOM   2643 H HD12 B LEU   A 1 127 ? 22.692 -8.166  -0.173  0.34 15.84 ?  127 LEU   A HD12 1 
ATOM   2644 H HD13 A LEU   A 1 127 ? 23.603 -7.589  -0.937  0.66 15.96 ?  127 LEU   A HD13 1 
ATOM   2645 H HD13 B LEU   A 1 127 ? 23.606 -7.006  -0.757  0.34 15.84 ?  127 LEU   A HD13 1 
ATOM   2646 H HD21 A LEU   A 1 127 ? 23.103 -5.860  1.206   0.66 16.38 ?  127 LEU   A HD21 1 
ATOM   2647 H HD21 B LEU   A 1 127 ? 23.001 -4.966  1.172   0.34 16.42 ?  127 LEU   A HD21 1 
ATOM   2648 H HD22 A LEU   A 1 127 ? 22.980 -5.226  -0.246  0.66 16.38 ?  127 LEU   A HD22 1 
ATOM   2649 H HD22 B LEU   A 1 127 ? 22.792 -4.512  -0.336  0.34 16.42 ?  127 LEU   A HD22 1 
ATOM   2650 H HD23 A LEU   A 1 127 ? 21.786 -5.073  0.791   0.66 16.38 ?  127 LEU   A HD23 1 
ATOM   2651 H HD23 B LEU   A 1 127 ? 21.608 -4.355  0.712   0.34 16.42 ?  127 LEU   A HD23 1 
ATOM   2652 N N    A SER   A 1 128 ? 19.747 -4.433  -3.245  0.66 11.39 ?  128 SER   A N    1 
ATOM   2653 N N    B SER   A 1 128 ? 19.640 -4.261  -3.330  0.34 13.42 ?  128 SER   A N    1 
ATOM   2654 C CA   A SER   A 1 128 ? 19.328 -4.038  -4.583  0.66 11.42 ?  128 SER   A CA   1 
ATOM   2655 C CA   B SER   A 1 128 ? 19.347 -3.996  -4.738  0.34 14.22 ?  128 SER   A CA   1 
ATOM   2656 C C    A SER   A 1 128 ? 17.870 -3.586  -4.659  0.66 11.42 ?  128 SER   A C    1 
ATOM   2657 C C    B SER   A 1 128 ? 17.888 -3.665  -5.030  0.34 15.45 ?  128 SER   A C    1 
ATOM   2658 O O    A SER   A 1 128 ? 17.402 -3.277  -5.758  0.66 12.44 ?  128 SER   A O    1 
ATOM   2659 O O    B SER   A 1 128 ? 17.562 -3.376  -6.188  0.34 15.79 ?  128 SER   A O    1 
ATOM   2660 C CB   A SER   A 1 128 ? 19.633 -5.095  -5.656  0.66 12.31 ?  128 SER   A CB   1 
ATOM   2661 C CB   B SER   A 1 128 ? 19.808 -5.122  -5.675  0.34 13.39 ?  128 SER   A CB   1 
ATOM   2662 O OG   A SER   A 1 128 ? 21.034 -5.345  -5.757  0.66 13.51 ?  128 SER   A OG   1 
ATOM   2663 O OG   B SER   A 1 128 ? 21.224 -5.221  -5.687  0.34 12.44 ?  128 SER   A OG   1 
ATOM   2664 H H    A SER   A 1 128 ? 20.344 -3.901  -2.920  0.66 13.64 ?  128 SER   A H    1 
ATOM   2665 H H    B SER   A 1 128 ? 20.148 -3.656  -2.992  0.34 16.07 ?  128 SER   A H    1 
ATOM   2666 H HA   A SER   A 1 128 ? 19.850 -3.261  -4.815  0.66 13.68 ?  128 SER   A HA   1 
ATOM   2667 H HA   B SER   A 1 128 ? 19.856 -3.213  -4.983  0.34 17.04 ?  128 SER   A HA   1 
ATOM   2668 H HB2  A SER   A 1 128 ? 19.174 -5.915  -5.430  0.66 14.75 ?  128 SER   A HB2  1 
ATOM   2669 H HB2  B SER   A 1 128 ? 19.431 -5.960  -5.371  0.34 16.04 ?  128 SER   A HB2  1 
ATOM   2670 H HB3  A SER   A 1 128 ? 19.322 -4.762  -6.514  0.66 14.75 ?  128 SER   A HB3  1 
ATOM   2671 H HB3  B SER   A 1 128 ? 19.496 -4.923  -6.574  0.34 16.04 ?  128 SER   A HB3  1 
ATOM   2672 H HG   A SER   A 1 128 ? 21.437 -4.625  -5.917  0.66 16.18 ?  128 SER   A HG   1 
ATOM   2673 H HG   B SER   A 1 128 ? 21.556 -4.493  -5.945  0.34 14.90 ?  128 SER   A HG   1 
ATOM   2674 N N    A ALA   A 1 129 ? 17.158 -3.490  -3.535  0.66 11.72 ?  129 ALA   A N    1 
ATOM   2675 N N    B ALA   A 1 129 ? 17.006 -3.676  -4.035  0.34 16.97 ?  129 ALA   A N    1 
ATOM   2676 C CA   A ALA   A 1 129 ? 15.784 -3.002  -3.549  0.66 11.83 ?  129 ALA   A CA   1 
ATOM   2677 C CA   B ALA   A 1 129 ? 15.574 -3.545  -4.270  0.34 18.74 ?  129 ALA   A CA   1 
ATOM   2678 C C    A ALA   A 1 129 ? 15.773 -1.473  -3.562  0.66 11.65 ?  129 ALA   A C    1 
ATOM   2679 C C    B ALA   A 1 129 ? 15.067 -2.112  -4.173  0.34 20.47 ?  129 ALA   A C    1 
ATOM   2680 O O    A ALA   A 1 129 ? 16.813 -0.818  -3.677  0.66 11.46 ?  129 ALA   A O    1 
ATOM   2681 O O    B ALA   A 1 129 ? 13.852 -1.895  -4.247  0.34 21.10 ?  129 ALA   A O    1 
ATOM   2682 C CB   A ALA   A 1 129 ? 14.997 -3.576  -2.371  0.66 12.96 ?  129 ALA   A CB   1 
ATOM   2683 C CB   B ALA   A 1 129 ? 14.799 -4.438  -3.301  0.34 18.82 ?  129 ALA   A CB   1 
ATOM   2684 H H    A ALA   A 1 129 ? 17.456 -3.691  -2.740  0.66 14.03 ?  129 ALA   A H    1 
ATOM   2685 H H    B ALA   A 1 129 ? 17.213 -3.760  -3.203  0.34 20.34 ?  129 ALA   A H    1 
ATOM   2686 H HA   A ALA   A 1 129 ? 15.365 -3.302  -4.358  0.66 14.17 ?  129 ALA   A HA   1 
ATOM   2687 H HA   B ALA   A 1 129 ? 15.384 -3.853  -5.166  0.34 22.46 ?  129 ALA   A HA   1 
ATOM   2688 H HB1  A ALA   A 1 129 ? 14.083 -3.249  -2.411  0.66 15.53 ?  129 ALA   A HB1  1 
ATOM   2689 H HB1  B ALA   A 1 129 ? 13.849 -4.333  -3.469  0.34 22.55 ?  129 ALA   A HB1  1 
ATOM   2690 H HB2  A ALA   A 1 129 ? 15.001 -4.545  -2.430  0.66 15.53 ?  129 ALA   A HB2  1 
ATOM   2691 H HB2  B ALA   A 1 129 ? 15.062 -5.360  -3.449  0.34 22.55 ?  129 ALA   A HB2  1 
ATOM   2692 H HB3  A ALA   A 1 129 ? 15.409 -3.296  -1.537  0.66 15.53 ?  129 ALA   A HB3  1 
ATOM   2693 H HB3  B ALA   A 1 129 ? 15.006 -4.175  -2.392  0.34 22.55 ?  129 ALA   A HB3  1 
ATOM   2694 N N    A GLY   A 1 130 ? 14.577 -0.896  -3.486  0.66 12.20 ?  130 GLY   A N    1 
ATOM   2695 N N    B GLY   A 1 130 ? 15.955 -1.136  -4.014  0.34 21.39 ?  130 GLY   A N    1 
ATOM   2696 C CA   A GLY   A 1 130 ? 14.467 0.554   -3.418  0.66 12.91 ?  130 GLY   A CA   1 
ATOM   2697 C CA   B GLY   A 1 130 ? 15.535 0.249   -3.986  0.34 21.72 ?  130 GLY   A CA   1 
ATOM   2698 C C    A GLY   A 1 130 ? 15.069 1.188   -4.655  0.66 12.26 ?  130 GLY   A C    1 
ATOM   2699 C C    B GLY   A 1 130 ? 15.721 0.916   -5.329  0.34 21.90 ?  130 GLY   A C    1 
ATOM   2700 O O    A GLY   A 1 130 ? 14.812 0.750   -5.781  0.66 12.72 ?  130 GLY   A O    1 
ATOM   2701 O O    B GLY   A 1 130 ? 15.088 0.532   -6.318  0.34 21.82 ?  130 GLY   A O    1 
ATOM   2702 H H    A GLY   A 1 130 ? 13.823 -1.321  -3.480  0.66 14.61 ?  130 GLY   A H    1 
ATOM   2703 H H    B GLY   A 1 130 ? 16.803 -1.251  -3.924  0.34 25.64 ?  130 GLY   A H    1 
ATOM   2704 H HA2  A GLY   A 1 130 ? 13.529 0.805   -3.343  0.66 15.47 ?  130 GLY   A HA2  1 
ATOM   2705 H HA2  B GLY   A 1 130 ? 14.599 0.307   -3.741  0.34 26.04 ?  130 GLY   A HA2  1 
ATOM   2706 H HA3  A GLY   A 1 130 ? 14.936 0.878   -2.634  0.66 15.47 ?  130 GLY   A HA3  1 
ATOM   2707 H HA3  B GLY   A 1 130 ? 16.056 0.734   -3.331  0.34 26.04 ?  130 GLY   A HA3  1 
ATOM   2708 N N    A ILE   A 1 131 ? 15.898 2.218   -4.445  0.66 11.60 ?  131 ILE   A N    1 
ATOM   2709 N N    B ILE   A 1 131 ? 16.602 1.920   -5.379  0.34 22.06 ?  131 ILE   A N    1 
ATOM   2710 C CA   A ILE   A 1 131 ? 16.457 2.983   -5.558  0.66 11.86 ?  131 ILE   A CA   1 
ATOM   2711 C CA   B ILE   A 1 131 ? 16.877 2.610   -6.636  0.34 22.30 ?  131 ILE   A CA   1 
ATOM   2712 C C    A ILE   A 1 131 ? 17.481 2.213   -6.378  0.66 11.04 ?  131 ILE   A C    1 
ATOM   2713 C C    B ILE   A 1 131 ? 17.791 1.810   -7.551  0.34 22.01 ?  131 ILE   A C    1 
ATOM   2714 O O    A ILE   A 1 131 ? 17.905 2.712   -7.428  0.66 11.82 ?  131 ILE   A O    1 
ATOM   2715 O O    B ILE   A 1 131 ? 18.044 2.242   -8.683  0.34 21.81 ?  131 ILE   A O    1 
ATOM   2716 C CB   A ILE   A 1 131 ? 17.026 4.348   -5.116  0.66 14.18 ?  131 ILE   A CB   1 
ATOM   2717 C CB   B ILE   A 1 131 ? 17.379 4.043   -6.363  0.34 23.12 ?  131 ILE   A CB   1 
ATOM   2718 C CG1  A ILE   A 1 131 ? 18.299 4.174   -4.278  0.66 16.00 ?  131 ILE   A CG1  1 
ATOM   2719 C CG1  B ILE   A 1 131 ? 18.860 4.038   -5.997  0.34 24.00 ?  131 ILE   A CG1  1 
ATOM   2720 C CG2  A ILE   A 1 131 ? 15.960 5.136   -4.366  0.66 14.94 ?  131 ILE   A CG2  1 
ATOM   2721 C CG2  B ILE   A 1 131 ? 16.557 4.699   -5.261  0.34 23.04 ?  131 ILE   A CG2  1 
ATOM   2722 C CD1  A ILE   A 1 131 ? 18.972 5.501   -3.905  0.66 17.31 ?  131 ILE   A CD1  1 
ATOM   2723 C CD1  B ILE   A 1 131 ? 19.716 4.712   -7.035  0.34 24.37 ?  131 ILE   A CD1  1 
ATOM   2724 H H    A ILE   A 1 131 ? 16.138 2.493   -3.663  0.66 13.89 ?  131 ILE   A H    1 
ATOM   2725 H H    B ILE   A 1 131 ? 17.051 2.216   -4.704  0.34 26.44 ?  131 ILE   A H    1 
ATOM   2726 H HA   A ILE   A 1 131 ? 15.729 3.173   -6.161  0.66 14.21 ?  131 ILE   A HA   1 
ATOM   2727 H HA   B ILE   A 1 131 ? 16.041 2.704   -7.108  0.34 26.73 ?  131 ILE   A HA   1 
ATOM   2728 H HB   A ILE   A 1 131 ? 17.255 4.841   -5.915  0.66 16.99 ?  131 ILE   A HB   1 
ATOM   2729 H HB   B ILE   A 1 131 ? 17.261 4.570   -7.164  0.34 27.72 ?  131 ILE   A HB   1 
ATOM   2730 H HG12 A ILE   A 1 131 ? 18.077 3.712   -3.457  0.66 19.18 ?  131 ILE   A HG12 1 
ATOM   2731 H HG12 B ILE   A 1 131 ? 18.971 4.520   -5.167  0.34 28.77 ?  131 ILE   A HG12 1 
ATOM   2732 H HG13 A ILE   A 1 131 ? 18.947 3.657   -4.783  0.66 19.18 ?  131 ILE   A HG13 1 
ATOM   2733 H HG13 B ILE   A 1 131 ? 19.172 3.126   -5.887  0.34 28.77 ?  131 ILE   A HG13 1 
ATOM   2734 H HG21 A ILE   A 1 131 ? 16.275 6.039   -4.227  0.66 17.90 ?  131 ILE   A HG21 1 
ATOM   2735 H HG21 B ILE   A 1 131 ? 16.744 5.651   -5.250  0.34 27.62 ?  131 ILE   A HG21 1 
ATOM   2736 H HG22 A ILE   A 1 131 ? 15.146 5.142   -4.892  0.66 17.90 ?  131 ILE   A HG22 1 
ATOM   2737 H HG22 B ILE   A 1 131 ? 15.615 4.552   -5.443  0.34 27.62 ?  131 ILE   A HG22 1 
ATOM   2738 H HG23 A ILE   A 1 131 ? 15.794 4.705   -3.510  0.66 17.90 ?  131 ILE   A HG23 1 
ATOM   2739 H HG23 B ILE   A 1 131 ? 16.795 4.305   -4.409  0.34 27.62 ?  131 ILE   A HG23 1 
ATOM   2740 H HD11 A ILE   A 1 131 ? 19.817 5.317   -3.460  0.66 20.74 ?  131 ILE   A HD11 1 
ATOM   2741 H HD11 B ILE   A 1 131 ? 20.617 4.372   -6.967  0.34 29.22 ?  131 ILE   A HD11 1 
ATOM   2742 H HD12 A ILE   A 1 131 ? 19.134 6.018   -4.711  0.66 20.74 ?  131 ILE   A HD12 1 
ATOM   2743 H HD12 B ILE   A 1 131 ? 19.358 4.519   -7.915  0.34 29.22 ?  131 ILE   A HD12 1 
ATOM   2744 H HD13 A ILE   A 1 131 ? 18.390 5.999   -3.307  0.66 20.74 ?  131 ILE   A HD13 1 
ATOM   2745 H HD13 B ILE   A 1 131 ? 19.703 5.670   -6.877  0.34 29.22 ?  131 ILE   A HD13 1 
ATOM   2746 N N    A PHE   A 1 132 ? 17.890 1.010   -5.937  0.66 11.10 ?  132 PHE   A N    1 
ATOM   2747 N N    B PHE   A 1 132 ? 18.292 0.656   -7.104  0.34 21.76 ?  132 PHE   A N    1 
ATOM   2748 C CA   A PHE   A 1 132 ? 18.758 0.161   -6.748  0.66 11.16 ?  132 PHE   A CA   1 
ATOM   2749 C CA   B PHE   A 1 132 ? 19.114 -0.195  -7.960  0.34 21.47 ?  132 PHE   A CA   1 
ATOM   2750 C C    A PHE   A 1 132 ? 17.998 -0.594  -7.838  0.66 12.43 ?  132 PHE   A C    1 
ATOM   2751 C C    B PHE   A 1 132 ? 18.300 -1.031  -8.937  0.34 21.22 ?  132 PHE   A C    1 
ATOM   2752 O O    A PHE   A 1 132 ? 18.629 -1.229  -8.690  0.66 13.66 ?  132 PHE   A O    1 
ATOM   2753 O O    B PHE   A 1 132 ? 18.889 -1.773  -9.729  0.34 20.97 ?  132 PHE   A O    1 
ATOM   2754 C CB   A PHE   A 1 132 ? 19.551 -0.817  -5.873  0.66 10.85 ?  132 PHE   A CB   1 
ATOM   2755 C CB   B PHE   A 1 132 ? 20.042 -1.089  -7.122  0.34 22.07 ?  132 PHE   A CB   1 
ATOM   2756 C CG   A PHE   A 1 132 ? 20.766 -0.211  -5.197  0.66 10.31 ?  132 PHE   A CG   1 
ATOM   2757 C CG   B PHE   A 1 132 ? 21.323 -0.411  -6.695  0.34 23.02 ?  132 PHE   A CG   1 
ATOM   2758 C CD1  A PHE   A 1 132 ? 20.638 0.812   -4.283  0.66 11.16 ?  132 PHE   A CD1  1 
ATOM   2759 C CD1  B PHE   A 1 132 ? 21.590 0.903   -7.060  0.34 23.34 ?  132 PHE   A CD1  1 
ATOM   2760 C CD2  A PHE   A 1 132 ? 22.028 -0.725  -5.434  0.66 11.30 ?  132 PHE   A CD2  1 
ATOM   2761 C CD2  B PHE   A 1 132 ? 22.262 -1.091  -5.938  0.34 23.33 ?  132 PHE   A CD2  1 
ATOM   2762 C CE1  A PHE   A 1 132 ? 21.758 1.347   -3.653  0.66 11.47 ?  132 PHE   A CE1  1 
ATOM   2763 C CE1  B PHE   A 1 132 ? 22.758 1.522   -6.678  0.34 23.46 ?  132 PHE   A CE1  1 
ATOM   2764 C CE2  A PHE   A 1 132 ? 23.146 -0.196  -4.806  0.66 12.15 ?  132 PHE   A CE2  1 
ATOM   2765 C CE2  B PHE   A 1 132 ? 23.437 -0.472  -5.550  0.34 23.55 ?  132 PHE   A CE2  1 
ATOM   2766 C CZ   A PHE   A 1 132 ? 23.007 0.833   -3.911  0.66 11.77 ?  132 PHE   A CZ   1 
ATOM   2767 C CZ   B PHE   A 1 132 ? 23.684 0.835   -5.921  0.34 23.47 ?  132 PHE   A CZ   1 
ATOM   2768 H H    A PHE   A 1 132 ? 17.683 0.666   -5.168  0.66 13.29 ?  132 PHE   A H    1 
ATOM   2769 H H    B PHE   A 1 132 ? 18.175 0.349   -6.308  0.34 26.08 ?  132 PHE   A H    1 
ATOM   2770 H HA   A PHE   A 1 132 ? 19.409 0.730   -7.185  0.66 13.36 ?  132 PHE   A HA   1 
ATOM   2771 H HA   B PHE   A 1 132 ? 19.659 0.376   -8.518  0.34 25.74 ?  132 PHE   A HA   1 
ATOM   2772 H HB2  A PHE   A 1 132 ? 18.969 -1.157  -5.173  0.66 12.99 ?  132 PHE   A HB2  1 
ATOM   2773 H HB2  B PHE   A 1 132 ? 19.574 -1.362  -6.318  0.34 26.45 ?  132 PHE   A HB2  1 
ATOM   2774 H HB3  A PHE   A 1 132 ? 19.861 -1.557  -6.423  0.66 12.99 ?  132 PHE   A HB3  1 
ATOM   2775 H HB3  B PHE   A 1 132 ? 20.277 -1.876  -7.643  0.34 26.45 ?  132 PHE   A HB3  1 
ATOM   2776 H HD1  A PHE   A 1 132 ? 19.798 1.160   -4.095  0.66 13.37 ?  132 PHE   A HD1  1 
ATOM   2777 H HD1  B PHE   A 1 132 ? 20.970 1.374   -7.574  0.34 27.97 ?  132 PHE   A HD1  1 
ATOM   2778 H HD2  A PHE   A 1 132 ? 22.133 -1.425  -6.040  0.66 13.54 ?  132 PHE   A HD2  1 
ATOM   2779 H HD2  B PHE   A 1 132 ? 22.102 -1.972  -5.686  0.34 27.97 ?  132 PHE   A HD2  1 
ATOM   2780 H HE1  A PHE   A 1 132 ? 21.660 2.044   -3.041  0.66 13.73 ?  132 PHE   A HE1  1 
ATOM   2781 H HE1  B PHE   A 1 132 ? 22.917 2.403   -6.932  0.34 28.12 ?  132 PHE   A HE1  1 
ATOM   2782 H HE2  A PHE   A 1 132 ? 23.987 -0.543  -4.989  0.66 14.55 ?  132 PHE   A HE2  1 
ATOM   2783 H HE2  B PHE   A 1 132 ? 24.060 -0.936  -5.040  0.34 28.23 ?  132 PHE   A HE2  1 
ATOM   2784 H HZ   A PHE   A 1 132 ? 23.752 1.193   -3.489  0.66 14.09 ?  132 PHE   A HZ   1 
ATOM   2785 H HZ   B PHE   A 1 132 ? 24.471 1.253   -5.662  0.34 28.14 ?  132 PHE   A HZ   1 
ATOM   2786 N N    A GLY   A 1 133 ? 16.667 -0.549  -7.832  0.66 12.45 ?  133 GLY   A N    1 
ATOM   2787 N N    B GLY   A 1 133 ? 16.975 -0.935  -8.898  0.34 21.42 ?  133 GLY   A N    1 
ATOM   2788 C CA   A GLY   A 1 133 ? 15.881 -0.914  -8.993  0.66 12.90 ?  133 GLY   A CA   1 
ATOM   2789 C CA   B GLY   A 1 133 ? 16.152 -1.407  -9.991  0.34 21.43 ?  133 GLY   A CA   1 
ATOM   2790 C C    A GLY   A 1 133 ? 15.530 -2.377  -9.161  0.66 12.87 ?  133 GLY   A C    1 
ATOM   2791 C C    B GLY   A 1 133 ? 15.796 -2.876  -9.982  0.34 21.12 ?  133 GLY   A C    1 
ATOM   2792 O O    A GLY   A 1 133 ? 14.828 -2.703  -10.128 0.66 14.19 ?  133 GLY   A O    1 
ATOM   2793 O O    B GLY   A 1 133 ? 15.287 -3.372  -10.994 0.34 22.00 ?  133 GLY   A O    1 
ATOM   2794 H H    A GLY   A 1 133 ? 16.194 -0.300  -7.158  0.66 14.91 ?  133 GLY   A H    1 
ATOM   2795 H H    B GLY   A 1 133 ? 16.537 -0.602  -8.241  0.34 25.68 ?  133 GLY   A H    1 
ATOM   2796 H HA2  A GLY   A 1 133 ? 15.044 -0.424  -8.967  0.66 15.46 ?  133 GLY   A HA2  1 
ATOM   2797 H HA2  B GLY   A 1 133 ? 15.321 -0.916  -9.984  0.34 25.69 ?  133 GLY   A HA2  1 
ATOM   2798 H HA3  A GLY   A 1 133 ? 16.357 -0.639  -9.792  0.66 15.46 ?  133 GLY   A HA3  1 
ATOM   2799 H HA3  B GLY   A 1 133 ? 16.608 -1.208  -10.828 0.34 25.69 ?  133 GLY   A HA3  1 
ATOM   2800 N N    A ALA   A 1 134 ? 15.970 -3.264  -8.269  0.66 13.11 ?  134 ALA   A N    1 
ATOM   2801 N N    B ALA   A 1 134 ? 16.022 -3.587  -8.883  0.34 19.73 ?  134 ALA   A N    1 
ATOM   2802 C CA   A ALA   A 1 134 ? 15.620 -4.672  -8.395  0.66 13.60 ?  134 ALA   A CA   1 
ATOM   2803 C CA   B ALA   A 1 134 ? 15.730 -5.012  -8.828  0.34 18.56 ?  134 ALA   A CA   1 
ATOM   2804 C C    A ALA   A 1 134 ? 14.272 -4.964  -7.735  0.66 14.15 ?  134 ALA   A C    1 
ATOM   2805 C C    B ALA   A 1 134 ? 14.362 -5.268  -8.206  0.34 18.05 ?  134 ALA   A C    1 
ATOM   2806 O O    A ALA   A 1 134 ? 13.764 -4.186  -6.922  0.66 15.28 ?  134 ALA   A O    1 
ATOM   2807 O O    B ALA   A 1 134 ? 13.806 -4.433  -7.489  0.34 18.19 ?  134 ALA   A O    1 
ATOM   2808 C CB   A ALA   A 1 134 ? 16.693 -5.563  -7.772  0.66 14.86 ?  134 ALA   A CB   1 
ATOM   2809 C CB   B ALA   A 1 134 ? 16.804 -5.771  -8.046  0.34 18.63 ?  134 ALA   A CB   1 
ATOM   2810 H H    A ALA   A 1 134 ? 16.460 -3.072  -7.586  0.66 15.71 ?  134 ALA   A H    1 
ATOM   2811 H H    B ALA   A 1 134 ? 16.340 -3.261  -8.154  0.34 23.64 ?  134 ALA   A H    1 
ATOM   2812 H HA   A ALA   A 1 134 ? 15.550 -4.892  -9.337  0.66 16.29 ?  134 ALA   A HA   1 
ATOM   2813 H HA   B ALA   A 1 134 ? 15.718 -5.364  -9.730  0.34 22.24 ?  134 ALA   A HA   1 
ATOM   2814 H HB1  A ALA   A 1 134 ? 16.447 -6.488  -7.912  0.66 17.80 ?  134 ALA   A HB1  1 
ATOM   2815 H HB1  B ALA   A 1 134 ? 16.592 -6.718  -8.064  0.34 22.33 ?  134 ALA   A HB1  1 
ATOM   2816 H HB2  A ALA   A 1 134 ? 17.541 -5.372  -8.201  0.66 17.80 ?  134 ALA   A HB2  1 
ATOM   2817 H HB2  B ALA   A 1 134 ? 17.665 -5.617  -8.463  0.34 22.33 ?  134 ALA   A HB2  1 
ATOM   2818 H HB3  A ALA   A 1 134 ? 16.747 -5.370  -6.825  0.66 17.80 ?  134 ALA   A HB3  1 
ATOM   2819 H HB3  B ALA   A 1 134 ? 16.815 -5.451  -7.132  0.34 22.33 ?  134 ALA   A HB3  1 
ATOM   2820 N N    A ASP   A 1 135 ? 13.702 -6.111  -8.101  0.66 14.83 ?  135 ASP   A N    1 
ATOM   2821 N N    B ASP   A 1 135 ? 13.826 -6.447  -8.498  0.34 17.47 ?  135 ASP   A N    1 
ATOM   2822 C CA   A ASP   A 1 135 ? 12.449 -6.583  -7.520  0.66 15.92 ?  135 ASP   A CA   1 
ATOM   2823 C CA   B ASP   A 1 135 ? 12.538 -6.858  -7.959  0.34 17.43 ?  135 ASP   A CA   1 
ATOM   2824 C C    A ASP   A 1 135 ? 12.696 -7.021  -6.083  0.66 15.33 ?  135 ASP   A C    1 
ATOM   2825 C C    B ASP   A 1 135 ? 12.713 -7.280  -6.505  0.34 16.11 ?  135 ASP   A C    1 
ATOM   2826 O O    A ASP   A 1 135 ? 13.468 -7.965  -5.861  0.66 14.86 ?  135 ASP   A O    1 
ATOM   2827 O O    B ASP   A 1 135 ? 13.504 -8.189  -6.228  0.34 15.49 ?  135 ASP   A O    1 
ATOM   2828 C CB   A ASP   A 1 135 ? 11.966 -7.772  -8.352  0.66 18.65 ?  135 ASP   A CB   1 
ATOM   2829 C CB   B ASP   A 1 135 ? 11.999 -8.029  -8.770  0.34 18.72 ?  135 ASP   A CB   1 
ATOM   2830 C CG   A ASP   A 1 135 ? 10.765 -8.487  -7.740  0.66 21.55 ?  135 ASP   A CG   1 
ATOM   2831 C CG   B ASP   A 1 135 ? 10.566 -8.385  -8.409  0.34 20.04 ?  135 ASP   A CG   1 
ATOM   2832 O OD1  A ASP   A 1 135 ? 10.127 -7.944  -6.813  0.66 21.55 ?  135 ASP   A OD1  1 
ATOM   2833 O OD1  B ASP   A 1 135 ? 10.058 -7.893  -7.380  0.34 20.94 ?  135 ASP   A OD1  1 
ATOM   2834 O OD2  A ASP   A 1 135 ? 10.471 -9.615  -8.195  0.66 24.56 -1 135 ASP   A OD2  1 
ATOM   2835 O OD2  B ASP   A 1 135 ? 9.940  -9.152  -9.166  0.34 20.36 -1 135 ASP   A OD2  1 
ATOM   2836 H H    A ASP   A 1 135 ? 14.023 -6.641  -8.692  0.66 17.77 ?  135 ASP   A H    1 
ATOM   2837 H H    B ASP   A 1 135 ? 14.192 -7.030  -9.006  0.34 20.94 ?  135 ASP   A H    1 
ATOM   2838 H HA   A ASP   A 1 135 ? 11.772 -5.881  -7.555  0.66 19.07 ?  135 ASP   A HA   1 
ATOM   2839 H HA   B ASP   A 1 135 ? 11.909 -6.123  -8.020  0.34 20.89 ?  135 ASP   A HA   1 
ATOM   2840 H HB2  A ASP   A 1 135 ? 11.735 -7.462  -9.245  0.66 22.35 ?  135 ASP   A HB2  1 
ATOM   2841 H HB2  B ASP   A 1 135 ? 12.017 -7.797  -9.711  0.34 22.44 ?  135 ASP   A HB2  1 
ATOM   2842 H HB3  A ASP   A 1 135 ? 12.677 -8.426  -8.407  0.66 22.35 ?  135 ASP   A HB3  1 
ATOM   2843 H HB3  B ASP   A 1 135 ? 12.557 -8.807  -8.611  0.34 22.44 ?  135 ASP   A HB3  1 
ATOM   2844 N N    A PRO   A 1 136 ? 12.092 -6.371  -5.082  0.66 15.21 ?  136 PRO   A N    1 
ATOM   2845 N N    B PRO   A 1 136 ? 12.010 -6.657  -5.555  0.34 15.72 ?  136 PRO   A N    1 
ATOM   2846 C CA   A PRO   A 1 136 ? 12.338 -6.789  -3.691  0.66 14.91 ?  136 PRO   A CA   1 
ATOM   2847 C CA   B PRO   A 1 136 ? 12.199 -7.039  -4.143  0.34 15.34 ?  136 PRO   A CA   1 
ATOM   2848 C C    A PRO   A 1 136 ? 11.895 -8.211  -3.377  0.66 13.96 ?  136 PRO   A C    1 
ATOM   2849 C C    B PRO   A 1 136 ? 11.847 -8.485  -3.842  0.34 14.98 ?  136 PRO   A C    1 
ATOM   2850 O O    A PRO   A 1 136 ? 12.478 -8.837  -2.484  0.66 12.48 ?  136 PRO   A O    1 
ATOM   2851 O O    B PRO   A 1 136 ? 12.531 -9.122  -3.032  0.34 14.79 ?  136 PRO   A O    1 
ATOM   2852 C CB   A PRO   A 1 136 ? 11.574 -5.742  -2.864  0.66 15.60 ?  136 PRO   A CB   1 
ATOM   2853 C CB   B PRO   A 1 136 ? 11.296 -6.049  -3.390  0.34 15.93 ?  136 PRO   A CB   1 
ATOM   2854 C CG   A PRO   A 1 136 ? 10.565 -5.175  -3.802  0.66 17.02 ?  136 PRO   A CG   1 
ATOM   2855 C CG   B PRO   A 1 136 ? 10.300 -5.587  -4.415  0.34 16.15 ?  136 PRO   A CG   1 
ATOM   2856 C CD   A PRO   A 1 136 ? 11.199 -5.201  -5.157  0.66 15.93 ?  136 PRO   A CD   1 
ATOM   2857 C CD   B PRO   A 1 136 ? 11.055 -5.547  -5.701  0.34 16.09 ?  136 PRO   A CD   1 
ATOM   2858 H HA   A PRO   A 1 136 ? 13.285 -6.707  -3.488  0.66 17.87 ?  136 PRO   A HA   1 
ATOM   2859 H HA   B PRO   A 1 136 ? 13.121 -6.890  -3.876  0.34 18.38 ?  136 PRO   A HA   1 
ATOM   2860 H HB2  A PRO   A 1 136 ? 11.141 -6.172  -2.112  0.66 18.69 ?  136 PRO   A HB2  1 
ATOM   2861 H HB2  B PRO   A 1 136 ? 10.854 -6.501  -2.654  0.34 19.09 ?  136 PRO   A HB2  1 
ATOM   2862 H HB3  A PRO   A 1 136 ? 12.186 -5.051  -2.562  0.66 18.69 ?  136 PRO   A HB3  1 
ATOM   2863 H HB3  B PRO   A 1 136 ? 11.830 -5.306  -3.064  0.34 19.09 ?  136 PRO   A HB3  1 
ATOM   2864 H HG2  A PRO   A 1 136 ? 9.768  -5.728  -3.793  0.66 20.39 ?  136 PRO   A HG2  1 
ATOM   2865 H HG2  B PRO   A 1 136 ? 9.569  -6.221  -4.469  0.34 19.35 ?  136 PRO   A HG2  1 
ATOM   2866 H HG3  A PRO   A 1 136 ? 10.353 -4.266  -3.544  0.66 20.39 ?  136 PRO   A HG3  1 
ATOM   2867 H HG3  B PRO   A 1 136 ? 9.977  -4.704  -4.184  0.34 19.35 ?  136 PRO   A HG3  1 
ATOM   2868 H HD2  A PRO   A 1 136 ? 10.523 -5.334  -5.843  0.66 19.09 ?  136 PRO   A HD2  1 
ATOM   2869 H HD2  B PRO   A 1 136 ? 10.461 -5.707  -6.449  0.34 19.28 ?  136 PRO   A HD2  1 
ATOM   2870 H HD3  A PRO   A 1 136 ? 11.708 -4.389  -5.314  0.66 19.09 ?  136 PRO   A HD3  1 
ATOM   2871 H HD3  B PRO   A 1 136 ? 11.532 -4.707  -5.795  0.34 19.28 ?  136 PRO   A HD3  1 
ATOM   2872 N N    A ILE   A 1 137 ? 10.882 -8.739  -4.073  0.66 14.93 ?  137 ILE   A N    1 
ATOM   2873 N N    B ILE   A 1 137 ? 10.787 -9.021  -4.454  0.34 14.64 ?  137 ILE   A N    1 
ATOM   2874 C CA   A ILE   A 1 137 ? 10.493 -10.134 -3.872  0.66 15.19 ?  137 ILE   A CA   1 
ATOM   2875 C CA   B ILE   A 1 137 ? 10.464 -10.434 -4.266  0.34 15.06 ?  137 ILE   A CA   1 
ATOM   2876 C C    A ILE   A 1 137 ? 11.634 -11.062 -4.272  0.66 14.82 ?  137 ILE   A C    1 
ATOM   2877 C C    B ILE   A 1 137 ? 11.668 -11.295 -4.617  0.34 14.96 ?  137 ILE   A C    1 
ATOM   2878 O O    A ILE   A 1 137 ? 11.955 -12.025 -3.562  0.66 15.24 ?  137 ILE   A O    1 
ATOM   2879 O O    B ILE   A 1 137 ? 11.951 -12.301 -3.954  0.34 15.24 ?  137 ILE   A O    1 
ATOM   2880 C CB   A ILE   A 1 137 ? 9.198  -10.447 -4.649  0.66 16.77 ?  137 ILE   A CB   1 
ATOM   2881 C CB   B ILE   A 1 137 ? 9.217  -10.816 -5.087  0.34 15.92 ?  137 ILE   A CB   1 
ATOM   2882 C CG1  A ILE   A 1 137 ? 8.038  -9.576  -4.152  0.66 18.57 ?  137 ILE   A CG1  1 
ATOM   2883 C CG1  B ILE   A 1 137 ? 7.997  -10.031 -4.598  0.34 16.51 ?  137 ILE   A CG1  1 
ATOM   2884 C CG2  A ILE   A 1 137 ? 8.847  -11.928 -4.532  0.66 17.67 ?  137 ILE   A CG2  1 
ATOM   2885 C CG2  B ILE   A 1 137 ? 8.946  -12.313 -4.989  0.34 15.98 ?  137 ILE   A CG2  1 
ATOM   2886 C CD1  A ILE   A 1 137 ? 6.744  -9.780  -4.919  0.66 19.74 ?  137 ILE   A CD1  1 
ATOM   2887 C CD1  B ILE   A 1 137 ? 6.735  -10.285 -5.400  0.34 17.31 ?  137 ILE   A CD1  1 
ATOM   2888 H H    A ILE   A 1 137 ? 10.415 -8.310  -4.655  0.66 17.89 ?  137 ILE   A H    1 
ATOM   2889 H H    B ILE   A 1 137 ? 10.249 -8.597  -4.969  0.34 17.54 ?  137 ILE   A H    1 
ATOM   2890 H HA   A ILE   A 1 137 ? 10.317 -10.272 -2.933  0.66 18.20 ?  137 ILE   A HA   1 
ATOM   2891 H HA   B ILE   A 1 137 ? 10.260 -10.592 -3.333  0.34 18.04 ?  137 ILE   A HA   1 
ATOM   2892 H HB   A ILE   A 1 137 ? 9.347  -10.243 -5.584  0.66 20.10 ?  137 ILE   A HB   1 
ATOM   2893 H HB   B ILE   A 1 137 ? 9.373  -10.591 -6.015  0.34 19.07 ?  137 ILE   A HB   1 
ATOM   2894 H HG12 A ILE   A 1 137 ? 7.869  -9.781  -3.220  0.66 22.25 ?  137 ILE   A HG12 1 
ATOM   2895 H HG12 B ILE   A 1 137 ? 7.816  -10.272 -3.676  0.34 19.78 ?  137 ILE   A HG12 1 
ATOM   2896 H HG13 A ILE   A 1 137 ? 8.289  -8.641  -4.242  0.66 22.25 ?  137 ILE   A HG13 1 
ATOM   2897 H HG13 B ILE   A 1 137 ? 8.193  -9.080  -4.654  0.34 19.78 ?  137 ILE   A HG13 1 
ATOM   2898 H HG21 A ILE   A 1 137 ? 7.989  -12.096 -4.953  0.66 21.18 ?  137 ILE   A HG21 1 
ATOM   2899 H HG21 B ILE   A 1 137 ? 8.258  -12.554 -5.627  0.34 19.14 ?  137 ILE   A HG21 1 
ATOM   2900 H HG22 A ILE   A 1 137 ? 9.529  -12.450 -4.978  0.66 21.18 ?  137 ILE   A HG22 1 
ATOM   2901 H HG22 B ILE   A 1 137 ? 9.749  -12.806 -5.192  0.34 19.14 ?  137 ILE   A HG22 1 
ATOM   2902 H HG23 A ILE   A 1 137 ? 8.803  -12.165 -3.595  0.66 21.18 ?  137 ILE   A HG23 1 
ATOM   2903 H HG23 B ILE   A 1 137 ? 8.648  -12.516 -4.089  0.34 19.14 ?  137 ILE   A HG23 1 
ATOM   2904 H HD11 A ILE   A 1 137 ? 6.060  -10.104 -4.310  0.66 23.66 ?  137 ILE   A HD11 1 
ATOM   2905 H HD11 B ILE   A 1 137 ? 5.975  -10.062 -4.847  0.34 20.75 ?  137 ILE   A HD11 1 
ATOM   2906 H HD12 A ILE   A 1 137 ? 6.482  -8.934  -5.301  0.66 23.66 ?  137 ILE   A HD12 1 
ATOM   2907 H HD12 B ILE   A 1 137 ? 6.749  -9.726  -6.191  0.34 20.75 ?  137 ILE   A HD12 1 
ATOM   2908 H HD13 A ILE   A 1 137 ? 6.885  -10.425 -5.632  0.66 23.66 ?  137 ILE   A HD13 1 
ATOM   2909 H HD13 B ILE   A 1 137 ? 6.680  -11.217 -5.654  0.34 20.75 ?  137 ILE   A HD13 1 
ATOM   2910 N N    A HIS   A 1 138 ? 12.267 -10.779 -5.414  0.66 15.65 ?  138 HIS   A N    1 
ATOM   2911 N N    B HIS   A 1 138 ? 12.396 -10.914 -5.667  0.34 15.37 ?  138 HIS   A N    1 
ATOM   2912 C CA   A HIS   A 1 138 ? 13.411 -11.573 -5.853  0.66 15.85 ?  138 HIS   A CA   1 
ATOM   2913 C CA   B HIS   A 1 138 ? 13.614 -11.638 -6.007  0.34 15.34 ?  138 HIS   A CA   1 
ATOM   2914 C C    A HIS   A 1 138 ? 14.575 -11.450 -4.878  0.66 14.97 ?  138 HIS   A C    1 
ATOM   2915 C C    B HIS   A 1 138 ? 14.688 -11.453 -4.940  0.34 14.64 ?  138 HIS   A C    1 
ATOM   2916 O O    A HIS   A 1 138 ? 15.224 -12.448 -4.538  0.66 15.90 ?  138 HIS   A O    1 
ATOM   2917 O O    B HIS   A 1 138 ? 15.370 -12.417 -4.572  0.34 14.71 ?  138 HIS   A O    1 
ATOM   2918 C CB   A HIS   A 1 138 ? 13.820 -11.143 -7.261  0.66 16.60 ?  138 HIS   A CB   1 
ATOM   2919 C CB   B HIS   A 1 138 ? 14.129 -11.212 -7.381  0.34 16.69 ?  138 HIS   A CB   1 
ATOM   2920 C CG   A HIS   A 1 138 ? 15.116 -11.740 -7.719  0.66 17.26 ?  138 HIS   A CG   1 
ATOM   2921 C CG   B HIS   A 1 138 ? 15.339 -11.971 -7.826  0.34 17.35 ?  138 HIS   A CG   1 
ATOM   2922 N ND1  A HIS   A 1 138 ? 15.267 -13.085 -7.979  0.66 18.12 ?  138 HIS   A ND1  1 
ATOM   2923 N ND1  B HIS   A 1 138 ? 15.334 -13.336 -8.014  0.34 18.00 ?  138 HIS   A ND1  1 
ATOM   2924 C CD2  A HIS   A 1 138 ? 16.324 -11.175 -7.952  0.66 16.89 ?  138 HIS   A CD2  1 
ATOM   2925 C CD2  B HIS   A 1 138 ? 16.598 -11.558 -8.105  0.34 17.50 ?  138 HIS   A CD2  1 
ATOM   2926 C CE1  A HIS   A 1 138 ? 16.510 -13.322 -8.358  0.66 18.15 ?  138 HIS   A CE1  1 
ATOM   2927 C CE1  B HIS   A 1 138 ? 16.534 -13.731 -8.399  0.34 18.20 ?  138 HIS   A CE1  1 
ATOM   2928 N NE2  A HIS   A 1 138 ? 17.173 -12.180 -8.349  0.66 17.11 ?  138 HIS   A NE2  1 
ATOM   2929 N NE2  B HIS   A 1 138 ? 17.320 -12.671 -8.460  0.34 17.52 ?  138 HIS   A NE2  1 
ATOM   2930 H H    A HIS   A 1 138 ? 12.058 -10.130 -5.945  0.66 18.75 ?  138 HIS   A H    1 
ATOM   2931 H H    B HIS   A 1 138 ? 12.208 -10.256 -6.189  0.34 18.42 ?  138 HIS   A H    1 
ATOM   2932 H HA   A HIS   A 1 138 ? 13.148 -12.501 -5.889  0.66 18.99 ?  138 HIS   A HA   1 
ATOM   2933 H HA   B HIS   A 1 138 ? 13.408 -12.583 -6.055  0.34 18.38 ?  138 HIS   A HA   1 
ATOM   2934 H HB2  A HIS   A 1 138 ? 13.129 -11.417 -7.886  0.66 19.90 ?  138 HIS   A HB2  1 
ATOM   2935 H HB2  B HIS   A 1 138 ? 13.428 -11.357 -8.037  0.34 20.00 ?  138 HIS   A HB2  1 
ATOM   2936 H HB3  A HIS   A 1 138 ? 13.916 -10.177 -7.283  0.66 19.90 ?  138 HIS   A HB3  1 
ATOM   2937 H HB3  B HIS   A 1 138 ? 14.362 -10.271 -7.353  0.34 20.00 ?  138 HIS   A HB3  1 
ATOM   2938 H HD1  A HIS   A 1 138 ? 14.645 -13.679 -7.908  0.66 21.72 ?  138 HIS   A HD1  1 
ATOM   2939 H HD2  A HIS   A 1 138 ? 16.534 -10.274 -7.862  0.66 20.23 ?  138 HIS   A HD2  1 
ATOM   2940 H HD2  B HIS   A 1 138 ? 16.912 -10.685 -8.066  0.34 20.97 ?  138 HIS   A HD2  1 
ATOM   2941 H HE1  A HIS   A 1 138 ? 16.858 -14.151 -8.588  0.66 21.75 ?  138 HIS   A HE1  1 
ATOM   2942 H HE1  B HIS   A 1 138 ? 16.781 -14.606 -8.590  0.34 21.81 ?  138 HIS   A HE1  1 
ATOM   2943 H HE2  B HIS   A 1 138 ? 18.148 -12.678 -8.685  0.34 20.99 ?  138 HIS   A HE2  1 
ATOM   2944 N N    . SER   A 1 139 ? 14.861 -10.231 -4.427  1.00 14.24 ?  139 SER   A N    1 
ATOM   2945 C CA   . SER   A 1 139 ? 15.920 -10.025 -3.447  1.00 14.09 ?  139 SER   A CA   1 
ATOM   2946 C C    . SER   A 1 139 ? 15.693 -10.863 -2.194  1.00 14.10 ?  139 SER   A C    1 
ATOM   2947 O O    . SER   A 1 139 ? 16.634 -11.450 -1.649  1.00 14.14 ?  139 SER   A O    1 
ATOM   2948 C CB   . SER   A 1 139 ? 16.047 -8.540  -3.101  1.00 14.09 ?  139 SER   A CB   1 
ATOM   2949 O OG   . SER   A 1 139 ? 17.126 -8.357  -2.201  1.00 14.87 ?  139 SER   A OG   1 
ATOM   2950 H H    A SER   A 1 139 ? 14.459 -9.511  -4.665  0.66 17.06 ?  139 SER   A H    1 
ATOM   2951 H H    B SER   A 1 139 ? 14.404 -9.532  -4.622  0.34 17.06 ?  139 SER   A H    1 
ATOM   2952 H HA   . SER   A 1 139 ? 16.768 -10.302 -3.831  1.00 16.88 ?  139 SER   A HA   1 
ATOM   2953 H HB2  . SER   A 1 139 ? 16.224 -8.029  -3.906  1.00 16.88 ?  139 SER   A HB2  1 
ATOM   2954 H HB3  . SER   A 1 139 ? 15.232 -8.231  -2.678  1.00 16.88 ?  139 SER   A HB3  1 
ATOM   2955 H HG   . SER   A 1 139 ? 17.213 -7.540  -1.996  1.00 17.81 ?  139 SER   A HG   1 
ATOM   2956 N N    . LEU   A 1 140 ? 14.451 -10.936 -1.724  1.00 13.88 ?  140 LEU   A N    1 
ATOM   2957 C CA   . LEU   A 1 140 ? 14.167 -11.733 -0.538  1.00 13.40 ?  140 LEU   A CA   1 
ATOM   2958 C C    . LEU   A 1 140 ? 14.437 -13.211 -0.799  1.00 13.46 ?  140 LEU   A C    1 
ATOM   2959 O O    . LEU   A 1 140 ? 14.983 -13.917 0.061   1.00 14.59 ?  140 LEU   A O    1 
ATOM   2960 C CB   . LEU   A 1 140 ? 12.721 -11.505 -0.104  1.00 13.88 ?  140 LEU   A CB   1 
ATOM   2961 C CG   . LEU   A 1 140 ? 12.256 -12.325 1.100   1.00 14.91 ?  140 LEU   A CG   1 
ATOM   2962 C CD1  . LEU   A 1 140 ? 13.168 -12.115 2.318   1.00 15.44 ?  140 LEU   A CD1  1 
ATOM   2963 C CD2  . LEU   A 1 140 ? 10.786 -12.003 1.427   1.00 15.49 ?  140 LEU   A CD2  1 
ATOM   2964 H H    . LEU   A 1 140 ? 13.769 -10.531 -2.063  1.00 16.63 ?  140 LEU   A H    1 
ATOM   2965 H HA   . LEU   A 1 140 ? 14.742 -11.448 0.185   1.00 16.06 ?  140 LEU   A HA   1 
ATOM   2966 H HB2  . LEU   A 1 140 ? 12.608 -10.575 0.126   1.00 16.63 ?  140 LEU   A HB2  1 
ATOM   2967 H HB3  . LEU   A 1 140 ? 12.137 -11.734 -0.845  1.00 16.63 ?  140 LEU   A HB3  1 
ATOM   2968 H HG   . LEU   A 1 140 ? 12.290 -13.271 0.869   1.00 17.87 ?  140 LEU   A HG   1 
ATOM   2969 H HD11 . LEU   A 1 140 ? 12.778 -12.565 3.087   1.00 18.51 ?  140 LEU   A HD11 1 
ATOM   2970 H HD12 . LEU   A 1 140 ? 14.040 -12.497 2.125   1.00 18.51 ?  140 LEU   A HD12 1 
ATOM   2971 H HD13 . LEU   A 1 140 ? 13.247 -11.169 2.493   1.00 18.51 ?  140 LEU   A HD13 1 
ATOM   2972 H HD21 . LEU   A 1 140 ? 10.503 -12.534 2.193   1.00 18.56 ?  140 LEU   A HD21 1 
ATOM   2973 H HD22 . LEU   A 1 140 ? 10.704 -11.061 1.633   1.00 18.56 ?  140 LEU   A HD22 1 
ATOM   2974 H HD23 . LEU   A 1 140 ? 10.231 -12.223 0.658   1.00 18.56 ?  140 LEU   A HD23 1 
ATOM   2975 N N    . ARG   A 1 141 ? 14.060 -13.696 -1.985  1.00 14.25 ?  141 ARG   A N    1 
ATOM   2976 C CA   . ARG   A 1 141 ? 14.305 -15.093 -2.334  1.00 15.82 ?  141 ARG   A CA   1 
ATOM   2977 C C    . ARG   A 1 141 ? 15.801 -15.394 -2.333  1.00 14.71 ?  141 ARG   A C    1 
ATOM   2978 O O    . ARG   A 1 141 ? 16.247 -16.400 -1.769  1.00 14.75 ?  141 ARG   A O    1 
ATOM   2979 C CB   . ARG   A 1 141 ? 13.699 -15.373 -3.709  1.00 17.92 ?  141 ARG   A CB   1 
ATOM   2980 C CG   . ARG   A 1 141 ? 13.736 -16.825 -4.140  1.00 21.28 ?  141 ARG   A CG   1 
ATOM   2981 C CD   . ARG   A 1 141 ? 12.685 -17.609 -3.416  1.00 24.50 ?  141 ARG   A CD   1 
ATOM   2982 N NE   . ARG   A 1 141 ? 13.260 -18.410 -2.348  1.00 25.58 ?  141 ARG   A NE   1 
ATOM   2983 C CZ   . ARG   A 1 141 ? 12.556 -18.924 -1.348  1.00 26.23 ?  141 ARG   A CZ   1 
ATOM   2984 N NH1  . ARG   A 1 141 ? 11.273 -18.640 -1.185  1.00 25.34 ?  141 ARG   A NH1  1 
ATOM   2985 N NH2  . ARG   A 1 141 ? 13.157 -19.732 -0.479  1.00 26.95 ?  141 ARG   A NH2  1 
ATOM   2986 H H    . ARG   A 1 141 ? 13.661 -13.239 -2.602  1.00 17.08 ?  141 ARG   A H    1 
ATOM   2987 H HA   . ARG   A 1 141 ? 13.878 -15.667 -1.686  1.00 18.96 ?  141 ARG   A HA   1 
ATOM   2988 H HB2  . ARG   A 1 141 ? 12.769 -15.088 -3.705  1.00 21.48 ?  141 ARG   A HB2  1 
ATOM   2989 H HB3  . ARG   A 1 141 ? 14.187 -14.863 -4.373  1.00 21.48 ?  141 ARG   A HB3  1 
ATOM   2990 H HG2  . ARG   A 1 141 ? 13.565 -16.889 -5.094  1.00 25.50 ?  141 ARG   A HG2  1 
ATOM   2991 H HG3  . ARG   A 1 141 ? 14.604 -17.210 -3.929  1.00 25.50 ?  141 ARG   A HG3  1 
ATOM   2992 H HD2  . ARG   A 1 141 ? 12.045 -17.000 -3.015  1.00 29.37 ?  141 ARG   A HD2  1 
ATOM   2993 H HD3  . ARG   A 1 141 ? 12.231 -18.197 -4.045  1.00 29.37 ?  141 ARG   A HD3  1 
ATOM   2994 H HE   . ARG   A 1 141 ? 14.070 -18.680 -2.440  1.00 30.67 ?  141 ARG   A HE   1 
ATOM   2995 H HH11 . ARG   A 1 141 ? 10.867 -18.126 -1.743  1.00 30.38 ?  141 ARG   A HH11 1 
ATOM   2996 H HH12 . ARG   A 1 141 ? 10.838 -18.975 -0.521  1.00 30.38 ?  141 ARG   A HH12 1 
ATOM   2997 H HH21 . ARG   A 1 141 ? 13.987 -19.926 -0.575  1.00 32.32 ?  141 ARG   A HH21 1 
ATOM   2998 H HH22 . ARG   A 1 141 ? 12.712 -20.059 0.184   1.00 32.32 ?  141 ARG   A HH22 1 
ATOM   2999 N N    . VAL   A 1 142 ? 16.595 -14.526 -2.963  1.00 13.71 ?  142 VAL   A N    1 
ATOM   3000 C CA   . VAL   A 1 142 ? 18.042 -14.733 -2.982  1.00 13.76 ?  142 VAL   A CA   1 
ATOM   3001 C C    . VAL   A 1 142 ? 18.602 -14.704 -1.568  1.00 13.04 ?  142 VAL   A C    1 
ATOM   3002 O O    . VAL   A 1 142 ? 19.463 -15.518 -1.209  1.00 13.57 ?  142 VAL   A O    1 
ATOM   3003 C CB   . VAL   A 1 142 ? 18.744 -13.716 -3.902  1.00 13.73 ?  142 VAL   A CB   1 
ATOM   3004 C CG1  . VAL   A 1 142 ? 20.262 -13.926 -3.860  1.00 13.97 ?  142 VAL   A CG1  1 
ATOM   3005 C CG2  . VAL   A 1 142 ? 18.250 -13.845 -5.322  1.00 15.48 ?  142 VAL   A CG2  1 
ATOM   3006 H H    . VAL   A 1 142 ? 16.328 -13.817 -3.383  1.00 16.43 ?  142 VAL   A H    1 
ATOM   3007 H HA   . VAL   A 1 142 ? 18.221 -15.606 -3.346  1.00 16.48 ?  142 VAL   A HA   1 
ATOM   3008 H HB   . VAL   A 1 142 ? 18.564 -12.809 -3.597  1.00 16.45 ?  142 VAL   A HB   1 
ATOM   3009 H HG11 . VAL   A 1 142 ? 20.678 -13.424 -4.584  1.00 16.73 ?  142 VAL   A HG11 1 
ATOM   3010 H HG12 . VAL   A 1 142 ? 20.612 -13.608 -3.009  1.00 16.73 ?  142 VAL   A HG12 1 
ATOM   3011 H HG13 . VAL   A 1 142 ? 20.458 -14.869 -3.965  1.00 16.73 ?  142 VAL   A HG13 1 
ATOM   3012 H HG21 . VAL   A 1 142 ? 18.713 -13.197 -5.881  1.00 18.54 ?  142 VAL   A HG21 1 
ATOM   3013 H HG22 . VAL   A 1 142 ? 18.435 -14.742 -5.637  1.00 18.54 ?  142 VAL   A HG22 1 
ATOM   3014 H HG23 . VAL   A 1 142 ? 17.298 -13.674 -5.339  1.00 18.54 ?  142 VAL   A HG23 1 
ATOM   3015 N N    . CYS   A 1 143 ? 18.130 -13.769 -0.743  1.00 12.89 ?  143 CYS   A N    1 
ATOM   3016 C CA   . CYS   A 1 143 ? 18.585 -13.709 0.640   1.00 13.40 ?  143 CYS   A CA   1 
ATOM   3017 C C    . CYS   A 1 143 ? 18.358 -15.045 1.341   1.00 13.25 ?  143 CYS   A C    1 
ATOM   3018 O O    . CYS   A 1 143 ? 19.275 -15.617 1.939   1.00 13.53 ?  143 CYS   A O    1 
ATOM   3019 C CB   . CYS   A 1 143 ? 17.851 -12.590 1.376   1.00 14.35 ?  143 CYS   A CB   1 
ATOM   3020 S SG   . CYS   A 1 143 ? 18.315 -12.401 3.089   1.00 14.12 ?  143 CYS   A SG   1 
ATOM   3021 H H    . CYS   A 1 143 ? 17.544 -13.177 -0.951  1.00 15.44 ?  143 CYS   A H    1 
ATOM   3022 H HA   . CYS   A 1 143 ? 19.535 -13.521 0.657   1.00 16.05 ?  143 CYS   A HA   1 
ATOM   3023 H HB2  . CYS   A 1 143 ? 18.032 -11.754 0.927   1.00 17.19 ?  143 CYS   A HB2  1 
ATOM   3024 H HB3  . CYS   A 1 143 ? 16.901 -12.777 1.348   1.00 17.19 ?  143 CYS   A HB3  1 
ATOM   3025 H HG   . CYS   A 1 143 ? 17.723 -11.465 3.545   1.00 16.91 ?  143 CYS   A HG   1 
ATOM   3026 N N    . VAL   A 1 144 ? 17.128 -15.559 1.272   1.00 13.74 ?  144 VAL   A N    1 
ATOM   3027 C CA   . VAL   A 1 144 ? 16.778 -16.786 1.976   1.00 15.62 ?  144 VAL   A CA   1 
ATOM   3028 C C    . VAL   A 1 144 ? 17.594 -17.959 1.462   1.00 15.58 ?  144 VAL   A C    1 
ATOM   3029 O O    . VAL   A 1 144 ? 17.958 -18.862 2.228   1.00 16.50 ?  144 VAL   A O    1 
ATOM   3030 C CB   . VAL   A 1 144 ? 15.262 -17.031 1.841   1.00 18.69 ?  144 VAL   A CB   1 
ATOM   3031 C CG1  . VAL   A 1 144 ? 14.904 -18.470 2.173   1.00 21.19 ?  144 VAL   A CG1  1 
ATOM   3032 C CG2  . VAL   A 1 144 ? 14.509 -16.035 2.717   1.00 18.85 ?  144 VAL   A CG2  1 
ATOM   3033 H H    . VAL   A 1 144 ? 16.475 -15.206 0.827   1.00 16.45 ?  144 VAL   A H    1 
ATOM   3034 H HA   . VAL   A 1 144 ? 16.970 -16.676 2.917   1.00 18.72 ?  144 VAL   A HA   1 
ATOM   3035 H HB   . VAL   A 1 144 ? 14.995 -16.865 0.918   1.00 22.39 ?  144 VAL   A HB   1 
ATOM   3036 H HG11 . VAL   A 1 144 ? 13.951 -18.522 2.358   1.00 25.40 ?  144 VAL   A HG11 1 
ATOM   3037 H HG12 . VAL   A 1 144 ? 15.123 -19.035 1.417   1.00 25.40 ?  144 VAL   A HG12 1 
ATOM   3038 H HG13 . VAL   A 1 144 ? 15.405 -18.743 2.955   1.00 25.40 ?  144 VAL   A HG13 1 
ATOM   3039 H HG21 . VAL   A 1 144 ? 13.551 -16.196 2.637   1.00 22.60 ?  144 VAL   A HG21 1 
ATOM   3040 H HG22 . VAL   A 1 144 ? 14.782 -16.150 3.639   1.00 22.60 ?  144 VAL   A HG22 1 
ATOM   3041 H HG23 . VAL   A 1 144 ? 14.710 -15.130 2.423   1.00 22.60 ?  144 VAL   A HG23 1 
ATOM   3042 N N    . ASP   A 1 145 ? 17.865 -17.988 0.161   1.00 16.06 ?  145 ASP   A N    1 
ATOM   3043 C CA   . ASP   A 1 145 ? 18.589 -19.095 -0.456  1.00 16.91 ?  145 ASP   A CA   1 
ATOM   3044 C C    . ASP   A 1 145 ? 20.106 -18.942 -0.392  1.00 15.97 ?  145 ASP   A C    1 
ATOM   3045 O O    . ASP   A 1 145 ? 20.817 -19.838 -0.858  1.00 18.26 ?  145 ASP   A O    1 
ATOM   3046 C CB   . ASP   A 1 145 ? 18.169 -19.243 -1.922  1.00 18.69 ?  145 ASP   A CB   1 
ATOM   3047 C CG   . ASP   A 1 145 ? 16.732 -19.713 -2.079  1.00 21.36 ?  145 ASP   A CG   1 
ATOM   3048 O OD1  . ASP   A 1 145 ? 16.149 -20.244 -1.109  1.00 22.45 ?  145 ASP   A OD1  1 
ATOM   3049 O OD2  . ASP   A 1 145 ? 16.187 -19.546 -3.186  1.00 22.69 -1 145 ASP   A OD2  1 
ATOM   3050 H H    . ASP   A 1 145 ? 17.613 -17.381 -0.399  1.00 19.24 ?  145 ASP   A H    1 
ATOM   3051 H HA   . ASP   A 1 145 ? 18.350 -19.916 -0.001  1.00 20.27 ?  145 ASP   A HA   1 
ATOM   3052 H HB2  . ASP   A 1 145 ? 18.264 -18.383 -2.366  1.00 22.40 ?  145 ASP   A HB2  1 
ATOM   3053 H HB3  . ASP   A 1 145 ? 18.747 -19.897 -2.348  1.00 22.40 ?  145 ASP   A HB3  1 
ATOM   3054 N N    . THR   A 1 146 ? 20.623 -17.846 0.164   1.00 13.90 ?  146 THR   A N    1 
ATOM   3055 C CA   . THR   A 1 146 ? 22.060 -17.587 0.179   1.00 13.26 ?  146 THR   A CA   1 
ATOM   3056 C C    . THR   A 1 146 ? 22.612 -17.406 1.582   1.00 13.35 ?  146 THR   A C    1 
ATOM   3057 O O    . THR   A 1 146 ? 23.682 -17.951 1.902   1.00 14.72 ?  146 THR   A O    1 
ATOM   3058 C CB   . THR   A 1 146 ? 22.383 -16.342 -0.672  1.00 13.88 ?  146 THR   A CB   1 
ATOM   3059 O OG1  . THR   A 1 146 ? 21.878 -16.522 -1.996  1.00 14.25 ?  146 THR   A OG1  1 
ATOM   3060 C CG2  . THR   A 1 146 ? 23.887 -16.104 -0.740  1.00 14.44 ?  146 THR   A CG2  1 
ATOM   3061 H H    . THR   A 1 146 ? 20.155 -17.221 0.534   1.00 16.66 ?  146 THR   A H    1 
ATOM   3062 H HA   . THR   A 1 146 ? 22.520 -18.335 -0.220  1.00 15.89 ?  146 THR   A HA   1 
ATOM   3063 H HB   . THR   A 1 146 ? 21.974 -15.557 -0.276  1.00 16.63 ?  146 THR   A HB   1 
ATOM   3064 H HG1  . THR   A 1 146 ? 21.046 -16.617 -1.972  1.00 17.08 ?  146 THR   A HG1  1 
ATOM   3065 H HG21 . THR   A 1 146 ? 24.088 -15.445 -1.424  1.00 17.30 ?  146 THR   A HG21 1 
ATOM   3066 H HG22 . THR   A 1 146 ? 24.213 -15.774 0.114   1.00 17.30 ?  146 THR   A HG22 1 
ATOM   3067 H HG23 . THR   A 1 146 ? 24.345 -16.930 -0.955  1.00 17.30 ?  146 THR   A HG23 1 
ATOM   3068 N N    . VAL   A 1 147 ? 21.942 -16.619 2.414   1.00 12.79 ?  147 VAL   A N    1 
ATOM   3069 C CA   . VAL   A 1 147 ? 22.439 -16.319 3.748   1.00 13.12 ?  147 VAL   A CA   1 
ATOM   3070 C C    . VAL   A 1 147 ? 22.116 -17.486 4.670   1.00 13.58 ?  147 VAL   A C    1 
ATOM   3071 O O    . VAL   A 1 147 ? 20.975 -17.969 4.717   1.00 14.43 ?  147 VAL   A O    1 
ATOM   3072 C CB   . VAL   A 1 147 ? 21.823 -15.008 4.267   1.00 13.25 ?  147 VAL   A CB   1 
ATOM   3073 C CG1  . VAL   A 1 147 ? 22.385 -14.677 5.629   1.00 14.89 ?  147 VAL   A CG1  1 
ATOM   3074 C CG2  . VAL   A 1 147 ? 22.065 -13.876 3.275   1.00 13.86 ?  147 VAL   A CG2  1 
ATOM   3075 H H    . VAL   A 1 147 ? 21.193 -16.241 2.231   1.00 15.32 ?  147 VAL   A H    1 
ATOM   3076 H HA   . VAL   A 1 147 ? 23.403 -16.213 3.719   1.00 15.71 ?  147 VAL   A HA   1 
ATOM   3077 H HB   . VAL   A 1 147 ? 20.869 -15.129 4.368   1.00 15.88 ?  147 VAL   A HB   1 
ATOM   3078 H HG11 . VAL   A 1 147 ? 22.121 -13.779 5.868   1.00 17.83 ?  147 VAL   A HG11 1 
ATOM   3079 H HG12 . VAL   A 1 147 ? 22.035 -15.310 6.280   1.00 17.83 ?  147 VAL   A HG12 1 
ATOM   3080 H HG13 . VAL   A 1 147 ? 23.353 -14.743 5.596   1.00 17.83 ?  147 VAL   A HG13 1 
ATOM   3081 H HG21 . VAL   A 1 147 ? 21.762 -13.043 3.672   1.00 16.60 ?  147 VAL   A HG21 1 
ATOM   3082 H HG22 . VAL   A 1 147 ? 23.008 -13.826 3.075   1.00 16.60 ?  147 VAL   A HG22 1 
ATOM   3083 H HG23 . VAL   A 1 147 ? 21.559 -14.058 2.467   1.00 16.60 ?  147 VAL   A HG23 1 
ATOM   3084 N N    . ARG   A 1 148 ? 23.130 -17.940 5.405   1.00 14.12 ?  148 ARG   A N    1 
ATOM   3085 C CA   . ARG   A 1 148 ? 22.999 -19.012 6.379   1.00 14.25 ?  148 ARG   A CA   1 
ATOM   3086 C C    . ARG   A 1 148 ? 23.121 -18.529 7.813   1.00 14.33 ?  148 ARG   A C    1 
ATOM   3087 O O    . ARG   A 1 148 ? 22.723 -19.256 8.733   1.00 15.77 ?  148 ARG   A O    1 
ATOM   3088 C CB   . ARG   A 1 148 ? 24.057 -20.099 6.125   1.00 15.31 ?  148 ARG   A CB   1 
ATOM   3089 C CG   . ARG   A 1 148 ? 23.939 -20.742 4.757   1.00 16.36 ?  148 ARG   A CG   1 
ATOM   3090 C CD   . ARG   A 1 148 ? 25.052 -21.767 4.502   1.00 17.13 ?  148 ARG   A CD   1 
ATOM   3091 N NE   . ARG   A 1 148 ? 26.389 -21.182 4.538   1.00 16.82 ?  148 ARG   A NE   1 
ATOM   3092 C CZ   . ARG   A 1 148 ? 26.908 -20.452 3.561   1.00 16.39 ?  148 ARG   A CZ   1 
ATOM   3093 N NH1  . ARG   A 1 148 ? 26.254 -20.252 2.427   1.00 16.76 ?  148 ARG   A NH1  1 
ATOM   3094 N NH2  . ARG   A 1 148 ? 28.110 -19.894 3.730   1.00 16.46 ?  148 ARG   A NH2  1 
ATOM   3095 H H    . ARG   A 1 148 ? 23.930 -17.624 5.353   1.00 16.91 ?  148 ARG   A H    1 
ATOM   3096 H HA   . ARG   A 1 148 ? 22.130 -19.421 6.285   1.00 17.07 ?  148 ARG   A HA   1 
ATOM   3097 H HB2  . ARG   A 1 148 ? 24.943 -19.711 6.193   1.00 18.34 ?  148 ARG   A HB2  1 
ATOM   3098 H HB3  . ARG   A 1 148 ? 23.956 -20.805 6.788   1.00 18.34 ?  148 ARG   A HB3  1 
ATOM   3099 H HG2  . ARG   A 1 148 ? 23.083 -21.193 4.696   1.00 19.60 ?  148 ARG   A HG2  1 
ATOM   3100 H HG3  . ARG   A 1 148 ? 24.000 -20.047 4.082   1.00 19.60 ?  148 ARG   A HG3  1 
ATOM   3101 H HD2  . ARG   A 1 148 ? 25.007 -22.452 5.186   1.00 20.53 ?  148 ARG   A HD2  1 
ATOM   3102 H HD3  . ARG   A 1 148 ? 24.919 -22.159 3.627   1.00 20.53 ?  148 ARG   A HD3  1 
ATOM   3103 H HE   . ARG   A 1 148 ? 26.863 -21.303 5.244   1.00 20.15 ?  148 ARG   A HE   1 
ATOM   3104 H HH11 . ARG   A 1 148 ? 25.481 -20.598 2.309   1.00 20.08 ?  148 ARG   A HH11 1 
ATOM   3105 H HH12 . ARG   A 1 148 ? 26.613 -19.773 1.806   1.00 20.08 ?  148 ARG   A HH12 1 
ATOM   3106 H HH21 . ARG   A 1 148 ? 28.538 -20.009 4.469   1.00 19.73 ?  148 ARG   A HH21 1 
ATOM   3107 H HH22 . ARG   A 1 148 ? 28.459 -19.415 3.106   1.00 19.73 ?  148 ARG   A HH22 1 
ATOM   3108 N N    . THR   A 1 149 ? 23.662 -17.331 8.017   1.00 14.46 ?  149 THR   A N    1 
ATOM   3109 C CA   . THR   A 1 149 ? 23.739 -16.719 9.329   1.00 14.50 ?  149 THR   A CA   1 
ATOM   3110 C C    . THR   A 1 149 ? 22.406 -16.029 9.628   1.00 13.96 ?  149 THR   A C    1 
ATOM   3111 O O    . THR   A 1 149 ? 21.478 -16.031 8.806   1.00 14.85 ?  149 THR   A O    1 
ATOM   3112 C CB   . THR   A 1 149 ? 24.938 -15.775 9.376   1.00 15.28 ?  149 THR   A CB   1 
ATOM   3113 O OG1  . THR   A 1 149 ? 24.813 -14.851 8.293   1.00 15.32 ?  149 THR   A OG1  1 
ATOM   3114 C CG2  . THR   A 1 149 ? 26.255 -16.569 9.255   1.00 15.75 ?  149 THR   A CG2  1 
ATOM   3115 H H    . THR   A 1 149 ? 24.009 -16.842 7.391   1.00 17.32 ?  149 THR   A H    1 
ATOM   3116 H HA   . THR   A 1 149 ? 23.868 -17.418 9.990   1.00 17.37 ?  149 THR   A HA   1 
ATOM   3117 H HB   . THR   A 1 149 ? 24.935 -15.303 10.220  1.00 18.31 ?  149 THR   A HB   1 
ATOM   3118 H HG1  . THR   A 1 149 ? 25.460 -14.319 8.295   1.00 18.35 ?  149 THR   A HG1  1 
ATOM   3119 H HG21 . THR   A 1 149 ? 27.013 -15.966 9.303   1.00 18.87 ?  149 THR   A HG21 1 
ATOM   3120 H HG22 . THR   A 1 149 ? 26.328 -17.219 9.975   1.00 18.87 ?  149 THR   A HG22 1 
ATOM   3121 H HG23 . THR   A 1 149 ? 26.287 -17.044 8.406   1.00 18.87 ?  149 THR   A HG23 1 
ATOM   3122 N N    . ASN   A 1 150 ? 22.272 -15.483 10.834  1.00 14.11 ?  150 ASN   A N    1 
ATOM   3123 C CA   . ASN   A 1 150 ? 20.985 -14.959 11.302  1.00 14.74 ?  150 ASN   A CA   1 
ATOM   3124 C C    . ASN   A 1 150 ? 20.813 -13.523 10.827  1.00 13.94 ?  150 ASN   A C    1 
ATOM   3125 O O    . ASN   A 1 150 ? 21.564 -12.626 11.235  1.00 15.23 ?  150 ASN   A O    1 
ATOM   3126 C CB   . ASN   A 1 150 ? 20.899 -15.062 12.818  1.00 17.35 ?  150 ASN   A CB   1 
ATOM   3127 C CG   . ASN   A 1 150 ? 20.809 -16.495 13.285  1.00 21.32 ?  150 ASN   A CG   1 
ATOM   3128 O OD1  . ASN   A 1 150 ? 20.209 -17.332 12.611  1.00 22.89 ?  150 ASN   A OD1  1 
ATOM   3129 N ND2  . ASN   A 1 150 ? 21.421 -16.795 14.428  1.00 24.54 ?  150 ASN   A ND2  1 
ATOM   3130 H H    . ASN   A 1 150 ? 22.911 -15.411 11.409  1.00 16.91 ?  150 ASN   A H    1 
ATOM   3131 H HA   . ASN   A 1 150 ? 20.270 -15.499 10.925  1.00 17.65 ?  150 ASN   A HA   1 
ATOM   3132 H HB2  . ASN   A 1 150 ? 21.691 -14.668 13.213  1.00 20.79 ?  150 ASN   A HB2  1 
ATOM   3133 H HB3  . ASN   A 1 150 ? 20.104 -14.600 13.126  1.00 20.79 ?  150 ASN   A HB3  1 
ATOM   3134 H HD21 . ASN   A 1 150 ? 21.404 -17.600 14.738  1.00 29.42 ?  150 ASN   A HD21 1 
ATOM   3135 H HD22 . ASN   A 1 150 ? 21.837 -16.181 14.869  1.00 29.42 ?  150 ASN   A HD22 1 
ATOM   3136 N N    . VAL   A 1 151 ? 19.829 -13.298 9.965   1.00 13.48 ?  151 VAL   A N    1 
ATOM   3137 C CA   . VAL   A 1 151 ? 19.615 -11.994 9.361   1.00 13.67 ?  151 VAL   A CA   1 
ATOM   3138 C C    . VAL   A 1 151 ? 18.228 -11.483 9.723   1.00 13.78 ?  151 VAL   A C    1 
ATOM   3139 O O    . VAL   A 1 151 ? 17.223 -12.195 9.572   1.00 15.18 ?  151 VAL   A O    1 
ATOM   3140 C CB   . VAL   A 1 151 ? 19.889 -12.002 7.843   1.00 15.43 ?  151 VAL   A CB   1 
ATOM   3141 C CG1  . VAL   A 1 151 ? 19.048 -13.026 7.120   1.00 16.77 ?  151 VAL   A CG1  1 
ATOM   3142 C CG2  . VAL   A 1 151 ? 19.709 -10.600 7.260   1.00 15.37 ?  151 VAL   A CG2  1 
ATOM   3143 H H    . VAL   A 1 151 ? 19.263 -13.899 9.714   1.00 16.15 ?  151 VAL   A H    1 
ATOM   3144 H HA   . VAL   A 1 151 ? 20.256 -11.379 9.754   1.00 16.37 ?  151 VAL   A HA   1 
ATOM   3145 H HB   . VAL   A 1 151 ? 20.819 -12.253 7.708   1.00 18.49 ?  151 VAL   A HB   1 
ATOM   3146 H HG11 . VAL   A 1 151 ? 19.241 -12.989 6.172   1.00 20.09 ?  151 VAL   A HG11 1 
ATOM   3147 H HG12 . VAL   A 1 151 ? 19.264 -13.916 7.462   1.00 20.09 ?  151 VAL   A HG12 1 
ATOM   3148 H HG13 . VAL   A 1 151 ? 18.109 -12.840 7.277   1.00 20.09 ?  151 VAL   A HG13 1 
ATOM   3149 H HG21 . VAL   A 1 151 ? 20.018 -10.602 6.339   1.00 18.41 ?  151 VAL   A HG21 1 
ATOM   3150 H HG22 . VAL   A 1 151 ? 18.773 -10.358 7.294   1.00 18.41 ?  151 VAL   A HG22 1 
ATOM   3151 H HG23 . VAL   A 1 151 ? 20.236 -9.972  7.780   1.00 18.41 ?  151 VAL   A HG23 1 
ATOM   3152 N N    . TYR   A 1 152 ? 18.199 -10.242 10.210  1.00 13.90 ?  152 TYR   A N    1 
ATOM   3153 C CA   . TYR   A 1 152 ? 16.999 -9.507  10.588  1.00 12.83 ?  152 TYR   A CA   1 
ATOM   3154 C C    . TYR   A 1 152 ? 16.805 -8.406  9.556   1.00 12.65 ?  152 TYR   A C    1 
ATOM   3155 O O    . TYR   A 1 152 ? 17.572 -7.435  9.520   1.00 13.40 ?  152 TYR   A O    1 
ATOM   3156 C CB   . TYR   A 1 152 ? 17.174 -8.953  11.999  1.00 14.09 ?  152 TYR   A CB   1 
ATOM   3157 C CG   . TYR   A 1 152 ? 17.133 -10.066 13.009  1.00 15.06 ?  152 TYR   A CG   1 
ATOM   3158 C CD1  . TYR   A 1 152 ? 18.260 -10.830 13.288  1.00 16.88 ?  152 TYR   A CD1  1 
ATOM   3159 C CD2  . TYR   A 1 152 ? 15.952 -10.396 13.648  1.00 15.59 ?  152 TYR   A CD2  1 
ATOM   3160 C CE1  . TYR   A 1 152 ? 18.216 -11.881 14.189  1.00 18.27 ?  152 TYR   A CE1  1 
ATOM   3161 C CE2  . TYR   A 1 152 ? 15.892 -11.451 14.552  1.00 17.22 ?  152 TYR   A CE2  1 
ATOM   3162 C CZ   . TYR   A 1 152 ? 17.033 -12.187 14.822  1.00 18.40 ?  152 TYR   A CZ   1 
ATOM   3163 O OH   . TYR   A 1 152 ? 16.988 -13.238 15.721  1.00 21.46 ?  152 TYR   A OH   1 
ATOM   3164 H H    . TYR   A 1 152 ? 18.915 -9.764  10.318  1.00 16.65 ?  152 TYR   A H    1 
ATOM   3165 H HA   . TYR   A 1 152 ? 16.232 -10.101 10.574  1.00 15.36 ?  152 TYR   A HA   1 
ATOM   3166 H HB2  . TYR   A 1 152 ? 18.036 -8.511  12.064  1.00 16.88 ?  152 TYR   A HB2  1 
ATOM   3167 H HB3  . TYR   A 1 152 ? 16.459 -8.332  12.193  1.00 16.88 ?  152 TYR   A HB3  1 
ATOM   3168 H HD1  . TYR   A 1 152 ? 19.061 -10.630 12.859  1.00 20.23 ?  152 TYR   A HD1  1 
ATOM   3169 H HD2  . TYR   A 1 152 ? 15.179 -9.904  13.466  1.00 18.68 ?  152 TYR   A HD2  1 
ATOM   3170 H HE1  . TYR   A 1 152 ? 18.980 -12.378 14.373  1.00 21.90 ?  152 TYR   A HE1  1 
ATOM   3171 H HE2  . TYR   A 1 152 ? 15.090 -11.652 14.983  1.00 20.64 ?  152 TYR   A HE2  1 
ATOM   3172 H HH   . TYR   A 1 152 ? 16.211 -13.304 16.041  1.00 25.72 ?  152 TYR   A HH   1 
ATOM   3173 N N    . LEU   A 1 153 ? 15.810 -8.588  8.691   1.00 12.69 ?  153 LEU   A N    1 
ATOM   3174 C CA   . LEU   A 1 153 ? 15.548 -7.677  7.588   1.00 12.87 ?  153 LEU   A CA   1 
ATOM   3175 C C    . LEU   A 1 153 ? 14.548 -6.610  8.002   1.00 13.06 ?  153 LEU   A C    1 
ATOM   3176 O O    . LEU   A 1 153 ? 13.460 -6.927  8.495   1.00 14.66 ?  153 LEU   A O    1 
ATOM   3177 C CB   . LEU   A 1 153 ? 14.976 -8.441  6.395   1.00 13.22 ?  153 LEU   A CB   1 
ATOM   3178 C CG   . LEU   A 1 153 ? 15.907 -9.462  5.745   1.00 13.34 ?  153 LEU   A CG   1 
ATOM   3179 C CD1  . LEU   A 1 153 ? 15.138 -10.337 4.769   1.00 13.78 ?  153 LEU   A CD1  1 
ATOM   3180 C CD2  . LEU   A 1 153 ? 17.053 -8.741  5.045   1.00 14.18 ?  153 LEU   A CD2  1 
ATOM   3181 H H    . LEU   A 1 153 ? 15.252 -9.248  8.731   1.00 15.20 ?  153 LEU   A H    1 
ATOM   3182 H HA   . LEU   A 1 153 ? 16.373 -7.252  7.327   1.00 15.42 ?  153 LEU   A HA   1 
ATOM   3183 H HB2  . LEU   A 1 153 ? 14.183 -8.913  6.692   1.00 15.84 ?  153 LEU   A HB2  1 
ATOM   3184 H HB3  . LEU   A 1 153 ? 14.732 -7.795  5.715   1.00 15.84 ?  153 LEU   A HB3  1 
ATOM   3185 H HG   . LEU   A 1 153 ? 16.283 -10.034 6.438   1.00 15.98 ?  153 LEU   A HG   1 
ATOM   3186 H HD11 . LEU   A 1 153 ? 15.721 -11.039 4.450   1.00 16.51 ?  153 LEU   A HD11 1 
ATOM   3187 H HD12 . LEU   A 1 153 ? 14.372 -10.717 5.220   1.00 16.51 ?  153 LEU   A HD12 1 
ATOM   3188 H HD13 . LEU   A 1 153 ? 14.844 -9.785  4.024   1.00 16.51 ?  153 LEU   A HD13 1 
ATOM   3189 H HD21 . LEU   A 1 153 ? 17.590 -9.392  4.575   1.00 16.99 ?  153 LEU   A HD21 1 
ATOM   3190 H HD22 . LEU   A 1 153 ? 16.682 -8.097  4.423   1.00 16.99 ?  153 LEU   A HD22 1 
ATOM   3191 H HD23 . LEU   A 1 153 ? 17.592 -8.283  5.712   1.00 16.99 ?  153 LEU   A HD23 1 
ATOM   3192 N N    A ALA   A 1 154 ? 14.919 -5.354  7.777   0.66 13.07 ?  154 ALA   A N    1 
ATOM   3193 N N    B ALA   A 1 154 ? 14.919 -5.348  7.808   0.34 13.01 ?  154 ALA   A N    1 
ATOM   3194 C CA   A ALA   A 1 154 ? 14.038 -4.212  7.977   0.66 13.94 ?  154 ALA   A CA   1 
ATOM   3195 C CA   B ALA   A 1 154 ? 14.062 -4.206  8.104   0.34 13.49 ?  154 ALA   A CA   1 
ATOM   3196 C C    A ALA   A 1 154 ? 13.550 -3.734  6.617   0.66 14.29 ?  154 ALA   A C    1 
ATOM   3197 C C    B ALA   A 1 154 ? 13.606 -3.603  6.781   0.34 13.59 ?  154 ALA   A C    1 
ATOM   3198 O O    A ALA   A 1 154 ? 14.359 -3.425  5.735   0.66 14.46 ?  154 ALA   A O    1 
ATOM   3199 O O    B ALA   A 1 154 ? 14.432 -3.107  6.006   0.34 12.93 ?  154 ALA   A O    1 
ATOM   3200 C CB   A ALA   A 1 154 ? 14.789 -3.083  8.679   0.66 14.25 ?  154 ALA   A CB   1 
ATOM   3201 C CB   B ALA   A 1 154 ? 14.822 -3.170  8.936   0.34 13.84 ?  154 ALA   A CB   1 
ATOM   3202 H H    A ALA   A 1 154 ? 15.708 -5.133  7.509   0.66 15.65 ?  154 ALA   A H    1 
ATOM   3203 H H    B ALA   A 1 154 ? 15.689 -5.120  7.498   0.34 15.58 ?  154 ALA   A H    1 
ATOM   3204 H HA   A ALA   A 1 154 ? 13.274 -4.471  8.515   0.66 16.69 ?  154 ALA   A HA   1 
ATOM   3205 H HA   B ALA   A 1 154 ? 13.283 -4.493  8.609   0.34 16.17 ?  154 ALA   A HA   1 
ATOM   3206 H HB1  A ALA   A 1 154 ? 14.186 -2.331  8.796   0.66 17.07 ?  154 ALA   A HB1  1 
ATOM   3207 H HB1  B ALA   A 1 154 ? 14.236 -2.419  9.123   0.34 16.58 ?  154 ALA   A HB1  1 
ATOM   3208 H HB2  A ALA   A 1 154 ? 15.100 -3.397  9.540   0.66 17.07 ?  154 ALA   A HB2  1 
ATOM   3209 H HB2  B ALA   A 1 154 ? 15.110 -3.577  9.770   0.34 16.58 ?  154 ALA   A HB2  1 
ATOM   3210 H HB3  A ALA   A 1 154 ? 15.544 -2.817  8.129   0.66 17.07 ?  154 ALA   A HB3  1 
ATOM   3211 H HB3  B ALA   A 1 154 ? 15.596 -2.867  8.434   0.34 16.58 ?  154 ALA   A HB3  1 
ATOM   3212 N N    A VAL   A 1 155 ? 12.232 -3.671  6.460   0.66 15.34 ?  155 VAL   A N    1 
ATOM   3213 N N    B VAL   A 1 155 ? 12.300 -3.647  6.527   0.34 14.75 ?  155 VAL   A N    1 
ATOM   3214 C CA   A VAL   A 1 155 ? 11.587 -3.178  5.251   0.66 16.15 ?  155 VAL   A CA   1 
ATOM   3215 C CA   B VAL   A 1 155 ? 11.711 -3.211  5.265   0.34 15.53 ?  155 VAL   A CA   1 
ATOM   3216 C C    A VAL   A 1 155 ? 10.855 -1.896  5.626   0.66 17.23 ?  155 VAL   A C    1 
ATOM   3217 C C    B VAL   A 1 155 ? 10.898 -1.952  5.541   0.34 16.53 ?  155 VAL   A C    1 
ATOM   3218 O O    A VAL   A 1 155 ? 9.927  -1.923  6.442   0.66 17.49 ?  155 VAL   A O    1 
ATOM   3219 O O    B VAL   A 1 155 ? 9.863  -2.001  6.216   0.34 16.59 ?  155 VAL   A O    1 
ATOM   3220 C CB   A VAL   A 1 155 ? 10.628 -4.225  4.662   0.66 15.74 ?  155 VAL   A CB   1 
ATOM   3221 C CB   B VAL   A 1 155 ? 10.848 -4.311  4.628   0.34 15.47 ?  155 VAL   A CB   1 
ATOM   3222 C CG1  A VAL   A 1 155 ? 9.908  -3.673  3.445   0.66 16.69 ?  155 VAL   A CG1  1 
ATOM   3223 C CG1  B VAL   A 1 155 ? 10.150 -3.793  3.378   0.34 15.34 ?  155 VAL   A CG1  1 
ATOM   3224 C CG2  A VAL   A 1 155 ? 11.402 -5.497  4.298   0.66 16.77 ?  155 VAL   A CG2  1 
ATOM   3225 C CG2  B VAL   A 1 155 ? 11.707 -5.523  4.292   0.34 15.87 ?  155 VAL   A CG2  1 
ATOM   3226 H H    A VAL   A 1 155 ? 11.675 -3.928  7.063   0.66 18.38 ?  155 VAL   A H    1 
ATOM   3227 H H    B VAL   A 1 155 ? 11.719 -3.937  7.090   0.34 17.67 ?  155 VAL   A H    1 
ATOM   3228 H HA   A VAL   A 1 155 ? 12.259 -2.971  4.588   0.66 19.36 ?  155 VAL   A HA   1 
ATOM   3229 H HA   B VAL   A 1 155 ? 12.419 -2.985  4.642   0.34 18.61 ?  155 VAL   A HA   1 
ATOM   3230 H HB   A VAL   A 1 155 ? 9.961  -4.458  5.330   0.66 18.86 ?  155 VAL   A HB   1 
ATOM   3231 H HB   B VAL   A 1 155 ? 10.171 -4.591  5.263   0.34 18.53 ?  155 VAL   A HB   1 
ATOM   3232 H HG11 A VAL   A 1 155 ? 9.437  -4.396  3.002   0.66 20.00 ?  155 VAL   A HG11 1 
ATOM   3233 H HG11 B VAL   A 1 155 ? 9.796  -4.547  2.879   0.34 18.38 ?  155 VAL   A HG11 1 
ATOM   3234 H HG12 A VAL   A 1 155 ? 9.273  -2.995  3.730   0.66 20.00 ?  155 VAL   A HG12 1 
ATOM   3235 H HG12 B VAL   A 1 155 ? 9.423  -3.205  3.641   0.34 18.38 ?  155 VAL   A HG12 1 
ATOM   3236 H HG13 A VAL   A 1 155 ? 10.559 -3.284  2.842   0.66 20.00 ?  155 VAL   A HG13 1 
ATOM   3237 H HG13 B VAL   A 1 155 ? 10.789 -3.309  2.834   0.34 18.38 ?  155 VAL   A HG13 1 
ATOM   3238 H HG21 A VAL   A 1 155 ? 10.795 -6.129  3.882   0.66 20.09 ?  155 VAL   A HG21 1 
ATOM   3239 H HG21 B VAL   A 1 155 ? 11.153 -6.192  3.860   0.34 19.02 ?  155 VAL   A HG21 1 
ATOM   3240 H HG22 A VAL   A 1 155 ? 12.114 -5.267  3.680   0.66 20.09 ?  155 VAL   A HG22 1 
ATOM   3241 H HG22 B VAL   A 1 155 ? 12.420 -5.248  3.694   0.34 19.02 ?  155 VAL   A HG22 1 
ATOM   3242 H HG23 A VAL   A 1 155 ? 11.778 -5.883  5.105   0.66 20.09 ?  155 VAL   A HG23 1 
ATOM   3243 H HG23 B VAL   A 1 155 ? 12.082 -5.882  5.111   0.34 19.02 ?  155 VAL   A HG23 1 
ATOM   3244 N N    A PHE   A 1 156 ? 11.290 -0.773  5.049   0.66 18.18 ?  156 PHE   A N    1 
ATOM   3245 N N    B PHE   A 1 156 ? 11.363 -0.824  5.001   0.34 17.78 ?  156 PHE   A N    1 
ATOM   3246 C CA   A PHE   A 1 156 ? 10.754 0.534   5.439   0.66 20.01 ?  156 PHE   A CA   1 
ATOM   3247 C CA   B PHE   A 1 156 ? 10.771 0.477   5.310   0.34 19.55 ?  156 PHE   A CA   1 
ATOM   3248 C C    A PHE   A 1 156 ? 9.290  0.697   5.039   0.66 20.48 ?  156 PHE   A C    1 
ATOM   3249 C C    B PHE   A 1 156 ? 9.345  0.592   4.781   0.34 19.99 ?  156 PHE   A C    1 
ATOM   3250 O O    A PHE   A 1 156 ? 8.489  1.254   5.801   0.66 21.07 ?  156 PHE   A O    1 
ATOM   3251 O O    B PHE   A 1 156 ? 8.437  1.016   5.505   0.34 20.38 ?  156 PHE   A O    1 
ATOM   3252 C CB   A PHE   A 1 156 ? 11.604 1.637   4.803   0.66 21.04 ?  156 PHE   A CB   1 
ATOM   3253 C CB   B PHE   A 1 156 ? 11.663 1.571   4.719   0.34 20.81 ?  156 PHE   A CB   1 
ATOM   3254 C CG   A PHE   A 1 156 ? 11.126 3.030   5.110   0.66 22.89 ?  156 PHE   A CG   1 
ATOM   3255 C CG   B PHE   A 1 156 ? 11.228 2.975   5.042   0.34 22.22 ?  156 PHE   A CG   1 
ATOM   3256 C CD1  A PHE   A 1 156 ? 10.942 3.432   6.423   0.66 23.57 ?  156 PHE   A CD1  1 
ATOM   3257 C CD1  B PHE   A 1 156 ? 11.646 3.595   6.209   0.34 22.80 ?  156 PHE   A CD1  1 
ATOM   3258 C CD2  A PHE   A 1 156 ? 10.875 3.938   4.092   0.66 23.55 ?  156 PHE   A CD2  1 
ATOM   3259 C CD2  B PHE   A 1 156 ? 10.429 3.686   4.160   0.34 22.87 ?  156 PHE   A CD2  1 
ATOM   3260 C CE1  A PHE   A 1 156 ? 10.508 4.713   6.716   0.66 24.43 ?  156 PHE   A CE1  1 
ATOM   3261 C CE1  B PHE   A 1 156 ? 11.257 4.892   6.502   0.34 23.35 ?  156 PHE   A CE1  1 
ATOM   3262 C CE2  A PHE   A 1 156 ? 10.442 5.224   4.378   0.66 24.55 ?  156 PHE   A CE2  1 
ATOM   3263 C CE2  B PHE   A 1 156 ? 10.034 4.983   4.447   0.34 23.31 ?  156 PHE   A CE2  1 
ATOM   3264 C CZ   A PHE   A 1 156 ? 10.260 5.611   5.693   0.66 25.04 ?  156 PHE   A CZ   1 
ATOM   3265 C CZ   B PHE   A 1 156 ? 10.453 5.587   5.619   0.34 23.52 ?  156 PHE   A CZ   1 
ATOM   3266 H H    A PHE   A 1 156 ? 11.902 -0.742  4.439   0.66 21.79 ?  156 PHE   A H    1 
ATOM   3267 H H    B PHE   A 1 156 ? 12.025 -0.788  4.456   0.34 21.30 ?  156 PHE   A H    1 
ATOM   3268 H HA   A PHE   A 1 156 ? 10.823 0.630   6.402   0.66 23.99 ?  156 PHE   A HA   1 
ATOM   3269 H HA   B PHE   A 1 156 ? 10.745 0.595   6.269   0.34 23.43 ?  156 PHE   A HA   1 
ATOM   3270 H HB2  A PHE   A 1 156 ? 12.518 1.562   5.125   0.66 25.22 ?  156 PHE   A HB2  1 
ATOM   3271 H HB2  B PHE   A 1 156 ? 12.572 1.453   5.041   0.34 24.95 ?  156 PHE   A HB2  1 
ATOM   3272 H HB3  A PHE   A 1 156 ? 11.591 1.528   3.838   0.66 25.22 ?  156 PHE   A HB3  1 
ATOM   3273 H HB3  B PHE   A 1 156 ? 11.637 1.483   3.760   0.34 24.95 ?  156 PHE   A HB3  1 
ATOM   3274 H HD1  A PHE   A 1 156 ? 11.113 2.830   7.113   0.66 28.26 ?  156 PHE   A HD1  1 
ATOM   3275 H HD1  B PHE   A 1 156 ? 12.187 3.130   6.806   0.34 27.33 ?  156 PHE   A HD1  1 
ATOM   3276 H HD2  A PHE   A 1 156 ? 10.998 3.680   3.206   0.66 28.23 ?  156 PHE   A HD2  1 
ATOM   3277 H HD2  B PHE   A 1 156 ? 10.147 3.287   3.368   0.34 27.41 ?  156 PHE   A HD2  1 
ATOM   3278 H HE1  A PHE   A 1 156 ? 10.390 4.968   7.603   0.66 29.29 ?  156 PHE   A HE1  1 
ATOM   3279 H HE1  B PHE   A 1 156 ? 11.537 5.294   7.292   0.34 27.99 ?  156 PHE   A HE1  1 
ATOM   3280 H HE2  A PHE   A 1 156 ? 10.274 5.820   3.688   0.66 29.43 ?  156 PHE   A HE2  1 
ATOM   3281 H HE2  B PHE   A 1 156 ? 9.495  5.449   3.850   0.34 27.94 ?  156 PHE   A HE2  1 
ATOM   3282 H HZ   A PHE   A 1 156 ? 9.968  6.468   5.891   0.66 30.02 ?  156 PHE   A HZ   1 
ATOM   3283 H HZ   B PHE   A 1 156 ? 10.189 6.457   5.815   0.34 28.20 ?  156 PHE   A HZ   1 
ATOM   3284 N N    A ASP   A 1 157 ? 8.931  0.232   3.849   0.66 19.86 ?  157 ASP   A N    1 
ATOM   3285 N N    B ASP   A 1 157 ? 9.129  0.229   3.520   0.34 19.96 ?  157 ASP   A N    1 
ATOM   3286 C CA   A ASP   A 1 157 ? 7.622  0.480   3.263   0.66 21.29 ?  157 ASP   A CA   1 
ATOM   3287 C CA   B ASP   A 1 157 ? 7.846  0.466   2.867   0.34 20.05 ?  157 ASP   A CA   1 
ATOM   3288 C C    A ASP   A 1 157 ? 6.636  -0.581  3.741   0.66 21.43 ?  157 ASP   A C    1 
ATOM   3289 C C    B ASP   A 1 157 ? 6.785  -0.490  3.410   0.34 20.56 ?  157 ASP   A C    1 
ATOM   3290 O O    A ASP   A 1 157 ? 6.823  -1.775  3.475   0.66 21.23 ?  157 ASP   A O    1 
ATOM   3291 O O    B ASP   A 1 157 ? 6.889  -1.708  3.233   0.34 20.44 ?  157 ASP   A O    1 
ATOM   3292 C CB   A ASP   A 1 157 ? 7.758  0.438   1.743   0.66 22.95 ?  157 ASP   A CB   1 
ATOM   3293 C CB   B ASP   A 1 157 ? 8.012  0.286   1.362   0.34 19.40 ?  157 ASP   A CB   1 
ATOM   3294 C CG   A ASP   A 1 157 ? 6.535  0.959   1.037   0.66 25.35 ?  157 ASP   A CG   1 
ATOM   3295 C CG   B ASP   A 1 157 ? 6.837  0.824   0.583   0.34 19.07 ?  157 ASP   A CG   1 
ATOM   3296 O OD1  A ASP   A 1 157 ? 6.363  2.193   0.971   0.66 27.01 ?  157 ASP   A OD1  1 
ATOM   3297 O OD1  B ASP   A 1 157 ? 5.752  0.211   0.653   0.34 19.91 ?  157 ASP   A OD1  1 
ATOM   3298 O OD2  A ASP   A 1 157 ? 5.736  0.128   0.556   0.66 26.17 -1 157 ASP   A OD2  1 
ATOM   3299 O OD2  B ASP   A 1 157 ? 6.992  1.871   -0.080  0.34 18.36 -1 157 ASP   A OD2  1 
ATOM   3300 H H    A ASP   A 1 157 ? 9.450  -0.247  3.353   0.66 23.81 ?  157 ASP   A H    1 
ATOM   3301 H H    B ASP   A 1 157 ? 9.714  -0.151  3.015   0.34 23.93 ?  157 ASP   A H    1 
ATOM   3302 H HA   A ASP   A 1 157 ? 7.306  1.354   3.533   0.66 25.51 ?  157 ASP   A HA   1 
ATOM   3303 H HA   B ASP   A 1 157 ? 7.558  1.379   3.034   0.34 24.03 ?  157 ASP   A HA   1 
ATOM   3304 H HB2  A ASP   A 1 157 ? 8.541  0.958   1.485   0.66 27.51 ?  157 ASP   A HB2  1 
ATOM   3305 H HB2  B ASP   A 1 157 ? 8.807  0.757   1.068   0.34 23.25 ?  157 ASP   A HB2  1 
ATOM   3306 H HB3  A ASP   A 1 157 ? 7.873  -0.481  1.463   0.66 27.51 ?  157 ASP   A HB3  1 
ATOM   3307 H HB3  B ASP   A 1 157 ? 8.103  -0.660  1.163   0.34 23.25 ?  157 ASP   A HB3  1 
ATOM   3308 N N    A LYS   A 1 158 ? 5.584  -0.144  4.438   0.66 22.82 ?  158 LYS   A N    1 
ATOM   3309 N N    B LYS   A 1 158 ? 5.751  0.064   4.056   0.34 21.34 ?  158 LYS   A N    1 
ATOM   3310 C CA   A LYS   A 1 158 ? 4.615  -1.090  4.985   0.66 23.99 ?  158 LYS   A CA   1 
ATOM   3311 C CA   B LYS   A 1 158 ? 4.747  -0.782  4.699   0.34 22.16 ?  158 LYS   A CA   1 
ATOM   3312 C C    A LYS   A 1 158 ? 3.914  -1.855  3.870   0.66 23.40 ?  158 LYS   A C    1 
ATOM   3313 C C    B LYS   A 1 158 ? 3.991  -1.624  3.679   0.34 22.23 ?  158 LYS   A C    1 
ATOM   3314 O O    A LYS   A 1 158 ? 3.760  -3.081  3.940   0.66 23.46 ?  158 LYS   A O    1 
ATOM   3315 O O    B LYS   A 1 158 ? 3.673  -2.791  3.939   0.34 22.41 ?  158 LYS   A O    1 
ATOM   3316 C CB   A LYS   A 1 158 ? 3.609  -0.348  5.869   0.66 25.48 ?  158 LYS   A CB   1 
ATOM   3317 C CB   B LYS   A 1 158 ? 3.788  0.062   5.553   0.34 22.99 ?  158 LYS   A CB   1 
ATOM   3318 C CG   A LYS   A 1 158 ? 2.401  -1.174  6.314   0.66 26.29 ?  158 LYS   A CG   1 
ATOM   3319 C CG   B LYS   A 1 158 ? 2.453  0.450   4.900   0.34 23.95 ?  158 LYS   A CG   1 
ATOM   3320 C CD   A LYS   A 1 158 ? 2.793  -2.420  7.116   0.66 27.39 ?  158 LYS   A CD   1 
ATOM   3321 C CD   B LYS   A 1 158 ? 1.349  -0.593  5.118   0.34 24.51 ?  158 LYS   A CD   1 
ATOM   3322 C CE   A LYS   A 1 158 ? 1.551  -3.110  7.692   0.66 27.77 ?  158 LYS   A CE   1 
ATOM   3323 C CE   B LYS   A 1 158 ? 0.617  -0.406  6.438   0.34 24.93 ?  158 LYS   A CE   1 
ATOM   3324 N NZ   A LYS   A 1 158 ? 1.804  -4.495  8.195   0.66 27.48 ?  158 LYS   A NZ   1 
ATOM   3325 N NZ   B LYS   A 1 158 ? -0.479 -1.406  6.584   0.34 25.17 ?  158 LYS   A NZ   1 
ATOM   3326 H H    A LYS   A 1 158 ? 5.416  0.679   4.604   0.66 27.35 ?  158 LYS   A H    1 
ATOM   3327 H H    B LYS   A 1 158 ? 5.619  0.911   4.135   0.34 25.58 ?  158 LYS   A H    1 
ATOM   3328 H HA   A LYS   A 1 158 ? 5.077  -1.734  5.544   0.66 28.76 ?  158 LYS   A HA   1 
ATOM   3329 H HA   B LYS   A 1 158 ? 5.205  -1.390  5.298   0.34 26.57 ?  158 LYS   A HA   1 
ATOM   3330 H HB2  A LYS   A 1 158 ? 4.064  -0.046  6.674   0.66 30.55 ?  158 LYS   A HB2  1 
ATOM   3331 H HB2  B LYS   A 1 158 ? 3.577  -0.441  6.355   0.34 27.56 ?  158 LYS   A HB2  1 
ATOM   3332 H HB3  A LYS   A 1 158 ? 3.272  0.420   5.382   0.66 30.55 ?  158 LYS   A HB3  1 
ATOM   3333 H HB3  B LYS   A 1 158 ? 4.237  0.884   5.800   0.34 27.56 ?  158 LYS   A HB3  1 
ATOM   3334 H HG2  A LYS   A 1 158 ? 1.835  -0.626  6.882   0.66 31.52 ?  158 LYS   A HG2  1 
ATOM   3335 H HG2  B LYS   A 1 158 ? 2.149  1.280   5.298   0.34 28.71 ?  158 LYS   A HG2  1 
ATOM   3336 H HG3  A LYS   A 1 158 ? 1.898  -1.463  5.536   0.66 31.52 ?  158 LYS   A HG3  1 
ATOM   3337 H HG3  B LYS   A 1 158 ? 2.573  0.575   3.948   0.34 28.71 ?  158 LYS   A HG3  1 
ATOM   3338 H HD2  A LYS   A 1 158 ? 3.247  -3.049  6.535   0.66 32.84 ?  158 LYS   A HD2  1 
ATOM   3339 H HD2  B LYS   A 1 158 ? 0.692  -0.517  4.410   0.34 29.39 ?  158 LYS   A HD2  1 
ATOM   3340 H HD3  A LYS   A 1 158 ? 3.370  -2.162  7.852   0.66 32.84 ?  158 LYS   A HD3  1 
ATOM   3341 H HD3  B LYS   A 1 158 ? 1.735  -1.480  5.121   0.34 29.39 ?  158 LYS   A HD3  1 
ATOM   3342 H HE2  A LYS   A 1 158 ? 1.208  -2.584  8.433   0.66 33.30 ?  158 LYS   A HE2  1 
ATOM   3343 H HE2  B LYS   A 1 158 ? 1.237  -0.526  7.174   0.34 29.89 ?  158 LYS   A HE2  1 
ATOM   3344 H HE3  A LYS   A 1 158 ? 0.878  -3.169  7.000   0.66 33.30 ?  158 LYS   A HE3  1 
ATOM   3345 H HE3  B LYS   A 1 158 ? 0.224  0.481   6.471   0.34 29.89 ?  158 LYS   A HE3  1 
ATOM   3346 H HZ1  A LYS   A 1 158 ? 1.052  -4.846  8.519   0.66 32.94 ?  158 LYS   A HZ1  1 
ATOM   3347 H HZ1  B LYS   A 1 158 ? -0.901 -1.288  7.360   0.34 30.17 ?  158 LYS   A HZ1  1 
ATOM   3348 H HZ2  A LYS   A 1 158 ? 2.098  -5.010  7.530   0.66 32.94 ?  158 LYS   A HZ2  1 
ATOM   3349 H HZ2  B LYS   A 1 158 ? -1.067 -1.314  5.921   0.34 30.17 ?  158 LYS   A HZ2  1 
ATOM   3350 H HZ3  A LYS   A 1 158 ? 2.417  -4.481  8.840   0.66 32.94 ?  158 LYS   A HZ3  1 
ATOM   3351 H HZ3  B LYS   A 1 158 ? -0.145 -2.231  6.561   0.34 30.17 ?  158 LYS   A HZ3  1 
ATOM   3352 N N    A ASN   A 1 159 ? 3.488  -1.148  2.823   0.66 23.75 ?  159 ASN   A N    1 
ATOM   3353 N N    B ASN   A 1 159 ? 3.692  -1.055  2.510   0.34 22.87 ?  159 ASN   A N    1 
ATOM   3354 C CA   A ASN   A 1 159 ? 2.840  -1.830  1.711   0.66 23.37 ?  159 ASN   A CA   1 
ATOM   3355 C CA   B ASN   A 1 159 ? 2.960  -1.816  1.505   0.34 23.32 ?  159 ASN   A CA   1 
ATOM   3356 C C    A ASN   A 1 159 ? 3.760  -2.894  1.117   0.66 22.36 ?  159 ASN   A C    1 
ATOM   3357 C C    B ASN   A 1 159 ? 3.826  -2.895  0.868   0.34 22.59 ?  159 ASN   A C    1 
ATOM   3358 O O    A ASN   A 1 159 ? 3.325  -4.020  0.847   0.66 21.30 ?  159 ASN   A O    1 
ATOM   3359 O O    B ASN   A 1 159 ? 3.309  -3.938  0.456   0.34 22.53 ?  159 ASN   A O    1 
ATOM   3360 C CB   A ASN   A 1 159 ? 2.378  -0.812  0.664   0.66 25.46 ?  159 ASN   A CB   1 
ATOM   3361 C CB   B ASN   A 1 159 ? 2.380  -0.878  0.444   0.34 24.96 ?  159 ASN   A CB   1 
ATOM   3362 C CG   A ASN   A 1 159 ? 1.137  -0.039  1.106   0.66 28.06 ?  159 ASN   A CG   1 
ATOM   3363 C CG   B ASN   A 1 159 ? 1.269  0.006   0.987   0.34 26.62 ?  159 ASN   A CG   1 
ATOM   3364 O OD1  A ASN   A 1 159 ? 0.272  -0.579  1.791   0.66 29.16 ?  159 ASN   A OD1  1 
ATOM   3365 O OD1  B ASN   A 1 159 ? 1.135  1.167   0.593   0.34 27.67 ?  159 ASN   A OD1  1 
ATOM   3366 N ND2  A ASN   A 1 159 ? 1.047  1.225   0.710   0.66 29.63 ?  159 ASN   A ND2  1 
ATOM   3367 N ND2  B ASN   A 1 159 ? 0.465  -0.540  1.896   0.34 27.12 ?  159 ASN   A ND2  1 
ATOM   3368 H H    A ASN   A 1 159 ? 3.572  -0.300  2.735   0.66 28.48 ?  159 ASN   A H    1 
ATOM   3369 H H    B ASN   A 1 159 ? 3.888  -0.248  2.287   0.34 27.41 ?  159 ASN   A H    1 
ATOM   3370 H HA   A ASN   A 1 159 ? 2.055  -2.286  2.045   0.66 28.02 ?  159 ASN   A HA   1 
ATOM   3371 H HA   B ASN   A 1 159 ? 2.229  -2.274  1.944   0.34 27.96 ?  159 ASN   A HA   1 
ATOM   3372 H HB2  A ASN   A 1 159 ? 3.086  -0.170  0.510   0.66 30.52 ?  159 ASN   A HB2  1 
ATOM   3373 H HB2  B ASN   A 1 159 ? 3.084  -0.298  0.114   0.34 29.92 ?  159 ASN   A HB2  1 
ATOM   3374 H HB3  A ASN   A 1 159 ? 2.164  -1.279  -0.157  0.66 30.52 ?  159 ASN   A HB3  1 
ATOM   3375 H HB3  B ASN   A 1 159 ? 2.016  -1.407  -0.281  0.34 29.92 ?  159 ASN   A HB3  1 
ATOM   3376 H HD21 A ASN   A 1 159 ? 0.367  1.694   0.938   0.66 35.53 ?  159 ASN   A HD21 1 
ATOM   3377 H HD21 B ASN   A 1 159 ? -0.177 -0.081  2.230   0.34 32.51 ?  159 ASN   A HD21 1 
ATOM   3378 H HD22 A ASN   A 1 159 ? 1.671  1.570   0.236   0.66 35.53 ?  159 ASN   A HD22 1 
ATOM   3379 H HD22 B ASN   A 1 159 ? 0.583  -1.353  2.155   0.34 32.51 ?  159 ASN   A HD22 1 
ATOM   3380 N N    A LEU   A 1 160 ? 5.046  -2.577  0.957   0.66 21.66 ?  160 LEU   A N    1 
ATOM   3381 N N    B LEU   A 1 160 ? 5.138  -2.673  0.787   0.34 21.57 ?  160 LEU   A N    1 
ATOM   3382 C CA   A LEU   A 1 160 ? 5.981  -3.580  0.456   0.66 20.63 ?  160 LEU   A CA   1 
ATOM   3383 C CA   B LEU   A 1 160 ? 6.025  -3.697  0.243   0.34 20.35 ?  160 LEU   A CA   1 
ATOM   3384 C C    A LEU   A 1 160 ? 6.159  -4.715  1.456   0.66 19.81 ?  160 LEU   A C    1 
ATOM   3385 C C    B LEU   A 1 160 ? 6.170  -4.867  1.207   0.34 19.41 ?  160 LEU   A C    1 
ATOM   3386 O O    A LEU   A 1 160 ? 6.201  -5.889  1.069   0.66 20.72 ?  160 LEU   A O    1 
ATOM   3387 O O    B LEU   A 1 160 ? 6.182  -6.031  0.786   0.34 19.65 ?  160 LEU   A O    1 
ATOM   3388 C CB   A LEU   A 1 160 ? 7.328  -2.941  0.129   0.66 20.19 ?  160 LEU   A CB   1 
ATOM   3389 C CB   B LEU   A 1 160 ? 7.388  -3.083  -0.061  0.34 20.12 ?  160 LEU   A CB   1 
ATOM   3390 C CG   A LEU   A 1 160 ? 8.386  -3.952  -0.308  0.66 20.39 ?  160 LEU   A CG   1 
ATOM   3391 C CG   B LEU   A 1 160 ? 8.487  -4.046  -0.503  0.34 20.21 ?  160 LEU   A CG   1 
ATOM   3392 C CD1  A LEU   A 1 160 ? 7.924  -4.693  -1.544  0.66 21.38 ?  160 LEU   A CD1  1 
ATOM   3393 C CD1  B LEU   A 1 160 ? 8.050  -4.829  -1.722  0.34 20.55 ?  160 LEU   A CD1  1 
ATOM   3394 C CD2  A LEU   A 1 160 ? 9.708  -3.263  -0.565  0.66 19.95 ?  160 LEU   A CD2  1 
ATOM   3395 C CD2  B LEU   A 1 160 ? 9.763  -3.277  -0.789  0.34 20.20 ?  160 LEU   A CD2  1 
ATOM   3396 H H    A LEU   A 1 160 ? 5.399  -1.811  1.143   0.66 25.97 ?  160 LEU   A H    1 
ATOM   3397 H H    B LEU   A 1 160 ? 5.529  -1.950  1.039   0.34 25.85 ?  160 LEU   A H    1 
ATOM   3398 H HA   A LEU   A 1 160 ? 5.623  -3.951  -0.361  0.66 24.73 ?  160 LEU   A HA   1 
ATOM   3399 H HA   B LEU   A 1 160 ? 5.649  -4.029  -0.584  0.34 24.39 ?  160 LEU   A HA   1 
ATOM   3400 H HB2  A LEU   A 1 160 ? 7.212  -2.291  -0.591  0.66 24.20 ?  160 LEU   A HB2  1 
ATOM   3401 H HB2  B LEU   A 1 160 ? 7.279  -2.418  -0.762  0.34 24.11 ?  160 LEU   A HB2  1 
ATOM   3402 H HB3  A LEU   A 1 160 ? 7.663  -2.494  0.921   0.66 24.20 ?  160 LEU   A HB3  1 
ATOM   3403 H HB3  B LEU   A 1 160 ? 7.703  -2.654  0.746   0.34 24.11 ?  160 LEU   A HB3  1 
ATOM   3404 H HG   A LEU   A 1 160 ? 8.527  -4.597  0.399   0.66 24.44 ?  160 LEU   A HG   1 
ATOM   3405 H HG   B LEU   A 1 160 ? 8.670  -4.674  0.215   0.34 24.23 ?  160 LEU   A HG   1 
ATOM   3406 H HD11 A LEU   A 1 160 ? 8.654  -5.235  -1.873  0.66 25.63 ?  160 LEU   A HD11 1 
ATOM   3407 H HD11 B LEU   A 1 160 ? 8.797  -5.356  -2.040  0.34 24.63 ?  160 LEU   A HD11 1 
ATOM   3408 H HD12 A LEU   A 1 160 ? 7.172  -5.261  -1.311  0.66 25.63 ?  160 LEU   A HD12 1 
ATOM   3409 H HD12 B LEU   A 1 160 ? 7.314  -5.412  -1.475  0.34 24.63 ?  160 LEU   A HD12 1 
ATOM   3410 H HD13 A LEU   A 1 160 ? 7.656  -4.048  -2.218  0.66 25.63 ?  160 LEU   A HD13 1 
ATOM   3411 H HD13 B LEU   A 1 160 ? 7.765  -4.207  -2.409  0.34 24.63 ?  160 LEU   A HD13 1 
ATOM   3412 H HD21 A LEU   A 1 160 ? 10.362 -3.927  -0.837  0.66 23.92 ?  160 LEU   A HD21 1 
ATOM   3413 H HD21 B LEU   A 1 160 ? 10.452 -3.900  -1.066  0.34 24.21 ?  160 LEU   A HD21 1 
ATOM   3414 H HD22 A LEU   A 1 160 ? 9.593  -2.606  -1.271  0.66 23.92 ?  160 LEU   A HD22 1 
ATOM   3415 H HD22 B LEU   A 1 160 ? 9.592  -2.636  -1.497  0.34 24.21 ?  160 LEU   A HD22 1 
ATOM   3416 H HD23 A LEU   A 1 160 ? 10.002 -2.824  0.249   0.66 23.92 ?  160 LEU   A HD23 1 
ATOM   3417 H HD23 B LEU   A 1 160 ? 10.040 -2.813  0.017   0.34 24.21 ?  160 LEU   A HD23 1 
ATOM   3418 N N    A TYR   A 1 161 ? 6.279  -4.383  2.742   0.66 19.03 ?  161 TYR   A N    1 
ATOM   3419 N N    B TYR   A 1 161 ? 6.287  -4.575  2.504   0.34 18.53 ?  161 TYR   A N    1 
ATOM   3420 C CA   A TYR   A 1 161 ? 6.395  -5.417  3.765   0.66 18.77 ?  161 TYR   A CA   1 
ATOM   3421 C CA   B TYR   A 1 161 ? 6.398  -5.630  3.505   0.34 18.25 ?  161 TYR   A CA   1 
ATOM   3422 C C    A TYR   A 1 161 ? 5.251  -6.419  3.666   0.66 19.49 ?  161 TYR   A C    1 
ATOM   3423 C C    B TYR   A 1 161 ? 5.206  -6.575  3.434   0.34 18.93 ?  161 TYR   A C    1 
ATOM   3424 O O    A TYR   A 1 161 ? 5.469  -7.636  3.695   0.66 18.92 ?  161 TYR   A O    1 
ATOM   3425 O O    B TYR   A 1 161 ? 5.370  -7.797  3.342   0.34 18.26 ?  161 TYR   A O    1 
ATOM   3426 C CB   A TYR   A 1 161 ? 6.442  -4.784  5.158   0.66 19.02 ?  161 TYR   A CB   1 
ATOM   3427 C CB   B TYR   A 1 161 ? 6.507  -5.007  4.897   0.34 17.61 ?  161 TYR   A CB   1 
ATOM   3428 C CG   A TYR   A 1 161 ? 6.354  -5.812  6.257   0.66 18.39 ?  161 TYR   A CG   1 
ATOM   3429 C CG   B TYR   A 1 161 ? 6.351  -6.009  6.013   0.34 16.92 ?  161 TYR   A CG   1 
ATOM   3430 C CD1  A TYR   A 1 161 ? 7.486  -6.490  6.689   0.66 17.99 ?  161 TYR   A CD1  1 
ATOM   3431 C CD1  B TYR   A 1 161 ? 7.432  -6.762  6.444   0.34 16.70 ?  161 TYR   A CD1  1 
ATOM   3432 C CD2  A TYR   A 1 161 ? 5.136  -6.121  6.851   0.66 18.90 ?  161 TYR   A CD2  1 
ATOM   3433 C CD2  B TYR   A 1 161 ? 5.122  -6.209  6.634   0.34 17.10 ?  161 TYR   A CD2  1 
ATOM   3434 C CE1  A TYR   A 1 161 ? 7.408  -7.442  7.684   0.66 18.59 ?  161 TYR   A CE1  1 
ATOM   3435 C CE1  B TYR   A 1 161 ? 7.299  -7.685  7.456   0.34 16.59 ?  161 TYR   A CE1  1 
ATOM   3436 C CE2  A TYR   A 1 161 ? 5.047  -7.073  7.847   0.66 18.97 ?  161 TYR   A CE2  1 
ATOM   3437 C CE2  B TYR   A 1 161 ? 4.979  -7.133  7.652   0.34 16.93 ?  161 TYR   A CE2  1 
ATOM   3438 C CZ   A TYR   A 1 161 ? 6.187  -7.733  8.261   0.66 18.94 ?  161 TYR   A CZ   1 
ATOM   3439 C CZ   B TYR   A 1 161 ? 6.073  -7.868  8.059   0.34 16.82 ?  161 TYR   A CZ   1 
ATOM   3440 O OH   A TYR   A 1 161 ? 6.120  -8.685  9.253   0.66 19.37 ?  161 TYR   A OH   1 
ATOM   3441 O OH   B TYR   A 1 161 ? 5.954  -8.793  9.070   0.34 17.10 ?  161 TYR   A OH   1 
ATOM   3442 H H    A TYR   A 1 161 ? 6.295  -3.576  3.041   0.66 22.81 ?  161 TYR   A H    1 
ATOM   3443 H H    B TYR   A 1 161 ? 6.299  -3.782  2.825   0.34 22.21 ?  161 TYR   A H    1 
ATOM   3444 H HA   A TYR   A 1 161 ? 7.219  -5.900  3.632   0.66 22.49 ?  161 TYR   A HA   1 
ATOM   3445 H HA   B TYR   A 1 161 ? 7.202  -6.146  3.343   0.34 21.88 ?  161 TYR   A HA   1 
ATOM   3446 H HB2  A TYR   A 1 161 ? 7.279  -4.302  5.259   0.66 22.79 ?  161 TYR   A HB2  1 
ATOM   3447 H HB2  B TYR   A 1 161 ? 7.380  -4.592  4.989   0.34 21.10 ?  161 TYR   A HB2  1 
ATOM   3448 H HB3  A TYR   A 1 161 ? 5.695  -4.170  5.257   0.66 22.79 ?  161 TYR   A HB3  1 
ATOM   3449 H HB3  B TYR   A 1 161 ? 5.812  -4.337  4.999   0.34 21.10 ?  161 TYR   A HB3  1 
ATOM   3450 H HD1  A TYR   A 1 161 ? 8.311  -6.298  6.306   0.66 21.56 ?  161 TYR   A HD1  1 
ATOM   3451 H HD1  B TYR   A 1 161 ? 8.261  -6.644  6.040   0.34 20.01 ?  161 TYR   A HD1  1 
ATOM   3452 H HD2  A TYR   A 1 161 ? 4.364  -5.682  6.575   0.66 22.65 ?  161 TYR   A HD2  1 
ATOM   3453 H HD2  B TYR   A 1 161 ? 4.382  -5.714  6.362   0.34 20.49 ?  161 TYR   A HD2  1 
ATOM   3454 H HE1  A TYR   A 1 161 ? 8.175  -7.888  7.969   0.66 22.28 ?  161 TYR   A HE1  1 
ATOM   3455 H HE1  B TYR   A 1 161 ? 8.033  -8.184  7.735   0.34 19.88 ?  161 TYR   A HE1  1 
ATOM   3456 H HE2  A TYR   A 1 161 ? 4.223  -7.271  8.238   0.66 22.74 ?  161 TYR   A HE2  1 
ATOM   3457 H HE2  B TYR   A 1 161 ? 4.150  -7.258  8.061   0.34 20.28 ?  161 TYR   A HE2  1 
ATOM   3458 H HH   A TYR   A 1 161 ? 5.319  -8.767  9.519   0.66 23.22 ?  161 TYR   A HH   1 
ATOM   3459 H HH   B TYR   A 1 161 ? 5.163  -8.799  9.365   0.34 20.49 ?  161 TYR   A HH   1 
ATOM   3460 N N    A ASP   A 1 162 ? 4.016  -5.920  3.541   0.66 20.57 ?  162 ASP   A N    1 
ATOM   3461 N N    B ASP   A 1 162 ? 3.992  -6.020  3.482   0.34 20.14 ?  162 ASP   A N    1 
ATOM   3462 C CA   A ASP   A 1 162 ? 2.862  -6.817  3.483   0.66 21.48 ?  162 ASP   A CA   1 
ATOM   3463 C CA   B ASP   A 1 162 ? 2.792  -6.845  3.377   0.34 21.29 ?  162 ASP   A CA   1 
ATOM   3464 C C    A ASP   A 1 162 ? 2.906  -7.693  2.235   0.66 21.05 ?  162 ASP   A C    1 
ATOM   3465 C C    B ASP   A 1 162 ? 2.827  -7.700  2.118   0.34 21.60 ?  162 ASP   A C    1 
ATOM   3466 O O    A ASP   A 1 162 ? 2.552  -8.878  2.285   0.66 22.06 ?  162 ASP   A O    1 
ATOM   3467 O O    B ASP   A 1 162 ? 2.420  -8.868  2.136   0.34 21.80 ?  162 ASP   A O    1 
ATOM   3468 C CB   A ASP   A 1 162 ? 1.555  -6.017  3.523   0.66 23.00 ?  162 ASP   A CB   1 
ATOM   3469 C CB   B ASP   A 1 162 ? 1.543  -5.958  3.379   0.34 22.33 ?  162 ASP   A CB   1 
ATOM   3470 C CG   A ASP   A 1 162 ? 1.259  -5.419  4.888   0.66 24.71 ?  162 ASP   A CG   1 
ATOM   3471 C CG   B ASP   A 1 162 ? 1.271  -5.321  4.727   0.34 23.54 ?  162 ASP   A CG   1 
ATOM   3472 O OD1  A ASP   A 1 162 ? 1.858  -5.860  5.886   0.66 25.54 ?  162 ASP   A OD1  1 
ATOM   3473 O OD1  B ASP   A 1 162 ? 1.955  -5.671  5.709   0.34 23.99 ?  162 ASP   A OD1  1 
ATOM   3474 O OD2  A ASP   A 1 162 ? 0.383  -4.526  4.960   0.66 26.08 -1 162 ASP   A OD2  1 
ATOM   3475 O OD2  B ASP   A 1 162 ? 0.359  -4.469  4.802   0.34 24.34 -1 162 ASP   A OD2  1 
ATOM   3476 H H    A ASP   A 1 162 ? 3.819  -5.078  3.487   0.66 24.65 ?  162 ASP   A H    1 
ATOM   3477 H H    B ASP   A 1 162 ? 3.841  -5.179  3.572   0.34 24.14 ?  162 ASP   A H    1 
ATOM   3478 H HA   A ASP   A 1 162 ? 2.878  -7.399  4.255   0.66 25.75 ?  162 ASP   A HA   1 
ATOM   3479 H HA   B ASP   A 1 162 ? 2.743  -7.439  4.141   0.34 25.52 ?  162 ASP   A HA   1 
ATOM   3480 H HB2  A ASP   A 1 162 ? 1.600  -5.292  2.889   0.66 27.57 ?  162 ASP   A HB2  1 
ATOM   3481 H HB2  B ASP   A 1 162 ? 1.657  -5.245  2.736   0.34 26.76 ?  162 ASP   A HB2  1 
ATOM   3482 H HB3  A ASP   A 1 162 ? 0.815  -6.607  3.312   0.66 27.57 ?  162 ASP   A HB3  1 
ATOM   3483 H HB3  B ASP   A 1 162 ? 0.771  -6.497  3.150   0.34 26.76 ?  162 ASP   A HB3  1 
ATOM   3484 N N    A LYS   A 1 163 ? 3.343  -7.132  1.105   0.66 22.11 ?  163 LYS   A N    1 
ATOM   3485 N N    B LYS   A 1 163 ? 3.312  -7.136  1.010   0.34 22.61 ?  163 LYS   A N    1 
ATOM   3486 C CA   A LYS   A 1 163 ? 3.405  -7.916  -0.125  0.66 22.80 ?  163 LYS   A CA   1 
ATOM   3487 C CA   B LYS   A 1 163 ? 3.430  -7.915  -0.218  0.34 23.43 ?  163 LYS   A CA   1 
ATOM   3488 C C    A LYS   A 1 163 ? 4.480  -8.994  -0.043  0.66 22.45 ?  163 LYS   A C    1 
ATOM   3489 C C    B LYS   A 1 163 ? 4.501  -8.992  -0.088  0.34 22.29 ?  163 LYS   A C    1 
ATOM   3490 O O    A LYS   A 1 163 ? 4.297  -10.108 -0.545  0.66 23.18 ?  163 LYS   A O    1 
ATOM   3491 O O    B LYS   A 1 163 ? 4.329  -10.110 -0.585  0.34 22.52 ?  163 LYS   A O    1 
ATOM   3492 C CB   A LYS   A 1 163 ? 3.659  -6.992  -1.317  0.66 25.38 ?  163 LYS   A CB   1 
ATOM   3493 C CB   B LYS   A 1 163 ? 3.738  -6.990  -1.396  0.34 25.91 ?  163 LYS   A CB   1 
ATOM   3494 C CG   A LYS   A 1 163 ? 3.749  -7.719  -2.648  0.66 28.34 ?  163 LYS   A CG   1 
ATOM   3495 C CG   B LYS   A 1 163 ? 3.833  -7.713  -2.730  0.34 28.44 ?  163 LYS   A CG   1 
ATOM   3496 C CD   A LYS   A 1 163 ? 4.131  -6.773  -3.772  0.66 31.81 ?  163 LYS   A CD   1 
ATOM   3497 C CD   B LYS   A 1 163 ? 4.302  -6.785  -3.835  0.34 31.20 ?  163 LYS   A CD   1 
ATOM   3498 C CE   A LYS   A 1 163 ? 4.063  -7.468  -5.122  0.66 34.28 ?  163 LYS   A CE   1 
ATOM   3499 C CE   B LYS   A 1 163 ? 4.291  -7.490  -5.181  0.34 33.17 ?  163 LYS   A CE   1 
ATOM   3500 N NZ   A LYS   A 1 163 ? 4.723  -6.672  -6.192  0.66 35.37 ?  163 LYS   A NZ   1 
ATOM   3501 N NZ   B LYS   A 1 163 ? 4.897  -6.656  -6.253  0.34 33.97 ?  163 LYS   A NZ   1 
ATOM   3502 H H    A LYS   A 1 163 ? 3.595  -6.308  1.028   0.66 26.51 ?  163 LYS   A H    1 
ATOM   3503 H H    B LYS   A 1 163 ? 3.567  -6.315  0.944   0.34 27.11 ?  163 LYS   A H    1 
ATOM   3504 H HA   A LYS   A 1 163 ? 2.545  -8.346  -0.262  0.66 27.33 ?  163 LYS   A HA   1 
ATOM   3505 H HA   B LYS   A 1 163 ? 2.580  -8.348  -0.396  0.34 28.09 ?  163 LYS   A HA   1 
ATOM   3506 H HB2  A LYS   A 1 163 ? 2.928  -6.349  -1.382  0.66 30.43 ?  163 LYS   A HB2  1 
ATOM   3507 H HB2  B LYS   A 1 163 ? 3.031  -6.326  -1.470  0.34 31.06 ?  163 LYS   A HB2  1 
ATOM   3508 H HB3  A LYS   A 1 163 ? 4.493  -6.520  -1.178  0.66 30.43 ?  163 LYS   A HB3  1 
ATOM   3509 H HB3  B LYS   A 1 163 ? 4.586  -6.549  -1.236  0.34 31.06 ?  163 LYS   A HB3  1 
ATOM   3510 H HG2  A LYS   A 1 163 ? 4.426  -8.410  -2.595  0.66 33.97 ?  163 LYS   A HG2  1 
ATOM   3511 H HG2  B LYS   A 1 163 ? 4.469  -8.441  -2.660  0.34 34.10 ?  163 LYS   A HG2  1 
ATOM   3512 H HG3  A LYS   A 1 163 ? 2.886  -8.110  -2.859  0.66 33.97 ?  163 LYS   A HG3  1 
ATOM   3513 H HG3  B LYS   A 1 163 ? 2.957  -8.055  -2.970  0.34 34.10 ?  163 LYS   A HG3  1 
ATOM   3514 H HD2  A LYS   A 1 163 ? 3.517  -6.023  -3.785  0.66 38.15 ?  163 LYS   A HD2  1 
ATOM   3515 H HD2  B LYS   A 1 163 ? 3.708  -6.020  -3.886  0.34 37.41 ?  163 LYS   A HD2  1 
ATOM   3516 H HD3  A LYS   A 1 163 ? 5.040  -6.461  -3.634  0.66 38.15 ?  163 LYS   A HD3  1 
ATOM   3517 H HD3  B LYS   A 1 163 ? 5.209  -6.496  -3.648  0.34 37.41 ?  163 LYS   A HD3  1 
ATOM   3518 H HE2  A LYS   A 1 163 ? 4.495  -8.334  -5.062  0.66 41.11 ?  163 LYS   A HE2  1 
ATOM   3519 H HE2  B LYS   A 1 163 ? 4.799  -8.313  -5.113  0.34 39.77 ?  163 LYS   A HE2  1 
ATOM   3520 H HE3  A LYS   A 1 163 ? 3.135  -7.584  -5.369  0.66 41.11 ?  163 LYS   A HE3  1 
ATOM   3521 H HE3  B LYS   A 1 163 ? 3.374  -7.686  -5.430  0.34 39.77 ?  163 LYS   A HE3  1 
ATOM   3522 H HZ1  A LYS   A 1 163 ? 4.670  -7.103  -6.969  0.66 42.41 ?  163 LYS   A HZ1  1 
ATOM   3523 H HZ1  B LYS   A 1 163 ? 4.877  -7.095  -7.026  0.34 40.74 ?  163 LYS   A HZ1  1 
ATOM   3524 H HZ2  A LYS   A 1 163 ? 4.323  -5.881  -6.271  0.66 42.41 ?  163 LYS   A HZ2  1 
ATOM   3525 H HZ2  B LYS   A 1 163 ? 4.443  -5.896  -6.338  0.34 40.74 ?  163 LYS   A HZ2  1 
ATOM   3526 H HZ3  A LYS   A 1 163 ? 5.581  -6.543  -5.991  0.66 42.41 ?  163 LYS   A HZ3  1 
ATOM   3527 H HZ3  B LYS   A 1 163 ? 5.743  -6.468  -6.049  0.34 40.74 ?  163 LYS   A HZ3  1 
ATOM   3528 N N    . LEU   A 1 164 ? 5.618  -8.673  0.570   1.00 20.52 ?  164 LEU   A N    1 
ATOM   3529 C CA   . LEU   A 1 164 ? 6.694  -9.654  0.708   1.00 19.79 ?  164 LEU   A CA   1 
ATOM   3530 C C    . LEU   A 1 164 ? 6.258  -10.834 1.566   1.00 20.07 ?  164 LEU   A C    1 
ATOM   3531 O O    . LEU   A 1 164 ? 6.537  -11.990 1.234   1.00 20.20 ?  164 LEU   A O    1 
ATOM   3532 C CB   . LEU   A 1 164 ? 7.916  -8.988  1.326   1.00 19.12 ?  164 LEU   A CB   1 
ATOM   3533 C CG   . LEU   A 1 164 ? 8.694  -8.009  0.452   1.00 19.09 ?  164 LEU   A CG   1 
ATOM   3534 C CD1  . LEU   A 1 164 ? 9.637  -7.175  1.308   1.00 18.54 ?  164 LEU   A CD1  1 
ATOM   3535 C CD2  . LEU   A 1 164 ? 9.475  -8.767  -0.608  1.00 19.76 ?  164 LEU   A CD2  1 
ATOM   3536 H H    A LEU   A 1 164 ? 5.791  -7.899  0.908   0.66 24.60 ?  164 LEU   A H    1 
ATOM   3537 H H    B LEU   A 1 164 ? 5.774  -7.907  0.933   0.34 24.60 ?  164 LEU   A H    1 
ATOM   3538 H HA   . LEU   A 1 164 ? 6.933  -9.988  -0.171  1.00 23.72 ?  164 LEU   A HA   1 
ATOM   3539 H HB2  . LEU   A 1 164 ? 7.627  -8.502  2.112   1.00 22.92 ?  164 LEU   A HB2  1 
ATOM   3540 H HB3  . LEU   A 1 164 ? 8.533  -9.687  1.589   1.00 22.92 ?  164 LEU   A HB3  1 
ATOM   3541 H HG   . LEU   A 1 164 ? 8.078  -7.407  0.010   1.00 22.88 ?  164 LEU   A HG   1 
ATOM   3542 H HD11 . LEU   A 1 164 ? 10.129 -6.564  0.741   1.00 22.22 ?  164 LEU   A HD11 1 
ATOM   3543 H HD12 . LEU   A 1 164 ? 9.115  -6.674  1.959   1.00 22.22 ?  164 LEU   A HD12 1 
ATOM   3544 H HD13 . LEU   A 1 164 ? 10.252 -7.767  1.772   1.00 22.22 ?  164 LEU   A HD13 1 
ATOM   3545 H HD21 . LEU   A 1 164 ? 9.988  -8.132  -1.134  1.00 23.69 ?  164 LEU   A HD21 1 
ATOM   3546 H HD22 . LEU   A 1 164 ? 10.072 -9.393  -0.172  1.00 23.69 ?  164 LEU   A HD22 1 
ATOM   3547 H HD23 . LEU   A 1 164 ? 8.851  -9.241  -1.176  1.00 23.69 ?  164 LEU   A HD23 1 
ATOM   3548 N N    . VAL   A 1 165 ? 5.594  -10.556 2.686   1.00 19.21 ?  165 VAL   A N    1 
ATOM   3549 C CA   . VAL   A 1 165 ? 5.119  -11.623 3.560   1.00 19.18 ?  165 VAL   A CA   1 
ATOM   3550 C C    . VAL   A 1 165 ? 4.066  -12.465 2.849   1.00 20.37 ?  165 VAL   A C    1 
ATOM   3551 O O    . VAL   A 1 165 ? 4.156  -13.698 2.809   1.00 20.46 ?  165 VAL   A O    1 
ATOM   3552 C CB   . VAL   A 1 165 ? 4.584  -11.027 4.875   1.00 20.08 ?  165 VAL   A CB   1 
ATOM   3553 C CG1  . VAL   A 1 165 ? 3.831  -12.080 5.684   1.00 21.17 ?  165 VAL   A CG1  1 
ATOM   3554 C CG2  . VAL   A 1 165 ? 5.722  -10.403 5.679   1.00 20.59 ?  165 VAL   A CG2  1 
ATOM   3555 H H    . VAL   A 1 165 ? 5.406  -9.763  2.959   1.00 23.03 ?  165 VAL   A H    1 
ATOM   3556 H HA   . VAL   A 1 165 ? 5.862  -12.204 3.784   1.00 22.99 ?  165 VAL   A HA   1 
ATOM   3557 H HB   . VAL   A 1 165 ? 3.955  -10.318 4.663   1.00 24.07 ?  165 VAL   A HB   1 
ATOM   3558 H HG11 . VAL   A 1 165 ? 3.750  -11.774 6.602   1.00 25.38 ?  165 VAL   A HG11 1 
ATOM   3559 H HG12 . VAL   A 1 165 ? 2.946  -12.201 5.301   1.00 25.38 ?  165 VAL   A HG12 1 
ATOM   3560 H HG13 . VAL   A 1 165 ? 4.324  -12.911 5.656   1.00 25.38 ?  165 VAL   A HG13 1 
ATOM   3561 H HG21 . VAL   A 1 165 ? 5.374  -10.094 6.532   1.00 24.68 ?  165 VAL   A HG21 1 
ATOM   3562 H HG22 . VAL   A 1 165 ? 6.409  -11.070 5.824   1.00 24.68 ?  165 VAL   A HG22 1 
ATOM   3563 H HG23 . VAL   A 1 165 ? 6.086  -9.653  5.181   1.00 24.68 ?  165 VAL   A HG23 1 
ATOM   3564 N N    A SER   A 1 166 ? 3.060  -11.809 2.268   0.66 20.74 ?  166 SER   A N    1 
ATOM   3565 N N    B SER   A 1 166 ? 3.058  -11.809 2.268   0.34 20.81 ?  166 SER   A N    1 
ATOM   3566 C CA   A SER   A 1 166 ? 1.940  -12.540 1.684   0.66 22.37 ?  166 SER   A CA   1 
ATOM   3567 C CA   B SER   A 1 166 ? 1.928  -12.521 1.680   0.34 21.92 ?  166 SER   A CA   1 
ATOM   3568 C C    A SER   A 1 166 ? 2.371  -13.390 0.500   0.66 23.06 ?  166 SER   A C    1 
ATOM   3569 C C    B SER   A 1 166 ? 2.307  -13.313 0.437   0.34 22.32 ?  166 SER   A C    1 
ATOM   3570 O O    A SER   A 1 166 ? 1.743  -14.420 0.219   0.66 24.73 ?  166 SER   A O    1 
ATOM   3571 O O    B SER   A 1 166 ? 1.558  -14.217 0.047   0.34 22.74 ?  166 SER   A O    1 
ATOM   3572 C CB   A SER   A 1 166 ? 0.842  -11.565 1.254   0.66 24.04 ?  166 SER   A CB   1 
ATOM   3573 C CB   B SER   A 1 166 ? 0.814  -11.536 1.321   0.34 23.10 ?  166 SER   A CB   1 
ATOM   3574 O OG   A SER   A 1 166 ? 0.265  -10.920 2.376   0.66 26.16 ?  166 SER   A OG   1 
ATOM   3575 O OG   B SER   A 1 166 ? 0.360  -10.843 2.471   0.34 24.58 ?  166 SER   A OG   1 
ATOM   3576 H H    A SER   A 1 166 ? 3.000  -10.955 2.204   0.66 24.86 ?  166 SER   A H    1 
ATOM   3577 H H    B SER   A 1 166 ? 3.005  -10.953 2.207   0.34 24.94 ?  166 SER   A H    1 
ATOM   3578 H HA   A SER   A 1 166 ? 1.562  -13.134 2.349   0.66 26.81 ?  166 SER   A HA   1 
ATOM   3579 H HA   B SER   A 1 166 ? 1.571  -13.142 2.333   0.34 26.28 ?  166 SER   A HA   1 
ATOM   3580 H HB2  A SER   A 1 166 ? 1.222  -10.905 0.651   0.66 28.81 ?  166 SER   A HB2  1 
ATOM   3581 H HB2  B SER   A 1 166 ? 1.154  -10.896 0.675   0.34 27.69 ?  166 SER   A HB2  1 
ATOM   3582 H HB3  A SER   A 1 166 ? 0.138  -12.056 0.804   0.66 28.81 ?  166 SER   A HB3  1 
ATOM   3583 H HB3  B SER   A 1 166 ? 0.069  -12.026 0.937   0.34 27.69 ?  166 SER   A HB3  1 
ATOM   3584 H HG   A SER   A 1 166 ? -0.311 -10.363 2.125   0.66 31.37 ?  166 SER   A HG   1 
ATOM   3585 H HG   B SER   A 1 166 ? 0.990  -10.399 2.805   0.34 29.46 ?  166 SER   A HG   1 
ATOM   3586 N N    . SER   A 1 167 ? 3.426  -12.983 -0.204  1.00 22.55 ?  167 SER   A N    1 
ATOM   3587 C CA   . SER   A 1 167 ? 3.889  -13.693 -1.389  1.00 23.44 ?  167 SER   A CA   1 
ATOM   3588 C C    . SER   A 1 167 ? 5.041  -14.647 -1.105  1.00 24.14 ?  167 SER   A C    1 
ATOM   3589 O O    . SER   A 1 167 ? 5.516  -15.313 -2.031  1.00 24.76 ?  167 SER   A O    1 
ATOM   3590 C CB   . SER   A 1 167 ? 4.307  -12.695 -2.481  1.00 24.32 ?  167 SER   A CB   1 
ATOM   3591 O OG   . SER   A 1 167 ? 5.364  -11.864 -2.032  1.00 24.76 ?  167 SER   A OG   1 
ATOM   3592 H H    A SER   A 1 167 ? 3.894  -12.280 -0.013  0.66 27.03 ?  167 SER   A H    1 
ATOM   3593 H H    B SER   A 1 167 ? 3.936  -12.323 0.027   0.34 27.03 ?  167 SER   A H    1 
ATOM   3594 H HA   . SER   A 1 167 ? 3.154  -14.209 -1.744  1.00 28.10 ?  167 SER   A HA   1 
ATOM   3595 H HB2  . SER   A 1 167 ? 4.605  -13.189 -3.262  1.00 29.16 ?  167 SER   A HB2  1 
ATOM   3596 H HB3  . SER   A 1 167 ? 3.538  -12.145 -2.721  1.00 29.16 ?  167 SER   A HB3  1 
ATOM   3597 H HG   . SER   A 1 167 ? 5.110  -11.422 -1.361  1.00 29.68 ?  167 SER   A HG   1 
ATOM   3598 N N    . PHE   A 1 168 ? 5.511  -14.728 0.137   1.00 24.30 ?  168 PHE   A N    1 
ATOM   3599 C CA   . PHE   A 1 168 ? 6.688  -15.537 0.426   1.00 25.84 ?  168 PHE   A CA   1 
ATOM   3600 C C    . PHE   A 1 168 ? 6.375  -17.019 0.272   1.00 31.40 ?  168 PHE   A C    1 
ATOM   3601 O O    . PHE   A 1 168 ? 5.313  -17.495 0.678   1.00 32.32 ?  168 PHE   A O    1 
ATOM   3602 C CB   . PHE   A 1 168 ? 7.191  -15.276 1.844   1.00 23.25 ?  168 PHE   A CB   1 
ATOM   3603 C CG   . PHE   A 1 168 ? 8.463  -16.013 2.168   1.00 21.48 ?  168 PHE   A CG   1 
ATOM   3604 C CD1  . PHE   A 1 168 ? 9.657  -15.633 1.583   1.00 21.08 ?  168 PHE   A CD1  1 
ATOM   3605 C CD2  . PHE   A 1 168 ? 8.466  -17.093 3.040   1.00 20.72 ?  168 PHE   A CD2  1 
ATOM   3606 C CE1  . PHE   A 1 168 ? 10.827 -16.308 1.864   1.00 20.62 ?  168 PHE   A CE1  1 
ATOM   3607 C CE2  . PHE   A 1 168 ? 9.642  -17.774 3.326   1.00 20.81 ?  168 PHE   A CE2  1 
ATOM   3608 C CZ   . PHE   A 1 168 ? 10.819 -17.377 2.736   1.00 20.83 ?  168 PHE   A CZ   1 
ATOM   3609 H H    . PHE   A 1 168 ? 5.176  -14.322 0.815   1.00 29.13 ?  168 PHE   A H    1 
ATOM   3610 H HA   . PHE   A 1 168 ? 7.396  -15.307 -0.198  1.00 30.99 ?  168 PHE   A HA   1 
ATOM   3611 H HB2  . PHE   A 1 168 ? 7.357  -14.326 1.948   1.00 27.87 ?  168 PHE   A HB2  1 
ATOM   3612 H HB3  . PHE   A 1 168 ? 6.509  -15.562 2.474   1.00 27.87 ?  168 PHE   A HB3  1 
ATOM   3613 H HD1  . PHE   A 1 168 ? 9.675  -14.912 0.991   1.00 25.27 ?  168 PHE   A HD1  1 
ATOM   3614 H HD2  . PHE   A 1 168 ? 7.668  -17.362 3.438   1.00 24.84 ?  168 PHE   A HD2  1 
ATOM   3615 H HE1  . PHE   A 1 168 ? 11.628 -16.042 1.467   1.00 24.71 ?  168 PHE   A HE1  1 
ATOM   3616 H HE2  . PHE   A 1 168 ? 9.632  -18.496 3.915   1.00 24.94 ?  168 PHE   A HE2  1 
ATOM   3617 H HZ   . PHE   A 1 168 ? 11.613 -17.829 2.925   1.00 24.97 ?  168 PHE   A HZ   1 
ATOM   3618 N N    . LEU   A 1 169 ? 7.314  -17.756 -0.306  1.00 36.89 ?  169 LEU   A N    1 
ATOM   3619 C CA   . LEU   A 1 169 ? 7.120  -19.185 -0.492  1.00 43.41 ?  169 LEU   A CA   1 
ATOM   3620 C C    . LEU   A 1 169 ? 8.003  -19.961 0.478   1.00 45.73 ?  169 LEU   A C    1 
