data_7HD3
# 
_entry.id   7HD3 
# 
_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   7HD3         pdb_00007hd3 10.2210/pdb7hd3/pdb 
WWPDB D_1001407321 ?            ?                   
# 
_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                        7HD3 
_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 'trifluoroacetic acid'                                                               114.023   1   ? ? ? ? 
3 non-polymer syn '[(3S)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-8-oxa-2-azaspiro[4.5]decan-3-yl]methanol' 288.345   1   ? ? ? ? 
4 water       nat water                                                                                18.015    411 ? ? ? ? 
# 
_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 'trifluoroacetic acid'                                                               TFA   
3 '[(3S)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-8-oxa-2-azaspiro[4.5]decan-3-yl]methanol' A1A61 
4 water                                                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A61 non-polymer         . '[(3S)-2-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-8-oxa-2-azaspiro[4.5]decan-3-yl]methanol' ? 'C15 H20 N4 O2' 
288.345 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                                               ? 'C2 H F3 O2' 
114.023 
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 TFA   1   201 201  TFA   TFA A . 
D 3 A1A61 1   202 201  A1A61 LA1 A . 
E 4 HOH   1   301 196  HOH   HOH A . 
E 4 HOH   2   302 292  HOH   HOH A . 
E 4 HOH   3   303 229  HOH   HOH A . 
E 4 HOH   4   304 195  HOH   HOH A . 
E 4 HOH   5   305 393  HOH   HOH A . 
E 4 HOH   6   306 625  HOH   HOH A . 
E 4 HOH   7   307 109  HOH   HOH A . 
E 4 HOH   8   308 1301 HOH   HOH A . 
E 4 HOH   9   309 247  HOH   HOH A . 
E 4 HOH   10  310 209  HOH   HOH A . 
E 4 HOH   11  311 86   HOH   HOH A . 
E 4 HOH   12  312 136  HOH   HOH A . 
E 4 HOH   13  313 76   HOH   HOH A . 
E 4 HOH   14  314 661  HOH   HOH A . 
E 4 HOH   15  315 1295 HOH   HOH A . 
E 4 HOH   16  316 281  HOH   HOH A . 
E 4 HOH   17  317 469  HOH   HOH A . 
E 4 HOH   18  318 192  HOH   HOH A . 
E 4 HOH   19  319 1300 HOH   HOH A . 
E 4 HOH   20  320 124  HOH   HOH A . 
E 4 HOH   21  321 354  HOH   HOH A . 
E 4 HOH   22  322 1283 HOH   HOH A . 
E 4 HOH   23  323 1290 HOH   HOH A . 
E 4 HOH   24  324 199  HOH   HOH A . 
E 4 HOH   25  325 461  HOH   HOH A . 
E 4 HOH   26  326 155  HOH   HOH A . 
E 4 HOH   27  327 15   HOH   HOH A . 
E 4 HOH   28  328 18   HOH   HOH A . 
E 4 HOH   29  329 140  HOH   HOH A . 
E 4 HOH   30  330 964  HOH   HOH A . 
E 4 HOH   31  331 164  HOH   HOH A . 
E 4 HOH   32  332 21   HOH   HOH A . 
E 4 HOH   33  333 165  HOH   HOH A . 
E 4 HOH   34  334 151  HOH   HOH A . 
E 4 HOH   35  335 241  HOH   HOH A . 
E 4 HOH   36  336 236  HOH   HOH A . 
E 4 HOH   37  337 153  HOH   HOH A . 
E 4 HOH   38  338 662  HOH   HOH A . 
E 4 HOH   39  339 96   HOH   HOH A . 
E 4 HOH   40  340 225  HOH   HOH A . 
E 4 HOH   41  341 33   HOH   HOH A . 
E 4 HOH   42  342 337  HOH   HOH A . 
E 4 HOH   43  343 39   HOH   HOH A . 
E 4 HOH   44  344 105  HOH   HOH A . 
E 4 HOH   45  345 169  HOH   HOH A . 
E 4 HOH   46  346 132  HOH   HOH A . 
E 4 HOH   47  347 8    HOH   HOH A . 
E 4 HOH   48  348 396  HOH   HOH A . 
E 4 HOH   49  349 409  HOH   HOH A . 
E 4 HOH   50  350 17   HOH   HOH A . 
E 4 HOH   51  351 320  HOH   HOH A . 
E 4 HOH   52  352 26   HOH   HOH A . 
E 4 HOH   53  353 92   HOH   HOH A . 
E 4 HOH   54  354 42   HOH   HOH A . 
E 4 HOH   55  355 56   HOH   HOH A . 
E 4 HOH   56  356 2    HOH   HOH A . 
E 4 HOH   57  357 93   HOH   HOH A . 
E 4 HOH   58  358 85   HOH   HOH A . 
E 4 HOH   59  359 102  HOH   HOH A . 
E 4 HOH   60  360 19   HOH   HOH A . 
E 4 HOH   61  361 630  HOH   HOH A . 
E 4 HOH   62  362 493  HOH   HOH A . 
E 4 HOH   63  363 66   HOH   HOH A . 
E 4 HOH   64  364 27   HOH   HOH A . 
E 4 HOH   65  365 81   HOH   HOH A . 
E 4 HOH   66  366 138  HOH   HOH A . 
E 4 HOH   67  367 5    HOH   HOH A . 
E 4 HOH   68  368 162  HOH   HOH A . 
E 4 HOH   69  369 154  HOH   HOH A . 
E 4 HOH   70  370 148  HOH   HOH A . 
E 4 HOH   71  371 46   HOH   HOH A . 
E 4 HOH   72  372 6    HOH   HOH A . 
E 4 HOH   73  373 366  HOH   HOH A . 
E 4 HOH   74  374 57   HOH   HOH A . 
E 4 HOH   75  375 186  HOH   HOH A . 
E 4 HOH   76  376 62   HOH   HOH A . 
E 4 HOH   77  377 218  HOH   HOH A . 
E 4 HOH   78  378 45   HOH   HOH A . 
E 4 HOH   79  379 333  HOH   HOH A . 
E 4 HOH   80  380 36   HOH   HOH A . 
E 4 HOH   81  381 49   HOH   HOH A . 
E 4 HOH   82  382 134  HOH   HOH A . 
E 4 HOH   83  383 12   HOH   HOH A . 
E 4 HOH   84  384 116  HOH   HOH A . 
E 4 HOH   85  385 139  HOH   HOH A . 
E 4 HOH   86  386 939  HOH   HOH A . 
E 4 HOH   87  387 35   HOH   HOH A . 
E 4 HOH   88  388 405  HOH   HOH A . 
E 4 HOH   89  389 1134 HOH   HOH A . 
E 4 HOH   90  390 140  HOH   HOH A . 
E 4 HOH   91  391 4    HOH   HOH A . 
E 4 HOH   92  392 83   HOH   HOH A . 
E 4 HOH   93  393 159  HOH   HOH A . 
E 4 HOH   94  394 381  HOH   HOH A . 
E 4 HOH   95  395 58   HOH   HOH A . 
E 4 HOH   96  396 24   HOH   HOH A . 
E 4 HOH   97  397 67   HOH   HOH A . 
E 4 HOH   98  398 1308 HOH   HOH A . 
E 4 HOH   99  399 1315 HOH   HOH A . 
E 4 HOH   100 400 351  HOH   HOH A . 
E 4 HOH   101 401 121  HOH   HOH A . 
E 4 HOH   102 402 74   HOH   HOH A . 
E 4 HOH   103 403 296  HOH   HOH A . 
E 4 HOH   104 404 68   HOH   HOH A . 
E 4 HOH   105 405 51   HOH   HOH A . 
E 4 HOH   106 406 1313 HOH   HOH A . 
E 4 HOH   107 407 303  HOH   HOH A . 
E 4 HOH   108 408 25   HOH   HOH A . 
E 4 HOH   109 409 34   HOH   HOH A . 
E 4 HOH   110 410 115  HOH   HOH A . 
E 4 HOH   111 411 122  HOH   HOH A . 
E 4 HOH   112 412 3    HOH   HOH A . 
E 4 HOH   113 413 53   HOH   HOH A . 
E 4 HOH   114 414 1310 HOH   HOH A . 
E 4 HOH   115 415 78   HOH   HOH A . 
E 4 HOH   116 416 1068 HOH   HOH A . 
E 4 HOH   117 417 1275 HOH   HOH A . 
E 4 HOH   118 418 123  HOH   HOH A . 
E 4 HOH   119 419 397  HOH   HOH A . 
E 4 HOH   120 420 278  HOH   HOH A . 
E 4 HOH   121 421 125  HOH   HOH A . 
E 4 HOH   122 422 7    HOH   HOH A . 
E 4 HOH   123 423 582  HOH   HOH A . 
E 4 HOH   124 424 156  HOH   HOH A . 
E 4 HOH   125 425 95   HOH   HOH A . 
E 4 HOH   126 426 1094 HOH   HOH A . 
E 4 HOH   127 427 1279 HOH   HOH A . 
E 4 HOH   128 428 212  HOH   HOH A . 
E 4 HOH   129 429 1289 HOH   HOH A . 
E 4 HOH   130 430 40   HOH   HOH A . 
E 4 HOH   131 431 1238 HOH   HOH A . 
E 4 HOH   132 432 70   HOH   HOH A . 
E 4 HOH   133 433 1222 HOH   HOH A . 
E 4 HOH   134 434 80   HOH   HOH A . 
E 4 HOH   135 435 16   HOH   HOH A . 
E 4 HOH   136 436 188  HOH   HOH A . 
E 4 HOH   137 437 73   HOH   HOH A . 
E 4 HOH   138 438 71   HOH   HOH A . 
E 4 HOH   139 439 94   HOH   HOH A . 
E 4 HOH   140 440 576  HOH   HOH A . 
E 4 HOH   141 441 944  HOH   HOH A . 
E 4 HOH   142 442 1309 HOH   HOH A . 
E 4 HOH   143 443 1286 HOH   HOH A . 
E 4 HOH   144 444 97   HOH   HOH A . 
E 4 HOH   145 445 104  HOH   HOH A . 
E 4 HOH   146 446 1189 HOH   HOH A . 
E 4 HOH   147 447 952  HOH   HOH A . 
E 4 HOH   148 448 79   HOH   HOH A . 
E 4 HOH   149 449 1296 HOH   HOH A . 
E 4 HOH   150 450 330  HOH   HOH A . 
E 4 HOH   151 451 1    HOH   HOH A . 
E 4 HOH   152 452 509  HOH   HOH A . 
E 4 HOH   153 453 107  HOH   HOH A . 
E 4 HOH   154 454 726  HOH   HOH A . 
E 4 HOH   155 455 163  HOH   HOH A . 
E 4 HOH   156 456 1119 HOH   HOH A . 
E 4 HOH   157 457 408  HOH   HOH A . 
E 4 HOH   158 458 756  HOH   HOH A . 
E 4 HOH   159 459 711  HOH   HOH A . 
E 4 HOH   160 460 126  HOH   HOH A . 
E 4 HOH   161 461 319  HOH   HOH A . 
E 4 HOH   162 462 521  HOH   HOH A . 
E 4 HOH   163 463 1307 HOH   HOH A . 
E 4 HOH   164 464 280  HOH   HOH A . 
E 4 HOH   165 465 361  HOH   HOH A . 
E 4 HOH   166 466 801  HOH   HOH A . 
E 4 HOH   167 467 556  HOH   HOH A . 
E 4 HOH   168 468 1276 HOH   HOH A . 
E 4 HOH   169 469 342  HOH   HOH A . 
E 4 HOH   170 470 63   HOH   HOH A . 
E 4 HOH   171 471 370  HOH   HOH A . 
E 4 HOH   172 472 267  HOH   HOH A . 
E 4 HOH   173 473 250  HOH   HOH A . 
E 4 HOH   174 474 224  HOH   HOH A . 
E 4 HOH   175 475 1287 HOH   HOH A . 
E 4 HOH   176 476 309  HOH   HOH A . 
E 4 HOH   177 477 695  HOH   HOH A . 
E 4 HOH   178 478 135  HOH   HOH A . 
E 4 HOH   179 479 2    HOH   HOH A . 
E 4 HOH   180 480 1306 HOH   HOH A . 
E 4 HOH   181 481 318  HOH   HOH A . 
E 4 HOH   182 482 674  HOH   HOH A . 
E 4 HOH   183 483 1314 HOH   HOH A . 
E 4 HOH   184 484 919  HOH   HOH A . 
E 4 HOH   185 485 202  HOH   HOH A . 
E 4 HOH   186 486 326  HOH   HOH A . 
E 4 HOH   187 487 1299 HOH   HOH A . 
E 4 HOH   188 488 331  HOH   HOH A . 
E 4 HOH   189 489 315  HOH   HOH A . 
E 4 HOH   190 490 1284 HOH   HOH A . 
E 4 HOH   191 491 941  HOH   HOH A . 
E 4 HOH   192 492 805  HOH   HOH A . 
E 4 HOH   193 493 263  HOH   HOH A . 
E 4 HOH   194 494 356  HOH   HOH A . 
E 4 HOH   195 495 152  HOH   HOH A . 
E 4 HOH   196 496 208  HOH   HOH A . 
E 4 HOH   197 497 1071 HOH   HOH A . 
E 4 HOH   198 498 350  HOH   HOH A . 
E 4 HOH   199 499 180  HOH   HOH A . 
E 4 HOH   200 500 363  HOH   HOH A . 
E 4 HOH   201 501 313  HOH   HOH A . 
E 4 HOH   202 502 371  HOH   HOH A . 
E 4 HOH   203 503 376  HOH   HOH A . 
E 4 HOH   204 504 185  HOH   HOH A . 
E 4 HOH   205 505 429  HOH   HOH A . 
E 4 HOH   206 506 772  HOH   HOH A . 
E 4 HOH   207 507 70   HOH   HOH A . 
E 4 HOH   208 508 1074 HOH   HOH A . 
E 4 HOH   209 509 1292 HOH   HOH A . 
E 4 HOH   210 510 346  HOH   HOH A . 
E 4 HOH   211 511 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 240  HOH   HOH B . 
F 4 HOH   3   203 549  HOH   HOH B . 
F 4 HOH   4   204 1249 HOH   HOH B . 
F 4 HOH   5   205 232  HOH   HOH B . 
F 4 HOH   6   206 654  HOH   HOH B . 
F 4 HOH   7   207 398  HOH   HOH B . 
F 4 HOH   8   208 364  HOH   HOH B . 
F 4 HOH   9   209 264  HOH   HOH B . 
F 4 HOH   10  210 50   HOH   HOH B . 
F 4 HOH   11  211 900  HOH   HOH B . 
F 4 HOH   12  212 452  HOH   HOH B . 
F 4 HOH   13  213 205  HOH   HOH B . 
F 4 HOH   14  214 120  HOH   HOH B . 
F 4 HOH   15  215 743  HOH   HOH B . 
F 4 HOH   16  216 353  HOH   HOH B . 
F 4 HOH   17  217 332  HOH   HOH B . 
F 4 HOH   18  218 758  HOH   HOH B . 
F 4 HOH   19  219 276  HOH   HOH B . 
F 4 HOH   20  220 531  HOH   HOH B . 
F 4 HOH   21  221 82   HOH   HOH B . 
F 4 HOH   22  222 131  HOH   HOH B . 
F 4 HOH   23  223 444  HOH   HOH B . 
F 4 HOH   24  224 1278 HOH   HOH B . 
F 4 HOH   25  225 75   HOH   HOH B . 
F 4 HOH   26  226 54   HOH   HOH B . 
F 4 HOH   27  227 325  HOH   HOH B . 
F 4 HOH   28  228 69   HOH   HOH B . 
F 4 HOH   29  229 282  HOH   HOH B . 
F 4 HOH   30  230 252  HOH   HOH B . 
F 4 HOH   31  231 110  HOH   HOH B . 
F 4 HOH   32  232 60   HOH   HOH B . 
F 4 HOH   33  233 1    HOH   HOH B . 
F 4 HOH   34  234 1140 HOH   HOH B . 
F 4 HOH   35  235 166  HOH   HOH B . 
F 4 HOH   36  236 172  HOH   HOH B . 
F 4 HOH   37  237 133  HOH   HOH B . 
F 4 HOH   38  238 127  HOH   HOH B . 
F 4 HOH   39  239 128  HOH   HOH B . 
F 4 HOH   40  240 300  HOH   HOH B . 
F 4 HOH   41  241 181  HOH   HOH B . 
F 4 HOH   42  242 14   HOH   HOH B . 
F 4 HOH   43  243 723  HOH   HOH B . 
F 4 HOH   44  244 41   HOH   HOH B . 
F 4 HOH   45  245 272  HOH   HOH B . 
F 4 HOH   46  246 144  HOH   HOH B . 
F 4 HOH   47  247 391  HOH   HOH B . 
F 4 HOH   48  248 9    HOH   HOH B . 
F 4 HOH   49  249 343  HOH   HOH B . 
F 4 HOH   50  250 52   HOH   HOH B . 
F 4 HOH   51  251 129  HOH   HOH B . 
F 4 HOH   52  252 358  HOH   HOH B . 
F 4 HOH   53  253 31   HOH   HOH B . 
F 4 HOH   54  254 30   HOH   HOH B . 
F 4 HOH   55  255 103  HOH   HOH B . 
F 4 HOH   56  256 150  HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 271  HOH   HOH B . 
F 4 HOH   59  259 59   HOH   HOH B . 
F 4 HOH   60  260 143  HOH   HOH B . 
F 4 HOH   61  261 1312 HOH   HOH B . 
F 4 HOH   62  262 72   HOH   HOH B . 
F 4 HOH   63  263 10   HOH   HOH B . 
F 4 HOH   64  264 61   HOH   HOH B . 
F 4 HOH   65  265 20   HOH   HOH B . 
F 4 HOH   66  266 302  HOH   HOH B . 
F 4 HOH   67  267 243  HOH   HOH B . 
F 4 HOH   68  268 242  HOH   HOH B . 
F 4 HOH   69  269 175  HOH   HOH B . 
F 4 HOH   70  270 11   HOH   HOH B . 
F 4 HOH   71  271 221  HOH   HOH B . 
F 4 HOH   72  272 117  HOH   HOH B . 
F 4 HOH   73  273 207  HOH   HOH B . 
F 4 HOH   74  274 84   HOH   HOH B . 
F 4 HOH   75  275 231  HOH   HOH B . 
F 4 HOH   76  276 114  HOH   HOH B . 
F 4 HOH   77  277 147  HOH   HOH B . 
F 4 HOH   78  278 347  HOH   HOH B . 
F 4 HOH   79  279 43   HOH   HOH B . 
F 4 HOH   80  280 197  HOH   HOH B . 
F 4 HOH   81  281 299  HOH   HOH B . 
F 4 HOH   82  282 77   HOH   HOH B . 
F 4 HOH   83  283 220  HOH   HOH B . 
F 4 HOH   84  284 22   HOH   HOH B . 
F 4 HOH   85  285 1277 HOH   HOH B . 
F 4 HOH   86  286 1066 HOH   HOH B . 
F 4 HOH   87  287 287  HOH   HOH B . 
F 4 HOH   88  288 106  HOH   HOH B . 
F 4 HOH   89  289 89   HOH   HOH B . 
F 4 HOH   90  290 1106 HOH   HOH B . 
F 4 HOH   91  291 99   HOH   HOH B . 
F 4 HOH   92  292 13   HOH   HOH B . 
F 4 HOH   93  293 235  HOH   HOH B . 
F 4 HOH   94  294 316  HOH   HOH B . 
F 4 HOH   95  295 416  HOH   HOH B . 
F 4 HOH   96  296 88   HOH   HOH B . 
F 4 HOH   97  297 216  HOH   HOH B . 
F 4 HOH   98  298 137  HOH   HOH B . 
F 4 HOH   99  299 215  HOH   HOH B . 
F 4 HOH   100 300 160  HOH   HOH B . 
F 4 HOH   101 301 297  HOH   HOH B . 
F 4 HOH   102 302 32   HOH   HOH B . 
F 4 HOH   103 303 311  HOH   HOH B . 
F 4 HOH   104 304 112  HOH   HOH B . 
F 4 HOH   105 305 1305 HOH   HOH B . 
F 4 HOH   106 306 142  HOH   HOH B . 
F 4 HOH   107 307 170  HOH   HOH B . 
F 4 HOH   108 308 1285 HOH   HOH B . 
F 4 HOH   109 309 635  HOH   HOH B . 
F 4 HOH   110 310 37   HOH   HOH B . 
F 4 HOH   111 311 101  HOH   HOH B . 
F 4 HOH   112 312 118  HOH   HOH B . 
F 4 HOH   113 313 177  HOH   HOH B . 
F 4 HOH   114 314 23   HOH   HOH B . 
F 4 HOH   115 315 38   HOH   HOH B . 
F 4 HOH   116 316 387  HOH   HOH B . 
F 4 HOH   117 317 161  HOH   HOH B . 
F 4 HOH   118 318 91   HOH   HOH B . 
F 4 HOH   119 319 182  HOH   HOH B . 
F 4 HOH   120 320 1126 HOH   HOH B . 
F 4 HOH   121 321 48   HOH   HOH B . 
F 4 HOH   122 322 44   HOH   HOH B . 
F 4 HOH   123 323 28   HOH   HOH B . 
F 4 HOH   124 324 100  HOH   HOH B . 
F 4 HOH   125 325 704  HOH   HOH B . 
F 4 HOH   126 326 1291 HOH   HOH B . 
F 4 HOH   127 327 1294 HOH   HOH B . 
F 4 HOH   128 328 334  HOH   HOH B . 
F 4 HOH   129 329 1274 HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 141  HOH   HOH B . 
F 4 HOH   132 332 717  HOH   HOH B . 
F 4 HOH   133 333 98   HOH   HOH B . 
F 4 HOH   134 334 55   HOH   HOH B . 
F 4 HOH   135 335 341  HOH   HOH B . 
F 4 HOH   136 336 1293 HOH   HOH B . 
F 4 HOH   137 337 445  HOH   HOH B . 
F 4 HOH   138 338 234  HOH   HOH B . 
F 4 HOH   139 339 339  HOH   HOH B . 
F 4 HOH   140 340 65   HOH   HOH B . 
F 4 HOH   141 341 362  HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 1304 HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 960  HOH   HOH B . 
F 4 HOH   147 347 87   HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 463  HOH   HOH B . 
F 4 HOH   150 350 623  HOH   HOH B . 
F 4 HOH   151 351 1280 HOH   HOH B . 
F 4 HOH   152 352 203  HOH   HOH B . 
F 4 HOH   153 353 1046 HOH   HOH B . 
F 4 HOH   154 354 335  HOH   HOH B . 
F 4 HOH   155 355 304  HOH   HOH B . 
F 4 HOH   156 356 541  HOH   HOH B . 
F 4 HOH   157 357 290  HOH   HOH B . 
F 4 HOH   158 358 479  HOH   HOH B . 
F 4 HOH   159 359 1077 HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 718  HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 291  HOH   HOH B . 
F 4 HOH   165 365 1316 HOH   HOH B . 
F 4 HOH   166 366 615  HOH   HOH B . 
F 4 HOH   167 367 898  HOH   HOH B . 
F 4 HOH   168 368 340  HOH   HOH B . 
F 4 HOH   169 369 667  HOH   HOH B . 
F 4 HOH   170 370 373  HOH   HOH B . 
F 4 HOH   171 371 190  HOH   HOH B . 
F 4 HOH   172 372 431  HOH   HOH B . 
F 4 HOH   173 373 1303 HOH   HOH B . 
F 4 HOH   174 374 1173 HOH   HOH B . 
F 4 HOH   175 375 310  HOH   HOH B . 
F 4 HOH   176 376 183  HOH   HOH B . 
F 4 HOH   177 377 149  HOH   HOH B . 
F 4 HOH   178 378 418  HOH   HOH B . 
F 4 HOH   179 379 1000 HOH   HOH B . 
F 4 HOH   180 380 1163 HOH   HOH B . 
F 4 HOH   181 381 176  HOH   HOH B . 
F 4 HOH   182 382 491  HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 1311 HOH   HOH B . 
F 4 HOH   185 385 981  HOH   HOH B . 
F 4 HOH   186 386 470  HOH   HOH B . 
F 4 HOH   187 387 1298 HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 355  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 274  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 314  HOH   HOH B . 
F 4 HOH   197 397 157  HOH   HOH B . 
F 4 HOH   198 398 321  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 558  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           7HD3 
_cell.length_a           88.820 
_cell.length_b           88.820 
_cell.length_c           39.511 
_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                         7HD3 
_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          7HD3 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.71 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HD3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.010 
_reflns.number_obs                   160679 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.054 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.300 
_reflns.B_iso_Wilson_estimate        12.540 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.058 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1026118 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.010 1.030  ? 36980 7362 ? 2.332 ? ? ? 5.000 ? 0.500  ? ? ? ? ? ? 93.300 2.601 1.127 0.346 
1 2 5.530 44.410 ? 7355  1070 ? 0.026 ? ? ? 6.900 ? 50.600 ? ? ? ? ? ? 99.800 0.028 0.010 0.999 
# 
_refine.entry_id                                 7HD3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0100 
_refine.ls_d_res_low                             39.7200 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3400 
_refine.ls_number_reflns_obs                     160060 
_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                          0.1528 
_refine.ls_R_factor_R_work                       0.1520 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1690 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7713 
_refine.ls_number_reflns_R_work                  152347 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.7365 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1400 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                82.260 
_refine.B_iso_min                                9.190 
_refine.pdbx_overall_phase_error                 20.0400 
_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                        39.7200 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             411 
_refine_hist.number_atoms_total               3001 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           20.96 
_refine_hist.pdbx_B_iso_mean_solvent          31.55 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0100 1.0200  30 83.0000  4231 . 0.4646 0.4942 . 201 0.0000 4432 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 99.0000  5122 . 0.4034 0.3927 . 214 0.0000 5336 . 'X-RAY DIFFRACTION' 
1.0300 1.0500  30 100.0000 5012 . 0.3432 0.3392 . 291 0.0000 5303 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5030 . 0.3033 0.3047 . 292 0.0000 5322 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5094 . 0.2776 0.3051 . 266 0.0000 5360 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5072 . 0.2803 0.2841 . 239 0.0000 5311 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5105 . 0.2500 0.2792 . 258 0.0000 5363 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5035 . 0.2276 0.2587 . 277 0.0000 5312 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5136 . 0.2096 0.2472 . 207 0.0000 5343 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5126 . 0.1911 0.1919 . 262 0.0000 5388 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5061 . 0.1692 0.2059 . 264 0.0000 5325 . 'X-RAY DIFFRACTION' 
1.1800 1.2000  30 100.0000 5106 . 0.1567 0.1901 . 259 0.0000 5365 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5000 . 0.1424 0.1779 . 278 0.0000 5278 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5147 . 0.1385 0.1679 . 242 0.0000 5389 . 'X-RAY DIFFRACTION' 
1.2500 1.2700  30 100.0000 5119 . 0.1405 0.1672 . 234 0.0000 5353 . 'X-RAY DIFFRACTION' 
1.2700 1.3000  30 100.0000 5071 . 0.1402 0.1636 . 248 0.0000 5319 . 'X-RAY DIFFRACTION' 
1.3000 1.3400  30 100.0000 5080 . 0.1390 0.1639 . 294 0.0000 5374 . 'X-RAY DIFFRACTION' 
1.3400 1.3700  30 100.0000 5092 . 0.1426 0.1531 . 268 0.0000 5360 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5152 . 0.1398 0.1847 . 226 0.0000 5378 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5043 . 0.1320 0.1681 . 272 0.0000 5315 . 'X-RAY DIFFRACTION' 
1.4600 1.5100  30 100.0000 5148 . 0.1238 0.1331 . 244 0.0000 5392 . 'X-RAY DIFFRACTION' 
1.5100 1.5700  30 100.0000 5113 . 0.1205 0.1327 . 273 0.0000 5386 . 'X-RAY DIFFRACTION' 
1.5700 1.6400  30 100.0000 5088 . 0.1230 0.1362 . 266 0.0000 5354 . 'X-RAY DIFFRACTION' 
1.6400 1.7300  30 100.0000 5162 . 0.1314 0.1607 . 231 0.0000 5393 . 'X-RAY DIFFRACTION' 
1.7300 1.8400  30 100.0000 5096 . 0.1361 0.1483 . 264 0.0000 5360 . 'X-RAY DIFFRACTION' 
1.8400 1.9800  30 100.0000 5142 . 0.1371 0.1463 . 281 0.0000 5423 . 'X-RAY DIFFRACTION' 
1.9800 2.1800  30 100.0000 5110 . 0.1396 0.1514 . 279 0.0000 5389 . 'X-RAY DIFFRACTION' 
2.1800 2.4900  30 100.0000 5159 . 0.1374 0.1378 . 264 0.0000 5423 . 'X-RAY DIFFRACTION' 
2.4900 3.1400  30 100.0000 5185 . 0.1507 0.1685 . 257 0.0000 5442 . 'X-RAY DIFFRACTION' 
3.1400 39.7200 30 100.0000 5310 . 0.1517 0.1766 . 262 0.0000 5572 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HD3 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003707' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HD3 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HD3 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HD3 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 7HD3 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HD3 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HD3 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HD3 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N 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                   7HD3 
_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 O B HOH 220 ? ? O B HOH 280 ? ? 2.05 
2 1 O A HOH 393 ? ? O A HOH 476 ? ? 2.17 
# 
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 ? ? 56.59 -133.17 
2 1 HIS B 86 ? ? 56.88 -127.17 
# 
_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 509 ? 5.88 . 
2 1 O ? A HOH 510 ? 5.97 . 
3 1 O ? A HOH 511 ? 7.65 . 
4 1 O ? B HOH 400 ? 6.29 . 
# 
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 
A1A61 N2   N Y N 1   
A1A61 C3   C N N 2   
A1A61 C6   C N N 3   
A1A61 C9   C N N 4   
A1A61 C12  C Y N 5   
A1A61 C14  C Y N 6   
A1A61 C1   C N N 7   
A1A61 C10  C Y N 8   
A1A61 C11  C Y N 9   
A1A61 C13  C Y N 10  
A1A61 C15  C Y N 11  
A1A61 C2   C N S 12  
A1A61 C4   C N N 13  
A1A61 C5   C N N 14  
A1A61 C7   C N N 15  
A1A61 C8   C N N 16  
A1A61 N1   N N N 17  
A1A61 N3   N Y N 18  
A1A61 N4   N Y N 19  
A1A61 O1   O N N 20  
A1A61 O2   O N N 21  
A1A61 H5   H N N 22  
A1A61 H6   H N N 23  
A1A61 H9   H N N 24  
A1A61 H10  H N N 25  
A1A61 H16  H N N 26  
A1A61 H15  H N N 27  
A1A61 H18  H N N 28  
A1A61 H4   H N N 29  
A1A61 H3   H N N 30  
A1A61 H17  H N N 31  
A1A61 H19  H N N 32  
A1A61 H1   H N N 33  
A1A61 H8   H N N 34  
A1A61 H7   H N N 35  
A1A61 H11  H N N 36  
A1A61 H12  H N N 37  
A1A61 H14  H N N 38  
A1A61 H13  H N N 39  
A1A61 H20  H N N 40  
A1A61 H2   H N N 41  
ALA   N    N N N 42  
ALA   CA   C N S 43  
ALA   C    C N N 44  
ALA   O    O N N 45  
ALA   CB   C N N 46  
ALA   OXT  O N N 47  
ALA   H    H N N 48  
ALA   H2   H N N 49  
ALA   HA   H N N 50  
ALA   HB1  H N N 51  
ALA   HB2  H N N 52  
ALA   HB3  H N N 53  
ALA   HXT  H N N 54  
ARG   N    N N N 55  
ARG   CA   C N S 56  
ARG   C    C N N 57  
ARG   O    O N N 58  
ARG   CB   C N N 59  
ARG   CG   C N N 60  
ARG   CD   C N N 61  
ARG   NE   N N N 62  
ARG   CZ   C N N 63  
ARG   NH1  N N N 64  
ARG   NH2  N N N 65  
ARG   OXT  O N N 66  
ARG   H    H N N 67  
ARG   H2   H N N 68  
ARG   HA   H N N 69  
ARG   HB2  H N N 70  
ARG   HB3  H N N 71  
ARG   HG2  H N N 72  
ARG   HG3  H N N 73  
ARG   HD2  H N N 74  
ARG   HD3  H N N 75  
ARG   HE   H N N 76  
ARG   HH11 H N N 77  
ARG   HH12 H N N 78  
ARG   HH21 H N N 79  
ARG   HH22 H N N 80  
ARG   HXT  H N N 81  
ASN   N    N N N 82  
ASN   CA   C N S 83  
ASN   C    C N N 84  
ASN   O    O N N 85  
ASN   CB   C N N 86  
ASN   CG   C N N 87  
ASN   OD1  O N N 88  
ASN   ND2  N N N 89  
ASN   OXT  O N N 90  
ASN   H    H N N 91  
ASN   H2   H N N 92  
ASN   HA   H N N 93  
ASN   HB2  H N N 94  
ASN   HB3  H N N 95  
ASN   HD21 H N N 96  
ASN   HD22 H N N 97  
ASN   HXT  H N N 98  
ASP   N    N N N 99  
ASP   CA   C N S 100 
ASP   C    C N N 101 
ASP   O    O N N 102 
ASP   CB   C N N 103 
ASP   CG   C N N 104 
ASP   OD1  O N N 105 
ASP   OD2  O N N 106 
ASP   OXT  O N N 107 
ASP   H    H N N 108 
ASP   H2   H N N 109 
ASP   HA   H N N 110 
ASP   HB2  H N N 111 
ASP   HB3  H N N 112 
ASP   HD2  H N N 113 
ASP   HXT  H N N 114 
CYS   N    N N N 115 
CYS   CA   C N R 116 
CYS   C    C N N 117 
CYS   O    O N N 118 
CYS   CB   C N N 119 
CYS   SG   S N N 120 
CYS   OXT  O N N 121 
CYS   H    H N N 122 
CYS   H2   H N N 123 
CYS   HA   H N N 124 
CYS   HB2  H N N 125 
CYS   HB3  H N N 126 
CYS   HG   H N N 127 
CYS   HXT  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
HIS   N    N N N 178 
HIS   CA   C N S 179 
HIS   C    C N N 180 
HIS   O    O N N 181 
HIS   CB   C N N 182 
HIS   CG   C Y N 183 
HIS   ND1  N Y N 184 
HIS   CD2  C Y N 185 
HIS   CE1  C Y N 186 
HIS   NE2  N Y N 187 
HIS   OXT  O N N 188 
HIS   H    H N N 189 
HIS   H2   H N N 190 
HIS   HA   H N N 191 
HIS   HB2  H N N 192 
HIS   HB3  H N N 193 
HIS   HD1  H N N 194 
HIS   HD2  H N N 195 
HIS   HE1  H N N 196 
HIS   HE2  H N N 197 
HIS   HXT  H N N 198 
HOH   O    O N N 199 
HOH   H1   H N N 200 
HOH   H2   H N N 201 
ILE   N    N N N 202 
ILE   CA   C N S 203 
ILE   C    C N N 204 
ILE   O    O N N 205 
ILE   CB   C N S 206 
ILE   CG1  C N N 207 
ILE   CG2  C N N 208 
ILE   CD1  C N N 209 
ILE   OXT  O N N 210 
ILE   H    H N N 211 
ILE   H2   H N N 212 
ILE   HA   H N N 213 
ILE   HB   H N N 214 
ILE   HG12 H N N 215 
ILE   HG13 H N N 216 
ILE   HG21 H N N 217 
ILE   HG22 H N N 218 
ILE   HG23 H N N 219 
ILE   HD11 H N N 220 
ILE   HD12 H N N 221 
ILE   HD13 H N N 222 
ILE   HXT  H N N 223 
LEU   N    N N N 224 
LEU   CA   C N S 225 
LEU   C    C N N 226 
LEU   O    O N N 227 
LEU   CB   C N N 228 
LEU   CG   C N N 229 
LEU   CD1  C N N 230 
LEU   CD2  C N N 231 
LEU   OXT  O N N 232 
LEU   H    H N N 233 
LEU   H2   H N N 234 
LEU   HA   H N N 235 
LEU   HB2  H N N 236 
LEU   HB3  H N N 237 
LEU   HG   H N N 238 
LEU   HD11 H N N 239 
LEU   HD12 H N N 240 
LEU   HD13 H N N 241 
LEU   HD21 H N N 242 
LEU   HD22 H N N 243 
LEU   HD23 H N N 244 
LEU   HXT  H N N 245 
LYS   N    N N N 246 
LYS   CA   C N S 247 
LYS   C    C N N 248 
LYS   O    O N N 249 
LYS   CB   C N N 250 
LYS   CG   C N N 251 
LYS   CD   C N N 252 
LYS   CE   C N N 253 
LYS   NZ   N N N 254 
LYS   OXT  O N N 255 
LYS   H    H N N 256 
LYS   H2   H N N 257 
LYS   HA   H N N 258 
LYS   HB2  H N N 259 
LYS   HB3  H N N 260 
LYS   HG2  H N N 261 
LYS   HG3  H N N 262 
LYS   HD2  H N N 263 
LYS   HD3  H N N 264 
LYS   HE2  H N N 265 
LYS   HE3  H N N 266 
LYS   HZ1  H N N 267 
LYS   HZ2  H N N 268 
LYS   HZ3  H N N 269 
LYS   HXT  H N N 270 
MET   N    N N N 271 
MET   CA   C N S 272 
MET   C    C N N 273 
MET   O    O N N 274 
MET   CB   C N N 275 
MET   CG   C N N 276 
MET   SD   S N N 277 
MET   CE   C N N 278 
MET   OXT  O N N 279 
MET   H    H N N 280 
MET   H2   H N N 281 
MET   HA   H N N 282 
MET   HB2  H N N 283 
MET   HB3  H N N 284 
MET   HG2  H N N 285 
MET   HG3  H N N 286 
MET   HE1  H N N 287 
MET   HE2  H N N 288 
MET   HE3  H N N 289 
MET   HXT  H N N 290 
PHE   N    N N N 291 
PHE   CA   C N S 292 
PHE   C    C N N 293 
PHE   O    O N N 294 
PHE   CB   C N N 295 
PHE   CG   C Y N 296 
PHE   CD1  C Y N 297 
PHE   CD2  C Y N 298 
PHE   CE1  C Y N 299 
PHE   CE2  C Y N 300 
PHE   CZ   C Y N 301 
PHE   OXT  O N N 302 
PHE   H    H N N 303 
PHE   H2   H N N 304 
PHE   HA   H N N 305 
PHE   HB2  H N N 306 
PHE   HB3  H N N 307 
PHE   HD1  H N N 308 
PHE   HD2  H N N 309 
PHE   HE1  H N N 310 
PHE   HE2  H N N 311 
PHE   HZ   H N N 312 
PHE   HXT  H N N 313 
PRO   N    N N N 314 
PRO   CA   C N S 315 
PRO   C    C N N 316 
PRO   O    O N N 317 
PRO   CB   C N N 318 
PRO   CG   C N N 319 
PRO   CD   C N N 320 
PRO   OXT  O N N 321 
PRO   H    H N N 322 
PRO   HA   H N N 323 
PRO   HB2  H N N 324 
PRO   HB3  H N N 325 
PRO   HG2  H N N 326 
PRO   HG3  H N N 327 
PRO   HD2  H N N 328 
PRO   HD3  H N N 329 
PRO   HXT  H N N 330 
SER   N    N N N 331 
SER   CA   C N S 332 
SER   C    C N N 333 
SER   O    O N N 334 
SER   CB   C N N 335 
SER   OG   O N N 336 
SER   OXT  O N N 337 
SER   H    H N N 338 
SER   H2   H N N 339 
SER   HA   H N N 340 
SER   HB2  H N N 341 
SER   HB3  H N N 342 
SER   HG   H N N 343 
SER   HXT  H N N 344 
TFA   C1   C N N 345 
TFA   C2   C N N 346 
TFA   O    O N N 347 
TFA   F1   F N N 348 
TFA   F2   F N N 349 
TFA   F3   F N N 350 
TFA   OXT  O N N 351 
TFA   HXT  H N N 352 
THR   N    N N N 353 
THR   CA   C N S 354 
THR   C    C N N 355 
THR   O    O N N 356 
THR   CB   C N R 357 
THR   OG1  O N N 358 
THR   CG2  C N N 359 
THR   OXT  O N N 360 
THR   H    H N N 361 
THR   H2   H N N 362 
THR   HA   H N N 363 
THR   HB   H N N 364 
THR   HG1  H N N 365 
THR   HG21 H N N 366 
THR   HG22 H N N 367 
THR   HG23 H N N 368 
THR   HXT  H N N 369 
TYR   N    N N N 370 
TYR   CA   C N S 371 
TYR   C    C N N 372 
TYR   O    O N N 373 
TYR   CB   C N N 374 
TYR   CG   C Y N 375 
TYR   CD1  C Y N 376 
TYR   CD2  C Y N 377 
TYR   CE1  C Y N 378 
TYR   CE2  C Y N 379 
TYR   CZ   C Y N 380 
TYR   OH   O N N 381 
TYR   OXT  O N N 382 
TYR   H    H N N 383 
TYR   H2   H N N 384 
TYR   HA   H N N 385 
TYR   HB2  H N N 386 
TYR   HB3  H N N 387 
TYR   HD1  H N N 388 
TYR   HD2  H N N 389 
TYR   HE1  H N N 390 
TYR   HE2  H N N 391 
TYR   HH   H N N 392 
TYR   HXT  H N N 393 
VAL   N    N N N 394 
VAL   CA   C N S 395 
VAL   C    C N N 396 
VAL   O    O N N 397 
VAL   CB   C N N 398 
VAL   CG1  C N N 399 
VAL   CG2  C N N 400 
VAL   OXT  O N N 401 
VAL   H    H N N 402 
VAL   H2   H N N 403 
VAL   HA   H N N 404 
VAL   HB   H N N 405 
VAL   HG11 H N N 406 
VAL   HG12 H N N 407 
VAL   HG13 H N N 408 
VAL   HG21 H N N 409 
VAL   HG22 H N N 410 
VAL   HG23 H N N 411 
VAL   HXT  H N N 412 
# 
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 
A1A61 C6  O2   sing N N 1   
A1A61 C6  C5   sing N N 2   
A1A61 O2  C7   sing N N 3   
A1A61 C5  C4   sing N N 4   
A1A61 C7  C8   sing N N 5   
A1A61 C3  C4   sing N N 6   
A1A61 C3  C2   sing N N 7   
A1A61 C4  C8   sing N N 8   
A1A61 C4  C9   sing N N 9   
A1A61 C9  N1   sing N N 10  
A1A61 C2  C1   sing N N 11  
A1A61 C2  N1   sing N N 12  
A1A61 C1  O1   sing N N 13  
A1A61 N1  C10  sing N N 14  
A1A61 C10 C13  doub Y N 15  
A1A61 C10 N2   sing Y N 16  
A1A61 C14 C13  sing Y N 17  
A1A61 C14 C15  doub Y N 18  
A1A61 C13 C12  sing Y N 19  
A1A61 N2  C11  doub Y N 20  
A1A61 C15 N4   sing Y N 21  
A1A61 C12 N4   sing Y N 22  
A1A61 C12 N3   doub Y N 23  
A1A61 C11 N3   sing Y N 24  
A1A61 C3  H5   sing N N 25  
A1A61 C3  H6   sing N N 26  
A1A61 C6  H9   sing N N 27  
A1A61 C6  H10  sing N N 28  
A1A61 C9  H16  sing N N 29  
A1A61 C9  H15  sing N N 30  
A1A61 C14 H18  sing N N 31  
A1A61 C1  H4   sing N N 32  
A1A61 C1  H3   sing N N 33  
A1A61 C11 H17  sing N N 34  
A1A61 C15 H19  sing N N 35  
A1A61 C2  H1   sing N N 36  
A1A61 C5  H8   sing N N 37  
A1A61 C5  H7   sing N N 38  
A1A61 C7  H11  sing N N 39  
A1A61 C7  H12  sing N N 40  
A1A61 C8  H14  sing N N 41  
A1A61 C8  H13  sing N N 42  
A1A61 N4  H20  sing N N 43  
A1A61 O1  H2   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
TFA   C1  C2   sing N N 334 
TFA   C1  O    doub N N 335 
TFA   C1  OXT  sing N N 336 
TFA   C2  F1   sing N N 337 
TFA   C2  F2   sing N N 338 
TFA   C2  F3   sing N N 339 
TFA   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TYR   N   CA   sing N N 357 
TYR   N   H    sing N N 358 
TYR   N   H2   sing N N 359 
TYR   CA  C    sing N N 360 
TYR   CA  CB   sing N N 361 
TYR   CA  HA   sing N N 362 
TYR   C   O    doub N N 363 
TYR   C   OXT  sing N N 364 
TYR   CB  CG   sing N N 365 
TYR   CB  HB2  sing N N 366 
TYR   CB  HB3  sing N N 367 
TYR   CG  CD1  doub Y N 368 
TYR   CG  CD2  sing Y N 369 
TYR   CD1 CE1  sing Y N 370 
TYR   CD1 HD1  sing N N 371 
TYR   CD2 CE2  doub Y N 372 
TYR   CD2 HD2  sing N N 373 
TYR   CE1 CZ   doub Y N 374 
TYR   CE1 HE1  sing N N 375 
TYR   CE2 CZ   sing Y N 376 
TYR   CE2 HE2  sing N N 377 
TYR   CZ  OH   sing N N 378 
TYR   OH  HH   sing N N 379 
TYR   OXT HXT  sing N N 380 
VAL   N   CA   sing N N 381 
VAL   N   H    sing N N 382 
VAL   N   H2   sing N N 383 
VAL   CA  C    sing N N 384 
VAL   CA  CB   sing N N 385 
VAL   CA  HA   sing N N 386 
VAL   C   O    doub N N 387 
VAL   C   OXT  sing N N 388 
VAL   CB  CG1  sing N N 389 
VAL   CB  CG2  sing N N 390 
VAL   CB  HB   sing N N 391 
VAL   CG1 HG11 sing N N 392 
VAL   CG1 HG12 sing N N 393 
VAL   CG1 HG13 sing N N 394 
VAL   CG2 HG21 sing N N 395 
VAL   CG2 HG22 sing N N 396 
VAL   CG2 HG23 sing N N 397 
VAL   OXT HXT  sing N N 398 
# 
_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                    7HD3 
_atom_sites.fract_transf_matrix[1][1]   0.011259 
_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]   0.011259 
_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]   0.025309 
_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 
F 
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   ? 19.628 -16.219 22.185  0.58 54.06 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.634 -15.962 22.325  0.42 52.80 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.656 -15.146 22.352  0.58 53.61 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.641 -14.908 22.493  0.42 52.37 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.306 -13.796 22.064  0.58 51.98 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.258 -13.550 22.175  0.42 50.75 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.417 -13.524 22.521  0.58 52.50 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.348 -13.229 22.650  0.42 51.24 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.020 -15.179 23.759  0.58 54.44 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.039 -14.929 23.912  0.42 53.22 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.989 -14.069 23.908  0.58 54.67 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.980 -13.845 24.056  0.42 53.47 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.386 -16.538 24.024  0.58 54.69 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.452 -16.299 24.224  0.42 53.48 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.943 -15.268 21.710  0.58 64.31 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.917 -15.058 21.869  0.42 62.82 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.711 -15.038 24.425  0.58 65.31 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.740 -14.751 24.558  0.42 63.84 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.484 -14.216 24.723  0.58 65.57 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.500 -13.982 24.888  0.42 64.14 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.446 -13.215 23.953  0.58 65.57 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.413 -12.977 24.065  0.42 64.14 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.393 -14.087 23.143  0.58 65.57 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.366 -13.903 23.307  0.42 64.14 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.931 -16.513 24.880  0.58 65.61 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.009 -16.264 25.086  0.42 64.15 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.750 -16.732 23.317  0.58 65.61 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.813 -16.532 23.533  0.42 64.15 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.081 -17.214 24.039  0.58 65.61 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.168 -16.953 24.247  0.42 64.15 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.613 -12.959 21.295  0.58 49.43 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.558 -12.756 21.366  0.42 48.24 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.054 -11.600 21.004  0.58 46.54 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.989 -11.408 21.018  0.42 45.44 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.899 -10.633 21.249  0.58 43.83 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.848 -10.430 21.287  0.42 42.74 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.786 -11.036 21.602  0.58 43.91 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.764 -10.813 21.736  0.42 42.84 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.625 -11.479 19.583  0.58 46.08 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.499 -11.327 19.572  0.42 45.10 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.638 -11.899 18.515  0.58 45.53 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.464 -11.760 18.557  0.42 44.69 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.498 -11.436 18.486  0.58 45.34 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.333 -11.273 18.556  0.42 44.55 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.074 -12.787 17.626  0.58 45.38 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.847 -12.685 17.684  0.42 44.57 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.866 -13.165 20.921  0.58 59.29 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.812 -12.986 21.004  0.42 57.86 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.763 -11.371 21.619  0.58 55.83 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.725 -11.166 21.593  0.42 54.50 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.869 -10.553 19.419  0.58 55.28 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.748 -10.409 19.375  0.42 54.09 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.408 -12.045 19.508  0.58 55.28 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.272 -11.905 19.476  0.42 54.09 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.556 -13.058 16.996  0.58 54.43 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.300 -12.965 17.084  0.42 53.46 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.878 -13.091 17.680  0.58 54.43 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.646 -13.005 17.719  0.42 53.46 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.170 -9.342  21.059  0.58 40.76 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.099 -9.151  21.005  0.42 39.72 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.245 -8.281  21.435  0.58 37.61 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.197 -8.073  21.390  0.42 36.65 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.406 -7.766  20.270  0.58 33.94 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.330 -7.570  20.239  0.42 33.18 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.750 -6.728  20.407  0.58 34.13 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.689 -6.523  20.376  0.42 33.28 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.003 -7.120  22.084  0.58 38.19 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.984 -6.910  21.995  0.42 37.07 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 18.962 -6.577  21.194  0.58 38.50 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.868 -6.342  21.045  0.42 37.28 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.898 -9.056  20.702  0.58 48.89 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.797 -8.883  20.581  0.42 47.64 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.638 -8.633  22.104  0.58 45.11 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.605 -8.407  22.080  0.42 43.95 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.369 -6.426  22.325  0.58 45.80 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.360 -6.229  22.293  0.42 44.46 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.455 -7.444  22.880  0.58 45.80 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.500 -7.237  22.749  0.42 44.46 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.371 -5.943  21.567  0.58 46.18 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.291 -5.704  21.393  0.42 44.71 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.411 -8.454  19.131  0.58 29.67 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.295 -8.279  19.115  0.42 29.32 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.509 -8.092  18.046  0.58 25.73 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.385 -7.909  18.039  0.42 25.68 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.080 -8.471  18.418  0.58 25.45 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.954 -8.263  18.428  0.42 25.09 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.826 -9.566  18.926  0.58 26.72 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.693 -9.336  18.979  0.42 25.98 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.918 -8.813  16.763  0.58 23.04 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.774 -8.632  16.751  0.42 23.36 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.201 -8.302  16.163  0.58 21.21 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.081 -8.168  16.165  0.42 21.81 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.220 -7.122  15.442  0.58 20.45 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.145 -7.002  15.422  0.42 21.11 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.383 -9.009  16.314  0.58 21.60 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.240 -8.902  16.352  0.42 21.94 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.396 -6.650  14.886  0.58 20.48 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.343 -6.572  14.879  0.42 21.01 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.558 -8.545  15.758  0.58 21.67 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.439 -8.480  15.811  0.42 21.88 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.565 -7.363  15.044  0.58 20.99 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.490 -7.312  15.074  0.42 21.33 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.919 -9.128  18.966  0.58 35.58 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.780 -8.972  18.953  0.42 35.17 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.546 -7.139  17.897  0.58 30.85 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.435 -6.956  17.888  0.42 30.79 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.035 -9.758  16.960  0.58 27.62 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.852 -9.581  16.937  0.42 28.01 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.216 -8.701  16.105  0.58 27.62 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.082 -8.484  16.089  0.42 28.01 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.433 -6.640  15.333  0.58 24.52 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.374 -6.500  15.288  0.42 25.31 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.382 -9.807  16.798  0.58 25.89 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.210 -9.689  16.849  0.42 26.30 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.398 -5.856  14.403  0.58 24.55 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.374 -5.786  14.382  0.42 25.19 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.348 -9.027  15.870  0.58 25.98 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.214 -8.979  15.945  0.42 26.24 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.357 -7.049  14.671  0.58 25.16 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.296 -7.025  14.709  0.42 25.57 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.139 -7.560  18.160  0.58 24.38 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.020 -7.355  18.142  0.42 23.92 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.767 -7.706  18.634  0.58 24.28 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.649 -7.479  18.621  0.42 23.48 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.768 -7.420  17.518  0.58 22.16 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.651 -7.287  17.487  0.42 21.38 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 10.978 -6.525  16.696  0.58 22.42 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.813 -6.401  16.645  0.42 21.27 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.507 -6.751  19.809  0.58 26.34 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.370 -6.447  19.722  0.42 25.22 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.153 -6.801  20.219  0.58 28.07 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.083 -6.635  20.279  0.42 26.84 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.276 -6.845  17.704  0.58 29.23 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.163 -6.652  17.667  0.42 28.68 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.624 -8.612  18.946  0.58 29.11 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.519 -8.364  18.995  0.42 28.16 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.070 -7.011  20.557  0.58 31.58 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.040 -6.541  20.419  0.42 30.24 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.725 -5.846  19.534  0.58 31.58 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.415 -5.558  19.339  0.42 30.24 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.028 -6.268  20.857  0.58 33.66 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 9.948  -6.073  20.887  0.42 32.18 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.673  -8.183  17.506  0.58 20.34 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.608  -8.117  17.481  0.42 19.71 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.584  -7.931  16.582  0.58 19.32 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.515  -7.944  16.545  0.42 18.83 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.793  -8.424  15.170  0.58 17.91 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.760  -8.456  15.146  0.42 17.67 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.056  -8.010  14.269  0.58 18.78 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.013  -8.091  14.232  0.42 18.26 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.542  -8.849  18.031  0.58 24.38 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.513  -8.784  18.014  0.42 23.63 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.781  -8.351  16.932  0.58 23.16 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.733  -8.399  16.894  0.42 22.57 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.425  -6.976  16.541  0.58 23.16 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.307  -6.999  16.482  0.42 22.57 ?  8   GLY   A HA3  1 