ATOM   3621 O O    . LEU   A 1 169 ? 7.529  -20.437 1.512   1.00 46.24 ?  169 LEU   A O    1 
ATOM   3622 C CB   . LEU   A 1 169 ? 7.420  -19.587 -1.939  1.00 46.53 ?  169 LEU   A CB   1 
ATOM   3623 C CG   . LEU   A 1 169 ? 7.043  -21.019 -2.329  1.00 48.94 ?  169 LEU   A CG   1 
ATOM   3624 C CD1  . LEU   A 1 169 ? 5.646  -21.367 -1.831  1.00 49.89 ?  169 LEU   A CD1  1 
ATOM   3625 C CD2  . LEU   A 1 169 ? 7.129  -21.197 -3.837  1.00 49.68 ?  169 LEU   A CD2  1 
ATOM   3626 O OXT  . LEU   A 1 169 ? 9.205  -20.119 0.261   1.00 46.02 -1 169 LEU   A OXT  1 
ATOM   3627 H H    . LEU   A 1 169 ? 8.068  -17.456 -0.589  1.00 44.24 ?  169 LEU   A H    1 
ATOM   3628 H HA   . LEU   A 1 169 ? 6.194  -19.397 -0.300  1.00 52.06 ?  169 LEU   A HA   1 
ATOM   3629 H HB2  . LEU   A 1 169 ? 6.934  -18.991 -2.529  1.00 55.80 ?  169 LEU   A HB2  1 
ATOM   3630 H HB3  . LEU   A 1 169 ? 8.372  -19.489 -2.092  1.00 55.80 ?  169 LEU   A HB3  1 
ATOM   3631 H HG   . LEU   A 1 169 ? 7.670  -21.636 -1.919  1.00 58.70 ?  169 LEU   A HG   1 
ATOM   3632 H HD11 . LEU   A 1 169 ? 5.337  -22.162 -2.289  1.00 59.84 ?  169 LEU   A HD11 1 
ATOM   3633 H HD12 . LEU   A 1 169 ? 5.683  -21.528 -0.875  1.00 59.84 ?  169 LEU   A HD12 1 
ATOM   3634 H HD13 . LEU   A 1 169 ? 5.052  -20.623 -2.019  1.00 59.84 ?  169 LEU   A HD13 1 
ATOM   3635 H HD21 . LEU   A 1 169 ? 6.897  -22.112 -4.061  1.00 59.58 ?  169 LEU   A HD21 1 
ATOM   3636 H HD22 . LEU   A 1 169 ? 6.507  -20.585 -4.262  1.00 59.58 ?  169 LEU   A HD22 1 
ATOM   3637 H HD23 . LEU   A 1 169 ? 8.034  -21.004 -4.126  1.00 59.58 ?  169 LEU   A HD23 1 
ATOM   3638 N N    A SER   B 1 1   ? 50.875 -9.267  -23.766 0.66 27.39 ?  1   SER   B N    1 
ATOM   3639 N N    B SER   B 1 1   ? 50.782 -9.252  -23.780 0.34 25.61 ?  1   SER   B N    1 
ATOM   3640 C CA   A SER   B 1 1   ? 51.353 -10.306 -22.833 0.66 27.52 ?  1   SER   B CA   1 
ATOM   3641 C CA   B SER   B 1 1   ? 51.255 -10.211 -22.760 0.34 25.63 ?  1   SER   B CA   1 
ATOM   3642 C C    A SER   B 1 1   ? 50.271 -11.346 -22.564 0.66 26.41 ?  1   SER   B C    1 
ATOM   3643 C C    B SER   B 1 1   ? 50.199 -11.273 -22.488 0.34 25.01 ?  1   SER   B C    1 
ATOM   3644 O O    A SER   B 1 1   ? 49.071 -11.128 -22.800 0.66 26.39 ?  1   SER   B O    1 
ATOM   3645 O O    B SER   B 1 1   ? 49.011 -11.092 -22.783 0.34 24.54 ?  1   SER   B O    1 
ATOM   3646 C CB   A SER   B 1 1   ? 51.805 -9.687  -21.515 0.66 28.50 ?  1   SER   B CB   1 
ATOM   3647 C CB   B SER   B 1 1   ? 51.602 -9.492  -21.461 0.34 26.17 ?  1   SER   B CB   1 
ATOM   3648 O OG   A SER   B 1 1   ? 50.692 -9.377  -20.700 0.66 31.08 ?  1   SER   B OG   1 
ATOM   3649 O OG   B SER   B 1 1   ? 50.558 -9.635  -20.515 0.34 27.39 ?  1   SER   B OG   1 
ATOM   3650 H H1   A SER   B 1 1   ? 50.784 -9.621  -24.575 0.66 32.84 ?  1   SER   B H1   1 
ATOM   3651 H H1   B SER   B 1 1   ? 51.487 -8.875  -24.170 0.34 30.71 ?  1   SER   B H1   1 
ATOM   3652 H H2   A SER   B 1 1   ? 50.095 -8.959  -23.480 0.66 32.84 ?  1   SER   B H2   1 
ATOM   3653 H H2   B SER   B 1 1   ? 50.300 -9.686  -24.386 0.34 30.71 ?  1   SER   B H2   1 
ATOM   3654 H H3   A SER   B 1 1   ? 51.470 -8.608  -23.791 0.66 32.84 ?  1   SER   B H3   1 
ATOM   3655 H H3   B SER   B 1 1   ? 50.288 -8.631  -23.386 0.34 30.71 ?  1   SER   B H3   1 
ATOM   3656 H HA   A SER   B 1 1   ? 52.114 -10.745 -23.242 0.66 33.00 ?  1   SER   B HA   1 
ATOM   3657 H HA   B SER   B 1 1   ? 52.053 -10.641 -23.098 0.34 30.73 ?  1   SER   B HA   1 
ATOM   3658 H HB2  A SER   B 1 1   ? 52.371 -10.324 -21.054 0.66 34.17 ?  1   SER   B HB2  1 
ATOM   3659 H HB2  B SER   B 1 1   ? 52.411 -9.881  -21.098 0.34 31.37 ?  1   SER   B HB2  1 
ATOM   3660 H HB3  A SER   B 1 1   ? 52.297 -8.873  -21.698 0.66 34.17 ?  1   SER   B HB3  1 
ATOM   3661 H HB3  B SER   B 1 1   ? 51.742 -8.549  -21.648 0.34 31.37 ?  1   SER   B HB3  1 
ATOM   3662 H HG   A SER   B 1 1   ? 50.949 -8.973  -20.008 0.66 37.27 ?  1   SER   B HG   1 
ATOM   3663 H HG   B SER   B 1 1   ? 50.660 -9.074  -19.897 0.34 32.84 ?  1   SER   B HG   1 
ATOM   3664 N N    A MET   B 1 2   ? 50.724 -12.484 -22.052 0.66 25.73 ?  2   MET   B N    1 
ATOM   3665 N N    B MET   B 1 2   ? 50.648 -12.379 -21.909 0.34 25.01 ?  2   MET   B N    1 
ATOM   3666 C CA   A MET   B 1 2   ? 49.905 -13.676 -21.885 0.66 25.75 ?  2   MET   B CA   1 
ATOM   3667 C CA   B MET   B 1 2   ? 49.833 -13.571 -21.720 0.34 25.04 ?  2   MET   B CA   1 
ATOM   3668 C C    A MET   B 1 2   ? 49.656 -13.888 -20.398 0.66 23.93 ?  2   MET   B C    1 
ATOM   3669 C C    B MET   B 1 2   ? 49.568 -13.742 -20.230 0.34 23.27 ?  2   MET   B C    1 
ATOM   3670 O O    A MET   B 1 2   ? 50.591 -14.164 -19.640 0.66 24.03 ?  2   MET   B O    1 
ATOM   3671 O O    B MET   B 1 2   ? 50.488 -14.034 -19.459 0.34 23.10 ?  2   MET   B O    1 
ATOM   3672 C CB   A MET   B 1 2   ? 50.640 -14.866 -22.488 0.66 29.55 ?  2   MET   B CB   1 
ATOM   3673 C CB   B MET   B 1 2   ? 50.579 -14.772 -22.286 0.34 27.50 ?  2   MET   B CB   1 
ATOM   3674 C CG   A MET   B 1 2   ? 49.820 -16.142 -22.591 0.66 33.52 ?  2   MET   B CG   1 
ATOM   3675 C CG   B MET   B 1 2   ? 49.703 -15.953 -22.673 0.34 29.93 ?  2   MET   B CG   1 
ATOM   3676 S SD   A MET   B 1 2   ? 50.674 -17.386 -23.580 0.66 37.53 ?  2   MET   B SD   1 
ATOM   3677 S SD   B MET   B 1 2   ? 50.619 -17.147 -23.656 0.34 32.40 ?  2   MET   B SD   1 
ATOM   3678 C CE   A MET   B 1 2   ? 51.190 -16.371 -24.957 0.66 37.36 ?  2   MET   B CE   1 
ATOM   3679 C CE   B MET   B 1 2   ? 51.622 -16.049 -24.642 0.34 32.22 ?  2   MET   B CE   1 
ATOM   3680 H H    A MET   B 1 2   ? 51.536 -12.597 -21.786 0.66 30.85 ?  2   MET   B H    1 
ATOM   3681 H H    B MET   B 1 2   ? 51.453 -12.470 -21.613 0.34 29.99 ?  2   MET   B H    1 
ATOM   3682 H HA   A MET   B 1 2   ? 49.062 -13.571 -22.351 0.66 30.87 ?  2   MET   B HA   1 
ATOM   3683 H HA   B MET   B 1 2   ? 48.998 -13.485 -22.208 0.34 30.01 ?  2   MET   B HA   1 
ATOM   3684 H HB2  A MET   B 1 2   ? 50.917 -14.596 -23.372 0.66 35.43 ?  2   MET   B HB2  1 
ATOM   3685 H HB2  B MET   B 1 2   ? 51.035 -14.436 -23.067 0.34 32.97 ?  2   MET   B HB2  1 
ATOM   3686 H HB3  A MET   B 1 2   ? 51.417 -15.074 -21.951 0.66 35.43 ?  2   MET   B HB3  1 
ATOM   3687 H HB3  B MET   B 1 2   ? 51.227 -15.100 -21.646 0.34 32.97 ?  2   MET   B HB3  1 
ATOM   3688 H HG2  A MET   B 1 2   ? 49.673 -16.503 -21.699 0.66 40.20 ?  2   MET   B HG2  1 
ATOM   3689 H HG2  B MET   B 1 2   ? 49.389 -16.400 -21.868 0.34 35.88 ?  2   MET   B HG2  1 
ATOM   3690 H HG3  A MET   B 1 2   ? 48.972 -15.952 -23.021 0.66 40.20 ?  2   MET   B HG3  1 
ATOM   3691 H HG3  B MET   B 1 2   ? 48.952 -15.652 -23.202 0.34 35.88 ?  2   MET   B HG3  1 
ATOM   3692 H HE1  A MET   B 1 2   ? 51.363 -16.941 -25.709 0.66 44.80 ?  2   MET   B HE1  1 
ATOM   3693 H HE1  B MET   B 1 2   ? 51.976 -16.553 -25.369 0.34 38.63 ?  2   MET   B HE1  1 
ATOM   3694 H HE2  A MET   B 1 2   ? 50.474 -15.745 -25.165 0.66 44.80 ?  2   MET   B HE2  1 
ATOM   3695 H HE2  B MET   B 1 2   ? 51.065 -15.322 -24.975 0.34 38.63 ?  2   MET   B HE2  1 
ATOM   3696 H HE3  A MET   B 1 2   ? 51.995 -15.878 -24.716 0.66 44.80 ?  2   MET   B HE3  1 
ATOM   3697 H HE3  B MET   B 1 2   ? 52.349 -15.694 -24.097 0.34 38.63 ?  2   MET   B HE3  1 
ATOM   3698 N N    A VAL   B 1 3   ? 48.401 -13.749 -19.981 0.66 21.38 ?  3   VAL   B N    1 
ATOM   3699 N N    B VAL   B 1 3   ? 48.318 -13.542 -19.827 0.34 21.56 ?  3   VAL   B N    1 
ATOM   3700 C CA   A VAL   B 1 3   ? 47.994 -13.982 -18.604 0.66 20.47 ?  3   VAL   B CA   1 
ATOM   3701 C CA   B VAL   B 1 3   ? 47.888 -13.794 -18.460 0.34 20.56 ?  3   VAL   B CA   1 
ATOM   3702 C C    A VAL   B 1 3   ? 46.755 -14.866 -18.615 0.66 19.37 ?  3   VAL   B C    1 
ATOM   3703 C C    B VAL   B 1 3   ? 46.629 -14.648 -18.487 0.34 19.17 ?  3   VAL   B C    1 
ATOM   3704 O O    A VAL   B 1 3   ? 46.056 -14.986 -19.624 0.66 19.46 ?  3   VAL   B O    1 
ATOM   3705 O O    B VAL   B 1 3   ? 45.801 -14.545 -19.397 0.34 19.26 ?  3   VAL   B O    1 
ATOM   3706 C CB   A VAL   B 1 3   ? 47.715 -12.668 -17.840 0.66 22.32 ?  3   VAL   B CB   1 
ATOM   3707 C CB   B VAL   B 1 3   ? 47.642 -12.497 -17.657 0.34 21.36 ?  3   VAL   B CB   1 
ATOM   3708 C CG1  A VAL   B 1 3   ? 48.983 -11.809 -17.754 0.66 23.42 ?  3   VAL   B CG1  1 
ATOM   3709 C CG1  B VAL   B 1 3   ? 48.922 -11.677 -17.548 0.34 21.83 ?  3   VAL   B CG1  1 
ATOM   3710 C CG2  A VAL   B 1 3   ? 46.582 -11.897 -18.501 0.66 22.95 ?  3   VAL   B CG2  1 
ATOM   3711 C CG2  B VAL   B 1 3   ? 46.520 -11.684 -18.284 0.34 21.52 ?  3   VAL   B CG2  1 
ATOM   3712 H H    A VAL   B 1 3   ? 47.753 -13.515 -20.495 0.66 25.62 ?  3   VAL   B H    1 
ATOM   3713 H H    B VAL   B 1 3   ? 47.697 -13.251 -20.344 0.34 25.84 ?  3   VAL   B H    1 
ATOM   3714 H HA   A VAL   B 1 3   ? 48.704 -14.454 -18.138 0.66 24.54 ?  3   VAL   B HA   1 
ATOM   3715 H HA   B VAL   B 1 3   ? 48.582 -14.296 -18.007 0.34 24.64 ?  3   VAL   B HA   1 
ATOM   3716 H HB   A VAL   B 1 3   ? 47.444 -12.884 -16.934 0.66 26.75 ?  3   VAL   B HB   1 
ATOM   3717 H HB   B VAL   B 1 3   ? 47.367 -12.740 -16.760 0.34 25.60 ?  3   VAL   B HB   1 
ATOM   3718 H HG11 A VAL   B 1 3   ? 48.780 -10.999 -17.260 0.66 28.08 ?  3   VAL   B HG11 1 
ATOM   3719 H HG11 B VAL   B 1 3   ? 48.739 -10.879 -17.028 0.34 26.17 ?  3   VAL   B HG11 1 
ATOM   3720 H HG12 A VAL   B 1 3   ? 49.674 -12.311 -17.295 0.66 28.08 ?  3   VAL   B HG12 1 
ATOM   3721 H HG12 B VAL   B 1 3   ? 49.601 -12.212 -17.107 0.34 26.17 ?  3   VAL   B HG12 1 
ATOM   3722 H HG13 A VAL   B 1 3   ? 49.274 -11.586 -18.651 0.66 28.08 ?  3   VAL   B HG13 1 
ATOM   3723 H HG13 B VAL   B 1 3   ? 49.217 -11.433 -18.438 0.34 26.17 ?  3   VAL   B HG13 1 
ATOM   3724 H HG21 A VAL   B 1 3   ? 46.525 -11.016 -18.101 0.66 27.51 ?  3   VAL   B HG21 1 
ATOM   3725 H HG21 B VAL   B 1 3   ? 46.487 -10.816 -17.857 0.34 25.80 ?  3   VAL   B HG21 1 
ATOM   3726 H HG22 A VAL   B 1 3   ? 46.764 -11.819 -19.450 0.66 27.51 ?  3   VAL   B HG22 1 
ATOM   3727 H HG22 B VAL   B 1 3   ? 46.696 -11.582 -19.232 0.34 25.80 ?  3   VAL   B HG22 1 
ATOM   3728 H HG23 A VAL   B 1 3   ? 45.750 -12.377 -18.362 0.66 27.51 ?  3   VAL   B HG23 1 
ATOM   3729 H HG23 B VAL   B 1 3   ? 45.679 -12.150 -18.152 0.34 25.80 ?  3   VAL   B HG23 1 
ATOM   3730 N N    . ASN   B 1 4   ? 46.491 -15.494 -17.470 1.00 17.75 ?  4   ASN   B N    1 
ATOM   3731 C CA   . ASN   B 1 4   ? 45.349 -16.395 -17.341 1.00 16.81 ?  4   ASN   B CA   1 
ATOM   3732 C C    . ASN   B 1 4   ? 45.290 -17.369 -18.516 1.00 17.23 ?  4   ASN   B C    1 
ATOM   3733 O O    . ASN   B 1 4   ? 44.230 -17.625 -19.080 1.00 17.63 ?  4   ASN   B O    1 
ATOM   3734 C CB   . ASN   B 1 4   ? 44.034 -15.619 -17.192 1.00 16.51 ?  4   ASN   B CB   1 
ATOM   3735 C CG   . ASN   B 1 4   ? 43.978 -14.822 -15.903 1.00 15.56 ?  4   ASN   B CG   1 
ATOM   3736 O OD1  . ASN   B 1 4   ? 44.269 -15.342 -14.833 1.00 15.43 ?  4   ASN   B OD1  1 
ATOM   3737 N ND2  . ASN   B 1 4   ? 43.640 -13.540 -16.005 1.00 16.90 ?  4   ASN   B ND2  1 
ATOM   3738 H H    A ASN   B 1 4   ? 46.964 -15.422 -16.759 0.66 21.28 ?  4   ASN   B H    1 
ATOM   3739 H H    B ASN   B 1 4   ? 47.059 -15.565 -16.830 0.34 21.28 ?  4   ASN   B H    1 
ATOM   3740 H HA   . ASN   B 1 4   ? 45.468 -16.919 -16.535 1.00 20.14 ?  4   ASN   B HA   1 
ATOM   3741 H HB2  . ASN   B 1 4   ? 43.939 -15.003 -17.932 1.00 19.78 ?  4   ASN   B HB2  1 
ATOM   3742 H HB3  . ASN   B 1 4   ? 43.295 -16.250 -17.185 1.00 19.78 ?  4   ASN   B HB3  1 
ATOM   3743 H HD21 . ASN   B 1 4   ? 43.601 -13.043 -15.297 1.00 20.26 ?  4   ASN   B HD21 1 
ATOM   3744 H HD22 . ASN   B 1 4   ? 43.453 -13.199 -16.771 1.00 20.26 ?  4   ASN   B HD22 1 
ATOM   3745 N N    . SER   B 1 5   ? 46.445 -17.912 -18.894 1.00 18.79 ?  5   SER   B N    1 
ATOM   3746 C CA   . SER   B 1 5   ? 46.535 -18.816 -20.039 1.00 20.38 ?  5   SER   B CA   1 
ATOM   3747 C C    . SER   B 1 5   ? 46.483 -20.256 -19.541 1.00 22.07 ?  5   SER   B C    1 
ATOM   3748 O O    . SER   B 1 5   ? 47.468 -20.985 -19.539 1.00 24.54 ?  5   SER   B O    1 
ATOM   3749 C CB   . SER   B 1 5   ? 47.805 -18.539 -20.842 1.00 22.14 ?  5   SER   B CB   1 
ATOM   3750 O OG   . SER   B 1 5   ? 48.973 -18.723 -20.057 1.00 25.31 ?  5   SER   B OG   1 
ATOM   3751 H H    . SER   B 1 5   ? 47.196 -17.781 -18.498 1.00 22.52 ?  5   SER   B H    1 
ATOM   3752 H HA   . SER   B 1 5   ? 45.776 -18.670 -20.624 1.00 24.43 ?  5   SER   B HA   1 
ATOM   3753 H HB2  . SER   B 1 5   ? 47.835 -19.143 -21.603 1.00 26.54 ?  5   SER   B HB2  1 
ATOM   3754 H HB3  . SER   B 1 5   ? 47.770 -17.621 -21.156 1.00 26.54 ?  5   SER   B HB3  1 
ATOM   3755 H HG   . SER   B 1 5   ? 49.010 -19.518 -19.789 1.00 30.35 ?  5   SER   B HG   1 
ATOM   3756 N N    . PHE   B 1 6   ? 45.294 -20.640 -19.086 1.00 22.36 ?  6   PHE   B N    1 
ATOM   3757 C CA   . PHE   B 1 6   ? 45.057 -21.993 -18.601 1.00 22.06 ?  6   PHE   B CA   1 
ATOM   3758 C C    . PHE   B 1 6   ? 44.943 -22.937 -19.789 1.00 25.55 ?  6   PHE   B C    1 
ATOM   3759 O O    . PHE   B 1 6   ? 44.263 -22.626 -20.771 1.00 27.44 ?  6   PHE   B O    1 
ATOM   3760 C CB   . PHE   B 1 6   ? 43.772 -22.025 -17.776 1.00 19.81 ?  6   PHE   B CB   1 
ATOM   3761 C CG   . PHE   B 1 6   ? 43.826 -21.178 -16.535 1.00 18.12 ?  6   PHE   B CG   1 
ATOM   3762 C CD1  . PHE   B 1 6   ? 44.329 -21.694 -15.355 1.00 17.06 ?  6   PHE   B CD1  1 
ATOM   3763 C CD2  . PHE   B 1 6   ? 43.379 -19.866 -16.553 1.00 17.55 ?  6   PHE   B CD2  1 
ATOM   3764 C CE1  . PHE   B 1 6   ? 44.370 -20.921 -14.205 1.00 16.88 ?  6   PHE   B CE1  1 
ATOM   3765 C CE2  . PHE   B 1 6   ? 43.421 -19.085 -15.412 1.00 17.93 ?  6   PHE   B CE2  1 
ATOM   3766 C CZ   . PHE   B 1 6   ? 43.928 -19.601 -14.241 1.00 17.18 ?  6   PHE   B CZ   1 
ATOM   3767 H H    . PHE   B 1 6   ? 44.601 -20.133 -19.053 1.00 26.80 ?  6   PHE   B H    1 
ATOM   3768 H HA   . PHE   B 1 6   ? 45.795 -22.280 -18.046 1.00 26.45 ?  6   PHE   B HA   1 
ATOM   3769 H HB2  . PHE   B 1 6   ? 43.038 -21.702 -18.327 1.00 23.74 ?  6   PHE   B HB2  1 
ATOM   3770 H HB3  . PHE   B 1 6   ? 43.594 -22.940 -17.504 1.00 23.74 ?  6   PHE   B HB3  1 
ATOM   3771 H HD1  . PHE   B 1 6   ? 44.637 -22.570 -15.332 1.00 20.44 ?  6   PHE   B HD1  1 
ATOM   3772 H HD2  . PHE   B 1 6   ? 43.032 -19.512 -17.340 1.00 21.04 ?  6   PHE   B HD2  1 
ATOM   3773 H HE1  . PHE   B 1 6   ? 44.721 -21.269 -13.419 1.00 20.23 ?  6   PHE   B HE1  1 
ATOM   3774 H HE2  . PHE   B 1 6   ? 43.112 -18.206 -15.439 1.00 21.49 ?  6   PHE   B HE2  1 
ATOM   3775 H HZ   . PHE   B 1 6   ? 43.957 -19.081 -13.471 1.00 20.58 ?  6   PHE   B HZ   1 
ATOM   3776 N N    A SER   B 1 7   ? 45.617 -24.084 -19.692 0.66 26.45 ?  7   SER   B N    1 
ATOM   3777 N N    B SER   B 1 7   ? 45.615 -24.085 -19.712 0.34 25.80 ?  7   SER   B N    1 
ATOM   3778 C CA   A SER   B 1 7   ? 45.699 -25.058 -20.769 0.66 29.14 ?  7   SER   B CA   1 
ATOM   3779 C CA   B SER   B 1 7   ? 45.625 -25.023 -20.825 0.34 26.84 ?  7   SER   B CA   1 
ATOM   3780 C C    A SER   B 1 7   ? 45.669 -26.463 -20.187 0.66 28.53 ?  7   SER   B C    1 
ATOM   3781 C C    B SER   B 1 7   ? 45.580 -26.454 -20.310 0.34 26.44 ?  7   SER   B C    1 
ATOM   3782 O O    A SER   B 1 7   ? 46.284 -26.729 -19.151 0.66 29.19 ?  7   SER   B O    1 
ATOM   3783 O O    B SER   B 1 7   ? 46.231 -26.790 -19.317 0.34 26.85 ?  7   SER   B O    1 
ATOM   3784 C CB   A SER   B 1 7   ? 46.994 -24.871 -21.575 0.66 31.67 ?  7   SER   B CB   1 
ATOM   3785 C CB   B SER   B 1 7   ? 46.862 -24.821 -21.712 0.34 27.87 ?  7   SER   B CB   1 
ATOM   3786 O OG   A SER   B 1 7   ? 47.142 -25.880 -22.559 0.66 33.74 ?  7   SER   B OG   1 
ATOM   3787 O OG   B SER   B 1 7   ? 46.665 -25.402 -22.990 0.34 28.66 ?  7   SER   B OG   1 
ATOM   3788 H H    A SER   B 1 7   ? 46.054 -24.322 -18.989 0.66 31.71 ?  7   SER   B H    1 
ATOM   3789 H H    B SER   B 1 7   ? 46.077 -24.339 -19.029 0.34 30.93 ?  7   SER   B H    1 
ATOM   3790 H HA   A SER   B 1 7   ? 44.946 -24.958 -21.365 0.66 34.94 ?  7   SER   B HA   1 
ATOM   3791 H HA   B SER   B 1 7   ? 44.841 -24.881 -21.371 0.34 32.18 ?  7   SER   B HA   1 
ATOM   3792 H HB2  A SER   B 1 7   ? 46.967 -24.008 -22.017 0.66 37.98 ?  7   SER   B HB2  1 
ATOM   3793 H HB2  B SER   B 1 7   ? 47.023 -23.869 -21.821 0.34 33.42 ?  7   SER   B HB2  1 
ATOM   3794 H HB3  A SER   B 1 7   ? 47.753 -24.906 -20.970 0.66 37.98 ?  7   SER   B HB3  1 
ATOM   3795 H HB3  B SER   B 1 7   ? 47.631 -25.238 -21.291 0.34 33.42 ?  7   SER   B HB3  1 
ATOM   3796 H HG   A SER   B 1 7   ? 47.857 -25.763 -22.988 0.66 40.46 ?  7   SER   B HG   1 
ATOM   3797 H HG   B SER   B 1 7   ? 47.348 -25.285 -23.468 0.34 34.37 ?  7   SER   B HG   1 
ATOM   3798 N N    A GLY   B 1 8   ? 44.950 -27.358 -20.860 0.66 28.25 ?  8   GLY   B N    1 
ATOM   3799 N N    B GLY   B 1 8   ? 44.804 -27.292 -20.996 0.34 26.07 ?  8   GLY   B N    1 
ATOM   3800 C CA   A GLY   B 1 8   ? 44.941 -28.751 -20.473 0.66 27.31 ?  8   GLY   B CA   1 
ATOM   3801 C CA   B GLY   B 1 8   ? 44.737 -28.700 -20.665 0.34 25.41 ?  8   GLY   B CA   1 
ATOM   3802 C C    A GLY   B 1 8   ? 44.017 -29.096 -19.334 0.66 25.72 ?  8   GLY   B C    1 
ATOM   3803 C C    B GLY   B 1 8   ? 43.877 -29.042 -19.474 0.34 24.53 ?  8   GLY   B C    1 
ATOM   3804 O O    A GLY   B 1 8   ? 44.194 -30.151 -18.713 0.66 27.25 ?  8   GLY   B O    1 
ATOM   3805 O O    B GLY   B 1 8   ? 44.079 -30.100 -18.868 0.34 25.61 ?  8   GLY   B O    1 
ATOM   3806 H H    A GLY   B 1 8   ? 44.464 -27.177 -21.540 0.66 33.87 ?  8   GLY   B H    1 
ATOM   3807 H H    B GLY   B 1 8   ? 44.315 -27.064 -21.663 0.34 31.25 ?  8   GLY   B H    1 
ATOM   3808 H HA2  A GLY   B 1 8   ? 44.679 -29.289 -21.235 0.66 32.74 ?  8   GLY   B HA2  1 
ATOM   3809 H HA2  B GLY   B 1 8   ? 44.383 -29.185 -21.426 0.34 30.47 ?  8   GLY   B HA2  1 
ATOM   3810 H HA3  A GLY   B 1 8   ? 45.835 -29.017 -20.210 0.66 32.74 ?  8   GLY   B HA3  1 
ATOM   3811 H HA3  B GLY   B 1 8   ? 45.633 -29.027 -20.490 0.34 30.47 ?  8   GLY   B HA3  1 
ATOM   3812 N N    A TYR   B 1 9   ? 43.023 -28.259 -19.048 0.66 23.56 ?  9   TYR   B N    1 
ATOM   3813 N N    B TYR   B 1 9   ? 42.912 -28.197 -19.124 0.34 22.96 ?  9   TYR   B N    1 
ATOM   3814 C CA   A TYR   B 1 9   ? 42.086 -28.538 -17.970 0.66 21.45 ?  9   TYR   B CA   1 
ATOM   3815 C CA   B TYR   B 1 9   ? 42.025 -28.476 -18.005 0.34 21.21 ?  9   TYR   B CA   1 
ATOM   3816 C C    A TYR   B 1 9   ? 40.887 -29.328 -18.473 0.66 21.10 ?  9   TYR   B C    1 
ATOM   3817 C C    B TYR   B 1 9   ? 40.814 -29.275 -18.463 0.34 20.73 ?  9   TYR   B C    1 
ATOM   3818 O O    A TYR   B 1 9   ? 40.475 -29.209 -19.631 0.66 22.49 ?  9   TYR   B O    1 
ATOM   3819 O O    B TYR   B 1 9   ? 40.316 -29.103 -19.579 0.34 21.56 ?  9   TYR   B O    1 
ATOM   3820 C CB   A TYR   B 1 9   ? 41.603 -27.249 -17.307 0.66 20.61 ?  9   TYR   B CB   1 
ATOM   3821 C CB   B TYR   B 1 9   ? 41.545 -27.183 -17.351 0.34 20.41 ?  9   TYR   B CB   1 
ATOM   3822 C CG   A TYR   B 1 9   ? 42.642 -26.640 -16.393 0.66 19.96 ?  9   TYR   B CG   1 
ATOM   3823 C CG   B TYR   B 1 9   ? 42.573 -26.548 -16.448 0.34 19.66 ?  9   TYR   B CG   1 
ATOM   3824 C CD1  A TYR   B 1 9   ? 43.749 -25.983 -16.914 0.66 20.23 ?  9   TYR   B CD1  1 
ATOM   3825 C CD1  B TYR   B 1 9   ? 43.628 -25.820 -16.976 0.34 19.60 ?  9   TYR   B CD1  1 
ATOM   3826 C CD2  A TYR   B 1 9   ? 42.528 -26.738 -15.014 0.66 19.71 ?  9   TYR   B CD2  1 
ATOM   3827 C CD2  B TYR   B 1 9   ? 42.491 -26.680 -15.069 0.34 19.27 ?  9   TYR   B CD2  1 
ATOM   3828 C CE1  A TYR   B 1 9   ? 44.714 -25.438 -16.088 0.66 20.43 ?  9   TYR   B CE1  1 
ATOM   3829 C CE1  B TYR   B 1 9   ? 44.575 -25.241 -16.158 0.34 19.68 ?  9   TYR   B CE1  1 
ATOM   3830 C CE2  A TYR   B 1 9   ? 43.489 -26.193 -14.177 0.66 20.14 ?  9   TYR   B CE2  1 
ATOM   3831 C CE2  B TYR   B 1 9   ? 43.436 -26.105 -14.241 0.34 19.38 ?  9   TYR   B CE2  1 
ATOM   3832 C CZ   A TYR   B 1 9   ? 44.580 -25.537 -14.722 0.66 20.54 ?  9   TYR   B CZ   1 
ATOM   3833 C CZ   B TYR   B 1 9   ? 44.476 -25.381 -14.792 0.34 19.57 ?  9   TYR   B CZ   1 
ATOM   3834 O OH   A TYR   B 1 9   ? 45.543 -25.000 -13.903 0.66 20.97 ?  9   TYR   B OH   1 
ATOM   3835 O OH   B TYR   B 1 9   ? 45.422 -24.805 -13.976 0.34 20.00 ?  9   TYR   B OH   1 
ATOM   3836 H H    A TYR   B 1 9   ? 42.856 -27.532 -19.477 0.66 28.24 ?  9   TYR   B H    1 
ATOM   3837 H H    B TYR   B 1 9   ? 42.742 -27.456 -19.527 0.34 27.52 ?  9   TYR   B H    1 
ATOM   3838 H HA   A TYR   B 1 9   ? 42.527 -29.071 -17.295 0.66 25.71 ?  9   TYR   B HA   1 
ATOM   3839 H HA   B TYR   B 1 9   ? 42.497 -28.997 -17.339 0.34 25.43 ?  9   TYR   B HA   1 
ATOM   3840 H HB2  A TYR   B 1 9   ? 41.379 -26.597 -17.991 0.66 24.71 ?  9   TYR   B HB2  1 
ATOM   3841 H HB2  B TYR   B 1 9   ? 41.309 -26.540 -18.039 0.34 24.47 ?  9   TYR   B HB2  1 
ATOM   3842 H HB3  A TYR   B 1 9   ? 40.821 -27.452 -16.773 0.66 24.71 ?  9   TYR   B HB3  1 
ATOM   3843 H HB3  B TYR   B 1 9   ? 40.771 -27.391 -16.811 0.34 24.47 ?  9   TYR   B HB3  1 
ATOM   3844 H HD1  A TYR   B 1 9   ? 43.844 -25.913 -17.836 0.66 24.25 ?  9   TYR   B HD1  1 
ATOM   3845 H HD1  B TYR   B 1 9   ? 43.700 -25.723 -17.897 0.34 23.49 ?  9   TYR   B HD1  1 
ATOM   3846 H HD2  A TYR   B 1 9   ? 41.791 -27.177 -14.645 0.66 23.62 ?  9   TYR   B HD2  1 
ATOM   3847 H HD2  B TYR   B 1 9   ? 41.788 -27.166 -14.696 0.34 23.09 ?  9   TYR   B HD2  1 
ATOM   3848 H HE1  A TYR   B 1 9   ? 45.445 -24.999 -16.453 0.66 24.49 ?  9   TYR   B HE1  1 
ATOM   3849 H HE1  B TYR   B 1 9   ? 45.276 -24.758 -16.527 0.34 23.59 ?  9   TYR   B HE1  1 
ATOM   3850 H HE2  A TYR   B 1 9   ? 43.394 -26.262 -13.251 0.66 24.14 ?  9   TYR   B HE2  1 
ATOM   3851 H HE2  B TYR   B 1 9   ? 43.366 -26.200 -13.317 0.34 23.23 ?  9   TYR   B HE2  1 
ATOM   3852 H HH   A TYR   B 1 9   ? 46.138 -24.631 -14.363 0.66 25.13 ?  9   TYR   B HH   1 
ATOM   3853 H HH   B TYR   B 1 9   ? 45.989 -24.401 -14.443 0.34 23.97 ?  9   TYR   B HH   1 
ATOM   3854 N N    . LEU   B 1 10  ? 40.344 -30.155 -17.581 1.00 19.85 ?  10  LEU   B N    1 
ATOM   3855 C CA   . LEU   B 1 10  ? 39.144 -30.935 -17.829 1.00 19.95 ?  10  LEU   B CA   1 
ATOM   3856 C C    . LEU   B 1 10  ? 37.954 -30.169 -17.273 1.00 20.07 ?  10  LEU   B C    1 
ATOM   3857 O O    . LEU   B 1 10  ? 37.971 -29.738 -16.116 1.00 19.89 ?  10  LEU   B O    1 
ATOM   3858 C CB   . LEU   B 1 10  ? 39.252 -32.287 -17.127 1.00 21.24 ?  10  LEU   B CB   1 
ATOM   3859 C CG   . LEU   B 1 10  ? 38.122 -33.267 -17.432 1.00 22.94 ?  10  LEU   B CG   1 
ATOM   3860 C CD1  . LEU   B 1 10  ? 38.263 -33.799 -18.850 1.00 24.13 ?  10  LEU   B CD1  1 
ATOM   3861 C CD2  . LEU   B 1 10  ? 38.094 -34.400 -16.421 1.00 24.01 ?  10  LEU   B CD2  1 
ATOM   3862 H H    A LEU   B 1 10  ? 40.667 -30.280 -16.790 0.66 23.79 ?  10  LEU   B H    1 
ATOM   3863 H H    B LEU   B 1 10  ? 40.707 -30.316 -16.815 0.34 23.79 ?  10  LEU   B H    1 
ATOM   3864 H HA   . LEU   B 1 10  ? 39.021 -31.073 -18.779 1.00 23.91 ?  10  LEU   B HA   1 
ATOM   3865 H HB2  . LEU   B 1 10  ? 40.085 -32.704 -17.395 1.00 25.46 ?  10  LEU   B HB2  1 
ATOM   3866 H HB3  . LEU   B 1 10  ? 39.259 -32.134 -16.168 1.00 25.46 ?  10  LEU   B HB3  1 
ATOM   3867 H HG   . LEU   B 1 10  ? 37.274 -32.797 -17.375 1.00 27.50 ?  10  LEU   B HG   1 
ATOM   3868 H HD11 . LEU   B 1 10  ? 37.576 -34.465 -19.004 1.00 28.93 ?  10  LEU   B HD11 1 
ATOM   3869 H HD12 . LEU   B 1 10  ? 38.159 -33.065 -19.475 1.00 28.93 ?  10  LEU   B HD12 1 
ATOM   3870 H HD13 . LEU   B 1 10  ? 39.141 -34.198 -18.950 1.00 28.93 ?  10  LEU   B HD13 1 
ATOM   3871 H HD21 . LEU   B 1 10  ? 37.368 -35.001 -16.645 1.00 28.78 ?  10  LEU   B HD21 1 
ATOM   3872 H HD22 . LEU   B 1 10  ? 38.940 -34.869 -16.452 1.00 28.78 ?  10  LEU   B HD22 1 
ATOM   3873 H HD23 . LEU   B 1 10  ? 37.953 -34.026 -15.536 1.00 28.78 ?  10  LEU   B HD23 1 
ATOM   3874 N N    A LYS   B 1 11  ? 36.934 -29.990 -18.102 0.66 21.12 ?  11  LYS   B N    1 
ATOM   3875 N N    B LYS   B 1 11  ? 36.924 -30.006 -18.097 0.34 21.36 ?  11  LYS   B N    1 
ATOM   3876 C CA   A LYS   B 1 11  ? 35.729 -29.284 -17.693 0.66 23.23 ?  11  LYS   B CA   1 
ATOM   3877 C CA   B LYS   B 1 11  ? 35.726 -29.281 -17.695 0.34 23.13 ?  11  LYS   B CA   1 
ATOM   3878 C C    A LYS   B 1 11  ? 34.886 -30.207 -16.819 0.66 22.24 ?  11  LYS   B C    1 
ATOM   3879 C C    B LYS   B 1 11  ? 34.853 -30.188 -16.834 0.34 22.13 ?  11  LYS   B C    1 
ATOM   3880 O O    A LYS   B 1 11  ? 34.560 -31.332 -17.223 0.66 23.97 ?  11  LYS   B O    1 
ATOM   3881 O O    B LYS   B 1 11  ? 34.461 -31.278 -17.270 0.34 23.27 ?  11  LYS   B O    1 
ATOM   3882 C CB   A LYS   B 1 11  ? 34.955 -28.857 -18.940 0.66 27.03 ?  11  LYS   B CB   1 
ATOM   3883 C CB   B LYS   B 1 11  ? 34.964 -28.835 -18.941 0.34 26.20 ?  11  LYS   B CB   1 
ATOM   3884 C CG   A LYS   B 1 11  ? 33.860 -27.830 -18.707 0.66 30.51 ?  11  LYS   B CG   1 
ATOM   3885 C CG   B LYS   B 1 11  ? 33.829 -27.862 -18.681 0.34 28.96 ?  11  LYS   B CG   1 
ATOM   3886 C CD   A LYS   B 1 11  ? 33.147 -27.497 -20.015 0.66 33.09 ?  11  LYS   B CD   1 
ATOM   3887 C CD   B LYS   B 1 11  ? 33.069 -27.564 -19.967 0.34 31.11 ?  11  LYS   B CD   1 
ATOM   3888 C CE   A LYS   B 1 11  ? 32.136 -26.374 -19.840 0.66 34.83 ?  11  LYS   B CE   1 
ATOM   3889 C CE   B LYS   B 1 11  ? 32.051 -26.449 -19.779 0.34 32.55 ?  11  LYS   B CE   1 
ATOM   3890 N NZ   A LYS   B 1 11  ? 32.794 -25.060 -19.601 0.66 35.81 ?  11  LYS   B NZ   1 
ATOM   3891 N NZ   B LYS   B 1 11  ? 32.700 -25.128 -19.551 0.34 33.34 ?  11  LYS   B NZ   1 
ATOM   3892 H H    A LYS   B 1 11  ? 36.909 -30.277 -18.913 0.66 25.32 ?  11  LYS   B H    1 
ATOM   3893 H H    B LYS   B 1 11  ? 36.891 -30.312 -18.901 0.34 25.61 ?  11  LYS   B H    1 
ATOM   3894 H HA   A LYS   B 1 11  ? 35.967 -28.490 -17.185 0.66 27.85 ?  11  LYS   B HA   1 
ATOM   3895 H HA   B LYS   B 1 11  ? 35.971 -28.495 -17.181 0.34 27.72 ?  11  LYS   B HA   1 
ATOM   3896 H HB2  A LYS   B 1 11  ? 35.580 -28.468 -19.576 0.66 32.40 ?  11  LYS   B HB2  1 
ATOM   3897 H HB2  B LYS   B 1 11  ? 35.586 -28.400 -19.547 0.34 31.41 ?  11  LYS   B HB2  1 
ATOM   3898 H HB3  A LYS   B 1 11  ? 34.540 -29.638 -19.332 0.66 32.40 ?  11  LYS   B HB3  1 
ATOM   3899 H HB3  B LYS   B 1 11  ? 34.585 -29.617 -19.371 0.34 31.41 ?  11  LYS   B HB3  1 
ATOM   3900 H HG2  A LYS   B 1 11  ? 33.209 -28.191 -18.087 0.66 36.58 ?  11  LYS   B HG2  1 
ATOM   3901 H HG2  B LYS   B 1 11  ? 33.211 -28.251 -18.043 0.34 34.72 ?  11  LYS   B HG2  1 
ATOM   3902 H HG3  A LYS   B 1 11  ? 34.250 -27.015 -18.355 0.66 36.58 ?  11  LYS   B HG3  1 
ATOM   3903 H HG3  B LYS   B 1 11  ? 34.190 -27.029 -18.338 0.34 34.72 ?  11  LYS   B HG3  1 
ATOM   3904 H HD2  A LYS   B 1 11  ? 33.802 -27.214 -20.673 0.66 39.68 ?  11  LYS   B HD2  1 
ATOM   3905 H HD2  B LYS   B 1 11  ? 33.699 -27.289 -20.652 0.34 37.30 ?  11  LYS   B HD2  1 
ATOM   3906 H HD3  A LYS   B 1 11  ? 32.675 -28.284 -20.331 0.66 39.68 ?  11  LYS   B HD3  1 
ATOM   3907 H HD3  B LYS   B 1 11  ? 32.596 -28.363 -20.249 0.34 37.30 ?  11  LYS   B HD3  1 
ATOM   3908 H HE2  A LYS   B 1 11  ? 31.598 -26.301 -20.644 0.66 41.76 ?  11  LYS   B HE2  1 
ATOM   3909 H HE2  B LYS   B 1 11  ? 31.502 -26.382 -20.576 0.34 39.03 ?  11  LYS   B HE2  1 
ATOM   3910 H HE3  A LYS   B 1 11  ? 31.570 -26.575 -19.078 0.66 41.76 ?  11  LYS   B HE3  1 
ATOM   3911 H HE3  B LYS   B 1 11  ? 31.498 -26.653 -19.009 0.34 39.03 ?  11  LYS   B HE3  1 
ATOM   3912 H HZ1  A LYS   B 1 11  ? 32.179 -24.424 -19.506 0.66 42.95 ?  11  LYS   B HZ1  1 
ATOM   3913 H HZ1  B LYS   B 1 11  ? 32.080 -24.493 -19.478 0.34 39.98 ?  11  LYS   B HZ1  1 
ATOM   3914 H HZ2  A LYS   B 1 11  ? 33.288 -25.098 -18.862 0.66 42.95 ?  11  LYS   B HZ2  1 
ATOM   3915 H HZ2  B LYS   B 1 11  ? 33.181 -25.149 -18.803 0.34 39.98 ?  11  LYS   B HZ2  1 
ATOM   3916 H HZ3  A LYS   B 1 11  ? 33.319 -24.854 -20.289 0.66 42.95 ?  11  LYS   B HZ3  1 
ATOM   3917 H HZ3  B LYS   B 1 11  ? 33.236 -24.930 -20.234 0.34 39.98 ?  11  LYS   B HZ3  1 
ATOM   3918 N N    . LEU   B 1 12  ? 34.552 -29.744 -15.613 1.00 20.54 ?  12  LEU   B N    1 
ATOM   3919 C CA   . LEU   B 1 12  ? 33.612 -30.450 -14.745 1.00 19.58 ?  12  LEU   B CA   1 
ATOM   3920 C C    . LEU   B 1 12  ? 32.220 -29.844 -14.813 1.00 18.85 ?  12  LEU   B C    1 
ATOM   3921 O O    . LEU   B 1 12  ? 31.236 -30.558 -14.991 1.00 19.63 ?  12  LEU   B O    1 
ATOM   3922 C CB   . LEU   B 1 12  ? 34.096 -30.476 -13.289 1.00 18.64 ?  12  LEU   B CB   1 
ATOM   3923 C CG   . LEU   B 1 12  ? 35.430 -31.174 -13.020 1.00 18.11 ?  12  LEU   B CG   1 
ATOM   3924 C CD1  . LEU   B 1 12  ? 35.799 -31.114 -11.548 1.00 18.09 ?  12  LEU   B CD1  1 
ATOM   3925 C CD2  . LEU   B 1 12  ? 35.409 -32.619 -13.501 1.00 19.05 ?  12  LEU   B CD2  1 
ATOM   3926 H H    A LEU   B 1 12  ? 34.863 -29.012 -15.274 0.66 24.62 ?  12  LEU   B H    1 
ATOM   3927 H H    B LEU   B 1 12  ? 34.879 -29.022 -15.267 0.34 24.62 ?  12  LEU   B H    1 
ATOM   3928 H HA   . LEU   B 1 12  ? 33.541 -31.363 -15.047 1.00 23.46 ?  12  LEU   B HA   1 
ATOM   3929 H HB2  . LEU   B 1 12  ? 34.182 -29.562 -12.979 1.00 22.34 ?  12  LEU   B HB2  1 
ATOM   3930 H HB3  . LEU   B 1 12  ? 33.424 -30.932 -12.758 1.00 22.34 ?  12  LEU   B HB3  1 
ATOM   3931 H HG   . LEU   B 1 12  ? 36.126 -30.711 -13.514 1.00 21.70 ?  12  LEU   B HG   1 
ATOM   3932 H HD11 . LEU   B 1 12  ? 36.654 -31.561 -11.417 1.00 21.68 ?  12  LEU   B HD11 1 
ATOM   3933 H HD12 . LEU   B 1 12  ? 35.872 -30.185 -11.275 1.00 21.68 ?  12  LEU   B HD12 1 
ATOM   3934 H HD13 . LEU   B 1 12  ? 35.113 -31.559 -11.029 1.00 21.68 ?  12  LEU   B HD13 1 
ATOM   3935 H HD21 . LEU   B 1 12  ? 36.223 -33.062 -13.212 1.00 22.84 ?  12  LEU   B HD21 1 
ATOM   3936 H HD22 . LEU   B 1 12  ? 34.637 -33.067 -13.120 1.00 22.84 ?  12  LEU   B HD22 1 
ATOM   3937 H HD23 . LEU   B 1 12  ? 35.353 -32.630 -14.469 1.00 22.84 ?  12  LEU   B HD23 1 
ATOM   3938 N N    . THR   B 1 13  ? 32.125 -28.529 -14.677 1.00 18.87 ?  13  THR   B N    1 
ATOM   3939 C CA   . THR   B 1 13  ? 30.899 -27.781 -14.889 1.00 19.13 ?  13  THR   B CA   1 
ATOM   3940 C C    . THR   B 1 13  ? 31.241 -26.599 -15.788 1.00 21.81 ?  13  THR   B C    1 
ATOM   3941 O O    . THR   B 1 13  ? 32.392 -26.421 -16.205 1.00 22.95 ?  13  THR   B O    1 
ATOM   3942 C CB   . THR   B 1 13  ? 30.309 -27.285 -13.564 1.00 18.74 ?  13  THR   B CB   1 
ATOM   3943 O OG1  . THR   B 1 13  ? 31.163 -26.272 -13.032 1.00 18.32 ?  13  THR   B OG1  1 
ATOM   3944 C CG2  . THR   B 1 13  ? 30.194 -28.418 -12.561 1.00 19.38 ?  13  THR   B CG2  1 
ATOM   3945 H H    . THR   B 1 13  ? 32.788 -28.023 -14.451 1.00 22.62 ?  13  THR   B H    1 
ATOM   3946 H HA   . THR   B 1 13  ? 30.240 -28.342 -15.326 1.00 22.92 ?  13  THR   B HA   1 
ATOM   3947 H HB   . THR   B 1 13  ? 29.423 -26.912 -13.715 1.00 22.47 ?  13  THR   B HB   1 
ATOM   3948 H HG1  . THR   B 1 13  ? 30.853 -25.500 -13.211 1.00 21.95 ?  13  THR   B HG1  1 
ATOM   3949 H HG21 . THR   B 1 13  ? 29.701 -28.123 -11.780 1.00 23.23 ?  13  THR   B HG21 1 
ATOM   3950 H HG22 . THR   B 1 13  ? 29.728 -29.166 -12.965 1.00 23.23 ?  13  THR   B HG22 1 
ATOM   3951 H HG23 . THR   B 1 13  ? 31.077 -28.708 -12.286 1.00 23.23 ?  13  THR   B HG23 1 
ATOM   3952 N N    A ASP   B 1 14  ? 30.238 -25.770 -16.076 0.66 23.31 ?  14  ASP   B N    1 
ATOM   3953 N N    B ASP   B 1 14  ? 30.240 -25.758 -16.063 0.34 22.81 ?  14  ASP   B N    1 
ATOM   3954 C CA   A ASP   B 1 14  ? 30.485 -24.623 -16.941 0.66 24.70 ?  14  ASP   B CA   1 
ATOM   3955 C CA   B ASP   B 1 14  ? 30.461 -24.611 -16.938 0.34 23.62 ?  14  ASP   B CA   1 
ATOM   3956 C C    A ASP   B 1 14  ? 31.600 -23.737 -16.400 0.66 22.47 ?  14  ASP   B C    1 
ATOM   3957 C C    B ASP   B 1 14  ? 31.474 -23.624 -16.376 0.34 21.70 ?  14  ASP   B C    1 
ATOM   3958 O O    A ASP   B 1 14  ? 32.317 -23.102 -17.184 0.66 23.92 ?  14  ASP   B O    1 
ATOM   3959 O O    B ASP   B 1 14  ? 31.960 -22.769 -17.124 0.34 22.36 ?  14  ASP   B O    1 
ATOM   3960 C CB   A ASP   B 1 14  ? 29.201 -23.820 -17.143 0.66 28.22 ?  14  ASP   B CB   1 
ATOM   3961 C CB   B ASP   B 1 14  ? 29.149 -23.874 -17.207 0.34 26.27 ?  14  ASP   B CB   1 
ATOM   3962 C CG   A ASP   B 1 14  ? 28.217 -24.512 -18.061 0.66 31.42 ?  14  ASP   B CG   1 
ATOM   3963 C CG   B ASP   B 1 14  ? 28.257 -24.615 -18.183 0.34 28.49 ?  14  ASP   B CG   1 
ATOM   3964 O OD1  A ASP   B 1 14  ? 28.595 -25.498 -18.733 0.66 32.49 ?  14  ASP   B OD1  1 
ATOM   3965 O OD1  B ASP   B 1 14  ? 28.793 -25.318 -19.067 0.34 29.26 ?  14  ASP   B OD1  1 
ATOM   3966 O OD2  A ASP   B 1 14  ? 27.051 -24.069 -18.101 0.66 32.75 -1 14  ASP   B OD2  1 
ATOM   3967 O OD2  B ASP   B 1 14  ? 27.019 -24.503 -18.066 0.34 29.27 -1 14  ASP   B OD2  1 
ATOM   3968 H H    A ASP   B 1 14  ? 29.431 -25.838 -15.784 0.66 27.94 ?  14  ASP   B H    1 
ATOM   3969 H H    B ASP   B 1 14  ? 29.439 -25.828 -15.760 0.34 27.35 ?  14  ASP   B H    1 
ATOM   3970 H HA   A ASP   B 1 14  ? 30.773 -24.940 -17.806 0.66 29.61 ?  14  ASP   B HA   1 
ATOM   3971 H HA   B ASP   B 1 14  ? 30.798 -24.931 -17.786 0.34 28.32 ?  14  ASP   B HA   1 
ATOM   3972 H HB2  A ASP   B 1 14  ? 28.752 -23.703 -16.295 0.66 33.84 ?  14  ASP   B HB2  1 
ATOM   3973 H HB2  B ASP   B 1 14  ? 28.665 -23.775 -16.373 0.34 31.49 ?  14  ASP   B HB2  1 
ATOM   3974 H HB3  A ASP   B 1 14  ? 29.414 -22.960 -17.534 0.66 33.84 ?  14  ASP   B HB3  1 
ATOM   3975 H HB3  B ASP   B 1 14  ? 29.354 -22.996 -17.574 0.34 31.49 ?  14  ASP   B HB3  1 
ATOM   3976 N N    . ASN   B 1 15  ? 31.785 -23.696 -15.078 1.00 19.52 ?  15  ASN   B N    1 
ATOM   3977 C CA   . ASN   B 1 15  ? 32.755 -22.779 -14.479 1.00 17.16 ?  15  ASN   B CA   1 
ATOM   3978 C C    . ASN   B 1 15  ? 33.854 -23.432 -13.652 1.00 15.59 ?  15  ASN   B C    1 
ATOM   3979 O O    . ASN   B 1 15  ? 34.729 -22.710 -13.160 1.00 15.68 ?  15  ASN   B O    1 
ATOM   3980 C CB   . ASN   B 1 15  ? 32.053 -21.719 -13.614 1.00 17.26 ?  15  ASN   B CB   1 
ATOM   3981 C CG   . ASN   B 1 15  ? 31.439 -22.311 -12.365 1.00 16.65 ?  15  ASN   B CG   1 
ATOM   3982 O OD1  . ASN   B 1 15  ? 30.493 -23.107 -12.439 1.00 18.60 ?  15  ASN   B OD1  1 
ATOM   3983 N ND2  . ASN   B 1 15  ? 31.977 -21.959 -11.214 1.00 15.80 ?  15  ASN   B ND2  1 
ATOM   3984 H H    A ASN   B 1 15  ? 31.360 -24.185 -14.511 0.66 23.40 ?  15  ASN   B H    1 
ATOM   3985 H H    B ASN   B 1 15  ? 31.420 -24.239 -14.521 0.34 23.40 ?  15  ASN   B H    1 
ATOM   3986 H HA   . ASN   B 1 15  ? 33.197 -22.297 -15.187 1.00 20.56 ?  15  ASN   B HA   1 
ATOM   3987 H HB2  . ASN   B 1 15  ? 32.706 -21.042 -13.348 1.00 20.68 ?  15  ASN   B HB2  1 
ATOM   3988 H HB3  . ASN   B 1 15  ? 31.345 -21.294 -14.131 1.00 20.68 ?  15  ASN   B HB3  1 
ATOM   3989 H HD21 . ASN   B 1 15  ? 31.662 -22.263 -10.476 1.00 18.94 ?  15  ASN   B HD21 1 
ATOM   3990 H HD22 . ASN   B 1 15  ? 32.648 -21.408 -11.194 1.00 18.94 ?  15  ASN   B HD22 1 
ATOM   3991 N N    . VAL   B 1 16  ? 33.840 -24.749 -13.469 1.00 15.74 ?  16  VAL   B N    1 
ATOM   3992 C CA   . VAL   B 1 16  ? 34.840 -25.442 -12.664 1.00 15.05 ?  16  VAL   B CA   1 
ATOM   3993 C C    . VAL   B 1 16  ? 35.623 -26.380 -13.567 1.00 15.37 ?  16  VAL   B C    1 
ATOM   3994 O O    . VAL   B 1 16  ? 35.040 -27.258 -14.223 1.00 16.06 ?  16  VAL   B O    1 
ATOM   3995 C CB   . VAL   B 1 16  ? 34.219 -26.208 -11.485 1.00 14.92 ?  16  VAL   B CB   1 
ATOM   3996 C CG1  . VAL   B 1 16  ? 35.297 -26.954 -10.695 1.00 15.23 ?  16  VAL   B CG1  1 
ATOM   3997 C CG2  . VAL   B 1 16  ? 33.427 -25.255 -10.589 1.00 15.77 ?  16  VAL   B CG2  1 
ATOM   3998 H H    . VAL   B 1 16  ? 33.236 -25.277 -13.800 1.00 18.86 ?  16  VAL   B H    1 
ATOM   3999 H HA   . VAL   B 1 16  ? 35.455 -24.795 -12.302 1.00 18.03 ?  16  VAL   B HA   1 
ATOM   4000 H HB   . VAL   B 1 16  ? 33.596 -26.871 -11.829 1.00 17.88 ?  16  VAL   B HB   1 
ATOM   4001 H HG11 . VAL   B 1 16  ? 34.913 -27.264 -9.855  1.00 18.25 ?  16  VAL   B HG11 1 
ATOM   4002 H HG12 . VAL   B 1 16  ? 35.605 -27.711 -11.213 1.00 18.25 ?  16  VAL   B HG12 1 
ATOM   4003 H HG13 . VAL   B 1 16  ? 36.030 -26.347 -10.515 1.00 18.25 ?  16  VAL   B HG13 1 
ATOM   4004 H HG21 . VAL   B 1 16  ? 33.091 -25.748 -9.821  1.00 18.90 ?  16  VAL   B HG21 1 
ATOM   4005 H HG22 . VAL   B 1 16  ? 34.007 -24.540 -10.296 1.00 18.90 ?  16  VAL   B HG22 1 
ATOM   4006 H HG23 . VAL   B 1 16  ? 32.681 -24.893 -11.096 1.00 18.90 ?  16  VAL   B HG23 1 
ATOM   4007 N N    . TYR   B 1 17  ? 36.942 -26.213 -13.560 1.00 15.96 ?  17  TYR   B N    1 
ATOM   4008 C CA   . TYR   B 1 17  ? 37.880 -26.953 -14.385 1.00 16.04 ?  17  TYR   B CA   1 
ATOM   4009 C C    . TYR   B 1 17  ? 38.949 -27.559 -13.484 1.00 14.89 ?  17  TYR   B C    1 
ATOM   4010 O O    . TYR   B 1 17  ? 39.240 -27.034 -12.407 1.00 15.16 ?  17  TYR   B O    1 
ATOM   4011 C CB   . TYR   B 1 17  ? 38.572 -26.025 -15.394 1.00 19.81 ?  17  TYR   B CB   1 
ATOM   4012 C CG   . TYR   B 1 17  ? 37.639 -25.265 -16.305 1.00 24.36 ?  17  TYR   B CG   1 
ATOM   4013 C CD1  . TYR   B 1 17  ? 37.103 -24.042 -15.927 1.00 26.63 ?  17  TYR   B CD1  1 
ATOM   4014 C CD2  . TYR   B 1 17  ? 37.300 -25.772 -17.552 1.00 26.76 ?  17  TYR   B CD2  1 
ATOM   4015 C CE1  . TYR   B 1 17  ? 36.248 -23.344 -16.765 1.00 28.56 ?  17  TYR   B CE1  1 
ATOM   4016 C CE2  . TYR   B 1 17  ? 36.448 -25.086 -18.396 1.00 28.77 ?  17  TYR   B CE2  1 
ATOM   4017 C CZ   . TYR   B 1 17  ? 35.924 -23.872 -17.998 1.00 29.75 ?  17  TYR   B CZ   1 
ATOM   4018 O OH   . TYR   B 1 17  ? 35.077 -23.184 -18.836 1.00 30.73 ?  17  TYR   B OH   1 
ATOM   4019 H H    . TYR   B 1 17  ? 37.337 -25.634 -13.053 1.00 19.12 ?  17  TYR   B H    1 
ATOM   4020 H HA   . TYR   B 1 17  ? 37.413 -27.660 -14.863 1.00 19.22 ?  17  TYR   B HA   1 
ATOM   4021 H HB2  . TYR   B 1 17  ? 39.115 -25.382 -14.915 1.00 23.74 ?  17  TYR   B HB2  1 
ATOM   4022 H HB3  . TYR   B 1 17  ? 39.129 -26.569 -15.962 1.00 23.74 ?  17  TYR   B HB3  1 
ATOM   4023 H HD1  . TYR   B 1 17  ? 37.320 -23.683 -15.098 1.00 31.93 ?  17  TYR   B HD1  1 
ATOM   4024 H HD2  . TYR   B 1 17  ? 37.647 -26.590 -17.825 1.00 32.08 ?  17  TYR   B HD2  1 
ATOM   4025 H HE1  . TYR   B 1 17  ? 35.894 -22.526 -16.501 1.00 34.25 ?  17  TYR   B HE1  1 
ATOM   4026 H HE2  . TYR   B 1 17  ? 36.226 -25.441 -19.229 1.00 34.50 ?  17  TYR   B HE2  1 
ATOM   4027 H HH   . TYR   B 1 17  ? 34.834 -22.466 -18.473 1.00 36.85 ?  17  TYR   B HH   1 
ATOM   4028 N N    . ILE   B 1 18  ? 39.553 -28.663 -13.926 1.00 15.03 ?  18  ILE   B N    1 
ATOM   4029 C CA   . ILE   B 1 18  ? 40.487 -29.398 -13.079 1.00 14.99 ?  18  ILE   B CA   1 
ATOM   4030 C C    . ILE   B 1 18  ? 41.635 -29.952 -13.915 1.00 15.65 ?  18  ILE   B C    1 
ATOM   4031 O O    . ILE   B 1 18  ? 41.463 -30.335 -15.075 1.00 16.73 ?  18  ILE   B O    1 
ATOM   4032 C CB   . ILE   B 1 18  ? 39.741 -30.509 -12.284 1.00 15.73 ?  18  ILE   B CB   1 
ATOM   4033 C CG1  . ILE   B 1 18  ? 40.604 -31.067 -11.148 1.00 16.32 ?  18  ILE   B CG1  1 
ATOM   4034 C CG2  . ILE   B 1 18  ? 39.227 -31.627 -13.211 1.00 16.39 ?  18  ILE   B CG2  1 
ATOM   4035 C CD1  . ILE   B 1 18  ? 39.823 -31.937 -10.171 1.00 17.57 ?  18  ILE   B CD1  1 
ATOM   4036 H H    . ILE   B 1 18  ? 39.446 -28.991 -14.709 1.00 18.01 ?  18  ILE   B H    1 
ATOM   4037 H HA   . ILE   B 1 18  ? 40.857 -28.778 -12.426 1.00 17.96 ?  18  ILE   B HA   1 
ATOM   4038 H HB   . ILE   B 1 18  ? 38.963 -30.100 -11.871 1.00 18.84 ?  18  ILE   B HB   1 
ATOM   4039 H HG12 . ILE   B 1 18  ? 41.312 -31.605 -11.526 1.00 19.55 ?  18  ILE   B HG12 1 
ATOM   4040 H HG13 . ILE   B 1 18  ? 40.980 -30.326 -10.647 1.00 19.55 ?  18  ILE   B HG13 1 
ATOM   4041 H HG21 . ILE   B 1 18  ? 38.641 -32.213 -12.705 1.00 19.63 ?  18  ILE   B HG21 1 
ATOM   4042 H HG22 . ILE   B 1 18  ? 38.734 -31.223 -13.943 1.00 19.63 ?  18  ILE   B HG22 1 
ATOM   4043 H HG23 . ILE   B 1 18  ? 39.981 -32.126 -13.554 1.00 19.63 ?  18  ILE   B HG23 1 
ATOM   4044 H HD11 . ILE   B 1 18  ? 40.410 -32.195 -9.442  1.00 21.05 ?  18  ILE   B HD11 1 
ATOM   4045 H HD12 . ILE   B 1 18  ? 39.071 -31.432 -9.827  1.00 21.05 ?  18  ILE   B HD12 1 
ATOM   4046 H HD13 . ILE   B 1 18  ? 39.508 -32.728 -10.636 1.00 21.05 ?  18  ILE   B HD13 1 
ATOM   4047 N N    . LYS   B 1 19  ? 42.820 -29.992 -13.308 1.00 16.40 ?  19  LYS   B N    1 
ATOM   4048 C CA   . LYS   B 1 19  ? 44.023 -30.465 -13.975 1.00 17.23 ?  19  LYS   B CA   1 
ATOM   4049 C C    . LYS   B 1 19  ? 44.924 -31.149 -12.958 1.00 16.85 ?  19  LYS   B C    1 
ATOM   4050 O O    . LYS   B 1 19  ? 45.016 -30.720 -11.806 1.00 16.70 ?  19  LYS   B O    1 
ATOM   4051 C CB   . LYS   B 1 19  ? 44.786 -29.300 -14.616 1.00 19.14 ?  19  LYS   B CB   1 
ATOM   4052 C CG   . LYS   B 1 19  ? 45.977 -29.711 -15.457 1.00 21.47 ?  19  LYS   B CG   1 
ATOM   4053 C CD   . LYS   B 1 19  ? 46.622 -28.485 -16.083 1.00 23.90 ?  19  LYS   B CD   1 
ATOM   4054 C CE   . LYS   B 1 19  ? 47.805 -28.848 -16.952 1.00 26.46 ?  19  LYS   B CE   1 
ATOM   4055 N NZ   . LYS   B 1 19  ? 48.487 -27.639 -17.483 1.00 28.18 ?  19  LYS   B NZ   1 
ATOM   4056 H H    . LYS   B 1 19  ? 42.938 -29.750 -12.493 1.00 19.66 ?  19  LYS   B H    1 
ATOM   4057 H HA   . LYS   B 1 19  ? 43.773 -31.103 -14.666 1.00 20.65 ?  19  LYS   B HA   1 
ATOM   4058 H HB2  . LYS   B 1 19  ? 44.177 -28.820 -15.195 1.00 22.94 ?  19  LYS   B HB2  1 
ATOM   4059 H HB3  . LYS   B 1 19  ? 45.100 -28.713 -13.910 1.00 22.94 ?  19  LYS   B HB3  1 
ATOM   4060 H HG2  . LYS   B 1 19  ? 46.630 -30.155 -14.897 1.00 25.73 ?  19  LYS   B HG2  1 
ATOM   4061 H HG3  . LYS   B 1 19  ? 45.679 -30.303 -16.168 1.00 25.73 ?  19  LYS   B HG3  1 
ATOM   4062 H HD2  . LYS   B 1 19  ? 45.966 -28.027 -16.635 1.00 28.65 ?  19  LYS   B HD2  1 
ATOM   4063 H HD3  . LYS   B 1 19  ? 46.931 -27.894 -15.376 1.00 28.65 ?  19  LYS   B HD3  1 
ATOM   4064 H HE2  . LYS   B 1 19  ? 48.444 -29.351 -16.424 1.00 31.72 ?  19  LYS   B HE2  1 
ATOM   4065 H HE3  . LYS   B 1 19  ? 47.497 -29.379 -17.702 1.00 31.72 ?  19  LYS   B HE3  1 
ATOM   4066 H HZ1  . LYS   B 1 19  ? 49.176 -27.879 -17.997 1.00 33.79 ?  19  LYS   B HZ1  1 
ATOM   4067 H HZ2  . LYS   B 1 19  ? 47.920 -27.157 -17.972 1.00 33.79 ?  19  LYS   B HZ2  1 
ATOM   4068 H HZ3  . LYS   B 1 19  ? 48.790 -27.138 -16.813 1.00 33.79 ?  19  LYS   B HZ3  1 
ATOM   4069 N N    . ASN   B 1 20  ? 45.600 -32.207 -13.394 1.00 18.76 ?  20  ASN   B N    1 
ATOM   4070 C CA   . ASN   B 1 20  ? 46.621 -32.845 -12.572 1.00 19.50 ?  20  ASN   B CA   1 
ATOM   4071 C C    . ASN   B 1 20  ? 47.911 -32.047 -12.742 1.00 19.90 ?  20  ASN   B C    1 
ATOM   4072 O O    . ASN   B 1 20  ? 48.555 -32.117 -13.797 1.00 22.13 ?  20  ASN   B O    1 
ATOM   4073 C CB   . ASN   B 1 20  ? 46.778 -34.301 -13.011 1.00 21.61 ?  20  ASN   B CB   1 
ATOM   4074 C CG   . ASN   B 1 20  ? 47.944 -35.011 -12.335 1.00 23.64 ?  20  ASN   B CG   1 
ATOM   4075 O OD1  . ASN   B 1 20  ? 48.624 -35.830 -12.960 1.00 25.78 ?  20  ASN   B OD1  1 
ATOM   4076 N ND2  . ASN   B 1 20  ? 48.171 -34.721 -11.062 1.00 23.53 ?  20  ASN   B ND2  1 
ATOM   4077 H H    . ASN   B 1 20  ? 45.479 -32.569 -14.163 1.00 22.49 ?  20  ASN   B H    1 
ATOM   4078 H HA   . ASN   B 1 20  ? 46.341 -32.823 -11.640 1.00 23.37 ?  20  ASN   B HA   1 
ATOM   4079 H HB2  . ASN   B 1 20  ? 45.958 -34.782 -12.796 1.00 25.91 ?  20  ASN   B HB2  1 
ATOM   4080 H HB3  . ASN   B 1 20  ? 46.921 -34.319 -13.970 1.00 25.91 ?  20  ASN   B HB3  1 
ATOM   4081 H HD21 . ASN   B 1 20  ? 48.817 -35.097 -10.644 1.00 28.21 ?  20  ASN   B HD21 1 
ATOM   4082 H HD22 . ASN   B 1 20  ? 47.674 -34.144 -10.653 1.00 28.21 ?  20  ASN   B HD22 1 
ATOM   4083 N N    . ALA   B 1 21  ? 48.280 -31.267 -11.724 1.00 19.67 ?  21  ALA   B N    1 
ATOM   4084 C CA   . ALA   B 1 21  ? 49.398 -30.347 -11.881 1.00 20.66 ?  21  ALA   B CA   1 
ATOM   4085 C C    . ALA   B 1 21  ? 49.868 -29.826 -10.527 1.00 18.96 ?  21  ALA   B C    1 
ATOM   4086 O O    . ALA   B 1 21  ? 49.131 -29.841 -9.536  1.00 18.81 ?  21  ALA   B O    1 
ATOM   4087 C CB   . ALA   B 1 21  ? 49.008 -29.181 -12.790 1.00 22.13 ?  21  ALA   B CB   1 
ATOM   4088 H H    . ALA   B 1 21  ? 47.899 -31.253 -10.949 1.00 23.57 ?  21  ALA   B H    1 
ATOM   4089 H HA   . ALA   B 1 21  ? 50.132 -30.825 -12.296 1.00 24.76 ?  21  ALA   B HA   1 
ATOM   4090 H HB1  . ALA   B 1 21  ? 49.796 -28.650 -12.955 1.00 26.52 ?  21  ALA   B HB1  1 
ATOM   4091 H HB2  . ALA   B 1 21  ? 48.667 -29.541 -13.625 1.00 26.52 ?  21  ALA   B HB2  1 
ATOM   4092 H HB3  . ALA   B 1 21  ? 48.324 -28.657 -12.351 1.00 26.52 ?  21  ALA   B HB3  1 
ATOM   4093 N N    . ASP   B 1 22  ? 51.129 -29.389 -10.512 1.00 17.62 ?  22  ASP   B N    1 
ATOM   4094 C CA   . ASP   B 1 22  ? 51.753 -28.697 -9.388  1.00 17.39 ?  22  ASP   B CA   1 
ATOM   4095 C C    . ASP   B 1 22  ? 51.346 -27.226 -9.458  1.00 15.94 ?  22  ASP   B C    1 
ATOM   4096 O O    . ASP   B 1 22  ? 51.641 -26.549 -10.447 1.00 15.91 ?  22  ASP   B O    1 
ATOM   4097 C CB   . ASP   B 1 22  ? 53.272 -28.875 -9.547  1.00 19.00 ?  22  ASP   B CB   1 
ATOM   4098 C CG   . ASP   B 1 22  ? 54.098 -28.117 -8.515  1.00 20.59 ?  22  ASP   B CG   1 
ATOM   4099 O OD1  . ASP   B 1 22  ? 53.737 -26.994 -8.129  1.00 20.23 ?  22  ASP   B OD1  1 
ATOM   4100 O OD2  . ASP   B 1 22  ? 55.163 -28.641 -8.118  1.00 23.15 -1 22  ASP   B OD2  1 
ATOM   4101 H H    . ASP   B 1 22  ? 51.666 -29.501 -11.178 1.00 21.12 ?  22  ASP   B H    1 
ATOM   4102 H HA   . ASP   B 1 22  ? 51.465 -29.084 -8.545  1.00 20.84 ?  22  ASP   B HA   1 
ATOM   4103 H HB2  . ASP   B 1 22  ? 53.493 -29.811 -9.469  1.00 22.78 ?  22  ASP   B HB2  1 
ATOM   4104 H HB3  . ASP   B 1 22  ? 53.534 -28.540 -10.419 1.00 22.78 ?  22  ASP   B HB3  1 
ATOM   4105 N N    . ILE   B 1 23  ? 50.641 -26.739 -8.427  1.00 15.39 ?  23  ILE   B N    1 
ATOM   4106 C CA   . ILE   B 1 23  ? 50.057 -25.393 -8.475  1.00 14.20 ?  23  ILE   B CA   1 
ATOM   4107 C C    . ILE   B 1 23  ? 51.120 -24.311 -8.617  1.00 13.63 ?  23  ILE   B C    1 
ATOM   4108 O O    . ILE   B 1 23  ? 50.857 -23.261 -9.218  1.00 13.06 ?  23  ILE   B O    1 
ATOM   4109 C CB   . ILE   B 1 23  ? 49.143 -25.148 -7.258  1.00 14.10 ?  23  ILE   B CB   1 
ATOM   4110 C CG1  . ILE   B 1 23  ? 48.326 -23.864 -7.446  1.00 14.96 ?  23  ILE   B CG1  1 
ATOM   4111 C CG2  . ILE   B 1 23  ? 49.940 -25.133 -5.963  1.00 15.49 ?  23  ILE   B CG2  1 
ATOM   4112 C CD1  . ILE   B 1 23  ? 47.198 -23.692 -6.438  1.00 15.80 ?  23  ILE   B CD1  1 
ATOM   4113 H H    . ILE   B 1 23  ? 50.488 -27.170 -7.702  1.00 18.44 ?  23  ILE   B H    1 
ATOM   4114 H HA   . ILE   B 1 23  ? 49.497 -25.340 -9.261  1.00 17.01 ?  23  ILE   B HA   1 
ATOM   4115 H HB   . ILE   B 1 23  ? 48.519 -25.889 -7.210  1.00 16.90 ?  23  ILE   B HB   1 
ATOM   4116 H HG12 . ILE   B 1 23  ? 48.931 -23.104 -7.356  1.00 17.93 ?  23  ILE   B HG12 1 
ATOM   4117 H HG13 . ILE   B 1 23  ? 47.945 -23.869 -8.337  1.00 17.93 ?  23  ILE   B HG13 1 
ATOM   4118 H HG21 . ILE   B 1 23  ? 49.323 -25.115 -5.216  1.00 18.57 ?  23  ILE   B HG21 1 
ATOM   4119 H HG22 . ILE   B 1 23  ? 50.489 -25.933 -5.920  1.00 18.57 ?  23  ILE   B HG22 1 
ATOM   4120 H HG23 . ILE   B 1 23  ? 50.504 -24.345 -5.948  1.00 18.57 ?  23  ILE   B HG23 1 
ATOM   4121 H HD11 . ILE   B 1 23  ? 46.710 -22.885 -6.653  1.00 18.94 ?  23  ILE   B HD11 1 
ATOM   4122 H HD12 . ILE   B 1 23  ? 46.612 -24.463 -6.497  1.00 18.94 ?  23  ILE   B HD12 1 
ATOM   4123 H HD13 . ILE   B 1 23  ? 47.577 -23.629 -5.549  1.00 18.94 ?  23  ILE   B HD13 1 
ATOM   4124 N N    . VAL   B 1 24  ? 52.315 -24.525 -8.061  1.00 13.93 ?  24  VAL   B N    1 
ATOM   4125 C CA   . VAL   B 1 24  ? 53.391 -23.546 -8.218  1.00 14.87 ?  24  VAL   B CA   1 
ATOM   4126 C C    . VAL   B 1 24  ? 53.846 -23.494 -9.668  1.00 15.46 ?  24  VAL   B C    1 
ATOM   4127 O O    . VAL   B 1 24  ? 53.988 -22.416 -10.258 1.00 15.69 ?  24  VAL   B O    1 
ATOM   4128 C CB   . VAL   B 1 24  ? 54.567 -23.869 -7.275  1.00 15.65 ?  24  VAL   B CB   1 
ATOM   4129 C CG1  . VAL   B 1 24  ? 55.777 -22.985 -7.606  1.00 16.66 ?  24  VAL   B CG1  1 
ATOM   4130 C CG2  . VAL   B 1 24  ? 54.158 -23.675 -5.833  1.00 16.21 ?  24  VAL   B CG2  1 
ATOM   4131 H H    . VAL   B 1 24  ? 52.527 -25.213 -7.594  1.00 16.69 ?  24  VAL   B H    1 
ATOM   4132 H HA   . VAL   B 1 24  ? 53.057 -22.666 -7.978  1.00 17.81 ?  24  VAL   B HA   1 
ATOM   4133 H HB   . VAL   B 1 24  ? 54.831 -24.794 -7.389  1.00 18.76 ?  24  VAL   B HB   1 
ATOM   4134 H HG11 . VAL   B 1 24  ? 56.377 -22.972 -6.843  1.00 19.96 ?  24  VAL   B HG11 1 
ATOM   4135 H HG12 . VAL   B 1 24  ? 56.234 -23.352 -8.378  1.00 19.96 ?  24  VAL   B HG12 1 
ATOM   4136 H HG13 . VAL   B 1 24  ? 55.468 -22.086 -7.796  1.00 19.96 ?  24  VAL   B HG13 1 
ATOM   4137 H HG21 . VAL   B 1 24  ? 54.878 -23.968 -5.254  1.00 19.42 ?  24  VAL   B HG21 1 
ATOM   4138 H HG22 . VAL   B 1 24  ? 53.977 -22.732 -5.681  1.00 19.42 ?  24  VAL   B HG22 1 
ATOM   4139 H HG23 . VAL   B 1 24  ? 53.359 -24.197 -5.659  1.00 19.42 ?  24  VAL   B HG23 1 
ATOM   4140 N N    . GLU   B 1 25  ? 54.113 -24.661 -10.257 1.00 16.28 ?  25  GLU   B N    1 
ATOM   4141 C CA   . GLU   B 1 25  ? 54.500 -24.697 -11.660 1.00 17.81 ?  25  GLU   B CA   1 
ATOM   4142 C C    . GLU   B 1 25  ? 53.385 -24.164 -12.546 1.00 16.37 ?  25  GLU   B C    1 
ATOM   4143 O O    . GLU   B 1 25  ? 53.649 -23.451 -13.525 1.00 17.17 ?  25  GLU   B O    1 
ATOM   4144 C CB   . GLU   B 1 25  ? 54.912 -26.112 -12.058 1.00 22.97 ?  25  GLU   B CB   1 
ATOM   4145 C CG   . GLU   B 1 25  ? 56.210 -26.555 -11.390 1.00 28.59 ?  25  GLU   B CG   1 
ATOM   4146 C CD   . GLU   B 1 25  ? 57.316 -25.506 -11.461 1.00 33.84 ?  25  GLU   B CD   1 
ATOM   4147 O OE1  . GLU   B 1 25  ? 57.706 -25.118 -12.584 1.00 35.52 ?  25  GLU   B OE1  1 
ATOM   4148 O OE2  . GLU   B 1 25  ? 57.785 -25.052 -10.390 1.00 35.44 -1 25  GLU   B OE2  1 
ATOM   4149 H H    . GLU   B 1 25  ? 54.072 -25.427 -9.872  1.00 19.51 ?  25  GLU   B H    1 
ATOM   4150 H HA   . GLU   B 1 25  ? 55.253 -24.103 -11.788 1.00 21.34 ?  25  GLU   B HA   1 
ATOM   4151 H HB2  . GLU   B 1 25  ? 54.215 -26.734 -11.792 1.00 27.53 ?  25  GLU   B HB2  1 
ATOM   4152 H HB3  . GLU   B 1 25  ? 55.038 -26.149 -13.019 1.00 27.53 ?  25  GLU   B HB3  1 
ATOM   4153 H HG2  . GLU   B 1 25  ? 56.047 -26.713 -10.453 1.00 34.28 ?  25  GLU   B HG2  1 
ATOM   4154 H HG3  . GLU   B 1 25  ? 56.525 -27.364 -11.823 1.00 34.28 ?  25  GLU   B HG3  1 
ATOM   4155 N N    A GLU   B 1 26  ? 52.131 -24.486 -12.216 0.66 15.15 ?  26  GLU   B N    1 
ATOM   4156 N N    B GLU   B 1 26  ? 52.130 -24.484 -12.214 0.34 15.59 ?  26  GLU   B N    1 
ATOM   4157 C CA   A GLU   B 1 26  ? 51.007 -23.955 -12.981 0.66 16.26 ?  26  GLU   B CA   1 
ATOM   4158 C CA   B GLU   B 1 26  ? 51.006 -23.959 -12.983 0.34 15.89 ?  26  GLU   B CA   1 
ATOM   4159 C C    A GLU   B 1 26  ? 50.963 -22.438 -12.903 0.66 15.11 ?  26  GLU   B C    1 
ATOM   4160 C C    B GLU   B 1 26  ? 50.944 -22.442 -12.899 0.34 14.84 ?  26  GLU   B C    1 
ATOM   4161 O O    A GLU   B 1 26  ? 50.769 -21.761 -13.918 0.66 16.42 ?  26  GLU   B O    1 
ATOM   4162 O O    B GLU   B 1 26  ? 50.725 -21.768 -13.911 0.34 15.56 ?  26  GLU   B O    1 
ATOM   4163 C CB   A GLU   B 1 26  ? 49.692 -24.534 -12.462 0.66 18.49 ?  26  GLU   B CB   1 
ATOM   4164 C CB   B GLU   B 1 26  ? 49.693 -24.560 -12.480 0.34 17.19 ?  26  GLU   B CB   1 
ATOM   4165 C CG   A GLU   B 1 26  ? 49.300 -25.854 -13.083 0.66 21.63 ?  26  GLU   B CG   1 
ATOM   4166 C CG   B GLU   B 1 26  ? 49.223 -25.775 -13.256 0.34 18.97 ?  26  GLU   B CG   1 
ATOM   4167 C CD   A GLU   B 1 26  ? 49.055 -25.764 -14.589 0.66 22.84 ?  26  GLU   B CD   1 
ATOM   4168 C CD   B GLU   B 1 26  ? 48.834 -25.433 -14.693 0.34 19.08 ?  26  GLU   B CD   1 
ATOM   4169 O OE1  A GLU   B 1 26  ? 48.220 -24.946 -15.036 0.66 23.08 ?  26  GLU   B OE1  1 
ATOM   4170 O OE1  B GLU   B 1 26  ? 47.735 -24.868 -14.910 0.34 20.20 ?  26  GLU   B OE1  1 
ATOM   4171 O OE2  A GLU   B 1 26  ? 49.700 -26.527 -15.327 0.66 23.75 -1 26  GLU   B OE2  1 
ATOM   4172 O OE2  B GLU   B 1 26  ? 49.632 -25.724 -15.601 0.34 18.49 -1 26  GLU   B OE2  1 
ATOM   4173 H H    A GLU   B 1 26  ? 51.906 -24.998 -11.561 0.66 18.15 ?  26  GLU   B H    1 
ATOM   4174 H H    B GLU   B 1 26  ? 51.908 -24.991 -11.556 0.34 18.68 ?  26  GLU   B H    1 
ATOM   4175 H HA   A GLU   B 1 26  ? 51.109 -24.207 -13.910 0.66 19.49 ?  26  GLU   B HA   1 
ATOM   4176 H HA   B GLU   B 1 26  ? 51.117 -24.205 -13.913 0.34 19.04 ?  26  GLU   B HA   1 
ATOM   4177 H HB2  A GLU   B 1 26  ? 49.771 -24.666 -11.502 0.66 22.16 ?  26  GLU   B HB2  1 
ATOM   4178 H HB2  B GLU   B 1 26  ? 49.804 -24.821 -11.554 0.34 20.60 ?  26  GLU   B HB2  1 
ATOM   4179 H HB3  A GLU   B 1 26  ? 48.982 -23.896 -12.642 0.66 22.16 ?  26  GLU   B HB3  1 
ATOM   4180 H HB3  B GLU   B 1 26  ? 48.998 -23.885 -12.548 0.34 20.60 ?  26  GLU   B HB3  1 
ATOM   4181 H HG2  A GLU   B 1 26  ? 50.018 -26.481 -12.926 0.66 25.92 ?  26  GLU   B HG2  1 
ATOM   4182 H HG2  B GLU   B 1 26  ? 49.935 -26.439 -13.244 0.34 22.74 ?  26  GLU   B HG2  1 
ATOM   4183 H HG3  A GLU   B 1 26  ? 48.484 -26.159 -12.663 0.66 25.92 ?  26  GLU   B HG3  1 
ATOM   4184 H HG3  B GLU   B 1 26  ? 48.431 -26.132 -12.832 0.34 22.74 ?  26  GLU   B HG3  1 
ATOM   4185 N N    . ALA   B 1 27  ? 51.122 -21.887 -11.699 1.00 13.74 ?  27  ALA   B N    1 
ATOM   4186 C CA   . ALA   B 1 27  ? 51.087 -20.438 -11.553 1.00 14.28 ?  27  ALA   B CA   1 
ATOM   4187 C C    . ALA   B 1 27  ? 52.160 -19.777 -12.411 1.00 15.63 ?  27  ALA   B C    1 
ATOM   4188 O O    . ALA   B 1 27  ? 51.898 -18.773 -13.086 1.00 16.36 ?  27  ALA   B O    1 
ATOM   4189 C CB   . ALA   B 1 27  ? 51.236 -20.048 -10.081 1.00 14.22 ?  27  ALA   B CB   1 
ATOM   4190 H H    A ALA   B 1 27  ? 51.248 -22.322 -10.969 0.66 16.46 ?  27  ALA   B H    1 
ATOM   4191 H H    B ALA   B 1 27  ? 51.258 -22.321 -10.970 0.34 16.46 ?  27  ALA   B H    1 
ATOM   4192 H HA   . ALA   B 1 27  ? 50.230 -20.112 -11.858 1.00 17.10 ?  27  ALA   B HA   1 
ATOM   4193 H HB1  . ALA   B 1 27  ? 51.202 -19.083 -10.005 1.00 17.03 ?  27  ALA   B HB1  1 
ATOM   4194 H HB2  . ALA   B 1 27  ? 50.501 -20.443 -9.580  1.00 17.03 ?  27  ALA   B HB2  1 
ATOM   4195 H HB3  . ALA   B 1 27  ? 52.080 -20.382 -9.747  1.00 17.03 ?  27  ALA   B HB3  1 
ATOM   4196 N N    . LYS   B 1 28  ? 53.373 -20.337 -12.421 1.00 17.43 ?  28  LYS   B N    1 
ATOM   4197 C CA   . LYS   B 1 28  ? 54.439 -19.714 -13.198 1.00 19.37 ?  28  LYS   B CA   1 
ATOM   4198 C C    . LYS   B 1 28  ? 54.181 -19.807 -14.696 1.00 19.47 ?  28  LYS   B C    1 
ATOM   4199 O O    . LYS   B 1 28  ? 54.603 -18.919 -15.450 1.00 20.93 ?  28  LYS   B O    1 
ATOM   4200 C CB   . LYS   B 1 28  ? 55.801 -20.299 -12.812 1.00 22.42 ?  28  LYS   B CB   1 
ATOM   4201 C CG   . LYS   B 1 28  ? 56.212 -19.935 -11.391 1.00 25.73 ?  28  LYS   B CG   1 
ATOM   4202 C CD   . LYS   B 1 28  ? 57.639 -20.345 -11.052 1.00 30.26 ?  28  LYS   B CD   1 
ATOM   4203 C CE   . LYS   B 1 28  ? 57.724 -21.806 -10.686 1.00 33.53 ?  28  LYS   B CE   1 
ATOM   4204 N NZ   . LYS   B 1 28  ? 59.076 -22.165 -10.162 1.00 35.69 ?  28  LYS   B NZ   1 
ATOM   4205 H H    . LYS   B 1 28  ? 53.597 -21.052 -12.002 1.00 20.89 ?  28  LYS   B H    1 
ATOM   4206 H HA   . LYS   B 1 28  ? 54.466 -18.773 -12.980 1.00 23.22 ?  28  LYS   B HA   1 
ATOM   4207 H HB2  . LYS   B 1 28  ? 55.766 -21.264 -12.876 1.00 26.87 ?  28  LYS   B HB2  1 
ATOM   4208 H HB3  . LYS   B 1 28  ? 56.479 -19.951 -13.417 1.00 26.87 ?  28  LYS   B HB3  1 
ATOM   4209 H HG2  . LYS   B 1 28  ? 56.140 -18.972 -11.285 1.00 30.85 ?  28  LYS   B HG2  1 
ATOM   4210 H HG3  . LYS   B 1 28  ? 55.615 -20.380 -10.773 1.00 30.85 ?  28  LYS   B HG3  1 
ATOM   4211 H HD2  . LYS   B 1 28  ? 58.206 -20.186 -11.824 1.00 36.28 ?  28  LYS   B HD2  1 
ATOM   4212 H HD3  . LYS   B 1 28  ? 57.945 -19.818 -10.297 1.00 36.28 ?  28  LYS   B HD3  1 
ATOM   4213 H HE2  . LYS   B 1 28  ? 57.069 -22.000 -9.997  1.00 40.21 ?  28  LYS   B HE2  1 
ATOM   4214 H HE3  . LYS   B 1 28  ? 57.550 -22.343 -11.474 1.00 40.21 ?  28  LYS   B HE3  1 
ATOM   4215 H HZ1  . LYS   B 1 28  ? 59.101 -23.030 -9.953  1.00 42.79 ?  28  LYS   B HZ1  1 
ATOM   4216 H HZ2  . LYS   B 1 28  ? 59.695 -21.998 -10.779 1.00 42.79 ?  28  LYS   B HZ2  1 
ATOM   4217 H HZ3  . LYS   B 1 28  ? 59.257 -21.686 -9.434  1.00 42.79 ?  28  LYS   B HZ3  1 
ATOM   4218 N N    . LYS   B 1 29  ? 53.472 -20.843 -15.146 1.00 20.74 ?  29  LYS   B N    1 
ATOM   4219 C CA   . LYS   B 1 29  ? 53.168 -20.994 -16.565 1.00 23.79 ?  29  LYS   B CA   1 
ATOM   4220 C C    . LYS   B 1 29  ? 51.917 -20.226 -16.990 1.00 23.08 ?  29  LYS   B C    1 
ATOM   4221 O O    . LYS   B 1 29  ? 51.907 -19.614 -18.064 1.00 24.89 ?  29  LYS   B O    1 
ATOM   4222 C CB   . LYS   B 1 29  ? 53.026 -22.477 -16.922 1.00 28.55 ?  29  LYS   B CB   1 
ATOM   4223 C CG   . LYS   B 1 29  ? 52.874 -22.745 -18.408 1.00 33.11 ?  29  LYS   B CG   1 
ATOM   4224 C CD   . LYS   B 1 29  ? 53.071 -24.223 -18.726 1.00 36.96 ?  29  LYS   B CD   1 
ATOM   4225 C CE   . LYS   B 1 29  ? 51.928 -25.078 -18.198 1.00 39.43 ?  29  LYS   B CE   1 
ATOM   4226 N NZ   . LYS   B 1 29  ? 52.162 -26.529 -18.458 1.00 40.50 ?  29  LYS   B NZ   1 
ATOM   4227 H H    . LYS   B 1 29  ? 53.158 -21.474 -14.647 1.00 24.86 ?  29  LYS   B H    1 
ATOM   4228 H HA   . LYS   B 1 29  ? 53.909 -20.647 -17.075 1.00 28.52 ?  29  LYS   B HA   1 
ATOM   4229 H HB2  . LYS   B 1 29  ? 53.821 -22.948 -16.622 1.00 34.23 ?  29  LYS   B HB2  1 
ATOM   4230 H HB3  . LYS   B 1 29  ? 52.245 -22.836 -16.479 1.00 34.23 ?  29  LYS   B HB3  1 
ATOM   4231 H HG2  . LYS   B 1 29  ? 51.983 -22.488 -18.691 1.00 39.70 ?  29  LYS   B HG2  1 
ATOM   4232 H HG3  . LYS   B 1 29  ? 53.542 -22.236 -18.897 1.00 39.70 ?  29  LYS   B HG3  1 
ATOM   4233 H HD2  . LYS   B 1 29  ? 53.118 -24.338 -19.687 1.00 44.32 ?  29  LYS   B HD2  1 
ATOM   4234 H HD3  . LYS   B 1 29  ? 53.894 -24.530 -18.312 1.00 44.32 ?  29  LYS   B HD3  1 
ATOM   4235 H HE2  . LYS   B 1 29  ? 51.846 -24.952 -17.240 1.00 47.29 ?  29  LYS   B HE2  1 
ATOM   4236 H HE3  . LYS   B 1 29  ? 51.104 -24.819 -18.641 1.00 47.29 ?  29  LYS   B HE3  1 
ATOM   4237 H HZ1  . LYS   B 1 29  ? 51.482 -27.009 -18.142 1.00 48.57 ?  29  LYS   B HZ1  1 
ATOM   4238 H HZ2  . LYS   B 1 29  ? 52.236 -26.674 -19.333 1.00 48.57 ?  29  LYS   B HZ2  1 
ATOM   4239 H HZ3  . LYS   B 1 29  ? 52.912 -26.793 -18.057 1.00 48.57 ?  29  LYS   B HZ3  1 
ATOM   4240 N N    . VAL   B 1 30  ? 50.866 -20.248 -16.164 1.00 21.01 ?  30  VAL   B N    1 
ATOM   4241 C CA   . VAL   B 1 30  ? 49.583 -19.633 -16.517 1.00 21.01 ?  30  VAL   B CA   1 
ATOM   4242 C C    . VAL   B 1 30  ? 49.615 -18.119 -16.361 1.00 19.82 ?  30  VAL   B C    1 
ATOM   4243 O O    . VAL   B 1 30  ? 48.886 -17.397 -17.060 1.00 20.78 ?  30  VAL   B O    1 
ATOM   4244 C CB   . VAL   B 1 30  ? 48.479 -20.236 -15.629 1.00 22.07 ?  30  VAL   B CB   1 
ATOM   4245 C CG1  . VAL   B 1 30  ? 47.196 -19.429 -15.723 1.00 22.81 ?  30  VAL   B CG1  1 
ATOM   4246 C CG2  . VAL   B 1 30  ? 48.241 -21.693 -15.997 1.00 23.14 ?  30  VAL   B CG2  1 
ATOM   4247 H H    . VAL   B 1 30  ? 50.862 -20.645 -15.390 1.00 25.18 ?  30  VAL   B H    1 
ATOM   4248 H HA   . VAL   B 1 30  ? 49.374 -19.851 -17.438 1.00 25.19 ?  30  VAL   B HA   1 
ATOM   4249 H HB   . VAL   B 1 30  ? 48.771 -20.217 -14.706 1.00 26.45 ?  30  VAL   B HB   1 
ATOM   4250 H HG11 . VAL   B 1 30  ? 46.452 -20.006 -15.486 1.00 27.34 ?  30  VAL   B HG11 1 
ATOM   4251 H HG12 . VAL   B 1 30  ? 47.243 -18.685 -15.106 1.00 27.34 ?  30  VAL   B HG12 1 
ATOM   4252 H HG13 . VAL   B 1 30  ? 47.084 -19.115 -16.629 1.00 27.34 ?  30  VAL   B HG13 1 
ATOM   4253 H HG21 . VAL   B 1 30  ? 47.545 -22.058 -15.424 1.00 27.74 ?  30  VAL   B HG21 1 
ATOM   4254 H HG22 . VAL   B 1 30  ? 47.959 -21.745 -16.926 1.00 27.74 ?  30  VAL   B HG22 1 
ATOM   4255 H HG23 . VAL   B 1 30  ? 49.063 -22.191 -15.874 1.00 27.74 ?  30  VAL   B HG23 1 
ATOM   4256 N N    . LYS   B 1 31  ? 50.417 -17.626 -15.426 1.00 19.27 ?  31  LYS   B N    1 
ATOM   4257 C CA   . LYS   B 1 31  ? 50.435 -16.220 -15.047 1.00 19.93 ?  31  LYS   B CA   1 
ATOM   4258 C C    . LYS   B 1 31  ? 49.032 -15.728 -14.678 1.00 17.43 ?  31  LYS   B C    1 
ATOM   4259 O O    . LYS   B 1 31  ? 48.502 -14.810 -15.313 1.00 17.82 ?  31  LYS   B O    1 
ATOM   4260 C CB   . LYS   B 1 31  ? 51.064 -15.366 -16.139 1.00 23.45 ?  31  LYS   B CB   1 
ATOM   4261 C CG   . LYS   B 1 31  ? 52.490 -15.819 -16.464 1.00 27.26 ?  31  LYS   B CG   1 
ATOM   4262 C CD   . LYS   B 1 31  ? 53.071 -15.081 -17.649 1.00 31.17 ?  31  LYS   B CD   1 
ATOM   4263 C CE   . LYS   B 1 31  ? 54.563 -15.314 -17.759 1.00 33.97 ?  31  LYS   B CE   1 
ATOM   4264 N NZ   . LYS   B 1 31  ? 55.268 -14.841 -16.534 1.00 35.42 ?  31  LYS   B NZ   1 
ATOM   4265 H H    . LYS   B 1 31  ? 50.985 -18.109 -14.993 1.00 23.10 ?  31  LYS   B H    1 
ATOM   4266 H HA   . LYS   B 1 31  ? 50.984 -16.135 -14.265 1.00 23.89 ?  31  LYS   B HA   1 
ATOM   4267 H HB2  . LYS   B 1 31  ? 50.535 -15.433 -16.948 1.00 28.11 ?  31  LYS   B HB2  1 
ATOM   4268 H HB3  . LYS   B 1 31  ? 51.102 -14.449 -15.834 1.00 28.11 ?  31  LYS   B HB3  1 
ATOM   4269 H HG2  . LYS   B 1 31  ? 53.055 -15.657 -15.692 1.00 32.69 ?  31  LYS   B HG2  1 
ATOM   4270 H HG3  . LYS   B 1 31  ? 52.487 -16.768 -16.676 1.00 32.69 ?  31  LYS   B HG3  1 
ATOM   4271 H HD2  . LYS   B 1 31  ? 52.647 -15.404 -18.459 1.00 37.38 ?  31  LYS   B HD2  1 
ATOM   4272 H HD3  . LYS   B 1 31  ? 52.913 -14.134 -17.536 1.00 37.38 ?  31  LYS   B HD3  1 
ATOM   4273 H HE2  . LYS   B 1 31  ? 54.736 -16.264 -17.865 1.00 40.74 ?  31  LYS   B HE2  1 
ATOM   4274 H HE3  . LYS   B 1 31  ? 54.907 -14.822 -18.521 1.00 40.74 ?  31  LYS   B HE3  1 
ATOM   4275 H HZ1  . LYS   B 1 31  ? 56.146 -14.821 -16.677 1.00 42.47 ?  31  LYS   B HZ1  1 
ATOM   4276 H HZ2  . LYS   B 1 31  ? 54.991 -14.022 -16.322 1.00 42.47 ?  31  LYS   B HZ2  1 
ATOM   4277 H HZ3  . LYS   B 1 31  ? 55.098 -15.388 -15.853 1.00 42.47 ?  31  LYS   B HZ3  1 
ATOM   4278 N N    . PRO   B 1 32  ? 48.411 -16.318 -13.654 1.00 14.96 ?  32  PRO   B N    1 
ATOM   4279 C CA   . PRO   B 1 32  ? 47.033 -15.956 -13.304 1.00 14.32 ?  32  PRO   B CA   1 
ATOM   4280 C C    . PRO   B 1 32  ? 46.964 -14.614 -12.598 1.00 14.34 ?  32  PRO   B C    1 
ATOM   4281 O O    . PRO   B 1 32  ? 47.896 -14.194 -11.908 1.00 15.46 ?  32  PRO   B O    1 
ATOM   4282 C CB   . PRO   B 1 32  ? 46.629 -17.071 -12.333 1.00 14.72 ?  32  PRO   B CB   1 
ATOM   4283 C CG   . PRO   B 1 32  ? 47.932 -17.426 -11.657 1.00 15.13 ?  32  PRO   B CG   1 
ATOM   4284 C CD   . PRO   B 1 32  ? 48.979 -17.316 -12.726 1.00 15.27 ?  32  PRO   B CD   1 
ATOM   4285 H HA   . PRO   B 1 32  ? 46.453 -15.963 -14.085 1.00 17.16 ?  32  PRO   B HA   1 
ATOM   4286 H HB2  . PRO   B 1 32  ? 45.984 -16.731 -11.691 1.00 17.64 ?  32  PRO   B HB2  1 
ATOM   4287 H HB3  . PRO   B 1 32  ? 46.270 -17.825 -12.823 1.00 17.64 ?  32  PRO   B HB3  1 
ATOM   4288 H HG2  . PRO   B 1 32  ? 48.114 -16.800 -10.938 1.00 18.13 ?  32  PRO   B HG2  1 
ATOM   4289 H HG3  . PRO   B 1 32  ? 47.890 -18.334 -11.316 1.00 18.13 ?  32  PRO   B HG3  1 
ATOM   4290 H HD2  . PRO   B 1 32  ? 49.811 -16.992 -12.354 1.00 18.30 ?  32  PRO   B HD2  1 
ATOM   4291 H HD3  . PRO   B 1 32  ? 49.093 -18.169 -13.173 1.00 18.30 ?  32  PRO   B HD3  1 
ATOM   4292 N N    . THR   B 1 33  ? 45.817 -13.948 -12.759 1.00 14.74 ?  33  THR   B N    1 
ATOM   4293 C CA   . THR   B 1 33  ? 45.547 -12.767 -11.950 1.00 14.59 ?  33  THR   B CA   1 
ATOM   4294 C C    . THR   B 1 33  ? 45.509 -13.122 -10.469 1.00 13.51 ?  33  THR   B C    1 
ATOM   4295 O O    . THR   B 1 33  ? 45.996 -12.352 -9.626  1.00 14.29 ?  33  THR   B O    1 
ATOM   4296 C CB   . THR   B 1 33  ? 44.226 -12.127 -12.382 1.00 15.09 ?  33  THR   B CB   1 
ATOM   4297 O OG1  . THR   B 1 33  ? 44.243 -11.885 -13.790 1.00 15.18 ?  33  THR   B OG1  1 
ATOM   4298 C CG2  . THR   B 1 33  ? 43.988 -10.823 -11.639 1.00 16.06 ?  33  THR   B CG2  1 
ATOM   4299 H H    . THR   B 1 33  ? 45.190 -14.163 -13.310 1.00 17.66 ?  33  THR   B H    1 
ATOM   4300 H HA   . THR   B 1 33  ? 46.254 -12.123 -12.087 1.00 17.48 ?  33  THR   B HA   1 
ATOM   4301 H HB   . THR   B 1 33  ? 43.493 -12.734 -12.178 1.00 18.08 ?  33  THR   B HB   1 
ATOM   4302 H HG1  . THR   B 1 33  ? 43.528 -11.502 -14.025 1.00 18.19 ?  33  THR   B HG1  1 
ATOM   4303 H HG21 . THR   B 1 33  ? 43.230 -10.359 -12.018 1.00 19.24 ?  33  THR   B HG21 1 
ATOM   4304 H HG22 . THR   B 1 33  ? 43.813 -11.002 -10.700 1.00 19.24 ?  33  THR   B HG22 1 
ATOM   4305 H HG23 . THR   B 1 33  ? 44.775 -10.258 -11.709 1.00 19.24 ?  33  THR   B HG23 1 
ATOM   4306 N N    . VAL   B 1 34  ? 44.929 -14.278 -10.128 1.00 13.09 ?  34  VAL   B N    1 
ATOM   4307 C CA   . VAL   B 1 34  ? 44.738 -14.673 -8.738  1.00 12.15 ?  34  VAL   B CA   1 
ATOM   4308 C C    . VAL   B 1 34  ? 45.158 -16.128 -8.573  1.00 11.61 ?  34  VAL   B C    1 
ATOM   4309 O O    . VAL   B 1 34  ? 44.615 -17.013 -9.247  1.00 12.39 ?  34  VAL   B O    1 
ATOM   4310 C CB   . VAL   B 1 34  ? 43.271 -14.521 -8.290  1.00 13.48 ?  34  VAL   B CB   1 
ATOM   4311 C CG1  . VAL   B 1 34  ? 43.097 -14.983 -6.852  1.00 14.06 ?  34  VAL   B CG1  1 
ATOM   4312 C CG2  . VAL   B 1 34  ? 42.781 -13.088 -8.466  1.00 14.08 ?  34  VAL   B CG2  1 
ATOM   4313 H H    . VAL   B 1 34  ? 44.643 -14.860 -10.694 1.00 15.68 ?  34  VAL   B H    1 
ATOM   4314 H HA   . VAL   B 1 34  ? 45.291 -14.127 -8.160  1.00 14.56 ?  34  VAL   B HA   1 
ATOM   4315 H HB   . VAL   B 1 34  ? 42.716 -15.085 -8.851  1.00 16.15 ?  34  VAL   B HB   1 
ATOM   4316 H HG11 . VAL   B 1 34  ? 42.245 -14.659 -6.516  1.00 16.84 ?  34  VAL   B HG11 1 
ATOM   4317 H HG12 . VAL   B 1 34  ? 43.109 -15.954 -6.826  1.00 16.84 ?  34  VAL   B HG12 1 
ATOM   4318 H HG13 . VAL   B 1 34  ? 43.819 -14.626 -6.314  1.00 16.84 ?  34  VAL   B HG13 1 
ATOM   4319 H HG21 . VAL   B 1 34  ? 41.861 -13.027 -8.160  1.00 16.87 ?  34  VAL   B HG21 1 
ATOM   4320 H HG22 . VAL   B 1 34  ? 43.343 -12.493 -7.946  1.00 16.87 ?  34  VAL   B HG22 1 
ATOM   4321 H HG23 . VAL   B 1 34  ? 42.828 -12.848 -9.407  1.00 16.87 ?  34  VAL   B HG23 1 
ATOM   4322 N N    . VAL   B 1 35  ? 46.075 -16.386 -7.645  1.00 10.76 ?  35  VAL   B N    1 
ATOM   4323 C CA   . VAL   B 1 35  ? 46.294 -17.734 -7.131  1.00 10.47 ?  35  VAL   B CA   1 
ATOM   4324 C C    . VAL   B 1 35  ? 45.753 -17.788 -5.710  1.00 10.24 ?  35  VAL   B C    1 
ATOM   4325 O O    . VAL   B 1 35  ? 45.980 -16.876 -4.910  1.00 10.40 ?  35  VAL   B O    1 
ATOM   4326 C CB   . VAL   B 1 35  ? 47.775 -18.173 -7.213  1.00 11.38 ?  35  VAL   B CB   1 
ATOM   4327 C CG1  . VAL   B 1 35  ? 48.673 -17.320 -6.310  1.00 12.90 ?  35  VAL   B CG1  1 
ATOM   4328 C CG2  . VAL   B 1 35  ? 47.903 -19.664 -6.880  1.00 12.34 ?  35  VAL   B CG2  1 
ATOM   4329 H H    . VAL   B 1 35  ? 46.584 -15.787 -7.290  1.00 12.88 ?  35  VAL   B H    1 
ATOM   4330 H HA   . VAL   B 1 35  ? 45.773 -18.355 -7.659  1.00 12.54 ?  35  VAL   B HA   1 
ATOM   4331 H HB   . VAL   B 1 35  ? 48.074 -18.053 -8.130  1.00 13.62 ?  35  VAL   B HB   1 
ATOM   4332 H HG11 . VAL   B 1 35  ? 49.596 -17.554 -6.485  1.00 15.46 ?  35  VAL   B HG11 1 
ATOM   4333 H HG12 . VAL   B 1 35  ? 48.519 -16.387 -6.506  1.00 15.46 ?  35  VAL   B HG12 1 
ATOM   4334 H HG13 . VAL   B 1 35  ? 48.452 -17.510 -5.384  1.00 15.46 ?  35  VAL   B HG13 1 
ATOM   4335 H HG21 . VAL   B 1 35  ? 48.823 -19.937 -6.998  1.00 14.79 ?  35  VAL   B HG21 1 
ATOM   4336 H HG22 . VAL   B 1 35  ? 47.630 -19.808 -5.958  1.00 14.79 ?  35  VAL   B HG22 1 
ATOM   4337 H HG23 . VAL   B 1 35  ? 47.326 -20.176 -7.474  1.00 14.79 ?  35  VAL   B HG23 1 
ATOM   4338 N N    . VAL   B 1 36  ? 45.026 -18.867 -5.394  1.00 10.49 ?  36  VAL   B N    1 
ATOM   4339 C CA   . VAL   B 1 36  ? 44.485 -19.063 -4.057  1.00 10.28 ?  36  VAL   B CA   1 
ATOM   4340 C C    . VAL   B 1 36  ? 45.492 -19.822 -3.202  1.00 9.70  ?  36  VAL   B C    1 
ATOM   4341 O O    . VAL   B 1 36  ? 46.032 -20.856 -3.624  1.00 10.92 ?  36  VAL   B O    1 
ATOM   4342 C CB   . VAL   B 1 36  ? 43.150 -19.827 -4.125  1.00 10.59 ?  36  VAL   B CB   1 
ATOM   4343 C CG1  . VAL   B 1 36  ? 42.645 -20.177 -2.729  1.00 11.41 ?  36  VAL   B CG1  1 
ATOM   4344 C CG2  . VAL   B 1 36  ? 42.122 -19.012 -4.889  1.00 11.47 ?  36  VAL   B CG2  1 
ATOM   4345 H H    . VAL   B 1 36  ? 44.847 -19.507 -5.937  1.00 12.56 ?  36  VAL   B H    1 
ATOM   4346 H HA   . VAL   B 1 36  ? 44.320 -18.203 -3.642  1.00 12.31 ?  36  VAL   B HA   1 
ATOM   4347 H HB   . VAL   B 1 36  ? 43.288 -20.659 -4.604  1.00 12.68 ?  36  VAL   B HB   1 
ATOM   4348 H HG11 . VAL   B 1 36  ? 41.708 -20.414 -2.782  1.00 13.67 ?  36  VAL   B HG11 1 
ATOM   4349 H HG12 . VAL   B 1 36  ? 43.157 -20.922 -2.381  1.00 13.67 ?  36  VAL   B HG12 1 
ATOM   4350 H HG13 . VAL   B 1 36  ? 42.755 -19.400 -2.153  1.00 13.67 ?  36  VAL   B HG13 1 
ATOM   4351 H HG21 . VAL   B 1 36  ? 41.280 -19.498 -4.901  1.00 13.74 ?  36  VAL   B HG21 1 
ATOM   4352 H HG22 . VAL   B 1 36  ? 42.008 -18.157 -4.456  1.00 13.74 ?  36  VAL   B HG22 1 
ATOM   4353 H HG23 . VAL   B 1 36  ? 42.437 -18.886 -5.801  1.00 13.74 ?  36  VAL   B HG23 1 
ATOM   4354 N N    . ASN   B 1 37  ? 45.710 -19.335 -1.985  1.00 9.66  ?  37  ASN   B N    1 
ATOM   4355 C CA   . ASN   B 1 37  ? 46.465 -20.050 -0.971  1.00 10.26 ?  37  ASN   B CA   1 
ATOM   4356 C C    . ASN   B 1 37  ? 45.515 -20.722 0.016   1.00 11.08 ?  37  ASN   B C    1 
ATOM   4357 O O    . ASN   B 1 37  ? 44.508 -20.139 0.432   1.00 11.19 ?  37  ASN   B O    1 
ATOM   4358 C CB   . ASN   B 1 37  ? 47.396 -19.100 -0.215  1.00 9.78  ?  37  ASN   B CB   1 
ATOM   4359 C CG   . ASN   B 1 37  ? 48.252 -19.819 0.796   1.00 10.83 ?  37  ASN   B CG   1 
ATOM   4360 O OD1  . ASN   B 1 37  ? 48.587 -20.999 0.619   1.00 11.91 ?  37  ASN   B OD1  1 
ATOM   4361 N ND2  . ASN   B 1 37  ? 48.603 -19.126 1.874   1.00 10.64 ?  37  ASN   B ND2  1 
ATOM   4362 H H    . ASN   B 1 37  ? 45.417 -18.567 -1.713  1.00 11.56 ?  37  ASN   B H    1 
ATOM   4363 H HA   . ASN   B 1 37  ? 47.006 -20.733 -1.386  1.00 12.28 ?  37  ASN   B HA   1 
ATOM   4364 H HB2  . ASN   B 1 37  ? 47.993 -18.668 -0.845  1.00 11.70 ?  37  ASN   B HB2  1 
ATOM   4365 H HB3  . ASN   B 1 37  ? 46.874 -18.436 0.260   1.00 11.70 ?  37  ASN   B HB3  1 
ATOM   4366 H HD21 . ASN   B 1 37  ? 49.097 -19.486 2.483   1.00 12.74 ?  37  ASN   B HD21 1 
ATOM   4367 H HD22 . ASN   B 1 37  ? 48.358 -18.309 1.963   1.00 12.74 ?  37  ASN   B HD22 1 
ATOM   4368 N N    . ALA   B 1 38  ? 45.863 -21.955 0.393   1.00 10.97 ?  38  ALA   B N    1 
ATOM   4369 C CA   . ALA   B 1 38  ? 45.213 -22.689 1.479   1.00 11.21 ?  38  ALA   B CA   1 
ATOM   4370 C C    . ALA   B 1 38  ? 45.809 -22.196 2.798   1.00 11.18 ?  38  ALA   B C    1 
ATOM   4371 O O    . ALA   B 1 38  ? 46.709 -22.807 3.387   1.00 12.32 ?  38  ALA   B O    1 
ATOM   4372 C CB   . ALA   B 1 38  ? 45.431 -24.189 1.304   1.00 12.78 ?  38  ALA   B CB   1 
ATOM   4373 H H    . ALA   B 1 38  ? 46.507 -22.400 0.032   1.00 13.14 ?  38  ALA   B H    1 
ATOM   4374 H HA   . ALA   B 1 38  ? 44.262 -22.506 1.480   1.00 13.42 ?  38  ALA   B HA   1 
ATOM   4375 H HB1  . ALA   B 1 38  ? 44.989 -24.661 2.036   1.00 15.31 ?  38  ALA   B HB1  1 
ATOM   4376 H HB2  . ALA   B 1 38  ? 45.043 -24.466 0.460   1.00 15.31 ?  38  ALA   B HB2  1 
ATOM   4377 H HB3  . ALA   B 1 38  ? 46.378 -24.379 1.318   1.00 15.31 ?  38  ALA   B HB3  1 
ATOM   4378 N N    . ALA   B 1 39  ? 45.288 -21.060 3.264   1.00 11.08 ?  39  ALA   B N    1 
ATOM   4379 C CA   . ALA   B 1 39  ? 45.844 -20.323 4.387   1.00 11.53 ?  39  ALA   B CA   1 
ATOM   4380 C C    . ALA   B 1 39  ? 45.227 -20.762 5.713   1.00 11.42 ?  39  ALA   B C    1 
ATOM   4381 O O    . ALA   B 1 39  ? 44.190 -21.430 5.764   1.00 12.55 ?  39  ALA   B O    1 
ATOM   4382 C CB   . ALA   B 1 39  ? 45.592 -18.825 4.192   1.00 11.62 ?  39  ALA   B CB   1 
ATOM   4383 H H    . ALA   B 1 39  ? 44.584 -20.695 2.937   1.00 13.27 ?  39  ALA   B H    1 
ATOM   4384 H HA   . ALA   B 1 39  ? 46.800 -20.466 4.433   1.00 13.80 ?  39  ALA   B HA   1 
ATOM   4385 H HB1  . ALA   B 1 39  ? 45.962 -18.334 4.944   1.00 13.91 ?  39  ALA   B HB1  1 
ATOM   4386 H HB2  . ALA   B 1 39  ? 46.013 -18.535 3.368   1.00 13.91 ?  39  ALA   B HB2  1 
ATOM   4387 H HB3  . ALA   B 1 39  ? 44.632 -18.666 4.141   1.00 13.91 ?  39  ALA   B HB3  1 
ATOM   4388 N N    . ASN   B 1 40  ? 45.873 -20.347 6.799   1.00 11.83 ?  40  ASN   B N    1 
ATOM   4389 C CA   . ASN   B 1 40  ? 45.316 -20.390 8.140   1.00 12.48 ?  40  ASN   B CA   1 
ATOM   4390 C C    . ASN   B 1 40  ? 45.137 -18.961 8.659   1.00 12.03 ?  40  ASN   B C    1 
ATOM   4391 O O    . ASN   B 1 40  ? 45.548 -17.989 8.019   1.00 12.32 ?  40  ASN   B O    1 
ATOM   4392 C CB   . ASN   B 1 40  ? 46.172 -21.257 9.079   1.00 13.66 ?  40  ASN   B CB   1 
ATOM   4393 C CG   . ASN   B 1 40  ? 47.625 -20.839 9.106   1.00 15.15 ?  40  ASN   B CG   1 
ATOM   4394 O OD1  . ASN   B 1 40  ? 47.939 -19.654 9.194   1.00 17.27 ?  40  ASN   B OD1  1 
ATOM   4395 N ND2  . ASN   B 1 40  ? 48.523 -21.809 9.034   1.00 15.25 ?  40  ASN   B ND2  1 
ATOM   4396 H H    . ASN   B 1 40  ? 46.667 -20.009 6.778   1.00 14.16 ?  40  ASN   B H    1 
ATOM   4397 H HA   . ASN   B 1 40  ? 44.434 -20.792 8.096   1.00 14.94 ?  40  ASN   B HA   1 
ATOM   4398 H HB2  . ASN   B 1 40  ? 45.815 -21.188 9.980   1.00 16.36 ?  40  ASN   B HB2  1 
ATOM   4399 H HB3  . ASN   B 1 40  ? 46.128 -22.178 8.778   1.00 16.36 ?  40  ASN   B HB3  1 
ATOM   4400 H HD21 . ASN   B 1 40  ? 49.361 -21.622 9.048   1.00 18.27 ?  40  ASN   B HD21 1 
ATOM   4401 H HD22 . ASN   B 1 40  ? 48.265 -22.627 8.968   1.00 18.27 ?  40  ASN   B HD22 1 
ATOM   4402 N N    . VAL   B 1 41  ? 44.488 -18.831 9.817   1.00 12.79 ?  41  VAL   B N    1 
ATOM   4403 C CA   . VAL   B 1 41  ? 44.026 -17.512 10.266  1.00 13.92 ?  41  VAL   B CA   1 
ATOM   4404 C C    . VAL   B 1 41  ? 45.176 -16.550 10.545  1.00 13.61 ?  41  VAL   B C    1 
ATOM   4405 O O    . VAL   B 1 41  ? 44.992 -15.330 10.454  1.00 13.97 ?  41  VAL   B O    1 
ATOM   4406 C CB   . VAL   B 1 41  ? 43.066 -17.598 11.471  1.00 15.43 ?  41  VAL   B CB   1 
ATOM   4407 C CG1  . VAL   B 1 41  ? 41.760 -18.298 11.090  1.00 15.75 ?  41  VAL   B CG1  1 
ATOM   4408 C CG2  . VAL   B 1 41  ? 43.739 -18.258 12.664  1.00 16.34 ?  41  VAL   B CG2  1 
ATOM   4409 H H    . VAL   B 1 41  ? 44.292 -19.475 10.348  1.00 15.32 ?  41  VAL   B H    1 
ATOM   4410 H HA   . VAL   B 1 41  ? 43.510 -17.119 9.544   1.00 16.68 ?  41  VAL   B HA   1 
ATOM   4411 H HB   . VAL   B 1 41  ? 42.829 -16.697 11.743  1.00 18.49 ?  41  VAL   B HB   1 
ATOM   4412 H HG11 . VAL   B 1 41  ? 41.168 -18.319 11.865  1.00 18.87 ?  41  VAL   B HG11 1 
ATOM   4413 H HG12 . VAL   B 1 41  ? 41.333 -17.809 10.369  1.00 18.87 ?  41  VAL   B HG12 1 
ATOM   4414 H HG13 . VAL   B 1 41  ? 41.954 -19.205 10.806  1.00 18.87 ?  41  VAL   B HG13 1 
ATOM   4415 H HG21 . VAL   B 1 41  ? 43.106 -18.316 13.396  1.00 19.58 ?  41  VAL   B HG21 1 
ATOM   4416 H HG22 . VAL   B 1 41  ? 44.033 -19.147 12.410  1.00 19.58 ?  41  VAL   B HG22 1 
ATOM   4417 H HG23 . VAL   B 1 41  ? 44.503 -17.721 12.930  1.00 19.58 ?  41  VAL   B HG23 1 
ATOM   4418 N N    . TYR   B 1 42  ? 46.354 -17.059 10.912  1.00 14.07 ?  42  TYR   B N    1 
ATOM   4419 C CA   . TYR   B 1 42  ? 47.509 -16.205 11.174  1.00 14.13 ?  42  TYR   B CA   1 
ATOM   4420 C C    . TYR   B 1 42  ? 48.471 -16.138 9.992   1.00 12.88 ?  42  TYR   B C    1 
ATOM   4421 O O    . TYR   B 1 42  ? 49.566 -15.573 10.123  1.00 14.56 ?  42  TYR   B O    1 
ATOM   4422 C CB   . TYR   B 1 42  ? 48.211 -16.610 12.477  1.00 15.92 ?  42  TYR   B CB   1 
ATOM   4423 C CG   . TYR   B 1 42  ? 47.603 -15.934 13.700  1.00 16.40 ?  42  TYR   B CG   1 
ATOM   4424 C CD1  . TYR   B 1 42  ? 47.801 -14.575 13.930  1.00 15.71 ?  42  TYR   B CD1  1 
ATOM   4425 C CD2  . TYR   B 1 42  ? 46.825 -16.640 14.608  1.00 18.10 ?  42  TYR   B CD2  1 
ATOM   4426 C CE1  . TYR   B 1 42  ? 47.249 -13.943 15.025  1.00 16.42 ?  42  TYR   B CE1  1 
ATOM   4427 C CE2  . TYR   B 1 42  ? 46.268 -16.015 15.714  1.00 18.38 ?  42  TYR   B CE2  1 
ATOM   4428 C CZ   . TYR   B 1 42  ? 46.484 -14.661 15.919  1.00 18.34 ?  42  TYR   B CZ   1 
ATOM   4429 O OH   . TYR   B 1 42  ? 45.942 -14.014 17.013  1.00 21.66 ?  42  TYR   B OH   1 
ATOM   4430 H H    . TYR   B 1 42  ? 46.504 -17.903 11.011  1.00 16.85 ?  42  TYR   B H    1 
ATOM   4431 H HA   . TYR   B 1 42  ? 47.177 -15.308 11.306  1.00 16.92 ?  42  TYR   B HA   1 
ATOM   4432 H HB2  . TYR   B 1 42  ? 48.135 -17.570 12.595  1.00 19.08 ?  42  TYR   B HB2  1 
ATOM   4433 H HB3  . TYR   B 1 42  ? 49.144 -16.353 12.422  1.00 19.08 ?  42  TYR   B HB3  1 
ATOM   4434 H HD1  . TYR   B 1 42  ? 48.316 -14.084 13.326  1.00 18.83 ?  42  TYR   B HD1  1 
ATOM   4435 H HD2  . TYR   B 1 42  ? 46.676 -17.551 14.467  1.00 21.69 ?  42  TYR   B HD2  1 
ATOM   4436 H HE1  . TYR   B 1 42  ? 47.395 -13.038 15.159  1.00 19.67 ?  42  TYR   B HE1  1 
ATOM   4437 H HE2  . TYR   B 1 42  ? 45.749 -16.504 16.311  1.00 22.02 ?  42  TYR   B HE2  1 
ATOM   4438 H HH   . TYR   B 1 42  ? 46.158 -13.208 16.996  1.00 25.97 ?  42  TYR   B HH   1 
ATOM   4439 N N    . LEU   B 1 43  ? 48.067 -16.656 8.835   1.00 12.41 ?  43  LEU   B N    1 
ATOM   4440 C CA   . LEU   B 1 43  ? 48.880 -16.595 7.622   1.00 12.01 ?  43  LEU   B CA   1 
ATOM   4441 C C    . LEU   B 1 43  ? 50.296 -17.104 7.878   1.00 12.28 ?  43  LEU   B C    1 
ATOM   4442 O O    . LEU   B 1 43  ? 51.277 -16.515 7.426   1.00 13.52 ?  43  LEU   B O    1 
ATOM   4443 C CB   . LEU   B 1 43  ? 48.897 -15.189 7.009   1.00 12.64 ?  43  LEU   B CB   1 
ATOM   4444 C CG   . LEU   B 1 43  ? 47.540 -14.576 6.640   1.00 12.70 ?  43  LEU   B CG   1 
ATOM   4445 C CD1  . LEU   B 1 43  ? 47.727 -13.171 6.065   1.00 14.16 ?  43  LEU   B CD1  1 
ATOM   4446 C CD2  . LEU   B 1 43  ? 46.752 -15.466 5.675   1.00 12.75 ?  43  LEU   B CD2  1 
ATOM   4447 H H    . LEU   B 1 43  ? 47.319 -17.074 8.724   1.00 14.87 ?  43  LEU   B H    1 
ATOM   4448 H HA   . LEU   B 1 43  ? 48.481 -17.189 6.964   1.00 14.39 ?  43  LEU   B HA   1 
ATOM   4449 H HB2  . LEU   B 1 43  ? 49.323 -14.591 7.638   1.00 15.13 ?  43  LEU   B HB2  1 
ATOM   4450 H HB3  . LEU   B 1 43  ? 49.425 -15.228 6.194   1.00 15.13 ?  43  LEU   B HB3  1 
ATOM   4451 H HG   . LEU   B 1 43  ? 47.016 -14.496 7.448   1.00 15.22 ?  43  LEU   B HG   1 
ATOM   4452 H HD11 . LEU   B 1 43  ? 46.853 -12.806 5.842   1.00 16.97 ?  43  LEU   B HD11 1 
ATOM   4453 H HD12 . LEU   B 1 43  ? 48.155 -12.613 6.733   1.00 16.97 ?  43  LEU   B HD12 1 
ATOM   4454 H HD13 . LEU   B 1 43  ? 48.276 -13.221 5.270   1.00 16.97 ?  43  LEU   B HD13 1 
ATOM   4455 H HD21 . LEU   B 1 43  ? 45.940 -15.002 5.412   1.00 15.27 ?  43  LEU   B HD21 1 
ATOM   4456 H HD22 . LEU   B 1 43  ? 47.295 -15.650 4.894   1.00 15.27 ?  43  LEU   B HD22 1 
ATOM   4457 H HD23 . LEU   B 1 43  ? 46.524 -16.297 6.123   1.00 15.27 ?  43  LEU   B HD23 1 
ATOM   4458 N N    . LYS   B 1 44  ? 50.397 -18.223 8.599   1.00 12.58 ?  44  LYS   B N    1 
ATOM   4459 C CA   . LYS   B 1 44  ? 51.668 -18.904 8.846   1.00 13.44 ?  44  LYS   B CA   1 
ATOM   4460 C C    . LYS   B 1 44  ? 51.781 -20.022 7.819   1.00 12.66 ?  44  LYS   B C    1 
ATOM   4461 O O    . LYS   B 1 44  ? 51.084 -21.036 7.906   1.00 14.44 ?  44  LYS   B O    1 
ATOM   4462 C CB   . LYS   B 1 44  ? 51.718 -19.419 10.281  1.00 15.38 ?  44  LYS   B CB   1 
ATOM   4463 C CG   . LYS   B 1 44  ? 51.908 -18.309 11.311  1.00 18.58 ?  44  LYS   B CG   1 
ATOM   4464 C CD   . LYS   B 1 44  ? 53.106 -17.446 10.909  1.00 21.86 ?  44  LYS   B CD   1 
ATOM   4465 C CE   . LYS   B 1 44  ? 53.637 -16.588 12.029  1.00 24.72 ?  44  LYS   B CE   1 
ATOM   4466 N NZ   . LYS   B 1 44  ? 54.797 -15.755 11.615  1.00 25.42 ?  44  LYS   B NZ   1 
ATOM   4467 H H    . LYS   B 1 44  ? 49.728 -18.608 8.977   1.00 15.07 ?  44  LYS   B H    1 
ATOM   4468 H HA   . LYS   B 1 44  ? 52.401 -18.290 8.685   1.00 16.09 ?  44  LYS   B HA   1 
ATOM   4469 H HB2  . LYS   B 1 44  ? 50.878 -19.872 10.481  1.00 18.42 ?  44  LYS   B HB2  1 
ATOM   4470 H HB3  . LYS   B 1 44  ? 52.454 -20.042 10.368  1.00 18.42 ?  44  LYS   B HB3  1 
ATOM   4471 H HG2  . LYS   B 1 44  ? 51.116 -17.756 11.344  1.00 22.26 ?  44  LYS   B HG2  1 
ATOM   4472 H HG3  . LYS   B 1 44  ? 52.089 -18.706 12.182  1.00 22.26 ?  44  LYS   B HG3  1 
ATOM   4473 H HD2  . LYS   B 1 44  ? 53.818 -18.033 10.593  1.00 26.20 ?  44  LYS   B HD2  1 
ATOM   4474 H HD3  . LYS   B 1 44  ? 52.828 -16.855 10.190  1.00 26.20 ?  44  LYS   B HD3  1 
ATOM   4475 H HE2  . LYS   B 1 44  ? 52.936 -15.988 12.302  1.00 29.64 ?  44  LYS   B HE2  1 
ATOM   4476 H HE3  . LYS   B 1 44  ? 53.912 -17.160 12.762  1.00 29.64 ?  44  LYS   B HE3  1 
ATOM   4477 H HZ1  . LYS   B 1 44  ? 55.075 -15.264 12.302  1.00 30.47 ?  44  LYS   B HZ1  1 
ATOM   4478 H HZ2  . LYS   B 1 44  ? 55.465 -16.271 11.336  1.00 30.47 ?  44  LYS   B HZ2  1 
ATOM   4479 H HZ3  . LYS   B 1 44  ? 54.557 -15.209 10.950  1.00 30.47 ?  44  LYS   B HZ3  1 
ATOM   4480 N N    . HIS   B 1 45  ? 52.625 -19.808 6.815   1.00 12.61 ?  45  HIS   B N    1 
ATOM   4481 C CA   . HIS   B 1 45  ? 52.639 -20.646 5.616   1.00 12.70 ?  45  HIS   B CA   1 
ATOM   4482 C C    . HIS   B 1 45  ? 53.668 -21.764 5.770   1.00 14.54 ?  45  HIS   B C    1 
ATOM   4483 O O    . HIS   B 1 45  ? 54.739 -21.762 5.168   1.00 17.03 ?  45  HIS   B O    1 
ATOM   4484 C CB   . HIS   B 1 45  ? 52.938 -19.797 4.392   1.00 12.64 ?  45  HIS   B CB   1 
ATOM   4485 C CG   . HIS   B 1 45  ? 52.071 -18.590 4.287   1.00 12.45 ?  45  HIS   B CG   1 
ATOM   4486 N ND1  . HIS   B 1 45  ? 50.693 -18.663 4.257   1.00 12.88 ?  45  HIS   B ND1  1 
ATOM   4487 C CD2  . HIS   B 1 45  ? 52.389 -17.277 4.207   1.00 13.42 ?  45  HIS   B CD2  1 
ATOM   4488 C CE1  . HIS   B 1 45  ? 50.206 -17.439 4.158   1.00 12.52 ?  45  HIS   B CE1  1 
ATOM   4489 N NE2  . HIS   B 1 45  ? 51.211 -16.581 4.129   1.00 13.06 ?  45  HIS   B NE2  1 
ATOM   4490 H H    . HIS   B 1 45  ? 53.200 -19.165 6.796   1.00 15.11 ?  45  HIS   B H    1 
ATOM   4491 H HA   . HIS   B 1 45  ? 51.758 -21.046 5.499   1.00 15.21 ?  45  HIS   B HA   1 
ATOM   4492 H HB2  . HIS   B 1 45  ? 53.857 -19.504 4.429   1.00 15.14 ?  45  HIS   B HB2  1 
ATOM   4493 H HB3  . HIS   B 1 45  ? 52.795 -20.339 3.594   1.00 15.14 ?  45  HIS   B HB3  1 
ATOM   4494 H HD2  . HIS   B 1 45  ? 53.245 -16.913 4.211   1.00 16.07 ?  45  HIS   B HD2  1 
ATOM   4495 H HE1  . HIS   B 1 45  ? 49.303 -17.222 4.115   1.00 14.99 ?  45  HIS   B HE1  1 
ATOM   4496 H HE2  . HIS   B 1 45  ? 51.134 -15.727 4.075   1.00 15.65 ?  45  HIS   B HE2  1 
ATOM   4497 N N    A GLY   B 1 46  ? 53.306 -22.745 6.589   0.66 15.72 ?  46  GLY   B N    1 
ATOM   4498 N N    B GLY   B 1 46  ? 53.315 -22.733 6.604   0.34 15.78 ?  46  GLY   B N    1 
ATOM   4499 C CA   A GLY   B 1 46  ? 54.236 -23.796 6.961   0.66 18.03 ?  46  GLY   B CA   1 
ATOM   4500 C CA   B GLY   B 1 46  ? 54.242 -23.794 6.936   0.34 17.48 ?  46  GLY   B CA   1 
ATOM   4501 C C    A GLY   B 1 46  ? 54.264 -25.031 6.079   0.66 20.15 ?  46  GLY   B C    1 
ATOM   4502 C C    B GLY   B 1 46  ? 54.249 -24.960 5.968   0.34 19.08 ?  46  GLY   B C    1 
ATOM   4503 O O    A GLY   B 1 46  ? 55.336 -25.474 5.659   0.66 22.45 ?  46  GLY   B O    1 
ATOM   4504 O O    B GLY   B 1 46  ? 55.279 -25.263 5.358   0.34 19.91 ?  46  GLY   B O    1 
ATOM   4505 H H    A GLY   B 1 46  ? 52.529 -22.809 6.956   0.66 18.84 ?  46  GLY   B H    1 
ATOM   4506 H H    B GLY   B 1 46  ? 52.548 -22.790 6.993   0.34 18.91 ?  46  GLY   B H    1 
ATOM   4507 H HA2  A GLY   B 1 46  ? 55.131 -23.422 6.978   0.66 21.61 ?  46  GLY   B HA2  1 
ATOM   4508 H HA2  B GLY   B 1 46  ? 55.139 -23.425 6.968   0.34 20.95 ?  46  GLY   B HA2  1 
ATOM   4509 H HA3  A GLY   B 1 46  ? 54.021 -24.090 7.859   0.66 21.61 ?  46  GLY   B HA3  1 
ATOM   4510 H HA3  B GLY   B 1 46  ? 54.026 -24.132 7.818   0.34 20.95 ?  46  GLY   B HA3  1 
ATOM   4511 N N    . GLY   B 1 47  ? 53.106 -25.624 5.808   1.00 19.50 ?  47  GLY   B N    1 
ATOM   4512 C CA   . GLY   B 1 47  ? 53.039 -26.892 5.110   1.00 16.80 ?  47  GLY   B CA   1 
ATOM   4513 C C    . GLY   B 1 47  ? 52.117 -26.859 3.907   1.00 14.80 ?  47  GLY   B C    1 
ATOM   4514 O O    . GLY   B 1 47  ? 51.466 -25.854 3.623   1.00 15.26 ?  47  GLY   B O    1 
ATOM   4515 H H    A GLY   B 1 47  ? 52.337 -25.311 6.038   0.66 23.37 ?  47  GLY   B H    1 
ATOM   4516 H H    B GLY   B 1 47  ? 52.344 -25.349 6.103   0.34 23.37 ?  47  GLY   B H    1 
ATOM   4517 H HA2  . GLY   B 1 47  ? 53.921 -27.146 4.802   1.00 20.13 ?  47  GLY   B HA2  1 
ATOM   4518 H HA3  . GLY   B 1 47  ? 52.720 -27.574 5.719   1.00 20.13 ?  47  GLY   B HA3  1 
ATOM   4519 N N    . GLY   B 1 48  ? 52.048 -28.001 3.224   1.00 14.16 ?  48  GLY   B N    1 
ATOM   4520 C CA   . GLY   B 1 48  ? 51.110 -28.143 2.124   1.00 13.69 ?  48  GLY   B CA   1 
ATOM   4521 C C    . GLY   B 1 48  ? 51.265 -27.045 1.095   1.00 12.76 ?  48  GLY   B C    1 
ATOM   4522 O O    . GLY   B 1 48  ? 52.376 -26.589 0.790   1.00 13.32 ?  48  GLY   B O    1 
ATOM   4523 H H    . GLY   B 1 48  ? 52.530 -28.692 3.374   1.00 16.96 ?  48  GLY   B H    1 
ATOM   4524 H HA2  . GLY   B 1 48  ? 51.248 -29.002 1.689   1.00 16.40 ?  48  GLY   B HA2  1 
ATOM   4525 H HA3  . GLY   B 1 48  ? 50.200 -28.119 2.464   1.00 16.40 ?  48  GLY   B HA3  1 
ATOM   4526 N N    . VAL   B 1 49  ? 50.128 -26.608 0.552   1.00 12.93 ?  49  VAL   B N    1 
ATOM   4527 C CA   . VAL   B 1 49  ? 50.122 -25.583 -0.489  1.00 12.56 ?  49  VAL   B CA   1 
ATOM   4528 C C    . VAL   B 1 49  ? 50.784 -24.298 0.004   1.00 11.49 ?  49  VAL   B C    1 
ATOM   4529 O O    . VAL   B 1 49  ? 51.582 -23.682 -0.711  1.00 12.60 ?  49  VAL   B O    1 
ATOM   4530 C CB   . VAL   B 1 49  ? 48.683 -25.330 -0.980  1.00 13.80 ?  49  VAL   B CB   1 
ATOM   4531 C CG1  . VAL   B 1 49  ? 48.609 -24.068 -1.836  1.00 14.11 ?  49  VAL   B CG1  1 
ATOM   4532 C CG2  . VAL   B 1 49  ? 48.170 -26.533 -1.754  1.00 15.71 ?  49  VAL   B CG2  1 
ATOM   4533 H H    . VAL   B 1 49  ? 49.342 -26.898 0.764   1.00 15.49 ?  49  VAL   B H    1 
ATOM   4534 H HA   . VAL   B 1 49  ? 50.631 -25.911 -1.247  1.00 15.04 ?  49  VAL   B HA   1 
ATOM   4535 H HB   . VAL   B 1 49  ? 48.104 -25.205 -0.213  1.00 16.53 ?  49  VAL   B HB   1 
ATOM   4536 H HG11 . VAL   B 1 49  ? 47.783 -24.076 -2.343  1.00 16.91 ?  49  VAL   B HG11 1 
ATOM   4537 H HG12 . VAL   B 1 49  ? 48.630 -23.289 -1.255  1.00 16.91 ?  49  VAL   B HG12 1 
ATOM   4538 H HG13 . VAL   B 1 49  ? 49.368 -24.050 -2.440  1.00 16.91 ?  49  VAL   B HG13 1 
ATOM   4539 H HG21 . VAL   B 1 49  ? 47.263 -26.355 -2.053  1.00 18.82 ?  49  VAL   B HG21 1 
ATOM   4540 H HG22 . VAL   B 1 49  ? 48.745 -26.685 -2.522  1.00 18.82 ?  49  VAL   B HG22 1 
ATOM   4541 H HG23 . VAL   B 1 49  ? 48.180 -27.311 -1.175  1.00 18.82 ?  49  VAL   B HG23 1 
ATOM   4542 N N    . ALA   B 1 50  ? 50.453 -23.866 1.222   1.00 11.58 ?  50  ALA   B N    1 
ATOM   4543 C CA   . ALA   B 1 50  ? 50.968 -22.584 1.698   1.00 11.42 ?  50  ALA   B CA   1 
ATOM   4544 C C    . ALA   B 1 50  ? 52.487 -22.612 1.804   1.00 11.78 ?  50  ALA   B C    1 
ATOM   4545 O O    . ALA   B 1 50  ? 53.164 -21.646 1.433   1.00 11.81 ?  50  ALA   B O    1 
ATOM   4546 C CB   . ALA   B 1 50  ? 50.344 -22.241 3.045   1.00 11.83 ?  50  ALA   B CB   1 
ATOM   4547 H H    . ALA   B 1 50  ? 49.941 -24.283 1.773   1.00 13.87 ?  50  ALA   B H    1 
ATOM   4548 H HA   . ALA   B 1 50  ? 50.728 -21.894 1.068   1.00 13.67 ?  50  ALA   B HA   1 
ATOM   4549 H HB1  . ALA   B 1 50  ? 50.695 -21.387 3.346   1.00 14.17 ?  50  ALA   B HB1  1 
ATOM   4550 H HB2  . ALA   B 1 50  ? 49.380 -22.180 2.939   1.00 14.17 ?  50  ALA   B HB2  1 
ATOM   4551 H HB3  . ALA   B 1 50  ? 50.562 -22.933 3.685   1.00 14.17 ?  50  ALA   B HB3  1 
ATOM   4552 N N    . GLY   B 1 51  ? 53.039 -23.706 2.313   1.00 12.14 ?  51  GLY   B N    1 
ATOM   4553 C CA   . GLY   B 1 51  ? 54.486 -23.804 2.381   1.00 13.11 ?  51  GLY   B CA   1 
ATOM   4554 C C    . GLY   B 1 51  ? 55.130 -23.764 1.010   1.00 12.99 ?  51  GLY   B C    1 
ATOM   4555 O O    . GLY   B 1 51  ? 56.175 -23.132 0.822   1.00 13.78 ?  51  GLY   B O    1 
ATOM   4556 H H    . GLY   B 1 51  ? 52.618 -24.394 2.610   1.00 14.54 ?  51  GLY   B H    1 
ATOM   4557 H HA2  . GLY   B 1 51  ? 54.841 -23.067 2.900   1.00 15.71 ?  51  GLY   B HA2  1 
ATOM   4558 H HA3  . GLY   B 1 51  ? 54.743 -24.636 2.810   1.00 15.71 ?  51  GLY   B HA3  1 
ATOM   4559 N N    . ALA   B 1 52  ? 54.518 -24.434 0.031   1.00 12.20 ?  52  ALA   B N    1 
ATOM   4560 C CA   . ALA   B 1 52  ? 55.076 -24.454 -1.315  1.00 12.77 ?  52  ALA   B CA   1 
ATOM   4561 C C    . ALA   B 1 52  ? 55.000 -23.078 -1.968  1.00 12.07 ?  52  ALA   B C    1 
ATOM   4562 O O    . ALA   B 1 52  ? 55.971 -22.626 -2.594  1.00 13.31 ?  52  ALA   B O    1 
ATOM   4563 C CB   . ALA   B 1 52  ? 54.352 -25.489 -2.169  1.00 13.40 ?  52  ALA   B CB   1 
ATOM   4564 H H    . ALA   B 1 52  ? 53.783 -24.877 0.122   1.00 14.62 ?  52  ALA   B H    1 
ATOM   4565 H HA   . ALA   B 1 52  ? 56.009 -24.706 -1.263  1.00 15.30 ?  52  ALA   B HA   1 
ATOM   4566 H HB1  . ALA   B 1 52  ? 54.737 -25.486 -3.059  1.00 16.05 ?  52  ALA   B HB1  1 
ATOM   4567 H HB2  . ALA   B 1 52  ? 54.460 -26.362 -1.763  1.00 16.05 ?  52  ALA   B HB2  1 
ATOM   4568 H HB3  . ALA   B 1 52  ? 53.411 -25.258 -2.215  1.00 16.05 ?  52  ALA   B HB3  1 
ATOM   4569 N N    . LEU   B 1 53  ? 53.858 -22.395 -1.840  1.00 11.70 ?  53  LEU   B N    1 
ATOM   4570 C CA   . LEU   B 1 53  ? 53.749 -21.055 -2.417  1.00 11.40 ?  53  LEU   B CA   1 
ATOM   4571 C C    . LEU   B 1 53  ? 54.754 -20.107 -1.776  1.00 11.88 ?  53  LEU   B C    1 
ATOM   4572 O O    . LEU   B 1 53  ? 55.458 -19.356 -2.472  1.00 12.83 ?  53  LEU   B O    1 
ATOM   4573 C CB   . LEU   B 1 53  ? 52.326 -20.508 -2.249  1.00 12.43 ?  53  LEU   B CB   1 
ATOM   4574 C CG   . LEU   B 1 53  ? 51.192 -21.240 -2.966  1.00 12.33 ?  53  LEU   B CG   1 
ATOM   4575 C CD1  . LEU   B 1 53  ? 49.864 -20.606 -2.630  1.00 14.29 ?  53  LEU   B CD1  1 
ATOM   4576 C CD2  . LEU   B 1 53  ? 51.388 -21.285 -4.476  1.00 14.70 ?  53  LEU   B CD2  1 
ATOM   4577 H H    . LEU   B 1 53  ? 53.154 -22.670 -1.431  1.00 14.01 ?  53  LEU   B H    1 
ATOM   4578 H HA   . LEU   B 1 53  ? 53.952 -21.106 -3.367  1.00 13.65 ?  53  LEU   B HA   1 
ATOM   4579 H HB2  . LEU   B 1 53  ? 52.119 -20.517 -1.306  1.00 14.88 ?  53  LEU   B HB2  1 
ATOM   4580 H HB3  . LEU   B 1 53  ? 52.324 -19.596 -2.573  1.00 14.88 ?  53  LEU   B HB3  1 
ATOM   4581 H HG   . LEU   B 1 53  ? 51.162 -22.153 -2.646  1.00 14.77 ?  53  LEU   B HG   1 
ATOM   4582 H HD11 . LEU   B 1 53  ? 49.156 -21.087 -3.092  1.00 17.12 ?  53  LEU   B HD11 1 
ATOM   4583 H HD12 . LEU   B 1 53  ? 49.720 -20.660 -1.670  1.00 17.12 ?  53  LEU   B HD12 1 
ATOM   4584 H HD13 . LEU   B 1 53  ? 49.870 -19.679 -2.911  1.00 17.12 ?  53  LEU   B HD13 1 
ATOM   4585 H HD21 . LEU   B 1 53  ? 50.659 -21.787 -4.877  1.00 17.61 ?  53  LEU   B HD21 1 
ATOM   4586 H HD22 . LEU   B 1 53  ? 51.399 -20.383 -4.826  1.00 17.61 ?  53  LEU   B HD22 1 
ATOM   4587 H HD23 . LEU   B 1 53  ? 52.232 -21.727 -4.672  1.00 17.61 ?  53  LEU   B HD23 1 
ATOM   4588 N N    . ASN   B 1 54  ? 54.852 -20.132 -0.447  1.00 11.60 ?  54  ASN   B N    1 
ATOM   4589 C CA   . ASN   B 1 54  ? 55.767 -19.215 0.220   1.00 11.93 ?  54  ASN   B CA   1 
ATOM   4590 C C    . ASN   B 1 54  ? 57.215 -19.500 -0.166  1.00 12.74 ?  54  ASN   B C    1 
ATOM   4591 O O    . ASN   B 1 54  ? 57.998 -18.564 -0.390  1.00 13.48 ?  54  ASN   B O    1 
ATOM   4592 C CB   . ASN   B 1 54  ? 55.602 -19.275 1.731   1.00 13.02 ?  54  ASN   B CB   1 
ATOM   4593 C CG   . ASN   B 1 54  ? 56.590 -18.372 2.438   1.00 13.49 ?  54  ASN   B CG   1 
ATOM   4594 O OD1  . ASN   B 1 54  ? 56.614 -17.159 2.200   1.00 14.15 ?  54  ASN   B OD1  1 
ATOM   4595 N ND2  . ASN   B 1 54  ? 57.433 -18.952 3.294   1.00 14.69 ?  54  ASN   B ND2  1 
ATOM   4596 H H    . ASN   B 1 54  ? 54.414 -20.658 0.076   1.00 13.89 ?  54  ASN   B H    1 
ATOM   4597 H HA   . ASN   B 1 54  ? 55.559 -18.312 -0.062  1.00 14.29 ?  54  ASN   B HA   1 
ATOM   4598 H HB2  . ASN   B 1 54  ? 54.708 -18.984 1.971   1.00 15.59 ?  54  ASN   B HB2  1 