ATOM   157  N N    . TYR   A 1 9   ? 9.773  -9.295  14.942  1.00 16.89 ?  9   TYR   A N    1 
ATOM   158  C CA   . TYR   A 1 9   ? 10.045 -9.826  13.615  1.00 15.51 ?  9   TYR   A CA   1 
ATOM   159  C C    . TYR   A 1 9   ? 9.192  -11.055 13.334  1.00 14.93 ?  9   TYR   A C    1 
ATOM   160  O O    . TYR   A 1 9   ? 8.935  -11.879 14.217  1.00 16.43 ?  9   TYR   A O    1 
ATOM   161  C CB   . TYR   A 1 9   ? 11.528 -10.200 13.464  1.00 15.65 ?  9   TYR   A CB   1 
ATOM   162  C CG   . TYR   A 1 9   ? 12.443 -9.002  13.300  1.00 15.63 ?  9   TYR   A CG   1 
ATOM   163  C CD1  . TYR   A 1 9   ? 12.752 -8.201  14.384  1.00 16.19 ?  9   TYR   A CD1  1 
ATOM   164  C CD2  . TYR   A 1 9   ? 12.970 -8.666  12.062  1.00 15.31 ?  9   TYR   A CD2  1 
ATOM   165  C CE1  . TYR   A 1 9   ? 13.563 -7.092  14.244  1.00 17.18 ?  9   TYR   A CE1  1 
ATOM   166  C CE2  . TYR   A 1 9   ? 13.782 -7.559  11.911  1.00 16.03 ?  9   TYR   A CE2  1 
ATOM   167  C CZ   . TYR   A 1 9   ? 14.076 -6.779  13.002  1.00 16.95 ?  9   TYR   A CZ   1 
ATOM   168  O OH   . TYR   A 1 9   ? 14.873 -5.679  12.844  1.00 18.74 ?  9   TYR   A OH   1 
ATOM   169  H H    A TYR   A 1 9   ? 10.299 -9.600  15.550  0.58 20.24 ?  9   TYR   A H    1 
ATOM   170  H H    B TYR   A 1 9   ? 10.308 -9.576  15.554  0.42 20.24 ?  9   TYR   A H    1 
ATOM   171  H HA   . TYR   A 1 9   ? 9.838  -9.150  12.952  1.00 18.58 ?  9   TYR   A HA   1 
ATOM   172  H HB2  . TYR   A 1 9   ? 11.807 -10.699 14.249  1.00 18.75 ?  9   TYR   A HB2  1 
ATOM   173  H HB3  . TYR   A 1 9   ? 11.615 -10.759 12.673  1.00 18.75 ?  9   TYR   A HB3  1 
ATOM   174  H HD1  . TYR   A 1 9   ? 12.390 -8.418  15.224  1.00 19.40 ?  9   TYR   A HD1  1 
ATOM   175  H HD2  . TYR   A 1 9   ? 12.771 -9.196  11.321  1.00 18.35 ?  9   TYR   A HD2  1 
ATOM   176  H HE1  . TYR   A 1 9   ? 13.758 -6.572  14.988  1.00 20.60 ?  9   TYR   A HE1  1 
ATOM   177  H HE2  . TYR   A 1 9   ? 14.139 -7.352  11.080  1.00 19.21 ?  9   TYR   A HE2  1 
ATOM   178  H HH   . TYR   A 1 9   ? 14.992 -5.307  13.590  1.00 22.46 ?  9   TYR   A HH   1 
ATOM   179  N N    . LEU   A 1 10  ? 8.765  -11.171 12.087  1.00 14.50 ?  10  LEU   A N    1 
ATOM   180  C CA   . LEU   A 1 10  ? 8.160  -12.396 11.592  1.00 14.31 ?  10  LEU   A CA   1 
ATOM   181  C C    . LEU   A 1 10  ? 9.282  -13.343 11.167  1.00 14.02 ?  10  LEU   A C    1 
ATOM   182  O O    . LEU   A 1 10  ? 10.240 -12.922 10.512  1.00 14.06 ?  10  LEU   A O    1 
ATOM   183  C CB   . LEU   A 1 10  ? 7.275  -12.055 10.397  1.00 15.45 ?  10  LEU   A CB   1 
ATOM   184  C CG   . LEU   A 1 10  ? 6.629  -13.244 9.693   1.00 17.83 ?  10  LEU   A CG   1 
ATOM   185  C CD1  . LEU   A 1 10  ? 5.589  -13.878 10.588  1.00 19.64 ?  10  LEU   A CD1  1 
ATOM   186  C CD2  . LEU   A 1 10  ? 6.036  -12.817 8.367   1.00 20.38 ?  10  LEU   A CD2  1 
ATOM   187  H H    . LEU   A 1 10  ? 8.825  -10.548 11.495  1.00 17.37 ?  10  LEU   A H    1 
ATOM   188  H HA   . LEU   A 1 10  ? 7.621  -12.811 12.289  1.00 17.14 ?  10  LEU   A HA   1 
ATOM   189  H HB2  . LEU   A 1 10  ? 6.556  -11.473 10.700  1.00 18.51 ?  10  LEU   A HB2  1 
ATOM   190  H HB3  . LEU   A 1 10  ? 7.813  -11.586 9.742   1.00 18.51 ?  10  LEU   A HB3  1 
ATOM   191  H HG   . LEU   A 1 10  ? 7.313  -13.911 9.518   1.00 21.38 ?  10  LEU   A HG   1 
ATOM   192  H HD11 . LEU   A 1 10  ? 5.210  -14.647 10.134  1.00 23.55 ?  10  LEU   A HD11 1 
ATOM   193  H HD12 . LEU   A 1 10  ? 6.007  -14.161 11.419  1.00 23.55 ?  10  LEU   A HD12 1 
ATOM   194  H HD13 . LEU   A 1 10  ? 4.894  -13.229 10.776  1.00 23.55 ?  10  LEU   A HD13 1 
ATOM   195  H HD21 . LEU   A 1 10  ? 5.636  -13.595 7.949   1.00 24.44 ?  10  LEU   A HD21 1 
ATOM   196  H HD22 . LEU   A 1 10  ? 5.369  -12.140 8.530   1.00 24.44 ?  10  LEU   A HD22 1 
ATOM   197  H HD23 . LEU   A 1 10  ? 6.747  -12.468 7.811   1.00 24.44 ?  10  LEU   A HD23 1 
ATOM   198  N N    . LYS   A 1 11  ? 9.177  -14.612 11.556  1.00 14.69 ?  11  LYS   A N    1 
ATOM   199  C CA   . LYS   A 1 11  ? 10.175 -15.617 11.216  1.00 14.57 ?  11  LYS   A CA   1 
ATOM   200  C C    . LYS   A 1 11  ? 9.827  -16.190 9.850   1.00 14.54 ?  11  LYS   A C    1 
ATOM   201  O O    . LYS   A 1 11  ? 8.736  -16.738 9.669   1.00 17.06 ?  11  LYS   A O    1 
ATOM   202  C CB   . LYS   A 1 11  ? 10.189 -16.707 12.287  1.00 14.40 ?  11  LYS   A CB   1 
ATOM   203  C CG   . LYS   A 1 11  ? 11.210 -17.806 12.092  1.00 14.78 ?  11  LYS   A CG   1 
ATOM   204  C CD   . LYS   A 1 11  ? 11.269 -18.678 13.345  1.00 15.34 ?  11  LYS   A CD   1 
ATOM   205  C CE   . LYS   A 1 11  ? 12.264 -19.827 13.224  1.00 15.45 ?  11  LYS   A CE   1 
ATOM   206  N NZ   . LYS   A 1 11  ? 13.663 -19.366 12.993  1.00 15.73 ?  11  LYS   A NZ   1 
ATOM   207  H H    . LYS   A 1 11  ? 8.515  -14.918 12.016  1.00 17.60 ?  11  LYS   A H    1 
ATOM   208  H HA   . LYS   A 1 11  ? 11.050 -15.200 11.170  1.00 17.45 ?  11  LYS   A HA   1 
ATOM   209  H HB2  . LYS   A 1 11  ? 10.370 -16.286 13.142  1.00 17.25 ?  11  LYS   A HB2  1 
ATOM   210  H HB3  . LYS   A 1 11  ? 9.313  -17.119 12.309  1.00 17.25 ?  11  LYS   A HB3  1 
ATOM   211  H HG2  . LYS   A 1 11  ? 10.955 -18.361 11.338  1.00 17.71 ?  11  LYS   A HG2  1 
ATOM   212  H HG3  . LYS   A 1 11  ? 12.088 -17.418 11.948  1.00 17.71 ?  11  LYS   A HG3  1 
ATOM   213  H HD2  . LYS   A 1 11  ? 11.525 -18.133 14.102  1.00 18.38 ?  11  LYS   A HD2  1 
ATOM   214  H HD3  . LYS   A 1 11  ? 10.385 -19.063 13.502  1.00 18.38 ?  11  LYS   A HD3  1 
ATOM   215  H HE2  . LYS   A 1 11  ? 12.249 -20.344 14.048  1.00 18.51 ?  11  LYS   A HE2  1 
ATOM   216  H HE3  . LYS   A 1 11  ? 12.006 -20.392 12.479  1.00 18.51 ?  11  LYS   A HE3  1 
ATOM   217  H HZ1  . LYS   A 1 11  ? 14.208 -20.069 12.932  1.00 18.86 ?  11  LYS   A HZ1  1 
ATOM   218  H HZ2  . LYS   A 1 11  ? 13.709 -18.899 12.239  1.00 18.86 ?  11  LYS   A HZ2  1 
ATOM   219  H HZ3  . LYS   A 1 11  ? 13.930 -18.854 13.670  1.00 18.86 ?  11  LYS   A HZ3  1 
ATOM   220  N N    . LEU   A 1 12  ? 10.736 -16.059 8.884   1.00 13.83 ?  12  LEU   A N    1 
ATOM   221  C CA   . LEU   A 1 12  ? 10.495 -16.621 7.558   1.00 14.02 ?  12  LEU   A CA   1 
ATOM   222  C C    . LEU   A 1 12  ? 11.065 -18.026 7.415   1.00 14.56 ?  12  LEU   A C    1 
ATOM   223  O O    . LEU   A 1 12  ? 10.428 -18.898 6.811   1.00 15.07 ?  12  LEU   A O    1 
ATOM   224  C CB   . LEU   A 1 12  ? 11.075 -15.731 6.456   1.00 14.67 ?  12  LEU   A CB   1 
ATOM   225  C CG   . LEU   A 1 12  ? 10.429 -14.363 6.258   1.00 16.12 ?  12  LEU   A CG   1 
ATOM   226  C CD1  . LEU   A 1 12  ? 11.171 -13.601 5.176   1.00 16.58 ?  12  LEU   A CD1  1 
ATOM   227  C CD2  . LEU   A 1 12  ? 8.954  -14.525 5.906   1.00 17.06 ?  12  LEU   A CD2  1 
ATOM   228  H H    . LEU   A 1 12  ? 11.503 -15.660 8.966   1.00 16.57 ?  12  LEU   A H    1 
ATOM   229  H HA   . LEU   A 1 12  ? 9.540  -16.687 7.420   1.00 16.81 ?  12  LEU   A HA   1 
ATOM   230  H HB2  . LEU   A 1 12  ? 12.012 -15.582 6.652   1.00 17.59 ?  12  LEU   A HB2  1 
ATOM   231  H HB3  . LEU   A 1 12  ? 10.998 -16.210 5.614   1.00 17.59 ?  12  LEU   A HB3  1 
ATOM   232  H HG   . LEU   A 1 12  ? 10.493 -13.859 7.083   1.00 19.31 ?  12  LEU   A HG   1 
ATOM   233  H HD11 . LEU   A 1 12  ? 10.756 -12.735 5.055   1.00 19.87 ?  12  LEU   A HD11 1 
ATOM   234  H HD12 . LEU   A 1 12  ? 12.099 -13.488 5.448   1.00 19.87 ?  12  LEU   A HD12 1 
ATOM   235  H HD13 . LEU   A 1 12  ? 11.134 -14.107 4.348   1.00 19.87 ?  12  LEU   A HD13 1 
ATOM   236  H HD21 . LEU   A 1 12  ? 8.605  -13.668 5.620   1.00 20.45 ?  12  LEU   A HD21 1 
ATOM   237  H HD22 . LEU   A 1 12  ? 8.872  -15.173 5.187   1.00 20.45 ?  12  LEU   A HD22 1 
ATOM   238  H HD23 . LEU   A 1 12  ? 8.475  -14.837 6.688   1.00 20.45 ?  12  LEU   A HD23 1 
ATOM   239  N N    . THR   A 1 13  ? 12.273 -18.246 7.926   1.00 14.41 ?  13  THR   A N    1 
ATOM   240  C CA   . THR   A 1 13  ? 12.955 -19.529 7.840   1.00 14.67 ?  13  THR   A CA   1 
ATOM   241  C C    . THR   A 1 13  ? 13.719 -19.747 9.141   1.00 14.93 ?  13  THR   A C    1 
ATOM   242  O O    . THR   A 1 13  ? 13.620 -18.969 10.095  1.00 14.93 ?  13  THR   A O    1 
ATOM   243  C CB   . THR   A 1 13  ? 13.931 -19.581 6.655   1.00 15.34 ?  13  THR   A CB   1 
ATOM   244  O OG1  . THR   A 1 13  ? 15.001 -18.665 6.897   1.00 15.87 ?  13  THR   A OG1  1 
ATOM   245  C CG2  . THR   A 1 13  ? 13.265 -19.222 5.334   1.00 16.51 ?  13  THR   A CG2  1 
ATOM   246  H H    . THR   A 1 13  ? 12.743 -17.642 8.322   1.00 17.26 ?  13  THR   A H    1 
ATOM   247  H HA   . THR   A 1 13  ? 12.302 -20.239 7.734   1.00 17.58 ?  13  THR   A HA   1 
ATOM   248  H HB   . THR   A 1 13  ? 14.290 -20.481 6.574   1.00 18.38 ?  13  THR   A HB   1 
ATOM   249  H HG1  . THR   A 1 13  ? 15.556 -18.695 6.255   1.00 19.02 ?  13  THR   A HG1  1 
ATOM   250  H HG21 . THR   A 1 13  ? 13.897 -19.340 4.602   1.00 19.79 ?  13  THR   A HG21 1 
ATOM   251  H HG22 . THR   A 1 13  ? 12.501 -19.796 5.182   1.00 19.79 ?  13  THR   A HG22 1 
ATOM   252  H HG23 . THR   A 1 13  ? 12.974 -18.299 5.349   1.00 19.79 ?  13  THR   A HG23 1 
ATOM   253  N N    . ASP   A 1 14  ? 14.524 -20.805 9.160   1.00 15.37 ?  14  ASP   A N    1 
ATOM   254  C CA   . ASP   A 1 14  ? 15.360 -21.075 10.318  1.00 16.24 ?  14  ASP   A CA   1 
ATOM   255  C C    . ASP   A 1 14  ? 16.195 -19.862 10.718  1.00 15.43 ?  14  ASP   A C    1 
ATOM   256  O O    . ASP   A 1 14  ? 16.427 -19.629 11.909  1.00 16.58 ?  14  ASP   A O    1 
ATOM   257  C CB   . ASP   A 1 14  ? 16.285 -22.247 10.010  1.00 19.34 ?  14  ASP   A CB   1 
ATOM   258  C CG   . ASP   A 1 14  ? 17.212 -22.545 11.154  1.00 23.73 ?  14  ASP   A CG   1 
ATOM   259  O OD1  . ASP   A 1 14  ? 16.710 -22.935 12.232  1.00 25.52 ?  14  ASP   A OD1  1 
ATOM   260  O OD2  . ASP   A 1 14  ? 18.432 -22.374 10.977  1.00 26.51 -1 14  ASP   A OD2  1 
ATOM   261  H H    . ASP   A 1 14  ? 14.612 -21.368 8.516   1.00 18.42 ?  14  ASP   A H    1 
ATOM   262  H HA   . ASP   A 1 14  ? 14.801 -21.323 11.070  1.00 19.47 ?  14  ASP   A HA   1 
ATOM   263  H HB2  . ASP   A 1 14  ? 15.748 -23.045 9.839   1.00 23.19 ?  14  ASP   A HB2  1 
ATOM   264  H HB3  . ASP   A 1 14  ? 16.814 -22.042 9.219   1.00 23.19 ?  14  ASP   A HB3  1 
ATOM   265  N N    . ASN   A 1 15  ? 16.656 -19.072 9.741   1.00 14.52 ?  15  ASN   A N    1 
ATOM   266  C CA   . ASN   A 1 15  ? 17.652 -18.039 10.007  1.00 14.95 ?  15  ASN   A CA   1 
ATOM   267  C C    . ASN   A 1 15  ? 17.290 -16.649 9.499   1.00 15.27 ?  15  ASN   A C    1 
ATOM   268  O O    . ASN   A 1 15  ? 18.062 -15.717 9.737   1.00 16.28 ?  15  ASN   A O    1 
ATOM   269  C CB   . ASN   A 1 15  ? 19.023 -18.444 9.426   1.00 14.90 ?  15  ASN   A CB   1 
ATOM   270  C CG   . ASN   A 1 15  ? 19.009 -18.545 7.917   1.00 15.27 ?  15  ASN   A CG   1 
ATOM   271  O OD1  . ASN   A 1 15  ? 18.290 -19.369 7.345   1.00 16.32 ?  15  ASN   A OD1  1 
ATOM   272  N ND2  . ASN   A 1 15  ? 19.802 -17.702 7.257   1.00 15.51 ?  15  ASN   A ND2  1 
ATOM   273  H H    . ASN   A 1 15  ? 16.396 -19.106 8.929   1.00 17.40 ?  15  ASN   A H    1 
ATOM   274  H HA   . ASN   A 1 15  ? 17.774 -17.966 10.967  1.00 17.92 ?  15  ASN   A HA   1 
ATOM   275  H HB2  . ASN   A 1 15  ? 19.690 -17.776 9.680   1.00 17.86 ?  15  ASN   A HB2  1 
ATOM   276  H HB3  . ASN   A 1 15  ? 19.282 -19.309 9.783   1.00 17.86 ?  15  ASN   A HB3  1 
ATOM   277  H HD21 . ASN   A 1 15  ? 19.827 -17.717 6.397   1.00 18.59 ?  15  ASN   A HD21 1 
ATOM   278  H HD22 . ASN   A 1 15  ? 20.293 -17.133 7.685   1.00 18.59 ?  15  ASN   A HD22 1 
ATOM   279  N N    . VAL   A 1 16  ? 16.160 -16.473 8.813   1.00 14.80 ?  16  VAL   A N    1 
ATOM   280  C CA   . VAL   A 1 16  ? 15.775 -15.191 8.232   1.00 14.75 ?  16  VAL   A CA   1 
ATOM   281  C C    . VAL   A 1 16  ? 14.498 -14.696 8.894   1.00 14.00 ?  16  VAL   A C    1 
ATOM   282  O O    . VAL   A 1 16  ? 13.500 -15.428 8.977   1.00 13.84 ?  16  VAL   A O    1 
ATOM   283  C CB   . VAL   A 1 16  ? 15.607 -15.277 6.706   1.00 15.22 ?  16  VAL   A CB   1 
ATOM   284  C CG1  . VAL   A 1 16  ? 15.171 -13.923 6.139   1.00 16.28 ?  16  VAL   A CG1  1 
ATOM   285  C CG2  . VAL   A 1 16  ? 16.892 -15.754 6.049   1.00 16.04 ?  16  VAL   A CG2  1 
ATOM   286  H H    . VAL   A 1 16  ? 15.591 -17.102 8.680   1.00 17.74 ?  16  VAL   A H    1 
ATOM   287  H HA   . VAL   A 1 16  ? 16.477 -14.546 8.420   1.00 17.68 ?  16  VAL   A HA   1 
ATOM   288  H HB   . VAL   A 1 16  ? 14.920 -15.924 6.510   1.00 18.24 ?  16  VAL   A HB   1 
ATOM   289  H HG11 . VAL   A 1 16  ? 15.264 -13.945 5.176   1.00 19.51 ?  16  VAL   A HG11 1 
ATOM   290  H HG12 . VAL   A 1 16  ? 14.240 -13.770 6.377   1.00 19.51 ?  16  VAL   A HG12 1 
ATOM   291  H HG13 . VAL   A 1 16  ? 15.727 -13.226 6.513   1.00 19.51 ?  16  VAL   A HG13 1 
ATOM   292  H HG21 . VAL   A 1 16  ? 16.782 -15.726 5.086   1.00 19.23 ?  16  VAL   A HG21 1 
ATOM   293  H HG22 . VAL   A 1 16  ? 17.624 -15.174 6.314   1.00 19.23 ?  16  VAL   A HG22 1 
ATOM   294  H HG23 . VAL   A 1 16  ? 17.077 -16.664 6.334   1.00 19.23 ?  16  VAL   A HG23 1 
ATOM   295  N N    . TYR   A 1 17  ? 14.538 -13.439 9.337   1.00 13.78 ?  17  TYR   A N    1 
ATOM   296  C CA   . TYR   A 1 17  ? 13.451 -12.756 10.022  1.00 13.67 ?  17  TYR   A CA   1 
ATOM   297  C C    . TYR   A 1 17  ? 13.187 -11.433 9.314   1.00 13.85 ?  17  TYR   A C    1 
ATOM   298  O O    . TYR   A 1 17  ? 14.095 -10.872 8.699   1.00 14.11 ?  17  TYR   A O    1 
ATOM   299  C CB   . TYR   A 1 17  ? 13.866 -12.474 11.465  1.00 14.45 ?  17  TYR   A CB   1 
ATOM   300  C CG   . TYR   A 1 17  ? 14.058 -13.731 12.279  1.00 15.62 ?  17  TYR   A CG   1 
ATOM   301  C CD1  . TYR   A 1 17  ? 15.232 -14.477 12.197  1.00 16.59 ?  17  TYR   A CD1  1 
ATOM   302  C CD2  . TYR   A 1 17  ? 13.057 -14.190 13.119  1.00 15.79 ?  17  TYR   A CD2  1 
ATOM   303  C CE1  . TYR   A 1 17  ? 15.401 -15.651 12.935  1.00 17.11 ?  17  TYR   A CE1  1 
ATOM   304  C CE2  . TYR   A 1 17  ? 13.212 -15.365 13.860  1.00 16.67 ?  17  TYR   A CE2  1 
ATOM   305  C CZ   . TYR   A 1 17  ? 14.387 -16.087 13.768  1.00 16.95 ?  17  TYR   A CZ   1 
ATOM   306  O OH   . TYR   A 1 17  ? 14.548 -17.246 14.501  1.00 18.29 ?  17  TYR   A OH   1 
ATOM   307  H H    . TYR   A 1 17  ? 15.234 -12.935 9.238   1.00 16.51 ?  17  TYR   A H    1 
ATOM   308  H HA   . TYR   A 1 17  ? 12.649 -13.301 10.006  1.00 16.38 ?  17  TYR   A HA   1 
ATOM   309  H HB2  . TYR   A 1 17  ? 14.704 -11.990 11.458  1.00 17.31 ?  17  TYR   A HB2  1 
ATOM   310  H HB3  . TYR   A 1 17  ? 13.178 -11.946 11.887  1.00 17.31 ?  17  TYR   A HB3  1 
ATOM   311  H HD1  . TYR   A 1 17  ? 15.917 -14.189 11.633  1.00 19.88 ?  17  TYR   A HD1  1 
ATOM   312  H HD2  . TYR   A 1 17  ? 12.259 -13.714 13.185  1.00 18.93 ?  17  TYR   A HD2  1 
ATOM   313  H HE1  . TYR   A 1 17  ? 16.198 -16.134 12.874  1.00 20.51 ?  17  TYR   A HE1  1 
ATOM   314  H HE2  . TYR   A 1 17  ? 12.530 -15.651 14.426  1.00 19.98 ?  17  TYR   A HE2  1 
ATOM   315  H HH   . TYR   A 1 17  ? 15.317 -17.564 14.359  1.00 21.92 ?  17  TYR   A HH   1 
ATOM   316  N N    . ILE   A 1 18  ? 11.952 -10.915 9.399   1.00 13.96 ?  18  ILE   A N    1 
ATOM   317  C CA   . ILE   A 1 18  ? 11.577 -9.712  8.653   1.00 13.96 ?  18  ILE   A CA   1 
ATOM   318  C C    . ILE   A 1 18  ? 10.604 -8.844  9.449   1.00 14.45 ?  18  ILE   A C    1 
ATOM   319  O O    . ILE   A 1 18  ? 9.774  -9.348  10.214  1.00 14.83 ?  18  ILE   A O    1 
ATOM   320  C CB   . ILE   A 1 18  ? 11.013 -10.096 7.271   1.00 13.86 ?  18  ILE   A CB   1 
ATOM   321  C CG1  . ILE   A 1 18  ? 10.979 -8.900  6.323   1.00 15.23 ?  18  ILE   A CG1  1 
ATOM   322  C CG2  . ILE   A 1 18  ? 9.648  -10.766 7.405   1.00 14.68 ?  18  ILE   A CG2  1 
ATOM   323  C CD1  . ILE   A 1 18  ? 10.744 -9.303  4.892   1.00 17.04 ?  18  ILE   A CD1  1 
ATOM   324  H H    . ILE   A 1 18  ? 11.318 -11.256 9.869   1.00 16.73 ?  18  ILE   A H    1 
ATOM   325  H HA   . ILE   A 1 18  ? 12.383 -9.189  8.501   1.00 16.73 ?  18  ILE   A HA   1 
ATOM   326  H HB   . ILE   A 1 18  ? 11.609 -10.745 6.886   1.00 16.61 ?  18  ILE   A HB   1 
ATOM   327  H HG12 . ILE   A 1 18  ? 10.272 -8.296  6.581   1.00 18.25 ?  18  ILE   A HG12 1 
ATOM   328  H HG13 . ILE   A 1 18  ? 11.839 -8.442  6.358   1.00 18.25 ?  18  ILE   A HG13 1 
ATOM   329  H HG21 . ILE   A 1 18  ? 9.393  -11.137 6.544   1.00 17.59 ?  18  ILE   A HG21 1 
ATOM   330  H HG22 . ILE   A 1 18  ? 9.706  -11.469 8.065   1.00 17.59 ?  18  ILE   A HG22 1 
ATOM   331  H HG23 . ILE   A 1 18  ? 8.990  -10.105 7.682   1.00 17.59 ?  18  ILE   A HG23 1 
ATOM   332  H HD11 . ILE   A 1 18  ? 10.833 -8.522  4.322   1.00 20.43 ?  18  ILE   A HD11 1 
ATOM   333  H HD12 . ILE   A 1 18  ? 11.399 -9.972  4.639   1.00 20.43 ?  18  ILE   A HD12 1 
ATOM   334  H HD13 . ILE   A 1 18  ? 9.849  -9.668  4.813   1.00 20.43 ?  18  ILE   A HD13 1 
ATOM   335  N N    A LYS   A 1 19  ? 10.687 -7.533  9.217   0.58 14.64 ?  19  LYS   A N    1 
ATOM   336  N N    B LYS   A 1 19  ? 10.715 -7.522  9.269   0.42 14.81 ?  19  LYS   A N    1 
ATOM   337  C CA   A LYS   A 1 19  ? 9.876  -6.560  9.933   0.58 15.47 ?  19  LYS   A CA   1 
ATOM   338  C CA   B LYS   A 1 19  ? 9.911  -6.560  10.018  0.42 15.67 ?  19  LYS   A CA   1 
ATOM   339  C C    A LYS   A 1 19  ? 9.678  -5.339  9.049   0.58 15.22 ?  19  LYS   A C    1 
ATOM   340  C C    B LYS   A 1 19  ? 9.747  -5.278  9.206   0.42 15.57 ?  19  LYS   A C    1 
ATOM   341  O O    A LYS   A 1 19  ? 10.540 -5.003  8.231   0.58 14.84 ?  19  LYS   A O    1 
ATOM   342  O O    B LYS   A 1 19  ? 10.700 -4.815  8.574   0.42 15.35 ?  19  LYS   A O    1 
ATOM   343  C CB   A LYS   A 1 19  ? 10.600 -6.132  11.215  0.58 15.99 ?  19  LYS   A CB   1 
ATOM   344  C CB   B LYS   A 1 19  ? 10.573 -6.244  11.370  0.42 16.28 ?  19  LYS   A CB   1 
ATOM   345  C CG   A LYS   A 1 19  ? 9.833  -5.229  12.169  0.58 17.59 ?  19  LYS   A CG   1 
ATOM   346  C CG   B LYS   A 1 19  ? 9.822  -5.245  12.241  0.42 17.44 ?  19  LYS   A CG   1 
ATOM   347  C CD   A LYS   A 1 19  ? 10.705 -4.971  13.396  0.58 19.06 ?  19  LYS   A CD   1 
ATOM   348  C CD   B LYS   A 1 19  ? 10.612 -4.930  13.504  0.42 18.66 ?  19  LYS   A CD   1 
ATOM   349  C CE   A LYS   A 1 19  ? 10.065 -4.049  14.416  0.58 20.17 ?  19  LYS   A CE   1 
ATOM   350  C CE   B LYS   A 1 19  ? 9.863  -3.976  14.419  0.42 19.73 ?  19  LYS   A CE   1 
ATOM   351  N NZ   A LYS   A 1 19  ? 10.974 -3.857  15.584  0.58 20.69 ?  19  LYS   A NZ   1 
ATOM   352  N NZ   B LYS   A 1 19  ? 10.675 -3.609  15.610  0.42 20.21 ?  19  LYS   A NZ   1 
ATOM   353  H H    A LYS   A 1 19  ? 11.224 -7.181  8.635   0.58 17.54 ?  19  LYS   A H    1 
ATOM   354  H H    B LYS   A 1 19  ? 11.263 -7.151  8.710   0.42 17.74 ?  19  LYS   A H    1 
ATOM   355  H HA   A LYS   A 1 19  ? 9.017  -6.945  10.151  0.58 18.54 ?  19  LYS   A HA   1 
ATOM   356  H HA   B LYS   A 1 19  ? 9.036  -6.931  10.187  0.42 18.78 ?  19  LYS   A HA   1 
ATOM   357  H HB2  A LYS   A 1 19  ? 10.836 -6.933  11.702  0.58 19.17 ?  19  LYS   A HB2  1 
ATOM   358  H HB2  B LYS   A 1 19  ? 10.650 -7.070  11.879  0.42 19.52 ?  19  LYS   A HB2  1 
ATOM   359  H HB3  A LYS   A 1 19  ? 11.409 -5.660  10.958  0.58 19.17 ?  19  LYS   A HB3  1 
ATOM   360  H HB3  B LYS   A 1 19  ? 11.459 -5.882  11.209  0.42 19.52 ?  19  LYS   A HB3  1 
ATOM   361  H HG2  A LYS   A 1 19  ? 9.637  -4.381  11.738  0.58 21.08 ?  19  LYS   A HG2  1 
ATOM   362  H HG2  B LYS   A 1 19  ? 9.693  -4.418  11.752  0.42 20.90 ?  19  LYS   A HG2  1 
ATOM   363  H HG3  A LYS   A 1 19  ? 9.014  -5.668  12.452  0.58 21.08 ?  19  LYS   A HG3  1 
ATOM   364  H HG3  B LYS   A 1 19  ? 8.967  -5.622  12.501  0.42 20.90 ?  19  LYS   A HG3  1 
ATOM   365  H HD2  A LYS   A 1 19  ? 10.886 -5.818  13.833  0.58 22.85 ?  19  LYS   A HD2  1 
ATOM   366  H HD2  B LYS   A 1 19  ? 10.775 -5.754  13.991  0.42 22.37 ?  19  LYS   A HD2  1 
ATOM   367  H HD3  A LYS   A 1 19  ? 11.537 -4.565  13.107  0.58 22.85 ?  19  LYS   A HD3  1 
ATOM   368  H HD3  B LYS   A 1 19  ? 11.455 -4.517  13.257  0.42 22.37 ?  19  LYS   A HD3  1 
ATOM   369  H HE2  A LYS   A 1 19  ? 9.899  -3.183  14.010  0.58 24.18 ?  19  LYS   A HE2  1 
ATOM   370  H HE2  B LYS   A 1 19  ? 9.656  -3.164  13.931  0.42 23.66 ?  19  LYS   A HE2  1 
ATOM   371  H HE3  A LYS   A 1 19  ? 9.235  -4.439  14.732  0.58 24.18 ?  19  LYS   A HE3  1 
ATOM   372  H HE3  B LYS   A 1 19  ? 9.048  -4.401  14.726  0.42 23.66 ?  19  LYS   A HE3  1 
ATOM   373  H HZ1  A LYS   A 1 19  ? 10.588 -3.325  16.185  0.58 24.80 ?  19  LYS   A HZ1  1 
ATOM   374  H HZ1  B LYS   A 1 19  ? 10.217 -3.052  16.131  0.42 24.23 ?  19  LYS   A HZ1  1 
ATOM   375  H HZ2  A LYS   A 1 19  ? 11.149 -4.642  15.965  0.58 24.80 ?  19  LYS   A HZ2  1 
ATOM   376  H HZ2  B LYS   A 1 19  ? 10.879 -4.340  16.076  0.42 24.23 ?  19  LYS   A HZ2  1 
ATOM   377  H HZ3  A LYS   A 1 19  ? 11.737 -3.487  15.319  0.58 24.80 ?  19  LYS   A HZ3  1 
ATOM   378  H HZ3  B LYS   A 1 19  ? 11.429 -3.210  15.354  0.42 24.23 ?  19  LYS   A HZ3  1 
ATOM   379  N N    A ASN   A 1 20  ? 8.534  -4.676  9.216   0.58 15.73 ?  20  ASN   A N    1 
ATOM   380  N N    B ASN   A 1 20  ? 8.535  -4.710  9.220   0.42 16.10 ?  20  ASN   A N    1 
ATOM   381  C CA   A ASN   A 1 20  ? 8.339  -3.342  8.656   0.58 16.35 ?  20  ASN   A CA   1 
ATOM   382  C CA   B ASN   A 1 20  ? 8.243  -3.426  8.570   0.42 16.61 ?  20  ASN   A CA   1 
ATOM   383  C C    A ASN   A 1 20  ? 8.974  -2.363  9.629   0.58 16.79 ?  20  ASN   A C    1 
ATOM   384  C C    B ASN   A 1 20  ? 8.785  -2.308  9.453   0.42 17.36 ?  20  ASN   A C    1 
ATOM   385  O O    A ASN   A 1 20  ? 8.495  -2.200  10.756  0.58 16.98 ?  20  ASN   A O    1 
ATOM   386  O O    B ASN   A 1 20  ? 8.104  -1.816  10.357  0.42 17.64 ?  20  ASN   A O    1 
ATOM   387  C CB   A ASN   A 1 20  ? 6.851  -3.062  8.461   0.58 17.11 ?  20  ASN   A CB   1 
ATOM   388  C CB   B ASN   A 1 20  ? 6.737  -3.270  8.356   0.42 16.75 ?  20  ASN   A CB   1 
ATOM   389  C CG   A ASN   A 1 20  ? 6.553  -1.616  8.077   0.58 18.01 ?  20  ASN   A CG   1 
ATOM   390  C CG   B ASN   A 1 20  ? 6.351  -1.990  7.590   0.42 17.00 ?  20  ASN   A CG   1 
ATOM   391  O OD1  A ASN   A 1 20  ? 5.534  -1.068  8.491   0.58 19.83 ?  20  ASN   A OD1  1 
ATOM   392  O OD1  B ASN   A 1 20  ? 5.190  -1.549  7.640   0.42 16.69 ?  20  ASN   A OD1  1 
ATOM   393  N ND2  A ASN   A 1 20  ? 7.424  -1.001  7.283   0.58 18.42 ?  20  ASN   A ND2  1 
ATOM   394  N ND2  B ASN   A 1 20  ? 7.308  -1.404  6.874   0.42 17.75 ?  20  ASN   A ND2  1 
ATOM   395  H H    A ASN   A 1 20  ? 7.861  -4.977  9.655   0.58 18.85 ?  20  ASN   A H    1 
ATOM   396  H H    B ASN   A 1 20  ? 7.851  -5.071  9.588   0.42 19.30 ?  20  ASN   A H    1 
ATOM   397  H HA   A ASN   A 1 20  ? 8.787  -3.276  7.802   0.58 19.60 ?  20  ASN   A HA   1 
ATOM   398  H HA   B ASN   A 1 20  ? 8.695  -3.394  7.713   0.42 19.91 ?  20  ASN   A HA   1 
ATOM   399  H HB2  A ASN   A 1 20  ? 6.515  -3.634  7.757   0.58 20.51 ?  20  ASN   A HB2  1 
ATOM   400  H HB2  B ASN   A 1 20  ? 6.396  -4.031  7.873   0.42 20.08 ?  20  ASN   A HB2  1 
ATOM   401  H HB3  A ASN   A 1 20  ? 6.385  -3.249  9.292   0.58 20.51 ?  20  ASN   A HB3  1 
ATOM   402  H HB3  B ASN   A 1 20  ? 6.306  -3.225  9.220   0.42 20.08 ?  20  ASN   A HB3  1 
ATOM   403  H HD21 A ASN   A 1 20  ? 7.290  -0.188  7.042   0.58 22.08 ?  20  ASN   A HD21 1 
ATOM   404  H HD21 B ASN   A 1 20  ? 7.132  -0.692  6.433   0.42 21.28 ?  20  ASN   A HD21 1 
ATOM   405  H HD22 A ASN   A 1 20  ? 8.130  -1.416  7.013   0.58 22.08 ?  20  ASN   A HD22 1 
ATOM   406  H HD22 B ASN   A 1 20  ? 8.108  -1.727  6.856   0.42 21.28 ?  20  ASN   A HD22 1 
ATOM   407  N N    A ALA   A 1 21  ? 10.074 -1.740  9.217   0.58 17.13 ?  21  ALA   A N    1 
ATOM   408  N N    B ALA   A 1 21  ? 10.019 -1.885  9.178   0.42 17.78 ?  21  ALA   A N    1 
ATOM   409  C CA   A ALA   A 1 21  ? 10.796 -0.882  10.137  0.58 16.95 ?  21  ALA   A CA   1 
ATOM   410  C CA   B ALA   A 1 21  ? 10.659 -0.867  10.001  0.42 17.88 ?  21  ALA   A CA   1 
ATOM   411  C C    A ALA   A 1 21  ? 11.714 0.042   9.361   0.58 16.55 ?  21  ALA   A C    1 
ATOM   412  C C    B ALA   A 1 21  ? 11.770 -0.186  9.215   0.42 16.89 ?  21  ALA   A C    1 
ATOM   413  O O    A ALA   A 1 21  ? 12.166 -0.281  8.260   0.58 16.79 ?  21  ALA   A O    1 
ATOM   414  O O    B ALA   A 1 21  ? 12.305 -0.737  8.250   0.42 16.88 ?  21  ALA   A O    1 
ATOM   415  C CB   A ALA   A 1 21  ? 11.616 -1.704  11.134  0.58 17.03 ?  21  ALA   A CB   1 
ATOM   416  C CB   B ALA   A 1 21  ? 11.211 -1.462  11.301  0.42 18.73 ?  21  ALA   A CB   1 
ATOM   417  H H    A ALA   A 1 21  ? 10.413 -1.794  8.426   0.58 20.54 ?  21  ALA   A H    1 
ATOM   418  H H    B ALA   A 1 21  ? 10.495 -2.165  8.520   0.42 21.31 ?  21  ALA   A H    1 
ATOM   419  H HA   A ALA   A 1 21  ? 10.159 -0.338  10.632  0.58 20.32 ?  21  ALA   A HA   1 
ATOM   420  H HA   B ALA   A 1 21  ? 9.999  -0.197  10.237  0.42 21.43 ?  21  ALA   A HA   1 
ATOM   421  H HB1  A ALA   A 1 21  ? 12.037 -1.097  11.759  0.58 20.42 ?  21  ALA   A HB1  1 
ATOM   422  H HB1  B ALA   A 1 21  ? 11.627 -0.755  11.819  0.42 22.45 ?  21  ALA   A HB1  1 
ATOM   423  H HB2  A ALA   A 1 21  ? 11.018 -2.305  11.607  0.58 20.42 ?  21  ALA   A HB2  1 
ATOM   424  H HB2  B ALA   A 1 21  ? 10.481 -1.857  11.806  0.42 22.45 ?  21  ALA   A HB2  1 
ATOM   425  H HB3  A ALA   A 1 21  ? 12.283 -2.209  10.650  0.58 20.42 ?  21  ALA   A HB3  1 
ATOM   426  H HB3  B ALA   A 1 21  ? 11.867 -2.143  11.083  0.42 22.45 ?  21  ALA   A HB3  1 
ATOM   427  N N    A ASP   A 1 22  ? 11.958 1.204   9.956   0.58 16.42 ?  22  ASP   A N    1 
ATOM   428  N N    B ASP   A 1 22  ? 12.091 1.035   9.643   0.42 16.34 ?  22  ASP   A N    1 
ATOM   429  C CA   A ASP   A 1 22  ? 12.996 2.115   9.505   0.58 15.97 ?  22  ASP   A CA   1 
ATOM   430  C CA   B ASP   A 1 22  ? 13.239 1.776   9.131   0.42 16.28 ?  22  ASP   A CA   1 
ATOM   431  C C    A ASP   A 1 22  ? 14.329 1.633   10.067  0.58 15.25 ?  22  ASP   A C    1 
ATOM   432  C C    B ASP   A 1 22  ? 14.503 1.230   9.792   0.42 15.09 ?  22  ASP   A C    1 
ATOM   433  O O    A ASP   A 1 22  ? 14.527 1.629   11.286  0.58 16.11 ?  22  ASP   A O    1 
ATOM   434  O O    B ASP   A 1 22  ? 14.602 1.195   11.023  0.42 15.41 ?  22  ASP   A O    1 
ATOM   435  C CB   A ASP   A 1 22  ? 12.667 3.514   10.020  0.58 17.30 ?  22  ASP   A CB   1 
ATOM   436  C CB   B ASP   A 1 22  ? 13.053 3.260   9.462   0.42 17.94 ?  22  ASP   A CB   1 
ATOM   437  C CG   A ASP   A 1 22  ? 13.687 4.552   9.602   0.58 19.07 ?  22  ASP   A CG   1 
ATOM   438  C CG   B ASP   A 1 22  ? 14.111 4.159   8.841   0.42 19.15 ?  22  ASP   A CG   1 
ATOM   439  O OD1  A ASP   A 1 22  ? 14.815 4.190   9.227   0.58 19.29 ?  22  ASP   A OD1  1 
ATOM   440  O OD1  B ASP   A 1 22  ? 15.151 3.652   8.376   0.42 18.77 ?  22  ASP   A OD1  1 
ATOM   441  O OD2  A ASP   A 1 22  ? 13.352 5.750   9.660   0.58 20.77 -1 22  ASP   A OD2  1 
ATOM   442  O OD2  B ASP   A 1 22  ? 13.898 5.393   8.827   0.42 20.71 -1 22  ASP   A OD2  1 
ATOM   443  H H    A ASP   A 1 22  ? 11.516 1.496   10.636  0.58 19.68 ?  22  ASP   A H    1 
ATOM   444  H H    B ASP   A 1 22  ? 11.636 1.468   10.236  0.42 19.58 ?  22  ASP   A H    1 
ATOM   445  H HA   A ASP   A 1 22  ? 13.039 2.131   8.536   0.58 19.14 ?  22  ASP   A HA   1 
ATOM   446  H HA   B ASP   A 1 22  ? 13.297 1.659   8.167   0.42 19.52 ?  22  ASP   A HA   1 
ATOM   447  H HB2  A ASP   A 1 22  ? 11.804 3.789   9.668   0.58 20.74 ?  22  ASP   A HB2  1 
ATOM   448  H HB2  B ASP   A 1 22  ? 12.191 3.551   9.137   0.42 21.51 ?  22  ASP   A HB2  1 
ATOM   449  H HB3  A ASP   A 1 22  ? 12.631 3.493   10.991  0.58 20.74 ?  22  ASP   A HB3  1 
ATOM   450  H HB3  B ASP   A 1 22  ? 13.109 3.374   10.420  0.42 21.51 ?  22  ASP   A HB3  1 
ATOM   451  N N    A ILE   A 1 23  ? 15.237 1.221   9.178   0.58 14.96 ?  23  ILE   A N    1 
ATOM   452  N N    B ILE   A 1 23  ? 15.465 0.792   8.973   0.42 14.63 ?  23  ILE   A N    1 
ATOM   453  C CA   A ILE   A 1 23  ? 16.480 0.585   9.609   0.58 14.76 ?  23  ILE   A CA   1 
ATOM   454  C CA   B ILE   A 1 23  ? 16.701 0.208   9.488   0.42 13.88 ?  23  ILE   A CA   1 
ATOM   455  C C    A ILE   A 1 23  ? 17.301 1.511   10.497  0.58 15.05 ?  23  ILE   A C    1 
ATOM   456  C C    B ILE   A 1 23  ? 17.428 1.194   10.389  0.42 14.25 ?  23  ILE   A C    1 
ATOM   457  O O    A ILE   A 1 23  ? 18.014 1.047   11.395  0.58 15.73 ?  23  ILE   A O    1 
ATOM   458  O O    B ILE   A 1 23  ? 18.106 0.791   11.343  0.42 14.32 ?  23  ILE   A O    1 
ATOM   459  C CB   A ILE   A 1 23  ? 17.272 0.064   8.390   0.58 14.20 ?  23  ILE   A CB   1 
ATOM   460  C CB   B ILE   A 1 23  ? 17.599 -0.312  8.339   0.42 12.93 ?  23  ILE   A CB   1 
ATOM   461  C CG1  A ILE   A 1 23  ? 18.421 -0.837  8.846   0.58 13.88 ?  23  ILE   A CG1  1 
ATOM   462  C CG1  B ILE   A 1 23  ? 18.668 -1.266  8.890   0.42 12.80 ?  23  ILE   A CG1  1 
ATOM   463  C CG2  A ILE   A 1 23  ? 17.774 1.224   7.531   0.58 14.48 ?  23  ILE   A CG2  1 
ATOM   464  C CG2  B ILE   A 1 23  ? 18.250 0.841   7.573   0.42 13.09 ?  23  ILE   A CG2  1 
ATOM   465  C CD1  A ILE   A 1 23  ? 19.078 -1.597  7.717   0.58 14.26 ?  23  ILE   A CD1  1 
ATOM   466  C CD1  B ILE   A 1 23  ? 19.541 -1.917  7.823   0.42 13.21 ?  23  ILE   A CD1  1 
ATOM   467  H H    A ILE   A 1 23  ? 15.146 1.293   8.332   0.58 17.93 ?  23  ILE   A H    1 
ATOM   468  H H    B ILE   A 1 23  ? 15.422 0.810   8.134   0.42 17.53 ?  23  ILE   A H    1 
ATOM   469  H HA   A ILE   A 1 23  ? 16.248 -0.190  10.146  0.58 17.69 ?  23  ILE   A HA   1 
ATOM   470  H HA   B ILE   A 1 23  ? 16.462 -0.559  10.027  0.42 16.63 ?  23  ILE   A HA   1 
ATOM   471  H HB   A ILE   A 1 23  ? 16.669 -0.470  7.848   0.58 17.02 ?  23  ILE   A HB   1 
ATOM   472  H HB   B ILE   A 1 23  ? 17.045 -0.813  7.719   0.42 15.49 ?  23  ILE   A HB   1 
ATOM   473  H HG12 A ILE   A 1 23  ? 19.099 -0.289  9.269   0.58 16.63 ?  23  ILE   A HG12 1 
ATOM   474  H HG12 B ILE   A 1 23  ? 19.253 -0.775  9.485   0.42 15.34 ?  23  ILE   A HG12 1 
ATOM   475  H HG13 A ILE   A 1 23  ? 18.077 -1.485  9.481   0.58 16.63 ?  23  ILE   A HG13 1 
ATOM   476  H HG13 B ILE   A 1 23  ? 18.228 -1.982  9.380   0.42 15.34 ?  23  ILE   A HG13 1 
ATOM   477  H HG21 A ILE   A 1 23  ? 18.136 0.870   6.704   0.58 17.35 ?  23  ILE   A HG21 1 
ATOM   478  H HG21 B ILE   A 1 23  ? 18.621 0.497   6.741   0.42 15.68 ?  23  ILE   A HG21 1 
ATOM   479  H HG22 A ILE   A 1 23  ? 17.028 1.816   7.335   0.58 17.35 ?  23  ILE   A HG22 1 
ATOM   480  H HG22 B ILE   A 1 23  ? 17.578 1.509   7.382   0.42 15.68 ?  23  ILE   A HG22 1 
ATOM   481  H HG23 A ILE   A 1 23  ? 18.458 1.706   8.016   0.58 17.35 ?  23  ILE   A HG23 1 
ATOM   482  H HG23 B ILE   A 1 23  ? 18.957 1.223   8.114   0.42 15.68 ?  23  ILE   A HG23 1 
ATOM   483  H HD11 A ILE   A 1 23  ? 19.751 -2.188  8.085   0.58 17.09 ?  23  ILE   A HD11 1 
ATOM   484  H HD11 B ILE   A 1 23  ? 20.128 -2.566  8.246   0.42 15.83 ?  23  ILE   A HD11 1 
ATOM   485  H HD12 A ILE   A 1 23  ? 18.401 -2.115  7.252   0.58 17.09 ?  23  ILE   A HD12 1 
ATOM   486  H HD12 B ILE   A 1 23  ? 18.973 -2.362  7.175   0.42 15.83 ?  23  ILE   A HD12 1 
ATOM   487  H HD13 A ILE   A 1 23  ? 19.487 -0.965  7.107   0.58 17.09 ?  23  ILE   A HD13 1 
ATOM   488  H HD13 B ILE   A 1 23  ? 20.070 -1.233  7.385   0.42 15.83 ?  23  ILE   A HD13 1 
ATOM   489  N N    A VAL   A 1 24  ? 17.206 2.825   10.281  0.58 15.76 ?  24  VAL   A N    1 
ATOM   490  N N    B VAL   A 1 24  ? 17.288 2.493   10.116  0.42 15.60 ?  24  VAL   A N    1 
ATOM   491  C CA   A VAL   A 1 24  ? 17.900 3.770   11.153  0.58 16.75 ?  24  VAL   A CA   1 
ATOM   492  C CA   B VAL   A 1 24  ? 17.923 3.507   10.953  0.42 16.70 ?  24  VAL   A CA   1 
ATOM   493  C C    A VAL   A 1 24  ? 17.370 3.664   12.577  0.58 17.36 ?  24  VAL   A C    1 
ATOM   494  C C    B VAL   A 1 24  ? 17.338 3.476   12.360  0.42 17.37 ?  24  VAL   A C    1 
ATOM   495  O O    A VAL   A 1 24  ? 18.140 3.542   13.541  0.58 17.84 ?  24  VAL   A O    1 
ATOM   496  O O    B VAL   A 1 24  ? 18.068 3.522   13.359  0.42 18.26 ?  24  VAL   A O    1 
ATOM   497  C CB   A VAL   A 1 24  ? 17.772 5.203   10.606  0.58 17.20 ?  24  VAL   A CB   1 
ATOM   498  C CB   B VAL   A 1 24  ? 17.785 4.897   10.305  0.42 17.40 ?  24  VAL   A CB   1 
ATOM   499  C CG1  A VAL   A 1 24  ? 18.209 6.224   11.656  0.58 17.46 ?  24  VAL   A CG1  1 
ATOM   500  C CG1  B VAL   A 1 24  ? 18.450 5.954   11.168  0.42 18.60 ?  24  VAL   A CG1  1 
ATOM   501  C CG2  A VAL   A 1 24  ? 18.584 5.360   9.330   0.58 18.01 ?  24  VAL   A CG2  1 
ATOM   502  C CG2  B VAL   A 1 24  ? 18.371 4.884   8.899   0.42 17.18 ?  24  VAL   A CG2  1 
ATOM   503  H H    A VAL   A 1 24  ? 16.751 3.187   9.647   0.58 18.89 ?  24  VAL   A H    1 
ATOM   504  H H    B VAL   A 1 24  ? 16.829 2.808   9.461   0.42 18.70 ?  24  VAL   A H    1 
ATOM   505  H HA   A VAL   A 1 24  ? 18.842 3.545   11.169  0.58 20.08 ?  24  VAL   A HA   1 
ATOM   506  H HA   B VAL   A 1 24  ? 18.867 3.304   11.022  0.42 20.02 ?  24  VAL   A HA   1 
ATOM   507  H HB   A VAL   A 1 24  ? 16.843 5.377   10.387  0.58 20.61 ?  24  VAL   A HB   1 
ATOM   508  H HB   B VAL   A 1 24  ? 16.842 5.117   10.231  0.42 20.86 ?  24  VAL   A HB   1 
ATOM   509  H HG11 A VAL   A 1 24  ? 18.401 7.064   11.213  0.58 20.93 ?  24  VAL   A HG11 1 
ATOM   510  H HG11 B VAL   A 1 24  ? 18.510 6.777   10.662  0.42 22.30 ?  24  VAL   A HG11 1 
ATOM   511  H HG12 A VAL   A 1 24  ? 17.492 6.343   12.296  0.58 20.93 ?  24  VAL   A HG12 1 
ATOM   512  H HG12 B VAL   A 1 24  ? 17.912 6.094   11.964  0.42 22.30 ?  24  VAL   A HG12 1 
ATOM   513  H HG13 A VAL   A 1 24  ? 19.006 5.895   12.100  0.58 20.93 ?  24  VAL   A HG13 1 
ATOM   514  H HG13 B VAL   A 1 24  ? 19.335 5.647   11.413  0.42 22.30 ?  24  VAL   A HG13 1 
ATOM   515  H HG21 A VAL   A 1 24  ? 18.360 6.207   8.913   0.58 21.59 ?  24  VAL   A HG21 1 
ATOM   516  H HG21 B VAL   A 1 24  ? 18.377 5.789   8.552   0.42 20.60 ?  24  VAL   A HG21 1 
ATOM   517  H HG22 A VAL   A 1 24  ? 19.529 5.343   9.552   0.58 21.59 ?  24  VAL   A HG22 1 
ATOM   518  H HG22 B VAL   A 1 24  ? 19.278 4.540   8.940   0.42 20.60 ?  24  VAL   A HG22 1 
ATOM   519  H HG23 A VAL   A 1 24  ? 18.373 4.630   8.726   0.58 21.59 ?  24  VAL   A HG23 1 
ATOM   520  H HG23 B VAL   A 1 24  ? 17.828 4.314   8.332   0.42 20.60 ?  24  VAL   A HG23 1 
ATOM   521  N N    A GLU   A 1 25  ? 16.046 3.729   12.733  0.58 17.80 ?  25  GLU   A N    1 
ATOM   522  N N    B GLU   A 1 25  ? 16.008 3.397   12.460  0.42 17.88 ?  25  GLU   A N    1 
ATOM   523  C CA   A GLU   A 1 25  ? 15.455 3.657   14.065  0.58 18.96 ?  25  GLU   A CA   1 
ATOM   524  C CA   B GLU   A 1 25  ? 15.368 3.337   13.770  0.42 19.00 ?  25  GLU   A CA   1 
ATOM   525  C C    A GLU   A 1 25  ? 15.669 2.287   14.694  0.58 17.90 ?  25  GLU   A C    1 
ATOM   526  C C    B GLU   A 1 25  ? 15.635 2.003   14.459  0.42 18.46 ?  25  GLU   A C    1 
ATOM   527  O O    A GLU   A 1 25  ? 15.881 2.183   15.908  0.58 18.40 ?  25  GLU   A O    1 
ATOM   528  O O    B GLU   A 1 25  ? 15.849 1.959   15.676  0.42 18.91 ?  25  GLU   A O    1 
ATOM   529  C CB   A GLU   A 1 25  ? 13.968 4.016   14.003  0.58 21.47 ?  25  GLU   A CB   1 
ATOM   530  C CB   B GLU   A 1 25  ? 13.866 3.605   13.636  0.42 20.84 ?  25  GLU   A CB   1 
ATOM   531  C CG   A GLU   A 1 25  ? 13.716 5.485   13.678  0.58 24.61 ?  25  GLU   A CG   1 
ATOM   532  C CG   B GLU   A 1 25  ? 13.538 5.008   13.139  0.42 23.63 ?  25  GLU   A CG   1 
ATOM   533  C CD   A GLU   A 1 25  ? 14.512 6.433   14.569  0.58 27.29 ?  25  GLU   A CD   1 
ATOM   534  C CD   B GLU   A 1 25  ? 14.185 6.088   13.973  0.42 26.25 ?  25  GLU   A CD   1 
ATOM   535  O OE1  A GLU   A 1 25  ? 14.546 6.216   15.800  0.58 28.22 ?  25  GLU   A OE1  1 
ATOM   536  O OE1  B GLU   A 1 25  ? 14.251 5.920   15.209  0.42 27.55 ?  25  GLU   A OE1  1 
ATOM   537  O OE2  A GLU   A 1 25  ? 15.123 7.381   14.034  0.58 28.30 -1 25  GLU   A OE2  1 
ATOM   538  O OE2  B GLU   A 1 25  ? 14.634 7.098   13.392  0.42 27.27 -1 25  GLU   A OE2  1 
ATOM   539  H H    A GLU   A 1 25  ? 15.480 3.827   12.092  0.58 21.34 ?  25  GLU   A H    1 
ATOM   540  H H    B GLU   A 1 25  ? 15.465 3.381   11.793  0.42 21.44 ?  25  GLU   A H    1 
ATOM   541  H HA   A GLU   A 1 25  ? 15.896 4.302   14.635  0.58 22.73 ?  25  GLU   A HA   1 
ATOM   542  H HA   B GLU   A 1 25  ? 15.745 4.029   14.330  0.42 22.78 ?  25  GLU   A HA   1 
ATOM   543  H HB2  A GLU   A 1 25  ? 13.538 3.483   13.312  0.58 25.74 ?  25  GLU   A HB2  1 
ATOM   544  H HB2  B GLU   A 1 25  ? 13.486 2.976   13.003  0.42 24.98 ?  25  GLU   A HB2  1 
ATOM   545  H HB3  A GLU   A 1 25  ? 13.557 3.830   14.862  0.58 25.74 ?  25  GLU   A HB3  1 
ATOM   546  H HB3  B GLU   A 1 25  ? 13.447 3.494   14.503  0.42 24.98 ?  25  GLU   A HB3  1 
ATOM   547  H HG2  A GLU   A 1 25  ? 13.973 5.650   12.758  0.58 29.51 ?  25  GLU   A HG2  1 
ATOM   548  H HG2  B GLU   A 1 25  ? 13.853 5.107   12.229  0.42 28.33 ?  25  GLU   A HG2  1 
ATOM   549  H HG3  A GLU   A 1 25  ? 12.771 5.676   13.799  0.58 29.51 ?  25  GLU   A HG3  1 
ATOM   550  H HG3  B GLU   A 1 25  ? 12.580 5.147   13.180  0.42 28.33 ?  25  GLU   A HG3  1 
ATOM   551  N N    A GLU   A 1 26  ? 15.625 1.225   13.886  0.58 17.55 ?  26  GLU   A N    1 
ATOM   552  N N    B GLU   A 1 26  ? 15.637 0.903   13.702  0.42 18.15 ?  26  GLU   A N    1 
ATOM   553  C CA   A GLU   A 1 26  ? 15.926 -0.107  14.403  0.58 17.69 ?  26  GLU   A CA   1 
ATOM   554  C CA   B GLU   A 1 26  ? 15.981 -0.388  14.287  0.42 18.24 ?  26  GLU   A CA   1 
ATOM   555  C C    A GLU   A 1 26  ? 17.348 -0.170  14.944  0.58 16.99 ?  26  GLU   A C    1 
ATOM   556  C C    B GLU   A 1 26  ? 17.398 -0.379  14.841  0.42 17.23 ?  26  GLU   A C    1 
ATOM   557  O O    A GLU   A 1 26  ? 17.578 -0.640  16.064  0.58 17.07 ?  26  GLU   A O    1 
ATOM   558  O O    B GLU   A 1 26  ? 17.667 -0.975  15.890  0.42 16.88 ?  26  GLU   A O    1 
ATOM   559  C CB   A GLU   A 1 26  ? 15.743 -1.154  13.303  0.58 19.50 ?  26  GLU   A CB   1 
ATOM   560  C CB   B GLU   A 1 26  ? 15.836 -1.499  13.247  0.42 19.53 ?  26  GLU   A CB   1 
ATOM   561  C CG   A GLU   A 1 26  ? 14.343 -1.712  13.175  0.58 22.26 ?  26  GLU   A CG   1 
ATOM   562  C CG   B GLU   A 1 26  ? 14.408 -1.913  12.979  0.42 20.61 ?  26  GLU   A CG   1 
ATOM   563  C CD   A GLU   A 1 26  ? 13.944 -2.593  14.356  0.58 23.51 ?  26  GLU   A CD   1 
ATOM   564  C CD   B GLU   A 1 26  ? 13.720 -2.459  14.207  0.42 20.56 ?  26  GLU   A CD   1 
ATOM   565  O OE1  A GLU   A 1 26  ? 14.306 -3.794  14.397  0.58 23.77 ?  26  GLU   A OE1  1 
ATOM   566  O OE1  B GLU   A 1 26  ? 14.302 -3.331  14.885  0.42 20.64 ?  26  GLU   A OE1  1 
ATOM   567  O OE2  A GLU   A 1 26  ? 13.265 -2.071  15.253  0.58 24.24 -1 26  GLU   A OE2  1 
ATOM   568  O OE2  B GLU   A 1 26  ? 12.601 -1.994  14.496  0.42 19.77 -1 26  GLU   A OE2  1 
ATOM   569  H H    A GLU   A 1 26  ? 15.429 1.252   13.050  0.58 21.04 ?  26  GLU   A H    1 
ATOM   570  H H    B GLU   A 1 26  ? 15.445 0.878   12.866  0.42 21.75 ?  26  GLU   A H    1 
ATOM   571  H HA   A GLU   A 1 26  ? 15.317 -0.312  15.127  0.58 21.20 ?  26  GLU   A HA   1 
ATOM   572  H HA   B GLU   A 1 26  ? 15.382 -0.577  15.023  0.42 21.86 ?  26  GLU   A HA   1 
ATOM   573  H HB2  A GLU   A 1 26  ? 15.977 -0.751  12.452  0.58 23.38 ?  26  GLU   A HB2  1 
ATOM   574  H HB2  B GLU   A 1 26  ? 16.215 -1.194  12.407  0.42 23.41 ?  26  GLU   A HB2  1 
ATOM   575  H HB3  A GLU   A 1 26  ? 16.337 -1.897  13.487  0.58 23.38 ?  26  GLU   A HB3  1 
ATOM   576  H HB3  B GLU   A 1 26  ? 16.319 -2.284  13.555  0.42 23.41 ?  26  GLU   A HB3  1 
ATOM   577  H HG2  A GLU   A 1 26  ? 13.723 -0.966  13.111  0.58 26.69 ?  26  GLU   A HG2  1 
ATOM   578  H HG2  B GLU   A 1 26  ? 13.902 -1.141  12.689  0.42 24.71 ?  26  GLU   A HG2  1 
ATOM   579  H HG3  A GLU   A 1 26  ? 14.291 -2.254  12.374  0.58 26.69 ?  26  GLU   A HG3  1 
ATOM   580  H HG3  B GLU   A 1 26  ? 14.397 -2.600  12.296  0.42 24.71 ?  26  GLU   A HG3  1 
ATOM   581  N N    . ALA   A 1 27  ? 18.320 0.294   14.152  1.00 16.32 ?  27  ALA   A N    1 
ATOM   582  C CA   . ALA   A 1 27  ? 19.708 0.281   14.599  1.00 16.82 ?  27  ALA   A CA   1 
ATOM   583  C C    . ALA   A 1 27  ? 19.875 1.085   15.881  1.00 18.21 ?  27  ALA   A C    1 
ATOM   584  O O    . ALA   A 1 27  ? 20.547 0.640   16.819  1.00 17.89 ?  27  ALA   A O    1 
ATOM   585  C CB   . ALA   A 1 27  ? 20.630 0.804   13.493  1.00 16.28 ?  27  ALA   A CB   1 
ATOM   586  H H    A ALA   A 1 27  ? 18.200 0.617   13.362  0.58 19.57 ?  27  ALA   A H    1 
ATOM   587  H H    B ALA   A 1 27  ? 18.169 0.758   13.441  0.42 19.57 ?  27  ALA   A H    1 
ATOM   588  H HA   . ALA   A 1 27  ? 19.964 -0.632  14.785  1.00 20.16 ?  27  ALA   A HA   1 
ATOM   589  H HB1  . ALA   A 1 27  ? 21.548 0.786   13.811  1.00 19.51 ?  27  ALA   A HB1  1 
ATOM   590  H HB2  . ALA   A 1 27  ? 20.544 0.234   12.710  1.00 19.51 ?  27  ALA   A HB2  1 
ATOM   591  H HB3  . ALA   A 1 27  ? 20.378 1.713   13.267  1.00 19.51 ?  27  ALA   A HB3  1 
ATOM   592  N N    A LYS   A 1 28  ? 19.255 2.264   15.958  0.58 19.91 ?  28  LYS   A N    1 
ATOM   593  N N    B LYS   A 1 28  ? 19.257 2.268   15.942  0.42 20.04 ?  28  LYS   A N    1 
ATOM   594  C CA   A LYS   A 1 28  ? 19.413 3.086   17.154  0.58 22.91 ?  28  LYS   A CA   1 
ATOM   595  C CA   B LYS   A 1 28  ? 19.365 3.102   17.135  0.42 22.79 ?  28  LYS   A CA   1 
ATOM   596  C C    A LYS   A 1 28  ? 18.851 2.404   18.395  0.58 24.02 ?  28  LYS   A C    1 
ATOM   597  C C    B LYS   A 1 28  ? 18.791 2.393   18.354  0.42 23.98 ?  28  LYS   A C    1 
ATOM   598  O O    A LYS   A 1 28  ? 19.330 2.653   19.507  0.58 25.61 ?  28  LYS   A O    1 
ATOM   599  O O    B LYS   A 1 28  ? 19.348 2.484   19.454  0.42 24.97 ?  28  LYS   A O    1 
ATOM   600  C CB   A LYS   A 1 28  ? 18.787 4.465   16.947  0.58 25.56 ?  28  LYS   A CB   1 
ATOM   601  C CB   B LYS   A 1 28  ? 18.671 4.447   16.902  0.42 24.91 ?  28  LYS   A CB   1 
ATOM   602  C CG   A LYS   A 1 28  ? 19.654 5.388   16.108  0.58 27.98 ?  28  LYS   A CG   1 
ATOM   603  C CG   B LYS   A 1 28  ? 19.434 5.376   15.971  0.42 27.00 ?  28  LYS   A CG   1 
ATOM   604  C CD   A LYS   A 1 28  ? 19.181 6.826   16.162  0.58 30.48 ?  28  LYS   A CD   1 
ATOM   605  C CD   B LYS   A 1 28  ? 18.951 6.816   16.069  0.42 29.30 ?  28  LYS   A CD   1 
ATOM   606  C CE   A LYS   A 1 28  ? 17.889 7.008   15.397  0.58 32.26 ?  28  LYS   A CE   1 
ATOM   607  C CE   B LYS   A 1 28  ? 17.705 7.051   15.238  0.42 31.06 ?  28  LYS   A CE   1 
ATOM   608  N NZ   A LYS   A 1 28  ? 17.479 8.437   15.361  0.58 33.39 ?  28  LYS   A NZ   1 
ATOM   609  N NZ   B LYS   A 1 28  ? 17.376 8.503   15.146  0.42 32.06 ?  28  LYS   A NZ   1 
ATOM   610  H H    A LYS   A 1 28  ? 18.758 2.603   15.346  0.58 23.87 ?  28  LYS   A H    1 
ATOM   611  H H    B LYS   A 1 28  ? 18.774 2.601   15.316  0.42 24.03 ?  28  LYS   A H    1 
ATOM   612  H HA   A LYS   A 1 28  ? 20.359 3.221   17.308  0.58 27.47 ?  28  LYS   A HA   1 
ATOM   613  H HA   B LYS   A 1 28  ? 20.300 3.281   17.312  0.42 27.33 ?  28  LYS   A HA   1 
ATOM   614  H HB2  A LYS   A 1 28  ? 17.936 4.363   16.495  0.58 30.65 ?  28  LYS   A HB2  1 
ATOM   615  H HB2  B LYS   A 1 28  ? 17.800 4.291   16.506  0.42 29.87 ?  28  LYS   A HB2  1 
ATOM   616  H HB3  A LYS   A 1 28  ? 18.655 4.886   17.812  0.58 30.65 ?  28  LYS   A HB3  1 
ATOM   617  H HB3  B LYS   A 1 28  ? 18.572 4.903   17.751  0.42 29.87 ?  28  LYS   A HB3  1 
ATOM   618  H HG2  A LYS   A 1 28  ? 20.565 5.358   16.440  0.58 33.55 ?  28  LYS   A HG2  1 
ATOM   619  H HG2  B LYS   A 1 28  ? 20.374 5.359   16.204  0.42 32.38 ?  28  LYS   A HG2  1 
ATOM   620  H HG3  A LYS   A 1 28  ? 19.626 5.096   15.184  0.58 33.55 ?  28  LYS   A HG3  1 
ATOM   621  H HG3  B LYS   A 1 28  ? 19.311 5.081   15.055  0.42 32.38 ?  28  LYS   A HG3  1 
ATOM   622  H HD2  A LYS   A 1 28  ? 19.026 7.080   17.086  0.58 36.55 ?  28  LYS   A HD2  1 
ATOM   623  H HD2  B LYS   A 1 28  ? 18.740 7.022   16.994  0.42 35.14 ?  28  LYS   A HD2  1 
ATOM   624  H HD3  A LYS   A 1 28  ? 19.854 7.401   15.764  0.58 36.55 ?  28  LYS   A HD3  1 
ATOM   625  H HD3  B LYS   A 1 28  ? 19.646 7.410   15.746  0.42 35.14 ?  28  LYS   A HD3  1 
ATOM   626  H HE2  A LYS   A 1 28  ? 18.013 6.702   14.485  0.58 38.69 ?  28  LYS   A HE2  1 
ATOM   627  H HE2  B LYS   A 1 28  ? 17.851 6.715   14.340  0.42 37.24 ?  28  LYS   A HE2  1 
ATOM   628  H HE3  A LYS   A 1 28  ? 17.186 6.499   15.830  0.58 38.69 ?  28  LYS   A HE3  1 
ATOM   629  H HE3  B LYS   A 1 28  ? 16.954 6.595   15.649  0.42 37.24 ?  28  LYS   A HE3  1 
ATOM   630  H HZ1  A LYS   A 1 28  ? 16.719 8.524   14.907  0.58 40.05 ?  28  LYS   A HZ1  1 
ATOM   631  H HZ1  B LYS   A 1 28  ? 16.644 8.619   14.654  0.42 38.44 ?  28  LYS   A HZ1  1 