ATOM   4599 H HB3  . ASN   B 1 54  ? 55.752 -20.183 2.038   1.00 15.59 ?  54  ASN   B HB3  1 
ATOM   4600 H HD21 . ASN   B 1 54  ? 58.021 -18.479 3.712   1.00 17.60 ?  54  ASN   B HD21 1 
ATOM   4601 H HD22 . ASN   B 1 54  ? 57.399 -19.802 3.428   1.00 17.60 ?  54  ASN   B HD22 1 
ATOM   4602 N N    . LYS   B 1 55  ? 57.594 -20.783 -0.227  1.00 13.48 ?  55  LYS   B N    1 
ATOM   4603 C CA   . LYS   B 1 55  ? 58.950 -21.129 -0.648  1.00 14.61 ?  55  LYS   B CA   1 
ATOM   4604 C C    . LYS   B 1 55  ? 59.237 -20.592 -2.043  1.00 14.15 ?  55  LYS   B C    1 
ATOM   4605 O O    . LYS   B 1 55  ? 60.331 -20.075 -2.304  1.00 15.02 ?  55  LYS   B O    1 
ATOM   4606 C CB   . LYS   B 1 55  ? 59.145 -22.646 -0.593  1.00 16.83 ?  55  LYS   B CB   1 
ATOM   4607 C CG   . LYS   B 1 55  ? 60.530 -23.109 -1.024  1.00 21.16 ?  55  LYS   B CG   1 
ATOM   4608 C CD   . LYS   B 1 55  ? 60.714 -24.605 -0.816  1.00 24.96 ?  55  LYS   B CD   1 
ATOM   4609 C CE   . LYS   B 1 55  ? 60.719 -24.978 0.666   1.00 28.02 ?  55  LYS   B CE   1 
ATOM   4610 N NZ   . LYS   B 1 55  ? 61.078 -26.402 0.883   1.00 29.90 ?  55  LYS   B NZ   1 
ATOM   4611 H H    . LYS   B 1 55  ? 57.088 -21.451 -0.040  1.00 16.15 ?  55  LYS   B H    1 
ATOM   4612 H HA   . LYS   B 1 55  ? 59.578 -20.721 -0.036  1.00 17.51 ?  55  LYS   B HA   1 
ATOM   4613 H HB2  . LYS   B 1 55  ? 58.996 -22.934 0.322   1.00 20.17 ?  55  LYS   B HB2  1 
ATOM   4614 H HB3  . LYS   B 1 55  ? 58.493 -23.063 -1.177  1.00 20.17 ?  55  LYS   B HB3  1 
ATOM   4615 H HG2  . LYS   B 1 55  ? 60.650 -22.914 -1.967  1.00 25.36 ?  55  LYS   B HG2  1 
ATOM   4616 H HG3  . LYS   B 1 55  ? 61.198 -22.640 -0.498  1.00 25.36 ?  55  LYS   B HG3  1 
ATOM   4617 H HD2  . LYS   B 1 55  ? 59.984 -25.079 -1.245  1.00 29.93 ?  55  LYS   B HD2  1 
ATOM   4618 H HD3  . LYS   B 1 55  ? 61.562 -24.879 -1.198  1.00 29.93 ?  55  LYS   B HD3  1 
ATOM   4619 H HE2  . LYS   B 1 55  ? 61.366 -24.420 1.129   1.00 33.60 ?  55  LYS   B HE2  1 
ATOM   4620 H HE3  . LYS   B 1 55  ? 59.831 -24.828 1.034   1.00 33.60 ?  55  LYS   B HE3  1 
ATOM   4621 H HZ1  . LYS   B 1 55  ? 61.062 -26.588 1.753   1.00 35.86 ?  55  LYS   B HZ1  1 
ATOM   4622 H HZ2  . LYS   B 1 55  ? 60.495 -26.927 0.463   1.00 35.86 ?  55  LYS   B HZ2  1 
ATOM   4623 H HZ3  . LYS   B 1 55  ? 61.892 -26.560 0.566   1.00 35.86 ?  55  LYS   B HZ3  1 
ATOM   4624 N N    . ALA   B 1 56  ? 58.262 -20.681 -2.950  1.00 13.79 ?  56  ALA   B N    1 
ATOM   4625 C CA   . ALA   B 1 56  ? 58.477 -20.184 -4.304  1.00 14.49 ?  56  ALA   B CA   1 
ATOM   4626 C C    . ALA   B 1 56  ? 58.768 -18.689 -4.313  1.00 14.42 ?  56  ALA   B C    1 
ATOM   4627 O O    . ALA   B 1 56  ? 59.500 -18.204 -5.189  1.00 15.14 ?  56  ALA   B O    1 
ATOM   4628 C CB   . ALA   B 1 56  ? 57.262 -20.497 -5.177  1.00 15.53 ?  56  ALA   B CB   1 
ATOM   4629 H H    . ALA   B 1 56  ? 57.473 -20.994 -2.802  1.00 16.52 ?  56  ALA   B H    1 
ATOM   4630 H HA   . ALA   B 1 56  ? 59.241 -20.634 -4.684  1.00 17.36 ?  56  ALA   B HA   1 
ATOM   4631 H HB1  . ALA   B 1 56  ? 57.424 -20.167 -6.076  1.00 18.60 ?  56  ALA   B HB1  1 
ATOM   4632 H HB2  . ALA   B 1 56  ? 57.131 -21.459 -5.199  1.00 18.60 ?  56  ALA   B HB2  1 
ATOM   4633 H HB3  . ALA   B 1 56  ? 56.478 -20.065 -4.803  1.00 18.60 ?  56  ALA   B HB3  1 
ATOM   4634 N N    . THR   B 1 57  ? 58.202 -17.941 -3.364  1.00 14.53 ?  57  THR   B N    1 
ATOM   4635 C CA   . THR   B 1 57  ? 58.450 -16.508 -3.255  1.00 14.27 ?  57  THR   B CA   1 
ATOM   4636 C C    . THR   B 1 57  ? 59.697 -16.181 -2.445  1.00 14.70 ?  57  THR   B C    1 
ATOM   4637 O O    . THR   B 1 57  ? 59.931 -15.006 -2.138  1.00 15.40 ?  57  THR   B O    1 
ATOM   4638 C CB   . THR   B 1 57  ? 57.245 -15.775 -2.633  1.00 13.17 ?  57  THR   B CB   1 
ATOM   4639 O OG1  . THR   B 1 57  ? 57.215 -15.974 -1.214  1.00 13.84 ?  57  THR   B OG1  1 
ATOM   4640 C CG2  . THR   B 1 57  ? 55.928 -16.206 -3.277  1.00 13.58 ?  57  THR   B CG2  1 
ATOM   4641 H H    . THR   B 1 57  ? 57.648 -18.243 -2.776  1.00 17.40 ?  57  THR   B H    1 
ATOM   4642 H HA   . THR   B 1 57  ? 58.572 -16.151 -4.150  1.00 17.10 ?  57  THR   B HA   1 
ATOM   4643 H HB   . THR   B 1 57  ? 57.347 -14.824 -2.810  1.00 15.77 ?  57  THR   B HB   1 
ATOM   4644 H HG1  . THR   B 1 57  ? 57.148 -16.791 -1.044  1.00 16.58 ?  57  THR   B HG1  1 
ATOM   4645 H HG21 . THR   B 1 57  ? 55.204 -15.644 -2.968  1.00 16.27 ?  57  THR   B HG21 1 
ATOM   4646 H HG22 . THR   B 1 57  ? 55.991 -16.139 -4.244  1.00 16.27 ?  57  THR   B HG22 1 
ATOM   4647 H HG23 . THR   B 1 57  ? 55.732 -17.128 -3.044  1.00 16.27 ?  57  THR   B HG23 1 
ATOM   4648 N N    . ASN   B 1 58  ? 60.494 -17.184 -2.090  1.00 15.61 ?  58  ASN   B N    1 
ATOM   4649 C CA   . ASN   B 1 58  ? 61.692 -16.965 -1.286  1.00 18.52 ?  58  ASN   B CA   1 
ATOM   4650 C C    . ASN   B 1 58  ? 61.364 -16.248 0.023   1.00 16.23 ?  58  ASN   B C    1 
ATOM   4651 O O    . ASN   B 1 58  ? 62.102 -15.369 0.475   1.00 16.86 ?  58  ASN   B O    1 
ATOM   4652 C CB   . ASN   B 1 58  ? 62.770 -16.213 -2.072  1.00 26.73 ?  58  ASN   B CB   1 
ATOM   4653 C CG   . ASN   B 1 58  ? 64.153 -16.382 -1.471  1.00 36.65 ?  58  ASN   B CG   1 
ATOM   4654 O OD1  . ASN   B 1 58  ? 64.455 -17.407 -0.862  1.00 39.14 ?  58  ASN   B OD1  1 
ATOM   4655 N ND2  . ASN   B 1 58  ? 65.000 -15.374 -1.640  1.00 44.11 ?  58  ASN   B ND2  1 
ATOM   4656 H H    . ASN   B 1 58  ? 60.361 -18.012 -2.300  1.00 18.70 ?  58  ASN   B H    1 
ATOM   4657 H HA   . ASN   B 1 58  ? 62.063 -17.836 -1.064  1.00 22.20 ?  58  ASN   B HA   1 
ATOM   4658 H HB2  . ASN   B 1 58  ? 62.799 -16.550 -2.984  1.00 32.05 ?  58  ASN   B HB2  1 
ATOM   4659 H HB3  . ASN   B 1 58  ? 62.563 -15.267 -2.074  1.00 32.05 ?  58  ASN   B HB3  1 
ATOM   4660 H HD21 . ASN   B 1 58  ? 65.796 -15.423 -1.318  1.00 52.91 ?  58  ASN   B HD21 1 
ATOM   4661 H HD22 . ASN   B 1 58  ? 64.752 -14.673 -2.071  1.00 52.91 ?  58  ASN   B HD22 1 
ATOM   4662 N N    . ASN   B 1 59  ? 60.243 -16.629 0.635   1.00 15.26 ?  59  ASN   B N    1 
ATOM   4663 C CA   . ASN   B 1 59  ? 59.770 -16.161 1.940   1.00 15.09 ?  59  ASN   B CA   1 
ATOM   4664 C C    . ASN   B 1 59  ? 59.175 -14.756 1.889   1.00 14.56 ?  59  ASN   B C    1 
ATOM   4665 O O    . ASN   B 1 59  ? 58.751 -14.248 2.937   1.00 14.89 ?  59  ASN   B O    1 
ATOM   4666 C CB   . ASN   B 1 59  ? 60.840 -16.219 3.043   1.00 16.28 ?  59  ASN   B CB   1 
ATOM   4667 C CG   . ASN   B 1 59  ? 60.247 -16.379 4.425   1.00 17.26 ?  59  ASN   B CG   1 
ATOM   4668 O OD1  . ASN   B 1 59  ? 59.425 -17.266 4.664   1.00 17.38 ?  59  ASN   B OD1  1 
ATOM   4669 N ND2  . ASN   B 1 59  ? 60.665 -15.524 5.348   1.00 18.05 ?  59  ASN   B ND2  1 
ATOM   4670 H H    . ASN   B 1 59  ? 59.697 -17.206 0.288   1.00 18.29 ?  59  ASN   B H    1 
ATOM   4671 H HA   . ASN   B 1 59  ? 59.060 -16.758 2.223   1.00 18.08 ?  59  ASN   B HA   1 
ATOM   4672 H HB2  . ASN   B 1 59  ? 61.428 -16.974 2.887   1.00 19.50 ?  59  ASN   B HB2  1 
ATOM   4673 H HB3  . ASN   B 1 59  ? 61.351 -15.394 3.038   1.00 19.50 ?  59  ASN   B HB3  1 
ATOM   4674 H HD21 . ASN   B 1 59  ? 60.354 -15.572 6.150   1.00 21.63 ?  59  ASN   B HD21 1 
ATOM   4675 H HD22 . ASN   B 1 59  ? 61.235 -14.914 5.146   1.00 21.63 ?  59  ASN   B HD22 1 
ATOM   4676 N N    . ALA   B 1 60  ? 59.105 -14.117 0.719   1.00 14.51 ?  60  ALA   B N    1 
ATOM   4677 C CA   . ALA   B 1 60  ? 58.509 -12.784 0.650   1.00 14.47 ?  60  ALA   B CA   1 
ATOM   4678 C C    . ALA   B 1 60  ? 57.041 -12.807 1.052   1.00 13.56 ?  60  ALA   B C    1 
ATOM   4679 O O    . ALA   B 1 60  ? 56.545 -11.853 1.664   1.00 14.00 ?  60  ALA   B O    1 
ATOM   4680 C CB   . ALA   B 1 60  ? 58.669 -12.201 -0.752  1.00 15.22 ?  60  ALA   B CB   1 
ATOM   4681 H H    . ALA   B 1 60  ? 59.399 -14.429 -0.028  1.00 17.38 ?  60  ALA   B H    1 
ATOM   4682 H HA   . ALA   B 1 60  ? 58.977 -12.206 1.269   1.00 17.34 ?  60  ALA   B HA   1 
ATOM   4683 H HB1  . ALA   B 1 60  ? 58.268 -11.320 -0.769  1.00 18.24 ?  60  ALA   B HB1  1 
ATOM   4684 H HB2  . ALA   B 1 60  ? 59.615 -12.139 -0.963  1.00 18.24 ?  60  ALA   B HB2  1 
ATOM   4685 H HB3  . ALA   B 1 60  ? 58.227 -12.783 -1.388  1.00 18.24 ?  60  ALA   B HB3  1 
ATOM   4686 N N    . MET   B 1 61  ? 56.327 -13.881 0.700   1.00 12.69 ?  61  MET   B N    1 
ATOM   4687 C CA   . MET   B 1 61  ? 54.929 -13.996 1.090   1.00 12.35 ?  61  MET   B CA   1 
ATOM   4688 C C    . MET   B 1 61  ? 54.786 -13.991 2.611   1.00 12.31 ?  61  MET   B C    1 
ATOM   4689 O O    . MET   B 1 61  ? 53.883 -13.338 3.155   1.00 12.50 ?  61  MET   B O    1 
ATOM   4690 C CB   . MET   B 1 61  ? 54.350 -15.272 0.474   1.00 12.26 ?  61  MET   B CB   1 
ATOM   4691 C CG   . MET   B 1 61  ? 52.893 -15.548 0.865   1.00 11.97 ?  61  MET   B CG   1 
ATOM   4692 S SD   . MET   B 1 61  ? 52.260 -17.056 0.119   1.00 12.71 ?  61  MET   B SD   1 
ATOM   4693 C CE   . MET   B 1 61  ? 52.012 -16.510 -1.565  1.00 13.98 ?  61  MET   B CE   1 
ATOM   4694 H H    . MET   B 1 61  ? 56.630 -14.555 0.242   1.00 15.19 ?  61  MET   B H    1 
ATOM   4695 H HA   . MET   B 1 61  ? 54.440 -13.246 0.721   1.00 14.79 ?  61  MET   B HA   1 
ATOM   4696 H HB2  . MET   B 1 61  ? 54.384 -15.198 -0.496  1.00 14.68 ?  61  MET   B HB2  1 
ATOM   4697 H HB3  . MET   B 1 61  ? 54.882 -16.031 0.760   1.00 14.68 ?  61  MET   B HB3  1 
ATOM   4698 H HG2  . MET   B 1 61  ? 52.835 -15.646 1.828   1.00 14.33 ?  61  MET   B HG2  1 
ATOM   4699 H HG3  . MET   B 1 61  ? 52.341 -14.806 0.571   1.00 14.33 ?  61  MET   B HG3  1 
ATOM   4700 H HE1  . MET   B 1 61  ? 51.646 -17.241 -2.087  1.00 16.75 ?  61  MET   B HE1  1 
ATOM   4701 H HE2  . MET   B 1 61  ? 51.396 -15.759 -1.571  1.00 16.75 ?  61  MET   B HE2  1 
ATOM   4702 H HE3  . MET   B 1 61  ? 52.867 -16.235 -1.938  1.00 16.75 ?  61  MET   B HE3  1 
ATOM   4703 N N    . GLN   B 1 62  ? 55.664 -14.708 3.319   1.00 12.29 ?  62  GLN   B N    1 
ATOM   4704 C CA   . GLN   B 1 62  ? 55.577 -14.750 4.774   1.00 12.86 ?  62  GLN   B CA   1 
ATOM   4705 C C    . GLN   B 1 62  ? 55.861 -13.388 5.395   1.00 13.47 ?  62  GLN   B C    1 
ATOM   4706 O O    . GLN   B 1 62  ? 55.176 -12.978 6.339   1.00 14.03 ?  62  GLN   B O    1 
ATOM   4707 C CB   . GLN   B 1 62  ? 56.545 -15.790 5.338   1.00 13.35 ?  62  GLN   B CB   1 
ATOM   4708 C CG   . GLN   B 1 62  ? 56.319 -16.079 6.814   1.00 13.94 ?  62  GLN   B CG   1 
ATOM   4709 C CD   . GLN   B 1 62  ? 54.937 -16.666 7.058   1.00 13.36 ?  62  GLN   B CD   1 
ATOM   4710 O OE1  . GLN   B 1 62  ? 54.665 -17.814 6.699   1.00 13.66 ?  62  GLN   B OE1  1 
ATOM   4711 N NE2  . GLN   B 1 62  ? 54.037 -15.865 7.620   1.00 14.23 ?  62  GLN   B NE2  1 
ATOM   4712 H H    . GLN   B 1 62  ? 56.307 -15.170 2.981   1.00 14.72 ?  62  GLN   B H    1 
ATOM   4713 H HA   . GLN   B 1 62  ? 54.677 -15.010 5.022   1.00 15.41 ?  62  GLN   B HA   1 
ATOM   4714 H HB2  . GLN   B 1 62  ? 56.436 -16.623 4.851   1.00 15.99 ?  62  GLN   B HB2  1 
ATOM   4715 H HB3  . GLN   B 1 62  ? 57.454 -15.466 5.233   1.00 15.99 ?  62  GLN   B HB3  1 
ATOM   4716 H HG2  . GLN   B 1 62  ? 56.983 -16.721 7.114   1.00 16.70 ?  62  GLN   B HG2  1 
ATOM   4717 H HG3  . GLN   B 1 62  ? 56.395 -15.256 7.315   1.00 16.70 ?  62  GLN   B HG3  1 
ATOM   4718 H HE21 . GLN   B 1 62  ? 54.257 -15.066 7.845   1.00 17.05 ?  62  GLN   B HE21 1 
ATOM   4719 H HE22 . GLN   B 1 62  ? 53.242 -16.154 7.768   1.00 17.05 ?  62  GLN   B HE22 1 
ATOM   4720 N N    . VAL   B 1 63  ? 56.881 -12.683 4.902   1.00 13.96 ?  63  VAL   B N    1 
ATOM   4721 C CA   . VAL   B 1 63  ? 57.188 -11.359 5.443   1.00 15.18 ?  63  VAL   B CA   1 
ATOM   4722 C C    . VAL   B 1 63  ? 55.993 -10.426 5.262   1.00 14.17 ?  63  VAL   B C    1 
ATOM   4723 O O    . VAL   B 1 63  ? 55.579 -9.719  6.192   1.00 14.43 ?  63  VAL   B O    1 
ATOM   4724 C CB   . VAL   B 1 63  ? 58.478 -10.805 4.810   1.00 16.26 ?  63  VAL   B CB   1 
ATOM   4725 C CG1  . VAL   B 1 63  ? 58.703 -9.361  5.245   1.00 17.19 ?  63  VAL   B CG1  1 
ATOM   4726 C CG2  . VAL   B 1 63  ? 59.672 -11.671 5.199   1.00 17.04 ?  63  VAL   B CG2  1 
ATOM   4727 H H    . VAL   B 1 63  ? 57.403 -12.947 4.266   1.00 16.72 ?  63  VAL   B H    1 
ATOM   4728 H HA   . VAL   B 1 63  ? 57.353 -11.448 6.392   1.00 18.19 ?  63  VAL   B HA   1 
ATOM   4729 H HB   . VAL   B 1 63  ? 58.401 -10.825 3.842   1.00 19.48 ?  63  VAL   B HB   1 
ATOM   4730 H HG11 . VAL   B 1 63  ? 59.621 -9.113  5.051   1.00 20.60 ?  63  VAL   B HG11 1 
ATOM   4731 H HG12 . VAL   B 1 63  ? 58.095 -8.786  4.758   1.00 20.60 ?  63  VAL   B HG12 1 
ATOM   4732 H HG13 . VAL   B 1 63  ? 58.538 -9.293  6.198   1.00 20.60 ?  63  VAL   B HG13 1 
ATOM   4733 H HG21 . VAL   B 1 63  ? 60.477 -11.295 4.805   1.00 20.42 ?  63  VAL   B HG21 1 
ATOM   4734 H HG22 . VAL   B 1 63  ? 59.753 -11.677 6.167   1.00 20.42 ?  63  VAL   B HG22 1 
ATOM   4735 H HG23 . VAL   B 1 63  ? 59.533 -12.571 4.872   1.00 20.42 ?  63  VAL   B HG23 1 
ATOM   4736 N N    . GLU   B 1 64  ? 55.416 -10.421 4.058   1.00 13.74 ?  64  GLU   B N    1 
ATOM   4737 C CA   . GLU   B 1 64  ? 54.249 -9.588  3.777   1.00 13.13 ?  64  GLU   B CA   1 
ATOM   4738 C C    . GLU   B 1 64  ? 53.067 -9.983  4.657   1.00 12.69 ?  64  GLU   B C    1 
ATOM   4739 O O    . GLU   B 1 64  ? 52.317 -9.124  5.153   1.00 13.06 ?  64  GLU   B O    1 
ATOM   4740 C CB   . GLU   B 1 64  ? 53.887 -9.756  2.302   1.00 13.16 ?  64  GLU   B CB   1 
ATOM   4741 C CG   . GLU   B 1 64  ? 52.626 -9.004  1.857   1.00 13.31 ?  64  GLU   B CG   1 
ATOM   4742 C CD   . GLU   B 1 64  ? 52.097 -9.494  0.522   1.00 14.40 ?  64  GLU   B CD   1 
ATOM   4743 O OE1  . GLU   B 1 64  ? 52.275 -10.704 0.220   1.00 15.38 ?  64  GLU   B OE1  1 
ATOM   4744 O OE2  . GLU   B 1 64  ? 51.488 -8.677  -0.214  1.00 15.05 -1 64  GLU   B OE2  1 
ATOM   4745 H H    . GLU   B 1 64  ? 55.693 -10.889 3.383   1.00 16.46 ?  64  GLU   B H    1 
ATOM   4746 H HA   . GLU   B 1 64  ? 54.468 -8.659  3.941   1.00 15.73 ?  64  GLU   B HA   1 
ATOM   4747 H HB2  . GLU   B 1 64  ? 54.623 -9.425  1.759   1.00 15.76 ?  64  GLU   B HB2  1 
ATOM   4748 H HB3  . GLU   B 1 64  ? 53.748 -10.696 2.121   1.00 15.76 ?  64  GLU   B HB3  1 
ATOM   4749 H HG2  . GLU   B 1 64  ? 51.923 -9.130  2.518   1.00 15.94 ?  64  GLU   B HG2  1 
ATOM   4750 H HG3  . GLU   B 1 64  ? 52.833 -8.063  1.772   1.00 15.94 ?  64  GLU   B HG3  1 
ATOM   4751 N N    . SER   B 1 65  ? 52.889 -11.288 4.858   1.00 12.21 ?  65  SER   B N    1 
ATOM   4752 C CA   . SER   B 1 65  ? 51.777 -11.789 5.656   1.00 12.46 ?  65  SER   B CA   1 
ATOM   4753 C C    . SER   B 1 65  ? 51.905 -11.391 7.119   1.00 12.71 ?  65  SER   B C    1 
ATOM   4754 O O    . SER   B 1 65  ? 50.905 -11.016 7.749   1.00 13.30 ?  65  SER   B O    1 
ATOM   4755 C CB   . SER   B 1 65  ? 51.679 -13.310 5.523   1.00 12.62 ?  65  SER   B CB   1 
ATOM   4756 O OG   . SER   B 1 65  ? 51.332 -13.704 4.205   1.00 13.14 ?  65  SER   B OG   1 
ATOM   4757 H H    . SER   B 1 65  ? 53.400 -11.912 4.546   1.00 14.63 ?  65  SER   B H    1 
ATOM   4758 H HA   . SER   B 1 65  ? 50.951 -11.407 5.318   1.00 14.93 ?  65  SER   B HA   1 
ATOM   4759 H HB2  . SER   B 1 65  ? 52.534 -13.702 5.746   1.00 15.11 ?  65  SER   B HB2  1 
ATOM   4760 H HB3  . SER   B 1 65  ? 50.998 -13.633 6.138   1.00 15.11 ?  65  SER   B HB3  1 
ATOM   4761 H HG   . SER   B 1 65  ? 51.902 -13.418 3.658   1.00 15.74 ?  65  SER   B HG   1 
ATOM   4762 N N    . ASP   B 1 66  ? 53.113 -11.489 7.693   1.00 13.19 ?  66  ASP   B N    1 
ATOM   4763 C CA   . ASP   B 1 66  ? 53.294 -11.092 9.088   1.00 13.48 ?  66  ASP   B CA   1 
ATOM   4764 C C    . ASP   B 1 66  ? 52.983 -9.612  9.281   1.00 13.71 ?  66  ASP   B C    1 
ATOM   4765 O O    . ASP   B 1 66  ? 52.418 -9.211  10.307  1.00 14.33 ?  66  ASP   B O    1 
ATOM   4766 C CB   . ASP   B 1 66  ? 54.723 -11.395 9.551   1.00 15.21 ?  66  ASP   B CB   1 
ATOM   4767 C CG   . ASP   B 1 66  ? 55.000 -12.892 9.698   1.00 16.56 ?  66  ASP   B CG   1 
ATOM   4768 O OD1  . ASP   B 1 66  ? 54.046 -13.701 9.650   1.00 17.14 ?  66  ASP   B OD1  1 
ATOM   4769 O OD2  . ASP   B 1 66  ? 56.184 -13.261 9.872   1.00 19.69 -1 66  ASP   B OD2  1 
ATOM   4770 H H    . ASP   B 1 66  ? 53.821 -11.787 7.309   1.00 15.80 ?  66  ASP   B H    1 
ATOM   4771 H HA   . ASP   B 1 66  ? 52.689 -11.597 9.654   1.00 16.15 ?  66  ASP   B HA   1 
ATOM   4772 H HB2  . ASP   B 1 66  ? 55.350 -11.036 8.904   1.00 18.22 ?  66  ASP   B HB2  1 
ATOM   4773 H HB3  . ASP   B 1 66  ? 54.874 -10.977 10.419  1.00 18.22 ?  66  ASP   B HB3  1 
ATOM   4774 N N    . ASP   B 1 67  ? 53.353 -8.781  8.310   1.00 13.49 ?  67  ASP   B N    1 
ATOM   4775 C CA   . ASP   B 1 67  ? 53.013 -7.367  8.386   1.00 14.12 ?  67  ASP   B CA   1 
ATOM   4776 C C    . ASP   B 1 67  ? 51.504 -7.157  8.298   1.00 14.16 ?  67  ASP   B C    1 
ATOM   4777 O O    . ASP   B 1 67  ? 50.941 -6.347  9.044   1.00 14.61 ?  67  ASP   B O    1 
ATOM   4778 C CB   . ASP   B 1 67  ? 53.732 -6.607  7.278   1.00 15.26 ?  67  ASP   B CB   1 
ATOM   4779 C CG   . ASP   B 1 67  ? 53.304 -5.165  7.217   1.00 16.75 ?  67  ASP   B CG   1 
ATOM   4780 O OD1  . ASP   B 1 67  ? 53.796 -4.342  8.030   1.00 18.29 ?  67  ASP   B OD1  1 
ATOM   4781 O OD2  . ASP   B 1 67  ? 52.439 -4.868  6.377   1.00 18.27 -1 67  ASP   B OD2  1 
ATOM   4782 H H    . ASP   B 1 67  ? 53.804 -9.007  7.616   1.00 16.16 ?  67  ASP   B H    1 
ATOM   4783 H HA   . ASP   B 1 67  ? 53.316 -7.006  9.235   1.00 16.91 ?  67  ASP   B HA   1 
ATOM   4784 H HB2  . ASP   B 1 67  ? 54.690 -6.642  7.435   1.00 18.29 ?  67  ASP   B HB2  1 
ATOM   4785 H HB3  . ASP   B 1 67  ? 53.527 -7.026  6.422   1.00 18.29 ?  67  ASP   B HB3  1 
ATOM   4786 N N    . TYR   B 1 68  ? 50.828 -7.887  7.402   1.00 13.83 ?  68  TYR   B N    1 
ATOM   4787 C CA   . TYR   B 1 68  ? 49.371 -7.806  7.325   1.00 14.48 ?  68  TYR   B CA   1 
ATOM   4788 C C    . TYR   B 1 68  ? 48.737 -8.158  8.667   1.00 13.94 ?  68  TYR   B C    1 
ATOM   4789 O O    . TYR   B 1 68  ? 47.798 -7.487  9.116   1.00 14.68 ?  68  TYR   B O    1 
ATOM   4790 C CB   . TYR   B 1 68  ? 48.835 -8.726  6.219   1.00 15.72 ?  68  TYR   B CB   1 
ATOM   4791 C CG   . TYR   B 1 68  ? 47.330 -8.881  6.281   1.00 17.13 ?  68  TYR   B CG   1 
ATOM   4792 C CD1  . TYR   B 1 68  ? 46.746 -9.842  7.103   1.00 17.60 ?  68  TYR   B CD1  1 
ATOM   4793 C CD2  . TYR   B 1 68  ? 46.497 -8.055  5.551   1.00 18.46 ?  68  TYR   B CD2  1 
ATOM   4794 C CE1  . TYR   B 1 68  ? 45.385 -9.966  7.198   1.00 18.70 ?  68  TYR   B CE1  1 
ATOM   4795 C CE2  . TYR   B 1 68  ? 45.119 -8.182  5.635   1.00 18.75 ?  68  TYR   B CE2  1 
ATOM   4796 C CZ   . TYR   B 1 68  ? 44.584 -9.139  6.462   1.00 18.82 ?  68  TYR   B CZ   1 
ATOM   4797 O OH   . TYR   B 1 68  ? 43.215 -9.265  6.562   1.00 19.91 ?  68  TYR   B OH   1 
ATOM   4798 H H    . TYR   B 1 68  ? 51.187 -8.438  6.840   1.00 16.56 ?  68  TYR   B H    1 
ATOM   4799 H HA   . TYR   B 1 68  ? 49.122 -6.896  7.106   1.00 17.35 ?  68  TYR   B HA   1 
ATOM   4800 H HB2  . TYR   B 1 68  ? 49.061 -8.351  5.355   1.00 18.84 ?  68  TYR   B HB2  1 
ATOM   4801 H HB3  . TYR   B 1 68  ? 49.232 -9.606  6.316   1.00 18.84 ?  68  TYR   B HB3  1 
ATOM   4802 H HD1  . TYR   B 1 68  ? 47.293 -10.408 7.607   1.00 21.09 ?  68  TYR   B HD1  1 
ATOM   4803 H HD2  . TYR   B 1 68  ? 46.866 -7.398  5.008   1.00 22.12 ?  68  TYR   B HD2  1 
ATOM   4804 H HE1  . TYR   B 1 68  ? 45.010 -10.626 7.741   1.00 22.41 ?  68  TYR   B HE1  1 
ATOM   4805 H HE2  . TYR   B 1 68  ? 44.558 -7.624  5.147   1.00 22.48 ?  68  TYR   B HE2  1 
ATOM   4806 H HH   . TYR   B 1 68  ? 42.826 -8.718  6.053   1.00 23.86 ?  68  TYR   B HH   1 
ATOM   4807 N N    . ILE   B 1 69  ? 49.229 -9.216  9.319   1.00 13.71 ?  69  ILE   B N    1 
ATOM   4808 C CA   . ILE   B 1 69  ? 48.664 -9.635  10.600  1.00 14.46 ?  69  ILE   B CA   1 
ATOM   4809 C C    . ILE   B 1 69  ? 48.912 -8.582  11.674  1.00 14.31 ?  69  ILE   B C    1 
ATOM   4810 O O    . ILE   B 1 69  ? 48.037 -8.300  12.503  1.00 14.81 ?  69  ILE   B O    1 
ATOM   4811 C CB   . ILE   B 1 69  ? 49.233 -11.009 11.005  1.00 15.05 ?  69  ILE   B CB   1 
ATOM   4812 C CG1  . ILE   B 1 69  ? 48.716 -12.120 10.079  1.00 15.62 ?  69  ILE   B CG1  1 
ATOM   4813 C CG2  . ILE   B 1 69  ? 48.919 -11.323 12.465  1.00 16.14 ?  69  ILE   B CG2  1 
ATOM   4814 C CD1  . ILE   B 1 69  ? 47.229 -12.431 10.219  1.00 16.03 ?  69  ILE   B CD1  1 
ATOM   4815 H H    . ILE   B 1 69  ? 49.879 -9.707  9.039   1.00 16.43 ?  69  ILE   B H    1 
ATOM   4816 H HA   . ILE   B 1 69  ? 47.708 -9.732  10.500  1.00 17.33 ?  69  ILE   B HA   1 
ATOM   4817 H HB   . ILE   B 1 69  ? 50.197 -10.978 10.912  1.00 18.03 ?  69  ILE   B HB   1 
ATOM   4818 H HG12 . ILE   B 1 69  ? 48.876 -11.859 9.158   1.00 18.72 ?  69  ILE   B HG12 1 
ATOM   4819 H HG13 . ILE   B 1 69  ? 49.205 -12.941 10.269  1.00 18.72 ?  69  ILE   B HG13 1 
ATOM   4820 H HG21 . ILE   B 1 69  ? 49.055 -12.275 12.619  1.00 19.34 ?  69  ILE   B HG21 1 
ATOM   4821 H HG22 . ILE   B 1 69  ? 49.513 -10.814 13.036  1.00 19.34 ?  69  ILE   B HG22 1 
ATOM   4822 H HG23 . ILE   B 1 69  ? 47.996 -11.092 12.648  1.00 19.34 ?  69  ILE   B HG23 1 
ATOM   4823 H HD11 . ILE   B 1 69  ? 46.998 -13.142 9.600   1.00 19.21 ?  69  ILE   B HD11 1 
ATOM   4824 H HD12 . ILE   B 1 69  ? 47.049 -12.716 11.128  1.00 19.21 ?  69  ILE   B HD12 1 
ATOM   4825 H HD13 . ILE   B 1 69  ? 46.719 -11.635 10.012  1.00 19.21 ?  69  ILE   B HD13 1 
ATOM   4826 N N    . ALA   B 1 70  ? 50.105 -7.990  11.693  1.00 13.96 ?  70  ALA   B N    1 
ATOM   4827 C CA   . ALA   B 1 70  ? 50.382 -6.954  12.684  1.00 13.95 ?  70  ALA   B CA   1 
ATOM   4828 C C    . ALA   B 1 70  ? 49.377 -5.816  12.574  1.00 14.61 ?  70  ALA   B C    1 
ATOM   4829 O O    . ALA   B 1 70  ? 48.920 -5.276  13.588  1.00 14.89 ?  70  ALA   B O    1 
ATOM   4830 C CB   . ALA   B 1 70  ? 51.808 -6.427  12.519  1.00 14.38 ?  70  ALA   B CB   1 
ATOM   4831 H H    . ALA   B 1 70  ? 50.752 -8.162  11.157  1.00 16.73 ?  70  ALA   B H    1 
ATOM   4832 H HA   . ALA   B 1 70  ? 50.308 -7.331  13.572  1.00 16.72 ?  70  ALA   B HA   1 
ATOM   4833 H HB1  . ALA   B 1 70  ? 51.993 -5.778  13.220  1.00 17.22 ?  70  ALA   B HB1  1 
ATOM   4834 H HB2  . ALA   B 1 70  ? 52.432 -7.168  12.588  1.00 17.22 ?  70  ALA   B HB2  1 
ATOM   4835 H HB3  . ALA   B 1 70  ? 51.897 -6.004  11.649  1.00 17.22 ?  70  ALA   B HB3  1 
ATOM   4836 N N    . THR   B 1 71  ? 49.008 -5.453  11.348  1.00 15.21 ?  71  THR   B N    1 
ATOM   4837 C CA   . THR   B 1 71  ? 48.114 -4.320  11.135  1.00 16.24 ?  71  THR   B CA   1 
ATOM   4838 C C    . THR   B 1 71  ? 46.648 -4.687  11.346  1.00 17.14 ?  71  THR   B C    1 
ATOM   4839 O O    . THR   B 1 71  ? 45.868 -3.871  11.855  1.00 18.36 ?  71  THR   B O    1 
ATOM   4840 C CB   . THR   B 1 71  ? 48.323 -3.758  9.726   1.00 17.82 ?  71  THR   B CB   1 
ATOM   4841 O OG1  . THR   B 1 71  ? 49.639 -3.202  9.627   1.00 19.78 ?  71  THR   B OG1  1 
ATOM   4842 C CG2  . THR   B 1 71  ? 47.288 -2.688  9.394   1.00 18.91 ?  71  THR   B CG2  1 
ATOM   4843 H H    . THR   B 1 71  ? 49.258 -5.849  10.626  1.00 18.22 ?  71  THR   B H    1 
ATOM   4844 H HA   . THR   B 1 71  ? 48.337 -3.623  11.766  1.00 19.46 ?  71  THR   B HA   1 
ATOM   4845 H HB   . THR   B 1 71  ? 48.239 -4.472  9.077   1.00 21.36 ?  71  THR   B HB   1 
ATOM   4846 H HG1  . THR   B 1 71  ? 49.764 -2.881  8.853   1.00 23.71 ?  71  THR   B HG1  1 
ATOM   4847 H HG21 . THR   B 1 71  ? 47.589 -2.162  8.634   1.00 22.66 ?  71  THR   B HG21 1 
ATOM   4848 H HG22 . THR   B 1 71  ? 46.441 -3.102  9.172   1.00 22.66 ?  71  THR   B HG22 1 
ATOM   4849 H HG23 . THR   B 1 71  ? 47.167 -2.098  10.153  1.00 22.66 ?  71  THR   B HG23 1 
ATOM   4850 N N    . ASN   B 1 72  ? 46.250 -5.898  10.955  1.00 16.43 ?  72  ASN   B N    1 
ATOM   4851 C CA   . ASN   B 1 72  ? 44.844 -6.255  10.835  1.00 16.90 ?  72  ASN   B CA   1 
ATOM   4852 C C    . ASN   B 1 72  ? 44.376 -7.344  11.786  1.00 17.40 ?  72  ASN   B C    1 
ATOM   4853 O O    . ASN   B 1 72  ? 43.162 -7.507  11.951  1.00 18.84 ?  72  ASN   B O    1 
ATOM   4854 C CB   . ASN   B 1 72  ? 44.522 -6.695  9.397   1.00 17.58 ?  72  ASN   B CB   1 
ATOM   4855 C CG   . ASN   B 1 72  ? 44.808 -5.611  8.382   1.00 18.78 ?  72  ASN   B CG   1 
ATOM   4856 O OD1  . ASN   B 1 72  ? 45.833 -5.624  7.700   1.00 20.26 ?  72  ASN   B OD1  1 
ATOM   4857 N ND2  . ASN   B 1 72  ? 43.918 -4.645  8.299   1.00 20.25 ?  72  ASN   B ND2  1 
ATOM   4858 H H    . ASN   B 1 72  ? 46.789 -6.546  10.751  1.00 19.69 ?  72  ASN   B H    1 
ATOM   4859 H HA   . ASN   B 1 72  ? 44.315 -5.466  11.018  1.00 20.25 ?  72  ASN   B HA   1 
ATOM   4860 H HB2  . ASN   B 1 72  ? 45.067 -7.469  9.172   1.00 21.06 ?  72  ASN   B HB2  1 
ATOM   4861 H HB3  . ASN   B 1 72  ? 43.584 -6.922  9.336   1.00 21.06 ?  72  ASN   B HB3  1 
ATOM   4862 H HD21 . ASN   B 1 72  ? 44.026 -4.002  7.736   1.00 24.27 ?  72  ASN   B HD21 1 
ATOM   4863 H HD22 . ASN   B 1 72  ? 43.212 -4.666  8.792   1.00 24.27 ?  72  ASN   B HD22 1 
ATOM   4864 N N    . GLY   B 1 73  ? 45.279 -8.098  12.401  1.00 16.64 ?  73  GLY   B N    1 
ATOM   4865 C CA   . GLY   B 1 73  ? 44.882 -9.226  13.204  1.00 15.73 ?  73  GLY   B CA   1 
ATOM   4866 C C    . GLY   B 1 73  ? 44.540 -10.425 12.347  1.00 14.25 ?  73  GLY   B C    1 
ATOM   4867 O O    . GLY   B 1 73  ? 44.527 -10.355 11.114  1.00 14.64 ?  73  GLY   B O    1 
ATOM   4868 H H    . GLY   B 1 73  ? 46.131 -7.971  12.367  1.00 19.94 ?  73  GLY   B H    1 
ATOM   4869 H HA2  . GLY   B 1 73  ? 45.602 -9.469  13.805  1.00 18.85 ?  73  GLY   B HA2  1 
ATOM   4870 H HA3  . GLY   B 1 73  ? 44.103 -8.991  13.734  1.00 18.85 ?  73  GLY   B HA3  1 
ATOM   4871 N N    . PRO   B 1 74  ? 44.237 -11.547 12.999  1.00 15.04 ?  74  PRO   B N    1 
ATOM   4872 C CA   . PRO   B 1 74  ? 43.976 -12.791 12.269  1.00 14.53 ?  74  PRO   B CA   1 
ATOM   4873 C C    . PRO   B 1 74  ? 42.680 -12.737 11.476  1.00 13.78 ?  74  PRO   B C    1 
ATOM   4874 O O    . PRO   B 1 74  ? 41.749 -11.992 11.798  1.00 15.37 ?  74  PRO   B O    1 
ATOM   4875 C CB   . PRO   B 1 74  ? 43.885 -13.836 13.389  1.00 15.57 ?  74  PRO   B CB   1 
ATOM   4876 C CG   . PRO   B 1 74  ? 43.444 -13.061 14.584  1.00 17.30 ?  74  PRO   B CG   1 
ATOM   4877 C CD   . PRO   B 1 74  ? 44.124 -11.727 14.455  1.00 16.48 ?  74  PRO   B CD   1 
ATOM   4878 H HA   . PRO   B 1 74  ? 44.720 -13.003 11.680  1.00 17.41 ?  74  PRO   B HA   1 
ATOM   4879 H HB2  . PRO   B 1 74  ? 43.231 -14.510 13.153  1.00 18.66 ?  74  PRO   B HB2  1 
ATOM   4880 H HB3  . PRO   B 1 74  ? 44.756 -14.233 13.539  1.00 18.66 ?  74  PRO   B HB3  1 
ATOM   4881 H HG2  . PRO   B 1 74  ? 42.477 -12.956 14.569  1.00 20.73 ?  74  PRO   B HG2  1 
ATOM   4882 H HG3  . PRO   B 1 74  ? 43.725 -13.514 15.393  1.00 20.73 ?  74  PRO   B HG3  1 
ATOM   4883 H HD2  . PRO   B 1 74  ? 43.571 -11.027 14.847  1.00 19.75 ?  74  PRO   B HD2  1 
ATOM   4884 H HD3  . PRO   B 1 74  ? 45.002 -11.754 14.863  1.00 19.75 ?  74  PRO   B HD3  1 
ATOM   4885 N N    . LEU   B 1 75  ? 42.644 -13.539 10.419  1.00 13.43 ?  75  LEU   B N    1 
ATOM   4886 C CA   . LEU   B 1 75  ? 41.438 -13.769 9.646   1.00 13.25 ?  75  LEU   B CA   1 
ATOM   4887 C C    . LEU   B 1 75  ? 40.457 -14.614 10.450  1.00 13.19 ?  75  LEU   B C    1 
ATOM   4888 O O    . LEU   B 1 75  ? 40.798 -15.197 11.480  1.00 14.47 ?  75  LEU   B O    1 
ATOM   4889 C CB   . LEU   B 1 75  ? 41.775 -14.510 8.352   1.00 12.80 ?  75  LEU   B CB   1 
ATOM   4890 C CG   . LEU   B 1 75  ? 42.577 -13.734 7.307   1.00 15.18 ?  75  LEU   B CG   1 
ATOM   4891 C CD1  . LEU   B 1 75  ? 42.757 -14.543 6.032   1.00 16.45 ?  75  LEU   B CD1  1 
ATOM   4892 C CD2  . LEU   B 1 75  ? 41.940 -12.408 6.998   1.00 19.48 ?  75  LEU   B CD2  1 
ATOM   4893 H H    . LEU   B 1 75  ? 43.325 -13.977 10.123  1.00 16.09 ?  75  LEU   B H    1 
ATOM   4894 H HA   . LEU   B 1 75  ? 41.016 -12.925 9.428   1.00 15.87 ?  75  LEU   B HA   1 
ATOM   4895 H HB2  . LEU   B 1 75  ? 42.291 -15.304 8.577   1.00 15.33 ?  75  LEU   B HB2  1 
ATOM   4896 H HB3  . LEU   B 1 75  ? 40.945 -14.784 7.927   1.00 15.33 ?  75  LEU   B HB3  1 
ATOM   4897 H HG   . LEU   B 1 75  ? 43.463 -13.559 7.667   1.00 18.19 ?  75  LEU   B HG   1 
ATOM   4898 H HD11 . LEU   B 1 75  ? 43.284 -14.028 5.399   1.00 19.71 ?  75  LEU   B HD11 1 
ATOM   4899 H HD12 . LEU   B 1 75  ? 43.218 -15.372 6.244   1.00 19.71 ?  75  LEU   B HD12 1 
ATOM   4900 H HD13 . LEU   B 1 75  ? 41.886 -14.738 5.654   1.00 19.71 ?  75  LEU   B HD13 1 
ATOM   4901 H HD21 . LEU   B 1 75  ? 42.363 -12.031 6.213   1.00 23.35 ?  75  LEU   B HD21 1 
ATOM   4902 H HD22 . LEU   B 1 75  ? 40.997 -12.546 6.838   1.00 23.35 ?  75  LEU   B HD22 1 
ATOM   4903 H HD23 . LEU   B 1 75  ? 42.066 -11.816 7.758   1.00 23.35 ?  75  LEU   B HD23 1 
ATOM   4904 N N    . LYS   B 1 76  ? 39.216 -14.666 9.963   1.00 14.65 ?  76  LYS   B N    1 
ATOM   4905 C CA   . LYS   B 1 76  ? 38.224 -15.620 10.444  1.00 15.90 ?  76  LYS   B CA   1 
ATOM   4906 C C    . LYS   B 1 76  ? 38.326 -16.907 9.631   1.00 14.53 ?  76  LYS   B C    1 
ATOM   4907 O O    . LYS   B 1 76  ? 38.614 -16.879 8.436   1.00 14.19 ?  76  LYS   B O    1 
ATOM   4908 C CB   . LYS   B 1 76  ? 36.803 -15.069 10.252  1.00 18.15 ?  76  LYS   B CB   1 
ATOM   4909 C CG   . LYS   B 1 76  ? 36.528 -13.676 10.834  1.00 19.61 ?  76  LYS   B CG   1 
ATOM   4910 C CD   . LYS   B 1 76  ? 35.104 -13.190 10.507  1.00 20.44 ?  76  LYS   B CD   1 
ATOM   4911 C CE   . LYS   B 1 76  ? 34.828 -11.824 11.107  1.00 22.34 ?  76  LYS   B CE   1 
ATOM   4912 N NZ   . LYS   B 1 76  ? 33.535 -11.239 10.653  1.00 22.93 ?  76  LYS   B NZ   1 
ATOM   4913 H H    . LYS   B 1 76  ? 38.921 -14.149 9.341   1.00 17.55 ?  76  LYS   B H    1 
ATOM   4914 H HA   . LYS   B 1 76  ? 38.370 -15.821 11.381  1.00 19.06 ?  76  LYS   B HA   1 
ATOM   4915 H HB2  . LYS   B 1 76  ? 36.619 -15.025 9.300   1.00 21.75 ?  76  LYS   B HB2  1 
ATOM   4916 H HB3  . LYS   B 1 76  ? 36.179 -15.683 10.671  1.00 21.75 ?  76  LYS   B HB3  1 
ATOM   4917 H HG2  . LYS   B 1 76  ? 36.622 -13.706 11.799  1.00 23.51 ?  76  LYS   B HG2  1 
ATOM   4918 H HG3  . LYS   B 1 76  ? 37.157 -13.040 10.456  1.00 23.51 ?  76  LYS   B HG3  1 
ATOM   4919 H HD2  . LYS   B 1 76  ? 34.999 -13.126 9.544   1.00 24.50 ?  76  LYS   B HD2  1 
ATOM   4920 H HD3  . LYS   B 1 76  ? 34.459 -13.817 10.872  1.00 24.50 ?  76  LYS   B HD3  1 
ATOM   4921 H HE2  . LYS   B 1 76  ? 34.798 -11.904 12.071  1.00 26.78 ?  76  LYS   B HE2  1 
ATOM   4922 H HE3  . LYS   B 1 76  ? 35.538 -11.217 10.845  1.00 26.78 ?  76  LYS   B HE3  1 
ATOM   4923 H HZ1  . LYS   B 1 76  ? 33.414 -10.439 11.028  1.00 27.49 ?  76  LYS   B HZ1  1 
ATOM   4924 H HZ2  . LYS   B 1 76  ? 33.534 -11.143 9.768   1.00 27.49 ?  76  LYS   B HZ2  1 
ATOM   4925 H HZ3  . LYS   B 1 76  ? 32.859 -11.770 10.887  1.00 27.49 ?  76  LYS   B HZ3  1 
ATOM   4926 N N    . VAL   B 1 77  ? 38.074 -18.047 10.281  1.00 15.59 ?  77  VAL   B N    1 
ATOM   4927 C CA   . VAL   B 1 77  ? 37.870 -19.271 9.516   1.00 15.86 ?  77  VAL   B CA   1 
ATOM   4928 C C    . VAL   B 1 77  ? 36.687 -19.051 8.587   1.00 14.57 ?  77  VAL   B C    1 
ATOM   4929 O O    . VAL   B 1 77  ? 35.619 -18.607 9.022   1.00 14.64 ?  77  VAL   B O    1 
ATOM   4930 C CB   . VAL   B 1 77  ? 37.658 -20.475 10.447  1.00 17.78 ?  77  VAL   B CB   1 
ATOM   4931 C CG1  . VAL   B 1 77  ? 37.392 -21.730 9.618   1.00 17.84 ?  77  VAL   B CG1  1 
ATOM   4932 C CG2  . VAL   B 1 77  ? 38.868 -20.668 11.360  1.00 19.18 ?  77  VAL   B CG2  1 
ATOM   4933 H H    . VAL   B 1 77  ? 38.021 -18.132 11.131  1.00 18.68 ?  77  VAL   B H    1 
ATOM   4934 H HA   . VAL   B 1 77  ? 38.649 -19.442 8.967   1.00 19.00 ?  77  VAL   B HA   1 
ATOM   4935 H HB   . VAL   B 1 77  ? 36.878 -20.310 11.002  1.00 21.30 ?  77  VAL   B HB   1 
ATOM   4936 H HG11 . VAL   B 1 77  ? 37.420 -22.501 10.203  1.00 21.38 ?  77  VAL   B HG11 1 
ATOM   4937 H HG12 . VAL   B 1 77  ? 36.515 -21.661 9.206   1.00 21.38 ?  77  VAL   B HG12 1 
ATOM   4938 H HG13 . VAL   B 1 77  ? 38.074 -21.805 8.934   1.00 21.38 ?  77  VAL   B HG13 1 
ATOM   4939 H HG21 . VAL   B 1 77  ? 38.731 -21.465 11.891  1.00 22.99 ?  77  VAL   B HG21 1 
ATOM   4940 H HG22 . VAL   B 1 77  ? 39.660 -20.761 10.812  1.00 22.99 ?  77  VAL   B HG22 1 
ATOM   4941 H HG23 . VAL   B 1 77  ? 38.950 -19.893 11.937  1.00 22.99 ?  77  VAL   B HG23 1 
ATOM   4942 N N    . GLY   B 1 78  ? 36.877 -19.334 7.299   1.00 14.05 ?  78  GLY   B N    1 
ATOM   4943 C CA   . GLY   B 1 78  ? 35.902 -19.022 6.281   1.00 13.92 ?  78  GLY   B CA   1 
ATOM   4944 C C    . GLY   B 1 78  ? 36.144 -17.713 5.564   1.00 13.38 ?  78  GLY   B C    1 
ATOM   4945 O O    . GLY   B 1 78  ? 35.458 -17.439 4.572   1.00 13.30 ?  78  GLY   B O    1 
ATOM   4946 H H    . GLY   B 1 78  ? 37.578 -19.722 6.991   1.00 16.83 ?  78  GLY   B H    1 
ATOM   4947 H HA2  . GLY   B 1 78  ? 35.894 -19.724 5.621   1.00 16.67 ?  78  GLY   B HA2  1 
ATOM   4948 H HA3  . GLY   B 1 78  ? 35.021 -18.976 6.689   1.00 16.67 ?  78  GLY   B HA3  1 
ATOM   4949 N N    . GLY   B 1 79  ? 37.086 -16.894 6.043   1.00 13.70 ?  79  GLY   B N    1 
ATOM   4950 C CA   . GLY   B 1 79  ? 37.379 -15.606 5.450   1.00 12.89 ?  79  GLY   B CA   1 
ATOM   4951 C C    . GLY   B 1 79  ? 38.609 -15.638 4.554   1.00 12.43 ?  79  GLY   B C    1 
ATOM   4952 O O    . GLY   B 1 79  ? 39.224 -16.674 4.316   1.00 12.80 ?  79  GLY   B O    1 
ATOM   4953 H H    . GLY   B 1 79  ? 37.586 -17.077 6.719   1.00 16.41 ?  79  GLY   B H    1 
ATOM   4954 H HA2  . GLY   B 1 79  ? 36.625 -15.315 4.916   1.00 15.43 ?  79  GLY   B HA2  1 
ATOM   4955 H HA3  . GLY   B 1 79  ? 37.530 -14.955 6.151   1.00 15.43 ?  79  GLY   B HA3  1 
ATOM   4956 N N    . SER   B 1 80  ? 38.977 -14.452 4.066   1.00 11.87 ?  80  SER   B N    1 
ATOM   4957 C CA   . SER   B 1 80  ? 40.084 -14.328 3.129   1.00 11.99 ?  80  SER   B CA   1 
ATOM   4958 C C    . SER   B 1 80  ? 40.661 -12.921 3.176   1.00 11.89 ?  80  SER   B C    1 
ATOM   4959 O O    . SER   B 1 80  ? 40.053 -11.990 3.706   1.00 13.12 ?  80  SER   B O    1 
ATOM   4960 C CB   . SER   B 1 80  ? 39.644 -14.629 1.697   1.00 12.19 ?  80  SER   B CB   1 
ATOM   4961 O OG   . SER   B 1 80  ? 38.805 -13.604 1.188   1.00 13.08 ?  80  SER   B OG   1 
ATOM   4962 H H    . SER   B 1 80  ? 38.603 -13.703 4.266   1.00 14.22 ?  80  SER   B H    1 
ATOM   4963 H HA   . SER   B 1 80  ? 40.778 -14.955 3.379   1.00 14.36 ?  80  SER   B HA   1 
ATOM   4964 H HB2  . SER   B 1 80  ? 40.429 -14.693 1.128   1.00 14.59 ?  80  SER   B HB2  1 
ATOM   4965 H HB3  . SER   B 1 80  ? 39.158 -15.467 1.684   1.00 14.59 ?  80  SER   B HB3  1 
ATOM   4966 H HG   . SER   B 1 80  ? 38.111 -13.535 1.667   1.00 15.67 ?  80  SER   B HG   1 
ATOM   4967 N N    . CYS   B 1 81  ? 41.853 -12.781 2.599   1.00 11.77 ?  81  CYS   B N    1 
ATOM   4968 C CA   . CYS   B 1 81  ? 42.412 -11.474 2.291   1.00 11.65 ?  81  CYS   B CA   1 
ATOM   4969 C C    . CYS   B 1 81  ? 43.173 -11.561 0.975   1.00 11.29 ?  81  CYS   B C    1 
ATOM   4970 O O    . CYS   B 1 81  ? 43.671 -12.624 0.592   1.00 12.42 ?  81  CYS   B O    1 
ATOM   4971 C CB   . CYS   B 1 81  ? 43.305 -10.933 3.416   1.00 12.26 ?  81  CYS   B CB   1 
ATOM   4972 S SG   . CYS   B 1 81  ? 44.830 -11.873 3.643   1.00 13.02 ?  81  CYS   B SG   1 
ATOM   4973 H H    . CYS   B 1 81  ? 42.367 -13.439 2.372   1.00 14.10 ?  81  CYS   B H    1 
ATOM   4974 H HA   . CYS   B 1 81  ? 41.681 -10.846 2.168   1.00 13.95 ?  81  CYS   B HA   1 
ATOM   4975 H HB2  . CYS   B 1 81  ? 43.544 -10.015 3.215   1.00 14.68 ?  81  CYS   B HB2  1 
ATOM   4976 H HB3  . CYS   B 1 81  ? 42.804 -10.963 4.251   1.00 14.68 ?  81  CYS   B HB3  1 
ATOM   4977 H HG   . CYS   B 1 81  ? 45.455 -11.380 4.545   1.00 15.59 ?  81  CYS   B HG   1 
ATOM   4978 N N    . VAL   B 1 82  ? 43.279 -10.417 0.302   1.00 11.45 ?  82  VAL   B N    1 
ATOM   4979 C CA   . VAL   B 1 82  ? 44.036 -10.288 -0.940  1.00 11.71 ?  82  VAL   B CA   1 
ATOM   4980 C C    . VAL   B 1 82  ? 45.385 -9.654  -0.636  1.00 11.82 ?  82  VAL   B C    1 
ATOM   4981 O O    . VAL   B 1 82  ? 45.448 -8.536  -0.109  1.00 13.10 ?  82  VAL   B O    1 
ATOM   4982 C CB   . VAL   B 1 82  ? 43.277 -9.450  -1.981  1.00 13.07 ?  82  VAL   B CB   1 
ATOM   4983 C CG1  . VAL   B 1 82  ? 44.095 -9.335  -3.259  1.00 14.42 ?  82  VAL   B CG1  1 
ATOM   4984 C CG2  . VAL   B 1 82  ? 41.906 -10.053 -2.268  1.00 14.13 ?  82  VAL   B CG2  1 
ATOM   4985 H H    . VAL   B 1 82  ? 42.903 -9.676  0.549   1.00 13.71 ?  82  VAL   B H    1 
ATOM   4986 H HA   . VAL   B 1 82  ? 44.190 -11.165 -1.312  1.00 14.03 ?  82  VAL   B HA   1 
ATOM   4987 H HB   . VAL   B 1 82  ? 43.143 -8.555  -1.636  1.00 15.65 ?  82  VAL   B HB   1 
ATOM   4988 H HG11 . VAL   B 1 82  ? 43.526 -8.998  -3.970  1.00 17.27 ?  82  VAL   B HG11 1 
ATOM   4989 H HG12 . VAL   B 1 82  ? 44.835 -8.725  -3.113  1.00 17.27 ?  82  VAL   B HG12 1 
ATOM   4990 H HG13 . VAL   B 1 82  ? 44.432 -10.214 -3.499  1.00 17.27 ?  82  VAL   B HG13 1 
ATOM   4991 H HG21 . VAL   B 1 82  ? 41.469 -9.538  -2.965  1.00 16.93 ?  82  VAL   B HG21 1 
ATOM   4992 H HG22 . VAL   B 1 82  ? 42.018 -10.973 -2.561  1.00 16.93 ?  82  VAL   B HG22 1 
ATOM   4993 H HG23 . VAL   B 1 82  ? 41.373 -10.030 -1.458  1.00 16.93 ?  82  VAL   B HG23 1 
ATOM   4994 N N    . LEU   B 1 83  ? 46.461 -10.344 -1.006  1.00 11.67 ?  83  LEU   B N    1 
ATOM   4995 C CA   . LEU   B 1 83  ? 47.822 -9.831  -0.893  1.00 11.59 ?  83  LEU   B CA   1 
ATOM   4996 C C    . LEU   B 1 83  ? 48.514 -9.983  -2.245  1.00 11.09 ?  83  LEU   B C    1 
ATOM   4997 O O    . LEU   B 1 83  ? 47.910 -10.411 -3.229  1.00 11.39 ?  83  LEU   B O    1 
ATOM   4998 C CB   . LEU   B 1 83  ? 48.586 -10.508 0.250   1.00 12.07 ?  83  LEU   B CB   1 
ATOM   4999 C CG   . LEU   B 1 83  ? 48.098 -10.155 1.658   1.00 13.17 ?  83  LEU   B CG   1 
ATOM   5000 C CD1  . LEU   B 1 83  ? 48.731 -11.030 2.729   1.00 13.69 ?  83  LEU   B CD1  1 
ATOM   5001 C CD2  . LEU   B 1 83  ? 48.312 -8.680  1.974   1.00 14.20 ?  83  LEU   B CD2  1 
ATOM   5002 H H    . LEU   B 1 83  ? 46.421 -11.139 -1.336  1.00 13.98 ?  83  LEU   B H    1 
ATOM   5003 H HA   . LEU   B 1 83  ? 47.776 -8.885  -0.699  1.00 13.88 ?  83  LEU   B HA   1 
ATOM   5004 H HB2  . LEU   B 1 83  ? 48.515 -11.469 0.144   1.00 14.46 ?  83  LEU   B HB2  1 
ATOM   5005 H HB3  . LEU   B 1 83  ? 49.520 -10.246 0.189   1.00 14.46 ?  83  LEU   B HB3  1 
ATOM   5006 H HG   . LEU   B 1 83  ? 47.146 -10.317 1.691   1.00 15.78 ?  83  LEU   B HG   1 
ATOM   5007 H HD11 . LEU   B 1 83  ? 48.379 -10.772 3.597   1.00 16.40 ?  83  LEU   B HD11 1 
ATOM   5008 H HD12 . LEU   B 1 83  ? 48.509 -11.960 2.550   1.00 16.40 ?  83  LEU   B HD12 1 
ATOM   5009 H HD13 . LEU   B 1 83  ? 49.692 -10.912 2.713   1.00 16.40 ?  83  LEU   B HD13 1 
ATOM   5010 H HD21 . LEU   B 1 83  ? 48.127 -8.529  2.914   1.00 17.01 ?  83  LEU   B HD21 1 
ATOM   5011 H HD22 . LEU   B 1 83  ? 49.232 -8.443  1.776   1.00 17.01 ?  83  LEU   B HD22 1 
ATOM   5012 H HD23 . LEU   B 1 83  ? 47.709 -8.151  1.429   1.00 17.01 ?  83  LEU   B HD23 1 
ATOM   5013 N N    . SER   B 1 84  ? 49.789 -9.608  -2.301  1.00 12.08 ?  84  SER   B N    1 
ATOM   5014 C CA   . SER   B 1 84  ? 50.530 -9.748  -3.545  1.00 12.55 ?  84  SER   B CA   1 
ATOM   5015 C C    . SER   B 1 84  ? 50.694 -11.216 -3.931  1.00 10.96 ?  84  SER   B C    1 
ATOM   5016 O O    . SER   B 1 84  ? 50.809 -12.097 -3.081  1.00 11.49 ?  84  SER   B O    1 
ATOM   5017 C CB   . SER   B 1 84  ? 51.922 -9.132  -3.406  1.00 14.52 ?  84  SER   B CB   1 
ATOM   5018 O OG   . SER   B 1 84  ? 52.659 -9.365  -4.592  1.00 15.89 ?  84  SER   B OG   1 
ATOM   5019 H H    . SER   B 1 84  ? 50.230 -9.268  -1.649  1.00 14.47 ?  84  SER   B H    1 
ATOM   5020 H HA   . SER   B 1 84  ? 50.063 -9.299  -4.259  1.00 15.03 ?  84  SER   B HA   1 
ATOM   5021 H HB2  . SER   B 1 84  ? 51.833 -8.176  -3.255  1.00 17.39 ?  84  SER   B HB2  1 
ATOM   5022 H HB3  . SER   B 1 84  ? 52.386 -9.543  -2.657  1.00 17.39 ?  84  SER   B HB3  1 
ATOM   5023 H HG   . SER   B 1 84  ? 53.427 -9.011  -4.522  1.00 19.04 ?  84  SER   B HG   1 
ATOM   5024 N N    . GLY   B 1 85  ? 50.760 -11.453 -5.235  1.00 12.48 ?  85  GLY   B N    1 
ATOM   5025 C CA   . GLY   B 1 85  ? 51.107 -12.751 -5.761  1.00 13.40 ?  85  GLY   B CA   1 
ATOM   5026 C C    . GLY   B 1 85  ? 52.581 -12.947 -6.067  1.00 12.71 ?  85  GLY   B C    1 
ATOM   5027 O O    . GLY   B 1 85  ? 52.965 -14.031 -6.508  1.00 12.96 ?  85  GLY   B O    1 
ATOM   5028 H H    . GLY   B 1 85  ? 50.614 -10.869 -5.841  1.00 14.95 ?  85  GLY   B H    1 
ATOM   5029 H HA2  . GLY   B 1 85  ? 50.846 -13.436 -5.123  1.00 16.05 ?  85  GLY   B HA2  1 
ATOM   5030 H HA3  . GLY   B 1 85  ? 50.612 -12.907 -6.579  1.00 16.05 ?  85  GLY   B HA3  1 
ATOM   5031 N N    . HIS   B 1 86  ? 53.436 -11.943 -5.863  1.00 12.88 ?  86  HIS   B N    1 
ATOM   5032 C CA   . HIS   B 1 86  ? 54.902 -12.103 -5.958  1.00 13.16 ?  86  HIS   B CA   1 
ATOM   5033 C C    . HIS   B 1 86  ? 55.266 -12.628 -7.346  1.00 13.16 ?  86  HIS   B C    1 
ATOM   5034 O O    . HIS   B 1 86  ? 54.870 -12.023 -8.355  1.00 14.15 ?  86  HIS   B O    1 
ATOM   5035 C CB   . HIS   B 1 86  ? 55.413 -12.926 -4.774  1.00 13.70 ?  86  HIS   B CB   1 
ATOM   5036 C CG   . HIS   B 1 86  ? 55.081 -12.319 -3.451  1.00 13.44 ?  86  HIS   B CG   1 
ATOM   5037 N ND1  . HIS   B 1 86  ? 55.905 -11.414 -2.819  1.00 15.19 ?  86  HIS   B ND1  1 
ATOM   5038 C CD2  . HIS   B 1 86  ? 53.993 -12.458 -2.655  1.00 13.46 ?  86  HIS   B CD2  1 
ATOM   5039 C CE1  . HIS   B 1 86  ? 55.334 -11.014 -1.695  1.00 14.66 ?  86  HIS   B CE1  1 
ATOM   5040 N NE2  . HIS   B 1 86  ? 54.171 -11.631 -1.573  1.00 14.23 ?  86  HIS   B NE2  1 
ATOM   5041 H H    . HIS   B 1 86  ? 53.191 -11.149 -5.658  1.00 15.43 ?  86  HIS   B H    1 
ATOM   5042 H HA   . HIS   B 1 86  ? 55.300 -11.229 -5.873  1.00 15.76 ?  86  HIS   B HA   1 
ATOM   5043 H HB2  . HIS   B 1 86  ? 55.025 -13.812 -4.803  1.00 16.42 ?  86  HIS   B HB2  1 
ATOM   5044 H HB3  . HIS   B 1 86  ? 56.385 -12.992 -4.831  1.00 16.42 ?  86  HIS   B HB3  1 
ATOM   5045 H HD2  . HIS   B 1 86  ? 53.250 -12.994 -2.822  1.00 16.13 ?  86  HIS   B HD2  1 
ATOM   5046 H HE1  . HIS   B 1 86  ? 55.701 -10.421 -1.079  1.00 17.57 ?  86  HIS   B HE1  1 
ATOM   5047 H HE2  . HIS   B 1 86  ? 53.626 -11.547 -0.911  1.00 17.05 ?  86  HIS   B HE2  1 
ATOM   5048 N N    . ASN   B 1 87  ? 56.031 -13.712 -7.455  1.00 13.39 ?  87  ASN   B N    1 
ATOM   5049 C CA   . ASN   B 1 87  ? 56.417 -14.292 -8.733  1.00 14.14 ?  87  ASN   B CA   1 
ATOM   5050 C C    . ASN   B 1 87  ? 55.424 -15.326 -9.234  1.00 13.86 ?  87  ASN   B C    1 
ATOM   5051 O O    . ASN   B 1 87  ? 55.721 -16.023 -10.211 1.00 15.99 ?  87  ASN   B O    1 
ATOM   5052 C CB   . ASN   B 1 87  ? 57.804 -14.937 -8.625  1.00 16.23 ?  87  ASN   B CB   1 
ATOM   5053 C CG   . ASN   B 1 87  ? 57.857 -16.049 -7.581  1.00 16.88 ?  87  ASN   B CG   1 
ATOM   5054 O OD1  . ASN   B 1 87  ? 57.242 -15.956 -6.516  1.00 16.14 ?  87  ASN   B OD1  1 
ATOM   5055 N ND2  . ASN   B 1 87  ? 58.593 -17.125 -7.894  1.00 19.58 ?  87  ASN   B ND2  1 
ATOM   5056 H H    . ASN   B 1 87  ? 56.345 -14.145 -6.781  1.00 16.04 ?  87  ASN   B H    1 
ATOM   5057 H HA   . ASN   B 1 87  ? 56.463 -13.591 -9.395  1.00 16.93 ?  87  ASN   B HA   1 
ATOM   5058 H HB2  . ASN   B 1 87  ? 58.044 -15.318 -9.489  1.00 19.45 ?  87  ASN   B HB2  1 
ATOM   5059 H HB3  . ASN   B 1 87  ? 58.447 -14.256 -8.377  1.00 19.45 ?  87  ASN   B HB3  1 
ATOM   5060 H HD21 . ASN   B 1 87  ? 58.663 -17.776 -7.341  1.00 23.47 ?  87  ASN   B HD21 1 
ATOM   5061 H HD22 . ASN   B 1 87  ? 59.013 -17.159 -8.650  1.00 23.47 ?  87  ASN   B HD22 1 
ATOM   5062 N N    . LEU   B 1 88  ? 54.254 -15.431 -8.601  1.00 12.94 ?  88  LEU   B N    1 
ATOM   5063 C CA   . LEU   B 1 88  ? 53.267 -16.456 -8.921  1.00 13.37 ?  88  LEU   B CA   1 
ATOM   5064 C C    . LEU   B 1 88  ? 52.035 -15.935 -9.640  1.00 13.35 ?  88  LEU   B C    1 
ATOM   5065 O O    . LEU   B 1 88  ? 51.421 -16.687 -10.409 1.00 15.02 ?  88  LEU   B O    1 
ATOM   5066 C CB   . LEU   B 1 88  ? 52.800 -17.142 -7.632  1.00 14.15 ?  88  LEU   B CB   1 
ATOM   5067 C CG   . LEU   B 1 88  ? 53.922 -17.801 -6.838  1.00 16.48 ?  88  LEU   B CG   1 
ATOM   5068 C CD1  . LEU   B 1 88  ? 53.443 -18.155 -5.443  1.00 18.27 ?  88  LEU   B CD1  1 
ATOM   5069 C CD2  . LEU   B 1 88  ? 54.405 -19.033 -7.576  1.00 20.31 ?  88  LEU   B CD2  1 
ATOM   5070 H H    . LEU   B 1 88  ? 54.003 -14.913 -7.954  1.00 15.50 ?  88  LEU   B H    1 
ATOM   5071 H HA   . LEU   B 1 88  ? 53.673 -17.130 -9.478  1.00 16.02 ?  88  LEU   B HA   1 
ATOM   5072 H HB2  . LEU   B 1 88  ? 52.374 -16.488 -7.053  1.00 16.95 ?  88  LEU   B HB2  1 
ATOM   5073 H HB3  . LEU   B 1 88  ? 52.152 -17.839 -7.857  1.00 16.95 ?  88  LEU   B HB3  1 
ATOM   5074 H HG   . LEU   B 1 88  ? 54.660 -17.180 -6.761  1.00 19.75 ?  88  LEU   B HG   1 
ATOM   5075 H HD11 . LEU   B 1 88  ? 54.129 -18.674 -5.000  1.00 21.90 ?  88  LEU   B HD11 1 
ATOM   5076 H HD12 . LEU   B 1 88  ? 53.273 -17.336 -4.953  1.00 21.90 ?  88  LEU   B HD12 1 
ATOM   5077 H HD13 . LEU   B 1 88  ? 52.626 -18.673 -5.516  1.00 21.90 ?  88  LEU   B HD13 1 
ATOM   5078 H HD21 . LEU   B 1 88  ? 55.053 -19.495 -7.023  1.00 24.35 ?  88  LEU   B HD21 1 
ATOM   5079 H HD22 . LEU   B 1 88  ? 53.648 -19.612 -7.755  1.00 24.35 ?  88  LEU   B HD22 1 
ATOM   5080 H HD23 . LEU   B 1 88  ? 54.818 -18.761 -8.412  1.00 24.35 ?  88  LEU   B HD23 1 
ATOM   5081 N N    . ALA   B 1 89  ? 51.637 -14.695 -9.379  1.00 12.88 ?  89  ALA   B N    1 
ATOM   5082 C CA   . ALA   B 1 89  ? 50.346 -14.194 -9.818  1.00 11.74 ?  89  ALA   B CA   1 
ATOM   5083 C C    . ALA   B 1 89  ? 50.334 -12.707 -9.518  1.00 12.30 ?  89  ALA   B C    1 
ATOM   5084 O O    . ALA   B 1 89  ? 51.168 -12.206 -8.763  1.00 13.10 ?  89  ALA   B O    1 
ATOM   5085 C CB   . ALA   B 1 89  ? 49.215 -14.877 -9.058  1.00 12.05 ?  89  ALA   B CB   1 
ATOM   5086 H H    . ALA   B 1 89  ? 52.103 -14.118 -8.943  1.00 15.43 ?  89  ALA   B H    1 
ATOM   5087 H HA   . ALA   B 1 89  ? 50.233 -14.336 -10.778 1.00 14.06 ?  89  ALA   B HA   1 
ATOM   5088 H HB1  . ALA   B 1 89  ? 48.367 -14.539 -9.390  1.00 14.43 ?  89  ALA   B HB1  1 
ATOM   5089 H HB2  . ALA   B 1 89  ? 49.270 -15.834 -9.210  1.00 14.43 ?  89  ALA   B HB2  1 
ATOM   5090 H HB3  . ALA   B 1 89  ? 49.310 -14.681 -8.119  1.00 14.43 ?  89  ALA   B HB3  1 
ATOM   5091 N N    . LYS   B 1 90  ? 49.365 -11.997 -10.090 1.00 13.06 ?  90  LYS   B N    1 
ATOM   5092 C CA   . LYS   B 1 90  ? 49.190 -10.608 -9.683  1.00 13.13 ?  90  LYS   B CA   1 
ATOM   5093 C C    . LYS   B 1 90  ? 48.859 -10.532 -8.199  1.00 12.51 ?  90  LYS   B C    1 
ATOM   5094 O O    . LYS   B 1 90  ? 49.505 -9.788  -7.448  1.00 13.30 ?  90  LYS   B O    1 
ATOM   5095 C CB   . LYS   B 1 90  ? 48.122 -9.938  -10.545 1.00 14.63 ?  90  LYS   B CB   1 
ATOM   5096 C CG   . LYS   B 1 90  ? 47.797 -8.501  -10.136 1.00 15.09 ?  90  LYS   B CG   1 
ATOM   5097 C CD   . LYS   B 1 90  ? 48.994 -7.588  -10.191 1.00 18.22 ?  90  LYS   B CD   1 
ATOM   5098 C CE   . LYS   B 1 90  ? 48.537 -6.164  -9.955  1.00 20.45 ?  90  LYS   B CE   1 
ATOM   5099 N NZ   . LYS   B 1 90  ? 49.688 -5.243  -9.810  1.00 19.78 ?  90  LYS   B NZ   1 
ATOM   5100 H H    . LYS   B 1 90  ? 48.821 -12.285 -10.694 1.00 15.64 ?  90  LYS   B H    1 
ATOM   5101 H HA   . LYS   B 1 90  ? 50.023 -10.136 -9.826  1.00 15.73 ?  90  LYS   B HA   1 
ATOM   5102 H HB2  . LYS   B 1 90  ? 48.433 -9.912  -11.468 1.00 17.52 ?  90  LYS   B HB2  1 
ATOM   5103 H HB3  . LYS   B 1 90  ? 47.304 -10.453 -10.495 1.00 17.52 ?  90  LYS   B HB3  1 
ATOM   5104 H HG2  . LYS   B 1 90  ? 47.120 -8.147  -10.739 1.00 18.08 ?  90  LYS   B HG2  1 
ATOM   5105 H HG3  . LYS   B 1 90  ? 47.450 -8.499  -9.227  1.00 18.08 ?  90  LYS   B HG3  1 
ATOM   5106 H HD2  . LYS   B 1 90  ? 49.622 -7.828  -9.493  1.00 21.83 ?  90  LYS   B HD2  1 
ATOM   5107 H HD3  . LYS   B 1 90  ? 49.408 -7.641  -11.064 1.00 21.83 ?  90  LYS   B HD3  1 
ATOM   5108 H HE2  . LYS   B 1 90  ? 48.006 -5.862  -10.713 1.00 24.51 ?  90  LYS   B HE2  1 
ATOM   5109 H HE3  . LYS   B 1 90  ? 48.011 -6.117  -9.141  1.00 24.51 ?  90  LYS   B HE3  1 
ATOM   5110 H HZ1  . LYS   B 1 90  ? 49.404 -4.409  -9.675  1.00 23.70 ?  90  LYS   B HZ1  1 
ATOM   5111 H HZ2  . LYS   B 1 90  ? 50.192 -5.491  -9.119  1.00 23.70 ?  90  LYS   B HZ2  1 
ATOM   5112 H HZ3  . LYS   B 1 90  ? 50.188 -5.259  -10.549 1.00 23.70 ?  90  LYS   B HZ3  1 
ATOM   5113 N N    . HIS   B 1 91  ? 47.885 -11.335 -7.754  1.00 11.18 ?  91  HIS   B N    1 
ATOM   5114 C CA   . HIS   B 1 91  ? 47.431 -11.362 -6.376  1.00 11.66 ?  91  HIS   B CA   1 
ATOM   5115 C C    . HIS   B 1 91  ? 47.420 -12.792 -5.859  1.00 10.70 ?  91  HIS   B C    1 
ATOM   5116 O O    . HIS   B 1 91  ? 47.180 -13.744 -6.617  1.00 11.35 ?  91  HIS   B O    1 
ATOM   5117 C CB   . HIS   B 1 91  ? 45.974 -10.871 -6.251  1.00 13.13 ?  91  HIS   B CB   1 
ATOM   5118 C CG   . HIS   B 1 91  ? 45.771 -9.452  -6.667  1.00 16.21 ?  91  HIS   B CG   1 
ATOM   5119 N ND1  . HIS   B 1 91  ? 46.403 -8.392  -6.054  1.00 18.81 ?  91  HIS   B ND1  1 
ATOM   5120 C CD2  . HIS   B 1 91  ? 44.972 -8.915  -7.618  1.00 19.03 ?  91  HIS   B CD2  1 
ATOM   5121 C CE1  . HIS   B 1 91  ? 46.019 -7.262  -6.623  1.00 20.04 ?  91  HIS   B CE1  1 
ATOM   5122 N NE2  . HIS   B 1 91  ? 45.147 -7.552  -7.573  1.00 20.65 ?  91  HIS   B NE2  1 
ATOM   5123 H H    . HIS   B 1 91  ? 47.460 -11.891 -8.258  1.00 13.39 ?  91  HIS   B H    1 
ATOM   5124 H HA   . HIS   B 1 91  ? 48.008 -10.808 -5.818  1.00 13.96 ?  91  HIS   B HA   1 
ATOM   5125 H HB2  . HIS   B 1 91  ? 45.409 -11.425 -6.808  1.00 15.73 ?  91  HIS   B HB2  1 
ATOM   5126 H HB3  . HIS   B 1 91  ? 45.698 -10.948 -5.322  1.00 15.73 ?  91  HIS   B HB3  1 
ATOM   5127 H HD2  . HIS   B 1 91  ? 44.417 -9.377  -8.202  1.00 22.81 ?  91  HIS   B HD2  1 
ATOM   5128 H HE1  . HIS   B 1 91  ? 46.306 -6.406  -6.389  1.00 24.02 ?  91  HIS   B HE1  1 
ATOM   5129 H HE2  . HIS   B 1 91  ? 44.761 -6.976  -8.085  1.00 24.75 ?  91  HIS   B HE2  1 
ATOM   5130 N N    . CYS   B 1 92  ? 47.604 -12.926 -4.550  1.00 10.70 ?  92  CYS   B N    1 
ATOM   5131 C CA   . CYS   B 1 92  ? 47.291 -14.163 -3.844  1.00 10.43 ?  92  CYS   B CA   1 
ATOM   5132 C C    . CYS   B 1 92  ? 46.070 -13.918 -2.966  1.00 10.51 ?  92  CYS   B C    1 
ATOM   5133 O O    . CYS   B 1 92  ? 46.078 -13.009 -2.125  1.00 11.43 ?  92  CYS   B O    1 
ATOM   5134 C CB   . CYS   B 1 92  ? 48.463 -14.628 -2.984  1.00 11.35 ?  92  CYS   B CB   1 
ATOM   5135 S SG   . CYS   B 1 92  ? 48.095 -16.157 -2.077  1.00 11.44 ?  92  CYS   B SG   1 
ATOM   5136 H H    . CYS   B 1 92  ? 47.922 -12.305 -4.042  1.00 12.81 ?  92  CYS   B H    1 
ATOM   5137 H HA   . CYS   B 1 92  ? 47.079 -14.855 -4.489  1.00 12.49 ?  92  CYS   B HA   1 
ATOM   5138 H HB2  . CYS   B 1 92  ? 49.225 -14.783 -3.557  1.00 13.59 ?  92  CYS   B HB2  1 
ATOM   5139 H HB3  . CYS   B 1 92  ? 48.662 -13.935 -2.336  1.00 13.59 ?  92  CYS   B HB3  1 
ATOM   5140 H HG   . CYS   B 1 92  ? 49.070 -16.476 -1.459  1.00 13.70 ?  92  CYS   B HG   1 
ATOM   5141 N N    . LEU   B 1 93  ? 45.024 -14.719 -3.172  1.00 10.74 ?  93  LEU   B N    1 
ATOM   5142 C CA   . LEU   B 1 93  ? 43.852 -14.736 -2.304  1.00 10.30 ?  93  LEU   B CA   1 
ATOM   5143 C C    . LEU   B 1 93  ? 44.079 -15.801 -1.237  1.00 9.47  ?  93  LEU   B C    1 
ATOM   5144 O O    . LEU   B 1 93  ? 44.026 -17.003 -1.526  1.00 10.83 ?  93  LEU   B O    1 
ATOM   5145 C CB   . LEU   B 1 93  ? 42.590 -15.025 -3.111  1.00 10.90 ?  93  LEU   B CB   1 
ATOM   5146 C CG   . LEU   B 1 93  ? 41.281 -15.032 -2.307  1.00 12.00 ?  93  LEU   B CG   1 
ATOM   5147 C CD1  . LEU   B 1 93  ? 40.911 -13.640 -1.813  1.00 12.37 ?  93  LEU   B CD1  1 
ATOM   5148 C CD2  . LEU   B 1 93  ? 40.150 -15.627 -3.122  1.00 12.30 ?  93  LEU   B CD2  1 
ATOM   5149 H H    . LEU   B 1 93  ? 44.970 -15.284 -3.825  1.00 12.85 ?  93  LEU   B H    1 
ATOM   5150 H HA   . LEU   B 1 93  ? 43.754 -13.872 -1.874  1.00 12.33 ?  93  LEU   B HA   1 
ATOM   5151 H HB2  . LEU   B 1 93  ? 42.500 -14.341 -3.799  1.00 13.05 ?  93  LEU   B HB2  1 
ATOM   5152 H HB3  . LEU   B 1 93  ? 42.679 -15.891 -3.528  1.00 13.05 ?  93  LEU   B HB3  1 
ATOM   5153 H HG   . LEU   B 1 93  ? 41.403 -15.592 -1.527  1.00 14.37 ?  93  LEU   B HG   1 
ATOM   5154 H HD11 . LEU   B 1 93  ? 40.064 -13.690 -1.344  1.00 14.82 ?  93  LEU   B HD11 1 
ATOM   5155 H HD12 . LEU   B 1 93  ? 41.604 -13.323 -1.215  1.00 14.82 ?  93  LEU   B HD12 1 
ATOM   5156 H HD13 . LEU   B 1 93  ? 40.833 -13.046 -2.576  1.00 14.82 ?  93  LEU   B HD13 1 
ATOM   5157 H HD21 . LEU   B 1 93  ? 39.334 -15.607 -2.596  1.00 14.73 ?  93  LEU   B HD21 1 
ATOM   5158 H HD22 . LEU   B 1 93  ? 40.031 -15.105 -3.933  1.00 14.73 ?  93  LEU   B HD22 1 
ATOM   5159 H HD23 . LEU   B 1 93  ? 40.371 -16.544 -3.351  1.00 14.73 ?  93  LEU   B HD23 1 
ATOM   5160 N N    . HIS   B 1 94  ? 44.364 -15.363 -0.020  1.00 9.68  ?  94  HIS   B N    1 
ATOM   5161 C CA   . HIS   B 1 94  ? 44.575 -16.260 1.105   1.00 9.78  ?  94  HIS   B CA   1 
ATOM   5162 C C    . HIS   B 1 94  ? 43.208 -16.602 1.680   1.00 11.11 ?  94  HIS   B C    1 
ATOM   5163 O O    . HIS   B 1 94  ? 42.545 -15.732 2.244   1.00 12.13 ?  94  HIS   B O    1 
ATOM   5164 C CB   . HIS   B 1 94  ? 45.450 -15.583 2.158   1.00 10.90 ?  94  HIS   B CB   1 
ATOM   5165 C CG   . HIS   B 1 94  ? 46.828 -15.280 1.681   1.00 10.82 ?  94  HIS   B CG   1 
ATOM   5166 N ND1  . HIS   B 1 94  ? 47.854 -16.196 1.759   1.00 10.99 ?  94  HIS   B ND1  1 
ATOM   5167 C CD2  . HIS   B 1 94  ? 47.335 -14.173 1.087   1.00 10.97 ?  94  HIS   B CD2  1 
ATOM   5168 C CE1  . HIS   B 1 94  ? 48.942 -15.650 1.247   1.00 11.39 ?  94  HIS   B CE1  1 
ATOM   5169 N NE2  . HIS   B 1 94  ? 48.655 -14.428 0.830   1.00 11.42 ?  94  HIS   B NE2  1 
ATOM   5170 H H    . HIS   B 1 94  ? 44.471 -14.524 0.177   1.00 11.59 ?  94  HIS   B H    1 
ATOM   5171 H HA   . HIS   B 1 94  ? 45.007 -17.073 0.805   1.00 11.71 ?  94  HIS   B HA   1 
ATOM   5172 H HB2  . HIS   B 1 94  ? 45.031 -14.747 2.417   1.00 13.05 ?  94  HIS   B HB2  1 
ATOM   5173 H HB3  . HIS   B 1 94  ? 45.521 -16.171 2.923   1.00 13.05 ?  94  HIS   B HB3  1 
ATOM   5174 H HD2  . HIS   B 1 94  ? 46.877 -13.387 0.894   1.00 13.13 ?  94  HIS   B HD2  1 
ATOM   5175 H HE1  . HIS   B 1 94  ? 49.771 -16.067 1.187   1.00 13.64 ?  94  HIS   B HE1  1 
ATOM   5176 H HE2  . HIS   B 1 94  ? 49.211 -13.883 0.466   1.00 13.68 ?  94  HIS   B HE2  1 
ATOM   5177 N N    . VAL   B 1 95  ? 42.769 -17.854 1.527   1.00 11.00 ?  95  VAL   B N    1 
ATOM   5178 C CA   . VAL   B 1 95  ? 41.444 -18.302 1.964   1.00 10.86 ?  95  VAL   B CA   1 
ATOM   5179 C C    . VAL   B 1 95  ? 41.608 -19.334 3.069   1.00 11.17 ?  95  VAL   B C    1 
ATOM   5180 O O    . VAL   B 1 95  ? 42.384 -20.282 2.919   1.00 11.74 ?  95  VAL   B O    1 
ATOM   5181 C CB   . VAL   B 1 95  ? 40.627 -18.911 0.807   1.00 11.22 ?  95  VAL   B CB   1 
ATOM   5182 C CG1  . VAL   B 1 95  ? 39.251 -19.350 1.295   1.00 13.05 ?  95  VAL   B CG1  1 
ATOM   5183 C CG2  . VAL   B 1 95  ? 40.506 -17.917 -0.328  1.00 11.02 ?  95  VAL   B CG2  1 
ATOM   5184 H H    . VAL   B 1 95  ? 43.232 -18.477 1.153   1.00 13.17 ?  95  VAL   B H    1 
ATOM   5185 H HA   . VAL   B 1 95  ? 40.948 -17.549 2.320   1.00 13.01 ?  95  VAL   B HA   1 
ATOM   5186 H HB   . VAL   B 1 95  ? 41.090 -19.689 0.467   1.00 13.43 ?  95  VAL   B HB   1 
ATOM   5187 H HG11 . VAL   B 1 95  ? 38.691 -19.541 0.523   1.00 15.63 ?  95  VAL   B HG11 1 
ATOM   5188 H HG12 . VAL   B 1 95  ? 39.346 -20.149 1.834   1.00 15.63 ?  95  VAL   B HG12 1 
ATOM   5189 H HG13 . VAL   B 1 95  ? 38.856 -18.637 1.817   1.00 15.63 ?  95  VAL   B HG13 1 
ATOM   5190 H HG21 . VAL   B 1 95  ? 39.922 -18.288 -1.005  1.00 13.20 ?  95  VAL   B HG21 1 
ATOM   5191 H HG22 . VAL   B 1 95  ? 40.128 -17.093 0.022   1.00 13.20 ?  95  VAL   B HG22 1 
ATOM   5192 H HG23 . VAL   B 1 95  ? 41.385 -17.751 -0.693  1.00 13.20 ?  95  VAL   B HG23 1 
ATOM   5193 N N    . VAL   B 1 96  ? 40.888 -19.152 4.170   1.00 11.77 ?  96  VAL   B N    1 
ATOM   5194 C CA   . VAL   B 1 96  ? 40.967 -20.059 5.314   1.00 11.90 ?  96  VAL   B CA   1 
ATOM   5195 C C    . VAL   B 1 96  ? 39.780 -21.021 5.269   1.00 12.65 ?  96  VAL   B C    1 
ATOM   5196 O O    . VAL   B 1 96  ? 38.661 -20.668 5.652   1.00 13.58 ?  96  VAL   B O    1 
ATOM   5197 C CB   . VAL   B 1 96  ? 41.013 -19.308 6.647   1.00 12.99 ?  96  VAL   B CB   1 
ATOM   5198 C CG1  . VAL   B 1 96  ? 41.187 -20.294 7.797   1.00 13.41 ?  96  VAL   B CG1  1 
ATOM   5199 C CG2  . VAL   B 1 96  ? 42.132 -18.272 6.659   1.00 13.58 ?  96  VAL   B CG2  1 
ATOM   5200 H H    . VAL   B 1 96  ? 40.336 -18.500 4.283   1.00 14.10 ?  96  VAL   B H    1 
ATOM   5201 H HA   . VAL   B 1 96  ? 41.784 -20.583 5.246   1.00 14.26 ?  96  VAL   B HA   1 
ATOM   5202 H HB   . VAL   B 1 96  ? 40.172 -18.841 6.779   1.00 15.56 ?  96  VAL   B HB   1 
ATOM   5203 H HG11 . VAL   B 1 96  ? 41.379 -19.803 8.614   1.00 16.06 ?  96  VAL   B HG11 1 
ATOM   5204 H HG12 . VAL   B 1 96  ? 40.373 -20.808 7.907   1.00 16.06 ?  96  VAL   B HG12 1 
ATOM   5205 H HG13 . VAL   B 1 96  ? 41.930 -20.889 7.595   1.00 16.06 ?  96  VAL   B HG13 1 
ATOM   5206 H HG21 . VAL   B 1 96  ? 42.171 -17.853 7.536   1.00 16.27 ?  96  VAL   B HG21 1 
ATOM   5207 H HG22 . VAL   B 1 96  ? 42.972 -18.707 6.462   1.00 16.27 ?  96  VAL   B HG22 1 
ATOM   5208 H HG23 . VAL   B 1 96  ? 41.944 -17.594 5.985   1.00 16.27 ?  96  VAL   B HG23 1 
ATOM   5209 N N    . GLY   B 1 97  ? 40.013 -22.250 4.821   1.00 12.71 ?  97  GLY   B N    1 
ATOM   5210 C CA   . GLY   B 1 97  ? 39.048 -23.306 5.003   1.00 13.67 ?  97  GLY   B CA   1 
ATOM   5211 C C    . GLY   B 1 97  ? 39.210 -23.901 6.385   1.00 15.26 ?  97  GLY   B C    1 
ATOM   5212 O O    . GLY   B 1 97  ? 40.264 -23.773 7.022   1.00 15.67 ?  97  GLY   B O    1 
ATOM   5213 H H    . GLY   B 1 97  ? 40.726 -22.483 4.393   1.00 15.22 ?  97  GLY   B H    1 
ATOM   5214 H HA2  . GLY   B 1 97  ? 38.150 -22.941 4.903   1.00 16.38 ?  97  GLY   B HA2  1 
ATOM   5215 H HA3  . GLY   B 1 97  ? 39.181 -23.994 4.335   1.00 16.38 ?  97  GLY   B HA3  1 
ATOM   5216 N N    . PRO   B 1 98  ? 38.172 -24.569 6.879   1.00 16.51 ?  98  PRO   B N    1 
ATOM   5217 C CA   . PRO   B 1 98  ? 38.291 -25.240 8.177   1.00 18.02 ?  98  PRO   B CA   1 
ATOM   5218 C C    . PRO   B 1 98  ? 39.307 -26.374 8.134   1.00 17.55 ?  98  PRO   B C    1 
ATOM   5219 O O    . PRO   B 1 98  ? 39.389 -27.128 7.161   1.00 17.01 ?  98  PRO   B O    1 
ATOM   5220 C CB   . PRO   B 1 98  ? 36.872 -25.763 8.435   1.00 18.78 ?  98  PRO   B CB   1 
ATOM   5221 C CG   . PRO   B 1 98  ? 36.264 -25.903 7.090   1.00 18.40 ?  98  PRO   B CG   1 
ATOM   5222 C CD   . PRO   B 1 98  ? 36.837 -24.763 6.281   1.00 17.31 ?  98  PRO   B CD   1 
ATOM   5223 H HA   . PRO   B 1 98  ? 38.537 -24.604 8.866   1.00 21.59 ?  98  PRO   B HA   1 
ATOM   5224 H HB2  . PRO   B 1 98  ? 36.919 -26.623 8.883   1.00 22.50 ?  98  PRO   B HB2  1 
ATOM   5225 H HB3  . PRO   B 1 98  ? 36.379 -25.123 8.969   1.00 22.50 ?  98  PRO   B HB3  1 
ATOM   5226 H HG2  . PRO   B 1 98  ? 36.519 -26.759 6.707   1.00 22.06 ?  98  PRO   B HG2  1 
ATOM   5227 H HG3  . PRO   B 1 98  ? 35.302 -25.830 7.158   1.00 22.06 ?  98  PRO   B HG3  1 
ATOM   5228 H HD2  . PRO   B 1 98  ? 36.913 -25.017 5.344   1.00 20.74 ?  98  PRO   B HD2  1 
ATOM   5229 H HD3  . PRO   B 1 98  ? 36.298 -23.965 6.388   1.00 20.74 ?  98  PRO   B HD3  1 
ATOM   5230 N N    A ASN   B 1 99  ? 40.092 -26.485 9.205   0.66 18.51 ?  99  ASN   B N    1 
ATOM   5231 N N    B ASN   B 1 99  ? 40.083 -26.489 9.211   0.34 19.14 ?  99  ASN   B N    1 
ATOM   5232 C CA   A ASN   B 1 99  ? 41.081 -27.553 9.367   0.66 19.53 ?  99  ASN   B CA   1 
ATOM   5233 C CA   B ASN   B 1 99  ? 41.077 -27.550 9.374   0.34 20.60 ?  99  ASN   B CA   1 
ATOM   5234 C C    A ASN   B 1 99  ? 40.469 -28.618 10.270  0.66 21.57 ?  99  ASN   B C    1 
ATOM   5235 C C    B ASN   B 1 99  ? 40.466 -28.620 10.273  0.34 22.24 ?  99  ASN   B C    1 
ATOM   5236 O O    A ASN   B 1 99  ? 40.435 -28.465 11.494  0.66 22.98 ?  99  ASN   B O    1 
ATOM   5237 O O    B ASN   B 1 99  ? 40.438 -28.475 11.498  0.34 23.09 ?  99  ASN   B O    1 
ATOM   5238 C CB   A ASN   B 1 99  ? 42.366 -26.990 9.965   0.66 19.72 ?  99  ASN   B CB   1 
ATOM   5239 C CB   B ASN   B 1 99  ? 42.357 -26.981 9.977   0.34 20.89 ?  99  ASN   B CB   1 
ATOM   5240 C CG   A ASN   B 1 99  ? 43.509 -27.994 9.961   0.66 20.44 ?  99  ASN   B CG   1 
ATOM   5241 C CG   B ASN   B 1 99  ? 43.507 -27.972 9.960   0.34 21.27 ?  99  ASN   B CG   1 
ATOM   5242 O OD1  A ASN   B 1 99  ? 43.317 -29.173 10.235  0.66 21.39 ?  99  ASN   B OD1  1 
ATOM   5243 O OD1  B ASN   B 1 99  ? 43.324 -29.160 10.214  0.34 21.69 ?  99  ASN   B OD1  1 
ATOM   5244 N ND2  A ASN   B 1 99  ? 44.704 -27.522 9.648   0.66 20.28 ?  99  ASN   B ND2  1 
ATOM   5245 N ND2  B ASN   B 1 99  ? 44.702 -27.482 9.656   0.34 21.27 ?  99  ASN   B ND2  1 
ATOM   5246 H H    A ASN   B 1 99  ? 40.068 -25.936 9.867   0.66 22.18 ?  99  ASN   B H    1 
ATOM   5247 H H    B ASN   B 1 99  ? 40.051 -25.947 9.878   0.34 22.93 ?  99  ASN   B H    1 
ATOM   5248 H HA   A ASN   B 1 99  ? 41.278 -27.952 8.507   0.66 23.41 ?  99  ASN   B HA   1 
ATOM   5249 H HA   B ASN   B 1 99  ? 41.282 -27.947 8.514   0.34 24.70 ?  99  ASN   B HA   1 
ATOM   5250 H HB2  A ASN   B 1 99  ? 42.636 -26.218 9.451   0.66 23.63 ?  99  ASN   B HB2  1 
ATOM   5251 H HB2  B ASN   B 1 99  ? 42.623 -26.201 9.471   0.34 25.04 ?  99  ASN   B HB2  1 
ATOM   5252 H HB3  A ASN   B 1 99  ? 42.191 -26.732 10.888  0.66 23.63 ?  99  ASN   B HB3  1 
ATOM   5253 H HB3  B ASN   B 1 99  ? 42.184 -26.735 10.902  0.34 25.04 ?  99  ASN   B HB3  1 
ATOM   5254 H HD21 A ASN   B 1 99  ? 45.381 -28.045 9.631   0.66 24.31 ?  99  ASN   B HD21 1 
ATOM   5255 H HD21 B ASN   B 1 99  ? 45.387 -27.999 9.633   0.34 25.49 ?  99  ASN   B HD21 1 
ATOM   5256 H HD22 A ASN   B 1 99  ? 44.795 -26.686 9.460   0.66 24.31 ?  99  ASN   B HD22 1 
ATOM   5257 H HD22 B ASN   B 1 99  ? 44.788 -26.643 9.482   0.34 25.49 ?  99  ASN   B HD22 1 
ATOM   5258 N N    . VAL   B 1 100 ? 39.972 -29.697 9.657   1.00 23.34 ?  100 VAL   B N    1 
ATOM   5259 C CA   . VAL   B 1 100 ? 39.361 -30.781 10.426  1.00 26.72 ?  100 VAL   B CA   1 
ATOM   5260 C C    . VAL   B 1 100 ? 40.381 -31.441 11.345  1.00 27.87 ?  100 VAL   B C    1 
ATOM   5261 O O    . VAL   B 1 100 ? 40.038 -31.898 12.442  1.00 29.39 ?  100 VAL   B O    1 
ATOM   5262 C CB   . VAL   B 1 100 ? 38.674 -31.791 9.481   1.00 29.21 ?  100 VAL   B CB   1 
ATOM   5263 C CG1  . VAL   B 1 100 ? 38.209 -33.019 10.245  1.00 30.23 ?  100 VAL   B CG1  1 
ATOM   5264 C CG2  . VAL   B 1 100 ? 37.496 -31.130 8.778   1.00 29.81 ?  100 VAL   B CG2  1 
ATOM   5265 H H    A VAL   B 1 100 ? 39.980 -29.826 8.805   0.66 27.97 ?  100 VAL   B H    1 
ATOM   5266 H H    B VAL   B 1 100 ? 39.978 -29.824 8.804   0.34 27.97 ?  100 VAL   B H    1 
ATOM   5267 H HA   . VAL   B 1 100 ? 38.665 -30.405 10.985  1.00 32.04 ?  100 VAL   B HA   1 
ATOM   5268 H HB   . VAL   B 1 100 ? 39.304 -32.079 8.803   1.00 35.03 ?  100 VAL   B HB   1 
ATOM   5269 H HG11 . VAL   B 1 100 ? 37.586 -33.518 9.691   1.00 36.25 ?  100 VAL   B HG11 1 
ATOM   5270 H HG12 . VAL   B 1 100 ? 38.977 -33.573 10.455  1.00 36.25 ?  100 VAL   B HG12 1 
ATOM   5271 H HG13 . VAL   B 1 100 ? 37.768 -32.736 11.060  1.00 36.25 ?  100 VAL   B HG13 1 
ATOM   5272 H HG21 . VAL   B 1 100 ? 37.069 -31.780 8.198   1.00 35.74 ?  100 VAL   B HG21 1 
ATOM   5273 H HG22 . VAL   B 1 100 ? 36.866 -30.819 9.447   1.00 35.74 ?  100 VAL   B HG22 1 
ATOM   5274 H HG23 . VAL   B 1 100 ? 37.822 -30.382 8.255   1.00 35.74 ?  100 VAL   B HG23 1 
ATOM   5275 N N    A ASN   B 1 101 ? 41.647 -31.507 10.924  0.66 28.05 ?  101 ASN   B N    1 
ATOM   5276 N N    B ASN   B 1 101 ? 41.643 -31.514 10.916  0.34 28.86 ?  101 ASN   B N    1 
ATOM   5277 C CA   A ASN   B 1 101 ? 42.683 -32.051 11.799  0.66 28.95 ?  101 ASN   B CA   1 
ATOM   5278 C CA   B ASN   B 1 101 ? 42.687 -32.058 11.778  0.34 30.24 ?  101 ASN   B CA   1 
ATOM   5279 C C    A ASN   B 1 101 ? 42.895 -31.199 13.042  0.66 31.68 ?  101 ASN   B C    1 
ATOM   5280 C C    B ASN   B 1 101 ? 42.919 -31.202 13.015  0.34 32.55 ?  101 ASN   B C    1 
ATOM   5281 O O    A ASN   B 1 101 ? 43.553 -31.658 13.985  0.66 32.70 ?  101 ASN   B O    1 
ATOM   5282 O O    B ASN   B 1 101 ? 43.577 -31.664 13.954  0.34 32.88 ?  101 ASN   B O    1 
ATOM   5283 C CB   A ASN   B 1 101 ? 44.000 -32.221 11.038  0.66 28.29 ?  101 ASN   B CB   1 
ATOM   5284 C CB   B ASN   B 1 101 ? 43.991 -32.228 10.995  0.34 29.69 ?  101 ASN   B CB   1 
ATOM   5285 C CG   A ASN   B 1 101 ? 43.959 -33.378 10.056  0.66 27.48 ?  101 ASN   B CG   1 
ATOM   5286 C CG   B ASN   B 1 101 ? 43.941 -33.396 10.028  0.34 29.19 ?  101 ASN   B CG   1 
ATOM   5287 O OD1  A ASN   B 1 101 ? 43.264 -34.366 10.279  0.66 28.08 ?  101 ASN   B OD1  1 
ATOM   5288 O OD1  B ASN   B 1 101 ? 43.260 -34.391 10.275  0.34 29.33 ?  101 ASN   B OD1  1 
ATOM   5289 N ND2  A ASN   B 1 101 ? 44.696 -33.253 8.959   0.66 26.80 ?  101 ASN   B ND2  1 
ATOM   5290 N ND2  B ASN   B 1 101 ? 44.663 -33.281 8.920   0.34 28.73 ?  101 ASN   B ND2  1 
ATOM   5291 H H    A ASN   B 1 101 ? 41.919 -31.255 10.150  0.66 33.63 ?  101 ASN   B H    1 
ATOM   5292 H H    B ASN   B 1 101 ? 41.910 -31.260 10.142  0.34 34.60 ?  101 ASN   B H    1 
ATOM   5293 H HA   A ASN   B 1 101 ? 42.401 -32.931 12.092  0.66 34.71 ?  101 ASN   B HA   1 
ATOM   5294 H HA   B ASN   B 1 101 ? 42.409 -32.937 12.077  0.34 36.26 ?  101 ASN   B HA   1 
ATOM   5295 H HB2  A ASN   B 1 101 ? 44.188 -31.412 10.540  0.66 33.92 ?  101 ASN   B HB2  1 
ATOM   5296 H HB2  B ASN   B 1 101 ? 44.164 -31.424 10.483  0.34 35.60 ?  101 ASN   B HB2  1 
ATOM   5297 H HB3  A ASN   B 1 101 ? 44.711 -32.394 11.674  0.66 33.92 ?  101 ASN   B HB3  1 
ATOM   5298 H HB3  B ASN   B 1 101 ? 44.716 -32.387 11.620  0.34 35.60 ?  101 ASN   B HB3  1 
ATOM   5299 H HD21 A ASN   B 1 101 ? 44.704 -33.883 8.373   0.66 32.13 ?  101 ASN   B HD21 1 
ATOM   5300 H HD21 B ASN   B 1 101 ? 44.667 -33.917 8.341   0.34 34.45 ?  101 ASN   B HD21 1 
ATOM   5301 H HD22 A ASN   B 1 101 ? 45.166 -32.545 8.836   0.66 32.13 ?  101 ASN   B HD22 1 
ATOM   5302 H HD22 B ASN   B 1 101 ? 45.127 -32.570 8.782   0.34 34.45 ?  101 ASN   B HD22 1 
ATOM   5303 N N    A LYS   B 1 102 ? 42.360 -29.978 13.061  0.66 34.39 ?  102 LYS   B N    1 
ATOM   5304 N N    B LYS   B 1 102 ? 42.401 -29.975 13.034  0.34 34.84 ?  102 LYS   B N    1 
ATOM   5305 C CA   A LYS   B 1 102 ? 42.295 -29.148 14.255  0.66 37.42 ?  102 LYS   B CA   1 
ATOM   5306 C CA   B LYS   B 1 102 ? 42.391 -29.133 14.222  0.34 37.21 ?  102 LYS   B CA   1 
ATOM   5307 C C    A LYS   B 1 102 ? 40.900 -29.128 14.867  0.66 37.75 ?  102 LYS   B C    1 
ATOM   5308 C C    B LYS   B 1 102 ? 41.026 -29.103 14.900  0.34 37.64 ?  102 LYS   B C    1 
ATOM   5309 O O    A LYS   B 1 102 ? 40.629 -28.299 15.740  0.66 38.28 ?  102 LYS   B O    1 
ATOM   5310 O O    B LYS   B 1 102 ? 40.834 -28.335 15.848  0.34 37.99 ?  102 LYS   B O    1 
ATOM   5311 C CB   A LYS   B 1 102 ? 42.710 -27.714 13.928  0.66 40.05 ?  102 LYS   B CB   1 
ATOM   5312 C CB   B LYS   B 1 102 ? 42.822 -27.708 13.870  0.34 39.00 ?  102 LYS   B CB   1 
ATOM   5313 C CG   A LYS   B 1 102 ? 44.158 -27.537 13.520  0.66 42.41 ?  102 LYS   B CG   1 
ATOM   5314 C CG   B LYS   B 1 102 ? 44.288 -27.560 13.502  0.34 40.61 ?  102 LYS   B CG   1 
ATOM   5315 C CD   A LYS   B 1 102 ? 44.403 -26.094 13.112  0.66 44.68 ?  102 LYS   B CD   1 
ATOM   5316 C CD   B LYS   B 1 102 ? 44.597 -26.123 13.107  0.34 42.21 ?  102 LYS   B CD   1 
ATOM   5317 C CE   A LYS   B 1 102 ? 45.865 -25.813 12.824  0.66 46.29 ?  102 LYS   B CE   1 
ATOM   5318 C CE   B LYS   B 1 102 ? 46.081 -25.906 12.869  0.34 43.37 ?  102 LYS   B CE   1 
ATOM   5319 N NZ   A LYS   B 1 102 ? 46.068 -24.389 12.425  0.66 47.28 ?  102 LYS   B NZ   1 
ATOM   5320 N NZ   B LYS   B 1 102 ? 46.368 -24.498 12.469  0.34 44.09 ?  102 LYS   B NZ   1 
ATOM   5321 H H    A LYS   B 1 102 ? 42.013 -29.599 12.370  0.66 41.24 ?  102 LYS   B H    1 
ATOM   5322 H H    B LYS   B 1 102 ? 42.042 -29.600 12.349  0.34 41.78 ?  102 LYS   B H    1 
ATOM   5323 H HA   A LYS   B 1 102 ? 42.914 -29.495 14.916  0.66 44.87 ?  102 LYS   B HA   1 
ATOM   5324 H HA   B LYS   B 1 102 ? 43.030 -29.485 14.858  0.34 44.62 ?  102 LYS   B HA   1 
ATOM   5325 H HB2  A LYS   B 1 102 ? 42.158 -27.395 13.197  0.66 48.03 ?  102 LYS   B HB2  1 
ATOM   5326 H HB2  B LYS   B 1 102 ? 42.298 -27.403 13.114  0.34 46.77 ?  102 LYS   B HB2  1 
ATOM   5327 H HB3  A LYS   B 1 102 ? 42.558 -27.164 14.713  0.66 48.03 ?  102 LYS   B HB3  1 
ATOM   5328 H HB3  B LYS   B 1 102 ? 42.654 -27.136 14.635  0.34 46.77 ?  102 LYS   B HB3  1 
ATOM   5329 H HG2  A LYS   B 1 102 ? 44.736 -27.750 14.269  0.66 50.86 ?  102 LYS   B HG2  1 
ATOM   5330 H HG2  B LYS   B 1 102 ? 44.839 -27.793 14.266  0.34 48.70 ?  102 LYS   B HG2  1 
ATOM   5331 H HG3  A LYS   B 1 102 ? 44.355 -28.111 12.763  0.66 50.86 ?  102 LYS   B HG3  1 
ATOM   5332 H HG3  B LYS   B 1 102 ? 44.493 -28.136 12.749  0.34 48.70 ?  102 LYS   B HG3  1 
ATOM   5333 H HD2  A LYS   B 1 102 ? 43.895 -25.902 12.308  0.66 53.59 ?  102 LYS   B HD2  1 
ATOM   5334 H HD2  B LYS   B 1 102 ? 44.124 -25.910 12.287  0.34 50.62 ?  102 LYS   B HD2  1 
ATOM   5335 H HD3  A LYS   B 1 102 ? 44.119 -25.509 13.832  0.66 53.59 ?  102 LYS   B HD3  1 
ATOM   5336 H HD3  B LYS   B 1 102 ? 44.314 -25.529 13.820  0.34 50.62 ?  102 LYS   B HD3  1 
ATOM   5337 H HE2  A LYS   B 1 102 ? 46.387 -25.985 13.624  0.66 55.52 ?  102 LYS   B HE2  1 
ATOM   5338 H HE2  B LYS   B 1 102 ? 46.568 -26.095 13.686  0.34 52.01 ?  102 LYS   B HE2  1 
ATOM   5339 H HE3  A LYS   B 1 102 ? 46.164 -26.381 12.097  0.66 55.52 ?  102 LYS   B HE3  1 
ATOM   5340 H HE3  B LYS   B 1 102 ? 46.380 -26.492 12.156  0.34 52.01 ?  102 LYS   B HE3  1 
ATOM   5341 H HZ1  A LYS   B 1 102 ? 46.929 -24.239 12.260  0.66 56.70 ?  102 LYS   B HZ1  1 
ATOM   5342 H HZ1  B LYS   B 1 102 ? 47.241 -24.392 12.335  0.34 52.88 ?  102 LYS   B HZ1  1 
ATOM   5343 H HZ2  A LYS   B 1 102 ? 45.596 -24.209 11.691  0.66 56.70 ?  102 LYS   B HZ2  1 
ATOM   5344 H HZ2  B LYS   B 1 102 ? 45.934 -24.301 11.718  0.34 52.88 ?  102 LYS   B HZ2  1 
ATOM   5345 H HZ3  A LYS   B 1 102 ? 45.800 -23.849 13.080  0.66 56.70 ?  102 LYS   B HZ3  1 
ATOM   5346 H HZ3  B LYS   B 1 102 ? 46.104 -23.940 13.110  0.34 52.88 ?  102 LYS   B HZ3  1 
ATOM   5347 N N    A GLY   B 1 103 ? 40.005 -30.001 14.411  0.66 37.90 ?  103 GLY   B N    1 
ATOM   5348 N N    B GLY   B 1 103 ? 40.075 -29.909 14.431  0.34 37.89 ?  103 GLY   B N    1 
ATOM   5349 C CA   A GLY   B 1 103 ? 38.665 -30.084 14.950  0.66 38.29 ?  103 GLY   B CA   1 
ATOM   5350 C CA   B GLY   B 1 103 ? 38.760 -29.989 15.032  0.34 38.18 ?  103 GLY   B CA   1 
ATOM   5351 C C    A GLY   B 1 103 ? 37.711 -29.005 14.487  0.66 38.14 ?  103 GLY   B C    1 
ATOM   5352 C C    B GLY   B 1 103 ? 37.766 -28.952 14.556  0.34 38.10 ?  103 GLY   B C    1 
ATOM   5353 O O    A GLY   B 1 103 ? 36.569 -28.971 14.963  0.66 38.51 ?  103 GLY   B O    1 
ATOM   5354 O O    B GLY   B 1 103 ? 36.650 -28.901 15.088  0.34 38.48 ?  103 GLY   B O    1 
ATOM   5355 H H    A GLY   B 1 103 ? 40.156 -30.561 13.779  0.66 45.45 ?  103 GLY   B H    1 
ATOM   5356 H H    B GLY   B 1 103 ? 40.174 -30.426 13.752  0.34 45.44 ?  103 GLY   B H    1 
ATOM   5357 H HA2  A GLY   B 1 103 ? 38.282 -30.942 14.705  0.66 45.93 ?  103 GLY   B HA2  1 
ATOM   5358 H HA2  B GLY   B 1 103 ? 38.391 -30.871 14.859  0.34 45.78 ?  103 GLY   B HA2  1 
ATOM   5359 H HA3  A GLY   B 1 103 ? 38.711 -30.043 15.917  0.66 45.93 ?  103 GLY   B HA3  1 
ATOM   5360 H HA3  B GLY   B 1 103 ? 38.846 -29.885 15.991  0.34 45.78 ?  103 GLY   B HA3  1 
ATOM   5361 N N    . GLU   B 1 104 ? 38.130 -28.128 13.578  1.00 37.20 ?  104 GLU   B N    1 
ATOM   5362 C CA   . GLU   B 1 104 ? 37.257 -27.061 13.117  1.00 35.40 ?  104 GLU   B CA   1 
ATOM   5363 C C    . GLU   B 1 104 ? 36.082 -27.620 12.317  1.00 35.84 ?  104 GLU   B C    1 
ATOM   5364 O O    . GLU   B 1 104 ? 36.128 -28.731 11.780  1.00 36.79 ?  104 GLU   B O    1 
ATOM   5365 C CB   . GLU   B 1 104 ? 38.053 -26.053 12.287  1.00 33.92 ?  104 GLU   B CB   1 
ATOM   5366 C CG   . GLU   B 1 104 ? 39.157 -25.390 13.093  1.00 32.71 ?  104 GLU   B CG   1 
ATOM   5367 C CD   . GLU   B 1 104 ? 40.066 -24.486 12.278  1.00 31.53 ?  104 GLU   B CD   1 
ATOM   5368 O OE1  . GLU   B 1 104 ? 40.078 -24.578 11.032  1.00 29.91 ?  104 GLU   B OE1  1 
ATOM   5369 O OE2  . GLU   B 1 104 ? 40.779 -23.672 12.898  1.00 31.85 -1 104 GLU   B OE2  1 
ATOM   5370 H H    A GLU   B 1 104 ? 38.908 -28.133 13.215  0.66 44.61 ?  104 GLU   B H    1 
ATOM   5371 H H    B GLU   B 1 104 ? 38.886 -28.161 13.172  0.34 44.61 ?  104 GLU   B H    1 
ATOM   5372 H HA   . GLU   B 1 104 ? 36.896 -26.596 13.888  1.00 42.45 ?  104 GLU   B HA   1 
ATOM   5373 H HB2  . GLU   B 1 104 ? 38.457 -26.512 11.536  1.00 40.67 ?  104 GLU   B HB2  1 
ATOM   5374 H HB3  . GLU   B 1 104 ? 37.450 -25.360 11.971  1.00 40.67 ?  104 GLU   B HB3  1 
ATOM   5375 H HG2  . GLU   B 1 104 ? 38.750 -24.849 13.788  1.00 39.22 ?  104 GLU   B HG2  1 
ATOM   5376 H HG3  . GLU   B 1 104 ? 39.707 -26.080 13.493  1.00 39.22 ?  104 GLU   B HG3  1 
ATOM   5377 N N    . ASP   B 1 105 ? 35.017 -26.822 12.242  1.00 34.97 ?  105 ASP   B N    1 
ATOM   5378 C CA   . ASP   B 1 105 ? 33.746 -27.280 11.697  1.00 35.32 ?  105 ASP   B CA   1 
ATOM   5379 C C    . ASP   B 1 105 ? 33.806 -27.318 10.177  1.00 32.46 ?  105 ASP   B C    1 
ATOM   5380 O O    . ASP   B 1 105 ? 33.997 -26.282 9.531   1.00 31.85 ?  105 ASP   B O    1 
ATOM   5381 C CB   . ASP   B 1 105 ? 32.621 -26.352 12.150  1.00 38.75 ?  105 ASP   B CB   1 
ATOM   5382 C CG   . ASP   B 1 105 ? 31.252 -26.873 11.769  1.00 41.43 ?  105 ASP   B CG   1 
ATOM   5383 O OD1  . ASP   B 1 105 ? 31.180 -27.949 11.140  1.00 41.71 ?  105 ASP   B OD1  1 
ATOM   5384 O OD2  . ASP   B 1 105 ? 30.245 -26.210 12.101  1.00 42.78 -1 105 ASP   B OD2  1 
ATOM   5385 H H    . ASP   B 1 105 ? 35.007 -26.003 12.503  1.00 41.93 ?  105 ASP   B H    1 
ATOM   5386 H HA   . ASP   B 1 105 ? 33.556 -28.175 12.018  1.00 42.35 ?  105 ASP   B HA   1 
ATOM   5387 H HB2  . ASP   B 1 105 ? 32.656 -26.257 13.113  1.00 46.47 ?  105 ASP   B HB2  1 
ATOM   5388 H HB3  . ASP   B 1 105 ? 32.732 -25.487 11.725  1.00 46.47 ?  105 ASP   B HB3  1 
ATOM   5389 N N    A ILE   B 1 106 ? 33.612 -28.512 9.609   0.66 31.23 ?  106 ILE   B N    1 
ATOM   5390 N N    B ILE   B 1 106 ? 33.627 -28.513 9.607   0.34 31.93 ?  106 ILE   B N    1 
ATOM   5391 C CA   A ILE   B 1 106 ? 33.597 -28.684 8.162   0.66 29.67 ?  106 ILE   B CA   1 
ATOM   5392 C CA   B ILE   B 1 106 ? 33.642 -28.675 8.158   0.34 31.26 ?  106 ILE   B CA   1 
ATOM   5393 C C    A ILE   B 1 106 ? 32.513 -27.842 7.501   0.66 27.31 ?  106 ILE   B C    1 
ATOM   5394 C C    B ILE   B 1 106 ? 32.537 -27.864 7.493   0.34 30.13 ?  106 ILE   B C    1 
ATOM   5395 O O    A ILE   B 1 106 ? 32.611 -27.538 6.308   0.66 26.46 ?  106 ILE   B O    1 
ATOM   5396 O O    B ILE   B 1 106 ? 32.609 -27.590 6.290   0.34 30.12 ?  106 ILE   B O    1 
ATOM   5397 C CB   A ILE   B 1 106 ? 33.455 -30.186 7.821   0.66 30.28 ?  106 ILE   B CB   1 
ATOM   5398 C CB   B ILE   B 1 106 ? 33.561 -30.178 7.802   0.34 31.64 ?  106 ILE   B CB   1 
ATOM   5399 C CG1  A ILE   B 1 106 ? 33.692 -30.442 6.331   0.66 30.59 ?  106 ILE   B CG1  1 
ATOM   5400 C CG1  B ILE   B 1 106 ? 33.832 -30.407 6.312   0.34 31.75 ?  106 ILE   B CG1  1 
ATOM   5401 C CG2  A ILE   B 1 106 ? 32.083 -30.702 8.239   0.66 31.06 ?  106 ILE   B CG2  1 
ATOM   5402 C CG2  B ILE   B 1 106 ? 32.202 -30.746 8.186   0.34 32.07 ?  106 ILE   B CG2  1 
ATOM   5403 C CD1  A ILE   B 1 106 ? 35.051 -29.997 5.852   0.66 30.58 ?  106 ILE   B CD1  1 
ATOM   5404 C CD1  B ILE   B 1 106 ? 35.168 -29.875 5.851   0.34 31.74 ?  106 ILE   B CD1  1 
ATOM   5405 H H    A ILE   B 1 106 ? 33.482 -29.239 10.047  0.66 37.45 ?  106 ILE   B H    1 
ATOM   5406 H H    B ILE   B 1 106 ? 33.494 -29.244 10.040  0.34 38.29 ?  106 ILE   B H    1 
ATOM   5407 H HA   A ILE   B 1 106 ? 34.443 -28.382 7.813   0.66 35.57 ?  106 ILE   B HA   1 
ATOM   5408 H HA   B ILE   B 1 106 ? 34.483 -28.337 7.829   0.34 37.48 ?  106 ILE   B HA   1 
ATOM   5409 H HB   A ILE   B 1 106 ? 34.122 -30.676 8.323   0.66 36.31 ?  106 ILE   B HB   1 
ATOM   5410 H HB   B ILE   B 1 106 ? 34.239 -30.649 8.309   0.34 37.94 ?  106 ILE   B HB   1 
ATOM   5411 H HG12 A ILE   B 1 106 ? 33.620 -31.397 6.162   0.66 36.68 ?  106 ILE   B HG12 1 
ATOM   5412 H HG12 B ILE   B 1 106 ? 33.819 -31.364 6.135   0.34 38.07 ?  106 ILE   B HG12 1 
ATOM   5413 H HG13 A ILE   B 1 106 ? 33.024 -29.968 5.816   0.66 36.68 ?  106 ILE   B HG13 1 
ATOM   5414 H HG13 B ILE   B 1 106 ? 33.140 -29.971 5.793   0.34 38.07 ?  106 ILE   B HG13 1 
ATOM   5415 H HG21 A ILE   B 1 106 ? 32.070 -31.669 8.156   0.66 37.24 ?  106 ILE   B HG21 1 
ATOM   5416 H HG21 B ILE   B 1 106 ? 32.228 -31.712 8.097   0.34 38.45 ?  106 ILE   B HG21 1 
ATOM   5417 H HG22 A ILE   B 1 106 ? 31.917 -30.449 9.160   0.66 37.24 ?  106 ILE   B HG22 1 
ATOM   5418 H HG22 B ILE   B 1 106 ? 32.009 -30.504 9.105   0.34 38.45 ?  106 ILE   B HG22 1 
ATOM   5419 H HG23 A ILE   B 1 106 ? 31.406 -30.314 7.663   0.66 37.24 ?  106 ILE   B HG23 1 
ATOM   5420 H HG23 B ILE   B 1 106 ? 31.526 -30.378 7.597   0.34 38.45 ?  106 ILE   B HG23 1 
ATOM   5421 H HD11 A ILE   B 1 106 ? 35.234 -30.410 4.995   0.66 36.67 ?  106 ILE   B HD11 1 
ATOM   5422 H HD11 B ILE   B 1 106 ? 35.390 -30.277 4.999   0.34 38.06 ?  106 ILE   B HD11 1 
ATOM   5423 H HD12 A ILE   B 1 106 ? 35.052 -29.031 5.760   0.66 36.67 ?  106 ILE   B HD12 1 
ATOM   5424 H HD12 B ILE   B 1 106 ? 35.107 -28.911 5.757   0.34 38.06 ?  106 ILE   B HD12 1 
ATOM   5425 H HD13 A ILE   B 1 106 ? 35.720 -30.270 6.500   0.66 36.67 ?  106 ILE   B HD13 1 
ATOM   5426 H HD13 B ILE   B 1 106 ? 35.842 -30.102 6.511   0.34 38.06 ?  106 ILE   B HD13 1 
ATOM   5427 N N    A GLN   B 1 107 ? 31.479 -27.449 8.251   0.66 27.47 ?  107 GLN   B N    1 
ATOM   5428 N N    B GLN   B 1 107 ? 31.511 -27.470 8.250   0.34 29.51 ?  107 GLN   B N    1 
ATOM   5429 C CA   A GLN   B 1 107 ? 30.393 -26.661 7.675   0.66 27.06 ?  107 GLN   B CA   1 
ATOM   5430 C CA   B GLN   B 1 107 ? 30.415 -26.685 7.691   0.34 28.63 ?  107 GLN   B CA   1 
ATOM   5431 C C    A GLN   B 1 107 ? 30.867 -25.307 7.171   0.66 24.88 ?  107 GLN   B C    1 
ATOM   5432 C C    B GLN   B 1 107 ? 30.871 -25.323 7.180   0.34 25.85 ?  107 GLN   B C    1 
ATOM   5433 O O    A GLN   B 1 107 ? 30.212 -24.725 6.302   0.66 25.01 ?  107 GLN   B O    1 
ATOM   5434 O O    B GLN   B 1 107 ? 30.199 -24.746 6.319   0.34 25.87 ?  107 GLN   B O    1 
ATOM   5435 C CB   A GLN   B 1 107 ? 29.268 -26.471 8.696   0.66 30.62 ?  107 GLN   B CB   1 
ATOM   5436 C CB   B GLN   B 1 107 ? 29.314 -26.519 8.744   0.34 31.08 ?  107 GLN   B CB   1 
ATOM   5437 C CG   A GLN   B 1 107 ? 27.932 -26.022 8.099   0.66 34.12 ?  107 GLN   B CG   1 
ATOM   5438 C CG   B GLN   B 1 107 ? 27.959 -26.091 8.192   0.34 33.33 ?  107 GLN   B CG   1 
ATOM   5439 C CD   A GLN   B 1 107 ? 27.815 -24.511 7.961   0.66 36.69 ?  107 GLN   B CD   1 
ATOM   5440 C CD   B GLN   B 1 107 ? 27.811 -24.584 8.087   0.34 35.09 ?  107 GLN   B CD   1 
ATOM   5441 O OE1  A GLN   B 1 107 ? 28.624 -23.762 8.509   0.66 37.69 ?  107 GLN   B OE1  1 
ATOM   5442 O OE1  B GLN   B 1 107 ? 28.591 -23.828 8.667   0.34 35.69 ?  107 GLN   B OE1  1 
ATOM   5443 N NE2  A GLN   B 1 107 ? 26.797 -24.059 7.230   0.66 37.65 ?  107 GLN   B NE2  1 
ATOM   5444 N NE2  B GLN   B 1 107 ? 26.800 -24.140 7.346   0.34 35.78 ?  107 GLN   B NE2  1 
ATOM   5445 H H    A GLN   B 1 107 ? 31.384 -27.615 9.082   0.66 32.94 ?  107 GLN   B H    1 
ATOM   5446 H H    B GLN   B 1 107 ? 31.422 -27.655 9.083   0.34 35.38 ?  107 GLN   B H    1 
ATOM   5447 H HA   A GLN   B 1 107 ? 30.027 -27.140 6.915   0.66 32.44 ?  107 GLN   B HA   1 
ATOM   5448 H HA   B GLN   B 1 107 ? 30.036 -27.169 6.941   0.34 34.32 ?  107 GLN   B HA   1 
ATOM   5449 H HB2  A GLN   B 1 107 ? 29.121 -27.313 9.142   0.66 36.72 ?  107 GLN   B HB2  1 
ATOM   5450 H HB2  B GLN   B 1 107 ? 29.190 -27.368 9.193   0.34 37.27 ?  107 GLN   B HB2  1 
ATOM   5451 H HB3  A GLN   B 1 107 ? 29.545 -25.800 9.339   0.66 36.72 ?  107 GLN   B HB3  1 
ATOM   5452 H HB3  B GLN   B 1 107 ? 29.598 -25.851 9.387   0.34 37.27 ?  107 GLN   B HB3  1 
ATOM   5453 H HG2  A GLN   B 1 107 ? 27.832 -26.409 7.215   0.66 40.91 ?  107 GLN   B HG2  1 
ATOM   5454 H HG2  B GLN   B 1 107 ? 27.845 -26.465 7.305   0.34 39.97 ?  107 GLN   B HG2  1 
ATOM   5455 H HG3  A GLN   B 1 107 ? 27.213 -26.330 8.675   0.66 40.91 ?  107 GLN   B HG3  1 
ATOM   5456 H HG3  B GLN   B 1 107 ? 27.260 -26.423 8.781   0.34 39.97 ?  107 GLN   B HG3  1 
ATOM   5457 H HE21 A GLN   B 1 107 ? 26.249 -24.612 6.862   0.66 45.15 ?  107 GLN   B HE21 1 
ATOM   5458 H HE21 B GLN   B 1 107 ? 26.275 -24.698 6.954   0.34 42.91 ?  107 GLN   B HE21 1 
ATOM   5459 H HE22 A GLN   B 1 107 ? 26.682 -23.212 7.126   0.66 45.15 ?  107 GLN   B HE22 1 
ATOM   5460 H HE22 B GLN   B 1 107 ? 26.671 -23.294 7.258   0.34 42.91 ?  107 GLN   B HE22 1 
ATOM   5461 N N    . LEU   B 1 108 ? 31.994 -24.797 7.681   1.00 23.22 ?  108 LEU   B N    1 
ATOM   5462 C CA   . LEU   B 1 108 ? 32.514 -23.499 7.245   1.00 20.54 ?  108 LEU   B CA   1 
ATOM   5463 C C    . LEU   B 1 108 ? 33.147 -23.541 5.863   1.00 17.67 ?  108 LEU   B C    1 
ATOM   5464 O O    . LEU   B 1 108 ? 33.578 -22.496 5.363   1.00 16.52 ?  108 LEU   B O    1 
ATOM   5465 C CB   . LEU   B 1 108 ? 33.514 -22.964 8.271   1.00 20.86 ?  108 LEU   B CB   1 
ATOM   5466 C CG   . LEU   B 1 108 ? 32.885 -22.409 9.551   1.00 22.59 ?  108 LEU   B CG   1 
ATOM   5467 C CD1  . LEU   B 1 108 ? 33.880 -22.409 10.695  1.00 23.20 ?  108 LEU   B CD1  1 
ATOM   5468 C CD2  . LEU   B 1 108 ? 32.366 -21.000 9.307   1.00 23.35 ?  108 LEU   B CD2  1 
ATOM   5469 H H    A LEU   B 1 108 ? 32.460 -25.176 8.291   0.66 27.83 ?  108 LEU   B H    1 
ATOM   5470 H H    B LEU   B 1 108 ? 32.469 -25.172 8.287   0.34 27.83 ?  108 LEU   B H    1 
ATOM   5471 H HA   . LEU   B 1 108 ? 31.776 -22.875 7.205   1.00 24.61 ?  108 LEU   B HA   1 
ATOM   5472 H HB2  . LEU   B 1 108 ? 34.108 -23.681 8.531   1.00 25.00 ?  108 LEU   B HB2  1 
ATOM   5473 H HB3  . LEU   B 1 108 ? 34.020 -22.246 7.865   1.00 25.00 ?  108 LEU   B HB3  1 
ATOM   5474 H HG   . LEU   B 1 108 ? 32.129 -22.963 9.809   1.00 27.08 ?  108 LEU   B HG   1 
ATOM   5475 H HD11 . LEU   B 1 108 ? 33.439 -22.092 11.501  1.00 27.82 ?  108 LEU   B HD11 1 
ATOM   5476 H HD12 . LEU   B 1 108 ? 34.202 -23.314 10.831  1.00 27.82 ?  108 LEU   B HD12 1 
ATOM   5477 H HD13 . LEU   B 1 108 ? 34.618 -21.823 10.472  1.00 27.82 ?  108 LEU   B HD13 1 
ATOM   5478 H HD21 . LEU   B 1 108 ? 31.972 -20.661 10.125  1.00 27.99 ?  108 LEU   B HD21 1 
ATOM   5479 H HD22 . LEU   B 1 108 ? 33.109 -20.437 9.038   1.00 27.99 ?  108 LEU   B HD22 1 
ATOM   5480 H HD23 . LEU   B 1 108 ? 31.700 -21.028 8.604   1.00 27.99 ?  108 LEU   B HD23 1 
ATOM   5481 N N    . LEU   B 1 109 ? 33.204 -24.713 5.237   1.00 16.31 ?  109 LEU   B N    1 
ATOM   5482 C CA   . LEU   B 1 109 ? 33.831 -24.835 3.927   1.00 15.26 ?  109 LEU   B CA   1 
ATOM   5483 C C    . LEU   B 1 109 ? 33.060 -24.063 2.859   1.00 14.72 ?  109 LEU   B C    1 
ATOM   5484 O O    . LEU   B 1 109 ? 33.668 -23.486 1.950   1.00 14.78 ?  109 LEU   B O    1 
ATOM   5485 C CB   . LEU   B 1 109 ? 33.964 -26.317 3.563   1.00 15.70 ?  109 LEU   B CB   1 
ATOM   5486 C CG   . LEU   B 1 109 ? 34.722 -26.670 2.285   1.00 15.09 ?  109 LEU   B CG   1 
ATOM   5487 C CD1  . LEU   B 1 109 ? 36.093 -26.009 2.256   1.00 14.82 ?  109 LEU   B CD1  1 
ATOM   5488 C CD2  . LEU   B 1 109 ? 34.863 -28.189 2.154   1.00 15.47 ?  109 LEU   B CD2  1 
ATOM   5489 H H    . LEU   B 1 109 ? 32.900 -25.452 5.546   1.00 19.55 ?  109 LEU   B H    1 
ATOM   5490 H HA   . LEU   B 1 109 ? 34.725 -24.461 3.968   1.00 18.29 ?  109 LEU   B HA   1 
ATOM   5491 H HB2  . LEU   B 1 109 ? 34.420 -26.766 4.292   1.00 18.81 ?  109 LEU   B HB2  1 
ATOM   5492 H HB3  . LEU   B 1 109 ? 33.071 -26.687 3.474   1.00 18.81 ?  109 LEU   B HB3  1 
ATOM   5493 H HG   . LEU   B 1 109 ? 34.215 -26.364 1.517   1.00 18.08 ?  109 LEU   B HG   1 
ATOM   5494 H HD11 . LEU   B 1 109 ? 36.603 -26.369 1.512   1.00 17.75 ?  109 LEU   B HD11 1 
ATOM   5495 H HD12 . LEU   B 1 109 ? 35.977 -25.056 2.148   1.00 17.75 ?  109 LEU   B HD12 1 
ATOM   5496 H HD13 . LEU   B 1 109 ? 36.551 -26.200 3.090   1.00 17.75 ?  109 LEU   B HD13 1 
ATOM   5497 H HD21 . LEU   B 1 109 ? 35.415 -28.392 1.379   1.00 18.53 ?  109 LEU   B HD21 1 
ATOM   5498 H HD22 . LEU   B 1 109 ? 35.279 -28.542 2.955   1.00 18.53 ?  109 LEU   B HD22 1 
ATOM   5499 H HD23 . LEU   B 1 109 ? 33.982 -28.586 2.039   1.00 18.53 ?  109 LEU   B HD23 1 
ATOM   5500 N N    . LYS   B 1 110 ? 31.726 -24.023 2.949   1.00 14.34 ?  110 LYS   B N    1 
ATOM   5501 C CA   . LYS   B 1 110 ? 30.968 -23.268 1.956   1.00 14.75 ?  110 LYS   B CA   1 
ATOM   5502 C C    . LYS   B 1 110 ? 31.302 -21.779 2.039   1.00 14.00 ?  110 LYS   B C    1 
ATOM   5503 O O    . LYS   B 1 110 ? 31.557 -21.134 1.016   1.00 13.80 ?  110 LYS   B O    1 
ATOM   5504 C CB   . LYS   B 1 110 ? 29.461 -23.515 2.109   1.00 14.90 ?  110 LYS   B CB   1 
ATOM   5505 C CG   . LYS   B 1 110 ? 28.647 -22.907 0.963   1.00 15.41 ?  110 LYS   B CG   1 
ATOM   5506 C CD   . LYS   B 1 110 ? 27.180 -23.342 0.995   1.00 15.53 ?  110 LYS   B CD   1 
ATOM   5507 C CE   . LYS   B 1 110 ? 26.418 -22.787 -0.204  1.00 16.22 ?  110 LYS   B CE   1 
ATOM   5508 N NZ   . LYS   B 1 110 ? 26.744 -23.511 -1.465  1.00 16.73 ?  110 LYS   B NZ   1 
ATOM   5509 H H    . LYS   B 1 110 ? 31.258 -24.416 3.553   1.00 17.17 ?  110 LYS   B H    1 
ATOM   5510 H HA   . LYS   B 1 110 ? 31.225 -23.574 1.075   1.00 17.67 ?  110 LYS   B HA   1 
ATOM   5511 H HB2  . LYS   B 1 110 ? 29.297 -24.470 2.123   1.00 17.85 ?  110 LYS   B HB2  1 
ATOM   5512 H HB3  . LYS   B 1 110 ? 29.156 -23.113 2.939   1.00 17.85 ?  110 LYS   B HB3  1 
ATOM   5513 H HG2  . LYS   B 1 110 ? 28.674 -21.942 1.031   1.00 18.47 ?  110 LYS   B HG2  1 
ATOM   5514 H HG3  . LYS   B 1 110 ? 29.027 -23.195 0.119   1.00 18.47 ?  110 LYS   B HG3  1 
ATOM   5515 H HD2  . LYS   B 1 110 ? 27.132 -24.314 0.968   1.00 18.61 ?  110 LYS   B HD2  1 
ATOM   5516 H HD3  . LYS   B 1 110 ? 26.764 -23.012 1.807   1.00 18.61 ?  110 LYS   B HD3  1 
ATOM   5517 H HE2  . LYS   B 1 110 ? 25.468 -22.872 -0.043  1.00 19.44 ?  110 LYS   B HE2  1 
ATOM   5518 H HE3  . LYS   B 1 110 ? 26.657 -21.854 -0.321  1.00 19.44 ?  110 LYS   B HE3  1 
ATOM   5519 H HZ1  . LYS   B 1 110 ? 26.286 -23.159 -2.141  1.00 20.05 ?  110 LYS   B HZ1  1 
ATOM   5520 H HZ2  . LYS   B 1 110 ? 27.615 -23.441 -1.638  1.00 20.05 ?  110 LYS   B HZ2  1 
ATOM   5521 H HZ3  . LYS   B 1 110 ? 26.532 -24.370 -1.385  1.00 20.05 ?  110 LYS   B HZ3  1 
ATOM   5522 N N    . SER   B 1 111 ? 31.323 -21.223 3.257   1.00 14.69 ?  111 SER   B N    1 
ATOM   5523 C CA   . SER   B 1 111 ? 31.719 -19.825 3.430   1.00 14.13 ?  111 SER   B CA   1 
ATOM   5524 C C    . SER   B 1 111 ? 33.094 -19.571 2.828   1.00 13.54 ?  111 SER   B C    1 
ATOM   5525 O O    . SER   B 1 111 ? 33.313 -18.553 2.157   1.00 13.90 ?  111 SER   B O    1 
ATOM   5526 C CB   . SER   B 1 111 ? 31.735 -19.469 4.916   1.00 15.25 ?  111 SER   B CB   1 
ATOM   5527 O OG   . SER   B 1 111 ? 30.440 -19.463 5.471   1.00 16.24 ?  111 SER   B OG   1 
ATOM   5528 H H    . SER   B 1 111 ? 31.132 -21.636 3.990   1.00 17.61 ?  111 SER   B H    1 
ATOM   5529 H HA   . SER   B 1 111 ? 31.077 -19.254 2.984   1.00 16.93 ?  111 SER   B HA   1 
ATOM   5530 H HB2  . SER   B 1 111 ? 32.266 -20.125 5.393   1.00 18.27 ?  111 SER   B HB2  1 
ATOM   5531 H HB3  . SER   B 1 111 ? 32.123 -18.589 5.025   1.00 18.27 ?  111 SER   B HB3  1 
ATOM   5532 H HG   . SER   B 1 111 ? 30.475 -19.256 6.296   1.00 19.45 ?  111 SER   B HG   1 
ATOM   5533 N N    . ALA   B 1 112 ? 34.036 -20.489 3.047   1.00 13.65 ?  112 ALA   B N    1 
ATOM   5534 C CA   . ALA   B 1 112 ? 35.380 -20.313 2.500   1.00 13.28 ?  112 ALA   B CA   1 
ATOM   5535 C C    . ALA   B 1 112 ? 35.347 -20.234 0.975   1.00 12.84 ?  112 ALA   B C    1 
ATOM   5536 O O    . ALA   B 1 112 ? 35.961 -19.344 0.371   1.00 13.28 ?  112 ALA   B O    1 
ATOM   5537 C CB   . ALA   B 1 112 ? 36.289 -21.442 2.988   1.00 13.76 ?  112 ALA   B CB   1 
ATOM   5538 H H    . ALA   B 1 112 ? 33.923 -21.208 3.509   1.00 16.36 ?  112 ALA   B H    1 
ATOM   5539 H HA   . ALA   B 1 112 ? 35.740 -19.477 2.835   1.00 15.91 ?  112 ALA   B HA   1 
ATOM   5540 H HB1  . ALA   B 1 112 ? 37.178 -21.308 2.618   1.00 16.48 ?  112 ALA   B HB1  1 
ATOM   5541 H HB2  . ALA   B 1 112 ? 36.333 -21.418 3.959   1.00 16.48 ?  112 ALA   B HB2  1 
ATOM   5542 H HB3  . ALA   B 1 112 ? 35.931 -22.290 2.693   1.00 16.48 ?  112 ALA   B HB3  1 
ATOM   5543 N N    . TYR   B 1 113 ? 34.608 -21.142 0.328   1.00 12.34 ?  113 TYR   B N    1 
ATOM   5544 C CA   . TYR   B 1 113 ? 34.528 -21.098 -1.129  1.00 12.35 ?  113 TYR   B CA   1 
ATOM   5545 C C    . TYR   B 1 113 ? 33.815 -19.847 -1.644  1.00 11.73 ?  113 TYR   B C    1 
ATOM   5546 O O    . TYR   B 1 113 ? 34.084 -19.413 -2.771  1.00 12.11 ?  113 TYR   B O    1 
ATOM   5547 C CB   . TYR   B 1 113 ? 33.856 -22.358 -1.673  1.00 12.34 ?  113 TYR   B CB   1 
ATOM   5548 C CG   . TYR   B 1 113 ? 34.822 -23.507 -1.930  1.00 12.99 ?  113 TYR   B CG   1 
ATOM   5549 C CD1  . TYR   B 1 113 ? 35.817 -23.409 -2.901  1.00 13.60 ?  113 TYR   B CD1  1 
ATOM   5550 C CD2  . TYR   B 1 113 ? 34.722 -24.690 -1.218  1.00 13.54 ?  113 TYR   B CD2  1 
ATOM   5551 C CE1  . TYR   B 1 113 ? 36.699 -24.439 -3.143  1.00 13.62 ?  113 TYR   B CE1  1 
ATOM   5552 C CE2  . TYR   B 1 113 ? 35.602 -25.744 -1.457  1.00 13.49 ?  113 TYR   B CE2  1 
ATOM   5553 C CZ   . TYR   B 1 113 ? 36.580 -25.611 -2.426  1.00 13.38 ?  113 TYR   B CZ   1 
ATOM   5554 O OH   . TYR   B 1 113 ? 37.459 -26.633 -2.691  1.00 14.39 ?  113 TYR   B OH   1 
ATOM   5555 H H    . TYR   B 1 113 ? 34.147 -21.770 0.703   1.00 14.77 ?  113 TYR   B H    1 
ATOM   5556 H HA   . TYR   B 1 113 ? 35.426 -21.076 -1.475  1.00 14.80 ?  113 TYR   B HA   1 
ATOM   5557 H HB2  . TYR   B 1 113 ? 33.195 -22.671 -1.032  1.00 14.78 ?  113 TYR   B HB2  1 
ATOM   5558 H HB3  . TYR   B 1 113 ? 33.417 -22.145 -2.513  1.00 14.78 ?  113 TYR   B HB3  1 
ATOM   5559 H HD1  . TYR   B 1 113 ? 35.897 -22.619 -3.391  1.00 16.29 ?  113 TYR   B HD1  1 
ATOM   5560 H HD2  . TYR   B 1 113 ? 34.061 -24.779 -0.573  1.00 16.22 ?  113 TYR   B HD2  1 
ATOM   5561 H HE1  . TYR   B 1 113 ? 37.355 -24.355 -3.798  1.00 16.31 ?  113 TYR   B HE1  1 
ATOM   5562 H HE2  . TYR   B 1 113 ? 35.524 -26.535 -0.976  1.00 16.16 ?  113 TYR   B HE2  1 
ATOM   5563 H HH   . TYR   B 1 113 ? 37.284 -27.295 -2.196  1.00 17.24 ?  113 TYR   B HH   1 
ATOM   5564 N N    . GLU   B 1 114 ? 32.892 -19.272 -0.862  1.00 12.29 ?  114 GLU   B N    1 
ATOM   5565 C CA   . GLU   B 1 114 ? 32.212 -18.061 -1.316  1.00 12.33 ?  114 GLU   B CA   1 
ATOM   5566 C C    . GLU   B 1 114 ? 33.198 -16.942 -1.629  1.00 12.23 ?  114 GLU   B C    1 
ATOM   5567 O O    . GLU   B 1 114 ? 32.910 -16.083 -2.468  1.00 12.57 ?  114 GLU   B O    1 
ATOM   5568 C CB   . GLU   B 1 114 ? 31.158 -17.626 -0.295  1.00 13.04 ?  114 GLU   B CB   1 
ATOM   5569 C CG   . GLU   B 1 114 ? 29.935 -18.560 -0.360  1.00 13.47 ?  114 GLU   B CG   1 
ATOM   5570 C CD   . GLU   B 1 114 ? 28.905 -18.357 0.740   1.00 13.40 ?  114 GLU   B CD   1 
ATOM   5571 O OE1  . GLU   B 1 114 ? 29.198 -17.723 1.774   1.00 13.55 ?  114 GLU   B OE1  1 
ATOM   5572 O OE2  . GLU   B 1 114 ? 27.780 -18.897 0.576   1.00 14.32 -1 114 GLU   B OE2  1 
ATOM   5573 H H    . GLU   B 1 114 ? 32.644 -19.565 -0.086  1.00 14.72 ?  114 GLU   B H    1 
ATOM   5574 H HA   . GLU   B 1 114 ? 31.741 -18.268 -2.136  1.00 14.77 ?  114 GLU   B HA   1 
ATOM   5575 H HB2  . GLU   B 1 114 ? 31.533 -17.671 0.601   1.00 15.62 ?  114 GLU   B HB2  1 
ATOM   5576 H HB3  . GLU   B 1 114 ? 30.865 -16.724 -0.493  1.00 15.62 ?  114 GLU   B HB3  1 