ATOM   632  H HZ2  A LYS   A 1 28  ? 17.359 8.739   16.189  0.58 40.05 ?  28  LYS   A HZ2  1 
ATOM   633  H HZ2  B LYS   A 1 28  ? 17.235 8.835   15.960  0.42 38.44 ?  28  LYS   A HZ2  1 
ATOM   634  H HZ3  A LYS   A 1 28  ? 18.111 8.924   14.964  0.58 40.05 ?  28  LYS   A HZ3  1 
ATOM   635  H HZ3  B LYS   A 1 28  ? 18.052 8.944   14.768  0.42 38.44 ?  28  LYS   A HZ3  1 
ATOM   636  N N    A LYS   A 1 29  ? 17.849 1.539   18.231  0.58 24.15 ?  29  LYS   A N    1 
ATOM   637  N N    B LYS   A 1 29  ? 17.684 1.670   18.176  0.42 24.54 ?  29  LYS   A N    1 
ATOM   638  C CA   A LYS   A 1 29  ? 17.267 0.841   19.374  0.58 25.47 ?  29  LYS   A CA   1 
ATOM   639  C CA   B LYS   A 1 29  ? 17.053 0.987   19.301  0.42 25.76 ?  29  LYS   A CA   1 
ATOM   640  C C    A LYS   A 1 29  ? 18.102 -0.373  19.770  0.58 24.83 ?  29  LYS   A C    1 
ATOM   641  C C    B LYS   A 1 29  ? 17.849 -0.243  19.717  0.42 25.06 ?  29  LYS   A C    1 
ATOM   642  O O    A LYS   A 1 29  ? 18.443 -0.547  20.945  0.58 26.16 ?  29  LYS   A O    1 
ATOM   643  O O    B LYS   A 1 29  ? 18.101 -0.458  20.908  0.42 25.72 ?  29  LYS   A O    1 
ATOM   644  C CB   A LYS   A 1 29  ? 15.835 0.412   19.040  0.58 27.95 ?  29  LYS   A CB   1 
ATOM   645  C CB   B LYS   A 1 29  ? 15.627 0.585   18.925  0.42 27.96 ?  29  LYS   A CB   1 
ATOM   646  C CG   A LYS   A 1 29  ? 15.115 -0.312  20.168  0.58 30.98 ?  29  LYS   A CG   1 
ATOM   647  C CG   B LYS   A 1 29  ? 14.854 -0.094  20.044  0.42 30.35 ?  29  LYS   A CG   1 
ATOM   648  C CD   A LYS   A 1 29  ? 14.752 0.643   21.292  0.58 33.70 ?  29  LYS   A CD   1 
ATOM   649  C CD   B LYS   A 1 29  ? 14.577 0.870   21.184  0.42 32.53 ?  29  LYS   A CD   1 
ATOM   650  C CE   A LYS   A 1 29  ? 13.878 -0.034  22.335  0.58 35.43 ?  29  LYS   A CE   1 
ATOM   651  C CE   B LYS   A 1 29  ? 13.708 0.230   22.251  0.42 33.97 ?  29  LYS   A CE   1 
ATOM   652  N NZ   A LYS   A 1 29  ? 13.430 0.925   23.381  0.58 36.45 ?  29  LYS   A NZ   1 
ATOM   653  N NZ   B LYS   A 1 29  ? 13.377 1.192   23.335  0.42 34.84 ?  29  LYS   A NZ   1 
ATOM   654  H H    A LYS   A 1 29  ? 17.491 1.341   17.476  0.58 28.96 ?  29  LYS   A H    1 
ATOM   655  H H    B LYS   A 1 29  ? 17.286 1.561   17.423  0.42 29.43 ?  29  LYS   A H    1 
ATOM   656  H HA   A LYS   A 1 29  ? 17.230 1.443   20.132  0.58 30.54 ?  29  LYS   A HA   1 
ATOM   657  H HA   B LYS   A 1 29  ? 17.011 1.591   20.058  0.42 30.89 ?  29  LYS   A HA   1 
ATOM   658  H HB2  A LYS   A 1 29  ? 15.316 1.203   18.823  0.58 33.52 ?  29  LYS   A HB2  1 
ATOM   659  H HB2  B LYS   A 1 29  ? 15.136 1.381   18.671  0.42 33.52 ?  29  LYS   A HB2  1 
ATOM   660  H HB3  A LYS   A 1 29  ? 15.857 -0.184  18.276  0.58 33.52 ?  29  LYS   A HB3  1 
ATOM   661  H HB3  B LYS   A 1 29  ? 15.664 -0.032  18.177  0.42 33.52 ?  29  LYS   A HB3  1 
ATOM   662  H HG2  A LYS   A 1 29  ? 14.295 -0.699  19.825  0.58 37.16 ?  29  LYS   A HG2  1 
ATOM   663  H HG2  B LYS   A 1 29  ? 14.005 -0.408  19.699  0.42 36.40 ?  29  LYS   A HG2  1 
ATOM   664  H HG3  A LYS   A 1 29  ? 15.685 -1.009  20.531  0.58 37.16 ?  29  LYS   A HG3  1 
ATOM   665  H HG3  B LYS   A 1 29  ? 15.369 -0.840  20.392  0.42 36.40 ?  29  LYS   A HG3  1 
ATOM   666  H HD2  A LYS   A 1 29  ? 15.564 0.949   21.726  0.58 40.42 ?  29  LYS   A HD2  1 
ATOM   667  H HD2  B LYS   A 1 29  ? 15.416 1.133   21.594  0.42 39.01 ?  29  LYS   A HD2  1 
ATOM   668  H HD3  A LYS   A 1 29  ? 14.263 1.396   20.925  0.58 40.42 ?  29  LYS   A HD3  1 
ATOM   669  H HD3  B LYS   A 1 29  ? 14.113 1.648   20.838  0.42 39.01 ?  29  LYS   A HD3  1 
ATOM   670  H HE2  A LYS   A 1 29  ? 13.091 -0.402  21.903  0.58 42.49 ?  29  LYS   A HE2  1 
ATOM   671  H HE2  B LYS   A 1 29  ? 12.879 -0.073  21.849  0.42 40.74 ?  29  LYS   A HE2  1 
ATOM   672  H HE3  A LYS   A 1 29  ? 14.384 -0.740  22.767  0.58 42.49 ?  29  LYS   A HE3  1 
ATOM   673  H HE3  B LYS   A 1 29  ? 14.183 -0.520  22.644  0.42 40.74 ?  29  LYS   A HE3  1 
ATOM   674  H HZ1  A LYS   A 1 29  ? 12.920 0.506   23.979  0.58 43.72 ?  29  LYS   A HZ1  1 
ATOM   675  H HZ1  B LYS   A 1 29  ? 12.868 0.796   23.948  0.42 41.78 ?  29  LYS   A HZ1  1 
ATOM   676  H HZ2  A LYS   A 1 29  ? 14.135 1.274   23.796  0.58 43.72 ?  29  LYS   A HZ2  1 
ATOM   677  H HZ2  B LYS   A 1 29  ? 14.124 1.482   23.722  0.42 41.78 ?  29  LYS   A HZ2  1 
ATOM   678  H HZ3  A LYS   A 1 29  ? 12.958 1.582   23.009  0.58 43.72 ?  29  LYS   A HZ3  1 
ATOM   679  H HZ3  B LYS   A 1 29  ? 12.936 1.888   22.999  0.42 41.78 ?  29  LYS   A HZ3  1 
ATOM   680  N N    A VAL   A 1 30  ? 18.430 -1.225  18.799  0.58 23.39 ?  30  VAL   A N    1 
ATOM   681  N N    B VAL   A 1 30  ? 18.236 -1.071  18.746  0.42 24.12 ?  30  VAL   A N    1 
ATOM   682  C CA   A VAL   A 1 30  ? 19.076 -2.500  19.095  0.58 22.92 ?  30  VAL   A CA   1 
ATOM   683  C CA   B VAL   A 1 30  ? 18.876 -2.344  19.062  0.42 23.60 ?  30  VAL   A CA   1 
ATOM   684  C C    A VAL   A 1 30  ? 20.578 -2.348  19.309  0.58 21.48 ?  30  VAL   A C    1 
ATOM   685  C C    B VAL   A 1 30  ? 20.373 -2.180  19.297  0.42 22.90 ?  30  VAL   A C    1 
ATOM   686  O O    A VAL   A 1 30  ? 21.170 -3.089  20.101  0.58 21.91 ?  30  VAL   A O    1 
ATOM   687  O O    B VAL   A 1 30  ? 20.956 -2.902  20.114  0.42 22.91 ?  30  VAL   A O    1 
ATOM   688  C CB   A VAL   A 1 30  ? 18.769 -3.501  17.967  0.58 23.73 ?  30  VAL   A CB   1 
ATOM   689  C CB   B VAL   A 1 30  ? 18.587 -3.362  17.945  0.42 23.87 ?  30  VAL   A CB   1 
ATOM   690  C CG1  A VAL   A 1 30  ? 19.546 -4.796  18.167  0.58 24.27 ?  30  VAL   A CG1  1 
ATOM   691  C CG1  B VAL   A 1 30  ? 19.315 -4.672  18.209  0.42 24.22 ?  30  VAL   A CG1  1 
ATOM   692  C CG2  A VAL   A 1 30  ? 17.274 -3.775  17.894  0.58 24.08 ?  30  VAL   A CG2  1 
ATOM   693  C CG2  B VAL   A 1 30  ? 17.091 -3.595  17.815  0.42 23.99 ?  30  VAL   A CG2  1 
ATOM   694  H H    A VAL   A 1 30  ? 18.273 -1.096  17.966  0.58 28.05 ?  30  VAL   A H    1 
ATOM   695  H H    B VAL   A 1 30  ? 18.127 -0.928  17.905  0.42 28.92 ?  30  VAL   A H    1 
ATOM   696  H HA   A VAL   A 1 30  ? 18.697 -2.860  19.911  0.58 27.48 ?  30  VAL   A HA   1 
ATOM   697  H HA   B VAL   A 1 30  ? 18.484 -2.690  19.878  0.42 28.29 ?  30  VAL   A HA   1 
ATOM   698  H HB   A VAL   A 1 30  ? 19.049 -3.118  17.121  0.58 28.45 ?  30  VAL   A HB   1 
ATOM   699  H HB   B VAL   A 1 30  ? 18.912 -3.008  17.103  0.42 28.62 ?  30  VAL   A HB   1 
ATOM   700  H HG11 A VAL   A 1 30  ? 19.166 -5.481  17.594  0.58 29.10 ?  30  VAL   A HG11 1 
ATOM   701  H HG11 B VAL   A 1 30  ? 18.937 -5.362  17.640  0.42 29.04 ?  30  VAL   A HG11 1 
ATOM   702  H HG12 A VAL   A 1 30  ? 20.476 -4.652  17.937  0.58 29.10 ?  30  VAL   A HG12 1 
ATOM   703  H HG12 B VAL   A 1 30  ? 20.257 -4.560  18.009  0.42 29.04 ?  30  VAL   A HG12 1 
ATOM   704  H HG13 A VAL   A 1 30  ? 19.471 -5.068  19.096  0.58 29.10 ?  30  VAL   A HG13 1 
ATOM   705  H HG13 B VAL   A 1 30  ? 19.199 -4.914  19.141  0.42 29.04 ?  30  VAL   A HG13 1 
ATOM   706  H HG21 A VAL   A 1 30  ? 17.109 -4.441  17.209  0.58 28.87 ?  30  VAL   A HG21 1 
ATOM   707  H HG21 B VAL   A 1 30  ? 16.935 -4.282  17.147  0.42 28.76 ?  30  VAL   A HG21 1 
ATOM   708  H HG22 A VAL   A 1 30  ? 16.971 -4.103  18.755  0.58 28.87 ?  30  VAL   A HG22 1 
ATOM   709  H HG22 B VAL   A 1 30  ? 16.741 -3.884  18.673  0.42 28.76 ?  30  VAL   A HG22 1 
ATOM   710  H HG23 A VAL   A 1 30  ? 16.814 -2.951  17.672  0.58 28.87 ?  30  VAL   A HG23 1 
ATOM   711  H HG23 B VAL   A 1 30  ? 16.665 -2.768  17.544  0.42 28.76 ?  30  VAL   A HG23 1 
ATOM   712  N N    A LYS   A 1 31  ? 21.219 -1.411  18.618  0.58 20.16 ?  31  LYS   A N    1 
ATOM   713  N N    B LYS   A 1 31  ? 21.014 -1.245  18.603  0.42 22.63 ?  31  LYS   A N    1 
ATOM   714  C CA   A LYS   A 1 31  ? 22.674 -1.308  18.578  0.58 21.11 ?  31  LYS   A CA   1 
ATOM   715  C CA   B LYS   A 1 31  ? 22.468 -1.139  18.567  0.42 23.13 ?  31  LYS   A CA   1 
ATOM   716  C C    A LYS   A 1 31  ? 23.290 -2.666  18.228  0.58 18.75 ?  31  LYS   A C    1 
ATOM   717  C C    B LYS   A 1 31  ? 23.086 -2.508  18.268  0.42 20.87 ?  31  LYS   A C    1 
ATOM   718  O O    A LYS   A 1 31  ? 24.075 -3.219  19.006  0.58 19.64 ?  31  LYS   A O    1 
ATOM   719  O O    B LYS   A 1 31  ? 23.840 -3.047  19.084  0.42 21.50 ?  31  LYS   A O    1 
ATOM   720  C CB   A LYS   A 1 31  ? 23.245 -0.770  19.882  0.58 25.75 ?  31  LYS   A CB   1 
ATOM   721  C CB   B LYS   A 1 31  ? 23.032 -0.556  19.855  0.42 26.60 ?  31  LYS   A CB   1 
ATOM   722  C CG   A LYS   A 1 31  ? 22.563 0.491   20.386  0.58 30.55 ?  31  LYS   A CG   1 
ATOM   723  C CG   B LYS   A 1 31  ? 22.376 0.741   20.283  0.42 30.29 ?  31  LYS   A CG   1 
ATOM   724  C CD   A LYS   A 1 31  ? 23.570 1.566   20.773  0.58 34.31 ?  31  LYS   A CD   1 
ATOM   725  C CD   B LYS   A 1 31  ? 23.398 1.719   20.836  0.42 33.18 ?  31  LYS   A CD   1 
ATOM   726  C CE   A LYS   A 1 31  ? 22.938 2.616   21.678  0.58 36.90 ?  31  LYS   A CE   1 
ATOM   727  C CE   B LYS   A 1 31  ? 22.732 2.802   21.669  0.42 35.26 ?  31  LYS   A CE   1 
ATOM   728  N NZ   A LYS   A 1 31  ? 21.706 3.214   21.095  0.58 38.19 ?  31  LYS   A NZ   1 
ATOM   729  N NZ   B LYS   A 1 31  ? 21.578 3.427   20.968  0.42 36.42 ?  31  LYS   A NZ   1 
ATOM   730  H H    A LYS   A 1 31  ? 20.824 -0.807  18.150  0.58 24.17 ?  31  LYS   A H    1 
ATOM   731  H H    B LYS   A 1 31  ? 20.618 -0.646  18.134  0.42 27.13 ?  31  LYS   A H    1 
ATOM   732  H HA   A LYS   A 1 31  ? 22.918 -0.685  17.877  0.58 25.31 ?  31  LYS   A HA   1 
ATOM   733  H HA   B LYS   A 1 31  ? 22.711 -0.540  17.848  0.42 27.73 ?  31  LYS   A HA   1 
ATOM   734  H HB2  A LYS   A 1 31  ? 23.156 -1.452  20.564  0.58 30.88 ?  31  LYS   A HB2  1 
ATOM   735  H HB2  B LYS   A 1 31  ? 22.908 -1.198  20.569  0.42 31.89 ?  31  LYS   A HB2  1 
ATOM   736  H HB3  A LYS   A 1 31  ? 24.186 -0.564  19.746  0.58 30.88 ?  31  LYS   A HB3  1 
ATOM   737  H HB3  B LYS   A 1 31  ? 23.981 -0.383  19.730  0.42 31.89 ?  31  LYS   A HB3  1 
ATOM   738  H HG2  A LYS   A 1 31  ? 21.994 0.848   19.687  0.58 36.64 ?  31  LYS   A HG2  1 
ATOM   739  H HG2  B LYS   A 1 31  ? 21.945 1.151   19.517  0.42 36.32 ?  31  LYS   A HG2  1 
ATOM   740  H HG3  A LYS   A 1 31  ? 22.035 0.275   21.170  0.58 36.64 ?  31  LYS   A HG3  1 
ATOM   741  H HG3  B LYS   A 1 31  ? 21.724 0.557   20.977  0.42 36.32 ?  31  LYS   A HG3  1 
ATOM   742  H HD2  A LYS   A 1 31  ? 24.310 1.158   21.250  0.58 41.15 ?  31  LYS   A HD2  1 
ATOM   743  H HD2  B LYS   A 1 31  ? 24.026 1.241   21.401  0.42 39.79 ?  31  LYS   A HD2  1 
ATOM   744  H HD3  A LYS   A 1 31  ? 23.892 2.008   19.970  0.58 41.15 ?  31  LYS   A HD3  1 
ATOM   745  H HD3  B LYS   A 1 31  ? 23.866 2.144   20.099  0.42 39.79 ?  31  LYS   A HD3  1 
ATOM   746  H HE2  A LYS   A 1 31  ? 22.700 2.202   22.523  0.58 44.25 ?  31  LYS   A HE2  1 
ATOM   747  H HE2  B LYS   A 1 31  ? 22.408 2.410   22.494  0.42 42.29 ?  31  LYS   A HE2  1 
ATOM   748  H HE3  A LYS   A 1 31  ? 23.576 3.331   21.827  0.58 44.25 ?  31  LYS   A HE3  1 
ATOM   749  H HE3  B LYS   A 1 31  ? 23.381 3.496   21.861  0.42 42.29 ?  31  LYS   A HE3  1 
ATOM   750  H HZ1  A LYS   A 1 31  ? 21.382 3.838   21.642  0.58 45.81 ?  31  LYS   A HZ1  1 
ATOM   751  H HZ1  B LYS   A 1 31  ? 21.253 4.095   21.457  0.42 43.68 ?  31  LYS   A HZ1  1 
ATOM   752  H HZ2  A LYS   A 1 31  ? 21.891 3.587   20.308  0.58 45.81 ?  31  LYS   A HZ2  1 
ATOM   753  H HZ2  B LYS   A 1 31  ? 21.838 3.744   20.178  0.42 43.68 ?  31  LYS   A HZ2  1 
ATOM   754  H HZ3  A LYS   A 1 31  ? 21.087 2.584   20.978  0.58 45.81 ?  31  LYS   A HZ3  1 
ATOM   755  H HZ3  B LYS   A 1 31  ? 20.936 2.823   20.840  0.42 43.68 ?  31  LYS   A HZ3  1 
ATOM   756  N N    A PRO   A 1 32  ? 22.960 -3.218  17.063  0.58 17.12 ?  32  PRO   A N    1 
ATOM   757  N N    B PRO   A 1 32  ? 22.788 -3.086  17.108  0.42 18.58 ?  32  PRO   A N    1 
ATOM   758  C CA   A PRO   A 1 32  ? 23.434 -4.560  16.719  0.58 17.45 ?  32  PRO   A CA   1 
ATOM   759  C CA   B PRO   A 1 32  ? 23.270 -4.436  16.808  0.42 17.91 ?  32  PRO   A CA   1 
ATOM   760  C C    A PRO   A 1 32  ? 24.936 -4.584  16.508  0.58 17.50 ?  32  PRO   A C    1 
ATOM   761  C C    B PRO   A 1 32  ? 24.777 -4.447  16.621  0.42 17.39 ?  32  PRO   A C    1 
ATOM   762  O O    A PRO   A 1 32  ? 25.580 -3.563  16.260  0.58 17.03 ?  32  PRO   A O    1 
ATOM   763  O O    B PRO   A 1 32  ? 25.432 -3.410  16.504  0.42 17.45 ?  32  PRO   A O    1 
ATOM   764  C CB   A PRO   A 1 32  ? 22.709 -4.854  15.403  0.58 17.52 ?  32  PRO   A CB   1 
ATOM   765  C CB   B PRO   A 1 32  ? 22.557 -4.768  15.495  0.42 18.05 ?  32  PRO   A CB   1 
ATOM   766  C CG   A PRO   A 1 32  ? 22.536 -3.504  14.784  0.58 16.64 ?  32  PRO   A CG   1 
ATOM   767  C CG   B PRO   A 1 32  ? 22.408 -3.441  14.829  0.42 17.67 ?  32  PRO   A CG   1 
ATOM   768  C CD   A PRO   A 1 32  ? 22.242 -2.590  15.941  0.58 16.56 ?  32  PRO   A CD   1 
ATOM   769  C CD   B PRO   A 1 32  ? 22.107 -2.481  15.950  0.42 17.85 ?  32  PRO   A CD   1 
ATOM   770  H HA   A PRO   A 1 32  ? 23.178 -5.205  17.397  0.58 20.91 ?  32  PRO   A HA   1 
ATOM   771  H HA   B PRO   A 1 32  ? 23.012 -5.064  17.499  0.42 21.46 ?  32  PRO   A HA   1 
ATOM   772  H HB2  A PRO   A 1 32  ? 23.259 -5.430  14.845  0.58 21.00 ?  32  PRO   A HB2  1 
ATOM   773  H HB2  B PRO   A 1 32  ? 23.104 -5.367  14.961  0.42 21.63 ?  32  PRO   A HB2  1 
ATOM   774  H HB3  A PRO   A 1 32  ? 21.851 -5.271  15.586  0.58 21.00 ?  32  PRO   A HB3  1 
ATOM   775  H HB3  B PRO   A 1 32  ? 21.689 -5.164  15.680  0.42 21.63 ?  32  PRO   A HB3  1 
ATOM   776  H HG2  A PRO   A 1 32  ? 23.355 -3.248  14.333  0.58 19.94 ?  32  PRO   A HG2  1 
ATOM   777  H HG2  B PRO   A 1 32  ? 23.237 -3.205  14.383  0.42 21.18 ?  32  PRO   A HG2  1 
ATOM   778  H HG3  A PRO   A 1 32  ? 21.792 -3.529  14.161  0.58 19.94 ?  32  PRO   A HG3  1 
ATOM   779  H HG3  B PRO   A 1 32  ? 21.674 -3.474  14.195  0.42 21.18 ?  32  PRO   A HG3  1 
ATOM   780  H HD2  A PRO   A 1 32  ? 22.595 -1.705  15.757  0.58 19.85 ?  32  PRO   A HD2  1 
ATOM   781  H HD2  B PRO   A 1 32  ? 22.481 -1.608  15.748  0.42 21.40 ?  32  PRO   A HD2  1 
ATOM   782  H HD3  A PRO   A 1 32  ? 21.291 -2.569  16.115  0.58 19.85 ?  32  PRO   A HD3  1 
ATOM   783  H HD3  B PRO   A 1 32  ? 21.152 -2.434  16.102  0.42 21.40 ?  32  PRO   A HD3  1 
ATOM   784  N N    A THR   A 1 33  ? 25.490 -5.795  16.579  0.58 17.42 ?  33  THR   A N    1 
ATOM   785  N N    B THR   A 1 33  ? 25.327 -5.661  16.583  0.42 17.10 ?  33  THR   A N    1 
ATOM   786  C CA   A THR   A 1 33  ? 26.900 -5.970  16.258  0.58 17.70 ?  33  THR   A CA   1 
ATOM   787  C CA   B THR   A 1 33  ? 26.748 -5.812  16.296  0.42 16.96 ?  33  THR   A CA   1 
ATOM   788  C C    A THR   A 1 33  ? 27.192 -5.519  14.834  0.58 16.13 ?  33  THR   A C    1 
ATOM   789  C C    B THR   A 1 33  ? 27.070 -5.346  14.881  0.42 15.72 ?  33  THR   A C    1 
ATOM   790  O O    A THR   A 1 33  ? 28.251 -4.935  14.568  0.58 16.15 ?  33  THR   A O    1 
ATOM   791  O O    B THR   A 1 33  ? 28.041 -4.611  14.662  0.42 15.59 ?  33  THR   A O    1 
ATOM   792  C CB   A THR   A 1 33  ? 27.302 -7.433  16.457  0.58 19.60 ?  33  THR   A CB   1 
ATOM   793  C CB   B THR   A 1 33  ? 27.164 -7.269  16.494  0.42 18.36 ?  33  THR   A CB   1 
ATOM   794  O OG1  A THR   A 1 33  ? 27.038 -7.826  17.808  0.58 20.99 ?  33  THR   A OG1  1 
ATOM   795  O OG1  B THR   A 1 33  ? 26.817 -7.687  17.819  0.42 19.32 ?  33  THR   A OG1  1 
ATOM   796  C CG2  A THR   A 1 33  ? 28.779 -7.631  16.169  0.58 20.44 ?  33  THR   A CG2  1 
ATOM   797  C CG2  B THR   A 1 33  ? 28.664 -7.430  16.292  0.42 19.06 ?  33  THR   A CG2  1 
ATOM   798  H H    A THR   A 1 33  ? 25.077 -6.516  16.794  0.58 20.88 ?  33  THR   A H    1 
ATOM   799  H H    B THR   A 1 33  ? 24.906 -6.399  16.725  0.42 20.49 ?  33  THR   A H    1 
ATOM   800  H HA   A THR   A 1 33  ? 27.433 -5.426  16.857  0.58 21.22 ?  33  THR   A HA   1 
ATOM   801  H HA   B THR   A 1 33  ? 27.256 -5.266  16.915  0.42 20.32 ?  33  THR   A HA   1 
ATOM   802  H HB   A THR   A 1 33  ? 26.788 -7.992  15.851  0.58 23.49 ?  33  THR   A HB   1 
ATOM   803  H HB   B THR   A 1 33  ? 26.704 -7.831  15.848  0.42 22.01 ?  33  THR   A HB   1 
ATOM   804  H HG1  A THR   A 1 33  ? 27.469 -7.335  18.338  0.58 25.17 ?  33  THR   A HG1  1 
ATOM   805  H HG1  B THR   A 1 33  ? 27.219 -7.209  18.384  0.42 23.16 ?  33  THR   A HG1  1 
ATOM   806  H HG21 A THR   A 1 33  ? 29.054 -8.513  16.464  0.58 24.51 ?  33  THR   A HG21 1 
ATOM   807  H HG21 B THR   A 1 33  ? 28.942 -8.316  16.570  0.42 22.85 ?  33  THR   A HG21 1 
ATOM   808  H HG22 A THR   A 1 33  ? 28.950 -7.550  15.219  0.58 24.51 ?  33  THR   A HG22 1 
ATOM   809  H HG22 B THR   A 1 33  ? 28.890 -7.310  15.355  0.42 22.85 ?  33  THR   A HG22 1 
ATOM   810  H HG23 A THR   A 1 33  ? 29.300 -6.965  16.644  0.58 24.51 ?  33  THR   A HG23 1 
ATOM   811  H HG23 B THR   A 1 33  ? 29.141 -6.770  16.819  0.42 22.85 ?  33  THR   A HG23 1 
ATOM   812  N N    . VAL   A 1 34  ? 26.260 -5.760  13.909  1.00 14.71 ?  34  VAL   A N    1 
ATOM   813  C CA   . VAL   A 1 34  ? 26.456 -5.428  12.499  1.00 13.18 ?  34  VAL   A CA   1 
ATOM   814  C C    . VAL   A 1 34  ? 25.162 -4.869  11.921  1.00 12.84 ?  34  VAL   A C    1 
ATOM   815  O O    . VAL   A 1 34  ? 24.124 -5.542  11.952  1.00 13.70 ?  34  VAL   A O    1 
ATOM   816  C CB   . VAL   A 1 34  ? 26.912 -6.641  11.667  1.00 13.82 ?  34  VAL   A CB   1 
ATOM   817  C CG1  . VAL   A 1 34  ? 27.081 -6.250  10.203  1.00 14.15 ?  34  VAL   A CG1  1 
ATOM   818  C CG2  . VAL   A 1 34  ? 28.196 -7.245  12.221  1.00 15.13 ?  34  VAL   A CG2  1 
ATOM   819  H H    A VAL   A 1 34  ? 25.494 -6.118  14.075  0.58 17.63 ?  34  VAL   A H    1 
ATOM   820  H H    B VAL   A 1 34  ? 25.565 -6.251  14.043  0.42 17.63 ?  34  VAL   A H    1 
ATOM   821  H HA   . VAL   A 1 34  ? 27.138 -4.738  12.423  1.00 15.79 ?  34  VAL   A HA   1 
ATOM   822  H HB   . VAL   A 1 34  ? 26.224 -7.321  11.717  1.00 16.55 ?  34  VAL   A HB   1 
ATOM   823  H HG11 . VAL   A 1 34  ? 27.582 -6.947  9.750   1.00 16.96 ?  34  VAL   A HG11 1 
ATOM   824  H HG12 . VAL   A 1 34  ? 26.206 -6.157  9.796   1.00 16.96 ?  34  VAL   A HG12 1 
ATOM   825  H HG13 . VAL   A 1 34  ? 27.564 -5.411  10.154  1.00 16.96 ?  34  VAL   A HG13 1 
ATOM   826  H HG21 . VAL   A 1 34  ? 28.481 -7.968  11.636  1.00 18.14 ?  34  VAL   A HG21 1 
ATOM   827  H HG22 . VAL   A 1 34  ? 28.881 -6.561  12.257  1.00 18.14 ?  34  VAL   A HG22 1 
ATOM   828  H HG23 . VAL   A 1 34  ? 28.026 -7.592  13.111  1.00 18.14 ?  34  VAL   A HG23 1 
ATOM   829  N N    . VAL   A 1 35  ? 25.230 -3.661  11.366  1.00 12.21 ?  35  VAL   A N    1 
ATOM   830  C CA   . VAL   A 1 35  ? 24.202 -3.150  10.466  1.00 11.89 ?  35  VAL   A CA   1 
ATOM   831  C C    . VAL   A 1 35  ? 24.763 -3.152  9.049   1.00 11.49 ?  35  VAL   A C    1 
ATOM   832  O O    . VAL   A 1 35  ? 25.912 -2.750  8.827   1.00 12.15 ?  35  VAL   A O    1 
ATOM   833  C CB   . VAL   A 1 35  ? 23.670 -1.756  10.872  1.00 12.46 ?  35  VAL   A CB   1 
ATOM   834  C CG1  . VAL   A 1 35  ? 24.745 -0.677  10.751  1.00 13.78 ?  35  VAL   A CG1  1 
ATOM   835  C CG2  . VAL   A 1 35  ? 22.439 -1.402  10.037  1.00 12.98 ?  35  VAL   A CG2  1 
ATOM   836  H H    . VAL   A 1 35  ? 25.872 -3.101  11.497  1.00 14.63 ?  35  VAL   A H    1 
ATOM   837  H HA   . VAL   A 1 35  ? 23.447 -3.759  10.485  1.00 14.25 ?  35  VAL   A HA   1 
ATOM   838  H HB   . VAL   A 1 35  ? 23.389 -1.789  11.796  1.00 14.93 ?  35  VAL   A HB   1 
ATOM   839  H HG11 . VAL   A 1 35  ? 24.399 0.153   11.120  1.00 16.52 ?  35  VAL   A HG11 1 
ATOM   840  H HG12 . VAL   A 1 35  ? 25.528 -0.957  11.245  1.00 16.52 ?  35  VAL   A HG12 1 
ATOM   841  H HG13 . VAL   A 1 35  ? 24.968 -0.551  9.815   1.00 16.52 ?  35  VAL   A HG13 1 
ATOM   842  H HG21 . VAL   A 1 35  ? 22.080 -0.558  10.343  1.00 15.55 ?  35  VAL   A HG21 1 
ATOM   843  H HG22 . VAL   A 1 35  ? 22.698 -1.334  9.102   1.00 15.55 ?  35  VAL   A HG22 1 
ATOM   844  H HG23 . VAL   A 1 35  ? 21.775 -2.104  10.142  1.00 15.55 ?  35  VAL   A HG23 1 
ATOM   845  N N    . VAL   A 1 36  ? 23.959 -3.617  8.094   1.00 10.85 ?  36  VAL   A N    1 
ATOM   846  C CA   . VAL   A 1 36  ? 24.338 -3.628  6.686   1.00 10.42 ?  36  VAL   A CA   1 
ATOM   847  C C    . VAL   A 1 36  ? 23.878 -2.341  6.016   1.00 10.65 ?  36  VAL   A C    1 
ATOM   848  O O    . VAL   A 1 36  ? 22.718 -1.929  6.150   1.00 11.50 ?  36  VAL   A O    1 
ATOM   849  C CB   . VAL   A 1 36  ? 23.743 -4.849  5.964   1.00 10.59 ?  36  VAL   A CB   1 
ATOM   850  C CG1  . VAL   A 1 36  ? 24.004 -4.760  4.477   1.00 11.10 ?  36  VAL   A CG1  1 
ATOM   851  C CG2  . VAL   A 1 36  ? 24.303 -6.136  6.531   1.00 11.79 ?  36  VAL   A CG2  1 
ATOM   852  H H    . VAL   A 1 36  ? 23.170 -3.944  8.242   1.00 13.00 ?  36  VAL   A H    1 
ATOM   853  H HA   . VAL   A 1 36  ? 25.308 -3.689  6.620   1.00 12.47 ?  36  VAL   A HA   1 
ATOM   854  H HB   . VAL   A 1 36  ? 22.780 -4.853  6.101   1.00 12.68 ?  36  VAL   A HB   1 
ATOM   855  H HG11 . VAL   A 1 36  ? 23.883 -5.635  4.083   1.00 13.30 ?  36  VAL   A HG11 1 
ATOM   856  H HG12 . VAL   A 1 36  ? 23.372 -4.132  4.079   1.00 13.30 ?  36  VAL   A HG12 1 
ATOM   857  H HG13 . VAL   A 1 36  ? 24.909 -4.450  4.333   1.00 13.30 ?  36  VAL   A HG13 1 
ATOM   858  H HG21 . VAL   A 1 36  ? 23.915 -6.889  6.053   1.00 14.13 ?  36  VAL   A HG21 1 
ATOM   859  H HG22 . VAL   A 1 36  ? 25.268 -6.138  6.413   1.00 14.13 ?  36  VAL   A HG22 1 
ATOM   860  H HG23 . VAL   A 1 36  ? 24.085 -6.195  7.472   1.00 14.13 ?  36  VAL   A HG23 1 
ATOM   861  N N    . ASN   A 1 37  ? 24.796 -1.710  5.284   1.00 10.22 ?  37  ASN   A N    1 
ATOM   862  C CA   . ASN   A 1 37  ? 24.466 -0.589  4.421   1.00 10.13 ?  37  ASN   A CA   1 
ATOM   863  C C    . ASN   A 1 37  ? 24.344 -1.059  2.982   1.00 10.07 ?  37  ASN   A C    1 
ATOM   864  O O    . ASN   A 1 37  ? 25.139 -1.884  2.508   1.00 10.68 ?  37  ASN   A O    1 
ATOM   865  C CB   . ASN   A 1 37  ? 25.548 0.488   4.507   1.00 10.66 ?  37  ASN   A CB   1 
ATOM   866  C CG   . ASN   A 1 37  ? 25.233 1.686   3.652   1.00 10.81 ?  37  ASN   A CG   1 
ATOM   867  O OD1  . ASN   A 1 37  ? 24.062 2.023   3.451   1.00 11.19 ?  37  ASN   A OD1  1 
ATOM   868  N ND2  . ASN   A 1 37  ? 26.277 2.347   3.152   1.00 11.07 ?  37  ASN   A ND2  1 
ATOM   869  H H    . ASN   A 1 37  ? 25.633 -1.917  5.276   1.00 12.24 ?  37  ASN   A H    1 
ATOM   870  H HA   . ASN   A 1 37  ? 23.625 -0.198  4.701   1.00 12.13 ?  37  ASN   A HA   1 
ATOM   871  H HB2  . ASN   A 1 37  ? 25.630 0.786   5.430   1.00 12.77 ?  37  ASN   A HB2  1 
ATOM   872  H HB3  . ASN   A 1 37  ? 26.395 0.113   4.209   1.00 12.77 ?  37  ASN   A HB3  1 
ATOM   873  H HD21 . ASN   A 1 37  ? 26.147 3.036   2.656   1.00 13.26 ?  37  ASN   A HD21 1 
ATOM   874  H HD22 . ASN   A 1 37  ? 27.072 2.082   3.315   1.00 13.26 ?  37  ASN   A HD22 1 
ATOM   875  N N    A ALA   A 1 38  ? 23.341 -0.505  2.294   0.58 10.41 ?  38  ALA   A N    1 
ATOM   876  N N    B ALA   A 1 38  ? 23.333 -0.551  2.284   0.42 11.00 ?  38  ALA   A N    1 
ATOM   877  C CA   A ALA   A 1 38  ? 23.162 -0.620  0.847   0.58 9.78  ?  38  ALA   A CA   1 
ATOM   878  C CA   B ALA   A 1 38  ? 23.163 -0.828  0.858   0.42 11.51 ?  38  ALA   A CA   1 
ATOM   879  C C    A ALA   A 1 38  ? 24.095 0.376   0.160   0.58 10.34 ?  38  ALA   A C    1 
ATOM   880  C C    B ALA   A 1 38  ? 23.965 0.213   0.084   0.42 11.41 ?  38  ALA   A C    1 
ATOM   881  O O    A ALA   A 1 38  ? 23.703 1.466   -0.265  0.58 9.63  ?  38  ALA   A O    1 
ATOM   882  O O    B ALA   A 1 38  ? 23.456 1.265   -0.306  0.42 11.65 ?  38  ALA   A O    1 
ATOM   883  C CB   A ALA   A 1 38  ? 21.704 -0.366  0.481   0.58 10.35 ?  38  ALA   A CB   1 
ATOM   884  C CB   B ALA   A 1 38  ? 21.688 -0.814  0.487   0.42 12.38 ?  38  ALA   A CB   1 
ATOM   885  H H    A ALA   A 1 38  ? 22.733 -0.029  2.668   0.58 12.47 ?  38  ALA   A H    1 
ATOM   886  H H    B ALA   A 1 38  ? 22.730 -0.037  2.619   0.42 13.17 ?  38  ALA   A H    1 
ATOM   887  H HA   A ALA   A 1 38  ? 23.405 -1.509  0.559   0.58 11.71 ?  38  ALA   A HA   1 
ATOM   888  H HA   B ALA   A 1 38  ? 23.524 -1.711  0.660   0.42 13.78 ?  38  ALA   A HA   1 
ATOM   889  H HB1  A ALA   A 1 38  ? 21.601 -0.445  -0.481  0.58 12.40 ?  38  ALA   A HB1  1 
ATOM   890  H HB1  B ALA   A 1 38  ? 21.607 -0.951  -0.468  0.42 14.84 ?  38  ALA   A HB1  1 
ATOM   891  H HB2  A ALA   A 1 38  ? 21.148 -1.023  0.928   0.58 12.40 ?  38  ALA   A HB2  1 
ATOM   892  H HB2  B ALA   A 1 38  ? 21.231 -1.525  0.965   0.42 14.84 ?  38  ALA   A HB2  1 
ATOM   893  H HB3  A ALA   A 1 38  ? 21.454 0.528   0.766   0.58 12.40 ?  38  ALA   A HB3  1 
ATOM   894  H HB3  B ALA   A 1 38  ? 21.313 0.045   0.731   0.42 14.84 ?  38  ALA   A HB3  1 
ATOM   895  N N    A ALA   A 1 39  ? 25.361 -0.013  0.059   0.58 10.24 ?  39  ALA   A N    1 
ATOM   896  N N    B ALA   A 1 39  ? 25.240 -0.085  -0.136  0.42 11.29 ?  39  ALA   A N    1 
ATOM   897  C CA   A ALA   A 1 39  ? 26.431 0.854   -0.407  0.58 9.56  ?  39  ALA   A CA   1 
ATOM   898  C CA   B ALA   A 1 39  ? 26.206 0.888   -0.621  0.42 10.94 ?  39  ALA   A CA   1 
ATOM   899  C C    A ALA   A 1 39  ? 26.569 0.801   -1.923  0.58 9.69  ?  39  ALA   A C    1 
ATOM   900  C C    B ALA   A 1 39  ? 26.357 0.815   -2.137  0.42 10.49 ?  39  ALA   A C    1 
ATOM   901  O O    A ALA   A 1 39  ? 26.076 -0.113  -2.590  0.58 10.44 ?  39  ALA   A O    1 
ATOM   902  O O    B ALA   A 1 39  ? 25.890 -0.115  -2.801  0.42 10.99 ?  39  ALA   A O    1 
ATOM   903  C CB   A ALA   A 1 39  ? 27.752 0.433   0.241   0.58 10.36 ?  39  ALA   A CB   1 
ATOM   904  C CB   B ALA   A 1 39  ? 27.561 0.662   0.058   0.42 12.02 ?  39  ALA   A CB   1 
ATOM   905  H H    A ALA   A 1 39  ? 25.632 -0.804  0.258   0.58 12.26 ?  39  ALA   A H    1 
ATOM   906  H H    B ALA   A 1 39  ? 25.573 -0.871  -0.008  0.42 13.52 ?  39  ALA   A H    1 
ATOM   907  H HA   A ALA   A 1 39  ? 26.241 1.768   -0.151  0.58 11.44 ?  39  ALA   A HA   1 
ATOM   908  H HA   B ALA   A 1 39  ? 25.895 1.776   -0.386  0.42 13.10 ?  39  ALA   A HA   1 
ATOM   909  H HB1  A ALA   A 1 39  ? 28.458 1.020   -0.077  0.58 12.41 ?  39  ALA   A HB1  1 
ATOM   910  H HB1  B ALA   A 1 39  ? 28.189 1.322   -0.274  0.42 14.39 ?  39  ALA   A HB1  1 
ATOM   911  H HB2  A ALA   A 1 39  ? 27.667 0.516   1.205   0.58 12.41 ?  39  ALA   A HB2  1 
ATOM   912  H HB2  B ALA   A 1 39  ? 27.455 0.764   1.020   0.42 14.39 ?  39  ALA   A HB2  1 
ATOM   913  H HB3  A ALA   A 1 39  ? 27.947 -0.482  0.001   0.58 12.41 ?  39  ALA   A HB3  1 
ATOM   914  H HB3  B ALA   A 1 39  ? 27.874 -0.230  -0.147  0.42 14.39 ?  39  ALA   A HB3  1 
ATOM   915  N N    A ASN   A 1 40  ? 27.279 1.793   -2.460  0.58 10.50 ?  40  ASN   A N    1 
ATOM   916  N N    B ASN   A 1 40  ? 27.011 1.833   -2.684  0.42 10.33 ?  40  ASN   A N    1 
ATOM   917  C CA   A ASN   A 1 40  ? 27.831 1.733   -3.806  0.58 10.42 ?  40  ASN   A CA   1 
ATOM   918  C CA   B ASN   A 1 40  ? 27.543 1.787   -4.036  0.42 10.54 ?  40  ASN   A CA   1 
ATOM   919  C C    A ASN   A 1 40  ? 29.354 1.627   -3.726  0.58 10.12 ?  40  ASN   A C    1 
ATOM   920  C C    B ASN   A 1 40  ? 29.060 1.636   -3.974  0.42 9.87  ?  40  ASN   A C    1 
ATOM   921  O O    A ASN   A 1 40  ? 29.945 1.736   -2.646  0.58 10.12 ?  40  ASN   A O    1 
ATOM   922  O O    B ASN   A 1 40  ? 29.669 1.705   -2.904  0.42 10.31 ?  40  ASN   A O    1 
ATOM   923  C CB   A ASN   A 1 40  ? 27.360 2.908   -4.684  0.58 11.45 ?  40  ASN   A CB   1 
ATOM   924  C CB   B ASN   A 1 40  ? 27.133 3.028   -4.843  0.42 11.35 ?  40  ASN   A CB   1 
ATOM   925  C CG   A ASN   A 1 40  ? 27.646 4.270   -4.073  0.58 12.86 ?  40  ASN   A CG   1 
ATOM   926  C CG   B ASN   A 1 40  ? 27.639 4.323   -4.238  0.42 11.60 ?  40  ASN   A CG   1 
ATOM   927  O OD1  A ASN   A 1 40  ? 28.767 4.552   -3.639  0.58 12.61 ?  40  ASN   A OD1  1 
ATOM   928  O OD1  B ASN   A 1 40  ? 28.846 4.529   -4.103  0.42 11.60 ?  40  ASN   A OD1  1 
ATOM   929  N ND2  A ASN   A 1 40  ? 26.624 5.131   -4.045  0.58 13.65 ?  40  ASN   A ND2  1 
ATOM   930  N ND2  B ASN   A 1 40  ? 26.716 5.214   -3.881  0.42 12.44 ?  40  ASN   A ND2  1 
ATOM   931  H H    A ASN   A 1 40  ? 27.463 2.529   -2.053  0.58 12.58 ?  40  ASN   A H    1 
ATOM   932  H H    B ASN   A 1 40  ? 27.157 2.577   -2.278  0.42 12.37 ?  40  ASN   A H    1 
ATOM   933  H HA   A ASN   A 1 40  ? 27.515 0.924   -4.233  0.58 12.49 ?  40  ASN   A HA   1 
ATOM   934  H HA   B ASN   A 1 40  ? 27.178 1.005   -4.485  0.42 12.63 ?  40  ASN   A HA   1 
ATOM   935  H HB2  A ASN   A 1 40  ? 27.815 2.862   -5.547  0.58 13.72 ?  40  ASN   A HB2  1 
ATOM   936  H HB2  B ASN   A 1 40  ? 27.498 2.950   -5.735  0.42 13.59 ?  40  ASN   A HB2  1 
ATOM   937  H HB3  A ASN   A 1 40  ? 26.403 2.839   -4.821  0.58 13.72 ?  40  ASN   A HB3  1 
ATOM   938  H HB3  B ASN   A 1 40  ? 26.166 3.068   -4.881  0.42 13.59 ?  40  ASN   A HB3  1 
ATOM   939  H HD21 A ASN   A 1 40  ? 26.735 5.923   -3.722  0.58 16.36 ?  40  ASN   A HD21 1 
ATOM   940  H HD21 B ASN   A 1 40  ? 26.958 5.965   -3.535  0.42 14.90 ?  40  ASN   A HD21 1 
ATOM   941  H HD22 A ASN   A 1 40  ? 25.857 4.897   -4.351  0.58 16.36 ?  40  ASN   A HD22 1 
ATOM   942  H HD22 B ASN   A 1 40  ? 25.885 5.040   -3.996  0.42 14.90 ?  40  ASN   A HD22 1 
ATOM   943  N N    A VAL   A 1 41  ? 29.982 1.367   -4.880  0.58 10.34 ?  41  VAL   A N    1 
ATOM   944  N N    B VAL   A 1 41  ? 29.669 1.400   -5.138  0.42 9.90  ?  41  VAL   A N    1 
ATOM   945  C CA   A VAL   A 1 41  ? 31.412 1.049   -4.902  0.58 11.03 ?  41  VAL   A CA   1 
ATOM   946  C CA   B VAL   A 1 41  ? 31.096 1.085   -5.186  0.42 10.72 ?  41  VAL   A CA   1 
ATOM   947  C C    A VAL   A 1 41  ? 32.261 2.202   -4.401  0.58 11.09 ?  41  VAL   A C    1 
ATOM   948  C C    B VAL   A 1 41  ? 31.981 2.217   -4.683  0.42 10.65 ?  41  VAL   A C    1 
ATOM   949  O O    A VAL   A 1 41  ? 33.366 1.984   -3.887  0.58 10.98 ?  41  VAL   A O    1 
ATOM   950  O O    B VAL   A 1 41  ? 33.148 1.973   -4.354  0.42 10.23 ?  41  VAL   A O    1 
ATOM   951  C CB   A VAL   A 1 41  ? 31.898 0.543   -6.285  0.58 11.01 ?  41  VAL   A CB   1 
ATOM   952  C CB   B VAL   A 1 41  ? 31.540 0.647   -6.599  0.42 11.96 ?  41  VAL   A CB   1 
ATOM   953  C CG1  A VAL   A 1 41  ? 31.183 -0.739  -6.684  0.58 11.95 ?  41  VAL   A CG1  1 
ATOM   954  C CG1  B VAL   A 1 41  ? 30.881 -0.670  -6.988  0.42 12.93 ?  41  VAL   A CG1  1 
ATOM   955  C CG2  A VAL   A 1 41  ? 31.775 1.610   -7.377  0.58 10.74 ?  41  VAL   A CG2  1 
ATOM   956  C CG2  B VAL   A 1 41  ? 31.246 1.736   -7.627  0.42 12.80 ?  41  VAL   A CG2  1 
ATOM   957  H H    A VAL   A 1 41  ? 29.612 1.358   -5.650  0.58 12.38 ?  41  VAL   A H    1 
ATOM   958  H H    B VAL   A 1 41  ? 29.274 1.399   -5.901  0.42 11.86 ?  41  VAL   A H    1 
ATOM   959  H HA   A VAL   A 1 41  ? 31.570 0.328   -4.281  0.58 13.21 ?  41  VAL   A HA   1 
ATOM   960  H HA   B VAL   A 1 41  ? 31.246 0.326   -4.599  0.42 12.84 ?  41  VAL   A HA   1 
ATOM   961  H HB   A VAL   A 1 41  ? 32.845 0.330   -6.215  0.58 13.19 ?  41  VAL   A HB   1 
ATOM   962  H HB   B VAL   A 1 41  ? 32.499 0.502   -6.586  0.42 14.33 ?  41  VAL   A HB   1 
ATOM   963  H HG11 A VAL   A 1 41  ? 31.522 -1.041  -7.542  0.58 14.32 ?  41  VAL   A HG11 1 
ATOM   964  H HG11 B VAL   A 1 41  ? 31.174 -0.915  -7.879  0.42 15.50 ?  41  VAL   A HG11 1 
ATOM   965  H HG12 A VAL   A 1 41  ? 31.343 -1.414  -6.008  0.58 14.32 ?  41  VAL   A HG12 1 
ATOM   966  H HG12 B VAL   A 1 41  ? 31.145 -1.355  -6.352  0.42 15.50 ?  41  VAL   A HG12 1 
ATOM   967  H HG13 A VAL   A 1 41  ? 30.230 -0.558  -6.753  0.58 14.32 ?  41  VAL   A HG13 1 
ATOM   968  H HG13 B VAL   A 1 41  ? 29.919 -0.559  -6.973  0.42 15.50 ?  41  VAL   A HG13 1 
ATOM   969  H HG21 A VAL   A 1 41  ? 32.022 1.217   -8.234  0.58 12.87 ?  41  VAL   A HG21 1 
ATOM   970  H HG21 B VAL   A 1 41  ? 31.566 1.440   -8.494  0.42 15.33 ?  41  VAL   A HG21 1 
ATOM   971  H HG22 A VAL   A 1 41  ? 30.859 1.921   -7.413  0.58 12.87 ?  41  VAL   A HG22 1 
ATOM   972  H HG22 B VAL   A 1 41  ? 30.290 1.890   -7.661  0.42 15.33 ?  41  VAL   A HG22 1 
ATOM   973  H HG23 A VAL   A 1 41  ? 32.371 2.347   -7.174  0.58 12.87 ?  41  VAL   A HG23 1 
ATOM   974  H HG23 B VAL   A 1 41  ? 31.705 2.549   -7.366  0.42 15.33 ?  41  VAL   A HG23 1 
ATOM   975  N N    A TYR   A 1 42  ? 31.780 3.436   -4.548  0.58 11.22 ?  42  TYR   A N    1 
ATOM   976  N N    B TYR   A 1 42  ? 31.472 3.453   -4.639  0.42 11.20 ?  42  TYR   A N    1 
ATOM   977  C CA   A TYR   A 1 42  ? 32.501 4.623   -4.104  0.58 11.43 ?  42  TYR   A CA   1 
ATOM   978  C CA   B TYR   A 1 42  ? 32.259 4.617   -4.237  0.42 11.26 ?  42  TYR   A CA   1 
ATOM   979  C C    A TYR   A 1 42  ? 32.188 4.977   -2.662  0.58 11.08 ?  42  TYR   A C    1 
ATOM   980  C C    B TYR   A 1 42  ? 32.052 5.019   -2.783  0.42 10.98 ?  42  TYR   A C    1 
ATOM   981  O O    A TYR   A 1 42  ? 32.769 5.930   -2.125  0.58 11.44 ?  42  TYR   A O    1 
ATOM   982  O O    B TYR   A 1 42  ? 32.601 6.040   -2.353  0.42 11.08 ?  42  TYR   A O    1 
ATOM   983  C CB   A TYR   A 1 42  ? 32.182 5.819   -5.020  0.58 12.28 ?  42  TYR   A CB   1 
ATOM   984  C CB   B TYR   A 1 42  ? 31.936 5.819   -5.135  0.42 12.33 ?  42  TYR   A CB   1 
ATOM   985  C CG   A TYR   A 1 42  ? 32.392 5.497   -6.485  0.58 12.61 ?  42  TYR   A CG   1 
ATOM   986  C CG   B TYR   A 1 42  ? 32.084 5.530   -6.608  0.42 12.88 ?  42  TYR   A CG   1 
ATOM   987  C CD1  A TYR   A 1 42  ? 33.665 5.294   -6.990  0.58 13.28 ?  42  TYR   A CD1  1 
ATOM   988  C CD1  B TYR   A 1 42  ? 33.332 5.314   -7.172  0.42 12.94 ?  42  TYR   A CD1  1 
ATOM   989  C CD2  A TYR   A 1 42  ? 31.315 5.360   -7.355  0.58 13.47 ?  42  TYR   A CD2  1 
ATOM   990  C CD2  B TYR   A 1 42  ? 30.970 5.467   -7.435  0.42 13.82 ?  42  TYR   A CD2  1 
ATOM   991  C CE1  A TYR   A 1 42  ? 33.865 4.974   -8.321  0.58 13.84 ?  42  TYR   A CE1  1 
ATOM   992  C CE1  B TYR   A 1 42  ? 33.467 5.038   -8.517  0.42 13.00 ?  42  TYR   A CE1  1 
ATOM   993  C CE2  A TYR   A 1 42  ? 31.508 5.046   -8.691  0.58 14.26 ?  42  TYR   A CE2  1 
ATOM   994  C CE2  B TYR   A 1 42  ? 31.096 5.201   -8.781  0.42 14.16 ?  42  TYR   A CE2  1 
ATOM   995  C CZ   A TYR   A 1 42  ? 32.788 4.855   -9.168  0.58 14.06 ?  42  TYR   A CZ   1 
ATOM   996  C CZ   B TYR   A 1 42  ? 32.347 4.987   -9.318  0.42 13.78 ?  42  TYR   A CZ   1 
ATOM   997  O OH   A TYR   A 1 42  ? 32.987 4.535   -10.492 0.58 15.33 ?  42  TYR   A OH   1 
ATOM   998  O OH   B TYR   A 1 42  ? 32.482 4.719   -10.660 0.42 14.48 ?  42  TYR   A OH   1 
ATOM   999  H H    A TYR   A 1 42  ? 31.019 3.616   -4.902  0.58 13.44 ?  42  TYR   A H    1 
ATOM   1000 H H    B TYR   A 1 42  ? 30.660 3.647   -4.860  0.42 13.42 ?  42  TYR   A H    1 
ATOM   1001 H HA   A TYR   A 1 42  ? 33.456 4.456   -4.170  0.58 13.70 ?  42  TYR   A HA   1 
ATOM   1002 H HA   B TYR   A 1 42  ? 33.196 4.411   -4.354  0.42 13.48 ?  42  TYR   A HA   1 
ATOM   1003 H HB2  A TYR   A 1 42  ? 31.253 6.075   -4.899  0.58 14.71 ?  42  TYR   A HB2  1 
ATOM   1004 H HB2  B TYR   A 1 42  ? 31.019 6.095   -4.978  0.42 14.77 ?  42  TYR   A HB2  1 
ATOM   1005 H HB3  A TYR   A 1 42  ? 32.762 6.564   -4.791  0.58 14.71 ?  42  TYR   A HB3  1 
ATOM   1006 H HB3  B TYR   A 1 42  ? 32.540 6.547   -4.914  0.42 14.77 ?  42  TYR   A HB3  1 
ATOM   1007 H HD1  A TYR   A 1 42  ? 34.401 5.375   -6.425  0.58 15.91 ?  42  TYR   A HD1  1 
ATOM   1008 H HD1  B TYR   A 1 42  ? 34.091 5.347   -6.633  0.42 15.50 ?  42  TYR   A HD1  1 
ATOM   1009 H HD2  A TYR   A 1 42  ? 30.450 5.491   -7.037  0.58 16.14 ?  42  TYR   A HD2  1 
ATOM   1010 H HD2  B TYR   A 1 42  ? 30.125 5.613   -7.075  0.42 16.56 ?  42  TYR   A HD2  1 
ATOM   1011 H HE1  A TYR   A 1 42  ? 34.729 4.851   -8.647  0.58 16.58 ?  42  TYR   A HE1  1 
ATOM   1012 H HE1  B TYR   A 1 42  ? 34.313 4.897   -8.883  0.42 15.57 ?  42  TYR   A HE1  1 
ATOM   1013 H HE2  A TYR   A 1 42  ? 30.777 4.966   -9.264  0.58 17.08 ?  42  TYR   A HE2  1 
ATOM   1014 H HE2  B TYR   A 1 42  ? 30.342 5.165   -9.325  0.42 16.97 ?  42  TYR   A HE2  1 
ATOM   1015 H HH   A TYR   A 1 42  ? 33.804 4.408   -10.638 0.58 18.38 ?  42  TYR   A HH   1 
ATOM   1016 H HH   B TYR   A 1 42  ? 31.732 4.719   -11.031 0.42 17.35 ?  42  TYR   A HH   1 
ATOM   1017 N N    . LEU   A 1 43  ? 31.275 4.245   -2.027  1.00 11.07 ?  43  LEU   A N    1 
ATOM   1018 C CA   . LEU   A 1 43  ? 30.833 4.588   -0.682  1.00 10.70 ?  43  LEU   A CA   1 
ATOM   1019 C C    . LEU   A 1 43  ? 30.350 6.034   -0.592  1.00 10.71 ?  43  LEU   A C    1 
ATOM   1020 O O    . LEU   A 1 43  ? 30.608 6.734   0.391   1.00 12.16 ?  43  LEU   A O    1 
ATOM   1021 C CB   . LEU   A 1 43  ? 31.875 4.275   0.390   1.00 11.25 ?  43  LEU   A CB   1 
ATOM   1022 C CG   . LEU   A 1 43  ? 32.362 2.820   0.477   1.00 11.68 ?  43  LEU   A CG   1 
ATOM   1023 C CD1  . LEU   A 1 43  ? 33.403 2.716   1.572   1.00 12.83 ?  43  LEU   A CD1  1 
ATOM   1024 C CD2  . LEU   A 1 43  ? 31.206 1.857   0.720   1.00 12.18 ?  43  LEU   A CD2  1 
ATOM   1025 H H    A LEU   A 1 43  ? 30.901 3.538   -2.351  0.58 13.26 ?  43  LEU   A H    1 
ATOM   1026 H H    B LEU   A 1 43  ? 30.985 3.473   -2.285  0.42 13.26 ?  43  LEU   A H    1 
ATOM   1027 H HA   . LEU   A 1 43  ? 30.066 4.033   -0.480  1.00 12.82 ?  43  LEU   A HA   1 
ATOM   1028 H HB2  . LEU   A 1 43  ? 32.654 4.830   0.235   1.00 13.47 ?  43  LEU   A HB2  1 
ATOM   1029 H HB3  . LEU   A 1 43  ? 31.493 4.493   1.256   1.00 13.47 ?  43  LEU   A HB3  1 
ATOM   1030 H HG   . LEU   A 1 43  ? 32.788 2.579   -0.363  1.00 13.99 ?  43  LEU   A HG   1 
ATOM   1031 H HD11 . LEU   A 1 43  ? 33.715 1.799   1.625   1.00 15.37 ?  43  LEU   A HD11 1 
ATOM   1032 H HD12 . LEU   A 1 43  ? 34.146 3.305   1.361   1.00 15.37 ?  43  LEU   A HD12 1 
ATOM   1033 H HD13 . LEU   A 1 43  ? 33.002 2.979   2.414   1.00 15.37 ?  43  LEU   A HD13 1 
ATOM   1034 H HD21 . LEU   A 1 43  ? 31.567 0.974   0.882   1.00 14.59 ?  43  LEU   A HD21 1 
ATOM   1035 H HD22 . LEU   A 1 43  ? 30.710 2.163   1.495   1.00 14.59 ?  43  LEU   A HD22 1 
ATOM   1036 H HD23 . LEU   A 1 43  ? 30.638 1.852   -0.061  1.00 14.59 ?  43  LEU   A HD23 1 
ATOM   1037 N N    A LYS   A 1 44  ? 29.636 6.483   -1.623  0.58 11.01 ?  44  LYS   A N    1 
ATOM   1038 N N    B LYS   A 1 44  ? 29.633 6.477   -1.626  0.42 11.39 ?  44  LYS   A N    1 
ATOM   1039 C CA   A LYS   A 1 44  ? 29.003 7.800   -1.611  0.58 11.60 ?  44  LYS   A CA   1 
ATOM   1040 C CA   B LYS   A 1 44  ? 28.985 7.788   -1.643  0.42 12.34 ?  44  LYS   A CA   1 
ATOM   1041 C C    A LYS   A 1 44  ? 27.570 7.615   -1.135  0.58 10.93 ?  44  LYS   A C    1 
ATOM   1042 C C    B LYS   A 1 44  ? 27.566 7.586   -1.130  0.42 11.38 ?  44  LYS   A C    1 
ATOM   1043 O O    A LYS   A 1 44  ? 26.713 7.119   -1.872  0.58 12.21 ?  44  LYS   A O    1 
ATOM   1044 O O    B LYS   A 1 44  ? 26.708 7.047   -1.835  0.42 12.17 ?  44  LYS   A O    1 
ATOM   1045 C CB   A LYS   A 1 44  ? 29.069 8.448   -2.987  0.58 13.79 ?  44  LYS   A CB   1 
ATOM   1046 C CB   B LYS   A 1 44  ? 28.984 8.363   -3.055  0.42 14.93 ?  44  LYS   A CB   1 
ATOM   1047 C CG   A LYS   A 1 44  ? 30.460 8.901   -3.388  0.58 16.70 ?  44  LYS   A CG   1 
ATOM   1048 C CG   B LYS   A 1 44  ? 30.354 8.732   -3.591  0.42 18.21 ?  44  LYS   A CG   1 
ATOM   1049 C CD   A LYS   A 1 44  ? 31.128 9.751   -2.317  0.58 21.21 ?  44  LYS   A CD   1 
ATOM   1050 C CD   B LYS   A 1 44  ? 31.000 9.846   -2.792  0.42 21.64 ?  44  LYS   A CD   1 
ATOM   1051 C CE   A LYS   A 1 44  ? 32.461 10.281  -2.802  0.58 23.77 ?  44  LYS   A CE   1 
ATOM   1052 C CE   B LYS   A 1 44  ? 32.348 10.213  -3.381  0.42 23.97 ?  44  LYS   A CE   1 
ATOM   1053 N NZ   A LYS   A 1 44  ? 33.286 10.817  -1.689  0.58 24.70 ?  44  LYS   A NZ   1 
ATOM   1054 N NZ   B LYS   A 1 44  ? 33.129 11.097  -2.476  0.42 25.04 ?  44  LYS   A NZ   1 
ATOM   1055 H H    A LYS   A 1 44  ? 29.504 6.037   -2.346  0.58 13.19 ?  44  LYS   A H    1 
ATOM   1056 H H    B LYS   A 1 44  ? 29.499 6.020   -2.343  0.42 13.65 ?  44  LYS   A H    1 
ATOM   1057 H HA   A LYS   A 1 44  ? 29.446 8.362   -0.961  0.58 13.89 ?  44  LYS   A HA   1 
ATOM   1058 H HA   B LYS   A 1 44  ? 29.448 8.394   -1.047  0.42 14.78 ?  44  LYS   A HA   1 
ATOM   1059 H HB2  A LYS   A 1 44  ? 28.760 7.811   -3.648  0.58 16.52 ?  44  LYS   A HB2  1 
ATOM   1060 H HB2  B LYS   A 1 44  ? 28.601 7.708   -3.657  0.42 17.89 ?  44  LYS   A HB2  1 
ATOM   1061 H HB3  A LYS   A 1 44  ? 28.491 9.229   -2.987  0.58 16.52 ?  44  LYS   A HB3  1 
ATOM   1062 H HB3  B LYS   A 1 44  ? 28.442 9.168   -3.059  0.42 17.89 ?  44  LYS   A HB3  1 
ATOM   1063 H HG2  A LYS   A 1 44  ? 31.015 8.122   -3.544  0.58 20.01 ?  44  LYS   A HG2  1 
ATOM   1064 H HG2  B LYS   A 1 44  ? 30.935 7.956   -3.549  0.42 21.83 ?  44  LYS   A HG2  1 
ATOM   1065 H HG3  A LYS   A 1 44  ? 30.399 9.434   -4.198  0.58 20.01 ?  44  LYS   A HG3  1 
ATOM   1066 H HG3  B LYS   A 1 44  ? 30.268 9.033   -4.510  0.42 21.83 ?  44  LYS   A HG3  1 
ATOM   1067 H HD2  A LYS   A 1 44  ? 30.552 10.501  -2.095  0.58 25.43 ?  44  LYS   A HD2  1 
ATOM   1068 H HD2  B LYS   A 1 44  ? 30.430 10.630  -2.813  0.42 25.95 ?  44  LYS   A HD2  1 
ATOM   1069 H HD3  A LYS   A 1 44  ? 31.295 9.208   -1.530  0.58 25.43 ?  44  LYS   A HD3  1 
ATOM   1070 H HD3  B LYS   A 1 44  ? 31.137 9.551   -1.877  0.42 25.95 ?  44  LYS   A HD3  1 
ATOM   1071 H HE2  A LYS   A 1 44  ? 32.955 9.558   -3.222  0.58 28.50 ?  44  LYS   A HE2  1 
ATOM   1072 H HE2  B LYS   A 1 44  ? 32.862 9.403   -3.528  0.42 28.74 ?  44  LYS   A HE2  1 
ATOM   1073 H HE3  A LYS   A 1 44  ? 32.306 10.994  -3.439  0.58 28.50 ?  44  LYS   A HE3  1 
ATOM   1074 H HE3  B LYS   A 1 44  ? 32.214 10.681  -4.219  0.42 28.74 ?  44  LYS   A HE3  1 
ATOM   1075 H HZ1  A LYS   A 1 44  ? 34.059 11.122  -2.004  0.58 29.62 ?  44  LYS   A HZ1  1 
ATOM   1076 H HZ1  B LYS   A 1 44  ? 33.913 11.294  -2.847  0.42 30.03 ?  44  LYS   A HZ1  1 
ATOM   1077 H HZ2  A LYS   A 1 44  ? 32.854 11.487  -1.289  0.58 29.62 ?  44  LYS   A HZ2  1 
ATOM   1078 H HZ2  B LYS   A 1 44  ? 32.681 11.850  -2.327  0.42 30.03 ?  44  LYS   A HZ2  1 
ATOM   1079 H HZ3  A LYS   A 1 44  ? 33.445 10.179  -1.092  0.58 29.62 ?  44  LYS   A HZ3  1 
ATOM   1080 H HZ3  B LYS   A 1 44  ? 33.271 10.686  -1.699  0.42 30.03 ?  44  LYS   A HZ3  1 
ATOM   1081 N N    . HIS   A 1 45  ? 27.317 7.998   0.112   1.00 10.93 ?  45  HIS   A N    1 
ATOM   1082 C CA   . HIS   A 1 45  ? 26.067 7.661   0.794   1.00 11.21 ?  45  HIS   A CA   1 
ATOM   1083 C C    . HIS   A 1 45  ? 25.048 8.787   0.627   1.00 11.99 ?  45  HIS   A C    1 
ATOM   1084 O O    . HIS   A 1 45  ? 24.779 9.572   1.536   1.00 14.31 ?  45  HIS   A O    1 
ATOM   1085 C CB   . HIS   A 1 45  ? 26.349 7.407   2.262   1.00 11.28 ?  45  HIS   A CB   1 
ATOM   1086 C CG   . HIS   A 1 45  ? 27.463 6.441   2.503   1.00 10.71 ?  45  HIS   A CG   1 
ATOM   1087 N ND1  . HIS   A 1 45  ? 27.463 5.152   2.009   1.00 10.99 ?  45  HIS   A ND1  1 
ATOM   1088 C CD2  . HIS   A 1 45  ? 28.621 6.592   3.191   1.00 10.97 ?  45  HIS   A CD2  1 
ATOM   1089 C CE1  . HIS   A 1 45  ? 28.573 4.552   2.399   1.00 10.69 ?  45  HIS   A CE1  1 
ATOM   1090 N NE2  . HIS   A 1 45  ? 29.296 5.403   3.109   1.00 10.96 ?  45  HIS   A NE2  1 
ATOM   1091 H H    A HIS   A 1 45  ? 27.856 8.466   0.595   0.58 13.10 ?  45  HIS   A H    1 
ATOM   1092 H H    B HIS   A 1 45  ? 27.854 8.476   0.587   0.42 13.10 ?  45  HIS   A H    1 
ATOM   1093 H HA   . HIS   A 1 45  ? 25.694 6.850   0.411   1.00 13.43 ?  45  HIS   A HA   1 
ATOM   1094 H HB2  . HIS   A 1 45  ? 26.575 8.246   2.690   1.00 13.52 ?  45  HIS   A HB2  1 
ATOM   1095 H HB3  . HIS   A 1 45  ? 25.538 7.043   2.676   1.00 13.52 ?  45  HIS   A HB3  1 
ATOM   1096 H HD2  . HIS   A 1 45  ? 28.902 7.364   3.633   1.00 13.14 ?  45  HIS   A HD2  1 
ATOM   1097 H HE1  . HIS   A 1 45  ? 28.811 3.674   2.208   1.00 12.80 ?  45  HIS   A HE1  1 
ATOM   1098 H HE2  . HIS   A 1 45  ? 30.060 5.240   3.466   1.00 13.13 ?  45  HIS   A HE2  1 
ATOM   1099 N N    A GLY   A 1 46  ? 24.499 8.871   -0.578  0.58 12.70 ?  46  GLY   A N    1 
ATOM   1100 N N    B GLY   A 1 46  ? 24.399 8.798   -0.533  0.42 12.02 ?  46  GLY   A N    1 
ATOM   1101 C CA   A GLY   A 1 46  ? 23.721 10.041  -0.942  0.58 13.59 ?  46  GLY   A CA   1 
ATOM   1102 C CA   B GLY   A 1 46  ? 23.495 9.883   -0.871  0.42 12.19 ?  46  GLY   A CA   1 
ATOM   1103 C C    A GLY   A 1 46  ? 22.225 9.912   -0.738  0.58 13.36 ?  46  GLY   A C    1 
ATOM   1104 C C    B GLY   A 1 46  ? 22.048 9.722   -0.436  0.42 11.67 ?  46  GLY   A C    1 
ATOM   1105 O O    A GLY   A 1 46  ? 21.541 10.905  -0.463  0.58 13.43 ?  46  GLY   A O    1 
ATOM   1106 O O    B GLY   A 1 46  ? 21.458 10.662  0.106   0.42 12.25 ?  46  GLY   A O    1 
ATOM   1107 H H    A GLY   A 1 46  ? 24.553 8.270   -1.190  0.58 15.21 ?  46  GLY   A H    1 
ATOM   1108 H H    B GLY   A 1 46  ? 24.460 8.189   -1.136  0.42 14.40 ?  46  GLY   A H    1 
ATOM   1109 H HA2  A GLY   A 1 46  ? 24.035 10.800  -0.424  0.58 16.29 ?  46  GLY   A HA2  1 
ATOM   1110 H HA2  B GLY   A 1 46  ? 23.824 10.700  -0.463  0.42 14.60 ?  46  GLY   A HA2  1 
ATOM   1111 H HA3  A GLY   A 1 46  ? 23.869 10.235  -1.878  0.58 16.29 ?  46  GLY   A HA3  1 
ATOM   1112 H HA3  B GLY   A 1 46  ? 23.510 10.010  -1.833  0.42 14.60 ?  46  GLY   A HA3  1 
ATOM   1113 N N    A GLY   A 1 47  ? 21.703 8.703   -0.890  0.58 13.30 ?  47  GLY   A N    1 
ATOM   1114 N N    B GLY   A 1 47  ? 21.453 8.553   -0.670  0.42 12.33 ?  47  GLY   A N    1 
ATOM   1115 C CA   A GLY   A 1 47  ? 20.270 8.488   -0.864  0.58 12.88 ?  47  GLY   A CA   1 
ATOM   1116 C CA   B GLY   A 1 47  ? 20.032 8.379   -0.448  0.42 12.24 ?  47  GLY   A CA   1 
ATOM   1117 C C    A GLY   A 1 47  ? 19.957 7.057   -0.483  0.58 11.97 ?  47  GLY   A C    1 
ATOM   1118 C C    B GLY   A 1 47  ? 19.700 6.957   -0.050  0.42 11.13 ?  47  GLY   A C    1 
ATOM   1119 O O    A GLY   A 1 47  ? 20.850 6.242   -0.242  0.58 12.25 ?  47  GLY   A O    1 
ATOM   1120 O O    B GLY   A 1 47  ? 20.584 6.113   0.114   0.42 10.59 ?  47  GLY   A O    1 
ATOM   1121 H H    A GLY   A 1 47  ? 22.161 7.989   -1.003  0.58 15.94 ?  47  GLY   A H    1 