ATOM   5577 H HG2  . GLU   B 1 114 ? 29.485 -18.418 -1.202  1.00 16.14 ?  114 GLU   B HG2  1 
ATOM   5578 H HG3  . GLU   B 1 114 ? 30.247 -19.476 -0.302  1.00 16.14 ?  114 GLU   B HG3  1 
ATOM   5579 N N    . ASN   B 1 115 ? 34.366 -16.928 -0.981  1.00 11.92 ?  115 ASN   B N    1 
ATOM   5580 C CA   . ASN   B 1 115 ? 35.356 -15.897 -1.293  1.00 11.51 ?  115 ASN   B CA   1 
ATOM   5581 C C    . ASN   B 1 115 ? 35.759 -15.927 -2.764  1.00 12.02 ?  115 ASN   B C    1 
ATOM   5582 O O    . ASN   B 1 115 ? 36.142 -14.888 -3.326  1.00 12.02 ?  115 ASN   B O    1 
ATOM   5583 C CB   . ASN   B 1 115 ? 36.598 -16.064 -0.410  1.00 12.22 ?  115 ASN   B CB   1 
ATOM   5584 C CG   . ASN   B 1 115 ? 36.328 -15.798 1.049   1.00 12.98 ?  115 ASN   B CG   1 
ATOM   5585 O OD1  . ASN   B 1 115 ? 36.312 -14.648 1.492   1.00 14.80 ?  115 ASN   B OD1  1 
ATOM   5586 N ND2  . ASN   B 1 115 ? 36.169 -16.865 1.826   1.00 13.12 ?  115 ASN   B ND2  1 
ATOM   5587 H H    . ASN   B 1 115 ? 34.601 -17.478 -0.357  1.00 14.28 ?  115 ASN   B H    1 
ATOM   5588 H HA   . ASN   B 1 115 ? 34.978 -15.027 -1.106  1.00 13.79 ?  115 ASN   B HA   1 
ATOM   5589 H HB2  . ASN   B 1 115 ? 36.931 -16.972 -0.495  1.00 14.64 ?  115 ASN   B HB2  1 
ATOM   5590 H HB3  . ASN   B 1 115 ? 37.280 -15.436 -0.701  1.00 14.64 ?  115 ASN   B HB3  1 
ATOM   5591 H HD21 . ASN   B 1 115 ? 36.024 -16.766 2.669   1.00 15.72 ?  115 ASN   B HD21 1 
ATOM   5592 H HD22 . ASN   B 1 115 ? 36.205 -17.655 1.487   1.00 15.72 ?  115 ASN   B HD22 1 
ATOM   5593 N N    . PHE   B 1 116 ? 35.733 -17.111 -3.392  1.00 11.67 ?  116 PHE   B N    1 
ATOM   5594 C CA   . PHE   B 1 116 ? 36.157 -17.207 -4.782  1.00 12.12 ?  116 PHE   B CA   1 
ATOM   5595 C C    . PHE   B 1 116 ? 35.255 -16.377 -5.691  1.00 11.35 ?  116 PHE   B C    1 
ATOM   5596 O O    . PHE   B 1 116 ? 35.683 -15.945 -6.764  1.00 12.20 ?  116 PHE   B O    1 
ATOM   5597 C CB   . PHE   B 1 116 ? 36.115 -18.657 -5.292  1.00 11.23 ?  116 PHE   B CB   1 
ATOM   5598 C CG   . PHE   B 1 116 ? 37.190 -19.607 -4.746  1.00 11.11 ?  116 PHE   B CG   1 
ATOM   5599 C CD1  . PHE   B 1 116 ? 37.842 -19.422 -3.534  1.00 12.12 ?  116 PHE   B CD1  1 
ATOM   5600 C CD2  . PHE   B 1 116 ? 37.498 -20.746 -5.486  1.00 11.47 ?  116 PHE   B CD2  1 
ATOM   5601 C CE1  . PHE   B 1 116 ? 38.785 -20.358 -3.086  1.00 12.40 ?  116 PHE   B CE1  1 
ATOM   5602 C CE2  . PHE   B 1 116 ? 38.431 -21.675 -5.043  1.00 11.83 ?  116 PHE   B CE2  1 
ATOM   5603 C CZ   . PHE   B 1 116 ? 39.065 -21.487 -3.844  1.00 12.11 ?  116 PHE   B CZ   1 
ATOM   5604 H H    . PHE   B 1 116 ? 35.465 -17.855 -3.043  1.00 13.97 ?  116 PHE   B H    1 
ATOM   5605 H HA   . PHE   B 1 116 ? 37.064 -16.884 -4.867  1.00 14.52 ?  116 PHE   B HA   1 
ATOM   5606 H HB2  . PHE   B 1 116 ? 35.244 -19.036 -5.063  1.00 13.45 ?  116 PHE   B HB2  1 
ATOM   5607 H HB3  . PHE   B 1 116 ? 36.203 -18.645 -6.259  1.00 13.45 ?  116 PHE   B HB3  1 
ATOM   5608 H HD1  . PHE   B 1 116 ? 37.640 -18.682 -3.013  1.00 14.52 ?  116 PHE   B HD1  1 
ATOM   5609 H HD2  . PHE   B 1 116 ? 37.057 -20.894 -6.297  1.00 13.74 ?  116 PHE   B HD2  1 
ATOM   5610 H HE1  . PHE   B 1 116 ? 39.221 -20.230 -2.276  1.00 14.85 ?  116 PHE   B HE1  1 
ATOM   5611 H HE2  . PHE   B 1 116 ? 38.622 -22.422 -5.565  1.00 14.16 ?  116 PHE   B HE2  1 
ATOM   5612 H HZ   . PHE   B 1 116 ? 39.706 -22.100 -3.560  1.00 14.50 ?  116 PHE   B HZ   1 
ATOM   5613 N N    . ASN   B 1 117 ? 33.987 -16.173 -5.300  1.00 11.83 ?  117 ASN   B N    1 
ATOM   5614 C CA   . ASN   B 1 117 ? 33.034 -15.467 -6.155  1.00 12.53 ?  117 ASN   B CA   1 
ATOM   5615 C C    . ASN   B 1 117 ? 33.348 -13.987 -6.306  1.00 12.69 ?  117 ASN   B C    1 
ATOM   5616 O O    . ASN   B 1 117 ? 32.755 -13.338 -7.171  1.00 13.74 ?  117 ASN   B O    1 
ATOM   5617 C CB   . ASN   B 1 117 ? 31.608 -15.692 -5.659  1.00 13.18 ?  117 ASN   B CB   1 
ATOM   5618 C CG   . ASN   B 1 117 ? 31.162 -17.106 -5.913  1.00 12.90 ?  117 ASN   B CG   1 
ATOM   5619 O OD1  . ASN   B 1 117 ? 31.524 -17.692 -6.936  1.00 13.84 ?  117 ASN   B OD1  1 
ATOM   5620 N ND2  . ASN   B 1 117 ? 30.425 -17.689 -4.975  1.00 12.94 ?  117 ASN   B ND2  1 
ATOM   5621 H H    . ASN   B 1 117 ? 33.667 -16.431 -4.544  1.00 14.17 ?  117 ASN   B H    1 
ATOM   5622 H HA   . ASN   B 1 117 ? 33.088 -15.861 -7.035  1.00 15.00 ?  117 ASN   B HA   1 
ATOM   5623 H HB2  . ASN   B 1 117 ? 31.567 -15.529 -4.700  1.00 15.78 ?  117 ASN   B HB2  1 
ATOM   5624 H HB3  . ASN   B 1 117 ? 31.006 -15.090 -6.124  1.00 15.78 ?  117 ASN   B HB3  1 
ATOM   5625 H HD21 . ASN   B 1 117 ? 30.153 -18.501 -5.081  1.00 15.49 ?  117 ASN   B HD21 1 
ATOM   5626 H HD22 . ASN   B 1 117 ? 30.201 -17.255 -4.266  1.00 15.49 ?  117 ASN   B HD22 1 
ATOM   5627 N N    . GLN   B 1 118 ? 34.286 -13.465 -5.534  1.00 12.57 ?  118 GLN   B N    1 
ATOM   5628 C CA   . GLN   B 1 118 ? 34.721 -12.082 -5.677  1.00 13.48 ?  118 GLN   B CA   1 
ATOM   5629 C C    . GLN   B 1 118 ? 35.790 -11.894 -6.749  1.00 13.52 ?  118 GLN   B C    1 
ATOM   5630 O O    . GLN   B 1 118 ? 36.265 -10.767 -6.925  1.00 14.98 ?  118 GLN   B O    1 
ATOM   5631 C CB   . GLN   B 1 118 ? 35.204 -11.551 -4.323  1.00 13.75 ?  118 GLN   B CB   1 
ATOM   5632 C CG   . GLN   B 1 118 ? 34.118 -11.577 -3.250  1.00 14.19 ?  118 GLN   B CG   1 
ATOM   5633 C CD   . GLN   B 1 118 ? 32.940 -10.679 -3.589  1.00 14.05 ?  118 GLN   B CD   1 
ATOM   5634 O OE1  . GLN   B 1 118 ? 33.120 -9.540  -4.032  1.00 15.00 ?  118 GLN   B OE1  1 
ATOM   5635 N NE2  . GLN   B 1 118 ? 31.729 -11.185 -3.387  1.00 14.51 ?  118 GLN   B NE2  1 
ATOM   5636 H H    . GLN   B 1 118 ? 34.703 -13.892 -4.915  1.00 15.06 ?  118 GLN   B H    1 
ATOM   5637 H HA   . GLN   B 1 118 ? 33.960 -11.546 -5.942  1.00 16.15 ?  118 GLN   B HA   1 
ATOM   5638 H HB2  . GLN   B 1 118 ? 35.945 -12.088 -4.013  1.00 16.47 ?  118 GLN   B HB2  1 
ATOM   5639 H HB3  . GLN   B 1 118 ? 35.486 -10.624 -4.425  1.00 16.47 ?  118 GLN   B HB3  1 
ATOM   5640 H HG2  . GLN   B 1 118 ? 33.791 -12.492 -3.159  1.00 17.00 ?  118 GLN   B HG2  1 
ATOM   5641 H HG3  . GLN   B 1 118 ? 34.497 -11.283 -2.406  1.00 17.00 ?  118 GLN   B HG3  1 
ATOM   5642 H HE21 . GLN   B 1 118 ? 31.643 -11.985 -3.071  1.00 17.38 ?  118 GLN   B HE21 1 
ATOM   5643 H HE22 . GLN   B 1 118 ? 31.037 -10.716 -3.561  1.00 17.38 ?  118 GLN   B HE22 1 
ATOM   5644 N N    . HIS   B 1 119 ? 36.149 -12.949 -7.487  1.00 12.64 ?  119 HIS   B N    1 
ATOM   5645 C CA   . HIS   B 1 119 ? 37.198 -12.896 -8.498  1.00 12.60 ?  119 HIS   B CA   1 
ATOM   5646 C C    . HIS   B 1 119 ? 36.706 -13.616 -9.742  1.00 13.22 ?  119 HIS   B C    1 
ATOM   5647 O O    . HIS   B 1 119 ? 36.188 -14.730 -9.646  1.00 13.52 ?  119 HIS   B O    1 
ATOM   5648 C CB   . HIS   B 1 119 ? 38.467 -13.541 -7.940  1.00 13.30 ?  119 HIS   B CB   1 
ATOM   5649 C CG   . HIS   B 1 119 ? 38.938 -12.855 -6.702  1.00 14.13 ?  119 HIS   B CG   1 
ATOM   5650 N ND1  . HIS   B 1 119 ? 39.741 -11.733 -6.735  1.00 15.74 ?  119 HIS   B ND1  1 
ATOM   5651 C CD2  . HIS   B 1 119 ? 38.636 -13.067 -5.400  1.00 15.14 ?  119 HIS   B CD2  1 
ATOM   5652 C CE1  . HIS   B 1 119 ? 39.945 -11.313 -5.500  1.00 16.35 ?  119 HIS   B CE1  1 
ATOM   5653 N NE2  . HIS   B 1 119 ? 39.282 -12.100 -4.673  1.00 16.64 ?  119 HIS   B NE2  1 
ATOM   5654 H H    . HIS   B 1 119 ? 35.781 -13.726 -7.423  1.00 15.14 ?  119 HIS   B H    1 
ATOM   5655 H HA   . HIS   B 1 119 ? 37.392 -11.970 -8.724  1.00 15.09 ?  119 HIS   B HA   1 
ATOM   5656 H HB2  . HIS   B 1 119 ? 38.282 -14.468 -7.727  1.00 15.93 ?  119 HIS   B HB2  1 
ATOM   5657 H HB3  . HIS   B 1 119 ? 39.169 -13.484 -8.609  1.00 15.93 ?  119 HIS   B HB3  1 
ATOM   5658 H HD2  . HIS   B 1 119 ? 38.101 -13.751 -5.064  1.00 18.14 ?  119 HIS   B HD2  1 
ATOM   5659 H HE1  . HIS   B 1 119 ? 40.478 -10.595 -5.253  1.00 19.59 ?  119 HIS   B HE1  1 
ATOM   5660 H HE2  . HIS   B 1 119 ? 39.278 -12.038 -3.815  1.00 19.95 ?  119 HIS   B HE2  1 
ATOM   5661 N N    A GLU   B 1 120 ? 36.862 -12.989 -10.908 0.66 13.38 ?  120 GLU   B N    1 
ATOM   5662 N N    B GLU   B 1 120 ? 36.872 -12.984 -10.906 0.34 14.46 ?  120 GLU   B N    1 
ATOM   5663 C CA   A GLU   B 1 120 ? 36.282 -13.563 -12.117 0.66 15.07 ?  120 GLU   B CA   1 
ATOM   5664 C CA   B GLU   B 1 120 ? 36.303 -13.544 -12.128 0.34 16.09 ?  120 GLU   B CA   1 
ATOM   5665 C C    A GLU   B 1 120 ? 36.956 -14.869 -12.526 0.66 13.96 ?  120 GLU   B C    1 
ATOM   5666 C C    B GLU   B 1 120 ? 36.960 -14.862 -12.522 0.34 14.68 ?  120 GLU   B C    1 
ATOM   5667 O O    A GLU   B 1 120 ? 36.291 -15.745 -13.095 0.66 14.32 ?  120 GLU   B O    1 
ATOM   5668 O O    B GLU   B 1 120 ? 36.286 -15.742 -13.073 0.34 14.76 ?  120 GLU   B O    1 
ATOM   5669 C CB   A GLU   B 1 120 ? 36.307 -12.546 -13.256 0.66 19.54 ?  120 GLU   B CB   1 
ATOM   5670 C CB   B GLU   B 1 120 ? 36.393 -12.528 -13.267 0.34 19.74 ?  120 GLU   B CB   1 
ATOM   5671 C CG   A GLU   B 1 120 ? 35.268 -11.448 -13.100 0.66 25.57 ?  120 GLU   B CG   1 
ATOM   5672 C CG   B GLU   B 1 120 ? 35.496 -11.315 -13.077 0.34 23.99 ?  120 GLU   B CG   1 
ATOM   5673 C CD   A GLU   B 1 120 ? 35.176 -10.539 -14.307 0.66 30.08 ?  120 GLU   B CD   1 
ATOM   5674 C CD   B GLU   B 1 120 ? 35.452 -10.421 -14.303 0.34 27.37 ?  120 GLU   B CD   1 
ATOM   5675 O OE1  A GLU   B 1 120 ? 36.213 -10.310 -14.967 0.66 31.83 ?  120 GLU   B OE1  1 
ATOM   5676 O OE1  B GLU   B 1 120 ? 36.410 -10.465 -15.105 0.34 28.72 ?  120 GLU   B OE1  1 
ATOM   5677 O OE2  A GLU   B 1 120 ? 34.063 -10.049 -14.593 0.66 32.54 -1 120 GLU   B OE2  1 
ATOM   5678 O OE2  B GLU   B 1 120 ? 34.468 -9.669  -14.462 0.34 28.63 -1 120 GLU   B OE2  1 
ATOM   5679 H H    A GLU   B 1 120 ? 37.287 -12.243 -11.020 0.66 16.02 ?  120 GLU   B H    1 
ATOM   5680 H H    B GLU   B 1 120 ? 37.302 -12.243 -11.010 0.34 17.32 ?  120 GLU   B H    1 
ATOM   5681 H HA   A GLU   B 1 120 ? 35.357 -13.770 -11.932 0.66 18.05 ?  120 GLU   B HA   1 
ATOM   5682 H HA   B GLU   B 1 120 ? 35.368 -13.725 -11.971 0.34 19.27 ?  120 GLU   B HA   1 
ATOM   5683 H HB2  A GLU   B 1 120 ? 37.178 -12.126 -13.287 0.66 23.42 ?  120 GLU   B HB2  1 
ATOM   5684 H HB2  B GLU   B 1 120 ? 37.305 -12.211 -13.337 0.34 23.66 ?  120 GLU   B HB2  1 
ATOM   5685 H HB3  A GLU   B 1 120 ? 36.129 -13.008 -14.089 0.66 23.42 ?  120 GLU   B HB3  1 
ATOM   5686 H HB3  B GLU   B 1 120 ? 36.130 -12.964 -14.093 0.34 23.66 ?  120 GLU   B HB3  1 
ATOM   5687 H HG2  A GLU   B 1 120 ? 34.396 -11.854 -12.963 0.66 30.65 ?  120 GLU   B HG2  1 
ATOM   5688 H HG2  B GLU   B 1 120 ? 34.595 -11.618 -12.865 0.34 28.76 ?  120 GLU   B HG2  1 
ATOM   5689 H HG3  A GLU   B 1 120 ? 35.500 -10.896 -12.340 0.66 30.65 ?  120 GLU   B HG3  1 
ATOM   5690 H HG3  B GLU   B 1 120 ? 35.840 -10.775 -12.351 0.34 28.76 ?  120 GLU   B HG3  1 
ATOM   5691 N N    . VAL   B 1 121 ? 38.255 -15.019 -12.255 1.00 13.74 ?  121 VAL   B N    1 
ATOM   5692 C CA   . VAL   B 1 121 ? 38.991 -16.232 -12.603 1.00 13.39 ?  121 VAL   B CA   1 
ATOM   5693 C C    . VAL   B 1 121 ? 40.108 -16.446 -11.587 1.00 12.78 ?  121 VAL   B C    1 
ATOM   5694 O O    . VAL   B 1 121 ? 40.790 -15.493 -11.195 1.00 13.44 ?  121 VAL   B O    1 
ATOM   5695 C CB   . VAL   B 1 121 ? 39.508 -16.171 -14.059 1.00 15.44 ?  121 VAL   B CB   1 
ATOM   5696 C CG1  . VAL   B 1 121 ? 40.374 -14.930 -14.288 1.00 16.95 ?  121 VAL   B CG1  1 
ATOM   5697 C CG2  . VAL   B 1 121 ? 40.256 -17.445 -14.427 1.00 17.05 ?  121 VAL   B CG2  1 
ATOM   5698 H H    A VAL   B 1 121 ? 38.747 -14.418 -11.876 0.66 16.46 ?  121 VAL   B H    1 
ATOM   5699 H H    B VAL   B 1 121 ? 38.748 -14.420 -11.874 0.34 16.46 ?  121 VAL   B H    1 
ATOM   5700 H HA   . VAL   B 1 121 ? 38.380 -16.982 -12.544 1.00 16.04 ?  121 VAL   B HA   1 
ATOM   5701 H HB   . VAL   B 1 121 ? 38.744 -16.105 -14.656 1.00 18.50 ?  121 VAL   B HB   1 
ATOM   5702 H HG11 . VAL   B 1 121 ? 40.699 -14.936 -15.203 1.00 20.31 ?  121 VAL   B HG11 1 
ATOM   5703 H HG12 . VAL   B 1 121 ? 39.837 -14.137 -14.135 1.00 20.31 ?  121 VAL   B HG12 1 
ATOM   5704 H HG13 . VAL   B 1 121 ? 41.123 -14.949 -13.672 1.00 20.31 ?  121 VAL   B HG13 1 
ATOM   5705 H HG21 . VAL   B 1 121 ? 40.461 -17.431 -15.378 1.00 20.43 ?  121 VAL   B HG21 1 
ATOM   5706 H HG22 . VAL   B 1 121 ? 41.082 -17.490 -13.917 1.00 20.43 ?  121 VAL   B HG22 1 
ATOM   5707 H HG23 . VAL   B 1 121 ? 39.700 -18.212 -14.223 1.00 20.43 ?  121 VAL   B HG23 1 
ATOM   5708 N N    . LEU   B 1 122 ? 40.291 -17.704 -11.164 1.00 12.20 ?  122 LEU   B N    1 
ATOM   5709 C CA   . LEU   B 1 122 ? 41.267 -18.067 -10.143 1.00 11.61 ?  122 LEU   B CA   1 
ATOM   5710 C C    . LEU   B 1 122 ? 41.918 -19.399 -10.477 1.00 11.79 ?  122 LEU   B C    1 
ATOM   5711 O O    . LEU   B 1 122 ? 41.259 -20.312 -10.991 1.00 13.06 ?  122 LEU   B O    1 
ATOM   5712 C CB   . LEU   B 1 122 ? 40.621 -18.291 -8.761  1.00 13.55 ?  122 LEU   B CB   1 
ATOM   5713 C CG   . LEU   B 1 122 ? 39.588 -17.270 -8.270  1.00 13.77 ?  122 LEU   B CG   1 
ATOM   5714 C CD1  . LEU   B 1 122 ? 38.176 -17.626 -8.730  1.00 14.69 ?  122 LEU   B CD1  1 
ATOM   5715 C CD2  . LEU   B 1 122 ? 39.639 -17.141 -6.760  1.00 13.22 ?  122 LEU   B CD2  1 
ATOM   5716 H H    . LEU   B 1 122 ? 39.852 -18.382 -11.465 1.00 14.61 ?  122 LEU   B H    1 
ATOM   5717 H HA   . LEU   B 1 122 ? 41.946 -17.380 -10.060 1.00 13.91 ?  122 LEU   B HA   1 
ATOM   5718 H HB2  . LEU   B 1 122 ? 40.172 -19.151 -8.772  1.00 16.23 ?  122 LEU   B HB2  1 
ATOM   5719 H HB3  . LEU   B 1 122 ? 41.324 -18.309 -8.094  1.00 16.23 ?  122 LEU   B HB3  1 
ATOM   5720 H HG   . LEU   B 1 122 ? 39.803 -16.401 -8.643  1.00 16.50 ?  122 LEU   B HG   1 
ATOM   5721 H HD11 . LEU   B 1 122 ? 37.550 -16.968 -8.378  1.00 17.59 ?  122 LEU   B HD11 1 
ATOM   5722 H HD12 . LEU   B 1 122 ? 38.146 -17.614 -9.701  1.00 17.59 ?  122 LEU   B HD12 1 
ATOM   5723 H HD13 . LEU   B 1 122 ? 37.945 -18.506 -8.402  1.00 17.59 ?  122 LEU   B HD13 1 
ATOM   5724 H HD21 . LEU   B 1 122 ? 38.959 -16.513 -6.466  1.00 15.84 ?  122 LEU   B HD21 1 
ATOM   5725 H HD22 . LEU   B 1 122 ? 39.479 -18.010 -6.360  1.00 15.84 ?  122 LEU   B HD22 1 
ATOM   5726 H HD23 . LEU   B 1 122 ? 40.518 -16.817 -6.500  1.00 15.84 ?  122 LEU   B HD23 1 
ATOM   5727 N N    . LEU   B 1 123 ? 43.205 -19.510 -10.119 1.00 11.06 ?  123 LEU   B N    1 
ATOM   5728 C CA   . LEU   B 1 123 ? 43.915 -20.783 -10.003 1.00 11.59 ?  123 LEU   B CA   1 
ATOM   5729 C C    . LEU   B 1 123 ? 43.890 -21.176 -8.532  1.00 11.35 ?  123 LEU   B C    1 
ATOM   5730 O O    . LEU   B 1 123 ? 44.246 -20.353 -7.677  1.00 11.51 ?  123 LEU   B O    1 
ATOM   5731 C CB   . LEU   B 1 123 ? 45.365 -20.602 -10.461 1.00 11.69 ?  123 LEU   B CB   1 
ATOM   5732 C CG   . LEU   B 1 123 ? 46.305 -21.792 -10.233 1.00 12.18 ?  123 LEU   B CG   1 
ATOM   5733 C CD1  . LEU   B 1 123 ? 45.862 -23.034 -10.996 1.00 13.52 ?  123 LEU   B CD1  1 
ATOM   5734 C CD2  . LEU   B 1 123 ? 47.722 -21.402 -10.619 1.00 13.55 ?  123 LEU   B CD2  1 
ATOM   5735 H H    . LEU   B 1 123 ? 43.699 -18.830 -9.911  1.00 13.24 ?  123 LEU   B H    1 
ATOM   5736 H HA   . LEU   B 1 123 ? 43.476 -21.464 -10.533 1.00 13.88 ?  123 LEU   B HA   1 
ATOM   5737 H HB2  . LEU   B 1 123 ? 45.355 -20.414 -11.413 1.00 14.00 ?  123 LEU   B HB2  1 
ATOM   5738 H HB3  . LEU   B 1 123 ? 45.738 -19.841 -9.988  1.00 14.00 ?  123 LEU   B HB3  1 
ATOM   5739 H HG   . LEU   B 1 123 ? 46.307 -22.010 -9.291  1.00 14.59 ?  123 LEU   B HG   1 
ATOM   5740 H HD11 . LEU   B 1 123 ? 46.500 -23.744 -10.833 1.00 16.19 ?  123 LEU   B HD11 1 
ATOM   5741 H HD12 . LEU   B 1 123 ? 44.982 -23.300 -10.684 1.00 16.19 ?  123 LEU   B HD12 1 
ATOM   5742 H HD13 . LEU   B 1 123 ? 45.828 -22.828 -11.943 1.00 16.19 ?  123 LEU   B HD13 1 
ATOM   5743 H HD21 . LEU   B 1 123 ? 48.305 -22.159 -10.473 1.00 16.23 ?  123 LEU   B HD21 1 
ATOM   5744 H HD22 . LEU   B 1 123 ? 47.734 -21.146 -11.555 1.00 16.23 ?  123 LEU   B HD22 1 
ATOM   5745 H HD23 . LEU   B 1 123 ? 48.001 -20.653 -10.068 1.00 16.23 ?  123 LEU   B HD23 1 
ATOM   5746 N N    . ALA   B 1 124 ? 43.450 -22.406 -8.225  1.00 11.19 ?  124 ALA   B N    1 
ATOM   5747 C CA   . ALA   B 1 124 ? 43.183 -22.721 -6.830  1.00 11.14 ?  124 ALA   B CA   1 
ATOM   5748 C C    . ALA   B 1 124 ? 43.460 -24.178 -6.494  1.00 10.53 ?  124 ALA   B C    1 
ATOM   5749 O O    . ALA   B 1 124 ? 43.335 -25.054 -7.358  1.00 11.61 ?  124 ALA   B O    1 
ATOM   5750 C CB   . ALA   B 1 124 ? 41.723 -22.414 -6.469  1.00 11.84 ?  124 ALA   B CB   1 
ATOM   5751 H H    . ALA   B 1 124 ? 43.300 -23.047 -8.787  1.00 13.40 ?  124 ALA   B H    1 
ATOM   5752 H HA   . ALA   B 1 124 ? 43.748 -22.165 -6.280  1.00 13.34 ?  124 ALA   B HA   1 
ATOM   5753 H HB1  . ALA   B 1 124 ? 41.569 -22.629 -5.539  1.00 14.17 ?  124 ALA   B HB1  1 
ATOM   5754 H HB2  . ALA   B 1 124 ? 41.551 -21.469 -6.624  1.00 14.17 ?  124 ALA   B HB2  1 
ATOM   5755 H HB3  . ALA   B 1 124 ? 41.136 -22.947 -7.034  1.00 14.17 ?  124 ALA   B HB3  1 
ATOM   5756 N N    . PRO   B 1 125 ? 43.763 -24.464 -5.234  1.00 11.25 ?  125 PRO   B N    1 
ATOM   5757 C CA   . PRO   B 1 125 ? 43.714 -25.833 -4.713  1.00 11.97 ?  125 PRO   B CA   1 
ATOM   5758 C C    . PRO   B 1 125 ? 42.316 -26.107 -4.160  1.00 12.54 ?  125 PRO   B C    1 
ATOM   5759 O O    . PRO   B 1 125 ? 41.519 -25.193 -3.964  1.00 12.75 ?  125 PRO   B O    1 
ATOM   5760 C CB   . PRO   B 1 125 ? 44.707 -25.759 -3.550  1.00 12.90 ?  125 PRO   B CB   1 
ATOM   5761 C CG   . PRO   B 1 125 ? 44.465 -24.377 -2.979  1.00 13.25 ?  125 PRO   B CG   1 
ATOM   5762 C CD   . PRO   B 1 125 ? 44.113 -23.498 -4.178  1.00 11.91 ?  125 PRO   B CD   1 
ATOM   5763 H HA   . PRO   B 1 125 ? 43.985 -26.504 -5.369  1.00 14.33 ?  125 PRO   B HA   1 
ATOM   5764 H HB2  . PRO   B 1 125 ? 44.502 -26.445 -2.893  1.00 15.45 ?  125 PRO   B HB2  1 
ATOM   5765 H HB3  . PRO   B 1 125 ? 45.616 -25.849 -3.875  1.00 15.45 ?  125 PRO   B HB3  1 
ATOM   5766 H HG2  . PRO   B 1 125 ? 43.724 -24.400 -2.353  1.00 15.87 ?  125 PRO   B HG2  1 
ATOM   5767 H HG3  . PRO   B 1 125 ? 45.270 -24.051 -2.545  1.00 15.87 ?  125 PRO   B HG3  1 
ATOM   5768 H HD2  . PRO   B 1 125 ? 43.349 -22.936 -3.988  1.00 14.26 ?  125 PRO   B HD2  1 
ATOM   5769 H HD3  . PRO   B 1 125 ? 44.884 -22.964 -4.450  1.00 14.26 ?  125 PRO   B HD3  1 
ATOM   5770 N N    . LEU   B 1 126 ? 42.051 -27.380 -3.855  1.00 13.19 ?  126 LEU   B N    1 
ATOM   5771 C CA   . LEU   B 1 126 ? 40.831 -27.745 -3.135  1.00 13.21 ?  126 LEU   B CA   1 
ATOM   5772 C C    . LEU   B 1 126 ? 40.947 -27.345 -1.668  1.00 13.06 ?  126 LEU   B C    1 
ATOM   5773 O O    . LEU   B 1 126 ? 41.841 -27.808 -0.954  1.00 15.69 ?  126 LEU   B O    1 
ATOM   5774 C CB   . LEU   B 1 126 ? 40.577 -29.244 -3.244  1.00 15.03 ?  126 LEU   B CB   1 
ATOM   5775 C CG   . LEU   B 1 126 ? 40.057 -29.732 -4.597  1.00 15.89 ?  126 LEU   B CG   1 
ATOM   5776 C CD1  . LEU   B 1 126 ? 40.108 -31.245 -4.662  1.00 17.87 ?  126 LEU   B CD1  1 
ATOM   5777 C CD2  . LEU   B 1 126 ? 38.641 -29.235 -4.871  1.00 16.19 ?  126 LEU   B CD2  1 
ATOM   5778 H H    . LEU   B 1 126 ? 42.566 -28.048 -4.043  1.00 15.79 ?  126 LEU   B H    1 
ATOM   5779 H HA   . LEU   B 1 126 ? 40.082 -27.269 -3.523  1.00 15.83 ?  126 LEU   B HA   1 
ATOM   5780 H HB2  . LEU   B 1 126 ? 41.407 -29.706 -3.066  1.00 18.00 ?  126 LEU   B HB2  1 
ATOM   5781 H HB3  . LEU   B 1 126 ? 39.917 -29.485 -2.577  1.00 18.00 ?  126 LEU   B HB3  1 
ATOM   5782 H HG   . LEU   B 1 126 ? 40.636 -29.376 -5.296  1.00 19.04 ?  126 LEU   B HG   1 
ATOM   5783 H HD11 . LEU   B 1 126 ? 39.776 -31.531 -5.526  1.00 21.42 ?  126 LEU   B HD11 1 
ATOM   5784 H HD12 . LEU   B 1 126 ? 41.026 -31.534 -4.545  1.00 21.42 ?  126 LEU   B HD12 1 
ATOM   5785 H HD13 . LEU   B 1 126 ? 39.552 -31.606 -3.955  1.00 21.42 ?  126 LEU   B HD13 1 
ATOM   5786 H HD21 . LEU   B 1 126 ? 38.319 -29.641 -5.691  1.00 19.40 ?  126 LEU   B HD21 1 
ATOM   5787 H HD22 . LEU   B 1 126 ? 38.070 -29.487 -4.130  1.00 19.40 ?  126 LEU   B HD22 1 
ATOM   5788 H HD23 . LEU   B 1 126 ? 38.650 -28.268 -4.965  1.00 19.40 ?  126 LEU   B HD23 1 
ATOM   5789 N N    . LEU   B 1 127 ? 40.022 -26.510 -1.204  1.00 13.01 ?  127 LEU   B N    1 
ATOM   5790 C CA   . LEU   B 1 127 ? 40.087 -26.014 0.161   1.00 13.42 ?  127 LEU   B CA   1 
ATOM   5791 C C    . LEU   B 1 127 ? 39.808 -27.131 1.163   1.00 13.74 ?  127 LEU   B C    1 
ATOM   5792 O O    . LEU   B 1 127 ? 38.976 -28.017 0.938   1.00 14.09 ?  127 LEU   B O    1 
ATOM   5793 C CB   . LEU   B 1 127 ? 39.076 -24.886 0.370   1.00 14.21 ?  127 LEU   B CB   1 
ATOM   5794 C CG   . LEU   B 1 127 ? 39.260 -23.628 -0.474  1.00 15.00 ?  127 LEU   B CG   1 
ATOM   5795 C CD1  . LEU   B 1 127 ? 38.132 -22.653 -0.180  1.00 15.51 ?  127 LEU   B CD1  1 
ATOM   5796 C CD2  . LEU   B 1 127 ? 40.614 -22.978 -0.226  1.00 15.64 ?  127 LEU   B CD2  1 
ATOM   5797 H H    . LEU   B 1 127 ? 39.351 -26.211 -1.663  1.00 15.58 ?  127 LEU   B H    1 
ATOM   5798 H HA   . LEU   B 1 127 ? 40.977 -25.657 0.327   1.00 16.08 ?  127 LEU   B HA   1 
ATOM   5799 H HB2  . LEU   B 1 127 ? 38.192 -25.237 0.171   1.00 17.03 ?  127 LEU   B HB2  1 
ATOM   5800 H HB3  . LEU   B 1 127 ? 39.112 -24.619 1.300   1.00 17.03 ?  127 LEU   B HB3  1 
ATOM   5801 H HG   . LEU   B 1 127 ? 39.207 -23.862 -1.410  1.00 17.97 ?  127 LEU   B HG   1 
ATOM   5802 H HD11 . LEU   B 1 127 ? 38.264 -21.846 -0.708  1.00 18.59 ?  127 LEU   B HD11 1 
ATOM   5803 H HD12 . LEU   B 1 127 ? 37.286 -23.063 -0.412  1.00 18.59 ?  127 LEU   B HD12 1 
ATOM   5804 H HD13 . LEU   B 1 127 ? 38.143 -22.427 0.765   1.00 18.59 ?  127 LEU   B HD13 1 
ATOM   5805 H HD21 . LEU   B 1 127 ? 40.650 -22.131 -0.694  1.00 18.74 ?  127 LEU   B HD21 1 
ATOM   5806 H HD22 . LEU   B 1 127 ? 40.726 -22.834 0.729   1.00 18.74 ?  127 LEU   B HD22 1 
ATOM   5807 H HD23 . LEU   B 1 127 ? 41.309 -23.570 -0.553  1.00 18.74 ?  127 LEU   B HD23 1 
ATOM   5808 N N    . SER   B 1 128 ? 40.490 -27.047 2.300   1.00 13.86 ?  128 SER   B N    1 
ATOM   5809 C CA   . SER   B 1 128 ? 40.365 -27.949 3.436   1.00 14.52 ?  128 SER   B CA   1 
ATOM   5810 C C    . SER   B 1 128 ? 40.854 -29.364 3.138   1.00 15.78 ?  128 SER   B C    1 
ATOM   5811 O O    . SER   B 1 128 ? 40.747 -30.234 4.002   1.00 17.68 ?  128 SER   B O    1 
ATOM   5812 C CB   . SER   B 1 128 ? 38.954 -27.941 4.049   1.00 14.68 ?  128 SER   B CB   1 
ATOM   5813 O OG   . SER   B 1 128 ? 38.655 -26.663 4.609   1.00 14.82 ?  128 SER   B OG   1 
ATOM   5814 H H    . SER   B 1 128 ? 41.067 -26.422 2.442   1.00 16.60 ?  128 SER   B H    1 
ATOM   5815 H HA   . SER   B 1 128 ? 40.948 -27.605 4.122   1.00 17.40 ?  128 SER   B HA   1 
ATOM   5816 H HB2  . SER   B 1 128 ? 38.298 -28.151 3.366   1.00 17.59 ?  128 SER   B HB2  1 
ATOM   5817 H HB3  . SER   B 1 128 ? 38.913 -28.614 4.757   1.00 17.59 ?  128 SER   B HB3  1 
ATOM   5818 H HG   . SER   B 1 128 ? 39.220 -26.476 5.205   1.00 17.75 ?  128 SER   B HG   1 
ATOM   5819 N N    . ALA   B 1 129 ? 41.427 -29.601 1.957   1.00 16.94 ?  129 ALA   B N    1 
ATOM   5820 C CA   . ALA   B 1 129 ? 41.964 -30.905 1.598   1.00 18.07 ?  129 ALA   B CA   1 
ATOM   5821 C C    . ALA   B 1 129 ? 43.367 -31.083 2.168   1.00 16.76 ?  129 ALA   B C    1 
ATOM   5822 O O    . ALA   B 1 129 ? 43.923 -30.193 2.824   1.00 16.24 ?  129 ALA   B O    1 
ATOM   5823 C CB   . ALA   B 1 129 ? 42.002 -31.061 0.081   1.00 20.26 ?  129 ALA   B CB   1 
ATOM   5824 H H    . ALA   B 1 129 ? 41.518 -29.013 1.331   1.00 20.30 ?  129 ALA   B H    1 
ATOM   5825 H HA   . ALA   B 1 129 ? 41.395 -31.598 1.960   1.00 21.65 ?  129 ALA   B HA   1 
ATOM   5826 H HB1  . ALA   B 1 129 ? 42.345 -31.942 -0.139  1.00 24.28 ?  129 ALA   B HB1  1 
ATOM   5827 H HB2  . ALA   B 1 129 ? 41.105 -30.958 -0.269  1.00 24.28 ?  129 ALA   B HB2  1 
ATOM   5828 H HB3  . ALA   B 1 129 ? 42.584 -30.379 -0.293  1.00 24.28 ?  129 ALA   B HB3  1 
ATOM   5829 N N    . GLY   B 1 130 ? 43.950 -32.247 1.889   1.00 16.75 ?  130 GLY   B N    1 
ATOM   5830 C CA   . GLY   B 1 130 ? 45.338 -32.475 2.245   1.00 17.35 ?  130 GLY   B CA   1 
ATOM   5831 C C    . GLY   B 1 130 ? 45.541 -32.385 3.738   1.00 17.06 ?  130 GLY   B C    1 
ATOM   5832 O O    . GLY   B 1 130 ? 44.828 -33.021 4.527   1.00 17.89 ?  130 GLY   B O    1 
ATOM   5833 H H    . GLY   B 1 130 ? 43.572 -32.905 1.485   1.00 20.07 ?  130 GLY   B H    1 
ATOM   5834 H HA2  . GLY   B 1 130 ? 45.611 -33.356 1.946   1.00 20.79 ?  130 GLY   B HA2  1 
ATOM   5835 H HA3  . GLY   B 1 130 ? 45.901 -31.813 1.812   1.00 20.79 ?  130 GLY   B HA3  1 
ATOM   5836 N N    . ILE   B 1 131 ? 46.523 -31.566 4.136   1.00 17.44 ?  131 ILE   B N    1 
ATOM   5837 C CA   . ILE   B 1 131 ? 46.897 -31.463 5.541   1.00 19.08 ?  131 ILE   B CA   1 
ATOM   5838 C C    . ILE   B 1 131 ? 45.799 -30.852 6.393   1.00 17.89 ?  131 ILE   B C    1 
ATOM   5839 O O    . ILE   B 1 131 ? 45.883 -30.915 7.622   1.00 19.50 ?  131 ILE   B O    1 
ATOM   5840 C CB   . ILE   B 1 131 ? 48.227 -30.698 5.744   1.00 20.42 ?  131 ILE   B CB   1 
ATOM   5841 C CG1  . ILE   B 1 131 ? 48.076 -29.209 5.404   1.00 21.21 ?  131 ILE   B CG1  1 
ATOM   5842 C CG2  . ILE   B 1 131 ? 49.346 -31.338 4.915   1.00 21.63 ?  131 ILE   B CG2  1 
ATOM   5843 C CD1  . ILE   B 1 131 ? 49.309 -28.369 5.714   1.00 22.49 ?  131 ILE   B CD1  1 
ATOM   5844 H H    . ILE   B 1 131 ? 46.977 -31.051 3.612   1.00 20.90 ?  131 ILE   B H    1 
ATOM   5845 H HA   . ILE   B 1 131 ? 47.039 -32.358 5.871   1.00 22.87 ?  131 ILE   B HA   1 
ATOM   5846 H HB   . ILE   B 1 131 ? 48.474 -30.768 6.679   1.00 24.48 ?  131 ILE   B HB   1 
ATOM   5847 H HG12 . ILE   B 1 131 ? 47.889 -29.125 4.457   1.00 25.43 ?  131 ILE   B HG12 1 
ATOM   5848 H HG13 . ILE   B 1 131 ? 47.340 -28.839 5.917   1.00 25.43 ?  131 ILE   B HG13 1 
ATOM   5849 H HG21 . ILE   B 1 131 ? 50.193 -30.938 5.165   1.00 25.93 ?  131 ILE   B HG21 1 
ATOM   5850 H HG22 . ILE   B 1 131 ? 49.363 -32.289 5.093   1.00 25.93 ?  131 ILE   B HG22 1 
ATOM   5851 H HG23 . ILE   B 1 131 ? 49.169 -31.179 3.974   1.00 25.93 ?  131 ILE   B HG23 1 
ATOM   5852 H HD11 . ILE   B 1 131 ? 49.098 -27.434 5.566   1.00 26.96 ?  131 ILE   B HD11 1 
ATOM   5853 H HD12 . ILE   B 1 131 ? 49.561 -28.508 6.641   1.00 26.96 ?  131 ILE   B HD12 1 
ATOM   5854 H HD13 . ILE   B 1 131 ? 50.033 -28.642 5.131   1.00 26.96 ?  131 ILE   B HD13 1 
ATOM   5855 N N    . PHE   B 1 132 ? 44.771 -30.262 5.775   1.00 16.76 ?  132 PHE   B N    1 
ATOM   5856 C CA   . PHE   B 1 132 ? 43.623 -29.746 6.512   1.00 17.42 ?  132 PHE   B CA   1 
ATOM   5857 C C    . PHE   B 1 132 ? 42.605 -30.831 6.862   1.00 19.21 ?  132 PHE   B C    1 
ATOM   5858 O O    . PHE   B 1 132 ? 41.726 -30.584 7.693   1.00 21.29 ?  132 PHE   B O    1 
ATOM   5859 C CB   . PHE   B 1 132 ? 42.937 -28.629 5.718   1.00 16.42 ?  132 PHE   B CB   1 
ATOM   5860 C CG   . PHE   B 1 132 ? 43.628 -27.283 5.814   1.00 15.63 ?  132 PHE   B CG   1 
ATOM   5861 C CD1  . PHE   B 1 132 ? 44.935 -27.109 5.372   1.00 17.25 ?  132 PHE   B CD1  1 
ATOM   5862 C CD2  . PHE   B 1 132 ? 42.945 -26.184 6.314   1.00 15.08 ?  132 PHE   B CD2  1 
ATOM   5863 C CE1  . PHE   B 1 132 ? 45.557 -25.865 5.457   1.00 17.97 ?  132 PHE   B CE1  1 
ATOM   5864 C CE2  . PHE   B 1 132 ? 43.556 -24.937 6.391   1.00 15.95 ?  132 PHE   B CE2  1 
ATOM   5865 C CZ   . PHE   B 1 132 ? 44.862 -24.781 5.965   1.00 17.02 ?  132 PHE   B CZ   1 
ATOM   5866 H H    . PHE   B 1 132 ? 44.714 -30.162 4.923   1.00 20.09 ?  132 PHE   B H    1 
ATOM   5867 H HA   . PHE   B 1 132 ? 43.942 -29.366 7.344   1.00 20.88 ?  132 PHE   B HA   1 
ATOM   5868 H HB2  . PHE   B 1 132 ? 42.920 -28.882 4.784   1.00 19.68 ?  132 PHE   B HB2  1 
ATOM   5869 H HB3  . PHE   B 1 132 ? 42.033 -28.522 6.050   1.00 19.68 ?  132 PHE   B HB3  1 
ATOM   5870 H HD1  . PHE   B 1 132 ? 45.406 -27.839 5.036   1.00 20.67 ?  132 PHE   B HD1  1 
ATOM   5871 H HD2  . PHE   B 1 132 ? 42.066 -26.285 6.606   1.00 18.06 ?  132 PHE   B HD2  1 
ATOM   5872 H HE1  . PHE   B 1 132 ? 46.433 -25.762 5.169   1.00 21.53 ?  132 PHE   B HE1  1 
ATOM   5873 H HE2  . PHE   B 1 132 ? 43.085 -24.210 6.741   1.00 19.12 ?  132 PHE   B HE2  1 
ATOM   5874 H HZ   . PHE   B 1 132 ? 45.269 -23.941 6.025   1.00 20.39 ?  132 PHE   B HZ   1 
ATOM   5875 N N    . GLY   B 1 133 ? 42.686 -32.018 6.247   1.00 18.62 ?  133 GLY   B N    1 
ATOM   5876 C CA   . GLY   B 1 133 ? 41.992 -33.191 6.750   1.00 19.58 ?  133 GLY   B CA   1 
ATOM   5877 C C    . GLY   B 1 133 ? 40.593 -33.466 6.232   1.00 20.46 ?  133 GLY   B C    1 
ATOM   5878 O O    . GLY   B 1 133 ? 40.021 -34.495 6.605   1.00 22.35 ?  133 GLY   B O    1 
ATOM   5879 H H    . GLY   B 1 133 ? 43.144 -32.159 5.531   1.00 22.32 ?  133 GLY   B H    1 
ATOM   5880 H HA2  . GLY   B 1 133 ? 42.534 -33.970 6.552   1.00 23.47 ?  133 GLY   B HA2  1 
ATOM   5881 H HA3  . GLY   B 1 133 ? 41.927 -33.116 7.712   1.00 23.47 ?  133 GLY   B HA3  1 
ATOM   5882 N N    . ALA   B 1 134 ? 40.016 -32.603 5.403   1.00 19.33 ?  134 ALA   B N    1 
ATOM   5883 C CA   . ALA   B 1 134 ? 38.697 -32.895 4.862   1.00 19.32 ?  134 ALA   B CA   1 
ATOM   5884 C C    . ALA   B 1 134 ? 38.800 -33.857 3.683   1.00 19.06 ?  134 ALA   B C    1 
ATOM   5885 O O    . ALA   B 1 134 ? 39.859 -34.029 3.072   1.00 19.55 ?  134 ALA   B O    1 
ATOM   5886 C CB   . ALA   B 1 134 ? 37.999 -31.613 4.414   1.00 19.18 ?  134 ALA   B CB   1 
ATOM   5887 H H    . ALA   B 1 134 ? 40.355 -31.850 5.152   1.00 23.17 ?  134 ALA   B H    1 
ATOM   5888 H HA   . ALA   B 1 134 ? 38.155 -33.310 5.552   1.00 23.16 ?  134 ALA   B HA   1 
ATOM   5889 H HB1  . ALA   B 1 134 ? 37.112 -31.836 4.087   1.00 22.99 ?  134 ALA   B HB1  1 
ATOM   5890 H HB2  . ALA   B 1 134 ? 37.930 -31.008 5.169   1.00 22.99 ?  134 ALA   B HB2  1 
ATOM   5891 H HB3  . ALA   B 1 134 ? 38.518 -31.201 3.706   1.00 22.99 ?  134 ALA   B HB3  1 
ATOM   5892 N N    A ASP   B 1 135 ? 37.679 -34.489 3.371   0.66 19.65 ?  135 ASP   B N    1 
ATOM   5893 N N    B ASP   B 1 135 ? 37.679 -34.489 3.372   0.34 19.22 ?  135 ASP   B N    1 
ATOM   5894 C CA   A ASP   B 1 135 ? 37.599 -35.373 2.217   0.66 20.50 ?  135 ASP   B CA   1 
ATOM   5895 C CA   B ASP   B 1 135 ? 37.607 -35.372 2.220   0.34 19.67 ?  135 ASP   B CA   1 
ATOM   5896 C C    A ASP   B 1 135 ? 37.678 -34.534 0.948   0.66 19.02 ?  135 ASP   B C    1 
ATOM   5897 C C    B ASP   B 1 135 ? 37.682 -34.532 0.951   0.34 18.83 ?  135 ASP   B C    1 
ATOM   5898 O O    A ASP   B 1 135 ? 36.810 -33.676 0.732   0.66 18.65 ?  135 ASP   B O    1 
ATOM   5899 O O    B ASP   B 1 135 ? 36.815 -33.673 0.738   0.34 18.54 ?  135 ASP   B O    1 
ATOM   5900 C CB   A ASP   B 1 135 ? 36.269 -36.119 2.275   0.66 22.39 ?  135 ASP   B CB   1 
ATOM   5901 C CB   B ASP   B 1 135 ? 36.294 -36.148 2.257   0.34 20.82 ?  135 ASP   B CB   1 
ATOM   5902 C CG   A ASP   B 1 135 ? 36.075 -37.091 1.124   0.66 24.15 ?  135 ASP   B CG   1 
ATOM   5903 C CG   B ASP   B 1 135 ? 36.218 -37.222 1.179   0.34 21.91 ?  135 ASP   B CG   1 
ATOM   5904 O OD1  A ASP   B 1 135 ? 36.964 -37.193 0.253   0.66 24.05 ?  135 ASP   B OD1  1 
ATOM   5905 O OD1  B ASP   B 1 135 ? 37.089 -37.232 0.285   0.34 22.12 ?  135 ASP   B OD1  1 
ATOM   5906 O OD2  A ASP   B 1 135 ? 35.013 -37.755 1.091   0.66 26.86 -1 135 ASP   B OD2  1 
ATOM   5907 O OD2  B ASP   B 1 135 ? 35.300 -38.073 1.236   0.34 22.89 -1 135 ASP   B OD2  1 
ATOM   5908 H H    A ASP   B 1 135 ? 36.945 -34.420 3.813   0.66 23.55 ?  135 ASP   B H    1 
ATOM   5909 H H    B ASP   B 1 135 ? 36.945 -34.424 3.813   0.34 23.04 ?  135 ASP   B H    1 
ATOM   5910 H HA   A ASP   B 1 135 ? 38.326 -36.015 2.246   0.66 24.57 ?  135 ASP   B HA   1 
ATOM   5911 H HA   B ASP   B 1 135 ? 38.342 -36.004 2.247   0.34 23.58 ?  135 ASP   B HA   1 
ATOM   5912 H HB2  A ASP   B 1 135 ? 36.220 -36.603 3.116   0.66 26.84 ?  135 ASP   B HB2  1 
ATOM   5913 H HB2  B ASP   B 1 135 ? 36.216 -36.587 3.118   0.34 24.96 ?  135 ASP   B HB2  1 
ATOM   5914 H HB3  A ASP   B 1 135 ? 35.548 -35.483 2.213   0.66 26.84 ?  135 ASP   B HB3  1 
ATOM   5915 H HB3  B ASP   B 1 135 ? 35.559 -35.522 2.139   0.34 24.96 ?  135 ASP   B HB3  1 
ATOM   5916 N N    . PRO   B 1 136 ? 38.683 -34.730 0.090   1.00 18.93 ?  136 PRO   B N    1 
ATOM   5917 C CA   . PRO   B 1 136 ? 38.757 -33.912 -1.135  1.00 18.22 ?  136 PRO   B CA   1 
ATOM   5918 C C    . PRO   B 1 136 ? 37.550 -34.069 -2.044  1.00 17.40 ?  136 PRO   B C    1 
ATOM   5919 O O    . PRO   B 1 136 ? 37.210 -33.131 -2.774  1.00 16.75 ?  136 PRO   B O    1 
ATOM   5920 C CB   . PRO   B 1 136 ? 40.061 -34.384 -1.799  1.00 18.77 ?  136 PRO   B CB   1 
ATOM   5921 C CG   . PRO   B 1 136 ? 40.304 -35.762 -1.220  1.00 20.33 ?  136 PRO   B CG   1 
ATOM   5922 C CD   . PRO   B 1 136 ? 39.795 -35.691 0.185   1.00 19.79 ?  136 PRO   B CD   1 
ATOM   5923 H HA   . PRO   B 1 136 ? 38.845 -32.976 -0.908  1.00 21.84 ?  136 PRO   B HA   1 
ATOM   5924 H HB2  . PRO   B 1 136 ? 39.948 -34.430 -2.762  1.00 22.49 ?  136 PRO   B HB2  1 
ATOM   5925 H HB3  . PRO   B 1 136 ? 40.784 -33.780 -1.566  1.00 22.49 ?  136 PRO   B HB3  1 
ATOM   5926 H HG2  . PRO   B 1 136 ? 39.809 -36.429 -1.725  1.00 24.37 ?  136 PRO   B HG2  1 
ATOM   5927 H HG3  . PRO   B 1 136 ? 41.253 -35.966 -1.226  1.00 24.37 ?  136 PRO   B HG3  1 
ATOM   5928 H HD2  . PRO   B 1 136 ? 39.473 -36.560 0.472   1.00 23.72 ?  136 PRO   B HD2  1 
ATOM   5929 H HD3  . PRO   B 1 136 ? 40.482 -35.352 0.786   1.00 23.72 ?  136 PRO   B HD3  1 
ATOM   5930 N N    . ILE   B 1 137 ? 36.898 -35.237 -2.030  1.00 17.95 ?  137 ILE   B N    1 
ATOM   5931 C CA   . ILE   B 1 137 ? 35.676 -35.419 -2.809  1.00 18.39 ?  137 ILE   B CA   1 
ATOM   5932 C C    . ILE   B 1 137 ? 34.594 -34.459 -2.328  1.00 17.50 ?  137 ILE   B C    1 
ATOM   5933 O O    . ILE   B 1 137 ? 33.865 -33.855 -3.130  1.00 16.93 ?  137 ILE   B O    1 
ATOM   5934 C CB   . ILE   B 1 137 ? 35.212 -36.889 -2.733  1.00 20.69 ?  137 ILE   B CB   1 
ATOM   5935 C CG1  . ILE   B 1 137 ? 36.212 -37.798 -3.454  1.00 22.35 ?  137 ILE   B CG1  1 
ATOM   5936 C CG2  . ILE   B 1 137 ? 33.802 -37.047 -3.304  1.00 21.42 ?  137 ILE   B CG2  1 
ATOM   5937 C CD1  . ILE   B 1 137 ? 35.924 -39.288 -3.297  1.00 24.84 ?  137 ILE   B CD1  1 
ATOM   5938 H H    . ILE   B 1 137 ? 37.141 -35.934 -1.587  1.00 21.51 ?  137 ILE   B H    1 
ATOM   5939 H HA   . ILE   B 1 137 ? 35.859 -35.216 -3.741  1.00 22.04 ?  137 ILE   B HA   1 
ATOM   5940 H HB   . ILE   B 1 137 ? 35.187 -37.150 -1.803  1.00 24.80 ?  137 ILE   B HB   1 
ATOM   5941 H HG12 . ILE   B 1 137 ? 36.197 -37.602 -4.402  1.00 26.79 ?  137 ILE   B HG12 1 
ATOM   5942 H HG13 . ILE   B 1 137 ? 37.098 -37.638 -3.097  1.00 26.79 ?  137 ILE   B HG13 1 
ATOM   5943 H HG21 . ILE   B 1 137 ? 33.570 -37.990 -3.343  1.00 25.67 ?  137 ILE   B HG21 1 
ATOM   5944 H HG22 . ILE   B 1 137 ? 33.171 -36.592 -2.728  1.00 25.67 ?  137 ILE   B HG22 1 
ATOM   5945 H HG23 . ILE   B 1 137 ? 33.776 -36.668 -4.195  1.00 25.67 ?  137 ILE   B HG23 1 
ATOM   5946 H HD11 . ILE   B 1 137 ? 36.555 -39.780 -3.842  1.00 29.78 ?  137 ILE   B HD11 1 
ATOM   5947 H HD12 . ILE   B 1 137 ? 36.026 -39.538 -2.363  1.00 29.78 ?  137 ILE   B HD12 1 
ATOM   5948 H HD13 . ILE   B 1 137 ? 35.022 -39.485 -3.594  1.00 29.78 ?  137 ILE   B HD13 1 
ATOM   5949 N N    . HIS   B 1 138 ? 34.473 -34.303 -1.011  1.00 17.85 ?  138 HIS   B N    1 
ATOM   5950 C CA   . HIS   B 1 138 ? 33.527 -33.335 -0.466  1.00 18.44 ?  138 HIS   B CA   1 
ATOM   5951 C C    . HIS   B 1 138 ? 33.937 -31.908 -0.799  1.00 17.35 ?  138 HIS   B C    1 
ATOM   5952 O O    . HIS   B 1 138 ? 33.087 -31.061 -1.093  1.00 18.14 ?  138 HIS   B O    1 
ATOM   5953 C CB   . HIS   B 1 138 ? 33.430 -33.516 1.043   1.00 20.11 ?  138 HIS   B CB   1 
ATOM   5954 C CG   . HIS   B 1 138 ? 32.524 -32.527 1.696   1.00 21.54 ?  138 HIS   B CG   1 
ATOM   5955 N ND1  . HIS   B 1 138 ? 31.181 -32.446 1.400   1.00 23.55 ?  138 HIS   B ND1  1 
ATOM   5956 C CD2  . HIS   B 1 138 ? 32.769 -31.564 2.613   1.00 21.68 ?  138 HIS   B CD2  1 
ATOM   5957 C CE1  . HIS   B 1 138 ? 30.636 -31.476 2.112   1.00 23.61 ?  138 HIS   B CE1  1 
ATOM   5958 N NE2  . HIS   B 1 138 ? 31.577 -30.926 2.858   1.00 22.40 ?  138 HIS   B NE2  1 
ATOM   5959 H H    . HIS   B 1 138 ? 34.928 -34.740 -0.422  1.00 21.40 ?  138 HIS   B H    1 
ATOM   5960 H HA   . HIS   B 1 138 ? 32.653 -33.505 -0.848  1.00 22.10 ?  138 HIS   B HA   1 
ATOM   5961 H HB2  . HIS   B 1 138 ? 33.090 -34.407 1.233   1.00 24.10 ?  138 HIS   B HB2  1 
ATOM   5962 H HB3  . HIS   B 1 138 ? 34.314 -33.415 1.430   1.00 24.10 ?  138 HIS   B HB3  1 
ATOM   5963 H HD1  . HIS   B 1 138 ? 30.765 -32.951 0.837   1.00 28.23 ?  138 HIS   B HD1  1 
ATOM   5964 H HD2  . HIS   B 1 138 ? 33.585 -31.374 3.011   1.00 25.99 ?  138 HIS   B HD2  1 
ATOM   5965 H HE1  . HIS   B 1 138 ? 29.736 -31.235 2.095   1.00 28.31 ?  138 HIS   B HE1  1 
ATOM   5966 N N    . SER   B 1 139 ? 35.232 -31.614 -0.739  1.00 16.67 ?  139 SER   B N    1 
ATOM   5967 C CA   . SER   B 1 139 ? 35.666 -30.266 -1.065  1.00 15.69 ?  139 SER   B CA   1 
ATOM   5968 C C    . SER   B 1 139 ? 35.317 -29.915 -2.502  1.00 14.47 ?  139 SER   B C    1 
ATOM   5969 O O    . SER   B 1 139 ? 34.872 -28.795 -2.777  1.00 14.89 ?  139 SER   B O    1 
ATOM   5970 C CB   . SER   B 1 139 ? 37.162 -30.109 -0.809  1.00 16.06 ?  139 SER   B CB   1 
ATOM   5971 O OG   . SER   B 1 139 ? 37.570 -28.773 -1.064  1.00 15.68 ?  139 SER   B OG   1 
ATOM   5972 H H    . SER   B 1 139 ? 35.862 -32.157 -0.532  1.00 19.98 ?  139 SER   B H    1 
ATOM   5973 H HA   . SER   B 1 139 ? 35.197 -29.637 -0.501  1.00 18.79 ?  139 SER   B HA   1 
ATOM   5974 H HB2  . SER   B 1 139 ? 37.345 -30.335 0.119   1.00 19.24 ?  139 SER   B HB2  1 
ATOM   5975 H HB3  . SER   B 1 139 ? 37.655 -30.696 -1.398  1.00 19.24 ?  139 SER   B HB3  1 
ATOM   5976 H HG   . SER   B 1 139 ? 38.394 -28.685 -0.893  1.00 18.79 ?  139 SER   B HG   1 
ATOM   5977 N N    . LEU   B 1 140 ? 35.500 -30.861 -3.430  1.00 14.15 ?  140 LEU   B N    1 
ATOM   5978 C CA   . LEU   B 1 140 ? 35.123 -30.612 -4.816  1.00 14.47 ?  140 LEU   B CA   1 
ATOM   5979 C C    . LEU   B 1 140 ? 33.621 -30.376 -4.931  1.00 14.38 ?  140 LEU   B C    1 
ATOM   5980 O O    . LEU   B 1 140 ? 33.181 -29.485 -5.664  1.00 14.52 ?  140 LEU   B O    1 
ATOM   5981 C CB   . LEU   B 1 140 ? 35.584 -31.774 -5.706  1.00 14.80 ?  140 LEU   B CB   1 
ATOM   5982 C CG   . LEU   B 1 140 ? 35.209 -31.678 -7.180  1.00 15.29 ?  140 LEU   B CG   1 
ATOM   5983 C CD1  . LEU   B 1 140 ? 35.786 -30.417 -7.798  1.00 16.25 ?  140 LEU   B CD1  1 
ATOM   5984 C CD2  . LEU   B 1 140 ? 35.690 -32.927 -7.906  1.00 16.37 ?  140 LEU   B CD2  1 
ATOM   5985 H H    . LEU   B 1 140 ? 35.833 -31.640 -3.288  1.00 16.95 ?  140 LEU   B H    1 
ATOM   5986 H HA   . LEU   B 1 140 ? 35.575 -29.813 -5.131  1.00 17.33 ?  140 LEU   B HA   1 
ATOM   5987 H HB2  . LEU   B 1 140 ? 36.555 -31.831 -5.665  1.00 17.74 ?  140 LEU   B HB2  1 
ATOM   5988 H HB3  . LEU   B 1 140 ? 35.201 -32.596 -5.370  1.00 17.74 ?  140 LEU   B HB3  1 
ATOM   5989 H HG   . LEU   B 1 140 ? 34.245 -31.634 -7.261  1.00 18.32 ?  140 LEU   B HG   1 
ATOM   5990 H HD11 . LEU   B 1 140 ? 35.643 -30.440 -8.756  1.00 19.47 ?  140 LEU   B HD11 1 
ATOM   5991 H HD12 . LEU   B 1 140 ? 35.341 -29.644 -7.415  1.00 19.47 ?  140 LEU   B HD12 1 
ATOM   5992 H HD13 . LEU   B 1 140 ? 36.737 -30.378 -7.607  1.00 19.47 ?  140 LEU   B HD13 1 
ATOM   5993 H HD21 . LEU   B 1 140 ? 35.445 -32.865 -8.843  1.00 19.61 ?  140 LEU   B HD21 1 
ATOM   5994 H HD22 . LEU   B 1 140 ? 36.649 -33.001 -7.816  1.00 19.61 ?  140 LEU   B HD22 1 
ATOM   5995 H HD23 . LEU   B 1 140 ? 35.259 -33.705 -7.508  1.00 19.61 ?  140 LEU   B HD23 1 
ATOM   5996 N N    . ARG   B 1 141 ? 32.823 -31.175 -4.214  1.00 14.90 ?  141 ARG   B N    1 
ATOM   5997 C CA   . ARG   B 1 141 ? 31.374 -31.003 -4.183  1.00 15.66 ?  141 ARG   B CA   1 
ATOM   5998 C C    . ARG   B 1 141 ? 30.995 -29.588 -3.764  1.00 15.21 ?  141 ARG   B C    1 
ATOM   5999 O O    . ARG   B 1 141 ? 30.192 -28.917 -4.430  1.00 15.74 ?  141 ARG   B O    1 
ATOM   6000 C CB   . ARG   B 1 141 ? 30.799 -32.018 -3.192  1.00 17.00 ?  141 ARG   B CB   1 
ATOM   6001 C CG   . ARG   B 1 141 ? 29.318 -31.907 -2.900  1.00 18.75 ?  141 ARG   B CG   1 
ATOM   6002 C CD   . ARG   B 1 141 ? 28.541 -32.559 -3.980  1.00 20.07 ?  141 ARG   B CD   1 
ATOM   6003 N NE   . ARG   B 1 141 ? 28.276 -31.647 -5.081  1.00 19.86 ?  141 ARG   B NE   1 
ATOM   6004 C CZ   . ARG   B 1 141 ? 28.242 -32.000 -6.359  1.00 19.84 ?  141 ARG   B CZ   1 
ATOM   6005 N NH1  . ARG   B 1 141 ? 28.672 -33.186 -6.763  1.00 19.04 ?  141 ARG   B NH1  1 
ATOM   6006 N NH2  . ARG   B 1 141 ? 27.751 -31.147 -7.253  1.00 21.25 ?  141 ARG   B NH2  1 
ATOM   6007 H H    . ARG   B 1 141 ? 33.110 -31.821 -3.724  1.00 17.85 ?  141 ARG   B H    1 
ATOM   6008 H HA   . ARG   B 1 141 ? 31.005 -31.167 -5.057  1.00 18.76 ?  141 ARG   B HA   1 
ATOM   6009 H HB2  . ARG   B 1 141 ? 30.968 -32.906 -3.538  1.00 20.37 ?  141 ARG   B HB2  1 
ATOM   6010 H HB3  . ARG   B 1 141 ? 31.261 -31.913 -2.347  1.00 20.37 ?  141 ARG   B HB3  1 
ATOM   6011 H HG2  . ARG   B 1 141 ? 29.122 -32.353 -2.062  1.00 22.47 ?  141 ARG   B HG2  1 
ATOM   6012 H HG3  . ARG   B 1 141 ? 29.049 -30.971 -2.847  1.00 22.47 ?  141 ARG   B HG3  1 
ATOM   6013 H HD2  . ARG   B 1 141 ? 29.046 -33.320 -4.318  1.00 24.05 ?  141 ARG   B HD2  1 
ATOM   6014 H HD3  . ARG   B 1 141 ? 27.697 -32.865 -3.623  1.00 24.05 ?  141 ARG   B HD3  1 
ATOM   6015 H HE   . ARG   B 1 141 ? 28.096 -30.830 -4.889  1.00 23.81 ?  141 ARG   B HE   1 
ATOM   6016 H HH11 . ARG   B 1 141 ? 28.978 -33.759 -6.197  1.00 22.82 ?  141 ARG   B HH11 1 
ATOM   6017 H HH12 . ARG   B 1 141 ? 28.649 -33.390 -7.598  1.00 22.82 ?  141 ARG   B HH12 1 
ATOM   6018 H HH21 . ARG   B 1 141 ? 27.476 -30.372 -7.004  1.00 25.47 ?  141 ARG   B HH21 1 
ATOM   6019 H HH22 . ARG   B 1 141 ? 27.746 -31.355 -8.090  1.00 25.47 ?  141 ARG   B HH22 1 
ATOM   6020 N N    . VAL   B 1 142 ? 31.537 -29.135 -2.632  1.00 15.50 ?  142 VAL   B N    1 
ATOM   6021 C CA   . VAL   B 1 142 ? 31.221 -27.794 -2.153  1.00 14.71 ?  142 VAL   B CA   1 
ATOM   6022 C C    . VAL   B 1 142 ? 31.690 -26.744 -3.154  1.00 14.58 ?  142 VAL   B C    1 
ATOM   6023 O O    . VAL   B 1 142 ? 30.984 -25.765 -3.423  1.00 15.28 ?  142 VAL   B O    1 
ATOM   6024 C CB   . VAL   B 1 142 ? 31.787 -27.563 -0.739  1.00 15.86 ?  142 VAL   B CB   1 
ATOM   6025 C CG1  . VAL   B 1 142 ? 31.458 -26.145 -0.259  1.00 15.58 ?  142 VAL   B CG1  1 
ATOM   6026 C CG2  . VAL   B 1 142 ? 31.239 -28.599 0.231   1.00 16.84 ?  142 VAL   B CG2  1 
ATOM   6027 H H    . VAL   B 1 142 ? 32.075 -29.578 -2.122  1.00 18.57 ?  142 VAL   B H    1 
ATOM   6028 H HA   . VAL   B 1 142 ? 30.262 -27.710 -2.078  1.00 17.62 ?  142 VAL   B HA   1 
ATOM   6029 H HB   . VAL   B 1 142 ? 32.758 -27.655 -0.759  1.00 19.00 ?  142 VAL   B HB   1 
ATOM   6030 H HG11 . VAL   B 1 142 ? 31.662 -26.076 0.687   1.00 18.67 ?  142 VAL   B HG11 1 
ATOM   6031 H HG12 . VAL   B 1 142 ? 31.997 -25.508 -0.757  1.00 18.67 ?  142 VAL   B HG12 1 
ATOM   6032 H HG13 . VAL   B 1 142 ? 30.518 -25.975 -0.409  1.00 18.67 ?  142 VAL   B HG13 1 
ATOM   6033 H HG21 . VAL   B 1 142 ? 31.558 -28.396 1.124   1.00 20.18 ?  142 VAL   B HG21 1 
ATOM   6034 H HG22 . VAL   B 1 142 ? 30.272 -28.565 0.207   1.00 20.18 ?  142 VAL   B HG22 1 
ATOM   6035 H HG23 . VAL   B 1 142 ? 31.548 -29.478 -0.039  1.00 20.18 ?  142 VAL   B HG23 1 
ATOM   6036 N N    . CYS   B 1 143 ? 32.872 -26.944 -3.744  1.00 13.83 ?  143 CYS   B N    1 
ATOM   6037 C CA   . CYS   B 1 143 ? 33.359 -26.008 -4.755  1.00 13.74 ?  143 CYS   B CA   1 
ATOM   6038 C C    . CYS   B 1 143 ? 32.352 -25.868 -5.893  1.00 13.86 ?  143 CYS   B C    1 
ATOM   6039 O O    . CYS   B 1 143 ? 31.943 -24.758 -6.257  1.00 14.29 ?  143 CYS   B O    1 
ATOM   6040 C CB   . CYS   B 1 143 ? 34.712 -26.488 -5.288  1.00 14.34 ?  143 CYS   B CB   1 
ATOM   6041 S SG   . CYS   B 1 143 ? 35.453 -25.398 -6.519  1.00 14.65 ?  143 CYS   B SG   1 
ATOM   6042 H H    . CYS   B 1 143 ? 33.406 -27.599 -3.573  1.00 16.56 ?  143 CYS   B H    1 
ATOM   6043 H HA   . CYS   B 1 143 ? 33.485 -25.135 -4.349  1.00 16.46 ?  143 CYS   B HA   1 
ATOM   6044 H HB2  . CYS   B 1 143 ? 35.337 -26.560 -4.547  1.00 17.18 ?  143 CYS   B HB2  1 
ATOM   6045 H HB3  . CYS   B 1 143 ? 34.596 -27.356 -5.695  1.00 17.18 ?  143 CYS   B HB3  1 
ATOM   6046 H HG   . CYS   B 1 143 ? 36.530 -25.843 -6.849  1.00 17.55 ?  143 CYS   B HG   1 
ATOM   6047 N N    . VAL   B 1 144 ? 31.942 -26.996 -6.469  1.00 14.74 ?  144 VAL   B N    1 
ATOM   6048 C CA   . VAL   B 1 144 ? 31.033 -26.942 -7.608  1.00 15.70 ?  144 VAL   B CA   1 
ATOM   6049 C C    . VAL   B 1 144 ? 29.691 -26.319 -7.235  1.00 15.98 ?  144 VAL   B C    1 
ATOM   6050 O O    . VAL   B 1 144 ? 29.072 -25.618 -8.049  1.00 17.07 ?  144 VAL   B O    1 
ATOM   6051 C CB   . VAL   B 1 144 ? 30.868 -28.361 -8.165  1.00 18.80 ?  144 VAL   B CB   1 
ATOM   6052 C CG1  . VAL   B 1 144 ? 29.590 -28.500 -8.979  1.00 21.75 ?  144 VAL   B CG1  1 
ATOM   6053 C CG2  . VAL   B 1 144 ? 32.093 -28.759 -8.975  1.00 19.14 ?  144 VAL   B CG2  1 
ATOM   6054 H H    . VAL   B 1 144 ? 32.174 -27.790 -6.225  1.00 17.66 ?  144 VAL   B H    1 
ATOM   6055 H HA   . VAL   B 1 144 ? 31.426 -26.394 -8.299  1.00 18.81 ?  144 VAL   B HA   1 
ATOM   6056 H HB   . VAL   B 1 144 ? 30.807 -28.983 -7.422  1.00 22.53 ?  144 VAL   B HB   1 
ATOM   6057 H HG11 . VAL   B 1 144 ? 29.658 -29.299 -9.533  1.00 26.08 ?  144 VAL   B HG11 1 
ATOM   6058 H HG12 . VAL   B 1 144 ? 28.836 -28.589 -8.376  1.00 26.08 ?  144 VAL   B HG12 1 
ATOM   6059 H HG13 . VAL   B 1 144 ? 29.485 -27.722 -9.542  1.00 26.08 ?  144 VAL   B HG13 1 
ATOM   6060 H HG21 . VAL   B 1 144 ? 31.978 -29.660 -9.312  1.00 22.94 ?  144 VAL   B HG21 1 
ATOM   6061 H HG22 . VAL   B 1 144 ? 32.194 -28.139 -9.719  1.00 22.94 ?  144 VAL   B HG22 1 
ATOM   6062 H HG23 . VAL   B 1 144 ? 32.879 -28.716 -8.406  1.00 22.94 ?  144 VAL   B HG23 1 
ATOM   6063 N N    . ASP   B 1 145 ? 29.218 -26.558 -6.014  1.00 15.93 ?  145 ASP   B N    1 
ATOM   6064 C CA   . ASP   B 1 145 ? 27.911 -26.083 -5.586  1.00 16.72 ?  145 ASP   B CA   1 
ATOM   6065 C C    . ASP   B 1 145 ? 27.950 -24.664 -5.046  1.00 16.43 ?  145 ASP   B C    1 
ATOM   6066 O O    . ASP   B 1 145 ? 26.895 -24.127 -4.691  1.00 17.97 ?  145 ASP   B O    1 
ATOM   6067 C CB   . ASP   B 1 145 ? 27.327 -26.990 -4.498  1.00 18.49 ?  145 ASP   B CB   1 
ATOM   6068 C CG   . ASP   B 1 145 ? 26.958 -28.365 -5.006  1.00 20.08 ?  145 ASP   B CG   1 
ATOM   6069 O OD1  . ASP   B 1 145 ? 26.837 -28.573 -6.234  1.00 19.85 ?  145 ASP   B OD1  1 
ATOM   6070 O OD2  . ASP   B 1 145 ? 26.773 -29.249 -4.150  1.00 22.34 -1 145 ASP   B OD2  1 
ATOM   6071 H H    . ASP   B 1 145 ? 29.651 -26.985 -5.405  1.00 19.08 ?  145 ASP   B H    1 
ATOM   6072 H HA   . ASP   B 1 145 ? 27.313 -26.080 -6.342  1.00 20.03 ?  145 ASP   B HA   1 
ATOM   6073 H HB2  . ASP   B 1 145 ? 27.981 -27.104 -3.795  1.00 22.15 ?  145 ASP   B HB2  1 
ATOM   6074 H HB3  . ASP   B 1 145 ? 26.524 -26.576 -4.143  1.00 22.15 ?  145 ASP   B HB3  1 
ATOM   6075 N N    . THR   B 1 146 ? 29.129 -24.042 -4.962  1.00 15.10 ?  146 THR   B N    1 
ATOM   6076 C CA   . THR   B 1 146 ? 29.269 -22.720 -4.358  1.00 14.83 ?  146 THR   B CA   1 
ATOM   6077 C C    . THR   B 1 146 ? 29.898 -21.700 -5.286  1.00 14.13 ?  146 THR   B C    1 
ATOM   6078 O O    . THR   B 1 146 ? 29.441 -20.545 -5.339  1.00 14.34 ?  146 THR   B O    1 
ATOM   6079 C CB   . THR   B 1 146 ? 30.104 -22.823 -3.075  1.00 14.73 ?  146 THR   B CB   1 
ATOM   6080 O OG1  . THR   B 1 146 ? 29.528 -23.808 -2.206  1.00 15.02 ?  146 THR   B OG1  1 
ATOM   6081 C CG2  . THR   B 1 146 ? 30.191 -21.477 -2.365  1.00 14.60 ?  146 THR   B CG2  1 
ATOM   6082 H H    . THR   B 1 146 ? 29.878 -24.361 -5.259  1.00 18.09 ?  146 THR   B H    1 
ATOM   6083 H HA   . THR   B 1 146 ? 28.399 -22.384 -4.116  1.00 17.77 ?  146 THR   B HA   1 
ATOM   6084 H HB   . THR   B 1 146 ? 31.009 -23.086 -3.301  1.00 17.65 ?  146 THR   B HB   1 
ATOM   6085 H HG1  . THR   B 1 146 ? 29.558 -24.566 -2.574  1.00 18.00 ?  146 THR   B HG1  1 
ATOM   6086 H HG21 . THR   B 1 146 ? 30.541 -21.595 -1.468  1.00 17.49 ?  146 THR   B HG21 1 
ATOM   6087 H HG22 . THR   B 1 146 ? 30.787 -20.881 -2.853  1.00 17.49 ?  146 THR   B HG22 1 
ATOM   6088 H HG23 . THR   B 1 146 ? 29.315 -21.071 -2.312  1.00 17.49 ?  146 THR   B HG23 1 
ATOM   6089 N N    . VAL   B 1 147 ? 30.951 -22.080 -5.999  1.00 13.88 ?  147 VAL   B N    1 
ATOM   6090 C CA   . VAL   B 1 147 ? 31.675 -21.137 -6.842  1.00 13.54 ?  147 VAL   B CA   1 
ATOM   6091 C C    . VAL   B 1 147 ? 30.943 -20.997 -8.163  1.00 14.18 ?  147 VAL   B C    1 
ATOM   6092 O O    . VAL   B 1 147 ? 30.562 -21.997 -8.787  1.00 14.70 ?  147 VAL   B O    1 
ATOM   6093 C CB   . VAL   B 1 147 ? 33.132 -21.588 -7.050  1.00 13.74 ?  147 VAL   B CB   1 
ATOM   6094 C CG1  . VAL   B 1 147 ? 33.884 -20.558 -7.891  1.00 14.06 ?  147 VAL   B CG1  1 
ATOM   6095 C CG2  . VAL   B 1 147 ? 33.832 -21.792 -5.709  1.00 13.91 ?  147 VAL   B CG2  1 
ATOM   6096 H H    . VAL   B 1 147 ? 31.269 -22.883 -6.020  1.00 16.63 ?  147 VAL   B H    1 
ATOM   6097 H HA   . VAL   B 1 147 ? 31.696 -20.270 -6.410  1.00 16.22 ?  147 VAL   B HA   1 
ATOM   6098 H HB   . VAL   B 1 147 ? 33.146 -22.432 -7.533  1.00 16.45 ?  147 VAL   B HB   1 
ATOM   6099 H HG11 . VAL   B 1 147 ? 34.833 -20.763 -7.877  1.00 16.85 ?  147 VAL   B HG11 1 
ATOM   6100 H HG12 . VAL   B 1 147 ? 33.556 -20.581 -8.802  1.00 16.85 ?  147 VAL   B HG12 1 
ATOM   6101 H HG13 . VAL   B 1 147 ? 33.738 -19.673 -7.511  1.00 16.85 ?  147 VAL   B HG13 1 
ATOM   6102 H HG21 . VAL   B 1 147 ? 34.767 -21.997 -5.865  1.00 16.67 ?  147 VAL   B HG21 1 
ATOM   6103 H HG22 . VAL   B 1 147 ? 33.755 -20.978 -5.188  1.00 16.67 ?  147 VAL   B HG22 1 
ATOM   6104 H HG23 . VAL   B 1 147 ? 33.406 -22.527 -5.240  1.00 16.67 ?  147 VAL   B HG23 1 
ATOM   6105 N N    . ARG   B 1 148 ? 30.736 -19.746 -8.581  1.00 13.46 ?  148 ARG   B N    1 
ATOM   6106 C CA   . ARG   B 1 148 ? 30.111 -19.425 -9.855  1.00 13.68 ?  148 ARG   B CA   1 
ATOM   6107 C C    . ARG   B 1 148 ? 31.061 -18.739 -10.828 1.00 13.73 ?  148 ARG   B C    1 
ATOM   6108 O O    . ARG   B 1 148 ? 30.764 -18.699 -12.027 1.00 15.21 ?  148 ARG   B O    1 
ATOM   6109 C CB   . ARG   B 1 148 ? 28.865 -18.549 -9.639  1.00 13.93 ?  148 ARG   B CB   1 
ATOM   6110 C CG   . ARG   B 1 148 ? 27.812 -19.258 -8.809  1.00 14.72 ?  148 ARG   B CG   1 
ATOM   6111 C CD   . ARG   B 1 148 ? 26.590 -18.381 -8.505  1.00 15.86 ?  148 ARG   B CD   1 
ATOM   6112 N NE   . ARG   B 1 148 ? 26.947 -17.177 -7.761  1.00 16.14 ?  148 ARG   B NE   1 
ATOM   6113 C CZ   . ARG   B 1 148 ? 27.255 -17.149 -6.470  1.00 15.15 ?  148 ARG   B CZ   1 
ATOM   6114 N NH1  . ARG   B 1 148 ? 27.209 -18.241 -5.721  1.00 15.19 ?  148 ARG   B NH1  1 
ATOM   6115 N NH2  . ARG   B 1 148 ? 27.651 -16.001 -5.922  1.00 15.35 ?  148 ARG   B NH2  1 
ATOM   6116 H H    . ARG   B 1 148 ? 30.963 -19.043 -8.124  1.00 16.13 ?  148 ARG   B H    1 
ATOM   6117 H HA   . ARG   B 1 148 ? 29.820 -20.251 -10.265 1.00 16.39 ?  148 ARG   B HA   1 
ATOM   6118 H HB2  . ARG   B 1 148 ? 29.126 -17.738 -9.173  1.00 16.68 ?  148 ARG   B HB2  1 
ATOM   6119 H HB3  . ARG   B 1 148 ? 28.481 -18.332 -10.500 1.00 16.68 ?  148 ARG   B HB3  1 
ATOM   6120 H HG2  . ARG   B 1 148 ? 27.508 -20.039 -9.293  1.00 17.63 ?  148 ARG   B HG2  1 
ATOM   6121 H HG3  . ARG   B 1 148 ? 28.207 -19.523 -7.963  1.00 17.63 ?  148 ARG   B HG3  1 
ATOM   6122 H HD2  . ARG   B 1 148 ? 26.181 -18.108 -9.340  1.00 19.01 ?  148 ARG   B HD2  1 
ATOM   6123 H HD3  . ARG   B 1 148 ? 25.962 -18.888 -7.971  1.00 19.01 ?  148 ARG   B HD3  1 
ATOM   6124 H HE   . ARG   B 1 148 ? 26.974 -16.432 -8.192  1.00 19.34 ?  148 ARG   B HE   1 
ATOM   6125 H HH11 . ARG   B 1 148 ? 26.960 -18.991 -6.063  1.00 18.20 ?  148 ARG   B HH11 1 
ATOM   6126 H HH12 . ARG   B 1 148 ? 27.411 -18.201 -4.885  1.00 18.20 ?  148 ARG   B HH12 1 
ATOM   6127 H HH21 . ARG   B 1 148 ? 27.694 -15.289 -6.399  1.00 18.39 ?  148 ARG   B HH21 1 
ATOM   6128 H HH22 . ARG   B 1 148 ? 27.854 -15.970 -5.086  1.00 18.39 ?  148 ARG   B HH22 1 
ATOM   6129 N N    . THR   B 1 149 ? 32.173 -18.191 -10.342 1.00 13.84 ?  149 THR   B N    1 
ATOM   6130 C CA   . THR   B 1 149 ? 33.210 -17.628 -11.191 1.00 13.89 ?  149 THR   B CA   1 
ATOM   6131 C C    . THR   B 1 149 ? 34.093 -18.762 -11.710 1.00 13.59 ?  149 THR   B C    1 
ATOM   6132 O O    . THR   B 1 149 ? 33.902 -19.934 -11.374 1.00 14.10 ?  149 THR   B O    1 
ATOM   6133 C CB   . THR   B 1 149 ? 33.988 -16.585 -10.402 1.00 14.17 ?  149 THR   B CB   1 
ATOM   6134 O OG1  . THR   B 1 149 ? 34.458 -17.194 -9.197  1.00 13.95 ?  149 THR   B OG1  1 
ATOM   6135 C CG2  . THR   B 1 149 ? 33.101 -15.381 -10.085 1.00 15.22 ?  149 THR   B CG2  1 
ATOM   6136 H H    . THR   B 1 149 ? 32.346 -18.134 -9.501  1.00 16.58 ?  149 THR   B H    1 
ATOM   6137 H HA   . THR   B 1 149 ? 32.796 -17.192 -11.951 1.00 16.64 ?  149 THR   B HA   1 
ATOM   6138 H HB   . THR   B 1 149 ? 34.743 -16.287 -10.925 1.00 16.98 ?  149 THR   B HB   1 
ATOM   6139 H HG1  . THR   B 1 149 ? 34.887 -16.629 -8.737  1.00 16.71 ?  149 THR   B HG1  1 
ATOM   6140 H HG21 . THR   B 1 149 ? 33.612 -14.715 -9.595  1.00 18.24 ?  149 THR   B HG21 1 
ATOM   6141 H HG22 . THR   B 1 149 ? 32.777 -14.983 -10.909 1.00 18.24 ?  149 THR   B HG22 1 
ATOM   6142 H HG23 . THR   B 1 149 ? 32.343 -15.654 -9.547  1.00 18.24 ?  149 THR   B HG23 1 
ATOM   6143 N N    . ASN   B 1 150 ? 35.051 -18.433 -12.565 1.00 13.72 ?  150 ASN   B N    1 
ATOM   6144 C CA   . ASN   B 1 150 ? 35.821 -19.453 -13.267 1.00 13.93 ?  150 ASN   B CA   1 
ATOM   6145 C C    . ASN   B 1 150 ? 36.989 -19.907 -12.395 1.00 13.45 ?  150 ASN   B C    1 
ATOM   6146 O O    . ASN   B 1 150 ? 37.932 -19.147 -12.158 1.00 14.27 ?  150 ASN   B O    1 
ATOM   6147 C CB   . ASN   B 1 150 ? 36.290 -18.924 -14.615 1.00 16.14 ?  150 ASN   B CB   1 
ATOM   6148 C CG   . ASN   B 1 150 ? 35.146 -18.709 -15.570 1.00 19.42 ?  150 ASN   B CG   1 
ATOM   6149 O OD1  . ASN   B 1 150 ? 34.230 -19.522 -15.639 1.00 20.60 ?  150 ASN   B OD1  1 
ATOM   6150 N ND2  . ASN   B 1 150 ? 35.171 -17.599 -16.289 1.00 21.63 ?  150 ASN   B ND2  1 
ATOM   6151 H H    . ASN   B 1 150 ? 35.281 -17.623 -12.752 1.00 16.43 ?  150 ASN   B H    1 
ATOM   6152 H HA   . ASN   B 1 150 ? 35.244 -20.221 -13.430 1.00 16.69 ?  150 ASN   B HA   1 
ATOM   6153 H HB2  . ASN   B 1 150 ? 36.737 -18.073 -14.482 1.00 19.34 ?  150 ASN   B HB2  1 
ATOM   6154 H HB3  . ASN   B 1 150 ? 36.900 -19.564 -15.012 1.00 19.34 ?  150 ASN   B HB3  1 
ATOM   6155 H HD21 . ASN   B 1 150 ? 34.540 -17.430 -16.852 1.00 25.92 ?  150 ASN   B HD21 1 
ATOM   6156 H HD22 . ASN   B 1 150 ? 35.826 -17.043 -16.208 1.00 25.92 ?  150 ASN   B HD22 1 
ATOM   6157 N N    . VAL   B 1 151 ? 36.935 -21.148 -11.917 1.00 13.17 ?  151 VAL   B N    1 
ATOM   6158 C CA   . VAL   B 1 151 ? 37.958 -21.687 -11.029 1.00 13.24 ?  151 VAL   B CA   1 
ATOM   6159 C C    . VAL   B 1 151 ? 38.652 -22.864 -11.705 1.00 13.00 ?  151 VAL   B C    1 
ATOM   6160 O O    . VAL   B 1 151 ? 37.999 -23.799 -12.198 1.00 14.23 ?  151 VAL   B O    1 
ATOM   6161 C CB   . VAL   B 1 151 ? 37.403 -22.046 -9.634  1.00 14.49 ?  151 VAL   B CB   1 
ATOM   6162 C CG1  . VAL   B 1 151 ? 36.221 -23.025 -9.712  1.00 16.05 ?  151 VAL   B CG1  1 
ATOM   6163 C CG2  . VAL   B 1 151 ? 38.508 -22.577 -8.740  1.00 14.82 ?  151 VAL   B CG2  1 
ATOM   6164 H H    . VAL   B 1 151 ? 36.299 -21.709 -12.103 1.00 15.77 ?  151 VAL   B H    1 
ATOM   6165 H HA   . VAL   B 1 151 ? 38.623 -20.996 -10.898 1.00 15.85 ?  151 VAL   B HA   1 
ATOM   6166 H HB   . VAL   B 1 151 ? 37.071 -21.229 -9.225  1.00 17.35 ?  151 VAL   B HB   1 
ATOM   6167 H HG11 . VAL   B 1 151 ? 35.917 -23.218 -8.811  1.00 19.23 ?  151 VAL   B HG11 1 
ATOM   6168 H HG12 . VAL   B 1 151 ? 35.504 -22.612 -10.220 1.00 19.23 ?  151 VAL   B HG12 1 
ATOM   6169 H HG13 . VAL   B 1 151 ? 36.514 -23.836 -10.147 1.00 19.23 ?  151 VAL   B HG13 1 
ATOM   6170 H HG21 . VAL   B 1 151 ? 38.170 -22.646 -7.832  1.00 17.76 ?  151 VAL   B HG21 1 
ATOM   6171 H HG22 . VAL   B 1 151 ? 38.779 -23.453 -9.056  1.00 17.76 ?  151 VAL   B HG22 1 
ATOM   6172 H HG23 . VAL   B 1 151 ? 39.259 -21.966 -8.766  1.00 17.76 ?  151 VAL   B HG23 1 
ATOM   6173 N N    . TYR   B 1 152 ? 39.984 -22.790 -11.726 1.00 12.58 ?  152 TYR   B N    1 
ATOM   6174 C CA   . TYR   B 1 152 ? 40.875 -23.779 -12.315 1.00 12.71 ?  152 TYR   B CA   1 
ATOM   6175 C C    . TYR   B 1 152 ? 41.600 -24.462 -11.160 1.00 12.14 ?  152 TYR   B C    1 
ATOM   6176 O O    . TYR   B 1 152 ? 42.450 -23.849 -10.509 1.00 12.81 ?  152 TYR   B O    1 
ATOM   6177 C CB   . TYR   B 1 152 ? 41.842 -23.075 -13.269 1.00 13.84 ?  152 TYR   B CB   1 
ATOM   6178 C CG   . TYR   B 1 152 ? 41.157 -22.591 -14.527 1.00 14.32 ?  152 TYR   B CG   1 
ATOM   6179 C CD1  . TYR   B 1 152 ? 40.509 -21.360 -14.571 1.00 14.46 ?  152 TYR   B CD1  1 
ATOM   6180 C CD2  . TYR   B 1 152 ? 41.123 -23.387 -15.660 1.00 15.61 ?  152 TYR   B CD2  1 
ATOM   6181 C CE1  . TYR   B 1 152 ? 39.870 -20.934 -15.715 1.00 16.33 ?  152 TYR   B CE1  1 
ATOM   6182 C CE2  . TYR   B 1 152 ? 40.486 -22.969 -16.808 1.00 16.73 ?  152 TYR   B CE2  1 
ATOM   6183 C CZ   . TYR   B 1 152 ? 39.866 -21.738 -16.834 1.00 16.72 ?  152 TYR   B CZ   1 
ATOM   6184 O OH   . TYR   B 1 152 ? 39.235 -21.327 -17.981 1.00 19.75 ?  152 TYR   B OH   1 
ATOM   6185 H H    . TYR   B 1 152 ? 40.421 -22.126 -11.377 1.00 15.07 ?  152 TYR   B H    1 
ATOM   6186 H HA   . TYR   B 1 152 ? 40.360 -24.437 -12.802 1.00 15.23 ?  152 TYR   B HA   1 
ATOM   6187 H HB2  . TYR   B 1 152 ? 42.225 -22.308 -12.817 1.00 16.58 ?  152 TYR   B HB2  1 
ATOM   6188 H HB3  . TYR   B 1 152 ? 42.545 -23.692 -13.522 1.00 16.58 ?  152 TYR   B HB3  1 
ATOM   6189 H HD1  . TYR   B 1 152 ? 40.515 -20.814 -13.815 1.00 17.32 ?  152 TYR   B HD1  1 
ATOM   6190 H HD2  . TYR   B 1 152 ? 41.544 -24.217 -15.648 1.00 18.71 ?  152 TYR   B HD2  1 
ATOM   6191 H HE1  . TYR   B 1 152 ? 39.448 -20.102 -15.736 1.00 19.57 ?  152 TYR   B HE1  1 
ATOM   6192 H HE2  . TYR   B 1 152 ? 40.482 -23.509 -17.564 1.00 20.04 ?  152 TYR   B HE2  1 
ATOM   6193 H HH   . TYR   B 1 152 ? 38.895 -20.561 -17.862 1.00 23.67 ?  152 TYR   B HH   1 
ATOM   6194 N N    . LEU   B 1 153 ? 41.238 -25.718 -10.887 1.00 12.41 ?  153 LEU   B N    1 
ATOM   6195 C CA   . LEU   B 1 153 ? 41.753 -26.459 -9.746  1.00 12.03 ?  153 LEU   B CA   1 
ATOM   6196 C C    . LEU   B 1 153 ? 42.978 -27.259 -10.155 1.00 12.27 ?  153 LEU   B C    1 
ATOM   6197 O O    . LEU   B 1 153 ? 42.946 -27.985 -11.153 1.00 13.63 ?  153 LEU   B O    1 
ATOM   6198 C CB   . LEU   B 1 153 ? 40.687 -27.423 -9.221  1.00 12.56 ?  153 LEU   B CB   1 
ATOM   6199 C CG   . LEU   B 1 153 ? 39.430 -26.776 -8.641  1.00 13.46 ?  153 LEU   B CG   1 
ATOM   6200 C CD1  . LEU   B 1 153 ? 38.341 -27.829 -8.487  1.00 14.37 ?  153 LEU   B CD1  1 
ATOM   6201 C CD2  . LEU   B 1 153 ? 39.740 -26.110 -7.304  1.00 13.80 ?  153 LEU   B CD2  1 
ATOM   6202 H H    . LEU   B 1 153 ? 40.663 -26.161 -11.355 1.00 14.86 ?  153 LEU   B H    1 
ATOM   6203 H HA   . LEU   B 1 153 ? 41.992 -25.842 -9.041  1.00 14.41 ?  153 LEU   B HA   1 
ATOM   6204 H HB2  . LEU   B 1 153 ? 40.404 -27.996 -9.947  1.00 15.04 ?  153 LEU   B HB2  1 
ATOM   6205 H HB3  . LEU   B 1 153 ? 41.083 -27.960 -8.517  1.00 15.04 ?  153 LEU   B HB3  1 
ATOM   6206 H HG   . LEU   B 1 153 ? 39.110 -26.088 -9.249  1.00 16.13 ?  153 LEU   B HG   1 
ATOM   6207 H HD11 . LEU   B 1 153 ? 37.538 -27.402 -8.143  1.00 17.22 ?  153 LEU   B HD11 1 
ATOM   6208 H HD12 . LEU   B 1 153 ? 38.160 -28.219 -9.353  1.00 17.22 ?  153 LEU   B HD12 1 
ATOM   6209 H HD13 . LEU   B 1 153 ? 38.645 -28.507 -7.868  1.00 17.22 ?  153 LEU   B HD13 1 
ATOM   6210 H HD21 . LEU   B 1 153 ? 38.925 -25.740 -6.933  1.00 16.53 ?  153 LEU   B HD21 1 
ATOM   6211 H HD22 . LEU   B 1 153 ? 40.106 -26.777 -6.698  1.00 16.53 ?  153 LEU   B HD22 1 
ATOM   6212 H HD23 . LEU   B 1 153 ? 40.392 -25.403 -7.444  1.00 16.53 ?  153 LEU   B HD23 1 
ATOM   6213 N N    . ALA   B 1 154 ? 44.040 -27.146 -9.365  1.00 12.54 ?  154 ALA   B N    1 
ATOM   6214 C CA   . ALA   B 1 154 ? 45.268 -27.908 -9.561  1.00 14.02 ?  154 ALA   B CA   1 
ATOM   6215 C C    . ALA   B 1 154 ? 45.345 -28.991 -8.491  1.00 15.12 ?  154 ALA   B C    1 
ATOM   6216 O O    . ALA   B 1 154 ? 45.313 -28.691 -7.289  1.00 17.24 ?  154 ALA   B O    1 
ATOM   6217 C CB   . ALA   B 1 154 ? 46.494 -26.998 -9.503  1.00 15.66 ?  154 ALA   B CB   1 
ATOM   6218 H H    . ALA   B 1 154 ? 44.067 -26.608 -8.694  1.00 15.02 ?  154 ALA   B H    1 
ATOM   6219 H HA   . ALA   B 1 154 ? 45.242 -28.334 -10.430 1.00 16.79 ?  154 ALA   B HA   1 
ATOM   6220 H HB1  . ALA   B 1 154 ? 47.289 -27.537 -9.635  1.00 18.76 ?  154 ALA   B HB1  1 
ATOM   6221 H HB2  . ALA   B 1 154 ? 46.427 -26.331 -10.207 1.00 18.76 ?  154 ALA   B HB2  1 
ATOM   6222 H HB3  . ALA   B 1 154 ? 46.527 -26.563 -8.638  1.00 18.76 ?  154 ALA   B HB3  1 
ATOM   6223 N N    . VAL   B 1 155 ? 45.430 -30.241 -8.926  1.00 14.22 ?  155 VAL   B N    1 
ATOM   6224 C CA   . VAL   B 1 155 ? 45.538 -31.384 -8.029  1.00 15.01 ?  155 VAL   B CA   1 
ATOM   6225 C C    . VAL   B 1 155 ? 46.864 -32.069 -8.325  1.00 14.53 ?  155 VAL   B C    1 
ATOM   6226 O O    . VAL   B 1 155 ? 47.082 -32.559 -9.441  1.00 16.70 ?  155 VAL   B O    1 
ATOM   6227 C CB   . VAL   B 1 155 ? 44.363 -32.364 -8.193  1.00 16.52 ?  155 VAL   B CB   1 
ATOM   6228 C CG1  . VAL   B 1 155 ? 44.551 -33.565 -7.276  1.00 16.64 ?  155 VAL   B CG1  1 
ATOM   6229 C CG2  . VAL   B 1 155 ? 43.037 -31.658 -7.908  1.00 17.41 ?  155 VAL   B CG2  1 
ATOM   6230 H H    . VAL   B 1 155 ? 45.439 -30.457 -9.760  1.00 17.03 ?  155 VAL   B H    1 
ATOM   6231 H HA   . VAL   B 1 155 ? 45.552 -31.077 -7.113  1.00 17.98 ?  155 VAL   B HA   1 
ATOM   6232 H HB   . VAL   B 1 155 ? 44.338 -32.683 -9.108  1.00 19.80 ?  155 VAL   B HB   1 
ATOM   6233 H HG11 . VAL   B 1 155 ? 43.718 -34.061 -7.229  1.00 19.94 ?  155 VAL   B HG11 1 
ATOM   6234 H HG12 . VAL   B 1 155 ? 45.251 -34.133 -7.634  1.00 19.94 ?  155 VAL   B HG12 1 
ATOM   6235 H HG13 . VAL   B 1 155 ? 44.797 -33.252 -6.391  1.00 19.94 ?  155 VAL   B HG13 1 
ATOM   6236 H HG21 . VAL   B 1 155 ? 42.312 -32.302 -7.985  1.00 20.87 ?  155 VAL   B HG21 1 
ATOM   6237 H HG22 . VAL   B 1 155 ? 43.057 -31.294 -7.008  1.00 20.87 ?  155 VAL   B HG22 1 
ATOM   6238 H HG23 . VAL   B 1 155 ? 42.909 -30.943 -8.551  1.00 20.87 ?  155 VAL   B HG23 1 
ATOM   6239 N N    . PHE   B 1 156 ? 47.741 -32.119 -7.320  1.00 15.11 ?  156 PHE   B N    1 
ATOM   6240 C CA   . PHE   B 1 156 ? 49.115 -32.586 -7.531  1.00 15.94 ?  156 PHE   B CA   1 
ATOM   6241 C C    . PHE   B 1 156 ? 49.197 -34.088 -7.805  1.00 17.25 ?  156 PHE   B C    1 
ATOM   6242 O O    . PHE   B 1 156 ? 49.893 -34.522 -8.731  1.00 19.23 ?  156 PHE   B O    1 
ATOM   6243 C CB   . PHE   B 1 156 ? 49.953 -32.220 -6.309  1.00 15.94 ?  156 PHE   B CB   1 
ATOM   6244 C CG   . PHE   B 1 156 ? 51.377 -32.682 -6.381  1.00 16.58 ?  156 PHE   B CG   1 
ATOM   6245 C CD1  . PHE   B 1 156 ? 52.232 -32.186 -7.345  1.00 18.44 ?  156 PHE   B CD1  1 
ATOM   6246 C CD2  . PHE   B 1 156 ? 51.863 -33.597 -5.470  1.00 16.73 ?  156 PHE   B CD2  1 
ATOM   6247 C CE1  . PHE   B 1 156 ? 53.554 -32.603 -7.405  1.00 18.99 ?  156 PHE   B CE1  1 
ATOM   6248 C CE2  . PHE   B 1 156 ? 53.178 -34.018 -5.527  1.00 18.21 ?  156 PHE   B CE2  1 
ATOM   6249 C CZ   . PHE   B 1 156 ? 54.020 -33.519 -6.498  1.00 18.91 ?  156 PHE   B CZ   1 
ATOM   6250 H H    . PHE   B 1 156 ? 47.565 -31.893 -6.511  1.00 18.11 ?  156 PHE   B H    1 
ATOM   6251 H HA   . PHE   B 1 156 ? 49.486 -32.124 -8.295  1.00 19.10 ?  156 PHE   B HA   1 
ATOM   6252 H HB2  . PHE   B 1 156 ? 49.959 -31.255 -6.218  1.00 19.10 ?  156 PHE   B HB2  1 
ATOM   6253 H HB3  . PHE   B 1 156 ? 49.551 -32.621 -5.522  1.00 19.10 ?  156 PHE   B HB3  1 
ATOM   6254 H HD1  . PHE   B 1 156 ? 51.917 -31.562 -7.964  1.00 22.10 ?  156 PHE   B HD1  1 
ATOM   6255 H HD2  . PHE   B 1 156 ? 51.295 -33.939 -4.816  1.00 20.04 ?  156 PHE   B HD2  1 
ATOM   6256 H HE1  . PHE   B 1 156 ? 54.119 -32.265 -8.062  1.00 22.76 ?  156 PHE   B HE1  1 
ATOM   6257 H HE2  . PHE   B 1 156 ? 53.497 -34.642 -4.913  1.00 21.83 ?  156 PHE   B HE2  1 
ATOM   6258 H HZ   . PHE   B 1 156 ? 54.903 -33.803 -6.537  1.00 22.66 ?  156 PHE   B HZ   1 
ATOM   6259 N N    . ASP   B 1 157 ? 48.548 -34.901 -6.983  1.00 17.86 ?  157 ASP   B N    1 
ATOM   6260 C CA   . ASP   B 1 157 ? 48.689 -36.349 -7.077  1.00 19.45 ?  157 ASP   B CA   1 
ATOM   6261 C C    . ASP   B 1 157 ? 47.765 -36.897 -8.160  1.00 19.30 ?  157 ASP   B C    1 
ATOM   6262 O O    . ASP   B 1 157 ? 46.539 -36.775 -8.056  1.00 18.69 ?  157 ASP   B O    1 
ATOM   6263 C CB   . ASP   B 1 157 ? 48.344 -36.957 -5.724  1.00 20.97 ?  157 ASP   B CB   1 
ATOM   6264 C CG   . ASP   B 1 157 ? 48.504 -38.461 -5.702  1.00 23.26 ?  157 ASP   B CG   1 
ATOM   6265 O OD1  . ASP   B 1 157 ? 48.838 -39.057 -6.752  1.00 23.56 ?  157 ASP   B OD1  1 
ATOM   6266 O OD2  . ASP   B 1 157 ? 48.299 -39.046 -4.623  1.00 25.62 -1 157 ASP   B OD2  1 
ATOM   6267 H H    . ASP   B 1 157 ? 48.025 -34.638 -6.359  1.00 21.41 ?  157 ASP   B H    1 
ATOM   6268 H HA   . ASP   B 1 157 ? 49.605 -36.582 -7.301  1.00 23.31 ?  157 ASP   B HA   1 
ATOM   6269 H HB2  . ASP   B 1 157 ? 48.919 -36.565 -5.047  1.00 25.13 ?  157 ASP   B HB2  1 
ATOM   6270 H HB3  . ASP   B 1 157 ? 47.417 -36.750 -5.520  1.00 25.13 ?  157 ASP   B HB3  1 
ATOM   6271 N N    A LYS   B 1 158 ? 48.353 -37.532 -9.180  0.66 20.18 ?  158 LYS   B N    1 
ATOM   6272 N N    B LYS   B 1 158 ? 48.356 -37.499 -9.198  0.34 19.83 ?  158 LYS   B N    1 
ATOM   6273 C CA   A LYS   B 1 158 ? 47.573 -38.158 -10.249 0.66 21.27 ?  158 LYS   B CA   1 
ATOM   6274 C CA   B LYS   B 1 158 ? 47.577 -38.065 -10.297 0.34 20.67 ?  158 LYS   B CA   1 
ATOM   6275 C C    A LYS   B 1 158 ? 46.509 -39.108 -9.701  0.66 21.58 ?  158 LYS   B C    1 
ATOM   6276 C C    B LYS   B 1 158 ? 46.518 -39.043 -9.801  0.34 20.57 ?  158 LYS   B C    1 
ATOM   6277 O O    A LYS   B 1 158 ? 45.390 -39.175 -10.227 0.66 21.52 ?  158 LYS   B O    1 
ATOM   6278 O O    B LYS   B 1 158 ? 45.431 -39.133 -10.385 0.34 20.56 ?  158 LYS   B O    1 
ATOM   6279 C CB   A LYS   B 1 158 ? 48.520 -38.899 -11.201 0.66 23.27 ?  158 LYS   B CB   1 
ATOM   6280 C CB   B LYS   B 1 158 ? 48.523 -38.753 -11.291 0.34 22.12 ?  158 LYS   B CB   1 
ATOM   6281 C CG   A LYS   B 1 158 ? 47.836 -39.809 -12.213 0.66 25.54 ?  158 LYS   B CG   1 
ATOM   6282 C CG   B LYS   B 1 158 ? 47.850 -39.689 -12.291 0.34 23.66 ?  158 LYS   B CG   1 
ATOM   6283 C CD   A LYS   B 1 158 ? 46.998 -39.026 -13.205 0.66 27.54 ?  158 LYS   B CD   1 
ATOM   6284 C CD   B LYS   B 1 158 ? 46.956 -38.941 -13.264 0.34 25.25 ?  158 LYS   B CD   1 
ATOM   6285 C CE   A LYS   B 1 158 ? 46.376 -39.949 -14.240 0.66 29.39 ?  158 LYS   B CE   1 
ATOM   6286 C CE   B LYS   B 1 158 ? 46.368 -39.885 -14.303 0.34 26.57 ?  158 LYS   B CE   1 
ATOM   6287 N NZ   A LYS   B 1 158 ? 45.312 -39.270 -15.032 0.66 30.01 ?  158 LYS   B NZ   1 
ATOM   6288 N NZ   B LYS   B 1 158 ? 45.319 -39.226 -15.131 0.34 27.03 ?  158 LYS   B NZ   1 
ATOM   6289 H H    A LYS   B 1 158 ? 49.206 -37.615 -9.269  0.66 24.19 ?  158 LYS   B H    1 
ATOM   6290 H H    B LYS   B 1 158 ? 49.206 -37.595 -9.285  0.34 23.77 ?  158 LYS   B H    1 
ATOM   6291 H HA   A LYS   B 1 158 ? 47.129 -37.464 -10.760 0.66 25.50 ?  158 LYS   B HA   1 
ATOM   6292 H HA   B LYS   B 1 158 ? 47.126 -37.349 -10.769 0.34 24.77 ?  158 LYS   B HA   1 
ATOM   6293 H HB2  A LYS   B 1 158 ? 49.034 -38.243 -11.704 0.66 27.90 ?  158 LYS   B HB2  1 
ATOM   6294 H HB2  B LYS   B 1 158 ? 48.985 -38.068 -11.805 0.34 26.52 ?  158 LYS   B HB2  1 
ATOM   6295 H HB3  A LYS   B 1 158 ? 49.125 -39.446 -10.676 0.66 27.90 ?  158 LYS   B HB3  1 
ATOM   6296 H HB3  B LYS   B 1 158 ? 49.172 -39.275 -10.795 0.34 26.52 ?  158 LYS   B HB3  1 
ATOM   6297 H HG2  A LYS   B 1 158 ? 48.516 -40.286 -12.713 0.66 30.61 ?  158 LYS   B HG2  1 
ATOM   6298 H HG2  B LYS   B 1 158 ? 48.538 -40.135 -12.806 0.34 28.37 ?  158 LYS   B HG2  1 
ATOM   6299 H HG3  A LYS   B 1 158 ? 47.262 -40.445 -11.757 0.66 30.61 ?  158 LYS   B HG3  1 
ATOM   6300 H HG3  B LYS   B 1 158 ? 47.316 -40.350 -11.823 0.34 28.37 ?  158 LYS   B HG3  1 
ATOM   6301 H HD2  A LYS   B 1 158 ? 46.284 -38.569 -12.734 0.66 33.02 ?  158 LYS   B HD2  1 
ATOM   6302 H HD2  B LYS   B 1 158 ? 46.225 -38.528 -12.779 0.34 30.28 ?  158 LYS   B HD2  1 
ATOM   6303 H HD3  A LYS   B 1 158 ? 47.561 -38.385 -13.667 0.66 33.02 ?  158 LYS   B HD3  1 
ATOM   6304 H HD3  B LYS   B 1 158 ? 47.478 -38.266 -13.726 0.34 30.28 ?  158 LYS   B HD3  1 
ATOM   6305 H HE2  A LYS   B 1 158 ? 47.065 -40.247 -14.853 0.66 35.24 ?  158 LYS   B HE2  1 
ATOM   6306 H HE2  B LYS   B 1 158 ? 47.075 -40.187 -14.895 0.34 31.85 ?  158 LYS   B HE2  1 
ATOM   6307 H HE3  A LYS   B 1 158 ? 45.979 -40.710 -13.789 0.66 35.24 ?  158 LYS   B HE3  1 
ATOM   6308 H HE3  B LYS   B 1 158 ? 45.965 -40.644 -13.852 0.34 31.85 ?  158 LYS   B HE3  1 
ATOM   6309 H HZ1  A LYS   B 1 158 ? 44.968 -39.834 -15.627 0.66 35.98 ?  158 LYS   B HZ1  1 
ATOM   6310 H HZ1  B LYS   B 1 158 ? 44.995 -39.802 -15.727 0.34 32.40 ?  158 LYS   B HZ1  1 
ATOM   6311 H HZ2  A LYS   B 1 158 ? 44.663 -38.988 -14.492 0.66 35.98 ?  158 LYS   B HZ2  1 
ATOM   6312 H HZ2  B LYS   B 1 158 ? 44.654 -38.944 -14.611 0.34 32.40 ?  158 LYS   B HZ2  1 
ATOM   6313 H HZ3  A LYS   B 1 158 ? 45.654 -38.569 -15.462 0.66 35.98 ?  158 LYS   B HZ3  1 
ATOM   6314 H HZ3  B LYS   B 1 158 ? 45.666 -38.528 -15.561 0.34 32.40 ?  158 LYS   B HZ3  1 
ATOM   6315 N N    A ASN   B 1 159 ? 46.839 -39.867 -8.655  0.66 21.70 ?  159 ASN   B N    1 
ATOM   6316 N N    B ASN   B 1 159 ? 46.815 -39.790 -8.736  0.34 20.58 ?  159 ASN   B N    1 
ATOM   6317 C CA   A ASN   B 1 159 ? 45.882 -40.841 -8.138  0.66 22.14 ?  159 ASN   B CA   1 
ATOM   6318 C CA   B ASN   B 1 159 ? 45.860 -40.778 -8.243  0.34 20.66 ?  159 ASN   B CA   1 
ATOM   6319 C C    A ASN   B 1 159 ? 44.690 -40.160 -7.468  0.66 20.87 ?  159 ASN   B C    1 
ATOM   6320 C C    B ASN   B 1 159 ? 44.673 -40.111 -7.549  0.34 20.26 ?  159 ASN   B C    1 
ATOM   6321 O O    A ASN   B 1 159 ? 43.562 -40.663 -7.542  0.66 20.84 ?  159 ASN   B O    1 
ATOM   6322 O O    B ASN   B 1 159 ? 43.533 -40.575 -7.676  0.34 20.11 ?  159 ASN   B O    1 
ATOM   6323 C CB   A ASN   B 1 159 ? 46.584 -41.806 -7.183  0.66 23.43 ?  159 ASN   B CB   1 
ATOM   6324 C CB   B ASN   B 1 159 ? 46.569 -41.776 -7.326  0.34 20.99 ?  159 ASN   B CB   1 
ATOM   6325 C CG   A ASN   B 1 159 ? 47.604 -42.681 -7.887  0.66 25.13 ?  159 ASN   B CG   1 
ATOM   6326 C CG   B ASN   B 1 159 ? 47.590 -42.621 -8.070  0.34 21.69 ?  159 ASN   B CG   1 
ATOM   6327 O OD1  A ASN   B 1 159 ? 47.349 -43.198 -8.981  0.66 26.07 ?  159 ASN   B OD1  1 
ATOM   6328 O OD1  B ASN   B 1 159 ? 47.348 -43.052 -9.201  0.34 22.04 ?  159 ASN   B OD1  1 
ATOM   6329 N ND2  A ASN   B 1 159 ? 48.769 -42.852 -7.263  0.66 25.72 ?  159 ASN   B ND2  1 
ATOM   6330 N ND2  B ASN   B 1 159 ? 48.742 -42.858 -7.441  0.34 22.17 ?  159 ASN   B ND2  1 
ATOM   6331 H H    A ASN   B 1 159 ? 47.587 -39.826 -8.237  0.66 26.01 ?  159 ASN   B H    1 
ATOM   6332 H H    B ASN   B 1 159 ? 47.551 -39.745 -8.297  0.34 24.66 ?  159 ASN   B H    1 
ATOM   6333 H HA   A ASN   B 1 159 ? 45.549 -41.361 -8.889  0.66 26.54 ?  159 ASN   B HA   1 
ATOM   6334 H HA   B ASN   B 1 159 ? 45.519 -41.277 -9.002  0.34 24.76 ?  159 ASN   B HA   1 
ATOM   6335 H HB2  A ASN   B 1 159 ? 47.045 -41.296 -6.500  0.66 28.08 ?  159 ASN   B HB2  1 
ATOM   6336 H HB2  B ASN   B 1 159 ? 47.033 -41.295 -6.626  0.34 25.16 ?  159 ASN   B HB2  1 
ATOM   6337 H HB3  A ASN   B 1 159 ? 45.922 -42.386 -6.782  0.66 28.08 ?  159 ASN   B HB3  1 
ATOM   6338 H HB3  B ASN   B 1 159 ? 45.911 -42.376 -6.941  0.34 25.16 ?  159 ASN   B HB3  1 
ATOM   6339 H HD21 A ASN   B 1 159 ? 49.382 -43.340 -7.619  0.66 30.83 ?  159 ASN   B HD21 1 
ATOM   6340 H HD21 B ASN   B 1 159 ? 49.354 -43.334 -7.819  0.34 26.57 ?  159 ASN   B HD21 1 
ATOM   6341 H HD22 A ASN   B 1 159 ? 48.906 -42.485 -6.496  0.66 30.83 ?  159 ASN   B HD22 1 
ATOM   6342 H HD22 B ASN   B 1 159 ? 48.875 -42.544 -6.650  0.34 26.57 ?  159 ASN   B HD22 1 
ATOM   6343 N N    . LEU   B 1 160 ? 44.909 -39.017 -6.819  1.00 20.19 ?  160 LEU   B N    1 
ATOM   6344 C CA   . LEU   B 1 160 ? 43.789 -38.270 -6.258  1.00 19.13 ?  160 LEU   B CA   1 
ATOM   6345 C C    . LEU   B 1 160 ? 42.989 -37.600 -7.367  1.00 18.42 ?  160 LEU   B C    1 
ATOM   6346 O O    . LEU   B 1 160 ? 41.751 -37.589 -7.330  1.00 17.86 ?  160 LEU   B O    1 
ATOM   6347 C CB   . LEU   B 1 160 ? 44.282 -37.238 -5.241  1.00 18.55 ?  160 LEU   B CB   1 
ATOM   6348 C CG   . LEU   B 1 160 ? 43.158 -36.336 -4.710  1.00 18.08 ?  160 LEU   B CG   1 
ATOM   6349 C CD1  . LEU   B 1 160 ? 42.047 -37.168 -4.083  1.00 19.60 ?  160 LEU   B CD1  1 
ATOM   6350 C CD2  . LEU   B 1 160 ? 43.687 -35.312 -3.709  1.00 17.73 ?  160 LEU   B CD2  1 
ATOM   6351 H H    A LEU   B 1 160 ? 45.685 -38.667 -6.695  0.66 24.20 ?  160 LEU   B H    1 
ATOM   6352 H H    B LEU   B 1 160 ? 45.689 -38.698 -6.650  0.34 24.20 ?  160 LEU   B H    1 
ATOM   6353 H HA   . LEU   B 1 160 ? 43.205 -38.889 -5.800  1.00 22.93 ?  160 LEU   B HA   1 
ATOM   6354 H HB2  . LEU   B 1 160 ? 44.679 -37.706 -4.485  1.00 22.23 ?  160 LEU   B HB2  1 
ATOM   6355 H HB3  . LEU   B 1 160 ? 44.953 -36.673 -5.662  1.00 22.23 ?  160 LEU   B HB3  1 
ATOM   6356 H HG   . LEU   B 1 160 ? 42.777 -35.843 -5.452  1.00 21.67 ?  160 LEU   B HG   1 
ATOM   6357 H HD11 . LEU   B 1 160 ? 41.439 -36.579 -3.616  1.00 23.49 ?  160 LEU   B HD11 1 
ATOM   6358 H HD12 . LEU   B 1 160 ? 41.571 -37.647 -4.783  1.00 23.49 ?  160 LEU   B HD12 1 
ATOM   6359 H HD13 . LEU   B 1 160 ? 42.439 -37.803 -3.460  1.00 23.49 ?  160 LEU   B HD13 1 
ATOM   6360 H HD21 . LEU   B 1 160 ? 42.954 -34.740 -3.431  1.00 21.25 ?  160 LEU   B HD21 1 
ATOM   6361 H HD22 . LEU   B 1 160 ? 44.054 -35.778 -2.943  1.00 21.25 ?  160 LEU   B HD22 1 
ATOM   6362 H HD23 . LEU   B 1 160 ? 44.378 -34.779 -4.136  1.00 21.25 ?  160 LEU   B HD23 1 
ATOM   6363 N N    A TYR   B 1 161 ? 43.681 -37.043 -8.365  0.66 18.49 ?  161 TYR   B N    1 
ATOM   6364 N N    B TYR   B 1 161 ? 43.678 -37.050 -8.373  0.34 18.34 ?  161 TYR   B N    1 
ATOM   6365 C CA   A TYR   B 1 161 ? 43.001 -36.476 -9.524  0.66 18.24 ?  161 TYR   B CA   1 
ATOM   6366 C CA   B TYR   B 1 161 ? 42.986 -36.472 -9.522  0.34 18.22 ?  161 TYR   B CA   1 
ATOM   6367 C C    A TYR   B 1 161 ? 42.044 -37.495 -10.131 0.66 18.16 ?  161 TYR   B C    1 
ATOM   6368 C C    B TYR   B 1 161 ? 42.046 -37.491 -10.152 0.34 18.21 ?  161 TYR   B C    1 
ATOM   6369 O O    A TYR   B 1 161 ? 40.871 -37.196 -10.377 0.66 18.48 ?  161 TYR   B O    1 
ATOM   6370 O O    B TYR   B 1 161 ? 40.885 -37.185 -10.447 0.34 18.28 ?  161 TYR   B O    1 
ATOM   6371 C CB   A TYR   B 1 161 ? 44.039 -36.014 -10.556 0.66 18.73 ?  161 TYR   B CB   1 
ATOM   6372 C CB   B TYR   B 1 161 ? 44.007 -35.968 -10.548 0.34 18.56 ?  161 TYR   B CB   1 
ATOM   6373 C CG   A TYR   B 1 161 ? 43.457 -35.538 -11.867 0.66 19.15 ?  161 TYR   B CG   1 
ATOM   6374 C CG   B TYR   B 1 161 ? 43.402 -35.500 -11.857 0.34 18.89 ?  161 TYR   B CG   1 
ATOM   6375 C CD1  A TYR   B 1 161 ? 43.089 -34.208 -12.039 0.66 19.15 ?  161 TYR   B CD1  1 
ATOM   6376 C CD1  B TYR   B 1 161 ? 43.005 -34.178 -12.027 0.34 18.99 ?  161 TYR   B CD1  1 
ATOM   6377 C CD2  A TYR   B 1 161 ? 43.267 -36.414 -12.929 0.66 19.64 ?  161 TYR   B CD2  1 
ATOM   6378 C CD2  B TYR   B 1 161 ? 43.228 -36.377 -12.922 0.34 19.03 ?  161 TYR   B CD2  1 
ATOM   6379 C CE1  A TYR   B 1 161 ? 42.555 -33.766 -13.232 0.66 20.18 ?  161 TYR   B CE1  1 
ATOM   6380 C CE1  B TYR   B 1 161 ? 42.451 -33.745 -13.219 0.34 19.58 ?  161 TYR   B CE1  1 
ATOM   6381 C CE2  A TYR   B 1 161 ? 42.730 -35.983 -14.123 0.66 20.64 ?  161 TYR   B CE2  1 
ATOM   6382 C CE2  B TYR   B 1 161 ? 42.673 -35.954 -14.116 0.34 19.65 ?  161 TYR   B CE2  1 
ATOM   6383 C CZ   A TYR   B 1 161 ? 42.376 -34.660 -14.271 0.66 20.88 ?  161 TYR   B CZ   1 
ATOM   6384 C CZ   B TYR   B 1 161 ? 42.288 -34.638 -14.259 0.34 19.95 ?  161 TYR   B CZ   1 
ATOM   6385 O OH   A TYR   B 1 161 ? 41.840 -34.228 -15.459 0.66 22.79 ?  161 TYR   B OH   1 
ATOM   6386 O OH   B TYR   B 1 161 ? 41.734 -34.213 -15.445 0.34 21.03 ?  161 TYR   B OH   1 
ATOM   6387 H H    A TYR   B 1 161 ? 44.538 -36.991 -8.399  0.66 22.16 ?  161 TYR   B H    1 
ATOM   6388 H H    B TYR   B 1 161 ? 44.535 -37.007 -8.417  0.34 21.98 ?  161 TYR   B H    1 
ATOM   6389 H HA   A TYR   B 1 161 ? 42.483 -35.707 -9.245  0.66 21.86 ?  161 TYR   B HA   1 
ATOM   6390 H HA   B TYR   B 1 161 ? 42.455 -35.718 -9.227  0.34 21.83 ?  161 TYR   B HA   1 
ATOM   6391 H HB2  A TYR   B 1 161 ? 44.543 -35.278 -10.176 0.66 22.45 ?  161 TYR   B HB2  1 
ATOM   6392 H HB2  B TYR   B 1 161 ? 44.488 -35.219 -10.163 0.34 22.24 ?  161 TYR   B HB2  1 
ATOM   6393 H HB3  A TYR   B 1 161 ? 44.633 -36.753 -10.752 0.66 22.45 ?  161 TYR   B HB3  1 
ATOM   6394 H HB3  B TYR   B 1 161 ? 44.625 -36.686 -10.752 0.34 22.24 ?  161 TYR   B HB3  1 
ATOM   6395 H HD1  A TYR   B 1 161 ? 43.207 -33.604 -11.341 0.66 22.95 ?  161 TYR   B HD1  1 
ATOM   6396 H HD1  B TYR   B 1 161 ? 43.112 -33.573 -11.329 0.34 22.76 ?  161 TYR   B HD1  1 
ATOM   6397 H HD2  A TYR   B 1 161 ? 43.499 -37.309 -12.834 0.66 23.54 ?  161 TYR   B HD2  1 
ATOM   6398 H HD2  B TYR   B 1 161 ? 43.485 -37.267 -12.830 0.34 22.80 ?  161 TYR   B HD2  1 
ATOM   6399 H HE1  A TYR   B 1 161 ? 42.311 -32.870 -13.332 0.66 24.18 ?  161 TYR   B HE1  1 
ATOM   6400 H HE1  B TYR   B 1 161 ? 42.188 -32.856 -13.318 0.34 23.46 ?  161 TYR   B HE1  1 
ATOM   6401 H HE2  A TYR   B 1 161 ? 42.604 -36.579 -14.826 0.66 24.74 ?  161 TYR   B HE2  1 
ATOM   6402 H HE2  B TYR   B 1 161 ? 42.561 -36.553 -14.819 0.34 23.55 ?  161 TYR   B HE2  1 
ATOM   6403 H HH   A TYR   B 1 161 ? 41.783 -34.864 -16.003 0.66 27.31 ?  161 TYR   B HH   1 
ATOM   6404 H HH   B TYR   B 1 161 ? 41.688 -34.852 -15.989 0.34 25.20 ?  161 TYR   B HH   1 
ATOM   6405 N N    . ASP   B 1 162 ? 42.533 -38.716 -10.359 1.00 18.62 ?  162 ASP   B N    1 
ATOM   6406 C CA   . ASP   B 1 162 ? 41.698 -39.752 -10.957 1.00 19.06 ?  162 ASP   B CA   1 
ATOM   6407 C C    . ASP   B 1 162 ? 40.497 -40.074 -10.073 1.00 19.01 ?  162 ASP   B C    1 
ATOM   6408 O O    . ASP   B 1 162 ? 39.381 -40.269 -10.573 1.00 19.70 ?  162 ASP   B O    1 
ATOM   6409 C CB   . ASP   B 1 162 ? 42.526 -41.019 -11.194 1.00 20.61 ?  162 ASP   B CB   1 
ATOM   6410 C CG   . ASP   B 1 162 ? 43.538 -40.873 -12.318 1.00 21.99 ?  162 ASP   B CG   1 
ATOM   6411 O OD1  . ASP   B 1 162 ? 43.430 -39.934 -13.128 1.00 22.03 ?  162 ASP   B OD1  1 
ATOM   6412 O OD2  . ASP   B 1 162 ? 44.419 -41.749 -12.419 1.00 23.83 -1 162 ASP   B OD2  1 
ATOM   6413 H H    A ASP   B 1 162 ? 43.336 -38.966 -10.179 0.66 22.32 ?  162 ASP   B H    1 
ATOM   6414 H H    B ASP   B 1 162 ? 43.332 -38.968 -10.166 0.34 22.32 ?  162 ASP   B H    1 
ATOM   6415 H HA   . ASP   B 1 162 ? 41.367 -39.445 -11.813 1.00 22.85 ?  162 ASP   B HA   1 
ATOM   6416 H HB2  . ASP   B 1 162 ? 43.023 -41.233 -10.393 1.00 24.70 ?  162 ASP   B HB2  1 
ATOM   6417 H HB3  . ASP   B 1 162 ? 41.934 -41.749 -11.429 1.00 24.70 ?  162 ASP   B HB3  1 
ATOM   6418 N N    . LYS   B 1 163 ? 40.708 -40.152 -8.756  1.00 18.53 ?  163 LYS   B N    1 
ATOM   6419 C CA   . LYS   B 1 163 ? 39.597 -40.424 -7.850  1.00 19.32 ?  163 LYS   B CA   1 
ATOM   6420 C C    . LYS   B 1 163 ? 38.557 -39.306 -7.895  1.00 18.12 ?  163 LYS   B C    1 
ATOM   6421 O O    . LYS   B 1 163 ? 37.345 -39.566 -7.857  1.00 19.14 ?  163 LYS   B O    1 
ATOM   6422 C CB   . LYS   B 1 163 ? 40.115 -40.616 -6.428  1.00 22.60 ?  163 LYS   B CB   1 
ATOM   6423 C CG   . LYS   B 1 163 ? 39.044 -41.070 -5.463  1.00 28.10 ?  163 LYS   B CG   1 
ATOM   6424 C CD   . LYS   B 1 163 ? 39.576 -41.285 -4.059  1.00 33.03 ?  163 LYS   B CD   1 
ATOM   6425 C CE   . LYS   B 1 163 ? 38.503 -41.908 -3.171  1.00 36.57 ?  163 LYS   B CE   1 
ATOM   6426 N NZ   . LYS   B 1 163 ? 38.780 -41.729 -1.719  1.00 39.25 ?  163 LYS   B NZ   1 
ATOM   6427 H H    . LYS   B 1 163 ? 41.474 -40.055 -8.372  1.00 22.21 ?  163 LYS   B H    1 
ATOM   6428 H HA   . LYS   B 1 163 ? 39.166 -41.247 -8.122  1.00 23.15 ?  163 LYS   B HA   1 
ATOM   6429 H HB2  . LYS   B 1 163 ? 40.815 -41.294 -6.435  1.00 27.09 ?  163 LYS   B HB2  1 
ATOM   6430 H HB3  . LYS   B 1 163 ? 40.475 -39.778 -6.103  1.00 27.09 ?  163 LYS   B HB3  1 
ATOM   6431 H HG2  . LYS   B 1 163 ? 38.351 -40.394 -5.421  1.00 33.70 ?  163 LYS   B HG2  1 
ATOM   6432 H HG3  . LYS   B 1 163 ? 38.671 -41.910 -5.778  1.00 33.70 ?  163 LYS   B HG3  1 
ATOM   6433 H HD2  . LYS   B 1 163 ? 40.335 -41.890 -4.091  1.00 39.60 ?  163 LYS   B HD2  1 
ATOM   6434 H HD3  . LYS   B 1 163 ? 39.836 -40.434 -3.678  1.00 39.60 ?  163 LYS   B HD3  1 
ATOM   6435 H HE2  . LYS   B 1 163 ? 37.646 -41.501 -3.370  1.00 43.85 ?  163 LYS   B HE2  1 
ATOM   6436 H HE3  . LYS   B 1 163 ? 38.461 -42.860 -3.352  1.00 43.85 ?  163 LYS   B HE3  1 
ATOM   6437 H HZ1  . LYS   B 1 163 ? 38.131 -42.103 -1.238  1.00 47.08 ?  163 LYS   B HZ1  1 
ATOM   6438 H HZ2  . LYS   B 1 163 ? 39.554 -42.113 -1.509  1.00 47.08 ?  163 LYS   B HZ2  1 
ATOM   6439 H HZ3  . LYS   B 1 163 ? 38.822 -40.862 -1.522  1.00 47.08 ?  163 LYS   B HZ3  1 
ATOM   6440 N N    . LEU   B 1 164 ? 39.016 -38.055 -7.973  1.00 16.41 ?  164 LEU   B N    1 
ATOM   6441 C CA   . LEU   B 1 164 ? 38.112 -36.909 -8.021  1.00 16.09 ?  164 LEU   B CA   1 
ATOM   6442 C C    . LEU   B 1 164 ? 37.312 -36.890 -9.319  1.00 16.79 ?  164 LEU   B C    1 
ATOM   6443 O O    . LEU   B 1 164 ? 36.086 -36.681 -9.307  1.00 17.91 ?  164 LEU   B O    1 
ATOM   6444 C CB   . LEU   B 1 164 ? 38.922 -35.620 -7.866  1.00 15.56 ?  164 LEU   B CB   1 
ATOM   6445 C CG   . LEU   B 1 164 ? 39.472 -35.349 -6.472  1.00 16.41 ?  164 LEU   B CG   1 
ATOM   6446 C CD1  . LEU   B 1 164 ? 40.556 -34.285 -6.548  1.00 16.71 ?  164 LEU   B CD1  1 
ATOM   6447 C CD2  . LEU   B 1 164 ? 38.365 -34.909 -5.529  1.00 17.62 ?  164 LEU   B CD2  1 
ATOM   6448 H H    . LEU   B 1 164 ? 39.855 -37.843 -7.997  1.00 19.67 ?  164 LEU   B H    1 
ATOM   6449 H HA   . LEU   B 1 164 ? 37.489 -36.969 -7.285  1.00 19.28 ?  164 LEU   B HA   1 
ATOM   6450 H HB2  . LEU   B 1 164 ? 39.679 -35.658 -8.474  1.00 18.64 ?  164 LEU   B HB2  1 
ATOM   6451 H HB3  . LEU   B 1 164 ? 38.354 -34.873 -8.104  1.00 18.64 ?  164 LEU   B HB3  1 
ATOM   6452 H HG   . LEU   B 1 164 ? 39.871 -36.160 -6.122  1.00 19.66 ?  164 LEU   B HG   1 
ATOM   6453 H HD11 . LEU   B 1 164 ? 40.895 -34.108 -5.655  1.00 20.03 ?  164 LEU   B HD11 1 
ATOM   6454 H HD12 . LEU   B 1 164 ? 41.282 -34.605 -7.113  1.00 20.03 ?  164 LEU   B HD12 1 
ATOM   6455 H HD13 . LEU   B 1 164 ? 40.184 -33.472 -6.925  1.00 20.03 ?  164 LEU   B HD13 1 
ATOM   6456 H HD21 . LEU   B 1 164 ? 38.752 -34.693 -4.667  1.00 21.11 ?  164 LEU   B HD21 1 
ATOM   6457 H HD22 . LEU   B 1 164 ? 37.925 -34.129 -5.900  1.00 21.11 ?  164 LEU   B HD22 1 
ATOM   6458 H HD23 . LEU   B 1 164 ? 37.728 -35.635 -5.433  1.00 21.11 ?  164 LEU   B HD23 1 
ATOM   6459 N N    . VAL   B 1 165 ? 37.990 -37.075 -10.454 1.00 19.11 ?  165 VAL   B N    1 
ATOM   6460 C CA   . VAL   B 1 165 ? 37.310 -37.006 -11.745 1.00 20.48 ?  165 VAL   B CA   1 
ATOM   6461 C C    . VAL   B 1 165 ? 36.364 -38.187 -11.905 1.00 22.85 ?  165 VAL   B C    1 
ATOM   6462 O O    . VAL   B 1 165 ? 35.185 -38.031 -12.254 1.00 24.55 ?  165 VAL   B O    1 
ATOM   6463 C CB   . VAL   B 1 165 ? 38.335 -36.953 -12.893 1.00 21.59 ?  165 VAL   B CB   1 
ATOM   6464 C CG1  . VAL   B 1 165 ? 37.630 -37.060 -14.227 1.00 23.10 ?  165 VAL   B CG1  1 
ATOM   6465 C CG2  . VAL   B 1 165 ? 39.151 -35.674 -12.827 1.00 21.21 ?  165 VAL   B CG2  1 
ATOM   6466 H H    . VAL   B 1 165 ? 38.842 -37.237 -10.503 1.00 22.91 ?  165 VAL   B H    1 
ATOM   6467 H HA   . VAL   B 1 165 ? 36.791 -36.191 -11.781 1.00 24.55 ?  165 VAL   B HA   1 
ATOM   6468 H HB   . VAL   B 1 165 ? 38.953 -37.697 -12.812 1.00 25.87 ?  165 VAL   B HB   1 
ATOM   6469 H HG11 . VAL   B 1 165 ? 38.218 -36.740 -14.927 1.00 27.69 ?  165 VAL   B HG11 1 
ATOM   6470 H HG12 . VAL   B 1 165 ? 37.409 -37.992 -14.388 1.00 27.69 ?  165 VAL   B HG12 1 
ATOM   6471 H HG13 . VAL   B 1 165 ? 36.821 -36.528 -14.201 1.00 27.69 ?  165 VAL   B HG13 1 
ATOM   6472 H HG21 . VAL   B 1 165 ? 39.769 -35.651 -13.577 1.00 25.42 ?  165 VAL   B HG21 1 
ATOM   6473 H HG22 . VAL   B 1 165 ? 38.550 -34.912 -12.877 1.00 25.42 ?  165 VAL   B HG22 1 
ATOM   6474 H HG23 . VAL   B 1 165 ? 39.645 -35.650 -11.993 1.00 25.42 ?  165 VAL   B HG23 1 
ATOM   6475 N N    . SER   B 1 166 ? 36.876 -39.395 -11.649 1.00 23.96 ?  166 SER   B N    1 
ATOM   6476 C CA   . SER   B 1 166 ? 36.116 -40.598 -11.948 1.00 25.67 ?  166 SER   B CA   1 
ATOM   6477 C C    . SER   B 1 166 ? 34.871 -40.700 -11.083 1.00 25.59 ?  166 SER   B C    1 
ATOM   6478 O O    . SER   B 1 166 ? 33.910 -41.354 -11.480 1.00 27.17 ?  166 SER   B O    1 
ATOM   6479 C CB   . SER   B 1 166 ? 36.986 -41.854 -11.807 1.00 26.54 ?  166 SER   B CB   1 
ATOM   6480 O OG   . SER   B 1 166 ? 37.358 -42.088 -10.459 1.00 26.63 ?  166 SER   B OG   1 
ATOM   6481 H H    . SER   B 1 166 ? 37.656 -39.539 -11.310 1.00 28.72 ?  166 SER   B H    1 
ATOM   6482 H HA   . SER   B 1 166 ? 35.826 -40.556 -12.874 1.00 30.78 ?  166 SER   B HA   1 
ATOM   6483 H HB2  . SER   B 1 166 ? 36.488 -42.620 -12.132 1.00 31.82 ?  166 SER   B HB2  1 
ATOM   6484 H HB3  . SER   B 1 166 ? 37.791 -41.738 -12.342 1.00 31.82 ?  166 SER   B HB3  1 
ATOM   6485 H HG   . SER   B 1 166 ? 37.798 -41.429 -10.171 1.00 31.93 ?  166 SER   B HG   1 
ATOM   6486 N N    . SER   B 1 167 ? 34.858 -40.080 -9.907  1.00 23.22 ?  167 SER   B N    1 
ATOM   6487 C CA   . SER   B 1 167 ? 33.705 -40.133 -9.016  1.00 23.54 ?  167 SER   B CA   1 
ATOM   6488 C C    . SER   B 1 167 ? 32.798 -38.904 -9.096  1.00 22.93 ?  167 SER   B C    1 
ATOM   6489 O O    . SER   B 1 167 ? 31.720 -38.916 -8.492  1.00 23.50 ?  167 SER   B O    1 
ATOM   6490 C CB   . SER   B 1 167 ? 34.164 -40.330 -7.565  1.00 23.51 ?  167 SER   B CB   1 
ATOM   6491 O OG   . SER   B 1 167 ? 34.855 -39.176 -7.104  1.00 23.60 ?  167 SER   B OG   1 
ATOM   6492 H H    . SER   B 1 167 ? 35.511 -39.627 -9.604  1.00 27.83 ?  167 SER   B H    1 
ATOM   6493 H HA   . SER   B 1 167 ? 33.160 -40.901 -9.255  1.00 28.22 ?  167 SER   B HA   1 
ATOM   6494 H HB2  . SER   B 1 167 ? 33.386 -40.483 -7.004  1.00 28.19 ?  167 SER   B HB2  1 
ATOM   6495 H HB3  . SER   B 1 167 ? 34.752 -41.107 -7.525  1.00 28.19 ?  167 SER   B HB3  1 
ATOM   6496 H HG   . SER   B 1 167 ? 35.542 -39.056 -7.572  1.00 28.30 ?  167 SER   B HG   1 
ATOM   6497 N N    . PHE   B 1 168 ? 33.189 -37.850 -9.821  1.00 22.37 ?  168 PHE   B N    1 
ATOM   6498 C CA   . PHE   B 1 168 ? 32.344 -36.655 -9.895  1.00 20.33 ?  168 PHE   B CA   1 
ATOM   6499 C C    . PHE   B 1 168 ? 31.057 -36.931 -10.672 1.00 17.38 ?  168 PHE   B C    1 
ATOM   6500 O O    . PHE   B 1 168 ? 29.989 -36.364 -10.357 1.00 17.43 ?  168 PHE   B O    1 
ATOM   6501 C CB   . PHE   B 1 168 ? 33.120 -35.491 -10.525 1.00 21.14 ?  168 PHE   B CB   1 
ATOM   6502 C CG   . PHE   B 1 168 ? 32.296 -34.259 -10.709 1.00 21.00 ?  168 PHE   B CG   1 
ATOM   6503 C CD1  . PHE   B 1 168 ? 31.922 -33.502 -9.612  1.00 22.41 ?  168 PHE   B CD1  1 
ATOM   6504 C CD2  . PHE   B 1 168 ? 31.876 -33.864 -11.966 1.00 20.36 ?  168 PHE   B CD2  1 
ATOM   6505 C CE1  . PHE   B 1 168 ? 31.143 -32.374 -9.761  1.00 22.21 ?  168 PHE   B CE1  1 
ATOM   6506 C CE2  . PHE   B 1 168 ? 31.108 -32.716 -12.129 1.00 22.23 ?  168 PHE   B CE2  1 
ATOM   6507 C CZ   . PHE   B 1 168 ? 30.736 -31.973 -11.022 1.00 21.92 ?  168 PHE   B CZ   1 
ATOM   6508 H H    . PHE   B 1 168 ? 33.925 -37.805 -10.269 1.00 26.82 ?  168 PHE   B H    1 
ATOM   6509 H HA   . PHE   B 1 168 ? 32.097 -36.394 -8.998  1.00 24.37 ?  168 PHE   B HA   1 
ATOM   6510 H HB2  . PHE   B 1 168 ? 33.868 -35.263 -9.949  1.00 25.34 ?  168 PHE   B HB2  1 
ATOM   6511 H HB3  . PHE   B 1 168 ? 33.448 -35.762 -11.397 1.00 25.34 ?  168 PHE   B HB3  1 
ATOM   6512 H HD1  . PHE   B 1 168 ? 32.192 -33.765 -8.764  1.00 26.87 ?  168 PHE   B HD1  1 
ATOM   6513 H HD2  . PHE   B 1 168 ? 32.120 -34.360 -12.711 1.00 24.40 ?  168 PHE   B HD2  1 
ATOM   6514 H HE1  . PHE   B 1 168 ? 30.903 -31.872 -9.016  1.00 26.62 ?  168 PHE   B HE1  1 
ATOM   6515 H HE2  . PHE   B 1 168 ? 30.825 -32.459 -12.980 1.00 26.65 ?  168 PHE   B HE2  1 
ATOM   6516 H HZ   . PHE   B 1 168 ? 30.213 -31.208 -11.127 1.00 26.28 ?  168 PHE   B HZ   1 
ATOM   6517 N N    . LEU   B 1 169 ? 31.146 -37.788 -11.688 1.00 17.94 ?  169 LEU   B N    1 
ATOM   6518 C CA   . LEU   B 1 169 ? 29.999 -38.134 -12.517 1.00 20.53 ?  169 LEU   B CA   1 
ATOM   6519 C C    . LEU   B 1 169 ? 29.978 -39.588 -12.974 1.00 23.87 ?  169 LEU   B C    1 
ATOM   6520 O O    . LEU   B 1 169 ? 29.088 -40.002 -13.720 1.00 26.38 ?  169 LEU   B O    1 
ATOM   6521 C CB   . LEU   B 1 169 ? 29.957 -37.244 -13.754 1.00 22.41 ?  169 LEU   B CB   1 
ATOM   6522 C CG   . LEU   B 1 169 ? 28.745 -36.318 -13.843 1.00 25.38 ?  169 LEU   B CG   1 
ATOM   6523 C CD1  . LEU   B 1 169 ? 28.657 -35.721 -15.225 1.00 26.21 ?  169 LEU   B CD1  1 
ATOM   6524 C CD2  . LEU   B 1 169 ? 27.460 -37.056 -13.496 1.00 25.78 ?  169 LEU   B CD2  1 
ATOM   6525 O OXT  . LEU   B 1 169 ? 30.835 -40.387 -12.629 1.00 24.57 -1 169 LEU   B OXT  1 
ATOM   6526 H H    . LEU   B 1 169 ? 31.877 -38.179 -11.928 1.00 21.50 ?  169 LEU   B H    1 
ATOM   6527 H HA   . LEU   B 1 169 ? 29.207 -37.972 -11.990 1.00 24.61 ?  169 LEU   B HA   1 
ATOM   6528 H HB2  . LEU   B 1 169 ? 30.749 -36.682 -13.766 1.00 26.86 ?  169 LEU   B HB2  1 
ATOM   6529 H HB3  . LEU   B 1 169 ? 29.946 -37.804 -14.546 1.00 26.86 ?  169 LEU   B HB3  1 
ATOM   6530 H HG   . LEU   B 1 169 ? 28.852 -35.590 -13.209 1.00 30.43 ?  169 LEU   B HG   1 
ATOM   6531 H HD11 . LEU   B 1 169 ? 27.903 -35.111 -15.258 1.00 31.43 ?  169 LEU   B HD11 1 
ATOM   6532 H HD12 . LEU   B 1 169 ? 29.479 -35.244 -15.414 1.00 31.43 ?  169 LEU   B HD12 1 
ATOM   6533 H HD13 . LEU   B 1 169 ? 28.532 -36.437 -15.868 1.00 31.43 ?  169 LEU   B HD13 1 
ATOM   6534 H HD21 . LEU   B 1 169 ? 26.721 -36.642 -13.961 1.00 30.91 ?  169 LEU   B HD21 1 
ATOM   6535 H HD22 . LEU   B 1 169 ? 27.548 -37.984 -13.773 1.00 30.91 ?  169 LEU   B HD22 1 
ATOM   6536 H HD23 . LEU   B 1 169 ? 27.319 -37.012 -12.537 1.00 30.91 ?  169 LEU   B HD23 1 
HETATM 6537 N N2   B A1A6N C 2 .   ? 14.796 -0.101  4.160   0.34 17.89 ?  201 A1A6N A N2   1 
HETATM 6538 C C3   B A1A6N C 2 .   ? 14.594 0.174   -0.160  0.34 25.24 ?  201 A1A6N A C3   1 
HETATM 6539 C C6   B A1A6N C 2 .   ? 14.920 1.062   3.474   0.34 18.83 ?  201 A1A6N A C6   1 
HETATM 6540 C C9   B A1A6N C 2 .   ? 15.193 2.284   4.136   0.34 16.34 ?  201 A1A6N A C9   1 
HETATM 6541 C C12  B A1A6N C 2 .   ? 15.171 -0.062  1.266   0.34 23.89 ?  201 A1A6N A C12  1 
HETATM 6542 C C1   B A1A6N C 2 .   ? 13.213 -2.022  -0.162  0.34 25.49 ?  201 A1A6N A C1   1 
HETATM 6543 C C10  B A1A6N C 2 .   ? 15.394 3.657   3.767   0.34 15.58 ?  201 A1A6N A C10  1 
HETATM 6544 C C11  B A1A6N C 2 .   ? 15.631 4.372   4.937   0.34 14.20 ?  201 A1A6N A C11  1 
HETATM 6545 C C2   B A1A6N C 2 .   ? 14.201 -1.130  -0.898  0.34 25.56 ?  201 A1A6N A C2   1 
HETATM 6546 C C4   B A1A6N C 2 .   ? 13.426 1.171   0.044   0.34 24.98 ?  201 A1A6N A C4   1 
HETATM 6547 C C5   B A1A6N C 2 .   ? 13.517 1.643   1.504   0.34 24.10 ?  201 A1A6N A C5   1 
HETATM 6548 C C7   B A1A6N C 2 .   ? 14.936 -0.018  5.523   0.34 17.16 ?  201 A1A6N A C7   1 
HETATM 6549 C C8   B A1A6N C 2 .   ? 15.316 2.219   5.544   0.34 15.78 ?  201 A1A6N A C8   1 
HETATM 6550 N N1   B A1A6N C 2 .   ? 14.797 1.130   2.045   0.34 22.32 ?  201 A1A6N A N1   1 
HETATM 6551 N N3   B A1A6N C 2 .   ? 15.189 1.068   6.259   0.34 16.23 ?  201 A1A6N A N3   1 
HETATM 6552 N N4   B A1A6N C 2 .   ? 15.582 3.491   6.038   0.34 14.76 ?  201 A1A6N A N4   1 
HETATM 6553 O O1   B A1A6N C 2 .   ? 15.518 0.874   -0.927  0.34 25.92 ?  201 A1A6N A O1   1 
HETATM 6554 H H15  B A1A6N C 2 .   ? 16.227 -0.310  1.284   0.34 28.64 ?  201 A1A6N A H15  1 
HETATM 6555 H H16  B A1A6N C 2 .   ? 14.663 -0.920  1.781   0.34 28.64 ?  201 A1A6N A H16  1 