ATOM   1122 H H    B GLY   A 1 47  ? 21.860 7.846   -0.952  0.42 14.77 ?  47  GLY   A H    1 
ATOM   1123 H HA2  A GLY   A 1 47  ? 19.853 9.087   -0.224  0.58 15.43 ?  47  GLY   A HA2  1 
ATOM   1124 H HA2  B GLY   A 1 47  ? 19.738 8.972   0.259   0.42 14.66 ?  47  GLY   A HA2  1 
ATOM   1125 H HA3  A GLY   A 1 47  ? 19.902 8.669   -1.746  0.58 15.43 ?  47  GLY   A HA3  1 
ATOM   1126 H HA3  B GLY   A 1 47  ? 19.545 8.599   -1.259  0.42 14.66 ?  47  GLY   A HA3  1 
ATOM   1127 N N    A GLY   A 1 48  ? 18.665 6.751   -0.448  0.58 11.62 ?  48  GLY   A N    1 
ATOM   1128 N N    B GLY   A 1 48  ? 18.401 6.697   0.101   0.42 10.99 ?  48  GLY   A N    1 
ATOM   1129 C CA   A GLY   A 1 48  ? 18.254 5.425   -0.045  0.58 11.39 ?  48  GLY   A CA   1 
ATOM   1130 C CA   B GLY   A 1 48  ? 17.958 5.383   0.538   0.42 10.53 ?  48  GLY   A CA   1 
ATOM   1131 C C    A GLY   A 1 48  ? 18.677 5.125   1.379   0.58 11.14 ?  48  GLY   A C    1 
ATOM   1132 C C    B GLY   A 1 48  ? 18.565 5.022   1.879   0.42 10.48 ?  48  GLY   A C    1 
ATOM   1133 O O    A GLY   A 1 48  ? 18.835 6.024   2.218   0.58 11.45 ?  48  GLY   A O    1 
ATOM   1134 O O    B GLY   A 1 48  ? 18.744 5.871   2.764   0.42 10.44 ?  48  GLY   A O    1 
ATOM   1135 H H    A GLY   A 1 48  ? 18.028 7.283   -0.653  0.58 13.92 ?  48  GLY   A H    1 
ATOM   1136 H H    B GLY   A 1 48  ? 17.758 7.258   -0.039  0.42 13.16 ?  48  GLY   A H    1 
ATOM   1137 H HA2  A GLY   A 1 48  ? 17.294 5.348   -0.103  0.58 13.65 ?  48  GLY   A HA2  1 
ATOM   1138 H HA2  B GLY   A 1 48  ? 16.985 5.366   0.612   0.42 12.62 ?  48  GLY   A HA2  1 
ATOM   1139 H HA3  A GLY   A 1 48  ? 18.661 4.762   -0.624  0.58 13.65 ?  48  GLY   A HA3  1 
ATOM   1140 H HA3  B GLY   A 1 48  ? 18.222 4.711   -0.115  0.42 12.62 ?  48  GLY   A HA3  1 
ATOM   1141 N N    A VAL   A 1 49  ? 18.875 3.833   1.653   0.58 11.49 ?  49  VAL   A N    1 
ATOM   1142 N N    B VAL   A 1 49  ? 18.885 3.735   2.029   0.42 10.57 ?  49  VAL   A N    1 
ATOM   1143 C CA   A VAL   A 1 49  ? 19.336 3.415   2.975   0.58 11.81 ?  49  VAL   A CA   1 
ATOM   1144 C CA   B VAL   A 1 49  ? 19.506 3.238   3.255   0.42 10.53 ?  49  VAL   A CA   1 
ATOM   1145 C C    A VAL   A 1 49  ? 20.654 4.094   3.328   0.58 10.62 ?  49  VAL   A C    1 
ATOM   1146 C C    B VAL   A 1 49  ? 20.787 4.004   3.565   0.42 9.92  ?  49  VAL   A C    1 
ATOM   1147 O O    A VAL   A 1 49  ? 20.844 4.544   4.461   0.58 10.86 ?  49  VAL   A O    1 
ATOM   1148 O O    B VAL   A 1 49  ? 21.031 4.393   4.713   0.42 10.23 ?  49  VAL   A O    1 
ATOM   1149 C CB   A VAL   A 1 49  ? 19.448 1.879   3.051   0.58 12.39 ?  49  VAL   A CB   1 
ATOM   1150 C CB   B VAL   A 1 49  ? 19.778 1.728   3.131   0.42 10.54 ?  49  VAL   A CB   1 
ATOM   1151 C CG1  A VAL   A 1 49  ? 20.233 1.456   4.291   0.58 12.90 ?  49  VAL   A CG1  1 
ATOM   1152 C CG1  B VAL   A 1 49  ? 20.623 1.244   4.302   0.42 10.19 ?  49  VAL   A CG1  1 
ATOM   1153 C CG2  A VAL   A 1 49  ? 18.066 1.238   3.056   0.58 13.82 ?  49  VAL   A CG2  1 
ATOM   1154 C CG2  B VAL   A 1 49  ? 18.475 0.942   3.025   0.42 11.24 ?  49  VAL   A CG2  1 
ATOM   1155 H H    A VAL   A 1 49  ? 18.758 3.186   1.099   0.58 13.76 ?  49  VAL   A H    1 
ATOM   1156 H H    B VAL   A 1 49  ? 18.749 3.128   1.433   0.42 12.66 ?  49  VAL   A H    1 
ATOM   1157 H HA   A VAL   A 1 49  ? 18.681 3.685   3.635   0.58 14.15 ?  49  VAL   A HA   1 
ATOM   1158 H HA   B VAL   A 1 49  ? 18.895 3.370   3.994   0.42 12.62 ?  49  VAL   A HA   1 
ATOM   1159 H HB   A VAL   A 1 49  ? 19.931 1.553   2.274   0.58 14.84 ?  49  VAL   A HB   1 
ATOM   1160 H HB   B VAL   A 1 49  ? 20.286 1.568   2.320   0.42 12.62 ?  49  VAL   A HB   1 
ATOM   1161 H HG11 A VAL   A 1 49  ? 20.051 0.521   4.476   0.58 15.46 ?  49  VAL   A HG11 1 
ATOM   1162 H HG11 B VAL   A 1 49  ? 20.543 0.281   4.368   0.42 12.21 ?  49  VAL   A HG11 1 
ATOM   1163 H HG12 A VAL   A 1 49  ? 21.181 1.581   4.131   0.58 15.46 ?  49  VAL   A HG12 1 
ATOM   1164 H HG12 B VAL   A 1 49  ? 21.550 1.488   4.148   0.42 12.21 ?  49  VAL   A HG12 1 
ATOM   1165 H HG13 A VAL   A 1 49  ? 19.948 1.999   5.045   0.58 15.46 ?  49  VAL   A HG13 1 
ATOM   1166 H HG13 B VAL   A 1 49  ? 20.299 1.660   5.116   0.42 12.21 ?  49  VAL   A HG13 1 
ATOM   1167 H HG21 A VAL   A 1 49  ? 18.165 0.274   3.092   0.58 16.56 ?  49  VAL   A HG21 1 
ATOM   1168 H HG21 B VAL   A 1 49  ? 18.682 0.004   2.888   0.42 13.47 ?  49  VAL   A HG21 1 
ATOM   1169 H HG22 A VAL   A 1 49  ? 17.579 1.553   3.832   0.58 16.56 ?  49  VAL   A HG22 1 
ATOM   1170 H HG22 B VAL   A 1 49  ? 17.973 1.053   3.847   0.42 13.47 ?  49  VAL   A HG22 1 
ATOM   1171 H HG23 A VAL   A 1 49  ? 17.603 1.495   2.245   0.58 16.56 ?  49  VAL   A HG23 1 
ATOM   1172 H HG23 B VAL   A 1 49  ? 17.962 1.280   2.274   0.42 13.47 ?  49  VAL   A HG23 1 
ATOM   1173 N N    A ALA   A 1 50  ? 21.595 4.140   2.380   0.58 10.41 ?  50  ALA   A N    1 
ATOM   1174 N N    B ALA   A 1 50  ? 21.646 4.180   2.557   0.42 9.99  ?  50  ALA   A N    1 
ATOM   1175 C CA   A ALA   A 1 50  ? 22.917 4.691   2.667   0.58 10.43 ?  50  ALA   A CA   1 
ATOM   1176 C CA   B ALA   A 1 50  ? 22.959 4.770   2.796   0.42 9.86  ?  50  ALA   A CA   1 
ATOM   1177 C C    A ALA   A 1 50  ? 22.836 6.155   3.067   0.58 10.24 ?  50  ALA   A C    1 
ATOM   1178 C C    B ALA   A 1 50  ? 22.837 6.222   3.228   0.42 9.53  ?  50  ALA   A C    1 
ATOM   1179 O O    A ALA   A 1 50  ? 23.498 6.581   4.017   0.58 10.77 ?  50  ALA   A O    1 
ATOM   1180 O O    B ALA   A 1 50  ? 23.421 6.631   4.237   0.42 9.87  ?  50  ALA   A O    1 
ATOM   1181 C CB   A ALA   A 1 50  ? 23.812 4.539   1.444   0.58 11.07 ?  50  ALA   A CB   1 
ATOM   1182 C CB   B ALA   A 1 50  ? 23.815 4.659   1.537   0.42 10.01 ?  50  ALA   A CB   1 
ATOM   1183 H H    A ALA   A 1 50  ? 21.494 3.862   1.579   0.58 12.47 ?  50  ALA   A H    1 
ATOM   1184 H H    B ALA   A 1 50  ? 21.491 3.974   1.735   0.42 11.97 ?  50  ALA   A H    1 
ATOM   1185 H HA   A ALA   A 1 50  ? 23.316 4.204   3.407   0.58 12.50 ?  50  ALA   A HA   1 
ATOM   1186 H HA   B ALA   A 1 50  ? 23.402 4.288   3.508   0.42 11.81 ?  50  ALA   A HA   1 
ATOM   1187 H HB1  A ALA   A 1 50  ? 24.685 4.914   1.649   0.58 13.26 ?  50  ALA   A HB1  1 
ATOM   1188 H HB1  B ALA   A 1 50  ? 24.687 5.054   1.712   0.42 11.99 ?  50  ALA   A HB1  1 
ATOM   1189 H HB2  A ALA   A 1 50  ? 23.894 3.601   1.231   0.58 13.26 ?  50  ALA   A HB2  1 
ATOM   1190 H HB2  B ALA   A 1 50  ? 23.919 3.723   1.307   0.42 11.99 ?  50  ALA   A HB2  1 
ATOM   1191 H HB3  A ALA   A 1 50  ? 23.412 5.021   0.705   0.58 13.26 ?  50  ALA   A HB3  1 
ATOM   1192 H HB3  B ALA   A 1 50  ? 23.379 5.133   0.813   0.42 11.99 ?  50  ALA   A HB3  1 
ATOM   1193 N N    A GLY   A 1 51  ? 22.030 6.943   2.358   0.58 10.87 ?  51  GLY   A N    1 
ATOM   1194 N N    B GLY   A 1 51  ? 22.069 7.015   2.479   0.42 10.26 ?  51  GLY   A N    1 
ATOM   1195 C CA   A GLY   A 1 51  ? 21.864 8.333   2.747   0.58 11.76 ?  51  GLY   A CA   1 
ATOM   1196 C CA   B GLY   A 1 51  ? 21.904 8.411   2.841   0.42 10.51 ?  51  GLY   A CA   1 
ATOM   1197 C C    A GLY   A 1 51  ? 21.267 8.469   4.133   0.58 11.65 ?  51  GLY   A C    1 
ATOM   1198 C C    B GLY   A 1 51  ? 21.280 8.576   4.211   0.42 10.42 ?  51  GLY   A C    1 
ATOM   1199 O O    A GLY   A 1 51  ? 21.665 9.345   4.906   0.58 12.19 ?  51  GLY   A O    1 
ATOM   1200 O O    B GLY   A 1 51  ? 21.653 9.476   4.969   0.42 10.76 ?  51  GLY   A O    1 
ATOM   1201 H H    A GLY   A 1 51  ? 21.592 6.703   1.663   0.58 13.02 ?  51  GLY   A H    1 
ATOM   1202 H H    B GLY   A 1 51  ? 21.641 6.769   1.773   0.42 12.29 ?  51  GLY   A H    1 
ATOM   1203 H HA2  A GLY   A 1 51  ? 22.723 8.781   2.738   0.58 14.08 ?  51  GLY   A HA2  1 
ATOM   1204 H HA2  B GLY   A 1 51  ? 22.767 8.851   2.839   0.42 12.59 ?  51  GLY   A HA2  1 
ATOM   1205 H HA3  A GLY   A 1 51  ? 21.275 8.778   2.118   0.58 14.08 ?  51  GLY   A HA3  1 
ATOM   1206 H HA3  B GLY   A 1 51  ? 21.333 8.849   2.188   0.42 12.59 ?  51  GLY   A HA3  1 
ATOM   1207 N N    A ALA   A 1 52  ? 20.306 7.598   4.467   0.58 12.08 ?  52  ALA   A N    1 
ATOM   1208 N N    B ALA   A 1 52  ? 20.316 7.710   4.547   0.42 10.37 ?  52  ALA   A N    1 
ATOM   1209 C CA   A ALA   A 1 52  ? 19.658 7.651   5.773   0.58 12.71 ?  52  ALA   A CA   1 
ATOM   1210 C CA   B ALA   A 1 52  ? 19.660 7.805   5.847   0.42 10.87 ?  52  ALA   A CA   1 
ATOM   1211 C C    A ALA   A 1 52  ? 20.625 7.283   6.896   0.58 12.27 ?  52  ALA   A C    1 
ATOM   1212 C C    B ALA   A 1 52  ? 20.566 7.316   6.976   0.42 10.67 ?  52  ALA   A C    1 
ATOM   1213 O O    A ALA   A 1 52  ? 20.710 7.988   7.908   0.58 12.88 ?  52  ALA   A O    1 
ATOM   1214 O O    B ALA   A 1 52  ? 20.612 7.934   8.047   0.42 11.27 ?  52  ALA   A O    1 
ATOM   1215 C CB   A ALA   A 1 52  ? 18.433 6.731   5.782   0.58 13.93 ?  52  ALA   A CB   1 
ATOM   1216 C CB   B ALA   A 1 52  ? 18.332 7.047   5.825   0.42 11.67 ?  52  ALA   A CB   1 
ATOM   1217 H H    A ALA   A 1 52  ? 20.030 6.963   3.962   0.58 14.48 ?  52  ALA   A H    1 
ATOM   1218 H H    B ALA   A 1 52  ? 20.034 7.070   4.042   0.42 12.42 ?  52  ALA   A H    1 
ATOM   1219 H HA   A ALA   A 1 52  ? 19.352 8.553   5.936   0.58 15.23 ?  52  ALA   A HA   1 
ATOM   1220 H HA   B ALA   A 1 52  ? 19.462 8.734   6.014   0.42 13.02 ?  52  ALA   A HA   1 
ATOM   1221 H HB1  A ALA   A 1 52  ? 18.007 6.779   6.654   0.58 16.69 ?  52  ALA   A HB1  1 
ATOM   1222 H HB1  B ALA   A 1 52  ? 17.912 7.129   6.695   0.42 13.98 ?  52  ALA   A HB1  1 
ATOM   1223 H HB2  A ALA   A 1 52  ? 17.814 7.027   5.096   0.58 16.69 ?  52  ALA   A HB2  1 
ATOM   1224 H HB2  B ALA   A 1 52  ? 17.760 7.434   5.144   0.42 13.98 ?  52  ALA   A HB2  1 
ATOM   1225 H HB3  A ALA   A 1 52  ? 18.717 5.821   5.602   0.58 16.69 ?  52  ALA   A HB3  1 
ATOM   1226 H HB3  B ALA   A 1 52  ? 18.501 6.113   5.625   0.42 13.98 ?  52  ALA   A HB3  1 
ATOM   1227 N N    A LEU   A 1 53  ? 21.364 6.177   6.743   0.58 11.62 ?  53  LEU   A N    1 
ATOM   1228 N N    B LEU   A 1 53  ? 21.291 6.210   6.770   0.42 10.65 ?  53  LEU   A N    1 
ATOM   1229 C CA   A LEU   A 1 53  ? 22.312 5.785   7.786   0.58 11.46 ?  53  LEU   A CA   1 
ATOM   1230 C CA   B LEU   A 1 53  ? 22.284 5.797   7.762   0.42 10.92 ?  53  LEU   A CA   1 
ATOM   1231 C C    A LEU   A 1 53  ? 23.380 6.849   7.977   0.58 10.58 ?  53  LEU   A C    1 
ATOM   1232 C C    B LEU   A 1 53  ? 23.315 6.896   7.973   0.42 10.44 ?  53  LEU   A C    1 
ATOM   1233 O O    A LEU   A 1 53  ? 23.750 7.180   9.110   0.58 11.63 ?  53  LEU   A O    1 
ATOM   1234 O O    B LEU   A 1 53  ? 23.590 7.306   9.107   0.42 10.94 ?  53  LEU   A O    1 
ATOM   1235 C CB   A LEU   A 1 53  ? 22.966 4.442   7.449   0.58 11.48 ?  53  LEU   A CB   1 
ATOM   1236 C CB   B LEU   A 1 53  ? 22.986 4.499   7.335   0.42 11.29 ?  53  LEU   A CB   1 
ATOM   1237 C CG   A LEU   A 1 53  ? 22.022 3.235   7.402   0.58 11.98 ?  53  LEU   A CG   1 
ATOM   1238 C CG   B LEU   A 1 53  ? 22.300 3.134   7.517   0.42 11.20 ?  53  LEU   A CG   1 
ATOM   1239 C CD1  A LEU   A 1 53  ? 22.746 2.038   6.830   0.58 11.83 ?  53  LEU   A CD1  1 
ATOM   1240 C CD1  B LEU   A 1 53  ? 23.154 2.037   6.894   0.42 11.59 ?  53  LEU   A CD1  1 
ATOM   1241 C CD2  A LEU   A 1 53  ? 21.482 2.917   8.786   0.58 12.69 ?  53  LEU   A CD2  1 
ATOM   1242 C CD2  B LEU   A 1 53  ? 22.024 2.813   8.982   0.42 11.33 ?  53  LEU   A CD2  1 
ATOM   1243 H H    A LEU   A 1 53  ? 21.335 5.649   6.063   0.58 13.92 ?  53  LEU   A H    1 
ATOM   1244 H H    B LEU   A 1 53  ? 21.223 5.691   6.086   0.42 12.76 ?  53  LEU   A H    1 
ATOM   1245 H HA   A LEU   A 1 53  ? 21.838 5.680   8.624   0.58 13.73 ?  53  LEU   A HA   1 
ATOM   1246 H HA   B LEU   A 1 53  ? 21.839 5.631   8.606   0.42 13.09 ?  53  LEU   A HA   1 
ATOM   1247 H HB2  A LEU   A 1 53  ? 23.387 4.514   6.575   0.58 13.75 ?  53  LEU   A HB2  1 
ATOM   1248 H HB2  B LEU   A 1 53  ? 23.183 4.574   6.388   0.42 13.53 ?  53  LEU   A HB2  1 
ATOM   1249 H HB3  A LEU   A 1 53  ? 23.645 4.252   8.116   0.58 13.75 ?  53  LEU   A HB3  1 
ATOM   1250 H HB3  B LEU   A 1 53  ? 23.821 4.447   7.822   0.42 13.53 ?  53  LEU   A HB3  1 
ATOM   1251 H HG   A LEU   A 1 53  ? 21.270 3.444   6.822   0.58 14.35 ?  53  LEU   A HG   1 
ATOM   1252 H HG   B LEU   A 1 53  ? 21.452 3.143   7.050   0.42 13.42 ?  53  LEU   A HG   1 
ATOM   1253 H HD11 A LEU   A 1 53  ? 22.136 1.286   6.811   0.58 14.17 ?  53  LEU   A HD11 1 
ATOM   1254 H HD11 B LEU   A 1 53  ? 22.711 1.182   7.019   0.42 13.88 ?  53  LEU   A HD11 1 
ATOM   1255 H HD12 A LEU   A 1 53  ? 23.042 2.251   5.933   0.58 14.17 ?  53  LEU   A HD12 1 
ATOM   1256 H HD12 B LEU   A 1 53  ? 23.260 2.219   5.947   0.42 13.88 ?  53  LEU   A HD12 1 
ATOM   1257 H HD13 A LEU   A 1 53  ? 23.507 1.837   7.395   0.58 14.17 ?  53  LEU   A HD13 1 
ATOM   1258 H HD13 B LEU   A 1 53  ? 24.021 2.026   7.329   0.42 13.88 ?  53  LEU   A HD13 1 
ATOM   1259 H HD21 A LEU   A 1 53  ? 20.941 2.115   8.736   0.58 15.21 ?  53  LEU   A HD21 1 
ATOM   1260 H HD21 B LEU   A 1 53  ? 21.625 1.930   9.044   0.42 13.57 ?  53  LEU   A HD21 1 
ATOM   1261 H HD22 A LEU   A 1 53  ? 22.228 2.778   9.389   0.58 15.21 ?  53  LEU   A HD22 1 
ATOM   1262 H HD22 B LEU   A 1 53  ? 22.859 2.835   9.475   0.42 13.57 ?  53  LEU   A HD22 1 
ATOM   1263 H HD23 A LEU   A 1 53  ? 20.942 3.662   9.095   0.58 15.21 ?  53  LEU   A HD23 1 
ATOM   1264 H HD23 B LEU   A 1 53  ? 21.412 3.477   9.339   0.42 13.57 ?  53  LEU   A HD23 1 
ATOM   1265 N N    . ASN   A 1 54  ? 23.883 7.404   6.881   1.00 10.18 ?  54  ASN   A N    1 
ATOM   1266 C CA   . ASN   A 1 54  ? 24.932 8.398   7.016   1.00 10.36 ?  54  ASN   A CA   1 
ATOM   1267 C C    . ASN   A 1 54  ? 24.419 9.647   7.734   1.00 10.69 ?  54  ASN   A C    1 
ATOM   1268 O O    . ASN   A 1 54  ? 25.105 10.199  8.605   1.00 11.54 ?  54  ASN   A O    1 
ATOM   1269 C CB   . ASN   A 1 54  ? 25.505 8.759   5.660   1.00 10.55 ?  54  ASN   A CB   1 
ATOM   1270 C CG   . ASN   A 1 54  ? 26.523 9.861   5.773   1.00 10.83 ?  54  ASN   A CG   1 
ATOM   1271 O OD1  . ASN   A 1 54  ? 27.529 9.718   6.483   1.00 10.88 ?  54  ASN   A OD1  1 
ATOM   1272 N ND2  . ASN   A 1 54  ? 26.276 10.977  5.101   1.00 11.89 ?  54  ASN   A ND2  1 
ATOM   1273 H H    A ASN   A 1 54  ? 23.640 7.226   6.075   0.58 12.19 ?  54  ASN   A H    1 
ATOM   1274 H H    B ASN   A 1 54  ? 23.678 7.192   6.073   0.42 12.19 ?  54  ASN   A H    1 
ATOM   1275 H HA   . ASN   A 1 54  ? 25.645 8.027   7.552   1.00 12.41 ?  54  ASN   A HA   1 
ATOM   1276 H HB2  . ASN   A 1 54  ? 25.939 7.972   5.281   1.00 12.63 ?  54  ASN   A HB2  1 
ATOM   1277 H HB3  . ASN   A 1 54  ? 24.790 9.055   5.075   1.00 12.63 ?  54  ASN   A HB3  1 
ATOM   1278 H HD21 . ASN   A 1 54  ? 26.830 11.630  5.142   1.00 14.24 ?  54  ASN   A HD21 1 
ATOM   1279 H HD22 . ASN   A 1 54  ? 25.563 11.043  4.624   1.00 14.24 ?  54  ASN   A HD22 1 
ATOM   1280 N N    . LYS   A 1 55  ? 23.209 10.108  7.383   1.00 11.31 ?  55  LYS   A N    1 
ATOM   1281 C CA   . LYS   A 1 55  ? 22.627 11.266  8.051   1.00 12.12 ?  55  LYS   A CA   1 
ATOM   1282 C C    . LYS   A 1 55  ? 22.532 11.034  9.554   1.00 12.15 ?  55  LYS   A C    1 
ATOM   1283 O O    . LYS   A 1 55  ? 22.807 11.938  10.354  1.00 12.83 ?  55  LYS   A O    1 
ATOM   1284 C CB   . LYS   A 1 55  ? 21.255 11.560  7.438   1.00 13.02 ?  55  LYS   A CB   1 
ATOM   1285 C CG   . LYS   A 1 55  ? 20.500 12.731  8.056   1.00 15.44 ?  55  LYS   A CG   1 
ATOM   1286 C CD   . LYS   A 1 55  ? 19.195 12.975  7.300   1.00 17.16 ?  55  LYS   A CD   1 
ATOM   1287 C CE   . LYS   A 1 55  ? 18.332 14.048  7.941   1.00 19.48 ?  55  LYS   A CE   1 
ATOM   1288 N NZ   . LYS   A 1 55  ? 16.978 14.137  7.306   1.00 20.11 ?  55  LYS   A NZ   1 
ATOM   1289 H H    . LYS   A 1 55  ? 22.704 9.754   6.776   1.00 13.54 ?  55  LYS   A H    1 
ATOM   1290 H HA   . LYS   A 1 55  ? 23.192 12.035  7.898   1.00 14.52 ?  55  LYS   A HA   1 
ATOM   1291 H HB2  . LYS   A 1 55  ? 21.370 11.759  6.497   1.00 15.60 ?  55  LYS   A HB2  1 
ATOM   1292 H HB3  . LYS   A 1 55  ? 20.694 10.773  7.536   1.00 15.60 ?  55  LYS   A HB3  1 
ATOM   1293 H HG2  . LYS   A 1 55  ? 20.280 12.526  8.980   1.00 18.51 ?  55  LYS   A HG2  1 
ATOM   1294 H HG3  . LYS   A 1 55  ? 21.039 13.532  8.004   1.00 18.51 ?  55  LYS   A HG3  1 
ATOM   1295 H HD2  . LYS   A 1 55  ? 19.404 13.257  6.394   1.00 20.57 ?  55  LYS   A HD2  1 
ATOM   1296 H HD3  . LYS   A 1 55  ? 18.681 12.151  7.277   1.00 20.57 ?  55  LYS   A HD3  1 
ATOM   1297 H HE2  . LYS   A 1 55  ? 18.210 13.843  8.880   1.00 23.35 ?  55  LYS   A HE2  1 
ATOM   1298 H HE3  . LYS   A 1 55  ? 18.767 14.910  7.840   1.00 23.35 ?  55  LYS   A HE3  1 
ATOM   1299 H HZ1  . LYS   A 1 55  ? 16.493 14.773  7.702   1.00 24.11 ?  55  LYS   A HZ1  1 
ATOM   1300 H HZ2  . LYS   A 1 55  ? 17.055 14.334  6.441   1.00 24.11 ?  55  LYS   A HZ2  1 
ATOM   1301 H HZ3  . LYS   A 1 55  ? 16.549 13.360  7.386   1.00 24.11 ?  55  LYS   A HZ3  1 
ATOM   1302 N N    . ALA   A 1 56  ? 22.137 9.825   9.957   1.00 12.70 ?  56  ALA   A N    1 
ATOM   1303 C CA   . ALA   A 1 56  ? 22.005 9.506   11.372  1.00 13.41 ?  56  ALA   A CA   1 
ATOM   1304 C C    . ALA   A 1 56  ? 23.339 9.529   12.106  1.00 12.71 ?  56  ALA   A C    1 
ATOM   1305 O O    . ALA   A 1 56  ? 23.348 9.717   13.323  1.00 14.11 ?  56  ALA   A O    1 
ATOM   1306 C CB   . ALA   A 1 56  ? 21.298 8.160   11.553  1.00 14.38 ?  56  ALA   A CB   1 
ATOM   1307 H H    . ALA   A 1 56  ? 21.936 9.181   9.430   1.00 15.21 ?  56  ALA   A H    1 
ATOM   1308 H HA   . ALA   A 1 56  ? 21.452 10.175  11.790  1.00 16.06 ?  56  ALA   A HA   1 
ATOM   1309 H HB1  . ALA   A 1 56  ? 21.224 7.965   12.503  1.00 17.24 ?  56  ALA   A HB1  1 
ATOM   1310 H HB2  . ALA   A 1 56  ? 20.412 8.218   11.160  1.00 17.24 ?  56  ALA   A HB2  1 
ATOM   1311 H HB3  . ALA   A 1 56  ? 21.811 7.466   11.113  1.00 17.24 ?  56  ALA   A HB3  1 
ATOM   1312 N N    . THR   A 1 57  ? 24.456 9.330   11.400  1.00 11.97 ?  57  THR   A N    1 
ATOM   1313 C CA   . THR   A 1 57  ? 25.796 9.464   11.980  1.00 11.95 ?  57  THR   A CA   1 
ATOM   1314 C C    . THR   A 1 57  ? 26.347 10.885  11.897  1.00 12.48 ?  57  THR   A C    1 
ATOM   1315 O O    . THR   A 1 57  ? 27.534 11.097  12.187  1.00 13.41 ?  57  THR   A O    1 
ATOM   1316 C CB   . THR   A 1 57  ? 26.812 8.511   11.321  1.00 12.10 ?  57  THR   A CB   1 
ATOM   1317 O OG1  . THR   A 1 57  ? 27.203 9.000   10.024  1.00 11.71 ?  57  THR   A OG1  1 
ATOM   1318 C CG2  . THR   A 1 57  ? 26.285 7.090   11.213  1.00 12.15 ?  57  THR   A CG2  1 
ATOM   1319 H H    . THR   A 1 57  ? 24.466 9.083   10.572  1.00 14.34 ?  57  THR   A H    1 
ATOM   1320 H HA   . THR   A 1 57  ? 25.749 9.216   12.920  1.00 14.31 ?  57  THR   A HA   1 
ATOM   1321 H HB   . THR   A 1 57  ? 27.607 8.476   11.882  1.00 14.50 ?  57  THR   A HB   1 
ATOM   1322 H HG1  . THR   A 1 57  ? 26.523 9.070   9.531   1.00 14.03 ?  57  THR   A HG1  1 
ATOM   1323 H HG21 . THR   A 1 57  ? 26.972 6.504   10.851  1.00 14.55 ?  57  THR   A HG21 1 
ATOM   1324 H HG22 . THR   A 1 57  ? 26.029 6.761   12.091  1.00 14.55 ?  57  THR   A HG22 1 
ATOM   1325 H HG23 . THR   A 1 57  ? 25.513 7.062   10.632  1.00 14.55 ?  57  THR   A HG23 1 
ATOM   1326 N N    . ASN   A 1 58  ? 25.535 11.859  11.485  1.00 12.96 ?  58  ASN   A N    1 
ATOM   1327 C CA   . ASN   A 1 58  ? 26.004 13.237  11.391  1.00 13.93 ?  58  ASN   A CA   1 
ATOM   1328 C C    . ASN   A 1 58  ? 27.168 13.356  10.398  1.00 12.66 ?  58  ASN   A C    1 
ATOM   1329 O O    . ASN   A 1 58  ? 28.066 14.192  10.562  1.00 13.69 ?  58  ASN   A O    1 
ATOM   1330 C CB   . ASN   A 1 58  ? 26.364 13.767  12.789  1.00 16.71 ?  58  ASN   A CB   1 
ATOM   1331 C CG   . ASN   A 1 58  ? 26.778 15.220  12.797  1.00 21.08 ?  58  ASN   A CG   1 
ATOM   1332 O OD1  . ASN   A 1 58  ? 26.159 16.057  12.145  1.00 22.88 ?  58  ASN   A OD1  1 
ATOM   1333 N ND2  . ASN   A 1 58  ? 27.830 15.532  13.563  1.00 22.57 ?  58  ASN   A ND2  1 
ATOM   1334 H H    . ASN   A 1 58  ? 24.715 11.736  11.238  1.00 15.52 ?  58  ASN   A H    1 
ATOM   1335 H HA   . ASN   A 1 58  ? 25.278 13.775  11.051  1.00 16.69 ?  58  ASN   A HA   1 
ATOM   1336 H HB2  . ASN   A 1 58  ? 25.583 13.676  13.367  1.00 20.03 ?  58  ASN   A HB2  1 
ATOM   1337 H HB3  . ASN   A 1 58  ? 27.096 13.249  13.151  1.00 20.03 ?  58  ASN   A HB3  1 
ATOM   1338 H HD21 . ASN   A 1 58  ? 28.105 16.347  13.608  1.00 27.06 ?  58  ASN   A HD21 1 
ATOM   1339 H HD22 . ASN   A 1 58  ? 28.231 14.918  14.011  1.00 27.06 ?  58  ASN   A HD22 1 
ATOM   1340 N N    . ASN   A 1 59  ? 27.153 12.534  9.344   1.00 11.54 ?  59  ASN   A N    1 
ATOM   1341 C CA   . ASN   A 1 59  ? 28.135 12.501  8.255   1.00 11.33 ?  59  ASN   A CA   1 
ATOM   1342 C C    . ASN   A 1 59  ? 29.443 11.816  8.656   1.00 11.07 ?  59  ASN   A C    1 
ATOM   1343 O O    . ASN   A 1 59  ? 30.366 11.769  7.834   1.00 11.13 ?  59  ASN   A O    1 
ATOM   1344 C CB   . ASN   A 1 59  ? 28.435 13.887  7.650   1.00 11.91 ?  59  ASN   A CB   1 
ATOM   1345 C CG   . ASN   A 1 59  ? 28.783 13.821  6.174   1.00 12.11 ?  59  ASN   A CG   1 
ATOM   1346 O OD1  . ASN   A 1 59  ? 28.074 13.201  5.380   1.00 12.48 ?  59  ASN   A OD1  1 
ATOM   1347 N ND2  . ASN   A 1 59  ? 29.881 14.472  5.795   1.00 12.86 ?  59  ASN   A ND2  1 
ATOM   1348 H H    . ASN   A 1 59  ? 26.539 11.942  9.225   1.00 13.83 ?  59  ASN   A H    1 
ATOM   1349 H HA   . ASN   A 1 59  ? 27.761 11.971  7.539   1.00 13.57 ?  59  ASN   A HA   1 
ATOM   1350 H HB2  . ASN   A 1 59  ? 27.658 14.456  7.745   1.00 14.27 ?  59  ASN   A HB2  1 
ATOM   1351 H HB3  . ASN   A 1 59  ? 29.195 14.283  8.110   1.00 14.27 ?  59  ASN   A HB3  1 
ATOM   1352 H HD21 . ASN   A 1 59  ? 30.121 14.469  4.964   1.00 15.41 ?  59  ASN   A HD21 1 
ATOM   1353 H HD22 . ASN   A 1 59  ? 30.361 14.895  6.371   1.00 15.41 ?  59  ASN   A HD22 1 
ATOM   1354 N N    . ALA   A 1 60  ? 29.558 11.271  9.866   1.00 11.29 ?  60  ALA   A N    1 
ATOM   1355 C CA   . ALA   A 1 60  ? 30.795 10.588  10.225  1.00 11.51 ?  60  ALA   A CA   1 
ATOM   1356 C C    . ALA   A 1 60  ? 31.019 9.351   9.367   1.00 11.61 ?  60  ALA   A C    1 
ATOM   1357 O O    . ALA   A 1 60  ? 32.165 9.015   9.054   1.00 11.87 ?  60  ALA   A O    1 
ATOM   1358 C CB   . ALA   A 1 60  ? 30.796 10.228  11.707  1.00 12.27 ?  60  ALA   A CB   1 
ATOM   1359 H H    . ALA   A 1 60  ? 28.955 11.282  10.479  1.00 13.52 ?  60  ALA   A H    1 
ATOM   1360 H HA   . ALA   A 1 60  ? 31.541 11.193  10.071  1.00 13.79 ?  60  ALA   A HA   1 
ATOM   1361 H HB1  . ALA   A 1 60  ? 31.626 9.779   11.925  1.00 14.70 ?  60  ALA   A HB1  1 
ATOM   1362 H HB2  . ALA   A 1 60  ? 30.716 11.045  12.231  1.00 14.70 ?  60  ALA   A HB2  1 
ATOM   1363 H HB3  . ALA   A 1 60  ? 30.043 9.646   11.891  1.00 14.70 ?  60  ALA   A HB3  1 
ATOM   1364 N N    . MET   A 1 61  ? 29.947 8.657   8.980   1.00 11.18 ?  61  MET   A N    1 
ATOM   1365 C CA   . MET   A 1 61  ? 30.091 7.518   8.076   1.00 11.10 ?  61  MET   A CA   1 
ATOM   1366 C C    . MET   A 1 61  ? 30.738 7.943   6.760   1.00 10.87 ?  61  MET   A C    1 
ATOM   1367 O O    . MET   A 1 61  ? 31.630 7.254   6.248   1.00 11.24 ?  61  MET   A O    1 
ATOM   1368 C CB   . MET   A 1 61  ? 28.729 6.853   7.851   1.00 11.28 ?  61  MET   A CB   1 
ATOM   1369 C CG   . MET   A 1 61  ? 28.737 5.684   6.878   1.00 11.76 ?  61  MET   A CG   1 
ATOM   1370 S SD   . MET   A 1 61  ? 27.118 4.947   6.667   1.00 12.55 ?  61  MET   A SD   1 
ATOM   1371 C CE   . MET   A 1 61  ? 26.976 4.055   8.218   1.00 14.03 ?  61  MET   A CE   1 
ATOM   1372 H H    . MET   A 1 61  ? 29.137 8.826   9.213   1.00 13.39 ?  61  MET   A H    1 
ATOM   1373 H HA   . MET   A 1 61  ? 30.666 6.862   8.500   1.00 13.30 ?  61  MET   A HA   1 
ATOM   1374 H HB2  . MET   A 1 61  ? 28.404 6.522   8.701   1.00 13.51 ?  61  MET   A HB2  1 
ATOM   1375 H HB3  . MET   A 1 61  ? 28.115 7.515   7.501   1.00 13.51 ?  61  MET   A HB3  1 
ATOM   1376 H HG2  . MET   A 1 61  ? 29.036 5.984   6.008   1.00 14.09 ?  61  MET   A HG2  1 
ATOM   1377 H HG3  . MET   A 1 61  ? 29.334 4.991   7.212   1.00 14.09 ?  61  MET   A HG3  1 
ATOM   1378 H HE1  . MET   A 1 61  ? 26.132 3.574   8.235   1.00 16.81 ?  61  MET   A HE1  1 
ATOM   1379 H HE2  . MET   A 1 61  ? 27.714 3.433   8.295   1.00 16.81 ?  61  MET   A HE2  1 
ATOM   1380 H HE3  . MET   A 1 61  ? 27.003 4.691   8.954   1.00 16.81 ?  61  MET   A HE3  1 
ATOM   1381 N N    . GLN   A 1 62  ? 30.298 9.071   6.194   1.00 11.13 ?  62  GLN   A N    1 
ATOM   1382 C CA   . GLN   A 1 62  ? 30.873 9.539   4.934   1.00 11.07 ?  62  GLN   A CA   1 
ATOM   1383 C C    . GLN   A 1 62  ? 32.345 9.906   5.091   1.00 10.94 ?  62  GLN   A C    1 
ATOM   1384 O O    . GLN   A 1 62  ? 33.159 9.590   4.216   1.00 11.41 ?  62  GLN   A O    1 
ATOM   1385 C CB   . GLN   A 1 62  ? 30.088 10.730  4.398   1.00 11.25 ?  62  GLN   A CB   1 
ATOM   1386 C CG   . GLN   A 1 62  ? 30.475 11.091  2.975   1.00 11.30 ?  62  GLN   A CG   1 
ATOM   1387 C CD   . GLN   A 1 62  ? 30.146 9.968   2.017   1.00 11.58 ?  62  GLN   A CD   1 
ATOM   1388 O OE1  . GLN   A 1 62  ? 28.965 9.663   1.801   1.00 12.10 ?  62  GLN   A OE1  1 
ATOM   1389 N NE2  . GLN   A 1 62  ? 31.165 9.302   1.485   1.00 12.28 ?  62  GLN   A NE2  1 
ATOM   1390 H H    . GLN   A 1 62  ? 29.672 9.564   6.511   1.00 13.33 ?  62  GLN   A H    1 
ATOM   1391 H HA   . GLN   A 1 62  ? 30.820 8.818   4.286   1.00 13.26 ?  62  GLN   A HA   1 
ATOM   1392 H HB2  . GLN   A 1 62  ? 29.145 10.520  4.415   1.00 13.47 ?  62  GLN   A HB2  1 
ATOM   1393 H HB3  . GLN   A 1 62  ? 30.270 11.502  4.960   1.00 13.47 ?  62  GLN   A HB3  1 
ATOM   1394 H HG2  . GLN   A 1 62  ? 29.972 11.871  2.699   1.00 13.53 ?  62  GLN   A HG2  1 
ATOM   1395 H HG3  . GLN   A 1 62  ? 31.424 11.261  2.928   1.00 13.53 ?  62  GLN   A HG3  1 
ATOM   1396 H HE21 . GLN   A 1 62  ? 31.971 9.531   1.674   1.00 14.71 ?  62  GLN   A HE21 1 
ATOM   1397 H HE22 . GLN   A 1 62  ? 31.018 8.651   0.942   1.00 14.71 ?  62  GLN   A HE22 1 
ATOM   1398 N N    . VAL   A 1 63  ? 32.700 10.582  6.189   1.00 11.48 ?  63  VAL   A N    1 
ATOM   1399 C CA   . VAL   A 1 63  ? 34.093 10.971  6.417   1.00 12.10 ?  63  VAL   A CA   1 
ATOM   1400 C C    . VAL   A 1 63  ? 34.983 9.734   6.487   1.00 11.54 ?  63  VAL   A C    1 
ATOM   1401 O O    . VAL   A 1 63  ? 36.038 9.662   5.843   1.00 12.47 ?  63  VAL   A O    1 
ATOM   1402 C CB   . VAL   A 1 63  ? 34.187 11.839  7.686   1.00 14.06 ?  63  VAL   A CB   1 
ATOM   1403 C CG1  . VAL   A 1 63  ? 35.632 12.062  8.095   1.00 15.57 ?  63  VAL   A CG1  1 
ATOM   1404 C CG2  . VAL   A 1 63  ? 33.488 13.182  7.458   1.00 14.44 ?  63  VAL   A CG2  1 
ATOM   1405 H H    . VAL   A 1 63  ? 32.153 10.829  6.812   1.00 13.75 ?  63  VAL   A H    1 
ATOM   1406 H HA   . VAL   A 1 63  ? 34.390 11.509  5.671   1.00 14.50 ?  63  VAL   A HA   1 
ATOM   1407 H HB   . VAL   A 1 63  ? 33.737 11.390  8.417   1.00 16.85 ?  63  VAL   A HB   1 
ATOM   1408 H HG11 . VAL   A 1 63  ? 35.666 12.788  8.739   1.00 18.66 ?  63  VAL   A HG11 1 
ATOM   1409 H HG12 . VAL   A 1 63  ? 35.976 11.250  8.497   1.00 18.66 ?  63  VAL   A HG12 1 
ATOM   1410 H HG13 . VAL   A 1 63  ? 36.149 12.294  7.309   1.00 18.66 ?  63  VAL   A HG13 1 
ATOM   1411 H HG21 . VAL   A 1 63  ? 33.565 13.720  8.262   1.00 17.31 ?  63  VAL   A HG21 1 
ATOM   1412 H HG22 . VAL   A 1 63  ? 33.915 13.637  6.714   1.00 17.31 ?  63  VAL   A HG22 1 
ATOM   1413 H HG23 . VAL   A 1 63  ? 32.554 13.021  7.255   1.00 17.31 ?  63  VAL   A HG23 1 
ATOM   1414 N N    . GLU   A 1 64  ? 34.551 8.724   7.247   1.00 11.74 ?  64  GLU   A N    1 
ATOM   1415 C CA   . GLU   A 1 64  ? 35.320 7.488   7.351   1.00 12.14 ?  64  GLU   A CA   1 
ATOM   1416 C C    . GLU   A 1 64  ? 35.409 6.793   5.998   1.00 11.76 ?  64  GLU   A C    1 
ATOM   1417 O O    . GLU   A 1 64  ? 36.456 6.241   5.626   1.00 12.10 ?  64  GLU   A O    1 
ATOM   1418 C CB   . GLU   A 1 64  ? 34.634 6.580   8.376   1.00 12.67 ?  64  GLU   A CB   1 
ATOM   1419 C CG   . GLU   A 1 64  ? 35.276 5.221   8.517   1.00 13.49 ?  64  GLU   A CG   1 
ATOM   1420 C CD   . GLU   A 1 64  ? 34.389 4.231   9.241   1.00 13.96 ?  64  GLU   A CD   1 
ATOM   1421 O OE1  . GLU   A 1 64  ? 33.149 4.324   9.106   1.00 14.49 ?  64  GLU   A OE1  1 
ATOM   1422 O OE2  . GLU   A 1 64  ? 34.938 3.333   9.918   1.00 14.30 -1 64  GLU   A OE2  1 
ATOM   1423 H H    . GLU   A 1 64  ? 33.818 8.728   7.701   1.00 14.06 ?  64  GLU   A H    1 
ATOM   1424 H HA   . GLU   A 1 64  ? 36.215 7.686   7.665   1.00 14.54 ?  64  GLU   A HA   1 
ATOM   1425 H HB2  . GLU   A 1 64  ? 34.665 7.011   9.249   1.00 15.18 ?  64  GLU   A HB2  1 
ATOM   1426 H HB3  . GLU   A 1 64  ? 33.710 6.452   8.111   1.00 15.18 ?  64  GLU   A HB3  1 
ATOM   1427 H HG2  . GLU   A 1 64  ? 35.466 4.856   7.635   1.00 16.17 ?  64  GLU   A HG2  1 
ATOM   1428 H HG3  . GLU   A 1 64  ? 36.098 5.313   9.018   1.00 16.17 ?  64  GLU   A HG3  1 
ATOM   1429 N N    . SER   A 1 65  ? 34.294 6.795   5.259   1.00 11.20 ?  65  SER   A N    1 
ATOM   1430 C CA   . SER   A 1 65  ? 34.245 6.145   3.955   1.00 11.18 ?  65  SER   A CA   1 
ATOM   1431 C C    . SER   A 1 65  ? 35.182 6.808   2.957   1.00 11.23 ?  65  SER   A C    1 
ATOM   1432 O O    . SER   A 1 65  ? 35.825 6.123   2.155   1.00 12.27 ?  65  SER   A O    1 
ATOM   1433 C CB   . SER   A 1 65  ? 32.813 6.162   3.413   1.00 11.53 ?  65  SER   A CB   1 
ATOM   1434 O OG   . SER   A 1 65  ? 31.947 5.339   4.183   1.00 11.68 ?  65  SER   A OG   1 
ATOM   1435 H H    . SER   A 1 65  ? 33.554 7.171   5.493   1.00 13.42 ?  65  SER   A H    1 
ATOM   1436 H HA   . SER   A 1 65  ? 34.523 5.220   4.055   1.00 13.39 ?  65  SER   A HA   1 
ATOM   1437 H HB2  . SER   A 1 65  ? 32.481 7.071   3.437   1.00 13.82 ?  65  SER   A HB2  1 
ATOM   1438 H HB3  . SER   A 1 65  ? 32.825 5.836   2.500   1.00 13.82 ?  65  SER   A HB3  1 
ATOM   1439 H HG   . SER   A 1 65  ? 31.929 5.605   4.981   1.00 13.99 ?  65  SER   A HG   1 
ATOM   1440 N N    . ASP   A 1 66  ? 35.258 8.140   2.971   1.00 11.50 ?  66  ASP   A N    1 
ATOM   1441 C CA   . ASP   A 1 66  ? 36.133 8.831   2.034   1.00 12.73 ?  66  ASP   A CA   1 
ATOM   1442 C C    . ASP   A 1 66  ? 37.593 8.470   2.285   1.00 12.43 ?  66  ASP   A C    1 
ATOM   1443 O O    . ASP   A 1 66  ? 38.372 8.310   1.339   1.00 13.07 ?  66  ASP   A O    1 
ATOM   1444 C CB   . ASP   A 1 66  ? 35.911 10.339  2.125   1.00 15.07 ?  66  ASP   A CB   1 
ATOM   1445 C CG   . ASP   A 1 66  ? 34.582 10.804  1.495   1.00 17.52 ?  66  ASP   A CG   1 
ATOM   1446 O OD1  . ASP   A 1 66  ? 33.880 10.017  0.826   1.00 18.04 ?  66  ASP   A OD1  1 
ATOM   1447 O OD2  . ASP   A 1 66  ? 34.267 11.999  1.658   1.00 20.61 -1 66  ASP   A OD2  1 
ATOM   1448 H H    . ASP   A 1 66  ? 34.806 8.655   3.500   1.00 13.77 ?  66  ASP   A H    1 
ATOM   1449 H HA   . ASP   A 1 66  ? 35.908 8.549   1.137   1.00 15.25 ?  66  ASP   A HA   1 
ATOM   1450 H HB2  . ASP   A 1 66  ? 35.886 10.604  3.054   1.00 18.06 ?  66  ASP   A HB2  1 
ATOM   1451 H HB3  . ASP   A 1 66  ? 36.632 10.791  1.664   1.00 18.06 ?  66  ASP   A HB3  1 
ATOM   1452 N N    . ASP   A 1 67  ? 37.984 8.341   3.555   1.00 12.42 ?  67  ASP   A N    1 
ATOM   1453 C CA   . ASP   A 1 67  ? 39.334 7.888   3.873   1.00 13.33 ?  67  ASP   A CA   1 
ATOM   1454 C C    . ASP   A 1 67  ? 39.555 6.448   3.412   1.00 13.41 ?  67  ASP   A C    1 
ATOM   1455 O O    . ASP   A 1 67  ? 40.621 6.120   2.873   1.00 14.36 ?  67  ASP   A O    1 
ATOM   1456 C CB   . ASP   A 1 67  ? 39.588 8.045   5.373   1.00 14.37 ?  67  ASP   A CB   1 
ATOM   1457 C CG   . ASP   A 1 67  ? 40.882 7.395   5.816   1.00 15.42 ?  67  ASP   A CG   1 
ATOM   1458 O OD1  . ASP   A 1 67  ? 41.954 8.043   5.720   1.00 18.11 ?  67  ASP   A OD1  1 
ATOM   1459 O OD2  . ASP   A 1 67  ? 40.821 6.225   6.253   1.00 15.88 -1 67  ASP   A OD2  1 
ATOM   1460 H H    . ASP   A 1 67  ? 37.493 8.518   4.242   1.00 14.88 ?  67  ASP   A H    1 
ATOM   1461 H HA   . ASP   A 1 67  ? 39.972 8.452   3.408   1.00 15.97 ?  67  ASP   A HA   1 
ATOM   1462 H HB2  . ASP   A 1 67  ? 39.640 8.987   5.590   1.00 17.22 ?  67  ASP   A HB2  1 
ATOM   1463 H HB3  . ASP   A 1 67  ? 38.860 7.630   5.865   1.00 17.22 ?  67  ASP   A HB3  1 
ATOM   1464 N N    . TYR   A 1 68  ? 38.551 5.578   3.587   1.00 13.29 ?  68  TYR   A N    1 
ATOM   1465 C CA   . TYR   A 1 68  ? 38.666 4.197   3.112   1.00 13.29 ?  68  TYR   A CA   1 
ATOM   1466 C C    . TYR   A 1 68  ? 38.920 4.149   1.606   1.00 13.02 ?  68  TYR   A C    1 
ATOM   1467 O O    . TYR   A 1 68  ? 39.798 3.411   1.135   1.00 13.44 ?  68  TYR   A O    1 
ATOM   1468 C CB   . TYR   A 1 68  ? 37.410 3.385   3.479   1.00 13.03 ?  68  TYR   A CB   1 
ATOM   1469 C CG   . TYR   A 1 68  ? 37.429 1.996   2.842   1.00 14.14 ?  68  TYR   A CG   1 
ATOM   1470 C CD1  . TYR   A 1 68  ? 36.979 1.810   1.542   1.00 15.38 ?  68  TYR   A CD1  1 
ATOM   1471 C CD2  . TYR   A 1 68  ? 37.972 0.902   3.505   1.00 16.06 ?  68  TYR   A CD2  1 
ATOM   1472 C CE1  . TYR   A 1 68  ? 37.040 0.596   0.923   1.00 16.66 ?  68  TYR   A CE1  1 
ATOM   1473 C CE2  . TYR   A 1 68  ? 38.034 -0.356  2.883   1.00 16.52 ?  68  TYR   A CE2  1 
ATOM   1474 C CZ   . TYR   A 1 68  ? 37.578 -0.484  1.591   1.00 17.10 ?  68  TYR   A CZ   1 
ATOM   1475 O OH   . TYR   A 1 68  ? 37.654 -1.702  0.955   1.00 18.38 ?  68  TYR   A OH   1 
ATOM   1476 H H    . TYR   A 1 68  ? 37.799 5.767   3.973   1.00 15.92 ?  68  TYR   A H    1 
ATOM   1477 H HA   . TYR   A 1 68  ? 39.419 3.787   3.555   1.00 15.93 ?  68  TYR   A HA   1 
ATOM   1478 H HB2  . TYR   A 1 68  ? 37.370 3.276   4.445   1.00 15.62 ?  68  TYR   A HB2  1 
ATOM   1479 H HB3  . TYR   A 1 68  ? 36.619 3.854   3.167   1.00 15.62 ?  68  TYR   A HB3  1 
ATOM   1480 H HD1  . TYR   A 1 68  ? 36.627 2.541   1.081   1.00 18.43 ?  68  TYR   A HD1  1 
ATOM   1481 H HD2  . TYR   A 1 68  ? 38.305 1.006   4.367   1.00 19.25 ?  68  TYR   A HD2  1 
ATOM   1482 H HE1  . TYR   A 1 68  ? 36.725 0.501   0.055   1.00 19.97 ?  68  TYR   A HE1  1 
ATOM   1483 H HE2  . TYR   A 1 68  ? 38.407 -1.086  3.320   1.00 19.80 ?  68  TYR   A HE2  1 
ATOM   1484 H HH   . TYR   A 1 68  ? 37.993 -2.274  1.464   1.00 22.04 ?  68  TYR   A HH   1 
ATOM   1485 N N    . ILE   A 1 69  ? 38.147 4.918   0.830   1.00 12.55 ?  69  ILE   A N    1 
ATOM   1486 C CA   . ILE   A 1 69  ? 38.298 4.910   -0.624  1.00 13.00 ?  69  ILE   A CA   1 
ATOM   1487 C C    . ILE   A 1 69  ? 39.650 5.494   -1.036  1.00 13.20 ?  69  ILE   A C    1 
ATOM   1488 O O    . ILE   A 1 69  ? 40.292 5.002   -1.971  1.00 13.83 ?  69  ILE   A O    1 
ATOM   1489 C CB   . ILE   A 1 69  ? 37.123 5.653   -1.290  1.00 13.67 ?  69  ILE   A CB   1 
ATOM   1490 C CG1  . ILE   A 1 69  ? 35.793 4.931   -1.046  1.00 13.65 ?  69  ILE   A CG1  1 
ATOM   1491 C CG2  . ILE   A 1 69  ? 37.396 5.868   -2.788  1.00 15.57 ?  69  ILE   A CG2  1 
ATOM   1492 C CD1  . ILE   A 1 69  ? 35.632 3.647   -1.839  1.00 13.95 ?  69  ILE   A CD1  1 
ATOM   1493 H H    . ILE   A 1 69  ? 37.543 5.455   1.125   1.00 15.03 ?  69  ILE   A H    1 
ATOM   1494 H HA   . ILE   A 1 69  ? 38.278 3.994   -0.926  1.00 15.58 ?  69  ILE   A HA   1 
ATOM   1495 H HB   . ILE   A 1 69  ? 37.059 6.527   -0.880  1.00 16.38 ?  69  ILE   A HB   1 
ATOM   1496 H HG12 . ILE   A 1 69  ? 35.732 4.706   -0.103  1.00 16.35 ?  69  ILE   A HG12 1 
ATOM   1497 H HG13 . ILE   A 1 69  ? 35.069 5.527   -1.288  1.00 16.35 ?  69  ILE   A HG13 1 
ATOM   1498 H HG21 . ILE   A 1 69  ? 36.557 6.087   -3.230  1.00 18.66 ?  69  ILE   A HG21 1 
ATOM   1499 H HG22 . ILE   A 1 69  ? 38.020 6.605   -2.895  1.00 18.66 ?  69  ILE   A HG22 1 
ATOM   1500 H HG23 . ILE   A 1 69  ? 37.765 5.059   -3.166  1.00 18.66 ?  69  ILE   A HG23 1 
ATOM   1501 H HD11 . ILE   A 1 69  ? 34.814 3.210   -1.558  1.00 16.72 ?  69  ILE   A HD11 1 
ATOM   1502 H HD12 . ILE   A 1 69  ? 35.579 3.867   -2.784  1.00 16.72 ?  69  ILE   A HD12 1 
ATOM   1503 H HD13 . ILE   A 1 69  ? 36.391 3.073   -1.673  1.00 16.72 ?  69  ILE   A HD13 1 
ATOM   1504 N N    A ALA   A 1 70  ? 40.055 6.597   -0.411  0.58 14.34 ?  70  ALA   A N    1 
ATOM   1505 N N    B ALA   A 1 70  ? 40.121 6.520   -0.322  0.42 13.74 ?  70  ALA   A N    1 
ATOM   1506 C CA   A ALA   A 1 70  ? 41.343 7.190   -0.755  0.58 15.55 ?  70  ALA   A CA   1 
ATOM   1507 C CA   B ALA   A 1 70  ? 41.426 7.105   -0.633  0.42 14.36 ?  70  ALA   A CA   1 
ATOM   1508 C C    A ALA   A 1 70  ? 42.460 6.163   -0.638  0.58 15.73 ?  70  ALA   A C    1 
ATOM   1509 C C    B ALA   A 1 70  ? 42.566 6.128   -0.377  0.42 14.84 ?  70  ALA   A C    1 
ATOM   1510 O O    A ALA   A 1 70  ? 43.365 6.116   -1.478  0.58 16.44 ?  70  ALA   A O    1 
ATOM   1511 O O    B ALA   A 1 70  ? 43.626 6.239   -1.004  0.42 15.89 ?  70  ALA   A O    1 
ATOM   1512 C CB   A ALA   A 1 70  ? 41.609 8.419   0.120   0.58 16.48 ?  70  ALA   A CB   1 
ATOM   1513 C CB   B ALA   A 1 70  ? 41.646 8.379   0.182   0.42 14.99 ?  70  ALA   A CB   1 
ATOM   1514 H H    A ALA   A 1 70  ? 39.612 7.019   0.190   0.58 17.18 ?  70  ALA   A H    1 
ATOM   1515 H H    B ALA   A 1 70  ? 39.713 6.894   0.331   0.42 16.47 ?  70  ALA   A H    1 
ATOM   1516 H HA   A ALA   A 1 70  ? 41.322 7.489   -1.677  0.58 18.63 ?  70  ALA   A HA   1 
ATOM   1517 H HA   B ALA   A 1 70  ? 41.446 7.346   -1.574  0.42 17.20 ?  70  ALA   A HA   1 
ATOM   1518 H HB1  A ALA   A 1 70  ? 42.471 8.799   -0.121  0.58 19.76 ?  70  ALA   A HB1  1 
ATOM   1519 H HB1  B ALA   A 1 70  ? 42.523 8.742   -0.034  0.42 17.97 ?  70  ALA   A HB1  1 
ATOM   1520 H HB2  A ALA   A 1 70  ? 40.909 9.075   -0.033  0.58 19.76 ?  70  ALA   A HB2  1 
ATOM   1521 H HB2  B ALA   A 1 70  ? 40.958 9.020   -0.044  0.42 17.97 ?  70  ALA   A HB2  1 
ATOM   1522 H HB3  A ALA   A 1 70  ? 41.614 8.151   1.050   0.58 19.76 ?  70  ALA   A HB3  1 
ATOM   1523 H HB3  B ALA   A 1 70  ? 41.605 8.160   1.125   0.42 17.97 ?  70  ALA   A HB3  1 
ATOM   1524 N N    A THR   A 1 71  ? 42.382 5.297   0.368   0.58 15.59 ?  71  THR   A N    1 
ATOM   1525 N N    B THR   A 1 71  ? 42.385 5.193   0.550   0.42 15.20 ?  71  THR   A N    1 
ATOM   1526 C CA   A THR   A 1 71  ? 43.429 4.306   0.599   0.58 16.81 ?  71  THR   A CA   1 
ATOM   1527 C CA   B THR   A 1 71  ? 43.406 4.196   0.847   0.42 16.26 ?  71  THR   A CA   1 
ATOM   1528 C C    A THR   A 1 71  ? 43.279 3.097   -0.316  0.58 16.38 ?  71  THR   A C    1 
ATOM   1529 C C    B THR   A 1 71  ? 43.291 2.943   -0.009  0.42 15.78 ?  71  THR   A C    1 
ATOM   1530 O O    A THR   A 1 71  ? 44.251 2.648   -0.936  0.58 17.03 ?  71  THR   A O    1 
ATOM   1531 O O    B THR   A 1 71  ? 44.315 2.317   -0.312  0.42 15.36 ?  71  THR   A O    1 
ATOM   1532 C CB   A THR   A 1 71  ? 43.378 3.855   2.056   0.58 18.87 ?  71  THR   A CB   1 
ATOM   1533 C CB   B THR   A 1 71  ? 43.305 3.778   2.315   0.42 18.45 ?  71  THR   A CB   1 
ATOM   1534 O OG1  A THR   A 1 71  ? 43.658 4.973   2.904   0.58 20.54 ?  71  THR   A OG1  1 
ATOM   1535 O OG1  B THR   A 1 71  ? 43.461 4.929   3.151   0.42 19.76 ?  71  THR   A OG1  1 
ATOM   1536 C CG2  A THR   A 1 71  ? 44.392 2.753   2.327   0.58 19.57 ?  71  THR   A CG2  1 
ATOM   1537 C CG2  B THR   A 1 71  ? 44.364 2.731   2.654   0.42 19.18 ?  71  THR   A CG2  1 
ATOM   1538 H H    A THR   A 1 71  ? 41.726 5.249   0.920   0.58 18.68 ?  71  THR   A H    1 
ATOM   1539 H H    B THR   A 1 71  ? 41.677 5.113   1.028   0.42 18.22 ?  71  THR   A H    1 
ATOM   1540 H HA   A THR   A 1 71  ? 44.289 4.704   0.426   0.58 20.14 ?  71  THR   A HA   1 
ATOM   1541 H HA   B THR   A 1 71  ? 44.284 4.582   0.701   0.42 19.49 ?  71  THR   A HA   1 
ATOM   1542 H HB   A THR   A 1 71  ? 42.489 3.502   2.248   0.58 22.62 ?  71  THR   A HB   1 
ATOM   1543 H HB   B THR   A 1 71  ? 42.436 3.389   2.482   0.42 22.11 ?  71  THR   A HB   1 
ATOM   1544 H HG1  A THR   A 1 71  ? 43.607 4.742   3.708   0.58 24.62 ?  71  THR   A HG1  1 
ATOM   1545 H HG1  B THR   A 1 71  ? 43.440 4.702   3.957   0.42 23.68 ?  71  THR   A HG1  1 
ATOM   1546 H HG21 A THR   A 1 71  ? 44.508 2.644   3.286   0.58 23.46 ?  71  THR   A HG21 1 
ATOM   1547 H HG21 B THR   A 1 71  ? 44.457 2.654   3.616   0.42 22.99 ?  71  THR   A HG21 1 
ATOM   1548 H HG22 A THR   A 1 71  ? 44.090 1.912   1.952   0.58 23.46 ?  71  THR   A HG22 1 
ATOM   1549 H HG22 B THR   A 1 71  ? 44.110 1.865   2.294   0.42 22.99 ?  71  THR   A HG22 1 
ATOM   1550 H HG23 A THR   A 1 71  ? 45.248 2.988   1.935   0.58 23.46 ?  71  THR   A HG23 1 
ATOM   1551 H HG23 B THR   A 1 71  ? 45.222 2.988   2.276   0.42 22.99 ?  71  THR   A HG23 1 
ATOM   1552 N N    . ASN   A 1 72  ? 42.070 2.544   -0.387  1.00 15.71 ?  72  ASN   A N    1 
ATOM   1553 C CA   . ASN   A 1 72  ? 41.834 1.231   -0.982  1.00 15.67 ?  72  ASN   A CA   1 
ATOM   1554 C C    . ASN   A 1 72  ? 41.223 1.238   -2.374  1.00 16.00 ?  72  ASN   A C    1 
ATOM   1555 O O    . ASN   A 1 72  ? 41.222 0.189   -3.031  1.00 16.61 ?  72  ASN   A O    1 
ATOM   1556 C CB   . ASN   A 1 72  ? 40.921 0.421   -0.057  1.00 16.45 ?  72  ASN   A CB   1 
ATOM   1557 C CG   . ASN   A 1 72  ? 41.523 0.258   1.314   1.00 17.64 ?  72  ASN   A CG   1 
ATOM   1558 O OD1  . ASN   A 1 72  ? 41.081 0.868   2.284   1.00 19.63 ?  72  ASN   A OD1  1 
ATOM   1559 N ND2  . ASN   A 1 72  ? 42.568 -0.529  1.391   1.00 18.23 ?  72  ASN   A ND2  1 
ATOM   1560 H H    A ASN   A 1 72  ? 41.356 2.909   -0.081  0.58 18.82 ?  72  ASN   A H    1 
ATOM   1561 H H    B ASN   A 1 72  ? 41.356 3.011   -0.288  0.42 18.82 ?  72  ASN   A H    1 
ATOM   1562 H HA   . ASN   A 1 72  ? 42.677 0.762   -1.045  1.00 18.78 ?  72  ASN   A HA   1 
ATOM   1563 H HB2  . ASN   A 1 72  ? 40.069 0.874   0.030   1.00 19.71 ?  72  ASN   A HB2  1 
ATOM   1564 H HB3  . ASN   A 1 72  ? 40.790 -0.465  -0.439  1.00 19.71 ?  72  ASN   A HB3  1 
ATOM   1565 H HD21 . ASN   A 1 72  ? 42.950 -0.653  2.151   1.00 21.85 ?  72  ASN   A HD21 1 
ATOM   1566 H HD22 . ASN   A 1 72  ? 42.860 -0.931  0.690   1.00 21.85 ?  72  ASN   A HD22 1 
ATOM   1567 N N    . GLY   A 1 73  ? 40.691 2.364   -2.836  1.00 15.27 ?  73  GLY   A N    1 
ATOM   1568 C CA   . GLY   A 1 73  ? 39.958 2.389   -4.078  1.00 14.99 ?  73  GLY   A CA   1 
ATOM   1569 C C    . GLY   A 1 73  ? 38.559 1.818   -3.918  1.00 14.15 ?  73  GLY   A C    1 
ATOM   1570 O O    . GLY   A 1 73  ? 38.158 1.374   -2.839  1.00 14.62 ?  73  GLY   A O    1 
ATOM   1571 H H    . GLY   A 1 73  ? 40.738 3.133   -2.443  1.00 18.30 ?  73  GLY   A H    1 
ATOM   1572 H HA2  . GLY   A 1 73  ? 39.886 3.307   -4.391  1.00 17.96 ?  73  GLY   A HA2  1 
ATOM   1573 H HA3  . GLY   A 1 73  ? 40.436 1.873   -4.746  1.00 17.96 ?  73  GLY   A HA3  1 
ATOM   1574 N N    . PRO   A 1 74  ? 37.792 1.824   -5.004  1.00 14.61 ?  74  PRO   A N    1 
ATOM   1575 C CA   . PRO   A 1 74  ? 36.389 1.410   -4.927  1.00 14.71 ?  74  PRO   A CA   1 
ATOM   1576 C C    . PRO   A 1 74  ? 36.226 -0.076  -4.627  1.00 13.69 ?  74  PRO   A C    1 
ATOM   1577 O O    . PRO   A 1 74  ? 37.089 -0.915  -4.905  1.00 14.74 ?  74  PRO   A O    1 
ATOM   1578 C CB   . PRO   A 1 74  ? 35.847 1.732   -6.324  1.00 16.13 ?  74  PRO   A CB   1 
ATOM   1579 C CG   . PRO   A 1 74  ? 36.826 2.662   -6.937  1.00 18.93 ?  74  PRO   A CG   1 
ATOM   1580 C CD   . PRO   A 1 74  ? 38.149 2.326   -6.339  1.00 16.04 ?  74  PRO   A CD   1 
ATOM   1581 H HA   . PRO   A 1 74  ? 35.916 1.937   -4.261  1.00 17.63 ?  74  PRO   A HA   1 
ATOM   1582 H HB2  . PRO   A 1 74  ? 35.780 0.914   -6.839  1.00 19.33 ?  74  PRO   A HB2  1 
ATOM   1583 H HB3  . PRO   A 1 74  ? 34.978 2.157   -6.242  1.00 19.33 ?  74  PRO   A HB3  1 
ATOM   1584 H HG2  . PRO   A 1 74  ? 36.847 2.528   -7.897  1.00 22.70 ?  74  PRO   A HG2  1 
ATOM   1585 H HG3  . PRO   A 1 74  ? 36.586 3.577   -6.726  1.00 22.70 ?  74  PRO   A HG3  1 
ATOM   1586 H HD2  . PRO   A 1 74  ? 38.594 1.632   -6.857  1.00 19.22 ?  74  PRO   A HD2  1 
ATOM   1587 H HD3  . PRO   A 1 74  ? 38.703 3.123   -6.278  1.00 19.22 ?  74  PRO   A HD3  1 
ATOM   1588 N N    . LEU   A 1 75  ? 35.068 -0.392  -4.055  1.00 12.94 ?  75  LEU   A N    1 
ATOM   1589 C CA   . LEU   A 1 75  ? 34.661 -1.780  -3.915  1.00 12.24 ?  75  LEU   A CA   1 
ATOM   1590 C C    . LEU   A 1 75  ? 34.284 -2.348  -5.281  1.00 12.62 ?  75  LEU   A C    1 
ATOM   1591 O O    . LEU   A 1 75  ? 34.165 -1.631  -6.275  1.00 14.08 ?  75  LEU   A O    1 
ATOM   1592 C CB   . LEU   A 1 75  ? 33.470 -1.899  -2.967  1.00 12.40 ?  75  LEU   A CB   1 
ATOM   1593 C CG   . LEU   A 1 75  ? 33.661 -1.479  -1.513  1.00 13.88 ?  75  LEU   A CG   1 
ATOM   1594 C CD1  . LEU   A 1 75  ? 32.368 -1.698  -0.730  1.00 15.73 ?  75  LEU   A CD1  1 
ATOM   1595 C CD2  . LEU   A 1 75  ? 34.798 -2.184  -0.839  1.00 17.16 ?  75  LEU   A CD2  1 
ATOM   1596 H H    . LEU   A 1 75  ? 34.500 0.179   -3.739  1.00 15.50 ?  75  LEU   A H    1 
ATOM   1597 H HA   . LEU   A 1 75  ? 35.395 -2.295  -3.559  1.00 14.67 ?  75  LEU   A HA   1 
ATOM   1598 H HB2  . LEU   A 1 75  ? 32.747 -1.363  -3.323  1.00 14.86 ?  75  LEU   A HB2  1 
ATOM   1599 H HB3  . LEU   A 1 75  ? 33.197 -2.831  -2.954  1.00 14.86 ?  75  LEU   A HB3  1 
ATOM   1600 H HG   . LEU   A 1 75  ? 33.861 -0.527  -1.495  1.00 16.63 ?  75  LEU   A HG   1 
ATOM   1601 H HD11 . LEU   A 1 75  ? 32.507 -1.418  0.190   1.00 18.85 ?  75  LEU   A HD11 1 
ATOM   1602 H HD12 . LEU   A 1 75  ? 31.665 -1.161  -1.133  1.00 18.85 ?  75  LEU   A HD12 1 
ATOM   1603 H HD13 . LEU   A 1 75  ? 32.134 -2.634  -0.763  1.00 18.85 ?  75  LEU   A HD13 1 
ATOM   1604 H HD21 . LEU   A 1 75  ? 34.842 -1.899  0.088   1.00 20.57 ?  75  LEU   A HD21 1 
ATOM   1605 H HD22 . LEU   A 1 75  ? 34.652 -3.139  -0.887  1.00 20.57 ?  75  LEU   A HD22 1 
ATOM   1606 H HD23 . LEU   A 1 75  ? 35.629 -1.953  -1.291  1.00 20.57 ?  75  LEU   A HD23 1 
ATOM   1607 N N    . LYS   A 1 76  ? 34.100 -3.668  -5.313  1.00 13.17 ?  76  LYS   A N    1 
ATOM   1608 C CA   . LYS   A 1 76  ? 33.519 -4.378  -6.447  1.00 13.75 ?  76  LYS   A CA   1 
ATOM   1609 C C    . LYS   A 1 76  ? 32.006 -4.461  -6.266  1.00 12.31 ?  76  LYS   A C    1 
ATOM   1610 O O    . LYS   A 1 76  ? 31.518 -4.572  -5.144  1.00 12.44 ?  76  LYS   A O    1 
ATOM   1611 C CB   . LYS   A 1 76  ? 34.066 -5.816  -6.510  1.00 15.32 ?  76  LYS   A CB   1 
ATOM   1612 C CG   . LYS   A 1 76  ? 35.576 -5.926  -6.683  1.00 16.40 ?  76  LYS   A CG   1 
ATOM   1613 C CD   . LYS   A 1 76  ? 36.085 -7.347  -6.516  1.00 17.86 ?  76  LYS   A CD   1 
ATOM   1614 C CE   . LYS   A 1 76  ? 37.591 -7.402  -6.683  1.00 20.40 ?  76  LYS   A CE   1 
ATOM   1615 N NZ   . LYS   A 1 76  ? 38.128 -8.764  -6.502  1.00 21.42 ?  76  LYS   A NZ   1 
ATOM   1616 H H    . LYS   A 1 76  ? 34.317 -4.189  -4.664  1.00 15.78 ?  76  LYS   A H    1 
ATOM   1617 H HA   . LYS   A 1 76  ? 33.724 -3.916  -7.278  1.00 16.48 ?  76  LYS   A HA   1 
ATOM   1618 H HB2  . LYS   A 1 76  ? 33.832 -6.267  -5.685  1.00 18.36 ?  76  LYS   A HB2  1 
ATOM   1619 H HB3  . LYS   A 1 76  ? 33.652 -6.267  -7.260  1.00 18.36 ?  76  LYS   A HB3  1 
ATOM   1620 H HG2  . LYS   A 1 76  ? 35.815 -5.622  -7.573  1.00 19.65 ?  76  LYS   A HG2  1 
ATOM   1621 H HG3  . LYS   A 1 76  ? 36.013 -5.371  -6.016  1.00 19.65 ?  76  LYS   A HG3  1 
ATOM   1622 H HD2  . LYS   A 1 76  ? 35.859 -7.669  -5.629  1.00 21.41 ?  76  LYS   A HD2  1 
ATOM   1623 H HD3  . LYS   A 1 76  ? 35.678 -7.916  -7.193  1.00 21.41 ?  76  LYS   A HD3  1 
ATOM   1624 H HE2  . LYS   A 1 76  ? 37.822 -7.103  -7.576  1.00 24.46 ?  76  LYS   A HE2  1 
ATOM   1625 H HE3  . LYS   A 1 76  ? 38.003 -6.827  -6.020  1.00 24.46 ?  76  LYS   A HE3  1 
ATOM   1626 H HZ1  . LYS   A 1 76  ? 39.013 -8.767  -6.607  1.00 25.68 ?  76  LYS   A HZ1  1 
ATOM   1627 H HZ2  . LYS   A 1 76  ? 37.935 -9.070  -5.687  1.00 25.68 ?  76  LYS   A HZ2  1 
ATOM   1628 H HZ3  . LYS   A 1 76  ? 37.770 -9.321  -7.104  1.00 25.68 ?  76  LYS   A HZ3  1 
ATOM   1629 N N    . VAL   A 1 77  ? 31.264 -4.425  -7.378  1.00 12.90 ?  77  VAL   A N    1 
ATOM   1630 C CA   . VAL   A 1 77  ? 29.854 -4.803  -7.300  1.00 13.07 ?  77  VAL   A CA   1 
ATOM   1631 C C    . VAL   A 1 77  ? 29.784 -6.258  -6.853  1.00 12.38 ?  77  VAL   A C    1 
ATOM   1632 O O    . VAL   A 1 77  ? 30.442 -7.130  -7.432  1.00 13.07 ?  77  VAL   A O    1 
ATOM   1633 C CB   . VAL   A 1 77  ? 29.144 -4.594  -8.645  1.00 14.12 ?  77  VAL   A CB   1 
ATOM   1634 C CG1  . VAL   A 1 77  ? 27.677 -5.016  -8.532  1.00 15.13 ?  77  VAL   A CG1  1 
ATOM   1635 C CG2  . VAL   A 1 77  ? 29.249 -3.147  -9.089  1.00 16.02 ?  77  VAL   A CG2  1 
ATOM   1636 H H    . VAL   A 1 77  ? 31.544 -4.182  -8.155  1.00 15.46 ?  77  VAL   A H    1 
ATOM   1637 H HA   . VAL   A 1 77  ? 29.414 -4.255  -6.631  1.00 15.66 ?  77  VAL   A HA   1 
ATOM   1638 H HB   . VAL   A 1 77  ? 29.570 -5.149  -9.316  1.00 16.92 ?  77  VAL   A HB   1 
ATOM   1639 H HG11 . VAL   A 1 77  ? 27.209 -4.723  -9.326  1.00 18.13 ?  77  VAL   A HG11 1 
ATOM   1640 H HG12 . VAL   A 1 77  ? 27.632 -5.982  -8.455  1.00 18.13 ?  77  VAL   A HG12 1 
ATOM   1641 H HG13 . VAL   A 1 77  ? 27.292 -4.601  -7.745  1.00 18.13 ?  77  VAL   A HG13 1 
ATOM   1642 H HG21 . VAL   A 1 77  ? 28.741 -3.036  -9.907  1.00 19.20 ?  77  VAL   A HG21 1 
ATOM   1643 H HG22 . VAL   A 1 77  ? 28.888 -2.579  -8.393  1.00 19.20 ?  77  VAL   A HG22 1 
ATOM   1644 H HG23 . VAL   A 1 77  ? 30.181 -2.932  -9.246  1.00 19.20 ?  77  VAL   A HG23 1 
ATOM   1645 N N    . GLY   A 1 78  ? 28.999 -6.525  -5.810  1.00 12.01 ?  78  GLY   A N    1 
ATOM   1646 C CA   . GLY   A 1 78  ? 28.970 -7.818  -5.164  1.00 12.32 ?  78  GLY   A CA   1 
ATOM   1647 C C    . GLY   A 1 78  ? 29.878 -7.916  -3.960  1.00 11.60 ?  78  GLY   A C    1 
ATOM   1648 O O    . GLY   A 1 78  ? 29.813 -8.925  -3.236  1.00 12.72 ?  78  GLY   A O    1 
ATOM   1649 H H    . GLY   A 1 78  ? 28.455 -5.949  -5.461  1.00 14.38 ?  78  GLY   A H    1 
ATOM   1650 H HA2  . GLY   A 1 78  ? 28.064 -8.010  -4.882  1.00 14.77 ?  78  GLY   A HA2  1 
ATOM   1651 H HA3  . GLY   A 1 78  ? 29.239 -8.495  -5.806  1.00 14.77 ?  78  GLY   A HA3  1 
ATOM   1652 N N    . GLY   A 1 79  ? 30.731 -6.909  -3.729  1.00 11.48 ?  79  GLY   A N    1 
ATOM   1653 C CA   . GLY   A 1 79  ? 31.689 -6.931  -2.646  1.00 11.88 ?  79  GLY   A CA   1 
ATOM   1654 C C    . GLY   A 1 79  ? 31.239 -6.130  -1.436  1.00 11.13 ?  79  GLY   A C    1 
ATOM   1655 O O    . GLY   A 1 79  ? 30.119 -5.618  -1.363  1.00 12.30 ?  79  GLY   A O    1 
ATOM   1656 H H    . GLY   A 1 79  ? 30.769 -6.189  -4.206  1.00 13.75 ?  79  GLY   A H    1 
ATOM   1657 H HA2  . GLY   A 1 79  ? 31.838 -7.854  -2.375  1.00 14.24 ?  79  GLY   A HA2  1 
ATOM   1658 H HA3  . GLY   A 1 79  ? 32.535 -6.572  -2.962  1.00 14.24 ?  79  GLY   A HA3  1 
ATOM   1659 N N    . SER   A 1 80  ? 32.139 -6.037  -0.459  1.00 12.08 ?  80  SER   A N    1 
ATOM   1660 C CA   . SER   A 1 80  ? 31.812 -5.405  0.808   1.00 11.03 ?  80  SER   A CA   1 
ATOM   1661 C C    . SER   A 1 80  ? 33.081 -4.954  1.515   1.00 11.15 ?  80  SER   A C    1 
ATOM   1662 O O    . SER   A 1 80  ? 34.191 -5.401  1.203   1.00 13.20 ?  80  SER   A O    1 
ATOM   1663 C CB   . SER   A 1 80  ? 31.048 -6.361  1.731   1.00 12.56 ?  80  SER   A CB   1 
ATOM   1664 O OG   . SER   A 1 80  ? 31.873 -7.420  2.194   1.00 14.67 ?  80  SER   A OG   1 
ATOM   1665 H H    . SER   A 1 80  ? 32.951 -6.326  -0.515  1.00 14.47 ?  80  SER   A H    1 
ATOM   1666 H HA   . SER   A 1 80  ? 31.261 -4.627  0.628   1.00 13.22 ?  80  SER   A HA   1 
ATOM   1667 H HB2  . SER   A 1 80  ? 30.724 -5.859  2.493   1.00 15.05 ?  80  SER   A HB2  1 
ATOM   1668 H HB3  . SER   A 1 80  ? 30.300 -6.734  1.239   1.00 15.05 ?  80  SER   A HB3  1 
ATOM   1669 H HG   . SER   A 1 80  ? 32.156 -7.867  1.541   1.00 17.58 ?  80  SER   A HG   1 
ATOM   1670 N N    . CYS   A 1 81  ? 32.892 -4.102  2.520   1.00 11.13 ?  81  CYS   A N    1 
ATOM   1671 C CA   . CYS   A 1 81  ? 33.931 -3.819  3.496   1.00 11.49 ?  81  CYS   A CA   1 
ATOM   1672 C C    . CYS   A 1 81  ? 33.278 -3.595  4.853   1.00 10.98 ?  81  CYS   A C    1 
ATOM   1673 O O    . CYS   A 1 81  ? 32.111 -3.198  4.939   1.00 12.52 ?  81  CYS   A O    1 
ATOM   1674 C CB   . CYS   A 1 81  ? 34.811 -2.624  3.091   1.00 12.10 ?  81  CYS   A CB   1 
ATOM   1675 S SG   . CYS   A 1 81  ? 33.915 -1.059  3.103   1.00 12.38 ?  81  CYS   A SG   1 
ATOM   1676 H H    . CYS   A 1 81  ? 32.156 -3.674  2.661   1.00 13.34 ?  81  CYS   A H    1 
ATOM   1677 H HA   . CYS   A 1 81  ? 34.509 -4.595  3.567   1.00 13.77 ?  81  CYS   A HA   1 
ATOM   1678 H HB2  . CYS   A 1 81  ? 35.554 -2.558  3.717   1.00 14.50 ?  81  CYS   A HB2  1 
ATOM   1679 H HB3  . CYS   A 1 81  ? 35.154 -2.772  2.194   1.00 14.50 ?  81  CYS   A HB3  1 
ATOM   1680 H HG   . CYS   A 1 81  ? 34.662 -0.172  2.788   1.00 14.84 ?  81  CYS   A HG   1 
ATOM   1681 N N    . VAL   A 1 82  ? 34.044 -3.848  5.909   1.00 11.19 ?  82  VAL   A N    1 
ATOM   1682 C CA   . VAL   A 1 82  ? 33.616 -3.605  7.278   1.00 12.12 ?  82  VAL   A CA   1 
ATOM   1683 C C    . VAL   A 1 82  ? 34.216 -2.291  7.755   1.00 12.34 ?  82  VAL   A C    1 
ATOM   1684 O O    . VAL   A 1 82  ? 35.442 -2.120  7.750   1.00 13.15 ?  82  VAL   A O    1 
ATOM   1685 C CB   . VAL   A 1 82  ? 34.035 -4.753  8.207   1.00 14.02 ?  82  VAL   A CB   1 
ATOM   1686 C CG1  . VAL   A 1 82  ? 33.594 -4.468  9.626   1.00 15.41 ?  82  VAL   A CG1  1 
ATOM   1687 C CG2  . VAL   A 1 82  ? 33.469 -6.079  7.728   1.00 14.92 ?  82  VAL   A CG2  1 
ATOM   1688 H H    . VAL   A 1 82  ? 34.841 -4.177  5.848   1.00 13.40 ?  82  VAL   A H    1 
ATOM   1689 H HA   . VAL   A 1 82  ? 32.647 -3.525  7.297   1.00 14.52 ?  82  VAL   A HA   1 
ATOM   1690 H HB   . VAL   A 1 82  ? 35.001 -4.818  8.202   1.00 16.80 ?  82  VAL   A HB   1 
ATOM   1691 H HG11 . VAL   A 1 82  ? 33.679 -5.278  10.147  1.00 18.47 ?  82  VAL   A HG11 1 
ATOM   1692 H HG12 . VAL   A 1 82  ? 34.155 -3.771  10.001  1.00 18.47 ?  82  VAL   A HG12 1 
ATOM   1693 H HG13 . VAL   A 1 82  ? 32.667 -4.177  9.615   1.00 18.47 ?  82  VAL   A HG13 1 
ATOM   1694 H HG21 . VAL   A 1 82  ? 33.719 -6.773  8.355   1.00 17.88 ?  82  VAL   A HG21 1 
ATOM   1695 H HG22 . VAL   A 1 82  ? 32.501 -6.010  7.680   1.00 17.88 ?  82  VAL   A HG22 1 
ATOM   1696 H HG23 . VAL   A 1 82  ? 33.828 -6.279  6.849   1.00 17.88 ?  82  VAL   A HG23 1 
ATOM   1697 N N    . LEU   A 1 83  ? 33.359 -1.369  8.184   1.00 12.14 ?  83  LEU   A N    1 
ATOM   1698 C CA   . LEU   A 1 83  ? 33.783 -0.107  8.773   1.00 11.84 ?  83  LEU   A CA   1 
ATOM   1699 C C    . LEU   A 1 83  ? 33.056 0.072   10.103  1.00 12.05 ?  83  LEU   A C    1 
ATOM   1700 O O    . LEU   A 1 83  ? 32.327 -0.815  10.557  1.00 12.83 ?  83  LEU   A O    1 
ATOM   1701 C CB   . LEU   A 1 83  ? 33.540 1.058   7.800   1.00 12.75 ?  83  LEU   A CB   1 
ATOM   1702 C CG   . LEU   A 1 83  ? 34.433 1.047   6.554   1.00 13.21 ?  83  LEU   A CG   1 
ATOM   1703 C CD1  . LEU   A 1 83  ? 34.029 2.115   5.552   1.00 13.66 ?  83  LEU   A CD1  1 
ATOM   1704 C CD2  . LEU   A 1 83  ? 35.911 1.230   6.936   1.00 14.24 ?  83  LEU   A CD2  1 
ATOM   1705 H H    . LEU   A 1 83  ? 32.504 -1.457  8.141   1.00 14.55 ?  83  LEU   A H    1 
ATOM   1706 H HA   . LEU   A 1 83  ? 34.733 -0.144  8.957   1.00 14.18 ?  83  LEU   A HA   1 
ATOM   1707 H HB2  . LEU   A 1 83  ? 32.620 1.028   7.495   1.00 15.27 ?  83  LEU   A HB2  1 
ATOM   1708 H HB3  . LEU   A 1 83  ? 33.700 1.895   8.263   1.00 15.27 ?  83  LEU   A HB3  1 
ATOM   1709 H HG   . LEU   A 1 83  ? 34.348 0.186   6.118   1.00 15.83 ?  83  LEU   A HG   1 
ATOM   1710 H HD11 . LEU   A 1 83  ? 34.621 2.061   4.780   1.00 16.36 ?  83  LEU   A HD11 1 
ATOM   1711 H HD12 . LEU   A 1 83  ? 33.116 1.962   5.278   1.00 16.36 ?  83  LEU   A HD12 1 
ATOM   1712 H HD13 . LEU   A 1 83  ? 34.115 2.987   5.967   1.00 16.36 ?  83  LEU   A HD13 1 
ATOM   1713 H HD21 . LEU   A 1 83  ? 36.431 1.384   6.130   1.00 17.06 ?  83  LEU   A HD21 1 
ATOM   1714 H HD22 . LEU   A 1 83  ? 35.994 1.990   7.532   1.00 17.06 ?  83  LEU   A HD22 1 
ATOM   1715 H HD23 . LEU   A 1 83  ? 36.227 0.426   7.381   1.00 17.06 ?  83  LEU   A HD23 1 
ATOM   1716 N N    . SER   A 1 84  ? 33.273 1.219   10.743  1.00 12.89 ?  84  SER   A N    1 
ATOM   1717 C CA   . SER   A 1 84  ? 32.614 1.487   12.012  1.00 12.82 ?  84  SER   A CA   1 
ATOM   1718 C C    . SER   A 1 84  ? 31.095 1.578   11.848  1.00 12.38 ?  84  SER   A C    1 
ATOM   1719 O O    . SER   A 1 84  ? 30.579 2.037   10.828  1.00 12.74 ?  84  SER   A O    1 
ATOM   1720 C CB   . SER   A 1 84  ? 33.106 2.813   12.584  1.00 13.75 ?  84  SER   A CB   1 
ATOM   1721 O OG   . SER   A 1 84  ? 32.481 3.073   13.822  1.00 14.90 ?  84  SER   A OG   1 
ATOM   1722 H H    . SER   A 1 84  ? 33.783 1.855   10.457  1.00 15.45 ?  84  SER   A H    1 
ATOM   1723 H HA   . SER   A 1 84  ? 32.824 0.779   12.637  1.00 15.36 ?  84  SER   A HA   1 
ATOM   1724 H HB2  . SER   A 1 84  ? 34.068 2.770   12.707  1.00 16.47 ?  84  SER   A HB2  1 
ATOM   1725 H HB3  . SER   A 1 84  ? 32.884 3.528   11.963  1.00 16.47 ?  84  SER   A HB3  1 
ATOM   1726 H HG   . SER   A 1 84  ? 32.762 3.803   14.137  1.00 17.85 ?  84  SER   A HG   1 
ATOM   1727 N N    . GLY   A 1 85  ? 30.376 1.179   12.894  1.00 13.55 ?  85  GLY   A N    1 
ATOM   1728 C CA   . GLY   A 1 85  ? 28.951 1.419   12.969  1.00 14.27 ?  85  GLY   A CA   1 
ATOM   1729 C C    . GLY   A 1 85  ? 28.581 2.737   13.613  1.00 13.92 ?  85  GLY   A C    1 
ATOM   1730 O O    . GLY   A 1 85  ? 27.392 3.057   13.718  1.00 14.67 ?  85  GLY   A O    1 
ATOM   1731 H H    . GLY   A 1 85  ? 30.700 0.771   13.576  1.00 16.24 ?  85  GLY   A H    1 
ATOM   1732 H HA2  . GLY   A 1 85  ? 28.582 1.405   12.072  1.00 17.10 ?  85  GLY   A HA2  1 
ATOM   1733 H HA3  . GLY   A 1 85  ? 28.540 0.706   13.476  1.00 17.10 ?  85  GLY   A HA3  1 
ATOM   1734 N N    . HIS   A 1 86  ? 29.564 3.503   14.071  1.00 13.62 ?  86  HIS   A N    1 
ATOM   1735 C CA   . HIS   A 1 86  ? 29.342 4.846   14.629  1.00 13.98 ?  86  HIS   A CA   1 
ATOM   1736 C C    . HIS   A 1 86  ? 28.349 4.736   15.781  1.00 14.95 ?  86  HIS   A C    1 
ATOM   1737 O O    . HIS   A 1 86  ? 28.519 3.855   16.639  1.00 16.45 ?  86  HIS   A O    1 
ATOM   1738 C CB   . HIS   A 1 86  ? 28.986 5.824   13.516  1.00 13.87 ?  86  HIS   A CB   1 
ATOM   1739 C CG   . HIS   A 1 86  ? 30.056 5.913   12.488  1.00 14.20 ?  86  HIS   A CG   1 
ATOM   1740 N ND1  . HIS   A 1 86  ? 31.147 6.743   12.630  1.00 15.41 ?  86  HIS   A ND1  1 
ATOM   1741 C CD2  . HIS   A 1 86  ? 30.249 5.221   11.343  1.00 13.89 ?  86  HIS   A CD2  1 
ATOM   1742 C CE1  . HIS   A 1 86  ? 31.953 6.573   11.598  1.00 15.19 ?  86  HIS   A CE1  1 
ATOM   1743 N NE2  . HIS   A 1 86  ? 31.437 5.650   10.808  1.00 14.39 ?  86  HIS   A NE2  1 
ATOM   1744 H H    . HIS   A 1 86  ? 30.384 3.272   14.076  1.00 16.32 ?  86  HIS   A H    1 
ATOM   1745 H HA   . HIS   A 1 86  ? 30.174 5.155   15.006  1.00 16.75 ?  86  HIS   A HA   1 
ATOM   1746 H HB2  . HIS   A 1 86  ? 28.167 5.537   13.078  1.00 16.62 ?  86  HIS   A HB2  1 
ATOM   1747 H HB3  . HIS   A 1 86  ? 28.860 6.714   13.893  1.00 16.62 ?  86  HIS   A HB3  1 
ATOM   1748 H HD2  . HIS   A 1 86  ? 29.688 4.566   10.986  1.00 16.65 ?  86  HIS   A HD2  1 
ATOM   1749 H HE1  . HIS   A 1 86  ? 32.751 7.026   11.446  1.00 18.20 ?  86  HIS   A HE1  1 
ATOM   1750 H HE2  . HIS   A 1 86  ? 31.783 5.371   10.064  1.00 17.25 ?  86  HIS   A HE2  1 
ATOM   1751 N N    . ASN   A 1 87  ? 27.335 5.592   15.845  1.00 16.15 ?  87  ASN   A N    1 
ATOM   1752 C CA   . ASN   A 1 87  ? 26.347 5.583   16.908  1.00 17.04 ?  87  ASN   A CA   1 
ATOM   1753 C C    . ASN   A 1 87  ? 25.213 4.602   16.656  1.00 18.30 ?  87  ASN   A C    1 
ATOM   1754 O O    . ASN   A 1 87  ? 24.269 4.564   17.450  1.00 20.85 ?  87  ASN   A O    1 
ATOM   1755 C CB   . ASN   A 1 87  ? 25.758 6.990   17.067  1.00 18.48 ?  87  ASN   A CB   1 
ATOM   1756 C CG   . ASN   A 1 87  ? 25.263 7.567   15.750  1.00 19.24 ?  87  ASN   A CG   1 
ATOM   1757 O OD1  . ASN   A 1 87  ? 25.916 7.437   14.717  1.00 19.48 ?  87  ASN   A OD1  1 
ATOM   1758 N ND2  . ASN   A 1 87  ? 24.101 8.196   15.779  1.00 20.48 ?  87  ASN   A ND2  1 
ATOM   1759 H H    . ASN   A 1 87  ? 27.192 6.205   15.260  1.00 19.36 ?  87  ASN   A H    1 
ATOM   1760 H HA   . ASN   A 1 87  ? 26.772 5.336   17.747  1.00 20.42 ?  87  ASN   A HA   1 
ATOM   1761 H HB2  . ASN   A 1 87  ? 25.005 6.949   17.684  1.00 22.15 ?  87  ASN   A HB2  1 
ATOM   1762 H HB3  . ASN   A 1 87  ? 26.441 7.578   17.418  1.00 22.15 ?  87  ASN   A HB3  1 
ATOM   1763 H HD21 . ASN   A 1 87  ? 23.782 8.532   15.057  1.00 24.56 ?  87  ASN   A HD21 1 
ATOM   1764 H HD22 . ASN   A 1 87  ? 23.671 8.272   16.519  1.00 24.56 ?  87  ASN   A HD22 1 
ATOM   1765 N N    A LEU   A 1 88  ? 25.283 3.813   15.586  0.58 17.25 ?  88  LEU   A N    1 
ATOM   1766 N N    B LEU   A 1 88  ? 25.280 3.803   15.592  0.42 17.46 ?  88  LEU   A N    1 
ATOM   1767 C CA   A LEU   A 1 88  ? 24.179 2.949   15.181  0.58 16.85 ?  88  LEU   A CA   1 
ATOM   1768 C CA   B LEU   A 1 88  ? 24.166 2.949   15.200  0.42 17.00 ?  88  LEU   A CA   1 
ATOM   1769 C C    A LEU   A 1 88  ? 24.396 1.477   15.503  0.58 16.61 ?  88  LEU   A C    1 
ATOM   1770 C C    B LEU   A 1 88  ? 24.394 1.466   15.450  0.42 16.59 ?  88  LEU   A C    1 
ATOM   1771 O O    A LEU   A 1 88  ? 23.419 0.754   15.728  0.58 17.43 ?  88  LEU   A O    1 
ATOM   1772 O O    B LEU   A 1 88  ? 23.415 0.721   15.566  0.42 17.07 ?  88  LEU   A O    1 
ATOM   1773 C CB   A LEU   A 1 88  ? 23.946 3.079   13.672  0.58 17.21 ?  88  LEU   A CB   1 
ATOM   1774 C CB   B LEU   A 1 88  ? 23.862 3.140   13.708  0.42 17.30 ?  88  LEU   A CB   1 
ATOM   1775 C CG   A LEU   A 1 88  ? 23.658 4.476   13.126  0.58 18.83 ?  88  LEU   A CG   1 
ATOM   1776 C CG   B LEU   A 1 88  ? 23.602 4.584   13.278  0.42 18.14 ?  88  LEU   A CG   1 
ATOM   1777 C CD1  A LEU   A 1 88  ? 23.518 4.410   11.617  0.58 19.20 ?  88  LEU   A CD1  1 
ATOM   1778 C CD1  B LEU   A 1 88  ? 23.458 4.672   11.769  0.42 18.18 ?  88  LEU   A CD1  1 
ATOM   1779 C CD2  A LEU   A 1 88  ? 22.407 5.060   13.761  0.58 20.30 ?  88  LEU   A CD2  1 
ATOM   1780 C CD2  B LEU   A 1 88  ? 22.368 5.135   13.971  0.42 19.02 ?  88  LEU   A CD2  1 
ATOM   1781 H H    A LEU   A 1 88  ? 25.973 3.760   15.076  0.58 20.67 ?  88  LEU   A H    1 
ATOM   1782 H H    B LEU   A 1 88  ? 25.968 3.738   15.084  0.42 20.93 ?  88  LEU   A H    1 
ATOM   1783 H HA   A LEU   A 1 88  ? 23.372 3.238   15.632  0.58 20.20 ?  88  LEU   A HA   1 
ATOM   1784 H HA   B LEU   A 1 88  ? 23.376 3.218   15.694  0.42 20.38 ?  88  LEU   A HA   1 
ATOM   1785 H HB2  A LEU   A 1 88  ? 24.734 2.755   13.214  0.58 20.63 ?  88  LEU   A HB2  1 
ATOM   1786 H HB2  B LEU   A 1 88  ? 24.616 2.813   13.196  0.42 20.74 ?  88  LEU   A HB2  1 
ATOM   1787 H HB3  A LEU   A 1 88  ? 23.186 2.525   13.437  0.58 20.63 ?  88  LEU   A HB3  1 
ATOM   1788 H HB3  B LEU   A 1 88  ? 23.071 2.623   13.489  0.42 20.74 ?  88  LEU   A HB3  1 
ATOM   1789 H HG   A LEU   A 1 88  ? 24.404 5.063   13.332  0.58 22.57 ?  88  LEU   A HG   1 
ATOM   1790 H HG   B LEU   A 1 88  ? 24.360 5.131   13.535  0.42 21.75 ?  88  LEU   A HG   1 
ATOM   1791 H HD11 A LEU   A 1 88  ? 23.345 5.301   11.274  0.58 23.01 ?  88  LEU   A HD11 1 
ATOM   1792 H HD11 B LEU   A 1 88  ? 23.297 5.596   11.521  0.42 21.79 ?  88  LEU   A HD11 1 
ATOM   1793 H HD12 A LEU   A 1 88  ? 24.342 4.064   11.238  0.58 23.01 ?  88  LEU   A HD12 1 
ATOM   1794 H HD12 B LEU   A 1 88  ? 24.276 4.356   11.354  0.42 21.79 ?  88  LEU   A HD12 1 
ATOM   1795 H HD13 A LEU   A 1 88  ? 22.779 3.822   11.395  0.58 23.01 ?  88  LEU   A HD13 1 
ATOM   1796 H HD13 B LEU   A 1 88  ? 22.711 4.120   11.490  0.42 21.79 ?  88  LEU   A HD13 1 
ATOM   1797 H HD21 A LEU   A 1 88  ? 22.202 5.907   13.335  0.58 24.34 ?  88  LEU   A HD21 1 
ATOM   1798 H HD21 B LEU   A 1 88  ? 22.164 6.006   13.598  0.42 22.80 ?  88  LEU   A HD21 1 
ATOM   1799 H HD22 A LEU   A 1 88  ? 21.673 4.440   13.634  0.58 24.34 ?  88  LEU   A HD22 1 
ATOM   1800 H HD22 B LEU   A 1 88  ? 21.628 4.528   13.821  0.42 22.80 ?  88  LEU   A HD22 1 
ATOM   1801 H HD23 A LEU   A 1 88  ? 22.569 5.195   14.707  0.58 24.34 ?  88  LEU   A HD23 1 
ATOM   1802 H HD23 B LEU   A 1 88  ? 22.549 5.212   14.919  0.42 22.80 ?  88  LEU   A HD23 1 
ATOM   1803 N N    . ALA   A 1 89  ? 25.644 1.022   15.521  1.00 15.76 ?  89  ALA   A N    1 
ATOM   1804 C CA   . ALA   A 1 89  ? 25.976 -0.390  15.639  1.00 15.53 ?  89  ALA   A CA   1 
ATOM   1805 C C    . ALA   A 1 89  ? 27.460 -0.461  15.959  1.00 15.88 ?  89  ALA   A C    1 
ATOM   1806 O O    . ALA   A 1 89  ? 28.177 0.534   15.851  1.00 16.97 ?  89  ALA   A O    1 
ATOM   1807 C CB   . ALA   A 1 89  ? 25.706 -1.109  14.319  1.00 14.89 ?  89  ALA   A CB   1 
ATOM   1808 H H    A ALA   A 1 89  ? 26.333 1.534   15.463  0.58 18.89 ?  89  ALA   A H    1 
ATOM   1809 H H    B ALA   A 1 89  ? 26.332 1.538   15.483  0.42 18.89 ?  89  ALA   A H    1 
ATOM   1810 H HA   . ALA   A 1 89  ? 25.461 -0.800  16.351  1.00 18.61 ?  89  ALA   A HA   1 
ATOM   1811 H HB1  . ALA   A 1 89  ? 25.953 -2.042  14.412  1.00 17.84 ?  89  ALA   A HB1  1 
ATOM   1812 H HB2  . ALA   A 1 89  ? 24.762 -1.037  14.102  1.00 17.84 ?  89  ALA   A HB2  1 
ATOM   1813 H HB3  . ALA   A 1 89  ? 26.237 -0.696  13.619  1.00 17.84 ?  89  ALA   A HB3  1 
ATOM   1814 N N    . LYS   A 1 90  ? 27.932 -1.643  16.344  1.00 16.02 ?  90  LYS   A N    1 
ATOM   1815 C CA   . LYS   A 1 90  ? 29.374 -1.800  16.498  1.00 17.21 ?  90  LYS   A CA   1 
ATOM   1816 C C    . LYS   A 1 90  ? 30.084 -1.621  15.158  1.00 15.80 ?  90  LYS   A C    1 
ATOM   1817 O O    . LYS   A 1 90  ? 31.019 -0.813  15.033  1.00 17.39 ?  90  LYS   A O    1 
ATOM   1818 C CB   . LYS   A 1 90  ? 29.703 -3.157  17.119  1.00 20.16 ?  90  LYS   A CB   1 
ATOM   1819 C CG   . LYS   A 1 90  ? 31.178 -3.313  17.461  1.00 25.25 ?  90  LYS   A CG   1 
ATOM   1820 C CD   . LYS   A 1 90  ? 31.427 -4.564  18.287  1.00 30.59 ?  90  LYS   A CD   1 
ATOM   1821 C CE   . LYS   A 1 90  ? 32.819 -4.566  18.906  1.00 34.71 ?  90  LYS   A CE   1 
ATOM   1822 N NZ   . LYS   A 1 90  ? 33.889 -4.894  17.925  1.00 37.20 ?  90  LYS   A NZ   1 
ATOM   1823 H H    . LYS   A 1 90  ? 27.454 -2.333  16.523  1.00 19.20 ?  90  LYS   A H    1 
ATOM   1824 H HA   . LYS   A 1 90  ? 29.699 -1.112  17.098  1.00 20.63 ?  90  LYS   A HA   1 
ATOM   1825 H HB2  . LYS   A 1 90  ? 29.190 -3.260  17.939  1.00 24.16 ?  90  LYS   A HB2  1 
ATOM   1826 H HB3  . LYS   A 1 90  ? 29.463 -3.858  16.493  1.00 24.16 ?  90  LYS   A HB3  1 
ATOM   1827 H HG2  . LYS   A 1 90  ? 31.692 -3.381  16.642  1.00 30.27 ?  90  LYS   A HG2  1 
ATOM   1828 H HG3  . LYS   A 1 90  ? 31.469 -2.544  17.978  1.00 30.27 ?  90  LYS   A HG3  1 
ATOM   1829 H HD2  . LYS   A 1 90  ? 30.776 -4.610  19.006  1.00 36.69 ?  90  LYS   A HD2  1 
ATOM   1830 H HD3  . LYS   A 1 90  ? 31.348 -5.346  17.717  1.00 36.69 ?  90  LYS   A HD3  1 
ATOM   1831 H HE2  . LYS   A 1 90  ? 33.005 -3.685  19.268  1.00 41.63 ?  90  LYS   A HE2  1 
ATOM   1832 H HE3  . LYS   A 1 90  ? 32.849 -5.228  19.615  1.00 41.63 ?  90  LYS   A HE3  1 
ATOM   1833 H HZ1  . LYS   A 1 90  ? 33.750 -5.705  17.583  1.00 44.62 ?  90  LYS   A HZ1  1 
ATOM   1834 H HZ2  . LYS   A 1 90  ? 33.891 -4.298  17.265  1.00 44.62 ?  90  LYS   A HZ2  1 
ATOM   1835 H HZ3  . LYS   A 1 90  ? 34.684 -4.884  18.327  1.00 44.62 ?  90  LYS   A HZ3  1 
ATOM   1836 N N    . HIS   A 1 91  ? 29.623 -2.343  14.136  1.00 14.00 ?  91  HIS   A N    1 
ATOM   1837 C CA   . HIS   A 1 91  ? 30.205 -2.324  12.809  1.00 13.28 ?  91  HIS   A CA   1 
ATOM   1838 C C    . HIS   A 1 91  ? 29.131 -2.049  11.774  1.00 12.22 ?  91  HIS   A C    1 
ATOM   1839 O O    . HIS   A 1 91  ? 27.964 -2.411  11.956  1.00 13.14 ?  91  HIS   A O    1 
ATOM   1840 C CB   . HIS   A 1 91  ? 30.810 -3.684  12.448  1.00 15.79 ?  91  HIS   A CB   1 
ATOM   1841 C CG   . HIS   A 1 91  ? 31.812 -4.183  13.437  1.00 20.27 ?  91  HIS   A CG   1 
ATOM   1842 N ND1  . HIS   A 1 91  ? 33.084 -3.665  13.531  1.00 22.52 ?  91  HIS   A ND1  1 
ATOM   1843 C CD2  . HIS   A 1 91  ? 31.734 -5.161  14.371  1.00 22.25 ?  91  HIS   A CD2  1 
ATOM   1844 C CE1  . HIS   A 1 91  ? 33.749 -4.300  14.480  1.00 23.46 ?  91  HIS   A CE1  1 
ATOM   1845 N NE2  . HIS   A 1 91  ? 32.951 -5.214  15.006  1.00 23.64 ?  91  HIS   A NE2  1 
ATOM   1846 H H    . HIS   A 1 91  ? 28.943 -2.882  14.201  1.00 16.77 ?  91  HIS   A H    1 
ATOM   1847 H HA   . HIS   A 1 91  ? 30.889 -1.647  12.751  1.00 15.91 ?  91  HIS   A HA   1 
ATOM   1848 H HB2  . HIS   A 1 91  ? 30.099 -4.344  12.394  1.00 18.92 ?  91  HIS   A HB2  1 
ATOM   1849 H HB3  . HIS   A 1 91  ? 31.253 -3.613  11.588  1.00 18.92 ?  91  HIS   A HB3  1 
ATOM   1850 H HD1  . HIS   A 1 91  ? 33.400 -3.029  13.041  1.00 27.00 ?  91  HIS   A HD1  1 
ATOM   1851 H HD2  . HIS   A 1 91  ? 31.001 -5.697  14.552  1.00 26.67 ?  91  HIS   A HD2  1 
ATOM   1852 H HE1  . HIS   A 1 91  ? 34.631 -4.127  14.733  1.00 28.13 ?  91  HIS   A HE1  1 
ATOM   1853 N N    . CYS   A 1 92  ? 29.544 -1.457  10.664  1.00 11.87 ?  92  CYS   A N    1 
ATOM   1854 C CA   . CYS   A 1 92  ? 28.719 -1.387  9.469   1.00 11.66 ?  92  CYS   A CA   1 
ATOM   1855 C C    . CYS   A 1 92  ? 29.374 -2.200  8.361   1.00 11.28 ?  92  CYS   A C    1 
ATOM   1856 O O    . CYS   A 1 92  ? 30.533 -1.949  7.995   1.00 12.14 ?  92  CYS   A O    1 
ATOM   1857 C CB   . CYS   A 1 92  ? 28.519 0.056   9.006   1.00 12.23 ?  92  CYS   A CB   1 
ATOM   1858 S SG   . CYS   A 1 92  ? 27.501 0.171   7.491   1.00 11.86 ?  92  CYS   A SG   1 
ATOM   1859 H H    . CYS   A 1 92  ? 30.315 -1.078  10.580  1.00 14.22 ?  92  CYS   A H    1 
ATOM   1860 H HA   . CYS   A 1 92  ? 27.851 -1.766  9.656   1.00 13.97 ?  92  CYS   A HA   1 
ATOM   1861 H HB2  . CYS   A 1 92  ? 28.069 0.559   9.704   1.00 14.65 ?  92  CYS   A HB2  1 
ATOM   1862 H HB3  . CYS   A 1 92  ? 29.382 0.456   8.814   1.00 14.65 ?  92  CYS   A HB3  1 
ATOM   1863 H HG   . CYS   A 1 92  ? 27.373 1.328   7.194   1.00 14.20 ?  92  CYS   A HG   1 
ATOM   1864 N N    . LEU   A 1 93  ? 28.638 -3.178  7.848   1.00 11.10 ?  93  LEU   A N    1 
ATOM   1865 C CA   . LEU   A 1 93  ? 29.046 -3.937  6.674   1.00 10.73 ?  93  LEU   A CA   1 
ATOM   1866 C C    . LEU   A 1 93  ? 28.459 -3.252  5.445   1.00 10.53 ?  93  LEU   A C    1 
ATOM   1867 O O    . LEU   A 1 93  ? 27.245 -3.308  5.215   1.00 10.43 ?  93  LEU   A O    1 
ATOM   1868 C CB   . LEU   A 1 93  ? 28.570 -5.387  6.785   1.00 11.38 ?  93  LEU   A CB   1 
ATOM   1869 C CG   . LEU   A 1 93  ? 28.959 -6.295  5.613   1.00 11.84 ?  93  LEU   A CG   1 
ATOM   1870 C CD1  . LEU   A 1 93  ? 30.464 -6.556  5.590   1.00 12.94 ?  93  LEU   A CD1  1 
ATOM   1871 C CD2  . LEU   A 1 93  ? 28.186 -7.623  5.640   1.00 12.61 ?  93  LEU   A CD2  1 
ATOM   1872 H H    . LEU   A 1 93  ? 27.877 -3.421  8.175   1.00 13.30 ?  93  LEU   A H    1 
ATOM   1873 H HA   . LEU   A 1 93  ? 30.008 -3.929  6.605   1.00 12.85 ?  93  LEU   A HA   1 
ATOM   1874 H HB2  . LEU   A 1 93  ? 28.950 -5.772  7.595   1.00 13.63 ?  93  LEU   A HB2  1 
ATOM   1875 H HB3  . LEU   A 1 93  ? 27.603 -5.393  6.852   1.00 13.63 ?  93  LEU   A HB3  1 
ATOM   1876 H HG   . LEU   A 1 93  ? 28.734 -5.845  4.790   1.00 14.19 ?  93  LEU   A HG   1 
ATOM   1877 H HD11 . LEU   A 1 93  ? 30.671 -7.158  4.862   1.00 15.51 ?  93  LEU   A HD11 1 
ATOM   1878 H HD12 . LEU   A 1 93  ? 30.931 -5.713  5.468   1.00 15.51 ?  93  LEU   A HD12 1 
ATOM   1879 H HD13 . LEU   A 1 93  ? 30.731 -6.956  6.437   1.00 15.51 ?  93  LEU   A HD13 1 
ATOM   1880 H HD21 . LEU   A 1 93  ? 28.465 -8.166  4.883   1.00 15.11 ?  93  LEU   A HD21 1 
ATOM   1881 H HD22 . LEU   A 1 93  ? 28.381 -8.092  6.467   1.00 15.11 ?  93  LEU   A HD22 1 
ATOM   1882 H HD23 . LEU   A 1 93  ? 27.236 -7.440  5.580   1.00 15.11 ?  93  LEU   A HD23 1 
ATOM   1883 N N    . HIS   A 1 94  ? 29.310 -2.560  4.684   1.00 10.30 ?  94  HIS   A N    1 
ATOM   1884 C CA   . HIS   A 1 94  ? 28.890 -1.884  3.460   1.00 10.26 ?  94  HIS   A CA   1 
ATOM   1885 C C    . HIS   A 1 94  ? 28.901 -2.920  2.352   1.00 10.42 ?  94  HIS   A C    1 
ATOM   1886 O O    . HIS   A 1 94  ? 29.964 -3.452  2.025   1.00 11.73 ?  94  HIS   A O    1 
ATOM   1887 C CB   . HIS   A 1 94  ? 29.854 -0.740  3.136   1.00 10.62 ?  94  HIS   A CB   1 
ATOM   1888 C CG   . HIS   A 1 94  ? 29.841 0.351   4.154   1.00 10.11 ?  94  HIS   A CG   1 
ATOM   1889 N ND1  . HIS   A 1 94  ? 28.963 1.413   4.098   1.00 10.60 ?  94  HIS   A ND1  1 
ATOM   1890 C CD2  . HIS   A 1 94  ? 30.569 0.516   5.280   1.00 10.97 ?  94  HIS   A CD2  1 
ATOM   1891 C CE1  . HIS   A 1 94  ? 29.176 2.197   5.140   1.00 10.81 ?  94  HIS   A CE1  1 
ATOM   1892 N NE2  . HIS   A 1 94  ? 30.139 1.671   5.875   1.00 11.01 ?  94  HIS   A NE2  1 
ATOM   1893 H H    . HIS   A 1 94  ? 30.149 -2.468  4.859   1.00 12.34 ?  94  HIS   A H    1 
ATOM   1894 H HA   . HIS   A 1 94  ? 27.990 -1.532  3.560   1.00 12.28 ?  94  HIS   A HA   1 
ATOM   1895 H HB2  . HIS   A 1 94  ? 30.751 -1.089  3.086   1.00 12.73 ?  94  HIS   A HB2  1 
ATOM   1896 H HB3  . HIS   A 1 94  ? 29.598 -0.350  2.282   1.00 12.73 ?  94  HIS   A HB3  1 
ATOM   1897 H HD2  . HIS   A 1 94  ? 31.239 -0.039  5.590   1.00 13.14 ?  94  HIS   A HD2  1 
ATOM   1898 H HE1  . HIS   A 1 94  ? 28.705 2.985   5.325   1.00 12.94 ?  94  HIS   A HE1  1 
ATOM   1899 H HE2  . HIS   A 1 94  ? 30.445 2.016   6.599   1.00 13.19 ?  94  HIS   A HE2  1 
ATOM   1900 N N    . VAL   A 1 95  ? 27.733 -3.240  1.796   1.00 9.89  ?  95  VAL   A N    1 
ATOM   1901 C CA   . VAL   A 1 95  ? 27.595 -4.274  0.772   1.00 10.10 ?  95  VAL   A CA   1 
ATOM   1902 C C    . VAL   A 1 95  ? 27.054 -3.636  -0.496  1.00 10.01 ?  95  VAL   A C    1 
ATOM   1903 O O    . VAL   A 1 95  ? 26.053 -2.908  -0.451  1.00 10.79 ?  95  VAL   A O    1 
ATOM   1904 C CB   . VAL   A 1 95  ? 26.669 -5.418  1.220   1.00 10.75 ?  95  VAL   A CB   1 
ATOM   1905 C CG1  . VAL   A 1 95  ? 26.548 -6.455  0.105   1.00 11.29 ?  95  VAL   A CG1  1 
ATOM   1906 C CG2  . VAL   A 1 95  ? 27.170 -6.038  2.501   1.00 10.90 ?  95  VAL   A CG2  1 
ATOM   1907 H H    . VAL   A 1 95  ? 26.986 -2.868  2.001   1.00 11.84 ?  95  VAL   A H    1 
ATOM   1908 H HA   . VAL   A 1 95  ? 28.465 -4.650  0.572   1.00 12.10 ?  95  VAL   A HA   1 
ATOM   1909 H HB   . VAL   A 1 95  ? 25.786 -5.064  1.388   1.00 12.87 ?  95  VAL   A HB   1 
ATOM   1910 H HG11 . VAL   A 1 95  ? 26.167 -7.273  0.468   1.00 13.52 ?  95  VAL   A HG11 1 
ATOM   1911 H HG12 . VAL   A 1 95  ? 25.970 -6.111  -0.596  1.00 13.52 ?  95  VAL   A HG12 1 
ATOM   1912 H HG13 . VAL   A 1 95  ? 27.430 -6.643  -0.258  1.00 13.52 ?  95  VAL   A HG13 1 
ATOM   1913 H HG21 . VAL   A 1 95  ? 26.609 -6.803  2.722   1.00 13.05 ?  95  VAL   A HG21 1 
ATOM   1914 H HG22 . VAL   A 1 95  ? 28.087 -6.333  2.374   1.00 13.05 ?  95  VAL   A HG22 1 
ATOM   1915 H HG23 . VAL   A 1 95  ? 27.126 -5.381  3.208   1.00 13.05 ?  95  VAL   A HG23 1 
ATOM   1916 N N    . VAL   A 1 96  ? 27.687 -3.935  -1.629  1.00 10.09 ?  96  VAL   A N    1 
ATOM   1917 C CA   . VAL   A 1 96  ? 27.284 -3.386  -2.916  1.00 10.73 ?  96  VAL   A CA   1 
ATOM   1918 C C    . VAL   A 1 96  ? 26.491 -4.436  -3.687  1.00 11.28 ?  96  VAL   A C    1 
ATOM   1919 O O    . VAL   A 1 96  ? 27.061 -5.386  -4.233  1.00 12.35 ?  96  VAL   A O    1 
ATOM   1920 C CB   . VAL   A 1 96  ? 28.485 -2.907  -3.735  1.00 11.11 ?  96  VAL   A CB   1 
ATOM   1921 C CG1  . VAL   A 1 96  ? 27.990 -2.272  -5.017  1.00 11.67 ?  96  VAL   A CG1  1 
ATOM   1922 C CG2  . VAL   A 1 96  ? 29.334 -1.935  -2.937  1.00 11.55 ?  96  VAL   A CG2  1 
ATOM   1923 H H    . VAL   A 1 96  ? 28.373 -4.461  -1.674  1.00 12.08 ?  96  VAL   A H    1 
ATOM   1924 H HA   . VAL   A 1 96  ? 26.704 -2.627  -2.763  1.00 12.85 ?  96  VAL   A HA   1 
ATOM   1925 H HB   . VAL   A 1 96  ? 29.037 -3.664  -3.968  1.00 13.31 ?  96  VAL   A HB   1 
ATOM   1926 H HG11 . VAL   A 1 96  ? 28.726 -1.790  -5.430  1.00 13.98 ?  96  VAL   A HG11 1 
ATOM   1927 H HG12 . VAL   A 1 96  ? 27.676 -2.966  -5.615  1.00 13.98 ?  96  VAL   A HG12 1 
ATOM   1928 H HG13 . VAL   A 1 96  ? 27.270 -1.657  -4.810  1.00 13.98 ?  96  VAL   A HG13 1 
ATOM   1929 H HG21 . VAL   A 1 96  ? 30.037 -1.585  -3.501  1.00 13.84 ?  96  VAL   A HG21 1 
ATOM   1930 H HG22 . VAL   A 1 96  ? 28.769 -1.203  -2.624  1.00 13.84 ?  96  VAL   A HG22 1 
ATOM   1931 H HG23 . VAL   A 1 96  ? 29.716 -2.397  -2.174  1.00 13.84 ?  96  VAL   A HG23 1 
ATOM   1932 N N    A GLY   A 1 97  ? 25.171 -4.281  -3.697  0.58 11.46 ?  97  GLY   A N    1 
ATOM   1933 N N    B GLY   A 1 97  ? 25.176 -4.257  -3.784  0.42 11.37 ?  97  GLY   A N    1 
ATOM   1934 C CA   A GLY   A 1 97  ? 24.336 -5.009  -4.613  0.58 12.18 ?  97  GLY   A CA   1 
ATOM   1935 C CA   B GLY   A 1 97  ? 24.384 -5.056  -4.688  0.42 11.72 ?  97  GLY   A CA   1 
ATOM   1936 C C    A GLY   A 1 97  ? 24.309 -4.311  -5.956  0.58 11.91 ?  97  GLY   A C    1 
ATOM   1937 C C    B GLY   A 1 97  ? 24.464 -4.521  -6.106  0.42 12.26 ?  97  GLY   A C    1 
ATOM   1938 O O    A GLY   A 1 97  ? 24.566 -3.108  -6.058  0.58 11.96 ?  97  GLY   A O    1 
ATOM   1939 O O    B GLY   A 1 97  ? 24.863 -3.374  -6.332  0.42 12.73 ?  97  GLY   A O    1 
ATOM   1940 H H    A GLY   A 1 97  ? 24.738 -3.749  -3.170  0.58 13.73 ?  97  GLY   A H    1 
ATOM   1941 H H    B GLY   A 1 97  ? 24.722 -3.677  -3.332  0.42 13.62 ?  97  GLY   A H    1 
ATOM   1942 H HA2  A GLY   A 1 97  ? 24.687 -5.902  -4.725  0.58 14.59 ?  97  GLY   A HA2  1 
ATOM   1943 H HA2  B GLY   A 1 97  ? 24.710 -5.969  -4.678  0.42 14.04 ?  97  GLY   A HA2  1 
ATOM   1944 H HA3  A GLY   A 1 97  ? 23.431 -5.065  -4.261  0.58 14.59 ?  97  GLY   A HA3  1 
ATOM   1945 H HA3  B GLY   A 1 97  ? 23.456 -5.054  -4.404  0.42 14.04 ?  97  GLY   A HA3  1 
ATOM   1946 N N    A PRO   A 1 98  ? 24.002 -5.051  -7.017  0.58 11.54 ?  98  PRO   A N    1 
ATOM   1947 N N    B PRO   A 1 98  ? 24.098 -5.339  -7.093  0.42 13.01 ?  98  PRO   A N    1 
ATOM   1948 C CA   A PRO   A 1 98  ? 23.890 -4.425  -8.337  0.58 11.98 ?  98  PRO   A CA   1 
ATOM   1949 C CA   B PRO   A 1 98  ? 24.110 -4.863  -8.481  0.42 14.15 ?  98  PRO   A CA   1 
ATOM   1950 C C    A PRO   A 1 98  ? 22.773 -3.394  -8.369  0.58 11.80 ?  98  PRO   A C    1 
ATOM   1951 C C    B PRO   A 1 98  ? 23.038 -3.815  -8.737  0.42 14.67 ?  98  PRO   A C    1 
ATOM   1952 O O    A PRO   A 1 98  ? 21.702 -3.588  -7.788  0.58 11.46 ?  98  PRO   A O    1 
ATOM   1953 O O    B PRO   A 1 98  ? 21.917 -3.895  -8.227  0.42 14.90 ?  98  PRO   A O    1 
ATOM   1954 C CB   A PRO   A 1 98  ? 23.583 -5.608  -9.261  0.58 12.39 ?  98  PRO   A CB   1 
ATOM   1955 C CB   B PRO   A 1 98  ? 23.853 -6.135  -9.299  0.42 14.07 ?  98  PRO   A CB   1 
ATOM   1956 C CG   A PRO   A 1 98  ? 22.959 -6.628  -8.370  0.58 12.22 ?  98  PRO   A CG   1 
ATOM   1957 C CG   B PRO   A 1 98  ? 23.168 -7.066  -8.351  0.42 14.13 ?  98  PRO   A CG   1 
ATOM   1958 C CD   A PRO   A 1 98  ? 23.693 -6.489  -7.060  0.58 11.57 ?  98  PRO   A CD   1 
ATOM   1959 C CD   B PRO   A 1 98  ? 23.769 -6.771  -7.003  0.42 13.25 ?  98  PRO   A CD   1 
ATOM   1960 H HA   A PRO   A 1 98  ? 24.727 -4.012  -8.587  0.58 14.35 ?  98  PRO   A HA   1 
ATOM   1961 H HA   B PRO   A 1 98  ? 24.980 -4.500  -8.712  0.42 16.95 ?  98  PRO   A HA   1 
ATOM   1962 H HB2  A PRO   A 1 98  ? 22.962 -5.331  -9.948  0.58 14.85 ?  98  PRO   A HB2  1 
ATOM   1963 H HB2  B PRO   A 1 98  ? 23.281 -5.930  -10.054 0.42 16.87 ?  98  PRO   A HB2  1 
ATOM   1964 H HB3  A PRO   A 1 98  ? 24.405 -5.943  -9.642  0.58 14.85 ?  98  PRO   A HB3  1 
ATOM   1965 H HB3  B PRO   A 1 98  ? 24.697 -6.509  -9.599  0.42 16.87 ?  98  PRO   A HB3  1 
ATOM   1966 H HG2  A PRO   A 1 98  ? 22.016 -6.435  -8.251  0.58 14.64 ?  98  PRO   A HG2  1 
ATOM   1967 H HG2  B PRO   A 1 98  ? 22.214 -6.884  -8.347  0.42 16.93 ?  98  PRO   A HG2  1 
ATOM   1968 H HG3  A PRO   A 1 98  ? 23.089 -7.514  -8.737  0.58 14.64 ?  98  PRO   A HG3  1 
ATOM   1969 H HG3  B PRO   A 1 98  ? 23.340 -7.984  -8.612  0.42 16.93 ?  98  PRO   A HG3  1 
ATOM   1970 H HD2  A PRO   A 1 98  ? 23.123 -6.742  -6.312  0.58 13.86 ?  98  PRO   A HD2  1 
ATOM   1971 H HD2  B PRO   A 1 98  ? 23.121 -6.927  -6.298  0.42 15.88 ?  98  PRO   A HD2  1 
ATOM   1972 H HD3  A PRO   A 1 98  ? 24.518 -7.002  -7.064  0.58 13.86 ?  98  PRO   A HD3  1 
ATOM   1973 H HD3  B PRO   A 1 98  ? 24.575 -7.298  -6.867  0.42 15.88 ?  98  PRO   A HD3  1 
ATOM   1974 N N    A ASN   A 1 99  ? 23.046 -2.280  -9.044  0.58 12.47 ?  99  ASN   A N    1 
ATOM   1975 N N    B ASN   A 1 99  ? 23.400 -2.825  -9.546  0.42 15.84 ?  99  ASN   A N    1 
ATOM   1976 C CA   A ASN   A 1 99  ? 22.066 -1.228  -9.279  0.58 12.85 ?  99  ASN   A CA   1 
ATOM   1977 C CA   B ASN   A 1 99  ? 22.486 -1.781  -9.998  0.42 18.17 ?  99  ASN   A CA   1 
ATOM   1978 C C    A ASN   A 1 99  ? 21.512 -1.404  -10.688 0.58 14.11 ?  99  ASN   A C    1 
ATOM   1979 C C    B ASN   A 1 99  ? 21.943 -2.233  -11.348 0.42 19.33 ?  99  ASN   A C    1 
ATOM   1980 O O    A ASN   A 1 99  ? 22.201 -1.123  -11.675 0.58 15.55 ?  99  ASN   A O    1 
ATOM   1981 O O    B ASN   A 1 99  ? 22.575 -2.025  -12.386 0.42 18.49 ?  99  ASN   A O    1 
ATOM   1982 C CB   A ASN   A 1 99  ? 22.714 0.145   -9.112  0.58 13.52 ?  99  ASN   A CB   1 
ATOM   1983 C CB   B ASN   A 1 99  ? 23.243 -0.463  -10.132 0.42 19.46 ?  99  ASN   A CB   1 
ATOM   1984 C CG   A ASN   A 1 99  ? 21.694 1.280   -9.089  0.58 14.38 ?  99  ASN   A CG   1 
ATOM   1985 C CG   B ASN   A 1 99  ? 22.333 0.730   -10.405 0.42 20.67 ?  99  ASN   A CG   1 
ATOM   1986 O OD1  A ASN   A 1 99  ? 20.686 1.238   -9.795  0.58 14.98 ?  99  ASN   A OD1  1 
ATOM   1987 O OD1  B ASN   A 1 99  ? 22.761 1.878   -10.282 0.42 22.61 ?  99  ASN   A OD1  1 
ATOM   1988 N ND2  A ASN   A 1 99  ? 21.957 2.297   -8.276  0.58 14.86 ?  99  ASN   A ND2  1 
ATOM   1989 N ND2  B ASN   A 1 99  ? 21.085 0.472   -10.774 0.42 19.95 ?  99  ASN   A ND2  1 
ATOM   1990 H H    A ASN   A 1 99  ? 23.821 -2.105  -9.364  0.58 14.94 ?  99  ASN   A H    1 
ATOM   1991 H H    B ASN   A 1 99  ? 24.193 -2.734  -9.857  0.42 18.98 ?  99  ASN   A H    1 
ATOM   1992 H HA   A ASN   A 1 99  ? 21.337 -1.309  -8.639  0.58 15.39 ?  99  ASN   A HA   1 
ATOM   1993 H HA   B ASN   A 1 99  ? 21.751 -1.668  -9.372  0.42 21.78 ?  99  ASN   A HA   1 
ATOM   1994 H HB2  A ASN   A 1 99  ? 23.208 0.166   -8.278  0.58 16.20 ?  99  ASN   A HB2  1 
ATOM   1995 H HB2  B ASN   A 1 99  ? 23.718 -0.289  -9.308  0.42 23.33 ?  99  ASN   A HB2  1 
ATOM   1996 H HB3  A ASN   A 1 99  ? 23.317 0.298   -9.858  0.58 16.20 ?  99  ASN   A HB3  1 
ATOM   1997 H HB3  B ASN   A 1 99  ? 23.878 -0.543  -10.866 0.42 23.33 ?  99  ASN   A HB3  1 
ATOM   1998 H HD21 A ASN   A 1 99  ? 21.410 2.957   -8.226  0.58 17.80 ?  99  ASN   A HD21 1 
ATOM   1999 H HD21 B ASN   A 1 99  ? 20.555 1.123   -10.931 0.42 23.92 ?  99  ASN   A HD21 1 
ATOM   2000 H HD22 A ASN   A 1 99  ? 22.671 2.291   -7.796  0.58 17.80 ?  99  ASN   A HD22 1 
ATOM   2001 H HD22 B ASN   A 1 99  ? 20.792 -0.331  -10.841 0.42 23.92 ?  99  ASN   A HD22 1 
ATOM   2002 N N    A VAL   A 1 100 ? 20.262 -1.869  -10.774 0.58 15.04 ?  100 VAL   A N    1 
ATOM   2003 N N    B VAL   A 1 100 ? 20.754 -2.843  -11.337 0.42 21.72 ?  100 VAL   A N    1 
ATOM   2004 C CA   A VAL   A 1 100 ? 19.632 -2.107  -12.069 0.58 17.19 ?  100 VAL   A CA   1 
ATOM   2005 C CA   B VAL   A 1 100 ? 20.186 -3.383  -12.569 0.42 24.26 ?  100 VAL   A CA   1 
ATOM   2006 C C    A VAL   A 1 100 ? 19.524 -0.813  -12.861 0.58 17.88 ?  100 VAL   A C    1 
ATOM   2007 C C    B VAL   A 1 100 ? 19.880 -2.274  -13.568 0.42 26.21 ?  100 VAL   A C    1 
ATOM   2008 O O    A VAL   A 1 100 ? 19.601 -0.825  -14.094 0.58 19.20 ?  100 VAL   A O    1 
ATOM   2009 O O    B VAL   A 1 100 ? 19.848 -2.513  -14.782 0.42 26.49 ?  100 VAL   A O    1 
ATOM   2010 C CB   A VAL   A 1 100 ? 18.264 -2.801  -11.884 0.58 18.31 ?  100 VAL   A CB   1 
ATOM   2011 C CB   B VAL   A 1 100 ? 18.945 -4.242  -12.255 0.42 24.94 ?  100 VAL   A CB   1 
ATOM   2012 C CG1  A VAL   A 1 100 ? 17.575 -3.019  -13.228 0.58 18.92 ?  100 VAL   A CG1  1 
ATOM   2013 C CG1  B VAL   A 1 100 ? 18.395 -4.873  -13.526 0.42 25.28 ?  100 VAL   A CG1  1 
ATOM   2014 C CG2  A VAL   A 1 100 ? 18.440 -4.128  -11.159 0.58 19.06 ?  100 VAL   A CG2  1 
ATOM   2015 C CG2  B VAL   A 1 100 ? 19.293 -5.312  -11.238 0.42 25.27 ?  100 VAL   A CG2  1 
ATOM   2016 H H    A VAL   A 1 100 ? 19.755 -2.046  -10.096 0.58 18.03 ?  100 VAL   A H    1 
ATOM   2017 H H    B VAL   A 1 100 ? 20.265 -2.959  -10.636 0.42 26.04 ?  100 VAL   A H    1 
ATOM   2018 H HA   A VAL   A 1 100 ? 20.192 -2.710  -12.576 0.58 20.61 ?  100 VAL   A HA   1 
ATOM   2019 H HA   B VAL   A 1 100 ? 20.844 -3.968  -12.974 0.42 29.08 ?  100 VAL   A HA   1 
ATOM   2020 H HB   A VAL   A 1 100 ? 17.689 -2.238  -11.344 0.58 21.95 ?  100 VAL   A HB   1 
ATOM   2021 H HB   B VAL   A 1 100 ? 18.253 -3.677  -11.878 0.42 29.90 ?  100 VAL   A HB   1 
ATOM   2022 H HG11 A VAL   A 1 100 ? 16.811 -3.604  -13.102 0.58 22.68 ?  100 VAL   A HG11 1 
ATOM   2023 H HG11 B VAL   A 1 100 ? 17.712 -5.520  -13.287 0.42 30.31 ?  100 VAL   A HG11 1 
ATOM   2024 H HG12 A VAL   A 1 100 ? 17.280 -2.164  -13.579 0.58 22.68 ?  100 VAL   A HG12 1 
ATOM   2025 H HG12 B VAL   A 1 100 ? 18.011 -4.182  -14.086 0.42 30.31 ?  100 VAL   A HG12 1 
ATOM   2026 H HG13 A VAL   A 1 100 ? 18.205 -3.430  -13.843 0.58 22.68 ?  100 VAL   A HG13 1 
ATOM   2027 H HG13 B VAL   A 1 100 ? 19.117 -5.320  -13.995 0.42 30.31 ?  100 VAL   A HG13 1 
ATOM   2028 H HG21 A VAL   A 1 100 ? 17.582 -4.582  -11.117 0.58 22.85 ?  100 VAL   A HG21 1 
ATOM   2029 H HG21 B VAL   A 1 100 ? 18.527 -5.894  -11.124 0.42 30.30 ?  100 VAL   A HG21 1 
ATOM   2030 H HG22 A VAL   A 1 100 ? 19.078 -4.673  -11.646 0.58 22.85 ?  100 VAL   A HG22 1 
ATOM   2031 H HG22 B VAL   A 1 100 ? 20.052 -5.822  -11.564 0.42 30.30 ?  100 VAL   A HG22 1 
ATOM   2032 H HG23 A VAL   A 1 100 ? 18.767 -3.958  -10.262 0.58 22.85 ?  100 VAL   A HG23 1 
ATOM   2033 H HG23 B VAL   A 1 100 ? 19.516 -4.890  -10.395 0.42 30.30 ?  100 VAL   A HG23 1 
ATOM   2034 N N    A ASN   A 1 101 ? 19.340 0.317   -12.179 0.58 18.40 ?  101 ASN   A N    1 
ATOM   2035 N N    B ASN   A 1 101 ? 19.642 -1.056  -13.088 0.42 27.19 ?  101 ASN   A N    1 
ATOM   2036 C CA   A ASN   A 1 101 ? 19.277 1.600   -12.869 0.58 19.61 ?  101 ASN   A CA   1 
ATOM   2037 C CA   B ASN   A 1 101 ? 19.441 0.068   -13.993 0.42 28.02 ?  101 ASN   A CA   1 
ATOM   2038 C C    A ASN   A 1 101 ? 20.633 2.048   -13.411 0.58 21.35 ?  101 ASN   A C    1 
ATOM   2039 C C    B ASN   A 1 101 ? 20.743 0.573   -14.603 0.42 28.57 ?  101 ASN   A C    1 
ATOM   2040 O O    A ASN   A 1 101 ? 20.698 3.102   -14.057 0.58 22.73 ?  101 ASN   A O    1 
ATOM   2041 O O    B ASN   A 1 101 ? 20.698 1.413   -15.509 0.42 29.09 ?  101 ASN   A O    1 
ATOM   2042 C CB   A ASN   A 1 101 ? 18.647 2.650   -11.950 0.58 19.53 ?  101 ASN   A CB   1 
ATOM   2043 C CB   B ASN   A 1 101 ? 18.725 1.210   -13.272 0.42 28.13 ?  101 ASN   A CB   1 
ATOM   2044 C CG   A ASN   A 1 101 ? 17.257 2.242   -11.471 0.58 19.53 ?  101 ASN   A CG   1 
ATOM   2045 C CG   B ASN   A 1 101 ? 17.369 0.798   -12.732 0.42 27.91 ?  101 ASN   A CG   1 
ATOM   2046 O OD1  A ASN   A 1 101 ? 16.433 1.760   -12.253 0.58 19.47 ?  101 ASN   A OD1  1 
ATOM   2047 O OD1  B ASN   A 1 101 ? 16.676 -0.030  -13.322 0.42 28.00 ?  101 ASN   A OD1  1 
ATOM   2048 N ND2  A ASN   A 1 101 ? 16.999 2.415   -10.181 0.58 19.97 ?  101 ASN   A ND2  1 
ATOM   2049 N ND2  B ASN   A 1 101 ? 16.986 1.373   -11.603 0.42 27.69 ?  101 ASN   A ND2  1 
ATOM   2050 H H    A ASN   A 1 101 ? 19.237 0.366   -11.329 0.58 22.05 ?  101 ASN   A H    1 
ATOM   2051 H H    B ASN   A 1 101 ? 19.583 -0.861  -12.254 0.42 32.60 ?  101 ASN   A H    1 
ATOM   2052 H HA   A ASN   A 1 101 ? 18.690 1.505   -13.632 0.58 23.51 ?  101 ASN   A HA   1 
ATOM   2053 H HA   B ASN   A 1 101 ? 18.870 -0.225  -14.719 0.42 33.60 ?  101 ASN   A HA   1 
ATOM   2054 H HB2  A ASN   A 1 101 ? 19.211 2.776   -11.173 0.58 23.42 ?  101 ASN   A HB2  1 
ATOM   2055 H HB2  B ASN   A 1 101 ? 19.271 1.505   -12.528 0.42 33.73 ?  101 ASN   A HB2  1 
ATOM   2056 H HB3  A ASN   A 1 101 ? 18.566 3.491   -12.438 0.58 23.42 ?  101 ASN   A HB3  1 
ATOM   2057 H HB3  B ASN   A 1 101 ? 18.590 1.938   -13.897 0.42 33.73 ?  101 ASN   A HB3  1 
ATOM   2058 H HD21 A ASN   A 1 101 ? 16.227 2.199   -9.868  0.58 23.94 ?  101 ASN   A HD21 1 
ATOM   2059 H HD21 B ASN   A 1 101 ? 16.227 1.170   -11.256 0.42 33.20 ?  101 ASN   A HD21 1 
ATOM   2060 H HD22 A ASN   A 1 101 ? 17.597 2.748   -9.663  0.58 23.94 ?  101 ASN   A HD22 1 
ATOM   2061 H HD22 B ASN   A 1 101 ? 17.496 1.948   -11.220 0.42 33.20 ?  101 ASN   A HD22 1 
ATOM   2062 N N    A LYS   A 1 102 ? 21.696 1.269   -13.185 0.58 22.86 ?  102 LYS   A N    1 
ATOM   2063 N N    B LYS   A 1 102 ? 21.892 0.094   -14.125 0.42 28.53 ?  102 LYS   A N    1 
ATOM   2064 C CA   A LYS   A 1 102 ? 22.991 1.468   -13.827 0.58 23.95 ?  102 LYS   A CA   1 
ATOM   2065 C CA   B LYS   A 1 102 ? 23.183 0.345   -14.751 0.42 28.32 ?  102 LYS   A CA   1 
ATOM   2066 C C    A LYS   A 1 102 ? 23.320 0.386   -14.846 0.58 24.71 ?  102 LYS   A C    1 
ATOM   2067 C C    B LYS   A 1 102 ? 23.620 -0.792  -15.665 0.42 26.77 ?  102 LYS   A C    1 
ATOM   2068 O O    A LYS   A 1 102 ? 24.401 0.433   -15.441 0.58 25.41 ?  102 LYS   A O    1 
ATOM   2069 O O    B LYS   A 1 102 ? 24.765 -0.794  -16.127 0.42 26.67 ?  102 LYS   A O    1 
ATOM   2070 C CB   A LYS   A 1 102 ? 24.114 1.502   -12.783 0.58 24.89 ?  102 LYS   A CB   1 
ATOM   2071 C CB   B LYS   A 1 102 ? 24.264 0.566   -13.691 0.42 29.74 ?  102 LYS   A CB   1 
ATOM   2072 C CG   A LYS   A 1 102 ? 24.019 2.627   -11.777 0.58 25.59 ?  102 LYS   A CG   1 
ATOM   2073 C CG   B LYS   A 1 102 ? 24.302 1.950   -13.074 0.42 31.08 ?  102 LYS   A CG   1 
ATOM   2074 C CD   A LYS   A 1 102 ? 25.165 2.551   -10.779 0.58 26.83 ?  102 LYS   A CD   1 
ATOM   2075 C CD   B LYS   A 1 102 ? 25.627 2.161   -12.352 0.42 32.29 ?  102 LYS   A CD   1 
ATOM   2076 C CE   A LYS   A 1 102 ? 25.100 3.673   -9.756  0.58 27.95 ?  102 LYS   A CE   1 
ATOM   2077 C CE   B LYS   A 1 102 ? 25.589 3.355   -11.416 0.42 33.11 ?  102 LYS   A CE   1 
ATOM   2078 N NZ   A LYS   A 1 102 ? 26.172 3.536   -8.727  0.58 28.45 ?  102 LYS   A NZ   1 
ATOM   2079 N NZ   B LYS   A 1 102 ? 25.250 2.953   -10.021 0.42 33.65 ?  102 LYS   A NZ   1 
ATOM   2080 H H    A LYS   A 1 102 ? 21.689 0.592   -12.654 0.58 27.41 ?  102 LYS   A H    1 
ATOM   2081 H H    B LYS   A 1 102 ? 21.948 -0.387  -13.415 0.42 34.21 ?  102 LYS   A H    1 
ATOM   2082 H HA   A LYS   A 1 102 ? 22.987 2.313   -14.294 0.58 28.72 ?  102 LYS   A HA   1 
ATOM   2083 H HA   B LYS   A 1 102 ? 23.125 1.147   -15.287 0.42 33.96 ?  102 LYS   A HA   1 
ATOM   2084 H HB2  A LYS   A 1 102 ? 24.104 0.664   -12.293 0.58 29.85 ?  102 LYS   A HB2  1 
ATOM   2085 H HB2  B LYS   A 1 102 ? 24.125 -0.071  -12.975 0.42 35.67 ?  102 LYS   A HB2  1 
ATOM   2086 H HB3  A LYS   A 1 102 ? 24.962 1.592   -13.248 0.58 29.85 ?  102 LYS   A HB3  1 
ATOM   2087 H HB3  B LYS   A 1 102 ? 25.132 0.410   -14.096 0.42 35.67 ?  102 LYS   A HB3  1 
ATOM   2088 H HG2  A LYS   A 1 102 ? 24.069 3.477   -12.240 0.58 30.68 ?  102 LYS   A HG2  1 
ATOM   2089 H HG2  B LYS   A 1 102 ? 24.226 2.617   -13.773 0.42 37.27 ?  102 LYS   A HG2  1 
ATOM   2090 H HG3  A LYS   A 1 102 ? 23.182 2.553   -11.292 0.58 30.68 ?  102 LYS   A HG3  1 
ATOM   2091 H HG3  B LYS   A 1 102 ? 23.577 2.045   -12.439 0.42 37.27 ?  102 LYS   A HG3  1 
ATOM   2092 H HD2  A LYS   A 1 102 ? 25.119 1.705   -10.305 0.58 32.17 ?  102 LYS   A HD2  1 
ATOM   2093 H HD2  B LYS   A 1 102 ? 25.831 1.371   -11.826 0.42 38.72 ?  102 LYS   A HD2  1 
ATOM   2094 H HD3  A LYS   A 1 102 ? 26.007 2.621   -11.256 0.58 32.17 ?  102 LYS   A HD3  1 
ATOM   2095 H HD3  B LYS   A 1 102 ? 26.325 2.313   -13.008 0.42 38.72 ?  102 LYS   A HD3  1 
ATOM   2096 H HE2  A LYS   A 1 102 ? 25.219 4.524   -10.209 0.58 33.52 ?  102 LYS   A HE2  1 
ATOM   2097 H HE2  B LYS   A 1 102 ? 26.460 3.781   -11.406 0.42 39.71 ?  102 LYS   A HE2  1 
ATOM   2098 H HE3  A LYS   A 1 102 ? 24.241 3.648   -9.308  0.58 33.52 ?  102 LYS   A HE3  1 
ATOM   2099 H HE3  B LYS   A 1 102 ? 24.914 3.980   -11.723 0.42 39.71 ?  102 LYS   A HE3  1 