HETATM 6556 H H3   B A1A6N C 2 .   ? 12.434 -2.401  -0.836  0.34 30.56 ?  201 A1A6N A H3   1 
HETATM 6557 H H2   B A1A6N C 2 .   ? 12.692 -1.499  0.634   0.34 30.56 ?  201 A1A6N A H2   1 
HETATM 6558 H H1   B A1A6N C 2 .   ? 13.685 -2.896  0.301   0.34 30.56 ?  201 A1A6N A H1   1 
HETATM 6559 H H12  B A1A6N C 2 .   ? 15.352 4.035   2.769   0.34 18.66 ?  201 A1A6N A H12  1 
HETATM 6560 H H13  B A1A6N C 2 .   ? 15.816 5.428   5.067   0.34 17.01 ?  201 A1A6N A H13  1 
HETATM 6561 H H4   B A1A6N C 2 .   ? 13.780 -0.895  -1.891  0.34 30.64 ?  201 A1A6N A H4   1 
HETATM 6562 H H5   B A1A6N C 2 .   ? 15.123 -1.705  -1.127  0.34 30.64 ?  201 A1A6N A H5   1 
HETATM 6563 H H8   B A1A6N C 2 .   ? 12.437 0.707   -0.168  0.34 29.95 ?  201 A1A6N A H8   1 
HETATM 6564 H H7   B A1A6N C 2 .   ? 13.452 2.028   -0.648  0.34 29.95 ?  201 A1A6N A H7   1 
HETATM 6565 H H9   B A1A6N C 2 .   ? 12.624 1.360   2.064   0.34 28.89 ?  201 A1A6N A H9   1 
HETATM 6566 H H10  B A1A6N C 2 .   ? 13.573 2.746   1.595   0.34 28.89 ?  201 A1A6N A H10  1 
HETATM 6567 H H11  B A1A6N C 2 .   ? 14.829 -0.954  6.112   0.34 20.57 ?  201 A1A6N A H11  1 
HETATM 6568 H H14  B A1A6N C 2 .   ? 15.718 3.739   7.003   0.34 17.69 ?  201 A1A6N A H14  1 
HETATM 6569 H H6   B A1A6N C 2 .   ? 16.359 0.444   -0.833  0.34 31.08 ?  201 A1A6N A H6   1 
HETATM 6570 O O    . HOH   D 3 .   ? 16.183 2.883   -1.562  1.00 18.48 ?  301 HOH   A O    1 
HETATM 6571 O O    . HOH   D 3 .   ? 12.029 0.313   14.718  1.00 32.39 ?  302 HOH   A O    1 
HETATM 6572 O O    . HOH   D 3 .   ? 4.705  3.750   0.534   1.00 26.09 ?  303 HOH   A O    1 
HETATM 6573 O O    A HOH   D 3 .   ? 14.777 -4.562  20.370  0.66 40.58 ?  304 HOH   A O    1 
HETATM 6574 O O    . HOH   D 3 .   ? 17.554 -1.719  0.304   1.00 22.05 ?  305 HOH   A O    1 
HETATM 6575 O O    . HOH   D 3 .   ? 34.373 -1.818  12.493  1.00 40.29 ?  306 HOH   A O    1 
HETATM 6576 O O    . HOH   D 3 .   ? 15.159 -12.260 18.623  1.00 44.46 ?  307 HOH   A O    1 
HETATM 6577 O O    . HOH   D 3 .   ? 26.857 11.449  1.575   1.00 17.77 ?  308 HOH   A O    1 
HETATM 6578 O O    . HOH   D 3 .   ? 3.648  -9.238  9.953   1.00 32.89 ?  309 HOH   A O    1 
HETATM 6579 O O    . HOH   D 3 .   ? 28.956 0.473   -9.782  1.00 23.15 ?  310 HOH   A O    1 
HETATM 6580 O O    . HOH   D 3 .   ? 0.844  -4.371  0.057   1.00 33.91 ?  311 HOH   A O    1 
HETATM 6581 O O    . HOH   D 3 .   ? 30.218 -13.316 -8.442  1.00 29.54 ?  312 HOH   A O    1 
HETATM 6582 O O    . HOH   D 3 .   ? -0.490 -3.078  2.845   1.00 39.13 ?  313 HOH   A O    1 
HETATM 6583 O O    . HOH   D 3 .   ? 28.114 -6.225  19.550  1.00 42.06 ?  314 HOH   A O    1 
HETATM 6584 O O    . HOH   D 3 .   ? 42.382 10.546  5.070   1.00 21.79 ?  315 HOH   A O    1 
HETATM 6585 O O    . HOH   D 3 .   ? 14.712 -13.905 16.717  1.00 28.11 ?  316 HOH   A O    1 
HETATM 6586 O O    . HOH   D 3 .   ? 23.891 -15.736 -9.150  1.00 35.90 ?  317 HOH   A O    1 
HETATM 6587 O O    . HOH   D 3 .   ? 13.294 -1.523  -6.739  1.00 20.97 ?  318 HOH   A O    1 
HETATM 6588 O O    . HOH   D 3 .   ? 15.229 -8.095  -9.914  1.00 26.05 ?  319 HOH   A O    1 
HETATM 6589 O O    . HOH   D 3 .   ? -0.700 -8.488  2.198   1.00 41.52 ?  320 HOH   A O    1 
HETATM 6590 O O    . HOH   D 3 .   ? 9.083  -10.008 19.253  1.00 44.30 ?  321 HOH   A O    1 
HETATM 6591 O O    . HOH   D 3 .   ? 7.913  -12.506 -0.938  1.00 25.01 ?  322 HOH   A O    1 
HETATM 6592 O O    A HOH   D 3 .   ? 14.088 -4.608  -11.785 0.66 25.27 ?  323 HOH   A O    1 
HETATM 6593 O O    . HOH   D 3 .   ? 30.882 6.187   -12.319 1.00 29.31 ?  324 HOH   A O    1 
HETATM 6594 O O    . HOH   D 3 .   ? 19.975 -12.629 -8.797  1.00 29.77 ?  325 HOH   A O    1 
HETATM 6595 O O    . HOH   D 3 .   ? 17.069 -17.956 14.966  1.00 29.06 ?  326 HOH   A O    1 
HETATM 6596 O O    . HOH   D 3 .   ? 37.497 2.859   10.232  1.00 26.45 ?  327 HOH   A O    1 
HETATM 6597 O O    . HOH   D 3 .   ? 38.243 10.251  7.055   1.00 44.76 ?  328 HOH   A O    1 
HETATM 6598 O O    . HOH   D 3 .   ? 11.753 -10.979 -10.106 1.00 50.87 ?  329 HOH   A O    1 
HETATM 6599 O O    A HOH   D 3 .   ? 28.239 -0.214  -13.386 0.66 29.91 ?  330 HOH   A O    1 
HETATM 6600 O O    . HOH   D 3 .   ? 13.597 -15.334 -7.582  1.00 29.02 ?  331 HOH   A O    1 
HETATM 6601 O O    B HOH   D 3 .   ? 14.925 -2.860  3.378   0.34 15.95 ?  332 HOH   A O    1 
HETATM 6602 O O    . HOH   D 3 .   ? 11.137 -0.408  1.853   1.00 24.68 ?  333 HOH   A O    1 
HETATM 6603 O O    . HOH   D 3 .   ? 18.667 -19.310 13.575  1.00 35.61 ?  334 HOH   A O    1 
HETATM 6604 O O    . HOH   D 3 .   ? 26.523 -19.353 -1.762  1.00 14.98 ?  335 HOH   A O    1 
HETATM 6605 O O    . HOH   D 3 .   ? 15.738 2.253   24.470  1.00 50.79 ?  336 HOH   A O    1 
HETATM 6606 O O    . HOH   D 3 .   ? 22.530 -11.962 21.799  1.00 55.39 ?  337 HOH   A O    1 
HETATM 6607 O O    . HOH   D 3 .   ? 25.739 -0.837  -7.405  1.00 19.24 ?  338 HOH   A O    1 
HETATM 6608 O O    . HOH   D 3 .   ? 33.995 -1.129  -8.943  1.00 28.28 ?  339 HOH   A O    1 
HETATM 6609 O O    . HOH   D 3 .   ? 6.857  -8.081  11.777  1.00 21.10 ?  340 HOH   A O    1 
HETATM 6610 O O    . HOH   D 3 .   ? 38.546 5.012   6.987   1.00 16.68 ?  341 HOH   A O    1 
HETATM 6611 O O    . HOH   D 3 .   ? 18.933 -21.987 6.982   1.00 37.48 ?  342 HOH   A O    1 
HETATM 6612 O O    . HOH   D 3 .   ? 31.654 8.258   14.795  1.00 25.39 ?  343 HOH   A O    1 
HETATM 6613 O O    . HOH   D 3 .   ? 36.274 -5.082  -0.493  1.00 32.50 ?  344 HOH   A O    1 
HETATM 6614 O O    . HOH   D 3 .   ? 31.075 -18.077 7.798   1.00 19.46 ?  345 HOH   A O    1 
HETATM 6615 O O    . HOH   D 3 .   ? 28.697 -10.592 -14.109 1.00 43.77 ?  346 HOH   A O    1 
HETATM 6616 O O    A HOH   D 3 .   ? 14.639 -3.648  3.045   0.66 17.20 ?  347 HOH   A O    1 
HETATM 6617 O O    . HOH   D 3 .   ? 14.391 -21.268 -4.273  1.00 31.18 ?  348 HOH   A O    1 
HETATM 6618 O O    A HOH   D 3 .   ? 14.274 0.586   6.739   0.66 19.56 ?  349 HOH   A O    1 
HETATM 6619 O O    . HOH   D 3 .   ? 21.253 -2.341  -2.284  1.00 18.16 ?  350 HOH   A O    1 
HETATM 6620 O O    . HOH   D 3 .   ? 20.667 -19.800 -5.051  1.00 27.88 ?  351 HOH   A O    1 
HETATM 6621 O O    . HOH   D 3 .   ? 44.343 7.190   6.378   1.00 27.55 ?  352 HOH   A O    1 
HETATM 6622 O O    . HOH   D 3 .   ? 22.142 -19.303 11.392  1.00 38.10 ?  353 HOH   A O    1 
HETATM 6623 O O    . HOH   D 3 .   ? 27.428 13.815  2.729   1.00 28.04 ?  354 HOH   A O    1 
HETATM 6624 O O    . HOH   D 3 .   ? 22.204 5.374   18.943  1.00 42.59 ?  355 HOH   A O    1 
HETATM 6625 O O    . HOH   D 3 .   ? 35.794 -12.619 6.878   1.00 16.01 ?  356 HOH   A O    1 
HETATM 6626 O O    . HOH   D 3 .   ? 24.032 -2.134  -2.138  1.00 11.68 ?  357 HOH   A O    1 
HETATM 6627 O O    . HOH   D 3 .   ? 14.924 3.933   17.726  1.00 40.25 ?  358 HOH   A O    1 
HETATM 6628 O O    . HOH   D 3 .   ? 43.376 7.779   2.667   1.00 36.49 ?  359 HOH   A O    1 
HETATM 6629 O O    . HOH   D 3 .   ? 39.773 -1.050  -5.202  1.00 21.55 ?  360 HOH   A O    1 
HETATM 6630 O O    . HOH   D 3 .   ? 42.596 4.290   5.480   1.00 35.16 ?  361 HOH   A O    1 
HETATM 6631 O O    . HOH   D 3 .   ? 18.528 9.465   8.962   1.00 24.18 ?  362 HOH   A O    1 
HETATM 6632 O O    . HOH   D 3 .   ? 31.792 -9.436  -6.750  1.00 25.78 ?  363 HOH   A O    1 
HETATM 6633 O O    . HOH   D 3 .   ? 22.708 12.502  1.559   1.00 15.27 ?  364 HOH   A O    1 
HETATM 6634 O O    . HOH   D 3 .   ? 21.228 10.305  14.966  1.00 34.58 ?  365 HOH   A O    1 
HETATM 6635 O O    . HOH   D 3 .   ? 14.401 -0.504  -12.346 1.00 30.57 ?  366 HOH   A O    1 
HETATM 6636 O O    . HOH   D 3 .   ? 31.116 -13.939 -2.433  1.00 15.15 ?  367 HOH   A O    1 
HETATM 6637 O O    . HOH   D 3 .   ? 9.941  -21.332 5.586   1.00 23.39 ?  368 HOH   A O    1 
HETATM 6638 O O    . HOH   D 3 .   ? 17.135 -17.829 -5.139  1.00 29.35 ?  369 HOH   A O    1 
HETATM 6639 O O    . HOH   D 3 .   ? 30.797 3.116   8.229   1.00 12.66 ?  370 HOH   A O    1 
HETATM 6640 O O    . HOH   D 3 .   ? 37.248 12.000  4.838   1.00 28.05 ?  371 HOH   A O    1 
HETATM 6641 O O    . HOH   D 3 .   ? 8.041  -21.574 3.993   1.00 42.64 ?  372 HOH   A O    1 
HETATM 6642 O O    . HOH   D 3 .   ? 10.916 1.671   12.512  1.00 24.90 ?  373 HOH   A O    1 
HETATM 6643 O O    . HOH   D 3 .   ? 37.246 -2.876  9.698   1.00 46.48 ?  374 HOH   A O    1 
HETATM 6644 O O    . HOH   D 3 .   ? 24.334 3.626   -1.860  1.00 18.99 ?  375 HOH   A O    1 
HETATM 6645 O O    . HOH   D 3 .   ? 21.303 3.089   -0.329  1.00 15.47 ?  376 HOH   A O    1 
HETATM 6646 O O    A HOH   D 3 .   ? 24.592 2.033   -7.041  0.66 17.26 ?  377 HOH   A O    1 
HETATM 6647 O O    . HOH   D 3 .   ? 29.742 -1.914  -12.790 1.00 49.44 ?  378 HOH   A O    1 
HETATM 6648 O O    . HOH   D 3 .   ? 7.629  -6.293  -6.660  1.00 42.77 ?  379 HOH   A O    1 
HETATM 6649 O O    . HOH   D 3 .   ? 24.192 -7.709  14.380  1.00 17.56 ?  380 HOH   A O    1 
HETATM 6650 O O    . HOH   D 3 .   ? 27.911 0.804   -7.214  1.00 14.88 ?  381 HOH   A O    1 
HETATM 6651 O O    . HOH   D 3 .   ? 27.465 -10.529 14.016  1.00 17.93 ?  382 HOH   A O    1 
HETATM 6652 O O    . HOH   D 3 .   ? 15.477 11.903  7.919   1.00 41.61 ?  383 HOH   A O    1 
HETATM 6653 O O    . HOH   D 3 .   ? 21.902 -21.928 8.475   1.00 28.92 ?  384 HOH   A O    1 
HETATM 6654 O O    . HOH   D 3 .   ? 17.035 -19.264 4.876   1.00 16.89 ?  385 HOH   A O    1 
HETATM 6655 O O    . HOH   D 3 .   ? 10.384 -22.161 -1.268  1.00 51.07 ?  386 HOH   A O    1 
HETATM 6656 O O    . HOH   D 3 .   ? 33.673 -7.145  4.322   1.00 17.97 ?  387 HOH   A O    1 
HETATM 6657 O O    . HOH   D 3 .   ? 23.438 11.401  4.034   1.00 12.43 ?  388 HOH   A O    1 
HETATM 6658 O O    . HOH   D 3 .   ? 44.032 8.539   -2.995  1.00 29.21 ?  389 HOH   A O    1 
HETATM 6659 O O    . HOH   D 3 .   ? 24.678 -17.466 12.736  1.00 24.89 ?  390 HOH   A O    1 
HETATM 6660 O O    . HOH   D 3 .   ? 13.866 -4.866  17.402  1.00 28.83 ?  391 HOH   A O    1 
HETATM 6661 O O    . HOH   D 3 .   ? 16.530 -22.153 0.932   1.00 30.79 ?  392 HOH   A O    1 
HETATM 6662 O O    . HOH   D 3 .   ? 31.923 -7.291  -9.818  1.00 23.31 ?  393 HOH   A O    1 
HETATM 6663 O O    . HOH   D 3 .   ? 30.047 -10.028 13.008  1.00 22.11 ?  394 HOH   A O    1 
HETATM 6664 O O    . HOH   D 3 .   ? 37.561 -2.053  5.855   1.00 28.10 ?  395 HOH   A O    1 
HETATM 6665 O O    . HOH   D 3 .   ? 16.223 16.639  8.546   1.00 39.12 ?  396 HOH   A O    1 
HETATM 6666 O O    . HOH   D 3 .   ? 6.364  -5.506  11.004  1.00 20.94 ?  397 HOH   A O    1 
HETATM 6667 O O    . HOH   D 3 .   ? 32.800 -9.237  6.003   1.00 19.78 ?  398 HOH   A O    1 
HETATM 6668 O O    . HOH   D 3 .   ? 26.911 4.185   -0.701  1.00 13.17 ?  399 HOH   A O    1 
HETATM 6669 O O    . HOH   D 3 .   ? 30.622 1.935   16.635  1.00 21.30 ?  400 HOH   A O    1 
HETATM 6670 O O    A HOH   D 3 .   ? 20.107 4.532   -7.608  0.66 18.65 ?  401 HOH   A O    1 
HETATM 6671 O O    . HOH   D 3 .   ? 23.971 -20.282 -1.354  1.00 18.82 ?  402 HOH   A O    1 
HETATM 6672 O O    . HOH   D 3 .   ? 15.976 6.902   2.884   1.00 16.15 ?  403 HOH   A O    1 
HETATM 6673 O O    . HOH   D 3 .   ? 18.916 -0.684  -1.713  1.00 16.61 ?  404 HOH   A O    1 
HETATM 6674 O O    . HOH   D 3 .   ? 20.537 -20.054 2.769   1.00 21.27 ?  405 HOH   A O    1 
HETATM 6675 O O    . HOH   D 3 .   ? 15.186 -21.493 14.185  1.00 19.38 ?  406 HOH   A O    1 
HETATM 6676 O O    . HOH   D 3 .   ? 6.640  -3.318  12.797  1.00 32.69 ?  407 HOH   A O    1 
HETATM 6677 O O    . HOH   D 3 .   ? 35.113 -5.240  -3.094  1.00 18.05 ?  408 HOH   A O    1 
HETATM 6678 O O    . HOH   D 3 .   ? 40.931 -8.200  -6.768  1.00 34.55 ?  409 HOH   A O    1 
HETATM 6679 O O    . HOH   D 3 .   ? 14.069 -23.030 7.346   1.00 21.25 ?  410 HOH   A O    1 
HETATM 6680 O O    . HOH   D 3 .   ? 27.352 2.299   18.730  1.00 33.74 ?  411 HOH   A O    1 
HETATM 6681 O O    . HOH   D 3 .   ? 27.611 -6.213  -14.089 1.00 42.15 ?  412 HOH   A O    1 
HETATM 6682 O O    . HOH   D 3 .   ? 30.323 -12.844 13.527  1.00 21.80 ?  413 HOH   A O    1 
HETATM 6683 O O    A HOH   D 3 .   ? 15.800 -0.934  5.214   0.66 23.34 ?  414 HOH   A O    1 
HETATM 6684 O O    A HOH   D 3 .   ? 18.592 -2.490  -16.389 0.66 35.12 ?  415 HOH   A O    1 
HETATM 6685 O O    . HOH   D 3 .   ? 36.672 -5.023  5.383   1.00 25.05 ?  416 HOH   A O    1 
HETATM 6686 O O    . HOH   D 3 .   ? 44.987 -0.632  2.925   1.00 44.16 ?  417 HOH   A O    1 
HETATM 6687 O O    . HOH   D 3 .   ? 38.128 -1.383  -1.968  1.00 20.27 ?  418 HOH   A O    1 
HETATM 6688 O O    . HOH   D 3 .   ? 24.035 3.933   -4.861  1.00 22.76 ?  419 HOH   A O    1 
HETATM 6689 O O    . HOH   D 3 .   ? 32.715 -4.364  -9.922  1.00 27.67 ?  420 HOH   A O    1 
HETATM 6690 O O    . HOH   D 3 .   ? 8.958  -12.043 17.243  1.00 37.69 ?  421 HOH   A O    1 
HETATM 6691 O O    . HOH   D 3 .   ? 41.652 1.447   5.025   1.00 37.73 ?  422 HOH   A O    1 
HETATM 6692 O O    . HOH   D 3 .   ? 22.602 8.247   18.318  1.00 42.02 ?  423 HOH   A O    1 
HETATM 6693 O O    . HOH   D 3 .   ? 21.780 -13.853 -8.224  1.00 44.98 ?  424 HOH   A O    1 
HETATM 6694 O O    . HOH   D 3 .   ? 26.992 -3.173  19.444  1.00 37.60 ?  425 HOH   A O    1 
HETATM 6695 O O    . HOH   D 3 .   ? 10.363 -13.764 -1.743  1.00 20.13 ?  426 HOH   A O    1 
HETATM 6696 O O    . HOH   D 3 .   ? 16.226 -14.199 20.166  1.00 51.28 ?  427 HOH   A O    1 
HETATM 6697 O O    . HOH   D 3 .   ? 18.832 2.007   -0.776  1.00 14.82 ?  428 HOH   A O    1 
HETATM 6698 O O    . HOH   D 3 .   ? 5.258  2.888   4.914   1.00 29.74 ?  429 HOH   A O    1 
HETATM 6699 O O    . HOH   D 3 .   ? 14.425 -24.613 11.469  1.00 40.13 ?  430 HOH   A O    1 
HETATM 6700 O O    . HOH   D 3 .   ? 11.587 -10.696 16.940  1.00 29.60 ?  431 HOH   A O    1 
HETATM 6701 O O    . HOH   D 3 .   ? 23.555 -7.984  17.049  1.00 24.27 ?  432 HOH   A O    1 
HETATM 6702 O O    B HOH   D 3 .   ? 18.881 -0.427  -3.870  0.34 23.46 ?  433 HOH   A O    1 
HETATM 6703 O O    . HOH   D 3 .   ? 18.490 4.831   -15.186 1.00 57.22 ?  434 HOH   A O    1 
HETATM 6704 O O    . HOH   D 3 .   ? 23.474 -20.926 1.326   1.00 20.85 ?  435 HOH   A O    1 
HETATM 6705 O O    . HOH   D 3 .   ? 32.376 -10.589 3.395   1.00 32.94 ?  436 HOH   A O    1 
HETATM 6706 O O    . HOH   D 3 .   ? 37.743 -8.807  -3.392  1.00 22.81 ?  437 HOH   A O    1 
HETATM 6707 O O    . HOH   D 3 .   ? 21.296 -9.027  21.247  1.00 52.77 ?  438 HOH   A O    1 
HETATM 6708 O O    . HOH   D 3 .   ? 9.486  -16.271 -2.063  1.00 37.90 ?  439 HOH   A O    1 
HETATM 6709 O O    . HOH   D 3 .   ? 21.485 -14.757 17.865  1.00 56.98 ?  440 HOH   A O    1 
HETATM 6710 O O    . HOH   D 3 .   ? 31.347 -12.784 0.042   1.00 20.98 ?  441 HOH   A O    1 
HETATM 6711 O O    . HOH   D 3 .   ? 34.473 -8.047  -0.598  1.00 31.30 ?  442 HOH   A O    1 
HETATM 6712 O O    . HOH   D 3 .   ? 18.419 -15.958 16.195  1.00 40.73 ?  443 HOH   A O    1 
HETATM 6713 O O    . HOH   D 3 .   ? 19.307 -10.529 24.020  1.00 87.52 ?  444 HOH   A O    1 
HETATM 6714 O O    . HOH   D 3 .   ? 23.276 7.401   -3.245  1.00 35.94 ?  445 HOH   A O    1 
HETATM 6715 O O    . HOH   D 3 .   ? 30.524 14.773  2.666   1.00 19.49 ?  446 HOH   A O    1 
HETATM 6716 O O    . HOH   D 3 .   ? 20.566 -17.726 24.850  1.00 52.43 ?  447 HOH   A O    1 
HETATM 6717 O O    A HOH   D 3 .   ? 14.029 -0.332  3.403   0.66 16.88 ?  448 HOH   A O    1 
HETATM 6718 O O    . HOH   D 3 .   ? -1.507 -4.903  7.576   1.00 43.17 ?  449 HOH   A O    1 
HETATM 6719 O O    . HOH   D 3 .   ? 32.443 -15.906 10.862  1.00 29.65 ?  450 HOH   A O    1 
HETATM 6720 O O    . HOH   D 3 .   ? 29.862 -16.089 10.829  1.00 37.33 ?  451 HOH   A O    1 
HETATM 6721 O O    . HOH   D 3 .   ? 25.348 8.223   -4.854  1.00 35.54 ?  452 HOH   A O    1 
HETATM 6722 O O    . HOH   D 3 .   ? 24.805 5.699   20.717  1.00 53.06 ?  453 HOH   A O    1 
HETATM 6723 O O    . HOH   D 3 .   ? 19.894 -17.370 -5.105  1.00 25.63 ?  454 HOH   A O    1 
HETATM 6724 O O    . HOH   D 3 .   ? 27.783 7.126   -6.715  1.00 42.87 ?  455 HOH   A O    1 
HETATM 6725 O O    . HOH   D 3 .   ? 23.159 -22.408 -3.355  1.00 37.19 ?  456 HOH   A O    1 
HETATM 6726 O O    . HOH   D 3 .   ? 11.073 -15.028 -6.141  1.00 39.53 ?  457 HOH   A O    1 
HETATM 6727 O O    . HOH   D 3 .   ? 16.002 -6.785  -11.911 1.00 46.65 ?  458 HOH   A O    1 
HETATM 6728 O O    . HOH   D 3 .   ? 24.552 14.677  7.734   1.00 37.86 ?  459 HOH   A O    1 
HETATM 6729 O O    . HOH   D 3 .   ? 26.877 11.684  -1.366  1.00 36.08 ?  460 HOH   A O    1 
HETATM 6730 O O    . HOH   D 3 .   ? 15.820 -21.568 3.666   1.00 26.27 ?  461 HOH   A O    1 
HETATM 6731 O O    . HOH   D 3 .   ? 18.783 10.936  11.244  1.00 34.18 ?  462 HOH   A O    1 
HETATM 6732 O O    . HOH   D 3 .   ? 18.198 -16.296 -8.932  1.00 43.46 ?  463 HOH   A O    1 
HETATM 6733 O O    . HOH   D 3 .   ? 28.716 -4.793  -12.269 1.00 43.97 ?  464 HOH   A O    1 
HETATM 6734 O O    . HOH   D 3 .   ? 27.512 -11.344 16.527  1.00 40.20 ?  465 HOH   A O    1 
HETATM 6735 O O    . HOH   D 3 .   ? 39.676 -6.993  -3.387  1.00 45.75 ?  466 HOH   A O    1 
HETATM 6736 O O    . HOH   D 3 .   ? 12.255 1.696   17.256  1.00 42.27 ?  467 HOH   A O    1 
HETATM 6737 O O    . HOH   D 3 .   ? 25.827 10.809  -3.740  1.00 30.21 ?  468 HOH   A O    1 
HETATM 6738 O O    . HOH   D 3 .   ? 23.419 13.698  5.507   1.00 19.71 ?  469 HOH   A O    1 
HETATM 6739 O O    . HOH   D 3 .   ? 22.338 5.095   -5.591  1.00 45.56 ?  470 HOH   A O    1 
HETATM 6740 O O    . HOH   D 3 .   ? 12.025 -13.259 16.335  1.00 51.13 ?  471 HOH   A O    1 
HETATM 6741 O O    . HOH   D 3 .   ? 28.806 8.939   17.458  1.00 35.81 ?  472 HOH   A O    1 
HETATM 6742 O O    . HOH   D 3 .   ? 23.151 11.855  -4.045  1.00 23.56 ?  473 HOH   A O    1 
HETATM 6743 O O    . HOH   D 3 .   ? 41.013 -3.905  -0.428  1.00 39.74 ?  474 HOH   A O    1 
HETATM 6744 O O    . HOH   D 3 .   ? 35.198 7.495   12.138  1.00 44.26 ?  475 HOH   A O    1 
HETATM 6745 O O    . HOH   D 3 .   ? 15.736 -17.368 -7.062  1.00 34.80 ?  476 HOH   A O    1 
HETATM 6746 O O    . HOH   D 3 .   ? 44.517 10.382  -1.618  1.00 34.34 ?  477 HOH   A O    1 
HETATM 6747 O O    . HOH   D 3 .   ? 17.386 -18.727 19.710  1.00 55.15 ?  478 HOH   A O    1 
HETATM 6748 O O    . HOH   D 3 .   ? 16.900 -20.475 16.051  1.00 31.82 ?  479 HOH   A O    1 
HETATM 6749 O O    . HOH   D 3 .   ? 25.799 -18.870 -11.852 1.00 41.72 ?  480 HOH   A O    1 
HETATM 6750 O O    . HOH   D 3 .   ? 30.792 0.708   19.210  1.00 40.93 ?  481 HOH   A O    1 
HETATM 6751 O O    . HOH   D 3 .   ? 41.704 9.314   -4.002  1.00 30.67 ?  482 HOH   A O    1 
HETATM 6752 O O    . HOH   D 3 .   ? 28.738 -7.945  -15.271 1.00 51.01 ?  483 HOH   A O    1 
HETATM 6753 O O    . HOH   D 3 .   ? 13.977 -10.330 -11.054 1.00 35.41 ?  484 HOH   A O    1 
HETATM 6754 O O    . HOH   D 3 .   ? 31.540 -0.575  -10.602 1.00 29.55 ?  485 HOH   A O    1 
HETATM 6755 O O    . HOH   D 3 .   ? 39.198 2.382   7.300   1.00 31.84 ?  486 HOH   A O    1 
HETATM 6756 O O    . HOH   D 3 .   ? 23.212 -12.830 19.271  1.00 57.80 ?  487 HOH   A O    1 
HETATM 6757 O O    . HOH   D 3 .   ? 18.390 -23.193 1.859   1.00 51.89 ?  488 HOH   A O    1 
HETATM 6758 O O    . HOH   D 3 .   ? 13.972 -25.183 8.923   1.00 37.15 ?  489 HOH   A O    1 
HETATM 6759 O O    . HOH   D 3 .   ? 40.611 -0.289  -7.773  1.00 32.01 ?  490 HOH   A O    1 
HETATM 6760 O O    . HOH   D 3 .   ? 20.135 -22.342 4.278   1.00 33.66 ?  491 HOH   A O    1 
HETATM 6761 O O    . HOH   D 3 .   ? 30.670 5.793   -14.721 1.00 32.40 ?  492 HOH   A O    1 
HETATM 6762 O O    . HOH   D 3 .   ? 20.643 -16.024 -7.451  1.00 30.34 ?  493 HOH   A O    1 
HETATM 6763 O O    . HOH   D 3 .   ? 16.222 -23.401 5.785   1.00 33.23 ?  494 HOH   A O    1 
HETATM 6764 O O    . HOH   D 3 .   ? 30.804 -5.861  -11.924 1.00 50.71 ?  495 HOH   A O    1 
HETATM 6765 O O    . HOH   D 3 .   ? 37.416 -6.626  7.582   1.00 24.71 ?  496 HOH   A O    1 
HETATM 6766 O O    . HOH   D 3 .   ? 39.508 -0.006  6.580   1.00 31.65 ?  497 HOH   A O    1 
HETATM 6767 O O    . HOH   D 3 .   ? 28.908 14.413  0.785   1.00 53.25 ?  498 HOH   A O    1 
HETATM 6768 O O    . HOH   D 3 .   ? 37.956 14.007  6.663   1.00 42.27 ?  499 HOH   A O    1 
HETATM 6769 O O    . HOH   D 3 .   ? 8.220  -3.146  -5.843  1.00 51.26 ?  500 HOH   A O    1 
HETATM 6770 O O    B HOH   D 3 .   ? 14.562 8.173   5.205   0.34 22.23 ?  501 HOH   A O    1 
HETATM 6771 O O    . HOH   D 3 .   ? 17.203 -6.827  -14.206 1.00 50.51 ?  502 HOH   A O    1 
HETATM 6772 O O    . HOH   D 3 .   ? 22.061 -24.002 4.516   1.00 30.02 ?  503 HOH   A O    1 
HETATM 6773 O O    . HOH   D 3 .   ? 36.479 -6.541  10.244  1.00 49.68 ?  504 HOH   A O    1 
HETATM 6774 O O    A HOH   D 3 .   ? 14.846 8.660   4.814   0.66 30.95 ?  505 HOH   A O    1 
HETATM 6775 O O    . HOH   D 3 .   ? 24.089 9.062   -7.246  1.00 42.74 ?  506 HOH   A O    1 
HETATM 6776 O O    . HOH   D 3 .   ? 15.750 -12.310 27.385  1.00 46.54 ?  507 HOH   A O    1 
HETATM 6777 O O    . HOH   D 3 .   ? 16.286 -21.121 18.762  1.00 38.72 ?  508 HOH   A O    1 
HETATM 6778 O O    . HOH   D 3 .   ? 14.703 -22.735 19.890  1.00 36.32 ?  509 HOH   A O    1 
HETATM 6779 O O    . HOH   E 3 .   ? 29.918 -22.446 5.539   1.00 20.19 ?  201 HOH   B O    1 
HETATM 6780 O O    . HOH   E 3 .   ? 38.168 -39.451 -0.084  1.00 41.05 ?  202 HOH   B O    1 
HETATM 6781 O O    . HOH   E 3 .   ? 31.156 -28.734 4.596   1.00 30.97 ?  203 HOH   B O    1 
HETATM 6782 O O    . HOH   E 3 .   ? 41.597 -36.038 -17.195 1.00 35.16 ?  204 HOH   B O    1 
HETATM 6783 O O    . HOH   E 3 .   ? 27.695 -29.167 -1.805  1.00 36.15 ?  205 HOH   B O    1 
HETATM 6784 O O    . HOH   E 3 .   ? 54.542 -9.488  -8.668  1.00 21.81 ?  206 HOH   B O    1 
HETATM 6785 O O    . HOH   E 3 .   ? 53.018 -13.527 -20.241 1.00 32.20 ?  207 HOH   B O    1 
HETATM 6786 O O    . HOH   E 3 .   ? 58.239 -12.938 8.328   1.00 33.64 ?  208 HOH   B O    1 
HETATM 6787 O O    . HOH   E 3 .   ? 30.224 -40.984 -8.015  1.00 18.97 ?  209 HOH   B O    1 
HETATM 6788 O O    . HOH   E 3 .   ? 59.208 -18.649 6.851   1.00 38.57 ?  210 HOH   B O    1 
HETATM 6789 O O    . HOH   E 3 .   ? 48.054 -6.887  15.457  1.00 28.25 ?  211 HOH   B O    1 
HETATM 6790 O O    . HOH   E 3 .   ? 27.917 -41.872 -15.128 1.00 38.92 ?  212 HOH   B O    1 
HETATM 6791 O O    . HOH   E 3 .   ? 41.387 -7.774  5.416   1.00 41.40 ?  213 HOH   B O    1 
HETATM 6792 O O    . HOH   E 3 .   ? 49.414 -22.742 -19.770 1.00 46.38 ?  214 HOH   B O    1 
HETATM 6793 O O    . HOH   E 3 .   ? 56.416 -19.726 7.165   1.00 31.16 ?  215 HOH   B O    1 
HETATM 6794 O O    . HOH   E 3 .   ? 50.266 -3.323  7.064   1.00 34.88 ?  216 HOH   B O    1 
HETATM 6795 O O    . HOH   E 3 .   ? 37.143 -19.697 -18.168 1.00 46.14 ?  217 HOH   B O    1 
HETATM 6796 O O    . HOH   E 3 .   ? 34.561 -36.427 -7.130  1.00 20.96 ?  218 HOH   B O    1 
HETATM 6797 O O    . HOH   E 3 .   ? 44.439 -7.125  1.932   1.00 37.88 ?  219 HOH   B O    1 
HETATM 6798 O O    . HOH   E 3 .   ? 30.046 -26.294 4.137   1.00 27.31 ?  220 HOH   B O    1 
HETATM 6799 O O    . HOH   E 3 .   ? 57.814 -24.410 5.148   1.00 39.06 ?  221 HOH   B O    1 
HETATM 6800 O O    . HOH   E 3 .   ? 50.855 -6.086  0.107   1.00 28.62 ?  222 HOH   B O    1 
HETATM 6801 O O    . HOH   E 3 .   ? 55.504 -16.614 -14.403 1.00 35.40 ?  223 HOH   B O    1 
HETATM 6802 O O    . HOH   E 3 .   ? 56.714 -30.810 -7.781  1.00 27.27 ?  224 HOH   B O    1 
HETATM 6803 O O    . HOH   E 3 .   ? 32.717 -43.763 -11.339 1.00 25.30 ?  225 HOH   B O    1 
HETATM 6804 O O    . HOH   E 3 .   ? 48.582 -36.591 -15.543 1.00 49.85 ?  226 HOH   B O    1 
HETATM 6805 O O    . HOH   E 3 .   ? 34.950 -24.683 13.884  1.00 41.60 ?  227 HOH   B O    1 
HETATM 6806 O O    . HOH   E 3 .   ? 41.541 -39.244 -14.932 1.00 22.65 ?  228 HOH   B O    1 
HETATM 6807 O O    . HOH   E 3 .   ? 57.436 -16.314 -12.280 1.00 18.01 ?  229 HOH   B O    1 
HETATM 6808 O O    . HOH   E 3 .   ? 25.492 -25.896 -1.209  1.00 33.90 ?  230 HOH   B O    1 
HETATM 6809 O O    . HOH   E 3 .   ? 57.198 -26.896 -7.705  1.00 39.49 ?  231 HOH   B O    1 
HETATM 6810 O O    . HOH   E 3 .   ? 41.460 -9.597  13.041  1.00 23.61 ?  232 HOH   B O    1 
HETATM 6811 O O    . HOH   E 3 .   ? 50.809 -12.981 -0.504  1.00 12.29 ?  233 HOH   B O    1 
HETATM 6812 O O    . HOH   E 3 .   ? 57.694 -24.354 -3.809  1.00 20.52 ?  234 HOH   B O    1 
HETATM 6813 O O    . HOH   E 3 .   ? 51.739 -6.480  4.292   1.00 20.22 ?  235 HOH   B O    1 
HETATM 6814 O O    . HOH   E 3 .   ? 46.420 -1.520  13.122  1.00 27.47 ?  236 HOH   B O    1 
HETATM 6815 O O    . HOH   E 3 .   ? 40.601 -16.117 14.046  1.00 24.06 ?  237 HOH   B O    1 
HETATM 6816 O O    . HOH   E 3 .   ? 35.117 -8.015  -2.948  1.00 18.32 ?  238 HOH   B O    1 
HETATM 6817 O O    . HOH   E 3 .   ? 39.384 -10.867 6.120   1.00 24.71 ?  239 HOH   B O    1 
HETATM 6818 O O    . HOH   E 3 .   ? 43.013 -43.279 -8.176  1.00 29.89 ?  240 HOH   B O    1 
HETATM 6819 O O    . HOH   E 3 .   ? 42.699 -22.846 3.866   1.00 12.58 ?  241 HOH   B O    1 
HETATM 6820 O O    . HOH   E 3 .   ? 44.582 -27.735 -0.693  1.00 22.75 ?  242 HOH   B O    1 
HETATM 6821 O O    . HOH   E 3 .   ? 44.901 -43.606 -10.438 1.00 28.52 ?  243 HOH   B O    1 
HETATM 6822 O O    . HOH   E 3 .   ? 45.155 -35.014 6.831   1.00 40.78 ?  244 HOH   B O    1 
HETATM 6823 O O    . HOH   E 3 .   ? 34.417 -18.371 11.496  1.00 27.13 ?  245 HOH   B O    1 
HETATM 6824 O O    . HOH   E 3 .   ? 28.428 -19.697 -13.109 1.00 25.96 ?  246 HOH   B O    1 
HETATM 6825 O O    . HOH   E 3 .   ? 42.635 -25.341 2.661   1.00 16.09 ?  247 HOH   B O    1 
HETATM 6826 O O    . HOH   E 3 .   ? 30.386 -42.264 -10.647 1.00 30.20 ?  248 HOH   B O    1 
HETATM 6827 O O    . HOH   E 3 .   ? 43.141 -32.418 -17.105 1.00 26.99 ?  249 HOH   B O    1 
HETATM 6828 O O    . HOH   E 3 .   ? 47.457 -7.210  -3.778  1.00 41.33 ?  250 HOH   B O    1 
HETATM 6829 O O    . HOH   E 3 .   ? 50.971 -39.976 -8.268  1.00 31.22 ?  251 HOH   B O    1 
HETATM 6830 O O    . HOH   E 3 .   ? 29.915 -34.151 -0.385  1.00 37.24 ?  252 HOH   B O    1 
HETATM 6831 O O    . HOH   E 3 .   ? 51.615 -13.795 10.985  1.00 26.27 ?  253 HOH   B O    1 
HETATM 6832 O O    . HOH   E 3 .   ? 38.477 -11.097 -2.210  1.00 19.20 ?  254 HOH   B O    1 
HETATM 6833 O O    . HOH   E 3 .   ? 39.586 -11.084 0.316   1.00 18.17 ?  255 HOH   B O    1 
HETATM 6834 O O    . HOH   E 3 .   ? 28.487 -30.898 -14.735 1.00 30.10 ?  256 HOH   B O    1 
HETATM 6835 O O    . HOH   E 3 .   ? 58.276 -10.716 -4.099  1.00 20.36 ?  257 HOH   B O    1 
HETATM 6836 O O    . HOH   E 3 .   ? 29.743 -25.196 -10.718 1.00 18.17 ?  258 HOH   B O    1 
HETATM 6837 O O    . HOH   E 3 .   ? 34.970 -33.246 -19.205 1.00 34.24 ?  259 HOH   B O    1 
HETATM 6838 O O    . HOH   E 3 .   ? 30.890 -15.717 2.711   1.00 14.91 ?  260 HOH   B O    1 
HETATM 6839 O O    . HOH   E 3 .   ? 40.368 -12.751 -11.476 1.00 16.15 ?  261 HOH   B O    1 
HETATM 6840 O O    . HOH   E 3 .   ? 33.561 -16.972 8.077   1.00 19.57 ?  262 HOH   B O    1 
HETATM 6841 O O    . HOH   E 3 .   ? 39.008 -11.881 12.356  1.00 37.03 ?  263 HOH   B O    1 
HETATM 6842 O O    . HOH   E 3 .   ? 41.986 -23.456 9.318   1.00 21.56 ?  264 HOH   B O    1 
HETATM 6843 O O    . HOH   E 3 .   ? 27.117 -31.812 -9.904  1.00 20.88 ?  265 HOH   B O    1 
HETATM 6844 O O    . HOH   E 3 .   ? 31.791 -17.851 -14.500 1.00 31.26 ?  266 HOH   B O    1 
HETATM 6845 O O    . HOH   E 3 .   ? 42.407 -9.890  9.327   1.00 22.97 ?  267 HOH   B O    1 
HETATM 6846 O O    . HOH   E 3 .   ? 56.172 -23.633 -14.752 1.00 29.38 ?  268 HOH   B O    1 
HETATM 6847 O O    . HOH   E 3 .   ? 46.980 -29.571 9.835   1.00 31.01 ?  269 HOH   B O    1 
HETATM 6848 O O    . HOH   E 3 .   ? 43.408 -15.781 -12.188 1.00 14.93 ?  270 HOH   B O    1 
HETATM 6849 O O    . HOH   E 3 .   ? 42.485 -34.690 3.845   1.00 25.73 ?  271 HOH   B O    1 
HETATM 6850 O O    . HOH   E 3 .   ? 51.678 -6.014  -7.972  1.00 45.08 ?  272 HOH   B O    1 
HETATM 6851 O O    . HOH   E 3 .   ? 49.350 -28.744 -6.925  1.00 16.47 ?  273 HOH   B O    1 
HETATM 6852 O O    . HOH   E 3 .   ? 34.551 -12.761 2.643   1.00 23.78 ?  274 HOH   B O    1 
HETATM 6853 O O    . HOH   E 3 .   ? 57.014 -8.606  8.363   1.00 19.79 ?  275 HOH   B O    1 
HETATM 6854 O O    . HOH   E 3 .   ? 27.997 -22.887 -7.954  1.00 18.73 ?  276 HOH   B O    1 
HETATM 6855 O O    . HOH   E 3 .   ? 49.789 -0.413  10.149  1.00 29.97 ?  277 HOH   B O    1 
HETATM 6856 O O    . HOH   E 3 .   ? 48.135 -22.804 5.845   1.00 19.63 ?  278 HOH   B O    1 
HETATM 6857 O O    . HOH   E 3 .   ? 28.266 -34.336 -9.340  1.00 17.24 ?  279 HOH   B O    1 
HETATM 6858 O O    . HOH   E 3 .   ? 57.548 -9.204  1.323   1.00 19.98 ?  280 HOH   B O    1 
HETATM 6859 O O    . HOH   E 3 .   ? 48.457 -25.046 3.118   1.00 14.36 ?  281 HOH   B O    1 
HETATM 6860 O O    . HOH   E 3 .   ? 42.834 -20.158 -20.670 1.00 37.30 ?  282 HOH   B O    1 
HETATM 6861 O O    . HOH   E 3 .   ? 27.570 -26.673 -15.606 1.00 35.36 ?  283 HOH   B O    1 
HETATM 6862 O O    . HOH   E 3 .   ? 57.174 -12.082 12.279  1.00 42.69 ?  284 HOH   B O    1 
HETATM 6863 O O    . HOH   E 3 .   ? 46.617 -31.230 -4.833  1.00 25.22 ?  285 HOH   B O    1 
HETATM 6864 O O    . HOH   E 3 .   ? 48.777 -20.003 5.927   1.00 14.39 ?  286 HOH   B O    1 
HETATM 6865 O O    . HOH   E 3 .   ? 33.571 -15.304 -13.937 1.00 22.48 ?  287 HOH   B O    1 
HETATM 6866 O O    . HOH   E 3 .   ? 47.106 -33.980 -4.663  1.00 19.43 ?  288 HOH   B O    1 
HETATM 6867 O O    . HOH   E 3 .   ? 41.230 -5.426  11.432  1.00 44.77 ?  289 HOH   B O    1 
HETATM 6868 O O    . HOH   E 3 .   ? 38.371 -12.225 -16.285 1.00 45.94 ?  290 HOH   B O    1 
HETATM 6869 O O    . HOH   E 3 .   ? 45.297 -33.356 -16.028 1.00 27.05 ?  291 HOH   B O    1 
HETATM 6870 O O    . HOH   E 3 .   ? 47.849 -24.417 -17.881 1.00 35.60 ?  292 HOH   B O    1 
HETATM 6871 O O    . HOH   E 3 .   ? 52.583 -10.374 12.956  1.00 24.89 ?  293 HOH   B O    1 
HETATM 6872 O O    . HOH   E 3 .   ? 37.476 -35.686 7.315   1.00 33.60 ?  294 HOH   B O    1 
HETATM 6873 O O    . HOH   E 3 .   ? 35.190 -33.701 4.631   1.00 34.32 ?  295 HOH   B O    1 
HETATM 6874 O O    . HOH   E 3 .   ? 51.212 -37.637 -9.718  1.00 28.41 ?  296 HOH   B O    1 
HETATM 6875 O O    . HOH   E 3 .   ? 36.064 -43.584 -8.325  1.00 44.06 ?  297 HOH   B O    1 
HETATM 6876 O O    . HOH   E 3 .   ? 43.302 -34.392 0.031   1.00 24.58 ?  298 HOH   B O    1 
HETATM 6877 O O    . HOH   E 3 .   ? 44.688 -27.494 2.041   1.00 16.71 ?  299 HOH   B O    1 
HETATM 6878 O O    . HOH   E 3 .   ? 44.719 -24.565 9.601   1.00 21.40 ?  300 HOH   B O    1 
HETATM 6879 O O    . HOH   E 3 .   ? 49.824 -24.810 5.803   1.00 36.40 ?  301 HOH   B O    1 
HETATM 6880 O O    . HOH   E 3 .   ? 36.766 -12.746 -1.438  1.00 29.02 ?  302 HOH   B O    1 
HETATM 6881 O O    . HOH   E 3 .   ? 52.593 -35.643 -8.843  1.00 32.21 ?  303 HOH   B O    1 
HETATM 6882 O O    . HOH   E 3 .   ? 25.986 -21.481 -3.434  1.00 17.59 ?  304 HOH   B O    1 
HETATM 6883 O O    . HOH   E 3 .   ? 42.760 -12.234 -18.474 1.00 28.26 ?  305 HOH   B O    1 
HETATM 6884 O O    . HOH   E 3 .   ? 40.282 -10.842 -9.482  1.00 18.44 ?  306 HOH   B O    1 
HETATM 6885 O O    . HOH   E 3 .   ? 43.573 -15.402 18.065  1.00 33.11 ?  307 HOH   B O    1 
HETATM 6886 O O    . HOH   E 3 .   ? 38.467 -9.370  -13.302 1.00 32.68 ?  308 HOH   B O    1 
HETATM 6887 O O    . HOH   E 3 .   ? 38.383 -12.700 7.927   1.00 18.04 ?  309 HOH   B O    1 
HETATM 6888 O O    . HOH   E 3 .   ? 59.851 -15.220 8.170   1.00 34.48 ?  310 HOH   B O    1 
HETATM 6889 O O    . HOH   E 3 .   ? 53.674 -12.649 -22.197 1.00 30.91 ?  311 HOH   B O    1 
HETATM 6890 O O    . HOH   E 3 .   ? 53.500 -30.226 4.527   1.00 18.81 ?  312 HOH   B O    1 
HETATM 6891 O O    . HOH   E 3 .   ? 62.784 -13.568 4.684   1.00 28.07 ?  313 HOH   B O    1 
HETATM 6892 O O    . HOH   E 3 .   ? 48.203 -32.694 -16.678 1.00 43.94 ?  314 HOH   B O    1 
HETATM 6893 O O    . HOH   E 3 .   ? 43.303 -21.403 10.691  1.00 17.44 ?  315 HOH   B O    1 
HETATM 6894 O O    . HOH   E 3 .   ? 45.868 -40.397 -3.598  1.00 32.79 ?  316 HOH   B O    1 
HETATM 6895 O O    . HOH   E 3 .   ? 37.925 -10.218 -10.732 1.00 18.95 ?  317 HOH   B O    1 
HETATM 6896 O O    . HOH   E 3 .   ? 44.090 -29.373 -4.671  1.00 23.09 ?  318 HOH   B O    1 
HETATM 6897 O O    . HOH   E 3 .   ? 37.481 -17.894 13.183  1.00 30.87 ?  319 HOH   B O    1 
HETATM 6898 O O    . HOH   E 3 .   ? 52.507 -29.284 -13.137 1.00 25.21 ?  320 HOH   B O    1 
HETATM 6899 O O    . HOH   E 3 .   ? 33.829 -31.062 11.116  1.00 37.94 ?  321 HOH   B O    1 
HETATM 6900 O O    . HOH   E 3 .   ? 57.564 -21.916 3.429   1.00 33.34 ?  322 HOH   B O    1 
HETATM 6901 O O    . HOH   E 3 .   ? 53.154 -16.085 -12.745 1.00 28.01 ?  323 HOH   B O    1 
HETATM 6902 O O    . HOH   E 3 .   ? 32.863 -34.618 -5.822  1.00 18.45 ?  324 HOH   B O    1 
HETATM 6903 O O    . HOH   E 3 .   ? 41.796 -8.076  1.392   1.00 24.96 ?  325 HOH   B O    1 
HETATM 6904 O O    . HOH   E 3 .   ? 44.211 -1.769  7.572   1.00 45.97 ?  326 HOH   B O    1 
HETATM 6905 O O    . HOH   E 3 .   ? 26.358 -21.058 -6.203  1.00 17.37 ?  327 HOH   B O    1 
HETATM 6906 O O    . HOH   E 3 .   ? 48.654 -12.064 -14.155 1.00 27.54 ?  328 HOH   B O    1 
HETATM 6907 O O    . HOH   E 3 .   ? 42.471 -9.731  -14.858 1.00 41.43 ?  329 HOH   B O    1 
HETATM 6908 O O    . HOH   E 3 .   ? 37.045 -30.623 -21.028 1.00 33.86 ?  330 HOH   B O    1 
HETATM 6909 O O    . HOH   E 3 .   ? 62.919 -20.193 -0.798  1.00 40.42 ?  331 HOH   B O    1 
HETATM 6910 O O    . HOH   E 3 .   ? 51.383 -33.181 -10.977 1.00 43.75 ?  332 HOH   B O    1 
HETATM 6911 O O    . HOH   E 3 .   ? 36.802 -12.376 4.299   1.00 18.54 ?  333 HOH   B O    1 
HETATM 6912 O O    . HOH   E 3 .   ? 47.339 -24.467 8.188   1.00 26.04 ?  334 HOH   B O    1 
HETATM 6913 O O    . HOH   E 3 .   ? 59.983 -17.349 -10.594 1.00 35.82 ?  335 HOH   B O    1 
HETATM 6914 O O    . HOH   E 3 .   ? 27.724 -14.773 -9.518  1.00 38.09 ?  336 HOH   B O    1 
HETATM 6915 O O    . HOH   E 3 .   ? 34.509 -10.359 7.864   1.00 23.36 ?  337 HOH   B O    1 
HETATM 6916 O O    . HOH   E 3 .   ? 42.824 -43.583 -14.330 1.00 41.28 ?  338 HOH   B O    1 
HETATM 6917 O O    . HOH   E 3 .   ? 47.516 -27.424 2.018   1.00 16.17 ?  339 HOH   B O    1 
HETATM 6918 O O    . HOH   E 3 .   ? 45.632 -36.300 -16.120 1.00 38.73 ?  340 HOH   B O    1 
HETATM 6919 O O    . HOH   E 3 .   ? 46.903 -19.838 12.214  1.00 33.71 ?  341 HOH   B O    1 
HETATM 6920 O O    . HOH   E 3 .   ? 37.030 -45.124 -9.720  1.00 33.09 ?  342 HOH   B O    1 
HETATM 6921 O O    . HOH   E 3 .   ? 37.088 -15.110 -16.604 1.00 43.37 ?  343 HOH   B O    1 
HETATM 6922 O O    . HOH   E 3 .   ? 28.868 -42.870 -12.298 1.00 43.00 ?  344 HOH   B O    1 
HETATM 6923 O O    . HOH   E 3 .   ? 41.383 -24.519 15.930  1.00 47.06 ?  345 HOH   B O    1 
HETATM 6924 O O    . HOH   E 3 .   ? 39.786 -44.110 -11.191 1.00 43.22 ?  346 HOH   B O    1 
HETATM 6925 O O    . HOH   E 3 .   ? 33.044 -14.647 1.081   1.00 21.96 ?  347 HOH   B O    1 
HETATM 6926 O O    . HOH   E 3 .   ? 33.633 -9.942  -8.768  1.00 30.42 ?  348 HOH   B O    1 
HETATM 6927 O O    . HOH   E 3 .   ? 38.612 -22.312 15.077  1.00 45.29 ?  349 HOH   B O    1 
HETATM 6928 O O    . HOH   E 3 .   ? 62.545 -20.089 -4.838  1.00 48.58 ?  350 HOH   B O    1 
HETATM 6929 O O    . HOH   E 3 .   ? 40.377 -43.494 -9.121  1.00 27.44 ?  351 HOH   B O    1 
HETATM 6930 O O    . HOH   E 3 .   ? 44.192 -37.416 -17.771 1.00 34.66 ?  352 HOH   B O    1 
HETATM 6931 O O    . HOH   E 3 .   ? 39.651 -23.658 -20.412 1.00 43.97 ?  353 HOH   B O    1 
HETATM 6932 O O    . HOH   E 3 .   ? 27.843 -26.606 -0.509  1.00 30.66 ?  354 HOH   B O    1 
HETATM 6933 O O    . HOH   E 3 .   ? 55.767 -8.229  10.786  1.00 23.73 ?  355 HOH   B O    1 
HETATM 6934 O O    . HOH   E 3 .   ? 23.304 -23.668 6.840   1.00 35.31 ?  356 HOH   B O    1 
HETATM 6935 O O    . HOH   E 3 .   ? 56.678 -7.241  2.940   1.00 26.80 ?  357 HOH   B O    1 
HETATM 6936 O O    . HOH   E 3 .   ? 43.227 -12.676 -21.159 1.00 43.58 ?  358 HOH   B O    1 
HETATM 6937 O O    . HOH   E 3 .   ? 34.051 -7.740  11.563  1.00 43.74 ?  359 HOH   B O    1 
HETATM 6938 O O    . HOH   E 3 .   ? 36.226 -8.419  -9.759  1.00 35.79 ?  360 HOH   B O    1 
HETATM 6939 O O    . HOH   E 3 .   ? 56.906 -21.635 -16.463 1.00 40.52 ?  361 HOH   B O    1 
HETATM 6940 O O    . HOH   E 3 .   ? 61.574 -19.922 1.749   1.00 38.18 ?  362 HOH   B O    1 
HETATM 6941 O O    . HOH   E 3 .   ? 27.188 -25.922 -11.296 1.00 36.64 ?  363 HOH   B O    1 
HETATM 6942 O O    . HOH   E 3 .   ? 40.334 -8.829  9.830   1.00 37.67 ?  364 HOH   B O    1 
HETATM 6943 O O    . HOH   E 3 .   ? 48.280 -26.435 8.812   1.00 44.68 ?  365 HOH   B O    1 
HETATM 6944 O O    . HOH   E 3 .   ? 40.458 -11.297 -13.893 1.00 34.11 ?  366 HOH   B O    1 
HETATM 6945 O O    . HOH   E 3 .   ? 58.989 -10.465 9.166   1.00 38.31 ?  367 HOH   B O    1 
HETATM 6946 O O    . HOH   E 3 .   ? 36.213 -8.719  8.997   1.00 33.10 ?  368 HOH   B O    1 
HETATM 6947 O O    . HOH   E 3 .   ? 32.664 -23.607 14.102  1.00 40.57 ?  369 HOH   B O    1 
HETATM 6948 O O    . HOH   E 3 .   ? 54.329 -5.730  2.854   1.00 36.93 ?  370 HOH   B O    1 
HETATM 6949 O O    . HOH   E 3 .   ? 52.124 -12.897 13.255  1.00 30.92 ?  371 HOH   B O    1 
HETATM 6950 O O    . HOH   E 3 .   ? 39.867 -7.090  7.771   1.00 41.61 ?  372 HOH   B O    1 
HETATM 6951 O O    . HOH   E 3 .   ? 41.910 -10.005 -17.512 1.00 58.53 ?  373 HOH   B O    1 
HETATM 6952 O O    . HOH   E 3 .   ? 42.767 -17.308 -23.088 1.00 45.71 ?  374 HOH   B O    1 
HETATM 6953 O O    . HOH   E 3 .   ? 63.102 -12.344 6.911   1.00 38.39 ?  375 HOH   B O    1 
HETATM 6954 O O    . HOH   E 3 .   ? 36.573 -22.826 13.279  1.00 31.55 ?  376 HOH   B O    1 
HETATM 6955 O O    . HOH   E 3 .   ? 56.121 -7.682  -0.646  1.00 35.80 ?  377 HOH   B O    1 
HETATM 6956 O O    . HOH   E 3 .   ? 38.089 -10.470 10.006  1.00 29.01 ?  378 HOH   B O    1 
HETATM 6957 O O    . HOH   E 3 .   ? 40.193 -7.677  3.109   1.00 41.82 ?  379 HOH   B O    1 
HETATM 6958 O O    . HOH   E 3 .   ? 41.850 -6.620  -4.873  1.00 45.63 ?  380 HOH   B O    1 
HETATM 6959 O O    . HOH   E 3 .   ? 39.652 -14.002 15.610  1.00 51.96 ?  381 HOH   B O    1 
HETATM 6960 O O    . HOH   E 3 .   ? 44.096 -5.548  -3.506  1.00 41.64 ?  382 HOH   B O    1 
HETATM 6961 O O    . HOH   E 3 .   ? 52.904 -29.935 7.172   1.00 24.14 ?  383 HOH   B O    1 
HETATM 6962 O O    . HOH   E 3 .   ? 60.542 -22.166 2.939   1.00 54.53 ?  384 HOH   B O    1 
HETATM 6963 O O    . HOH   E 3 .   ? 46.759 -5.461  2.888   1.00 40.72 ?  385 HOH   B O    1 
HETATM 6964 O O    . HOH   E 3 .   ? 41.065 -9.729  15.765  1.00 52.20 ?  386 HOH   B O    1 
HETATM 6965 O O    . HOH   E 3 .   ? 23.204 -23.788 1.490   1.00 37.87 ?  387 HOH   B O    1 
HETATM 6966 O O    . HOH   E 3 .   ? 35.501 -33.685 7.386   1.00 43.74 ?  388 HOH   B O    1 
HETATM 6967 O O    . HOH   E 3 .   ? 35.294 -20.400 13.288  1.00 36.86 ?  389 HOH   B O    1 
HETATM 6968 O O    . HOH   E 3 .   ? 23.933 -20.937 -7.623  1.00 30.56 ?  390 HOH   B O    1 
HETATM 6969 O O    . HOH   E 3 .   ? 40.736 -6.614  -0.841  1.00 27.44 ?  391 HOH   B O    1 
HETATM 6970 O O    . HOH   E 3 .   ? 44.150 -31.814 -3.816  1.00 41.95 ?  392 HOH   B O    1 
HETATM 6971 O O    . HOH   E 3 .   ? 28.004 -27.048 2.356   1.00 30.10 ?  393 HOH   B O    1 
HETATM 6972 O O    . HOH   E 3 .   ? 26.590 -27.863 -13.371 1.00 38.41 ?  394 HOH   B O    1 
HETATM 6973 O O    . HOH   E 3 .   ? 24.649 -20.622 -10.466 1.00 41.06 ?  395 HOH   B O    1 
HETATM 6974 O O    . HOH   E 3 .   ? 50.709 -30.886 8.746   1.00 30.95 ?  396 HOH   B O    1 
HETATM 6975 O O    . HOH   E 3 .   ? 26.805 -30.587 -12.604 1.00 28.95 ?  397 HOH   B O    1 
HETATM 6976 O O    . HOH   E 3 .   ? 34.395 -33.511 9.636   1.00 39.17 ?  398 HOH   B O    1 
HETATM 6977 O O    . HOH   E 3 .   ? 45.694 -20.060 15.300  1.00 46.43 ?  399 HOH   B O    1 
HETATM 6978 O O    . HOH   E 3 .   ? 57.592 -6.450  -2.309  1.00 33.62 ?  400 HOH   B O    1 
HETATM 6979 O O    . HOH   E 3 .   ? 40.869 -11.754 -22.216 1.00 42.76 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.7321 0.7411 0.8514 -0.0070 -0.0274 0.0813  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7122 0.7124 0.8126 -0.0093 -0.0155 0.0396  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7283 0.7374 0.8411 -0.0089 -0.0270 0.0827  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7085 0.7084 0.8032 -0.0103 -0.0154 0.0401  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.7072 0.7214 0.7993 -0.0172 -0.0254 0.0868  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6892 0.6916 0.7640 -0.0154 -0.0155 0.0415  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.7109 0.7251 0.8153 -0.0154 -0.0270 0.0886  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6925 0.6949 0.7760 -0.0145 -0.0162 0.0422  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7420 0.7472 0.8611 -0.0048 -0.0273 0.0814  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7207 0.7187 0.8230 -0.0075 -0.0151 0.0397  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7472 0.7506 0.8662 -0.0032 -0.0278 0.0811  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7254 0.7225 0.8287 -0.0065 -0.0151 0.0396  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7463 0.7500 0.8668 -0.0035 -0.0270 0.0819  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7244 0.7216 0.8291 -0.0066 -0.0148 0.0401  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6788 0.6982 0.7310 -0.0279 -0.0204 0.0885  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6635 0.6682 0.7044 -0.0220 -0.0141 0.0419  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6466 0.6716 0.6538 -0.0399 -0.0140 0.0878  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6346 0.6419 0.6385 -0.0291 -0.0122 0.0407  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.6008 0.6373 0.6057 -0.0556 -0.0004 0.0740  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5954 0.6082 0.5963 -0.0386 -0.0040 0.0343  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.6028 0.6392 0.6031 -0.0546 -0.0030 0.0767  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5970 0.6099 0.5956 -0.0383 -0.0050 0.0363  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6568 0.6771 0.6165 -0.0376 -0.0201 0.1009  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6424 0.6474 0.6099 -0.0276 -0.0177 0.0461  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6645 0.6806 0.5832 -0.0367 -0.0260 0.1124  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6481 0.6510 0.5849 -0.0268 -0.0229 0.0502  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6682 0.6817 0.5719 -0.0365 -0.0315 0.1159  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6504 0.6520 0.5764 -0.0264 -0.0265 0.0515  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6664 0.6819 0.5732 -0.0361 -0.0249 0.1192  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6497 0.6522 0.5776 -0.0264 -0.0234 0.0532  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5504 0.5990 0.5531 -0.0739 0.0160  0.0589  5   SER   A N   
60   N N   B SER   A 5   ? 0.5529 0.5712 0.5507 -0.0489 0.0050  0.0262  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4985 0.5602 0.5028 -0.0903 0.0363  0.0456  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.5096 0.5336 0.5065 -0.0586 0.0159  0.0190  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4386 0.5111 0.4343 -0.1048 0.0597  0.0437  5   SER   A C   
64   C C   B SER   A 5   ? 0.4621 0.4899 0.4453 -0.0657 0.0263  0.0158  5   SER   A C   
65   O O   A SER   A 5   ? 0.4412 0.5131 0.4283 -0.1033 0.0650  0.0361  5   SER   A O   
66   O O   B SER   A 5   ? 0.4634 0.4909 0.4415 -0.0651 0.0307  0.0120  5   SER   A O   
67   C CB  A SER   A 5   ? 0.5070 0.5696 0.5248 -0.0906 0.0358  0.0358  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.5144 0.5391 0.5244 -0.0599 0.0175  0.0154  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.5123 0.5752 0.5411 -0.0904 0.0351  0.0294  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.5175 0.5425 0.5362 -0.0602 0.0180  0.0128  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3752 0.4595 0.3658 -0.1191 0.0764  0.0500  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.4130 0.4458 0.3866 -0.0724 0.0313  0.0159  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3148 0.4069 0.3085 -0.1298 0.0792  0.0608  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3651 0.4016 0.3338 -0.0775 0.0324  0.0189  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3060 0.3996 0.3101 -0.1287 0.0914  0.0591  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3473 0.3860 0.3307 -0.0790 0.0426  0.0169  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3143 0.4106 0.3395 -0.1274 0.0875  0.0750  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3511 0.3895 0.3458 -0.0768 0.0436  0.0240  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2820 0.3661 0.2642 -0.1284 0.0579  0.0695  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.3407 0.3753 0.2934 -0.0784 0.0230  0.0227  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2564 0.3394 0.2364 -0.1138 0.0348  0.0611  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.3198 0.3543 0.2639 -0.0764 0.0145  0.0231  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2438 0.3261 0.2226 -0.1045 0.0182  0.0539  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.3110 0.3445 0.2504 -0.0747 0.0101  0.0238  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2609 0.3306 0.2511 -0.0943 0.0242  0.0537  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.3149 0.3455 0.2617 -0.0722 0.0127  0.0231  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2393 0.3143 0.2169 -0.1012 0.0185  0.0540  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.3062 0.3371 0.2437 -0.0746 0.0109  0.0263  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2549 0.3213 0.2447 -0.0907 0.0208  0.0495  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.3098 0.3394 0.2537 -0.0715 0.0127  0.0237  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2463 0.3139 0.2350 -0.0969 0.0114  0.0449  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.3066 0.3359 0.2485 -0.0739 0.0097  0.0238  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2896 0.3747 0.2827 -0.1260 0.0984  0.0462  7   SER   A N   
122  N N   B SER   A 7   ? 0.3260 0.3649 0.3141 -0.0802 0.0474  0.0080  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2907 0.3677 0.2823 -0.1068 0.0904  0.0153  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.3113 0.3497 0.3102 -0.0742 0.0461  -0.0039 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2699 0.3229 0.2388 -0.1017 0.0995  0.0191  7   SER   A C   
126  C C   B SER   A 7   ? 0.2848 0.3185 0.2771 -0.0722 0.0501  -0.0047 7   SER   A C   
127  O O   A SER   A 7   ? 0.2850 0.3111 0.2261 -0.1084 0.0907  0.0241  7   SER   A O   
128  O O   B SER   A 7   ? 0.2877 0.3136 0.2712 -0.0777 0.0498  -0.0063 7   SER   A O   
129  C CB  A SER   A 7   ? 0.3144 0.3966 0.3247 -0.0934 0.0768  0.0049  7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3234 0.3654 0.3409 -0.0689 0.0415  -0.0057 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.3339 0.4114 0.3687 -0.0799 0.0632  -0.0008 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3345 0.3754 0.3696 -0.0622 0.0357  -0.0063 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2463 0.2928 0.2431 -0.0850 0.0990  0.0071  8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2595 0.2934 0.2642 -0.0633 0.0522  -0.0022 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2320 0.2595 0.2569 -0.0623 0.0886  0.0074  8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2386 0.2675 0.2616 -0.0503 0.0534  0.0048  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.2070 0.2374 0.2574 -0.0450 0.0710  0.0088  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2120 0.2466 0.2561 -0.0400 0.0519  0.0116  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.2107 0.2301 0.2825 -0.0200 0.0626  -0.0092 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2152 0.2455 0.2655 -0.0275 0.0466  0.0027  8   GLY   A O   
157  N N   . TYR   A 9   ? 0.1867 0.2302 0.2542 -0.0329 0.0505  0.0276  9   TYR   A N   
158  C CA  . TYR   A 9   ? 0.1675 0.2101 0.2214 -0.0251 0.0314  0.0440  9   TYR   A CA  
159  C C   . TYR   A 9   ? 0.1620 0.1929 0.2173 -0.0168 0.0392  0.0601  9   TYR   A C   
160  O O   . TYR   A 9   ? 0.1882 0.2142 0.2287 -0.0145 0.0331  0.0598  9   TYR   A O   
161  C CB  . TYR   A 9   ? 0.1653 0.2244 0.2248 -0.0167 0.0303  0.0462  9   TYR   A CB  
162  C CG  . TYR   A 9   ? 0.1677 0.2302 0.2126 -0.0089 0.0361  0.0277  9   TYR   A CG  
163  C CD1 . TYR   A 9   ? 0.1712 0.2428 0.2230 -0.0268 0.0312  0.0086  9   TYR   A CD1 
164  C CD2 . TYR   A 9   ? 0.1646 0.2237 0.2047 -0.0143 0.0276  0.0402  9   TYR   A CD2 
165  C CE1 . TYR   A 9   ? 0.1765 0.2493 0.2300 -0.0301 0.0404  -0.0028 9   TYR   A CE1 
166  C CE2 . TYR   A 9   ? 0.1729 0.2341 0.2243 -0.0223 0.0361  0.0234  9   TYR   A CE2 
167  C CZ  . TYR   A 9   ? 0.1731 0.2435 0.2456 -0.0372 0.0461  0.0072  9   TYR   A CZ  
168  O OH  . TYR   A 9   ? 0.1851 0.2494 0.2839 -0.0540 0.0524  -0.0080 9   TYR   A OH  
179  N N   . LEU   A 10  ? 0.1576 0.1824 0.2239 -0.0120 0.0319  0.0469  10  LEU   A N   
180  C CA  . LEU   A 10  ? 0.1526 0.1798 0.2227 -0.0227 0.0198  0.0549  10  LEU   A CA  
181  C C   . LEU   A 10  ? 0.1557 0.1762 0.2070 -0.0241 0.0068  0.0544  10  LEU   A C   
182  O O   . LEU   A 10  ? 0.1620 0.1633 0.2191 -0.0282 0.0282  0.0487  10  LEU   A O   
183  C CB  . LEU   A 10  ? 0.1671 0.1880 0.2672 -0.0266 -0.0004 0.0725  10  LEU   A CB  
184  C CG  . LEU   A 10  ? 0.1815 0.2019 0.3258 -0.0175 -0.0422 0.0921  10  LEU   A CG  
185  C CD1 . LEU   A 10  ? 0.2014 0.2209 0.3658 -0.0168 -0.0366 0.0846  10  LEU   A CD1 
186  C CD2 . LEU   A 10  ? 0.2168 0.2323 0.3609 -0.0145 -0.0211 0.0662  10  LEU   A CD2 
198  N N   . LYS   A 11  ? 0.1604 0.1818 0.2089 -0.0335 0.0068  0.0559  11  LYS   A N   
199  C CA  . LYS   A 11  ? 0.1604 0.1738 0.2097 -0.0343 0.0002  0.0647  11  LYS   A CA  
200  C C   . LYS   A 11  ? 0.1612 0.1829 0.2107 -0.0451 0.0048  0.0581  11  LYS   A C   
201  O O   . LYS   A 11  ? 0.1692 0.2355 0.2359 -0.0768 0.0092  0.0357  11  LYS   A O   
202  C CB  . LYS   A 11  ? 0.1680 0.1597 0.2041 -0.0349 0.0056  0.0326  11  LYS   A CB  
203  C CG  . LYS   A 11  ? 0.1788 0.1621 0.1963 -0.0280 0.0037  0.0428  11  LYS   A CG  
204  C CD  . LYS   A 11  ? 0.1873 0.1695 0.1987 -0.0248 0.0048  0.0389  11  LYS   A CD  
205  C CE  . LYS   A 11  ? 0.2027 0.1781 0.1956 -0.0258 0.0139  0.0383  11  LYS   A CE  
206  N NZ  . LYS   A 11  ? 0.2044 0.1769 0.2168 -0.0148 -0.0002 0.0552  11  LYS   A NZ  
220  N N   . LEU   A 12  ? 0.1453 0.1753 0.1980 -0.0353 -0.0020 0.0439  12  LEU   A N   
221  C CA  . LEU   A 12  ? 0.1462 0.1953 0.1947 -0.0302 -0.0058 0.0535  12  LEU   A CA  
222  C C   . LEU   A 12  ? 0.1528 0.1860 0.1937 -0.0353 0.0067  0.0525  12  LEU   A C   
223  O O   . LEU   A 12  ? 0.1590 0.1955 0.2101 -0.0424 -0.0035 0.0480  12  LEU   A O   
224  C CB  . LEU   A 12  ? 0.1608 0.2030 0.2142 -0.0220 0.0000  0.0594  12  LEU   A CB  
225  C CG  . LEU   A 12  ? 0.1706 0.2098 0.2316 -0.0169 0.0143  0.0591  12  LEU   A CG  
226  C CD1 . LEU   A 12  ? 0.1928 0.2157 0.2244 -0.0031 0.0301  0.0686  12  LEU   A CD1 
227  C CD2 . LEU   A 12  ? 0.1723 0.2157 0.2612 -0.0144 0.0130  0.0597  12  LEU   A CD2 
239  N N   . THR   A 13  ? 0.1553 0.1692 0.2112 -0.0299 0.0155  0.0388  13  THR   A N   
240  C CA  . THR   A 13  ? 0.1581 0.1703 0.2091 -0.0307 0.0186  0.0388  13  THR   A CA  
241  C C   . THR   A 13  ? 0.1543 0.1594 0.2255 -0.0360 0.0158  0.0441  13  THR   A C   
242  O O   . THR   A 13  ? 0.1600 0.1627 0.2324 -0.0252 0.0039  0.0440  13  THR   A O   
243  C CB  . THR   A 13  ? 0.1727 0.1926 0.2183 -0.0301 0.0129  0.0474  13  THR   A CB  
244  O OG1 . THR   A 13  ? 0.1680 0.1912 0.2408 -0.0385 0.0221  0.0515  13  THR   A OG1 
245  C CG2 . THR   A 13  ? 0.1854 0.2092 0.2298 -0.0285 0.0206  0.0295  13  THR   A CG2 
253  N N   . ASP   A 14  ? 0.1613 0.1636 0.2661 -0.0346 0.0029  0.0529  14  ASP   A N   
254  C CA  . ASP   A 14  ? 0.1679 0.1716 0.2826 -0.0327 0.0022  0.0617  14  ASP   A CA  
255  C C   . ASP   A 14  ? 0.1568 0.1721 0.2561 -0.0284 -0.0033 0.0653  14  ASP   A C   
256  O O   . ASP   A 14  ? 0.1825 0.1975 0.2720 -0.0463 -0.0209 0.0647  14  ASP   A O   
257  C CB  . ASP   A 14  ? 0.2045 0.2084 0.3335 -0.0334 0.0047  0.0894  14  ASP   A CB  
258  C CG  . ASP   A 14  ? 0.2267 0.2654 0.3935 -0.0337 0.0091  0.0837  14  ASP   A CG  
259  O OD1 . ASP   A 14  ? 0.2401 0.2872 0.4216 -0.0102 -0.0161 0.0886  14  ASP   A OD1 
260  O OD2 . ASP   A 14  ? 0.2423 0.3168 0.4412 -0.0150 0.0041  0.0575  14  ASP   A OD2 
265  N N   . ASN   A 15  ? 0.1446 0.1560 0.2489 -0.0317 0.0043  0.0633  15  ASN   A N   
266  C CA  . ASN   A 15  ? 0.1491 0.1570 0.2532 -0.0128 -0.0060 0.0487  15  ASN   A CA  
267  C C   . ASN   A 15  ? 0.1459 0.1559 0.2642 -0.0198 -0.0033 0.0509  15  ASN   A C   
268  O O   . ASN   A 15  ? 0.1523 0.1584 0.3038 -0.0220 -0.0209 0.0637  15  ASN   A O   
269  C CB  . ASN   A 15  ? 0.1490 0.1609 0.2470 -0.0098 0.0057  0.0536  15  ASN   A CB  
270  C CG  . ASN   A 15  ? 0.1468 0.1642 0.2596 -0.0050 0.0047  0.0379  15  ASN   A CG  
271  O OD1 . ASN   A 15  ? 0.1577 0.1736 0.2878 -0.0274 -0.0045 0.0403  15  ASN   A OD1 
272  N ND2 . ASN   A 15  ? 0.1580 0.1674 0.2439 -0.0118 0.0103  0.0310  15  ASN   A ND2 
279  N N   . VAL   A 16  ? 0.1481 0.1631 0.2476 -0.0234 -0.0019 0.0586  16  VAL   A N   
280  C CA  . VAL   A 16  ? 0.1498 0.1654 0.2425 -0.0198 0.0058  0.0599  16  VAL   A CA  
281  C C   . VAL   A 16  ? 0.1469 0.1639 0.2243 -0.0284 0.0099  0.0531  16  VAL   A C   
282  O O   . VAL   A 16  ? 0.1399 0.1567 0.2315 -0.0274 0.0136  0.0383  16  VAL   A O   
283  C CB  . VAL   A 16  ? 0.1648 0.1769 0.2501 0.0068  0.0190  0.0701  16  VAL   A CB  
284  C CG1 . VAL   A 16  ? 0.1821 0.1899 0.2570 0.0168  0.0311  0.0637  16  VAL   A CG1 
285  C CG2 . VAL   A 16  ? 0.1652 0.1823 0.2593 0.0114  0.0507  0.0594  16  VAL   A CG2 
295  N N   . TYR   A 17  ? 0.1419 0.1518 0.2254 -0.0203 0.0175  0.0495  17  TYR   A N   
296  C CA  . TYR   A 17  ? 0.1501 0.1623 0.2134 -0.0238 0.0213  0.0511  17  TYR   A CA  
297  C C   . TYR   A 17  ? 0.1477 0.1561 0.2266 -0.0196 0.0058  0.0592  17  TYR   A C   
298  O O   . TYR   A 17  ? 0.1380 0.1622 0.2297 -0.0222 0.0175  0.0605  17  TYR   A O   
299  C CB  . TYR   A 17  ? 0.1627 0.1687 0.2282 -0.0266 -0.0044 0.0564  17  TYR   A CB  
300  C CG  . TYR   A 17  ? 0.1905 0.1707 0.2162 -0.0319 -0.0201 0.0526  17  TYR   A CG  
301  C CD1 . TYR   A 17  ? 0.2092 0.1751 0.2465 -0.0209 -0.0371 0.0553  17  TYR   A CD1 
302  C CD2 . TYR   A 17  ? 0.2156 0.1867 0.2026 -0.0475 -0.0136 0.0520  17  TYR   A CD2 
303  C CE1 . TYR   A 17  ? 0.2244 0.1805 0.2529 -0.0293 -0.0409 0.0586  17  TYR   A CE1 
304  C CE2 . TYR   A 17  ? 0.2383 0.1891 0.2139 -0.0472 -0.0276 0.0439  17  TYR   A CE2 
305  C CZ  . TYR   A 17  ? 0.2476 0.1817 0.2254 -0.0448 -0.0467 0.0602  17  TYR   A CZ  
306  O OH  . TYR   A 17  ? 0.2738 0.1892 0.2507 -0.0410 -0.0393 0.0468  17  TYR   A OH  
316  N N   A ILE   A 18  ? 0.1380 0.1634 0.2303 -0.0154 0.0140  0.0630  18  ILE   A N   
317  N N   B ILE   A 18  ? 0.1488 0.1689 0.2158 -0.0183 0.0138  0.0576  18  ILE   A N   
318  C CA  A ILE   A 18  ? 0.1420 0.1729 0.2244 -0.0056 0.0279  0.0689  18  ILE   A CA  
319  C CA  B ILE   A 18  ? 0.1577 0.1816 0.2027 -0.0137 0.0236  0.0558  18  ILE   A CA  
320  C C   A ILE   A 18  ? 0.1517 0.1748 0.2285 -0.0184 0.0336  0.0779  18  ILE   A C   
321  C C   B ILE   A 18  ? 0.1653 0.1894 0.1941 -0.0141 0.0195  0.0524  18  ILE   A C   
322  O O   A ILE   A 18  ? 0.1486 0.1898 0.2352 -0.0221 0.0316  0.0729  18  ILE   A O   
323  O O   B ILE   A 18  ? 0.1675 0.1980 0.1862 -0.0171 0.0121  0.0453  18  ILE   A O   
324  C CB  A ILE   A 18  ? 0.1573 0.1754 0.2055 0.0011  0.0258  0.0710  18  ILE   A CB  
325  C CB  B ILE   A 18  ? 0.1697 0.1841 0.1981 -0.0154 0.0311  0.0584  18  ILE   A CB  
326  C CG1 A ILE   A 18  ? 0.1699 0.1944 0.2189 0.0009  0.0099  0.0838  18  ILE   A CG1 
327  C CG1 B ILE   A 18  ? 0.1796 0.1949 0.2040 -0.0236 0.0271  0.0631  18  ILE   A CG1 
328  C CG2 A ILE   A 18  ? 0.1637 0.1778 0.2102 -0.0015 0.0231  0.0546  18  ILE   A CG2 
329  C CG2 B ILE   A 18  ? 0.1739 0.1874 0.2034 -0.0182 0.0328  0.0604  18  ILE   A CG2 
330  C CD1 A ILE   A 18  ? 0.1880 0.2145 0.2441 0.0126  0.0056  0.0782  18  ILE   A CD1 
331  C CD1 B ILE   A 18  ? 0.1931 0.2077 0.2171 -0.0202 0.0263  0.0595  18  ILE   A CD1 
354  N N   A LYS   A 19  ? 0.1521 0.1757 0.2343 -0.0073 0.0530  0.0646  19  LYS   A N   
355  N N   B LYS   A 19  ? 0.1646 0.1938 0.2074 -0.0021 0.0332  0.0430  19  LYS   A N   
356  C CA  A LYS   A 19  ? 0.1815 0.1883 0.2490 -0.0011 0.0601  0.0593  19  LYS   A CA  
357  C CA  B LYS   A 19  ? 0.1751 0.2041 0.2233 0.0049  0.0329  0.0385  19  LYS   A CA  
358  C C   A LYS   A 19  ? 0.1702 0.1798 0.2623 -0.0015 0.0714  0.0582  19  LYS   A C   
359  C C   B LYS   A 19  ? 0.1548 0.1991 0.2262 0.0059  0.0278  0.0422  19  LYS   A C   
360  O O   A LYS   A 19  ? 0.1605 0.1753 0.2681 0.0024  0.0634  0.0714  19  LYS   A O   
361  O O   B LYS   A 19  ? 0.1462 0.1963 0.2230 0.0028  0.0158  0.0419  19  LYS   A O   
362  C CB  A LYS   A 19  ? 0.1953 0.2099 0.2341 -0.0012 0.0671  0.0653  19  LYS   A CB  
363  C CB  B LYS   A 19  ? 0.1949 0.2206 0.2278 0.0069  0.0405  0.0339  19  LYS   A CB  
364  C CG  A LYS   A 19  ? 0.2286 0.2228 0.2465 -0.0027 0.0586  0.0557  19  LYS   A CG  
365  C CG  B LYS   A 19  ? 0.2171 0.2306 0.2390 0.0027  0.0412  0.0246  19  LYS   A CG  
366  C CD  A LYS   A 19  ? 0.2557 0.2468 0.2571 -0.0003 0.0606  0.0503  19  LYS   A CD  
367  C CD  B LYS   A 19  ? 0.2354 0.2475 0.2501 0.0005  0.0449  0.0212  19  LYS   A CD  
368  C CE  A LYS   A 19  ? 0.2721 0.2552 0.2738 -0.0106 0.0531  0.0407  19  LYS   A CE  
369  C CE  B LYS   A 19  ? 0.2472 0.2571 0.2593 -0.0088 0.0489  0.0190  19  LYS   A CE  
370  N NZ  A LYS   A 19  ? 0.2773 0.2585 0.2781 -0.0242 0.0668  0.0326  19  LYS   A NZ  
371  N NZ  B LYS   A 19  ? 0.2539 0.2637 0.2563 -0.0160 0.0552  0.0154  19  LYS   A NZ  
398  N N   A ASN   A 20  ? 0.1789 0.1788 0.2819 -0.0076 0.0688  0.0580  20  ASN   A N   
399  N N   B ASN   A 20  ? 0.1491 0.1983 0.2367 0.0094  0.0266  0.0505  20  ASN   A N   
400  C CA  A ASN   A 20  ? 0.1928 0.1955 0.2866 0.0117  0.0695  0.0506  20  ASN   A CA  
401  C CA  B ASN   A 20  ? 0.1504 0.2062 0.2398 0.0250  0.0284  0.0478  20  ASN   A CA  
402  C C   A ASN   A 20  ? 0.2012 0.1971 0.2688 0.0103  0.0744  0.0496  20  ASN   A C   
403  C C   B ASN   A 20  ? 0.1671 0.2056 0.2457 0.0253  0.0422  0.0394  20  ASN   A C   
404  O O   A ASN   A 20  ? 0.2097 0.2054 0.2537 0.0101  0.0661  0.0410  20  ASN   A O   
405  O O   B ASN   A 20  ? 0.1708 0.2131 0.2525 0.0330  0.0357  0.0405  20  ASN   A O   
406  C CB  A ASN   A 20  ? 0.2016 0.2003 0.3004 0.0195  0.0681  0.0464  20  ASN   A CB  
407  C CB  B ASN   A 20  ? 0.1365 0.2080 0.2359 0.0281  0.0195  0.0481  20  ASN   A CB  
408  C CG  A ASN   A 20  ? 0.2155 0.2064 0.3303 0.0328  0.0715  0.0399  20  ASN   A CG  
409  C CG  B ASN   A 20  ? 0.1275 0.2088 0.2438 0.0320  0.0134  0.0471  20  ASN   A CG  
410  O OD1 A ASN   A 20  ? 0.2365 0.2201 0.3720 0.0372  0.0775  0.0268  20  ASN   A OD1 
411  O OD1 B ASN   A 20  ? 0.1254 0.2022 0.2434 0.0353  0.0199  0.0301  20  ASN   A OD1 
412  N ND2 A ASN   A 20  ? 0.2290 0.1965 0.3371 0.0358  0.0548  0.0579  20  ASN   A ND2 
413  N ND2 B ASN   A 20  ? 0.1434 0.2100 0.2639 0.0250  0.0001  0.0658  20  ASN   A ND2 
426  N N   A ALA   A 21  ? 0.2079 0.1965 0.2839 0.0069  0.0661  0.0368  21  ALA   A N   
427  N N   B ALA   A 21  ? 0.1821 0.1991 0.2561 0.0187  0.0461  0.0186  21  ALA   A N   
428  C CA  A ALA   A 21  ? 0.2129 0.1926 0.2733 0.0040  0.0595  0.0579  21  ALA   A CA  
429  C CA  B ALA   A 21  ? 0.1958 0.1898 0.2571 0.0117  0.0482  0.0113  21  ALA   A CA  
430  C C   A ALA   A 21  ? 0.2044 0.1955 0.2734 0.0048  0.0478  0.0491  21  ALA   A C   
431  C C   B ALA   A 21  ? 0.1890 0.1749 0.2421 0.0025  0.0655  0.0034  21  ALA   A C   
432  O O   A ALA   A 21  ? 0.2052 0.2044 0.2796 0.0064  0.0511  0.0481  21  ALA   A O   
433  O O   B ALA   A 21  ? 0.1822 0.1630 0.2446 0.0006  0.0803  -0.0053 21  ALA   A O   
434  C CB  A ALA   A 21  ? 0.2235 0.1979 0.2883 0.0056  0.0525  0.0628  21  ALA   A CB  
435  C CB  B ALA   A 21  ? 0.2079 0.1990 0.2788 0.0169  0.0314  0.0004  21  ALA   A CB  
446  N N   A ASP   A 22  ? 0.2025 0.1831 0.2849 0.0059  0.0429  0.0411  22  ASP   A N   
447  N N   B ASP   A 22  ? 0.1905 0.1677 0.2441 0.0001  0.0748  0.0047  22  ASP   A N   
448  C CA  A ASP   A 22  ? 0.2004 0.1661 0.2693 0.0200  0.0397  0.0500  22  ASP   A CA  
449  C CA  B ASP   A 22  ? 0.1937 0.1675 0.2408 -0.0037 0.0767  0.0068  22  ASP   A CA  
450  C C   A ASP   A 22  ? 0.1842 0.1741 0.2364 0.0130  0.0474  0.0483  22  ASP   A C   
451  C C   B ASP   A 22  ? 0.1862 0.1520 0.2211 -0.0201 0.0772  0.0106  22  ASP   A C   
452  O O   A ASP   A 22  ? 0.2010 0.1824 0.2448 0.0003  0.0431  0.0500  22  ASP   A O   
453  O O   B ASP   A 22  ? 0.1920 0.1492 0.2307 -0.0296 0.0792  0.0028  22  ASP   A O   
454  C CB  A ASP   A 22  ? 0.2264 0.1679 0.2993 0.0280  0.0417  0.0329  22  ASP   A CB  
455  C CB  B ASP   A 22  ? 0.2036 0.1795 0.2612 0.0069  0.0823  0.0028  22  ASP   A CB  
456  C CG  A ASP   A 22  ? 0.2432 0.1728 0.3305 0.0171  0.0279  0.0300  22  ASP   A CG  
457  C CG  B ASP   A 22  ? 0.2076 0.1801 0.2826 0.0167  0.0753  0.0079  22  ASP   A CG  
458  O OD1 A ASP   A 22  ? 0.2419 0.1697 0.3228 -0.0086 0.0060  0.0436  22  ASP   A OD1 
459  O OD1 B ASP   A 22  ? 0.2081 0.1698 0.2682 0.0064  0.0755  0.0102  22  ASP   A OD1 
460  O OD2 A ASP   A 22  ? 0.2548 0.1847 0.3708 0.0425  0.0443  0.0079  22  ASP   A OD2 
461  O OD2 B ASP   A 22  ? 0.2163 0.2018 0.3227 0.0174  0.0623  0.0127  22  ASP   A OD2 
470  N N   A ILE   A 23  ? 0.1769 0.1826 0.2143 0.0112  0.0394  0.0369  23  ILE   A N   
471  N N   B ILE   A 23  ? 0.1806 0.1518 0.2021 -0.0100 0.0593  0.0173  23  ILE   A N   
472  C CA  A ILE   A 23  ? 0.1735 0.1740 0.1999 0.0058  0.0389  0.0342  23  ILE   A CA  
473  C CA  B ILE   A 23  ? 0.1760 0.1687 0.1886 -0.0068 0.0410  0.0261  23  ILE   A CA  
474  C C   A ILE   A 23  ? 0.1778 0.1843 0.1950 0.0017  0.0510  0.0362  23  ILE   A C   
475  C C   B ILE   A 23  ? 0.1850 0.1843 0.1832 -0.0157 0.0475  0.0228  23  ILE   A C   
476  O O   A ILE   A 23  ? 0.1827 0.1977 0.2015 0.0048  0.0304  0.0311  23  ILE   A O   
477  O O   B ILE   A 23  ? 0.1858 0.1793 0.1633 -0.0121 0.0488  0.0206  23  ILE   A O   
478  C CB  A ILE   A 23  ? 0.1862 0.1741 0.1755 0.0021  0.0284  0.0356  23  ILE   A CB  
479  C CB  B ILE   A 23  ? 0.1684 0.1650 0.1744 0.0106  0.0252  0.0329  23  ILE   A CB  
480  C CG1 A ILE   A 23  ? 0.1880 0.1696 0.1714 -0.0021 0.0338  0.0255  23  ILE   A CG1 
481  C CG1 B ILE   A 23  ? 0.1709 0.1661 0.1746 0.0130  0.0120  0.0166  23  ILE   A CG1 
482  C CG2 A ILE   A 23  ? 0.1842 0.1886 0.1728 -0.0029 0.0315  0.0453  23  ILE   A CG2 
483  C CG2 B ILE   A 23  ? 0.1646 0.1589 0.1617 0.0261  0.0256  0.0354  23  ILE   A CG2 
484  C CD1 A ILE   A 23  ? 0.1942 0.1736 0.1684 -0.0099 0.0194  0.0055  23  ILE   A CD1 
485  C CD1 B ILE   A 23  ? 0.1674 0.1638 0.1769 0.0175  -0.0039 0.0111  23  ILE   A CD1 
508  N N   A VAL   A 24  ? 0.1871 0.1894 0.2200 -0.0027 0.0538  0.0173  24  VAL   A N   
509  N N   B VAL   A 24  ? 0.1989 0.2039 0.2108 -0.0236 0.0402  0.0123  24  VAL   A N   
510  C CA  A VAL   A 24  ? 0.2018 0.1946 0.2336 -0.0193 0.0582  0.0090  24  VAL   A CA  
511  C CA  B VAL   A 24  ? 0.2132 0.2154 0.2281 -0.0287 0.0400  0.0166  24  VAL   A CA  
512  C C   A VAL   A 24  ? 0.2061 0.2104 0.2389 -0.0258 0.0501  0.0028  24  VAL   A C   
513  C C   B VAL   A 24  ? 0.2217 0.2337 0.2323 -0.0225 0.0418  0.0143  24  VAL   A C   
514  O O   A VAL   A 24  ? 0.2182 0.2089 0.2551 -0.0251 0.0462  0.0031  24  VAL   A O   
515  O O   B VAL   A 24  ? 0.2259 0.2353 0.2440 -0.0207 0.0415  0.0155  24  VAL   A O   
516  C CB  A VAL   A 24  ? 0.2100 0.1947 0.2699 -0.0267 0.0601  0.0142  24  VAL   A CB  
517  C CB  B VAL   A 24  ? 0.2155 0.2177 0.2570 -0.0373 0.0339  0.0236  24  VAL   A CB  
518  C CG1 A VAL   A 24  ? 0.2184 0.2054 0.2765 -0.0163 0.0650  -0.0001 24  VAL   A CG1 
519  C CG1 B VAL   A 24  ? 0.2258 0.2265 0.2744 -0.0341 0.0317  0.0244  24  VAL   A CG1 
520  C CG2 A VAL   A 24  ? 0.2251 0.2042 0.2823 -0.0258 0.0671  0.0310  24  VAL   A CG2 
521  C CG2 B VAL   A 24  ? 0.2170 0.2142 0.2572 -0.0472 0.0292  0.0240  24  VAL   A CG2 
540  N N   A GLU   A 25  ? 0.2080 0.2393 0.2352 -0.0321 0.0644  -0.0040 25  GLU   A N   
541  N N   B GLU   A 25  ? 0.2280 0.2533 0.2314 -0.0200 0.0563  0.0146  25  GLU   A N   
542  C CA  A GLU   A 25  ? 0.2229 0.2685 0.2425 -0.0183 0.0724  -0.0006 25  GLU   A CA  
543  C CA  B GLU   A 25  ? 0.2398 0.2764 0.2437 -0.0176 0.0571  0.0160  25  GLU   A CA  
544  C C   A GLU   A 25  ? 0.2134 0.2704 0.1982 -0.0297 0.0664  0.0092  25  GLU   A C   
545  C C   B GLU   A 25  ? 0.2320 0.2798 0.2123 -0.0223 0.0588  0.0146  25  GLU   A C   
546  O O   A GLU   A 25  ? 0.2154 0.2847 0.2089 -0.0354 0.0704  0.0100  25  GLU   A O   
547  O O   B GLU   A 25  ? 0.2384 0.2877 0.2259 -0.0231 0.0579  0.0151  25  GLU   A O   
548  C CB  A GLU   A 25  ? 0.2527 0.2983 0.2857 -0.0072 0.0863  0.0111  25  GLU   A CB  
549  C CB  B GLU   A 25  ? 0.2608 0.2954 0.2802 -0.0119 0.0583  0.0215  25  GLU   A CB  
550  C CG  A GLU   A 25  ? 0.2949 0.3298 0.3582 -0.0032 0.0712  0.0076  25  GLU   A CG  
551  C CG  B GLU   A 25  ? 0.2874 0.3147 0.3322 -0.0074 0.0497  0.0202  25  GLU   A CG  
552  C CD  A GLU   A 25  ? 0.3267 0.3592 0.4258 0.0025  0.0520  0.0024  25  GLU   A CD  
553  C CD  B GLU   A 25  ? 0.3077 0.3310 0.3799 -0.0044 0.0346  0.0169  25  GLU   A CD  
554  O OE1 A GLU   A 25  ? 0.3401 0.3730 0.4453 0.0095  0.0417  -0.0093 25  GLU   A OE1 
555  O OE1 B GLU   A 25  ? 0.3178 0.3399 0.4016 -0.0008 0.0234  0.0181  25  GLU   A OE1 
556  O OE2 A GLU   A 25  ? 0.3380 0.3689 0.4600 0.0007  0.0405  -0.0062 25  GLU   A OE2 
557  O OE2 B GLU   A 25  ? 0.3149 0.3320 0.3981 -0.0059 0.0315  0.0098  25  GLU   A OE2 
570  N N   A GLU   A 26  ? 0.2059 0.2543 0.2044 -0.0554 0.0704  0.0058  26  GLU   A N   
571  N N   B GLU   A 26  ? 0.2216 0.2749 0.1924 -0.0335 0.0718  0.0101  26  GLU   A N   
572  C CA  A GLU   A 26  ? 0.2242 0.2459 0.1971 -0.0692 0.0725  0.0017  26  GLU   A CA  
573  C CA  B GLU   A 26  ? 0.2219 0.2708 0.1851 -0.0412 0.0722  0.0033  26  GLU   A CA  
574  C C   A GLU   A 26  ? 0.2267 0.2344 0.1729 -0.0605 0.0511  0.0035  26  GLU   A C   
575  C C   B GLU   A 26  ? 0.2205 0.2494 0.1787 -0.0425 0.0655  -0.0011 26  GLU   A C   
576  O O   A GLU   A 26  ? 0.2365 0.2248 0.1858 -0.0773 0.0400  0.0089  26  GLU   A O   
577  O O   B GLU   A 26  ? 0.2256 0.2472 0.1791 -0.0421 0.0721  -0.0090 26  GLU   A O   
578  C CB  A GLU   A 26  ? 0.2553 0.2475 0.2386 -0.0816 0.0687  0.0100  26  GLU   A CB  
579  C CB  B GLU   A 26  ? 0.2315 0.2876 0.2046 -0.0458 0.0448  -0.0000 26  GLU   A CB  
580  C CG  A GLU   A 26  ? 0.2800 0.2610 0.3033 -0.0844 0.0840  -0.0054 26  GLU   A CG  
581  C CG  B GLU   A 26  ? 0.2420 0.3001 0.2326 -0.0447 0.0262  -0.0054 26  GLU   A CG  
582  C CD  A GLU   A 26  ? 0.2846 0.2618 0.3194 -0.0981 0.1221  -0.0132 26  GLU   A CD  
583  C CD  B GLU   A 26  ? 0.2431 0.3054 0.2342 -0.0483 0.0208  -0.0056 26  GLU   A CD  
584  O OE1 A GLU   A 26  ? 0.2717 0.2780 0.3131 -0.0913 0.1538  -0.0729 26  GLU   A OE1 
585  O OE1 B GLU   A 26  ? 0.2507 0.3119 0.2237 -0.0471 0.0243  -0.0116 26  GLU   A OE1 
586  O OE2 A GLU   A 26  ? 0.3011 0.2694 0.3296 -0.0989 0.1261  0.0046  26  GLU   A OE2 
587  O OE2 B GLU   A 26  ? 0.2369 0.3057 0.2416 -0.0510 0.0092  -0.0063 26  GLU   A OE2 
600  N N   . ALA   A 27  ? 0.2100 0.2304 0.1779 -0.0509 0.0627  0.0002  27  ALA   A N   
601  C CA  . ALA   A 27  ? 0.2109 0.2433 0.1813 -0.0377 0.0613  -0.0024 27  ALA   A CA  
602  C C   . ALA   A 27  ? 0.2438 0.2680 0.1884 -0.0599 0.0635  -0.0123 27  ALA   A C   
603  O O   . ALA   A 27  ? 0.2495 0.2570 0.2000 -0.0733 0.0421  -0.0015 27  ALA   A O   
604  C CB  . ALA   A 27  ? 0.1866 0.2290 0.1899 -0.0358 0.0513  0.0123  27  ALA   A CB  
611  N N   A LYS   A 28  ? 0.2747 0.2865 0.1921 -0.0571 0.0548  -0.0433 28  LYS   A N   
612  N N   B LYS   A 28  ? 0.2766 0.2919 0.2185 -0.0518 0.0490  -0.0231 28  LYS   A N   
613  C CA  A LYS   A 28  ? 0.3142 0.3244 0.2280 -0.0444 0.0576  -0.0643 28  LYS   A CA  
614  C CA  B LYS   A 28  ? 0.3128 0.3250 0.2648 -0.0391 0.0388  -0.0322 28  LYS   A CA  
615  C C   A LYS   A 28  ? 0.3350 0.3602 0.2172 -0.0498 0.0726  -0.0476 28  LYS   A C   
616  C C   B LYS   A 28  ? 0.3349 0.3498 0.2743 -0.0369 0.0367  -0.0263 28  LYS   A C   
617  O O   A LYS   A 28  ? 0.3475 0.3727 0.2596 -0.0457 0.0518  -0.0462 28  LYS   A O   
618  O O   B LYS   A 28  ? 0.3426 0.3567 0.2884 -0.0352 0.0301  -0.0265 28  LYS   A O   
619  C CB  A LYS   A 28  ? 0.3384 0.3372 0.2951 -0.0296 0.0493  -0.0736 28  LYS   A CB  
620  C CB  B LYS   A 28  ? 0.3299 0.3368 0.3080 -0.0313 0.0324  -0.0377 28  LYS   A CB  
621  C CG  A LYS   A 28  ? 0.3582 0.3494 0.3506 -0.0172 0.0450  -0.0755 28  LYS   A CG  
622  C CG  B LYS   A 28  ? 0.3454 0.3478 0.3480 -0.0240 0.0282  -0.0400 28  LYS   A CG  
623  C CD  A LYS   A 28  ? 0.3774 0.3701 0.4119 -0.0058 0.0356  -0.0770 28  LYS   A CD  
624  C CD  B LYS   A 28  ? 0.3603 0.3630 0.3929 -0.0164 0.0228  -0.0418 28  LYS   A CD  
625  C CE  A LYS   A 28  ? 0.3893 0.3840 0.4527 -0.0006 0.0284  -0.0803 28  LYS   A CE  
626  C CE  B LYS   A 28  ? 0.3706 0.3733 0.4240 -0.0133 0.0186  -0.0444 28  LYS   A CE  
627  N NZ  A LYS   A 28  ? 0.3965 0.3915 0.4809 0.0069  0.0268  -0.0828 28  LYS   A NZ  
628  N NZ  B LYS   A 28  ? 0.3767 0.3787 0.4445 -0.0085 0.0165  -0.0472 28  LYS   A NZ  
655  N N   A LYS   A 29  ? 0.3429 0.3865 0.2047 -0.0632 0.1062  -0.0125 29  LYS   A N   
656  N N   B LYS   A 29  ? 0.3481 0.3681 0.2858 -0.0380 0.0425  -0.0127 29  LYS   A N   
657  C CA  A LYS   A 29  ? 0.3585 0.4153 0.2351 -0.0702 0.1209  0.0042  29  LYS   A CA  
658  C CA  B LYS   A 29  ? 0.3622 0.3862 0.3055 -0.0382 0.0440  -0.0042 29  LYS   A CA  
659  C C   A LYS   A 29  ? 0.3562 0.4082 0.2267 -0.0844 0.1021  0.0162  29  LYS   A C   
660  C C   B LYS   A 29  ? 0.3592 0.3797 0.2769 -0.0433 0.0334  0.0041  29  LYS   A C   
661  O O   A LYS   A 29  ? 0.3715 0.4218 0.2523 -0.0757 0.0999  0.0191  29  LYS   A O   
662  O O   B LYS   A 29  ? 0.3629 0.3849 0.2743 -0.0429 0.0358  0.0087  29  LYS   A O   
663  C CB  A LYS   A 29  ? 0.3747 0.4480 0.2996 -0.0612 0.1358  0.0024  29  LYS   A CB  
664  C CB  B LYS   A 29  ? 0.3777 0.4081 0.3605 -0.0324 0.0512  -0.0049 29  LYS   A CB  
665  C CG  A LYS   A 29  ? 0.3935 0.4744 0.3793 -0.0512 0.1325  0.0017  29  LYS   A CG  
666  C CG  B LYS   A 29  ? 0.3936 0.4269 0.4163 -0.0267 0.0534  -0.0053 29  LYS   A CG  
667  C CD  A LYS   A 29  ? 0.4102 0.4974 0.4560 -0.0431 0.1247  -0.0017 29  LYS   A CD  
668  C CD  B LYS   A 29  ? 0.4068 0.4425 0.4678 -0.0221 0.0539  -0.0051 29  LYS   A CD  
669  C CE  A LYS   A 29  ? 0.4221 0.5126 0.5033 -0.0380 0.1220  -0.0044 29  LYS   A CE  
670  C CE  B LYS   A 29  ? 0.4159 0.4533 0.5017 -0.0192 0.0553  -0.0060 29  LYS   A CE  
671  N NZ  A LYS   A 29  ? 0.4273 0.5206 0.5313 -0.0340 0.1181  -0.0075 29  LYS   A NZ  
672  N NZ  B LYS   A 29  ? 0.4207 0.4594 0.5205 -0.0171 0.0541  -0.0064 29  LYS   A NZ  
699  N N   A VAL   A 30  ? 0.3350 0.3838 0.1916 -0.1045 0.0990  0.0269  30  VAL   A N   
700  N N   B VAL   A 30  ? 0.3519 0.3664 0.2550 -0.0490 0.0262  0.0081  30  VAL   A N   
701  C CA  A VAL   A 30  ? 0.3217 0.3623 0.1932 -0.1154 0.0613  0.0313  30  VAL   A CA  
702  C CA  B VAL   A 30  ? 0.3449 0.3534 0.2446 -0.0541 0.0114  0.0132  30  VAL   A CA  
703  C C   A VAL   A 30  ? 0.3159 0.3402 0.1510 -0.1105 0.0432  0.0379  30  VAL   A C   
704  C C   B VAL   A 30  ? 0.3403 0.3430 0.2259 -0.0542 0.0037  0.0124  30  VAL   A C   
705  O O   A VAL   A 30  ? 0.3239 0.3405 0.1730 -0.1095 0.0345  0.0445  30  VAL   A O   
706  O O   B VAL   A 30  ? 0.3419 0.3433 0.2291 -0.0526 -0.0016 0.0131  30  VAL   A O   
707  C CB  A VAL   A 30  ? 0.3182 0.3606 0.2421 -0.1286 0.0409  0.0276  30  VAL   A CB  
708  C CB  B VAL   A 30  ? 0.3432 0.3511 0.2590 -0.0587 0.0055  0.0153  30  VAL   A CB  
709  C CG1 A VAL   A 30  ? 0.3260 0.3608 0.2583 -0.1283 0.0287  0.0297  30  VAL   A CG1 
710  C CG1 B VAL   A 30  ? 0.3464 0.3504 0.2655 -0.0589 0.0016  0.0172  30  VAL   A CG1 
711  C CG2 A VAL   A 30  ? 0.3142 0.3603 0.2734 -0.1395 0.0418  0.0277  30  VAL   A CG2 
712  C CG2 B VAL   A 30  ? 0.3418 0.3511 0.2729 -0.0626 0.0068  0.0185  30  VAL   A CG2 
731  N N   A LYS   A 31  ? 0.3017 0.3179 0.1360 -0.1099 0.0254  0.0348  31  LYS   A N   
732  N N   B LYS   A 31  ? 0.3329 0.3317 0.2201 -0.0582 0.0003  0.0128  31  LYS   A N   
733  C CA  A LYS   A 31  ? 0.3140 0.3185 0.1488 -0.0947 -0.0030 0.0363  31  LYS   A CA  
734  C CA  B LYS   A 31  ? 0.3311 0.3265 0.2264 -0.0588 -0.0063 0.0187  31  LYS   A CA  
735  C C   A LYS   A 31  ? 0.2892 0.2887 0.1162 -0.0671 -0.0136 0.0657  31  LYS   A C   
736  C C   B LYS   A 31  ? 0.3052 0.3017 0.1695 -0.0625 -0.0072 0.0430  31  LYS   A C   
737  O O   A LYS   A 31  ? 0.3022 0.3003 0.1371 -0.0721 -0.0280 0.0819  31  LYS   A O   
738  O O   B LYS   A 31  ? 0.3119 0.3070 0.1861 -0.0608 -0.0137 0.0501  31  LYS   A O   
739  C CB  A LYS   A 31  ? 0.3436 0.3442 0.2682 -0.0874 -0.0154 0.0079  31  LYS   A CB  
740  C CB  B LYS   A 31  ? 0.3551 0.3474 0.3081 -0.0551 -0.0105 0.0032  31  LYS   A CB  
741  C CG  A LYS   A 31  ? 0.3791 0.3737 0.4003 -0.0762 -0.0258 -0.0112 31  LYS   A CG  
742  C CG  B LYS   A 31  ? 0.3781 0.3656 0.3954 -0.0485 -0.0150 -0.0079 31  LYS   A CG  
743  C CD  A LYS   A 31  ? 0.4103 0.4015 0.4983 -0.0654 -0.0350 -0.0290 31  LYS   A CD  
744  C CD  B LYS   A 31  ? 0.3972 0.3812 0.4657 -0.0419 -0.0203 -0.0176 31  LYS   A CD  
745  C CE  A LYS   A 31  ? 0.4294 0.4201 0.5604 -0.0564 -0.0445 -0.0431 31  LYS   A CE  
746  C CE  B LYS   A 31  ? 0.4098 0.3936 0.5117 -0.0365 -0.0255 -0.0245 31  LYS   A CE  
747  N NZ  A LYS   A 31  ? 0.4386 0.4225 0.5942 -0.0500 -0.0505 -0.0499 31  LYS   A NZ  
748  N NZ  B LYS   A 31  ? 0.4176 0.3984 0.5383 -0.0324 -0.0278 -0.0279 31  LYS   A NZ  
775  N N   . PRO   A 32  ? 0.2726 0.2730 0.1220 -0.0731 0.0042  0.0486  32  PRO   A N   
776  C CA  . PRO   A 32  ? 0.2582 0.2487 0.1701 -0.0640 -0.0123 0.0591  32  PRO   A CA  
777  C C   . PRO   A 32  ? 0.2447 0.2489 0.1731 -0.0516 -0.0139 0.0615  32  PRO   A C   
778  O O   . PRO   A 32  ? 0.2360 0.2424 0.1927 -0.0474 -0.0226 0.0482  32  PRO   A O   
779  C CB  . PRO   A 32  ? 0.2526 0.2501 0.1792 -0.0613 -0.0173 0.0424  32  PRO   A CB  
780  C CG  . PRO   A 32  ? 0.2539 0.2568 0.1373 -0.0557 -0.0200 0.0222  32  PRO   A CG  
781  C CD  . PRO   A 32  ? 0.2559 0.2644 0.1112 -0.0655 -0.0104 0.0327  32  PRO   A CD  
789  N N   . THR   A 33  ? 0.2537 0.2551 0.1624 -0.0458 -0.0112 0.0619  33  THR   A N   
790  C CA  . THR   A 33  ? 0.2572 0.2594 0.1631 -0.0303 -0.0302 0.0607  33  THR   A CA  
791  C C   . THR   A 33  ? 0.2257 0.2350 0.1555 -0.0370 -0.0335 0.0505  33  THR   A C   
792  O O   . THR   A 33  ? 0.2131 0.2330 0.1764 -0.0456 -0.0407 0.0588  33  THR   A O   
793  C CB  . THR   A 33  ? 0.2819 0.2814 0.1792 -0.0201 -0.0356 0.0798  33  THR   A CB  
794  O OG1 . THR   A 33  ? 0.3125 0.3026 0.2056 -0.0135 -0.0272 0.0973  33  THR   A OG1 
795  C CG2 . THR   A 33  ? 0.2809 0.2885 0.2058 -0.0120 -0.0416 0.0760  33  THR   A CG2 
803  N N   . VAL   A 34  ? 0.2003 0.2179 0.1357 -0.0366 -0.0176 0.0454  34  VAL   A N   
804  C CA  . VAL   A 34  ? 0.1851 0.1981 0.1201 -0.0250 -0.0148 0.0380  34  VAL   A CA  
805  C C   . VAL   A 34  ? 0.1762 0.1836 0.1290 -0.0285 -0.0048 0.0403  34  VAL   A C   
806  O O   . VAL   A 34  ? 0.1794 0.1828 0.1562 -0.0370 0.0055  0.0339  34  VAL   A O   
807  C CB  . VAL   A 34  ? 0.1825 0.1943 0.1536 -0.0273 -0.0006 0.0253  34  VAL   A CB  
808  C CG1 . VAL   A 34  ? 0.1927 0.1943 0.1551 -0.0259 0.0020  0.0194  34  VAL   A CG1 
809  C CG2 . VAL   A 34  ? 0.1905 0.2116 0.1812 -0.0171 -0.0082 0.0208  34  VAL   A CG2 
819  N N   . VAL   A 35  ? 0.1681 0.1720 0.1126 -0.0309 -0.0093 0.0308  35  VAL   A N   
820  C CA  . VAL   A 35  ? 0.1604 0.1687 0.0990 -0.0332 -0.0097 0.0240  35  VAL   A CA  
821  C C   . VAL   A 35  ? 0.1558 0.1560 0.0854 -0.0202 -0.0124 0.0246  35  VAL   A C   
822  O O   . VAL   A 35  ? 0.1429 0.1611 0.1532 -0.0267 0.0149  0.0191  35  VAL   A O   
823  C CB  . VAL   A 35  ? 0.1577 0.1725 0.1549 -0.0172 0.0101  0.0128  35  VAL   A CB  
824  C CG1 . VAL   A 35  ? 0.1693 0.1692 0.1502 -0.0111 0.0047  0.0203  35  VAL   A CG1 
825  C CG2 . VAL   A 35  ? 0.1553 0.1756 0.1857 -0.0139 0.0149  0.0086  35  VAL   A CG2 
835  N N   . VAL   A 36  ? 0.1426 0.1499 0.0810 -0.0160 -0.0033 0.0239  36  VAL   A N   
836  C CA  . VAL   A 36  ? 0.1392 0.1377 0.1070 -0.0052 -0.0060 0.0025  36  VAL   A CA  
837  C C   . VAL   A 36  ? 0.1380 0.1388 0.1341 -0.0122 0.0131  0.0175  36  VAL   A C   
838  O O   . VAL   A 36  ? 0.1344 0.1368 0.1551 -0.0075 0.0232  0.0177  36  VAL   A O   
839  C CB  . VAL   A 36  ? 0.1358 0.1312 0.1235 -0.0045 -0.0013 0.0173  36  VAL   A CB  
840  C CG1 . VAL   A 36  ? 0.1360 0.1407 0.1471 -0.0127 0.0062  0.0144  36  VAL   A CG1 
841  C CG2 . VAL   A 36  ? 0.1454 0.1443 0.1499 -0.0163 0.0016  0.0231  36  VAL   A CG2 
851  N N   . ASN   A 37  ? 0.1368 0.1341 0.1075 -0.0043 0.0065  0.0143  37  ASN   A N   
852  C CA  . ASN   A 37  ? 0.1301 0.1361 0.1071 0.0027  0.0050  0.0268  37  ASN   A CA  
853  C C   . ASN   A 37  ? 0.1277 0.1255 0.1130 -0.0052 0.0136  0.0332  37  ASN   A C   
854  O O   . ASN   A 37  ? 0.1363 0.1348 0.1249 0.0010  0.0124  0.0083  37  ASN   A O   
855  C CB  . ASN   A 37  ? 0.1333 0.1304 0.1249 0.0004  0.0061  0.0254  37  ASN   A CB  
856  C CG  . ASN   A 37  ? 0.1354 0.1218 0.1441 0.0003  0.0122  0.0158  37  ASN   A CG  
857  O OD1 . ASN   A 37  ? 0.1268 0.1301 0.1706 0.0022  0.0096  0.0231  37  ASN   A OD1 
858  N ND2 . ASN   A 37  ? 0.1394 0.1258 0.1406 -0.0029 0.0135  0.0258  37  ASN   A ND2 
865  N N   A ALA   A 38  ? 0.1350 0.1390 0.1164 -0.0031 0.0098  0.0184  38  ALA   A N   
866  N N   B ALA   A 38  ? 0.1318 0.1349 0.1225 -0.0065 0.0013  0.0286  38  ALA   A N   
867  C CA  A ALA   A 38  ? 0.1372 0.1460 0.1068 -0.0059 0.0051  0.0091  38  ALA   A CA  
868  C CA  B ALA   A 38  ? 0.1330 0.1430 0.1349 -0.0107 -0.0087 0.0299  38  ALA   A CA  
869  C C   A ALA   A 38  ? 0.1325 0.1444 0.1217 0.0030  -0.0026 -0.0001 38  ALA   A C   
870  C C   B ALA   A 38  ? 0.1270 0.1428 0.1451 -0.0059 -0.0138 0.0188  38  ALA   A C   
871  O O   A ALA   A 38  ? 0.1242 0.1318 0.1374 -0.0033 -0.0001 0.0028  38  ALA   A O   
872  O O   B ALA   A 38  ? 0.1108 0.1392 0.1637 -0.0031 -0.0235 0.0162  38  ALA   A O   
873  C CB  A ALA   A 38  ? 0.1334 0.1606 0.1227 -0.0211 0.0017  0.0065  38  ALA   A CB  
874  C CB  B ALA   A 38  ? 0.1343 0.1476 0.1580 -0.0147 -0.0187 0.0215  38  ALA   A CB  
885  N N   A ALA   A 39  ? 0.1238 0.1359 0.1262 0.0065  -0.0016 0.0099  39  ALA   A N   
886  N N   B ALA   A 39  ? 0.1329 0.1398 0.1497 -0.0103 0.0075  0.0302  39  ALA   A N   
887  C CA  A ALA   A 39  ? 0.1196 0.1217 0.1306 0.0092  0.0021  0.0163  39  ALA   A CA  
888  C CA  B ALA   A 39  ? 0.1319 0.1320 0.1351 -0.0094 -0.0065 0.0268  39  ALA   A CA  
889  C C   A ALA   A 39  ? 0.1224 0.1305 0.1184 0.0014  -0.0059 0.0086  39  ALA   A C   
890  C C   B ALA   A 39  ? 0.1279 0.1270 0.1457 -0.0084 0.0047  0.0294  39  ALA   A C   
891  O O   A ALA   A 39  ? 0.1465 0.1371 0.1340 -0.0109 0.0008  -0.0019 39  ALA   A O   
892  O O   B ALA   A 39  ? 0.1415 0.1266 0.1533 -0.0126 0.0155  0.0222  39  ALA   A O   
893  C CB  A ALA   A 39  ? 0.1226 0.1211 0.1454 0.0127  -0.0044 0.0107  39  ALA   A CB  
894  C CB  B ALA   A 39  ? 0.1475 0.1373 0.1303 0.0014  -0.0187 0.0193  39  ALA   A CB  
905  N N   A ASN   A 40  ? 0.1330 0.1354 0.1246 -0.0063 0.0128  0.0069  40  ASN   A N   
906  N N   B ASN   A 40  ? 0.1269 0.1230 0.1452 -0.0038 0.0050  0.0325  40  ASN   A N   
907  C CA  A ASN   A 40  ? 0.1425 0.1397 0.1301 0.0008  0.0075  0.0050  40  ASN   A CA  
908  C CA  B ASN   A 40  ? 0.1352 0.1217 0.1461 0.0072  -0.0068 0.0353  40  ASN   A CA  
909  C C   A ASN   A 40  ? 0.1375 0.1375 0.1131 0.0029  0.0221  0.0075  40  ASN   A C   
910  C C   B ASN   A 40  ? 0.1390 0.1258 0.1585 0.0039  0.0051  0.0364  40  ASN   A C   
911  O O   A ASN   A 40  ? 0.1284 0.1368 0.1311 -0.0062 0.0244  0.0066  40  ASN   A O   
912  O O   B ASN   A 40  ? 0.1286 0.1228 0.1737 -0.0060 -0.0098 0.0469  40  ASN   A O   
913  C CB  A ASN   A 40  ? 0.1549 0.1518 0.1589 -0.0041 0.0063  0.0053  40  ASN   A CB  
914  C CB  B ASN   A 40  ? 0.1395 0.1264 0.1493 0.0064  0.0019  0.0240  40  ASN   A CB  
915  C CG  A ASN   A 40  ? 0.1617 0.1522 0.1986 -0.0018 0.0047  0.0062  40  ASN   A CG  
916  C CG  B ASN   A 40  ? 0.1432 0.1253 0.1615 0.0050  0.0071  0.0181  40  ASN   A CG  
917  O OD1 A ASN   A 40  ? 0.1631 0.1495 0.2014 -0.0021 -0.0035 0.0114  40  ASN   A OD1 
918  O OD1 B ASN   A 40  ? 0.1460 0.1269 0.1605 0.0028  0.0134  0.0139  40  ASN   A OD1 
919  N ND2 A ASN   A 40  ? 0.1720 0.1623 0.2224 0.0004  0.0033  -0.0116 40  ASN   A ND2 
920  N ND2 B ASN   A 40  ? 0.1492 0.1324 0.1866 0.0052  0.0064  -0.0009 40  ASN   A ND2 
933  N N   A VAL   A 41  ? 0.1418 0.1338 0.1176 0.0071  0.0263  0.0086  41  VAL   A N   
934  N N   B VAL   A 41  ? 0.1475 0.1279 0.1505 0.0036  0.0151  0.0343  41  VAL   A N   
935  C CA  A VAL   A 41  ? 0.1476 0.1424 0.1361 0.0087  0.0335  0.0172  41  VAL   A CA  
936  C CA  B VAL   A 41  ? 0.1517 0.1356 0.1459 -0.0002 0.0274  0.0314  41  VAL   A CA  
937  C C   A VAL   A 41  ? 0.1504 0.1460 0.1397 0.0091  0.0243  0.0162  41  VAL   A C   
938  C C   B VAL   A 41  ? 0.1513 0.1295 0.1460 -0.0011 0.0201  0.0293  41  VAL   A C   
939  O O   A VAL   A 41  ? 0.1498 0.1454 0.1641 0.0037  0.0321  0.0031  41  VAL   A O   
940  O O   B VAL   A 41  ? 0.1502 0.1166 0.1652 -0.0107 0.0164  0.0336  41  VAL   A O   
941  C CB  A VAL   A 41  ? 0.1614 0.1525 0.1438 -0.0027 0.0370  0.0081  41  VAL   A CB  
942  C CB  B VAL   A 41  ? 0.1576 0.1502 0.1545 -0.0075 0.0436  0.0293  41  VAL   A CB  
943  C CG1 A VAL   A 41  ? 0.1696 0.1610 0.1590 0.0016  0.0317  0.0047  41  VAL   A CG1 
944  C CG1 B VAL   A 41  ? 0.1673 0.1580 0.1732 -0.0079 0.0521  0.0187  41  VAL   A CG1 
945  C CG2 A VAL   A 41  ? 0.1908 0.1621 0.1284 -0.0141 0.0377  0.0030  41  VAL   A CG2 
946  C CG2 B VAL   A 41  ? 0.1750 0.1594 0.1507 -0.0164 0.0383  0.0234  41  VAL   A CG2 
965  N N   A TYR   A 42  ? 0.1360 0.1364 0.1552 0.0009  0.0276  0.0237  42  TYR   A N   
966  N N   B TYR   A 42  ? 0.1465 0.1316 0.1469 0.0068  0.0258  0.0272  42  TYR   A N   
967  C CA  A TYR   A 42  ? 0.1406 0.1289 0.1587 -0.0081 0.0330  0.0351  42  TYR   A CA  
968  C CA  B TYR   A 42  ? 0.1457 0.1319 0.1497 0.0075  0.0209  0.0332  42  TYR   A CA  
969  C C   A TYR   A 42  ? 0.1359 0.1244 0.1472 -0.0066 0.0303  0.0334  42  TYR   A C   
970  C C   B TYR   A 42  ? 0.1393 0.1287 0.1451 0.0042  0.0207  0.0288  42  TYR   A C   
971  O O   A TYR   A 42  ? 0.1330 0.1274 0.1885 -0.0197 0.0292  0.0019  42  TYR   A O   
972  O O   B TYR   A 42  ? 0.1368 0.1353 0.1692 0.0008  0.0155  0.0091  42  TYR   A O   
973  C CB  A TYR   A 42  ? 0.1653 0.1474 0.1645 -0.0038 0.0447  0.0358  42  TYR   A CB  
974  C CB  B TYR   A 42  ? 0.1625 0.1449 0.1578 0.0122  0.0166  0.0355  42  TYR   A CB  
975  C CG  A TYR   A 42  ? 0.1776 0.1506 0.1577 -0.0052 0.0502  0.0274  42  TYR   A CG  
976  C CG  B TYR   A 42  ? 0.1717 0.1518 0.1580 0.0168  0.0143  0.0334  42  TYR   A CG  
977  C CD1 A TYR   A 42  ? 0.1805 0.1574 0.1682 -0.0088 0.0467  0.0342  42  TYR   A CD1 
978  C CD1 B TYR   A 42  ? 0.1722 0.1543 0.1643 0.0082  0.0186  0.0411  42  TYR   A CD1 
979  C CD2 A TYR   A 42  ? 0.1920 0.1760 0.1873 0.0003  0.0489  0.0246  42  TYR   A CD2 
980  C CD2 B TYR   A 42  ? 0.1768 0.1660 0.1684 0.0192  0.0191  0.0321  42  TYR   A CD2 
981  C CE1 A TYR   A 42  ? 0.1838 0.1654 0.1690 -0.0099 0.0421  0.0149  42  TYR   A CE1 
982  C CE1 B TYR   A 42  ? 0.1698 0.1646 0.1633 0.0045  0.0213  0.0324  42  TYR   A CE1 
983  C CE2 A TYR   A 42  ? 0.1957 0.1826 0.1929 -0.0072 0.0520  0.0257  42  TYR   A CE2 
984  C CE2 B TYR   A 42  ? 0.1804 0.1759 0.1702 0.0192  0.0242  0.0310  42  TYR   A CE2 
985  C CZ  A TYR   A 42  ? 0.1964 0.1823 0.1717 -0.0128 0.0571  0.0249  42  TYR   A CZ  
986  C CZ  B TYR   A 42  ? 0.1745 0.1781 0.1590 0.0123  0.0237  0.0265  42  TYR   A CZ  
987  O OH  A TYR   A 42  ? 0.1997 0.1852 0.2120 -0.0220 0.0440  0.0096  42  TYR   A OH  
988  O OH  B TYR   A 42  ? 0.1672 0.1908 0.1680 0.0079  0.0303  0.0196  42  TYR   A OH  
1007 N N   . LEU   A 43  ? 0.1387 0.1285 0.1420 -0.0073 0.0227  0.0194  43  LEU   A N   
1008 C CA  . LEU   A 43  ? 0.1290 0.1303 0.1328 -0.0077 0.0122  0.0165  43  LEU   A CA  
1009 C C   . LEU   A 43  ? 0.1343 0.1297 0.1362 -0.0001 0.0130  0.0134  43  LEU   A C   
1010 O O   . LEU   A 43  ? 0.1495 0.1384 0.1752 0.0078  0.0021  0.0058  43  LEU   A O   
1011 C CB  . LEU   A 43  ? 0.1405 0.1343 0.1750 -0.0079 0.0090  0.0221  43  LEU   A CB  
1012 C CG  . LEU   A 43  ? 0.1403 0.1292 0.1835 -0.0008 -0.0019 0.0186  43  LEU   A CG  
1013 C CD1 . LEU   A 43  ? 0.1489 0.1305 0.2002 -0.0006 -0.0002 0.0159  43  LEU   A CD1 
1014 C CD2 . LEU   A 43  ? 0.1496 0.1310 0.1642 -0.0032 0.0055  0.0225  43  LEU   A CD2 
1027 N N   A LYS   A 44  ? 0.1332 0.1275 0.1505 0.0012  0.0163  0.0143  44  LYS   A N   
1028 N N   B LYS   A 44  ? 0.1430 0.1426 0.1567 -0.0046 0.0095  0.0115  44  LYS   A N   
1029 C CA  A LYS   A 44  ? 0.1432 0.1269 0.1413 0.0037  0.0236  0.0190  44  LYS   A CA  
1030 C CA  B LYS   A 44  ? 0.1575 0.1557 0.1694 -0.0084 0.0089  0.0124  44  LYS   A CA  
1031 C C   A LYS   A 44  ? 0.1305 0.1265 0.1211 0.0060  0.0087  0.0105  44  LYS   A C   
1032 C C   B LYS   A 44  ? 0.1527 0.1555 0.1547 -0.0033 -0.0016 0.0067  44  LYS   A C   
1033 O O   A LYS   A 44  ? 0.1451 0.1450 0.1510 0.0029  0.0087  -0.0029 44  LYS   A O   
1034 O O   B LYS   A 44  ? 0.1579 0.1620 0.1636 -0.0057 0.0015  0.0041  44  LYS   A O   
1035 C CB  A LYS   A 44  ? 0.1756 0.1503 0.1745 0.0073  0.0292  0.0252  44  LYS   A CB  
1036 C CB  B LYS   A 44  ? 0.1792 0.1780 0.1987 -0.0150 0.0141  0.0160  44  LYS   A CB  
1037 C CG  A LYS   A 44  ? 0.2083 0.1906 0.2340 0.0007  0.0493  0.0272  44  LYS   A CG  
1038 C CG  B LYS   A 44  ? 0.2013 0.1989 0.2397 -0.0214 0.0243  0.0156  44  LYS   A CG  
1039 C CD  A LYS   A 44  ? 0.2400 0.2467 0.3012 -0.0054 0.0503  0.0314  44  LYS   A CD  
1040 C CD  B LYS   A 44  ? 0.2253 0.2289 0.2916 -0.0256 0.0239  0.0205  44  LYS   A CD  
1041 C CE  A LYS   A 44  ? 0.2565 0.2788 0.3404 -0.0084 0.0496  0.0298  44  LYS   A CE  
1042 C CE  B LYS   A 44  ? 0.2407 0.2526 0.3274 -0.0310 0.0219  0.0244  44  LYS   A CE  
1043 N NZ  A LYS   A 44  ? 0.2655 0.2991 0.3579 -0.0100 0.0446  0.0215  44  LYS   A NZ  
1044 N NZ  B LYS   A 44  ? 0.2516 0.2710 0.3428 -0.0367 0.0203  0.0306  44  LYS   A NZ  
1071 N N   A HIS   A 45  ? 0.1233 0.1251 0.1268 -0.0000 0.0097  0.0179  45  HIS   A N   
1072 N N   B HIS   A 45  ? 0.1499 0.1544 0.1538 -0.0007 -0.0103 0.0100  45  HIS   A N   
1073 C CA  A HIS   A 45  ? 0.1254 0.1197 0.1433 -0.0029 0.0200  0.0204  45  HIS   A CA  
1074 C CA  B HIS   A 45  ? 0.1471 0.1519 0.1591 0.0064  -0.0111 0.0061  45  HIS   A CA  
1075 C C   A HIS   A 45  ? 0.1289 0.1390 0.1462 0.0036  0.0225  0.0246  45  HIS   A C   
1076 C C   B HIS   A 45  ? 0.1520 0.1532 0.1740 0.0072  -0.0063 0.0050  45  HIS   A C   
1077 O O   A HIS   A 45  ? 0.1286 0.1354 0.1644 0.0075  0.0191  0.0159  45  HIS   A O   
1078 O O   B HIS   A 45  ? 0.1584 0.1546 0.1924 0.0165  -0.0005 0.0088  45  HIS   A O   
1079 C CB  A HIS   A 45  ? 0.1300 0.1148 0.1442 -0.0134 0.0228  0.0149  45  HIS   A CB  
1080 C CB  B HIS   A 45  ? 0.1424 0.1531 0.1424 0.0173  -0.0198 -0.0039 45  HIS   A CB  
1081 C CG  A HIS   A 45  ? 0.1306 0.1123 0.1447 -0.0108 0.0210  0.0109  45  HIS   A CG  
1082 C CG  B HIS   A 45  ? 0.1315 0.1548 0.1135 0.0237  -0.0182 -0.0089 45  HIS   A CG  
1083 N ND1 A HIS   A 45  ? 0.1288 0.1193 0.1576 -0.0194 0.0248  0.0194  45  HIS   A ND1 
1084 N ND1 B HIS   A 45  ? 0.1251 0.1629 0.1258 0.0264  -0.0343 0.0029  45  HIS   A ND1 
1085 C CD2 A HIS   A 45  ? 0.1261 0.1206 0.1618 -0.0065 0.0254  0.0270  45  HIS   A CD2 
1086 C CD2 B HIS   A 45  ? 0.1250 0.1548 0.0896 0.0243  -0.0222 -0.0151 45  HIS   A CD2 
1087 C CE1 A HIS   A 45  ? 0.1323 0.1270 0.1726 -0.0133 0.0312  0.0282  45  HIS   A CE1 
1088 C CE1 B HIS   A 45  ? 0.1160 0.1581 0.0956 0.0278  -0.0461 -0.0058 45  HIS   A CE1 
1089 N NE2 A HIS   A 45  ? 0.1360 0.1238 0.1768 -0.0013 0.0337  0.0424  45  HIS   A NE2 
1090 N NE2 B HIS   A 45  ? 0.1129 0.1540 0.0768 0.0224  -0.0465 -0.0079 45  HIS   A NE2 
1105 N N   A GLY   A 46  ? 0.1379 0.1541 0.1791 0.0123  -0.0026 0.0459  46  GLY   A N   
1106 N N   B GLY   A 46  ? 0.1515 0.1474 0.1854 -0.0003 -0.0117 0.0069  46  GLY   A N   
1107 C CA  A GLY   A 46  ? 0.1440 0.1601 0.1995 0.0106  0.0033  0.0535  46  GLY   A CA  
1108 C CA  B GLY   A 46  ? 0.1408 0.1458 0.1721 -0.0059 -0.0088 0.0058  46  GLY   A CA  
1109 C C   A GLY   A 46  ? 0.1411 0.1630 0.1988 0.0260  0.0018  0.0610  46  GLY   A C   
1110 C C   B GLY   A 46  ? 0.1364 0.1392 0.1586 -0.0017 0.0104  0.0040  46  GLY   A C   
1111 O O   A GLY   A 46  ? 0.1488 0.1666 0.2140 0.0238  -0.0099 0.0575  46  GLY   A O   
1112 O O   B GLY   A 46  ? 0.1443 0.1420 0.1489 -0.0032 -0.0071 -0.0007 46  GLY   A O   
1119 N N   A GLY   A 47  ? 0.1366 0.1619 0.1857 0.0242  -0.0062 0.0441  47  GLY   A N   
1120 N N   B GLY   A 47  ? 0.1437 0.1360 0.1521 0.0003  0.0229  -0.0112 47  GLY   A N   
1121 C CA  A GLY   A 47  ? 0.1427 0.1713 0.1782 0.0179  -0.0104 0.0326  47  GLY   A CA  
1122 C CA  B GLY   A 47  ? 0.1439 0.1461 0.1574 -0.0045 0.0156  -0.0116 47  GLY   A CA  
1123 C C   A GLY   A 47  ? 0.1403 0.1594 0.1620 0.0157  -0.0145 0.0347  47  GLY   A C   
1124 C C   B GLY   A 47  ? 0.1373 0.1362 0.1283 0.0011  0.0239  -0.0189 47  GLY   A C   
1125 O O   A GLY   A 47  ? 0.1378 0.1495 0.1819 0.0186  -0.0257 0.0339  47  GLY   A O   
1126 O O   B GLY   A 47  ? 0.1250 0.1301 0.1133 0.0039  0.0186  -0.0028 47  GLY   A O   
1133 N N   A GLY   A 48  ? 0.1410 0.1650 0.1489 0.0172  -0.0106 0.0283  48  GLY   A N   
1134 N N   B GLY   A 48  ? 0.1428 0.1393 0.1174 0.0006  0.0339  -0.0119 48  GLY   A N   
1135 C CA  A GLY   A 48  ? 0.1358 0.1577 0.1384 0.0115  -0.0140 0.0110  48  GLY   A CA  
1136 C CA  B GLY   A 48  ? 0.1420 0.1312 0.1117 -0.0013 0.0339  -0.0100 48  GLY   A CA  
1137 C C   A GLY   A 48  ? 0.1378 0.1527 0.1207 0.0094  -0.0045 0.0003  48  GLY   A C   
1138 C C   B GLY   A 48  ? 0.1451 0.1346 0.1156 0.0032  0.0242  0.0009  48  GLY   A C   
1139 O O   A GLY   A 48  ? 0.1428 0.1390 0.1349 0.0116  0.0069  0.0109  48  GLY   A O   
1140 O O   B GLY   A 48  ? 0.1529 0.1397 0.1094 0.0010  0.0178  -0.0021 48  GLY   A O   
1147 N N   A VAL   A 49  ? 0.1392 0.1444 0.1411 -0.0050 -0.0166 0.0072  49  VAL   A N   
1148 N N   B VAL   A 49  ? 0.1378 0.1295 0.1183 0.0057  0.0151  -0.0017 49  VAL   A N   
1149 C CA  A VAL   A 49  ? 0.1407 0.1370 0.1496 -0.0157 -0.0139 0.0213  49  VAL   A CA  
1150 C CA  B VAL   A 49  ? 0.1341 0.1371 0.1142 -0.0044 0.0116  -0.0030 49  VAL   A CA  
1151 C C   A VAL   A 49  ? 0.1337 0.1313 0.1367 -0.0152 -0.0092 0.0261  49  VAL   A C   
1152 C C   B VAL   A 49  ? 0.1376 0.1360 0.0734 0.0043  0.0213  -0.0298 49  VAL   A C   
1153 O O   A VAL   A 49  ? 0.1348 0.1380 0.1470 -0.0154 -0.0282 0.0204  49  VAL   A O   
1154 O O   B VAL   A 49  ? 0.1362 0.1400 0.0595 0.0139  0.0367  -0.0178 49  VAL   A O   
1155 C CB  A VAL   A 49  ? 0.1512 0.1349 0.1952 -0.0086 -0.0238 0.0072  49  VAL   A CB  
1156 C CB  B VAL   A 49  ? 0.1336 0.1428 0.1304 -0.0001 -0.0058 0.0101  49  VAL   A CB  
1157 C CG1 A VAL   A 49  ? 0.1604 0.1333 0.2085 -0.0098 -0.0084 0.0085  49  VAL   A CG1 
1158 C CG1 B VAL   A 49  ? 0.1235 0.1372 0.1301 0.0122  -0.0031 0.0299  49  VAL   A CG1 
1159 C CG2 A VAL   A 49  ? 0.1691 0.1508 0.2460 -0.0369 -0.0253 0.0114  49  VAL   A CG2 
1160 C CG2 B VAL   A 49  ? 0.1445 0.1529 0.1645 -0.0102 -0.0272 0.0251  49  VAL   A CG2 