ATOM   2100 H HZ1  A LYS   A 1 102 ? 26.117 4.201   -8.141  0.58 34.12 ?  102 LYS   A HZ1  1 
ATOM   2101 H HZ1  B LYS   A 1 102 ? 25.235 3.670   -9.494  0.42 40.36 ?  102 LYS   A HZ1  1 
ATOM   2102 H HZ2  A LYS   A 1 102 ? 26.082 2.761   -8.297  0.58 34.12 ?  102 LYS   A HZ2  1 
ATOM   2103 H HZ2  B LYS   A 1 102 ? 24.451 2.562   -10.002 0.42 40.36 ?  102 LYS   A HZ2  1 
ATOM   2104 H HZ3  A LYS   A 1 102 ? 26.972 3.558   -9.117  0.58 34.12 ?  102 LYS   A HZ3  1 
ATOM   2105 H HZ3  B LYS   A 1 102 ? 25.860 2.381   -9.714  0.42 40.36 ?  102 LYS   A HZ3  1 
ATOM   2106 N N    A GLY   A 1 103 ? 22.439 -0.594  -15.048 0.58 25.41 ?  103 GLY   A N    1 
ATOM   2107 N N    B GLY   A 1 103 ? 22.748 -1.763  -15.926 0.42 25.74 ?  103 GLY   A N    1 
ATOM   2108 C CA   A GLY   A 1 103 ? 22.708 -1.675  -15.976 0.58 26.26 ?  103 GLY   A CA   1 
ATOM   2109 C CA   B GLY   A 1 103 ? 23.143 -2.913  -16.712 0.42 24.79 ?  103 GLY   A CA   1 
ATOM   2110 C C    A GLY   A 1 103 ? 23.576 -2.781  -15.426 0.58 26.79 ?  103 GLY   A C    1 
ATOM   2111 C C    B GLY   A 1 103 ? 23.962 -3.932  -15.957 0.42 23.67 ?  103 GLY   A C    1 
ATOM   2112 O O    A GLY   A 1 103 ? 24.191 -3.513  -16.206 0.58 27.85 ?  103 GLY   A O    1 
ATOM   2113 O O    B GLY   A 1 103 ? 24.551 -4.819  -16.584 0.42 23.91 ?  103 GLY   A O    1 
ATOM   2114 H H    A GLY   A 1 103 ? 21.681 -0.663  -14.652 0.58 30.47 ?  103 GLY   A H    1 
ATOM   2115 H H    B GLY   A 1 103 ? 21.931 -1.780  -15.656 0.42 30.86 ?  103 GLY   A H    1 
ATOM   2116 H HA2  A GLY   A 1 103 ? 21.865 -2.059  -16.280 0.58 31.48 ?  103 GLY   A HA2  1 
ATOM   2117 H HA2  B GLY   A 1 103 ? 22.354 -3.362  -17.044 0.42 29.72 ?  103 GLY   A HA2  1 
ATOM   2118 H HA3  A GLY   A 1 103 ? 23.167 -1.323  -16.754 0.58 31.48 ?  103 GLY   A HA3  1 
ATOM   2119 H HA3  B GLY   A 1 103 ? 23.663 -2.608  -17.476 0.42 29.72 ?  103 GLY   A HA3  1 
ATOM   2120 N N    A GLU   A 1 104 ? 23.652 -2.927  -14.107 0.58 25.40 ?  104 GLU   A N    1 
ATOM   2121 N N    B GLU   A 1 104 ? 24.013 -3.838  -14.632 0.42 22.40 ?  104 GLU   A N    1 
ATOM   2122 C CA   A GLU   A 1 104 ? 24.529 -3.912  -13.491 0.58 24.14 ?  104 GLU   A CA   1 
ATOM   2123 C CA   B GLU   A 1 104 ? 24.855 -4.723  -13.842 0.42 21.36 ?  104 GLU   A CA   1 
ATOM   2124 C C    A GLU   A 1 104 ? 23.845 -5.274  -13.383 0.58 24.63 ?  104 GLU   A C    1 
ATOM   2125 C C    B GLU   A 1 104 ? 24.158 -6.059  -13.615 0.42 21.46 ?  104 GLU   A C    1 
ATOM   2126 O O    A GLU   A 1 104 ? 22.626 -5.373  -13.217 0.58 24.63 ?  104 GLU   A O    1 
ATOM   2127 O O    B GLU   A 1 104 ? 22.943 -6.119  -13.400 0.42 21.70 ?  104 GLU   A O    1 
ATOM   2128 C CB   A GLU   A 1 104 ? 25.001 -3.406  -12.124 0.58 22.07 ?  104 GLU   A CB   1 
ATOM   2129 C CB   B GLU   A 1 104 ? 25.230 -4.050  -12.519 0.42 21.06 ?  104 GLU   A CB   1 
ATOM   2130 C CG   A GLU   A 1 104 ? 25.809 -2.106  -12.263 0.58 20.78 ?  104 GLU   A CG   1 
ATOM   2131 C CG   B GLU   A 1 104 ? 26.078 -2.793  -12.727 0.42 21.26 ?  104 GLU   A CG   1 
ATOM   2132 C CD   A GLU   A 1 104 ? 26.211 -1.438  -10.953 0.58 19.37 ?  104 GLU   A CD   1 
ATOM   2133 C CD   B GLU   A 1 104 ? 26.493 -2.111  -11.440 0.42 21.69 ?  104 GLU   A CD   1 
ATOM   2134 O OE1  A GLU   A 1 104 ? 25.668 -1.792  -9.888  0.58 17.62 ?  104 GLU   A OE1  1 
ATOM   2135 O OE1  B GLU   A 1 104 ? 25.952 -2.454  -10.371 0.42 21.90 ?  104 GLU   A OE1  1 
ATOM   2136 O OE2  A GLU   A 1 104 ? 27.072 -0.527  -11.008 0.58 19.98 -1 104 GLU   A OE2  1 
ATOM   2137 O OE2  B GLU   A 1 104 ? 27.363 -1.214  -11.505 0.42 21.93 -1 104 GLU   A OE2  1 
ATOM   2138 H H    A GLU   A 1 104 ? 23.208 -2.454  -13.543 0.58 30.45 ?  104 GLU   A H    1 
ATOM   2139 H H    B GLU   A 1 104 ? 23.563 -3.271  -14.172 0.42 26.85 ?  104 GLU   A H    1 
ATOM   2140 H HA   A GLU   A 1 104 ? 25.307 -4.021  -14.055 0.58 28.94 ?  104 GLU   A HA   1 
ATOM   2141 H HA   B GLU   A 1 104 ? 25.676 -4.893  -14.330 0.42 25.60 ?  104 GLU   A HA   1 
ATOM   2142 H HB2  A GLU   A 1 104 ? 24.227 -3.234  -11.566 0.58 26.45 ?  104 GLU   A HB2  1 
ATOM   2143 H HB2  B GLU   A 1 104 ? 24.422 -3.792  -12.052 0.42 25.25 ?  104 GLU   A HB2  1 
ATOM   2144 H HB3  A GLU   A 1 104 ? 25.565 -4.082  -11.718 0.58 26.45 ?  104 GLU   A HB3  1 
ATOM   2145 H HB3  B GLU   A 1 104 ? 25.744 -4.672  -11.981 0.42 25.25 ?  104 GLU   A HB3  1 
ATOM   2146 H HG2  A GLU   A 1 104 ? 26.617 -2.307  -12.759 0.58 24.91 ?  104 GLU   A HG2  1 
ATOM   2147 H HG2  B GLU   A 1 104 ? 26.881 -3.031  -13.218 0.42 25.49 ?  104 GLU   A HG2  1 
ATOM   2148 H HG3  A GLU   A 1 104 ? 25.272 -1.468  -12.757 0.58 24.91 ?  104 GLU   A HG3  1 
ATOM   2149 H HG3  B GLU   A 1 104 ? 25.564 -2.144  -13.231 0.42 25.49 ?  104 GLU   A HG3  1 
ATOM   2150 N N    A ASP   A 1 105 ? 24.657 -6.326  -13.492 0.58 25.43 ?  105 ASP   A N    1 
ATOM   2151 N N    B ASP   A 1 105 ? 24.945 -7.131  -13.681 0.42 21.76 ?  105 ASP   A N    1 
ATOM   2152 C CA   A ASP   A 1 105 ? 24.152 -7.690  -13.602 0.58 26.44 ?  105 ASP   A CA   1 
ATOM   2153 C CA   B ASP   A 1 105 ? 24.422 -8.492  -13.691 0.42 22.44 ?  105 ASP   A CA   1 
ATOM   2154 C C    A ASP   A 1 105 ? 23.462 -8.120  -12.310 0.58 25.07 ?  105 ASP   A C    1 
ATOM   2155 C C    B ASP   A 1 105 ? 23.628 -8.784  -12.424 0.42 21.43 ?  105 ASP   A C    1 
ATOM   2156 O O    A ASP   A 1 105 ? 24.056 -8.068  -11.230 0.58 24.60 ?  105 ASP   A O    1 
ATOM   2157 O O    B ASP   A 1 105 ? 24.158 -8.699  -11.313 0.42 19.21 ?  105 ASP   A O    1 
ATOM   2158 C CB   A ASP   A 1 105 ? 25.322 -8.626  -13.907 0.58 28.81 ?  105 ASP   A CB   1 
ATOM   2159 C CB   B ASP   A 1 105 ? 25.598 -9.461  -13.814 0.42 24.08 ?  105 ASP   A CB   1 
ATOM   2160 C CG   A ASP   A 1 105 ? 24.877 -10.039 -14.202 0.58 30.65 ?  105 ASP   A CG   1 
ATOM   2161 C CG   B ASP   A 1 105 ? 25.164 -10.905 -13.904 0.42 25.74 ?  105 ASP   A CG   1 
ATOM   2162 O OD1  A ASP   A 1 105 ? 23.653 -10.275 -14.268 0.58 31.04 ?  105 ASP   A OD1  1 
ATOM   2163 O OD1  B ASP   A 1 105 ? 23.947 -11.166 -13.985 0.42 25.90 ?  105 ASP   A OD1  1 
ATOM   2164 O OD2  A ASP   A 1 105 ? 25.755 -10.912 -14.374 0.58 31.91 -1 105 ASP   A OD2  1 
ATOM   2165 O OD2  B ASP   A 1 105 ? 26.053 -11.784 -13.889 0.42 26.75 -1 105 ASP   A OD2  1 
ATOM   2166 H H    A ASP   A 1 105 ? 25.515 -6.275  -13.511 0.58 30.49 ?  105 ASP   A H    1 
ATOM   2167 H H    B ASP   A 1 105 ? 25.800 -7.092  -13.727 0.42 26.09 ?  105 ASP   A H    1 
ATOM   2168 H HA   A ASP   A 1 105 ? 23.518 -7.755  -14.335 0.58 31.70 ?  105 ASP   A HA   1 
ATOM   2169 H HA   B ASP   A 1 105 ? 23.837 -8.614  -14.454 0.42 26.90 ?  105 ASP   A HA   1 
ATOM   2170 H HB2  A ASP   A 1 105 ? 25.799 -8.303  -14.689 0.58 34.54 ?  105 ASP   A HB2  1 
ATOM   2171 H HB2  B ASP   A 1 105 ? 26.109 -9.240  -14.612 0.42 28.88 ?  105 ASP   A HB2  1 
ATOM   2172 H HB3  A ASP   A 1 105 ? 25.921 -8.647  -13.142 0.58 34.54 ?  105 ASP   A HB3  1 
ATOM   2173 H HB3  B ASP   A 1 105 ? 26.162 -9.383  -13.030 0.42 28.88 ?  105 ASP   A HB3  1 
ATOM   2174 N N    A ILE   A 1 106 ? 22.210 -8.573  -12.428 0.58 24.17 ?  106 ILE   A N    1 
ATOM   2175 N N    B ILE   A 1 106 ? 22.354 -9.149  -12.598 0.42 22.65 ?  106 ILE   A N    1 
ATOM   2176 C CA   A ILE   A 1 106 ? 21.435 -8.970  -11.255 0.58 23.33 ?  106 ILE   A CA   1 
ATOM   2177 C CA   B ILE   A 1 106 ? 21.522 -9.515  -11.456 0.42 23.59 ?  106 ILE   A CA   1 
ATOM   2178 C C    A ILE   A 1 106 ? 21.949 -10.266 -10.638 0.58 22.77 ?  106 ILE   A C    1 
ATOM   2179 C C    B ILE   A 1 106 ? 22.119 -10.699 -10.717 0.42 23.72 ?  106 ILE   A C    1 
ATOM   2180 O O    A ILE   A 1 106 ? 21.689 -10.527 -9.458  0.58 21.59 ?  106 ILE   A O    1 
ATOM   2181 O O    B ILE   A 1 106 ? 21.921 -10.848 -9.504  0.42 23.70 ?  106 ILE   A O    1 
ATOM   2182 C CB   A ILE   A 1 106 ? 19.934 -9.056  -11.607 0.58 24.23 ?  106 ILE   A CB   1 
ATOM   2183 C CB   B ILE   A 1 106 ? 20.078 -9.802  -11.908 0.42 24.31 ?  106 ILE   A CB   1 
ATOM   2184 C CG1  A ILE   A 1 106 ? 19.078 -9.120  -10.339 0.58 24.75 ?  106 ILE   A CG1  1 
ATOM   2185 C CG1  B ILE   A 1 106 ? 19.148 -9.935  -10.702 0.42 24.64 ?  106 ILE   A CG1  1 
ATOM   2186 C CG2  A ILE   A 1 106 ? 19.656 -10.269 -12.480 0.58 24.72 ?  106 ILE   A CG2  1 
ATOM   2187 C CG2  B ILE   A 1 106 ? 20.021 -11.094 -12.690 0.42 24.60 ?  106 ILE   A CG2  1 
ATOM   2188 C CD1  A ILE   A 1 106 ? 19.197 -7.894  -9.458  0.58 25.22 ?  106 ILE   A CD1  1 
ATOM   2189 C CD1  B ILE   A 1 106 ? 19.084 -8.708  -9.838  0.42 25.02 ?  106 ILE   A CD1  1 
ATOM   2190 H H    A ILE   A 1 106 ? 21.793 -8.658  -13.174 0.58 28.98 ?  106 ILE   A H    1 
ATOM   2191 H H    B ILE   A 1 106 ? 21.959 -9.188  -13.357 0.42 27.16 ?  106 ILE   A H    1 
ATOM   2192 H HA   A ILE   A 1 106 ? 21.540 -8.278  -10.588 0.58 27.97 ?  106 ILE   A HA   1 
ATOM   2193 H HA   B ILE   A 1 106 ? 21.504 -8.770  -10.842 0.42 28.29 ?  106 ILE   A HA   1 
ATOM   2194 H HB   A ILE   A 1 106 ? 19.690 -8.258  -12.102 0.58 29.05 ?  106 ILE   A HB   1 
ATOM   2195 H HB   B ILE   A 1 106 ? 19.769 -9.076  -12.473 0.42 29.15 ?  106 ILE   A HB   1 
ATOM   2196 H HG12 A ILE   A 1 106 ? 18.147 -9.206  -10.597 0.58 29.68 ?  106 ILE   A HG12 1 
ATOM   2197 H HG12 B ILE   A 1 106 ? 18.251 -10.119 -11.022 0.42 29.55 ?  106 ILE   A HG12 1 
ATOM   2198 H HG13 A ILE   A 1 106 ? 19.346 -9.890  -9.815  0.58 29.68 ?  106 ILE   A HG13 1 
ATOM   2199 H HG13 B ILE   A 1 106 ? 19.455 -10.671 -10.152 0.42 29.55 ?  106 ILE   A HG13 1 
ATOM   2200 H HG21 A ILE   A 1 106 ? 18.767 -10.186 -12.855 0.58 29.63 ?  106 ILE   A HG21 1 
ATOM   2201 H HG21 B ILE   A 1 106 ? 19.150 -11.169 -13.105 0.42 29.50 ?  106 ILE   A HG21 1 
ATOM   2202 H HG22 A ILE   A 1 106 ? 20.316 -10.301 -13.189 0.58 29.63 ?  106 ILE   A HG22 1 
ATOM   2203 H HG22 B ILE   A 1 106 ? 20.715 -11.085 -13.365 0.42 29.50 ?  106 ILE   A HG22 1 
ATOM   2204 H HG23 A ILE   A 1 106 ? 19.714 -11.069 -11.935 0.58 29.63 ?  106 ILE   A HG23 1 
ATOM   2205 H HG23 B ILE   A 1 106 ? 20.158 -11.839 -12.082 0.42 29.50 ?  106 ILE   A HG23 1 
ATOM   2206 H HD11 A ILE   A 1 106 ? 18.459 -7.886  -8.830  0.58 30.23 ?  106 ILE   A HD11 1 
ATOM   2207 H HD11 B ILE   A 1 106 ? 18.299 -8.765  -9.276  0.42 30.00 ?  106 ILE   A HD11 1 
ATOM   2208 H HD12 A ILE   A 1 106 ? 20.039 -7.929  -8.977  0.58 30.23 ?  106 ILE   A HD12 1 
ATOM   2209 H HD12 B ILE   A 1 106 ? 19.884 -8.668  -9.292  0.42 30.00 ?  106 ILE   A HD12 1 
ATOM   2210 H HD13 A ILE   A 1 106 ? 19.166 -7.100  -10.015 0.58 30.23 ?  106 ILE   A HD13 1 
ATOM   2211 H HD13 B ILE   A 1 106 ? 19.030 -7.929  -10.410 0.42 30.00 ?  106 ILE   A HD13 1 
ATOM   2212 N N    A GLN   A 1 107 ? 22.699 -11.073 -11.398 0.58 23.86 ?  107 GLN   A N    1 
ATOM   2213 N N    B GLN   A 1 107 ? 22.854 -11.561 -11.425 0.42 23.98 ?  107 GLN   A N    1 
ATOM   2214 C CA   A GLN   A 1 107 ? 23.250 -12.317 -10.861 0.58 25.52 ?  107 GLN   A CA   1 
ATOM   2215 C CA   B GLN   A 1 107 ? 23.529 -12.668 -10.763 0.42 25.41 ?  107 GLN   A CA   1 
ATOM   2216 C C    A GLN   A 1 107 ? 24.220 -12.052 -9.714  0.58 23.42 ?  107 GLN   A C    1 
ATOM   2217 C C    B GLN   A 1 107 ? 24.510 -12.178 -9.712  0.42 23.41 ?  107 GLN   A C    1 
ATOM   2218 O O    A GLN   A 1 107 ? 24.370 -12.886 -8.813  0.58 24.09 ?  107 GLN   A O    1 
ATOM   2219 O O    B GLN   A 1 107 ? 24.938 -12.971 -8.865  0.42 24.27 ?  107 GLN   A O    1 
ATOM   2220 C CB   A GLN   A 1 107 ? 23.950 -13.089 -11.983 0.58 29.58 ?  107 GLN   A CB   1 
ATOM   2221 C CB   B GLN   A 1 107 ? 24.261 -13.544 -11.785 0.42 28.56 ?  107 GLN   A CB   1 
ATOM   2222 C CG   A GLN   A 1 107 ? 23.095 -13.274 -13.230 0.58 33.71 ?  107 GLN   A CG   1 
ATOM   2223 C CG   B GLN   A 1 107 ? 23.374 -14.065 -12.907 0.42 31.58 ?  107 GLN   A CG   1 
ATOM   2224 C CD   A GLN   A 1 107 ? 21.813 -14.032 -12.948 0.58 37.03 ?  107 GLN   A CD   1 
ATOM   2225 C CD   B GLN   A 1 107 ? 22.241 -14.936 -12.406 0.42 34.25 ?  107 GLN   A CD   1 
ATOM   2226 O OE1  A GLN   A 1 107 ? 21.830 -15.096 -12.328 0.58 38.47 ?  107 GLN   A OE1  1 
ATOM   2227 O OE1  B GLN   A 1 107 ? 22.370 -15.621 -11.390 0.42 35.15 ?  107 GLN   A OE1  1 
ATOM   2228 N NE2  A GLN   A 1 107 ? 20.690 -13.484 -13.395 0.58 38.12 ?  107 GLN   A NE2  1 
ATOM   2229 N NE2  B GLN   A 1 107 ? 21.116 -14.911 -13.117 0.42 35.07 ?  107 GLN   A NE2  1 
ATOM   2230 H H    A GLN   A 1 107 ? 22.916 -10.911 -12.213 0.58 28.60 ?  107 GLN   A H    1 
ATOM   2231 H H    B GLN   A 1 107 ? 22.982 -11.523 -12.272 0.42 28.75 ?  107 GLN   A H    1 
ATOM   2232 H HA   A GLN   A 1 107 ? 22.532 -12.864 -10.523 0.58 30.59 ?  107 GLN   A HA   1 
ATOM   2233 H HA   B GLN   A 1 107 ? 22.869 -13.222 -10.321 0.42 30.46 ?  107 GLN   A HA   1 
ATOM   2234 H HB2  A GLN   A 1 107 ? 24.753 -12.611 -12.245 0.58 35.48 ?  107 GLN   A HB2  1 
ATOM   2235 H HB2  B GLN   A 1 107 ? 24.975 -13.029 -12.188 0.42 34.25 ?  107 GLN   A HB2  1 
ATOM   2236 H HB3  A GLN   A 1 107 ? 24.187 -13.972 -11.658 0.58 35.48 ?  107 GLN   A HB3  1 
ATOM   2237 H HB3  B GLN   A 1 107 ? 24.634 -14.315 -11.326 0.42 34.25 ?  107 GLN   A HB3  1 
ATOM   2238 H HG2  A GLN   A 1 107 ? 22.857 -12.405 -13.591 0.58 40.43 ?  107 GLN   A HG2  1 
ATOM   2239 H HG2  B GLN   A 1 107 ? 22.987 -13.314 -13.381 0.42 37.87 ?  107 GLN   A HG2  1 
ATOM   2240 H HG3  A GLN   A 1 107 ? 23.603 -13.774 -13.889 0.58 40.43 ?  107 GLN   A HG3  1 
ATOM   2241 H HG3  B GLN   A 1 107 ? 23.913 -14.597 -13.514 0.42 37.87 ?  107 GLN   A HG3  1 
ATOM   2242 H HE21 A GLN   A 1 107 ? 20.715 -12.739 -13.822 0.58 45.72 ?  107 GLN   A HE21 1 
ATOM   2243 H HE21 B GLN   A 1 107 ? 21.064 -14.418 -13.821 0.42 42.06 ?  107 GLN   A HE21 1 
ATOM   2244 H HE22 A GLN   A 1 107 ? 19.938 -13.877 -13.258 0.58 45.72 ?  107 GLN   A HE22 1 
ATOM   2245 H HE22 B GLN   A 1 107 ? 20.442 -15.387 -12.876 0.42 42.06 ?  107 GLN   A HE22 1 
ATOM   2246 N N    . LEU   A 1 108 ? 24.879 -10.893 -9.732  1.00 20.76 ?  108 LEU   A N    1 
ATOM   2247 C CA   . LEU   A 1 108 ? 25.761 -10.423 -8.676  1.00 17.50 ?  108 LEU   A CA   1 
ATOM   2248 C C    . LEU   A 1 108 ? 25.037 -10.231 -7.353  1.00 14.89 ?  108 LEU   A C    1 
ATOM   2249 O O    . LEU   A 1 108 ? 25.703 -10.057 -6.331  1.00 15.08 ?  108 LEU   A O    1 
ATOM   2250 C CB   . LEU   A 1 108 ? 26.455 -9.118  -9.097  1.00 17.25 ?  108 LEU   A CB   1 
ATOM   2251 C CG   . LEU   A 1 108 ? 27.466 -9.311  -10.228 1.00 19.09 ?  108 LEU   A CG   1 
ATOM   2252 C CD1  . LEU   A 1 108 ? 27.920 -7.978  -10.804 1.00 20.18 ?  108 LEU   A CD1  1 
ATOM   2253 C CD2  . LEU   A 1 108 ? 28.669 -10.108 -9.740  1.00 20.82 ?  108 LEU   A CD2  1 
ATOM   2254 H H    A LEU   A 1 108 ? 24.826 -10.340 -10.384 0.58 24.89 ?  108 LEU   A H    1 
ATOM   2255 H H    B LEU   A 1 108 ? 24.656 -10.314 -10.320 0.42 24.89 ?  108 LEU   A H    1 
ATOM   2256 H HA   . LEU   A 1 108 ? 26.452 -11.086 -8.528  1.00 20.98 ?  108 LEU   A HA   1 
ATOM   2257 H HB2  . LEU   A 1 108 ? 25.780 -8.492  -9.406  1.00 20.67 ?  108 LEU   A HB2  1 
ATOM   2258 H HB3  . LEU   A 1 108 ? 26.923 -8.748  -8.334  1.00 20.67 ?  108 LEU   A HB3  1 
ATOM   2259 H HG   . LEU   A 1 108 ? 27.049 -9.817  -10.941 1.00 22.88 ?  108 LEU   A HG   1 
ATOM   2260 H HD11 . LEU   A 1 108 ? 28.541 -8.142  -11.535 1.00 24.19 ?  108 LEU   A HD11 1 
ATOM   2261 H HD12 . LEU   A 1 108 ? 27.148 -7.494  -11.133 1.00 24.19 ?  108 LEU   A HD12 1 
ATOM   2262 H HD13 . LEU   A 1 108 ? 28.362 -7.464  -10.109 1.00 24.19 ?  108 LEU   A HD13 1 
ATOM   2263 H HD21 . LEU   A 1 108 ? 29.372 -10.055 -10.403 1.00 24.96 ?  108 LEU   A HD21 1 
ATOM   2264 H HD22 . LEU   A 1 108 ? 28.976 -9.729  -8.900  1.00 24.96 ?  108 LEU   A HD22 1 
ATOM   2265 H HD23 . LEU   A 1 108 ? 28.405 -11.031 -9.607  1.00 24.96 ?  108 LEU   A HD23 1 
ATOM   2266 N N    . LEU   A 1 109 ? 23.701 -10.290 -7.332  1.00 14.11 ?  109 LEU   A N    1 
ATOM   2267 C CA   . LEU   A 1 109 ? 22.991 -10.158 -6.066  1.00 13.27 ?  109 LEU   A CA   1 
ATOM   2268 C C    . LEU   A 1 109 ? 23.322 -11.312 -5.123  1.00 12.47 ?  109 LEU   A C    1 
ATOM   2269 O O    . LEU   A 1 109 ? 23.451 -11.112 -3.912  1.00 12.97 ?  109 LEU   A O    1 
ATOM   2270 C CB   . LEU   A 1 109 ? 21.488 -10.063 -6.326  1.00 13.84 ?  109 LEU   A CB   1 
ATOM   2271 C CG   . LEU   A 1 109 ? 20.582 -9.765  -5.132  1.00 14.30 ?  109 LEU   A CG   1 
ATOM   2272 C CD1  . LEU   A 1 109 ? 21.009 -8.492  -4.415  1.00 14.27 ?  109 LEU   A CD1  1 
ATOM   2273 C CD2  . LEU   A 1 109 ? 19.132 -9.638  -5.584  1.00 15.22 ?  109 LEU   A CD2  1 
ATOM   2274 H H    . LEU   A 1 109 ? 23.195 -10.407 -8.019  1.00 16.91 ?  109 LEU   A H    1 
ATOM   2275 H HA   . LEU   A 1 109 ? 23.275 -9.333  -5.640  1.00 15.90 ?  109 LEU   A HA   1 
ATOM   2276 H HB2  . LEU   A 1 109 ? 21.341 -9.357  -6.974  1.00 16.58 ?  109 LEU   A HB2  1 
ATOM   2277 H HB3  . LEU   A 1 109 ? 21.194 -10.905 -6.696  1.00 16.58 ?  109 LEU   A HB3  1 
ATOM   2278 H HG   . LEU   A 1 109 ? 20.635 -10.493 -4.498  1.00 17.13 ?  109 LEU   A HG   1 
ATOM   2279 H HD11 . LEU   A 1 109 ? 20.330 -8.247  -3.764  1.00 17.10 ?  109 LEU   A HD11 1 
ATOM   2280 H HD12 . LEU   A 1 109 ? 21.854 -8.642  -3.968  1.00 17.10 ?  109 LEU   A HD12 1 
ATOM   2281 H HD13 . LEU   A 1 109 ? 21.103 -7.774  -5.068  1.00 17.10 ?  109 LEU   A HD13 1 
ATOM   2282 H HD21 . LEU   A 1 109 ? 18.594 -9.298  -4.848  1.00 18.24 ?  109 LEU   A HD21 1 
ATOM   2283 H HD22 . LEU   A 1 109 ? 19.081 -9.026  -6.335  1.00 18.24 ?  109 LEU   A HD22 1 
ATOM   2284 H HD23 . LEU   A 1 109 ? 18.804 -10.513 -5.851  1.00 18.24 ?  109 LEU   A HD23 1 
ATOM   2285 N N    . LYS   A 1 110 ? 23.473 -12.528 -5.655  1.00 12.62 ?  110 LYS   A N    1 
ATOM   2286 C CA   . LYS   A 1 110 ? 23.840 -13.645 -4.791  1.00 12.52 ?  110 LYS   A CA   1 
ATOM   2287 C C    . LYS   A 1 110 ? 25.222 -13.425 -4.185  1.00 11.86 ?  110 LYS   A C    1 
ATOM   2288 O O    . LYS   A 1 110 ? 25.420 -13.624 -2.983  1.00 12.21 ?  110 LYS   A O    1 
ATOM   2289 C CB   . LYS   A 1 110 ? 23.767 -14.967 -5.555  1.00 13.85 ?  110 LYS   A CB   1 
ATOM   2290 C CG   . LYS   A 1 110 ? 23.965 -16.181 -4.651  1.00 14.02 ?  110 LYS   A CG   1 
ATOM   2291 C CD   . LYS   A 1 110 ? 23.743 -17.502 -5.374  1.00 14.66 ?  110 LYS   A CD   1 
ATOM   2292 C CE   . LYS   A 1 110 ? 23.842 -18.702 -4.427  1.00 15.37 ?  110 LYS   A CE   1 
ATOM   2293 N NZ   . LYS   A 1 110 ? 22.658 -18.809 -3.528  1.00 15.68 ?  110 LYS   A NZ   1 
ATOM   2294 H H    . LYS   A 1 110 ? 23.368 -12.723 -6.482  1.00 15.12 ?  110 LYS   A H    1 
ATOM   2295 H HA   . LYS   A 1 110 ? 23.200 -13.693 -4.060  1.00 15.00 ?  110 LYS   A HA   1 
ATOM   2296 H HB2  . LYS   A 1 110 ? 22.894 -15.044 -5.970  1.00 16.59 ?  110 LYS   A HB2  1 
ATOM   2297 H HB3  . LYS   A 1 110 ? 24.460 -14.979 -6.230  1.00 16.59 ?  110 LYS   A HB3  1 
ATOM   2298 H HG2  . LYS   A 1 110 ? 24.875 -16.173 -4.308  1.00 16.80 ?  110 LYS   A HG2  1 
ATOM   2299 H HG3  . LYS   A 1 110 ? 23.337 -16.132 -3.914  1.00 16.80 ?  110 LYS   A HG3  1 
ATOM   2300 H HD2  . LYS   A 1 110 ? 22.862 -17.506 -5.769  1.00 17.56 ?  110 LYS   A HD2  1 
ATOM   2301 H HD3  . LYS   A 1 110 ? 24.422 -17.607 -6.061  1.00 17.56 ?  110 LYS   A HD3  1 
ATOM   2302 H HE2  . LYS   A 1 110 ? 23.905 -19.518 -4.946  1.00 18.42 ?  110 LYS   A HE2  1 
ATOM   2303 H HE3  . LYS   A 1 110 ? 24.636 -18.604 -3.868  1.00 18.42 ?  110 LYS   A HE3  1 
ATOM   2304 H HZ1  . LYS   A 1 110 ? 22.742 -19.508 -2.990  1.00 18.79 ?  110 LYS   A HZ1  1 
ATOM   2305 H HZ2  . LYS   A 1 110 ? 22.584 -18.069 -3.034  1.00 18.79 ?  110 LYS   A HZ2  1 
ATOM   2306 H HZ3  . LYS   A 1 110 ? 21.918 -18.901 -4.016  1.00 18.79 ?  110 LYS   A HZ3  1 
ATOM   2307 N N    . SER   A 1 111 ? 26.185 -12.985 -5.000  1.00 12.17 ?  111 SER   A N    1 
ATOM   2308 C CA   . SER   A 1 111 ? 27.514 -12.665 -4.482  1.00 12.31 ?  111 SER   A CA   1 
ATOM   2309 C C    . SER   A 1 111 ? 27.443 -11.622 -3.373  1.00 11.82 ?  111 SER   A C    1 
ATOM   2310 O O    . SER   A 1 111 ? 28.132 -11.734 -2.353  1.00 12.44 ?  111 SER   A O    1 
ATOM   2311 C CB   . SER   A 1 111 ? 28.409 -12.166 -5.619  1.00 13.54 ?  111 SER   A CB   1 
ATOM   2312 O OG   . SER   A 1 111 ? 28.517 -13.154 -6.629  1.00 15.41 ?  111 SER   A OG   1 
ATOM   2313 H H    . SER   A 1 111 ? 26.088 -12.865 -5.843  1.00 14.58 ?  111 SER   A H    1 
ATOM   2314 H HA   . SER   A 1 111 ? 27.912 -13.469 -4.117  1.00 14.75 ?  111 SER   A HA   1 
ATOM   2315 H HB2  . SER   A 1 111 ? 28.013 -11.370 -6.009  1.00 16.22 ?  111 SER   A HB2  1 
ATOM   2316 H HB3  . SER   A 1 111 ? 29.287 -11.965 -5.269  1.00 16.22 ?  111 SER   A HB3  1 
ATOM   2317 H HG   . SER   A 1 111 ? 29.023 -12.876 -7.252  1.00 18.47 ?  111 SER   A HG   1 
ATOM   2318 N N    . ALA   A 1 112 ? 26.593 -10.607 -3.546  1.00 12.27 ?  112 ALA   A N    1 
ATOM   2319 C CA   . ALA   A 1 112 ? 26.445 -9.573  -2.523  1.00 11.64 ?  112 ALA   A CA   1 
ATOM   2320 C C    . ALA   A 1 112 ? 25.960 -10.175 -1.205  1.00 11.73 ?  112 ALA   A C    1 
ATOM   2321 O O    . ALA   A 1 112 ? 26.505 -9.883  -0.132  1.00 12.12 ?  112 ALA   A O    1 
ATOM   2322 C CB   . ALA   A 1 112 ? 25.485 -8.486  -3.010  1.00 12.37 ?  112 ALA   A CB   1 
ATOM   2323 H H    . ALA   A 1 112 ? 26.098 -10.492 -4.240  1.00 14.70 ?  112 ALA   A H    1 
ATOM   2324 H HA   . ALA   A 1 112 ? 27.307 -9.156  -2.364  1.00 13.94 ?  112 ALA   A HA   1 
ATOM   2325 H HB1  . ALA   A 1 112 ? 25.414 -7.794  -2.327  1.00 14.82 ?  112 ALA   A HB1  1 
ATOM   2326 H HB2  . ALA   A 1 112 ? 25.827 -8.099  -3.830  1.00 14.82 ?  112 ALA   A HB2  1 
ATOM   2327 H HB3  . ALA   A 1 112 ? 24.611 -8.878  -3.167  1.00 14.82 ?  112 ALA   A HB3  1 
ATOM   2328 N N    . TYR   A 1 113 ? 24.922 -11.015 -1.264  1.00 11.81 ?  113 TYR   A N    1 
ATOM   2329 C CA   . TYR   A 1 113 ? 24.404 -11.627 -0.044  1.00 11.54 ?  113 TYR   A CA   1 
ATOM   2330 C C    . TYR   A 1 113 ? 25.400 -12.586 0.606   1.00 11.20 ?  113 TYR   A C    1 
ATOM   2331 O O    . TYR   A 1 113 ? 25.362 -12.763 1.829   1.00 12.03 ?  113 TYR   A O    1 
ATOM   2332 C CB   . TYR   A 1 113 ? 23.078 -12.340 -0.321  1.00 12.08 ?  113 TYR   A CB   1 
ATOM   2333 C CG   . TYR   A 1 113 ? 21.863 -11.434 -0.254  1.00 11.53 ?  113 TYR   A CG   1 
ATOM   2334 C CD1  . TYR   A 1 113 ? 21.493 -10.826 0.940   1.00 11.81 ?  113 TYR   A CD1  1 
ATOM   2335 C CD2  . TYR   A 1 113 ? 21.066 -11.219 -1.368  1.00 11.99 ?  113 TYR   A CD2  1 
ATOM   2336 C CE1  . TYR   A 1 113 ? 20.368 -10.031 1.019   1.00 12.15 ?  113 TYR   A CE1  1 
ATOM   2337 C CE2  . TYR   A 1 113 ? 19.925 -10.410 -1.295  1.00 12.26 ?  113 TYR   A CE2  1 
ATOM   2338 C CZ   . TYR   A 1 113 ? 19.589 -9.828  -0.097  1.00 11.89 ?  113 TYR   A CZ   1 
ATOM   2339 O OH   . TYR   A 1 113 ? 18.468 -9.029  0.009   1.00 12.93 ?  113 TYR   A OH   1 
ATOM   2340 H H    . TYR   A 1 113 ? 24.514 -11.240 -1.987  1.00 14.15 ?  113 TYR   A H    1 
ATOM   2341 H HA   . TYR   A 1 113 ? 24.229 -10.924 0.597   1.00 13.83 ?  113 TYR   A HA   1 
ATOM   2342 H HB2  . TYR   A 1 113 ? 23.106 -12.721 -1.209  1.00 14.47 ?  113 TYR   A HB2  1 
ATOM   2343 H HB3  . TYR   A 1 113 ? 22.960 -13.042 0.337   1.00 14.47 ?  113 TYR   A HB3  1 
ATOM   2344 H HD1  . TYR   A 1 113 ? 22.014 -10.970 1.704   1.00 14.15 ?  113 TYR   A HD1  1 
ATOM   2345 H HD2  . TYR   A 1 113 ? 21.285 -11.627 -2.171  1.00 14.36 ?  113 TYR   A HD2  1 
ATOM   2346 H HE1  . TYR   A 1 113 ? 20.144 -9.632  1.831   1.00 14.55 ?  113 TYR   A HE1  1 
ATOM   2347 H HE2  . TYR   A 1 113 ? 19.392 -10.272 -2.041  1.00 14.68 ?  113 TYR   A HE2  1 
ATOM   2348 H HH   . TYR   A 1 113 ? 18.020 -9.081  -0.702  1.00 15.49 ?  113 TYR   A HH   1 
ATOM   2349 N N    . GLU   A 1 114 ? 26.307 -13.197 -0.175  1.00 11.40 ?  114 GLU   A N    1 
ATOM   2350 C CA   . GLU   A 1 114 ? 27.301 -14.094 0.420   1.00 11.74 ?  114 GLU   A CA   1 
ATOM   2351 C C    . GLU   A 1 114 ? 28.151 -13.384 1.471   1.00 11.52 ?  114 GLU   A C    1 
ATOM   2352 O O    . GLU   A 1 114 ? 28.624 -14.018 2.421   1.00 11.89 ?  114 GLU   A O    1 
ATOM   2353 C CB   . GLU   A 1 114 ? 28.171 -14.738 -0.669  1.00 11.98 ?  114 GLU   A CB   1 
ATOM   2354 C CG   . GLU   A 1 114 ? 27.410 -15.775 -1.465  1.00 12.30 ?  114 GLU   A CG   1 
ATOM   2355 C CD   . GLU   A 1 114 ? 28.127 -16.307 -2.697  1.00 12.63 ?  114 GLU   A CD   1 
ATOM   2356 O OE1  . GLU   A 1 114 ? 29.083 -15.678 -3.187  1.00 12.76 ?  114 GLU   A OE1  1 
ATOM   2357 O OE2  . GLU   A 1 114 ? 27.698 -17.375 -3.189  1.00 14.09 -1 114 GLU   A OE2  1 
ATOM   2358 H H    . GLU   A 1 114 ? 26.366 -13.101 -1.035  1.00 13.66 ?  114 GLU   A H    1 
ATOM   2359 H HA   . GLU   A 1 114 ? 26.828 -14.807 0.861   1.00 14.06 ?  114 GLU   A HA   1 
ATOM   2360 H HB2  . GLU   A 1 114 ? 28.477 -14.053 -1.289  1.00 14.35 ?  114 GLU   A HB2  1 
ATOM   2361 H HB3  . GLU   A 1 114 ? 28.929 -15.175 -0.256  1.00 14.35 ?  114 GLU   A HB3  1 
ATOM   2362 H HG2  . GLU   A 1 114 ? 27.231 -16.535 -0.892  1.00 14.73 ?  114 GLU   A HG2  1 
ATOM   2363 H HG3  . GLU   A 1 114 ? 26.571 -15.388 -1.762  1.00 14.73 ?  114 GLU   A HG3  1 
ATOM   2364 N N    . ASN   A 1 115 ? 28.338 -12.067 1.342   1.00 11.38 ?  115 ASN   A N    1 
ATOM   2365 C CA   . ASN   A 1 115 ? 29.100 -11.340 2.352   1.00 11.95 ?  115 ASN   A CA   1 
ATOM   2366 C C    . ASN   A 1 115 ? 28.474 -11.466 3.736   1.00 11.67 ?  115 ASN   A C    1 
ATOM   2367 O O    . ASN   A 1 115 ? 29.187 -11.399 4.745   1.00 12.14 ?  115 ASN   A O    1 
ATOM   2368 C CB   . ASN   A 1 115 ? 29.214 -9.865  1.979   1.00 12.16 ?  115 ASN   A CB   1 
ATOM   2369 C CG   . ASN   A 1 115 ? 30.015 -9.644  0.721   1.00 12.85 ?  115 ASN   A CG   1 
ATOM   2370 O OD1  . ASN   A 1 115 ? 31.237 -9.757  0.737   1.00 16.23 ?  115 ASN   A OD1  1 
ATOM   2371 N ND2  . ASN   A 1 115 ? 29.343 -9.333  -0.372  1.00 12.39 ?  115 ASN   A ND2  1 
ATOM   2372 H H    . ASN   A 1 115 ? 28.030 -11.579 0.706   1.00 13.63 ?  115 ASN   A H    1 
ATOM   2373 H HA   . ASN   A 1 115 ? 29.993 -11.711 2.400   1.00 14.31 ?  115 ASN   A HA   1 
ATOM   2374 H HB2  . ASN   A 1 115 ? 28.323 -9.506  1.846   1.00 14.56 ?  115 ASN   A HB2  1 
ATOM   2375 H HB3  . ASN   A 1 115 ? 29.656 -9.394  2.704   1.00 14.56 ?  115 ASN   A HB3  1 
ATOM   2376 H HD21 . ASN   A 1 115 ? 29.760 -9.194  -1.110  1.00 14.84 ?  115 ASN   A HD21 1 
ATOM   2377 H HD22 . ASN   A 1 115 ? 28.483 -9.275  -0.347  1.00 14.84 ?  115 ASN   A HD22 1 
ATOM   2378 N N    . PHE   A 1 116 ? 27.145 -11.637 3.812   1.00 11.51 ?  116 PHE   A N    1 
ATOM   2379 C CA   . PHE   A 1 116 ? 26.496 -11.724 5.117   1.00 11.60 ?  116 PHE   A CA   1 
ATOM   2380 C C    . PHE   A 1 116 ? 26.961 -12.961 5.890   1.00 11.91 ?  116 PHE   A C    1 
ATOM   2381 O O    . PHE   A 1 116 ? 26.887 -12.984 7.121   1.00 12.57 ?  116 PHE   A O    1 
ATOM   2382 C CB   . PHE   A 1 116 ? 24.968 -11.850 4.984   1.00 11.64 ?  116 PHE   A CB   1 
ATOM   2383 C CG   . PHE   A 1 116 ? 24.214 -10.607 4.509   1.00 10.98 ?  116 PHE   A CG   1 
ATOM   2384 C CD1  . PHE   A 1 116 ? 24.791 -9.592  3.757   1.00 11.49 ?  116 PHE   A CD1  1 
ATOM   2385 C CD2  . PHE   A 1 116 ? 22.857 -10.500 4.820   1.00 11.75 ?  116 PHE   A CD2  1 
ATOM   2386 C CE1  . PHE   A 1 116 ? 24.028 -8.513  3.328   1.00 11.86 ?  116 PHE   A CE1  1 
ATOM   2387 C CE2  . PHE   A 1 116 ? 22.093 -9.430  4.402   1.00 12.16 ?  116 PHE   A CE2  1 
ATOM   2388 C CZ   . PHE   A 1 116 ? 22.666 -8.434  3.652   1.00 11.70 ?  116 PHE   A CZ   1 
ATOM   2389 H H    . PHE   A 1 116 ? 26.609 -11.693 3.137   1.00 13.78 ?  116 PHE   A H    1 
ATOM   2390 H HA   . PHE   A 1 116 ? 26.692 -10.933 5.642   1.00 13.89 ?  116 PHE   A HA   1 
ATOM   2391 H HB2  . PHE   A 1 116 ? 24.775 -12.561 4.352   1.00 13.94 ?  116 PHE   A HB2  1 
ATOM   2392 H HB3  . PHE   A 1 116 ? 24.606 -12.094 5.854   1.00 13.94 ?  116 PHE   A HB3  1 
ATOM   2393 H HD1  . PHE   A 1 116 ? 25.687 -9.654  3.530   1.00 13.76 ?  116 PHE   A HD1  1 
ATOM   2394 H HD2  . PHE   A 1 116 ? 22.450 -11.180 5.319   1.00 14.08 ?  116 PHE   A HD2  1 
ATOM   2395 H HE1  . PHE   A 1 116 ? 24.426 -7.841  2.829   1.00 14.21 ?  116 PHE   A HE1  1 
ATOM   2396 H HE2  . PHE   A 1 116 ? 21.189 -9.386  4.629   1.00 14.57 ?  116 PHE   A HE2  1 
ATOM   2397 H HZ   . PHE   A 1 116 ? 22.162 -7.703  3.380   1.00 14.02 ?  116 PHE   A HZ   1 
ATOM   2398 N N    . ASN   A 1 117 ? 27.416 -14.009 5.189   1.00 12.15 ?  117 ASN   A N    1 
ATOM   2399 C CA   . ASN   A 1 117 ? 27.779 -15.254 5.860   1.00 12.49 ?  117 ASN   A CA   1 
ATOM   2400 C C    . ASN   A 1 117 ? 29.036 -15.134 6.701   1.00 13.16 ?  117 ASN   A C    1 
ATOM   2401 O O    . ASN   A 1 117 ? 29.335 -16.060 7.463   1.00 13.96 ?  117 ASN   A O    1 
ATOM   2402 C CB   . ASN   A 1 117 ? 27.896 -16.380 4.836   1.00 12.93 ?  117 ASN   A CB   1 
ATOM   2403 C CG   . ASN   A 1 117 ? 26.546 -16.766 4.295   1.00 12.94 ?  117 ASN   A CG   1 
ATOM   2404 O OD1  . ASN   A 1 117 ? 25.569 -16.794 5.041   1.00 13.92 ?  117 ASN   A OD1  1 
ATOM   2405 N ND2  . ASN   A 1 117 ? 26.469 -17.025 3.003   1.00 12.48 ?  117 ASN   A ND2  1 
ATOM   2406 H H    . ASN   A 1 117 ? 27.499 -14.021 4.328   1.00 14.56 ?  117 ASN   A H    1 
ATOM   2407 H HA   . ASN   A 1 117 ? 27.052 -15.486 6.458   1.00 14.97 ?  117 ASN   A HA   1 
ATOM   2408 H HB2  . ASN   A 1 117 ? 28.449 -16.080 4.094   1.00 15.49 ?  117 ASN   A HB2  1 
ATOM   2409 H HB3  . ASN   A 1 117 ? 28.290 -17.151 5.261   1.00 15.49 ?  117 ASN   A HB3  1 
ATOM   2410 H HD21 . ASN   A 1 117 ? 25.718 -17.244 2.656   1.00 14.95 ?  117 ASN   A HD21 1 
ATOM   2411 H HD22 . ASN   A 1 117 ? 27.178 -16.983 2.516   1.00 14.95 ?  117 ASN   A HD22 1 
ATOM   2412 N N    . GLN   A 1 118 ? 29.764 -14.024 6.589   1.00 12.77 ?  118 GLN   A N    1 
ATOM   2413 C CA   . GLN   A 1 118 ? 30.940 -13.790 7.417   1.00 13.38 ?  118 GLN   A CA   1 
ATOM   2414 C C    . GLN   A 1 118 ? 30.591 -13.216 8.783   1.00 13.47 ?  118 GLN   A C    1 
ATOM   2415 O O    . GLN   A 1 118 ? 31.505 -12.927 9.567   1.00 14.89 ?  118 GLN   A O    1 
ATOM   2416 C CB   . GLN   A 1 118 ? 31.941 -12.887 6.685   1.00 13.85 ?  118 GLN   A CB   1 
ATOM   2417 C CG   . GLN   A 1 118 ? 32.409 -13.470 5.361   1.00 13.45 ?  118 GLN   A CG   1 
ATOM   2418 C CD   . GLN   A 1 118 ? 33.245 -14.728 5.535   1.00 14.27 ?  118 GLN   A CD   1 
ATOM   2419 O OE1  . GLN   A 1 118 ? 34.094 -14.799 6.429   1.00 15.06 ?  118 GLN   A OE1  1 
ATOM   2420 N NE2  . GLN   A 1 118 ? 33.010 -15.726 4.681   1.00 14.28 ?  118 GLN   A NE2  1 
ATOM   2421 H H    . GLN   A 1 118 ? 29.590 -13.378 6.034   1.00 15.30 ?  118 GLN   A H    1 
ATOM   2422 H HA   . GLN   A 1 118 ? 31.369 -14.645 7.565   1.00 16.03 ?  118 GLN   A HA   1 
ATOM   2423 H HB2  . GLN   A 1 118 ? 31.518 -12.031 6.508   1.00 16.60 ?  118 GLN   A HB2  1 
ATOM   2424 H HB3  . GLN   A 1 118 ? 32.716 -12.762 7.254   1.00 16.60 ?  118 GLN   A HB3  1 
ATOM   2425 H HG2  . GLN   A 1 118 ? 31.635 -13.693 4.818   1.00 16.12 ?  118 GLN   A HG2  1 
ATOM   2426 H HG3  . GLN   A 1 118 ? 32.955 -12.813 4.903   1.00 16.12 ?  118 GLN   A HG3  1 
ATOM   2427 H HE21 . GLN   A 1 118 ? 32.403 -15.638 4.071   1.00 17.11 ?  118 GLN   A HE21 1 
ATOM   2428 H HE22 . GLN   A 1 118 ? 33.449 -16.461 4.739   1.00 17.11 ?  118 GLN   A HE22 1 
ATOM   2429 N N    . HIS   A 1 119 ? 29.299 -13.053 9.085   1.00 13.04 ?  119 HIS   A N    1 
ATOM   2430 C CA   . HIS   A 1 119 ? 28.842 -12.451 10.331  1.00 13.77 ?  119 HIS   A CA   1 
ATOM   2431 C C    . HIS   A 1 119 ? 27.700 -13.270 10.905  1.00 13.99 ?  119 HIS   A C    1 
ATOM   2432 O O    . HIS   A 1 119 ? 26.759 -13.618 10.185  1.00 14.25 ?  119 HIS   A O    1 
ATOM   2433 C CB   . HIS   A 1 119 ? 28.384 -11.020 10.059  1.00 14.32 ?  119 HIS   A CB   1 
ATOM   2434 C CG   . HIS   A 1 119 ? 29.469 -10.201 9.457   1.00 15.25 ?  119 HIS   A CG   1 
ATOM   2435 N ND1  . HIS   A 1 119 ? 30.430 -9.583  10.224  1.00 17.46 ?  119 HIS   A ND1  1 
ATOM   2436 C CD2  . HIS   A 1 119 ? 29.830 -10.010 8.168   1.00 16.16 ?  119 HIS   A CD2  1 
ATOM   2437 C CE1  . HIS   A 1 119 ? 31.300 -8.986  9.431   1.00 17.79 ?  119 HIS   A CE1  1 
ATOM   2438 N NE2  . HIS   A 1 119 ? 30.969 -9.241  8.177   1.00 17.75 ?  119 HIS   A NE2  1 
ATOM   2439 H H    . HIS   A 1 119 ? 28.646 -13.300 8.571   1.00 15.62 ?  119 HIS   A H    1 
ATOM   2440 H HA   . HIS   A 1 119 ? 29.566 -12.432 10.971  1.00 16.50 ?  119 HIS   A HA   1 
ATOM   2441 H HB2  . HIS   A 1 119 ? 27.632 -11.038 9.442   1.00 17.16 ?  119 HIS   A HB2  1 
ATOM   2442 H HB3  . HIS   A 1 119 ? 28.116 -10.609 10.897  1.00 17.16 ?  119 HIS   A HB3  1 
ATOM   2443 H HD1  . HIS   A 1 119 ? 30.435 -9.561  11.084  1.00 20.93 ?  119 HIS   A HD1  1 
ATOM   2444 H HD2  . HIS   A 1 119 ? 29.383 -10.328 7.414   1.00 19.36 ?  119 HIS   A HD2  1 
ATOM   2445 H HE1  . HIS   A 1 119 ? 32.025 -8.477  9.709   1.00 21.32 ?  119 HIS   A HE1  1 
ATOM   2446 N N    . GLU   A 1 120 ? 27.778 -13.565 12.205  1.00 14.71 ?  120 GLU   A N    1 
ATOM   2447 C CA   . GLU   A 1 120 ? 26.825 -14.495 12.810  1.00 17.37 ?  120 GLU   A CA   1 
ATOM   2448 C C    . GLU   A 1 120 ? 25.407 -13.934 12.852  1.00 16.02 ?  120 GLU   A C    1 
ATOM   2449 O O    . GLU   A 1 120 ? 24.436 -14.697 12.737  1.00 15.92 ?  120 GLU   A O    1 
ATOM   2450 C CB   . GLU   A 1 120 ? 27.284 -14.876 14.217  1.00 22.30 ?  120 GLU   A CB   1 
ATOM   2451 C CG   . GLU   A 1 120 ? 28.480 -15.813 14.246  1.00 29.12 ?  120 GLU   A CG   1 
ATOM   2452 C CD   . GLU   A 1 120 ? 28.616 -16.556 15.557  1.00 35.45 ?  120 GLU   A CD   1 
ATOM   2453 O OE1  . GLU   A 1 120 ? 28.195 -16.011 16.600  1.00 37.18 ?  120 GLU   A OE1  1 
ATOM   2454 O OE2  . GLU   A 1 120 ? 29.143 -17.689 15.545  1.00 39.06 -1 120 GLU   A OE2  1 
ATOM   2455 H H    . GLU   A 1 120 ? 28.373 -13.255 12.749  1.00 17.63 ?  120 GLU   A H    1 
ATOM   2456 H HA   . GLU   A 1 120 ? 26.803 -15.304 12.286  1.00 20.82 ?  120 GLU   A HA   1 
ATOM   2457 H HB2  . GLU   A 1 120 ? 27.532 -14.076 14.705  1.00 26.74 ?  120 GLU   A HB2  1 
ATOM   2458 H HB3  . GLU   A 1 120 ? 26.554 -15.325 14.680  1.00 26.74 ?  120 GLU   A HB3  1 
ATOM   2459 H HG2  . GLU   A 1 120 ? 28.394 -16.462 13.532  1.00 34.92 ?  120 GLU   A HG2  1 
ATOM   2460 H HG3  . GLU   A 1 120 ? 29.292 -15.298 14.138  1.00 34.92 ?  120 GLU   A HG3  1 
ATOM   2461 N N    . VAL   A 1 121 ? 25.268 -12.623 13.065  1.00 15.51 ?  121 VAL   A N    1 
ATOM   2462 C CA   . VAL   A 1 121 ? 23.972 -11.953 13.178  1.00 15.10 ?  121 VAL   A CA   1 
ATOM   2463 C C    . VAL   A 1 121 ? 24.083 -10.574 12.534  1.00 13.76 ?  121 VAL   A C    1 
ATOM   2464 O O    . VAL   A 1 121 ? 25.048 -9.845  12.785  1.00 14.55 ?  121 VAL   A O    1 
ATOM   2465 C CB   . VAL   A 1 121 ? 23.538 -11.787 14.653  1.00 18.19 ?  121 VAL   A CB   1 
ATOM   2466 C CG1  . VAL   A 1 121 ? 22.151 -11.151 14.739  1.00 18.82 ?  121 VAL   A CG1  1 
ATOM   2467 C CG2  . VAL   A 1 121 ? 23.552 -13.107 15.392  1.00 20.32 ?  121 VAL   A CG2  1 
ATOM   2468 H H    . VAL   A 1 121 ? 25.933 -12.080 13.149  1.00 18.59 ?  121 VAL   A H    1 
ATOM   2469 H HA   . VAL   A 1 121 ? 23.298 -12.471 12.712  1.00 18.10 ?  121 VAL   A HA   1 
ATOM   2470 H HB   . VAL   A 1 121 ? 24.160 -11.194 15.098  1.00 21.80 ?  121 VAL   A HB   1 
ATOM   2471 H HG11 . VAL   A 1 121 ? 21.835 -11.203 15.657  1.00 22.56 ?  121 VAL   A HG11 1 
ATOM   2472 H HG12 . VAL   A 1 121 ? 22.205 -10.224 14.462  1.00 22.56 ?  121 VAL   A HG12 1 
ATOM   2473 H HG13 . VAL   A 1 121 ? 21.542 -11.637 14.158  1.00 22.56 ?  121 VAL   A HG13 1 
ATOM   2474 H HG21 . VAL   A 1 121 ? 23.205 -12.971 16.294  1.00 24.35 ?  121 VAL   A HG21 1 
ATOM   2475 H HG22 . VAL   A 1 121 ? 22.988 -13.744 14.922  1.00 24.35 ?  121 VAL   A HG22 1 
ATOM   2476 H HG23 . VAL   A 1 121 ? 24.459 -13.440 15.439  1.00 24.35 ?  121 VAL   A HG23 1 
ATOM   2477 N N    . LEU   A 1 122 ? 23.076 -10.192 11.744  1.00 13.42 ?  122 LEU   A N    1 
ATOM   2478 C CA   . LEU   A 1 122 ? 23.076 -8.894  11.078  1.00 13.19 ?  122 LEU   A CA   1 
ATOM   2479 C C    . LEU   A 1 122 ? 21.679 -8.299  11.027  1.00 12.91 ?  122 LEU   A C    1 
ATOM   2480 O O    . LEU   A 1 122 ? 20.689 -9.020  10.887  1.00 13.95 ?  122 LEU   A O    1 
ATOM   2481 C CB   . LEU   A 1 122 ? 23.532 -8.987  9.616   1.00 14.55 ?  122 LEU   A CB   1 
ATOM   2482 C CG   . LEU   A 1 122 ? 24.730 -9.852  9.253   1.00 14.63 ?  122 LEU   A CG   1 
ATOM   2483 C CD1  . LEU   A 1 122 ? 24.310 -11.295 9.021   1.00 15.03 ?  122 LEU   A CD1  1 
ATOM   2484 C CD2  . LEU   A 1 122 ? 25.419 -9.290  8.019   1.00 14.29 ?  122 LEU   A CD2  1 
ATOM   2485 H H    . LEU   A 1 122 ? 22.375 -10.667 11.580  1.00 16.08 ?  122 LEU   A H    1 
ATOM   2486 H HA   . LEU   A 1 122 ? 23.664 -8.281  11.548  1.00 15.80 ?  122 LEU   A HA   1 
ATOM   2487 H HB2  . LEU   A 1 122 ? 22.797 -9.321  9.092   1.00 17.43 ?  122 LEU   A HB2  1 
ATOM   2488 H HB3  . LEU   A 1 122 ? 23.756 -8.092  9.317   1.00 17.43 ?  122 LEU   A HB3  1 
ATOM   2489 H HG   . LEU   A 1 122 ? 25.379 -9.844  9.976   1.00 17.53 ?  122 LEU   A HG   1 
ATOM   2490 H HD11 . LEU   A 1 122 ? 25.078 -11.819 8.742   1.00 18.01 ?  122 LEU   A HD11 1 
ATOM   2491 H HD12 . LEU   A 1 122 ? 23.950 -11.656 9.847   1.00 18.01 ?  122 LEU   A HD12 1 
ATOM   2492 H HD13 . LEU   A 1 122 ? 23.629 -11.320 8.328   1.00 18.01 ?  122 LEU   A HD13 1 
ATOM   2493 H HD21 . LEU   A 1 122 ? 26.161 -9.874  7.763   1.00 17.13 ?  122 LEU   A HD21 1 
ATOM   2494 H HD22 . LEU   A 1 122 ? 24.784 -9.237  7.289   1.00 17.13 ?  122 LEU   A HD22 1 
ATOM   2495 H HD23 . LEU   A 1 122 ? 25.766 -8.404  8.219   1.00 17.13 ?  122 LEU   A HD23 1 
ATOM   2496 N N    A LEU   A 1 123 ? 21.619 -6.970  11.095  0.58 13.03 ?  123 LEU   A N    1 
ATOM   2497 N N    B LEU   A 1 123 ? 21.622 -6.978  11.182  0.42 12.59 ?  123 LEU   A N    1 
ATOM   2498 C CA   A LEU   A 1 123 ? 20.452 -6.192  10.695  0.58 12.44 ?  123 LEU   A CA   1 
ATOM   2499 C CA   B LEU   A 1 123 ? 20.457 -6.171  10.846  0.42 12.12 ?  123 LEU   A CA   1 
ATOM   2500 C C    A LEU   A 1 123 ? 20.712 -5.669  9.291   0.58 12.18 ?  123 LEU   A C    1 
ATOM   2501 C C    B LEU   A 1 123 ? 20.697 -5.622  9.447   0.42 11.43 ?  123 LEU   A C    1 
ATOM   2502 O O    A LEU   A 1 123 ? 21.815 -5.192  9.007   0.58 11.89 ?  123 LEU   A O    1 
ATOM   2503 O O    B LEU   A 1 123 ? 21.654 -4.868  9.241   0.42 10.86 ?  123 LEU   A O    1 
ATOM   2504 C CB   A LEU   A 1 123 ? 20.272 -5.006  11.642  0.58 13.16 ?  123 LEU   A CB   1 
ATOM   2505 C CB   B LEU   A 1 123 ? 20.335 -5.018  11.842  0.42 12.84 ?  123 LEU   A CB   1 
ATOM   2506 C CG   A LEU   A 1 123 ? 19.231 -3.944  11.282  0.58 13.77 ?  123 LEU   A CG   1 
ATOM   2507 C CG   B LEU   A 1 123 ? 19.322 -3.925  11.493  0.42 13.25 ?  123 LEU   A CG   1 
ATOM   2508 C CD1  A LEU   A 1 123 ? 17.835 -4.544  11.295  0.58 14.32 ?  123 LEU   A CD1  1 
ATOM   2509 C CD1  B LEU   A 1 123 ? 17.906 -4.486  11.427  0.42 13.77 ?  123 LEU   A CD1  1 
ATOM   2510 C CD2  A LEU   A 1 123 ? 19.321 -2.757  12.245  0.58 14.00 ?  123 LEU   A CD2  1 
ATOM   2511 C CD2  B LEU   A 1 123 ? 19.407 -2.770  12.485  0.42 13.75 ?  123 LEU   A CD2  1 
ATOM   2512 H H    A LEU   A 1 123 ? 22.277 -6.481  11.365  0.58 15.61 ?  123 LEU   A H    1 
ATOM   2513 H H    B LEU   A 1 123 ? 22.277 -6.508  11.489  0.42 15.08 ?  123 LEU   A H    1 
ATOM   2514 H HA   A LEU   A 1 123 ? 19.661 -6.748  10.693  0.58 14.90 ?  123 LEU   A HA   1 
ATOM   2515 H HA   B LEU   A 1 123 ? 19.649 -6.705  10.857  0.42 14.52 ?  123 LEU   A HA   1 
ATOM   2516 H HB2  A LEU   A 1 123 ? 20.018 -5.358  12.509  0.58 15.77 ?  123 LEU   A HB2  1 
ATOM   2517 H HB2  B LEU   A 1 123 ? 20.078 -5.386  12.702  0.42 15.39 ?  123 LEU   A HB2  1 
ATOM   2518 H HB3  A LEU   A 1 123 ? 21.120 -4.550  11.718  0.58 15.77 ?  123 LEU   A HB3  1 
ATOM   2519 H HB3  B LEU   A 1 123 ? 21.202 -4.590  11.923  0.42 15.39 ?  123 LEU   A HB3  1 
ATOM   2520 H HG   A LEU   A 1 123 ? 19.401 -3.606  10.387  0.58 16.50 ?  123 LEU   A HG   1 
ATOM   2521 H HG   B LEU   A 1 123 ? 19.533 -3.566  10.619  0.42 15.88 ?  123 LEU   A HG   1 
ATOM   2522 H HD11 A LEU   A 1 123 ? 17.186 -3.850  11.096  0.58 17.16 ?  123 LEU   A HD11 1 
ATOM   2523 H HD11 B LEU   A 1 123 ? 17.286 -3.762  11.242  0.42 16.50 ?  123 LEU   A HD11 1 
ATOM   2524 H HD12 A LEU   A 1 123 ? 17.787 -5.242  10.624  0.58 17.16 ?  123 LEU   A HD12 1 
ATOM   2525 H HD12 B LEU   A 1 123 ? 17.860 -5.147  10.717  0.42 16.50 ?  123 LEU   A HD12 1 
ATOM   2526 H HD13 A LEU   A 1 123 ? 17.661 -4.917  12.174  0.58 17.16 ?  123 LEU   A HD13 1 
ATOM   2527 H HD13 B LEU   A 1 123 ? 17.687 -4.899  12.277  0.42 16.50 ?  123 LEU   A HD13 1 
ATOM   2528 H HD21 A LEU   A 1 123 ? 18.655 -2.094  12.004  0.58 16.77 ?  123 LEU   A HD21 1 
ATOM   2529 H HD21 B LEU   A 1 123 ? 18.754 -2.096  12.239  0.42 16.47 ?  123 LEU   A HD21 1 
ATOM   2530 H HD22 A LEU   A 1 123 ? 19.158 -3.073  13.150  0.58 16.77 ?  123 LEU   A HD22 1 
ATOM   2531 H HD22 B LEU   A 1 123 ? 19.218 -3.105  13.375  0.42 16.47 ?  123 LEU   A HD22 1 
ATOM   2532 H HD23 A LEU   A 1 123 ? 20.209 -2.370  12.188  0.58 16.77 ?  123 LEU   A HD23 1 
ATOM   2533 H HD23 B LEU   A 1 123 ? 20.300 -2.395  12.453  0.42 16.47 ?  123 LEU   A HD23 1 
ATOM   2534 N N    A ALA   A 1 124 ? 19.714 -5.742  8.409   0.58 11.33 ?  124 ALA   A N    1 
ATOM   2535 N N    B ALA   A 1 124 ? 19.850 -5.995  8.489   0.42 11.29 ?  124 ALA   A N    1 
ATOM   2536 C CA   A ALA   A 1 124 ? 20.012 -5.499  7.003   0.58 10.61 ?  124 ALA   A CA   1 
ATOM   2537 C CA   B ALA   A 1 124 ? 20.138 -5.709  7.090   0.42 11.80 ?  124 ALA   A CA   1 
ATOM   2538 C C    A ALA   A 1 124 ? 18.761 -5.047  6.261   0.58 10.65 ?  124 ALA   A C    1 
ATOM   2539 C C    B ALA   A 1 124 ? 18.913 -5.222  6.331   0.42 11.47 ?  124 ALA   A C    1 
ATOM   2540 O O    A ALA   A 1 124 ? 17.635 -5.374  6.660   0.58 11.64 ?  124 ALA   A O    1 
ATOM   2541 O O    B ALA   A 1 124 ? 17.778 -5.591  6.661   0.42 11.88 ?  124 ALA   A O    1 
ATOM   2542 C CB   A ALA   A 1 124 ? 20.595 -6.752  6.335   0.58 10.82 ?  124 ALA   A CB   1 
ATOM   2543 C CB   B ALA   A 1 124 ? 20.697 -6.950  6.375   0.42 12.41 ?  124 ALA   A CB   1 
ATOM   2544 H H    A ALA   A 1 124 ? 18.892 -5.916  8.606   0.58 13.57 ?  124 ALA   A H    1 
ATOM   2545 H H    B ALA   A 1 124 ? 19.110 -6.418  8.617   0.42 13.53 ?  124 ALA   A H    1 
ATOM   2546 H HA   A ALA   A 1 124 ? 20.667 -4.789  6.955   0.58 12.70 ?  124 ALA   A HA   1 
ATOM   2547 H HA   B ALA   A 1 124 ? 20.813 -5.018  7.051   0.42 14.13 ?  124 ALA   A HA   1 
ATOM   2548 H HB1  A ALA   A 1 124 ? 20.777 -6.557  5.401   0.58 12.96 ?  124 ALA   A HB1  1 
ATOM   2549 H HB1  B ALA   A 1 124 ? 20.881 -6.731  5.445   0.42 14.86 ?  124 ALA   A HB1  1 
ATOM   2550 H HB2  A ALA   A 1 124 ? 21.419 -6.995  6.787   0.58 12.96 ?  124 ALA   A HB2  1 
ATOM   2551 H HB2  B ALA   A 1 124 ? 21.519 -7.226  6.813   0.42 14.86 ?  124 ALA   A HB2  1 
ATOM   2552 H HB3  A ALA   A 1 124 ? 19.955 -7.477  6.402   0.58 12.96 ?  124 ALA   A HB3  1 
ATOM   2553 H HB3  B ALA   A 1 124 ? 20.044 -7.666  6.419   0.42 14.86 ?  124 ALA   A HB3  1 
ATOM   2554 N N    A PRO   A 1 125 ? 18.938 -4.326  5.155   0.58 11.10 ?  125 PRO   A N    1 
ATOM   2555 N N    B PRO   A 1 125 ? 19.120 -4.425  5.285   0.42 10.47 ?  125 PRO   A N    1 
ATOM   2556 C CA   A PRO   A 1 125 ? 17.878 -4.134  4.168   0.58 11.55 ?  125 PRO   A CA   1 
ATOM   2557 C CA   B PRO   A 1 125 ? 18.036 -4.062  4.374   0.42 10.94 ?  125 PRO   A CA   1 
ATOM   2558 C C    A PRO   A 1 125 ? 17.961 -5.205  3.083   0.58 11.20 ?  125 PRO   A C    1 
ATOM   2559 C C    B PRO   A 1 125 ? 17.975 -5.087  3.245   0.42 12.19 ?  125 PRO   A C    1 
ATOM   2560 O O    A PRO   A 1 125 ? 18.933 -5.959  2.988   0.58 11.73 ?  125 PRO   A O    1 
ATOM   2561 O O    B PRO   A 1 125 ? 18.862 -5.929  3.089   0.42 12.67 ?  125 PRO   A O    1 
ATOM   2562 C CB   A PRO   A 1 125 ? 18.265 -2.775  3.569   0.58 12.08 ?  125 PRO   A CB   1 
ATOM   2563 C CB   B PRO   A 1 125 ? 18.532 -2.715  3.831   0.42 10.51 ?  125 PRO   A CB   1 
ATOM   2564 C CG   A PRO   A 1 125 ? 19.778 -2.865  3.507   0.58 12.01 ?  125 PRO   A CG   1 
ATOM   2565 C CG   B PRO   A 1 125 ? 20.027 -2.941  3.683   0.42 10.19 ?  125 PRO   A CG   1 
ATOM   2566 C CD   A PRO   A 1 125 ? 20.165 -3.591  4.785   0.58 11.57 ?  125 PRO   A CD   1 
ATOM   2567 C CD   B PRO   A 1 125 ? 20.415 -3.897  4.808   0.42 9.90  ?  125 PRO   A CD   1 
ATOM   2568 H HA   A PRO   A 1 125 ? 16.995 -4.107  4.577   0.58 13.83 ?  125 PRO   A HA   1 
ATOM   2569 H HA   B PRO   A 1 125 ? 17.181 -3.965  4.832   0.42 13.10 ?  125 PRO   A HA   1 
ATOM   2570 H HB2  A PRO   A 1 125 ? 17.878 -2.677  2.686   0.58 14.48 ?  125 PRO   A HB2  1 
ATOM   2571 H HB2  B PRO   A 1 125 ? 18.116 -2.525  2.974   0.42 12.59 ?  125 PRO   A HB2  1 
ATOM   2572 H HB3  A PRO   A 1 125 ? 17.978 -2.058  4.159   0.58 14.48 ?  125 PRO   A HB3  1 
ATOM   2573 H HB3  B PRO   A 1 125 ? 18.345 -2.005  4.471   0.42 12.59 ?  125 PRO   A HB3  1 
ATOM   2574 H HG2  A PRO   A 1 125 ? 20.047 -3.377  2.726   0.58 14.39 ?  125 PRO   A HG2  1 
ATOM   2575 H HG2  B PRO   A 1 125 ? 20.211 -3.336  2.816   0.42 12.21 ?  125 PRO   A HG2  1 
ATOM   2576 H HG3  A PRO   A 1 125 ? 20.163 -1.975  3.485   0.58 14.39 ?  125 PRO   A HG3  1 
ATOM   2577 H HG3  B PRO   A 1 125 ? 20.496 -2.094  3.775   0.42 12.21 ?  125 PRO   A HG3  1 
ATOM   2578 H HD2  A PRO   A 1 125 ? 20.896 -4.205  4.624   0.58 13.85 ?  125 PRO   A HD2  1 
ATOM   2579 H HD2  B PRO   A 1 125 ? 20.973 -4.613  4.459   0.42 11.86 ?  125 PRO   A HD2  1 
ATOM   2580 H HD3  A PRO   A 1 125 ? 20.384 -2.952  5.484   0.58 13.85 ?  125 PRO   A HD3  1 
ATOM   2581 H HD3  B PRO   A 1 125 ? 20.868 -3.411  5.515   0.42 11.86 ?  125 PRO   A HD3  1 
ATOM   2582 N N    A LEU   A 1 126 ? 16.929 -5.237  2.242   0.58 11.27 ?  126 LEU   A N    1 
ATOM   2583 N N    B LEU   A 1 126 ? 16.915 -4.993  2.444   0.42 13.08 ?  126 LEU   A N    1 
ATOM   2584 C CA   A LEU   A 1 126 ? 16.957 -6.055  1.039   0.58 11.34 ?  126 LEU   A CA   1 
ATOM   2585 C CA   B LEU   A 1 126 ? 16.866 -5.770  1.210   0.42 13.32 ?  126 LEU   A CA   1 
ATOM   2586 C C    A LEU   A 1 126 ? 17.874 -5.429  -0.007  0.58 11.25 ?  126 LEU   A C    1 
ATOM   2587 C C    B LEU   A 1 126 ? 17.839 -5.165  0.205   0.42 13.29 ?  126 LEU   A C    1 
ATOM   2588 O O    A LEU   A 1 126 ? 17.603 -4.341  -0.529  0.58 11.34 ?  126 LEU   A O    1 
ATOM   2589 O O    B LEU   A 1 126 ? 17.738 -3.981  -0.125  0.42 14.30 ?  126 LEU   A O    1 
ATOM   2590 C CB   A LEU   A 1 126 ? 15.545 -6.220  0.494   0.58 11.47 ?  126 LEU   A CB   1 
ATOM   2591 C CB   B LEU   A 1 126 ? 15.455 -5.758  0.628   0.42 14.84 ?  126 LEU   A CB   1 
ATOM   2592 C CG   A LEU   A 1 126 ? 14.646 -7.124  1.335   0.58 12.09 ?  126 LEU   A CG   1 
ATOM   2593 C CG   B LEU   A 1 126 ? 14.493 -6.908  0.926   0.42 16.19 ?  126 LEU   A CG   1 
ATOM   2594 C CD1  A LEU   A 1 126 ? 13.214 -6.996  0.865   0.58 12.53 ?  126 LEU   A CD1  1 
ATOM   2595 C CD1  B LEU   A 1 126 ? 13.226 -6.725  0.109   0.42 16.83 ?  126 LEU   A CD1  1 
ATOM   2596 C CD2  A LEU   A 1 126 ? 15.106 -8.570  1.249   0.58 11.67 ?  126 LEU   A CD2  1 
ATOM   2597 C CD2  B LEU   A 1 126 ? 15.119 -8.261  0.628   0.42 16.61 ?  126 LEU   A CD2  1 
ATOM   2598 H H    A LEU   A 1 126 ? 16.204 -4.791  2.340   0.58 13.49 ?  126 LEU   A H    1 
ATOM   2599 H H    B LEU   A 1 126 ? 16.224 -4.488  2.585   0.42 15.68 ?  126 LEU   A H    1 
ATOM   2600 H HA   A LEU   A 1 126 ? 17.304 -6.936  1.250   0.58 13.59 ?  126 LEU   A HA   1 
ATOM   2601 H HA   B LEU   A 1 126 ? 17.132 -6.683  1.397   0.42 15.96 ?  126 LEU   A HA   1 
ATOM   2602 H HB2  A LEU   A 1 126 ? 15.121 -5.350  0.452   0.58 13.74 ?  126 LEU   A HB2  1 
ATOM   2603 H HB2  B LEU   A 1 126 ? 15.020 -4.948  0.935   0.42 17.78 ?  126 LEU   A HB2  1 
ATOM   2604 H HB3  A LEU   A 1 126 ? 15.591 -6.605  -0.396  0.58 13.74 ?  126 LEU   A HB3  1 
ATOM   2605 H HB3  B LEU   A 1 126 ? 15.545 -5.718  -0.335  0.42 17.78 ?  126 LEU   A HB3  1 
ATOM   2606 H HG   A LEU   A 1 126 ? 14.686 -6.850  2.265   0.58 14.49 ?  126 LEU   A HG   1 
ATOM   2607 H HG   B LEU   A 1 126 ? 14.251 -6.885  1.864   0.42 19.41 ?  126 LEU   A HG   1 
ATOM   2608 H HD11 A LEU   A 1 126 ? 12.651 -7.579  1.399   0.58 15.01 ?  126 LEU   A HD11 1 
ATOM   2609 H HD11 B LEU   A 1 126 ? 12.613 -7.450  0.308   0.42 20.17 ?  126 LEU   A HD11 1 
ATOM   2610 H HD12 A LEU   A 1 126 ? 12.931 -6.076  0.967   0.58 15.01 ?  126 LEU   A HD12 1 
ATOM   2611 H HD12 B LEU   A 1 126 ? 12.819 -5.875  0.339   0.42 20.17 ?  126 LEU   A HD12 1 
ATOM   2612 H HD13 A LEU   A 1 126 ? 13.166 -7.257  -0.069  0.58 15.01 ?  126 LEU   A HD13 1 
ATOM   2613 H HD13 B LEU   A 1 126 ? 13.454 -6.737  -0.836  0.42 20.17 ?  126 LEU   A HD13 1 
ATOM   2614 H HD21 A LEU   A 1 126 ? 14.441 -9.143  1.660   0.58 13.98 ?  126 LEU   A HD21 1 
ATOM   2615 H HD21 B LEU   A 1 126 ? 14.425 -8.935  0.625   0.42 19.91 ?  126 LEU   A HD21 1 
ATOM   2616 H HD22 A LEU   A 1 126 ? 15.220 -8.810  0.315   0.58 13.98 ?  126 LEU   A HD22 1 
ATOM   2617 H HD22 B LEU   A 1 126 ? 15.549 -8.223  -0.242  0.42 19.91 ?  126 LEU   A HD22 1 
ATOM   2618 H HD23 A LEU   A 1 126 ? 15.954 -8.661  1.716   0.58 13.98 ?  126 LEU   A HD23 1 
ATOM   2619 H HD23 B LEU   A 1 126 ? 15.776 -8.462  1.312   0.42 19.91 ?  126 LEU   A HD23 1 
ATOM   2620 N N    A LEU   A 1 127 ? 18.954 -6.135  -0.325  0.58 11.48 ?  127 LEU   A N    1 
ATOM   2621 N N    B LEU   A 1 127 ? 18.788 -5.959  -0.280  0.42 12.78 ?  127 LEU   A N    1 
ATOM   2622 C CA   A LEU   A 1 127 ? 19.940 -5.634  -1.270  0.58 11.49 ?  127 LEU   A CA   1 
ATOM   2623 C CA   B LEU   A 1 127 ? 19.787 -5.426  -1.198  0.42 13.06 ?  127 LEU   A CA   1 
ATOM   2624 C C    A LEU   A 1 127 ? 19.324 -5.455  -2.647  0.58 11.11 ?  127 LEU   A C    1 
ATOM   2625 C C    B LEU   A 1 127 ? 19.230 -5.293  -2.611  0.42 13.64 ?  127 LEU   A C    1 
ATOM   2626 O O    A LEU   A 1 127 ? 18.513 -6.267  -3.100  0.58 11.48 ?  127 LEU   A O    1 
ATOM   2627 O O    B LEU   A 1 127 ? 18.352 -6.049  -3.040  0.42 13.91 ?  127 LEU   A O    1 
ATOM   2628 C CB   A LEU   A 1 127 ? 21.105 -6.616  -1.367  0.58 12.23 ?  127 LEU   A CB   1 
ATOM   2629 C CB   B LEU   A 1 127 ? 21.041 -6.303  -1.226  0.42 12.97 ?  127 LEU   A CB   1 
ATOM   2630 C CG   A LEU   A 1 127 ? 21.871 -6.887  -0.077  0.58 12.81 ?  127 LEU   A CG   1 
ATOM   2631 C CG   B LEU   A 1 127 ? 21.853 -6.371  0.074   0.42 13.06 ?  127 LEU   A CG   1 
ATOM   2632 C CD1  A LEU   A 1 127 ? 22.950 -7.905  -0.355  0.58 12.79 ?  127 LEU   A CD1  1 
ATOM   2633 C CD1  B LEU   A 1 127 ? 23.025 -7.340  -0.052  0.42 13.43 ?  127 LEU   A CD1  1 
ATOM   2634 C CD2  A LEU   A 1 127 ? 22.486 -5.613  0.447   0.58 13.76 ?  127 LEU   A CD2  1 
ATOM   2635 C CD2  B LEU   A 1 127 ? 22.348 -4.989  0.493   0.42 13.53 ?  127 LEU   A CD2  1 
ATOM   2636 H H    A LEU   A 1 127 ? 19.140 -6.911  0.001   0.58 13.75 ?  127 LEU   A H    1 
ATOM   2637 H H    B LEU   A 1 127 ? 18.882 -6.793  -0.083  0.42 15.32 ?  127 LEU   A H    1 
ATOM   2638 H HA   A LEU   A 1 127 ? 20.280 -4.779  -0.968  0.58 13.77 ?  127 LEU   A HA   1 
ATOM   2639 H HA   B LEU   A 1 127 ? 20.044 -4.543  -0.892  0.42 15.65 ?  127 LEU   A HA   1 
ATOM   2640 H HB2  A LEU   A 1 127 ? 20.758 -7.466  -1.682  0.58 14.65 ?  127 LEU   A HB2  1 
ATOM   2641 H HB2  B LEU   A 1 127 ? 20.773 -7.207  -1.451  0.42 15.54 ?  127 LEU   A HB2  1 
ATOM   2642 H HB3  A LEU   A 1 127 ? 21.742 -6.270  -2.009  0.58 14.65 ?  127 LEU   A HB3  1 
ATOM   2643 H HB3  B LEU   A 1 127 ? 21.628 -5.960  -1.919  0.42 15.54 ?  127 LEU   A HB3  1 
ATOM   2644 H HG   A LEU   A 1 127 ? 21.265 -7.252  0.595   0.58 15.35 ?  127 LEU   A HG   1 
ATOM   2645 H HG   B LEU   A 1 127 ? 21.275 -6.701  0.777   0.42 15.65 ?  127 LEU   A HG   1 
ATOM   2646 H HD11 A LEU   A 1 127 ? 23.408 -8.115  0.473   0.58 15.32 ?  127 LEU   A HD11 1 
ATOM   2647 H HD11 B LEU   A 1 127 ? 23.522 -7.340  0.782   0.42 16.09 ?  127 LEU   A HD11 1 
ATOM   2648 H HD12 A LEU   A 1 127 ? 22.542 -8.709  -0.720  0.58 15.32 ?  127 LEU   A HD12 1 
ATOM   2649 H HD12 B LEU   A 1 127 ? 22.680 -8.229  -0.231  0.42 16.09 ?  127 LEU   A HD12 1 
ATOM   2650 H HD13 A LEU   A 1 127 ? 23.572 -7.532  -0.996  0.58 15.32 ?  127 LEU   A HD13 1 
ATOM   2651 H HD13 B LEU   A 1 127 ? 23.597 -7.052  -0.779  0.42 16.09 ?  127 LEU   A HD13 1 
ATOM   2652 H HD21 A LEU   A 1 127 ? 23.072 -5.828  1.186   0.58 16.49 ?  127 LEU   A HD21 1 
ATOM   2653 H HD21 B LEU   A 1 127 ? 22.964 -5.089  1.235   0.42 16.21 ?  127 LEU   A HD21 1 
ATOM   2654 H HD22 A LEU   A 1 127 ? 22.992 -5.197  -0.269  0.58 16.49 ?  127 LEU   A HD22 1 
ATOM   2655 H HD22 B LEU   A 1 127 ? 22.798 -4.573  -0.258  0.42 16.21 ?  127 LEU   A HD22 1 
ATOM   2656 H HD23 A LEU   A 1 127 ? 21.779 -5.020  0.741   0.58 16.49 ?  127 LEU   A HD23 1 
ATOM   2657 H HD23 B LEU   A 1 127 ? 21.587 -4.451  0.764   0.42 16.21 ?  127 LEU   A HD23 1 
ATOM   2658 N N    A SER   A 1 128 ? 19.725 -4.381  -3.316  0.58 11.09 ?  128 SER   A N    1 
ATOM   2659 N N    B SER   A 1 128 ? 19.756 -4.304  -3.329  0.42 14.10 ?  128 SER   A N    1 
ATOM   2660 C CA   A SER   A 1 128 ? 19.307 -4.008  -4.658  0.58 11.31 ?  128 SER   A CA   1 
ATOM   2661 C CA   B SER   A 1 128 ? 19.462 -4.000  -4.727  0.42 14.61 ?  128 SER   A CA   1 
ATOM   2662 C C    A SER   A 1 128 ? 17.851 -3.569  -4.743  0.58 10.66 ?  128 SER   A C    1 
ATOM   2663 C C    B SER   A 1 128 ? 18.047 -3.488  -4.970  0.42 16.15 ?  128 SER   A C    1 
ATOM   2664 O O    A SER   A 1 128 ? 17.393 -3.245  -5.841  0.58 12.24 ?  128 SER   A O    1 
ATOM   2665 O O    B SER   A 1 128 ? 17.664 -3.301  -6.131  0.42 16.05 ?  128 SER   A O    1 
ATOM   2666 C CB   A SER   A 1 128 ? 19.632 -5.071  -5.719  0.58 11.71 ?  128 SER   A CB   1 
ATOM   2667 C CB   B SER   A 1 128 ? 19.811 -5.147  -5.682  0.42 13.64 ?  128 SER   A CB   1 
ATOM   2668 O OG   A SER   A 1 128 ? 21.036 -5.280  -5.788  0.58 12.23 ?  128 SER   A OG   1 
ATOM   2669 O OG   B SER   A 1 128 ? 21.220 -5.293  -5.783  0.42 13.27 ?  128 SER   A OG   1 
ATOM   2670 H H    A SER   A 1 128 ? 20.284 -3.821  -2.988  0.58 13.29 ?  128 SER   A H    1 
ATOM   2671 H H    B SER   A 1 128 ? 20.335 -3.763  -3.000  0.42 16.90 ?  128 SER   A H    1 
ATOM   2672 H HA   A SER   A 1 128 ? 19.813 -3.232  -4.896  0.58 13.55 ?  128 SER   A HA   1 
ATOM   2673 H HA   B SER   A 1 128 ? 20.038 -3.269  -4.972  0.42 17.50 ?  128 SER   A HA   1 
ATOM   2674 H HB2  A SER   A 1 128 ? 19.187 -5.902  -5.489  0.58 14.03 ?  128 SER   A HB2  1 
ATOM   2675 H HB2  B SER   A 1 128 ? 19.422 -5.968  -5.347  0.42 16.35 ?  128 SER   A HB2  1 
ATOM   2676 H HB3  A SER   A 1 128 ? 19.316 -4.755  -6.585  0.58 14.03 ?  128 SER   A HB3  1 
ATOM   2677 H HB3  B SER   A 1 128 ? 19.448 -4.942  -6.562  0.42 16.35 ?  128 SER   A HB3  1 
ATOM   2678 H HG   A SER   A 1 128 ? 21.413 -4.550  -5.960  0.58 14.65 ?  128 SER   A HG   1 
ATOM   2679 H HG   B SER   A 1 128 ? 21.554 -4.573  -6.059  0.42 15.90 ?  128 SER   A HG   1 
ATOM   2680 N N    A ALA   A 1 129 ? 17.122 -3.513  -3.629  0.58 10.39 ?  129 ALA   A N    1 
ATOM   2681 N N    B ALA   A 1 129 ? 17.268 -3.237  -3.921  0.42 18.03 ?  129 ALA   A N    1 
ATOM   2682 C CA   A ALA   A 1 129 ? 15.753 -3.018  -3.650  0.58 10.62 ?  129 ALA   A CA   1 
ATOM   2683 C CA   B ALA   A 1 129 ? 16.005 -2.534  -4.083  0.42 20.04 ?  129 ALA   A CA   1 
ATOM   2684 C C    A ALA   A 1 129 ? 15.742 -1.486  -3.596  0.58 10.43 ?  129 ALA   A C    1 
ATOM   2685 C C    B ALA   A 1 129 ? 16.267 -1.039  -4.296  0.42 21.47 ?  129 ALA   A C    1 
ATOM   2686 O O    A ALA   A 1 129 ? 16.784 -0.825  -3.616  0.58 10.52 ?  129 ALA   A O    1 
ATOM   2687 O O    B ALA   A 1 129 ? 17.406 -0.566  -4.261  0.42 22.07 ?  129 ALA   A O    1 
ATOM   2688 C CB   A ALA   A 1 129 ? 14.947 -3.635  -2.504  0.58 12.06 ?  129 ALA   A CB   1 
ATOM   2689 C CB   B ALA   A 1 129 ? 15.096 -2.788  -2.881  0.42 20.66 ?  129 ALA   A CB   1 
ATOM   2690 H H    A ALA   A 1 129 ? 17.390 -3.758  -2.842  0.58 12.44 ?  129 ALA   A H    1 
ATOM   2691 H H    B ALA   A 1 129 ? 17.441 -3.472  -3.109  0.42 21.61 ?  129 ALA   A H    1 
ATOM   2692 H HA   A ALA   A 1 129 ? 15.329 -3.288  -4.472  0.58 12.72 ?  129 ALA   A HA   1 
ATOM   2693 H HA   B ALA   A 1 129 ? 15.552 -2.872  -4.870  0.42 24.02 ?  129 ALA   A HA   1 
ATOM   2694 H HB1  A ALA   A 1 129 ? 14.031 -3.301  -2.535  0.58 14.45 ?  129 ALA   A HB1  1 
ATOM   2695 H HB1  B ALA   A 1 129 ? 14.260 -2.311  -3.009  0.42 24.77 ?  129 ALA   A HB1  1 
ATOM   2696 H HB2  A ALA   A 1 129 ? 14.943 -4.600  -2.595  0.58 14.45 ?  129 ALA   A HB2  1 
ATOM   2697 H HB2  B ALA   A 1 129 ? 14.923 -3.741  -2.811  0.42 24.77 ?  129 ALA   A HB2  1 
ATOM   2698 H HB3  A ALA   A 1 129 ? 15.350 -3.388  -1.653  0.58 14.45 ?  129 ALA   A HB3  1 
ATOM   2699 H HB3  B ALA   A 1 129 ? 15.537 -2.473  -2.077  0.42 24.77 ?  129 ALA   A HB3  1 
ATOM   2700 N N    A GLY   A 1 130 ? 14.544 -0.915  -3.531  0.58 10.90 ?  130 GLY   A N    1 
ATOM   2701 N N    B GLY   A 1 130 ? 15.197 -0.284  -4.520  0.42 22.71 ?  130 GLY   A N    1 
ATOM   2702 C CA   A GLY   A 1 130 ? 14.431 0.533   -3.469  0.58 12.03 ?  130 GLY   A CA   1 
ATOM   2703 C CA   B GLY   A 1 130 ? 15.323 1.155   -4.719  0.42 23.52 ?  130 GLY   A CA   1 
ATOM   2704 C C    A GLY   A 1 130 ? 15.041 1.176   -4.698  0.58 11.97 ?  130 GLY   A C    1 
ATOM   2705 C C    B GLY   A 1 130 ? 15.985 1.518   -6.035  0.42 24.02 ?  130 GLY   A C    1 
ATOM   2706 O O    A GLY   A 1 130 ? 14.822 0.735   -5.831  0.58 11.28 ?  130 GLY   A O    1 
ATOM   2707 O O    B GLY   A 1 130 ? 15.651 0.969   -7.091  0.42 23.77 ?  130 GLY   A O    1 
ATOM   2708 H H    A GLY   A 1 130 ? 13.791 -1.340  -3.523  0.58 13.06 ?  130 GLY   A H    1 
ATOM   2709 H H    B GLY   A 1 130 ? 14.394 -0.569  -4.536  0.42 27.23 ?  130 GLY   A H    1 
ATOM   2710 H HA2  A GLY   A 1 130 ? 13.490 0.783   -3.412  0.58 14.42 ?  130 GLY   A HA2  1 
ATOM   2711 H HA2  B GLY   A 1 130 ? 14.436 1.550   -4.699  0.42 28.20 ?  130 GLY   A HA2  1 
ATOM   2712 H HA3  A GLY   A 1 130 ? 14.888 0.864   -2.686  0.58 14.42 ?  130 GLY   A HA3  1 
ATOM   2713 H HA3  B GLY   A 1 130 ? 15.848 1.540   -4.016  0.42 28.20 ?  130 GLY   A HA3  1 
ATOM   2714 N N    A ILE   A 1 131 ? 15.837 2.227   -4.474  0.58 11.89 ?  131 ILE   A N    1 
ATOM   2715 N N    B ILE   A 1 131 ? 16.936 2.461   -5.982  0.42 24.79 ?  131 ILE   A N    1 
ATOM   2716 C CA   A ILE   A 1 131 ? 16.405 3.002   -5.576  0.58 11.88 ?  131 ILE   A CA   1 
ATOM   2717 C CA   B ILE   A 1 131 ? 17.519 2.995   -7.212  0.42 25.59 ?  131 ILE   A CA   1 
ATOM   2718 C C    A ILE   A 1 131 ? 17.455 2.240   -6.374  0.58 11.20 ?  131 ILE   A C    1 
ATOM   2719 C C    B ILE   A 1 131 ? 18.150 1.886   -8.038  0.42 25.18 ?  131 ILE   A C    1 
ATOM   2720 O O    A ILE   A 1 131 ? 17.887 2.735   -7.420  0.58 11.80 ?  131 ILE   A O    1 
ATOM   2721 O O    B ILE   A 1 131 ? 18.197 1.969   -9.271  0.42 25.51 ?  131 ILE   A O    1 
ATOM   2722 C CB   A ILE   A 1 131 ? 16.943 4.377   -5.123  0.58 13.35 ?  131 ILE   A CB   1 
ATOM   2723 C CB   B ILE   A 1 131 ? 18.516 4.139   -6.919  0.42 26.82 ?  131 ILE   A CB   1 
ATOM   2724 C CG1  A ILE   A 1 131 ? 18.189 4.221   -4.243  0.58 14.67 ?  131 ILE   A CG1  1 
ATOM   2725 C CG1  B ILE   A 1 131 ? 19.679 3.632   -6.063  0.42 27.50 ?  131 ILE   A CG1  1 
ATOM   2726 C CG2  A ILE   A 1 131 ? 15.848 5.167   -4.411  0.58 14.27 ?  131 ILE   A CG2  1 
ATOM   2727 C CG2  B ILE   A 1 131 ? 17.805 5.311   -6.249  0.42 27.16 ?  131 ILE   A CG2  1 
ATOM   2728 C CD1  A ILE   A 1 131 ? 18.844 5.550   -3.876  0.58 16.07 ?  131 ILE   A CD1  1 
ATOM   2729 C CD1  B ILE   A 1 131 ? 20.881 4.538   -6.062  0.42 27.85 ?  131 ILE   A CD1  1 
ATOM   2730 H H    A ILE   A 1 131 ? 16.041 2.515   -3.695  0.58 14.24 ?  131 ILE   A H    1 
ATOM   2731 H H    B ILE   A 1 131 ? 17.273 2.792   -5.259  0.42 29.73 ?  131 ILE   A H    1 
ATOM   2732 H HA   A ILE   A 1 131 ? 15.690 3.178   -6.202  0.58 14.23 ?  131 ILE   A HA   1 
ATOM   2733 H HA   B ILE   A 1 131 ? 16.814 3.379   -7.749  0.42 30.69 ?  131 ILE   A HA   1 
ATOM   2734 H HB   A ILE   A 1 131 ? 17.193 4.867   -5.919  0.58 15.99 ?  131 ILE   A HB   1 
ATOM   2735 H HB   B ILE   A 1 131 ? 18.877 4.461   -7.760  0.42 32.16 ?  131 ILE   A HB   1 
ATOM   2736 H HG12 A ILE   A 1 131 ? 17.938 3.774   -3.423  0.58 17.58 ?  131 ILE   A HG12 1 
ATOM   2737 H HG12 B ILE   A 1 131 ? 19.375 3.544   -5.149  0.42 32.98 ?  131 ILE   A HG12 1 
ATOM   2738 H HG13 A ILE   A 1 131 ? 18.849 3.694   -4.719  0.58 17.58 ?  131 ILE   A HG13 1 
ATOM   2739 H HG13 B ILE   A 1 131 ? 19.968 2.773   -6.399  0.42 32.98 ?  131 ILE   A HG13 1 
ATOM   2740 H HG21 A ILE   A 1 131 ? 16.158 6.073   -4.268  0.58 17.10 ?  131 ILE   A HG21 1 
ATOM   2741 H HG21 B ILE   A 1 131 ? 18.438 6.036   -6.117  0.42 32.57 ?  131 ILE   A HG21 1 
ATOM   2742 H HG22 A ILE   A 1 131 ? 15.051 5.174   -4.967  0.58 17.10 ?  131 ILE   A HG22 1 
ATOM   2743 H HG22 B ILE   A 1 131 ? 17.081 5.609   -6.824  0.42 32.57 ?  131 ILE   A HG22 1 
ATOM   2744 H HG23 A ILE   A 1 131 ? 15.652 4.742   -3.561  0.58 17.10 ?  131 ILE   A HG23 1 
ATOM   2745 H HG23 B ILE   A 1 131 ? 17.452 5.020   -5.395  0.42 32.57 ?  131 ILE   A HG23 1 
ATOM   2746 H HD11 A ILE   A 1 131 ? 19.677 5.372   -3.411  0.58 19.26 ?  131 ILE   A HD11 1 
ATOM   2747 H HD11 B ILE   A 1 131 ? 21.578 4.129   -5.524  0.42 33.40 ?  131 ILE   A HD11 1 
ATOM   2748 H HD12 A ILE   A 1 131 ? 19.021 6.053   -4.687  0.58 19.26 ?  131 ILE   A HD12 1 
ATOM   2749 H HD12 B ILE   A 1 131 ? 21.191 4.651   -6.974  0.42 33.40 ?  131 ILE   A HD12 1 
ATOM   2750 H HD13 A ILE   A 1 131 ? 18.245 6.051   -3.301  0.58 19.26 ?  131 ILE   A HD13 1 
ATOM   2751 H HD13 B ILE   A 1 131 ? 20.631 5.394   -5.686  0.42 33.40 ?  131 ILE   A HD13 1 
ATOM   2752 N N    A PHE   A 1 132 ? 17.871 1.046   -5.924  0.58 10.91 ?  132 PHE   A N    1 
ATOM   2753 N N    B PHE   A 1 132 ? 18.638 0.829   -7.384  0.42 24.61 ?  132 PHE   A N    1 
ATOM   2754 C CA   A PHE   A 1 132 ? 18.750 0.214   -6.738  0.58 10.89 ?  132 PHE   A CA   1 
ATOM   2755 C CA   B PHE   A 1 132 ? 19.280 -0.253  -8.119  0.42 24.05 ?  132 PHE   A CA   1 
ATOM   2756 C C    A PHE   A 1 132 ? 17.999 -0.543  -7.831  0.58 11.88 ?  132 PHE   A C    1 
ATOM   2757 C C    B PHE   A 1 132 ? 18.300 -1.085  -8.930  0.42 23.20 ?  132 PHE   A C    1 
ATOM   2758 O O    A PHE   A 1 132 ? 18.638 -1.163  -8.686  0.58 12.45 ?  132 PHE   A O    1 
ATOM   2759 O O    B PHE   A 1 132 ? 18.739 -1.841  -9.802  0.42 23.06 ?  132 PHE   A O    1 
ATOM   2760 C CB   A PHE   A 1 132 ? 19.552 -0.765  -5.867  0.58 10.64 ?  132 PHE   A CB   1 
ATOM   2761 C CB   B PHE   A 1 132 ? 20.130 -1.120  -7.188  0.42 24.54 ?  132 PHE   A CB   1 
ATOM   2762 C CG   A PHE   A 1 132 ? 20.777 -0.161  -5.203  0.58 10.57 ?  132 PHE   A CG   1 
ATOM   2763 C CG   B PHE   A 1 132 ? 21.409 -0.455  -6.747  0.42 25.39 ?  132 PHE   A CG   1 
ATOM   2764 C CD1  A PHE   A 1 132 ? 20.662 0.876   -4.294  0.58 11.55 ?  132 PHE   A CD1  1 
ATOM   2765 C CD1  B PHE   A 1 132 ? 21.760 0.801   -7.227  0.42 25.88 ?  132 PHE   A CD1  1 
ATOM   2766 C CD2  A PHE   A 1 132 ? 22.033 -0.686  -5.446  0.58 11.25 ?  132 PHE   A CD2  1 
ATOM   2767 C CD2  B PHE   A 1 132 ? 22.261 -1.087  -5.862  0.42 25.48 ?  132 PHE   A CD2  1 
ATOM   2768 C CE1  A PHE   A 1 132 ? 21.790 1.403   -3.672  0.58 11.73 ?  132 PHE   A CE1  1 
ATOM   2769 C CE1  B PHE   A 1 132 ? 22.926 1.409   -6.830  0.42 26.01 ?  132 PHE   A CE1  1 
ATOM   2770 C CE2  A PHE   A 1 132 ? 23.158 -0.168  -4.827  0.58 11.84 ?  132 PHE   A CE2  1 
ATOM   2771 C CE2  B PHE   A 1 132 ? 23.432 -0.481  -5.459  0.42 25.69 ?  132 PHE   A CE2  1 
ATOM   2772 C CZ   A PHE   A 1 132 ? 23.035 0.873   -3.939  0.58 11.64 ?  132 PHE   A CZ   1 
ATOM   2773 C CZ   B PHE   A 1 132 ? 23.765 0.769   -5.944  0.42 25.82 ?  132 PHE   A CZ   1 
ATOM   2774 H H    A PHE   A 1 132 ? 17.662 0.697   -5.158  0.58 13.07 ?  132 PHE   A H    1 
ATOM   2775 H H    B PHE   A 1 132 ? 18.611 0.723   -6.530  0.42 29.50 ?  132 PHE   A H    1 
ATOM   2776 H HA   A PHE   A 1 132 ? 19.395 0.791   -7.171  0.58 13.04 ?  132 PHE   A HA   1 
ATOM   2777 H HA   B PHE   A 1 132 ? 19.870 0.139   -8.771  0.42 28.83 ?  132 PHE   A HA   1 
ATOM   2778 H HB2  A PHE   A 1 132 ? 18.977 -1.104  -5.164  0.58 12.74 ?  132 PHE   A HB2  1 
ATOM   2779 H HB2  B PHE   A 1 132 ? 19.617 -1.324  -6.392  0.42 29.42 ?  132 PHE   A HB2  1 
ATOM   2780 H HB3  A PHE   A 1 132 ? 19.858 -1.501  -6.422  0.58 12.74 ?  132 PHE   A HB3  1 
ATOM   2781 H HB3  B PHE   A 1 132 ? 20.364 -1.943  -7.648  0.42 29.42 ?  132 PHE   A HB3  1 
ATOM   2782 H HD1  A PHE   A 1 132 ? 19.827 1.237   -4.103  0.58 13.84 ?  132 PHE   A HD1  1 
ATOM   2783 H HD1  B PHE   A 1 132 ? 21.199 1.240   -7.828  0.42 31.03 ?  132 PHE   A HD1  1 
ATOM   2784 H HD2  A PHE   A 1 132 ? 22.129 -1.389  -6.042  0.58 13.48 ?  132 PHE   A HD2  1 
ATOM   2785 H HD2  B PHE   A 1 132 ? 22.041 -1.928  -5.534  0.42 30.56 ?  132 PHE   A HD2  1 
ATOM   2786 H HE1  A PHE   A 1 132 ? 21.709 2.110   -3.067  0.58 14.05 ?  132 PHE   A HE1  1 
ATOM   2787 H HE1  B PHE   A 1 132 ? 23.144 2.251   -7.161  0.42 31.19 ?  132 PHE   A HE1  1 
ATOM   2788 H HE2  A PHE   A 1 132 ? 23.996 -0.523  -5.013  0.58 14.18 ?  132 PHE   A HE2  1 
ATOM   2789 H HE2  B PHE   A 1 132 ? 23.997 -0.914  -4.862  0.42 30.81 ?  132 PHE   A HE2  1 
ATOM   2790 H HZ   A PHE   A 1 132 ? 23.792 1.228   -3.526  0.58 13.94 ?  132 PHE   A HZ   1 
ATOM   2791 H HZ   B PHE   A 1 132 ? 24.552 1.178   -5.674  0.42 30.96 ?  132 PHE   A HZ   1 
ATOM   2792 N N    A GLY   A 1 133 ? 16.668 -0.513  -7.823  0.58 11.79 ?  133 GLY   A N    1 
ATOM   2793 N N    B GLY   A 1 133 ? 17.000 -0.969  -8.676  0.42 22.77 ?  133 GLY   A N    1 
ATOM   2794 C CA   A GLY   A 1 133 ? 15.883 -0.856  -8.991  0.58 12.86 ?  133 GLY   A CA   1 
ATOM   2795 C CA   B GLY   A 1 133 ? 16.034 -1.417  -9.656  0.42 22.32 ?  133 GLY   A CA   1 
ATOM   2796 C C    A GLY   A 1 133 ? 15.521 -2.314  -9.183  0.58 13.26 ?  133 GLY   A C    1 
ATOM   2797 C C    B GLY   A 1 133 ? 15.779 -2.904  -9.709  0.42 22.00 ?  133 GLY   A C    1 
ATOM   2798 O O    A GLY   A 1 133 ? 14.851 -2.630  -10.175 0.58 14.16 ?  133 GLY   A O    1 
ATOM   2799 O O    B GLY   A 1 133 ? 15.195 -3.379  -10.688 0.42 22.76 ?  133 GLY   A O    1 
ATOM   2800 H H    A GLY   A 1 133 ? 16.194 -0.285  -7.143  0.58 14.12 ?  133 GLY   A H    1 
ATOM   2801 H H    B GLY   A 1 133 ? 16.660 -0.652  -7.947  0.42 27.30 ?  133 GLY   A H    1 
ATOM   2802 H HA2  A GLY   A 1 133 ? 15.049 -0.360  -8.956  0.58 15.41 ?  133 GLY   A HA2  1 
ATOM   2803 H HA2  B GLY   A 1 133 ? 15.192 -0.981  -9.485  0.42 26.76 ?  133 GLY   A HA2  1 
ATOM   2804 H HA3  A GLY   A 1 133 ? 16.361 -0.571  -9.785  0.58 15.41 ?  133 GLY   A HA3  1 
ATOM   2805 H HA3  B GLY   A 1 133 ? 16.345 -1.139  -10.534 0.42 26.76 ?  133 GLY   A HA3  1 
ATOM   2806 N N    A ALA   A 1 134 ? 15.921 -3.212  -8.284  0.58 13.43 ?  134 ALA   A N    1 
ATOM   2807 N N    B ALA   A 1 134 ? 16.193 -3.659  -8.699  0.42 21.03 ?  134 ALA   A N    1 
ATOM   2808 C CA   A ALA   A 1 134 ? 15.560 -4.612  -8.452  0.58 14.10 ?  134 ALA   A CA   1 
ATOM   2809 C CA   B ALA   A 1 134 ? 15.889 -5.080  -8.648  0.42 20.26 ?  134 ALA   A CA   1 
ATOM   2810 C C    A ALA   A 1 134 ? 14.206 -4.915  -7.806  0.58 14.65 ?  134 ALA   A C    1 
ATOM   2811 C C    B ALA   A 1 134 ? 14.530 -5.292  -7.992  0.42 20.33 ?  134 ALA   A C    1 
ATOM   2812 O O    A ALA   A 1 134 ? 13.652 -4.117  -7.048  0.58 15.37 ?  134 ALA   A O    1 
ATOM   2813 O O    B ALA   A 1 134 ? 14.127 -4.543  -7.098  0.42 20.70 ?  134 ALA   A O    1 
ATOM   2814 C CB   A ALA   A 1 134 ? 16.636 -5.531  -7.880  0.58 14.60 ?  134 ALA   A CB   1 
ATOM   2815 C CB   B ALA   A 1 134 ? 16.967 -5.840  -7.874  0.42 20.15 ?  134 ALA   A CB   1 
ATOM   2816 H H    A ALA   A 1 134 ? 16.393 -3.034  -7.584  0.58 16.09 ?  134 ALA   A H    1 
ATOM   2817 H H    B ALA   A 1 134 ? 16.653 -3.373  -8.031  0.42 25.21 ?  134 ALA   A H    1 
ATOM   2818 H HA   A ALA   A 1 134 ? 15.484 -4.797  -9.400  0.58 16.89 ?  134 ALA   A HA   1 
ATOM   2819 H HA   B ALA   A 1 134 ? 15.855 -5.438  -9.549  0.42 24.29 ?  134 ALA   A HA   1 
ATOM   2820 H HB1  A ALA   A 1 134 ? 16.371 -6.449  -8.033  0.58 17.50 ?  134 ALA   A HB1  1 
ATOM   2821 H HB1  B ALA   A 1 134 ? 16.748 -6.785  -7.872  0.42 24.16 ?  134 ALA   A HB1  1 
ATOM   2822 H HB2  A ALA   A 1 134 ? 17.474 -5.344  -8.329  0.58 17.50 ?  134 ALA   A HB2  1 
ATOM   2823 H HB2  B ALA   A 1 134 ? 17.825 -5.702  -8.309  0.42 24.16 ?  134 ALA   A HB2  1 
ATOM   2824 H HB3  A ALA   A 1 134 ? 16.721 -5.360  -6.931  0.58 17.50 ?  134 ALA   A HB3  1 
ATOM   2825 H HB3  B ALA   A 1 134 ? 17.001 -5.506  -6.965  0.42 24.16 ?  134 ALA   A HB3  1 
ATOM   2826 N N    A ASP   A 1 135 ? 13.681 -6.094  -8.127  0.58 15.33 ?  135 ASP   A N    1 
ATOM   2827 N N    B ASP   A 1 135 ? 13.819 -6.309  -8.456  0.42 20.06 ?  135 ASP   A N    1 
ATOM   2828 C CA   A ASP   A 1 135 ? 12.433 -6.597  -7.553  0.58 16.24 ?  135 ASP   A CA   1 
ATOM   2829 C CA   B ASP   A 1 135 ? 12.511 -6.621  -7.894  0.42 20.13 ?  135 ASP   A CA   1 
ATOM   2830 C C    A ASP   A 1 135 ? 12.683 -7.023  -6.112  0.58 14.97 ?  135 ASP   A C    1 
ATOM   2831 C C    B ASP   A 1 135 ? 12.686 -7.126  -6.467  0.42 18.90 ?  135 ASP   A C    1 
ATOM   2832 O O    A ASP   A 1 135 ? 13.478 -7.944  -5.880  0.58 14.07 ?  135 ASP   A O    1 
ATOM   2833 O O    B ASP   A 1 135 ? 13.423 -8.097  -6.250  0.42 18.65 ?  135 ASP   A O    1 
ATOM   2834 C CB   A ASP   A 1 135 ? 12.002 -7.806  -8.387  0.58 18.43 ?  135 ASP   A CB   1 
ATOM   2835 C CB   B ASP   A 1 135 ? 11.822 -7.681  -8.741  0.42 21.93 ?  135 ASP   A CB   1 
ATOM   2836 C CG   A ASP   A 1 135 ? 10.729 -8.478  -7.874  0.58 20.52 ?  135 ASP   A CG   1 
ATOM   2837 C CG   B ASP   A 1 135 ? 10.382 -7.912  -8.329  0.42 23.55 ?  135 ASP   A CG   1 
ATOM   2838 O OD1  A ASP   A 1 135 ? 10.107 -7.982  -6.912  0.58 20.38 ?  135 ASP   A OD1  1 
ATOM   2839 O OD1  B ASP   A 1 135 ? 9.940  -7.303  -7.332  0.42 24.54 ?  135 ASP   A OD1  1 
ATOM   2840 O OD2  A ASP   A 1 135 ? 10.357 -9.521  -8.453  0.58 23.33 -1 135 ASP   A OD2  1 
ATOM   2841 O OD2  B ASP   A 1 135 ? 9.696  -8.713  -8.997  0.42 23.92 -1 135 ASP   A OD2  1 
ATOM   2842 H H    A ASP   A 1 135 ? 14.035 -6.633  -8.688  0.58 18.37 ?  135 ASP   A H    1 
ATOM   2843 H H    B ASP   A 1 135 ? 14.063 -6.830  -9.094  0.42 24.05 ?  135 ASP   A H    1 
ATOM   2844 H HA   A ASP   A 1 135 ? 11.742 -5.913  -7.594  0.58 19.46 ?  135 ASP   A HA   1 
ATOM   2845 H HA   B ASP   A 1 135 ? 11.965 -5.820  -7.901  0.42 24.13 ?  135 ASP   A HA   1 
ATOM   2846 H HB2  A ASP   A 1 135 ? 11.852 -7.517  -9.300  0.58 22.09 ?  135 ASP   A HB2  1 
ATOM   2847 H HB2  B ASP   A 1 135 ? 11.857 -7.409  -9.672  0.42 26.29 ?  135 ASP   A HB2  1 
ATOM   2848 H HB3  A ASP   A 1 135 ? 12.708 -8.468  -8.361  0.58 22.09 ?  135 ASP   A HB3  1 
ATOM   2849 H HB3  B ASP   A 1 135 ? 12.273 -8.525  -8.620  0.42 26.29 ?  135 ASP   A HB3  1 
ATOM   2850 N N    A PRO   A 1 136 ? 12.048 -6.393  -5.119  0.58 14.75 ?  136 PRO   A N    1 
ATOM   2851 N N    B PRO   A 1 136 ? 12.046 -6.509  -5.472  0.42 18.45 ?  136 PRO   A N    1 
ATOM   2852 C CA   A PRO   A 1 136 ? 12.292 -6.800  -3.723  0.58 14.73 ?  136 PRO   A CA   1 
ATOM   2853 C CA   B PRO   A 1 136 ? 12.301 -6.915  -4.079  0.42 17.99 ?  136 PRO   A CA   1 
ATOM   2854 C C    A PRO   A 1 136 ? 11.859 -8.227  -3.411  0.58 13.58 ?  136 PRO   A C    1 
ATOM   2855 C C    B PRO   A 1 136 ? 11.959 -8.363  -3.765  0.42 17.47 ?  136 PRO   A C    1 
ATOM   2856 O O    A PRO   A 1 136 ? 12.450 -8.861  -2.531  0.58 12.51 ?  136 PRO   A O    1 
ATOM   2857 O O    B PRO   A 1 136 ? 12.650 -8.981  -2.947  0.42 17.18 ?  136 PRO   A O    1 
ATOM   2858 C CB   A PRO   A 1 136 ? 11.517 -5.751  -2.911  0.58 15.82 ?  136 PRO   A CB   1 
ATOM   2859 C CB   B PRO   A 1 136 ? 11.463 -5.916  -3.270  0.42 18.29 ?  136 PRO   A CB   1 
ATOM   2860 C CG   A PRO   A 1 136 ? 10.464 -5.255  -3.851  0.58 15.87 ?  136 PRO   A CG   1 
ATOM   2861 C CG   B PRO   A 1 136 ? 11.351 -4.722  -4.164  0.42 18.42 ?  136 PRO   A CG   1 
ATOM   2862 C CD   A PRO   A 1 136 ? 11.064 -5.300  -5.218  0.58 15.77 ?  136 PRO   A CD   1 
ATOM   2863 C CD   B PRO   A 1 136 ? 11.263 -5.266  -5.551  0.42 18.66 ?  136 PRO   A CD   1 
ATOM   2864 H HA   A PRO   A 1 136 ? 13.237 -6.705  -3.511  0.58 17.66 ?  136 PRO   A HA   1 
ATOM   2865 H HA   B PRO   A 1 136 ? 13.235 -6.782  -3.861  0.42 21.56 ?  136 PRO   A HA   1 
ATOM   2866 H HB2  A PRO   A 1 136 ? 11.113 -6.160  -2.131  0.58 18.97 ?  136 PRO   A HB2  1 
ATOM   2867 H HB2  B PRO   A 1 136 ? 10.589 -6.293  -3.086  0.42 21.92 ?  136 PRO   A HB2  1 
ATOM   2868 H HB3  A PRO   A 1 136 ? 12.110 -5.023  -2.648  0.58 18.97 ?  136 PRO   A HB3  1 
ATOM   2869 H HB3  B PRO   A 1 136 ? 11.924 -5.690  -2.447  0.42 21.92 ?  136 PRO   A HB3  1 
ATOM   2870 H HG2  A PRO   A 1 136 ? 9.691  -5.834  -3.804  0.58 19.02 ?  136 PRO   A HG2  1 
ATOM   2871 H HG2  B PRO   A 1 136 ? 10.551 -4.222  -3.948  0.42 22.09 ?  136 PRO   A HG2  1 
ATOM   2872 H HG3  A PRO   A 1 136 ? 10.223 -4.343  -3.620  0.58 19.02 ?  136 PRO   A HG3  1 
ATOM   2873 H HG3  B PRO   A 1 136 ? 12.141 -4.166  -4.069  0.42 22.09 ?  136 PRO   A HG3  1 
ATOM   2874 H HD2  A PRO   A 1 136 ? 10.383 -5.520  -5.876  0.58 18.91 ?  136 PRO   A HD2  1 
ATOM   2875 H HD2  B PRO   A 1 136 ? 10.345 -5.466  -5.789  0.42 22.37 ?  136 PRO   A HD2  1 
ATOM   2876 H HD3  A PRO   A 1 136 ? 11.503 -4.461  -5.429  0.58 18.91 ?  136 PRO   A HD3  1 
ATOM   2877 H HD3  B PRO   A 1 136 ? 11.670 -4.648  -6.179  0.42 22.37 ?  136 PRO   A HD3  1 
ATOM   2878 N N    A ILE   A 1 137 ? 10.831 -8.745  -4.090  0.58 14.19 ?  137 ILE   A N    1 
ATOM   2879 N N    B ILE   A 1 137 ? 10.911 -8.926  -4.367  0.42 17.68 ?  137 ILE   A N    1 
ATOM   2880 C CA   A ILE   A 1 137 ? 10.452 -10.146 -3.914  0.58 14.82 ?  137 ILE   A CA   1 
ATOM   2881 C CA   B ILE   A 1 137 ? 10.591 -10.324 -4.087  0.42 18.42 ?  137 ILE   A CA   1 
ATOM   2882 C C    A ILE   A 1 137 ? 11.622 -11.054 -4.268  0.58 13.60 ?  137 ILE   A C    1 
ATOM   2883 C C    B ILE   A 1 137 ? 11.715 -11.222 -4.582  0.42 17.62 ?  137 ILE   A C    1 
ATOM   2884 O O    A ILE   A 1 137 ? 11.921 -12.024 -3.559  0.58 13.26 ?  137 ILE   A O    1 
ATOM   2885 O O    B ILE   A 1 137 ? 12.049 -12.235 -3.956  0.42 17.50 ?  137 ILE   A O    1 
ATOM   2886 C CB   A ILE   A 1 137 ? 9.203  -10.469 -4.760  0.58 16.42 ?  137 ILE   A CB   1 
ATOM   2887 C CB   B ILE   A 1 137 ? 9.228  -10.715 -4.686  0.42 20.18 ?  137 ILE   A CB   1 
ATOM   2888 C CG1  A ILE   A 1 137 ? 7.971  -9.725  -4.228  0.58 17.93 ?  137 ILE   A CG1  1 
ATOM   2889 C CG1  B ILE   A 1 137 ? 8.220  -9.570  -4.549  0.42 21.70 ?  137 ILE   A CG1  1 
ATOM   2890 C CG2  A ILE   A 1 137 ? 8.957  -11.979 -4.801  0.58 16.55 ?  137 ILE   A CG2  1 
ATOM   2891 C CG2  B ILE   A 1 137 ? 8.693  -11.966 -3.991  0.42 20.38 ?  137 ILE   A CG2  1 
ATOM   2892 C CD1  A ILE   A 1 137 ? 6.734  -9.920  -5.084  0.58 18.77 ?  137 ILE   A CD1  1 
ATOM   2893 C CD1  B ILE   A 1 137 ? 7.614  -9.156  -5.862  0.42 22.43 ?  137 ILE   A CD1  1 
ATOM   2894 H H    A ILE   A 1 137 ? 10.348 -8.296  -4.643  0.58 17.00 ?  137 ILE   A H    1 
ATOM   2895 H H    B ILE   A 1 137 ? 10.383 -8.530  -4.923  0.42 21.19 ?  137 ILE   A H    1 
ATOM   2896 H HA   A ILE   A 1 137 ? 10.225 -10.286 -2.982  0.58 17.76 ?  137 ILE   A HA   1 
ATOM   2897 H HA   B ILE   A 1 137 ? 10.524 -10.446 -3.128  0.42 22.08 ?  137 ILE   A HA   1 
ATOM   2898 H HB   A ILE   A 1 137 ? 9.365  -10.158 -5.663  0.58 19.68 ?  137 ILE   A HB   1 
ATOM   2899 H HB   B ILE   A 1 137 ? 9.342  -10.919 -5.626  0.42 24.19 ?  137 ILE   A HB   1 
ATOM   2900 H HG12 A ILE   A 1 137 ? 7.771  -10.040 -3.334  0.58 21.50 ?  137 ILE   A HG12 1 
ATOM   2901 H HG12 B ILE   A 1 137 ? 7.503  -9.877  -3.987  0.42 26.01 ?  137 ILE   A HG12 1 
ATOM   2902 H HG13 A ILE   A 1 137 ? 8.163  -8.770  -4.203  0.58 21.50 ?  137 ILE   A HG13 1 
ATOM   2903 H HG13 B ILE   A 1 137 ? 8.626  -8.789  -4.134  0.42 26.01 ?  137 ILE   A HG13 1 
ATOM   2904 H HG21 A ILE   A 1 137 ? 8.054  -12.158 -5.105  0.58 19.84 ?  137 ILE   A HG21 1 
ATOM   2905 H HG21 B ILE   A 1 137 ? 7.837  -12.206 -4.379  0.42 24.43 ?  137 ILE   A HG21 1 
ATOM   2906 H HG22 A ILE   A 1 137 ? 9.590  -12.374 -5.414  0.58 19.84 ?  137 ILE   A HG22 1 
ATOM   2907 H HG22 B ILE   A 1 137 ? 9.326  -12.692 -4.113  0.42 24.43 ?  137 ILE   A HG22 1 
ATOM   2908 H HG23 A ILE   A 1 137 ? 9.079  -12.334 -3.912  0.58 19.84 ?  137 ILE   A HG23 1 
ATOM   2909 H HG23 B ILE   A 1 137 ? 8.585  -11.780 -3.044  0.42 24.43 ?  137 ILE   A HG23 1 
ATOM   2910 H HD11 A ILE   A 1 137 ? 6.025  -10.292 -4.535  0.58 22.50 ?  137 ILE   A HD11 1 
ATOM   2911 H HD11 B ILE   A 1 137 ? 7.004  -8.421  -5.707  0.42 26.90 ?  137 ILE   A HD11 1 
ATOM   2912 H HD12 A ILE   A 1 137 ? 6.470  -9.062  -5.439  0.58 22.50 ?  137 ILE   A HD12 1 
ATOM   2913 H HD12 B ILE   A 1 137 ? 8.321  -8.880  -6.468  0.42 26.90 ?  137 ILE   A HD12 1 
ATOM   2914 H HD13 A ILE   A 1 137 ? 6.937  -10.522 -5.817  0.58 22.50 ?  137 ILE   A HD13 1 
ATOM   2915 H HD13 B ILE   A 1 137 ? 7.137  -9.913  -6.236  0.42 26.90 ?  137 ILE   A HD13 1 
ATOM   2916 N N    A HIS   A 1 138 ? 12.303 -10.748 -5.373  0.58 14.04 ?  138 HIS   A N    1 
ATOM   2917 N N    B HIS   A 1 138 ? 12.326 -10.854 -5.708  0.42 17.49 ?  138 HIS   A N    1 
ATOM   2918 C CA   A HIS   A 1 138 ? 13.480 -11.516 -5.761  0.58 13.47 ?  138 HIS   A CA   1 
ATOM   2919 C CA   B HIS   A 1 138 ? 13.502 -11.566 -6.190  0.42 17.05 ?  138 HIS   A CA   1 
ATOM   2920 C C    A HIS   A 1 138 ? 14.618 -11.335 -4.761  0.58 12.50 ?  138 HIS   A C    1 
ATOM   2921 C C    B HIS   A 1 138 ? 14.634 -11.497 -5.174  0.42 15.59 ?  138 HIS   A C    1 
ATOM   2922 O O    A HIS   A 1 138 ? 15.307 -12.305 -4.415  0.58 12.87 ?  138 HIS   A O    1 
ATOM   2923 O O    B HIS   A 1 138 ? 15.255 -12.516 -4.847  0.42 15.47 ?  138 HIS   A O    1 
ATOM   2924 C CB   A HIS   A 1 138 ? 13.903 -11.122 -7.177  0.58 14.59 ?  138 HIS   A CB   1 
ATOM   2925 C CB   B HIS   A 1 138 ? 13.942 -10.974 -7.528  0.42 18.38 ?  138 HIS   A CB   1 
ATOM   2926 C CG   A HIS   A 1 138 ? 15.153 -11.796 -7.650  0.58 15.50 ?  138 HIS   A CG   1 
ATOM   2927 C CG   B HIS   A 1 138 ? 15.283 -11.452 -7.981  0.42 19.65 ?  138 HIS   A CG   1 
ATOM   2928 N ND1  A HIS   A 1 138 ? 15.219 -13.146 -7.925  0.58 16.47 ?  138 HIS   A ND1  1 
ATOM   2929 N ND1  B HIS   A 1 138 ? 15.550 -12.778 -8.237  0.42 20.39 ?  138 HIS   A ND1  1 
ATOM   2930 C CD2  A HIS   A 1 138 ? 16.386 -11.299 -7.907  0.58 15.78 ?  138 HIS   A CD2  1 
ATOM   2931 C CD2  B HIS   A 1 138 ? 16.438 -10.784 -8.210  0.42 20.15 ?  138 HIS   A CD2  1 
ATOM   2932 C CE1  A HIS   A 1 138 ? 16.441 -13.451 -8.327  0.58 16.93 ?  138 HIS   A CE1  1 
ATOM   2933 C CE1  B HIS   A 1 138 ? 16.809 -12.907 -8.612  0.42 20.51 ?  138 HIS   A CE1  1 
ATOM   2934 N NE2  A HIS   A 1 138 ? 17.169 -12.347 -8.324  0.58 16.31 ?  138 HIS   A NE2  1 
ATOM   2935 N NE2  B HIS   A 1 138 ? 17.371 -11.712 -8.606  0.42 20.39 ?  138 HIS   A NE2  1 
ATOM   2936 H H    A HIS   A 1 138 ? 12.102 -10.103 -5.910  0.58 16.82 ?  138 HIS   A H    1 
ATOM   2937 H H    B HIS   A 1 138 ? 12.087 -10.193 -6.200  0.42 20.96 ?  138 HIS   A H    1 
ATOM   2938 H HA   A HIS   A 1 138 ? 13.243 -12.452 -5.769  0.58 16.14 ?  138 HIS   A HA   1 
ATOM   2939 H HA   B HIS   A 1 138 ? 13.279 -12.497 -6.327  0.42 20.44 ?  138 HIS   A HA   1 
ATOM   2940 H HB2  A HIS   A 1 138 ? 13.188 -11.360 -7.789  0.58 17.49 ?  138 HIS   A HB2  1 
ATOM   2941 H HB2  B HIS   A 1 138 ? 13.292 -11.222 -8.203  0.42 22.03 ?  138 HIS   A HB2  1 
ATOM   2942 H HB3  A HIS   A 1 138 ? 14.054 -10.165 -7.204  0.58 17.49 ?  138 HIS   A HB3  1 
ATOM   2943 H HB3  B HIS   A 1 138 ? 13.980 -10.008 -7.449  0.42 22.03 ?  138 HIS   A HB3  1 
ATOM   2944 H HD1  A HIS   A 1 138 ? 14.567 -13.704 -7.847  0.58 19.74 ?  138 HIS   A HD1  1 
ATOM   2945 H HD1  B HIS   A 1 138 ? 14.983 -13.419 -8.165  0.42 24.44 ?  138 HIS   A HD1  1 
ATOM   2946 H HD2  A HIS   A 1 138 ? 16.650 -10.414 -7.811  0.58 18.91 ?  138 HIS   A HD2  1 
ATOM   2947 H HD2  B HIS   A 1 138 ? 16.571 -9.864  -8.120  0.42 24.16 ?  138 HIS   A HD2  1 
ATOM   2948 H HE1  A HIS   A 1 138 ? 16.737 -14.299 -8.568  0.58 20.29 ?  138 HIS   A HE1  1 
ATOM   2949 H HE1  B HIS   A 1 138 ? 17.230 -13.701 -8.839  0.42 24.59 ?  138 HIS   A HE1  1 
ATOM   2950 N N    A SER   A 1 139 ? 14.829 -10.106 -4.281  0.58 12.03 ?  139 SER   A N    1 
ATOM   2951 N N    B SER   A 1 139 ? 14.919 -10.297 -4.664  0.42 13.99 ?  139 SER   A N    1 
ATOM   2952 C CA   A SER   A 1 139 ? 15.887 -9.874  -3.304  0.58 11.77 ?  139 SER   A CA   1 
ATOM   2953 C CA   B SER   A 1 139 ? 15.993 -10.142 -3.691  0.42 12.86 ?  139 SER   A CA   1 
ATOM   2954 C C    A SER   A 1 139 ? 15.685 -10.721 -2.053  0.58 11.46 ?  139 SER   A C    1 
ATOM   2955 C C    B SER   A 1 139 ? 15.735 -10.974 -2.442  0.42 12.85 ?  139 SER   A C    1 
ATOM   2956 O O    A SER   A 1 139 ? 16.644 -11.301 -1.526  0.58 11.50 ?  139 SER   A O    1 
ATOM   2957 O O    B SER   A 1 139 ? 16.660 -11.585 -1.894  0.42 12.34 ?  139 SER   A O    1 
ATOM   2958 C CB   A SER   A 1 139 ? 15.976 -8.384  -2.962  0.58 12.20 ?  139 SER   A CB   1 
ATOM   2959 C CB   B SER   A 1 139 ? 16.158 -8.665  -3.331  0.42 11.63 ?  139 SER   A CB   1 
ATOM   2960 O OG   A SER   A 1 139 ? 17.019 -8.164  -2.029  0.58 12.65 ?  139 SER   A OG   1 
ATOM   2961 O OG   B SER   A 1 139 ? 17.239 -8.486  -2.434  0.42 10.81 ?  139 SER   A OG   1 
ATOM   2962 H H    A SER   A 1 139 ? 14.382 -9.401  -4.494  0.58 14.41 ?  139 SER   A H    1 
ATOM   2963 H H    B SER   A 1 139 ? 14.510 -9.568  -4.857  0.42 16.76 ?  139 SER   A H    1 
ATOM   2964 H HA   A SER   A 1 139 ? 16.738 -10.126 -3.689  0.58 14.10 ?  139 SER   A HA   1 
ATOM   2965 H HA   B SER   A 1 139 ? 16.825 -10.448 -4.080  0.42 15.41 ?  139 SER   A HA   1 
ATOM   2966 H HB2  A SER   A 1 139 ? 16.163 -7.873  -3.772  0.58 14.62 ?  139 SER   A HB2  1 
ATOM   2967 H HB2  B SER   A 1 139 ? 16.345 -8.160  -4.137  0.42 13.94 ?  139 SER   A HB2  1 
ATOM   2968 H HB3  A SER   A 1 139 ? 15.140 -8.082  -2.573  0.58 14.62 ?  139 SER   A HB3  1 
ATOM   2969 H HB3  B SER   A 1 139 ? 15.343 -8.343  -2.916  0.42 13.94 ?  139 SER   A HB3  1 
ATOM   2970 H HG   A SER   A 1 139 ? 17.771 -8.256  -2.393  0.58 15.16 ?  139 SER   A HG   1 
ATOM   2971 H HG   B SER   A 1 139 ? 17.321 -7.677  -2.229  0.42 12.95 ?  139 SER   A HG   1 
ATOM   2972 N N    A LEU   A 1 140 ? 14.447 -10.809 -1.566  0.58 11.14 ?  140 LEU   A N    1 
ATOM   2973 N N    B LEU   A 1 140 ? 14.486 -11.006 -1.973  0.42 12.89 ?  140 LEU   A N    1 
ATOM   2974 C CA   A LEU   A 1 140 ? 14.180 -11.628 -0.387  0.58 11.28 ?  140 LEU   A CA   1 
ATOM   2975 C CA   B LEU   A 1 140 ? 14.163 -11.798 -0.790  0.42 13.32 ?  140 LEU   A CA   1 
ATOM   2976 C C    A LEU   A 1 140 ? 14.444 -13.107 -0.670  0.58 11.95 ?  140 LEU   A C    1 
ATOM   2977 C C    B LEU   A 1 140 ? 14.443 -13.275 -1.035  0.42 13.66 ?  140 LEU   A C    1 
ATOM   2978 O O    A LEU   A 1 140 ? 14.983 -13.824 0.183   0.58 12.26 ?  140 LEU   A O    1 
ATOM   2979 O O    B LEU   A 1 140 ? 15.012 -13.960 -0.177  0.42 13.90 ?  140 LEU   A O    1 
ATOM   2980 C CB   A LEU   A 1 140 ? 12.745 -11.394 0.092   0.58 11.47 ?  140 LEU   A CB   1 
ATOM   2981 C CB   B LEU   A 1 140 ? 12.700 -11.582 -0.400  0.42 13.95 ?  140 LEU   A CB   1 
ATOM   2982 C CG   A LEU   A 1 140 ? 12.284 -12.277 1.250   0.58 12.44 ?  140 LEU   A CG   1 
ATOM   2983 C CG   B LEU   A 1 140 ? 12.218 -12.313 0.856   0.42 14.41 ?  140 LEU   A CG   1 
ATOM   2984 C CD1  A LEU   A 1 140 ? 13.214 -12.158 2.447   0.58 12.55 ?  140 LEU   A CD1  1 
ATOM   2985 C CD1  B LEU   A 1 140 ? 13.022 -11.908 2.085   0.42 14.63 ?  140 LEU   A CD1  1 
ATOM   2986 C CD2  A LEU   A 1 140 ? 10.847 -11.940 1.640   0.58 13.04 ?  140 LEU   A CD2  1 
ATOM   2987 C CD2  B LEU   A 1 140 ? 10.730 -12.057 1.081   0.42 14.49 ?  140 LEU   A CD2  1 
ATOM   2988 H H    A LEU   A 1 140 ? 13.755 -10.403 -1.890  0.58 13.35 ?  140 LEU   A H    1 
ATOM   2989 H H    B LEU   A 1 140 ? 13.817 -10.589 -2.313  0.42 15.44 ?  140 LEU   A H    1 
ATOM   2990 H HA   A LEU   A 1 140 ? 14.769 -11.344 0.328   0.58 13.51 ?  140 LEU   A HA   1 
ATOM   2991 H HA   B LEU   A 1 140 ? 14.713 -11.508 -0.045  0.42 15.96 ?  140 LEU   A HA   1 
ATOM   2992 H HB2  A LEU   A 1 140 ? 12.658 -10.471 0.385   0.58 13.73 ?  140 LEU   A HB2  1 
ATOM   2993 H HB2  B LEU   A 1 140 ? 12.556 -10.636 -0.249  0.42 16.72 ?  140 LEU   A HB2  1 
ATOM   2994 H HB3  A LEU   A 1 140 ? 12.140 -11.553 -0.649  0.58 13.73 ?  140 LEU   A HB3  1 
ATOM   2995 H HB3  B LEU   A 1 140 ? 12.138 -11.881 -1.133  0.42 16.72 ?  140 LEU   A HB3  1 
ATOM   2996 H HG   A LEU   A 1 140 ? 12.295 -13.202 0.959   0.58 14.90 ?  140 LEU   A HG   1 
ATOM   2997 H HG   B LEU   A 1 140 ? 12.332 -13.269 0.732   0.42 17.27 ?  140 LEU   A HG   1 
ATOM   2998 H HD11 A LEU   A 1 140 ? 12.836 -12.657 3.188   0.58 15.04 ?  140 LEU   A HD11 1 
ATOM   2999 H HD11 B LEU   A 1 140 ? 12.620 -12.306 2.874   0.42 17.53 ?  140 LEU   A HD11 1 
ATOM   3000 H HD12 A LEU   A 1 140 ? 14.080 -12.526 2.210   0.58 15.04 ?  140 LEU   A HD12 1 
ATOM   3001 H HD12 B LEU   A 1 140 ? 13.933 -12.224 1.984   0.42 17.53 ?  140 LEU   A HD12 1 
ATOM   3002 H HD13 A LEU   A 1 140 ? 13.301 -11.224 2.686   0.58 15.04 ?  140 LEU   A HD13 1 
ATOM   3003 H HD13 B LEU   A 1 140 ? 13.013 -10.941 2.163   0.42 17.53 ?  140 LEU   A HD13 1 
ATOM   3004 H HD21 A LEU   A 1 140 ? 10.576 -12.517 2.375   0.58 15.63 ?  140 LEU   A HD21 1 
ATOM   3005 H HD21 B LEU   A 1 140 ? 10.433 -12.561 1.858   0.42 17.36 ?  140 LEU   A HD21 1 
ATOM   3006 H HD22 A LEU   A 1 140 ? 10.801 -11.013 1.914   0.58 15.63 ?  140 LEU   A HD22 1 
ATOM   3007 H HD22 B LEU   A 1 140 ? 10.590 -11.109 1.231   0.42 17.36 ?  140 LEU   A HD22 1 
ATOM   3008 H HD23 A LEU   A 1 140 ? 10.267 -12.091 0.876   0.58 15.63 ?  140 LEU   A HD23 1 
ATOM   3009 H HD23 B LEU   A 1 140 ? 10.236 -12.345 0.296   0.42 17.36 ?  140 LEU   A HD23 1 
ATOM   3010 N N    A ARG   A 1 141 ? 14.077 -13.575 -1.867  0.58 12.35 ?  141 ARG   A N    1 
ATOM   3011 N N    B ARG   A 1 141 ? 14.057 -13.779 -2.208  0.42 14.34 ?  141 ARG   A N    1 
ATOM   3012 C CA   A ARG   A 1 141 ? 14.299 -14.973 -2.231  0.58 13.30 ?  141 ARG   A CA   1 
ATOM   3013 C CA   B ARG   A 1 141 ? 14.341 -15.170 -2.541  0.42 15.67 ?  141 ARG   A CA   1 
ATOM   3014 C C    A ARG   A 1 141 ? 15.792 -15.299 -2.257  0.58 12.56 ?  141 ARG   A C    1 
ATOM   3015 C C    B ARG   A 1 141 ? 15.841 -15.438 -2.548  0.42 14.66 ?  141 ARG   A C    1 
ATOM   3016 O O    A ARG   A 1 141 ? 16.241 -16.280 -1.648  0.58 12.18 ?  141 ARG   A O    1 
ATOM   3017 O O    B ARG   A 1 141 ? 16.290 -16.504 -2.112  0.42 14.12 ?  141 ARG   A O    1 
ATOM   3018 C CB   A ARG   A 1 141 ? 13.654 -15.245 -3.595  0.58 14.15 ?  141 ARG   A CB   1 
ATOM   3019 C CB   B ARG   A 1 141 ? 13.724 -15.511 -3.896  0.42 18.14 ?  141 ARG   A CB   1 
ATOM   3020 C CG   A ARG   A 1 141 ? 13.689 -16.700 -4.071  0.58 16.09 ?  141 ARG   A CG   1 
ATOM   3021 C CG   B ARG   A 1 141 ? 12.203 -15.489 -3.912  0.42 20.99 ?  141 ARG   A CG   1 
ATOM   3022 C CD   A ARG   A 1 141 ? 12.659 -17.529 -3.359  0.58 18.10 ?  141 ARG   A CD   1 
ATOM   3023 C CD   B ARG   A 1 141 ? 11.676 -15.906 -5.276  0.42 23.28 ?  141 ARG   A CD   1 
ATOM   3024 N NE   A ARG   A 1 141 ? 13.266 -18.330 -2.310  0.58 18.99 ?  141 ARG   A NE   1 
ATOM   3025 N NE   B ARG   A 1 141 ? 10.265 -16.271 -5.244  0.42 25.09 ?  141 ARG   A NE   1 
ATOM   3026 C CZ   A ARG   A 1 141 ? 12.585 -18.905 -1.328  0.58 19.56 ?  141 ARG   A CZ   1 
ATOM   3027 C CZ   B ARG   A 1 141 ? 9.280  -15.533 -5.741  0.42 26.42 ?  141 ARG   A CZ   1 
ATOM   3028 N NH1  A ARG   A 1 141 ? 11.294 -18.673 -1.154  0.58 19.26 ?  141 ARG   A NH1  1 
ATOM   3029 N NH1  B ARG   A 1 141 ? 9.514  -14.375 -6.337  0.42 27.04 ?  141 ARG   A NH1  1 
ATOM   3030 N NH2  A ARG   A 1 141 ? 13.217 -19.725 -0.494  0.58 20.41 ?  141 ARG   A NH2  1 
ATOM   3031 N NH2  B ARG   A 1 141 ? 8.029  -15.974 -5.646  0.42 26.90 ?  141 ARG   A NH2  1 
ATOM   3032 H H    A ARG   A 1 141 ? 13.701 -13.101 -2.479  0.58 14.79 ?  141 ARG   A H    1 
ATOM   3033 H H    B ARG   A 1 141 ? 13.635 -13.342 -2.814  0.42 17.18 ?  141 ARG   A H    1 
ATOM   3034 H HA   A ARG   A 1 141 ? 13.874 -15.543 -1.572  0.58 15.94 ?  141 ARG   A HA   1 
ATOM   3035 H HA   B ARG   A 1 141 ? 13.938 -15.746 -1.873  0.42 18.78 ?  141 ARG   A HA   1 
ATOM   3036 H HB2  A ARG   A 1 141 ? 12.720 -14.971 -3.552  0.58 16.96 ?  141 ARG   A HB2  1 
ATOM   3037 H HB2  B ARG   A 1 141 ? 14.037 -14.869 -4.551  0.42 21.75 ?  141 ARG   A HB2  1 
ATOM   3038 H HB3  A ARG   A 1 141 ? 14.110 -14.709 -4.259  0.58 16.96 ?  141 ARG   A HB3  1 
ATOM   3039 H HB3  B ARG   A 1 141 ? 14.009 -16.404 -4.149  0.42 21.75 ?  141 ARG   A HB3  1 
ATOM   3040 H HG2  A ARG   A 1 141 ? 13.502 -16.728 -5.024  0.58 19.29 ?  141 ARG   A HG2  1 
ATOM   3041 H HG2  B ARG   A 1 141 ? 11.865 -16.111 -3.250  0.42 25.16 ?  141 ARG   A HG2  1 
ATOM   3042 H HG3  A ARG   A 1 141 ? 14.566 -17.077 -3.892  0.58 19.29 ?  141 ARG   A HG3  1 
ATOM   3043 H HG3  B ARG   A 1 141 ? 11.890 -14.591 -3.720  0.42 25.16 ?  141 ARG   A HG3  1 
ATOM   3044 H HD2  A ARG   A 1 141 ? 12.003 -16.945 -2.949  0.58 21.69 ?  141 ARG   A HD2  1 
ATOM   3045 H HD2  B ARG   A 1 141 ? 11.808 -15.177 -5.902  0.42 27.91 ?  141 ARG   A HD2  1 
ATOM   3046 H HD3  A ARG   A 1 141 ? 12.227 -18.119 -3.999  0.58 21.69 ?  141 ARG   A HD3  1 
ATOM   3047 H HD3  B ARG   A 1 141 ? 12.172 -16.681 -5.574  0.42 27.91 ?  141 ARG   A HD3  1 
ATOM   3048 H HE   A ARG   A 1 141 ? 14.096 -18.538 -2.395  0.58 22.77 ?  141 ARG   A HE   1 
ATOM   3049 H HE   B ARG   A 1 141 ? 10.076 -17.081 -5.024  0.42 30.08 ?  141 ARG   A HE   1 
ATOM   3050 H HH11 A ARG   A 1 141 ? 10.869 -18.157 -1.695  0.58 23.09 ?  141 ARG   A HH11 1 
ATOM   3051 H HH11 B ARG   A 1 141 ? 10.316 -14.075 -6.409  0.42 32.43 ?  141 ARG   A HH11 1 
ATOM   3052 H HH12 A ARG   A 1 141 ? 10.872 -19.055 -0.509  0.58 23.09 ?  141 ARG   A HH12 1 
ATOM   3053 H HH12 B ARG   A 1 141 ? 8.859  -13.920 -6.652  0.42 32.43 ?  141 ARG   A HH12 1 
ATOM   3054 H HH21 A ARG   A 1 141 ? 14.057 -19.880 -0.599  0.58 24.47 ?  141 ARG   A HH21 1 
ATOM   3055 H HH21 B ARG   A 1 141 ? 7.865  -16.726 -5.262  0.42 32.25 ?  141 ARG   A HH21 1 
ATOM   3056 H HH22 A ARG   A 1 141 ? 12.789 -20.094 0.154   0.58 24.47 ?  141 ARG   A HH22 1 
ATOM   3057 H HH22 B ARG   A 1 141 ? 7.383  -15.506 -5.967  0.42 32.25 ?  141 ARG   A HH22 1 
ATOM   3058 N N    A VAL   A 1 142 ? 16.583 -14.483 -2.962  0.58 12.69 ?  142 VAL   A N    1 
ATOM   3059 N N    B VAL   A 1 142 ? 16.637 -14.483 -3.034  0.42 14.33 ?  142 VAL   A N    1 
ATOM   3060 C CA   A VAL   A 1 142 ? 18.026 -14.707 -3.002  0.58 13.31 ?  142 VAL   A CA   1 
ATOM   3061 C CA   B VAL   A 1 142 ? 18.085 -14.668 -3.026  0.42 14.16 ?  142 VAL   A CA   1 
ATOM   3062 C C    A VAL   A 1 142 ? 18.609 -14.673 -1.595  0.58 12.96 ?  142 VAL   A C    1 
ATOM   3063 C C    B VAL   A 1 142 ? 18.618 -14.668 -1.598  0.42 13.37 ?  142 VAL   A C    1 
ATOM   3064 O O    A VAL   A 1 142 ? 19.484 -15.475 -1.251  0.58 13.53 ?  142 VAL   A O    1 
ATOM   3065 O O    B VAL   A 1 142 ? 19.463 -15.495 -1.238  0.42 13.68 ?  142 VAL   A O    1 
ATOM   3066 C CB   A VAL   A 1 142 ? 18.717 -13.701 -3.942  0.58 13.78 ?  142 VAL   A CB   1 
ATOM   3067 C CB   B VAL   A 1 142 ? 18.788 -13.622 -3.909  0.42 14.58 ?  142 VAL   A CB   1 
ATOM   3068 C CG1  A VAL   A 1 142 ? 20.234 -13.875 -3.887  0.58 13.90 ?  142 VAL   A CG1  1 
ATOM   3069 C CG1  B VAL   A 1 142 ? 20.295 -13.832 -3.866  0.42 14.66 ?  142 VAL   A CG1  1 
ATOM   3070 C CG2  A VAL   A 1 142 ? 18.227 -13.876 -5.369  0.58 14.78 ?  142 VAL   A CG2  1 
ATOM   3071 C CG2  B VAL   A 1 142 ? 18.291 -13.707 -5.341  0.42 15.16 ?  142 VAL   A CG2  1 
ATOM   3072 H H    A VAL   A 1 142 ? 16.310 -13.801 -3.415  0.58 15.21 ?  142 VAL   A H    1 
ATOM   3073 H H    B VAL   A 1 142 ? 16.367 -13.734 -3.369  0.42 17.17 ?  142 VAL   A H    1 
ATOM   3074 H HA   A VAL   A 1 142 ? 18.187 -15.589 -3.360  0.58 15.95 ?  142 VAL   A HA   1 
ATOM   3075 H HA   B VAL   A 1 142 ? 18.279 -15.535 -3.406  0.42 16.97 ?  142 VAL   A HA   1 
ATOM   3076 H HB   A VAL   A 1 142 ? 18.510 -12.795 -3.659  0.58 16.51 ?  142 VAL   A HB   1 
ATOM   3077 H HB   B VAL   A 1 142 ? 18.597 -12.730 -3.574  0.42 17.47 ?  142 VAL   A HB   1 
ATOM   3078 H HG11 A VAL   A 1 142 ? 20.634 -13.399 -4.633  0.58 16.65 ?  142 VAL   A HG11 1 