1179 N N   A ALA   A 50  ? 0.1266 0.1232 0.1494 -0.0107 -0.0197 0.0200  50  ALA   A N   
1180 N N   B ALA   A 50  ? 0.1342 0.1315 0.0796 0.0061  -0.0005 -0.0357 50  ALA   A N   
1181 C CA  A ALA   A 50  ? 0.1267 0.1185 0.1514 -0.0148 -0.0033 0.0281  50  ALA   A CA  
1182 C CA  B ALA   A 50  ? 0.1332 0.1270 0.0706 0.0026  -0.0103 -0.0343 50  ALA   A CA  
1183 C C   A ALA   A 50  ? 0.1205 0.1265 0.1520 -0.0111 0.0021  0.0255  50  ALA   A C   
1184 C C   B ALA   A 50  ? 0.1324 0.1247 0.0455 -0.0020 -0.0090 -0.0291 50  ALA   A C   
1185 O O   A ALA   A 50  ? 0.1237 0.1276 0.1789 -0.0031 -0.0042 0.0173  50  ALA   A O   
1186 O O   B ALA   A 50  ? 0.1371 0.1297 0.0492 0.0042  -0.0163 -0.0281 50  ALA   A O   
1187 C CB  A ALA   A 50  ? 0.1226 0.1240 0.1656 -0.0023 0.0022  0.0109  50  ALA   A CB  
1188 C CB  B ALA   A 50  ? 0.1318 0.1256 0.0800 0.0084  -0.0042 -0.0356 50  ALA   A CB  
1199 N N   A GLY   A 51  ? 0.1198 0.1228 0.1419 0.0048  -0.0060 0.0217  51  GLY   A N   
1200 N N   B GLY   A 51  ? 0.1380 0.1343 0.0891 0.0003  -0.0080 -0.0250 51  GLY   A N   
1201 C CA  A GLY   A 51  ? 0.1348 0.1188 0.1609 0.0064  -0.0006 0.0223  51  GLY   A CA  
1202 C CA  B GLY   A 51  ? 0.1455 0.1288 0.0738 -0.0024 -0.0010 -0.0458 51  GLY   A CA  
1203 C C   A GLY   A 51  ? 0.1182 0.1225 0.1513 0.0048  0.0093  0.0038  51  GLY   A C   
1204 C C   B GLY   A 51  ? 0.1402 0.1354 0.0858 -0.0020 -0.0046 -0.0451 51  GLY   A C   
1205 O O   A GLY   A 51  ? 0.1294 0.1388 0.1513 0.0029  -0.0032 0.0035  51  GLY   A O   
1206 O O   B GLY   A 51  ? 0.1451 0.1419 0.0758 -0.0026 -0.0008 -0.0357 51  GLY   A O   
1213 N N   A ALA   A 52  ? 0.1195 0.1350 0.1511 -0.0019 -0.0028 0.0151  52  ALA   A N   
1214 N N   B ALA   A 52  ? 0.1404 0.1393 0.0821 -0.0040 -0.0073 -0.0447 52  ALA   A N   
1215 C CA  A ALA   A 52  ? 0.1264 0.1474 0.1532 -0.0080 0.0015  0.0073  52  ALA   A CA  
1216 C CA  B ALA   A 52  ? 0.1390 0.1451 0.0989 0.0010  0.0074  -0.0286 52  ALA   A CA  
1217 C C   A ALA   A 52  ? 0.1321 0.1455 0.1500 -0.0077 0.0071  0.0145  52  ALA   A C   
1218 C C   B ALA   A 52  ? 0.1335 0.1394 0.0887 0.0013  0.0169  -0.0274 52  ALA   A C   
1219 O O   A ALA   A 52  ? 0.1421 0.1567 0.1707 -0.0028 -0.0011 0.0090  52  ALA   A O   
1220 O O   B ALA   A 52  ? 0.1358 0.1392 0.0952 -0.0027 0.0178  -0.0191 52  ALA   A O   
1221 C CB  A ALA   A 52  ? 0.1354 0.1718 0.1701 -0.0102 -0.0069 0.0150  52  ALA   A CB  
1222 C CB  B ALA   A 52  ? 0.1429 0.1627 0.1341 0.0053  0.0019  -0.0222 52  ALA   A CB  
1233 N N   A LEU   A 53  ? 0.1300 0.1434 0.1408 -0.0120 0.0049  0.0167  53  LEU   A N   
1234 N N   B LEU   A 53  ? 0.1299 0.1422 0.0997 0.0034  0.0028  -0.0232 53  LEU   A N   
1235 C CA  A LEU   A 53  ? 0.1380 0.1468 0.1447 -0.0124 0.0041  0.0233  53  LEU   A CA  
1236 C CA  B LEU   A 53  ? 0.1304 0.1438 0.0941 0.0004  -0.0070 -0.0195 53  LEU   A CA  
1237 C C   A LEU   A 53  ? 0.1375 0.1489 0.0988 -0.0011 0.0052  0.0188  53  LEU   A C   
1238 C C   B LEU   A 53  ? 0.1390 0.1404 0.0984 0.0086  0.0040  -0.0295 53  LEU   A C   
1239 O O   A LEU   A 53  ? 0.1511 0.1609 0.1393 -0.0155 0.0055  0.0153  53  LEU   A O   
1240 O O   B LEU   A 53  ? 0.1515 0.1449 0.1202 0.0060  0.0146  -0.0275 53  LEU   A O   
1241 C CB  A LEU   A 53  ? 0.1453 0.1548 0.1825 -0.0152 0.0122  0.0214  53  LEU   A CB  
1242 C CB  B LEU   A 53  ? 0.1257 0.1508 0.0891 -0.0016 -0.0123 -0.0123 53  LEU   A CB  
1243 C CG  A LEU   A 53  ? 0.1475 0.1570 0.1784 -0.0183 0.0088  0.0159  53  LEU   A CG  
1244 C CG  B LEU   A 53  ? 0.1138 0.1545 0.0911 -0.0024 -0.0165 -0.0121 53  LEU   A CG  
1245 C CD1 A LEU   A 53  ? 0.1498 0.1655 0.1655 0.0041  -0.0082 0.0215  53  LEU   A CD1 
1246 C CD1 B LEU   A 53  ? 0.1133 0.1602 0.1137 -0.0000 -0.0091 -0.0176 53  LEU   A CD1 
1247 C CD2 A LEU   A 53  ? 0.1582 0.1680 0.1822 -0.0183 0.0082  0.0252  53  LEU   A CD2 
1248 C CD2 B LEU   A 53  ? 0.1219 0.1592 0.0974 -0.0058 -0.0184 0.0041  53  LEU   A CD2 
1271 N N   A ASN   A 54  ? 0.1286 0.1442 0.1070 -0.0074 -0.0122 0.0159  54  ASN   A N   
1272 N N   B ASN   A 54  ? 0.1353 0.1358 0.1400 0.0017  0.0030  -0.0248 54  ASN   A N   
1273 C CA  A ASN   A 54  ? 0.1204 0.1433 0.1263 -0.0031 -0.0081 0.0106  54  ASN   A CA  
1274 C CA  B ASN   A 54  ? 0.1256 0.1338 0.1402 -0.0016 0.0082  -0.0261 54  ASN   A CA  
1275 C C   A ASN   A 54  ? 0.1301 0.1446 0.1269 -0.0087 -0.0038 0.0123  54  ASN   A C   
1276 C C   B ASN   A 54  ? 0.1310 0.1388 0.1364 -0.0063 -0.0028 -0.0118 54  ASN   A C   
1277 O O   A ASN   A 54  ? 0.1347 0.1592 0.1467 -0.0072 -0.0039 0.0046  54  ASN   A O   
1278 O O   B ASN   A 54  ? 0.1327 0.1399 0.1432 -0.0105 -0.0086 -0.0190 54  ASN   A O   
1279 C CB  A ASN   A 54  ? 0.1238 0.1471 0.1425 -0.0025 -0.0312 0.0181  54  ASN   A CB  
1280 C CB  B ASN   A 54  ? 0.1221 0.1310 0.1312 -0.0012 0.0200  -0.0312 54  ASN   A CB  
1281 C CG  A ASN   A 54  ? 0.1358 0.1549 0.1725 -0.0090 -0.0360 0.0274  54  ASN   A CG  
1282 C CG  B ASN   A 54  ? 0.1204 0.1314 0.1163 -0.0035 0.0191  -0.0408 54  ASN   A CG  
1283 O OD1 A ASN   A 54  ? 0.1350 0.1514 0.2084 -0.0085 -0.0351 0.0315  54  ASN   A OD1 
1284 O OD1 B ASN   A 54  ? 0.1096 0.1249 0.1084 0.0029  0.0199  -0.0511 54  ASN   A OD1 
1285 N ND2 A ASN   A 54  ? 0.1364 0.1620 0.1952 -0.0107 -0.0323 0.0487  54  ASN   A ND2 
1286 N ND2 B ASN   A 54  ? 0.1204 0.1356 0.1387 -0.0118 0.0177  -0.0255 54  ASN   A ND2 
1299 N N   . LYS   A 55  ? 0.1300 0.1433 0.1437 0.0011  -0.0056 -0.0064 55  LYS   A N   
1300 C CA  . LYS   A 55  ? 0.1408 0.1601 0.1429 0.0074  -0.0106 -0.0236 55  LYS   A CA  
1301 C C   . LYS   A 55  ? 0.1348 0.1642 0.1364 -0.0032 -0.0125 -0.0230 55  LYS   A C   
1302 O O   . LYS   A 55  ? 0.1445 0.1776 0.1551 0.0020  -0.0120 -0.0260 55  LYS   A O   
1303 C CB  . LYS   A 55  ? 0.1491 0.1643 0.1674 0.0151  0.0044  -0.0271 55  LYS   A CB  
1304 C CG  . LYS   A 55  ? 0.1641 0.1963 0.1876 0.0311  -0.0074 -0.0275 55  LYS   A CG  
1305 C CD  . LYS   A 55  ? 0.1855 0.2344 0.2006 0.0519  -0.0019 -0.0248 55  LYS   A CD  
1306 C CE  . LYS   A 55  ? 0.2181 0.2732 0.2254 0.0759  -0.0272 -0.0272 55  LYS   A CE  
1307 N NZ  . LYS   A 55  ? 0.2354 0.3003 0.2447 0.0820  -0.0433 -0.0264 55  LYS   A NZ  
1322 N N   . ALA   A 56  ? 0.1414 0.1731 0.1577 -0.0090 0.0028  -0.0182 56  ALA   A N   
1323 C CA  . ALA   A 56  ? 0.1631 0.1891 0.1452 -0.0139 0.0030  -0.0159 56  ALA   A CA  
1324 C C   . ALA   A 56  ? 0.1623 0.1930 0.1021 -0.0061 0.0115  -0.0355 56  ALA   A C   
1325 O O   . ALA   A 56  ? 0.1674 0.2268 0.1166 -0.0012 0.0193  -0.0196 56  ALA   A O   
1326 C CB  . ALA   A 56  ? 0.1645 0.2129 0.1628 -0.0280 0.0150  0.0060  56  ALA   A CB  
1332 N N   . THR   A 57  ? 0.1472 0.1774 0.1314 -0.0095 0.0130  -0.0204 57  THR   A N   
1333 C CA  . THR   A 57  ? 0.1472 0.1706 0.1383 -0.0162 0.0038  -0.0071 57  THR   A CA  
1334 C C   . THR   A 57  ? 0.1552 0.1777 0.1328 -0.0134 -0.0002 -0.0042 57  THR   A C   
1335 O O   . THR   A 57  ? 0.1550 0.1807 0.1549 -0.0209 -0.0038 -0.0254 57  THR   A O   
1336 C CB  . THR   A 57  ? 0.1433 0.1673 0.1331 -0.0051 0.0040  -0.0166 57  THR   A CB  
1337 O OG1 . THR   A 57  ? 0.1394 0.1680 0.1282 -0.0016 0.0002  -0.0126 57  THR   A OG1 
1338 C CG2 . THR   A 57  ? 0.1471 0.1700 0.1373 -0.0103 0.0045  -0.0104 57  THR   A CG2 
1346 N N   . ASN   A 58  ? 0.1462 0.1675 0.1699 -0.0122 0.0110  -0.0196 58  ASN   A N   
1347 C CA  . ASN   A 58  ? 0.1652 0.1709 0.1922 -0.0142 0.0129  -0.0319 58  ASN   A CA  
1348 C C   . ASN   A 58  ? 0.1480 0.1579 0.1688 0.0058  0.0095  -0.0226 58  ASN   A C   
1349 O O   . ASN   A 58  ? 0.1503 0.1706 0.1927 -0.0117 -0.0094 -0.0256 58  ASN   A O   
1350 C CB  . ASN   A 58  ? 0.2156 0.1832 0.2034 -0.0124 0.0351  -0.0497 58  ASN   A CB  
1351 C CG  . ASN   A 58  ? 0.2547 0.2102 0.2686 -0.0147 0.0309  -0.0203 58  ASN   A CG  
1352 O OD1 . ASN   A 58  ? 0.2812 0.1979 0.3166 0.0265  0.0611  -0.0050 58  ASN   A OD1 
1353 N ND2 . ASN   A 58  ? 0.2618 0.2170 0.2802 -0.0184 0.0111  -0.0168 58  ASN   A ND2 
1360 N N   . ASN   A 59  ? 0.1376 0.1420 0.1581 -0.0055 -0.0017 -0.0140 59  ASN   A N   
1361 C CA  . ASN   A 59  ? 0.1449 0.1362 0.1459 0.0024  -0.0074 -0.0019 59  ASN   A CA  
1362 C C   . ASN   A 59  ? 0.1402 0.1460 0.1340 -0.0106 -0.0045 0.0027  59  ASN   A C   
1363 O O   . ASN   A 59  ? 0.1451 0.1494 0.1403 -0.0116 -0.0025 0.0072  59  ASN   A O   
1364 C CB  . ASN   A 59  ? 0.1467 0.1349 0.1496 0.0001  -0.0124 -0.0107 59  ASN   A CB  
1365 C CG  . ASN   A 59  ? 0.1498 0.1367 0.1586 0.0019  -0.0303 0.0005  59  ASN   A CG  
1366 O OD1 . ASN   A 59  ? 0.1564 0.1448 0.1557 -0.0098 -0.0200 -0.0005 59  ASN   A OD1 
1367 N ND2 . ASN   A 59  ? 0.1590 0.1495 0.1788 -0.0217 -0.0200 0.0081  59  ASN   A ND2 
1374 N N   . ALA   A 60  ? 0.1349 0.1514 0.1455 -0.0036 0.0006  0.0037  60  ALA   A N   
1375 C CA  . ALA   A 60  ? 0.1344 0.1456 0.1536 0.0048  -0.0139 0.0085  60  ALA   A CA  
1376 C C   . ALA   A 60  ? 0.1368 0.1443 0.1559 -0.0017 -0.0000 0.0063  60  ALA   A C   
1377 O O   . ALA   A 60  ? 0.1290 0.1416 0.1901 -0.0068 -0.0051 -0.0045 60  ALA   A O   
1378 C CB  . ALA   A 60  ? 0.1351 0.1523 0.1570 0.0018  -0.0149 -0.0111 60  ALA   A CB  
1384 N N   . MET   A 61  ? 0.1360 0.1369 0.1467 -0.0070 0.0017  -0.0113 61  MET   A N   
1385 C CA  . MET   A 61  ? 0.1296 0.1373 0.1362 -0.0080 -0.0004 0.0004  61  MET   A CA  
1386 C C   . MET   A 61  ? 0.1248 0.1406 0.1432 -0.0157 0.0039  0.0016  61  MET   A C   
1387 O O   . MET   A 61  ? 0.1300 0.1299 0.1631 -0.0051 0.0123  0.0024  61  MET   A O   
1388 C CB  . MET   A 61  ? 0.1449 0.1381 0.1254 -0.0071 -0.0001 -0.0006 61  MET   A CB  
1389 C CG  . MET   A 61  ? 0.1408 0.1470 0.1526 -0.0083 0.0050  0.0050  61  MET   A CG  
1390 S SD  . MET   A 61  ? 0.1431 0.1428 0.1778 -0.0095 0.0036  -0.0091 61  MET   A SD  
1391 C CE  . MET   A 61  ? 0.1559 0.1564 0.2197 -0.0023 0.0077  -0.0249 61  MET   A CE  
1401 N N   . GLN   A 62  ? 0.1293 0.1328 0.1513 -0.0128 0.0053  0.0062  62  GLN   A N   
1402 C CA  . GLN   A 62  ? 0.1335 0.1254 0.1604 -0.0081 0.0051  0.0149  62  GLN   A CA  
1403 C C   . GLN   A 62  ? 0.1390 0.1121 0.1583 0.0009  0.0012  0.0027  62  GLN   A C   
1404 O O   . GLN   A 62  ? 0.1408 0.1345 0.1692 -0.0023 0.0063  -0.0033 62  GLN   A O   
1405 C CB  . GLN   A 62  ? 0.1346 0.1232 0.1750 -0.0089 0.0005  0.0093  62  GLN   A CB  
1406 C CG  . GLN   A 62  ? 0.1354 0.1263 0.1757 -0.0033 -0.0034 0.0240  62  GLN   A CG  
1407 C CD  . GLN   A 62  ? 0.1417 0.1286 0.1664 0.0009  0.0033  0.0086  62  GLN   A CD  
1408 O OE1 . GLN   A 62  ? 0.1433 0.1432 0.1612 -0.0012 -0.0030 0.0095  62  GLN   A OE1 
1409 N NE2 . GLN   A 62  ? 0.1516 0.1286 0.1682 0.0028  0.0036  -0.0078 62  GLN   A NE2 
1418 N N   . VAL   A 63  ? 0.1334 0.1272 0.1717 -0.0085 0.0057  -0.0133 63  VAL   A N   
1419 C CA  . VAL   A 63  ? 0.1333 0.1415 0.1903 -0.0147 -0.0038 -0.0098 63  VAL   A CA  
1420 C C   . VAL   A 63  ? 0.1221 0.1445 0.1839 -0.0184 -0.0073 -0.0084 63  VAL   A C   
1421 O O   . VAL   A 63  ? 0.1262 0.1417 0.2050 -0.0245 -0.0064 -0.0038 63  VAL   A O   
1422 C CB  . VAL   A 63  ? 0.1513 0.1627 0.2406 -0.0119 -0.0152 -0.0309 63  VAL   A CB  
1423 C CG1 . VAL   A 63  ? 0.1678 0.1819 0.2794 -0.0152 -0.0164 -0.0568 63  VAL   A CG1 
1424 C CG2 . VAL   A 63  ? 0.1519 0.1572 0.2460 -0.0073 0.0032  -0.0254 63  VAL   A CG2 
1434 N N   . GLU   A 64  ? 0.1213 0.1511 0.1817 -0.0042 0.0022  -0.0013 64  GLU   A N   
1435 C CA  . GLU   A 64  ? 0.1283 0.1485 0.1619 -0.0052 0.0029  0.0016  64  GLU   A CA  
1436 C C   . GLU   A 64  ? 0.1240 0.1359 0.1626 -0.0044 0.0017  0.0040  64  GLU   A C   
1437 O O   . GLU   A 64  ? 0.1337 0.1398 0.1750 -0.0003 0.0084  -0.0007 64  GLU   A O   
1438 C CB  . GLU   A 64  ? 0.1348 0.1548 0.1790 -0.0047 0.0099  0.0010  64  GLU   A CB  
1439 C CG  . GLU   A 64  ? 0.1406 0.1650 0.1804 -0.0043 0.0091  0.0099  64  GLU   A CG  
1440 C CD  . GLU   A 64  ? 0.1578 0.1743 0.1960 -0.0061 0.0032  0.0068  64  GLU   A CD  
1441 O OE1 . GLU   A 64  ? 0.1575 0.1762 0.2078 -0.0172 0.0143  0.0167  64  GLU   A OE1 
1442 O OE2 . GLU   A 64  ? 0.1703 0.1732 0.1893 -0.0216 -0.0038 0.0110  64  GLU   A OE2 
1449 N N   . SER   A 65  ? 0.1269 0.1445 0.1463 -0.0001 -0.0055 -0.0021 65  SER   A N   
1450 C CA  . SER   A 65  ? 0.1343 0.1362 0.1370 0.0040  -0.0029 0.0001  65  SER   A CA  
1451 C C   . SER   A 65  ? 0.1327 0.1416 0.1500 -0.0045 -0.0082 0.0017  65  SER   A C   
1452 O O   . SER   A 65  ? 0.1396 0.1392 0.1787 0.0027  0.0166  0.0073  65  SER   A O   
1453 C CB  . SER   A 65  ? 0.1315 0.1332 0.1527 -0.0028 -0.0013 0.0049  65  SER   A CB  
1454 O OG  . SER   A 65  ? 0.1308 0.1416 0.1654 -0.0092 0.0020  0.0142  65  SER   A OG  
1460 N N   . ASP   A 66  ? 0.1349 0.1384 0.1588 -0.0023 0.0184  0.0136  66  ASP   A N   
1461 C CA  . ASP   A 66  ? 0.1418 0.1411 0.1736 -0.0037 0.0042  0.0230  66  ASP   A CA  
1462 C C   . ASP   A 66  ? 0.1454 0.1468 0.1689 -0.0062 0.0130  0.0227  66  ASP   A C   
1463 O O   . ASP   A 66  ? 0.1506 0.1563 0.1959 -0.0073 0.0328  0.0299  66  ASP   A O   
1464 C CB  . ASP   A 66  ? 0.1508 0.1505 0.2266 0.0129  0.0199  0.0401  66  ASP   A CB  
1465 C CG  . ASP   A 66  ? 0.1707 0.1626 0.2499 0.0017  0.0164  0.0664  66  ASP   A CG  
1466 O OD1 . ASP   A 66  ? 0.1691 0.1890 0.2439 -0.0110 0.0071  0.0610  66  ASP   A OD1 
1467 O OD2 . ASP   A 66  ? 0.1858 0.1854 0.3137 0.0228  -0.0128 0.0349  66  ASP   A OD2 
1472 N N   . ASP   A 67  ? 0.1341 0.1416 0.1951 -0.0053 0.0116  0.0178  67  ASP   A N   
1473 C CA  . ASP   A 67  ? 0.1356 0.1664 0.2190 0.0004  0.0088  0.0293  67  ASP   A CA  
1474 C C   . ASP   A 67  ? 0.1344 0.1658 0.2066 0.0032  0.0223  0.0208  67  ASP   A C   
1475 O O   . ASP   A 67  ? 0.1361 0.1709 0.2158 -0.0044 0.0247  0.0288  67  ASP   A O   
1476 C CB  . ASP   A 67  ? 0.1447 0.1710 0.2422 -0.0053 -0.0084 0.0399  67  ASP   A CB  
1477 C CG  . ASP   A 67  ? 0.1462 0.1919 0.2803 -0.0155 -0.0198 0.0558  67  ASP   A CG  
1478 O OD1 . ASP   A 67  ? 0.1458 0.2115 0.3785 -0.0149 -0.0271 0.0643  67  ASP   A OD1 
1479 O OD2 . ASP   A 67  ? 0.1445 0.2017 0.2622 -0.0002 -0.0152 0.0434  67  ASP   A OD2 
1484 N N   . TYR   A 68  ? 0.1426 0.1419 0.2141 0.0084  0.0299  0.0325  68  TYR   A N   
1485 C CA  . TYR   A 68  ? 0.1530 0.1466 0.2058 0.0032  0.0300  0.0295  68  TYR   A CA  
1486 C C   . TYR   A 68  ? 0.1407 0.1459 0.1973 0.0010  0.0313  0.0226  68  TYR   A C   
1487 O O   . TYR   A 68  ? 0.1428 0.1488 0.2253 0.0086  0.0343  0.0162  68  TYR   A O   
1488 C CB  . TYR   A 68  ? 0.1613 0.1448 0.2110 0.0064  0.0426  0.0360  68  TYR   A CB  
1489 C CG  . TYR   A 68  ? 0.1589 0.1554 0.2596 0.0074  0.0590  0.0336  68  TYR   A CG  
1490 C CD1 . TYR   A 68  ? 0.1703 0.1623 0.3069 -0.0273 0.0557  -0.0133 68  TYR   A CD1 
1491 C CD2 . TYR   A 68  ? 0.1798 0.1656 0.3047 0.0102  0.0659  0.0296  68  TYR   A CD2 
1492 C CE1 . TYR   A 68  ? 0.1704 0.1747 0.3496 -0.0308 0.0699  -0.0263 68  TYR   A CE1 
1493 C CE2 . TYR   A 68  ? 0.1822 0.1641 0.3377 -0.0094 0.0784  -0.0023 68  TYR   A CE2 
1494 C CZ  . TYR   A 68  ? 0.1786 0.1687 0.3657 -0.0230 0.0667  -0.0339 68  TYR   A CZ  
1495 O OH  . TYR   A 68  ? 0.2047 0.1803 0.4128 -0.0181 0.0444  -0.0619 68  TYR   A OH  
1505 N N   . ILE   A 69  ? 0.1338 0.1447 0.1860 0.0015  0.0152  0.0224  69  ILE   A N   
1506 C CA  . ILE   A 69  ? 0.1444 0.1466 0.1816 0.0033  0.0069  0.0026  69  ILE   A CA  
1507 C C   . ILE   A 69  ? 0.1494 0.1496 0.1744 0.0082  0.0222  0.0177  69  ILE   A C   
1508 O O   . ILE   A 69  ? 0.1432 0.1539 0.1802 0.0033  0.0209  0.0159  69  ILE   A O   
1509 C CB  . ILE   A 69  ? 0.1504 0.1652 0.1863 0.0033  0.0063  0.0030  69  ILE   A CB  
1510 C CG1 . ILE   A 69  ? 0.1523 0.1711 0.1904 0.0070  0.0192  -0.0152 69  ILE   A CG1 
1511 C CG2 . ILE   A 69  ? 0.1615 0.1871 0.2061 0.0119  0.0066  -0.0125 69  ILE   A CG2 
1512 C CD1 . ILE   A 69  ? 0.1576 0.1875 0.2037 -0.0054 0.0180  -0.0236 69  ILE   A CD1 
1524 N N   . ALA   A 70  ? 0.1498 0.1538 0.1926 -0.0016 0.0167  0.0344  70  ALA   A N   
1525 C CA  . ALA   A 70  ? 0.1495 0.1597 0.2106 -0.0159 0.0288  0.0346  70  ALA   A CA  
1526 C C   . ALA   A 70  ? 0.1485 0.1785 0.2055 -0.0165 0.0336  0.0307  70  ALA   A C   
1527 O O   . ALA   A 70  ? 0.1731 0.2065 0.2244 0.0104  0.0482  0.0468  70  ALA   A O   
1528 C CB  . ALA   A 70  ? 0.1514 0.1698 0.2465 -0.0152 0.0239  0.0368  70  ALA   A CB  
1534 N N   . THR   A 71  ? 0.1425 0.1794 0.2101 -0.0017 0.0266  0.0436  71  THR   A N   
1535 C CA  . THR   A 71  ? 0.1565 0.1997 0.2421 0.0210  0.0263  0.0490  71  THR   A CA  
1536 C C   . THR   A 71  ? 0.1492 0.1864 0.2742 0.0216  0.0370  0.0376  71  THR   A C   
1537 O O   . THR   A 71  ? 0.1575 0.2080 0.3205 0.0094  0.0385  0.0065  71  THR   A O   
1538 C CB  . THR   A 71  ? 0.1872 0.2245 0.2645 0.0232  -0.0134 0.0597  71  THR   A CB  
1539 O OG1 . THR   A 71  ? 0.2175 0.2493 0.2923 0.0181  -0.0433 0.0404  71  THR   A OG1 
1540 C CG2 . THR   A 71  ? 0.2065 0.2459 0.2955 0.0253  -0.0255 0.0814  71  THR   A CG2 
1548 N N   . ASN   A 72  ? 0.1510 0.1699 0.2470 0.0221  0.0339  0.0319  72  ASN   A N   
1549 C CA  . ASN   A 72  ? 0.1583 0.1726 0.2511 0.0252  0.0536  0.0344  72  ASN   A CA  
1550 C C   . ASN   A 72  ? 0.1652 0.1706 0.2468 0.0136  0.0548  0.0264  72  ASN   A C   
1551 O O   . ASN   A 72  ? 0.1856 0.1695 0.2622 0.0188  0.0420  0.0177  72  ASN   A O   
1552 C CB  . ASN   A 72  ? 0.1791 0.1890 0.2488 0.0256  0.0589  0.0414  72  ASN   A CB  
1553 C CG  . ASN   A 72  ? 0.2027 0.2044 0.2453 0.0240  0.0499  0.0451  72  ASN   A CG  
1554 O OD1 . ASN   A 72  ? 0.2211 0.2309 0.2568 0.0246  0.0456  0.0450  72  ASN   A OD1 
1555 N ND2 . ASN   A 72  ? 0.2205 0.1922 0.2464 0.0545  0.0326  0.0473  72  ASN   A ND2 
1562 N N   . GLY   A 73  ? 0.1584 0.1609 0.2240 0.0110  0.0527  0.0139  73  GLY   A N   
1563 C CA  . GLY   A 73  ? 0.1678 0.1557 0.1964 -0.0050 0.0441  0.0098  73  GLY   A CA  
1564 C C   . GLY   A 73  ? 0.1661 0.1517 0.1757 0.0069  0.0572  0.0341  73  GLY   A C   
1565 O O   . GLY   A 73  ? 0.1710 0.1571 0.2008 0.0203  0.0458  0.0369  73  GLY   A O   
1569 N N   . PRO   A 74  ? 0.1826 0.1552 0.1884 -0.0057 0.0541  0.0208  74  PRO   A N   
1570 C CA  . PRO   A 74  ? 0.1737 0.1471 0.2016 -0.0020 0.0513  0.0250  74  PRO   A CA  
1571 C C   . PRO   A 74  ? 0.1654 0.1342 0.2025 0.0028  0.0311  0.0149  74  PRO   A C   
1572 O O   . PRO   A 74  ? 0.1741 0.1460 0.2134 0.0025  0.0322  -0.0034 74  PRO   A O   
1573 C CB  . PRO   A 74  ? 0.1927 0.1728 0.2301 -0.0005 0.0490  0.0295  74  PRO   A CB  
1574 C CG  . PRO   A 74  ? 0.2245 0.2167 0.2818 -0.0212 0.0342  0.0173  74  PRO   A CG  
1575 C CD  . PRO   A 74  ? 0.2019 0.1873 0.2124 -0.0192 0.0375  0.0124  74  PRO   A CD  
1583 N N   . LEU   A 75  ? 0.1724 0.1322 0.1711 0.0027  0.0339  0.0102  75  LEU   A N   
1584 C CA  . LEU   A 75  ? 0.1711 0.1321 0.1512 0.0056  0.0205  0.0147  75  LEU   A CA  
1585 C C   . LEU   A 75  ? 0.1748 0.1443 0.1540 0.0093  0.0190  0.0294  75  LEU   A C   
1586 O O   . LEU   A 75  ? 0.2081 0.1477 0.1637 0.0122  0.0119  0.0105  75  LEU   A O   
1587 C CB  . LEU   A 75  ? 0.1726 0.1356 0.1424 0.0024  0.0216  0.0264  75  LEU   A CB  
1588 C CG  . LEU   A 75  ? 0.1904 0.1705 0.1639 -0.0261 0.0231  0.0092  75  LEU   A CG  
1589 C CD1 . LEU   A 75  ? 0.2012 0.2201 0.1880 -0.0381 0.0264  -0.0073 75  LEU   A CD1 
1590 C CD2 . LEU   A 75  ? 0.2256 0.2202 0.2077 -0.0052 0.0147  0.0278  75  LEU   A CD2 
1602 N N   . LYS   A 76  ? 0.1741 0.1379 0.1729 -0.0006 0.0100  0.0101  76  LYS   A N   
1603 C CA  . LYS   A 76  ? 0.1665 0.1599 0.1713 -0.0015 0.0090  0.0054  76  LYS   A CA  
1604 C C   . LYS   A 76  ? 0.1678 0.1490 0.1335 0.0019  0.0022  0.0162  76  LYS   A C   
1605 O O   . LYS   A 76  ? 0.1744 0.1393 0.1462 -0.0013 0.0165  0.0141  76  LYS   A O   
1606 C CB  . LYS   A 76  ? 0.1646 0.1842 0.2157 0.0075  0.0137  -0.0295 76  LYS   A CB  
1607 C CG  . LYS   A 76  ? 0.1794 0.1769 0.2528 0.0095  0.0043  -0.0271 76  LYS   A CG  
1608 C CD  . LYS   A 76  ? 0.1906 0.1779 0.2908 0.0149  -0.0112 -0.0242 76  LYS   A CD  
1609 C CE  . LYS   A 76  ? 0.2071 0.2018 0.3452 0.0075  -0.0089 -0.0283 76  LYS   A CE  
1610 N NZ  . LYS   A 76  ? 0.2086 0.1872 0.3921 -0.0086 -0.0136 -0.0343 76  LYS   A NZ  
1624 N N   . VAL   A 77  ? 0.1805 0.1559 0.1456 -0.0081 0.0197  0.0186  77  VAL   A N   
1625 C CA  . VAL   A 77  ? 0.1766 0.1588 0.1410 -0.0009 0.0061  0.0205  77  VAL   A CA  
1626 C C   . VAL   A 77  ? 0.1717 0.1548 0.1474 0.0072  0.0141  0.0094  77  VAL   A C   
1627 O O   . VAL   A 77  ? 0.1789 0.1658 0.1549 0.0072  0.0329  -0.0054 77  VAL   A O   
1628 C CB  . VAL   A 77  ? 0.1981 0.1791 0.1628 -0.0107 0.0152  0.0279  77  VAL   A CB  
1629 C CG1 . VAL   A 77  ? 0.2008 0.1849 0.1753 -0.0015 0.0014  0.0178  77  VAL   A CG1 
1630 C CG2 . VAL   A 77  ? 0.2173 0.1881 0.1897 -0.0148 -0.0093 0.0286  77  VAL   A CG2 
1640 N N   . GLY   A 78  ? 0.1605 0.1483 0.1395 0.0016  0.0192  0.0062  78  GLY   A N   
1641 C CA  . GLY   A 78  ? 0.1640 0.1486 0.1559 0.0046  0.0313  0.0060  78  GLY   A CA  
1642 C C   . GLY   A 78  ? 0.1514 0.1420 0.1570 0.0052  0.0268  0.0132  78  GLY   A C   
1643 O O   . GLY   A 78  ? 0.1493 0.1463 0.1833 0.0007  0.0139  0.0281  78  GLY   A O   
1647 N N   . GLY   A 79  ? 0.1578 0.1381 0.1611 -0.0025 0.0231  0.0180  79  GLY   A N   
1648 C CA  . GLY   A 79  ? 0.1549 0.1336 0.1761 -0.0025 0.0179  0.0167  79  GLY   A CA  
1649 C C   . GLY   A 79  ? 0.1377 0.1263 0.1590 -0.0040 0.0202  0.0075  79  GLY   A C   
1650 O O   . GLY   A 79  ? 0.1389 0.1409 0.1825 0.0124  0.0145  0.0032  79  GLY   A O   
1654 N N   . SER   A 80  ? 0.1322 0.1438 0.1742 0.0015  0.0216  0.0032  80  SER   A N   
1655 C CA  . SER   A 80  ? 0.1388 0.1374 0.1613 0.0035  0.0123  0.0058  80  SER   A CA  
1656 C C   . SER   A 80  ? 0.1463 0.1346 0.1510 -0.0047 0.0146  0.0225  80  SER   A C   
1657 O O   . SER   A 80  ? 0.1350 0.1611 0.2029 0.0076  0.0169  0.0069  80  SER   A O   
1658 C CB  . SER   A 80  ? 0.1511 0.1414 0.1786 -0.0002 0.0238  0.0074  80  SER   A CB  
1659 O OG  . SER   A 80  ? 0.1720 0.1335 0.2232 0.0065  -0.0004 0.0264  80  SER   A OG  
1665 N N   . CYS   A 81  ? 0.1420 0.1321 0.1444 0.0018  0.0076  0.0209  81  CYS   A N   
1666 C CA  . CYS   A 81  ? 0.1393 0.1472 0.1413 -0.0107 -0.0106 0.0207  81  CYS   A CA  
1667 C C   . CYS   A 81  ? 0.1336 0.1455 0.1381 -0.0129 0.0013  0.0332  81  CYS   A C   
1668 O O   . CYS   A 81  ? 0.1283 0.1686 0.1718 -0.0030 0.0058  0.0420  81  CYS   A O   
1669 C CB  . CYS   A 81  ? 0.1427 0.1523 0.1627 -0.0094 0.0054  0.0269  81  CYS   A CB  
1670 S SG  . CYS   A 81  ? 0.1501 0.1399 0.1746 -0.0143 0.0042  0.0150  81  CYS   A SG  
1676 N N   . VAL   A 82  ? 0.1455 0.1464 0.1388 -0.0020 -0.0100 0.0216  82  VAL   A N   
1677 C CA  . VAL   A 82  ? 0.1525 0.1564 0.1426 0.0035  -0.0070 0.0256  82  VAL   A CA  
1678 C C   . VAL   A 82  ? 0.1465 0.1561 0.1580 -0.0111 -0.0026 0.0264  82  VAL   A C   
1679 O O   . VAL   A 82  ? 0.1436 0.1618 0.2043 -0.0081 0.0037  0.0028  82  VAL   A O   
1680 C CB  . VAL   A 82  ? 0.1819 0.1692 0.1704 0.0046  -0.0011 0.0372  82  VAL   A CB  
1681 C CG1 . VAL   A 82  ? 0.1999 0.1739 0.1945 0.0001  0.0008  0.0312  82  VAL   A CG1 
1682 C CG2 . VAL   A 82  ? 0.1790 0.1710 0.2060 -0.0008 -0.0035 0.0308  82  VAL   A CG2 
1692 N N   . LEU   A 83  ? 0.1360 0.1558 0.1709 -0.0146 -0.0071 0.0124  83  LEU   A N   
1693 C CA  . LEU   A 83  ? 0.1411 0.1592 0.1446 -0.0216 -0.0117 0.0150  83  LEU   A CA  
1694 C C   . LEU   A 83  ? 0.1518 0.1587 0.1414 -0.0233 -0.0208 0.0174  83  LEU   A C   
1695 O O   . LEU   A 83  ? 0.1623 0.1553 0.1609 -0.0179 0.0018  0.0222  83  LEU   A O   
1696 C CB  . LEU   A 83  ? 0.1500 0.1645 0.1576 -0.0196 -0.0171 0.0228  83  LEU   A CB  
1697 C CG  . LEU   A 83  ? 0.1613 0.1734 0.1609 -0.0157 0.0066  0.0170  83  LEU   A CG  
1698 C CD1 . LEU   A 83  ? 0.1716 0.1684 0.1603 -0.0209 0.0018  0.0272  83  LEU   A CD1 
1699 C CD2 . LEU   A 83  ? 0.1606 0.1859 0.1919 -0.0087 0.0126  0.0186  83  LEU   A CD2 
1711 N N   . SER   A 84  ? 0.1725 0.1621 0.1335 -0.0187 -0.0204 0.0172  84  SER   A N   
1712 C CA  . SER   A 84  ? 0.1885 0.1652 0.1135 -0.0181 -0.0200 0.0102  84  SER   A CA  
1713 C C   . SER   A 84  ? 0.1771 0.1684 0.1262 -0.0247 -0.0024 0.0241  84  SER   A C   
1714 O O   . SER   A 84  ? 0.1675 0.1801 0.1317 -0.0168 -0.0038 0.0222  84  SER   A O   
1715 C CB  . SER   A 84  ? 0.2015 0.1849 0.1303 -0.0133 -0.0214 -0.0027 84  SER   A CB  
1716 O OG  . SER   A 84  ? 0.1915 0.2107 0.1577 -0.0131 -0.0239 -0.0150 84  SER   A OG  
1722 N N   . GLY   A 85  ? 0.1956 0.1816 0.1403 -0.0270 0.0124  0.0137  85  GLY   A N   
1723 C CA  . GLY   A 85  ? 0.2011 0.1909 0.1621 -0.0242 0.0253  -0.0109 85  GLY   A CA  
1724 C C   . GLY   A 85  ? 0.1867 0.1945 0.1443 -0.0211 -0.0019 0.0082  85  GLY   A C   
1725 O O   . GLY   A 85  ? 0.1896 0.2093 0.1615 -0.0319 0.0113  -0.0093 85  GLY   A O   
1729 N N   . HIS   A 86  ? 0.1784 0.1942 0.1263 -0.0171 -0.0023 0.0138  86  HIS   A N   
1730 C CA  . HIS   A 86  ? 0.2021 0.2003 0.1305 -0.0207 0.0032  0.0196  86  HIS   A CA  
1731 C C   . HIS   A 86  ? 0.2298 0.2136 0.1091 -0.0237 -0.0062 0.0170  86  HIS   A C   
1732 O O   . HIS   A 86  ? 0.2414 0.2354 0.1275 -0.0291 0.0114  0.0018  86  HIS   A O   
1733 C CB  . HIS   A 86  ? 0.1964 0.1948 0.1345 -0.0120 -0.0020 0.0225  86  HIS   A CB  
1734 C CG  . HIS   A 86  ? 0.1839 0.1940 0.1444 -0.0120 -0.0083 0.0218  86  HIS   A CG  
1735 N ND1 . HIS   A 86  ? 0.1976 0.1975 0.1753 -0.0149 -0.0072 0.0200  86  HIS   A ND1 
1736 C CD2 . HIS   A 86  ? 0.1824 0.1870 0.1434 -0.0066 -0.0017 0.0191  86  HIS   A CD2 
1737 C CE1 . HIS   A 86  ? 0.1892 0.1935 0.1646 -0.0042 0.0165  0.0174  86  HIS   A CE1 
1738 N NE2 . HIS   A 86  ? 0.1897 0.1913 0.1664 0.0053  0.0095  0.0320  86  HIS   A NE2 
1746 N N   . ASN   A 87  ? 0.2418 0.2237 0.1392 -0.0111 0.0029  0.0056  87  ASN   A N   
1747 C CA  . ASN   A 87  ? 0.2602 0.2287 0.1320 -0.0161 0.0318  -0.0032 87  ASN   A CA  
1748 C C   . ASN   A 87  ? 0.2650 0.2458 0.1611 -0.0289 0.0563  -0.0029 87  ASN   A C   
1749 O O   . ASN   A 87  ? 0.2911 0.2660 0.1980 -0.0538 0.0922  -0.0076 87  ASN   A O   
1750 C CB  . ASN   A 87  ? 0.2761 0.2308 0.1571 -0.0080 0.0346  -0.0036 87  ASN   A CB  
1751 C CG  . ASN   A 87  ? 0.2810 0.2277 0.1422 -0.0048 0.0534  0.0004  87  ASN   A CG  
1752 O OD1 . ASN   A 87  ? 0.3028 0.2245 0.1485 0.0041  0.0484  0.0171  87  ASN   A OD1 
1753 N ND2 . ASN   A 87  ? 0.2794 0.2598 0.1747 -0.0048 0.0521  -0.0032 87  ASN   A ND2 
1760 N N   . LEU   A 88  ? 0.2367 0.2310 0.1710 -0.0284 0.0362  0.0148  88  LEU   A N   
1761 C CA  . LEU   A 88  ? 0.2103 0.2253 0.1889 -0.0328 0.0425  0.0353  88  LEU   A CA  
1762 C C   . LEU   A 88  ? 0.2024 0.2337 0.1814 -0.0357 0.0287  0.0348  88  LEU   A C   
1763 O O   . LEU   A 88  ? 0.2104 0.2321 0.2117 -0.0381 0.0354  0.0476  88  LEU   A O   
1764 C CB  . LEU   A 88  ? 0.2056 0.2276 0.2021 -0.0392 -0.0014 0.0342  88  LEU   A CB  
1765 C CG  . LEU   A 88  ? 0.2148 0.2337 0.2281 -0.0327 -0.0245 0.0430  88  LEU   A CG  
1766 C CD1 . LEU   A 88  ? 0.2294 0.2434 0.2218 -0.0315 -0.0346 0.0261  88  LEU   A CD1 
1767 C CD2 . LEU   A 88  ? 0.2263 0.2479 0.2749 -0.0217 -0.0139 0.0318  88  LEU   A CD2 
1779 N N   . ALA   A 89  ? 0.2023 0.2279 0.1599 -0.0290 0.0158  0.0137  89  ALA   A N   
1780 C CA  . ALA   A 89  ? 0.2046 0.2326 0.1371 -0.0234 0.0055  0.0256  89  ALA   A CA  
1781 C C   . ALA   A 89  ? 0.2081 0.2290 0.1456 -0.0174 0.0025  0.0306  89  ALA   A C   
1782 O O   . ALA   A 89  ? 0.2019 0.2232 0.1933 -0.0352 -0.0030 0.0023  89  ALA   A O   
1783 C CB  . ALA   A 89  ? 0.1950 0.2285 0.1324 -0.0162 -0.0039 0.0302  89  ALA   A CB  
1789 N N   . LYS   A 90  ? 0.2188 0.2437 0.1476 -0.0305 -0.0092 0.0375  90  LYS   A N   
1790 C CA  . LYS   A 90  ? 0.2287 0.2521 0.1408 -0.0151 -0.0228 0.0328  90  LYS   A CA  
1791 C C   . LYS   A 90  ? 0.2082 0.2387 0.1224 -0.0226 -0.0238 0.0216  90  LYS   A C   
1792 O O   . LYS   A 90  ? 0.2126 0.2393 0.1687 -0.0334 -0.0304 0.0123  90  LYS   A O   
1793 C CB  . LYS   A 90  ? 0.2599 0.2900 0.1877 -0.0170 -0.0316 0.0589  90  LYS   A CB  
1794 C CG  . LYS   A 90  ? 0.3118 0.3339 0.2878 -0.0156 -0.0241 0.0659  90  LYS   A CG  
1795 C CD  . LYS   A 90  ? 0.3659 0.3864 0.4008 -0.0187 -0.0053 0.0646  90  LYS   A CD  
1796 C CE  . LYS   A 90  ? 0.4070 0.4235 0.4847 -0.0223 0.0132  0.0584  90  LYS   A CE  
1797 N NZ  . LYS   A 90  ? 0.4427 0.4427 0.5434 -0.0277 0.0210  0.0514  90  LYS   A NZ  
1811 N N   . HIS   A 91  ? 0.2004 0.2061 0.0703 -0.0162 -0.0323 0.0276  91  HIS   A N   
1812 C CA  . HIS   A 91  ? 0.2011 0.1935 0.0999 -0.0231 -0.0260 0.0219  91  HIS   A CA  
1813 C C   . HIS   A 91  ? 0.1725 0.1730 0.0518 0.0054  -0.0212 0.0161  91  HIS   A C   
1814 O O   . HIS   A 91  ? 0.1584 0.2026 0.1398 -0.0251 -0.0088 0.0338  91  HIS   A O   
1815 C CB  . HIS   A 91  ? 0.2090 0.2188 0.1862 0.0015  -0.0394 0.0278  91  HIS   A CB  
1816 C CG  . HIS   A 91  ? 0.2449 0.2694 0.2611 0.0108  -0.0675 0.0056  91  HIS   A CG  
1817 N ND1 . HIS   A 91  ? 0.2566 0.2983 0.2982 0.0132  -0.0818 -0.0242 91  HIS   A ND1 
1818 C CD2 . HIS   A 91  ? 0.2681 0.2959 0.2983 0.0182  -0.0860 0.0124  91  HIS   A CD2 
1819 C CE1 . HIS   A 91  ? 0.2681 0.3068 0.3176 0.0203  -0.0829 -0.0108 91  HIS   A CE1 
1820 N NE2 . HIS   A 91  ? 0.2786 0.3095 0.3205 0.0261  -0.0931 -0.0050 91  HIS   A NE2 
1828 N N   . CYS   A 92  ? 0.1640 0.1727 0.0862 -0.0160 -0.0142 0.0259  92  CYS   A N   
1829 C CA  . CYS   A 92  ? 0.1609 0.1619 0.0881 -0.0178 0.0046  0.0325  92  CYS   A CA  
1830 C C   . CYS   A 92  ? 0.1452 0.1572 0.1283 -0.0234 0.0044  0.0211  92  CYS   A C   
1831 O O   . CYS   A 92  ? 0.1445 0.1626 0.1570 -0.0185 0.0105  0.0223  92  CYS   A O   
1832 C CB  . CYS   A 92  ? 0.1497 0.1564 0.1387 -0.0090 -0.0003 0.0145  92  CYS   A CB  
1833 S SG  . CYS   A 92  ? 0.1475 0.1462 0.1525 -0.0154 -0.0005 0.0157  92  CYS   A SG  
1839 N N   . LEU   A 93  ? 0.1427 0.1414 0.1416 -0.0076 0.0070  0.0154  93  LEU   A N   
1840 C CA  . LEU   A 93  ? 0.1349 0.1306 0.1376 -0.0087 0.0041  0.0145  93  LEU   A CA  
1841 C C   . LEU   A 93  ? 0.1413 0.1263 0.1316 0.0022  0.0014  0.0190  93  LEU   A C   
1842 O O   . LEU   A 93  ? 0.1272 0.1382 0.1402 -0.0035 -0.0044 0.0133  93  LEU   A O   
1843 C CB  . LEU   A 93  ? 0.1394 0.1411 0.1588 -0.0028 -0.0023 0.0269  93  LEU   A CB  
1844 C CG  . LEU   A 93  ? 0.1443 0.1414 0.1637 -0.0047 0.0123  0.0246  93  LEU   A CG  
1845 C CD1 . LEU   A 93  ? 0.1439 0.1452 0.1856 -0.0009 0.0155  0.0165  93  LEU   A CD1 
1846 C CD2 . LEU   A 93  ? 0.1581 0.1335 0.1895 -0.0074 0.0099  0.0197  93  LEU   A CD2 
1858 N N   . HIS   A 94  ? 0.1271 0.1265 0.1271 -0.0030 0.0133  0.0256  94  HIS   A N   
1859 C CA  . HIS   A 94  ? 0.1270 0.1299 0.1306 -0.0038 0.0081  0.0222  94  HIS   A CA  
1860 C C   . HIS   A 94  ? 0.1289 0.1278 0.1319 -0.0052 0.0124  0.0108  94  HIS   A C   
1861 O O   . HIS   A 94  ? 0.1296 0.1450 0.1771 -0.0010 0.0107  -0.0088 94  HIS   A O   
1862 C CB  . HIS   A 94  ? 0.1301 0.1289 0.1364 -0.0070 -0.0019 0.0118  94  HIS   A CB  
1863 C CG  . HIS   A 94  ? 0.1338 0.1221 0.1407 -0.0093 0.0038  0.0159  94  HIS   A CG  
1864 N ND1 . HIS   A 94  ? 0.1322 0.1222 0.1469 -0.0100 -0.0024 0.0165  94  HIS   A ND1 
1865 C CD2 . HIS   A 94  ? 0.1403 0.1356 0.1575 -0.0116 -0.0005 0.0117  94  HIS   A CD2 
1866 C CE1 . HIS   A 94  ? 0.1352 0.1264 0.1408 -0.0105 -0.0139 0.0197  94  HIS   A CE1 
1867 N NE2 . HIS   A 94  ? 0.1400 0.1347 0.1375 -0.0133 -0.0075 0.0017  94  HIS   A NE2 
1875 N N   . VAL   A 95  ? 0.1231 0.1278 0.1200 -0.0060 0.0016  0.0098  95  VAL   A N   
1876 C CA  . VAL   A 95  ? 0.1364 0.1356 0.0921 -0.0081 0.0133  0.0080  95  VAL   A CA  
1877 C C   . VAL   A 95  ? 0.1351 0.1386 0.0912 -0.0192 0.0132  0.0151  95  VAL   A C   
1878 O O   . VAL   A 95  ? 0.1318 0.1398 0.1361 0.0149  0.0102  0.0057  95  VAL   A O   
1879 C CB  . VAL   A 95  ? 0.1292 0.1413 0.1424 -0.0094 0.0103  0.0078  95  VAL   A CB  
1880 C CG1 . VAL   A 95  ? 0.1477 0.1391 0.1545 -0.0178 0.0090  0.0068  95  VAL   A CG1 
1881 C CG2 . VAL   A 95  ? 0.1392 0.1391 0.1351 -0.0120 0.0170  0.0303  95  VAL   A CG2 
1891 N N   . VAL   A 96  ? 0.1407 0.1230 0.0831 -0.0104 0.0108  0.0163  96  VAL   A N   
1892 C CA  . VAL   A 96  ? 0.1513 0.1300 0.1155 -0.0091 0.0210  0.0197  96  VAL   A CA  
1893 C C   . VAL   A 96  ? 0.1433 0.1450 0.1365 -0.0001 0.0075  0.0156  96  VAL   A C   
1894 O O   . VAL   A 96  ? 0.1497 0.1465 0.1629 -0.0065 0.0259  -0.0026 96  VAL   A O   
1895 C CB  . VAL   A 96  ? 0.1512 0.1383 0.1116 -0.0068 0.0234  0.0195  96  VAL   A CB  
1896 C CG1 . VAL   A 96  ? 0.1604 0.1474 0.1137 -0.0148 0.0196  0.0187  96  VAL   A CG1 
1897 C CG2 . VAL   A 96  ? 0.1429 0.1370 0.1515 -0.0148 0.0176  0.0037  96  VAL   A CG2 
1907 N N   A GLY   A 97  ? 0.1407 0.1443 0.1377 -0.0047 0.0069  0.0081  97  GLY   A N   
1908 N N   B GLY   A 97  ? 0.1451 0.1438 0.1317 -0.0067 0.0147  0.0207  97  GLY   A N   
1909 C CA  A GLY   A 97  ? 0.1473 0.1643 0.1327 0.0006  -0.0063 0.0057  97  GLY   A CA  
1910 C CA  B GLY   A 97  ? 0.1512 0.1505 0.1361 -0.0049 0.0096  0.0251  97  GLY   A CA  
1911 C C   A GLY   A 97  ? 0.1500 0.1735 0.1173 -0.0062 -0.0063 0.0022  97  GLY   A C   
1912 C C   B GLY   A 97  ? 0.1548 0.1483 0.1431 -0.0105 0.0131  0.0327  97  GLY   A C   
1913 O O   A GLY   A 97  ? 0.1601 0.1647 0.1450 -0.0053 0.0018  -0.0081 97  GLY   A O   
1914 O O   B GLY   A 97  ? 0.1531 0.1412 0.1545 -0.0192 0.0190  0.0382  97  GLY   A O   
1921 N N   A PRO   A 98  ? 0.1554 0.1706 0.1095 -0.0104 -0.0108 0.0066  98  PRO   A N   
1922 N N   B PRO   A 98  ? 0.1695 0.1476 0.1548 -0.0025 0.0169  0.0430  98  PRO   A N   
1923 C CA  A PRO   A 98  ? 0.1662 0.1757 0.1201 -0.0092 -0.0027 -0.0000 98  PRO   A CA  
1924 C CA  B PRO   A 98  ? 0.1865 0.1526 0.1727 -0.0048 0.0107  0.0261  98  PRO   A CA  
1925 C C   A PRO   A 98  ? 0.1707 0.1896 0.0985 -0.0193 -0.0015 0.0148  98  PRO   A C   
1926 C C   B PRO   A 98  ? 0.2068 0.1544 0.1645 -0.0021 0.0094  0.0238  98  PRO   A C   
1927 O O   A PRO   A 98  ? 0.1640 0.1677 0.1223 -0.0144 0.0135  0.0080  98  PRO   A O   
1928 O O   B PRO   A 98  ? 0.2059 0.1548 0.1836 0.0011  0.0136  0.0256  98  PRO   A O   
1929 C CB  A PRO   A 98  ? 0.1720 0.1856 0.1216 0.0086  0.0154  -0.0041 98  PRO   A CB  
1930 C CB  B PRO   A 98  ? 0.1865 0.1482 0.1732 0.0045  0.0119  0.0232  98  PRO   A CB  
1931 C CG  A PRO   A 98  ? 0.1717 0.1790 0.1303 0.0032  0.0042  -0.0086 98  PRO   A CG  
1932 C CG  B PRO   A 98  ? 0.1853 0.1468 0.1632 0.0045  0.0121  0.0347  98  PRO   A CG  
1933 C CD  A PRO   A 98  ? 0.1633 0.1697 0.1294 -0.0052 -0.0078 -0.0059 98  PRO   A CD  
1934 C CD  B PRO   A 98  ? 0.1748 0.1402 0.1394 0.0017  0.0077  0.0569  98  PRO   A CD  
1949 N N   A ASN   A 99  ? 0.1750 0.2136 0.0930 -0.0249 0.0048  0.0340  99  ASN   A N   
1950 N N   B ASN   A 99  ? 0.2255 0.1526 0.1451 0.0063  0.0095  0.0375  99  ASN   A N   
1951 C CA  A ASN   A 99  ? 0.1907 0.2310 0.1101 -0.0200 0.0066  0.0432  99  ASN   A CA  
1952 C CA  B ASN   A 99  ? 0.2451 0.1572 0.1438 0.0090  0.0132  0.0396  99  ASN   A CA  
1953 C C   A ASN   A 99  ? 0.2107 0.2667 0.1232 -0.0268 -0.0001 0.0485  99  ASN   A C   
1954 C C   B ASN   A 99  ? 0.2541 0.1660 0.1436 0.0119  0.0034  0.0416  99  ASN   A C   
1955 O O   A ASN   A 99  ? 0.2221 0.2851 0.1568 -0.0194 -0.0068 0.0288  99  ASN   A O   
1956 O O   B ASN   A 99  ? 0.2494 0.1527 0.1337 0.0175  -0.0005 0.0423  99  ASN   A O   
1957 C CB  A ASN   A 99  ? 0.1803 0.2230 0.1282 -0.0155 -0.0125 0.0468  99  ASN   A CB  
1958 C CB  B ASN   A 99  ? 0.2526 0.1574 0.1693 0.0073  0.0176  0.0384  99  ASN   A CB  
1959 C CG  A ASN   A 99  ? 0.1791 0.2216 0.1641 -0.0061 -0.0243 0.0306  99  ASN   A CG  
1960 C CG  B ASN   A 99  ? 0.2600 0.1584 0.1880 0.0127  0.0177  0.0379  99  ASN   A CG  
1961 O OD1 A ASN   A 99  ? 0.1948 0.2272 0.1821 0.0024  -0.0180 0.0158  99  ASN   A OD1 
1962 O OD1 B ASN   A 99  ? 0.2546 0.1547 0.1818 0.0267  0.0134  0.0449  99  ASN   A OD1 
1963 N ND2 A ASN   A 99  ? 0.1869 0.2158 0.1936 0.0009  -0.0212 0.0486  99  ASN   A ND2 
1964 N ND2 B ASN   A 99  ? 0.2661 0.1665 0.2296 0.0110  0.0101  0.0225  99  ASN   A ND2 
1977 N N   A VAL   A 100 ? 0.2267 0.2808 0.1091 -0.0480 -0.0189 0.0457  100 VAL   A N   
1978 N N   B VAL   A 100 ? 0.2741 0.2039 0.2000 0.0110  0.0079  0.0324  100 VAL   A N   
1979 C CA  A VAL   A 100 ? 0.2523 0.3085 0.1332 -0.0545 -0.0289 0.0482  100 VAL   A CA  
1980 C CA  B VAL   A 100 ? 0.2978 0.2358 0.2419 0.0119  0.0005  0.0213  100 VAL   A CA  
1981 C C   A VAL   A 100 ? 0.2715 0.3347 0.1498 -0.0618 -0.0444 0.0764  100 VAL   A C   
1982 C C   B VAL   A 100 ? 0.3129 0.2587 0.2558 0.0180  -0.0083 0.0176  100 VAL   A C   
1983 O O   A VAL   A 100 ? 0.2811 0.3478 0.1820 -0.0625 -0.0370 0.0841  100 VAL   A O   
1984 O O   B VAL   A 100 ? 0.3132 0.2633 0.2530 0.0197  -0.0241 0.0189  100 VAL   A O   
1985 C CB  A VAL   A 100 ? 0.2641 0.3069 0.1625 -0.0541 -0.0324 0.0302  100 VAL   A CB  
1986 C CB  B VAL   A 100 ? 0.3074 0.2450 0.2734 0.0037  0.0018  0.0160  100 VAL   A CB  
1987 C CG1 A VAL   A 100 ? 0.2679 0.3136 0.1999 -0.0544 -0.0132 0.0201  100 VAL   A CG1 
1988 C CG1 B VAL   A 100 ? 0.3087 0.2450 0.2878 -0.0002 -0.0041 0.0102  100 VAL   A CG1 
1989 C CG2 A VAL   A 100 ? 0.2742 0.3083 0.1443 -0.0556 -0.0284 0.0343  100 VAL   A CG2 
1990 C CG2 B VAL   A 100 ? 0.3137 0.2512 0.2933 0.0041  0.0078  0.0144  100 VAL   A CG2 
2009 N N   A ASN   A 101 ? 0.2803 0.3382 0.1720 -0.0747 -0.0615 0.1060  101 ASN   A N   
2010 N N   B ASN   A 101 ? 0.3264 0.2792 0.2678 0.0227  -0.0072 0.0145  101 ASN   A N   
2011 C CA  A ASN   A 101 ? 0.3066 0.3505 0.2033 -0.0782 -0.0692 0.1179  101 ASN   A CA  
2012 C CA  B ASN   A 101 ? 0.3400 0.2988 0.2831 0.0307  -0.0092 0.0175  101 ASN   A CA  
2013 C C   A ASN   A 101 ? 0.3315 0.3752 0.2207 -0.0744 -0.0293 0.1460  101 ASN   A C   
2014 C C   B ASN   A 101 ? 0.3507 0.3025 0.2841 0.0270  -0.0099 0.0207  101 ASN   A C   
2015 O O   A ASN   A 101 ? 0.3476 0.3826 0.2725 -0.0674 -0.0270 0.1321  101 ASN   A O   
2016 O O   B ASN   A 101 ? 0.3538 0.3032 0.2784 0.0255  -0.0147 0.0250  101 ASN   A O   
2017 C CB  A ASN   A 101 ? 0.3065 0.3300 0.1975 -0.0827 -0.1049 0.1016  101 ASN   A CB  
2018 C CB  B ASN   A 101 ? 0.3450 0.3120 0.3002 0.0368  -0.0109 0.0140  101 ASN   A CB  
2019 C CG  A ASN   A 101 ? 0.3154 0.3188 0.2056 -0.0971 -0.1073 0.0774  101 ASN   A CG  
2020 C CG  B ASN   A 101 ? 0.3481 0.3208 0.3155 0.0444  -0.0120 0.0101  101 ASN   A CG  
2021 O OD1 A ASN   A 101 ? 0.3139 0.3311 0.2202 -0.0837 -0.1114 0.0460  101 ASN   A OD1 
2022 O OD1 B ASN   A 101 ? 0.3458 0.3239 0.3250 0.0472  -0.0187 0.0084  101 ASN   A OD1 
2023 N ND2 A ASN   A 101 ? 0.3214 0.3086 0.2196 -0.1034 -0.1027 0.0748  101 ASN   A ND2 
2024 N ND2 B ASN   A 101 ? 0.3538 0.3257 0.3191 0.0448  -0.0102 0.0097  101 ASN   A ND2 
2037 N N   A LYS   A 102 ? 0.3362 0.3995 0.2475 -0.0809 -0.0017 0.1393  102 LYS   A N   
2038 N N   B LYS   A 102 ? 0.3541 0.3065 0.3031 0.0297  -0.0042 0.0165  102 LYS   A N   
2039 C CA  A LYS   A 102 ? 0.3516 0.4236 0.2621 -0.0755 -0.0071 0.1200  102 LYS   A CA  
2040 C CA  B LYS   A 102 ? 0.3579 0.3143 0.2978 0.0263  0.0038  0.0196  102 LYS   A CA  
2041 C C   A LYS   A 102 ? 0.3647 0.4461 0.2507 -0.0582 -0.0064 0.1012  102 LYS   A C   
2042 C C   B LYS   A 102 ? 0.3483 0.3048 0.2665 0.0341  0.0112  0.0316  102 LYS   A C   
2043 O O   A LYS   A 102 ? 0.3701 0.4596 0.2684 -0.0482 -0.0124 0.0896  102 LYS   A O   
2044 O O   B LYS   A 102 ? 0.3520 0.3026 0.2647 0.0358  0.0200  0.0437  102 LYS   A O   
2045 C CB  A LYS   A 102 ? 0.3601 0.4277 0.3156 -0.0829 -0.0254 0.0985  102 LYS   A CB  
2046 C CB  B LYS   A 102 ? 0.3684 0.3289 0.3298 0.0205  -0.0038 0.0095  102 LYS   A CB  
2047 C CG  A LYS   A 102 ? 0.3654 0.4320 0.3572 -0.0884 -0.0417 0.0723  102 LYS   A CG  
2048 C CG  B LYS   A 102 ? 0.3790 0.3431 0.3622 0.0145  -0.0109 0.0020  102 LYS   A CG  
2049 C CD  A LYS   A 102 ? 0.3760 0.4369 0.4012 -0.0907 -0.0524 0.0470  102 LYS   A CD  
2050 C CD  B LYS   A 102 ? 0.3886 0.3570 0.4002 0.0114  -0.0149 -0.0049 102 LYS   A CD  
2051 C CE  A LYS   A 102 ? 0.3869 0.4418 0.4365 -0.0892 -0.0586 0.0296  102 LYS   A CE  
2052 C CE  B LYS   A 102 ? 0.3969 0.3680 0.4297 0.0103  -0.0174 -0.0071 102 LYS   A CE  
2053 N NZ  A LYS   A 102 ? 0.3935 0.4441 0.4537 -0.0945 -0.0601 0.0159  102 LYS   A NZ  
2054 N NZ  B LYS   A 102 ? 0.4031 0.3743 0.4491 0.0092  -0.0172 -0.0086 102 LYS   A NZ  
2081 N N   A GLY   A 103 ? 0.3658 0.4595 0.2567 -0.0456 -0.0055 0.0719  103 GLY   A N   
2082 N N   B GLY   A 103 ? 0.3350 0.2992 0.2423 0.0443  0.0071  0.0164  103 GLY   A N   
2083 C CA  A GLY   A 103 ? 0.3695 0.4665 0.2578 -0.0335 0.0075  0.0490  103 GLY   A CA  
2084 C CA  B GLY   A 103 ? 0.3183 0.2921 0.2427 0.0543  0.0041  0.0153  103 GLY   A CA  
2085 C C   A GLY   A 103 ? 0.3656 0.4732 0.2604 -0.0282 0.0253  0.0298  103 GLY   A C   
2086 C C   B GLY   A 103 ? 0.3024 0.2835 0.2463 0.0597  -0.0026 0.0138  103 GLY   A C   
2087 O O   A GLY   A 103 ? 0.3786 0.4831 0.2920 -0.0207 0.0294  0.0195  103 GLY   A O   
2088 O O   B GLY   A 103 ? 0.3069 0.2898 0.2582 0.0670  -0.0093 -0.0019 103 GLY   A O   
2095 N N   A GLU   A 104 ? 0.3430 0.4651 0.2178 -0.0381 0.0383  0.0173  104 GLU   A N   
2096 N N   B GLU   A 104 ? 0.2757 0.2625 0.2242 0.0566  -0.0101 0.0365  104 GLU   A N   
2097 C CA  A GLU   A 104 ? 0.3190 0.4517 0.2005 -0.0506 0.0383  0.0072  104 GLU   A CA  
2098 C CA  B GLU   A 104 ? 0.2545 0.2513 0.1978 0.0427  -0.0020 0.0449  104 GLU   A CA  
2099 C C   A GLU   A 104 ? 0.3226 0.4530 0.2034 -0.0511 0.0332  -0.0157 104 GLU   A C   
2100 C C   B GLU   A 104 ? 0.2357 0.2443 0.1799 0.0412  -0.0074 0.0401  104 GLU   A C   
2101 O O   A GLU   A 104 ? 0.3188 0.4535 0.2125 -0.0558 0.0264  -0.0245 104 GLU   A O   
2102 O O   B GLU   A 104 ? 0.2324 0.2405 0.1940 0.0361  -0.0031 0.0347  104 GLU   A O   
2103 C CB  A GLU   A 104 ? 0.2855 0.4352 0.1724 -0.0604 0.0430  0.0268  104 GLU   A CB  
2104 C CB  B GLU   A 104 ? 0.2565 0.2428 0.1956 0.0280  0.0114  0.0651  104 GLU   A CB  
2105 C CG  A GLU   A 104 ? 0.2619 0.4163 0.1718 -0.0651 0.0259  0.0392  104 GLU   A CG  
2106 C CG  B GLU   A 104 ? 0.2631 0.2415 0.1983 0.0172  0.0173  0.0709  104 GLU   A CG  
2107 C CD  A GLU   A 104 ? 0.2304 0.3975 0.1582 -0.0710 0.0096  0.0546  104 GLU   A CD  
2108 C CD  B GLU   A 104 ? 0.2712 0.2406 0.1958 0.0126  0.0122  0.0715  104 GLU   A CD  
2109 O OE1 A GLU   A 104 ? 0.2064 0.3778 0.1198 -0.0724 -0.0169 0.0616  104 GLU   A OE1 
2110 O OE1 B GLU   A 104 ? 0.2784 0.2490 0.2125 0.0148  0.0171  0.0538  104 GLU   A OE1 
2111 O OE2 A GLU   A 104 ? 0.2450 0.3920 0.1901 -0.0678 0.0098  0.0720  104 GLU   A OE2 
2112 O OE2 B GLU   A 104 ? 0.2760 0.2372 0.1779 0.0080  0.0167  0.0809  104 GLU   A OE2 
2125 N N   A ASP   A 105 ? 0.3263 0.4525 0.2179 -0.0449 0.0347  -0.0332 105 ASP   A N   
2126 N N   B ASP   A 105 ? 0.2311 0.2385 0.1824 0.0353  -0.0172 0.0293  105 ASP   A N   
2127 C CA  A ASP   A 105 ? 0.3258 0.4516 0.2562 -0.0344 0.0393  -0.0630 105 ASP   A CA  
2128 C CA  B ASP   A 105 ? 0.2310 0.2345 0.2060 0.0357  -0.0051 0.0052  105 ASP   A CA  
2129 C C   A ASP   A 105 ? 0.2916 0.4363 0.2323 -0.0447 0.0326  -0.0907 105 ASP   A C   
2130 C C   B ASP   A 105 ? 0.2264 0.2184 0.1798 0.0214  -0.0062 -0.0002 105 ASP   A C   
2131 O O   A ASP   A 105 ? 0.2846 0.4373 0.2084 -0.0479 0.0406  -0.1162 105 ASP   A O   
2132 O O   B ASP   A 105 ? 0.2104 0.1885 0.1234 0.0264  -0.0036 0.0080  105 ASP   A O   
2133 C CB  A ASP   A 105 ? 0.3528 0.4621 0.3105 -0.0160 0.0458  -0.0676 105 ASP   A CB  
2134 C CB  B ASP   A 105 ? 0.2343 0.2485 0.2518 0.0499  0.0053  -0.0193 105 ASP   A CB  
2135 C CG  A ASP   A 105 ? 0.3758 0.4704 0.3619 -0.0007 0.0457  -0.0804 105 ASP   A CG  
2136 C CG  B ASP   A 105 ? 0.2430 0.2630 0.2958 0.0585  0.0142  -0.0415 105 ASP   A CG  
2137 O OD1 A ASP   A 105 ? 0.3831 0.4758 0.3717 0.0014  0.0423  -0.0924 105 ASP   A OD1 
2138 O OD1 B ASP   A 105 ? 0.2455 0.2656 0.2898 0.0581  0.0065  -0.0533 105 ASP   A OD1 
2139 O OD2 A ASP   A 105 ? 0.3893 0.4736 0.4022 0.0077  0.0468  -0.0758 105 ASP   A OD2 
2140 O OD2 B ASP   A 105 ? 0.2445 0.2686 0.3264 0.0676  0.0284  -0.0471 105 ASP   A OD2 
2149 N N   A ILE   A 106 ? 0.2646 0.4155 0.2399 -0.0520 0.0093  -0.1008 106 ILE   A N   
2150 N N   B ILE   A 106 ? 0.2378 0.2433 0.2176 0.0117  -0.0126 -0.0057 106 ILE   A N   
2151 C CA  A ILE   A 106 ? 0.2361 0.3921 0.2413 -0.0638 -0.0140 -0.1110 106 ILE   A CA  
2152 C CA  B ILE   A 106 ? 0.2486 0.2570 0.2533 0.0014  -0.0197 -0.0117 106 ILE   A CA  
2153 C C   A ILE   A 106 ? 0.2185 0.3626 0.2463 -0.0803 -0.0064 -0.1275 106 ILE   A C   
2154 C C   B ILE   A 106 ? 0.2621 0.2501 0.2539 0.0023  -0.0121 0.0034  106 ILE   A C   
2155 O O   A ILE   A 106 ? 0.1974 0.3468 0.2652 -0.0857 0.0182  -0.1225 106 ILE   A O   
2156 O O   B ILE   A 106 ? 0.2614 0.2522 0.2615 -0.0001 -0.0058 0.0083  106 ILE   A O   
2157 C CB  A ILE   A 106 ? 0.2365 0.4024 0.2754 -0.0505 -0.0366 -0.0828 106 ILE   A CB  
2158 C CB  B ILE   A 106 ? 0.2520 0.2794 0.2830 -0.0094 -0.0328 -0.0317 106 ILE   A CB  
2159 C CG1 A ILE   A 106 ? 0.2287 0.4046 0.3106 -0.0380 -0.0427 -0.0570 106 ILE   A CG1 
2160 C CG1 B ILE   A 106 ? 0.2521 0.2878 0.3009 -0.0132 -0.0348 -0.0425 106 ILE   A CG1 
2161 C CG2 A ILE   A 106 ? 0.2451 0.4074 0.2935 -0.0434 -0.0407 -0.0777 106 ILE   A CG2 
2162 C CG2 B ILE   A 106 ? 0.2568 0.2859 0.2871 -0.0132 -0.0382 -0.0410 106 ILE   A CG2 
2163 C CD1 A ILE   A 106 ? 0.2274 0.4038 0.3215 -0.0274 -0.0486 -0.0495 106 ILE   A CD1 
2164 C CD1 B ILE   A 106 ? 0.2499 0.2935 0.3203 -0.0173 -0.0332 -0.0459 106 ILE   A CD1 
2187 N N   A GLN   A 107 ? 0.2342 0.3466 0.2762 -0.0770 -0.0032 -0.1415 107 GLN   A N   
2188 N N   B GLN   A 107 ? 0.2733 0.2388 0.2618 0.0088  -0.0070 0.0107  107 GLN   A N   
2189 C CA  A GLN   A 107 ? 0.2641 0.3283 0.3520 -0.0654 0.0170  -0.1251 107 GLN   A CA  
2190 C CA  B GLN   A 107 ? 0.2885 0.2397 0.2951 0.0075  -0.0061 0.0213  107 GLN   A CA  
2191 C C   A GLN   A 107 ? 0.2351 0.2765 0.3405 -0.0570 0.0453  -0.0999 107 GLN   A C   
2192 C C   B GLN   A 107 ? 0.2660 0.2050 0.2644 0.0062  0.0062  0.0274  107 GLN   A C   
2193 O O   A GLN   A 107 ? 0.2414 0.2760 0.4085 -0.0583 0.0510  -0.1000 107 GLN   A O   
2194 O O   B GLN   A 107 ? 0.2715 0.2005 0.2606 0.0030  -0.0061 0.0224  107 GLN   A O   
2195 C CB  A GLN   A 107 ? 0.3173 0.3625 0.4362 -0.0665 0.0018  -0.1246 107 GLN   A CB  
2196 C CB  B GLN   A 107 ? 0.3212 0.2819 0.3538 0.0003  -0.0166 0.0103  107 GLN   A CB  
2197 C CG  A GLN   A 107 ? 0.3722 0.3992 0.5355 -0.0655 -0.0076 -0.1124 107 GLN   A CG  
2198 C CG  B GLN   A 107 ? 0.3524 0.3266 0.4128 -0.0037 -0.0280 0.0101  107 GLN   A CG  
2199 C CD  A GLN   A 107 ? 0.4164 0.4241 0.6206 -0.0623 -0.0102 -0.0958 107 GLN   A CD  
2200 C CD  B GLN   A 107 ? 0.3750 0.3567 0.4633 -0.0060 -0.0373 0.0131  107 GLN   A CD  
2201 O OE1 A GLN   A 107 ? 0.4292 0.4363 0.6578 -0.0583 -0.0098 -0.0874 107 GLN   A OE1 
2202 O OE1 B GLN   A 107 ? 0.3828 0.3660 0.4803 -0.0055 -0.0427 0.0167  107 GLN   A OE1 
2203 N NE2 A GLN   A 107 ? 0.4311 0.4326 0.6478 -0.0620 -0.0135 -0.0946 107 GLN   A NE2 
2204 N NE2 B GLN   A 107 ? 0.3818 0.3635 0.4774 -0.0072 -0.0403 0.0106  107 GLN   A NE2 
2221 N N   A LEU   A 108 ? 0.2044 0.2319 0.2644 -0.0553 0.0607  -0.0845 108 LEU   A N   
2222 N N   B LEU   A 108 ? 0.2417 0.1900 0.2370 0.0019  0.0225  0.0275  108 LEU   A N   
2223 C CA  A LEU   A 108 ? 0.1937 0.1987 0.2322 -0.0344 0.0510  -0.0428 108 LEU   A CA  
2224 C CA  B LEU   A 108 ? 0.2199 0.1810 0.2196 0.0053  0.0284  0.0174  108 LEU   A CA  
2225 C C   A LEU   A 108 ? 0.1698 0.1591 0.2162 -0.0127 0.0366  -0.0119 108 LEU   A C   
2226 C C   B LEU   A 108 ? 0.1904 0.1631 0.2096 0.0066  0.0273  0.0110  108 LEU   A C   
2227 O O   A LEU   A 108 ? 0.1729 0.1528 0.2265 -0.0041 0.0343  -0.0077 108 LEU   A O   
2228 O O   B LEU   A 108 ? 0.1941 0.1658 0.2137 0.0134  0.0287  0.0069  108 LEU   A O   
2229 C CB  A LEU   A 108 ? 0.2000 0.2156 0.2237 -0.0386 0.0555  -0.0439 108 LEU   A CB  
2230 C CB  B LEU   A 108 ? 0.2235 0.1965 0.2090 0.0057  0.0329  0.0037  108 LEU   A CB  
2231 C CG  A LEU   A 108 ? 0.2122 0.2330 0.2585 -0.0384 0.0548  -0.0480 108 LEU   A CG  
2232 C CG  B LEU   A 108 ? 0.2280 0.2081 0.2187 0.0100  0.0337  -0.0059 108 LEU   A CG  
2233 C CD1 A LEU   A 108 ? 0.2179 0.2398 0.2741 -0.0500 0.0581  -0.0484 108 LEU   A CD1 
2234 C CD1 B LEU   A 108 ? 0.2344 0.2138 0.2210 0.0108  0.0368  -0.0065 108 LEU   A CD1 
2235 C CD2 A LEU   A 108 ? 0.2168 0.2459 0.2951 -0.0335 0.0470  -0.0386 108 LEU   A CD2 
2236 C CD2 B LEU   A 108 ? 0.2259 0.2134 0.2310 0.0129  0.0276  -0.0091 108 LEU   A CD2 
2259 N N   . LEU   A 109 ? 0.1616 0.1534 0.2083 0.0027  0.0317  0.0053  109 LEU   A N   
2260 C CA  . LEU   A 109 ? 0.1585 0.1523 0.1891 0.0008  0.0061  0.0107  109 LEU   A CA  
2261 C C   . LEU   A 109 ? 0.1460 0.1445 0.1808 -0.0073 0.0114  0.0050  109 LEU   A C   
2262 O O   . LEU   A 109 ? 0.1549 0.1366 0.2053 -0.0048 0.0072  -0.0009 109 LEU   A O   
2263 C CB  . LEU   A 109 ? 0.1576 0.1594 0.2176 0.0107  0.0032  0.0167  109 LEU   A CB  
2264 C CG  . LEU   A 109 ? 0.1525 0.1680 0.2406 0.0038  0.0152  0.0331  109 LEU   A CG  
2265 C CD1 . LEU   A 109 ? 0.1608 0.1569 0.2417 -0.0027 0.0236  0.0171  109 LEU   A CD1 
2266 C CD2 . LEU   A 109 ? 0.1488 0.1921 0.2677 0.0038  0.0080  0.0277  109 LEU   A CD2 
2279 N N   . LYS   A 110 ? 0.1483 0.1462 0.1910 -0.0033 0.0040  0.0031  110 LYS   A N   
2280 C CA  . LYS   A 110 ? 0.1500 0.1411 0.2051 -0.0047 -0.0094 0.0066  110 LYS   A CA  
2281 C C   . LYS   A 110 ? 0.1481 0.1303 0.1787 -0.0083 0.0047  0.0039  110 LYS   A C   
2282 O O   . LYS   A 110 ? 0.1395 0.1313 0.1992 -0.0037 0.0100  -0.0037 110 LYS   A O   
2283 C CB  . LYS   A 110 ? 0.1554 0.1422 0.2389 -0.0043 -0.0227 -0.0092 110 LYS   A CB  
2284 C CG  . LYS   A 110 ? 0.1499 0.1458 0.2445 0.0026  -0.0176 -0.0049 110 LYS   A CG  
2285 C CD  . LYS   A 110 ? 0.1548 0.1582 0.2533 -0.0094 0.0019  -0.0139 110 LYS   A CD  
2286 C CE  . LYS   A 110 ? 0.1651 0.1601 0.2644 -0.0078 0.0098  -0.0029 110 LYS   A CE  
2287 N NZ  . LYS   A 110 ? 0.1642 0.1486 0.2691 -0.0150 0.0131  0.0124  110 LYS   A NZ  
2301 N N   . SER   A 111 ? 0.1512 0.1314 0.1873 0.0016  0.0021  0.0094  111 SER   A N   
2302 C CA  . SER   A 111 ? 0.1437 0.1445 0.1801 -0.0020 0.0126  -0.0058 111 SER   A CA  
2303 C C   . SER   A 111 ? 0.1402 0.1322 0.1828 -0.0087 0.0135  0.0064  111 SER   A C   
2304 O O   . SER   A 111 ? 0.1496 0.1292 0.2197 -0.0063 0.0159  0.0015  111 SER   A O   
2305 C CB  . SER   A 111 ? 0.1645 0.1687 0.1874 -0.0005 0.0276  -0.0161 111 SER   A CB  
2306 O OG  . SER   A 111 ? 0.2013 0.1879 0.2065 0.0129  0.0199  -0.0205 111 SER   A OG  
2312 N N   . ALA   A 112 ? 0.1466 0.1316 0.1895 -0.0006 0.0196  -0.0000 112 ALA   A N   
2313 C CA  . ALA   A 112 ? 0.1466 0.1324 0.1716 -0.0010 0.0272  -0.0080 112 ALA   A CA  
2314 C C   . ALA   A 112 ? 0.1345 0.1239 0.1773 0.0043  0.0122  -0.0036 112 ALA   A C   
2315 O O   . ALA   A 112 ? 0.1340 0.1271 0.2012 -0.0106 0.0150  0.0148  112 ALA   A O   
2316 C CB  . ALA   A 112 ? 0.1619 0.1334 0.1779 -0.0024 0.0152  0.0163  112 ALA   A CB  
2322 N N   . TYR   A 113 ? 0.1258 0.1303 0.1927 -0.0055 0.0103  0.0167  113 TYR   A N   
2323 C CA  . TYR   A 113 ? 0.1266 0.1298 0.1816 -0.0022 0.0190  0.0195  113 TYR   A CA  
2324 C C   . TYR   A 113 ? 0.1267 0.1280 0.1777 -0.0078 0.0202  0.0107  113 TYR   A C   
2325 O O   . TYR   A 113 ? 0.1330 0.1275 0.1952 -0.0030 0.0219  0.0037  113 TYR   A O   
2326 C CB  . TYR   A 113 ? 0.1311 0.1402 0.1884 -0.0001 0.0110  0.0222  113 TYR   A CB  
2327 C CG  . TYR   A 113 ? 0.1314 0.1441 0.1584 -0.0116 0.0178  0.0288  113 TYR   A CG  
2328 C CD1 . TYR   A 113 ? 0.1340 0.1619 0.1612 -0.0002 0.0195  0.0205  113 TYR   A CD1 
2329 C CD2 . TYR   A 113 ? 0.1398 0.1504 0.1705 -0.0179 0.0074  0.0253  113 TYR   A CD2 
2330 C CE1 . TYR   A 113 ? 0.1471 0.1758 0.1722 0.0005  0.0226  0.0114  113 TYR   A CE1 
2331 C CE2 . TYR   A 113 ? 0.1357 0.1558 0.1840 -0.0082 0.0030  0.0269  113 TYR   A CE2 
2332 C CZ  . TYR   A 113 ? 0.1420 0.1649 0.1724 0.0031  0.0158  0.0242  113 TYR   A CZ  
2333 O OH  . TYR   A 113 ? 0.1363 0.1684 0.2093 0.0144  0.0141  0.0289  113 TYR   A OH  
2343 N N   . GLU   A 114 ? 0.1247 0.1282 0.1880 -0.0018 0.0118  0.0203  114 GLU   A N   
2344 C CA  . GLU   A 114 ? 0.1260 0.1277 0.2043 0.0037  0.0202  0.0203  114 GLU   A CA  
2345 C C   . GLU   A 114 ? 0.1295 0.1231 0.1878 -0.0038 0.0118  0.0229  114 GLU   A C   
2346 O O   . GLU   A 114 ? 0.1443 0.1202 0.1931 -0.0010 0.0049  0.0124  114 GLU   A O   
2347 C CB  . GLU   A 114 ? 0.1269 0.1305 0.1975 -0.0088 0.0163  0.0183  114 GLU   A CB  
2348 C CG  . GLU   A 114 ? 0.1428 0.1332 0.2122 0.0012  0.0150  0.0067  114 GLU   A CG  
2349 C CD  . GLU   A 114 ? 0.1548 0.1342 0.2249 -0.0027 0.0092  0.0060  114 GLU   A CD  
2350 O OE1 . GLU   A 114 ? 0.1485 0.1291 0.2452 -0.0102 0.0163  -0.0039 114 GLU   A OE1 
2351 O OE2 . GLU   A 114 ? 0.1680 0.1444 0.2365 -0.0059 0.0173  -0.0211 114 GLU   A OE2 
2358 N N   . ASN   A 115 ? 0.1217 0.1306 0.1860 -0.0065 0.0089  0.0183  115 ASN   A N   
2359 C CA  . ASN   A 115 ? 0.1300 0.1415 0.1999 -0.0125 0.0137  0.0181  115 ASN   A CA  
2360 C C   . ASN   A 115 ? 0.1363 0.1353 0.1898 -0.0129 0.0055  0.0091  115 ASN   A C   
2361 O O   . ASN   A 115 ? 0.1387 0.1378 0.1956 -0.0096 0.0250  0.0117  115 ASN   A O   
2362 C CB  . ASN   A 115 ? 0.1382 0.1411 0.1912 -0.0141 0.0209  0.0158  115 ASN   A CB  
2363 C CG  . ASN   A 115 ? 0.1425 0.1569 0.1985 -0.0155 0.0252  0.0071  115 ASN   A CG  
2364 O OD1 . ASN   A 115 ? 0.1458 0.2490 0.2236 -0.0142 0.0299  0.0254  115 ASN   A OD1 
2365 N ND2 . ASN   A 115 ? 0.1373 0.1362 0.1977 -0.0121 0.0274  0.0064  115 ASN   A ND2 
2372 N N   . PHE   A 116 ? 0.1292 0.1284 0.1995 -0.0037 0.0147  0.0304  116 PHE   A N   
2373 C CA  . PHE   A 116 ? 0.1366 0.1352 0.1796 -0.0036 0.0199  0.0226  116 PHE   A CA  
2374 C C   . PHE   A 116 ? 0.1316 0.1464 0.1737 -0.0091 0.0215  0.0165  116 PHE   A C   
2375 O O   . PHE   A 116 ? 0.1390 0.1443 0.1919 0.0038  0.0212  0.0312  116 PHE   A O   
2376 C CB  . PHE   A 116 ? 0.1276 0.1318 0.1923 -0.0017 0.0285  0.0220  116 PHE   A CB  
2377 C CG  . PHE   A 116 ? 0.1352 0.1266 0.1873 0.0003  0.0210  0.0212  116 PHE   A CG  
2378 C CD1 . PHE   A 116 ? 0.1429 0.1267 0.1818 0.0008  0.0241  0.0112  116 PHE   A CD1 
2379 C CD2 . PHE   A 116 ? 0.1326 0.1391 0.1923 -0.0032 0.0173  0.0170  116 PHE   A CD2 
2380 C CE1 . PHE   A 116 ? 0.1434 0.1325 0.2058 -0.0192 0.0117  0.0109  116 PHE   A CE1 
2381 C CE2 . PHE   A 116 ? 0.1343 0.1395 0.2034 -0.0007 0.0343  0.0104  116 PHE   A CE2 
2382 C CZ  . PHE   A 116 ? 0.1458 0.1288 0.1995 -0.0058 0.0178  0.0105  116 PHE   A CZ  
2392 N N   . ASN   A 117 ? 0.1308 0.1424 0.1832 -0.0096 0.0180  0.0250  117 ASN   A N   
2393 C CA  . ASN   A 117 ? 0.1390 0.1412 0.1938 -0.0053 0.0148  0.0274  117 ASN   A CA  
2394 C C   . ASN   A 117 ? 0.1418 0.1434 0.2164 -0.0056 0.0205  0.0211  117 ASN   A C   
2395 O O   . ASN   A 117 ? 0.1492 0.1505 0.2318 -0.0031 0.0102  0.0425  117 ASN   A O   
2396 C CB  . ASN   A 117 ? 0.1392 0.1410 0.2163 -0.0056 0.0122  0.0287  117 ASN   A CB  
2397 C CG  . ASN   A 117 ? 0.1311 0.1383 0.2443 -0.0056 0.0118  0.0255  117 ASN   A CG  
2398 O OD1 . ASN   A 117 ? 0.1326 0.1610 0.2437 -0.0100 0.0180  0.0255  117 ASN   A OD1 
2399 N ND2 . ASN   A 117 ? 0.1297 0.1336 0.2342 -0.0067 0.0126  0.0319  117 ASN   A ND2 
2406 N N   . GLN   A 118 ? 0.1389 0.1442 0.2284 -0.0047 0.0140  0.0282  118 GLN   A N   
2407 C CA  . GLN   A 118 ? 0.1475 0.1562 0.2225 -0.0113 0.0045  0.0326  118 GLN   A CA  
2408 C C   . GLN   A 118 ? 0.1432 0.1641 0.2020 -0.0103 -0.0000 0.0352  118 GLN   A C   
2409 O O   . GLN   A 118 ? 0.1417 0.1942 0.2251 -0.0043 -0.0040 0.0078  118 GLN   A O   
2410 C CB  . GLN   A 118 ? 0.1413 0.1513 0.2450 -0.0040 0.0161  0.0263  118 GLN   A CB  
2411 C CG  . GLN   A 118 ? 0.1280 0.1517 0.2478 -0.0028 0.0136  0.0275  118 GLN   A CG  
2412 C CD  . GLN   A 118 ? 0.1289 0.1606 0.2434 -0.0036 0.0139  0.0264  118 GLN   A CD  
2413 O OE1 . GLN   A 118 ? 0.1337 0.1753 0.2746 0.0054  -0.0009 0.0082  118 GLN   A OE1 
2414 N NE2 . GLN   A 118 ? 0.1494 0.1604 0.2449 0.0046  0.0098  0.0339  118 GLN   A NE2 
2423 N N   . HIS   A 119 ? 0.1462 0.1538 0.1938 -0.0039 0.0075  0.0406  119 HIS   A N   
2424 C CA  . HIS   A 119 ? 0.1536 0.1638 0.2011 -0.0030 0.0078  0.0416  119 HIS   A CA  
2425 C C   . HIS   A 119 ? 0.1665 0.1694 0.1969 -0.0084 0.0156  0.0529  119 HIS   A C   
2426 O O   . HIS   A 119 ? 0.1629 0.1773 0.2115 -0.0263 -0.0053 0.0496  119 HIS   A O   
2427 C CB  . HIS   A 119 ? 0.1570 0.1588 0.2178 -0.0039 0.0191  0.0245  119 HIS   A CB  
2428 C CG  . HIS   A 119 ? 0.1598 0.1641 0.2409 -0.0080 0.0150  0.0336  119 HIS   A CG  
2429 N ND1 . HIS   A 119 ? 0.1780 0.1874 0.2857 -0.0110 0.0204  0.0347  119 HIS   A ND1 
2430 C CD2 . HIS   A 119 ? 0.1675 0.1704 0.2549 0.0073  0.0328  0.0513  119 HIS   A CD2 
2431 C CE1 . HIS   A 119 ? 0.1726 0.1816 0.2901 -0.0128 0.0325  0.0552  119 HIS   A CE1 
2432 N NE2 . HIS   A 119 ? 0.1735 0.1750 0.2919 -0.0002 0.0391  0.0656  119 HIS   A NE2 
2440 N N   . GLU   A 120 ? 0.1742 0.1914 0.2109 -0.0072 0.0039  0.0751  120 GLU   A N   
2441 C CA  . GLU   A 120 ? 0.1907 0.2211 0.2399 0.0043  0.0018  0.1138  120 GLU   A CA  
2442 C C   . GLU   A 120 ? 0.1682 0.2135 0.2070 -0.0071 0.0081  0.1012  120 GLU   A C   
2443 O O   . GLU   A 120 ? 0.1642 0.2142 0.2373 -0.0148 0.0028  0.0894  120 GLU   A O   
2444 C CB  . GLU   A 120 ? 0.2457 0.2793 0.2853 0.0161  -0.0005 0.1673  120 GLU   A CB  
2445 C CG  . GLU   A 120 ? 0.3235 0.3347 0.3986 0.0289  -0.0108 0.1555  120 GLU   A CG  
2446 C CD  . GLU   A 120 ? 0.3943 0.3872 0.4940 0.0391  -0.0161 0.1515  120 GLU   A CD  
2447 O OE1 . GLU   A 120 ? 0.4209 0.4151 0.5068 0.0393  -0.0167 0.1442  120 GLU   A OE1 
2448 O OE2 . GLU   A 120 ? 0.4253 0.3969 0.5464 0.0368  -0.0181 0.1527  120 GLU   A OE2 
2455 N N   . VAL   A 121 ? 0.1646 0.2096 0.1894 -0.0044 0.0149  0.0710  121 VAL   A N   
2456 C CA  . VAL   A 121 ? 0.1746 0.2207 0.1749 -0.0053 0.0311  0.0709  121 VAL   A CA  
2457 C C   . VAL   A 121 ? 0.1667 0.1961 0.1604 -0.0168 0.0220  0.0581  121 VAL   A C   
2458 O O   . VAL   A 121 ? 0.1784 0.1970 0.1728 -0.0344 0.0002  0.0417  121 VAL   A O   
2459 C CB  . VAL   A 121 ? 0.2099 0.2718 0.2088 0.0066  0.0457  0.0791  121 VAL   A CB  
2460 C CG1 . VAL   A 121 ? 0.2073 0.2929 0.2081 0.0097  0.0570  0.0735  121 VAL   A CG1 
2461 C CG2 . VAL   A 121 ? 0.2359 0.2936 0.2597 -0.0088 0.0505  0.0658  121 VAL   A CG2 
2471 N N   . LEU   A 122 ? 0.1570 0.1706 0.1624 -0.0149 0.0091  0.0526  122 LEU   A N   
2472 C CA  . LEU   A 122 ? 0.1596 0.1549 0.1628 -0.0181 0.0258  0.0540  122 LEU   A CA  
2473 C C   . LEU   A 122 ? 0.1577 0.1602 0.1726 -0.0212 0.0131  0.0440  122 LEU   A C   
2474 O O   . LEU   A 122 ? 0.1551 0.1722 0.1940 -0.0292 0.0079  0.0436  122 LEU   A O   
2475 C CB  . LEU   A 122 ? 0.1828 0.1630 0.1944 -0.0144 0.0138  0.0507  122 LEU   A CB  
2476 C CG  . LEU   A 122 ? 0.1749 0.1644 0.2011 -0.0149 0.0215  0.0316  122 LEU   A CG  
2477 C CD1 . LEU   A 122 ? 0.1948 0.1720 0.2013 -0.0193 0.0229  0.0356  122 LEU   A CD1 
2478 C CD2 . LEU   A 122 ? 0.1633 0.1593 0.1920 -0.0040 0.0281  0.0292  122 LEU   A CD2 
2490 N N   A LEU   A 123 ? 0.1473 0.1565 0.1620 -0.0206 0.0134  0.0390  123 LEU   A N   
2491 N N   B LEU   A 123 ? 0.1568 0.1567 0.1651 -0.0214 0.0044  0.0260  123 LEU   A N   
2492 C CA  A LEU   A 123 ? 0.1427 0.1614 0.1449 -0.0168 0.0158  0.0325  123 LEU   A CA  
2493 C CA  B LEU   A 123 ? 0.1590 0.1589 0.1596 -0.0187 -0.0012 0.0056  123 LEU   A CA  
2494 C C   A LEU   A 123 ? 0.1425 0.1492 0.1350 -0.0137 0.0106  0.0320  123 LEU   A C   
2495 C C   B LEU   A 123 ? 0.1579 0.1502 0.1435 -0.0184 -0.0012 0.0093  123 LEU   A C   
2496 O O   A LEU   A 123 ? 0.1304 0.1422 0.1621 -0.0193 0.0116  0.0298  123 LEU   A O   
2497 O O   B LEU   A 123 ? 0.1542 0.1419 0.1351 -0.0127 -0.0056 0.0015  123 LEU   A O   
2498 C CB  A LEU   A 123 ? 0.1576 0.1674 0.1513 -0.0214 0.0356  0.0393  123 LEU   A CB  
2499 C CB  B LEU   A 123 ? 0.1696 0.1661 0.1747 -0.0205 -0.0053 -0.0016 123 LEU   A CB  
2500 C CG  A LEU   A 123 ? 0.1648 0.1766 0.1530 -0.0108 0.0294  0.0270  123 LEU   A CG  
2501 C CG  B LEU   A 123 ? 0.1747 0.1761 0.1874 -0.0226 -0.0055 0.0010  123 LEU   A CG  
2502 C CD1 A LEU   A 123 ? 0.1669 0.1872 0.1648 0.0024  0.0298  0.0087  123 LEU   A CD1 
2503 C CD1 B LEU   A 123 ? 0.1769 0.1836 0.2049 -0.0186 -0.0024 -0.0106 123 LEU   A CD1 
2504 C CD2 A LEU   A 123 ? 0.1706 0.1792 0.1519 -0.0074 0.0255  0.0283  123 LEU   A CD2 
2505 C CD2 B LEU   A 123 ? 0.1798 0.1831 0.2043 -0.0239 -0.0088 -0.0028 123 LEU   A CD2 
2528 N N   A ALA   A 124 ? 0.1367 0.1365 0.1090 -0.0083 0.0074  0.0220  124 ALA   A N   
2529 N N   B ALA   A 124 ? 0.1543 0.1426 0.1410 -0.0236 0.0027  0.0082  124 ALA   A N   
2530 C CA  A ALA   A 124 ? 0.1309 0.1364 0.1168 0.0041  -0.0012 0.0344  124 ALA   A CA  
2531 C CA  B ALA   A 124 ? 0.1548 0.1522 0.1512 -0.0331 0.0016  0.0108  124 ALA   A CA  
2532 C C   A ALA   A 124 ? 0.1255 0.1386 0.1331 -0.0007 0.0127  0.0277  124 ALA   A C   
2533 C C   B ALA   A 124 ? 0.1587 0.1631 0.1469 -0.0298 -0.0045 0.0117  124 ALA   A C   
2534 O O   A ALA   A 124 ? 0.1227 0.1311 0.1490 -0.0103 0.0168  0.0316  124 ALA   A O   
2535 O O   B ALA   A 124 ? 0.1656 0.1725 0.1509 -0.0247 -0.0016 0.0238  124 ALA   A O   
2536 C CB  A ALA   A 124 ? 0.1308 0.1282 0.1442 0.0050  -0.0021 0.0298  124 ALA   A CB  
2537 C CB  B ALA   A 124 ? 0.1558 0.1468 0.1713 -0.0447 0.0058  0.0145  124 ALA   A CB  
2548 N N   A PRO   A 125 ? 0.1279 0.1387 0.1393 -0.0066 0.0114  0.0326  125 PRO   A N   
2549 N N   B PRO   A 125 ? 0.1482 0.1579 0.1331 -0.0201 -0.0094 0.0206  125 PRO   A N   
2550 C CA  A PRO   A 125 ? 0.1397 0.1413 0.1358 -0.0013 0.0095  0.0349  125 PRO   A CA  
2551 C CA  B PRO   A 125 ? 0.1516 0.1573 0.1277 -0.0156 -0.0190 0.0177  125 PRO   A CA  
2552 C C   A PRO   A 125 ? 0.1307 0.1449 0.1605 -0.0018 0.0145  0.0296  125 PRO   A C   
2553 C C   B PRO   A 125 ? 0.1547 0.1640 0.1473 -0.0090 -0.0142 0.0071  125 PRO   A C   
2554 O O   A PRO   A 125 ? 0.1309 0.1340 0.1728 -0.0019 0.0082  0.0340  125 PRO   A O   
2555 O O   B PRO   A 125 ? 0.1526 0.1606 0.1687 -0.0080 -0.0124 0.0074  125 PRO   A O   
2556 C CB  A PRO   A 125 ? 0.1562 0.1379 0.1361 -0.0025 0.0203  0.0275  125 PRO   A CB  
2557 C CB  B PRO   A 125 ? 0.1524 0.1548 0.1389 -0.0156 -0.0190 0.0166  125 PRO   A CB  
2558 C CG  A PRO   A 125 ? 0.1617 0.1370 0.1467 -0.0078 0.0195  0.0309  125 PRO   A CG  
2559 C CG  B PRO   A 125 ? 0.1530 0.1591 0.1423 -0.0140 -0.0118 0.0244  125 PRO   A CG  
2560 C CD  A PRO   A 125 ? 0.1394 0.1406 0.1529 -0.0125 0.0248  0.0382  125 PRO   A CD  
2561 C CD  B PRO   A 125 ? 0.1421 0.1570 0.1422 -0.0202 0.0007  0.0209  125 PRO   A CD  
2576 N N   A LEU   A 126 ? 0.1301 0.1432 0.1696 0.0080  0.0201  0.0323  126 LEU   A N   
2577 N N   B LEU   A 126 ? 0.1675 0.1680 0.1479 -0.0030 -0.0187 0.0053  126 LEU   A N   
2578 C CA  A LEU   A 126 ? 0.1360 0.1529 0.1752 -0.0019 0.0022  0.0412  126 LEU   A CA  
2579 C CA  B LEU   A 126 ? 0.1731 0.1567 0.1544 0.0018  -0.0145 0.0132  126 LEU   A CA  
2580 C C   A LEU   A 126 ? 0.1422 0.1445 0.1708 0.0001  0.0012  0.0263  126 LEU   A C   
2581 C C   B LEU   A 126 ? 0.1734 0.1499 0.1612 0.0147  -0.0022 0.0109  126 LEU   A C   
2582 O O   A LEU   A 126 ? 0.1559 0.1339 0.2004 0.0084  0.0294  0.0248  126 LEU   A O   
2583 O O   B LEU   A 126 ? 0.1935 0.1456 0.1950 0.0148  0.0112  0.0281  126 LEU   A O   
2584 C CB  A LEU   A 126 ? 0.1463 0.1646 0.1970 0.0013  -0.0128 0.0319  126 LEU   A CB  
2585 C CB  B LEU   A 126 ? 0.1828 0.1615 0.1869 -0.0041 -0.0162 0.0158  126 LEU   A CB  
2586 C CG  A LEU   A 126 ? 0.1409 0.1879 0.2184 0.0010  -0.0012 0.0364  126 LEU   A CG  
2587 C CG  B LEU   A 126 ? 0.1795 0.1555 0.2309 0.0037  -0.0144 0.0199  126 LEU   A CG  
2588 C CD1 A LEU   A 126 ? 0.1368 0.1904 0.2380 0.0004  0.0051  0.0310  126 LEU   A CD1 
2589 C CD1 B LEU   A 126 ? 0.1790 0.1483 0.2460 -0.0000 -0.0197 0.0087  126 LEU   A CD1 
2590 C CD2 A LEU   A 126 ? 0.1476 0.1754 0.1948 -0.0198 -0.0026 0.0564  126 LEU   A CD2 
2591 C CD2 B LEU   A 126 ? 0.1741 0.1569 0.2442 0.0061  -0.0215 0.0288  126 LEU   A CD2 
2614 N N   A LEU   A 127 ? 0.1453 0.1508 0.1643 -0.0040 0.0131  0.0261  127 LEU   A N   
2615 N N   B LEU   A 127 ? 0.1632 0.1540 0.1547 0.0175  0.0049  0.0198  127 LEU   A N   
2616 C CA  A LEU   A 127 ? 0.1413 0.1499 0.1602 -0.0000 0.0047  0.0241  127 LEU   A CA  
2617 C CA  B LEU   A 127 ? 0.1542 0.1634 0.1534 0.0163  -0.0004 0.0326  127 LEU   A CA  
2618 C C   A LEU   A 127 ? 0.1353 0.1386 0.1554 -0.0028 0.0096  0.0091  127 LEU   A C   
2619 C C   B LEU   A 127 ? 0.1544 0.1695 0.1564 0.0131  -0.0105 0.0355  127 LEU   A C   
2620 O O   A LEU   A 127 ? 0.1465 0.1441 0.1604 -0.0194 0.0127  0.0016  127 LEU   A O   
2621 O O   B LEU   A 127 ? 0.1646 0.1723 0.1593 0.0057  -0.0089 0.0487  127 LEU   A O   
2622 C CB  A LEU   A 127 ? 0.1512 0.1615 0.1707 0.0182  0.0077  0.0219  127 LEU   A CB  
2623 C CB  B LEU   A 127 ? 0.1508 0.1762 0.1593 0.0176  0.0051  0.0302  127 LEU   A CB  
2624 C CG  A LEU   A 127 ? 0.1604 0.1536 0.1669 0.0177  0.0063  0.0359  127 LEU   A CG  
2625 C CG  B LEU   A 127 ? 0.1495 0.1843 0.1668 0.0189  0.0093  0.0387  127 LEU   A CG  
2626 C CD1 A LEU   A 127 ? 0.1692 0.1525 0.1844 0.0138  0.0092  0.0490  127 LEU   A CD1 
2627 C CD1 B LEU   A 127 ? 0.1468 0.1838 0.1718 0.0193  0.0265  0.0451  127 LEU   A CD1 
2628 C CD2 A LEU   A 127 ? 0.1713 0.1588 0.1895 0.0159  -0.0012 0.0327  127 LEU   A CD2 
2629 C CD2 B LEU   A 127 ? 0.1555 0.1903 0.1751 0.0188  0.0024  0.0246  127 LEU   A CD2 
2652 N N   A SER   A 128 ? 0.1484 0.1348 0.1496 -0.0139 0.0031  0.0197  128 SER   A N   
2653 N N   B SER   A 128 ? 0.1618 0.1823 0.1658 0.0024  -0.0182 0.0302  128 SER   A N   
2654 C CA  A SER   A 128 ? 0.1596 0.1390 0.1354 -0.0104 0.0011  0.0212  128 SER   A CA  
2655 C CA  B SER   A 128 ? 0.1723 0.1969 0.1712 0.0038  -0.0276 0.0218  128 SER   A CA  
2656 C C   A SER   A 128 ? 0.1659 0.1399 0.1284 -0.0070 -0.0144 0.0179  128 SER   A C   
2657 C C   B SER   A 128 ? 0.1937 0.2064 0.1869 0.0180  -0.0387 0.0299  128 SER   A C   
2658 O O   A SER   A 128 ? 0.1810 0.1506 0.1412 -0.0084 -0.0019 0.0105  128 SER   A O   
2659 O O   B SER   A 128 ? 0.2037 0.2020 0.1941 0.0216  -0.0271 0.0259  128 SER   A O   
2660 C CB  A SER   A 128 ? 0.1560 0.1615 0.1505 -0.0135 0.0166  0.0207  128 SER   A CB  
2661 C CB  B SER   A 128 ? 0.1581 0.2023 0.1484 -0.0088 -0.0352 0.0171  128 SER   A CB  
2662 O OG  A SER   A 128 ? 0.1569 0.1749 0.1814 -0.0147 0.0225  0.0181  128 SER   A OG  
2663 O OG  B SER   A 128 ? 0.1442 0.2042 0.1242 -0.0203 -0.0384 0.0031  128 SER   A OG  
2674 N N   A ALA   A 129 ? 0.1495 0.1437 0.1521 -0.0121 -0.0151 0.0326  129 ALA   A N   
2675 N N   B ALA   A 129 ? 0.2039 0.2270 0.2139 0.0252  -0.0340 0.0331  129 ALA   A N   
2676 C CA  A ALA   A 129 ? 0.1323 0.1413 0.1760 -0.0052 -0.0149 0.0348  129 ALA   A CA  
2677 C CA  B ALA   A 129 ? 0.2218 0.2501 0.2401 0.0274  -0.0187 0.0309  129 ALA   A CA  
2678 C C   A ALA   A 129 ? 0.1397 0.1445 0.1585 -0.0064 -0.0267 0.0215  129 ALA   A C   
2679 C C   B ALA   A 129 ? 0.2476 0.2679 0.2624 0.0272  -0.0073 0.0222  129 ALA   A C   
2680 O O   A ALA   A 129 ? 0.1399 0.1438 0.1517 -0.0037 -0.0150 0.0420  129 ALA   A O   
2681 O O   B ALA   A 129 ? 0.2549 0.2744 0.2724 0.0333  -0.0032 0.0143  129 ALA   A O   
2682 C CB  A ALA   A 129 ? 0.1345 0.1612 0.1968 0.0077  -0.0017 0.0354  129 ALA   A CB  
2683 C CB  B ALA   A 129 ? 0.2191 0.2514 0.2444 0.0237  -0.0070 0.0406  129 ALA   A CB  
2694 N N   A GLY   A 130 ? 0.1428 0.1430 0.1778 -0.0062 -0.0197 0.0252  130 GLY   A N   
2695 N N   B GLY   A 130 ? 0.2677 0.2723 0.2727 0.0261  -0.0076 0.0251  130 GLY   A N   
2696 C CA  A GLY   A 130 ? 0.1642 0.1459 0.1806 0.0055  -0.0081 0.0105  130 GLY   A CA  
2697 C CA  B GLY   A 130 ? 0.2772 0.2767 0.2715 0.0256  -0.0057 0.0262  130 GLY   A CA  
2698 C C   A GLY   A 130 ? 0.1649 0.1421 0.1587 0.0091  -0.0205 -0.0084 130 GLY   A C   
2699 C C   B GLY   A 130 ? 0.2836 0.2780 0.2706 0.0238  -0.0071 0.0258  130 GLY   A C   
2700 O O   A GLY   A 130 ? 0.1712 0.1372 0.1747 0.0057  -0.0245 0.0027  130 GLY   A O   
2701 O O   B GLY   A 130 ? 0.2823 0.2743 0.2725 0.0235  -0.0125 0.0292  130 GLY   A O   
2708 N N   A ILE   A 131 ? 0.1771 0.1365 0.1271 -0.0034 -0.0166 0.0067  131 ILE   A N   
2709 N N   B ILE   A 131 ? 0.2884 0.2780 0.2718 0.0251  0.0012  0.0317  131 ILE   A N   
2710 C CA  A ILE   A 131 ? 0.1975 0.1419 0.1114 -0.0175 -0.0343 0.0120  131 ILE   A CA  
2711 C CA  B ILE   A 131 ? 0.2904 0.2770 0.2799 0.0262  0.0073  0.0351  131 ILE   A CA  
2712 C C   A ILE   A 131 ? 0.1809 0.1475 0.0912 -0.0238 -0.0289 0.0264  131 ILE   A C   
2713 C C   B ILE   A 131 ? 0.2856 0.2720 0.2785 0.0266  -0.0004 0.0502  131 ILE   A C   
2714 O O   A ILE   A 131 ? 0.1878 0.1396 0.1216 -0.0171 -0.0271 0.0254  131 ILE   A O   
2715 O O   B ILE   A 131 ? 0.2809 0.2713 0.2765 0.0313  0.0105  0.0670  131 ILE   A O   
2716 C CB  A ILE   A 131 ? 0.2290 0.1642 0.1457 -0.0290 -0.0364 0.0089  131 ILE   A CB  
2717 C CB  B ILE   A 131 ? 0.2963 0.2831 0.2991 0.0264  0.0167  0.0206  131 ILE   A CB  
2718 C CG1 A ILE   A 131 ? 0.2428 0.1934 0.1719 -0.0476 -0.0464 -0.0034 131 ILE   A CG1 
2719 C CG1 B ILE   A 131 ? 0.3020 0.2890 0.3209 0.0205  0.0180  0.0132  131 ILE   A CG1 
2720 C CG2 A ILE   A 131 ? 0.2403 0.1545 0.1729 -0.0299 -0.0126 0.0018  131 ILE   A CG2 
2721 C CG2 B ILE   A 131 ? 0.2954 0.2848 0.2954 0.0290  0.0207  0.0143  131 ILE   A CG2 
2722 C CD1 A ILE   A 131 ? 0.2488 0.2101 0.1987 -0.0455 -0.0563 -0.0136 131 ILE   A CD1 
2723 C CD1 B ILE   A 131 ? 0.3024 0.2912 0.3325 0.0169  0.0184  0.0086  131 ILE   A CD1 
2746 N N   A PHE   A 132 ? 0.1740 0.1477 0.1001 -0.0211 -0.0108 0.0308  132 PHE   A N   
2747 N N   B PHE   A 132 ? 0.2827 0.2665 0.2775 0.0203  -0.0169 0.0511  132 PHE   A N   
2748 C CA  A PHE   A 132 ? 0.1817 0.1567 0.0855 -0.0272 -0.0075 0.0089  132 PHE   A CA  
2749 C CA  B PHE   A 132 ? 0.2789 0.2633 0.2736 0.0128  -0.0286 0.0461  132 PHE   A CA  
2750 C C   A PHE   A 132 ? 0.1930 0.1665 0.1127 -0.0228 -0.0160 0.0061  132 PHE   A C   
2751 C C   B PHE   A 132 ? 0.2731 0.2696 0.2635 0.0142  -0.0286 0.0368  132 PHE   A C   
2752 O O   A PHE   A 132 ? 0.2107 0.1825 0.1260 -0.0194 -0.0254 0.0085  132 PHE   A O   
2753 O O   B PHE   A 132 ? 0.2756 0.2703 0.2508 0.0163  -0.0290 0.0387  132 PHE   A O   
2754 C CB  A PHE   A 132 ? 0.1759 0.1471 0.0893 -0.0278 -0.0091 0.0269  132 PHE   A CB  
2755 C CB  B PHE   A 132 ? 0.2803 0.2593 0.2989 0.0033  -0.0432 0.0404  132 PHE   A CB  
2756 C CG  A PHE   A 132 ? 0.1702 0.1384 0.0831 -0.0142 -0.0256 0.0207  132 PHE   A CG  
2757 C CG  B PHE   A 132 ? 0.2852 0.2602 0.3292 -0.0084 -0.0493 0.0344  132 PHE   A CG  
2758 C CD1 A PHE   A 132 ? 0.1642 0.1435 0.1164 -0.0023 -0.0316 0.0001  132 PHE   A CD1 
2759 C CD1 B PHE   A 132 ? 0.2860 0.2611 0.3395 -0.0126 -0.0502 0.0304  132 PHE   A CD1 
2760 C CD2 A PHE   A 132 ? 0.1752 0.1405 0.1138 -0.0076 -0.0234 0.0054  132 PHE   A CD2 
2761 C CD2 B PHE   A 132 ? 0.2867 0.2615 0.3382 -0.0127 -0.0524 0.0318  132 PHE   A CD2 
2762 C CE1 A PHE   A 132 ? 0.1609 0.1498 0.1251 -0.0002 -0.0291 0.0022  132 PHE   A CE1 
2763 C CE1 B PHE   A 132 ? 0.2868 0.2613 0.3431 -0.0147 -0.0517 0.0246  132 PHE   A CE1 
2764 C CE2 A PHE   A 132 ? 0.1700 0.1547 0.1370 -0.0024 -0.0297 0.0158  132 PHE   A CE2 
2765 C CE2 B PHE   A 132 ? 0.2881 0.2631 0.3435 -0.0166 -0.0540 0.0269  132 PHE   A CE2 
2766 C CZ  A PHE   A 132 ? 0.1593 0.1541 0.1337 -0.0088 -0.0319 0.0107  132 PHE   A CZ  
2767 C CZ  B PHE   A 132 ? 0.2867 0.2621 0.3431 -0.0177 -0.0582 0.0217  132 PHE   A CZ  
2786 N N   A GLY   A 133 ? 0.1850 0.1712 0.1167 -0.0205 -0.0295 0.0257  133 GLY   A N   
2787 N N   B GLY   A 133 ? 0.2686 0.2730 0.2724 0.0111  -0.0263 0.0228  133 GLY   A N   
2788 C CA  A GLY   A 133 ? 0.1886 0.1817 0.1200 -0.0144 -0.0299 0.0097  133 GLY   A CA  
2789 C CA  B GLY   A 133 ? 0.2636 0.2749 0.2758 0.0015  -0.0265 0.0085  133 GLY   A CA  
2790 C C   A GLY   A 133 ? 0.1844 0.1915 0.1129 -0.0083 -0.0456 -0.0032 133 GLY   A C   
2791 C C   B GLY   A 133 ? 0.2575 0.2720 0.2732 -0.0088 -0.0254 -0.0042 133 GLY   A C   
2792 O O   A GLY   A 133 ? 0.1971 0.2040 0.1381 -0.0076 -0.0408 -0.0223 133 GLY   A O   
2793 O O   B GLY   A 133 ? 0.2674 0.2837 0.2848 -0.0034 -0.0282 -0.0007 133 GLY   A O   
2800 N N   A ALA   A 134 ? 0.1857 0.1896 0.1229 -0.0134 -0.0438 -0.0068 134 ALA   A N   
2801 N N   B ALA   A 134 ? 0.2417 0.2553 0.2526 -0.0214 -0.0173 -0.0164 134 ALA   A N   
2802 C CA  A ALA   A 134 ? 0.1842 0.1869 0.1457 -0.0070 -0.0285 -0.0022 134 ALA   A CA  
2803 C CA  B ALA   A 134 ? 0.2270 0.2409 0.2371 -0.0330 -0.0209 -0.0262 134 ALA   A CA  
2804 C C   A ALA   A 134 ? 0.1955 0.1903 0.1520 -0.0053 -0.0160 -0.0101 134 ALA   A C   
2805 C C   B ALA   A 134 ? 0.2166 0.2387 0.2306 -0.0413 -0.0302 -0.0223 134 ALA   A C   
2806 O O   A ALA   A 134 ? 0.2148 0.1995 0.1663 0.0028  0.0089  -0.0007 134 ALA   A O   
2807 O O   B ALA   A 134 ? 0.2222 0.2376 0.2313 -0.0451 -0.0345 -0.0237 134 ALA   A O   
2808 C CB  A ALA   A 134 ? 0.1901 0.1883 0.1860 -0.0089 -0.0135 -0.0016 134 ALA   A CB  
2809 C CB  B ALA   A 134 ? 0.2293 0.2340 0.2445 -0.0334 -0.0187 -0.0315 134 ALA   A CB  
2820 N N   A ASP   A 135 ? 0.2042 0.1943 0.1650 -0.0078 -0.0160 0.0079  135 ASP   A N   
2821 N N   B ASP   A 135 ? 0.2069 0.2322 0.2246 -0.0394 -0.0326 -0.0110 135 ASP   A N   
2822 C CA  A ASP   A 135 ? 0.1972 0.2131 0.1946 -0.0196 -0.0309 0.0180  135 ASP   A CA  
2823 C CA  B ASP   A 135 ? 0.2030 0.2352 0.2242 -0.0406 -0.0279 0.0150  135 ASP   A CA  
2824 C C   A ASP   A 135 ? 0.1841 0.2022 0.1963 -0.0104 -0.0350 0.0278  135 ASP   A C   
2825 C C   B ASP   A 135 ? 0.1906 0.2211 0.2003 -0.0273 -0.0204 0.0165  135 ASP   A C   
2826 O O   A ASP   A 135 ? 0.1771 0.1922 0.1956 -0.0088 -0.0336 0.0408  135 ASP   A O   
2827 O O   B ASP   A 135 ? 0.1839 0.2143 0.1902 -0.0241 -0.0120 0.0217  135 ASP   A O   
2828 C CB  A ASP   A 135 ? 0.2164 0.2550 0.2371 -0.0453 -0.0506 0.0122  135 ASP   A CB  
2829 C CB  B ASP   A 135 ? 0.2128 0.2529 0.2457 -0.0572 -0.0363 0.0265  135 ASP   A CB  
2830 C CG  A ASP   A 135 ? 0.2327 0.2936 0.2925 -0.0570 -0.0589 0.0069  135 ASP   A CG  
2831 C CG  B ASP   A 135 ? 0.2232 0.2690 0.2693 -0.0625 -0.0441 0.0306  135 ASP   A CG  
2832 O OD1 A ASP   A 135 ? 0.2318 0.3128 0.2742 -0.0644 -0.0764 0.0256  135 ASP   A OD1 
2833 O OD1 B ASP   A 135 ? 0.2281 0.2792 0.2884 -0.0580 -0.0342 0.0330  135 ASP   A OD1 
2834 O OD2 A ASP   A 135 ? 0.2582 0.3118 0.3630 -0.0545 -0.0259 0.0170  135 ASP   A OD2 
2835 O OD2 B ASP   A 135 ? 0.2243 0.2758 0.2736 -0.0726 -0.0619 0.0311  135 ASP   A OD2 
2844 N N   A PRO   A 136 ? 0.1768 0.2050 0.1962 0.0006  -0.0248 0.0388  136 PRO   A N   
2845 N N   B PRO   A 136 ? 0.1855 0.2148 0.1969 -0.0132 -0.0174 0.0205  136 PRO   A N   
2846 C CA  A PRO   A 136 ? 0.1634 0.2030 0.2002 -0.0071 -0.0119 0.0231  136 PRO   A CA  
2847 C CA  B PRO   A 136 ? 0.1793 0.2078 0.1958 -0.0080 -0.0152 0.0142  136 PRO   A CA  
2848 C C   A PRO   A 136 ? 0.1442 0.1972 0.1890 -0.0085 -0.0042 0.0194  136 PRO   A C   
2849 C C   B PRO   A 136 ? 0.1703 0.2038 0.1950 -0.0061 -0.0110 0.0076  136 PRO   A C   
2850 O O   A PRO   A 136 ? 0.1337 0.1863 0.1541 -0.0005 0.0072  0.0266  136 PRO   A O   
2851 O O   B PRO   A 136 ? 0.1692 0.2116 0.1811 -0.0014 -0.0027 0.0048  136 PRO   A O   
2852 C CB  A PRO   A 136 ? 0.1775 0.2077 0.2074 -0.0029 -0.0252 0.0085  136 PRO   A CB  
2853 C CB  B PRO   A 136 ? 0.1866 0.2108 0.2079 -0.0022 -0.0154 0.0189  136 PRO   A CB  
2854 C CG  A PRO   A 136 ? 0.1969 0.2183 0.2313 0.0072  -0.0228 0.0150  136 PRO   A CG  
2855 C CG  B PRO   A 136 ? 0.1903 0.2146 0.2087 -0.0047 -0.0222 0.0100  136 PRO   A CG  
2856 C CD  A PRO   A 136 ? 0.1880 0.2082 0.2091 0.0046  -0.0097 0.0407  136 PRO   A CD  
2857 C CD  B PRO   A 136 ? 0.1908 0.2161 0.2046 -0.0058 -0.0244 0.0173  136 PRO   A CD  
2872 N N   A ILE   A 137 ? 0.1488 0.2024 0.2162 -0.0104 -0.0132 0.0227  137 ILE   A N   
2873 N N   B ILE   A 137 ? 0.1636 0.1928 0.1998 -0.0101 -0.0124 0.0129  137 ILE   A N   
2874 C CA  A ILE   A 137 ? 0.1510 0.2141 0.2122 -0.0183 -0.0129 0.0216  137 ILE   A CA  
2875 C CA  B ILE   A 137 ? 0.1653 0.1957 0.2112 -0.0142 -0.0057 0.0163  137 ILE   A CA  
2876 C C   A ILE   A 137 ? 0.1505 0.2187 0.1941 -0.0194 -0.0134 0.0282  137 ILE   A C   
2877 C C   B ILE   A 137 ? 0.1629 0.1946 0.2110 -0.0116 0.0025  0.0224  137 ILE   A C   
2878 O O   A ILE   A 137 ? 0.1598 0.2227 0.1965 -0.0270 -0.0136 0.0201  137 ILE   A O   
2879 O O   B ILE   A 137 ? 0.1659 0.1843 0.2289 -0.0109 0.0168  0.0138  137 ILE   A O   
2880 C CB  A ILE   A 137 ? 0.1631 0.2290 0.2453 -0.0203 -0.0331 0.0085  137 ILE   A CB  
2881 C CB  B ILE   A 137 ? 0.1730 0.2056 0.2262 -0.0158 -0.0159 -0.0043 137 ILE   A CB  
2882 C CG1 A ILE   A 137 ? 0.1800 0.2546 0.2708 -0.0056 -0.0413 0.0118  137 ILE   A CG1 
2883 C CG1 B ILE   A 137 ? 0.1790 0.2128 0.2356 -0.0125 -0.0210 -0.0217 137 ILE   A CG1 
2884 C CG2 A ILE   A 137 ? 0.1755 0.2266 0.2693 -0.0250 -0.0473 0.0038  137 ILE   A CG2 
2885 C CG2 B ILE   A 137 ? 0.1781 0.2068 0.2220 -0.0174 -0.0222 -0.0166 137 ILE   A CG2 
2886 C CD1 A ILE   A 137 ? 0.1990 0.2652 0.2860 0.0037  -0.0380 0.0132  137 ILE   A CD1 
2887 C CD1 B ILE   A 137 ? 0.1926 0.2202 0.2450 -0.0095 -0.0225 -0.0362 137 ILE   A CD1 
2910 N N   A HIS   A 138 ? 0.1539 0.2341 0.2066 -0.0123 -0.0025 0.0291  138 HIS   A N   
2911 N N   B HIS   A 138 ? 0.1628 0.2088 0.2125 -0.0078 0.0044  0.0235  138 HIS   A N   
2912 C CA  A HIS   A 138 ? 0.1572 0.2362 0.2088 -0.0100 0.0007  0.0256  138 HIS   A CA  
2913 C CA  B HIS   A 138 ? 0.1633 0.2161 0.2035 -0.0132 0.0062  0.0266  138 HIS   A CA  
2914 C C   A HIS   A 138 ? 0.1480 0.2195 0.2012 -0.0069 -0.0056 0.0349  138 HIS   A C   
2915 C C   B HIS   A 138 ? 0.1507 0.2098 0.1957 -0.0130 -0.0063 0.0339  138 HIS   A C   
2916 O O   A HIS   A 138 ? 0.1576 0.2199 0.2266 -0.0016 0.0095  0.0396  138 HIS   A O   
2917 O O   B HIS   A 138 ? 0.1461 0.2097 0.2033 -0.0143 0.0000  0.0369  138 HIS   A O   
2918 C CB  A HIS   A 138 ? 0.1671 0.2522 0.2116 -0.0019 0.0027  0.0110  138 HIS   A CB  
2919 C CB  B HIS   A 138 ? 0.1908 0.2304 0.2130 -0.0155 0.0005  0.0236  138 HIS   A CB  
2920 C CG  A HIS   A 138 ? 0.1813 0.2536 0.2207 -0.0086 0.0089  -0.0081 138 HIS   A CG  
2921 C CG  B HIS   A 138 ? 0.2066 0.2314 0.2213 -0.0215 0.0088  0.0210  138 HIS   A CG  
2922 N ND1 A HIS   A 138 ? 0.1945 0.2589 0.2351 -0.0142 0.0073  -0.0286 138 HIS   A ND1 
2923 N ND1 B HIS   A 138 ? 0.2157 0.2357 0.2327 -0.0239 0.0096  0.0112  138 HIS   A ND1 
2924 C CD2 A HIS   A 138 ? 0.1750 0.2487 0.2180 0.0007  0.0097  -0.0116 138 HIS   A CD2 
2925 C CD2 B HIS   A 138 ? 0.2110 0.2320 0.2219 -0.0207 0.0055  0.0138  138 HIS   A CD2 
2926 C CE1 A HIS   A 138 ? 0.1962 0.2545 0.2388 -0.0021 0.0123  -0.0198 138 HIS   A CE1 
2927 C CE1 B HIS   A 138 ? 0.2207 0.2343 0.2364 -0.0195 0.0077  0.0099  138 HIS   A CE1 
2928 N NE2 A HIS   A 138 ? 0.1837 0.2510 0.2153 0.0002  0.0174  -0.0205 138 HIS   A NE2 
2929 N NE2 B HIS   A 138 ? 0.2154 0.2315 0.2187 -0.0174 0.0072  0.0102  138 HIS   A NE2 
2944 N N   . SER   A 139 ? 0.1458 0.2020 0.1933 -0.0056 -0.0059 0.0419  139 SER   A N   
2945 C CA  . SER   A 139 ? 0.1369 0.1889 0.2095 -0.0108 0.0097  0.0459  139 SER   A CA  
2946 C C   . SER   A 139 ? 0.1353 0.1848 0.2155 -0.0125 0.0080  0.0426  139 SER   A C   
2947 O O   . SER   A 139 ? 0.1249 0.1732 0.2391 -0.0137 0.0023  0.0491  139 SER   A O   
2948 C CB  . SER   A 139 ? 0.1422 0.1851 0.2081 -0.0126 0.0123  0.0461  139 SER   A CB  
2949 O OG  . SER   A 139 ? 0.1383 0.1869 0.2396 -0.0125 -0.0030 0.0499  139 SER   A OG  
2956 N N   . LEU   A 140 ? 0.1313 0.1958 0.2004 -0.0087 0.0097  0.0543  140 LEU   A N   
2957 C CA  . LEU   A 140 ? 0.1310 0.1887 0.1896 -0.0049 0.0010  0.0490  140 LEU   A CA  
2958 C C   . LEU   A 140 ? 0.1266 0.1918 0.1930 -0.0184 -0.0011 0.0502  140 LEU   A C   
2959 O O   . LEU   A 140 ? 0.1359 0.1923 0.2262 -0.0147 0.0012  0.0568  140 LEU   A O   
2960 C CB  . LEU   A 140 ? 0.1315 0.1947 0.2013 -0.0054 0.0089  0.0481  140 LEU   A CB  
2961 C CG  . LEU   A 140 ? 0.1335 0.2093 0.2239 -0.0228 0.0130  0.0552  140 LEU   A CG  
2962 C CD1 . LEU   A 140 ? 0.1391 0.2130 0.2347 -0.0131 0.0029  0.0487  140 LEU   A CD1 
2963 C CD2 . LEU   A 140 ? 0.1477 0.2246 0.2162 -0.0196 0.0169  0.0605  140 LEU   A CD2 
2975 N N   . ARG   A 141 ? 0.1389 0.1952 0.2075 -0.0199 -0.0083 0.0311  141 ARG   A N   
2976 C CA  . ARG   A 141 ? 0.1536 0.1992 0.2483 -0.0247 -0.0047 0.0258  141 ARG   A CA  
2977 C C   . ARG   A 141 ? 0.1510 0.1786 0.2291 -0.0096 -0.0069 0.0202  141 ARG   A C   
2978 O O   . ARG   A 141 ? 0.1434 0.1797 0.2372 -0.0161 -0.0005 0.0175  141 ARG   A O   
2979 C CB  . ARG   A 141 ? 0.1701 0.2185 0.2924 -0.0284 -0.0128 0.0090  141 ARG   A CB  
2980 C CG  . ARG   A 141 ? 0.2138 0.2572 0.3374 -0.0400 -0.0059 0.0016  141 ARG   A CG  
2981 C CD  . ARG   A 141 ? 0.2540 0.2978 0.3789 -0.0510 -0.0129 0.0091  141 ARG   A CD  
2982 N NE  . ARG   A 141 ? 0.2476 0.3284 0.3959 -0.0533 -0.0212 0.0162  141 ARG   A NE  
2983 C CZ  . ARG   A 141 ? 0.2507 0.3487 0.3974 -0.0703 -0.0177 0.0181  141 ARG   A CZ  
2984 N NH1 . ARG   A 141 ? 0.2309 0.3527 0.3792 -0.0780 0.0006  0.0018  141 ARG   A NH1 
2985 N NH2 . ARG   A 141 ? 0.2569 0.3547 0.4124 -0.0662 -0.0366 0.0255  141 ARG   A NH2 
2999 N N   . VAL   A 142 ? 0.1417 0.1682 0.2111 -0.0112 -0.0053 0.0116  142 VAL   A N   
3000 C CA  . VAL   A 142 ? 0.1444 0.1703 0.2080 -0.0059 0.0133  0.0027  142 VAL   A CA  
3001 C C   . VAL   A 142 ? 0.1352 0.1603 0.1998 -0.0159 0.0055  0.0262  142 VAL   A C   
3002 O O   . VAL   A 142 ? 0.1334 0.1654 0.2169 -0.0056 0.0165  0.0221  142 VAL   A O   
3003 C CB  . VAL   A 142 ? 0.1521 0.1740 0.1957 -0.0071 0.0164  0.0143  142 VAL   A CB  
3004 C CG1 . VAL   A 142 ? 0.1495 0.1698 0.2115 -0.0156 0.0190  0.0170  142 VAL   A CG1 
3005 C CG2 . VAL   A 142 ? 0.1720 0.1940 0.2219 -0.0075 0.0313  0.0226  142 VAL   A CG2 
3015 N N   . CYS   A 143 ? 0.1331 0.1589 0.1978 -0.0197 0.0031  0.0249  143 CYS   A N   
3016 C CA  . CYS   A 143 ? 0.1402 0.1650 0.2039 -0.0177 0.0129  0.0311  143 CYS   A CA  
3017 C C   . CYS   A 143 ? 0.1400 0.1595 0.2040 -0.0125 0.0059  0.0439  143 CYS   A C   
3018 O O   . CYS   A 143 ? 0.1331 0.1593 0.2215 -0.0034 0.0086  0.0365  143 CYS   A O   
3019 C CB  . CYS   A 143 ? 0.1555 0.1678 0.2220 -0.0097 0.0238  0.0381  143 CYS   A CB  
3020 S SG  . CYS   A 143 ? 0.1651 0.1701 0.2013 0.0088  0.0151  0.0271  143 CYS   A SG  
3026 N N   . VAL   A 144 ? 0.1342 0.1587 0.2291 -0.0111 0.0116  0.0409  144 VAL   A N   
3027 C CA  . VAL   A 144 ? 0.1456 0.1786 0.2694 -0.0124 0.0331  0.0525  144 VAL   A CA  
3028 C C   . VAL   A 144 ? 0.1408 0.1772 0.2739 -0.0201 -0.0186 0.0445  144 VAL   A C   
3029 O O   . VAL   A 144 ? 0.1638 0.1742 0.2891 -0.0096 -0.0040 0.0591  144 VAL   A O   
3030 C CB  . VAL   A 144 ? 0.1801 0.2017 0.3282 -0.0011 0.0549  0.0591  144 VAL   A CB  
3031 C CG1 . VAL   A 144 ? 0.2000 0.2286 0.3766 -0.0121 0.0302  0.0496  144 VAL   A CG1 
3032 C CG2 . VAL   A 144 ? 0.1731 0.2115 0.3317 0.0039  0.0526  0.0691  144 VAL   A CG2 
3042 N N   . ASP   A 145 ? 0.1542 0.1645 0.2914 -0.0267 -0.0032 0.0314  145 ASP   A N   
3043 C CA  . ASP   A 145 ? 0.1688 0.1709 0.3029 -0.0246 -0.0144 0.0172  145 ASP   A CA  
3044 C C   . ASP   A 145 ? 0.1686 0.1556 0.2827 -0.0143 -0.0024 0.0063  145 ASP   A C   
3045 O O   . ASP   A 145 ? 0.1892 0.1543 0.3501 -0.0227 -0.0083 -0.0260 145 ASP   A O   
3046 C CB  . ASP   A 145 ? 0.1803 0.1948 0.3351 -0.0389 -0.0345 0.0113  145 ASP   A CB  
3047 C CG  . ASP   A 145 ? 0.2015 0.2459 0.3640 -0.0581 -0.0413 0.0159  145 ASP   A CG  
3048 O OD1 . ASP   A 145 ? 0.1972 0.2660 0.3900 -0.0688 -0.0296 0.0221  145 ASP   A OD1 
3049 O OD2 . ASP   A 145 ? 0.2169 0.2736 0.3714 -0.0683 -0.0519 0.0183  145 ASP   A OD2 
3054 N N   . THR   A 146 ? 0.1503 0.1486 0.2294 -0.0151 0.0096  0.0116  146 THR   A N   
3055 C CA  . THR   A 146 ? 0.1446 0.1461 0.2132 -0.0060 0.0114  0.0168  146 THR   A CA  
3056 C C   . THR   A 146 ? 0.1379 0.1474 0.2220 0.0011  0.0097  0.0201  146 THR   A C   
3057 O O   . THR   A 146 ? 0.1483 0.1502 0.2609 0.0006  0.0013  0.0091  146 THR   A O   
3058 C CB  . THR   A 146 ? 0.1405 0.1567 0.2302 -0.0020 0.0046  0.0234  146 THR   A CB  
3059 O OG1 . THR   A 146 ? 0.1361 0.1660 0.2395 0.0005  0.0066  0.0075  146 THR   A OG1 
3060 C CG2 . THR   A 146 ? 0.1414 0.1513 0.2559 -0.0045 0.0070  0.0259  146 THR   A CG2 
3068 N N   . VAL   A 147 ? 0.1272 0.1411 0.2178 -0.0019 0.0124  0.0090  147 VAL   A N   
3069 C CA  . VAL   A 147 ? 0.1300 0.1464 0.2219 -0.0139 0.0217  0.0154  147 VAL   A CA  
3070 C C   . VAL   A 147 ? 0.1404 0.1440 0.2314 -0.0145 0.0273  0.0329  147 VAL   A C   
3071 O O   . VAL   A 147 ? 0.1472 0.1559 0.2451 -0.0161 0.0226  0.0451  147 VAL   A O   
3072 C CB  . VAL   A 147 ? 0.1433 0.1458 0.2145 -0.0111 0.0188  0.0308  147 VAL   A CB  
3073 C CG1 . VAL   A 147 ? 0.1854 0.1614 0.2188 -0.0104 0.0161  0.0462  147 VAL   A CG1 
3074 C CG2 . VAL   A 147 ? 0.1489 0.1564 0.2213 -0.0139 0.0124  0.0333  147 VAL   A CG2 
3084 N N   . ARG   A 148 ? 0.1436 0.1470 0.2458 -0.0133 0.0206  0.0508  148 ARG   A N   
3085 C CA  . ARG   A 148 ? 0.1436 0.1535 0.2442 -0.0130 0.0123  0.0492  148 ARG   A CA  
3086 C C   . ARG   A 148 ? 0.1484 0.1539 0.2420 -0.0120 0.0268  0.0603  148 ARG   A C   
3087 O O   . ARG   A 148 ? 0.1747 0.1624 0.2620 -0.0118 0.0343  0.0575  148 ARG   A O   
3088 C CB  . ARG   A 148 ? 0.1588 0.1532 0.2697 -0.0130 0.0212  0.0502  148 ARG   A CB  
3089 C CG  . ARG   A 148 ? 0.1691 0.1536 0.2987 -0.0102 0.0496  0.0404  148 ARG   A CG  
3090 C CD  . ARG   A 148 ? 0.1853 0.1521 0.3134 -0.0044 0.0580  0.0576  148 ARG   A CD  
3091 N NE  . ARG   A 148 ? 0.1778 0.1486 0.3127 0.0139  0.0568  0.0639  148 ARG   A NE  
3092 C CZ  . ARG   A 148 ? 0.1783 0.1437 0.3006 0.0147  0.0508  0.0660  148 ARG   A CZ  
3093 N NH1 . ARG   A 148 ? 0.1817 0.1483 0.3066 -0.0009 0.0547  0.0315  148 ARG   A NH1 
3094 N NH2 . ARG   A 148 ? 0.1600 0.1615 0.3040 0.0202  0.0580  0.0505  148 ARG   A NH2 
3108 N N   . THR   A 149 ? 0.1511 0.1649 0.2334 -0.0101 0.0072  0.0608  149 THR   A N   
3109 C CA  . THR   A 149 ? 0.1544 0.1657 0.2307 -0.0091 0.0135  0.0493  149 THR   A CA  
3110 C C   . THR   A 149 ? 0.1456 0.1676 0.2171 -0.0191 0.0198  0.0587  149 THR   A C   
3111 O O   . THR   A 149 ? 0.1444 0.1754 0.2446 -0.0220 0.0183  0.0536  149 THR   A O   
3112 C CB  . THR   A 149 ? 0.1556 0.1781 0.2468 -0.0086 0.0091  0.0439  149 THR   A CB  
3113 O OG1 . THR   A 149 ? 0.1619 0.1626 0.2575 -0.0215 0.0093  0.0565  149 THR   A OG1 
3114 C CG2 . THR   A 149 ? 0.1502 0.1950 0.2531 -0.0033 0.0071  0.0307  149 THR   A CG2 
3122 N N   . ASN   A 150 ? 0.1455 0.1715 0.2192 -0.0074 0.0063  0.0692  150 ASN   A N   
3123 C CA  . ASN   A 150 ? 0.1671 0.1777 0.2152 -0.0129 -0.0029 0.0537  150 ASN   A CA  
3124 C C   . ASN   A 150 ? 0.1456 0.1695 0.2148 -0.0125 0.0068  0.0515  150 ASN   A C   
3125 O O   . ASN   A 150 ? 0.1521 0.1867 0.2397 -0.0172 -0.0092 0.0575  150 ASN   A O   
3126 C CB  . ASN   A 150 ? 0.2103 0.2041 0.2446 -0.0225 0.0122  0.0714  150 ASN   A CB  
3127 C CG  . ASN   A 150 ? 0.2680 0.2327 0.3095 -0.0244 -0.0023 0.0707  150 ASN   A CG  
3128 O OD1 . ASN   A 150 ? 0.2955 0.2378 0.3363 -0.0271 0.0062  0.0830  150 ASN   A OD1 
3129 N ND2 . ASN   A 150 ? 0.3093 0.2564 0.3668 -0.0169 -0.0097 0.0762  150 ASN   A ND2 
3136 N N   . VAL   A 151 ? 0.1446 0.1541 0.2133 -0.0198 -0.0025 0.0481  151 VAL   A N   
3137 C CA  . VAL   A 151 ? 0.1568 0.1528 0.2098 -0.0172 0.0215  0.0594  151 VAL   A CA  
3138 C C   . VAL   A 151 ? 0.1524 0.1502 0.2210 -0.0252 0.0208  0.0527  151 VAL   A C   
3139 O O   . VAL   A 151 ? 0.1601 0.1595 0.2571 -0.0200 0.0199  0.0491  151 VAL   A O   
3140 C CB  . VAL   A 151 ? 0.1888 0.1816 0.2160 -0.0086 0.0178  0.0407  151 VAL   A CB  
3141 C CG1 . VAL   A 151 ? 0.1878 0.2057 0.2436 -0.0129 0.0082  0.0354  151 VAL   A CG1 
3142 C CG2 . VAL   A 151 ? 0.2042 0.1743 0.2053 -0.0017 0.0210  0.0443  151 VAL   A CG2 
3152 N N   . TYR   A 152 ? 0.1546 0.1492 0.2244 -0.0250 0.0109  0.0530  152 TYR   A N   
3153 C CA  . TYR   A 152 ? 0.1510 0.1677 0.1687 -0.0205 0.0120  0.0443  152 TYR   A CA  
3154 C C   . TYR   A 152 ? 0.1420 0.1713 0.1673 -0.0226 0.0174  0.0350  152 TYR   A C   
3155 O O   . TYR   A 152 ? 0.1559 0.1522 0.2012 -0.0188 0.0191  0.0346  152 TYR   A O   
3156 C CB  . TYR   A 152 ? 0.1648 0.1817 0.1890 -0.0239 0.0201  0.0548  152 TYR   A CB  
3157 C CG  . TYR   A 152 ? 0.1823 0.2052 0.1847 -0.0193 0.0292  0.0641  152 TYR   A CG  
3158 C CD1 . TYR   A 152 ? 0.1976 0.2257 0.2182 -0.0081 0.0336  0.0718  152 TYR   A CD1 
3159 C CD2 . TYR   A 152 ? 0.1891 0.2119 0.1914 -0.0385 0.0240  0.0643  152 TYR   A CD2 
3160 C CE1 . TYR   A 152 ? 0.2246 0.2391 0.2307 -0.0067 0.0204  0.0805  152 TYR   A CE1 
3161 C CE2 . TYR   A 152 ? 0.2174 0.2303 0.2066 -0.0412 0.0176  0.0676  152 TYR   A CE2 
3162 C CZ  . TYR   A 152 ? 0.2440 0.2317 0.2234 -0.0288 0.0219  0.0975  152 TYR   A CZ  
3163 O OH  . TYR   A 152 ? 0.2765 0.2605 0.2782 -0.0222 0.0218  0.1072  152 TYR   A OH  
3173 N N   . LEU   A 153 ? 0.1440 0.1640 0.1741 -0.0248 0.0171  0.0459  153 LEU   A N   
3174 C CA  . LEU   A 153 ? 0.1375 0.1550 0.1965 -0.0122 0.0190  0.0513  153 LEU   A CA  
3175 C C   . LEU   A 153 ? 0.1394 0.1577 0.1993 -0.0105 0.0335  0.0444  153 LEU   A C   
3176 O O   . LEU   A 153 ? 0.1612 0.1649 0.2310 -0.0024 0.0444  0.0497  153 LEU   A O   
3177 C CB  . LEU   A 153 ? 0.1334 0.1581 0.2109 -0.0097 0.0215  0.0404  153 LEU   A CB  
3178 C CG  . LEU   A 153 ? 0.1391 0.1610 0.2066 -0.0180 0.0225  0.0374  153 LEU   A CG  
3179 C CD1 . LEU   A 153 ? 0.1497 0.1586 0.2155 -0.0064 0.0095  0.0322  153 LEU   A CD1 
3180 C CD2 . LEU   A 153 ? 0.1518 0.1676 0.2194 -0.0138 0.0191  0.0145  153 LEU   A CD2 
3192 N N   A ALA   A 154 ? 0.1380 0.1556 0.2030 -0.0024 0.0371  0.0460  154 ALA   A N   
3193 N N   B ALA   A 154 ? 0.1408 0.1635 0.1901 -0.0102 0.0250  0.0420  154 ALA   A N   
3194 C CA  A ALA   A 154 ? 0.1571 0.1569 0.2155 0.0014  0.0348  0.0519  154 ALA   A CA  
3195 C CA  B ALA   A 154 ? 0.1531 0.1702 0.1894 -0.0117 0.0188  0.0431  154 ALA   A CA  
3196 C C   A ALA   A 154 ? 0.1600 0.1569 0.2261 0.0094  0.0466  0.0621  154 ALA   A C   
3197 C C   B ALA   A 154 ? 0.1565 0.1776 0.1821 -0.0116 0.0310  0.0429  154 ALA   A C   
3198 O O   A ALA   A 154 ? 0.1658 0.1610 0.2226 0.0094  0.0365  0.0589  154 ALA   A O   
3199 O O   B ALA   A 154 ? 0.1553 0.1779 0.1581 -0.0170 0.0301  0.0387  154 ALA   A O   
3200 C CB  A ALA   A 154 ? 0.1665 0.1517 0.2232 0.0132  0.0351  0.0380  154 ALA   A CB  
3201 C CB  B ALA   A 154 ? 0.1576 0.1660 0.2025 -0.0062 0.0084  0.0398  154 ALA   A CB  
3212 N N   A VAL   A 155 ? 0.1616 0.1680 0.2533 0.0255  0.0441  0.0769  155 VAL   A N   
3213 N N   B VAL   A 155 ? 0.1615 0.1881 0.2109 -0.0045 0.0407  0.0432  155 VAL   A N   
3214 C CA  A VAL   A 155 ? 0.1691 0.1873 0.2574 0.0247  0.0345  0.0906  155 VAL   A CA  
3215 C CA  B VAL   A 155 ? 0.1660 0.2012 0.2230 -0.0040 0.0417  0.0451  155 VAL   A CA  
3216 C C   A VAL   A 155 ? 0.1745 0.1966 0.2837 0.0355  0.0282  0.0973  155 VAL   A C   
3217 C C   B VAL   A 155 ? 0.1771 0.2078 0.2433 -0.0095 0.0462  0.0617  155 VAL   A C   
3218 O O   A VAL   A 155 ? 0.1716 0.1998 0.2930 0.0434  0.0263  0.0856  155 VAL   A O   
3219 O O   B VAL   A 155 ? 0.1749 0.2060 0.2493 -0.0072 0.0651  0.0686  155 VAL   A O   
3220 C CB  A VAL   A 155 ? 0.1723 0.1939 0.2319 0.0340  0.0186  0.0857  155 VAL   A CB  
3221 C CB  B VAL   A 155 ? 0.1666 0.2083 0.2129 0.0130  0.0321  0.0247  155 VAL   A CB  
3222 C CG1 A VAL   A 155 ? 0.1937 0.2100 0.2304 0.0364  0.0093  0.0821  155 VAL   A CG1 
3223 C CG1 B VAL   A 155 ? 0.1720 0.2125 0.1982 0.0233  0.0335  0.0183  155 VAL   A CG1 
3224 C CG2 A VAL   A 155 ? 0.1807 0.2044 0.2520 0.0315  -0.0051 0.0705  155 VAL   A CG2 
3225 C CG2 B VAL   A 155 ? 0.1646 0.2140 0.2245 0.0167  0.0215  0.0188  155 VAL   A CG2 
3244 N N   A PHE   A 156 ? 0.1815 0.1949 0.3144 0.0415  0.0399  0.1168  156 PHE   A N   
3245 N N   B PHE   A 156 ? 0.1907 0.2152 0.2696 -0.0121 0.0361  0.0721  156 PHE   A N   
3246 C CA  A PHE   A 156 ? 0.2113 0.1975 0.3516 0.0503  0.0373  0.1177  156 PHE   A CA  
3247 C CA  B PHE   A 156 ? 0.2166 0.2296 0.2967 -0.0088 0.0220  0.0676  156 PHE   A CA  
3248 C C   A PHE   A 156 ? 0.2111 0.2043 0.3628 0.0618  0.0502  0.1070  156 PHE   A C   
3249 C C   B PHE   A 156 ? 0.2193 0.2366 0.3037 -0.0151 0.0351  0.0802  156 PHE   A C   
3250 O O   A PHE   A 156 ? 0.2140 0.2070 0.3795 0.0574  0.0525  0.0880  156 PHE   A O   
3251 O O   B PHE   A 156 ? 0.2213 0.2360 0.3169 -0.0234 0.0431  0.0827  156 PHE   A O   
3252 C CB  A PHE   A 156 ? 0.2428 0.1938 0.3628 0.0408  0.0273  0.1345  156 PHE   A CB  
3253 C CB  B PHE   A 156 ? 0.2385 0.2362 0.3160 0.0008  0.0003  0.0512  156 PHE   A CB  
3254 C CG  A PHE   A 156 ? 0.2776 0.2042 0.3878 0.0430  0.0131  0.1144  156 PHE   A CG  
3255 C CG  B PHE   A 156 ? 0.2610 0.2473 0.3360 0.0134  -0.0223 0.0264  156 PHE   A CG  
3256 C CD1 A PHE   A 156 ? 0.2870 0.2131 0.3957 0.0423  0.0126  0.0993  156 PHE   A CD1 
3257 C CD1 B PHE   A 156 ? 0.2704 0.2542 0.3416 0.0220  -0.0353 0.0182  156 PHE   A CD1 
3258 C CD2 A PHE   A 156 ? 0.2882 0.2122 0.3945 0.0496  0.0134  0.1195  156 PHE   A CD2 
3259 C CD2 B PHE   A 156 ? 0.2676 0.2535 0.3477 0.0182  -0.0271 0.0184  156 PHE   A CD2 
3260 C CE1 A PHE   A 156 ? 0.2971 0.2221 0.4090 0.0468  0.0130  0.0936  156 PHE   A CE1 
3261 C CE1 B PHE   A 156 ? 0.2775 0.2582 0.3514 0.0219  -0.0381 0.0087  156 PHE   A CE1 
3262 C CE2 A PHE   A 156 ? 0.3058 0.2254 0.4016 0.0500  0.0113  0.1114  156 PHE   A CE2 
3263 C CE2 B PHE   A 156 ? 0.2754 0.2584 0.3518 0.0197  -0.0316 0.0118  156 PHE   A CE2 
3264 C CZ  A PHE   A 156 ? 0.3072 0.2279 0.4163 0.0536  0.0132  0.0872  156 PHE   A CZ  
3265 C CZ  B PHE   A 156 ? 0.2791 0.2601 0.3545 0.0232  -0.0343 0.0052  156 PHE   A CZ  
3284 N N   A ASP   A 157 ? 0.2093 0.2161 0.3293 0.0693  0.0466  0.1350  157 ASP   A N   
3285 N N   B ASP   A 157 ? 0.2156 0.2476 0.2954 -0.0141 0.0341  0.0965  157 ASP   A N   
3286 C CA  A ASP   A 157 ? 0.2247 0.2414 0.3426 0.0648  0.0385  0.1486  157 ASP   A CA  
3287 C CA  B ASP   A 157 ? 0.2144 0.2591 0.2882 -0.0049 0.0289  0.1025  157 ASP   A CA  
3288 C C   A ASP   A 157 ? 0.1958 0.2641 0.3544 0.0744  0.0500  0.1595  157 ASP   A C   
3289 C C   B ASP   A 157 ? 0.2191 0.2766 0.2853 0.0082  0.0301  0.1069  157 ASP   A C   
3290 O O   A ASP   A 157 ? 0.1845 0.2683 0.3539 0.0743  0.0623  0.1612  157 ASP   A O   
3291 O O   B ASP   A 157 ? 0.2136 0.2807 0.2822 0.0101  0.0393  0.1071  157 ASP   A O   
3292 C CB  A ASP   A 157 ? 0.2558 0.2523 0.3638 0.0600  0.0256  0.1340  157 ASP   A CB  
3293 C CB  B ASP   A 157 ? 0.2019 0.2539 0.2813 0.0004  0.0324  0.1045  157 ASP   A CB  
3294 C CG  A ASP   A 157 ? 0.2844 0.2647 0.4142 0.0619  0.0030  0.1171  157 ASP   A CG  
3295 C CG  B ASP   A 157 ? 0.1881 0.2474 0.2892 0.0084  0.0282  0.1085  157 ASP   A CG  
3296 O OD1 A ASP   A 157 ? 0.3097 0.2779 0.4385 0.0565  -0.0095 0.0955  157 ASP   A OD1 
3297 O OD1 B ASP   A 157 ? 0.1846 0.2426 0.3293 0.0062  0.0184  0.1035  157 ASP   A OD1 
3298 O OD2 A ASP   A 157 ? 0.2836 0.2602 0.4506 0.0576  0.0002  0.1309  157 ASP   A OD2 
3299 O OD2 B ASP   A 157 ? 0.1797 0.2439 0.2740 0.0128  0.0244  0.1153  157 ASP   A OD2 
3308 N N   A LYS   A 158 ? 0.2008 0.2881 0.3781 0.0680  0.0628  0.1589  158 LYS   A N   
3309 N N   B LYS   A 158 ? 0.2351 0.2882 0.2874 0.0105  0.0289  0.1058  158 LYS   A N   
3310 C CA  A LYS   A 158 ? 0.2032 0.3136 0.3947 0.0673  0.0747  0.1341  158 LYS   A CA  
3311 C CA  B LYS   A 158 ? 0.2479 0.2998 0.2944 0.0166  0.0194  0.0931  158 LYS   A CA  
3312 C C   A LYS   A 158 ? 0.1825 0.3221 0.3846 0.0641  0.0666  0.1530  158 LYS   A C   
3313 C C   B LYS   A 158 ? 0.2437 0.3027 0.2982 0.0279  0.0036  0.0980  158 LYS   A C   
3314 O O   A LYS   A 158 ? 0.1731 0.3258 0.3927 0.0572  0.0757  0.1482  158 LYS   A O   
3315 O O   B LYS   A 158 ? 0.2426 0.3006 0.3082 0.0330  -0.0055 0.0935  158 LYS   A O   
3316 C CB  A LYS   A 158 ? 0.2230 0.3306 0.4144 0.0666  0.0924  0.1015  158 LYS   A CB  
3317 C CB  B LYS   A 158 ? 0.2658 0.3075 0.3003 0.0096  0.0243  0.0748  158 LYS   A CB  
3318 C CG  A LYS   A 158 ? 0.2342 0.3430 0.4219 0.0697  0.1051  0.0842  158 LYS   A CG  
3319 C CG  B LYS   A 158 ? 0.2832 0.3142 0.3126 0.0052  0.0209  0.0583  158 LYS   A CG  
3320 C CD  A LYS   A 158 ? 0.2453 0.3534 0.4422 0.0701  0.1127  0.0848  158 LYS   A CD  
3321 C CD  B LYS   A 158 ? 0.2947 0.3165 0.3202 0.0080  0.0120  0.0499  158 LYS   A CD  
3322 C CE  A LYS   A 158 ? 0.2532 0.3553 0.4467 0.0604  0.1227  0.1045  158 LYS   A CE  
3323 C CE  B LYS   A 158 ? 0.3022 0.3178 0.3272 0.0148  0.0012  0.0404  158 LYS   A CE  
3324 N NZ  A LYS   A 158 ? 0.2454 0.3530 0.4456 0.0541  0.1359  0.1205  158 LYS   A NZ  
3325 N NZ  B LYS   A 158 ? 0.3047 0.3185 0.3331 0.0185  -0.0021 0.0372  158 LYS   A NZ  
3352 N N   A ASN   A 159 ? 0.1795 0.3272 0.3959 0.0678  0.0542  0.1540  159 ASN   A N   
3353 N N   B ASN   A 159 ? 0.2447 0.3103 0.3138 0.0319  0.0070  0.0893  159 ASN   A N   
3354 C CA  A ASN   A 159 ? 0.1801 0.3240 0.3840 0.0627  0.0255  0.1686  159 ASN   A CA  
3355 C CA  B ASN   A 159 ? 0.2471 0.3139 0.3252 0.0316  0.0082  0.0835  159 ASN   A CA  
3356 C C   A ASN   A 159 ? 0.1701 0.3268 0.3525 0.0458  0.0244  0.1627  159 ASN   A C   
3357 C C   B ASN   A 159 ? 0.2368 0.3147 0.3068 0.0309  0.0161  0.0768  159 ASN   A C   
3358 O O   A ASN   A 159 ? 0.1514 0.3278 0.3300 0.0375  0.0011  0.1456  159 ASN   A O   
3359 O O   B ASN   A 159 ? 0.2338 0.3182 0.3042 0.0262  0.0120  0.0648  159 ASN   A O   
3360 C CB  A ASN   A 159 ? 0.2068 0.3308 0.4298 0.0627  0.0033  0.1662  159 ASN   A CB  
3361 C CB  B ASN   A 159 ? 0.2647 0.3221 0.3615 0.0297  0.0005  0.0781  159 ASN   A CB  
3362 C CG  A ASN   A 159 ? 0.2367 0.3400 0.4896 0.0595  -0.0057 0.1480  159 ASN   A CG  
3363 C CG  B ASN   A 159 ? 0.2809 0.3282 0.4023 0.0270  -0.0044 0.0655  159 ASN   A CG  
3364 O OD1 A ASN   A 159 ? 0.2404 0.3516 0.5160 0.0581  0.0065  0.1373  159 ASN   A OD1 
3365 O OD1 B ASN   A 159 ? 0.2922 0.3351 0.4242 0.0223  -0.0068 0.0547  159 ASN   A OD1 
3366 N ND2 A ASN   A 159 ? 0.2560 0.3491 0.5207 0.0506  -0.0072 0.1302  159 ASN   A ND2 
3367 N ND2 B ASN   A 159 ? 0.2813 0.3339 0.4151 0.0280  0.0020  0.0618  159 ASN   A ND2 
3380 N N   A LEU   A 160 ? 0.1642 0.3170 0.3418 0.0413  0.0123  0.1661  160 LEU   A N   
3381 N N   B LEU   A 160 ? 0.2234 0.3059 0.2902 0.0327  0.0138  0.0804  160 LEU   A N   
3382 C CA  A LEU   A 160 ? 0.1645 0.3083 0.3110 0.0236  0.0288  0.1625  160 LEU   A CA  
3383 C CA  B LEU   A 160 ? 0.2125 0.2961 0.2645 0.0293  0.0175  0.0803  160 LEU   A CA  
3384 C C   A LEU   A 160 ? 0.1463 0.3123 0.2939 0.0138  0.0339  0.1580  160 LEU   A C   
3385 C C   B LEU   A 160 ? 0.1976 0.2925 0.2473 0.0275  0.0184  0.0811  160 LEU   A C   
3386 O O   A LEU   A 160 ? 0.1453 0.3316 0.3104 0.0141  0.0301  0.1519  160 LEU   A O   
3387 O O   B LEU   A 160 ? 0.1949 0.3018 0.2497 0.0279  0.0152  0.0790  160 LEU   A O   
3388 C CB  A LEU   A 160 ? 0.1728 0.3003 0.2940 0.0098  0.0408  0.1514  160 LEU   A CB  
3389 C CB  B LEU   A 160 ? 0.2147 0.2920 0.2577 0.0246  0.0215  0.0729  160 LEU   A CB  
3390 C CG  A LEU   A 160 ? 0.1830 0.2947 0.2971 -0.0056 0.0339  0.1268  160 LEU   A CG  
3391 C CG  B LEU   A 160 ? 0.2174 0.2915 0.2591 0.0188  0.0186  0.0584  160 LEU   A CG  
3392 C CD1 A LEU   A 160 ? 0.1980 0.3013 0.3132 -0.0148 0.0335  0.1072  160 LEU   A CD1 
3393 C CD1 B LEU   A 160 ? 0.2211 0.2947 0.2649 0.0134  0.0231  0.0508  160 LEU   A CD1 
3394 C CD2 A LEU   A 160 ? 0.1848 0.2874 0.2860 -0.0123 0.0478  0.1191  160 LEU   A CD2 
3395 C CD2 B LEU   A 160 ? 0.2196 0.2888 0.2591 0.0151  0.0211  0.0509  160 LEU   A CD2 
3418 N N   A TYR   A 161 ? 0.1519 0.2983 0.2731 0.0124  0.0467  0.1529  161 TYR   A N   
3419 N N   B TYR   A 161 ? 0.1926 0.2825 0.2290 0.0279  0.0257  0.0797  161 TYR   A N   
3420 C CA  A TYR   A 161 ? 0.1581 0.2865 0.2686 0.0081  0.0453  0.1375  161 TYR   A CA  
3421 C CA  B TYR   A 161 ? 0.1899 0.2738 0.2299 0.0268  0.0235  0.0770  161 TYR   A CA  
3422 C C   A TYR   A 161 ? 0.1520 0.3039 0.2847 -0.0002 0.0295  0.1317  161 TYR   A C   
3423 C C   B TYR   A 161 ? 0.1899 0.2901 0.2391 0.0237  0.0116  0.0766  161 TYR   A C   
3424 O O   A TYR   A 161 ? 0.1412 0.3052 0.2724 -0.0071 0.0325  0.1176  161 TYR   A O   
3425 O O   B TYR   A 161 ? 0.1838 0.2896 0.2203 0.0211  0.0068  0.0739  161 TYR   A O   
3426 C CB  A TYR   A 161 ? 0.1742 0.2704 0.2780 0.0096  0.0414  0.1258  161 TYR   A CB  
3427 C CB  B TYR   A 161 ? 0.1870 0.2550 0.2270 0.0285  0.0305  0.0686  161 TYR   A CB  
3428 C CG  A TYR   A 161 ? 0.1731 0.2483 0.2772 0.0165  0.0374  0.1006  161 TYR   A CG  
3429 C CG  B TYR   A 161 ? 0.1796 0.2387 0.2246 0.0309  0.0354  0.0531  161 TYR   A CG  
3430 C CD1 A TYR   A 161 ? 0.1649 0.2340 0.2845 0.0124  0.0290  0.0874  161 TYR   A CD1 
3431 C CD1 B TYR   A 161 ? 0.1718 0.2298 0.2327 0.0299  0.0327  0.0422  161 TYR   A CD1 
3432 C CD2 A TYR   A 161 ? 0.1741 0.2506 0.2933 0.0197  0.0288  0.0951  161 TYR   A CD2 
3433 C CD2 B TYR   A 161 ? 0.1781 0.2363 0.2352 0.0324  0.0330  0.0470  161 TYR   A CD2 
3434 C CE1 A TYR   A 161 ? 0.1716 0.2367 0.2981 0.0091  0.0175  0.0937  161 TYR   A CE1 
3435 C CE1 B TYR   A 161 ? 0.1754 0.2248 0.2302 0.0275  0.0272  0.0411  161 TYR   A CE1 
3436 C CE2 A TYR   A 161 ? 0.1780 0.2440 0.2988 0.0127  0.0217  0.1036  161 TYR   A CE2 
3437 C CE2 B TYR   A 161 ? 0.1784 0.2294 0.2353 0.0298  0.0282  0.0478  161 TYR   A CE2 
3438 C CZ  A TYR   A 161 ? 0.1832 0.2350 0.3012 0.0032  0.0122  0.1071  161 TYR   A CZ  
3439 C CZ  B TYR   A 161 ? 0.1819 0.2228 0.2345 0.0249  0.0253  0.0429  161 TYR   A CZ  
3440 O OH  A TYR   A 161 ? 0.1954 0.2297 0.3109 -0.0067 -0.0072 0.1148  161 TYR   A OH  
3441 O OH  B TYR   A 161 ? 0.1921 0.2192 0.2382 0.0212  0.0162  0.0380  161 TYR   A OH  
3460 N N   A ASP   A 162 ? 0.1456 0.3209 0.3148 0.0070  0.0412  0.1392  162 ASP   A N   
3461 N N   B ASP   A 162 ? 0.1922 0.3062 0.2669 0.0249  0.0154  0.0798  162 ASP   A N   
3462 C CA  A ASP   A 162 ? 0.1426 0.3489 0.3248 0.0037  0.0436  0.1267  162 ASP   A CA  
3463 C CA  B ASP   A 162 ? 0.1985 0.3280 0.2825 0.0187  0.0128  0.0765  162 ASP   A CA  
3464 C C   A ASP   A 162 ? 0.1359 0.3586 0.3051 0.0048  0.0482  0.1283  162 ASP   A C   
3465 C C   B ASP   A 162 ? 0.2010 0.3407 0.2791 0.0139  0.0083  0.0850  162 ASP   A C   
3466 O O   A ASP   A 162 ? 0.1425 0.3641 0.3317 0.0080  0.0425  0.1119  162 ASP   A O   
3467 O O   B ASP   A 162 ? 0.2029 0.3410 0.2844 0.0115  0.0002  0.0824  162 ASP   A O   
3468 C CB  A ASP   A 162 ? 0.1480 0.3717 0.3543 0.0103  0.0452  0.1004  162 ASP   A CB  
3469 C CB  B ASP   A 162 ? 0.2024 0.3403 0.3055 0.0220  0.0174  0.0591  162 ASP   A CB  
3470 C CG  A ASP   A 162 ? 0.1625 0.3955 0.3807 0.0180  0.0495  0.0813  162 ASP   A CG  
3471 C CG  B ASP   A 162 ? 0.2118 0.3533 0.3292 0.0255  0.0191  0.0482  162 ASP   A CG  
3472 O OD1 A ASP   A 162 ? 0.1755 0.4072 0.3878 0.0102  0.0553  0.0748  162 ASP   A OD1 
3473 O OD1 B ASP   A 162 ? 0.2183 0.3590 0.3340 0.0218  0.0258  0.0490  162 ASP   A OD1 
3474 O OD2 A ASP   A 162 ? 0.1758 0.4073 0.4080 0.0351  0.0501  0.0631  162 ASP   A OD2 
3475 O OD2 B ASP   A 162 ? 0.2173 0.3609 0.3467 0.0341  0.0166  0.0365  162 ASP   A OD2 
3484 N N   A LYS   A 163 ? 0.1616 0.3692 0.3094 0.0108  0.0146  0.1267  163 LYS   A N   
3485 N N   B LYS   A 163 ? 0.2113 0.3545 0.2934 0.0120  0.0022  0.0868  163 LYS   A N   
3486 C CA  A LYS   A 163 ? 0.1827 0.3752 0.3085 0.0100  0.0055  0.1147  163 LYS   A CA  
3487 C CA  B LYS   A 163 ? 0.2193 0.3649 0.3060 0.0087  0.0030  0.0837  163 LYS   A CA  
3488 C C   A LYS   A 163 ? 0.1794 0.3689 0.3048 -0.0014 0.0106  0.1015  163 LYS   A C   
3489 C C   B LYS   A 163 ? 0.1959 0.3605 0.2904 0.0003  0.0075  0.0888  163 LYS   A C   
3490 O O   A LYS   A 163 ? 0.1744 0.3803 0.3259 -0.0073 0.0061  0.0993  163 LYS   A O   
3491 O O   B LYS   A 163 ? 0.1933 0.3679 0.2944 -0.0023 0.0057  0.0891  163 LYS   A O   
3492 C CB  A LYS   A 163 ? 0.2242 0.3948 0.3453 0.0209  -0.0111 0.1035  163 LYS   A CB  
3493 C CB  B LYS   A 163 ? 0.2555 0.3811 0.3478 0.0140  -0.0022 0.0722  163 LYS   A CB  
3494 C CG  A LYS   A 163 ? 0.2647 0.4125 0.3993 0.0227  -0.0097 0.0892  163 LYS   A CG  
3495 C CG  B LYS   A 163 ? 0.2895 0.3946 0.3965 0.0152  -0.0009 0.0604  163 LYS   A CG  
3496 C CD  A LYS   A 163 ? 0.3159 0.4283 0.4646 0.0221  -0.0097 0.0752  163 LYS   A CD  
3497 C CD  B LYS   A 163 ? 0.3301 0.4068 0.4485 0.0157  -0.0008 0.0498  163 LYS   A CD  
3498 C CE  A LYS   A 163 ? 0.3494 0.4391 0.5141 0.0187  -0.0086 0.0709  163 LYS   A CE  
3499 C CE  B LYS   A 163 ? 0.3572 0.4153 0.4878 0.0154  0.0006  0.0459  163 LYS   A CE  
3500 N NZ  A LYS   A 163 ? 0.3570 0.4455 0.5413 0.0163  -0.0075 0.0717  163 LYS   A NZ  
3501 N NZ  B LYS   A 163 ? 0.3603 0.4198 0.5106 0.0156  0.0005  0.0446  163 LYS   A NZ  
3528 N N   . LEU   A 164 ? 0.1643 0.3436 0.2719 -0.0050 0.0042  0.0992  164 LEU   A N   
3529 C CA  . LEU   A 164 ? 0.1743 0.3195 0.2583 -0.0110 0.0235  0.0882  164 LEU   A CA  
3530 C C   . LEU   A 164 ? 0.1790 0.3227 0.2608 -0.0171 0.0216  0.0821  164 LEU   A C   
3531 O O   . LEU   A 164 ? 0.1819 0.3206 0.2652 -0.0175 0.0330  0.0752  164 LEU   A O   
3532 C CB  . LEU   A 164 ? 0.1666 0.3011 0.2590 -0.0132 0.0224  0.0914  164 LEU   A CB  
3533 C CG  . LEU   A 164 ? 0.1679 0.2831 0.2743 -0.0058 0.0297  0.0940  164 LEU   A CG  
3534 C CD1 . LEU   A 164 ? 0.1582 0.2783 0.2680 -0.0008 0.0275  0.0907  164 LEU   A CD1 
3535 C CD2 . LEU   A 164 ? 0.1743 0.2797 0.2968 -0.0035 0.0279  0.0844  164 LEU   A CD2 
3548 N N   . VAL   A 165 ? 0.1724 0.3219 0.2356 -0.0191 0.0263  0.0968  165 VAL   A N   
3549 C CA  . VAL   A 165 ? 0.1776 0.3260 0.2251 -0.0218 0.0380  0.1090  165 VAL   A CA  
3550 C C   . VAL   A 165 ? 0.1771 0.3460 0.2509 -0.0149 0.0264  0.0994  165 VAL   A C   
3551 O O   . VAL   A 165 ? 0.1747 0.3447 0.2581 -0.0152 0.0270  0.0904  165 VAL   A O   
3552 C CB  . VAL   A 165 ? 0.2044 0.3174 0.2412 -0.0190 0.0416  0.0983  165 VAL   A CB  
3553 C CG1 . VAL   A 165 ? 0.2218 0.3287 0.2540 -0.0212 0.0468  0.0825  165 VAL   A CG1 
3554 C CG2 . VAL   A 165 ? 0.2218 0.3115 0.2490 -0.0128 0.0339  0.1018  165 VAL   A CG2 
3564 N N   A SER   A 166 ? 0.1623 0.3563 0.2694 -0.0123 0.0229  0.0884  166 SER   A N   
3565 N N   B SER   A 166 ? 0.1724 0.3552 0.2631 -0.0096 0.0204  0.0885  166 SER   A N   
3566 C CA  A SER   A 166 ? 0.1768 0.3770 0.2961 -0.0186 0.0156  0.0768  166 SER   A CA  
3567 C CA  B SER   A 166 ? 0.1828 0.3695 0.2805 -0.0097 0.0128  0.0773  166 SER   A CA  
3568 C C   A SER   A 166 ? 0.1830 0.3860 0.3074 -0.0217 -0.0007 0.0662  166 SER   A C   
3569 C C   B SER   A 166 ? 0.1811 0.3767 0.2904 -0.0090 -0.0004 0.0710  166 SER   A C   
3570 O O   A SER   A 166 ? 0.1971 0.3998 0.3426 -0.0347 0.0006  0.0500  166 SER   A O   
3571 O O   B SER   A 166 ? 0.1805 0.3794 0.3042 -0.0103 -0.0021 0.0664  166 SER   A O   
3572 C CB  A SER   A 166 ? 0.1927 0.3920 0.3285 -0.0056 0.0123  0.0622  166 SER   A CB  
3573 C CB  B SER   A 166 ? 0.1977 0.3785 0.3014 -0.0018 0.0143  0.0649  166 SER   A CB  
3574 O OG  A SER   A 166 ? 0.2277 0.4032 0.3632 -0.0098 0.0199  0.0674  166 SER   A OG  
3575 O OG  B SER   A 166 ? 0.2201 0.3859 0.3278 -0.0030 0.0208  0.0641  166 SER   A OG  
3586 N N   . SER   A 167 ? 0.1822 0.3858 0.2886 -0.0034 -0.0115 0.0711  167 SER   A N   
3587 C CA  . SER   A 167 ? 0.2198 0.3835 0.2872 0.0045  -0.0192 0.0617  167 SER   A CA  
3588 C C   . SER   A 167 ? 0.2349 0.3818 0.3007 0.0081  -0.0102 0.0600  167 SER   A C   
3589 O O   . SER   A 167 ? 0.2548 0.3767 0.3092 0.0062  -0.0140 0.0616  167 SER   A O   
3590 C CB  . SER   A 167 ? 0.2367 0.3916 0.2958 0.0112  -0.0138 0.0602  167 SER   A CB  
3591 O OG  . SER   A 167 ? 0.2408 0.3974 0.3026 0.0197  -0.0045 0.0638  167 SER   A OG  
3598 N N   . PHE   A 168 ? 0.2287 0.3853 0.3092 0.0172  -0.0183 0.0621  168 PHE   A N   
3599 C CA  . PHE   A 168 ? 0.2471 0.3926 0.3423 0.0112  -0.0126 0.0585  168 PHE   A CA  
3600 C C   . PHE   A 168 ? 0.3198 0.4378 0.4355 -0.0092 -0.0087 0.0410  168 PHE   A C   
3601 O O   . PHE   A 168 ? 0.3219 0.4384 0.4676 -0.0169 0.0148  0.0510  168 PHE   A O   
3602 C CB  . PHE   A 168 ? 0.2109 0.3634 0.3092 0.0103  -0.0124 0.0692  168 PHE   A CB  
3603 C CG  . PHE   A 168 ? 0.1894 0.3433 0.2834 -0.0001 -0.0085 0.0703  168 PHE   A CG  
3604 C CD1 . PHE   A 168 ? 0.1844 0.3386 0.2780 -0.0080 -0.0075 0.0797  168 PHE   A CD1 
3605 C CD2 . PHE   A 168 ? 0.1801 0.3338 0.2734 0.0014  0.0131  0.0637  168 PHE   A CD2 
3606 C CE1 . PHE   A 168 ? 0.1727 0.3297 0.2810 -0.0062 0.0007  0.0872  168 PHE   A CE1 
3607 C CE2 . PHE   A 168 ? 0.1821 0.3235 0.2851 -0.0024 0.0214  0.0691  168 PHE   A CE2 
3608 C CZ  . PHE   A 168 ? 0.1787 0.3259 0.2869 -0.0096 0.0078  0.0770  168 PHE   A CZ  
3618 N N   . LEU   A 169 ? 0.4046 0.4827 0.5145 -0.0230 -0.0270 0.0103  169 LEU   A N   
3619 C CA  . LEU   A 169 ? 0.5038 0.5337 0.6118 -0.0317 -0.0405 -0.0147 169 LEU   A CA  
3620 C C   . LEU   A 169 ? 0.5437 0.5473 0.6465 -0.0367 -0.0466 -0.0183 169 LEU   A C   
3621 O O   . LEU   A 169 ? 0.5540 0.5513 0.6516 -0.0387 -0.0488 -0.0226 169 LEU   A O   
3622 C CB  . LEU   A 169 ? 0.5521 0.5650 0.6508 -0.0384 -0.0453 -0.0359 169 LEU   A CB  
3623 C CG  . LEU   A 169 ? 0.5842 0.5877 0.6876 -0.0435 -0.0462 -0.0561 169 LEU   A CG  
3624 C CD1 . LEU   A 169 ? 0.5962 0.5964 0.7030 -0.0438 -0.0498 -0.0636 169 LEU   A CD1 
3625 C CD2 . LEU   A 169 ? 0.5940 0.5949 0.6985 -0.0460 -0.0422 -0.0623 169 LEU   A CD2 
3626 O OXT . LEU   A 169 ? 0.5479 0.5502 0.6503 -0.0394 -0.0416 -0.0167 169 LEU   A OXT 
3638 N N   A SER   B 1   ? 0.3575 0.3242 0.3589 -0.1170 -0.0868 0.0225  1   SER   B N   
3639 N N   B SER   B 1   ? 0.3419 0.3062 0.3250 -0.0812 -0.0454 0.0014  1   SER   B N   
3640 C CA  A SER   B 1   ? 0.3477 0.3365 0.3615 -0.1241 -0.0968 0.0203  1   SER   B CA  
3641 C CA  B SER   B 1   ? 0.3359 0.3127 0.3253 -0.0843 -0.0472 0.0014  1   SER   B CA  
3642 C C   A SER   B 1   ? 0.3210 0.3361 0.3465 -0.1264 -0.1003 0.0425  1   SER   B C   
3643 C C   B SER   B 1   ? 0.3191 0.3168 0.3143 -0.0821 -0.0526 0.0191  1   SER   B C   
3644 O O   A SER   B 1   ? 0.3378 0.3411 0.3238 -0.1090 -0.0896 0.0411  1   SER   B O   
3645 O O   B SER   B 1   ? 0.3229 0.3168 0.2927 -0.0751 -0.0506 0.0160  1   SER   B O   
3646 C CB  A SER   B 1   ? 0.3620 0.3423 0.3786 -0.1238 -0.0879 -0.0031 1   SER   B CB  
3647 C CB  B SER   B 1   ? 0.3449 0.3115 0.3377 -0.0860 -0.0367 -0.0189 1   SER   B CB  
3648 O OG  A SER   B 1   ? 0.3805 0.3604 0.4400 -0.1170 -0.0693 -0.0089 1   SER   B OG  
3649 O OG  B SER   B 1   ? 0.3547 0.3158 0.3701 -0.0858 -0.0320 -0.0318 1   SER   B OG  
3664 N N   A MET   B 2   ? 0.2955 0.3315 0.3506 -0.1335 -0.0870 0.0919  2   MET   B N   
3665 N N   B MET   B 2   ? 0.3071 0.3227 0.3205 -0.0808 -0.0478 0.0531  2   MET   B N   
3666 C CA  A MET   B 2   ? 0.2808 0.3362 0.3614 -0.1137 -0.0828 0.1131  2   MET   B CA  
3667 C CA  B MET   B 2   ? 0.2972 0.3305 0.3235 -0.0700 -0.0453 0.0714  2   MET   B CA  
3668 C C   A MET   B 2   ? 0.2456 0.3284 0.3353 -0.0905 -0.0929 0.1345  2   MET   B C   
3669 C C   B MET   B 2   ? 0.2749 0.3207 0.2885 -0.0639 -0.0425 0.0819  2   MET   B C   
3670 O O   A MET   B 2   ? 0.2362 0.3403 0.3366 -0.0754 -0.1104 0.1465  2   MET   B O   
3671 O O   B MET   B 2   ? 0.2736 0.3242 0.2799 -0.0592 -0.0412 0.0818  2   MET   B O   
3672 C CB  A MET   B 2   ? 0.3117 0.3671 0.4438 -0.0904 -0.0565 0.0831  2   MET   B CB  
3673 C CB  B MET   B 2   ? 0.3130 0.3541 0.3776 -0.0564 -0.0400 0.0662  2   MET   B CB  
3674 C CG  A MET   B 2   ? 0.3438 0.3981 0.5318 -0.0656 -0.0287 0.0646  2   MET   B CG  
3675 C CG  B MET   B 2   ? 0.3283 0.3762 0.4325 -0.0419 -0.0321 0.0680  2   MET   B CG  
3676 S SD  A MET   B 2   ? 0.3772 0.4303 0.6184 -0.0419 -0.0029 0.0502  2   MET   B SD  
3677 S SD  B MET   B 2   ? 0.3444 0.3999 0.4868 -0.0257 -0.0259 0.0679  2   MET   B SD  
3678 C CE  A MET   B 2   ? 0.3772 0.4314 0.6110 -0.0432 0.0057  0.0497  2   MET   B CE  
3679 C CE  B MET   B 2   ? 0.3425 0.4015 0.4800 -0.0275 -0.0245 0.0651  2   MET   B CE  
3698 N N   A VAL   B 3   ? 0.2144 0.2960 0.3018 -0.0915 -0.0897 0.1501  3   VAL   B N   
3699 N N   B VAL   B 3   ? 0.2526 0.3038 0.2626 -0.0644 -0.0400 0.0950  3   VAL   B N   
3700 C CA  A VAL   B 3   ? 0.2081 0.2739 0.2959 -0.0860 -0.0851 0.1233  3   VAL   B CA  
3701 C CA  B VAL   B 3   ? 0.2367 0.2891 0.2552 -0.0603 -0.0415 0.0921  3   VAL   B CA  
3702 C C   A VAL   B 3   ? 0.1997 0.2640 0.2724 -0.0735 -0.0709 0.1039  3   VAL   B C   
3703 C C   B VAL   B 3   ? 0.2178 0.2748 0.2358 -0.0583 -0.0422 0.0921  3   VAL   B C   
3704 O O   A VAL   B 3   ? 0.1936 0.2577 0.2882 -0.0665 -0.0738 0.1111  3   VAL   B O   
3705 O O   B VAL   B 3   ? 0.2188 0.2805 0.2326 -0.0457 -0.0388 0.0960  3   VAL   B O   
3706 C CB  A VAL   B 3   ? 0.2334 0.2668 0.3478 -0.0882 -0.0742 0.1039  3   VAL   B CB  
3707 C CB  B VAL   B 3   ? 0.2464 0.2875 0.2775 -0.0577 -0.0376 0.0840  3   VAL   B CB  
3708 C CG1 A VAL   B 3   ? 0.2508 0.2637 0.3755 -0.0881 -0.0702 0.0936  3   VAL   B CG1 
3709 C CG1 B VAL   B 3   ? 0.2528 0.2859 0.2908 -0.0584 -0.0360 0.0770  3   VAL   B CG1 
3710 C CG2 A VAL   B 3   ? 0.2410 0.2668 0.3641 -0.0873 -0.0578 0.1143  3   VAL   B CG2 
3711 C CG2 B VAL   B 3   ? 0.2494 0.2880 0.2804 -0.0556 -0.0341 0.0896  3   VAL   B CG2 
3730 N N   . ASN   B 4   ? 0.2017 0.2459 0.2270 -0.0680 -0.0613 0.0911  4   ASN   B N   
3731 C CA  . ASN   B 4   ? 0.2064 0.2446 0.1878 -0.0642 -0.0551 0.0524  4   ASN   B CA  
3732 C C   . ASN   B 4   ? 0.2102 0.2558 0.1887 -0.0637 -0.0475 0.0476  4   ASN   B C   
3733 O O   . ASN   B 4   ? 0.2112 0.2531 0.2055 -0.0629 -0.0469 0.0237  4   ASN   B O   
3734 C CB  . ASN   B 4   ? 0.2125 0.2278 0.1869 -0.0633 -0.0626 0.0378  4   ASN   B CB  
3735 C CG  . ASN   B 4   ? 0.2106 0.2047 0.1759 -0.0622 -0.0602 0.0364  4   ASN   B CG  
3736 O OD1 . ASN   B 4   ? 0.2091 0.1997 0.1777 -0.0593 -0.0549 0.0354  4   ASN   B OD1 
3737 N ND2 . ASN   B 4   ? 0.2345 0.2034 0.2044 -0.0413 -0.0576 0.0409  4   ASN   B ND2 
3745 N N   . SER   B 5   ? 0.2144 0.2817 0.2179 -0.0611 -0.0312 0.0402  5   SER   B N   
3746 C CA  . SER   B 5   ? 0.2290 0.3127 0.2329 -0.0542 -0.0142 0.0442  5   SER   B CA  
3747 C C   . SER   B 5   ? 0.2543 0.3139 0.2705 -0.0663 0.0097  0.0378  5   SER   B C   
3748 O O   . SER   B 5   ? 0.2724 0.3032 0.3568 -0.0488 0.0546  0.0280  5   SER   B O   
3749 C CB  . SER   B 5   ? 0.2449 0.3349 0.2615 -0.0381 -0.0098 0.0603  5   SER   B CB  
3750 O OG  . SER   B 5   ? 0.2855 0.3618 0.3145 -0.0205 -0.0080 0.0654  5   SER   B OG  
3756 N N   . PHE   B 6   ? 0.2804 0.3286 0.2403 -0.0839 0.0288  0.0395  6   PHE   B N   
3757 C CA  . PHE   B 6   ? 0.2978 0.3294 0.2111 -0.1049 0.0352  0.0170  6   PHE   B CA  
3758 C C   . PHE   B 6   ? 0.3442 0.3594 0.2673 -0.1144 0.0641  -0.0172 6   PHE   B C   
3759 O O   . PHE   B 6   ? 0.3538 0.3899 0.2988 -0.1106 0.0388  -0.0292 6   PHE   B O   
3760 C CB  . PHE   B 6   ? 0.2717 0.3086 0.1724 -0.0951 0.0147  0.0097  6   PHE   B CB  
3761 C CG  . PHE   B 6   ? 0.2383 0.2798 0.1704 -0.0926 -0.0100 0.0104  6   PHE   B CG  
3762 C CD1 . PHE   B 6   ? 0.2373 0.2538 0.1570 -0.0873 -0.0222 0.0160  6   PHE   B CD1 
3763 C CD2 . PHE   B 6   ? 0.2168 0.2750 0.1752 -0.0756 -0.0147 0.0421  6   PHE   B CD2 
3764 C CE1 . PHE   B 6   ? 0.2360 0.2325 0.1730 -0.0699 -0.0195 0.0260  6   PHE   B CE1 
3765 C CE2 . PHE   B 6   ? 0.2177 0.2594 0.2043 -0.0660 -0.0036 0.0458  6   PHE   B CE2 
3766 C CZ  . PHE   B 6   ? 0.2212 0.2327 0.1986 -0.0663 -0.0194 0.0348  6   PHE   B CZ  
3776 N N   A SER   B 7   ? 0.3723 0.3510 0.2817 -0.1304 0.0969  -0.0434 7   SER   B N   
3777 N N   B SER   B 7   ? 0.3527 0.3466 0.2809 -0.1212 0.0684  -0.0321 7   SER   B N   
3778 C CA  A SER   B 7   ? 0.4042 0.3686 0.3342 -0.1219 0.1124  -0.0556 7   SER   B CA  
3779 C CA  B SER   B 7   ? 0.3626 0.3462 0.3110 -0.1148 0.0642  -0.0396 7   SER   B CA  
3780 C C   A SER   B 7   ? 0.4004 0.3595 0.3242 -0.1261 0.1353  -0.0723 7   SER   B C   
3781 C C   B SER   B 7   ? 0.3543 0.3355 0.3149 -0.1170 0.0708  -0.0490 7   SER   B C   
3782 O O   A SER   B 7   ? 0.4095 0.3626 0.3370 -0.1305 0.1427  -0.0724 7   SER   B O   
3783 O O   B SER   B 7   ? 0.3590 0.3341 0.3271 -0.1234 0.0701  -0.0535 7   SER   B O   
3784 C CB  A SER   B 7   ? 0.4263 0.3826 0.3946 -0.1151 0.1146  -0.0465 7   SER   B CB  
3785 C CB  B SER   B 7   ? 0.3742 0.3482 0.3366 -0.1094 0.0598  -0.0344 7   SER   B CB  
3786 O OG  A SER   B 7   ? 0.4405 0.3934 0.4481 -0.1093 0.1121  -0.0354 7   SER   B OG  
3787 O OG  B SER   B 7   ? 0.3821 0.3493 0.3576 -0.1047 0.0547  -0.0281 7   SER   B OG  
3798 N N   A GLY   B 8   ? 0.3981 0.3515 0.3237 -0.1101 0.1422  -0.0838 8   GLY   B N   
3799 N N   B GLY   B 8   ? 0.3483 0.3289 0.3132 -0.1025 0.0719  -0.0529 8   GLY   B N   
3800 C CA  A GLY   B 8   ? 0.3854 0.3331 0.3190 -0.1017 0.1493  -0.0870 8   GLY   B CA  
3801 C CA  B GLY   B 8   ? 0.3391 0.3171 0.3094 -0.0907 0.0762  -0.0500 8   GLY   B CA  
3802 C C   A GLY   B 8   ? 0.3664 0.3037 0.3073 -0.1001 0.1512  -0.0892 8   GLY   B C   
3803 C C   B GLY   B 8   ? 0.3283 0.3003 0.3034 -0.0840 0.0800  -0.0484 8   GLY   B C   
3804 O O   A GLY   B 8   ? 0.3818 0.3151 0.3387 -0.0844 0.1582  -0.1013 8   GLY   B O   
3805 O O   B GLY   B 8   ? 0.3387 0.3075 0.3269 -0.0736 0.0835  -0.0538 8   GLY   B O   
3812 N N   A TYR   B 9   ? 0.3430 0.2723 0.2799 -0.0995 0.1231  -0.0982 9   TYR   B N   
3813 N N   B TYR   B 9   ? 0.3120 0.2797 0.2805 -0.0849 0.0682  -0.0541 9   TYR   B N   
3814 C CA  A TYR   B 9   ? 0.3190 0.2480 0.2480 -0.0829 0.1002  -0.0831 9   TYR   B CA  
3815 C CA  B TYR   B 9   ? 0.2944 0.2615 0.2501 -0.0807 0.0597  -0.0543 9   TYR   B CA  
3816 C C   A TYR   B 9   ? 0.3067 0.2446 0.2505 -0.0821 0.0631  -0.0672 9   TYR   B C   
3817 C C   B TYR   B 9   ? 0.2929 0.2485 0.2463 -0.0819 0.0457  -0.0554 9   TYR   B C   
3818 O O   A TYR   B 9   ? 0.3114 0.2498 0.2932 -0.0848 0.0569  -0.0561 9   TYR   B O   
3819 O O   B TYR   B 9   ? 0.2955 0.2524 0.2713 -0.0800 0.0433  -0.0518 9   TYR   B O   
3820 C CB  A TYR   B 9   ? 0.3181 0.2264 0.2386 -0.0786 0.0878  -0.0823 9   TYR   B CB  
3821 C CB  B TYR   B 9   ? 0.2831 0.2552 0.2372 -0.0798 0.0535  -0.0548 9   TYR   B CB  
3822 C CG  A TYR   B 9   ? 0.3153 0.2086 0.2347 -0.0885 0.0763  -0.0873 9   TYR   B CG  
3823 C CG  B TYR   B 9   ? 0.2702 0.2490 0.2278 -0.0872 0.0466  -0.0543 9   TYR   B CG  
3824 C CD1 A TYR   B 9   ? 0.3185 0.2056 0.2445 -0.0973 0.0830  -0.0824 9   TYR   B CD1 
3825 C CD1 B TYR   B 9   ? 0.2664 0.2481 0.2300 -0.0919 0.0510  -0.0510 9   TYR   B CD1 
3826 C CD2 A TYR   B 9   ? 0.3107 0.2065 0.2316 -0.0827 0.0700  -0.0942 9   TYR   B CD2 
3827 C CD2 B TYR   B 9   ? 0.2637 0.2489 0.2194 -0.0884 0.0412  -0.0577 9   TYR   B CD2 
3828 C CE1 A TYR   B 9   ? 0.3210 0.2094 0.2458 -0.1005 0.0812  -0.0903 9   TYR   B CE1 
3829 C CE1 B TYR   B 9   ? 0.2639 0.2504 0.2336 -0.0943 0.0439  -0.0555 9   TYR   B CE1 
3830 C CE2 A TYR   B 9   ? 0.3166 0.2047 0.2438 -0.0864 0.0663  -0.0860 9   TYR   B CE2 
3831 C CE2 B TYR   B 9   ? 0.2634 0.2489 0.2240 -0.0906 0.0367  -0.0537 9   TYR   B CE2 
3832 C CZ  A TYR   B 9   ? 0.3196 0.2107 0.2502 -0.0935 0.0714  -0.1025 9   TYR   B CZ  
3833 C CZ  B TYR   B 9   ? 0.2620 0.2516 0.2299 -0.0948 0.0345  -0.0595 9   TYR   B CZ  
3834 O OH  A TYR   B 9   ? 0.3184 0.2136 0.2648 -0.0979 0.0787  -0.1087 9   TYR   B OH  
3835 O OH  B TYR   B 9   ? 0.2573 0.2583 0.2443 -0.0980 0.0305  -0.0566 9   TYR   B OH  
3854 N N   . LEU   B 10  ? 0.2875 0.2295 0.2370 -0.0889 0.0370  -0.0562 10  LEU   B N   
3855 C CA  . LEU   B 10  ? 0.2941 0.2297 0.2342 -0.1040 -0.0045 -0.0417 10  LEU   B CA  
3856 C C   . LEU   B 10  ? 0.2847 0.2368 0.2410 -0.0970 -0.0224 -0.0377 10  LEU   B C   
3857 O O   . LEU   B 10  ? 0.2645 0.2423 0.2490 -0.0772 -0.0074 -0.0284 10  LEU   B O   
3858 C CB  . LEU   B 10  ? 0.3243 0.2253 0.2573 -0.1043 -0.0197 -0.0128 10  LEU   B CB  
3859 C CG  . LEU   B 10  ? 0.3553 0.2331 0.2831 -0.0954 -0.0618 -0.0021 10  LEU   B CG  
3860 C CD1 . LEU   B 10  ? 0.3733 0.2375 0.3061 -0.0879 -0.0576 -0.0197 10  LEU   B CD1 
3861 C CD2 . LEU   B 10  ? 0.3641 0.2367 0.3113 -0.0999 -0.0573 0.0236  10  LEU   B CD2 
3874 N N   A LYS   B 11  ? 0.3014 0.2558 0.2454 -0.0917 -0.0342 -0.0307 11  LYS   B N   
3875 N N   B LYS   B 11  ? 0.2983 0.2534 0.2599 -0.0898 -0.0267 -0.0325 11  LYS   B N   
3876 C CA  A LYS   B 11  ? 0.3241 0.2774 0.2810 -0.0799 -0.0359 -0.0390 11  LYS   B CA  
3877 C CA  B LYS   B 11  ? 0.3143 0.2708 0.2936 -0.0798 -0.0268 -0.0364 11  LYS   B CA  
3878 C C   A LYS   B 11  ? 0.3090 0.2501 0.2857 -0.0964 -0.0242 -0.0611 11  LYS   B C   
3879 C C   B LYS   B 11  ? 0.3009 0.2518 0.2883 -0.0910 -0.0226 -0.0527 11  LYS   B C   
3880 O O   A LYS   B 11  ? 0.3300 0.2638 0.3170 -0.1035 -0.0253 -0.0862 11  LYS   B O   
3881 O O   B LYS   B 11  ? 0.3132 0.2637 0.3074 -0.0934 -0.0231 -0.0656 11  LYS   B O   
3882 C CB  A LYS   B 11  ? 0.3592 0.3248 0.3430 -0.0512 -0.0428 -0.0315 11  LYS   B CB  
3883 C CB  B LYS   B 11  ? 0.3417 0.3057 0.3481 -0.0584 -0.0290 -0.0285 11  LYS   B CB  
3884 C CG  A LYS   B 11  ? 0.3903 0.3563 0.4125 -0.0334 -0.0483 -0.0280 11  LYS   B CG  
3885 C CG  B LYS   B 11  ? 0.3655 0.3301 0.4048 -0.0443 -0.0309 -0.0234 11  LYS   B CG  
3886 C CD  A LYS   B 11  ? 0.4117 0.3744 0.4711 -0.0243 -0.0511 -0.0274 11  LYS   B CD  
3887 C CD  B LYS   B 11  ? 0.3825 0.3451 0.4543 -0.0357 -0.0320 -0.0211 11  LYS   B CD  
3888 C CE  A LYS   B 11  ? 0.4270 0.3849 0.5113 -0.0224 -0.0540 -0.0242 11  LYS   B CE  
3889 C CE  B LYS   B 11  ? 0.3945 0.3540 0.4882 -0.0314 -0.0332 -0.0168 11  LYS   B CE  
3890 N NZ  A LYS   B 11  ? 0.4363 0.3922 0.5322 -0.0216 -0.0549 -0.0198 11  LYS   B NZ  
3891 N NZ  B LYS   B 11  ? 0.4012 0.3592 0.5062 -0.0296 -0.0339 -0.0133 11  LYS   B NZ  
3918 N N   . LEU   B 12  ? 0.2746 0.2319 0.2741 -0.0910 -0.0281 -0.0594 12  LEU   B N   
3919 C CA  . LEU   B 12  ? 0.2499 0.2061 0.2878 -0.0720 -0.0125 -0.0524 12  LEU   B CA  
3920 C C   . LEU   B 12  ? 0.2356 0.2037 0.2768 -0.0700 -0.0409 -0.0448 12  LEU   B C   
3921 O O   . LEU   B 12  ? 0.2330 0.2058 0.3071 -0.0697 -0.0654 -0.0299 12  LEU   B O   
3922 C CB  . LEU   B 12  ? 0.2456 0.1804 0.2822 -0.0599 0.0023  -0.0514 12  LEU   B CB  
3923 C CG  . LEU   B 12  ? 0.2457 0.1660 0.2762 -0.0529 0.0148  -0.0459 12  LEU   B CG  
3924 C CD1 . LEU   B 12  ? 0.2503 0.1678 0.2694 -0.0347 0.0094  -0.0170 12  LEU   B CD1 
3925 C CD2 . LEU   B 12  ? 0.2566 0.1756 0.2918 -0.0535 0.0199  -0.0482 12  LEU   B CD2 
3938 N N   . THR   B 13  ? 0.2313 0.2008 0.2849 -0.0693 -0.0288 -0.0464 13  THR   B N   
3939 C CA  . THR   B 13  ? 0.2317 0.2120 0.2831 -0.0740 -0.0632 -0.0380 13  THR   B CA  
3940 C C   . THR   B 13  ? 0.2791 0.2307 0.3190 -0.0927 -0.0885 -0.0354 13  THR   B C   
3941 O O   . THR   B 13  ? 0.3062 0.2375 0.3284 -0.0865 -0.0564 -0.0411 13  THR   B O   
3942 C CB  . THR   B 13  ? 0.2095 0.2157 0.2870 -0.0594 -0.0612 -0.0240 13  THR   B CB  
3943 O OG1 . THR   B 13  ? 0.1954 0.2039 0.2966 -0.0536 -0.0389 -0.0316 13  THR   B OG1 
3944 C CG2 . THR   B 13  ? 0.2130 0.2237 0.2998 -0.0542 -0.0556 0.0012  13  THR   B CG2 
3952 N N   A ASP   B 14  ? 0.2957 0.2541 0.3358 -0.1058 -0.1128 -0.0179 14  ASP   B N   
3953 N N   B ASP   B 14  ? 0.2906 0.2472 0.3290 -0.0934 -0.0981 -0.0163 14  ASP   B N   
3954 C CA  A ASP   B 14  ? 0.3103 0.2690 0.3592 -0.1079 -0.1169 0.0050  14  ASP   B CA  
3955 C CA  B ASP   B 14  ? 0.2991 0.2570 0.3415 -0.0897 -0.0994 0.0032  14  ASP   B CA  
3956 C C   A ASP   B 14  ? 0.2947 0.2467 0.3122 -0.1113 -0.1076 0.0093  14  ASP   B C   
3957 C C   B ASP   B 14  ? 0.2829 0.2387 0.3030 -0.0921 -0.1017 0.0085  14  ASP   B C   
3958 O O   A ASP   B 14  ? 0.3225 0.2664 0.3199 -0.1081 -0.0962 0.0250  14  ASP   B O   
3959 O O   B ASP   B 14  ? 0.2988 0.2423 0.3084 -0.0865 -0.0961 0.0153  14  ASP   B O   
3960 C CB  A ASP   B 14  ? 0.3332 0.3082 0.4310 -0.0964 -0.1303 0.0103  14  ASP   B CB  
3961 C CB  B ASP   B 14  ? 0.3195 0.2850 0.3935 -0.0784 -0.0988 0.0098  14  ASP   B CB  
3962 C CG  A ASP   B 14  ? 0.3552 0.3415 0.4973 -0.0832 -0.1318 -0.0010 14  ASP   B CG  
3963 C CG  B ASP   B 14  ? 0.3371 0.3080 0.4373 -0.0674 -0.0961 0.0055  14  ASP   B CG  
3964 O OD1 A ASP   B 14  ? 0.3706 0.3526 0.5111 -0.0808 -0.1338 -0.0131 14  ASP   B OD1 
3965 O OD1 B ASP   B 14  ? 0.3463 0.3173 0.4480 -0.0634 -0.0940 0.0022  14  ASP   B OD1 
3966 O OD2 A ASP   B 14  ? 0.3556 0.3566 0.5321 -0.0812 -0.1314 0.0028  14  ASP   B OD2 
3967 O OD2 B ASP   B 14  ? 0.3402 0.3164 0.4554 -0.0679 -0.0980 0.0062  14  ASP   B OD2 
3976 N N   . ASN   B 15  ? 0.2538 0.2167 0.2712 -0.0878 -0.1099 0.0161  15  ASN   B N   
3977 C CA  . ASN   B 15  ? 0.2122 0.1865 0.2534 -0.0574 -0.0754 0.0134  15  ASN   B CA  
3978 C C   . ASN   B 15  ? 0.1864 0.1694 0.2364 -0.0379 -0.0546 0.0053  15  ASN   B C   
3979 O O   . ASN   B 15  ? 0.1860 0.1589 0.2509 -0.0368 -0.0526 -0.0040 15  ASN   B O   
3980 C CB  . ASN   B 15  ? 0.2054 0.1811 0.2693 -0.0251 -0.0714 0.0126  15  ASN   B CB  
3981 C CG  . ASN   B 15  ? 0.1831 0.1692 0.2802 -0.0343 -0.0397 0.0108  15  ASN   B CG  
3982 O OD1 . ASN   B 15  ? 0.1902 0.2037 0.3130 -0.0515 -0.0421 0.0111  15  ASN   B OD1 
3983 N ND2 . ASN   B 15  ? 0.1753 0.1483 0.2768 -0.0194 -0.0001 -0.0130 15  ASN   B ND2 
3991 N N   . VAL   B 16  ? 0.1804 0.1666 0.2511 -0.0396 -0.0612 -0.0018 16  VAL   B N   
3992 C CA  . VAL   B 16  ? 0.1753 0.1655 0.2310 -0.0294 -0.0352 -0.0236 16  VAL   B CA  
3993 C C   . VAL   B 16  ? 0.1749 0.1784 0.2306 -0.0393 -0.0355 -0.0169 16  VAL   B C   
3994 O O   . VAL   B 16  ? 0.1733 0.1874 0.2495 -0.0257 -0.0321 -0.0389 16  VAL   B O   
3995 C CB  . VAL   B 16  ? 0.1793 0.1613 0.2263 -0.0148 -0.0205 -0.0309 16  VAL   B CB  
3996 C CG1 . VAL   B 16  ? 0.1885 0.1660 0.2242 0.0022  -0.0126 -0.0309 16  VAL   B CG1 
3997 C CG2 . VAL   B 16  ? 0.1895 0.1643 0.2454 -0.0085 -0.0095 -0.0367 16  VAL   B CG2 
4007 N N   . TYR   B 17  ? 0.1861 0.1933 0.2270 -0.0456 -0.0196 -0.0284 17  TYR   B N   
4008 C CA  . TYR   B 17  ? 0.2019 0.1962 0.2116 -0.0572 -0.0242 -0.0120 17  TYR   B CA  
4009 C C   . TYR   B 17  ? 0.1971 0.1723 0.1963 -0.0487 -0.0139 -0.0259 17  TYR   B C   
4010 O O   . TYR   B 17  ? 0.1867 0.1810 0.2081 -0.0391 -0.0144 -0.0499 17  TYR   B O   
4011 C CB  . TYR   B 17  ? 0.2436 0.2551 0.2539 -0.0364 -0.0263 0.0339  17  TYR   B CB  
4012 C CG  . TYR   B 17  ? 0.2861 0.3212 0.3181 -0.0240 -0.0544 0.0494  17  TYR   B CG  
4013 C CD1 . TYR   B 17  ? 0.3071 0.3489 0.3558 -0.0234 -0.0690 0.0556  17  TYR   B CD1 
4014 C CD2 . TYR   B 17  ? 0.3113 0.3553 0.3502 -0.0153 -0.0721 0.0523  17  TYR   B CD2 
4015 C CE1 . TYR   B 17  ? 0.3252 0.3817 0.3784 -0.0145 -0.0836 0.0539  17  TYR   B CE1 
4016 C CE2 . TYR   B 17  ? 0.3281 0.3858 0.3792 0.0002  -0.0915 0.0612  17  TYR   B CE2 
4017 C CZ  . TYR   B 17  ? 0.3381 0.3988 0.3933 -0.0012 -0.0952 0.0562  17  TYR   B CZ  
4018 O OH  . TYR   B 17  ? 0.3540 0.4112 0.4024 0.0053  -0.0978 0.0587  17  TYR   B OH  
4028 N N   . ILE   B 18  ? 0.2073 0.1792 0.1846 -0.0461 -0.0083 -0.0286 18  ILE   B N   
4029 C CA  . ILE   B 18  ? 0.2100 0.1697 0.1898 -0.0507 0.0048  -0.0388 18  ILE   B CA  
4030 C C   . ILE   B 18  ? 0.2226 0.1747 0.1974 -0.0610 0.0123  -0.0558 18  ILE   B C   
4031 O O   . ILE   B 18  ? 0.2370 0.1895 0.2089 -0.0522 0.0120  -0.0594 18  ILE   B O   
4032 C CB  . ILE   B 18  ? 0.2138 0.1698 0.2139 -0.0491 0.0013  -0.0235 18  ILE   B CB  
4033 C CG1 . ILE   B 18  ? 0.2156 0.1718 0.2326 -0.0452 -0.0047 -0.0206 18  ILE   B CG1 
4034 C CG2 . ILE   B 18  ? 0.2151 0.1823 0.2252 -0.0560 -0.0149 -0.0287 18  ILE   B CG2 
4035 C CD1 . ILE   B 18  ? 0.2208 0.1912 0.2555 -0.0358 -0.0312 0.0146  18  ILE   B CD1 
4047 N N   . LYS   B 19  ? 0.2166 0.1846 0.2221 -0.0458 0.0494  -0.0527 19  LYS   B N   
4048 C CA  . LYS   B 19  ? 0.2190 0.1869 0.2488 -0.0475 0.0482  -0.0623 19  LYS   B CA  
4049 C C   . LYS   B 19  ? 0.2101 0.1716 0.2586 -0.0377 0.0505  -0.0850 19  LYS   B C   
4050 O O   . LYS   B 19  ? 0.1996 0.1839 0.2509 -0.0303 0.0342  -0.0694 19  LYS   B O   
4051 C CB  . LYS   B 19  ? 0.2457 0.2157 0.2658 -0.0529 0.0673  -0.0486 19  LYS   B CB  
4052 C CG  . LYS   B 19  ? 0.2753 0.2348 0.3056 -0.0579 0.0783  -0.0566 19  LYS   B CG  
4053 C CD  . LYS   B 19  ? 0.3105 0.2693 0.3284 -0.0632 0.0941  -0.0652 19  LYS   B CD  
4054 C CE  . LYS   B 19  ? 0.3411 0.2973 0.3670 -0.0681 0.0869  -0.0724 19  LYS   B CE  
4055 N NZ  . LYS   B 19  ? 0.3644 0.3174 0.3889 -0.0758 0.0853  -0.0726 19  LYS   B NZ  
4069 N N   . ASN   B 20  ? 0.2196 0.1905 0.3028 -0.0308 0.0571  -0.0879 20  ASN   B N   
4070 C CA  . ASN   B 20  ? 0.2144 0.1973 0.3290 -0.0198 0.0624  -0.1091 20  ASN   B CA  
4071 C C   . ASN   B 20  ? 0.2062 0.2246 0.3254 -0.0171 0.0723  -0.1234 20  ASN   B C   
4072 O O   . ASN   B 20  ? 0.2313 0.2706 0.3391 -0.0311 0.0658  -0.1182 20  ASN   B O   
4073 C CB  . ASN   B 20  ? 0.2534 0.2031 0.3648 0.0103  0.0363  -0.1152 20  ASN   B CB  
4074 C CG  . ASN   B 20  ? 0.2877 0.2184 0.3921 0.0459  0.0338  -0.1191 20  ASN   B CG  
4075 O OD1 . ASN   B 20  ? 0.3216 0.2473 0.4106 0.0566  0.0257  -0.1140 20  ASN   B OD1 
4076 N ND2 . ASN   B 20  ? 0.2831 0.2188 0.3922 0.0518  0.0192  -0.1177 20  ASN   B ND2 
4083 N N   . ALA   B 21  ? 0.2056 0.2080 0.3336 -0.0281 0.0669  -0.1024 21  ALA   B N   
4084 C CA  . ALA   B 21  ? 0.2224 0.2162 0.3463 -0.0328 0.0523  -0.0852 21  ALA   B CA  
4085 C C   . ALA   B 21  ? 0.2191 0.1945 0.3067 -0.0280 0.0603  -0.0759 21  ALA   B C   
4086 O O   . ALA   B 21  ? 0.2291 0.1934 0.2922 -0.0397 0.0602  -0.0696 21  ALA   B O   
4087 C CB  . ALA   B 21  ? 0.2345 0.2402 0.3660 -0.0499 0.0559  -0.0620 21  ALA   B CB  
4093 N N   . ASP   B 22  ? 0.2068 0.1739 0.2889 -0.0300 0.0381  -0.0553 22  ASP   B N   
4094 C CA  . ASP   B 22  ? 0.2046 0.1739 0.2820 -0.0083 0.0294  -0.0387 22  ASP   B CA  
4095 C C   . ASP   B 22  ? 0.2048 0.1627 0.2380 -0.0201 0.0199  -0.0208 22  ASP   B C   
4096 O O   . ASP   B 22  ? 0.2035 0.1701 0.2311 -0.0086 0.0139  -0.0152 22  ASP   B O   
4097 C CB  . ASP   B 22  ? 0.2102 0.1865 0.3254 -0.0036 0.0299  -0.0224 22  ASP   B CB  
4098 C CG  . ASP   B 22  ? 0.2079 0.2058 0.3685 0.0068  0.0142  -0.0105 22  ASP   B CG  
4099 O OD1 . ASP   B 22  ? 0.2228 0.1889 0.3569 0.0059  -0.0027 -0.0037 22  ASP   B OD1 
4100 O OD2 . ASP   B 22  ? 0.2122 0.2340 0.4334 0.0156  -0.0116 -0.0277 22  ASP   B OD2 
4105 N N   . ILE   B 23  ? 0.1993 0.1567 0.2290 -0.0070 -0.0040 0.0100  23  ILE   B N   
4106 C CA  . ILE   B 23  ? 0.1880 0.1563 0.1952 -0.0134 -0.0061 0.0034  23  ILE   B CA  
4107 C C   . ILE   B 23  ? 0.1772 0.1614 0.1792 -0.0045 -0.0113 0.0059  23  ILE   B C   
4108 O O   . ILE   B 23  ? 0.1627 0.1556 0.1780 -0.0063 -0.0059 0.0044  23  ILE   B O   
4109 C CB  . ILE   B 23  ? 0.1730 0.1568 0.2061 -0.0214 -0.0030 0.0123  23  ILE   B CB  
4110 C CG1 . ILE   B 23  ? 0.1727 0.1710 0.2248 -0.0098 0.0002  0.0189  23  ILE   B CG1 
4111 C CG2 . ILE   B 23  ? 0.1898 0.1789 0.2200 -0.0176 -0.0007 0.0119  23  ILE   B CG2 
4112 C CD1 . ILE   B 23  ? 0.1822 0.1844 0.2339 -0.0050 0.0017  0.0255  23  ILE   B CD1 
4124 N N   . VAL   B 24  ? 0.1766 0.1539 0.1988 -0.0085 -0.0179 -0.0059 24  VAL   B N   
4125 C CA  . VAL   B 24  ? 0.1759 0.1595 0.2295 -0.0124 -0.0196 -0.0077 24  VAL   B CA  
4126 C C   . VAL   B 24  ? 0.1802 0.1738 0.2336 -0.0039 -0.0096 -0.0057 24  VAL   B C   
4127 O O   . VAL   B 24  ? 0.1732 0.1805 0.2426 -0.0182 -0.0034 0.0095  24  VAL   B O   
4128 C CB  . VAL   B 24  ? 0.1818 0.1677 0.2452 -0.0030 -0.0274 0.0076  24  VAL   B CB  
4129 C CG1 . VAL   B 24  ? 0.1784 0.1743 0.2803 -0.0004 -0.0276 0.0115  24  VAL   B CG1 
4130 C CG2 . VAL   B 24  ? 0.1957 0.1907 0.2295 -0.0001 -0.0248 0.0002  24  VAL   B CG2 
4140 N N   . GLU   B 25  ? 0.2008 0.1858 0.2319 -0.0064 0.0009  -0.0155 25  GLU   B N   
4141 C CA  . GLU   B 25  ? 0.2134 0.2068 0.2565 0.0028  0.0251  -0.0265 25  GLU   B CA  
4142 C C   . GLU   B 25  ? 0.2090 0.1933 0.2197 -0.0173 0.0262  -0.0107 25  GLU   B C   
4143 O O   . GLU   B 25  ? 0.2090 0.2071 0.2364 -0.0130 0.0290  -0.0081 25  GLU   B O   
4144 C CB  . GLU   B 25  ? 0.2564 0.2677 0.3484 0.0321  0.0279  -0.0232 25  GLU   B CB  
4145 C CG  . GLU   B 25  ? 0.2939 0.3348 0.4575 0.0361  0.0241  -0.0258 25  GLU   B CG  
4146 C CD  . GLU   B 25  ? 0.3533 0.3921 0.5405 0.0288  0.0218  -0.0265 25  GLU   B CD  
4147 O OE1 . GLU   B 25  ? 0.3741 0.4115 0.5641 0.0329  0.0346  -0.0242 25  GLU   B OE1 
4148 O OE2 . GLU   B 25  ? 0.3724 0.4083 0.5660 0.0288  0.0110  -0.0365 25  GLU   B OE2 
4155 N N   A GLU   B 26  ? 0.2096 0.1775 0.1886 -0.0286 0.0361  -0.0115 26  GLU   B N   
4156 N N   B GLU   B 26  ? 0.2030 0.1835 0.2058 -0.0263 0.0219  -0.0005 26  GLU   B N   
4157 C CA  A GLU   B 26  ? 0.2180 0.1985 0.2015 -0.0403 0.0188  -0.0056 26  GLU   B CA  
4158 C CA  B GLU   B 26  ? 0.2010 0.1900 0.2126 -0.0332 0.0071  0.0089  26  GLU   B CA  
4159 C C   A GLU   B 26  ? 0.1920 0.1970 0.1852 -0.0337 0.0152  0.0100  26  GLU   B C   
4160 C C   B GLU   B 26  ? 0.1843 0.1895 0.1899 -0.0314 0.0109  0.0161  26  GLU   B C   
4161 O O   A GLU   B 26  ? 0.2004 0.2207 0.2030 -0.0312 0.0129  0.0122  26  GLU   B O   
4162 O O   B GLU   B 26  ? 0.1892 0.2035 0.1985 -0.0309 0.0105  0.0174  26  GLU   B O   
4163 C CB  A GLU   B 26  ? 0.2549 0.2207 0.2269 -0.0470 0.0450  0.0107  26  GLU   B CB  
4164 C CB  B GLU   B 26  ? 0.2167 0.1955 0.2410 -0.0364 0.0065  0.0219  26  GLU   B CB  
4165 C CG  A GLU   B 26  ? 0.2913 0.2540 0.2764 -0.0439 0.0568  -0.0066 26  GLU   B CG  
4166 C CG  B GLU   B 26  ? 0.2317 0.2086 0.2805 -0.0344 -0.0031 0.0119  26  GLU   B CG  
4167 C CD  A GLU   B 26  ? 0.3102 0.2639 0.2936 -0.0572 0.0793  -0.0253 26  GLU   B CD  
4168 C CD  B GLU   B 26  ? 0.2294 0.2025 0.2931 -0.0461 -0.0160 -0.0024 26  GLU   B CD  
4169 O OE1 A GLU   B 26  ? 0.3188 0.2561 0.3020 -0.0621 0.1227  -0.0214 26  GLU   B OE1 
4170 O OE1 B GLU   B 26  ? 0.2246 0.2041 0.3389 -0.0655 -0.0032 -0.0257 26  GLU   B OE1 
4171 O OE2 A GLU   B 26  ? 0.3071 0.2751 0.3201 -0.0665 0.0911  -0.0057 26  GLU   B OE2 
4172 O OE2 B GLU   B 26  ? 0.2284 0.1935 0.2808 -0.0428 -0.0158 0.0099  26  GLU   B OE2 
4185 N N   . ALA   B 27  ? 0.1689 0.1782 0.1748 -0.0291 0.0125  0.0195  27  ALA   B N   
4186 C CA  . ALA   B 27  ? 0.1698 0.1813 0.1913 -0.0173 -0.0058 0.0299  27  ALA   B CA  
4187 C C   . ALA   B 27  ? 0.1742 0.1926 0.2269 -0.0216 0.0078  0.0390  27  ALA   B C   
4188 O O   . ALA   B 27  ? 0.1751 0.2000 0.2465 -0.0123 0.0066  0.0465  27  ALA   B O   
4189 C CB  . ALA   B 27  ? 0.1760 0.1663 0.1979 -0.0136 -0.0025 0.0266  27  ALA   B CB  
4196 N N   . LYS   B 28  ? 0.1733 0.2163 0.2726 -0.0235 0.0197  0.0618  28  LYS   B N   
4197 C CA  . LYS   B 28  ? 0.1914 0.2534 0.2912 -0.0096 0.0495  0.0853  28  LYS   B CA  
4198 C C   . LYS   B 28  ? 0.2150 0.2608 0.2640 -0.0069 0.0677  0.0840  28  LYS   B C   
4199 O O   . LYS   B 28  ? 0.2384 0.2694 0.2874 -0.0100 0.0666  0.0805  28  LYS   B O   
4200 C CB  . LYS   B 28  ? 0.2126 0.2942 0.3450 0.0063  0.0683  0.0986  28  LYS   B CB  
4201 C CG  . LYS   B 28  ? 0.2393 0.3525 0.3858 0.0179  0.0821  0.1006  28  LYS   B CG  
4202 C CD  . LYS   B 28  ? 0.2830 0.4171 0.4496 0.0258  0.0970  0.0955  28  LYS   B CD  
4203 C CE  . LYS   B 28  ? 0.3136 0.4591 0.5015 0.0357  0.0995  0.1000  28  LYS   B CE  
4204 N NZ  . LYS   B 28  ? 0.3521 0.4779 0.5259 0.0454  0.0967  0.1005  28  LYS   B NZ  
4218 N N   . LYS   B 29  ? 0.2345 0.2892 0.2643 0.0110  0.0639  0.0555  29  LYS   B N   
4219 C CA  . LYS   B 29  ? 0.2836 0.3248 0.2955 0.0106  0.0578  0.0537  29  LYS   B CA  
4220 C C   . LYS   B 29  ? 0.2811 0.3260 0.2700 0.0042  0.0448  0.0626  29  LYS   B C   
4221 O O   . LYS   B 29  ? 0.3003 0.3553 0.2900 0.0078  0.0580  0.0664  29  LYS   B O   
4222 C CB  . LYS   B 29  ? 0.3383 0.3622 0.3841 0.0130  0.0522  0.0332  29  LYS   B CB  
4223 C CG  . LYS   B 29  ? 0.3856 0.3932 0.4791 0.0120  0.0503  0.0294  29  LYS   B CG  
4224 C CD  . LYS   B 29  ? 0.4299 0.4237 0.5505 0.0099  0.0584  0.0229  29  LYS   B CD  
4225 C CE  . LYS   B 29  ? 0.4604 0.4427 0.5952 0.0051  0.0704  0.0183  29  LYS   B CE  
4226 N NZ  . LYS   B 29  ? 0.4700 0.4444 0.6245 0.0016  0.0753  0.0149  29  LYS   B NZ  
4240 N N   . VAL   B 30  ? 0.2471 0.2993 0.2520 -0.0198 0.0253  0.0595  30  VAL   B N   
4241 C CA  . VAL   B 30  ? 0.2371 0.2849 0.2763 -0.0289 -0.0134 0.0653  30  VAL   B CA  
4242 C C   . VAL   B 30  ? 0.2074 0.2826 0.2629 -0.0300 -0.0085 0.0917  30  VAL   B C   
4243 O O   . VAL   B 30  ? 0.2114 0.3070 0.2709 -0.0314 -0.0100 0.1002  30  VAL   B O   
4244 C CB  . VAL   B 30  ? 0.2416 0.2713 0.3255 -0.0495 -0.0401 0.0590  30  VAL   B CB  
4245 C CG1 . VAL   B 30  ? 0.2537 0.2770 0.3359 -0.0483 -0.0259 0.0484  30  VAL   B CG1 
4246 C CG2 . VAL   B 30  ? 0.2589 0.2707 0.3496 -0.0587 -0.0534 0.0395  30  VAL   B CG2 
4256 N N   . LYS   B 31  ? 0.1853 0.2544 0.2926 -0.0389 -0.0053 0.0842  31  LYS   B N   
4257 C CA  . LYS   B 31  ? 0.1749 0.2535 0.3288 -0.0439 -0.0045 0.0890  31  LYS   B CA  
4258 C C   . LYS   B 31  ? 0.1720 0.2136 0.2767 -0.0443 -0.0312 0.0803  31  LYS   B C   
4259 O O   . LYS   B 31  ? 0.1674 0.2301 0.2796 -0.0415 -0.0223 0.1048  31  LYS   B O   
4260 C CB  . LYS   B 31  ? 0.1906 0.3052 0.3952 -0.0264 0.0234  0.1060  31  LYS   B CB  
4261 C CG  . LYS   B 31  ? 0.2393 0.3535 0.4430 -0.0327 0.0479  0.1210  31  LYS   B CG  
4262 C CD  . LYS   B 31  ? 0.2790 0.4088 0.4966 -0.0253 0.0433  0.1173  31  LYS   B CD  
4263 C CE  . LYS   B 31  ? 0.3052 0.4414 0.5442 -0.0221 0.0336  0.1077  31  LYS   B CE  
4264 N NZ  . LYS   B 31  ? 0.3361 0.4544 0.5551 -0.0157 0.0237  0.0959  31  LYS   B NZ  
4278 N N   . PRO   B 32  ? 0.1816 0.1759 0.2108 -0.0391 -0.0478 0.0579  32  PRO   B N   
4279 C CA  . PRO   B 32  ? 0.1907 0.1679 0.1856 -0.0430 -0.0336 0.0353  32  PRO   B CA  
4280 C C   . PRO   B 32  ? 0.2024 0.1616 0.1809 -0.0555 -0.0563 0.0340  32  PRO   B C   
4281 O O   . PRO   B 32  ? 0.2119 0.1590 0.2163 -0.0475 -0.0759 0.0356  32  PRO   B O   
4282 C CB  . PRO   B 32  ? 0.1974 0.1689 0.1931 -0.0495 -0.0228 0.0223  32  PRO   B CB  
4283 C CG  . PRO   B 32  ? 0.2164 0.1640 0.1944 -0.0355 -0.0498 0.0296  32  PRO   B CG  
4284 C CD  . PRO   B 32  ? 0.2065 0.1607 0.2131 -0.0307 -0.0577 0.0293  32  PRO   B CD  
4292 N N   . THR   B 33  ? 0.2099 0.1624 0.1878 -0.0466 -0.0587 0.0296  33  THR   B N   
4293 C CA  . THR   B 33  ? 0.2099 0.1615 0.1829 -0.0475 -0.0507 0.0348  33  THR   B CA  
4294 C C   . THR   B 33  ? 0.2060 0.1477 0.1595 -0.0443 -0.0475 0.0240  33  THR   B C   
4295 O O   . THR   B 33  ? 0.2269 0.1476 0.1686 -0.0545 -0.0526 0.0270  33  THR   B O   
4296 C CB  . THR   B 33  ? 0.2265 0.1687 0.1781 -0.0357 -0.0632 0.0360  33  THR   B CB  
4297 O OG1 . THR   B 33  ? 0.2107 0.1774 0.1886 -0.0349 -0.0600 0.0449  33  THR   B OG1 
4298 C CG2 . THR   B 33  ? 0.2547 0.1675 0.1879 -0.0298 -0.0582 0.0335  33  THR   B CG2 
4306 N N   . VAL   B 34  ? 0.1878 0.1508 0.1588 -0.0469 -0.0398 0.0201  34  VAL   B N   
4307 C CA  . VAL   B 34  ? 0.1758 0.1455 0.1405 -0.0340 -0.0341 0.0147  34  VAL   B CA  
4308 C C   . VAL   B 34  ? 0.1599 0.1409 0.1405 -0.0322 -0.0309 0.0018  34  VAL   B C   
4309 O O   . VAL   B 34  ? 0.1785 0.1494 0.1430 -0.0249 -0.0374 0.0082  34  VAL   B O   
4310 C CB  . VAL   B 34  ? 0.1821 0.1498 0.1803 -0.0109 -0.0114 0.0061  34  VAL   B CB  
4311 C CG1 . VAL   B 34  ? 0.1763 0.1687 0.1891 -0.0199 -0.0005 -0.0033 34  VAL   B CG1 
4312 C CG2 . VAL   B 34  ? 0.1744 0.1553 0.2053 -0.0043 -0.0171 -0.0050 34  VAL   B CG2 
4322 N N   . VAL   B 35  ? 0.1541 0.1365 0.1181 -0.0305 -0.0135 0.0120  35  VAL   B N   
4323 C CA  . VAL   B 35  ? 0.1540 0.1264 0.1173 -0.0178 -0.0080 0.0159  35  VAL   B CA  
4324 C C   . VAL   B 35  ? 0.1426 0.1266 0.1198 -0.0159 -0.0164 0.0064  35  VAL   B C   
4325 O O   . VAL   B 35  ? 0.1408 0.1335 0.1211 -0.0215 -0.0003 -0.0007 35  VAL   B O   
4326 C CB  . VAL   B 35  ? 0.1481 0.1475 0.1367 -0.0178 0.0044  0.0048  35  VAL   B CB  
4327 C CG1 . VAL   B 35  ? 0.1440 0.1630 0.1834 -0.0306 -0.0061 -0.0058 35  VAL   B CG1 
4328 C CG2 . VAL   B 35  ? 0.1459 0.1505 0.1727 -0.0097 -0.0032 -0.0002 35  VAL   B CG2 
4338 N N   . VAL   B 36  ? 0.1371 0.1275 0.1341 -0.0188 -0.0154 0.0156  36  VAL   B N   
4339 C CA  . VAL   B 36  ? 0.1354 0.1243 0.1309 -0.0177 -0.0120 0.0086  36  VAL   B CA  
4340 C C   . VAL   B 36  ? 0.1330 0.1297 0.1060 -0.0046 -0.0051 -0.0014 36  VAL   B C   
4341 O O   . VAL   B 36  ? 0.1362 0.1391 0.1396 -0.0115 -0.0025 -0.0123 36  VAL   B O   
4342 C CB  . VAL   B 36  ? 0.1388 0.1285 0.1351 -0.0133 -0.0029 0.0160  36  VAL   B CB  
4343 C CG1 . VAL   B 36  ? 0.1309 0.1379 0.1648 -0.0253 -0.0088 0.0059  36  VAL   B CG1 
4344 C CG2 . VAL   B 36  ? 0.1522 0.1460 0.1377 -0.0181 -0.0102 0.0144  36  VAL   B CG2 
4354 N N   . ASN   B 37  ? 0.1331 0.1275 0.1064 -0.0042 -0.0107 0.0063  37  ASN   B N   
4355 C CA  . ASN   B 37  ? 0.1357 0.1323 0.1219 -0.0050 -0.0162 0.0094  37  ASN   B CA  
4356 C C   . ASN   B 37  ? 0.1426 0.1340 0.1443 0.0025  -0.0156 -0.0007 37  ASN   B C   
4357 O O   . ASN   B 37  ? 0.1460 0.1383 0.1407 0.0016  0.0042  0.0050  37  ASN   B O   
4358 C CB  . ASN   B 37  ? 0.1331 0.1356 0.1027 0.0043  -0.0210 -0.0011 37  ASN   B CB  
4359 C CG  . ASN   B 37  ? 0.1416 0.1386 0.1312 -0.0039 -0.0090 -0.0078 37  ASN   B CG  
4360 O OD1 . ASN   B 37  ? 0.1474 0.1406 0.1645 0.0110  -0.0168 -0.0070 37  ASN   B OD1 
4361 N ND2 . ASN   B 37  ? 0.1414 0.1317 0.1311 0.0020  -0.0201 0.0030  37  ASN   B ND2 
4368 N N   . ALA   B 38  ? 0.1538 0.1309 0.1320 0.0057  0.0023  0.0082  38  ALA   B N   
4369 C CA  . ALA   B 38  ? 0.1543 0.1354 0.1361 -0.0019 0.0083  0.0078  38  ALA   B CA  
4370 C C   . ALA   B 38  ? 0.1568 0.1350 0.1330 0.0004  -0.0010 0.0109  38  ALA   B C   
4371 O O   . ALA   B 38  ? 0.1740 0.1377 0.1563 0.0021  -0.0028 0.0179  38  ALA   B O   
4372 C CB  . ALA   B 38  ? 0.1849 0.1449 0.1560 -0.0112 0.0189  0.0071  38  ALA   B CB  
4378 N N   . ALA   B 39  ? 0.1610 0.1365 0.1237 0.0100  -0.0053 0.0008  39  ALA   B N   
4379 C CA  . ALA   B 39  ? 0.1686 0.1454 0.1239 0.0097  -0.0069 -0.0004 39  ALA   B CA  
4380 C C   . ALA   B 39  ? 0.1718 0.1489 0.1133 0.0133  -0.0070 -0.0085 39  ALA   B C   
4381 O O   . ALA   B 39  ? 0.1746 0.1493 0.1528 0.0002  -0.0060 0.0042  39  ALA   B O   
4382 C CB  . ALA   B 39  ? 0.1520 0.1425 0.1469 -0.0036 -0.0001 0.0034  39  ALA   B CB  
4388 N N   . ASN   B 40  ? 0.1725 0.1765 0.1005 0.0065  -0.0087 -0.0103 40  ASN   B N   
4389 C CA  . ASN   B 40  ? 0.1826 0.1800 0.1115 0.0096  -0.0062 -0.0086 40  ASN   B CA  
4390 C C   . ASN   B 40  ? 0.1825 0.1708 0.1039 0.0150  -0.0010 -0.0005 40  ASN   B C   
4391 O O   . ASN   B 40  ? 0.1817 0.1635 0.1230 0.0090  -0.0043 0.0061  40  ASN   B O   
4392 C CB  . ASN   B 40  ? 0.1911 0.1724 0.1553 0.0169  -0.0070 0.0014  40  ASN   B CB  
4393 C CG  . ASN   B 40  ? 0.1958 0.1783 0.2017 0.0076  -0.0178 0.0171  40  ASN   B CG  
4394 O OD1 . ASN   B 40  ? 0.1912 0.1736 0.2915 0.0063  -0.0259 0.0199  40  ASN   B OD1 
4395 N ND2 . ASN   B 40  ? 0.2070 0.1716 0.2009 0.0001  -0.0228 0.0141  40  ASN   B ND2 
4402 N N   . VAL   B 41  ? 0.1905 0.1713 0.1242 0.0194  0.0102  -0.0019 41  VAL   B N   
4403 C CA  . VAL   B 41  ? 0.1948 0.1895 0.1446 0.0112  0.0084  -0.0024 41  VAL   B CA  
4404 C C   . VAL   B 41  ? 0.1925 0.1882 0.1362 0.0161  -0.0069 -0.0107 41  VAL   B C   
4405 O O   . VAL   B 41  ? 0.1831 0.1853 0.1623 0.0135  -0.0113 -0.0147 41  VAL   B O   
4406 C CB  . VAL   B 41  ? 0.2118 0.2102 0.1645 0.0009  0.0193  -0.0205 41  VAL   B CB  
4407 C CG1 . VAL   B 41  ? 0.2096 0.2127 0.1760 -0.0103 0.0368  -0.0185 41  VAL   B CG1 
4408 C CG2 . VAL   B 41  ? 0.2227 0.2286 0.1694 -0.0079 0.0112  -0.0088 41  VAL   B CG2 
4418 N N   . TYR   B 42  ? 0.2024 0.1876 0.1446 0.0234  -0.0215 -0.0048 42  TYR   B N   
4419 C CA  . TYR   B 42  ? 0.2064 0.1894 0.1409 0.0225  -0.0269 -0.0198 42  TYR   B CA  
4420 C C   . TYR   B 42  ? 0.1902 0.1672 0.1321 0.0244  -0.0265 -0.0209 42  TYR   B C   
4421 O O   . TYR   B 42  ? 0.1875 0.1828 0.1829 0.0148  -0.0231 -0.0207 42  TYR   B O   
4422 C CB  . TYR   B 42  ? 0.2304 0.2196 0.1549 0.0136  -0.0211 -0.0152 42  TYR   B CB  
4423 C CG  . TYR   B 42  ? 0.2301 0.2377 0.1555 0.0032  -0.0180 0.0072  42  TYR   B CG  
4424 C CD1 . TYR   B 42  ? 0.2196 0.2371 0.1404 -0.0020 0.0003  0.0140  42  TYR   B CD1 
4425 C CD2 . TYR   B 42  ? 0.2432 0.2417 0.2028 0.0059  -0.0053 0.0092  42  TYR   B CD2 
4426 C CE1 . TYR   B 42  ? 0.2360 0.2500 0.1377 0.0087  -0.0044 0.0078  42  TYR   B CE1 
4427 C CE2 . TYR   B 42  ? 0.2486 0.2558 0.1938 0.0076  0.0288  0.0276  42  TYR   B CE2 
4428 C CZ  . TYR   B 42  ? 0.2585 0.2708 0.1676 0.0290  0.0291  0.0023  42  TYR   B CZ  
4429 O OH  . TYR   B 42  ? 0.2988 0.3113 0.2131 0.0448  0.0365  0.0116  42  TYR   B OH  
4439 N N   . LEU   B 43  ? 0.1817 0.1611 0.1289 0.0095  -0.0133 -0.0117 43  LEU   B N   
4440 C CA  . LEU   B 43  ? 0.1754 0.1602 0.1209 0.0112  -0.0158 -0.0125 43  LEU   B CA  
4441 C C   . LEU   B 43  ? 0.1793 0.1534 0.1340 0.0028  -0.0176 -0.0053 43  LEU   B C   
4442 O O   . LEU   B 43  ? 0.1759 0.1608 0.1770 0.0034  -0.0198 -0.0011 43  LEU   B O   
4443 C CB  . LEU   B 43  ? 0.1703 0.1556 0.1541 0.0008  -0.0169 -0.0058 43  LEU   B CB  
4444 C CG  . LEU   B 43  ? 0.1714 0.1448 0.1665 0.0001  -0.0191 -0.0035 43  LEU   B CG  
4445 C CD1 . LEU   B 43  ? 0.1814 0.1615 0.1953 -0.0036 -0.0371 -0.0071 43  LEU   B CD1 
4446 C CD2 . LEU   B 43  ? 0.1709 0.1421 0.1713 -0.0049 -0.0213 -0.0031 43  LEU   B CD2 
4458 N N   . LYS   B 44  ? 0.1812 0.1517 0.1453 0.0128  -0.0083 -0.0084 44  LYS   B N   
4459 C CA  . LYS   B 44  ? 0.1870 0.1736 0.1499 0.0187  -0.0104 -0.0070 44  LYS   B CA  
4460 C C   . LYS   B 44  ? 0.1727 0.1631 0.1453 0.0215  -0.0121 0.0012  44  LYS   B C   
4461 O O   . LYS   B 44  ? 0.1857 0.1610 0.2019 0.0062  -0.0050 -0.0033 44  LYS   B O   
4462 C CB  . LYS   B 44  ? 0.2103 0.2007 0.1733 0.0350  -0.0369 -0.0162 44  LYS   B CB  
4463 C CG  . LYS   B 44  ? 0.2523 0.2325 0.2210 0.0261  -0.0597 -0.0030 44  LYS   B CG  
4464 C CD  . LYS   B 44  ? 0.2924 0.2563 0.2819 -0.0010 -0.0723 -0.0117 44  LYS   B CD  
4465 C CE  . LYS   B 44  ? 0.3284 0.2856 0.3253 -0.0172 -0.0764 0.0038  44  LYS   B CE  
4466 N NZ  . LYS   B 44  ? 0.3415 0.2963 0.3279 -0.0161 -0.0931 0.0238  44  LYS   B NZ  
4480 N N   . HIS   B 45  ? 0.1737 0.1709 0.1345 0.0058  -0.0115 0.0124  45  HIS   B N   
4481 C CA  . HIS   B 45  ? 0.1700 0.1659 0.1466 0.0105  -0.0048 -0.0007 45  HIS   B CA  
4482 C C   . HIS   B 45  ? 0.1828 0.1882 0.1815 0.0212  -0.0061 0.0001  45  HIS   B C   
4483 O O   . HIS   B 45  ? 0.2016 0.2114 0.2339 0.0417  0.0182  0.0087  45  HIS   B O   
4484 C CB  . HIS   B 45  ? 0.1639 0.1686 0.1477 0.0049  -0.0067 -0.0080 45  HIS   B CB  
4485 C CG  . HIS   B 45  ? 0.1621 0.1570 0.1540 -0.0056 -0.0154 -0.0015 45  HIS   B CG  
4486 N ND1 . HIS   B 45  ? 0.1693 0.1541 0.1660 0.0043  -0.0221 -0.0049 45  HIS   B ND1 
4487 C CD2 . HIS   B 45  ? 0.1678 0.1648 0.1772 -0.0134 -0.0303 -0.0018 45  HIS   B CD2 
4488 C CE1 . HIS   B 45  ? 0.1737 0.1412 0.1606 -0.0000 -0.0365 -0.0177 45  HIS   B CE1 
4489 N NE2 . HIS   B 45  ? 0.1801 0.1574 0.1589 -0.0020 -0.0312 -0.0144 45  HIS   B NE2 
4497 N N   A GLY   B 46  ? 0.1989 0.1828 0.2157 0.0248  -0.0283 0.0080  46  GLY   B N   
4498 N N   B GLY   B 46  ? 0.1991 0.1928 0.2077 0.0245  -0.0215 0.0092  46  GLY   B N   
4499 C CA  A GLY   B 46  ? 0.2229 0.1993 0.2630 0.0182  -0.0323 0.0125  46  GLY   B CA  
4500 C CA  B GLY   B 46  ? 0.2172 0.2070 0.2399 0.0211  -0.0281 0.0164  46  GLY   B CA  
4501 C C   A GLY   B 46  ? 0.2373 0.2151 0.3133 0.0107  -0.0202 0.0191  46  GLY   B C   
4502 C C   B GLY   B 46  ? 0.2304 0.2198 0.2747 0.0165  -0.0247 0.0239  46  GLY   B C   
4503 O O   A GLY   B 46  ? 0.2436 0.2210 0.3884 0.0164  -0.0027 0.0019  46  GLY   B O   
4504 O O   B GLY   B 46  ? 0.2322 0.2297 0.2945 0.0304  -0.0220 0.0249  46  GLY   B O   
4511 N N   . GLY   B 47  ? 0.2398 0.2226 0.2786 -0.0074 -0.0211 0.0159  47  GLY   B N   
4512 C CA  . GLY   B 47  ? 0.2257 0.1848 0.2278 -0.0149 -0.0169 0.0085  47  GLY   B CA  
4513 C C   . GLY   B 47  ? 0.2004 0.1719 0.1902 -0.0086 -0.0022 0.0083  47  GLY   B C   
4514 O O   . GLY   B 47  ? 0.2176 0.1538 0.2083 -0.0007 -0.0102 0.0171  47  GLY   B O   
4519 N N   . GLY   B 48  ? 0.1728 0.1614 0.2036 0.0003  -0.0110 0.0154  48  GLY   B N   
4520 C CA  . GLY   B 48  ? 0.1679 0.1532 0.1989 -0.0090 -0.0097 0.0114  48  GLY   B CA  
4521 C C   . GLY   B 48  ? 0.1557 0.1484 0.1807 -0.0046 0.0069  0.0115  48  GLY   B C   
4522 O O   . GLY   B 48  ? 0.1479 0.1450 0.2130 0.0047  -0.0099 0.0161  48  GLY   B O   
4526 N N   . VAL   B 49  ? 0.1576 0.1505 0.1833 0.0112  -0.0053 0.0044  49  VAL   B N   
4527 C CA  . VAL   B 49  ? 0.1584 0.1587 0.1601 0.0129  -0.0204 -0.0127 49  VAL   B CA  
4528 C C   . VAL   B 49  ? 0.1474 0.1496 0.1398 0.0146  -0.0090 -0.0061 49  VAL   B C   
4529 O O   . VAL   B 49  ? 0.1533 0.1489 0.1764 0.0027  0.0014  -0.0033 49  VAL   B O   
4530 C CB  . VAL   B 49  ? 0.1710 0.1752 0.1782 0.0061  -0.0282 -0.0090 49  VAL   B CB  
4531 C CG1 . VAL   B 49  ? 0.1744 0.1814 0.1805 0.0073  -0.0332 -0.0037 49  VAL   B CG1 
4532 C CG2 . VAL   B 49  ? 0.1912 0.2005 0.2052 -0.0078 -0.0456 -0.0142 49  VAL   B CG2 
4542 N N   . ALA   B 50  ? 0.1500 0.1443 0.1457 -0.0009 -0.0077 -0.0003 50  ALA   B N   
4543 C CA  . ALA   B 50  ? 0.1501 0.1368 0.1469 0.0109  -0.0098 -0.0036 50  ALA   B CA  
4544 C C   . ALA   B 50  ? 0.1452 0.1439 0.1586 0.0043  -0.0007 0.0031  50  ALA   B C   
4545 O O   . ALA   B 50  ? 0.1462 0.1463 0.1561 0.0050  0.0039  -0.0026 50  ALA   B O   
4546 C CB  . ALA   B 50  ? 0.1601 0.1311 0.1584 -0.0003 -0.0079 0.0005  50  ALA   B CB  
4552 N N   . GLY   B 51  ? 0.1517 0.1469 0.1627 0.0153  -0.0159 0.0062  51  GLY   B N   
4553 C CA  . GLY   B 51  ? 0.1571 0.1593 0.1819 0.0197  -0.0234 0.0046  51  GLY   B CA  
4554 C C   . GLY   B 51  ? 0.1590 0.1541 0.1803 0.0257  -0.0095 0.0032  51  GLY   B C   
4555 O O   . GLY   B 51  ? 0.1528 0.1667 0.2042 0.0105  -0.0026 -0.0093 51  GLY   B O   
4559 N N   . ALA   B 52  ? 0.1517 0.1441 0.1678 0.0143  -0.0079 0.0029  52  ALA   B N   
4560 C CA  . ALA   B 52  ? 0.1578 0.1468 0.1808 0.0134  -0.0023 -0.0092 52  ALA   B CA  
4561 C C   . ALA   B 52  ? 0.1467 0.1442 0.1676 0.0029  -0.0021 -0.0068 52  ALA   B C   
4562 O O   . ALA   B 52  ? 0.1456 0.1579 0.2022 0.0023  -0.0007 -0.0111 52  ALA   B O   
4563 C CB  . ALA   B 52  ? 0.1710 0.1450 0.1929 0.0065  -0.0000 -0.0150 52  ALA   B CB  
4569 N N   . LEU   B 53  ? 0.1408 0.1484 0.1554 0.0099  -0.0013 0.0041  53  LEU   B N   
4570 C CA  . LEU   B 53  ? 0.1475 0.1559 0.1295 0.0075  -0.0130 0.0046  53  LEU   B CA  
4571 C C   . LEU   B 53  ? 0.1535 0.1491 0.1486 0.0076  -0.0007 0.0022  53  LEU   B C   
4572 O O   . LEU   B 53  ? 0.1561 0.1566 0.1746 0.0002  -0.0028 0.0082  53  LEU   B O   
4573 C CB  . LEU   B 53  ? 0.1513 0.1583 0.1625 0.0100  -0.0059 0.0079  53  LEU   B CB  
4574 C CG  . LEU   B 53  ? 0.1425 0.1622 0.1638 0.0053  0.0007  0.0142  53  LEU   B CG  
4575 C CD1 . LEU   B 53  ? 0.1579 0.1774 0.2079 0.0128  0.0112  0.0051  53  LEU   B CD1 
4576 C CD2 . LEU   B 53  ? 0.1628 0.2030 0.1927 -0.0063 -0.0154 -0.0124 53  LEU   B CD2 
4588 N N   . ASN   B 54  ? 0.1550 0.1372 0.1486 0.0071  -0.0051 0.0030  54  ASN   B N   
4589 C CA  . ASN   B 54  ? 0.1575 0.1566 0.1391 0.0039  -0.0153 -0.0115 54  ASN   B CA  
4590 C C   . ASN   B 54  ? 0.1467 0.1533 0.1841 0.0062  0.0025  -0.0109 54  ASN   B C   
4591 O O   . ASN   B 54  ? 0.1448 0.1573 0.2101 -0.0017 0.0059  -0.0089 54  ASN   B O   
4592 C CB  . ASN   B 54  ? 0.1615 0.1758 0.1574 0.0055  -0.0193 -0.0062 54  ASN   B CB  
4593 C CG  . ASN   B 54  ? 0.1560 0.1855 0.1709 0.0042  -0.0149 -0.0198 54  ASN   B CG  
4594 O OD1 . ASN   B 54  ? 0.1548 0.1731 0.2096 -0.0002 -0.0116 -0.0267 54  ASN   B OD1 
4595 N ND2 . ASN   B 54  ? 0.1592 0.1949 0.2040 0.0054  -0.0365 -0.0046 54  ASN   B ND2 
4602 N N   . LYS   B 55  ? 0.1495 0.1586 0.2043 0.0106  0.0038  -0.0022 55  LYS   B N   
4603 C CA  . LYS   B 55  ? 0.1608 0.1735 0.2208 0.0148  0.0080  -0.0140 55  LYS   B CA  
4604 C C   . LYS   B 55  ? 0.1498 0.1690 0.2190 0.0117  0.0109  -0.0066 55  LYS   B C   
4605 O O   . LYS   B 55  ? 0.1429 0.1900 0.2377 0.0067  0.0021  -0.0144 55  LYS   B O   
4606 C CB  . LYS   B 55  ? 0.1712 0.1901 0.2782 0.0413  0.0071  -0.0169 55  LYS   B CB  
4607 C CG  . LYS   B 55  ? 0.2154 0.2348 0.3538 0.0428  0.0161  -0.0013 55  LYS   B CG  
4608 C CD  . LYS   B 55  ? 0.2625 0.2676 0.4183 0.0478  0.0338  0.0132  55  LYS   B CD  
4609 C CE  . LYS   B 55  ? 0.2938 0.2898 0.4812 0.0507  0.0577  0.0157  55  LYS   B CE  
4610 N NZ  . LYS   B 55  ? 0.3094 0.3075 0.5193 0.0485  0.0518  0.0254  55  LYS   B NZ  
4624 N N   . ALA   B 56  ? 0.1499 0.1700 0.2041 0.0110  -0.0000 -0.0133 56  ALA   B N   
4625 C CA  . ALA   B 56  ? 0.1674 0.1850 0.1982 0.0025  -0.0051 -0.0094 56  ALA   B CA  
4626 C C   . ALA   B 56  ? 0.1634 0.1844 0.2001 -0.0014 0.0237  0.0025  56  ALA   B C   
4627 O O   . ALA   B 56  ? 0.1697 0.1938 0.2117 0.0045  0.0268  0.0029  56  ALA   B O   
4628 C CB  . ALA   B 56  ? 0.1843 0.2043 0.2013 -0.0125 -0.0089 -0.0111 56  ALA   B CB  
4634 N N   . THR   B 57  ? 0.1515 0.1775 0.2229 0.0028  0.0259  -0.0043 57  THR   B N   
4635 C CA  . THR   B 57  ? 0.1619 0.1725 0.2079 0.0008  0.0238  -0.0159 57  THR   B CA  
4636 C C   . THR   B 57  ? 0.1631 0.1830 0.2127 -0.0006 0.0292  -0.0189 57  THR   B C   
4637 O O   . THR   B 57  ? 0.1670 0.1888 0.2294 -0.0193 0.0174  -0.0126 57  THR   B O   
4638 C CB  . THR   B 57  ? 0.1741 0.1531 0.1732 -0.0029 0.0180  0.0041  57  THR   B CB  
4639 O OG1 . THR   B 57  ? 0.1655 0.1550 0.2054 -0.0049 0.0151  -0.0019 57  THR   B OG1 
4640 C CG2 . THR   B 57  ? 0.1594 0.1648 0.1919 -0.0031 0.0295  -0.0013 57  THR   B CG2 
4648 N N   . ASN   B 58  ? 0.1648 0.2035 0.2246 -0.0108 0.0111  -0.0352 58  ASN   B N   
4649 C CA  . ASN   B 58  ? 0.1908 0.2503 0.2626 -0.0302 0.0435  -0.0263 58  ASN   B CA  
4650 C C   . ASN   B 58  ? 0.1583 0.2257 0.2327 -0.0216 0.0085  -0.0224 58  ASN   B C   
4651 O O   . ASN   B 58  ? 0.1581 0.2335 0.2490 -0.0113 -0.0018 -0.0387 58  ASN   B O   
4652 C CB  . ASN   B 58  ? 0.2936 0.3498 0.3722 -0.0434 0.0875  -0.0196 58  ASN   B CB  
4653 C CG  . ASN   B 58  ? 0.4192 0.4479 0.5256 -0.0448 0.1122  0.0008  58  ASN   B CG  
4654 O OD1 . ASN   B 58  ? 0.4359 0.4700 0.5814 -0.0445 0.1158  0.0094  58  ASN   B OD1 
4655 N ND2 . ASN   B 58  ? 0.5446 0.5446 0.5868 -0.0462 0.1208  0.0044  58  ASN   B ND2 
4662 N N   . ASN   B 59  ? 0.1545 0.2137 0.2117 -0.0136 0.0017  -0.0023 59  ASN   B N   
4663 C CA  . ASN   B 59  ? 0.1598 0.2138 0.1998 -0.0107 -0.0056 0.0025  59  ASN   B CA  
4664 C C   . ASN   B 59  ? 0.1526 0.2057 0.1949 -0.0126 -0.0110 -0.0174 59  ASN   B C   
4665 O O   . ASN   B 59  ? 0.1483 0.2091 0.2084 -0.0189 -0.0062 -0.0095 59  ASN   B O   
4666 C CB  . ASN   B 59  ? 0.1702 0.2337 0.2145 -0.0087 -0.0277 0.0056  59  ASN   B CB  
4667 C CG  . ASN   B 59  ? 0.1795 0.2434 0.2330 -0.0020 -0.0465 0.0025  59  ASN   B CG  
4668 O OD1 . ASN   B 59  ? 0.1787 0.2433 0.2384 -0.0077 -0.0331 0.0246  59  ASN   B OD1 
4669 N ND2 . ASN   B 59  ? 0.1858 0.2465 0.2535 -0.0042 -0.0517 -0.0041 59  ASN   B ND2 
4676 N N   . ALA   B 60  ? 0.1567 0.1909 0.2038 -0.0098 0.0073  -0.0243 60  ALA   B N   
4677 C CA  . ALA   B 60  ? 0.1646 0.1836 0.2017 -0.0155 0.0132  -0.0092 60  ALA   B CA  
4678 C C   . ALA   B 60  ? 0.1628 0.1689 0.1835 -0.0100 -0.0037 -0.0068 60  ALA   B C   
4679 O O   . ALA   B 60  ? 0.1692 0.1641 0.1988 -0.0202 0.0026  -0.0069 60  ALA   B O   
4680 C CB  . ALA   B 60  ? 0.1812 0.1751 0.2221 -0.0113 0.0178  -0.0027 60  ALA   B CB  
4686 N N   . MET   B 61  ? 0.1543 0.1563 0.1714 -0.0071 0.0003  0.0012  61  MET   B N   
4687 C CA  . MET   B 61  ? 0.1524 0.1549 0.1619 -0.0095 -0.0099 0.0067  61  MET   B CA  
4688 C C   . MET   B 61  ? 0.1539 0.1530 0.1608 -0.0155 -0.0081 0.0028  61  MET   B C   
4689 O O   . MET   B 61  ? 0.1557 0.1475 0.1719 -0.0030 -0.0064 -0.0197 61  MET   B O   
4690 C CB  . MET   B 61  ? 0.1447 0.1525 0.1685 -0.0068 -0.0093 -0.0031 61  MET   B CB  
4691 C CG  . MET   B 61  ? 0.1442 0.1499 0.1606 -0.0053 -0.0147 0.0022  61  MET   B CG  
4692 S SD  . MET   B 61  ? 0.1503 0.1527 0.1798 -0.0037 -0.0068 -0.0108 61  MET   B SD  
4693 C CE  . MET   B 61  ? 0.1550 0.1721 0.2041 -0.0029 -0.0062 -0.0306 61  MET   B CE  
4703 N N   . GLN   B 62  ? 0.1560 0.1606 0.1502 -0.0119 -0.0237 0.0046  62  GLN   B N   
4704 C CA  . GLN   B 62  ? 0.1613 0.1621 0.1653 -0.0012 -0.0250 -0.0004 62  GLN   B CA  
4705 C C   . GLN   B 62  ? 0.1688 0.1645 0.1786 -0.0067 -0.0324 -0.0133 62  GLN   B C   
4706 O O   . GLN   B 62  ? 0.1822 0.1613 0.1894 -0.0044 -0.0302 -0.0214 62  GLN   B O   
4707 C CB  . GLN   B 62  ? 0.1628 0.1712 0.1732 0.0071  -0.0129 0.0053  62  GLN   B CB  
4708 C CG  . GLN   B 62  ? 0.1669 0.1839 0.1789 0.0032  -0.0209 -0.0119 62  GLN   B CG  
4709 C CD  . GLN   B 62  ? 0.1648 0.1767 0.1661 0.0031  -0.0282 -0.0110 62  GLN   B CD  
4710 O OE1 . GLN   B 62  ? 0.1669 0.1676 0.1845 0.0027  -0.0416 -0.0236 62  GLN   B OE1 
4711 N NE2 . GLN   B 62  ? 0.1715 0.1768 0.1925 0.0077  -0.0255 -0.0174 62  GLN   B NE2 
4720 N N   . VAL   B 63  ? 0.1671 0.1610 0.2022 -0.0133 -0.0271 -0.0245 63  VAL   B N   
4721 C CA  . VAL   B 63  ? 0.1788 0.1709 0.2272 -0.0080 -0.0242 -0.0120 63  VAL   B CA  
4722 C C   . VAL   B 63  ? 0.1770 0.1655 0.1957 -0.0198 -0.0314 -0.0331 63  VAL   B C   
4723 O O   . VAL   B 63  ? 0.1866 0.1639 0.1976 -0.0159 -0.0445 -0.0270 63  VAL   B O   
4724 C CB  . VAL   B 63  ? 0.1726 0.1847 0.2606 -0.0170 -0.0313 -0.0151 63  VAL   B CB  
4725 C CG1 . VAL   B 63  ? 0.1777 0.1911 0.2842 -0.0258 -0.0232 -0.0077 63  VAL   B CG1 
4726 C CG2 . VAL   B 63  ? 0.1695 0.2133 0.2645 -0.0027 -0.0383 -0.0212 63  VAL   B CG2 
4736 N N   . GLU   B 64  ? 0.1706 0.1588 0.1928 -0.0107 -0.0306 -0.0253 64  GLU   B N   
4737 C CA  . GLU   B 64  ? 0.1639 0.1456 0.1895 -0.0129 -0.0383 -0.0144 64  GLU   B CA  
4738 C C   . GLU   B 64  ? 0.1613 0.1509 0.1700 -0.0082 -0.0382 -0.0192 64  GLU   B C   
4739 O O   . GLU   B 64  ? 0.1683 0.1588 0.1692 -0.0144 -0.0320 -0.0200 64  GLU   B O   
4740 C CB  . GLU   B 64  ? 0.1648 0.1535 0.1816 -0.0191 -0.0317 -0.0057 64  GLU   B CB  
4741 C CG  . GLU   B 64  ? 0.1724 0.1577 0.1755 -0.0210 -0.0299 -0.0032 64  GLU   B CG  
4742 C CD  . GLU   B 64  ? 0.1734 0.1766 0.1970 -0.0263 -0.0234 -0.0073 64  GLU   B CD  
4743 O OE1 . GLU   B 64  ? 0.1792 0.1943 0.2109 -0.0340 -0.0083 -0.0425 64  GLU   B OE1 
4744 O OE2 . GLU   B 64  ? 0.1884 0.1771 0.2064 -0.0318 -0.0360 -0.0194 64  GLU   B OE2 
4751 N N   . SER   B 65  ? 0.1656 0.1478 0.1506 -0.0082 -0.0210 -0.0178 65  SER   B N   
4752 C CA  . SER   B 65  ? 0.1672 0.1480 0.1583 -0.0041 -0.0181 -0.0162 65  SER   B CA  
4753 C C   . SER   B 65  ? 0.1720 0.1523 0.1587 0.0061  -0.0223 -0.0224 65  SER   B C   
4754 O O   . SER   B 65  ? 0.1791 0.1559 0.1703 0.0044  -0.0237 -0.0224 65  SER   B O   
4755 C CB  . SER   B 65  ? 0.1649 0.1472 0.1672 -0.0094 -0.0117 -0.0205 65  SER   B CB  
4756 O OG  . SER   B 65  ? 0.1617 0.1557 0.1819 -0.0028 -0.0133 -0.0330 65  SER   B OG  
4762 N N   . ASP   B 66  ? 0.1800 0.1636 0.1577 -0.0021 -0.0391 -0.0268 66  ASP   B N   
4763 C CA  . ASP   B 66  ? 0.1899 0.1697 0.1525 0.0056  -0.0514 -0.0216 66  ASP   B CA  
4764 C C   . ASP   B 66  ? 0.1913 0.1710 0.1585 -0.0030 -0.0317 -0.0292 66  ASP   B C   
4765 O O   . ASP   B 66  ? 0.2020 0.1791 0.1633 0.0022  -0.0317 -0.0243 66  ASP   B O   
4766 C CB  . ASP   B 66  ? 0.2077 0.1862 0.1838 0.0120  -0.0476 -0.0218 66  ASP   B CB  
4767 C CG  . ASP   B 66  ? 0.2214 0.1968 0.2111 0.0211  -0.0554 -0.0087 66  ASP   B CG  
4768 O OD1 . ASP   B 66  ? 0.2423 0.1961 0.2131 0.0118  -0.0519 0.0083  66  ASP   B OD1 
4769 O OD2 . ASP   B 66  ? 0.2402 0.2268 0.2811 0.0446  -0.0494 -0.0110 66  ASP   B OD2 
4774 N N   . ASP   B 67  ? 0.1808 0.1624 0.1694 -0.0118 -0.0296 -0.0232 67  ASP   B N   
4775 C CA  . ASP   B 67  ? 0.1999 0.1603 0.1762 -0.0119 -0.0267 -0.0118 67  ASP   B CA  
4776 C C   . ASP   B 67  ? 0.1923 0.1573 0.1883 -0.0005 -0.0261 -0.0229 67  ASP   B C   
4777 O O   . ASP   B 67  ? 0.1947 0.1684 0.1919 -0.0030 -0.0184 -0.0346 67  ASP   B O   
4778 C CB  . ASP   B 67  ? 0.2182 0.1637 0.1981 -0.0085 -0.0395 -0.0120 67  ASP   B CB  
4779 C CG  . ASP   B 67  ? 0.2562 0.1786 0.2018 -0.0047 -0.0752 -0.0204 67  ASP   B CG  
4780 O OD1 . ASP   B 67  ? 0.2808 0.1878 0.2265 -0.0025 -0.0698 -0.0160 67  ASP   B OD1 
4781 O OD2 . ASP   B 67  ? 0.2763 0.1934 0.2246 0.0085  -0.0799 -0.0151 67  ASP   B OD2 
4786 N N   . TYR   B 68  ? 0.1842 0.1552 0.1859 0.0036  -0.0450 -0.0379 68  TYR   B N   
4787 C CA  . TYR   B 68  ? 0.1781 0.1770 0.1952 0.0137  -0.0473 -0.0386 68  TYR   B CA  
4788 C C   . TYR   B 68  ? 0.1720 0.1697 0.1880 0.0076  -0.0349 -0.0387 68  TYR   B C   
4789 O O   . TYR   B 68  ? 0.1775 0.1778 0.2026 0.0134  -0.0335 -0.0604 68  TYR   B O   
4790 C CB  . TYR   B 68  ? 0.1829 0.2033 0.2111 0.0124  -0.0545 -0.0570 68  TYR   B CB  
4791 C CG  . TYR   B 68  ? 0.1943 0.2270 0.2296 0.0183  -0.0382 -0.0842 68  TYR   B CG  
4792 C CD1 . TYR   B 68  ? 0.1932 0.2343 0.2411 0.0041  -0.0334 -0.0887 68  TYR   B CD1 
4793 C CD2 . TYR   B 68  ? 0.2056 0.2531 0.2426 0.0225  -0.0589 -0.0913 68  TYR   B CD2 
4794 C CE1 . TYR   B 68  ? 0.1972 0.2560 0.2573 0.0066  -0.0282 -0.0927 68  TYR   B CE1 
4795 C CE2 . TYR   B 68  ? 0.1975 0.2609 0.2542 0.0222  -0.0471 -0.1143 68  TYR   B CE2 
4796 C CZ  . TYR   B 68  ? 0.1868 0.2595 0.2688 0.0111  -0.0356 -0.0971 68  TYR   B CZ  
4797 O OH  . TYR   B 68  ? 0.1837 0.2733 0.2993 0.0020  -0.0244 -0.0737 68  TYR   B OH  
4807 N N   . ILE   B 69  ? 0.1770 0.1609 0.1831 0.0008  -0.0286 -0.0275 69  ILE   B N   
4808 C CA  . ILE   B 69  ? 0.1891 0.1685 0.1918 -0.0034 -0.0354 -0.0365 69  ILE   B CA  
4809 C C   . ILE   B 69  ? 0.1847 0.1645 0.1945 0.0089  -0.0470 -0.0230 69  ILE   B C   
4810 O O   . ILE   B 69  ? 0.1942 0.1764 0.1922 0.0085  -0.0313 -0.0388 69  ILE   B O   
4811 C CB  . ILE   B 69  ? 0.1949 0.1706 0.2062 0.0025  -0.0103 -0.0327 69  ILE   B CB  
4812 C CG1 . ILE   B 69  ? 0.1966 0.1827 0.2143 -0.0063 0.0078  -0.0354 69  ILE   B CG1 
4813 C CG2 . ILE   B 69  ? 0.2106 0.1832 0.2194 -0.0064 -0.0106 -0.0293 69  ILE   B CG2 
4814 C CD1 . ILE   B 69  ? 0.1949 0.1840 0.2303 -0.0232 0.0009  -0.0482 69  ILE   B CD1 
4826 N N   . ALA   B 70  ? 0.1856 0.1675 0.1773 0.0066  -0.0472 -0.0322 70  ALA   B N   
4827 C CA  . ALA   B 70  ? 0.1881 0.1762 0.1659 -0.0003 -0.0525 -0.0291 70  ALA   B CA  
4828 C C   . ALA   B 70  ? 0.1946 0.1774 0.1831 0.0041  -0.0467 -0.0464 70  ALA   B C   
4829 O O   . ALA   B 70  ? 0.1969 0.1721 0.1968 0.0055  -0.0395 -0.0408 70  ALA   B O   
4830 C CB  . ALA   B 70  ? 0.1882 0.1929 0.1652 -0.0069 -0.0450 -0.0370 70  ALA   B CB  
4836 N N   . THR   B 71  ? 0.2030 0.1779 0.1969 0.0098  -0.0589 -0.0442 71  THR   B N   
4837 C CA  . THR   B 71  ? 0.2159 0.1791 0.2220 0.0151  -0.0633 -0.0385 71  THR   B CA  
4838 C C   . THR   B 71  ? 0.2046 0.1760 0.2706 0.0324  -0.0579 -0.0534 71  THR   B C   
4839 O O   . THR   B 71  ? 0.2205 0.1801 0.2972 0.0355  -0.0623 -0.0724 71  THR   B O   
4840 C CB  . THR   B 71  ? 0.2413 0.1936 0.2424 0.0082  -0.0727 -0.0184 71  THR   B CB  
4841 O OG1 . THR   B 71  ? 0.2531 0.2140 0.2845 -0.0176 -0.0727 0.0084  71  THR   B OG1 
4842 C CG2 . THR   B 71  ? 0.2601 0.1966 0.2616 0.0095  -0.0590 -0.0096 71  THR   B CG2 
4850 N N   . ASN   B 72  ? 0.1871 0.1860 0.2514 0.0150  -0.0711 -0.0772 72  ASN   B N   
4851 C CA  . ASN   B 72  ? 0.1886 0.1931 0.2604 0.0182  -0.0635 -0.0826 72  ASN   B CA  
4852 C C   . ASN   B 72  ? 0.1934 0.2028 0.2647 0.0007  -0.0362 -0.0755 72  ASN   B C   
4853 O O   . ASN   B 72  ? 0.1978 0.2147 0.3033 0.0054  -0.0136 -0.0805 72  ASN   B O   
4854 C CB  . ASN   B 72  ? 0.1893 0.2049 0.2737 0.0144  -0.0808 -0.0728 72  ASN   B CB  
4855 C CG  . ASN   B 72  ? 0.2081 0.2240 0.2815 0.0291  -0.0799 -0.0406 72  ASN   B CG  
4856 O OD1 . ASN   B 72  ? 0.2348 0.2455 0.2893 0.0143  -0.0491 -0.0413 72  ASN   B OD1 
4857 N ND2 . ASN   B 72  ? 0.2178 0.2370 0.3145 0.0520  -0.0739 -0.0177 72  ASN   B ND2 
4864 N N   . GLY   B 73  ? 0.1984 0.2034 0.2305 -0.0062 -0.0325 -0.0653 73  GLY   B N   
4865 C CA  . GLY   B 73  ? 0.1879 0.2186 0.1913 -0.0091 -0.0173 -0.0588 73  GLY   B CA  
4866 C C   . GLY   B 73  ? 0.1834 0.2100 0.1481 0.0068  -0.0199 -0.0500 73  GLY   B C   
4867 O O   . GLY   B 73  ? 0.1787 0.2002 0.1773 0.0069  -0.0179 -0.0502 73  GLY   B O   
4871 N N   . PRO   B 74  ? 0.1913 0.2226 0.1574 0.0070  -0.0190 -0.0423 74  PRO   B N   
4872 C CA  . PRO   B 74  ? 0.1803 0.2210 0.1508 0.0067  -0.0163 -0.0326 74  PRO   B CA  
4873 C C   . PRO   B 74  ? 0.1671 0.2013 0.1551 0.0055  -0.0074 -0.0320 74  PRO   B C   
4874 O O   . PRO   B 74  ? 0.1707 0.2039 0.2093 0.0077  0.0007  -0.0401 74  PRO   B O   
4875 C CB  . PRO   B 74  ? 0.1986 0.2408 0.1524 0.0031  -0.0258 -0.0274 74  PRO   B CB  
4876 C CG  . PRO   B 74  ? 0.2249 0.2524 0.1799 0.0005  -0.0116 -0.0169 74  PRO   B CG  
4877 C CD  . PRO   B 74  ? 0.2202 0.2340 0.1719 0.0151  -0.0059 -0.0279 74  PRO   B CD  
4885 N N   . LEU   B 75  ? 0.1730 0.1930 0.1443 0.0078  -0.0144 -0.0314 75  LEU   B N   
4886 C CA  . LEU   B 75  ? 0.1787 0.1936 0.1311 0.0045  -0.0101 -0.0052 75  LEU   B CA  
4887 C C   . LEU   B 75  ? 0.1852 0.1987 0.1174 0.0142  -0.0092 0.0101  75  LEU   B C   
4888 O O   . LEU   B 75  ? 0.1957 0.2160 0.1380 -0.0045 -0.0109 -0.0013 75  LEU   B O   
4889 C CB  . LEU   B 75  ? 0.1674 0.2089 0.1100 -0.0099 -0.0149 0.0005  75  LEU   B CB  
4890 C CG  . LEU   B 75  ? 0.2027 0.2170 0.1571 -0.0335 0.0032  0.0074  75  LEU   B CG  
4891 C CD1 . LEU   B 75  ? 0.2382 0.2296 0.1573 -0.0446 0.0154  0.0035  75  LEU   B CD1 
4892 C CD2 . LEU   B 75  ? 0.2487 0.2417 0.2497 -0.0213 0.0106  0.0102  75  LEU   B CD2 
4904 N N   . LYS   B 76  ? 0.1858 0.2054 0.1654 0.0125  0.0037  0.0186  76  LYS   B N   
4905 C CA  . LYS   B 76  ? 0.1948 0.2138 0.1957 0.0019  0.0291  0.0041  76  LYS   B CA  
4906 C C   . LYS   B 76  ? 0.1874 0.2035 0.1613 0.0015  0.0338  0.0169  76  LYS   B C   
4907 O O   . LYS   B 76  ? 0.1893 0.1767 0.1733 -0.0044 0.0145  0.0121  76  LYS   B O   
4908 C CB  . LYS   B 76  ? 0.2072 0.2154 0.2669 -0.0001 0.0402  -0.0242 76  LYS   B CB  
4909 C CG  . LYS   B 76  ? 0.2156 0.2327 0.2968 0.0066  0.0305  -0.0308 76  LYS   B CG  
4910 C CD  . LYS   B 76  ? 0.2242 0.2365 0.3159 0.0064  0.0254  -0.0307 76  LYS   B CD  
4911 C CE  . LYS   B 76  ? 0.2380 0.2567 0.3543 0.0041  0.0100  -0.0335 76  LYS   B CE  
4912 N NZ  . LYS   B 76  ? 0.2354 0.2629 0.3731 -0.0058 -0.0032 -0.0518 76  LYS   B NZ  
4926 N N   . VAL   B 77  ? 0.1957 0.2193 0.1774 0.0074  0.0253  0.0195  77  VAL   B N   
4927 C CA  . VAL   B 77  ? 0.1983 0.2115 0.1928 0.0072  0.0253  0.0474  77  VAL   B CA  
4928 C C   . VAL   B 77  ? 0.1884 0.1781 0.1872 0.0046  0.0374  0.0278  77  VAL   B C   
4929 O O   . VAL   B 77  ? 0.1885 0.1740 0.1938 0.0154  0.0504  0.0154  77  VAL   B O   
4930 C CB  . VAL   B 77  ? 0.2110 0.2245 0.2400 0.0038  0.0322  0.0610  77  VAL   B CB  
4931 C CG1 . VAL   B 77  ? 0.2037 0.2111 0.2631 -0.0004 0.0418  0.0736  77  VAL   B CG1 
4932 C CG2 . VAL   B 77  ? 0.2318 0.2446 0.2525 -0.0028 0.0052  0.0654  77  VAL   B CG2 
4942 N N   . GLY   B 78  ? 0.1824 0.1618 0.1897 0.0016  0.0264  0.0252  78  GLY   B N   
4943 C CA  . GLY   B 78  ? 0.1798 0.1648 0.1841 -0.0001 0.0319  0.0177  78  GLY   B CA  
4944 C C   . GLY   B 78  ? 0.1726 0.1659 0.1700 0.0084  0.0302  0.0296  78  GLY   B C   
4945 O O   . GLY   B 78  ? 0.1675 0.1556 0.1823 0.0180  0.0222  0.0289  78  GLY   B O   
4949 N N   . GLY   B 79  ? 0.1645 0.1671 0.1889 0.0047  0.0201  0.0150  79  GLY   B N   
4950 C CA  . GLY   B 79  ? 0.1617 0.1536 0.1743 0.0051  0.0155  0.0072  79  GLY   B CA  
4951 C C   . GLY   B 79  ? 0.1503 0.1530 0.1689 0.0139  0.0251  0.0031  79  GLY   B C   
4952 O O   . GLY   B 79  ? 0.1584 0.1549 0.1730 0.0096  0.0253  0.0167  79  GLY   B O   
4956 N N   . SER   B 80  ? 0.1475 0.1409 0.1628 0.0098  0.0223  0.0041  80  SER   B N   
4957 C CA  . SER   B 80  ? 0.1449 0.1533 0.1574 0.0017  0.0097  0.0112  80  SER   B CA  
4958 C C   . SER   B 80  ? 0.1428 0.1440 0.1648 0.0024  0.0027  0.0027  80  SER   B C   
4959 O O   . SER   B 80  ? 0.1536 0.1449 0.2002 0.0067  0.0111  0.0002  80  SER   B O   
4960 C CB  . SER   B 80  ? 0.1496 0.1591 0.1543 -0.0030 0.0155  0.0173  80  SER   B CB  
4961 O OG  . SER   B 80  ? 0.1571 0.1636 0.1763 -0.0047 -0.0038 0.0165  80  SER   B OG  
4967 N N   . CYS   B 81  ? 0.1416 0.1345 0.1712 0.0049  -0.0080 -0.0024 81  CYS   B N   
4968 C CA  . CYS   B 81  ? 0.1485 0.1327 0.1613 0.0030  -0.0159 0.0080  81  CYS   B CA  
4969 C C   . CYS   B 81  ? 0.1507 0.1347 0.1433 -0.0053 -0.0139 -0.0028 81  CYS   B C   
4970 O O   . CYS   B 81  ? 0.1686 0.1320 0.1715 0.0102  -0.0014 -0.0055 81  CYS   B O   
4971 C CB  . CYS   B 81  ? 0.1597 0.1430 0.1630 -0.0013 -0.0083 0.0068  81  CYS   B CB  
4972 S SG  . CYS   B 81  ? 0.1689 0.1639 0.1617 -0.0049 -0.0264 -0.0110 81  CYS   B SG  
4978 N N   . VAL   B 82  ? 0.1484 0.1379 0.1488 0.0037  -0.0083 -0.0005 82  VAL   B N   
4979 C CA  . VAL   B 82  ? 0.1591 0.1366 0.1494 -0.0039 -0.0004 0.0014  82  VAL   B CA  
4980 C C   . VAL   B 82  ? 0.1651 0.1270 0.1569 -0.0127 -0.0024 -0.0028 82  VAL   B C   
4981 O O   . VAL   B 82  ? 0.1732 0.1338 0.1906 -0.0088 -0.0052 -0.0178 82  VAL   B O   
4982 C CB  . VAL   B 82  ? 0.1706 0.1560 0.1699 -0.0012 -0.0159 0.0104  82  VAL   B CB  
4983 C CG1 . VAL   B 82  ? 0.1860 0.1783 0.1835 0.0037  -0.0185 0.0201  82  VAL   B CG1 
4984 C CG2 . VAL   B 82  ? 0.1776 0.1683 0.1911 -0.0148 -0.0333 0.0197  82  VAL   B CG2 
4994 N N   . LEU   B 83  ? 0.1478 0.1336 0.1621 -0.0140 -0.0161 -0.0129 83  LEU   B N   
4995 C CA  . LEU   B 83  ? 0.1572 0.1398 0.1434 -0.0135 -0.0149 -0.0050 83  LEU   B CA  
4996 C C   . LEU   B 83  ? 0.1554 0.1279 0.1382 -0.0199 -0.0214 -0.0051 83  LEU   B C   
4997 O O   . LEU   B 83  ? 0.1553 0.1448 0.1325 -0.0245 -0.0102 -0.0019 83  LEU   B O   
4998 C CB  . LEU   B 83  ? 0.1645 0.1511 0.1430 -0.0196 -0.0201 -0.0170 83  LEU   B CB  
4999 C CG  . LEU   B 83  ? 0.1839 0.1636 0.1530 -0.0216 -0.0051 -0.0090 83  LEU   B CG  
5000 C CD1 . LEU   B 83  ? 0.1986 0.1658 0.1559 -0.0143 -0.0144 -0.0056 83  LEU   B CD1 
5001 C CD2 . LEU   B 83  ? 0.2042 0.1658 0.1694 -0.0124 -0.0034 -0.0254 83  LEU   B CD2 
5013 N N   . SER   B 84  ? 0.1571 0.1418 0.1602 -0.0262 -0.0203 0.0001  84  SER   B N   
5014 C CA  . SER   B 84  ? 0.1583 0.1645 0.1540 -0.0326 -0.0094 0.0167  84  SER   B CA  
5015 C C   . SER   B 84  ? 0.1498 0.1738 0.0929 -0.0230 -0.0142 0.0249  84  SER   B C   
5016 O O   . SER   B 84  ? 0.1588 0.1719 0.1060 -0.0132 -0.0076 -0.0003 84  SER   B O   
5017 C CB  . SER   B 84  ? 0.1780 0.1642 0.2094 -0.0261 0.0150  0.0054  84  SER   B CB  
5018 O OG  . SER   B 84  ? 0.1651 0.1807 0.2578 -0.0411 0.0047  0.0158  84  SER   B OG  
5024 N N   . GLY   B 85  ? 0.1531 0.1893 0.1317 -0.0188 -0.0139 0.0241  85  GLY   B N   
5025 C CA  . GLY   B 85  ? 0.1608 0.1961 0.1522 -0.0302 0.0054  -0.0055 85  GLY   B CA  
5026 C C   . GLY   B 85  ? 0.1541 0.1776 0.1513 -0.0357 -0.0032 0.0031  85  GLY   B C   
5027 O O   . GLY   B 85  ? 0.1604 0.1801 0.1519 -0.0470 0.0170  -0.0150 85  GLY   B O   
5031 N N   . HIS   B 86  ? 0.1496 0.1661 0.1739 -0.0250 -0.0095 0.0068  86  HIS   B N   
5032 C CA  . HIS   B 86  ? 0.1567 0.1685 0.1748 -0.0353 -0.0215 0.0097  86  HIS   B CA  
5033 C C   . HIS   B 86  ? 0.1571 0.1814 0.1614 -0.0394 -0.0022 0.0363  86  HIS   B C   
5034 O O   . HIS   B 86  ? 0.1728 0.1879 0.1769 -0.0304 0.0016  0.0380  86  HIS   B O   
5035 C CB  . HIS   B 86  ? 0.1687 0.1827 0.1693 -0.0217 -0.0287 0.0027  86  HIS   B CB  
5036 C CG  . HIS   B 86  ? 0.1632 0.1901 0.1572 -0.0085 -0.0258 0.0066  86  HIS   B CG  
5037 N ND1 . HIS   B 86  ? 0.1683 0.2181 0.1908 -0.0229 -0.0184 -0.0121 86  HIS   B ND1 
5038 C CD2 . HIS   B 86  ? 0.1652 0.1905 0.1558 -0.0070 -0.0121 0.0066  86  HIS   B CD2 
5039 C CE1 . HIS   B 86  ? 0.1786 0.2032 0.1754 -0.0166 0.0036  -0.0359 86  HIS   B CE1 
5040 N NE2 . HIS   B 86  ? 0.1725 0.1967 0.1717 -0.0001 -0.0022 -0.0034 86  HIS   B NE2 
5048 N N   . ASN   B 87  ? 0.1571 0.1842 0.1676 -0.0227 0.0103  0.0306  87  ASN   B N   
5049 C CA  . ASN   B 87  ? 0.1702 0.2000 0.1669 -0.0272 0.0305  0.0183  87  ASN   B CA  
5050 C C   . ASN   B 87  ? 0.1838 0.1817 0.1610 -0.0300 0.0407  0.0085  87  ASN   B C   
5051 O O   . ASN   B 87  ? 0.2135 0.1934 0.2006 -0.0257 0.0608  0.0052  87  ASN   B O   
5052 C CB  . ASN   B 87  ? 0.1795 0.2349 0.2022 -0.0209 0.0313  0.0135  87  ASN   B CB  
5053 C CG  . ASN   B 87  ? 0.1797 0.2545 0.2072 0.0085  0.0432  0.0297  87  ASN   B CG  
5054 O OD1 . ASN   B 87  ? 0.1702 0.2394 0.2037 0.0135  0.0570  0.0508  87  ASN   B OD1 
5055 N ND2 . ASN   B 87  ? 0.2138 0.2680 0.2622 0.0128  0.0488  0.0225  87  ASN   B ND2 
5062 N N   . LEU   B 88  ? 0.1657 0.1795 0.1466 -0.0267 0.0077  0.0148  88  LEU   B N   
5063 C CA  . LEU   B 88  ? 0.1830 0.1727 0.1525 -0.0321 -0.0055 0.0029  88  LEU   B CA  
5064 C C   . LEU   B 88  ? 0.1861 0.1626 0.1585 -0.0368 -0.0075 -0.0046 88  LEU   B C   
5065 O O   . LEU   B 88  ? 0.2071 0.1659 0.1977 -0.0196 -0.0274 -0.0178 88  LEU   B O   
5066 C CB  . LEU   B 88  ? 0.1976 0.1738 0.1664 -0.0382 -0.0044 -0.0046 88  LEU   B CB  
5067 C CG  . LEU   B 88  ? 0.2393 0.1973 0.1897 -0.0356 -0.0211 0.0277  88  LEU   B CG  
5068 C CD1 . LEU   B 88  ? 0.2538 0.2238 0.2167 -0.0521 -0.0184 0.0423  88  LEU   B CD1 
5069 C CD2 . LEU   B 88  ? 0.2752 0.2305 0.2660 0.0095  -0.0490 0.0135  88  LEU   B CD2 
5081 N N   . ALA   B 89  ? 0.1714 0.1680 0.1500 -0.0375 0.0153  -0.0063 89  ALA   B N   
5082 C CA  . ALA   B 89  ? 0.1681 0.1559 0.1220 -0.0367 0.0071  -0.0036 89  ALA   B CA  
5083 C C   . ALA   B 89  ? 0.1747 0.1629 0.1296 -0.0399 0.0149  0.0013  89  ALA   B C   
5084 O O   . ALA   B 89  ? 0.1522 0.1674 0.1781 -0.0414 0.0147  -0.0232 89  ALA   B O   
5085 C CB  . ALA   B 89  ? 0.1555 0.1533 0.1489 -0.0349 0.0078  0.0095  89  ALA   B CB  
5091 N N   . LYS   B 90  ? 0.2037 0.1474 0.1452 -0.0471 -0.0112 0.0100  90  LYS   B N   
5092 C CA  . LYS   B 90  ? 0.2128 0.1446 0.1416 -0.0443 -0.0128 0.0093  90  LYS   B CA  
5093 C C   . LYS   B 90  ? 0.1915 0.1400 0.1440 -0.0389 -0.0183 -0.0044 90  LYS   B C   
5094 O O   . LYS   B 90  ? 0.1932 0.1571 0.1551 -0.0506 -0.0058 0.0040  90  LYS   B O   
5095 C CB  . LYS   B 90  ? 0.2219 0.1470 0.1869 -0.0355 0.0029  0.0184  90  LYS   B CB  
5096 C CG  . LYS   B 90  ? 0.2183 0.1686 0.1865 -0.0214 0.0213  0.0048  90  LYS   B CG  
5097 C CD  . LYS   B 90  ? 0.2466 0.2021 0.2435 -0.0081 0.0302  -0.0079 90  LYS   B CD  
5098 C CE  . LYS   B 90  ? 0.2570 0.2274 0.2925 -0.0099 0.0361  -0.0199 90  LYS   B CE  
5099 N NZ  . LYS   B 90  ? 0.2595 0.2198 0.2721 -0.0305 0.0665  -0.0212 90  LYS   B NZ  
5113 N N   . HIS   B 91  ? 0.1619 0.1368 0.1262 -0.0339 -0.0165 0.0057  91  HIS   B N   
5114 C CA  . HIS   B 91  ? 0.1597 0.1353 0.1480 -0.0210 -0.0125 0.0032  91  HIS   B CA  
5115 C C   . HIS   B 91  ? 0.1478 0.1358 0.1228 -0.0240 -0.0041 0.0111  91  HIS   B C   
5116 O O   . HIS   B 91  ? 0.1613 0.1494 0.1206 -0.0237 -0.0151 0.0003  91  HIS   B O   
5117 C CB  . HIS   B 91  ? 0.1796 0.1399 0.1794 -0.0097 -0.0073 0.0144  91  HIS   B CB  
5118 C CG  . HIS   B 91  ? 0.2107 0.1605 0.2447 -0.0030 0.0187  0.0158  91  HIS   B CG  
5119 N ND1 . HIS   B 91  ? 0.2387 0.1611 0.3148 -0.0013 0.0269  0.0090  91  HIS   B ND1 
5120 C CD2 . HIS   B 91  ? 0.2281 0.1837 0.3111 0.0114  0.0057  0.0542  91  HIS   B CD2 
5121 C CE1 . HIS   B 91  ? 0.2448 0.1772 0.3393 0.0168  0.0278  0.0115  91  HIS   B CE1 
5122 N NE2 . HIS   B 91  ? 0.2415 0.1912 0.3519 0.0299  0.0251  0.0548  91  HIS   B NE2 
5130 N N   . CYS   B 92  ? 0.1404 0.1390 0.1270 -0.0211 -0.0125 -0.0033 92  CYS   B N   
5131 C CA  . CYS   B 92  ? 0.1461 0.1363 0.1139 -0.0250 -0.0040 -0.0038 92  CYS   B CA  
5132 C C   . CYS   B 92  ? 0.1486 0.1287 0.1222 -0.0190 0.0070  -0.0066 92  CYS   B C   
5133 O O   . CYS   B 92  ? 0.1541 0.1415 0.1384 -0.0161 0.0038  -0.0002 92  CYS   B O   
5134 C CB  . CYS   B 92  ? 0.1488 0.1460 0.1362 -0.0175 -0.0058 0.0033  92  CYS   B CB  
5135 S SG  . CYS   B 92  ? 0.1473 0.1400 0.1473 -0.0098 -0.0092 0.0059  92  CYS   B SG  
5141 N N   . LEU   B 93  ? 0.1417 0.1303 0.1359 -0.0171 -0.0014 -0.0057 93  LEU   B N   
5142 C CA  . LEU   B 93  ? 0.1428 0.1366 0.1119 -0.0078 -0.0071 0.0026  93  LEU   B CA  
5143 C C   . LEU   B 93  ? 0.1351 0.1370 0.0875 -0.0003 -0.0061 0.0090  93  LEU   B C   
5144 O O   . LEU   B 93  ? 0.1411 0.1245 0.1458 -0.0061 -0.0085 -0.0078 93  LEU   B O   
5145 C CB  . LEU   B 93  ? 0.1463 0.1292 0.1386 -0.0070 -0.0050 0.0034  93  LEU   B CB  
5146 C CG  . LEU   B 93  ? 0.1411 0.1430 0.1718 -0.0103 -0.0071 0.0164  93  LEU   B CG  
5147 C CD1 . LEU   B 93  ? 0.1431 0.1472 0.1798 0.0132  0.0004  -0.0077 93  LEU   B CD1 
5148 C CD2 . LEU   B 93  ? 0.1394 0.1526 0.1752 -0.0048 -0.0143 -0.0005 93  LEU   B CD2 
5160 N N   . HIS   B 94  ? 0.1441 0.1304 0.0933 -0.0052 -0.0138 0.0012  94  HIS   B N   
5161 C CA  . HIS   B 94  ? 0.1498 0.1254 0.0964 -0.0049 -0.0093 0.0064  94  HIS   B CA  
5162 C C   . HIS   B 94  ? 0.1401 0.1275 0.1545 -0.0062 -0.0079 0.0083  94  HIS   B C   
5163 O O   . HIS   B 94  ? 0.1396 0.1336 0.1876 -0.0030 0.0176  -0.0072 94  HIS   B O   
5164 C CB  . HIS   B 94  ? 0.1423 0.1335 0.1384 -0.0017 -0.0108 0.0008  94  HIS   B CB  
5165 C CG  . HIS   B 94  ? 0.1384 0.1316 0.1412 -0.0083 -0.0173 -0.0005 94  HIS   B CG  
5166 N ND1 . HIS   B 94  ? 0.1428 0.1401 0.1346 -0.0065 -0.0175 -0.0047 94  HIS   B ND1 
5167 C CD2 . HIS   B 94  ? 0.1401 0.1370 0.1396 0.0013  -0.0077 -0.0000 94  HIS   B CD2 
5168 C CE1 . HIS   B 94  ? 0.1464 0.1396 0.1469 -0.0064 -0.0185 -0.0044 94  HIS   B CE1 
5169 N NE2 . HIS   B 94  ? 0.1360 0.1450 0.1530 -0.0110 -0.0129 0.0063  94  HIS   B NE2 
5177 N N   . VAL   B 95  ? 0.1280 0.1317 0.1582 -0.0044 -0.0037 0.0000  95  VAL   B N   
5178 C CA  . VAL   B 95  ? 0.1309 0.1405 0.1413 -0.0014 -0.0031 0.0162  95  VAL   B CA  
5179 C C   . VAL   B 95  ? 0.1485 0.1395 0.1364 -0.0034 0.0117  0.0162  95  VAL   B C   
5180 O O   . VAL   B 95  ? 0.1497 0.1313 0.1651 0.0089  0.0083  0.0217  95  VAL   B O   
5181 C CB  . VAL   B 95  ? 0.1398 0.1343 0.1521 -0.0007 -0.0071 0.0127  95  VAL   B CB  
5182 C CG1 . VAL   B 95  ? 0.1565 0.1473 0.1920 -0.0075 0.0119  0.0212  95  VAL   B CG1 
5183 C CG2 . VAL   B 95  ? 0.1403 0.1319 0.1466 0.0051  0.0003  -0.0025 95  VAL   B CG2 
5193 N N   . VAL   B 96  ? 0.1590 0.1444 0.1439 0.0058  0.0092  0.0195  96  VAL   B N   
5194 C CA  . VAL   B 96  ? 0.1729 0.1474 0.1320 0.0074  0.0134  0.0252  96  VAL   B CA  
5195 C C   . VAL   B 96  ? 0.1747 0.1505 0.1554 0.0116  0.0270  0.0136  96  VAL   B C   
5196 O O   . VAL   B 96  ? 0.1754 0.1521 0.1884 -0.0022 0.0386  0.0008  96  VAL   B O   
5197 C CB  . VAL   B 96  ? 0.1699 0.1772 0.1465 0.0116  0.0036  0.0149  96  VAL   B CB  
5198 C CG1 . VAL   B 96  ? 0.1703 0.1908 0.1483 0.0175  0.0102  0.0006  96  VAL   B CG1 
5199 C CG2 . VAL   B 96  ? 0.1780 0.1759 0.1622 0.0069  0.0124  0.0045  96  VAL   B CG2 
5209 N N   . GLY   B 97  ? 0.1822 0.1520 0.1488 0.0084  0.0150  0.0215  97  GLY   B N   
5210 C CA  . GLY   B 97  ? 0.2029 0.1570 0.1596 0.0109  0.0168  0.0292  97  GLY   B CA  
5211 C C   . GLY   B 97  ? 0.2303 0.1697 0.1799 0.0140  0.0261  0.0316  97  GLY   B C   
5212 O O   . GLY   B 97  ? 0.2451 0.1748 0.1756 0.0144  0.0138  0.0201  97  GLY   B O   
5216 N N   . PRO   B 98  ? 0.2489 0.1842 0.1941 0.0235  0.0613  0.0493  98  PRO   B N   
5217 C CA  . PRO   B 98  ? 0.2713 0.2097 0.2036 0.0437  0.0727  0.0470  98  PRO   B CA  
5218 C C   . PRO   B 98  ? 0.2844 0.2066 0.1756 0.0594  0.0750  0.0593  98  PRO   B C   
5219 O O   . PRO   B 98  ? 0.2625 0.1968 0.1869 0.0411  0.0691  0.0460  98  PRO   B O   
5220 C CB  . PRO   B 98  ? 0.2654 0.2196 0.2284 0.0414  0.0919  0.0567  98  PRO   B CB  
5221 C CG  . PRO   B 98  ? 0.2509 0.2012 0.2472 0.0338  0.0824  0.0748  98  PRO   B CG  
5222 C CD  . PRO   B 98  ? 0.2342 0.1833 0.2402 0.0369  0.0863  0.0638  98  PRO   B CD  
5230 N N   A ASN   B 99  ? 0.2973 0.2243 0.1818 0.0849  0.0754  0.0488  99  ASN   B N   
5231 N N   B ASN   B 99  ? 0.2995 0.2283 0.1993 0.0708  0.0717  0.0549  99  ASN   B N   
5232 C CA  A ASN   B 99  ? 0.3142 0.2385 0.1893 0.0982  0.0701  0.0695  99  ASN   B CA  
5233 C CA  B ASN   B 99  ? 0.3152 0.2466 0.2211 0.0778  0.0689  0.0663  99  ASN   B CA  
5234 C C   A ASN   B 99  ? 0.3271 0.2724 0.2199 0.1058  0.1008  0.0857  99  ASN   B C   
5235 C C   B ASN   B 99  ? 0.3267 0.2715 0.2468 0.0890  0.0914  0.0837  99  ASN   B C   
5236 O O   A ASN   B 99  ? 0.3452 0.2904 0.2375 0.1043  0.1006  0.0867  99  ASN   B O   
5237 O O   B ASN   B 99  ? 0.3355 0.2821 0.2595 0.0896  0.0894  0.0835  99  ASN   B O   
5238 C CB  A ASN   B 99  ? 0.3245 0.2317 0.1931 0.0969  0.0561  0.0692  99  ASN   B CB  
5239 C CB  B ASN   B 99  ? 0.3219 0.2456 0.2261 0.0723  0.0544  0.0593  99  ASN   B CB  
5240 C CG  A ASN   B 99  ? 0.3315 0.2350 0.2101 0.0869  0.0558  0.0619  99  ASN   B CG  
5241 C CG  B ASN   B 99  ? 0.3268 0.2482 0.2332 0.0640  0.0489  0.0513  99  ASN   B CG  
5242 O OD1 A ASN   B 99  ? 0.3313 0.2353 0.2460 0.0871  0.0680  0.0681  99  ASN   B OD1 
5243 O OD1 B ASN   B 99  ? 0.3280 0.2480 0.2479 0.0632  0.0521  0.0556  99  ASN   B OD1 
5244 N ND2 A ASN   B 99  ? 0.3337 0.2332 0.2036 0.0824  0.0356  0.0467  99  ASN   B ND2 
5245 N ND2 B ASN   B 99  ? 0.3283 0.2486 0.2312 0.0601  0.0387  0.0409  99  ASN   B ND2 
5258 N N   . VAL   B 100 ? 0.3334 0.2808 0.2724 0.0857  0.1100  0.1044  100 VAL   B N   
5259 C CA  . VAL   B 100 ? 0.3658 0.3110 0.3386 0.0728  0.0972  0.1313  100 VAL   B CA  
5260 C C   . VAL   B 100 ? 0.4003 0.3297 0.3288 0.0704  0.0873  0.1583  100 VAL   B C   
5261 O O   . VAL   B 100 ? 0.4088 0.3535 0.3546 0.0760  0.1129  0.1502  100 VAL   B O   
5262 C CB  . VAL   B 100 ? 0.3704 0.3222 0.4174 0.0425  0.0917  0.1451  100 VAL   B CB  
5263 C CG1 . VAL   B 100 ? 0.3781 0.3294 0.4411 0.0356  0.0915  0.1396  100 VAL   B CG1 
5264 C CG2 . VAL   B 100 ? 0.3640 0.3265 0.4420 0.0316  0.0896  0.1522  100 VAL   B CG2 
5275 N N   A ASN   B 101 ? 0.4154 0.3236 0.3266 0.0786  0.0613  0.1689  101 ASN   B N   
5276 N N   B ASN   B 101 ? 0.4163 0.3444 0.3357 0.0640  0.0644  0.1346  101 ASN   B N   
5277 C CA  A ASN   B 101 ? 0.4390 0.3302 0.3308 0.0733  0.0336  0.1739  101 ASN   B CA  
5278 C CA  B ASN   B 101 ? 0.4360 0.3643 0.3485 0.0525  0.0405  0.1089  101 ASN   B CA  
5279 C C   A ASN   B 101 ? 0.4789 0.3678 0.3569 0.0664  0.0200  0.1662  101 ASN   B C   
5280 C C   B ASN   B 101 ? 0.4652 0.3944 0.3773 0.0467  0.0300  0.0927  101 ASN   B C   
5281 O O   A ASN   B 101 ? 0.4794 0.3776 0.3853 0.0693  0.0257  0.1373  101 ASN   B O   
5282 O O   B ASN   B 101 ? 0.4641 0.3975 0.3876 0.0491  0.0320  0.0813  101 ASN   B O   
5283 C CB  A ASN   B 101 ? 0.4272 0.3069 0.3408 0.0655  0.0303  0.1576  101 ASN   B CB  
5284 C CB  B ASN   B 101 ? 0.4279 0.3554 0.3447 0.0455  0.0328  0.0918  101 ASN   B CB  
5285 C CG  A ASN   B 101 ? 0.4145 0.2863 0.3433 0.0638  0.0235  0.1539  101 ASN   B CG  
5286 C CG  B ASN   B 101 ? 0.4204 0.3481 0.3404 0.0410  0.0267  0.0808  101 ASN   B CG  
5287 O OD1 A ASN   B 101 ? 0.4133 0.2841 0.3693 0.0541  0.0375  0.1486  101 ASN   B OD1 
5288 O OD1 B ASN   B 101 ? 0.4187 0.3469 0.3486 0.0381  0.0302  0.0767  101 ASN   B OD1 
5289 N ND2 A ASN   B 101 ? 0.4063 0.2773 0.3345 0.0673  0.0142  0.1412  101 ASN   B ND2 
5290 N ND2 B ASN   B 101 ? 0.4162 0.3445 0.3310 0.0397  0.0219  0.0745  101 ASN   B ND2 
5303 N N   A LYS   B 102 ? 0.5167 0.4045 0.3853 0.0524  0.0161  0.1587  102 LYS   B N   
5304 N N   B LYS   B 102 ? 0.4945 0.4226 0.4066 0.0383  0.0233  0.0816  102 LYS   B N   
5305 C CA  A LYS   B 102 ? 0.5518 0.4471 0.4229 0.0339  0.0176  0.1329  102 LYS   B CA  
5306 C CA  B LYS   B 102 ? 0.5216 0.4515 0.4406 0.0285  0.0199  0.0674  102 LYS   B CA  
5307 C C   A LYS   B 102 ? 0.5631 0.4620 0.4091 0.0359  0.0216  0.1382  102 LYS   B C   
5308 C C   B LYS   B 102 ? 0.5329 0.4616 0.4358 0.0320  0.0256  0.0769  102 LYS   B C   
5309 O O   A LYS   B 102 ? 0.5728 0.4662 0.4153 0.0351  0.0067  0.1364  102 LYS   B O   
5310 O O   B LYS   B 102 ? 0.5386 0.4640 0.4408 0.0306  0.0177  0.0728  102 LYS   B O   
5311 C CB  A LYS   B 102 ? 0.5708 0.4723 0.4787 0.0169  0.0271  0.0908  102 LYS   B CB  
5312 C CB  B LYS   B 102 ? 0.5341 0.4678 0.4800 0.0177  0.0176  0.0419  102 LYS   B CB  
5313 C CG  A LYS   B 102 ? 0.5864 0.4941 0.5307 0.0036  0.0366  0.0509  102 LYS   B CG  
5314 C CG  B LYS   B 102 ? 0.5442 0.4815 0.5173 0.0089  0.0167  0.0194  102 LYS   B CG  
5315 C CD  A LYS   B 102 ? 0.6009 0.5124 0.5845 -0.0061 0.0458  0.0207  102 LYS   B CD  
5316 C CD  B LYS   B 102 ? 0.5535 0.4935 0.5567 0.0025  0.0177  0.0026  102 LYS   B CD  
5317 C CE  A LYS   B 102 ? 0.6109 0.5243 0.6237 -0.0133 0.0531  -0.0009 102 LYS   B CE  
5318 C CE  B LYS   B 102 ? 0.5602 0.5022 0.5854 -0.0019 0.0182  -0.0094 102 LYS   B CE  
5319 N NZ  A LYS   B 102 ? 0.6169 0.5324 0.6470 -0.0162 0.0554  -0.0143 102 LYS   B NZ  
5320 N NZ  B LYS   B 102 ? 0.5646 0.5077 0.6028 -0.0044 0.0174  -0.0166 102 LYS   B NZ  
5347 N N   A GLY   B 103 ? 0.5609 0.4690 0.4101 0.0387  0.0414  0.1371  103 GLY   B N   
5348 N N   B GLY   B 103 ? 0.5366 0.4669 0.4362 0.0373  0.0400  0.0873  103 GLY   B N   
5349 C CA  A GLY   B 103 ? 0.5552 0.4724 0.4274 0.0472  0.0592  0.1264  103 GLY   B CA  
5350 C CA  B GLY   B 103 ? 0.5380 0.4696 0.4429 0.0458  0.0562  0.0938  103 GLY   B CA  
5351 C C   A GLY   B 103 ? 0.5450 0.4711 0.4332 0.0555  0.0755  0.1158  103 GLY   B C   
5352 C C   B GLY   B 103 ? 0.5357 0.4686 0.4431 0.0549  0.0729  0.0986  103 GLY   B C   
5353 O O   A GLY   B 103 ? 0.5492 0.4776 0.4363 0.0530  0.0804  0.1193  103 GLY   B O   
5354 O O   B GLY   B 103 ? 0.5392 0.4732 0.4498 0.0531  0.0758  0.1019  103 GLY   B O   
5361 N N   . GLU   B 104 ? 0.5277 0.4607 0.4251 0.0659  0.0892  0.0950  104 GLU   B N   
5362 C CA  . GLU   B 104 ? 0.5005 0.4417 0.4029 0.0906  0.1087  0.0724  104 GLU   B CA  
5363 C C   . GLU   B 104 ? 0.4926 0.4404 0.4288 0.0711  0.1559  0.0738  104 GLU   B C   
5364 O O   . GLU   B 104 ? 0.4932 0.4437 0.4607 0.0651  0.1594  0.0772  104 GLU   B O   
5365 C CB  . GLU   B 104 ? 0.4875 0.4254 0.3757 0.1286  0.0726  0.0359  104 GLU   B CB  
5366 C CG  . GLU   B 104 ? 0.4775 0.4153 0.3499 0.1612  0.0271  0.0003  104 GLU   B CG  
5367 C CD  . GLU   B 104 ? 0.4720 0.4119 0.3141 0.1831  -0.0115 -0.0285 104 GLU   B CD  
5368 O OE1 . GLU   B 104 ? 0.4665 0.4033 0.2667 0.1958  -0.0071 -0.0384 104 GLU   B OE1 
5369 O OE2 . GLU   B 104 ? 0.4722 0.4216 0.3162 0.1837  -0.0498 -0.0406 104 GLU   B OE2 
5377 N N   . ASP   B 105 ? 0.4778 0.4358 0.4149 0.0582  0.1939  0.0729  105 ASP   B N   
5378 C CA  . ASP   B 105 ? 0.4732 0.4360 0.4327 0.0389  0.2124  0.0552  105 ASP   B CA  
5379 C C   . ASP   B 105 ? 0.4411 0.3945 0.3977 0.0145  0.2126  0.0441  105 ASP   B C   
5380 O O   . ASP   B 105 ? 0.4310 0.3920 0.3872 0.0234  0.2295  0.0491  105 ASP   B O   
5381 C CB  . ASP   B 105 ? 0.4939 0.4737 0.5048 0.0464  0.2250  0.0422  105 ASP   B CB  
5382 C CG  . ASP   B 105 ? 0.5049 0.4966 0.5728 0.0480  0.2441  0.0382  105 ASP   B CG  
5383 O OD1 . ASP   B 105 ? 0.5034 0.5026 0.5788 0.0414  0.2690  0.0566  105 ASP   B OD1 
5384 O OD2 . ASP   B 105 ? 0.5080 0.5065 0.6111 0.0548  0.2395  0.0204  105 ASP   B OD2 
5389 N N   A ILE   B 106 ? 0.4260 0.3644 0.3962 0.0025  0.2056  0.0433  106 ILE   B N   
5390 N N   B ILE   B 106 ? 0.4333 0.3848 0.3952 0.0062  0.1775  0.0352  106 ILE   B N   
5391 C CA  A ILE   B 106 ? 0.4004 0.3334 0.3933 -0.0133 0.2062  0.0375  106 ILE   B CA  
5392 C CA  B ILE   B 106 ? 0.4198 0.3734 0.3944 -0.0029 0.1483  0.0247  106 ILE   B CA  
5393 C C   A ILE   B 106 ? 0.3549 0.3109 0.3719 -0.0129 0.2134  0.0244  106 ILE   B C   
5394 C C   B ILE   B 106 ? 0.3946 0.3600 0.3902 -0.0030 0.1368  0.0165  106 ILE   B C   
5395 O O   A ILE   B 106 ? 0.3394 0.2882 0.3777 -0.0207 0.2073  0.0257  106 ILE   B O   
5396 O O   B ILE   B 106 ? 0.3936 0.3548 0.3959 -0.0058 0.1346  0.0143  106 ILE   B O   
5397 C CB  A ILE   B 106 ? 0.4184 0.3273 0.4048 -0.0285 0.2009  0.0456  106 ILE   B CB  
5398 C CB  B ILE   B 106 ? 0.4299 0.3752 0.3972 -0.0111 0.1328  0.0230  106 ILE   B CB  
5399 C CG1 A ILE   B 106 ? 0.4277 0.3245 0.4100 -0.0258 0.1834  0.0414  106 ILE   B CG1 
5400 C CG1 B ILE   B 106 ? 0.4345 0.3749 0.3969 -0.0114 0.1193  0.0196  106 ILE   B CG1 
5401 C CG2 A ILE   B 106 ? 0.4229 0.3324 0.4248 -0.0365 0.2033  0.0437  106 ILE   B CG2 
5402 C CG2 B ILE   B 106 ? 0.4330 0.3792 0.4062 -0.0150 0.1307  0.0213  106 ILE   B CG2 
5403 C CD1 A ILE   B 106 ? 0.4321 0.3239 0.4060 -0.0223 0.1731  0.0430  106 ILE   B CD1 
5404 C CD1 B ILE   B 106 ? 0.4365 0.3745 0.3950 -0.0109 0.1111  0.0186  106 ILE   B CD1 
5427 N N   A GLN   B 107 ? 0.3333 0.3178 0.3927 -0.0193 0.2033  0.0234  107 GLN   B N   
5428 N N   B GLN   B 107 ? 0.3715 0.3532 0.3965 -0.0049 0.1274  0.0149  107 GLN   B N   
5429 C CA  A GLN   B 107 ? 0.3062 0.3204 0.4016 -0.0276 0.1781  0.0255  107 GLN   B CA  
5430 C CA  B GLN   B 107 ? 0.3462 0.3440 0.3976 -0.0061 0.1128  0.0155  107 GLN   B CA  
5431 C C   A GLN   B 107 ? 0.2799 0.2974 0.3682 -0.0195 0.1448  0.0154  107 GLN   B C   
5432 C C   B GLN   B 107 ? 0.3071 0.3138 0.3612 -0.0021 0.1141  0.0132  107 GLN   B C   
5433 O O   A GLN   B 107 ? 0.2586 0.2997 0.3920 -0.0106 0.1095  -0.0174 107 GLN   B O   
5434 O O   B GLN   B 107 ? 0.3009 0.3154 0.3669 0.0025  0.0965  0.0006  107 GLN   B O   
5435 C CB  A GLN   B 107 ? 0.3354 0.3622 0.4658 -0.0323 0.1555  0.0244  107 GLN   B CB  
5436 C CB  B GLN   B 107 ? 0.3675 0.3687 0.4448 -0.0096 0.0910  0.0154  107 GLN   B CB  
5437 C CG  A GLN   B 107 ? 0.3688 0.4015 0.5260 -0.0321 0.1154  0.0234  107 GLN   B CG  
5438 C CG  B GLN   B 107 ? 0.3867 0.3901 0.4897 -0.0102 0.0667  0.0157  107 GLN   B CG  
5439 C CD  A GLN   B 107 ? 0.3950 0.4280 0.5711 -0.0356 0.0834  0.0245  107 GLN   B CD  
5440 C CD  B GLN   B 107 ? 0.4022 0.4064 0.5249 -0.0121 0.0470  0.0163  107 GLN   B CD  
5441 O OE1 A GLN   B 107 ? 0.4063 0.4390 0.5866 -0.0323 0.0801  0.0223  107 GLN   B OE1 
5442 O OE1 B GLN   B 107 ? 0.4080 0.4127 0.5354 -0.0116 0.0453  0.0167  107 GLN   B OE1 
5443 N NE2 A GLN   B 107 ? 0.4057 0.4352 0.5895 -0.0349 0.0630  0.0274  107 GLN   B NE2 
5444 N NE2 B GLN   B 107 ? 0.4085 0.4115 0.5393 -0.0115 0.0357  0.0171  107 GLN   B NE2 
5461 N N   . LEU   B 108 ? 0.2689 0.2840 0.3292 0.0074  0.1267  0.0186  108 LEU   B N   
5462 C CA  . LEU   B 108 ? 0.2473 0.2575 0.2755 0.0210  0.0934  0.0373  108 LEU   B CA  
5463 C C   . LEU   B 108 ? 0.2037 0.2083 0.2593 0.0118  0.0610  0.0316  108 LEU   B C   
5464 O O   . LEU   B 108 ? 0.1882 0.1895 0.2500 0.0191  0.0552  0.0287  108 LEU   B O   
5465 C CB  . LEU   B 108 ? 0.2648 0.2852 0.2424 0.0308  0.0993  0.0602  108 LEU   B CB  
5466 C CG  . LEU   B 108 ? 0.2830 0.3185 0.2567 0.0383  0.0868  0.0429  108 LEU   B CG  
5467 C CD1 . LEU   B 108 ? 0.2979 0.3364 0.2473 0.0348  0.0870  0.0458  108 LEU   B CD1 
5468 C CD2 . LEU   B 108 ? 0.2958 0.3275 0.2637 0.0437  0.0653  0.0249  108 LEU   B CD2 
5481 N N   . LEU   B 109 ? 0.1869 0.1778 0.2552 -0.0022 0.0539  0.0201  109 LEU   B N   
5482 C CA  . LEU   B 109 ? 0.1583 0.1584 0.2633 -0.0021 0.0414  0.0319  109 LEU   B CA  
5483 C C   . LEU   B 109 ? 0.1539 0.1433 0.2620 0.0011  0.0420  0.0203  109 LEU   B C   
5484 O O   . LEU   B 109 ? 0.1577 0.1426 0.2612 0.0013  0.0352  0.0236  109 LEU   B O   
5485 C CB  . LEU   B 109 ? 0.1749 0.1463 0.2754 0.0005  0.0306  0.0280  109 LEU   B CB  
5486 C CG  . LEU   B 109 ? 0.1684 0.1407 0.2642 0.0049  0.0266  0.0120  109 LEU   B CG  
5487 C CD1 . LEU   B 109 ? 0.1588 0.1466 0.2575 0.0058  0.0191  0.0120  109 LEU   B CD1 
5488 C CD2 . LEU   B 109 ? 0.1766 0.1395 0.2715 0.0046  0.0274  0.0187  109 LEU   B CD2 
5500 N N   . LYS   B 110 ? 0.1512 0.1396 0.2539 -0.0086 0.0317  0.0108  110 LYS   B N   
5501 C CA  . LYS   B 110 ? 0.1545 0.1423 0.2636 -0.0060 0.0339  0.0169  110 LYS   B CA  
5502 C C   . LYS   B 110 ? 0.1466 0.1414 0.2440 -0.0031 0.0423  0.0152  110 LYS   B C   
5503 O O   . LYS   B 110 ? 0.1423 0.1398 0.2423 -0.0089 0.0333  -0.0006 110 LYS   B O   
5504 C CB  . LYS   B 110 ? 0.1569 0.1327 0.2764 -0.0052 0.0423  0.0092  110 LYS   B CB  
5505 C CG  . LYS   B 110 ? 0.1551 0.1357 0.2948 -0.0077 0.0170  0.0204  110 LYS   B CG  
5506 C CD  . LYS   B 110 ? 0.1656 0.1403 0.2843 -0.0118 0.0180  0.0224  110 LYS   B CD  
5507 C CE  . LYS   B 110 ? 0.1602 0.1528 0.3033 -0.0056 0.0264  0.0036  110 LYS   B CE  
5508 N NZ  . LYS   B 110 ? 0.1622 0.1679 0.3055 0.0032  0.0163  0.0125  110 LYS   B NZ  
5522 N N   . SER   B 111 ? 0.1477 0.1399 0.2707 -0.0041 0.0341  0.0125  111 SER   B N   
5523 C CA  . SER   B 111 ? 0.1546 0.1436 0.2387 -0.0059 0.0237  0.0122  111 SER   B CA  
5524 C C   . SER   B 111 ? 0.1526 0.1410 0.2207 -0.0059 0.0189  -0.0008 111 SER   B C   
5525 O O   . SER   B 111 ? 0.1472 0.1459 0.2352 -0.0108 0.0155  -0.0071 111 SER   B O   
5526 C CB  . SER   B 111 ? 0.1653 0.1662 0.2480 0.0135  0.0475  0.0173  111 SER   B CB  
5527 O OG  . SER   B 111 ? 0.1841 0.1887 0.2441 0.0195  0.0479  0.0330  111 SER   B OG  
5533 N N   . ALA   B 112 ? 0.1441 0.1452 0.2295 0.0026  0.0319  0.0050  112 ALA   B N   
5534 C CA  . ALA   B 112 ? 0.1377 0.1475 0.2195 0.0024  0.0231  0.0085  112 ALA   B CA  
5535 C C   . ALA   B 112 ? 0.1257 0.1424 0.2198 0.0026  0.0213  0.0049  112 ALA   B C   
5536 O O   . ALA   B 112 ? 0.1336 0.1444 0.2267 -0.0078 0.0182  -0.0029 112 ALA   B O   
5537 C CB  . ALA   B 112 ? 0.1471 0.1473 0.2285 0.0080  0.0120  0.0128  112 ALA   B CB  
5543 N N   . TYR   B 113 ? 0.1349 0.1282 0.2056 -0.0064 0.0171  0.0029  113 TYR   B N   
5544 C CA  . TYR   B 113 ? 0.1297 0.1370 0.2027 -0.0062 0.0167  -0.0030 113 TYR   B CA  
5545 C C   . TYR   B 113 ? 0.1267 0.1238 0.1953 -0.0112 0.0198  0.0002  113 TYR   B C   
5546 O O   . TYR   B 113 ? 0.1329 0.1280 0.1992 -0.0059 0.0086  -0.0016 113 TYR   B O   
5547 C CB  . TYR   B 113 ? 0.1293 0.1227 0.2168 -0.0017 0.0163  0.0082  113 TYR   B CB  
5548 C CG  . TYR   B 113 ? 0.1335 0.1287 0.2313 -0.0081 0.0060  0.0107  113 TYR   B CG  
5549 C CD1 . TYR   B 113 ? 0.1402 0.1349 0.2416 -0.0094 0.0145  0.0130  113 TYR   B CD1 
5550 C CD2 . TYR   B 113 ? 0.1452 0.1313 0.2381 -0.0066 0.0041  0.0113  113 TYR   B CD2 
5551 C CE1 . TYR   B 113 ? 0.1458 0.1461 0.2254 -0.0061 0.0113  0.0063  113 TYR   B CE1 
5552 C CE2 . TYR   B 113 ? 0.1494 0.1295 0.2336 -0.0012 0.0068  0.0135  113 TYR   B CE2 
5553 C CZ  . TYR   B 113 ? 0.1365 0.1336 0.2383 0.0002  0.0025  0.0113  113 TYR   B CZ  
5554 O OH  . TYR   B 113 ? 0.1476 0.1239 0.2753 0.0033  0.0155  -0.0058 113 TYR   B OH  
5564 N N   . GLU   B 114 ? 0.1296 0.1229 0.2144 -0.0039 0.0183  0.0015  114 GLU   B N   
5565 C CA  . GLU   B 114 ? 0.1353 0.1187 0.2145 0.0040  0.0110  -0.0021 114 GLU   B CA  
5566 C C   . GLU   B 114 ? 0.1352 0.1218 0.2076 0.0016  0.0040  -0.0019 114 GLU   B C   
5567 O O   . GLU   B 114 ? 0.1267 0.1258 0.2252 0.0045  0.0042  0.0059  114 GLU   B O   
5568 C CB  . GLU   B 114 ? 0.1310 0.1280 0.2366 -0.0001 0.0257  -0.0082 114 GLU   B CB  
5569 C CG  . GLU   B 114 ? 0.1347 0.1245 0.2527 -0.0059 0.0221  -0.0020 114 GLU   B CG  
5570 C CD  . GLU   B 114 ? 0.1383 0.1219 0.2490 -0.0119 0.0165  0.0047  114 GLU   B CD  
5571 O OE1 . GLU   B 114 ? 0.1325 0.1406 0.2418 -0.0101 0.0193  0.0094  114 GLU   B OE1 
5572 O OE2 . GLU   B 114 ? 0.1389 0.1459 0.2594 -0.0203 0.0113  -0.0028 114 GLU   B OE2 
5579 N N   . ASN   B 115 ? 0.1395 0.1227 0.1907 -0.0049 0.0070  -0.0010 115 ASN   B N   
5580 C CA  . ASN   B 115 ? 0.1374 0.1262 0.1737 -0.0157 0.0087  0.0122  115 ASN   B CA  
5581 C C   . ASN   B 115 ? 0.1319 0.1301 0.1946 -0.0145 0.0078  0.0018  115 ASN   B C   
5582 O O   . ASN   B 115 ? 0.1369 0.1317 0.1880 -0.0123 0.0068  0.0009  115 ASN   B O   
5583 C CB  . ASN   B 115 ? 0.1449 0.1353 0.1842 -0.0131 0.0090  0.0075  115 ASN   B CB  
5584 C CG  . ASN   B 115 ? 0.1535 0.1517 0.1881 -0.0027 0.0057  -0.0054 115 ASN   B CG  
5585 O OD1 . ASN   B 115 ? 0.1878 0.1644 0.2102 -0.0079 0.0286  -0.0167 115 ASN   B OD1 
5586 N ND2 . ASN   B 115 ? 0.1482 0.1620 0.1884 -0.0084 0.0184  0.0072  115 ASN   B ND2 
5593 N N   . PHE   B 116 ? 0.1372 0.1310 0.1752 -0.0009 0.0045  -0.0171 116 PHE   B N   
5594 C CA  . PHE   B 116 ? 0.1422 0.1349 0.1835 -0.0095 0.0019  -0.0135 116 PHE   B CA  
5595 C C   . PHE   B 116 ? 0.1382 0.1130 0.1802 -0.0140 0.0007  0.0072  116 PHE   B C   
5596 O O   . PHE   B 116 ? 0.1390 0.1349 0.1895 -0.0086 -0.0087 0.0055  116 PHE   B O   
5597 C CB  . PHE   B 116 ? 0.1358 0.1268 0.1642 -0.0055 -0.0046 0.0000  116 PHE   B CB  
5598 C CG  . PHE   B 116 ? 0.1246 0.1319 0.1657 -0.0080 -0.0027 0.0030  116 PHE   B CG  
5599 C CD1 . PHE   B 116 ? 0.1258 0.1388 0.1960 -0.0026 0.0045  0.0020  116 PHE   B CD1 
5600 C CD2 . PHE   B 116 ? 0.1292 0.1433 0.1634 -0.0046 0.0035  -0.0071 116 PHE   B CD2 
5601 C CE1 . PHE   B 116 ? 0.1359 0.1328 0.2024 -0.0027 -0.0161 0.0070  116 PHE   B CE1 
5602 C CE2 . PHE   B 116 ? 0.1259 0.1431 0.1804 -0.0076 -0.0019 0.0064  116 PHE   B CE2 
5603 C CZ  . PHE   B 116 ? 0.1232 0.1460 0.1908 -0.0008 -0.0094 0.0099  116 PHE   B CZ  
5613 N N   . ASN   B 117 ? 0.1352 0.1237 0.1908 -0.0096 -0.0037 0.0111  117 ASN   B N   
5614 C CA  . ASN   B 117 ? 0.1478 0.1306 0.1976 -0.0008 -0.0043 0.0091  117 ASN   B CA  
5615 C C   . ASN   B 117 ? 0.1509 0.1248 0.2067 -0.0012 -0.0052 0.0071  117 ASN   B C   
5616 O O   . ASN   B 117 ? 0.1502 0.1308 0.2409 -0.0083 -0.0383 0.0084  117 ASN   B O   
5617 C CB  . ASN   B 117 ? 0.1478 0.1340 0.2188 -0.0073 -0.0057 -0.0001 117 ASN   B CB  
5618 C CG  . ASN   B 117 ? 0.1395 0.1322 0.2186 -0.0029 0.0011  -0.0084 117 ASN   B CG  
5619 O OD1 . ASN   B 117 ? 0.1545 0.1335 0.2380 -0.0164 0.0045  -0.0055 117 ASN   B OD1 
5620 N ND2 . ASN   B 117 ? 0.1437 0.1387 0.2090 -0.0071 0.0002  -0.0093 117 ASN   B ND2 
5627 N N   . GLN   B 118 ? 0.1378 0.1282 0.2116 -0.0088 -0.0088 0.0004  118 GLN   B N   
5628 C CA  . GLN   B 118 ? 0.1484 0.1365 0.2273 0.0010  -0.0090 0.0045  118 GLN   B CA  
5629 C C   . GLN   B 118 ? 0.1439 0.1322 0.2375 -0.0040 -0.0075 -0.0007 118 GLN   B C   
5630 O O   . GLN   B 118 ? 0.1598 0.1327 0.2768 -0.0094 -0.0040 0.0126  118 GLN   B O   
5631 C CB  . GLN   B 118 ? 0.1559 0.1379 0.2285 -0.0040 -0.0168 0.0038  118 GLN   B CB  
5632 C CG  . GLN   B 118 ? 0.1656 0.1426 0.2308 0.0056  -0.0170 -0.0006 118 GLN   B CG  
5633 C CD  . GLN   B 118 ? 0.1694 0.1340 0.2304 0.0014  -0.0177 -0.0137 118 GLN   B CD  
5634 O OE1 . GLN   B 118 ? 0.1737 0.1377 0.2583 0.0075  0.0038  0.0017  118 GLN   B OE1 
5635 N NE2 . GLN   B 118 ? 0.1778 0.1333 0.2402 0.0059  -0.0252 -0.0020 118 GLN   B NE2 
5644 N N   . HIS   B 119 ? 0.1538 0.1393 0.1873 -0.0032 -0.0115 0.0040  119 HIS   B N   
5645 C CA  . HIS   B 119 ? 0.1634 0.1488 0.1666 -0.0034 -0.0170 0.0103  119 HIS   B CA  
5646 C C   . HIS   B 119 ? 0.1737 0.1542 0.1743 -0.0014 -0.0384 0.0096  119 HIS   B C   
5647 O O   . HIS   B 119 ? 0.1684 0.1498 0.1955 -0.0300 -0.0232 0.0087  119 HIS   B O   
5648 C CB  . HIS   B 119 ? 0.1698 0.1517 0.1838 -0.0057 -0.0218 0.0055  119 HIS   B CB  
5649 C CG  . HIS   B 119 ? 0.1669 0.1725 0.1973 0.0042  -0.0444 -0.0084 119 HIS   B CG  
5650 N ND1 . HIS   B 119 ? 0.1738 0.1784 0.2459 -0.0035 -0.0412 -0.0310 119 HIS   B ND1 
5651 C CD2 . HIS   B 119 ? 0.1791 0.1946 0.2017 0.0312  -0.0532 -0.0164 119 HIS   B CD2 
5652 C CE1 . HIS   B 119 ? 0.1939 0.1934 0.2339 0.0067  -0.0540 -0.0389 119 HIS   B CE1 
5653 N NE2 . HIS   B 119 ? 0.1999 0.2140 0.2185 0.0238  -0.0506 -0.0316 119 HIS   B NE2 
5661 N N   A GLU   B 120 ? 0.1899 0.1512 0.1671 -0.0112 -0.0529 0.0209  120 GLU   B N   
5662 N N   B GLU   B 120 ? 0.1920 0.1647 0.1928 -0.0084 -0.0363 0.0155  120 GLU   B N   
5663 C CA  A GLU   B 120 ? 0.2208 0.1739 0.1777 -0.0068 -0.0659 0.0429  120 GLU   B CA  
5664 C CA  B GLU   B 120 ? 0.2131 0.1827 0.2154 -0.0095 -0.0383 0.0269  120 GLU   B CA  
5665 C C   A GLU   B 120 ? 0.1942 0.1571 0.1791 -0.0259 -0.0515 0.0303  120 GLU   B C   
5666 C C   B GLU   B 120 ? 0.1945 0.1653 0.1978 -0.0235 -0.0341 0.0244  120 GLU   B C   
5667 O O   A GLU   B 120 ? 0.1859 0.1708 0.1874 -0.0243 -0.0461 0.0206  120 GLU   B O   
5668 O O   B GLU   B 120 ? 0.1902 0.1731 0.1975 -0.0217 -0.0274 0.0177  120 GLU   B O   
5669 C CB  A GLU   B 120 ? 0.2827 0.2139 0.2459 0.0120  -0.0891 0.0619  120 GLU   B CB  
5670 C CB  B GLU   B 120 ? 0.2545 0.2169 0.2788 0.0018  -0.0497 0.0362  120 GLU   B CB  
5671 C CG  A GLU   B 120 ? 0.3387 0.2787 0.3541 0.0204  -0.0906 0.0709  120 GLU   B CG  
5672 C CG  B GLU   B 120 ? 0.2944 0.2653 0.3519 0.0075  -0.0532 0.0457  120 GLU   B CG  
5673 C CD  A GLU   B 120 ? 0.3731 0.3269 0.4430 0.0288  -0.0938 0.0871  120 GLU   B CD  
5674 C CD  B GLU   B 120 ? 0.3228 0.3005 0.4165 0.0124  -0.0529 0.0565  120 GLU   B CD  
5675 O OE1 A GLU   B 120 ? 0.3898 0.3436 0.4760 0.0252  -0.0829 0.1038  120 GLU   B OE1 
5676 O OE1 B GLU   B 120 ? 0.3348 0.3142 0.4424 0.0129  -0.0490 0.0652  120 GLU   B OE1 
5677 O OE2 A GLU   B 120 ? 0.3944 0.3501 0.4919 0.0285  -0.0931 0.0774  120 GLU   B OE2 
5678 O OE2 B GLU   B 120 ? 0.3353 0.3107 0.4419 0.0115  -0.0576 0.0579  120 GLU   B OE2 
5691 N N   . VAL   B 121 ? 0.1814 0.1498 0.1908 -0.0330 -0.0353 0.0329  121 VAL   B N   
5692 C CA  . VAL   B 121 ? 0.1767 0.1568 0.1754 -0.0261 -0.0278 0.0296  121 VAL   B CA  
5693 C C   . VAL   B 121 ? 0.1748 0.1505 0.1604 -0.0221 -0.0236 0.0251  121 VAL   B C   
5694 O O   . VAL   B 121 ? 0.1782 0.1443 0.1881 -0.0378 -0.0364 0.0140  121 VAL   B O   
5695 C CB  . VAL   B 121 ? 0.1957 0.2056 0.1853 -0.0115 -0.0316 0.0302  121 VAL   B CB  
5696 C CG1 . VAL   B 121 ? 0.1973 0.2185 0.2283 -0.0281 -0.0084 0.0297  121 VAL   B CG1 
5697 C CG2 . VAL   B 121 ? 0.2264 0.2348 0.1866 0.0057  -0.0164 0.0099  121 VAL   B CG2 
5708 N N   . LEU   B 122 ? 0.1687 0.1453 0.1495 -0.0158 -0.0293 0.0119  122 LEU   B N   
5709 C CA  . LEU   B 122 ? 0.1510 0.1621 0.1283 -0.0196 -0.0236 0.0128  122 LEU   B CA  
5710 C C   . LEU   B 122 ? 0.1499 0.1450 0.1531 -0.0226 -0.0136 0.0064  122 LEU   B C   
5711 O O   . LEU   B 122 ? 0.1659 0.1478 0.1823 -0.0366 -0.0224 0.0022  122 LEU   B O   
5712 C CB  . LEU   B 122 ? 0.1753 0.1805 0.1590 -0.0019 -0.0289 0.0121  122 LEU   B CB  
5713 C CG  . LEU   B 122 ? 0.1664 0.1797 0.1773 -0.0213 -0.0185 -0.0027 122 LEU   B CG  
5714 C CD1 . LEU   B 122 ? 0.1748 0.1998 0.1834 -0.0279 -0.0294 0.0004  122 LEU   B CD1 
5715 C CD2 . LEU   B 122 ? 0.1681 0.1765 0.1577 -0.0145 -0.0082 -0.0184 122 LEU   B CD2 
5727 N N   . LEU   B 123 ? 0.1493 0.1340 0.1369 -0.0226 -0.0182 0.0150  123 LEU   B N   
5728 C CA  . LEU   B 123 ? 0.1538 0.1409 0.1456 -0.0233 -0.0218 0.0062  123 LEU   B CA  
5729 C C   . LEU   B 123 ? 0.1476 0.1396 0.1440 -0.0269 -0.0230 -0.0012 123 LEU   B C   
5730 O O   . LEU   B 123 ? 0.1588 0.1389 0.1398 -0.0304 -0.0135 -0.0002 123 LEU   B O   
5731 C CB  . LEU   B 123 ? 0.1524 0.1461 0.1456 -0.0258 -0.0112 0.0018  123 LEU   B CB  
5732 C CG  . LEU   B 123 ? 0.1529 0.1429 0.1671 -0.0243 -0.0075 -0.0021 123 LEU   B CG  
5733 C CD1 . LEU   B 123 ? 0.1725 0.1570 0.1840 -0.0234 -0.0014 -0.0234 123 LEU   B CD1 
5734 C CD2 . LEU   B 123 ? 0.1678 0.1570 0.1898 -0.0251 -0.0028 0.0141  123 LEU   B CD2 
5746 N N   . ALA   B 124 ? 0.1450 0.1280 0.1524 -0.0218 -0.0074 0.0006  124 ALA   B N   
5747 C CA  . ALA   B 124 ? 0.1380 0.1271 0.1583 -0.0160 -0.0043 -0.0040 124 ALA   B CA  
5748 C C   . ALA   B 124 ? 0.1359 0.1294 0.1349 -0.0196 -0.0139 -0.0001 124 ALA   B C   
5749 O O   . ALA   B 124 ? 0.1507 0.1336 0.1569 -0.0183 -0.0152 0.0012  124 ALA   B O   
5750 C CB  . ALA   B 124 ? 0.1475 0.1325 0.1698 -0.0024 0.0102  -0.0080 124 ALA   B CB  
5756 N N   . PRO   B 125 ? 0.1490 0.1339 0.1446 -0.0191 -0.0217 0.0114  125 PRO   B N   
5757 C CA  . PRO   B 125 ? 0.1589 0.1336 0.1622 -0.0212 -0.0174 0.0293  125 PRO   B CA  
5758 C C   . PRO   B 125 ? 0.1426 0.1325 0.2014 -0.0197 -0.0044 0.0154  125 PRO   B C   
5759 O O   . PRO   B 125 ? 0.1444 0.1292 0.2108 -0.0103 -0.0012 0.0119  125 PRO   B O   
5760 C CB  . PRO   B 125 ? 0.1618 0.1516 0.1767 -0.0248 -0.0250 0.0304  125 PRO   B CB  
5761 C CG  . PRO   B 125 ? 0.1709 0.1576 0.1748 -0.0361 -0.0237 0.0260  125 PRO   B CG  
5762 C CD  . PRO   B 125 ? 0.1612 0.1428 0.1485 -0.0350 -0.0226 0.0043  125 PRO   B CD  
5770 N N   . LEU   B 126 ? 0.1444 0.1342 0.2223 -0.0179 0.0090  0.0183  126 LEU   B N   
5771 C CA  . LEU   B 126 ? 0.1604 0.1367 0.2049 -0.0139 0.0183  0.0228  126 LEU   B CA  
5772 C C   . LEU   B 126 ? 0.1538 0.1543 0.1879 0.0031  0.0181  0.0246  126 LEU   B C   
5773 O O   . LEU   B 126 ? 0.1822 0.1821 0.2317 0.0234  0.0025  -0.0165 126 LEU   B O   
5774 C CB  . LEU   B 126 ? 0.1909 0.1407 0.2394 -0.0198 0.0163  0.0109  126 LEU   B CB  
5775 C CG  . LEU   B 126 ? 0.1997 0.1508 0.2533 -0.0234 0.0188  -0.0149 126 LEU   B CG  
5776 C CD1 . LEU   B 126 ? 0.2132 0.1569 0.3090 -0.0181 0.0211  -0.0173 126 LEU   B CD1 
5777 C CD2 . LEU   B 126 ? 0.1951 0.1715 0.2485 -0.0355 0.0060  -0.0184 126 LEU   B CD2 
5789 N N   . LEU   B 127 ? 0.1564 0.1394 0.1984 0.0063  0.0255  0.0096  127 LEU   B N   
5790 C CA  . LEU   B 127 ? 0.1544 0.1455 0.2100 -0.0069 0.0314  0.0162  127 LEU   B CA  
5791 C C   . LEU   B 127 ? 0.1466 0.1403 0.2352 -0.0015 0.0193  0.0162  127 LEU   B C   
5792 O O   . LEU   B 127 ? 0.1517 0.1481 0.2356 -0.0193 0.0070  0.0135  127 LEU   B O   
5793 C CB  . LEU   B 127 ? 0.1706 0.1474 0.2220 -0.0055 0.0259  0.0147  127 LEU   B CB  
5794 C CG  . LEU   B 127 ? 0.1906 0.1408 0.2387 0.0001  0.0362  0.0093  127 LEU   B CG  
5795 C CD1 . LEU   B 127 ? 0.1993 0.1402 0.2499 0.0086  0.0338  -0.0002 127 LEU   B CD1 
5796 C CD2 . LEU   B 127 ? 0.1919 0.1448 0.2577 -0.0209 0.0301  0.0202  127 LEU   B CD2 
5808 N N   . SER   B 128 ? 0.1606 0.1367 0.2291 0.0044  -0.0003 0.0109  128 SER   B N   
5809 C CA  . SER   B 128 ? 0.1762 0.1493 0.2262 0.0072  -0.0172 0.0207  128 SER   B CA  
5810 C C   . SER   B 128 ? 0.1853 0.1466 0.2675 0.0055  -0.0293 0.0235  128 SER   B C   
5811 O O   . SER   B 128 ? 0.2049 0.1539 0.3130 0.0034  -0.0229 0.0326  128 SER   B O   
5812 C CB  . SER   B 128 ? 0.1833 0.1479 0.2267 -0.0084 0.0012  0.0335  128 SER   B CB  
5813 O OG  . SER   B 128 ? 0.1747 0.1637 0.2246 -0.0018 0.0105  0.0324  128 SER   B OG  
5819 N N   . ALA   B 129 ? 0.1940 0.1526 0.2970 0.0247  -0.0082 0.0042  129 ALA   B N   
5820 C CA  . ALA   B 129 ? 0.2062 0.1667 0.3135 0.0301  -0.0096 -0.0130 129 ALA   B CA  
5821 C C   . ALA   B 129 ? 0.1939 0.1538 0.2892 0.0201  0.0062  -0.0045 129 ALA   B C   
5822 O O   . ALA   B 129 ? 0.1911 0.1545 0.2713 0.0180  0.0073  -0.0067 129 ALA   B O   
5823 C CB  . ALA   B 129 ? 0.2314 0.1921 0.3462 0.0328  0.0138  -0.0250 129 ALA   B CB  
5829 N N   . GLY   B 130 ? 0.1938 0.1547 0.2879 0.0269  0.0107  -0.0166 130 GLY   B N   
5830 C CA  . GLY   B 130 ? 0.1972 0.1647 0.2972 0.0232  0.0324  -0.0062 130 GLY   B CA  
5831 C C   . GLY   B 130 ? 0.1986 0.1657 0.2840 0.0183  0.0192  0.0096  130 GLY   B C   
5832 O O   . GLY   B 130 ? 0.2021 0.1859 0.2917 0.0165  0.0044  0.0097  130 GLY   B O   
5836 N N   . ILE   B 131 ? 0.1928 0.1802 0.2897 0.0292  0.0205  0.0115  131 ILE   B N   
5837 C CA  . ILE   B 131 ? 0.2270 0.1993 0.2988 0.0200  0.0103  0.0242  131 ILE   B CA  
5838 C C   . ILE   B 131 ? 0.2310 0.1873 0.2613 0.0114  0.0083  0.0291  131 ILE   B C   
5839 O O   . ILE   B 131 ? 0.2607 0.2068 0.2734 0.0089  -0.0073 0.0355  131 ILE   B O   
5840 C CB  . ILE   B 131 ? 0.2278 0.2212 0.3269 0.0130  0.0045  0.0335  131 ILE   B CB  
5841 C CG1 . ILE   B 131 ? 0.2321 0.2375 0.3364 -0.0185 0.0054  0.0339  131 ILE   B CG1 
5842 C CG2 . ILE   B 131 ? 0.2271 0.2385 0.3564 0.0243  0.0032  0.0267  131 ILE   B CG2 
5843 C CD1 . ILE   B 131 ? 0.2449 0.2545 0.3552 -0.0356 -0.0066 0.0293  131 ILE   B CD1 
5855 N N   . PHE   B 132 ? 0.2174 0.1743 0.2452 0.0105  0.0299  0.0228  132 PHE   B N   
5856 C CA  . PHE   B 132 ? 0.2306 0.1769 0.2546 0.0090  0.0512  0.0157  132 PHE   B CA  
5857 C C   . PHE   B 132 ? 0.2445 0.1958 0.2897 0.0118  0.0684  0.0111  132 PHE   B C   
5858 O O   . PHE   B 132 ? 0.2644 0.2203 0.3241 0.0111  0.0790  0.0131  132 PHE   B O   
5859 C CB  . PHE   B 132 ? 0.2138 0.1753 0.2350 0.0072  0.0556  0.0187  132 PHE   B CB  
5860 C CG  . PHE   B 132 ? 0.1987 0.1826 0.2126 0.0133  0.0293  0.0106  132 PHE   B CG  
5861 C CD1 . PHE   B 132 ? 0.2122 0.1829 0.2602 0.0116  0.0316  0.0246  132 PHE   B CD1 
5862 C CD2 . PHE   B 132 ? 0.2054 0.1839 0.1835 0.0193  0.0138  0.0205  132 PHE   B CD2 
5863 C CE1 . PHE   B 132 ? 0.2255 0.1917 0.2654 0.0027  0.0193  0.0260  132 PHE   B CE1 
5864 C CE2 . PHE   B 132 ? 0.2182 0.1913 0.1967 0.0223  0.0061  0.0249  132 PHE   B CE2 
5865 C CZ  . PHE   B 132 ? 0.2235 0.1904 0.2327 0.0135  0.0012  0.0346  132 PHE   B CZ  
5875 N N   . GLY   B 133 ? 0.2315 0.1861 0.2900 0.0054  0.0514  0.0359  133 GLY   B N   
5876 C CA  . GLY   B 133 ? 0.2475 0.1984 0.2980 -0.0237 0.0502  0.0470  133 GLY   B CA  
5877 C C   . GLY   B 133 ? 0.2578 0.2083 0.3112 -0.0376 0.0562  0.0534  133 GLY   B C   
5878 O O   . GLY   B 133 ? 0.2804 0.2228 0.3460 -0.0561 0.0554  0.0578  133 GLY   B O   
5882 N N   . ALA   B 134 ? 0.2401 0.1985 0.2960 -0.0305 0.0513  0.0303  134 ALA   B N   
5883 C CA  . ALA   B 134 ? 0.2370 0.1944 0.3028 -0.0171 0.0571  0.0158  134 ALA   B CA  
5884 C C   . ALA   B 134 ? 0.2496 0.1799 0.2949 -0.0141 0.0480  0.0341  134 ALA   B C   
5885 O O   . ALA   B 134 ? 0.2472 0.1980 0.2977 -0.0007 0.0378  0.0305  134 ALA   B O   
5886 C CB  . ALA   B 134 ? 0.2216 0.1925 0.3148 -0.0123 0.0482  -0.0044 134 ALA   B CB  
5892 N N   A ASP   B 135 ? 0.2642 0.1732 0.3092 -0.0114 0.0332  0.0348  135 ASP   B N   
5893 N N   B ASP   B 135 ? 0.2578 0.1763 0.2963 -0.0094 0.0334  0.0337  135 ASP   B N   
5894 C CA  A ASP   B 135 ? 0.2800 0.1710 0.3279 -0.0140 0.0254  0.0357  135 ASP   B CA  
5895 C CA  B ASP   B 135 ? 0.2677 0.1748 0.3050 -0.0079 0.0223  0.0328  135 ASP   B CA  
5896 C C   A ASP   B 135 ? 0.2583 0.1586 0.3058 -0.0080 0.0179  0.0317  135 ASP   B C   
5897 C C   B ASP   B 135 ? 0.2549 0.1654 0.2952 -0.0003 0.0119  0.0293  135 ASP   B C   
5898 O O   A ASP   B 135 ? 0.2492 0.1449 0.3144 -0.0170 0.0186  0.0326  135 ASP   B O   
5899 O O   B ASP   B 135 ? 0.2510 0.1597 0.2937 -0.0045 0.0108  0.0294  135 ASP   B O   
5900 C CB  A ASP   B 135 ? 0.3125 0.1798 0.3585 -0.0384 0.0215  0.0377  135 ASP   B CB  
5901 C CB  B ASP   B 135 ? 0.2881 0.1820 0.3212 -0.0224 0.0200  0.0337  135 ASP   B CB  
5902 C CG  A ASP   B 135 ? 0.3369 0.1815 0.3991 -0.0628 0.0164  0.0339  135 ASP   B CG  
5903 C CG  B ASP   B 135 ? 0.3030 0.1843 0.3453 -0.0370 0.0171  0.0310  135 ASP   B CG  
5904 O OD1 A ASP   B 135 ? 0.3479 0.1643 0.4015 -0.0489 0.0039  0.0261  135 ASP   B OD1 
5905 O OD1 B ASP   B 135 ? 0.3077 0.1791 0.3535 -0.0273 0.0078  0.0226  135 ASP   B OD1 
5906 O OD2 A ASP   B 135 ? 0.3560 0.2211 0.4436 -0.0694 0.0147  0.0273  135 ASP   B OD2 
5907 O OD2 B ASP   B 135 ? 0.3151 0.1934 0.3611 -0.0454 0.0190  0.0370  135 ASP   B OD2 
5916 N N   . PRO   B 136 ? 0.2450 0.1642 0.3102 0.0162  -0.0065 0.0251  136 PRO   B N   
5917 C CA  . PRO   B 136 ? 0.2134 0.1584 0.3206 0.0202  -0.0107 0.0106  136 PRO   B CA  
5918 C C   . PRO   B 136 ? 0.1871 0.1409 0.3332 0.0205  -0.0094 -0.0012 136 PRO   B C   
5919 O O   . PRO   B 136 ? 0.1671 0.1421 0.3274 0.0081  -0.0059 0.0069  136 PRO   B O   
5920 C CB  . PRO   B 136 ? 0.2143 0.1757 0.3230 0.0326  -0.0073 0.0061  136 PRO   B CB  
5921 C CG  . PRO   B 136 ? 0.2431 0.1849 0.3444 0.0283  0.0073  0.0037  136 PRO   B CG  
5922 C CD  . PRO   B 136 ? 0.2522 0.1750 0.3247 0.0334  0.0068  0.0123  136 PRO   B CD  
5930 N N   . ILE   B 137 ? 0.1943 0.1368 0.3508 0.0129  -0.0164 -0.0116 137 ILE   B N   
5931 C CA  . ILE   B 137 ? 0.2069 0.1341 0.3578 -0.0058 -0.0105 -0.0052 137 ILE   B CA  
5932 C C   . ILE   B 137 ? 0.1955 0.1335 0.3360 -0.0085 0.0170  0.0021  137 ILE   B C   
5933 O O   . ILE   B 137 ? 0.1934 0.1451 0.3049 -0.0110 0.0093  0.0012  137 ILE   B O   
5934 C CB  . ILE   B 137 ? 0.2447 0.1398 0.4016 -0.0081 -0.0129 -0.0061 137 ILE   B CB  
5935 C CG1 . ILE   B 137 ? 0.2605 0.1556 0.4330 -0.0040 -0.0203 -0.0152 137 ILE   B CG1 
5936 C CG2 . ILE   B 137 ? 0.2552 0.1377 0.4209 -0.0338 -0.0089 -0.0011 137 ILE   B CG2 
5937 C CD1 . ILE   B 137 ? 0.2875 0.1852 0.4709 0.0068  -0.0283 -0.0117 137 ILE   B CD1 
5949 N N   . HIS   B 138 ? 0.2042 0.1327 0.3415 -0.0067 0.0209  0.0100  138 HIS   B N   
5950 C CA  . HIS   B 138 ? 0.2136 0.1462 0.3410 -0.0042 0.0378  0.0144  138 HIS   B CA  
5951 C C   . HIS   B 138 ? 0.1952 0.1393 0.3247 -0.0081 0.0270  0.0326  138 HIS   B C   
5952 O O   . HIS   B 138 ? 0.1859 0.1520 0.3513 0.0019  0.0304  0.0319  138 HIS   B O   
5953 C CB  . HIS   B 138 ? 0.2442 0.1654 0.3543 -0.0144 0.0658  0.0022  138 HIS   B CB  
5954 C CG  . HIS   B 138 ? 0.2732 0.1818 0.3637 -0.0156 0.0999  0.0243  138 HIS   B CG  
5955 N ND1 . HIS   B 138 ? 0.2913 0.2024 0.4009 -0.0118 0.1069  0.0275  138 HIS   B ND1 
5956 C CD2 . HIS   B 138 ? 0.2911 0.1862 0.3467 -0.0096 0.1147  0.0242  138 HIS   B CD2 
5957 C CE1 . HIS   B 138 ? 0.3010 0.2039 0.3923 -0.0040 0.1106  0.0288  138 HIS   B CE1 
5958 N NE2 . HIS   B 138 ? 0.3061 0.1879 0.3573 0.0041  0.1143  0.0208  138 HIS   B NE2 
5966 N N   . SER   B 139 ? 0.1904 0.1329 0.3103 -0.0072 0.0151  0.0170  139 SER   B N   
5967 C CA  . SER   B 139 ? 0.1869 0.1293 0.2798 -0.0040 0.0152  0.0023  139 SER   B CA  
5968 C C   . SER   B 139 ? 0.1563 0.1273 0.2663 0.0031  0.0088  -0.0058 139 SER   B C   
5969 O O   . SER   B 139 ? 0.1573 0.1349 0.2736 0.0012  0.0103  0.0045  139 SER   B O   
5970 C CB  . SER   B 139 ? 0.1934 0.1337 0.2829 -0.0038 0.0008  0.0040  139 SER   B CB  
5971 O OG  . SER   B 139 ? 0.1861 0.1350 0.2747 -0.0065 -0.0234 0.0186  139 SER   B OG  
5977 N N   . LEU   B 140 ? 0.1593 0.1184 0.2599 -0.0050 0.0229  -0.0042 140 LEU   B N   
5978 C CA  . LEU   B 140 ? 0.1597 0.1234 0.2665 -0.0030 0.0153  -0.0012 140 LEU   B CA  
5979 C C   . LEU   B 140 ? 0.1528 0.1210 0.2725 -0.0067 0.0002  -0.0163 140 LEU   B C   
5980 O O   . LEU   B 140 ? 0.1484 0.1426 0.2608 -0.0051 0.0039  -0.0003 140 LEU   B O   
5981 C CB  . LEU   B 140 ? 0.1635 0.1249 0.2741 -0.0093 0.0177  0.0003  140 LEU   B CB  
5982 C CG  . LEU   B 140 ? 0.1679 0.1328 0.2803 -0.0144 0.0035  0.0012  140 LEU   B CG  
5983 C CD1 . LEU   B 140 ? 0.1810 0.1400 0.2964 -0.0203 0.0291  0.0062  140 LEU   B CD1 
5984 C CD2 . LEU   B 140 ? 0.1828 0.1551 0.2840 -0.0048 -0.0011 -0.0071 140 LEU   B CD2 
5996 N N   . ARG   B 141 ? 0.1469 0.1248 0.2944 -0.0024 0.0147  -0.0008 141 ARG   B N   
5997 C CA  . ARG   B 141 ? 0.1493 0.1297 0.3158 -0.0114 0.0253  0.0005  141 ARG   B CA  
5998 C C   . ARG   B 141 ? 0.1438 0.1249 0.3093 -0.0145 0.0114  0.0012  141 ARG   B C   
5999 O O   . ARG   B 141 ? 0.1522 0.1378 0.3082 -0.0175 0.0007  -0.0108 141 ARG   B O   
6000 C CB  . ARG   B 141 ? 0.1626 0.1501 0.3332 -0.0172 0.0280  -0.0014 141 ARG   B CB  
6001 C CG  . ARG   B 141 ? 0.1973 0.1697 0.3452 -0.0215 0.0293  -0.0008 141 ARG   B CG  
6002 C CD  . ARG   B 141 ? 0.2352 0.1884 0.3387 -0.0155 0.0075  -0.0193 141 ARG   B CD  
6003 N NE  . ARG   B 141 ? 0.2469 0.1870 0.3208 -0.0286 0.0052  -0.0276 141 ARG   B NE  
6004 C CZ  . ARG   B 141 ? 0.2715 0.1873 0.2951 -0.0224 0.0076  -0.0414 141 ARG   B CZ  
6005 N NH1 . ARG   B 141 ? 0.2859 0.1687 0.2688 -0.0131 0.0047  -0.0400 141 ARG   B NH1 
6006 N NH2 . ARG   B 141 ? 0.2830 0.2007 0.3238 -0.0088 -0.0067 -0.0348 141 ARG   B NH2 
6020 N N   . VAL   B 142 ? 0.1544 0.1254 0.3092 -0.0096 0.0182  -0.0117 142 VAL   B N   
6021 C CA  . VAL   B 142 ? 0.1491 0.1198 0.2900 -0.0051 0.0291  -0.0073 142 VAL   B CA  
6022 C C   . VAL   B 142 ? 0.1390 0.1287 0.2861 -0.0070 0.0152  -0.0122 142 VAL   B C   
6023 O O   . VAL   B 142 ? 0.1493 0.1297 0.3015 0.0037  0.0180  0.0013  142 VAL   B O   
6024 C CB  . VAL   B 142 ? 0.1585 0.1474 0.2967 -0.0034 0.0257  0.0058  142 VAL   B CB  
6025 C CG1 . VAL   B 142 ? 0.1533 0.1424 0.2964 0.0046  0.0190  -0.0009 142 VAL   B CG1 
6026 C CG2 . VAL   B 142 ? 0.1876 0.1517 0.3007 -0.0046 0.0191  0.0125  142 VAL   B CG2 
6036 N N   . CYS   B 143 ? 0.1341 0.1360 0.2554 -0.0050 0.0138  -0.0052 143 CYS   B N   
6037 C CA  . CYS   B 143 ? 0.1297 0.1368 0.2557 -0.0058 0.0136  -0.0012 143 CYS   B CA  
6038 C C   . CYS   B 143 ? 0.1327 0.1365 0.2575 -0.0102 0.0131  -0.0098 143 CYS   B C   
6039 O O   . CYS   B 143 ? 0.1409 0.1383 0.2639 -0.0078 -0.0057 -0.0082 143 CYS   B O   
6040 C CB  . CYS   B 143 ? 0.1432 0.1429 0.2588 -0.0021 0.0052  -0.0037 143 CYS   B CB  
6041 S SG  . CYS   B 143 ? 0.1502 0.1509 0.2554 -0.0041 0.0039  -0.0005 143 CYS   B SG  
6047 N N   . VAL   B 144 ? 0.1390 0.1407 0.2805 -0.0085 -0.0027 -0.0192 144 VAL   B N   
6048 C CA  . VAL   B 144 ? 0.1450 0.1444 0.3071 -0.0175 -0.0026 -0.0169 144 VAL   B CA  
6049 C C   . VAL   B 144 ? 0.1385 0.1454 0.3231 -0.0098 -0.0082 0.0028  144 VAL   B C   
6050 O O   . VAL   B 144 ? 0.1507 0.1619 0.3361 -0.0001 -0.0137 0.0206  144 VAL   B O   
6051 C CB  . VAL   B 144 ? 0.1760 0.1635 0.3746 -0.0146 -0.0099 -0.0406 144 VAL   B CB  
6052 C CG1 . VAL   B 144 ? 0.2050 0.2069 0.4146 -0.0106 -0.0102 -0.0350 144 VAL   B CG1 
6053 C CG2 . VAL   B 144 ? 0.1878 0.1606 0.3787 -0.0045 -0.0205 -0.0568 144 VAL   B CG2 
6063 N N   . ASP   B 145 ? 0.1464 0.1296 0.3292 -0.0092 0.0012  -0.0232 145 ASP   B N   
6064 C CA  . ASP   B 145 ? 0.1496 0.1367 0.3489 -0.0117 0.0162  -0.0231 145 ASP   B CA  
6065 C C   . ASP   B 145 ? 0.1498 0.1417 0.3326 -0.0148 0.0133  -0.0220 145 ASP   B C   
6066 O O   . ASP   B 145 ? 0.1474 0.1614 0.3739 -0.0114 0.0164  -0.0182 145 ASP   B O   
6067 C CB  . ASP   B 145 ? 0.1607 0.1465 0.3952 -0.0125 0.0205  -0.0184 145 ASP   B CB  
6068 C CG  . ASP   B 145 ? 0.1755 0.1600 0.4275 -0.0141 0.0343  -0.0174 145 ASP   B CG  
6069 O OD1 . ASP   B 145 ? 0.1769 0.1588 0.4186 -0.0301 -0.0012 -0.0298 145 ASP   B OD1 
6070 O OD2 . ASP   B 145 ? 0.2040 0.1754 0.4694 -0.0262 0.0670  -0.0075 145 ASP   B OD2 
6075 N N   . THR   B 146 ? 0.1439 0.1245 0.3055 -0.0154 0.0112  -0.0071 146 THR   B N   
6076 C CA  . THR   B 146 ? 0.1472 0.1321 0.2844 -0.0105 0.0129  -0.0039 146 THR   B CA  
6077 C C   . THR   B 146 ? 0.1449 0.1343 0.2579 -0.0020 0.0052  -0.0089 146 THR   B C   
6078 O O   . THR   B 146 ? 0.1430 0.1354 0.2665 -0.0076 -0.0036 -0.0017 146 THR   B O   
6079 C CB  . THR   B 146 ? 0.1467 0.1352 0.2777 -0.0101 0.0213  -0.0051 146 THR   B CB  
6080 O OG1 . THR   B 146 ? 0.1442 0.1387 0.2878 -0.0080 0.0252  0.0119  146 THR   B OG1 
6081 C CG2 . THR   B 146 ? 0.1545 0.1342 0.2658 -0.0057 0.0241  -0.0026 146 THR   B CG2 
6089 N N   . VAL   B 147 ? 0.1484 0.1311 0.2480 0.0033  0.0135  0.0067  147 VAL   B N   
6090 C CA  . VAL   B 147 ? 0.1468 0.1270 0.2405 -0.0089 -0.0039 0.0045  147 VAL   B CA  
6091 C C   . VAL   B 147 ? 0.1458 0.1362 0.2569 -0.0192 -0.0059 0.0005  147 VAL   B C   
6092 O O   . VAL   B 147 ? 0.1540 0.1444 0.2601 -0.0226 -0.0313 -0.0073 147 VAL   B O   
6093 C CB  . VAL   B 147 ? 0.1483 0.1399 0.2336 -0.0103 -0.0143 -0.0069 147 VAL   B CB  
6094 C CG1 . VAL   B 147 ? 0.1577 0.1516 0.2249 -0.0144 -0.0140 -0.0068 147 VAL   B CG1 
6095 C CG2 . VAL   B 147 ? 0.1495 0.1337 0.2454 -0.0060 -0.0055 -0.0099 147 VAL   B CG2 
6105 N N   . ARG   B 148 ? 0.1370 0.1337 0.2407 -0.0134 -0.0200 0.0021  148 ARG   B N   
6106 C CA  . ARG   B 148 ? 0.1520 0.1410 0.2270 -0.0084 -0.0241 -0.0141 148 ARG   B CA  
6107 C C   . ARG   B 148 ? 0.1545 0.1511 0.2162 -0.0100 -0.0386 -0.0068 148 ARG   B C   
6108 O O   . ARG   B 148 ? 0.1695 0.1859 0.2226 -0.0302 -0.0503 0.0050  148 ARG   B O   
6109 C CB  . ARG   B 148 ? 0.1546 0.1531 0.2214 -0.0017 -0.0269 -0.0149 148 ARG   B CB  
6110 C CG  . ARG   B 148 ? 0.1562 0.1687 0.2343 -0.0055 -0.0316 -0.0397 148 ARG   B CG  
6111 C CD  . ARG   B 148 ? 0.1647 0.1837 0.2544 0.0044  -0.0323 -0.0388 148 ARG   B CD  
6112 N NE  . ARG   B 148 ? 0.1765 0.1804 0.2563 0.0208  -0.0383 -0.0357 148 ARG   B NE  
6113 C CZ  . ARG   B 148 ? 0.1681 0.1754 0.2322 0.0201  -0.0310 -0.0289 148 ARG   B CZ  
6114 N NH1 . ARG   B 148 ? 0.1537 0.1811 0.2423 0.0124  -0.0142 -0.0286 148 ARG   B NH1 
6115 N NH2 . ARG   B 148 ? 0.1884 0.1549 0.2400 0.0233  -0.0176 -0.0258 148 ARG   B NH2 
6129 N N   . THR   B 149 ? 0.1576 0.1479 0.2205 -0.0144 -0.0268 -0.0002 149 THR   B N   
6130 C CA  . THR   B 149 ? 0.1625 0.1538 0.2115 -0.0154 -0.0302 0.0081  149 THR   B CA  
6131 C C   . THR   B 149 ? 0.1663 0.1527 0.1975 -0.0169 -0.0264 0.0059  149 THR   B C   
6132 O O   . THR   B 149 ? 0.1694 0.1508 0.2153 -0.0214 -0.0185 -0.0021 149 THR   B O   
6133 C CB  . THR   B 149 ? 0.1707 0.1509 0.2169 -0.0157 -0.0378 -0.0059 149 THR   B CB  
6134 O OG1 . THR   B 149 ? 0.1684 0.1531 0.2084 -0.0268 -0.0432 0.0002  149 THR   B OG1 
6135 C CG2 . THR   B 149 ? 0.1871 0.1618 0.2294 -0.0050 -0.0291 0.0118  149 THR   B CG2 
6143 N N   . ASN   B 150 ? 0.1718 0.1530 0.1965 -0.0186 -0.0369 0.0082  150 ASN   B N   
6144 C CA  . ASN   B 150 ? 0.1819 0.1650 0.1823 -0.0280 -0.0351 -0.0037 150 ASN   B CA  
6145 C C   . ASN   B 150 ? 0.1691 0.1581 0.1837 -0.0223 -0.0284 -0.0047 150 ASN   B C   
6146 O O   . ASN   B 150 ? 0.1743 0.1602 0.2077 -0.0309 -0.0496 -0.0008 150 ASN   B O   
6147 C CB  . ASN   B 150 ? 0.2139 0.2047 0.1947 -0.0315 -0.0484 0.0121  150 ASN   B CB  
6148 C CG  . ASN   B 150 ? 0.2421 0.2439 0.2521 -0.0377 -0.0525 0.0266  150 ASN   B CG  
6149 O OD1 . ASN   B 150 ? 0.2453 0.2686 0.2687 -0.0447 -0.0636 0.0262  150 ASN   B OD1 
6150 N ND2 . ASN   B 150 ? 0.2560 0.2661 0.2996 -0.0277 -0.0683 0.0739  150 ASN   B ND2 
6157 N N   . VAL   B 151 ? 0.1590 0.1582 0.1831 -0.0257 -0.0357 -0.0078 151 VAL   B N   
6158 C CA  . VAL   B 151 ? 0.1620 0.1628 0.1781 -0.0326 -0.0313 -0.0053 151 VAL   B CA  
6159 C C   . VAL   B 151 ? 0.1691 0.1529 0.1720 -0.0363 -0.0413 -0.0131 151 VAL   B C   
6160 O O   . VAL   B 151 ? 0.1837 0.1583 0.1988 -0.0265 -0.0260 -0.0211 151 VAL   B O   
6161 C CB  . VAL   B 151 ? 0.1874 0.1667 0.1963 -0.0172 -0.0246 -0.0020 151 VAL   B CB  
6162 C CG1 . VAL   B 151 ? 0.1869 0.1708 0.2521 -0.0407 -0.0077 0.0017  151 VAL   B CG1 
6163 C CG2 . VAL   B 151 ? 0.2025 0.1840 0.1767 -0.0086 -0.0234 0.0129  151 VAL   B CG2 
6173 N N   . TYR   B 152 ? 0.1625 0.1367 0.1788 -0.0255 -0.0261 -0.0135 152 TYR   B N   
6174 C CA  . TYR   B 152 ? 0.1608 0.1567 0.1655 -0.0296 -0.0184 -0.0050 152 TYR   B CA  
6175 C C   . TYR   B 152 ? 0.1636 0.1402 0.1574 -0.0226 -0.0187 -0.0079 152 TYR   B C   
6176 O O   . TYR   B 152 ? 0.1682 0.1425 0.1763 -0.0272 -0.0144 0.0010  152 TYR   B O   
6177 C CB  . TYR   B 152 ? 0.1900 0.1742 0.1616 -0.0448 -0.0142 -0.0007 152 TYR   B CB  
6178 C CG  . TYR   B 152 ? 0.2031 0.1884 0.1525 -0.0565 -0.0073 -0.0137 152 TYR   B CG  
6179 C CD1 . TYR   B 152 ? 0.2152 0.2008 0.1334 -0.0482 -0.0217 -0.0121 152 TYR   B CD1 
6180 C CD2 . TYR   B 152 ? 0.2228 0.2126 0.1579 -0.0567 -0.0140 -0.0171 152 TYR   B CD2 
6181 C CE1 . TYR   B 152 ? 0.2362 0.2230 0.1611 -0.0433 -0.0361 0.0201  152 TYR   B CE1 
6182 C CE2 . TYR   B 152 ? 0.2357 0.2338 0.1660 -0.0552 -0.0313 -0.0130 152 TYR   B CE2 
6183 C CZ  . TYR   B 152 ? 0.2409 0.2438 0.1506 -0.0455 -0.0552 0.0157  152 TYR   B CZ  
6184 O OH  . TYR   B 152 ? 0.2664 0.2784 0.2054 -0.0300 -0.0547 0.0156  152 TYR   B OH  
6194 N N   . LEU   B 153 ? 0.1713 0.1362 0.1640 -0.0286 -0.0114 -0.0054 153 LEU   B N   
6195 C CA  . LEU   B 153 ? 0.1719 0.1366 0.1486 -0.0311 0.0025  -0.0237 153 LEU   B CA  
6196 C C   . LEU   B 153 ? 0.1764 0.1398 0.1500 -0.0293 -0.0125 -0.0320 153 LEU   B C   
6197 O O   . LEU   B 153 ? 0.1733 0.1703 0.1743 -0.0280 -0.0060 -0.0406 153 LEU   B O   
6198 C CB  . LEU   B 153 ? 0.1696 0.1301 0.1775 -0.0264 -0.0006 -0.0058 153 LEU   B CB  
6199 C CG  . LEU   B 153 ? 0.1581 0.1392 0.2142 -0.0243 0.0083  -0.0074 153 LEU   B CG  
6200 C CD1 . LEU   B 153 ? 0.1745 0.1522 0.2194 -0.0244 0.0188  0.0012  153 LEU   B CD1 
6201 C CD2 . LEU   B 153 ? 0.1655 0.1548 0.2042 -0.0171 0.0198  0.0120  153 LEU   B CD2 
6213 N N   . ALA   B 154 ? 0.1615 0.1402 0.1747 -0.0070 -0.0106 -0.0207 154 ALA   B N   
6214 C CA  . ALA   B 154 ? 0.1756 0.1436 0.2132 -0.0096 -0.0139 -0.0308 154 ALA   B CA  
6215 C C   . ALA   B 154 ? 0.1894 0.1553 0.2299 0.0011  -0.0252 -0.0390 154 ALA   B C   
6216 O O   . ALA   B 154 ? 0.2390 0.1567 0.2594 0.0087  -0.0167 -0.0194 154 ALA   B O   
6217 C CB  . ALA   B 154 ? 0.1799 0.1625 0.2526 -0.0080 0.0034  -0.0423 154 ALA   B CB  
6223 N N   . VAL   B 155 ? 0.1462 0.1484 0.2456 -0.0092 0.0078  -0.0304 155 VAL   B N   
6224 C CA  . VAL   B 155 ? 0.1540 0.1474 0.2689 -0.0118 -0.0003 -0.0209 155 VAL   B CA  
6225 C C   . VAL   B 155 ? 0.1481 0.1431 0.2607 -0.0028 -0.0066 -0.0377 155 VAL   B C   
6226 O O   . VAL   B 155 ? 0.1710 0.1608 0.3029 0.0106  -0.0069 -0.0558 155 VAL   B O   
6227 C CB  . VAL   B 155 ? 0.1604 0.1553 0.3121 -0.0092 -0.0094 -0.0041 155 VAL   B CB  
6228 C CG1 . VAL   B 155 ? 0.1664 0.1550 0.3109 -0.0147 -0.0202 -0.0065 155 VAL   B CG1 
6229 C CG2 . VAL   B 155 ? 0.1595 0.1666 0.3356 -0.0064 -0.0126 0.0251  155 VAL   B CG2 
6239 N N   . PHE   B 156 ? 0.1363 0.1562 0.2816 0.0023  0.0042  -0.0268 156 PHE   B N   
6240 C CA  . PHE   B 156 ? 0.1370 0.1581 0.3105 0.0074  0.0011  -0.0384 156 PHE   B CA  
6241 C C   . PHE   B 156 ? 0.1404 0.1686 0.3464 0.0134  -0.0054 -0.0548 156 PHE   B C   
6242 O O   . PHE   B 156 ? 0.1741 0.1923 0.3644 0.0262  0.0033  -0.0661 156 PHE   B O   
6243 C CB  . PHE   B 156 ? 0.1501 0.1508 0.3049 -0.0024 -0.0051 -0.0292 156 PHE   B CB  
6244 C CG  . PHE   B 156 ? 0.1515 0.1707 0.3077 -0.0027 -0.0065 -0.0126 156 PHE   B CG  
6245 C CD1 . PHE   B 156 ? 0.1562 0.1993 0.3451 0.0091  0.0038  0.0288  156 PHE   B CD1 
6246 C CD2 . PHE   B 156 ? 0.1591 0.1811 0.2953 0.0096  -0.0219 -0.0097 156 PHE   B CD2 
6247 C CE1 . PHE   B 156 ? 0.1593 0.2130 0.3492 0.0086  -0.0002 0.0337  156 PHE   B CE1 
6248 C CE2 . PHE   B 156 ? 0.1725 0.2018 0.3178 0.0177  -0.0225 0.0026  156 PHE   B CE2 
6249 C CZ  . PHE   B 156 ? 0.1656 0.2098 0.3430 0.0165  -0.0183 0.0092  156 PHE   B CZ  
6259 N N   . ASP   B 157 ? 0.1527 0.1572 0.3688 0.0156  -0.0245 -0.0419 157 ASP   B N   
6260 C CA  . ASP   B 157 ? 0.1803 0.1658 0.3928 0.0135  -0.0241 -0.0466 157 ASP   B CA  
6261 C C   . ASP   B 157 ? 0.1746 0.1694 0.3893 0.0077  -0.0204 -0.0679 157 ASP   B C   
6262 O O   . ASP   B 157 ? 0.1542 0.1598 0.3960 0.0095  -0.0194 -0.0448 157 ASP   B O   
6263 C CB  . ASP   B 157 ? 0.2131 0.1817 0.4019 0.0100  -0.0423 -0.0297 157 ASP   B CB  
6264 C CG  . ASP   B 157 ? 0.2582 0.2060 0.4197 0.0056  -0.0419 -0.0323 157 ASP   B CG  
6265 O OD1 . ASP   B 157 ? 0.2623 0.2039 0.4291 0.0145  -0.0336 -0.0247 157 ASP   B OD1 
6266 O OD2 . ASP   B 157 ? 0.2927 0.2308 0.4498 0.0057  -0.0316 -0.0321 157 ASP   B OD2 
6271 N N   A LYS   B 158 ? 0.1743 0.1902 0.4022 0.0048  -0.0039 -0.0945 158 LYS   B N   
6272 N N   B LYS   B 158 ? 0.1885 0.1940 0.3710 0.0083  -0.0097 -0.0739 158 LYS   B N   
6273 C CA  A LYS   B 158 ? 0.1829 0.2122 0.4131 0.0057  0.0058  -0.1128 158 LYS   B CA  
6274 C CA  B LYS   B 158 ? 0.2087 0.2172 0.3594 0.0118  -0.0037 -0.0776 158 LYS   B CA  
6275 C C   A LYS   B 158 ? 0.1812 0.1985 0.4404 0.0095  -0.0100 -0.1006 158 LYS   B C   
6276 C C   B LYS   B 158 ? 0.2098 0.2157 0.3563 0.0160  -0.0114 -0.0695 158 LYS   B C   
6277 O O   A LYS   B 158 ? 0.1728 0.1866 0.4581 -0.0013 -0.0129 -0.1201 158 LYS   B O   
6278 O O   B LYS   B 158 ? 0.2098 0.2173 0.3541 0.0129  -0.0116 -0.0716 158 LYS   B O   
6279 C CB  A LYS   B 158 ? 0.2086 0.2638 0.4119 0.0000  0.0170  -0.1254 158 LYS   B CB  
6280 C CB  B LYS   B 158 ? 0.2331 0.2442 0.3631 0.0103  0.0023  -0.0854 158 LYS   B CB  
6281 C CG  A LYS   B 158 ? 0.2449 0.3115 0.4138 0.0012  0.0192  -0.1356 158 LYS   B CG  
6282 C CG  B LYS   B 158 ? 0.2597 0.2671 0.3723 0.0104  0.0059  -0.0933 158 LYS   B CG  
6283 C CD  A LYS   B 158 ? 0.2654 0.3581 0.4229 0.0030  0.0242  -0.1293 158 LYS   B CD  
6284 C CD  B LYS   B 158 ? 0.2785 0.2942 0.3869 0.0093  0.0101  -0.0903 158 LYS   B CD  
6285 C CE  A LYS   B 158 ? 0.2875 0.3923 0.4370 0.0042  0.0225  -0.1209 158 LYS   B CE  
6286 C CE  B LYS   B 158 ? 0.2948 0.3127 0.4018 0.0102  0.0105  -0.0880 158 LYS   B CE  
6287 N NZ  A LYS   B 158 ? 0.2904 0.4119 0.4379 -0.0009 0.0208  -0.1191 158 LYS   B NZ  
6288 N NZ  B LYS   B 158 ? 0.2998 0.3206 0.4064 0.0074  0.0096  -0.0895 158 LYS   B NZ  
6315 N N   A ASN   B 159 ? 0.1838 0.1784 0.4622 0.0139  -0.0191 -0.0767 159 ASN   B N   
6316 N N   B ASN   B 159 ? 0.2080 0.2052 0.3687 0.0191  -0.0190 -0.0615 159 ASN   B N   
6317 C CA  A ASN   B 159 ? 0.1987 0.1772 0.4653 0.0189  -0.0459 -0.0670 159 ASN   B CA  
6318 C CA  B ASN   B 159 ? 0.2076 0.1988 0.3786 0.0228  -0.0340 -0.0603 159 ASN   B CA  
6319 C C   A ASN   B 159 ? 0.1851 0.1572 0.4508 0.0102  -0.0680 -0.0575 159 ASN   B C   
6320 C C   B ASN   B 159 ? 0.1930 0.1749 0.4018 0.0186  -0.0476 -0.0626 159 ASN   B C   
6321 O O   A ASN   B 159 ? 0.1832 0.1419 0.4669 -0.0034 -0.0731 -0.0397 159 ASN   B O   
6322 O O   B ASN   B 159 ? 0.1916 0.1664 0.4062 0.0218  -0.0411 -0.0620 159 ASN   B O   
6323 C CB  A ASN   B 159 ? 0.2165 0.1927 0.4809 0.0318  -0.0500 -0.0627 159 ASN   B CB  
6324 C CB  B ASN   B 159 ? 0.2149 0.2113 0.3713 0.0326  -0.0372 -0.0520 159 ASN   B CB  
6325 C CG  A ASN   B 159 ? 0.2447 0.2181 0.4919 0.0416  -0.0621 -0.0614 159 ASN   B CG  
6326 C CG  B ASN   B 159 ? 0.2267 0.2279 0.3696 0.0418  -0.0446 -0.0434 159 ASN   B CG  
6327 O OD1 A ASN   B 159 ? 0.2628 0.2237 0.5040 0.0544  -0.0544 -0.0672 159 ASN   B OD1 
6328 O OD1 B ASN   B 159 ? 0.2328 0.2333 0.3714 0.0509  -0.0463 -0.0373 159 ASN   B OD1 
6329 N ND2 A ASN   B 159 ? 0.2458 0.2323 0.4991 0.0424  -0.0709 -0.0537 159 ASN   B ND2 
6330 N ND2 B ASN   B 159 ? 0.2282 0.2376 0.3765 0.0445  -0.0465 -0.0388 159 ASN   B ND2 
6343 N N   . LEU   B 160 ? 0.1787 0.1658 0.4226 0.0093  -0.0528 -0.0609 160 LEU   B N   
6344 C CA  . LEU   B 160 ? 0.1743 0.1617 0.3911 0.0121  -0.0341 -0.0447 160 LEU   B CA  
6345 C C   . LEU   B 160 ? 0.1717 0.1510 0.3771 0.0037  -0.0207 -0.0503 160 LEU   B C   
6346 O O   . LEU   B 160 ? 0.1512 0.1485 0.3791 0.0027  -0.0254 -0.0272 160 LEU   B O   
6347 C CB  . LEU   B 160 ? 0.1710 0.1665 0.3674 0.0043  -0.0304 -0.0331 160 LEU   B CB  
6348 C CG  . LEU   B 160 ? 0.1715 0.1802 0.3353 0.0035  -0.0301 -0.0246 160 LEU   B CG  
6349 C CD1 . LEU   B 160 ? 0.1924 0.2025 0.3498 0.0003  -0.0121 -0.0223 160 LEU   B CD1 
6350 C CD2 . LEU   B 160 ? 0.1711 0.1875 0.3150 0.0209  -0.0277 -0.0172 160 LEU   B CD2 
6363 N N   A TYR   B 161 ? 0.1681 0.1512 0.3832 -0.0072 -0.0012 -0.0647 161 TYR   B N   
6364 N N   B TYR   B 161 ? 0.1766 0.1572 0.3629 -0.0013 -0.0065 -0.0577 161 TYR   B N   
6365 C CA  A TYR   B 161 ? 0.1726 0.1506 0.3697 -0.0229 0.0198  -0.0507 161 TYR   B CA  
6366 C CA  B TYR   B 161 ? 0.1853 0.1635 0.3433 -0.0080 0.0084  -0.0506 161 TYR   B CA  
6367 C C   A TYR   B 161 ? 0.1787 0.1510 0.3601 -0.0177 0.0235  -0.0398 161 TYR   B C   
6368 C C   B TYR   B 161 ? 0.1843 0.1606 0.3469 -0.0084 0.0126  -0.0487 161 TYR   B C   
6369 O O   A TYR   B 161 ? 0.1876 0.1541 0.3604 -0.0243 0.0237  -0.0384 161 TYR   B O   
6370 O O   B TYR   B 161 ? 0.1891 0.1642 0.3412 -0.0085 0.0133  -0.0500 161 TYR   B O   
6371 C CB  A TYR   B 161 ? 0.1872 0.1598 0.3647 -0.0393 0.0315  -0.0650 161 TYR   B CB  
6372 C CB  B TYR   B 161 ? 0.2033 0.1772 0.3247 -0.0123 0.0168  -0.0532 161 TYR   B CB  
6373 C CG  A TYR   B 161 ? 0.2117 0.1747 0.3411 -0.0447 0.0509  -0.0653 161 TYR   B CG  
6374 C CG  B TYR   B 161 ? 0.2252 0.1926 0.2998 -0.0172 0.0258  -0.0514 161 TYR   B CG  
6375 C CD1 A TYR   B 161 ? 0.2162 0.1752 0.3362 -0.0557 0.0458  -0.0684 161 TYR   B CD1 
6376 C CD1 B TYR   B 161 ? 0.2317 0.1964 0.2935 -0.0220 0.0272  -0.0529 161 TYR   B CD1 
6377 C CD2 A TYR   B 161 ? 0.2320 0.1897 0.3244 -0.0334 0.0443  -0.0691 161 TYR   B CD2 
6378 C CD2 B TYR   B 161 ? 0.2372 0.2015 0.2842 -0.0138 0.0220  -0.0503 161 TYR   B CD2 
6379 C CE1 A TYR   B 161 ? 0.2348 0.1933 0.3385 -0.0573 0.0433  -0.0681 161 TYR   B CE1 
6380 C CE1 B TYR   B 161 ? 0.2438 0.2074 0.2925 -0.0256 0.0246  -0.0498 161 TYR   B CE1 
6381 C CE2 A TYR   B 161 ? 0.2503 0.2026 0.3313 -0.0432 0.0491  -0.0607 161 TYR   B CE2 
6382 C CE2 B TYR   B 161 ? 0.2497 0.2102 0.2867 -0.0201 0.0259  -0.0455 161 TYR   B CE2 
6383 C CZ  A TYR   B 161 ? 0.2536 0.2013 0.3385 -0.0623 0.0340  -0.0596 161 TYR   B CZ  
6384 C CZ  B TYR   B 161 ? 0.2542 0.2121 0.2916 -0.0291 0.0189  -0.0431 161 TYR   B CZ  
6385 O OH  A TYR   B 161 ? 0.2820 0.2257 0.3580 -0.0680 0.0331  -0.0592 161 TYR   B OH  
6386 O OH  B TYR   B 161 ? 0.2704 0.2253 0.3033 -0.0348 0.0205  -0.0409 161 TYR   B OH  
6405 N N   . ASP   B 162 ? 0.1815 0.1588 0.3673 -0.0128 0.0053  -0.0593 162 ASP   B N   
6406 C CA  . ASP   B 162 ? 0.1806 0.1657 0.3779 -0.0043 -0.0159 -0.0604 162 ASP   B CA  
6407 C C   . ASP   B 162 ? 0.1845 0.1548 0.3830 -0.0098 -0.0276 -0.0467 162 ASP   B C   
6408 O O   . ASP   B 162 ? 0.1948 0.1573 0.3965 -0.0152 -0.0516 -0.0386 162 ASP   B O   
6409 C CB  . ASP   B 162 ? 0.2009 0.1816 0.4005 0.0080  -0.0221 -0.0825 162 ASP   B CB  
6410 C CG  . ASP   B 162 ? 0.2055 0.2065 0.4236 0.0162  -0.0251 -0.0936 162 ASP   B CG  
6411 O OD1 . ASP   B 162 ? 0.2026 0.2248 0.4097 0.0089  -0.0054 -0.1001 162 ASP   B OD1 
6412 O OD2 . ASP   B 162 ? 0.2253 0.2240 0.4561 0.0348  -0.0301 -0.0965 162 ASP   B OD2 
6418 N N   . LYS   B 163 ? 0.1836 0.1445 0.3761 -0.0166 -0.0404 -0.0292 163 LYS   B N   
6419 C CA  . LYS   B 163 ? 0.1930 0.1585 0.3824 -0.0176 -0.0198 -0.0137 163 LYS   B CA  
6420 C C   . LYS   B 163 ? 0.1648 0.1493 0.3743 -0.0206 -0.0173 0.0039  163 LYS   B C   
6421 O O   . LYS   B 163 ? 0.1666 0.1580 0.4026 -0.0234 -0.0207 0.0144  163 LYS   B O   
6422 C CB  . LYS   B 163 ? 0.2441 0.2014 0.4130 -0.0127 -0.0310 -0.0059 163 LYS   B CB  
6423 C CG  . LYS   B 163 ? 0.3239 0.2783 0.4656 -0.0101 -0.0180 0.0005  163 LYS   B CG  
6424 C CD  . LYS   B 163 ? 0.3851 0.3485 0.5212 -0.0178 -0.0170 0.0049  163 LYS   B CD  
6425 C CE  . LYS   B 163 ? 0.4351 0.4004 0.5539 -0.0217 -0.0126 0.0105  163 LYS   B CE  
6426 N NZ  . LYS   B 163 ? 0.4683 0.4470 0.5762 -0.0252 -0.0127 0.0075  163 LYS   B NZ  
6440 N N   . LEU   B 164 ? 0.1512 0.1371 0.3352 -0.0188 -0.0135 -0.0044 164 LEU   B N   
6441 C CA  . LEU   B 164 ? 0.1471 0.1466 0.3177 -0.0105 -0.0158 -0.0030 164 LEU   B CA  
6442 C C   . LEU   B 164 ? 0.1636 0.1449 0.3296 -0.0182 -0.0281 0.0050  164 LEU   B C   
6443 O O   . LEU   B 164 ? 0.1662 0.1695 0.3448 -0.0205 -0.0368 0.0069  164 LEU   B O   
6444 C CB  . LEU   B 164 ? 0.1474 0.1432 0.3005 -0.0094 -0.0163 0.0027  164 LEU   B CB  
6445 C CG  . LEU   B 164 ? 0.1628 0.1547 0.3060 -0.0100 -0.0129 -0.0013 164 LEU   B CG  
6446 C CD1 . LEU   B 164 ? 0.1754 0.1523 0.3074 -0.0176 -0.0259 -0.0060 164 LEU   B CD1 
6447 C CD2 . LEU   B 164 ? 0.1765 0.1847 0.3081 -0.0053 0.0057  -0.0128 164 LEU   B CD2 
6459 N N   . VAL   B 165 ? 0.2122 0.1496 0.3644 -0.0339 -0.0438 -0.0031 165 VAL   B N   
6460 C CA  . VAL   B 165 ? 0.2487 0.1604 0.3691 -0.0436 -0.0675 -0.0018 165 VAL   B CA  
6461 C C   . VAL   B 165 ? 0.2784 0.1823 0.4074 -0.0466 -0.1135 0.0089  165 VAL   B C   
6462 O O   . VAL   B 165 ? 0.3031 0.1997 0.4300 -0.0483 -0.1261 0.0254  165 VAL   B O   
6463 C CB  . VAL   B 165 ? 0.2751 0.1833 0.3617 -0.0257 -0.0439 -0.0316 165 VAL   B CB  
6464 C CG1 . VAL   B 165 ? 0.3015 0.1897 0.3865 -0.0165 -0.0353 -0.0289 165 VAL   B CG1 
6465 C CG2 . VAL   B 165 ? 0.2757 0.1886 0.3415 -0.0257 -0.0237 -0.0362 165 VAL   B CG2 
6475 N N   . SER   B 166 ? 0.2928 0.1712 0.4463 -0.0500 -0.1327 -0.0193 166 SER   B N   
6476 C CA  . SER   B 166 ? 0.2904 0.1795 0.5056 -0.0415 -0.1086 -0.0293 166 SER   B CA  
6477 C C   . SER   B 166 ? 0.2627 0.1909 0.5189 -0.0478 -0.0888 0.0029  166 SER   B C   
6478 O O   . SER   B 166 ? 0.2640 0.2138 0.5545 -0.0614 -0.1017 -0.0299 166 SER   B O   
6479 C CB  . SER   B 166 ? 0.2909 0.1867 0.5308 -0.0317 -0.1011 -0.0329 166 SER   B CB  
6480 O OG  . SER   B 166 ? 0.2739 0.1914 0.5466 -0.0257 -0.1077 -0.0160 166 SER   B OG  
6486 N N   . SER   B 167 ? 0.2279 0.1818 0.4724 -0.0516 -0.0996 0.0489  167 SER   B N   
6487 C CA  . SER   B 167 ? 0.2283 0.1951 0.4709 -0.0395 -0.0637 0.0517  167 SER   B CA  
6488 C C   . SER   B 167 ? 0.2163 0.2098 0.4449 -0.0550 -0.0589 0.0776  167 SER   B C   
6489 O O   . SER   B 167 ? 0.2111 0.2296 0.4521 -0.0636 -0.0637 0.0689  167 SER   B O   
6490 C CB  . SER   B 167 ? 0.2146 0.1852 0.4936 -0.0396 -0.0338 0.0352  167 SER   B CB  
6491 O OG  . SER   B 167 ? 0.2099 0.1890 0.4980 -0.0313 -0.0058 0.0294  167 SER   B OG  
6497 N N   . PHE   B 168 ? 0.2140 0.2100 0.4260 -0.0536 -0.0422 0.0775  168 PHE   B N   
6498 C CA  . PHE   B 168 ? 0.2110 0.1977 0.3639 -0.0541 -0.0333 0.0406  168 PHE   B CA  
6499 C C   . PHE   B 168 ? 0.1912 0.1789 0.2903 -0.0298 -0.0145 0.0100  168 PHE   B C   
6500 O O   . PHE   B 168 ? 0.2176 0.1656 0.2791 -0.0055 -0.0103 -0.0128 168 PHE   B O   
6501 C CB  . PHE   B 168 ? 0.2249 0.2028 0.3755 -0.0549 -0.0393 0.0506  168 PHE   B CB  
6502 C CG  . PHE   B 168 ? 0.2434 0.1863 0.3681 -0.0581 -0.0305 0.0328  168 PHE   B CG  
6503 C CD1 . PHE   B 168 ? 0.2693 0.2061 0.3761 -0.0555 -0.0388 0.0219  168 PHE   B CD1 
6504 C CD2 . PHE   B 168 ? 0.2281 0.1789 0.3666 -0.0576 -0.0323 0.0363  168 PHE   B CD2 
6505 C CE1 . PHE   B 168 ? 0.2771 0.2002 0.3665 -0.0518 -0.0289 0.0423  168 PHE   B CE1 
6506 C CE2 . PHE   B 168 ? 0.2612 0.1975 0.3860 -0.0405 -0.0340 0.0329  168 PHE   B CE2 
6507 C CZ  . PHE   B 168 ? 0.2696 0.1925 0.3707 -0.0364 -0.0364 0.0500  168 PHE   B CZ  
6517 N N   . LEU   B 169 ? 0.2118 0.1866 0.2832 0.0008  0.0028  0.0062  169 LEU   B N   
6518 C CA  . LEU   B 169 ? 0.2490 0.2173 0.3137 0.0048  0.0051  -0.0378 169 LEU   B CA  
6519 C C   . LEU   B 169 ? 0.2898 0.2502 0.3671 0.0124  0.0010  -0.0480 169 LEU   B C   
6520 O O   . LEU   B 169 ? 0.3134 0.2719 0.4170 0.0076  0.0044  -0.0681 169 LEU   B O   
6521 C CB  . LEU   B 169 ? 0.2739 0.2537 0.3236 -0.0049 -0.0088 -0.0120 169 LEU   B CB  
6522 C CG  . LEU   B 169 ? 0.3137 0.2871 0.3637 0.0012  -0.0026 -0.0032 169 LEU   B CG  
6523 C CD1 . LEU   B 169 ? 0.3287 0.3073 0.3599 -0.0058 -0.0077 0.0155  169 LEU   B CD1 
6524 C CD2 . LEU   B 169 ? 0.3101 0.2925 0.3768 0.0106  0.0129  -0.0111 169 LEU   B CD2 
6525 O OXT . LEU   B 169 ? 0.3028 0.2604 0.3703 0.0462  0.0146  -0.0411 169 LEU   B OXT 
6537 N N2  B A1A6N C .   ? 0.1981 0.2685 0.2132 -0.0061 -0.0063 -0.0108 201 A1A6N A N2  
6538 C C3  B A1A6N C .   ? 0.2845 0.3463 0.3280 0.0022  -0.0216 -0.0278 201 A1A6N A C3  
6539 C C6  B A1A6N C .   ? 0.2105 0.2771 0.2280 -0.0023 -0.0079 -0.0075 201 A1A6N A C6  
6540 C C9  B A1A6N C .   ? 0.1802 0.2528 0.1878 0.0005  0.0081  0.0093  201 A1A6N A C9  
6541 C C12 B A1A6N C .   ? 0.2641 0.3327 0.3109 0.0061  -0.0125 -0.0226 201 A1A6N A C12 
6542 C C1  B A1A6N C .   ? 0.2939 0.3480 0.3266 -0.0029 -0.0415 -0.0371 201 A1A6N A C1  
6543 C C10 B A1A6N C .   ? 0.1699 0.2460 0.1759 -0.0038 0.0210  0.0218  201 A1A6N A C10 
6544 C C11 B A1A6N C .   ? 0.1444 0.2310 0.1643 -0.0018 0.0146  0.0385  201 A1A6N A C11 
6545 C C2  B A1A6N C .   ? 0.2914 0.3488 0.3309 -0.0000 -0.0295 -0.0322 201 A1A6N A C2  
6546 C C4  B A1A6N C .   ? 0.2824 0.3449 0.3219 0.0048  -0.0170 -0.0260 201 A1A6N A C4  
6547 C C5  B A1A6N C .   ? 0.2703 0.3335 0.3118 0.0024  -0.0132 -0.0257 201 A1A6N A C5  
6548 C C7  B A1A6N C .   ? 0.1888 0.2637 0.1996 -0.0053 0.0011  -0.0019 201 A1A6N A C7  
6549 C C8  B A1A6N C .   ? 0.1709 0.2450 0.1837 0.0036  0.0062  0.0123  201 A1A6N A C8  
6550 N N1  B A1A6N C .   ? 0.2516 0.3131 0.2834 0.0024  -0.0100 -0.0198 201 A1A6N A N1  
6551 N N3  B A1A6N C .   ? 0.1808 0.2546 0.1814 -0.0053 0.0204  0.0077  201 A1A6N A N3  
6552 N N4  B A1A6N C .   ? 0.1554 0.2309 0.1747 0.0214  -0.0083 0.0312  201 A1A6N A N4  
6553 O O1  B A1A6N C .   ? 0.2903 0.3544 0.3403 0.0069  -0.0249 -0.0294 201 A1A6N A O1  
6570 O O   . HOH   D .   ? 0.2430 0.2045 0.2547 0.0005  -0.0558 -0.0109 301 HOH   A O   
6571 O O   . HOH   D .   ? 0.3921 0.3445 0.4941 0.0162  0.1524  0.0325  302 HOH   A O   
6572 O O   . HOH   D .   ? 0.2895 0.2388 0.4629 -0.0489 -0.0909 0.0444  303 HOH   A O   
6573 O O   A HOH   D .   ? 0.4032 0.6621 0.4767 -0.0916 0.0108  0.0540  304 HOH   A O   
6574 O O   . HOH   D .   ? 0.3933 0.2084 0.2363 0.0085  0.0268  0.0225  305 HOH   A O   
6575 O O   . HOH   D .   ? 0.7002 0.4612 0.3693 0.2091  -0.1668 0.0437  306 HOH   A O   
6576 O O   . HOH   D .   ? 0.6350 0.4463 0.6082 -0.0935 0.1503  0.2086  307 HOH   A O   
6577 O O   . HOH   D .   ? 0.2364 0.1916 0.2474 0.0316  -0.0352 -0.0035 308 HOH   A O   
6578 O O   . HOH   D .   ? 0.2590 0.4439 0.5466 0.0146  0.1132  0.2322  309 HOH   A O   
6579 O O   . HOH   D .   ? 0.2975 0.3973 0.1849 -0.0755 0.0347  0.0423  310 HOH   A O   
6580 O O   . HOH   D .   ? 0.2930 0.5552 0.4402 0.0396  -0.0505 0.0694  311 HOH   A O   
6581 O O   . HOH   D .   ? 0.1959 0.4999 0.4267 0.1247  0.0172  0.0779  312 HOH   A O   
6582 O O   . HOH   D .   ? 0.2947 0.5667 0.6254 0.0732  0.0688  0.0803  313 HOH   A O   
6583 O O   . HOH   D .   ? 0.5954 0.6285 0.3741 -0.0770 -0.0578 0.1081  314 HOH   A O   
6584 O O   . HOH   D .   ? 0.2251 0.2061 0.3969 -0.0546 0.0092  -0.0483 315 HOH   A O   
6585 O O   . HOH   D .   ? 0.3300 0.3367 0.4014 -0.1030 0.0166  0.0909  316 HOH   A O   
6586 O O   . HOH   D .   ? 0.5064 0.3512 0.5065 0.1223  -0.0004 -0.0486 317 HOH   A O   
6587 O O   . HOH   D .   ? 0.2561 0.2019 0.3389 -0.0177 -0.0842 0.0027  318 HOH   A O   
6588 O O   . HOH   D .   ? 0.2551 0.3712 0.3634 0.0018  -0.0309 -0.0692 319 HOH   A O   
6589 O O   . HOH   D .   ? 0.5979 0.4536 0.5259 0.0521  -0.0452 0.0098  320 HOH   A O   
6590 O O   . HOH   D .   ? 0.5774 0.4416 0.6641 -0.0929 0.1000  0.2563  321 HOH   A O   
6591 O O   . HOH   D .   ? 0.1776 0.4403 0.3323 0.0273  0.0354  0.1301  322 HOH   A O   
6592 O O   A HOH   D .   ? 0.3379 0.3553 0.2671 -0.0798 -0.0521 0.0208  323 HOH   A O   
6593 O O   . HOH   D .   ? 0.4944 0.2853 0.3339 -0.1337 0.0279  0.0237  324 HOH   A O   
6594 O O   . HOH   D .   ? 0.2274 0.3582 0.5457 -0.0604 0.0692  -0.1179 325 HOH   A O   
6595 O O   . HOH   D .   ? 0.2884 0.2932 0.5224 -0.0371 -0.1238 0.1683  326 HOH   A O   
6596 O O   . HOH   D .   ? 0.2250 0.3611 0.4187 -0.0176 -0.0788 0.1294  327 HOH   A O   
6597 O O   . HOH   D .   ? 0.6339 0.5728 0.4941 0.0617  -0.0811 -0.0685 328 HOH   A O   
6598 O O   . HOH   D .   ? 0.6721 0.6151 0.6455 -0.1050 -0.1345 -0.0983 329 HOH   A O   
6599 O O   A HOH   D .   ? 0.3733 0.5088 0.2544 -0.1369 0.0764  0.0887  330 HOH   A O   
6600 O O   . HOH   D .   ? 0.3907 0.3103 0.4017 -0.0897 -0.0246 -0.0043 331 HOH   A O   
6601 O O   B HOH   D .   ? 0.1935 0.1911 0.2215 0.0292  0.0173  0.0792  332 HOH   A O   
6602 O O   . HOH   D .   ? 0.3035 0.2823 0.3519 0.0534  0.0969  0.0968  333 HOH   A O   
6603 O O   . HOH   D .   ? 0.4408 0.4299 0.4823 -0.1919 -0.1319 0.2242  334 HOH   A O   
6604 O O   . HOH   D .   ? 0.1586 0.1547 0.2559 -0.0213 0.0086  0.0100  335 HOH   A O   
6605 O O   . HOH   D .   ? 0.6442 0.6781 0.6077 0.0737  -0.0053 0.0445  336 HOH   A O   
6606 O O   . HOH   D .   ? 0.6229 0.6355 0.8460 -0.1230 -0.0603 0.1223  337 HOH   A O   
6607 O O   . HOH   D .   ? 0.2021 0.2691 0.2599 -0.0558 -0.0194 0.1060  338 HOH   A O   
6608 O O   . HOH   D .   ? 0.3535 0.4192 0.3017 -0.0466 0.0483  0.0362  339 HOH   A O   
6609 O O   . HOH   D .   ? 0.2356 0.2696 0.2965 0.0205  0.0614  0.0909  340 HOH   A O   
6610 O O   . HOH   D .   ? 0.1571 0.2290 0.2476 -0.0023 -0.0175 0.0529  341 HOH   A O   
6611 O O   . HOH   D .   ? 0.5359 0.2636 0.6247 0.1170  -0.0270 -0.0568 342 HOH   A O   
6612 O O   . HOH   D .   ? 0.3022 0.4135 0.2489 -0.1373 -0.0081 -0.0727 343 HOH   A O   
6613 O O   . HOH   D .   ? 0.3637 0.3990 0.4722 -0.0094 0.1600  0.1116  344 HOH   A O   
6614 O O   . HOH   D .   ? 0.2315 0.2031 0.3048 0.0298  0.0325  0.0319  345 HOH   A O   
6615 O O   . HOH   D .   ? 0.4877 0.7509 0.4245 0.2517  -0.0018 -0.0522 346 HOH   A O   
6616 O O   A HOH   D .   ? 0.1589 0.2493 0.2454 0.0548  0.0625  0.0688  347 HOH   A O   
6617 O O   . HOH   D .   ? 0.2987 0.3565 0.5297 -0.0797 -0.1042 -0.0625 348 HOH   A O   
6618 O O   A HOH   D .   ? 0.2105 0.3142 0.2185 0.0525  0.0324  0.0268  349 HOH   A O   
6619 O O   . HOH   D .   ? 0.1721 0.1888 0.3289 0.0170  -0.0453 -0.0412 350 HOH   A O   
6620 O O   . HOH   D .   ? 0.2518 0.4136 0.3941 -0.0600 -0.0449 -0.0367 351 HOH   A O   
6621 O O   . HOH   D .   ? 0.2615 0.4367 0.3485 0.1228  -0.0656 -0.0149 352 HOH   A O   
6622 O O   . HOH   D .   ? 0.6603 0.4539 0.3333 0.0832  0.0353  0.1390  353 HOH   A O   
6623 O O   . HOH   D .   ? 0.4397 0.2201 0.4057 0.0400  -0.1230 0.0285  354 HOH   A O   
6624 O O   . HOH   D .   ? 0.5505 0.5466 0.5210 0.0665  0.2689  -0.0677 355 HOH   A O   
6625 O O   . HOH   D .   ? 0.1535 0.1974 0.2575 0.0028  0.0047  0.0031  356 HOH   A O   
6626 O O   . HOH   D .   ? 0.1397 0.1364 0.1677 -0.0034 0.0144  0.0104  357 HOH   A O   
6627 O O   . HOH   D .   ? 0.4749 0.5216 0.5329 0.1697  0.0804  -0.0794 358 HOH   A O   
6628 O O   . HOH   D .   ? 0.4177 0.5817 0.3868 0.0863  -0.0288 0.1237  359 HOH   A O   
6629 O O   . HOH   D .   ? 0.2034 0.1976 0.4179 0.0294  0.0972  0.0057  360 HOH   A O   
6630 O O   . HOH   D .   ? 0.3441 0.4655 0.5263 0.1529  0.0782  0.0376  361 HOH   A O   
6631 O O   . HOH   D .   ? 0.2070 0.2777 0.4338 0.0119  0.0771  -0.1000 362 HOH   A O   
6632 O O   . HOH   D .   ? 0.4013 0.2344 0.3437 0.0965  0.0622  0.0301  363 HOH   A O   
6633 O O   . HOH   D .   ? 0.1750 0.1933 0.2118 0.0135  -0.0200 0.0268  364 HOH   A O   
6634 O O   . HOH   D .   ? 0.3569 0.6370 0.3201 0.1282  0.0401  -0.0833 365 HOH   A O   
6635 O O   . HOH   D .   ? 0.4731 0.3763 0.3121 -0.0707 -0.1151 0.0116  366 HOH   A O   
6636 O O   . HOH   D .   ? 0.1738 0.1466 0.2552 -0.0134 0.0373  -0.0111 367 HOH   A O   
6637 O O   . HOH   D .   ? 0.3483 0.2369 0.3036 -0.0340 0.0239  -0.0379 368 HOH   A O   
6638 O O   . HOH   D .   ? 0.2658 0.4368 0.4125 -0.0345 0.0547  -0.0011 369 HOH   A O   
6639 O O   . HOH   D .   ? 0.1552 0.1610 0.1648 -0.0080 -0.0036 -0.0002 370 HOH   A O   
6640 O O   . HOH   D .   ? 0.4427 0.2471 0.3758 -0.1036 0.1591  -0.0203 371 HOH   A O   
6641 O O   . HOH   D .   ? 0.7021 0.3922 0.5259 0.0247  -0.1455 -0.0002 372 HOH   A O   
6642 O O   . HOH   D .   ? 0.2564 0.3348 0.3550 0.0027  0.1073  -0.0069 373 HOH   A O   
6643 O O   . HOH   D .   ? 0.4372 0.7271 0.6017 -0.0832 -0.1453 0.0813  374 HOH   A O   
6644 O O   . HOH   D .   ? 0.2573 0.2325 0.2319 -0.0132 0.0466  0.0192  375 HOH   A O   
6645 O O   . HOH   D .   ? 0.1599 0.1958 0.2322 0.0186  -0.0439 -0.0610 376 HOH   A O   
6646 O O   A HOH   D .   ? 0.1699 0.1900 0.2960 0.0070  -0.0390 0.0477  377 HOH   A O   
6647 O O   . HOH   D .   ? 0.6109 0.7052 0.5624 -0.0872 0.1700  0.0708  378 HOH   A O   
6648 O O   . HOH   D .   ? 0.2998 0.7468 0.5784 -0.0132 -0.0793 0.1626  379 HOH   A O   
6649 O O   . HOH   D .   ? 0.2440 0.2009 0.2224 -0.0542 0.0060  0.0434  380 HOH   A O   
6650 O O   . HOH   D .   ? 0.2119 0.1741 0.1793 -0.0079 0.0188  0.0282  381 HOH   A O   
6651 O O   . HOH   D .   ? 0.1946 0.2348 0.2517 -0.0270 -0.0277 0.0358  382 HOH   A O   
6652 O O   . HOH   D .   ? 0.4731 0.5269 0.5811 0.1420  -0.0738 0.0744  383 HOH   A O   
6653 O O   . HOH   D .   ? 0.3964 0.2382 0.4640 -0.1192 0.0783  0.0315  384 HOH   A O   
6654 O O   . HOH   D .   ? 0.1809 0.1803 0.2806 -0.0214 0.0237  0.0346  385 HOH   A O   
6655 O O   . HOH   D .   ? 0.6072 0.6944 0.6389 -0.1167 0.0246  -0.0551 386 HOH   A O   
6656 O O   . HOH   D .   ? 0.1899 0.2177 0.2754 -0.0323 0.0141  0.0337  387 HOH   A O   
6657 O O   . HOH   D .   ? 0.1363 0.1466 0.1893 0.0042  -0.0132 0.0057  388 HOH   A O   
6658 O O   . HOH   D .   ? 0.2669 0.4673 0.3758 0.0681  0.1034  0.2151  389 HOH   A O   
6659 O O   . HOH   D .   ? 0.2755 0.3061 0.3640 -0.0117 -0.0356 0.0987  390 HOH   A O   
6660 O O   . HOH   D .   ? 0.3546 0.3243 0.4166 -0.1448 0.1241  -0.0067 391 HOH   A O   
6661 O O   . HOH   D .   ? 0.3955 0.2556 0.5187 -0.0756 -0.0046 -0.0437 392 HOH   A O   
6662 O O   . HOH   D .   ? 0.3256 0.3739 0.1861 -0.0063 0.0596  -0.0249 393 HOH   A O   
6663 O O   . HOH   D .   ? 0.1935 0.2767 0.3698 -0.0126 -0.0143 0.0448  394 HOH   A O   
6664 O O   . HOH   D .   ? 0.2944 0.4051 0.3683 -0.0134 0.1143  -0.0548 395 HOH   A O   
6665 O O   . HOH   D .   ? 0.4927 0.5335 0.4602 0.1748  -0.1399 -0.1676 396 HOH   A O   
6666 O O   . HOH   D .   ? 0.1880 0.2590 0.3484 -0.0046 0.0713  0.1042  397 HOH   A O   
6667 O O   . HOH   D .   ? 0.2022 0.1881 0.3611 0.0310  0.1067  0.0729  398 HOH   A O   
6668 O O   . HOH   D .   ? 0.1853 0.1399 0.1754 -0.0187 0.0307  0.0065  399 HOH   A O   
6669 O O   . HOH   D .   ? 0.3082 0.2513 0.2496 -0.0435 -0.0921 0.0339  400 HOH   A O   
6670 O O   A HOH   D .   ? 0.2012 0.2303 0.2772 0.0117  0.0095  0.0628  401 HOH   A O   
6671 O O   . HOH   D .   ? 0.1602 0.1819 0.3728 0.0093  0.0082  0.0254  402 HOH   A O   
6672 O O   . HOH   D .   ? 0.1760 0.1798 0.2578 0.0150  -0.0359 0.0248  403 HOH   A O   
6673 O O   . HOH   D .   ? 0.1920 0.1862 0.2528 0.0146  -0.0232 0.0068  404 HOH   A O   
6674 O O   . HOH   D .   ? 0.2436 0.1894 0.3751 0.0127  -0.0452 0.0134  405 HOH   A O   
6675 O O   . HOH   D .   ? 0.2054 0.2320 0.2990 -0.0199 -0.0317 0.0851  406 HOH   A O   
6676 O O   . HOH   D .   ? 0.3322 0.4046 0.5052 -0.0564 0.1380  0.0244  407 HOH   A O   
6677 O O   . HOH   D .   ? 0.3174 0.1411 0.2275 -0.0095 -0.0388 0.0141  408 HOH   A O   
6678 O O   . HOH   D .   ? 0.2466 0.3501 0.7162 0.0038  0.0502  -0.0812 409 HOH   A O   
6679 O O   . HOH   D .   ? 0.2853 0.2238 0.2984 0.0087  0.0149  0.0362  410 HOH   A O   
6680 O O   . HOH   D .   ? 0.5054 0.5584 0.2183 -0.0077 0.0713  0.0782  411 HOH   A O   
6681 O O   . HOH   D .   ? 0.3790 0.7467 0.4759 -0.0978 -0.0552 0.1801  412 HOH   A O   
6682 O O   . HOH   D .   ? 0.2160 0.3106 0.3016 -0.0142 -0.0511 0.0784  413 HOH   A O   
6683 O O   A HOH   D .   ? 0.2514 0.2196 0.4159 -0.0127 0.1040  0.0083  414 HOH   A O   
6684 O O   A HOH   D .   ? 0.5675 0.4805 0.2865 -0.1301 0.0267  0.1585  415 HOH   A O   
6685 O O   . HOH   D .   ? 0.2502 0.4112 0.2904 0.1525  0.0016  0.0526  416 HOH   A O   
6686 O O   . HOH   D .   ? 0.6569 0.4305 0.5904 0.1711  -0.1077 0.1795  417 HOH   A O   
6687 O O   . HOH   D .   ? 0.2566 0.2196 0.2939 -0.0485 0.0022  0.0530  418 HOH   A O   
6688 O O   . HOH   D .   ? 0.2315 0.2504 0.3830 0.0038  -0.0224 -0.0336 419 HOH   A O   
6689 O O   . HOH   D .   ? 0.2560 0.6104 0.1849 -0.0126 0.0538  0.0241  420 HOH   A O   
6690 O O   . HOH   D .   ? 0.6117 0.3728 0.4477 -0.1351 0.0197  0.0652  421 HOH   A O   
6691 O O   . HOH   D .   ? 0.4023 0.6215 0.4099 -0.0864 0.0055  0.1176  422 HOH   A O   
6692 O O   . HOH   D .   ? 0.5302 0.7068 0.3594 -0.0117 0.2153  -0.0912 423 HOH   A O   
6693 O O   . HOH   D .   ? 0.4546 0.6689 0.5854 0.2111  0.1962  -0.0101 424 HOH   A O   
6694 O O   . HOH   D .   ? 0.5224 0.5030 0.4032 -0.0342 -0.1674 0.0156  425 HOH   A O   
6695 O O   . HOH   D .   ? 0.1839 0.2435 0.3374 -0.0165 0.0008  0.0488  426 HOH   A O   
6696 O O   . HOH   D .   ? 0.5615 0.6977 0.6894 0.0279  -0.0009 -0.0385 427 HOH   A O   
6697 O O   . HOH   D .   ? 0.2075 0.1680 0.1877 0.0075  -0.0220 -0.0103 428 HOH   A O   
6698 O O   . HOH   D .   ? 0.2721 0.3459 0.5119 0.0534  0.0673  0.0183  429 HOH   A O   
6699 O O   . HOH   D .   ? 0.4314 0.4988 0.5944 0.1892  0.0684  -0.1271 430 HOH   A O   
6700 O O   . HOH   D .   ? 0.5058 0.3304 0.2883 -0.0794 -0.0263 0.0226  431 HOH   A O   
6701 O O   . HOH   D .   ? 0.3969 0.3054 0.2196 -0.1023 0.0296  0.0764  432 HOH   A O   
6702 O O   B HOH   D .   ? 0.3669 0.3190 0.2054 0.0531  -0.0135 0.0088  433 HOH   A O   
6703 O O   . HOH   D .   ? 0.7291 0.8615 0.5836 0.2432  -0.1173 0.2630  434 HOH   A O   
6704 O O   . HOH   D .   ? 0.2897 0.1806 0.3220 0.0236  0.0111  0.0155  435 HOH   A O   
6705 O O   . HOH   D .   ? 0.4094 0.2470 0.5953 -0.0951 -0.2496 0.1113  436 HOH   A O   
6706 O O   . HOH   D .   ? 0.1913 0.2282 0.4472 -0.0202 -0.0756 0.0400  437 HOH   A O   
6707 O O   . HOH   D .   ? 0.6426 0.6384 0.7239 -0.1604 0.0345  -0.1196 438 HOH   A O   
6708 O O   . HOH   D .   ? 0.4829 0.3277 0.6294 -0.0147 0.0709  -0.0881 439 HOH   A O   
6709 O O   . HOH   D .   ? 0.7491 0.6072 0.8087 -0.0729 -0.0998 0.1891  440 HOH   A O   
6710 O O   . HOH   D .   ? 0.2395 0.2988 0.2589 0.0294  -0.0078 -0.0417 441 HOH   A O   
6711 O O   . HOH   D .   ? 0.4231 0.3781 0.3880 0.2332  -0.0652 -0.0403 442 HOH   A O   
6712 O O   . HOH   D .   ? 0.5277 0.5370 0.4827 -0.0598 -0.0779 -0.1479 443 HOH   A O   
6713 O O   . HOH   D .   ? 1.1733 1.1757 0.9764 0.0494  -0.0964 0.0613  444 HOH   A O   
6714 O O   . HOH   D .   ? 0.3082 0.4192 0.6383 -0.0103 0.0795  -0.2035 445 HOH   A O   
6715 O O   . HOH   D .   ? 0.2413 0.2006 0.2987 -0.0153 0.0048  0.0157  446 HOH   A O   
6716 O O   . HOH   D .   ? 0.6684 0.6297 0.6938 0.1157  -0.0981 -0.0380 447 HOH   A O   
6717 O O   A HOH   D .   ? 0.1413 0.1610 0.3389 -0.0128 -0.0001 0.0742  448 HOH   A O   
6718 O O   . HOH   D .   ? 0.6389 0.4212 0.5800 -0.0779 0.0857  0.1802  449 HOH   A O   
6719 O O   . HOH   D .   ? 0.4238 0.3446 0.3580 0.0589  0.0452  0.0380  450 HOH   A O   
6720 O O   . HOH   D .   ? 0.5487 0.4794 0.3901 0.0178  0.1082  0.0127  451 HOH   A O   
6721 O O   . HOH   D .   ? 0.5181 0.4449 0.3875 0.2618  -0.0734 0.0356  452 HOH   A O   
6722 O O   . HOH   D .   ? 0.7638 0.7625 0.4896 0.0555  -0.0275 -0.0872 453 HOH   A O   
6723 O O   . HOH   D .   ? 0.2848 0.2814 0.4077 -0.0347 0.0296  -0.0849 454 HOH   A O   
6724 O O   . HOH   D .   ? 0.5515 0.6175 0.4599 0.0298  -0.0237 0.1056  455 HOH   A O   
6725 O O   . HOH   D .   ? 0.3195 0.5452 0.5484 -0.1317 0.0918  -0.1316 456 HOH   A O   
6726 O O   . HOH   D .   ? 0.4729 0.5966 0.4324 0.0455  -0.0750 -0.0674 457 HOH   A O   
6727 O O   . HOH   D .   ? 0.7028 0.5058 0.5637 -0.1217 -0.0419 -0.0774 458 HOH   A O   
6728 O O   . HOH   D .   ? 0.3805 0.5472 0.5110 0.0476  -0.0623 0.1518  459 HOH   A O   
6729 O O   . HOH   D .   ? 0.4108 0.4856 0.4743 -0.1094 0.0803  -0.0026 460 HOH   A O   
6730 O O   . HOH   D .   ? 0.2968 0.3025 0.3991 -0.0910 0.0510  -0.0467 461 HOH   A O   
6731 O O   . HOH   D .   ? 0.2980 0.4379 0.5626 0.0549  0.0415  -0.1688 462 HOH   A O   
6732 O O   . HOH   D .   ? 0.5987 0.6107 0.4420 0.1137  -0.0611 -0.0483 463 HOH   A O   
6733 O O   . HOH   D .   ? 0.7999 0.3875 0.4830 -0.1317 0.1153  -0.0265 464 HOH   A O   
6734 O O   . HOH   D .   ? 0.4063 0.7127 0.4085 -0.1138 -0.1344 0.2590  465 HOH   A O   
6735 O O   . HOH   D .   ? 0.6543 0.4282 0.6560 0.0851  -0.0336 0.2720  466 HOH   A O   
6736 O O   . HOH   D .   ? 0.5958 0.4858 0.5244 0.0101  0.1327  0.0269  467 HOH   A O   
6737 O O   . HOH   D .   ? 0.3982 0.3084 0.4410 0.0238  0.1482  0.0226  468 HOH   A O   
6738 O O   . HOH   D .   ? 0.2740 0.1849 0.2899 0.0105  -0.0866 -0.0340 469 HOH   A O   
6739 O O   . HOH   D .   ? 0.6408 0.4714 0.6190 -0.0198 0.0311  -0.0381 470 HOH   A O   
6740 O O   . HOH   D .   ? 0.7070 0.6593 0.5766 0.0253  0.0978  0.2424  471 HOH   A O   
6741 O O   . HOH   D .   ? 0.4174 0.4915 0.4517 -0.2075 0.0082  0.0002  472 HOH   A O   
6742 O O   . HOH   D .   ? 0.2967 0.3140 0.2846 0.0746  -0.0019 0.0050  473 HOH   A O   
6743 O O   . HOH   D .   ? 0.5963 0.4453 0.4683 -0.0143 0.0022  -0.1383 474 HOH   A O   
6744 O O   . HOH   D .   ? 0.5125 0.5909 0.5782 -0.2031 -0.1430 0.1096  475 HOH   A O   
6745 O O   . HOH   D .   ? 0.4575 0.5474 0.3172 0.0082  -0.0147 0.0423  476 HOH   A O   
6746 O O   . HOH   D .   ? 0.3268 0.4983 0.4797 0.0604  0.1417  0.1328  477 HOH   A O   
6747 O O   . HOH   D .   ? 0.7656 0.5980 0.7319 -0.0425 0.0682  -0.0496 478 HOH   A O   
6748 O O   . HOH   D .   ? 0.5178 0.2935 0.3978 -0.1240 -0.1577 0.0643  479 HOH   A O   
6749 O O   . HOH   D .   ? 0.5199 0.5690 0.4962 0.0161  -0.0496 0.0012  480 HOH   A O   
6750 O O   . HOH   D .   ? 0.8137 0.3743 0.3672 0.0177  -0.1449 0.0351  481 HOH   A O   
6751 O O   . HOH   D .   ? 0.2582 0.5275 0.3795 0.0954  0.0852  0.2512  482 HOH   A O   
6752 O O   . HOH   D .   ? 0.6350 0.6298 0.6734 0.0554  0.2749  -0.1142 483 HOH   A O   
6753 O O   . HOH   D .   ? 0.4537 0.5104 0.3815 -0.0055 -0.0257 0.0160  484 HOH   A O   
6754 O O   . HOH   D .   ? 0.4256 0.3840 0.3130 -0.0903 0.1330  -0.0813 485 HOH   A O   
6755 O O   . HOH   D .   ? 0.2548 0.2484 0.7064 -0.0066 -0.1008 0.0439  486 HOH   A O   
6756 O O   . HOH   D .   ? 0.8058 0.8372 0.5533 -0.0625 0.1338  0.1785  487 HOH   A O   
6757 O O   . HOH   D .   ? 0.6205 0.6821 0.6690 0.0925  -0.0983 0.1207  488 HOH   A O   
6758 O O   . HOH   D .   ? 0.4344 0.4513 0.5256 -0.1664 0.0580  0.0561  489 HOH   A O   
6759 O O   . HOH   D .   ? 0.4119 0.3327 0.4716 -0.0213 0.1928  0.0552  490 HOH   A O   
6760 O O   . HOH   D .   ? 0.3292 0.2483 0.7013 0.0117  0.0661  0.1262  491 HOH   A O   
6761 O O   . HOH   D .   ? 0.5386 0.2697 0.4227 -0.0524 0.0876  0.0477  492 HOH   A O   
6762 O O   . HOH   D .   ? 0.2970 0.4614 0.3945 -0.0021 -0.0428 -0.0661 493 HOH   A O   
6763 O O   . HOH   D .   ? 0.2853 0.3161 0.6611 -0.0180 0.1239  -0.0581 494 HOH   A O   
6764 O O   . HOH   D .   ? 0.4055 0.9361 0.5853 -0.1073 -0.0242 0.2425  495 HOH   A O   
6765 O O   . HOH   D .   ? 0.2232 0.3433 0.3724 0.0321  -0.0392 0.0692  496 HOH   A O   
6766 O O   . HOH   D .   ? 0.3090 0.4155 0.4780 0.0507  -0.0364 -0.0026 497 HOH   A O   
6767 O O   . HOH   D .   ? 0.6051 0.8420 0.5761 0.1234  0.0097  0.1317  498 HOH   A O   
6768 O O   . HOH   D .   ? 0.6397 0.3707 0.5959 -0.1405 -0.0864 0.1496  499 HOH   A O   
6769 O O   . HOH   D .   ? 0.6008 0.7911 0.5559 0.0871  -0.1688 -0.0066 500 HOH   A O   
6770 O O   B HOH   D .   ? 0.2559 0.4008 0.1879 0.0455  0.0103  -0.0380 501 HOH   A O   
6771 O O   . HOH   D .   ? 0.6908 0.6725 0.5559 -0.0787 -0.1175 -0.1393 502 HOH   A O   
6772 O O   . HOH   D .   ? 0.3659 0.2594 0.5152 -0.0091 0.0248  0.0621  503 HOH   A O   
6773 O O   . HOH   D .   ? 0.5619 0.6780 0.6476 0.3297  -0.0299 0.1368  504 HOH   A O   
6774 O O   A HOH   D .   ? 0.2840 0.6575 0.2344 0.0902  0.0497  0.0942  505 HOH   A O   
6775 O O   . HOH   D .   ? 0.3208 0.7850 0.5183 0.0674  0.0849  -0.1102 506 HOH   A O   
6776 O O   . HOH   D .   ? 0.5108 0.7203 0.5372 -0.0639 -0.0837 0.1045  507 HOH   A O   
6777 O O   . HOH   D .   ? 0.4647 0.5535 0.4531 0.1019  -0.0658 0.1434  508 HOH   A O   
6778 O O   . HOH   D .   ? 0.3030 0.4798 0.5971 0.0219  -0.0393 0.2855  509 HOH   A O   
6779 O O   . HOH   E .   ? 0.2159 0.2285 0.3226 0.0043  0.0417  0.0247  201 HOH   B O   
6780 O O   . HOH   E .   ? 0.7507 0.3555 0.4535 0.0621  0.0475  -0.0181 202 HOH   B O   
6781 O O   . HOH   E .   ? 0.3284 0.2344 0.6140 -0.0213 0.2259  0.0094  203 HOH   B O   
6782 O O   . HOH   E .   ? 0.5500 0.3556 0.4303 -0.0240 0.0258  -0.1782 204 HOH   B O   
6783 O O   . HOH   E .   ? 0.3783 0.2881 0.7070 -0.0273 0.0904  -0.0089 205 HOH   B O   
6784 O O   . HOH   E .   ? 0.2008 0.2610 0.3668 0.0067  0.0136  -0.0489 206 HOH   B O   
6785 O O   . HOH   E .   ? 0.3255 0.3856 0.5125 -0.0761 0.0319  -0.1326 207 HOH   B O   
6786 O O   . HOH   E .   ? 0.5055 0.3986 0.3741 0.0123  -0.1438 0.0356  208 HOH   B O   
6787 O O   . HOH   E .   ? 0.1631 0.2096 0.3483 -0.0263 -0.0053 0.0211  209 HOH   B O   
6788 O O   . HOH   E .   ? 0.3138 0.6958 0.4558 0.0567  -0.0128 0.2699  210 HOH   B O   
6789 O O   . HOH   E .   ? 0.3352 0.4153 0.3231 -0.0609 0.0045  -0.1345 211 HOH   B O   
6790 O O   . HOH   E .   ? 0.3095 0.6169 0.5523 0.0081  0.1816  -0.1579 212 HOH   B O   
6791 O O   . HOH   E .   ? 0.5156 0.6130 0.4443 0.3049  -0.1186 -0.0141 213 HOH   B O   
6792 O O   . HOH   E .   ? 0.6008 0.6354 0.5260 0.1414  0.0988  0.0251  214 HOH   B O   
6793 O O   . HOH   E .   ? 0.2965 0.2562 0.6312 0.0648  -0.0831 0.0604  215 HOH   B O   
6794 O O   . HOH   E .   ? 0.4344 0.5027 0.3881 0.2146  -0.0235 0.0409  216 HOH   B O   
6795 O O   . HOH   E .   ? 0.5537 0.7610 0.4385 0.3198  0.1257  0.1099  217 HOH   B O   
6796 O O   . HOH   E .   ? 0.1784 0.2462 0.3717 -0.0204 0.0320  -0.0347 218 HOH   B O   
6797 O O   . HOH   E .   ? 0.5542 0.4599 0.4251 0.0249  0.1228  -0.1879 219 HOH   B O   
6798 O O   . HOH   E .   ? 0.3180 0.2031 0.5167 0.0040  0.1715  0.0646  220 HOH   B O   
6799 O O   . HOH   E .   ? 0.3867 0.5071 0.5901 0.1923  0.0723  -0.0669 221 HOH   B O   
6800 O O   . HOH   E .   ? 0.5496 0.2146 0.3234 0.0147  -0.0757 -0.0025 222 HOH   B O   
6801 O O   . HOH   E .   ? 0.5755 0.3157 0.4539 -0.1603 -0.0042 0.0046  223 HOH   B O   
6802 O O   . HOH   E .   ? 0.3126 0.2845 0.4392 0.0688  -0.0907 -0.0588 224 HOH   B O   
6803 O O   . HOH   E .   ? 0.2612 0.3534 0.3468 -0.0935 0.0297  0.0019  225 HOH   B O   
6804 O O   . HOH   E .   ? 0.7537 0.5904 0.5502 0.2082  -0.0541 -0.0808 226 HOH   B O   
6805 O O   . HOH   E .   ? 0.6618 0.5927 0.3260 -0.1187 0.0204  -0.0653 227 HOH   B O   
6806 O O   . HOH   E .   ? 0.2310 0.2203 0.4092 -0.0267 0.0077  -0.0367 228 HOH   B O   
6807 O O   . HOH   E .   ? 0.2464 0.1731 0.2647 -0.0331 0.0900  -0.0119 229 HOH   B O   
6808 O O   . HOH   E .   ? 0.5911 0.2884 0.4085 -0.2111 0.0301  0.0163  230 HOH   B O   
6809 O O   . HOH   E .   ? 0.4540 0.4229 0.6237 -0.0027 -0.1779 -0.0788 231 HOH   B O   
6810 O O   . HOH   E .   ? 0.2807 0.2697 0.3469 0.0228  0.0324  -0.0970 232 HOH   B O   
6811 O O   . HOH   E .   ? 0.1603 0.1520 0.1548 -0.0075 -0.0079 -0.0077 233 HOH   B O   
6812 O O   . HOH   E .   ? 0.2681 0.2174 0.2940 0.0470  0.0451  -0.0100 234 HOH   B O   
6813 O O   . HOH   E .   ? 0.3686 0.2011 0.1985 0.0146  -0.0783 -0.0218 235 HOH   B O   
6814 O O   . HOH   E .   ? 0.3493 0.2647 0.4295 0.0406  -0.0812 -0.1258 236 HOH   B O   
6815 O O   . HOH   E .   ? 0.3849 0.2864 0.2429 0.0185  0.0582  0.0331  237 HOH   B O   
6816 O O   . HOH   E .   ? 0.2094 0.1410 0.3456 0.0147  -0.0588 -0.0129 238 HOH   B O   
6817 O O   . HOH   E .   ? 0.3001 0.3199 0.3189 -0.0664 0.0104  -0.0271 239 HOH   B O   
6818 O O   . HOH   E .   ? 0.3343 0.1886 0.6128 -0.0350 -0.1329 -0.0166 240 HOH   B O   
6819 O O   . HOH   E .   ? 0.1620 0.1387 0.1772 -0.0015 -0.0130 0.0010  241 HOH   B O   
6820 O O   . HOH   E .   ? 0.2282 0.3692 0.2669 -0.0117 -0.0049 0.0371  242 HOH   B O   
6821 O O   . HOH   E .   ? 0.3712 0.2689 0.4436 0.0798  -0.0652 -0.1101 243 HOH   B O   
6822 O O   . HOH   E .   ? 0.5531 0.6184 0.3780 0.0223  -0.0423 0.0960  244 HOH   B O   
6823 O O   . HOH   E .   ? 0.3590 0.4053 0.2663 0.0136  0.1042  0.0290  245 HOH   B O   
6824 O O   . HOH   E .   ? 0.2485 0.3720 0.3659 -0.0554 -0.0886 -0.0402 246 HOH   B O   
6825 O O   . HOH   E .   ? 0.1592 0.1611 0.2910 -0.0044 0.0065  -0.0106 247 HOH   B O   
6826 O O   . HOH   E .   ? 0.4602 0.3615 0.3259 0.0806  0.0052  -0.0513 248 HOH   B O   
6827 O O   . HOH   E .   ? 0.3731 0.3033 0.3490 -0.0425 0.0195  -0.0673 249 HOH   B O   
6828 O O   . HOH   E .   ? 0.5135 0.4187 0.6382 0.0849  -0.0355 0.2732  250 HOH   B O   
6829 O O   . HOH   E .   ? 0.2932 0.3411 0.5520 0.0874  -0.0790 -0.0851 251 HOH   B O   
6830 O O   . HOH   E .   ? 0.4321 0.3825 0.6003 -0.1583 -0.0308 0.1282  252 HOH   B O   
6831 O O   . HOH   E .   ? 0.2882 0.3769 0.3330 -0.1017 -0.0352 -0.0205 253 HOH   B O   
6832 O O   . HOH   E .   ? 0.2377 0.2088 0.2830 0.0659  -0.0772 -0.0595 254 HOH   B O   
6833 O O   . HOH   E .   ? 0.2410 0.2106 0.2387 -0.0501 -0.0425 0.0310  255 HOH   B O   
6834 O O   . HOH   E .   ? 0.2117 0.4538 0.4780 -0.0451 -0.0110 -0.1254 256 HOH   B O   
6835 O O   . HOH   E .   ? 0.2440 0.2952 0.2342 -0.0513 0.0451  0.0283  257 HOH   B O   
6836 O O   . HOH   E .   ? 0.1660 0.1808 0.3436 -0.0349 -0.0112 0.0128  258 HOH   B O   
6837 O O   . HOH   E .   ? 0.4577 0.3722 0.4709 -0.1146 0.1091  -0.0880 259 HOH   B O   
6838 O O   . HOH   E .   ? 0.1534 0.1785 0.2347 -0.0034 0.0018  0.0164  260 HOH   B O   
6839 O O   . HOH   E .   ? 0.2119 0.1663 0.2355 -0.0294 -0.0532 0.0337  261 HOH   B O   
6840 O O   . HOH   E .   ? 0.1938 0.2645 0.2854 0.0312  0.0392  0.0828  262 HOH   B O   
6841 O O   . HOH   E .   ? 0.2877 0.4857 0.6337 -0.0466 -0.0113 -0.1353 263 HOH   B O   
6842 O O   . HOH   E .   ? 0.3864 0.2180 0.2149 0.0534  -0.0478 -0.0193 264 HOH   B O   
6843 O O   . HOH   E .   ? 0.2242 0.2043 0.3647 -0.0046 -0.0484 -0.0469 265 HOH   B O   
6844 O O   . HOH   E .   ? 0.3082 0.5064 0.3732 -0.0044 -0.0845 0.1073  266 HOH   B O   
6845 O O   . HOH   E .   ? 0.2732 0.2965 0.3032 -0.0584 -0.0854 0.0556  267 HOH   B O   
6846 O O   . HOH   E .   ? 0.2905 0.4045 0.4214 0.0044  0.1282  0.0258  268 HOH   B O   
6847 O O   . HOH   E .   ? 0.3650 0.3665 0.4467 0.1334  -0.0235 -0.0926 269 HOH   B O   
6848 O O   . HOH   E .   ? 0.1946 0.1908 0.1819 -0.0471 -0.0472 0.0100  270 HOH   B O   
6849 O O   . HOH   E .   ? 0.3073 0.2037 0.4666 0.0187  0.0343  0.0537  271 HOH   B O   
6850 O O   . HOH   E .   ? 0.5485 0.6059 0.5584 0.2522  -0.0748 0.0464  272 HOH   B O   
6851 O O   . HOH   E .   ? 0.2233 0.1660 0.2366 -0.0323 -0.0322 0.0099  273 HOH   B O   
6852 O O   . HOH   E .   ? 0.2615 0.2973 0.3450 -0.0331 0.0535  -0.0749 274 HOH   B O   
6853 O O   . HOH   E .   ? 0.2421 0.2646 0.2450 -0.0479 -0.0576 -0.0350 275 HOH   B O   
6854 O O   . HOH   E .   ? 0.1758 0.1756 0.3602 -0.0134 0.0207  -0.0167 276 HOH   B O   
6855 O O   . HOH   E .   ? 0.4183 0.2868 0.4335 -0.0349 -0.1160 -0.0212 277 HOH   B O   
6856 O O   . HOH   E .   ? 0.2499 0.2689 0.2269 -0.0039 0.0073  -0.0122 278 HOH   B O   
6857 O O   . HOH   E .   ? 0.1862 0.1471 0.3219 -0.0090 -0.0171 -0.0241 279 HOH   B O   
6858 O O   . HOH   E .   ? 0.2462 0.1996 0.3134 -0.0559 0.0159  -0.0030 280 HOH   B O   
6859 O O   . HOH   E .   ? 0.1752 0.1584 0.2119 -0.0002 0.0087  -0.0077 281 HOH   B O   
6860 O O   . HOH   E .   ? 0.5094 0.6319 0.2758 -0.1078 -0.0869 0.0802  282 HOH   B O   
6861 O O   . HOH   E .   ? 0.3138 0.4880 0.5418 -0.0997 -0.0962 0.0679  283 HOH   B O   
6862 O O   . HOH   E .   ? 0.4941 0.6088 0.5192 0.0252  -0.1665 0.0628  284 HOH   B O   
6863 O O   . HOH   E .   ? 0.2703 0.4258 0.2622 0.1402  -0.0645 -0.0561 285 HOH   B O   
6864 O O   . HOH   E .   ? 0.1676 0.2069 0.1723 -0.0075 -0.0182 0.0039  286 HOH   B O   
6865 O O   . HOH   E .   ? 0.2524 0.2720 0.3299 -0.0068 -0.0855 0.0201  287 HOH   B O   
6866 O O   . HOH   E .   ? 0.1914 0.2108 0.3360 0.0106  0.0145  -0.0094 288 HOH   B O   
6867 O O   . HOH   E .   ? 0.3207 0.6366 0.7438 0.0938  -0.0515 -0.1390 289 HOH   B O   
6868 O O   . HOH   E .   ? 0.6851 0.7039 0.3564 0.0276  0.0354  0.1195  290 HOH   B O   
6869 O O   . HOH   E .   ? 0.3022 0.3618 0.3639 -0.0195 0.0295  -0.1726 291 HOH   B O   
6870 O O   . HOH   E .   ? 0.4375 0.4392 0.4758 -0.1587 0.0804  -0.1872 292 HOH   B O   
6871 O O   . HOH   E .   ? 0.4080 0.3164 0.2213 0.0329  -0.0723 0.0023  293 HOH   B O   
6872 O O   . HOH   E .   ? 0.4992 0.3359 0.4416 -0.0670 0.0690  0.0809  294 HOH   B O   
6873 O O   . HOH   E .   ? 0.3504 0.5062 0.4474 -0.2163 0.1146  -0.0737 295 HOH   B O   
6874 O O   . HOH   E .   ? 0.1826 0.4026 0.4944 0.0525  -0.0110 -0.1603 296 HOH   B O   
6875 O O   . HOH   E .   ? 0.4062 0.5578 0.7102 -0.0018 0.1281  -0.0358 297 HOH   B O   
6876 O O   . HOH   E .   ? 0.2507 0.3216 0.3616 0.0777  -0.0597 -0.1180 298 HOH   B O   
6877 O O   . HOH   E .   ? 0.1894 0.1709 0.2747 0.0127  0.0032  0.0166  299 HOH   B O   
6878 O O   . HOH   E .   ? 0.3438 0.2250 0.2443 0.0331  -0.0377 0.0139  300 HOH   B O   
6879 O O   . HOH   E .   ? 0.5922 0.3995 0.3912 0.2665  0.1414  0.0971  301 HOH   B O   
6880 O O   . HOH   E .   ? 0.3939 0.2331 0.4758 -0.1121 -0.2001 0.0816  302 HOH   B O   
6881 O O   . HOH   E .   ? 0.2435 0.4259 0.5545 0.1215  -0.0712 -0.1838 303 HOH   B O   
6882 O O   . HOH   E .   ? 0.1623 0.1577 0.3485 0.0160  0.0113  -0.0048 304 HOH   B O   
6883 O O   . HOH   E .   ? 0.4214 0.4016 0.2505 0.1355  -0.0746 0.0352  305 HOH   B O   
6884 O O   . HOH   E .   ? 0.2303 0.1813 0.2891 -0.0356 -0.0178 -0.0044 306 HOH   B O   
6885 O O   . HOH   E .   ? 0.4960 0.4872 0.2746 0.1769  -0.1129 -0.0528 307 HOH   B O   
6886 O O   . HOH   E .   ? 0.6066 0.2805 0.3545 0.0495  0.0239  0.0830  308 HOH   B O   
6887 O O   . HOH   E .   ? 0.1725 0.2693 0.2437 -0.0158 -0.0164 0.0591  309 HOH   B O   
6888 O O   . HOH   E .   ? 0.2725 0.7510 0.2864 0.1309  -0.0529 -0.1052 310 HOH   B O   
6889 O O   . HOH   E .   ? 0.2420 0.4552 0.4772 -0.0691 -0.0159 -0.0031 311 HOH   B O   
6890 O O   . HOH   E .   ? 0.2032 0.1745 0.3371 0.0384  -0.0766 0.0081  312 HOH   B O   
6891 O O   . HOH   E .   ? 0.2157 0.3016 0.5491 -0.0114 -0.0755 -0.0306 313 HOH   B O   
6892 O O   . HOH   E .   ? 0.6908 0.4770 0.5016 0.1143  0.1538  0.0236  314 HOH   B O   
6893 O O   . HOH   E .   ? 0.2420 0.2004 0.2202 -0.0118 0.0116  0.0123  315 HOH   B O   
6894 O O   . HOH   E .   ? 0.3447 0.3058 0.5954 -0.0435 -0.0592 0.1159  316 HOH   B O   
6895 O O   . HOH   E .   ? 0.2775 0.1480 0.2945 -0.0172 -0.0220 0.0234  317 HOH   B O   
6896 O O   . HOH   E .   ? 0.3156 0.1930 0.3685 0.0708  0.0870  0.0418  318 HOH   B O   
6897 O O   . HOH   E .   ? 0.4377 0.4888 0.2463 0.0417  0.0943  0.1038  319 HOH   B O   
6898 O O   . HOH   E .   ? 0.2836 0.2893 0.3849 -0.0184 0.1120  -0.0881 320 HOH   B O   
6899 O O   . HOH   E .   ? 0.5749 0.4175 0.4490 0.1288  0.1597  0.2086  321 HOH   B O   
6900 O O   . HOH   E .   ? 0.3040 0.3721 0.5908 -0.0859 -0.1788 0.2061  322 HOH   B O   
6901 O O   . HOH   E .   ? 0.4934 0.3041 0.2668 -0.1683 0.0458  -0.0264 323 HOH   B O   
6902 O O   . HOH   E .   ? 0.1768 0.2007 0.3237 -0.0326 -0.0082 -0.0036 324 HOH   B O   
6903 O O   . HOH   E .   ? 0.4097 0.2161 0.3224 0.1368  0.0870  0.0154  325 HOH   B O   
6904 O O   . HOH   E .   ? 0.5830 0.5174 0.6462 0.1587  -0.0635 0.1673  326 HOH   B O   
6905 O O   . HOH   E .   ? 0.1730 0.1678 0.3193 -0.0145 -0.0085 -0.0235 327 HOH   B O   
6906 O O   . HOH   E .   ? 0.2340 0.2626 0.5497 -0.0660 0.0030  0.1438  328 HOH   B O   
6907 O O   . HOH   E .   ? 0.4702 0.6536 0.4502 0.0999  -0.0947 0.0994  329 HOH   B O   
6908 O O   . HOH   E .   ? 0.5902 0.4078 0.2887 -0.0402 -0.0742 -0.0172 330 HOH   B O   
6909 O O   . HOH   E .   ? 0.5022 0.4482 0.5853 0.0399  0.0084  0.0250  331 HOH   B O   
6910 O O   . HOH   E .   ? 0.3666 0.4534 0.8421 -0.0312 -0.1303 0.2343  332 HOH   B O   
6911 O O   . HOH   E .   ? 0.2112 0.1947 0.2984 0.0315  0.0612  0.0173  333 HOH   B O   
6912 O O   . HOH   E .   ? 0.2755 0.2022 0.5119 0.0114  0.0046  0.0600  334 HOH   B O   
6913 O O   . HOH   E .   ? 0.4518 0.3315 0.5778 0.1489  0.2147  0.1941  335 HOH   B O   
6914 O O   . HOH   E .   ? 0.8490 0.2294 0.3689 0.0630  -0.1144 0.0028  336 HOH   B O   
6915 O O   . HOH   E .   ? 0.2699 0.2022 0.4155 0.0442  -0.0849 -0.0254 337 HOH   B O   
6916 O O   . HOH   E .   ? 0.5786 0.4536 0.5362 -0.0426 -0.0972 -0.1412 338 HOH   B O   
6917 O O   . HOH   E .   ? 0.1854 0.1666 0.2625 0.0000  -0.0101 0.0164  339 HOH   B O   
6918 O O   . HOH   E .   ? 0.5636 0.4351 0.4729 -0.0144 0.1369  -0.1582 340 HOH   B O   
6919 O O   . HOH   E .   ? 0.5496 0.3482 0.3832 0.0454  -0.1562 -0.0744 341 HOH   B O   
6920 O O   . HOH   E .   ? 0.3211 0.5165 0.4199 -0.0735 -0.0770 -0.0480 342 HOH   B O   
6921 O O   . HOH   E .   ? 0.4687 0.7317 0.4473 -0.0762 -0.0813 0.1823  343 HOH   B O   
6922 O O   . HOH   E .   ? 0.3698 0.5379 0.7261 -0.1086 -0.0479 0.0107  344 HOH   B O   
6923 O O   . HOH   E .   ? 0.5668 0.5861 0.6351 -0.0957 -0.0987 0.1593  345 HOH   B O   
6924 O O   . HOH   E .   ? 0.4307 0.6090 0.6026 0.0073  -0.1271 -0.0389 346 HOH   B O   
6925 O O   . HOH   E .   ? 0.2485 0.2186 0.3673 -0.0056 0.1109  -0.0168 347 HOH   B O   
6926 O O   . HOH   E .   ? 0.2307 0.6003 0.3248 0.1458  -0.0598 -0.1391 348 HOH   B O   
6927 O O   . HOH   E .   ? 0.4673 0.6695 0.5841 -0.1376 0.0158  0.1745  349 HOH   B O   
6928 O O   . HOH   E .   ? 0.4652 0.6698 0.7108 0.0851  0.1131  -0.0382 350 HOH   B O   
6929 O O   . HOH   E .   ? 0.3210 0.2294 0.4924 -0.0212 -0.0872 -0.0546 351 HOH   B O   
6930 O O   . HOH   E .   ? 0.4202 0.4005 0.4961 -0.1652 0.0139  -0.0293 352 HOH   B O   
6931 O O   . HOH   E .   ? 0.6313 0.6267 0.4126 -0.0849 -0.1237 0.0983  353 HOH   B O   
6932 O O   . HOH   E .   ? 0.2606 0.3691 0.5353 -0.0150 0.0182  -0.0225 354 HOH   B O   
6933 O O   . HOH   E .   ? 0.3627 0.2269 0.3121 -0.0554 -0.0087 -0.0756 355 HOH   B O   
6934 O O   . HOH   E .   ? 0.4652 0.2776 0.5988 -0.0622 0.0927  0.0693  356 HOH   B O   
6935 O O   . HOH   E .   ? 0.3403 0.2759 0.4018 -0.0607 0.0032  -0.0690 357 HOH   B O   
6936 O O   . HOH   E .   ? 0.5286 0.5064 0.6209 0.0043  0.0181  0.0657  358 HOH   B O   
6937 O O   . HOH   E .   ? 0.5123 0.6333 0.5164 0.2370  -0.1057 0.1286  359 HOH   B O   
6938 O O   . HOH   E .   ? 0.5623 0.3252 0.4724 0.0540  0.1768  -0.0698 360 HOH   B O   
6939 O O   . HOH   E .   ? 0.5420 0.3843 0.6132 -0.0070 0.1072  0.0387  361 HOH   B O   
6940 O O   . HOH   E .   ? 0.5997 0.3348 0.5162 -0.0185 -0.1804 -0.0326 362 HOH   B O   
6941 O O   . HOH   E .   ? 0.2447 0.4001 0.7475 -0.0828 -0.0700 -0.0717 363 HOH   B O   
6942 O O   . HOH   E .   ? 0.3865 0.7143 0.3304 0.1809  -0.0693 -0.0091 364 HOH   B O   
6943 O O   . HOH   E .   ? 0.5669 0.6215 0.5094 -0.1059 -0.0371 -0.1362 365 HOH   B O   
6944 O O   . HOH   E .   ? 0.6667 0.2448 0.3847 -0.0411 0.0374  0.0440  366 HOH   B O   
6945 O O   . HOH   E .   ? 0.5836 0.5328 0.3391 0.1586  -0.1703 0.0278  367 HOH   B O   
6946 O O   . HOH   E .   ? 0.4967 0.2907 0.4701 -0.0305 -0.1713 0.0073  368 HOH   B O   
6947 O O   . HOH   E .   ? 0.6258 0.4704 0.4454 0.0958  0.0295  0.0332  369 HOH   B O   
6948 O O   . HOH   E .   ? 0.5077 0.3127 0.5829 -0.1287 -0.0795 0.0133  370 HOH   B O   
6949 O O   . HOH   E .   ? 0.4179 0.3625 0.3944 0.1080  -0.0923 -0.0164 371 HOH   B O   
6950 O O   . HOH   E .   ? 0.4107 0.6218 0.5486 0.2622  0.0578  0.1752  372 HOH   B O   
6951 O O   . HOH   E .   ? 0.8722 0.7599 0.5918 0.2866  -0.1170 0.0706  373 HOH   B O   
6952 O O   . HOH   E .   ? 0.5192 0.7509 0.4667 -0.1490 0.0216  -0.1422 374 HOH   B O   
6953 O O   . HOH   E .   ? 0.4564 0.5073 0.4949 -0.0680 -0.0755 -0.0107 375 HOH   B O   
6954 O O   . HOH   E .   ? 0.3585 0.5852 0.2552 -0.0360 0.0190  -0.0069 376 HOH   B O   
6955 O O   . HOH   E .   ? 0.6049 0.4049 0.3503 -0.0554 -0.1223 -0.0854 377 HOH   B O   
6956 O O   . HOH   E .   ? 0.2448 0.3700 0.4874 0.0038  -0.0395 -0.0756 378 HOH   B O   
6957 O O   . HOH   E .   ? 0.3449 0.5912 0.6529 0.0809  -0.0230 -0.0135 379 HOH   B O   
6958 O O   . HOH   E .   ? 0.4785 0.6552 0.6000 0.0531  -0.0198 0.2500  380 HOH   B O   
6959 O O   . HOH   E .   ? 0.5745 0.7076 0.6923 -0.0481 0.2528  0.0919  381 HOH   B O   
6960 O O   . HOH   E .   ? 0.7115 0.3724 0.4982 -0.0889 -0.0325 0.0144  382 HOH   B O   
6961 O O   . HOH   E .   ? 0.2948 0.2690 0.3534 -0.0009 0.0525  0.0215  383 HOH   B O   
6962 O O   . HOH   E .   ? 0.5291 0.9401 0.6027 0.1641  0.1821  0.0498  384 HOH   B O   
6963 O O   . HOH   E .   ? 0.5996 0.5214 0.4261 0.0902  0.0699  -0.0733 385 HOH   B O   
6964 O O   . HOH   E .   ? 0.8442 0.6073 0.5318 0.2228  -0.0096 -0.0397 386 HOH   B O   
6965 O O   . HOH   E .   ? 0.5229 0.3470 0.5688 -0.2056 -0.0189 0.0968  387 HOH   B O   
6966 O O   . HOH   E .   ? 0.6022 0.4716 0.5884 -0.0430 0.0699  0.0264  388 HOH   B O   
6967 O O   . HOH   E .   ? 0.5574 0.4434 0.3996 -0.0203 0.0520  -0.0373 389 HOH   B O   
6968 O O   . HOH   E .   ? 0.2413 0.4617 0.4580 -0.0634 -0.1005 -0.0640 390 HOH   B O   
6969 O O   . HOH   E .   ? 0.4169 0.2529 0.3730 0.0718  -0.0275 -0.0108 391 HOH   B O   
6970 O O   . HOH   E .   ? 0.6066 0.4482 0.5393 0.0897  0.1133  0.0557  392 HOH   B O   
6971 O O   . HOH   E .   ? 0.3883 0.2214 0.5339 -0.0423 -0.0381 0.0688  393 HOH   B O   
6972 O O   . HOH   E .   ? 0.2394 0.5162 0.7039 -0.1221 -0.0685 -0.0455 394 HOH   B O   
6973 O O   . HOH   E .   ? 0.4872 0.5876 0.4852 0.1433  -0.0224 -0.1164 395 HOH   B O   
6974 O O   . HOH   E .   ? 0.3520 0.3823 0.4415 0.0164  0.0251  -0.0934 396 HOH   B O   
6975 O O   . HOH   E .   ? 0.2198 0.2717 0.6083 -0.0429 -0.0552 -0.0609 397 HOH   B O   
6976 O O   . HOH   E .   ? 0.4916 0.5155 0.4811 0.1388  0.1495  0.1266  398 HOH   B O   
6977 O O   . HOH   E .   ? 0.5304 0.5828 0.6508 -0.0188 -0.1518 0.2898  399 HOH   B O   
6978 O O   . HOH   E .   ? 0.5260 0.4353 0.3162 -0.2568 -0.0878 0.1207  400 HOH   B O   
6979 O O   . HOH   E .   ? 0.6949 0.5346 0.3951 0.1226  -0.0351 -0.0062 401 HOH   B O   
# 