ATOM   3079 H HG11 B VAL   A 1 142 ? 20.705 -13.312 -4.574  0.42 17.56 ?  142 VAL   A HG11 1 
ATOM   3080 H HG12 A VAL   A 1 142 ? 20.567 -13.512 -3.051  0.58 16.65 ?  142 VAL   A HG12 1 
ATOM   3081 H HG12 B VAL   A 1 142 ? 20.632 -13.541 -3.005  0.42 17.56 ?  142 VAL   A HG12 1 
ATOM   3082 H HG13 A VAL   A 1 142 ? 20.445 -14.819 -3.948  0.58 16.65 ?  142 VAL   A HG13 1 
ATOM   3083 H HG13 B VAL   A 1 142 ? 20.483 -14.774 -3.997  0.42 17.56 ?  142 VAL   A HG13 1 
ATOM   3084 H HG21 A VAL   A 1 142 ? 18.693 -13.246 -5.943  0.58 17.71 ?  142 VAL   A HG21 1 
ATOM   3085 H HG21 B VAL   A 1 142 ? 18.729 -13.021 -5.868  0.42 18.17 ?  142 VAL   A HG21 1 
ATOM   3086 H HG22 A VAL   A 1 142 ? 18.416 -14.784 -5.655  0.58 17.71 ?  142 VAL   A HG22 1 
ATOM   3087 H HG22 B VAL   A 1 142 ? 18.509 -14.585 -5.694  0.42 18.17 ?  142 VAL   A HG22 1 
ATOM   3088 H HG23 A VAL   A 1 142 ? 17.275 -13.709 -5.397  0.58 17.71 ?  142 VAL   A HG23 1 
ATOM   3089 H HG23 B VAL   A 1 142 ? 17.333 -13.574 -5.353  0.42 18.17 ?  142 VAL   A HG23 1 
ATOM   3090 N N    . CYS   A 1 143 ? 18.141 -13.741 -0.763  1.00 12.75 ?  143 CYS   A N    1 
ATOM   3091 C CA   . CYS   A 1 143 ? 18.597 -13.686 0.622   1.00 12.99 ?  143 CYS   A CA   1 
ATOM   3092 C C    . CYS   A 1 143 ? 18.363 -15.021 1.325   1.00 13.12 ?  143 CYS   A C    1 
ATOM   3093 O O    . CYS   A 1 143 ? 19.280 -15.608 1.908   1.00 13.55 ?  143 CYS   A O    1 
ATOM   3094 C CB   . CYS   A 1 143 ? 17.867 -12.561 1.354   1.00 13.50 ?  143 CYS   A CB   1 
ATOM   3095 S SG   . CYS   A 1 143 ? 18.343 -12.378 3.073   1.00 13.76 ?  143 CYS   A SG   1 
ATOM   3096 H H    A CYS   A 1 143 ? 17.564 -13.140 -0.973  0.58 15.28 ?  143 CYS   A H    1 
ATOM   3097 H H    B CYS   A 1 143 ? 17.558 -13.145 -0.971  0.42 15.28 ?  143 CYS   A H    1 
ATOM   3098 H HA   . CYS   A 1 143 ? 19.547 -13.500 0.641   1.00 15.56 ?  143 CYS   A HA   1 
ATOM   3099 H HB2  . CYS   A 1 143 ? 18.048 -11.725 0.902   1.00 16.18 ?  143 CYS   A HB2  1 
ATOM   3100 H HB3  . CYS   A 1 143 ? 16.916 -12.743 1.330   1.00 16.18 ?  143 CYS   A HB3  1 
ATOM   3101 H HG   . CYS   A 1 143 ? 17.759 -11.434 3.534   1.00 16.48 ?  143 CYS   A HG   1 
ATOM   3102 N N    . VAL   A 1 144 ? 17.126 -15.515 1.273   1.00 13.90 ?  144 VAL   A N    1 
ATOM   3103 C CA   . VAL   A 1 144 ? 16.771 -16.748 1.967   1.00 15.29 ?  144 VAL   A CA   1 
ATOM   3104 C C    . VAL   A 1 144 ? 17.596 -17.920 1.454   1.00 15.35 ?  144 VAL   A C    1 
ATOM   3105 O O    . VAL   A 1 144 ? 17.956 -18.825 2.217   1.00 16.05 ?  144 VAL   A O    1 
ATOM   3106 C CB   . VAL   A 1 144 ? 15.256 -16.990 1.817   1.00 17.94 ?  144 VAL   A CB   1 
ATOM   3107 C CG1  . VAL   A 1 144 ? 14.885 -18.436 2.119   1.00 19.58 ?  144 VAL   A CG1  1 
ATOM   3108 C CG2  . VAL   A 1 144 ? 14.493 -16.001 2.702   1.00 17.95 ?  144 VAL   A CG2  1 
ATOM   3109 H H    . VAL   A 1 144 ? 16.472 -15.148 0.843   1.00 16.65 ?  144 VAL   A H    1 
ATOM   3110 H HA   . VAL   A 1 144 ? 16.951 -16.638 2.911   1.00 18.33 ?  144 VAL   A HA   1 
ATOM   3111 H HB   . VAL   A 1 144 ? 14.998 -16.803 0.897   1.00 21.50 ?  144 VAL   A HB   1 
ATOM   3112 H HG11 . VAL   A 1 144 ? 13.927 -18.489 2.278   1.00 23.48 ?  144 VAL   A HG11 1 
ATOM   3113 H HG12 . VAL   A 1 144 ? 15.120 -18.988 1.358   1.00 23.48 ?  144 VAL   A HG12 1 
ATOM   3114 H HG13 . VAL   A 1 144 ? 15.365 -18.724 2.908   1.00 23.48 ?  144 VAL   A HG13 1 
ATOM   3115 H HG21 . VAL   A 1 144 ? 13.536 -16.159 2.610   1.00 21.51 ?  144 VAL   A HG21 1 
ATOM   3116 H HG22 . VAL   A 1 144 ? 14.758 -16.129 3.625   1.00 21.51 ?  144 VAL   A HG22 1 
ATOM   3117 H HG23 . VAL   A 1 144 ? 14.699 -15.093 2.422   1.00 21.51 ?  144 VAL   A HG23 1 
ATOM   3118 N N    . ASP   A 1 145 ? 17.872 -17.947 0.154   1.00 15.63 ?  145 ASP   A N    1 
ATOM   3119 C CA   . ASP   A 1 145 ? 18.580 -19.057 -0.469  1.00 16.49 ?  145 ASP   A CA   1 
ATOM   3120 C C    . ASP   A 1 145 ? 20.100 -18.914 -0.419  1.00 15.99 ?  145 ASP   A C    1 
ATOM   3121 O O    . ASP   A 1 145 ? 20.799 -19.821 -0.881  1.00 18.05 ?  145 ASP   A O    1 
ATOM   3122 C CB   . ASP   A 1 145 ? 18.138 -19.208 -1.930  1.00 18.42 ?  145 ASP   A CB   1 
ATOM   3123 C CG   . ASP   A 1 145 ? 16.693 -19.652 -2.070  1.00 20.82 ?  145 ASP   A CG   1 
ATOM   3124 O OD1  . ASP   A 1 145 ? 16.134 -20.197 -1.097  1.00 21.41 ?  145 ASP   A OD1  1 
ATOM   3125 O OD2  . ASP   A 1 145 ? 16.118 -19.451 -3.159  1.00 22.70 -1 145 ASP   A OD2  1 
ATOM   3126 H H    . ASP   A 1 145 ? 17.638 -17.329 -0.397  1.00 18.73 ?  145 ASP   A H    1 
ATOM   3127 H HA   . ASP   A 1 145 ? 18.340 -19.875 -0.004  1.00 19.76 ?  145 ASP   A HA   1 
ATOM   3128 H HB2  . ASP   A 1 145 ? 18.238 -18.351 -2.376  1.00 22.07 ?  145 ASP   A HB2  1 
ATOM   3129 H HB3  . ASP   A 1 145 ? 18.695 -19.872 -2.358  1.00 22.07 ?  145 ASP   A HB3  1 
ATOM   3130 N N    . THR   A 1 146 ? 20.629 -17.822 0.129   1.00 13.77 ?  146 THR   A N    1 
ATOM   3131 C CA   . THR   A 1 146 ? 22.070 -17.573 0.155   1.00 13.15 ?  146 THR   A CA   1 
ATOM   3132 C C    . THR   A 1 146 ? 22.621 -17.387 1.555   1.00 12.94 ?  146 THR   A C    1 
ATOM   3133 O O    . THR   A 1 146 ? 23.697 -17.916 1.869   1.00 14.44 ?  146 THR   A O    1 
ATOM   3134 C CB   . THR   A 1 146 ? 22.398 -16.321 -0.681  1.00 12.95 ?  146 THR   A CB   1 
ATOM   3135 O OG1  . THR   A 1 146 ? 21.883 -16.484 -2.003  1.00 13.91 ?  146 THR   A OG1  1 
ATOM   3136 C CG2  . THR   A 1 146 ? 23.902 -16.090 -0.745  1.00 13.28 ?  146 THR   A CG2  1 
ATOM   3137 H H    . THR   A 1 146 ? 20.164 -17.191 0.495   1.00 16.50 ?  146 THR   A H    1 
ATOM   3138 H HA   . THR   A 1 146 ? 22.527 -18.322 -0.244  1.00 15.76 ?  146 THR   A HA   1 
ATOM   3139 H HB   . THR   A 1 146 ? 22.000 -15.539 -0.268  1.00 15.51 ?  146 THR   A HB   1 
ATOM   3140 H HG1  . THR   A 1 146 ? 21.047 -16.551 -1.974  1.00 16.67 ?  146 THR   A HG1  1 
ATOM   3141 H HG21 . THR   A 1 146 ? 24.111 -15.436 -1.430  1.00 15.92 ?  146 THR   A HG21 1 
ATOM   3142 H HG22 . THR   A 1 146 ? 24.229 -15.759 0.110   1.00 15.92 ?  146 THR   A HG22 1 
ATOM   3143 H HG23 . THR   A 1 146 ? 24.358 -16.920 -0.954  1.00 15.92 ?  146 THR   A HG23 1 
ATOM   3144 N N    . VAL   A 1 147 ? 21.940 -16.609 2.385   1.00 12.92 ?  147 VAL   A N    1 
ATOM   3145 C CA   . VAL   A 1 147 ? 22.418 -16.304 3.724   1.00 13.08 ?  147 VAL   A CA   1 
ATOM   3146 C C    . VAL   A 1 147 ? 22.094 -17.471 4.646   1.00 13.91 ?  147 VAL   A C    1 
ATOM   3147 O O    . VAL   A 1 147 ? 20.951 -17.949 4.695   1.00 14.39 ?  147 VAL   A O    1 
ATOM   3148 C CB   . VAL   A 1 147 ? 21.789 -14.998 4.230   1.00 13.26 ?  147 VAL   A CB   1 
ATOM   3149 C CG1  . VAL   A 1 147 ? 22.307 -14.667 5.613   1.00 14.24 ?  147 VAL   A CG1  1 
ATOM   3150 C CG2  . VAL   A 1 147 ? 22.053 -13.856 3.253   1.00 13.63 ?  147 VAL   A CG2  1 
ATOM   3151 H H    . VAL   A 1 147 ? 21.185 -16.239 2.196   1.00 15.48 ?  147 VAL   A H    1 
ATOM   3152 H HA   . VAL   A 1 147 ? 23.381 -16.189 3.701   1.00 15.67 ?  147 VAL   A HA   1 
ATOM   3153 H HB   . VAL   A 1 147 ? 20.829 -15.121 4.295   1.00 15.88 ?  147 VAL   A HB   1 
ATOM   3154 H HG11 . VAL   A 1 147 ? 22.038 -13.766 5.841   1.00 17.06 ?  147 VAL   A HG11 1 
ATOM   3155 H HG12 . VAL   A 1 147 ? 21.925 -15.296 6.252   1.00 17.06 ?  147 VAL   A HG12 1 
ATOM   3156 H HG13 . VAL   A 1 147 ? 23.272 -14.740 5.615   1.00 17.06 ?  147 VAL   A HG13 1 
ATOM   3157 H HG21 . VAL   A 1 147 ? 21.724 -13.030 3.641   1.00 16.33 ?  147 VAL   A HG21 1 
ATOM   3158 H HG22 . VAL   A 1 147 ? 23.005 -13.792 3.094   1.00 16.33 ?  147 VAL   A HG22 1 
ATOM   3159 H HG23 . VAL   A 1 147 ? 21.587 -14.039 2.422   1.00 16.33 ?  147 VAL   A HG23 1 
ATOM   3160 N N    . ARG   A 1 148 ? 23.114 -17.944 5.362   1.00 14.12 ?  148 ARG   A N    1 
ATOM   3161 C CA   . ARG   A 1 148 ? 22.984 -19.022 6.327   1.00 13.98 ?  148 ARG   A CA   1 
ATOM   3162 C C    . ARG   A 1 148 ? 23.102 -18.549 7.763   1.00 14.43 ?  148 ARG   A C    1 
ATOM   3163 O O    . ARG   A 1 148 ? 22.700 -19.281 8.676   1.00 16.12 ?  148 ARG   A O    1 
ATOM   3164 C CB   . ARG   A 1 148 ? 24.036 -20.111 6.058   1.00 14.56 ?  148 ARG   A CB   1 
ATOM   3165 C CG   . ARG   A 1 148 ? 23.876 -20.763 4.696   1.00 16.10 ?  148 ARG   A CG   1 
ATOM   3166 C CD   . ARG   A 1 148 ? 24.968 -21.786 4.401   1.00 16.84 ?  148 ARG   A CD   1 
ATOM   3167 N NE   . ARG   A 1 148 ? 26.307 -21.205 4.429   1.00 16.98 ?  148 ARG   A NE   1 
ATOM   3168 C CZ   . ARG   A 1 148 ? 26.823 -20.475 3.449   1.00 15.95 ?  148 ARG   A CZ   1 
ATOM   3169 N NH1  . ARG   A 1 148 ? 26.153 -20.242 2.332   1.00 16.58 ?  148 ARG   A NH1  1 
ATOM   3170 N NH2  . ARG   A 1 148 ? 28.037 -19.941 3.599   1.00 16.36 ?  148 ARG   A NH2  1 
ATOM   3171 H H    . ARG   A 1 148 ? 23.920 -17.635 5.298   1.00 16.92 ?  148 ARG   A H    1 
ATOM   3172 H HA   . ARG   A 1 148 ? 22.112 -19.424 6.225   1.00 16.75 ?  148 ARG   A HA   1 
ATOM   3173 H HB2  . ARG   A 1 148 ? 24.921 -19.721 6.098   1.00 17.45 ?  148 ARG   A HB2  1 
ATOM   3174 H HB3  . ARG   A 1 148 ? 23.948 -20.809 6.728   1.00 17.45 ?  148 ARG   A HB3  1 
ATOM   3175 H HG2  . ARG   A 1 148 ? 23.015 -21.212 4.665   1.00 19.29 ?  148 ARG   A HG2  1 
ATOM   3176 H HG3  . ARG   A 1 148 ? 23.909 -20.069 4.016   1.00 19.29 ?  148 ARG   A HG3  1 
ATOM   3177 H HD2  . ARG   A 1 148 ? 24.932 -22.484 5.069   1.00 20.19 ?  148 ARG   A HD2  1 
ATOM   3178 H HD3  . ARG   A 1 148 ? 24.818 -22.157 3.518   1.00 20.19 ?  148 ARG   A HD3  1 
ATOM   3179 H HE   . ARG   A 1 148 ? 26.788 -21.332 5.125   1.00 20.35 ?  148 ARG   A HE   1 
ATOM   3180 H HH11 . ARG   A 1 148 ? 25.367 -20.563 2.222   1.00 19.87 ?  148 ARG   A HH11 1 
ATOM   3181 H HH12 . ARG   A 1 148 ? 26.507 -19.754 1.713   1.00 19.87 ?  148 ARG   A HH12 1 
ATOM   3182 H HH21 . ARG   A 1 148 ? 28.475 -20.073 4.324   1.00 19.61 ?  148 ARG   A HH21 1 
ATOM   3183 H HH22 . ARG   A 1 148 ? 28.376 -19.456 2.972   1.00 19.61 ?  148 ARG   A HH22 1 
ATOM   3184 N N    . THR   A 1 149 ? 23.640 -17.351 7.979   1.00 14.52 ?  149 THR   A N    1 
ATOM   3185 C CA   . THR   A 1 149 ? 23.715 -16.746 9.294   1.00 14.43 ?  149 THR   A CA   1 
ATOM   3186 C C    . THR   A 1 149 ? 22.389 -16.047 9.594   1.00 14.30 ?  149 THR   A C    1 
ATOM   3187 O O    . THR   A 1 149 ? 21.463 -16.037 8.774   1.00 14.80 ?  149 THR   A O    1 
ATOM   3188 C CB   . THR   A 1 149 ? 24.919 -15.812 9.351   1.00 14.91 ?  149 THR   A CB   1 
ATOM   3189 O OG1  . THR   A 1 149 ? 24.798 -14.880 8.274   1.00 14.99 ?  149 THR   A OG1  1 
ATOM   3190 C CG2  . THR   A 1 149 ? 26.231 -16.613 9.234   1.00 15.35 ?  149 THR   A CG2  1 
ATOM   3191 H H    . THR   A 1 149 ? 23.983 -16.857 7.360   1.00 17.40 ?  149 THR   A H    1 
ATOM   3192 H HA   . THR   A 1 149 ? 23.838 -17.449 9.955   1.00 17.29 ?  149 THR   A HA   1 
ATOM   3193 H HB   . THR   A 1 149 ? 24.913 -15.340 10.198  1.00 17.87 ?  149 THR   A HB   1 
ATOM   3194 H HG1  . THR   A 1 149 ? 25.453 -14.354 8.280   1.00 17.96 ?  149 THR   A HG1  1 
ATOM   3195 H HG21 . THR   A 1 149 ? 26.989 -16.015 9.288   1.00 18.39 ?  149 THR   A HG21 1 
ATOM   3196 H HG22 . THR   A 1 149 ? 26.291 -17.266 9.951   1.00 18.39 ?  149 THR   A HG22 1 
ATOM   3197 H HG23 . THR   A 1 149 ? 26.260 -17.083 8.383   1.00 18.39 ?  149 THR   A HG23 1 
ATOM   3198 N N    . ASN   A 1 150 ? 22.262 -15.509 10.800  1.00 14.64 ?  150 ASN   A N    1 
ATOM   3199 C CA   . ASN   A 1 150 ? 20.981 -14.993 11.279  1.00 15.30 ?  150 ASN   A CA   1 
ATOM   3200 C C    . ASN   A 1 150 ? 20.809 -13.554 10.808  1.00 14.05 ?  150 ASN   A C    1 
ATOM   3201 O O    . ASN   A 1 150 ? 21.557 -12.661 11.227  1.00 15.24 ?  150 ASN   A O    1 
ATOM   3202 C CB   . ASN   A 1 150 ? 20.920 -15.093 12.798  1.00 18.23 ?  150 ASN   A CB   1 
ATOM   3203 C CG   . ASN   A 1 150 ? 20.817 -16.518 13.269  1.00 22.28 ?  150 ASN   A CG   1 
ATOM   3204 O OD1  . ASN   A 1 150 ? 20.212 -17.351 12.597  1.00 23.64 ?  150 ASN   A OD1  1 
ATOM   3205 N ND2  . ASN   A 1 150 ? 21.419 -16.818 14.417  1.00 24.90 ?  150 ASN   A ND2  1 
ATOM   3206 H H    . ASN   A 1 150 ? 22.901 -15.440 11.368  1.00 17.54 ?  150 ASN   A H    1 
ATOM   3207 H HA   . ASN   A 1 150 ? 20.257 -15.533 10.913  1.00 18.33 ?  150 ASN   A HA   1 
ATOM   3208 H HB2  . ASN   A 1 150 ? 21.726 -14.711 13.176  1.00 21.85 ?  150 ASN   A HB2  1 
ATOM   3209 H HB3  . ASN   A 1 150 ? 20.139 -14.620 13.120  1.00 21.85 ?  150 ASN   A HB3  1 
ATOM   3210 H HD21 . ASN   A 1 150 ? 21.392 -17.622 14.732  1.00 29.85 ?  150 ASN   A HD21 1 
ATOM   3211 H HD22 . ASN   A 1 150 ? 21.833 -16.205 14.858  1.00 29.85 ?  150 ASN   A HD22 1 
ATOM   3212 N N    . VAL   A 1 151 ? 19.828 -13.325 9.943   1.00 13.46 ?  151 VAL   A N    1 
ATOM   3213 C CA   . VAL   A 1 151 ? 19.619 -12.018 9.340   1.00 13.75 ?  151 VAL   A CA   1 
ATOM   3214 C C    . VAL   A 1 151 ? 18.231 -11.504 9.696   1.00 14.07 ?  151 VAL   A C    1 
ATOM   3215 O O    . VAL   A 1 151 ? 17.227 -12.220 9.549   1.00 15.46 ?  151 VAL   A O    1 
ATOM   3216 C CB   . VAL   A 1 151 ? 19.912 -12.019 7.824   1.00 14.99 ?  151 VAL   A CB   1 
ATOM   3217 C CG1  . VAL   A 1 151 ? 19.104 -13.067 7.084   1.00 16.30 ?  151 VAL   A CG1  1 
ATOM   3218 C CG2  . VAL   A 1 151 ? 19.716 -10.625 7.231   1.00 15.02 ?  151 VAL   A CG2  1 
ATOM   3219 H H    . VAL   A 1 151 ? 19.270 -13.927 9.680   1.00 16.12 ?  151 VAL   A H    1 
ATOM   3220 H HA   . VAL   A 1 151 ? 20.259 -11.406 9.737   1.00 16.48 ?  151 VAL   A HA   1 
ATOM   3221 H HB   . VAL   A 1 151 ? 20.849 -12.249 7.699   1.00 17.96 ?  151 VAL   A HB   1 
ATOM   3222 H HG11 . VAL   A 1 151 ? 19.301 -13.017 6.134   1.00 19.53 ?  151 VAL   A HG11 1 
ATOM   3223 H HG12 . VAL   A 1 151 ? 19.348 -13.953 7.416   1.00 19.53 ?  151 VAL   A HG12 1 
ATOM   3224 H HG13 . VAL   A 1 151 ? 18.160 -12.914 7.235   1.00 19.53 ?  151 VAL   A HG13 1 
ATOM   3225 H HG21 . VAL   A 1 151 ? 20.031 -10.628 6.310   1.00 18.00 ?  151 VAL   A HG21 1 
ATOM   3226 H HG22 . VAL   A 1 151 ? 18.774 -10.400 7.254   1.00 18.00 ?  151 VAL   A HG22 1 
ATOM   3227 H HG23 . VAL   A 1 151 ? 20.227 -9.986  7.750   1.00 18.00 ?  151 VAL   A HG23 1 
ATOM   3228 N N    . TYR   A 1 152 ? 18.205 -10.258 10.182  1.00 13.92 ?  152 TYR   A N    1 
ATOM   3229 C CA   . TYR   A 1 152 ? 17.004 -9.524  10.561  1.00 13.63 ?  152 TYR   A CA   1 
ATOM   3230 C C    . TYR   A 1 152 ? 16.808 -8.423  9.531   1.00 12.86 ?  152 TYR   A C    1 
ATOM   3231 O O    . TYR   A 1 152 ? 17.577 -7.458  9.492   1.00 13.07 ?  152 TYR   A O    1 
ATOM   3232 C CB   . TYR   A 1 152 ? 17.163 -8.971  11.974  1.00 14.72 ?  152 TYR   A CB   1 
ATOM   3233 C CG   . TYR   A 1 152 ? 17.117 -10.089 12.976  1.00 15.24 ?  152 TYR   A CG   1 
ATOM   3234 C CD1  . TYR   A 1 152 ? 18.248 -10.843 13.261  1.00 16.67 ?  152 TYR   A CD1  1 
ATOM   3235 C CD2  . TYR   A 1 152 ? 15.930 -10.430 13.603  1.00 15.73 ?  152 TYR   A CD2  1 
ATOM   3236 C CE1  . TYR   A 1 152 ? 18.205 -11.893 14.154  1.00 18.39 ?  152 TYR   A CE1  1 
ATOM   3237 C CE2  . TYR   A 1 152 ? 15.873 -11.486 14.501  1.00 16.99 ?  152 TYR   A CE2  1 
ATOM   3238 C CZ   . TYR   A 1 152 ? 17.015 -12.212 14.776  1.00 18.18 ?  152 TYR   A CZ   1 
ATOM   3239 O OH   . TYR   A 1 152 ? 16.967 -13.269 15.667  1.00 21.12 ?  152 TYR   A OH   1 
ATOM   3240 H H    . TYR   A 1 152 ? 18.925 -9.785  10.292  1.00 16.67 ?  152 TYR   A H    1 
ATOM   3241 H HA   . TYR   A 1 152 ? 16.242 -10.117 10.539  1.00 16.33 ?  152 TYR   A HA   1 
ATOM   3242 H HB2  . TYR   A 1 152 ? 18.023 -8.526  12.055  1.00 17.64 ?  152 TYR   A HB2  1 
ATOM   3243 H HB3  . TYR   A 1 152 ? 16.442 -8.358  12.167  1.00 17.64 ?  152 TYR   A HB3  1 
ATOM   3244 H HD1  . TYR   A 1 152 ? 19.053 -10.632 12.840  1.00 19.98 ?  152 TYR   A HD1  1 
ATOM   3245 H HD2  . TYR   A 1 152 ? 15.158 -9.943  13.414  1.00 18.85 ?  152 TYR   A HD2  1 
ATOM   3246 H HE1  . TYR   A 1 152 ? 18.974 -12.380 14.340  1.00 22.04 ?  152 TYR   A HE1  1 
ATOM   3247 H HE2  . TYR   A 1 152 ? 15.070 -11.694 14.919  1.00 20.36 ?  152 TYR   A HE2  1 
ATOM   3248 H HH   . TYR   A 1 152 ? 16.190 -13.339 15.973  1.00 25.32 ?  152 TYR   A HH   1 
ATOM   3249 N N    . LEU   A 1 153 ? 15.801 -8.589  8.681   1.00 13.24 ?  153 LEU   A N    1 
ATOM   3250 C CA   . LEU   A 1 153 ? 15.557 -7.692  7.560   1.00 13.19 ?  153 LEU   A CA   1 
ATOM   3251 C C    . LEU   A 1 153 ? 14.557 -6.612  7.941   1.00 13.85 ?  153 LEU   A C    1 
ATOM   3252 O O    . LEU   A 1 153 ? 13.458 -6.915  8.423   1.00 14.66 ?  153 LEU   A O    1 
ATOM   3253 C CB   . LEU   A 1 153 ? 14.991 -8.476  6.377   1.00 13.42 ?  153 LEU   A CB   1 
ATOM   3254 C CG   . LEU   A 1 153 ? 15.940 -9.477  5.720   1.00 13.13 ?  153 LEU   A CG   1 
ATOM   3255 C CD1  . LEU   A 1 153 ? 15.177 -10.369 4.768   1.00 13.45 ?  153 LEU   A CD1  1 
ATOM   3256 C CD2  . LEU   A 1 153 ? 17.062 -8.761  4.988   1.00 13.48 ?  153 LEU   A CD2  1 
ATOM   3257 H H    . LEU   A 1 153 ? 15.225 -9.225  8.745   1.00 15.87 ?  153 LEU   A H    1 
ATOM   3258 H HA   . LEU   A 1 153 ? 16.386 -7.277  7.299   1.00 15.80 ?  153 LEU   A HA   1 
ATOM   3259 H HB2  . LEU   A 1 153 ? 14.214 -8.968  6.688   1.00 16.08 ?  153 LEU   A HB2  1 
ATOM   3260 H HB3  . LEU   A 1 153 ? 14.722 -7.840  5.699   1.00 16.08 ?  153 LEU   A HB3  1 
ATOM   3261 H HG   . LEU   A 1 153 ? 16.340 -10.035 6.412   1.00 15.74 ?  153 LEU   A HG   1 
ATOM   3262 H HD11 . LEU   A 1 153 ? 15.766 -11.065 4.453   1.00 16.11 ?  153 LEU   A HD11 1 
ATOM   3263 H HD12 . LEU   A 1 153 ? 14.424 -10.754 5.240   1.00 16.11 ?  153 LEU   A HD12 1 
ATOM   3264 H HD13 . LEU   A 1 153 ? 14.863 -9.829  4.027   1.00 16.11 ?  153 LEU   A HD13 1 
ATOM   3265 H HD21 . LEU   A 1 153 ? 17.618 -9.417  4.555   1.00 16.15 ?  153 LEU   A HD21 1 
ATOM   3266 H HD22 . LEU   A 1 153 ? 16.666 -8.165  4.333   1.00 16.15 ?  153 LEU   A HD22 1 
ATOM   3267 H HD23 . LEU   A 1 153 ? 17.578 -8.250  5.631   1.00 16.15 ?  153 LEU   A HD23 1 
ATOM   3268 N N    A ALA   A 1 154 ? 14.951 -5.361  7.724   0.58 13.52 ?  154 ALA   A N    1 
ATOM   3269 N N    B ALA   A 1 154 ? 14.919 -5.355  7.687   0.42 13.38 ?  154 ALA   A N    1 
ATOM   3270 C CA   A ALA   A 1 154 ? 14.096 -4.200  7.930   0.58 14.23 ?  154 ALA   A CA   1 
ATOM   3271 C CA   B ALA   A 1 154 ? 14.053 -4.202  7.925   0.42 13.53 ?  154 ALA   A CA   1 
ATOM   3272 C C    A ALA   A 1 154 ? 13.596 -3.722  6.573   0.58 14.37 ?  154 ALA   A C    1 
ATOM   3273 C C    B ALA   A 1 154 ? 13.572 -3.669  6.576   0.42 13.59 ?  154 ALA   A C    1 
ATOM   3274 O O    A ALA   A 1 154 ? 14.397 -3.408  5.684   0.58 15.25 ?  154 ALA   A O    1 
ATOM   3275 O O    B ALA   A 1 154 ? 14.371 -3.157  5.783   0.42 14.39 ?  154 ALA   A O    1 
ATOM   3276 C CB   A ALA   A 1 154 ? 14.864 -3.084  8.637   0.58 15.08 ?  154 ALA   A CB   1 
ATOM   3277 C CB   B ALA   A 1 154 ? 14.800 -3.126  8.711   0.42 13.80 ?  154 ALA   A CB   1 
ATOM   3278 H H    A ALA   A 1 154 ? 15.738 -5.153  7.438   0.58 16.20 ?  154 ALA   A H    1 
ATOM   3279 H H    B ALA   A 1 154 ? 15.688 -5.137  7.363   0.42 16.04 ?  154 ALA   A H    1 
ATOM   3280 H HA   A ALA   A 1 154 ? 13.334 -4.445  8.471   0.58 17.05 ?  154 ALA   A HA   1 
ATOM   3281 H HA   B ALA   A 1 154 ? 13.281 -4.477  8.445   0.42 16.21 ?  154 ALA   A HA   1 
ATOM   3282 H HB1  A ALA   A 1 154 ? 14.272 -2.323  8.757   0.58 18.08 ?  154 ALA   A HB1  1 
ATOM   3283 H HB1  B ALA   A 1 154 ? 14.208 -2.372  8.857   0.42 16.54 ?  154 ALA   A HB1  1 
ATOM   3284 H HB2  A ALA   A 1 154 ? 15.167 -3.408  9.497   0.58 18.08 ?  154 ALA   A HB2  1 
ATOM   3285 H HB2  B ALA   A 1 154 ? 15.085 -3.494  9.562   0.42 16.54 ?  154 ALA   A HB2  1 
ATOM   3286 H HB3  A ALA   A 1 154 ? 15.624 -2.827  8.090   0.58 18.08 ?  154 ALA   A HB3  1 
ATOM   3287 H HB3  B ALA   A 1 154 ? 15.576 -2.843  8.199   0.42 16.54 ?  154 ALA   A HB3  1 
ATOM   3288 N N    A VAL   A 1 155 ? 12.274 -3.686  6.419   0.28 13.31 ?  155 VAL   A N    1 
ATOM   3289 N N    B VAL   A 1 155 ? 12.266 -3.776  6.331   0.42 12.48 ?  155 VAL   A N    1 
ATOM   3290 C CA   A VAL   A 1 155 ? 11.606 -3.179  5.225   0.28 14.03 ?  155 VAL   A CA   1 
ATOM   3291 C CA   B VAL   A 1 155 ? 11.639 -3.418  5.060   0.42 13.94 ?  155 VAL   A CA   1 
ATOM   3292 C CA   T VAL   A 1 155 ? 11.580 -3.272  5.248   0.30 15.83 ?  155 VAL   A CA   1 
ATOM   3293 C C    A VAL   A 1 155 ? 10.927 -1.875  5.613   0.28 14.89 ?  155 VAL   A C    1 
ATOM   3294 C C    B VAL   A 1 155 ? 10.880 -2.113  5.262   0.42 14.25 ?  155 VAL   A C    1 
ATOM   3295 C C    T VAL   A 1 155 ? 11.009 -1.899  5.599   0.30 15.79 ?  155 VAL   A C    1 
ATOM   3296 O O    A VAL   A 1 155 ? 10.003 -1.871  6.434   0.28 15.40 ?  155 VAL   A O    1 
ATOM   3297 O O    B VAL   A 1 155 ? 9.928  -2.058  6.048   0.42 14.22 ?  155 VAL   A O    1 
ATOM   3298 O O    T VAL   A 1 155 ? 10.156 -1.774  6.476   0.30 16.14 ?  155 VAL   A O    1 
ATOM   3299 C CB   A VAL   A 1 155 ? 10.580 -4.188  4.683   0.28 13.65 ?  155 VAL   A CB   1 
ATOM   3300 C CB   B VAL   A 1 155 ? 10.707 -4.535  4.556   0.42 14.27 ?  155 VAL   A CB   1 
ATOM   3301 C CB   T VAL   A 1 155 ? 10.500 -4.229  4.699   0.30 15.46 ?  155 VAL   A CB   1 
ATOM   3302 C CG1  A VAL   A 1 155 ? 9.935  -3.661  3.407   0.28 14.10 ?  155 VAL   A CG1  1 
ATOM   3303 C CG1  B VAL   A 1 155 ? 9.875  -4.055  3.387   0.42 14.97 ?  155 VAL   A CG1  1 
ATOM   3304 C CG1  T VAL   A 1 155 ? 9.884  -3.662  3.430   0.30 15.99 ?  155 VAL   A CG1  1 
ATOM   3305 C CG2  A VAL   A 1 155 ? 11.239 -5.540  4.436   0.28 13.99 ?  155 VAL   A CG2  1 
ATOM   3306 C CG2  B VAL   A 1 155 ? 11.517 -5.762  4.141   0.42 14.96 ?  155 VAL   A CG2  1 
ATOM   3307 C CG2  T VAL   A 1 155 ? 11.094 -5.612  4.438   0.30 15.66 ?  155 VAL   A CG2  1 
ATOM   3308 H H    A VAL   A 1 155 ? 11.723 -3.967  7.016   0.28 15.94 ?  155 VAL   A H    1 
ATOM   3309 H H    B VAL   A 1 155 ? 11.700 -4.067  6.910   0.42 14.95 ?  155 VAL   A H    1 
ATOM   3310 H HA   A VAL   A 1 155 ? 12.259 -2.997  4.533   0.28 16.81 ?  155 VAL   A HA   1 
ATOM   3311 H HA   B VAL   A 1 155 ? 12.321 -3.275  4.388   0.42 16.71 ?  155 VAL   A HA   1 
ATOM   3312 H HB   A VAL   A 1 155 ? 9.880  -4.311  5.343   0.28 16.36 ?  155 VAL   A HB   1 
ATOM   3313 H HB   B VAL   A 1 155 ? 10.107 -4.806  5.269   0.42 17.09 ?  155 VAL   A HB   1 
ATOM   3314 H HB   T VAL   A 1 155 ? 9.798  -4.324  5.361   0.30 18.53 ?  155 VAL   A HB   1 
ATOM   3315 H HG11 A VAL   A 1 155 ? 9.389  -4.363  3.019   0.28 16.90 ?  155 VAL   A HG11 1 
ATOM   3316 H HG11 B VAL   A 1 155 ? 9.499  -4.825  2.931   0.42 17.94 ?  155 VAL   A HG11 1 
ATOM   3317 H HG11 T VAL   A 1 155 ? 9.300  -4.330  3.039   0.30 19.16 ?  155 VAL   A HG11 1 
ATOM   3318 H HG12 A VAL   A 1 155 ? 9.380  -2.895  3.623   0.28 16.90 ?  155 VAL   A HG12 1 
ATOM   3319 H HG12 B VAL   A 1 155 ? 9.161  -3.491  3.720   0.42 17.94 ?  155 VAL   A HG12 1 
ATOM   3320 H HG12 T VAL   A 1 155 ? 9.375  -2.867  3.653   0.30 19.16 ?  155 VAL   A HG12 1 
ATOM   3321 H HG13 A VAL   A 1 155 ? 10.631 -3.402  2.784   0.28 16.90 ?  155 VAL   A HG13 1 
ATOM   3322 H HG13 B VAL   A 1 155 ? 10.443 -3.557  2.782   0.42 17.94 ?  155 VAL   A HG13 1 
ATOM   3323 H HG13 T VAL   A 1 155 ? 10.593 -3.438  2.807   0.30 19.16 ?  155 VAL   A HG13 1 
ATOM   3324 H HG21 A VAL   A 1 155 ? 10.594 -6.132  4.020   0.28 16.76 ?  155 VAL   A HG21 1 
ATOM   3325 H HG21 B VAL   A 1 155 ? 10.931 -6.396  3.697   0.42 17.93 ?  155 VAL   A HG21 1 
ATOM   3326 H HG21 T VAL   A 1 155 ? 10.399 -6.195  4.094   0.30 18.77 ?  155 VAL   A HG21 1 
ATOM   3327 H HG22 A VAL   A 1 155 ? 12.002 -5.415  3.850   0.28 16.76 ?  155 VAL   A HG22 1 
ATOM   3328 H HG22 B VAL   A 1 155 ? 12.220 -5.484  3.531   0.42 17.93 ?  155 VAL   A HG22 1 
ATOM   3329 H HG22 T VAL   A 1 155 ? 11.809 -5.531  3.786   0.30 18.77 ?  155 VAL   A HG22 1 
ATOM   3330 H HG23 A VAL   A 1 155 ? 11.530 -5.909  5.284   0.28 16.76 ?  155 VAL   A HG23 1 
ATOM   3331 H HG23 B VAL   A 1 155 ? 11.907 -6.168  4.930   0.42 17.93 ?  155 VAL   A HG23 1 
ATOM   3332 H HG23 T VAL   A 1 155 ? 11.444 -5.969  5.269   0.30 18.77 ?  155 VAL   A HG23 1 
ATOM   3333 N N    A PHE   A 1 156 ? 11.383 -0.766  5.028   0.28 15.45 ?  156 PHE   A N    1 
ATOM   3334 N N    B PHE   A 1 156 ? 11.283 -1.077  4.524   0.42 15.48 ?  156 PHE   A N    1 
ATOM   3335 N N    T PHE   A 1 156 ? 11.494 -0.869  4.902   0.30 15.59 ?  156 PHE   A N    1 
ATOM   3336 C CA   A PHE   A 1 156 ? 10.853 0.538   5.419   0.28 16.26 ?  156 PHE   A CA   1 
ATOM   3337 C CA   B PHE   A 1 156 ? 10.787 0.281   4.757   0.42 16.14 ?  156 PHE   A CA   1 
ATOM   3338 C CA   T PHE   A 1 156 ? 11.078 0.502   5.198   0.30 15.47 ?  156 PHE   A CA   1 
ATOM   3339 C C    A PHE   A 1 156 ? 9.395  0.706   5.005   0.28 16.24 ?  156 PHE   A C    1 
ATOM   3340 C C    B PHE   A 1 156 ? 9.317  0.428   4.364   0.42 17.10 ?  156 PHE   A C    1 
ATOM   3341 C C    T PHE   A 1 156 ? 9.620  0.744   4.820   0.30 15.26 ?  156 PHE   A C    1 
ATOM   3342 O O    A PHE   A 1 156 ? 8.589  1.262   5.760   0.28 16.83 ?  156 PHE   A O    1 
ATOM   3343 O O    B PHE   A 1 156 ? 8.497  0.899   5.162   0.42 17.94 ?  156 PHE   A O    1 
ATOM   3344 O O    T PHE   A 1 156 ? 8.888  1.425   5.549   0.30 15.67 ?  156 PHE   A O    1 
ATOM   3345 C CB   A PHE   A 1 156 ? 11.711 1.655   4.824   0.28 17.22 ?  156 PHE   A CB   1 
ATOM   3346 C CB   B PHE   A 1 156 ? 11.667 1.255   3.969   0.42 16.26 ?  156 PHE   A CB   1 
ATOM   3347 C CB   T PHE   A 1 156 ? 11.991 1.477   4.449   0.30 15.53 ?  156 PHE   A CB   1 
ATOM   3348 C CG   A PHE   A 1 156 ? 11.185 3.033   5.113   0.28 18.23 ?  156 PHE   A CG   1 
ATOM   3349 C CG   B PHE   A 1 156 ? 11.467 2.709   4.307   0.42 17.41 ?  156 PHE   A CG   1 
ATOM   3350 C CG   T PHE   A 1 156 ? 11.597 2.928   4.592   0.30 16.12 ?  156 PHE   A CG   1 
ATOM   3351 C CD1  A PHE   A 1 156 ? 11.072 3.478   6.418   0.28 18.53 ?  156 PHE   A CD1  1 
ATOM   3352 C CD1  B PHE   A 1 156 ? 12.072 3.264   5.424   0.42 18.90 ?  156 PHE   A CD1  1 
ATOM   3353 C CD1  T PHE   A 1 156 ? 11.919 3.638   5.741   0.30 16.64 ?  156 PHE   A CD1  1 
ATOM   3354 C CD2  A PHE   A 1 156 ? 10.808 3.883   4.084   0.28 19.05 ?  156 PHE   A CD2  1 
ATOM   3355 C CD2  B PHE   A 1 156 ? 10.723 3.530   3.474   0.42 18.33 ?  156 PHE   A CD2  1 
ATOM   3356 C CD2  T PHE   A 1 156 ? 10.931 3.586   3.569   0.30 16.89 ?  156 PHE   A CD2  1 
ATOM   3357 C CE1  A PHE   A 1 156 ? 10.590 4.741   6.696   0.28 19.09 ?  156 PHE   A CE1  1 
ATOM   3358 C CE1  B PHE   A 1 156 ? 11.909 4.603   5.728   0.42 19.68 ?  156 PHE   A CE1  1 
ATOM   3359 C CE1  T PHE   A 1 156 ? 11.566 4.971   5.875   0.30 17.28 ?  156 PHE   A CE1  1 
ATOM   3360 C CE2  A PHE   A 1 156 ? 10.322 5.151   4.356   0.28 19.43 ?  156 PHE   A CE2  1 
ATOM   3361 C CE2  B PHE   A 1 156 ? 10.557 4.873   3.771   0.42 19.41 ?  156 PHE   A CE2  1 
ATOM   3362 C CE2  T PHE   A 1 156 ? 10.577 4.920   3.696   0.30 17.48 ?  156 PHE   A CE2  1 
ATOM   3363 C CZ   A PHE   A 1 156 ? 10.217 5.580   5.664   0.28 19.52 ?  156 PHE   A CZ   1 
ATOM   3364 C CZ   B PHE   A 1 156 ? 11.155 5.411   4.899   0.42 19.91 ?  156 PHE   A CZ   1 
ATOM   3365 C CZ   T PHE   A 1 156 ? 10.897 5.613   4.851   0.30 17.71 ?  156 PHE   A CZ   1 
ATOM   3366 H H    A PHE   A 1 156 ? 11.983 -0.743  4.412   0.28 18.52 ?  156 PHE   A H    1 
ATOM   3367 H H    B PHE   A 1 156 ? 11.846 -1.139  3.884   0.42 18.55 ?  156 PHE   A H    1 
ATOM   3368 H H    T PHE   A 1 156 ? 12.062 -0.938  4.259   0.30 18.68 ?  156 PHE   A H    1 
ATOM   3369 H HA   A PHE   A 1 156 ? 10.898 0.619   6.382   0.28 19.48 ?  156 PHE   A HA   1 
ATOM   3370 H HA   B PHE   A 1 156 ? 10.866 0.492   5.698   0.42 19.34 ?  156 PHE   A HA   1 
ATOM   3371 H HA   T PHE   A 1 156 ? 11.180 0.666   6.149   0.30 18.53 ?  156 PHE   A HA   1 
ATOM   3372 H HB2  A PHE   A 1 156 ? 12.607 1.596   5.194   0.28 20.64 ?  156 PHE   A HB2  1 
ATOM   3373 H HB2  B PHE   A 1 156 ? 12.595 1.033   4.137   0.42 19.49 ?  156 PHE   A HB2  1 
ATOM   3374 H HB2  T PHE   A 1 156 ? 12.895 1.382   4.787   0.30 18.61 ?  156 PHE   A HB2  1 
ATOM   3375 H HB3  A PHE   A 1 156 ? 11.747 1.547   3.861   0.28 20.64 ?  156 PHE   A HB3  1 
ATOM   3376 H HB3  B PHE   A 1 156 ? 11.462 1.148   3.035   0.42 19.49 ?  156 PHE   A HB3  1 
ATOM   3377 H HB3  T PHE   A 1 156 ? 11.970 1.259   3.504   0.30 18.61 ?  156 PHE   A HB3  1 
ATOM   3378 H HD1  A PHE   A 1 156 ? 11.324 2.917   7.117   0.28 22.21 ?  156 PHE   A HD1  1 
ATOM   3379 H HD1  B PHE   A 1 156 ? 12.580 2.723   5.987   0.42 22.65 ?  156 PHE   A HD1  1 
ATOM   3380 H HD1  T PHE   A 1 156 ? 12.369 3.206   6.435   0.30 19.95 ?  156 PHE   A HD1  1 
ATOM   3381 H HD2  A PHE   A 1 156 ? 10.881 3.596   3.202   0.28 22.83 ?  156 PHE   A HD2  1 
ATOM   3382 H HD2  B PHE   A 1 156 ? 10.319 3.173   2.717   0.42 21.98 ?  156 PHE   A HD2  1 
ATOM   3383 H HD2  T PHE   A 1 156 ? 10.711 3.126   2.794   0.30 20.25 ?  156 PHE   A HD2  1 
ATOM   3384 H HE1  A PHE   A 1 156 ? 10.520 5.028   7.579   0.28 22.88 ?  156 PHE   A HE1  1 
ATOM   3385 H HE1  B PHE   A 1 156 ? 12.311 4.960   6.488   0.42 23.59 ?  156 PHE   A HE1  1 
ATOM   3386 H HE1  T PHE   A 1 156 ? 11.784 5.430   6.655   0.30 20.71 ?  156 PHE   A HE1  1 
ATOM   3387 H HE2  A PHE   A 1 156 ? 10.075 5.714   3.659   0.28 23.29 ?  156 PHE   A HE2  1 
ATOM   3388 H HE2  B PHE   A 1 156 ? 10.047 5.415   3.214   0.42 23.27 ?  156 PHE   A HE2  1 
ATOM   3389 H HE2  T PHE   A 1 156 ? 10.124 5.350   3.010   0.30 20.95 ?  156 PHE   A HE2  1 
ATOM   3390 H HZ   A PHE   A 1 156 ? 9.893  6.432   5.851   0.28 23.40 ?  156 PHE   A HZ   1 
ATOM   3391 H HZ   B PHE   A 1 156 ? 11.042 6.311   5.104   0.42 23.87 ?  156 PHE   A HZ   1 
ATOM   3392 H HZ   T PHE   A 1 156 ? 10.659 6.506   4.943   0.30 21.23 ?  156 PHE   A HZ   1 
ATOM   3393 N N    A ASP   A 1 157 ? 9.039  0.239   3.813   0.28 16.23 ?  157 ASP   A N    1 
ATOM   3394 N N    B ASP   A 1 157 ? 8.964  0.051   3.136   0.42 18.43 ?  157 ASP   A N    1 
ATOM   3395 N N    T ASP   A 1 157 ? 9.186  0.206   3.685   0.30 15.51 ?  157 ASP   A N    1 
ATOM   3396 C CA   A ASP   A 1 157 ? 7.718  0.483   3.247   0.28 16.99 ?  157 ASP   A CA   1 
ATOM   3397 C CA   B ASP   A 1 157 ? 7.632  0.341   2.623   0.42 19.45 ?  157 ASP   A CA   1 
ATOM   3398 C CA   T ASP   A 1 157 ? 7.892  0.529   3.096   0.30 15.87 ?  157 ASP   A CA   1 
ATOM   3399 C C    A ASP   A 1 157 ? 6.737  -0.558  3.779   0.28 17.39 ?  157 ASP   A C    1 
ATOM   3400 C C    B ASP   A 1 157 ? 6.616  -0.668  3.145   0.42 19.38 ?  157 ASP   A C    1 
ATOM   3401 C C    T ASP   A 1 157 ? 6.843  -0.457  3.601   0.30 16.21 ?  157 ASP   A C    1 
ATOM   3402 O O    A ASP   A 1 157 ? 6.949  -1.763  3.605   0.28 17.59 ?  157 ASP   A O    1 
ATOM   3403 O O    B ASP   A 1 157 ? 6.783  -1.880  2.982   0.42 18.92 ?  157 ASP   A O    1 
ATOM   3404 O O    T ASP   A 1 157 ? 6.971  -1.667  3.387   0.30 16.31 ?  157 ASP   A O    1 
ATOM   3405 C CB   A ASP   A 1 157 ? 7.808  0.403   1.725   0.28 17.48 ?  157 ASP   A CB   1 
ATOM   3406 C CB   B ASP   A 1 157 ? 7.626  0.359   1.094   0.42 20.26 ?  157 ASP   A CB   1 
ATOM   3407 C CB   T ASP   A 1 157 ? 8.029  0.444   1.576   0.30 15.61 ?  157 ASP   A CB   1 
ATOM   3408 C CG   A ASP   A 1 157 ? 6.589  0.975   1.036   0.28 18.15 ?  157 ASP   A CG   1 
ATOM   3409 C CG   B ASP   A 1 157 ? 6.245  0.626   0.527   0.42 20.94 ?  157 ASP   A CG   1 
ATOM   3410 C CG   T ASP   A 1 157 ? 6.828  0.990   0.844   0.30 15.62 ?  157 ASP   A CG   1 
ATOM   3411 O OD1  A ASP   A 1 157 ? 6.451  2.216   0.995   0.28 18.87 ?  157 ASP   A OD1  1 
ATOM   3412 O OD1  B ASP   A 1 157 ? 5.689  1.710   0.805   0.42 21.75 ?  157 ASP   A OD1  1 
ATOM   3413 O OD1  T ASP   A 1 157 ? 5.737  0.404   1.002   0.30 15.90 ?  157 ASP   A OD1  1 
ATOM   3414 O OD2  A ASP   A 1 157 ? 5.764  0.182   0.536   0.28 17.66 -1 157 ASP   A OD2  1 
ATOM   3415 O OD2  B ASP   A 1 157 ? 5.707  -0.248  -0.186  0.42 20.58 -1 157 ASP   A OD2  1 
ATOM   3416 O OD2  T ASP   A 1 157 ? 6.972  1.999   0.114   0.30 15.25 -1 157 ASP   A OD2  1 
ATOM   3417 H H    A ASP   A 1 157 ? 9.551  -0.231  3.310   0.28 19.45 ?  157 ASP   A H    1 
ATOM   3418 H H    B ASP   A 1 157 ? 9.471  -0.372  2.585   0.42 22.09 ?  157 ASP   A H    1 
ATOM   3419 H H    T ASP   A 1 157 ? 9.644  -0.356  3.220   0.30 18.59 ?  157 ASP   A H    1 
ATOM   3420 H HA   A ASP   A 1 157 ? 7.409  1.370   3.494   0.28 20.36 ?  157 ASP   A HA   1 
ATOM   3421 H HA   B ASP   A 1 157 ? 7.357  1.220   2.926   0.42 23.32 ?  157 ASP   A HA   1 
ATOM   3422 H HA   T ASP   A 1 157 ? 7.631  1.432   3.343   0.30 19.02 ?  157 ASP   A HA   1 
ATOM   3423 H HB2  A ASP   A 1 157 ? 8.589  0.894   1.422   0.28 20.95 ?  157 ASP   A HB2  1 
ATOM   3424 H HB2  B ASP   A 1 157 ? 8.225  1.059   0.792   0.42 24.29 ?  157 ASP   A HB2  1 
ATOM   3425 H HB2  T ASP   A 1 157 ? 8.804  0.950   1.297   0.30 18.71 ?  157 ASP   A HB2  1 
ATOM   3426 H HB3  A ASP   A 1 157 ? 7.886  -0.528  1.461   0.28 20.95 ?  157 ASP   A HB3  1 
ATOM   3427 H HB3  B ASP   A 1 157 ? 7.931  -0.490  0.746   0.42 24.29 ?  157 ASP   A HB3  1 
ATOM   3428 H HB3  T ASP   A 1 157 ? 8.133  -0.489  1.325   0.30 18.71 ?  157 ASP   A HB3  1 
ATOM   3429 N N    A LYS   A 1 158 ? 5.663  -0.098  4.426   0.28 18.04 ?  158 LYS   A N    1 
ATOM   3430 N N    B LYS   A 1 158 ? 5.553  -0.152  3.767   0.42 20.45 ?  158 LYS   A N    1 
ATOM   3431 N N    T LYS   A 1 158 ? 5.800  0.058   4.263   0.30 17.10 ?  158 LYS   A N    1 
ATOM   3432 C CA   A LYS   A 1 158 ? 4.692  -1.033  4.989   0.28 18.87 ?  158 LYS   A CA   1 
ATOM   3433 C CA   B LYS   A 1 158 ? 4.501  -1.006  4.306   0.42 21.44 ?  158 LYS   A CA   1 
ATOM   3434 C CA   T LYS   A 1 158 ? 4.810  -0.830  4.870   0.30 18.11 ?  158 LYS   A CA   1 
ATOM   3435 C C    A LYS   A 1 158 ? 3.948  -1.786  3.894   0.28 18.48 ?  158 LYS   A C    1 
ATOM   3436 C C    B LYS   A 1 158 ? 3.890  -1.877  3.216   0.42 21.04 ?  158 LYS   A C    1 
ATOM   3437 C C    T LYS   A 1 158 ? 4.051  -1.628  3.817   0.30 17.57 ?  158 LYS   A C    1 
ATOM   3438 O O    A LYS   A 1 158 ? 3.724  -2.997  4.009   0.28 18.64 ?  158 LYS   A O    1 
ATOM   3439 O O    B LYS   A 1 158 ? 3.724  -3.089  3.390   0.42 19.98 ?  158 LYS   A O    1 
ATOM   3440 O O    T LYS   A 1 158 ? 3.808  -2.827  3.997   0.30 17.69 ?  158 LYS   A O    1 
ATOM   3441 C CB   A LYS   A 1 158 ? 3.713  -0.298  5.906   0.28 20.07 ?  158 LYS   A CB   1 
ATOM   3442 C CB   B LYS   A 1 158 ? 3.435  -0.133  4.972   0.42 23.29 ?  158 LYS   A CB   1 
ATOM   3443 C CB   T LYS   A 1 158 ? 3.839  -0.040  5.752   0.30 19.85 ?  158 LYS   A CB   1 
ATOM   3444 C CG   A LYS   A 1 158 ? 2.492  -1.119  6.333   0.28 21.27 ?  158 LYS   A CG   1 
ATOM   3445 C CG   B LYS   A 1 158 ? 2.087  -0.801  5.141   0.42 25.26 ?  158 LYS   A CG   1 
ATOM   3446 C CG   T LYS   A 1 158 ? 2.621  -0.845  6.219   0.30 21.60 ?  158 LYS   A CG   1 
ATOM   3447 C CD   A LYS   A 1 158 ? 2.862  -2.377  7.120   0.28 22.34 ?  158 LYS   A CD   1 
ATOM   3448 C CD   B LYS   A 1 158 ? 2.200  -2.059  5.966   0.42 27.10 ?  158 LYS   A CD   1 
ATOM   3449 C CD   T LYS   A 1 158 ? 3.012  -2.066  7.053   0.30 23.41 ?  158 LYS   A CD   1 
ATOM   3450 C CE   A LYS   A 1 158 ? 1.610  -3.082  7.638   0.28 23.06 ?  158 LYS   A CE   1 
ATOM   3451 C CE   B LYS   A 1 158 ? 1.418  -1.947  7.248   0.42 28.25 ?  158 LYS   A CE   1 
ATOM   3452 C CE   T LYS   A 1 158 ? 1.785  -2.890  7.439   0.30 24.72 ?  158 LYS   A CE   1 
ATOM   3453 N NZ   A LYS   A 1 158 ? 1.896  -4.417  8.239   0.28 23.33 ?  158 LYS   A NZ   1 
ATOM   3454 N NZ   B LYS   A 1 158 ? 1.571  -3.175  8.069   0.42 28.94 ?  158 LYS   A NZ   1 
ATOM   3455 N NZ   T LYS   A 1 158 ? 2.133  -4.110  8.224   0.30 25.41 ?  158 LYS   A NZ   1 
ATOM   3456 H H    A LYS   A 1 158 ? 5.482  0.734   4.547   0.28 21.62 ?  158 LYS   A H    1 
ATOM   3457 H H    B LYS   A 1 158 ? 5.419  0.686   3.887   0.42 24.52 ?  158 LYS   A H    1 
ATOM   3458 H H    T LYS   A 1 158 ? 5.648  0.898   4.367   0.30 20.49 ?  158 LYS   A H    1 
ATOM   3459 H HA   A LYS   A 1 158 ? 5.167  -1.685  5.525   0.28 22.62 ?  158 LYS   A HA   1 
ATOM   3460 H HA   B LYS   A 1 158 ? 4.879  -1.590  4.980   0.42 25.70 ?  158 LYS   A HA   1 
ATOM   3461 H HA   T LYS   A 1 158 ? 5.273  -1.462  5.440   0.30 21.71 ?  158 LYS   A HA   1 
ATOM   3462 H HB2  A LYS   A 1 158 ? 4.185  -0.033  6.712   0.28 24.07 ?  158 LYS   A HB2  1 
ATOM   3463 H HB2  B LYS   A 1 158 ? 3.748  0.117   5.857   0.42 27.92 ?  158 LYS   A HB2  1 
ATOM   3464 H HB2  T LYS   A 1 158 ? 4.312  0.262   6.545   0.30 23.79 ?  158 LYS   A HB2  1 
ATOM   3465 H HB3  A LYS   A 1 158 ? 3.389  0.491   5.446   0.28 24.07 ?  158 LYS   A HB3  1 
ATOM   3466 H HB3  B LYS   A 1 158 ? 3.304  0.664   4.436   0.42 27.92 ?  158 LYS   A HB3  1 
ATOM   3467 H HB3  T LYS   A 1 158 ? 3.514  0.725   5.255   0.30 23.79 ?  158 LYS   A HB3  1 
ATOM   3468 H HG2  A LYS   A 1 158 ? 1.935  -0.569  6.903   0.28 25.50 ?  158 LYS   A HG2  1 
ATOM   3469 H HG2  B LYS   A 1 158 ? 1.493  -0.192  5.605   0.42 30.29 ?  158 LYS   A HG2  1 
ATOM   3470 H HG2  T LYS   A 1 158 ? 2.065  -0.277  6.772   0.30 25.90 ?  158 LYS   A HG2  1 
ATOM   3471 H HG3  A LYS   A 1 158 ? 1.990  -1.389  5.548   0.28 25.50 ?  158 LYS   A HG3  1 
ATOM   3472 H HG3  B LYS   A 1 158 ? 1.712  -1.024  4.272   0.42 30.29 ?  158 LYS   A HG3  1 
ATOM   3473 H HG3  T LYS   A 1 158 ? 2.113  -1.151  5.450   0.30 25.90 ?  158 LYS   A HG3  1 
ATOM   3474 H HD2  A LYS   A 1 158 ? 3.343  -2.990  6.543   0.28 26.79 ?  158 LYS   A HD2  1 
ATOM   3475 H HD2  B LYS   A 1 158 ? 1.846  -2.800  5.462   0.42 32.50 ?  158 LYS   A HD2  1 
ATOM   3476 H HD2  T LYS   A 1 158 ? 3.606  -2.635  6.541   0.30 28.06 ?  158 LYS   A HD2  1 
ATOM   3477 H HD3  A LYS   A 1 158 ? 3.411  -2.129  7.882   0.28 26.79 ?  158 LYS   A HD3  1 
ATOM   3478 H HD3  B LYS   A 1 158 ? 3.126  -2.225  6.196   0.42 32.50 ?  158 LYS   A HD3  1 
ATOM   3479 H HD3  T LYS   A 1 158 ? 3.448  -1.772  7.869   0.30 28.06 ?  158 LYS   A HD3  1 
ATOM   3480 H HE2  A LYS   A 1 158 ? 1.193  -2.531  8.319   0.28 27.65 ?  158 LYS   A HE2  1 
ATOM   3481 H HE2  B LYS   A 1 158 ? 1.751  -1.191  7.755   0.42 33.88 ?  158 LYS   A HE2  1 
ATOM   3482 H HE2  T LYS   A 1 158 ? 1.192  -2.346  7.981   0.30 29.64 ?  158 LYS   A HE2  1 
ATOM   3483 H HE3  A LYS   A 1 158 ? 0.996  -3.214  6.901   0.28 27.65 ?  158 LYS   A HE3  1 
ATOM   3484 H HE3  B LYS   A 1 158 ? 0.479  -1.829  7.037   0.42 33.88 ?  158 LYS   A HE3  1 
ATOM   3485 H HE3  T LYS   A 1 158 ? 1.328  -3.176  6.633   0.30 29.64 ?  158 LYS   A HE3  1 
ATOM   3486 H HZ1  A LYS   A 1 158 ? 1.142  -4.791  8.527   0.28 27.98 ?  158 LYS   A HZ1  1 
ATOM   3487 H HZ1  B LYS   A 1 158 ? 1.408  -2.990  8.922   0.42 34.70 ?  158 LYS   A HZ1  1 
ATOM   3488 H HZ1  T LYS   A 1 158 ? 1.394  -4.563  8.430   0.30 30.47 ?  158 LYS   A HZ1  1 
ATOM   3489 H HZ2  A LYS   A 1 158 ? 2.269  -4.950  7.630   0.28 27.98 ?  158 LYS   A HZ2  1 
ATOM   3490 H HZ2  B LYS   A 1 158 ? 1.001  -3.799  7.792   0.42 34.70 ?  158 LYS   A HZ2  1 
ATOM   3491 H HZ2  T LYS   A 1 158 ? 2.670  -4.637  7.747   0.30 30.47 ?  158 LYS   A HZ2  1 
ATOM   3492 H HZ3  A LYS   A 1 158 ? 2.456  -4.329  8.926   0.28 27.98 ?  158 LYS   A HZ3  1 
ATOM   3493 H HZ3  B LYS   A 1 158 ? 2.401  -3.486  7.997   0.42 34.70 ?  158 LYS   A HZ3  1 
ATOM   3494 H HZ3  T LYS   A 1 158 ? 2.549  -3.881  8.977   0.30 30.47 ?  158 LYS   A HZ3  1 
ATOM   3495 N N    A ASN   A 1 159 ? 3.551  -1.092  2.826   0.28 18.54 ?  159 ASN   A N    1 
ATOM   3496 N N    B ASN   A 1 159 ? 3.528  -1.269  2.087   0.42 22.02 ?  159 ASN   A N    1 
ATOM   3497 N N    T ASN   A 1 159 ? 3.651  -0.988  2.725   0.30 17.93 ?  159 ASN   A N    1 
ATOM   3498 C CA   A ASN   A 1 159 ? 2.849  -1.769  1.741   0.28 18.52 ?  159 ASN   A CA   1 
ATOM   3499 C CA   B ASN   A 1 159 ? 2.990  -2.052  0.982   0.42 23.46 ?  159 ASN   A CA   1 
ATOM   3500 C CA   T ASN   A 1 159 ? 2.900  -1.687  1.686   0.30 18.37 ?  159 ASN   A CA   1 
ATOM   3501 C C    A ASN   A 1 159 ? 3.721  -2.852  1.114   0.28 17.45 ?  159 ASN   A C    1 
ATOM   3502 C C    B ASN   A 1 159 ? 4.009  -3.074  0.502   0.42 22.96 ?  159 ASN   A C    1 
ATOM   3503 C C    T ASN   A 1 159 ? 3.716  -2.815  1.053   0.30 18.20 ?  159 ASN   A C    1 
ATOM   3504 O O    A ASN   A 1 159 ? 3.255  -3.967  0.851   0.28 16.50 ?  159 ASN   A O    1 
ATOM   3505 O O    B ASN   A 1 159 ? 3.646  -4.202  0.147   0.42 23.08 ?  159 ASN   A O    1 
ATOM   3506 O O    T ASN   A 1 159 ? 3.176  -3.857  0.696   0.30 17.85 ?  159 ASN   A O    1 
ATOM   3507 C CB   A ASN   A 1 159 ? 2.378  -0.751  0.699   0.28 19.59 ?  159 ASN   A CB   1 
ATOM   3508 C CB   B ASN   A 1 159 ? 2.548  -1.120  -0.143  0.42 25.33 ?  159 ASN   A CB   1 
ATOM   3509 C CB   T ASN   A 1 159 ? 2.401  -0.709  0.620   0.30 19.20 ?  159 ASN   A CB   1 
ATOM   3510 C CG   A ASN   A 1 159 ? 1.151  0.020   1.154   0.28 20.77 ?  159 ASN   A CG   1 
ATOM   3511 C CG   B ASN   A 1 159 ? 1.483  -0.146  0.306   0.42 27.41 ?  159 ASN   A CG   1 
ATOM   3512 C CG   T ASN   A 1 159 ? 1.182  0.072   1.075   0.30 20.18 ?  159 ASN   A CG   1 
ATOM   3513 O OD1  A ASN   A 1 159 ? 0.315  -0.509  1.884   0.28 21.70 ?  159 ASN   A OD1  1 
ATOM   3514 O OD1  B ASN   A 1 159 ? 1.733  1.054   0.430   0.42 28.60 ?  159 ASN   A OD1  1 
ATOM   3515 O OD1  T ASN   A 1 159 ? 0.391  -0.416  1.878   0.30 21.12 ?  159 ASN   A OD1  1 
ATOM   3516 N ND2  A ASN   A 1 159 ? 1.037  1.272   0.724   0.28 21.19 ?  159 ASN   A ND2  1 
ATOM   3517 N ND2  B ASN   A 1 159 ? 0.286  -0.661  0.563   0.42 28.11 ?  159 ASN   A ND2  1 
ATOM   3518 N ND2  T ASN   A 1 159 ? 1.024  1.287   0.564   0.30 20.52 ?  159 ASN   A ND2  1 
ATOM   3519 H H    A ASN   A 1 159 ? 3.676  -0.249  2.709   0.28 22.22 ?  159 ASN   A H    1 
ATOM   3520 H H    B ASN   A 1 159 ? 3.587  -0.427  1.937   0.42 26.40 ?  159 ASN   A H    1 
ATOM   3521 H H    T ASN   A 1 159 ? 3.792  -0.155  2.567   0.30 21.49 ?  159 ASN   A H    1 
ATOM   3522 H HA   A ASN   A 1 159 ? 2.061  -2.200  2.104   0.28 22.20 ?  159 ASN   A HA   1 
ATOM   3523 H HA   B ASN   A 1 159 ? 2.211  -2.540  1.283   0.42 28.12 ?  159 ASN   A HA   1 
ATOM   3524 H HA   T ASN   A 1 159 ? 2.123  -2.094  2.095   0.30 22.02 ?  159 ASN   A HA   1 
ATOM   3525 H HB2  A ASN   A 1 159 ? 3.083  -0.109  0.535   0.28 23.49 ?  159 ASN   A HB2  1 
ATOM   3526 H HB2  B ASN   A 1 159 ? 3.311  -0.609  -0.450  0.42 30.37 ?  159 ASN   A HB2  1 
ATOM   3527 H HB2  T ASN   A 1 159 ? 3.101  -0.074  0.416   0.30 23.02 ?  159 ASN   A HB2  1 
ATOM   3528 H HB3  A ASN   A 1 159 ? 2.150  -1.216  -0.121  0.28 23.49 ?  159 ASN   A HB3  1 
ATOM   3529 H HB3  B ASN   A 1 159 ? 2.180  -1.645  -0.868  0.42 30.37 ?  159 ASN   A HB3  1 
ATOM   3530 H HB3  T ASN   A 1 159 ? 2.159  -1.209  -0.177  0.30 23.02 ?  159 ASN   A HB3  1 
ATOM   3531 H HD21 A ASN   A 1 159 ? 0.357  1.746   0.954   0.28 25.41 ?  159 ASN   A HD21 1 
ATOM   3532 H HD21 B ASN   A 1 159 ? -0.354 -0.152  0.830   0.42 33.71 ?  159 ASN   A HD21 1 
ATOM   3533 H HD21 T ASN   A 1 159 ? 0.345  1.763   0.791   0.30 24.60 ?  159 ASN   A HD21 1 
ATOM   3534 H HD22 A ASN   A 1 159 ? 1.642  1.608   0.217   0.28 25.41 ?  159 ASN   A HD22 1 
ATOM   3535 H HD22 B ASN   A 1 159 ? 0.151  -1.504  0.460   0.42 33.71 ?  159 ASN   A HD22 1 
ATOM   3536 H HD22 T ASN   A 1 159 ? 1.601  1.593   0.009   0.30 24.60 ?  159 ASN   A HD22 1 
ATOM   3537 N N    A LEU   A 1 160 ? 5.001  -2.561  0.898   0.28 16.90 ?  160 LEU   A N    1 
ATOM   3538 N N    B LEU   A 1 160 ? 5.292  -2.703  0.505   0.42 22.07 ?  160 LEU   A N    1 
ATOM   3539 N N    T LEU   A 1 160 ? 5.019  -2.618  0.926   0.30 17.98 ?  160 LEU   A N    1 
ATOM   3540 C CA   A LEU   A 1 160 ? 5.881  -3.584  0.346   0.28 16.43 ?  160 LEU   A CA   1 
ATOM   3541 C CA   B LEU   A 1 160 ? 6.346  -3.671  0.218   0.42 21.10 ?  160 LEU   A CA   1 
ATOM   3542 C CA   T LEU   A 1 160 ? 5.875  -3.663  0.377   0.30 17.60 ?  160 LEU   A CA   1 
ATOM   3543 C C    A LEU   A 1 160 ? 6.059  -4.738  1.322   0.28 15.85 ?  160 LEU   A C    1 
ATOM   3544 C C    B LEU   A 1 160 ? 6.333  -4.801  1.241   0.42 19.47 ?  160 LEU   A C    1 
ATOM   3545 O O    A LEU   A 1 160 ? 6.077  -5.905  0.913   0.28 15.73 ?  160 LEU   A O    1 
ATOM   3546 O O    B LEU   A 1 160 ? 6.244  -5.982  0.885   0.42 19.21 ?  160 LEU   A O    1 
ATOM   3547 C CB   A LEU   A 1 160 ? 7.231  -2.977  -0.021  0.28 16.62 ?  160 LEU   A CB   1 
ATOM   3548 C CB   B LEU   A 1 160 ? 7.709  -2.971  0.206   0.42 22.03 ?  160 LEU   A CB   1 
ATOM   3549 C CB   T LEU   A 1 160 ? 7.218  -3.085  -0.051  0.30 17.28 ?  160 LEU   A CB   1 
ATOM   3550 C CG   A LEU   A 1 160 ? 8.292  -3.997  -0.428  0.28 17.12 ?  160 LEU   A CG   1 
ATOM   3551 C CG   B LEU   A 1 160 ? 8.958  -3.828  -0.012  0.42 23.03 ?  160 LEU   A CG   1 
ATOM   3552 C CG   T LEU   A 1 160 ? 8.265  -4.110  -0.484  0.30 17.38 ?  160 LEU   A CG   1 
ATOM   3553 C CD1  A LEU   A 1 160 ? 7.820  -4.800  -1.623  0.28 17.73 ?  160 LEU   A CD1  1 
ATOM   3554 C CD1  B LEU   A 1 160 ? 8.806  -4.668  -1.264  0.42 23.19 ?  160 LEU   A CD1  1 
ATOM   3555 C CD1  T LEU   A 1 160 ? 7.814  -4.851  -1.725  0.30 17.96 ?  160 LEU   A CD1  1 
ATOM   3556 C CD2  A LEU   A 1 160 ? 9.601  -3.300  -0.727  0.28 17.14 ?  160 LEU   A CD2  1 
ATOM   3557 C CD2  B LEU   A 1 160 ? 10.222 -2.964  -0.084  0.42 23.41 ?  160 LEU   A CD2  1 
ATOM   3558 C CD2  T LEU   A 1 160 ? 9.592  -3.418  -0.725  0.30 17.22 ?  160 LEU   A CD2  1 
ATOM   3559 H H    A LEU   A 1 160 ? 5.376  -1.810  1.072   0.28 20.26 ?  160 LEU   A H    1 
ATOM   3560 H H    B LEU   A 1 160 ? 5.575  -1.903  0.674   0.42 26.46 ?  160 LEU   A H    1 
ATOM   3561 H H    T LEU   A 1 160 ? 5.431  -1.900  1.151   0.30 21.55 ?  160 LEU   A H    1 
ATOM   3562 H HA   A LEU   A 1 160 ? 5.481  -3.937  -0.460  0.28 19.69 ?  160 LEU   A HA   1 
ATOM   3563 H HA   B LEU   A 1 160 ? 6.193  -4.049  -0.661  0.42 25.30 ?  160 LEU   A HA   1 
ATOM   3564 H HB2  A LEU   A 1 160 ? 7.105  -2.362  -0.763  0.28 19.92 ?  160 LEU   A HB2  1 
ATOM   3565 H HB2  B LEU   A 1 160 ? 7.700  -2.297  -0.491  0.42 26.41 ?  160 LEU   A HB2  1 
ATOM   3566 H HB2  T LEU   A 1 160 ? 7.074  -2.483  -0.798  0.30 20.72 ?  160 LEU   A HB2  1 
ATOM   3567 H HB3  A LEU   A 1 160 ? 7.569  -2.497  0.749   0.28 19.92 ?  160 LEU   A HB3  1 
ATOM   3568 H HB3  B LEU   A 1 160 ? 7.827  -2.544  1.066   0.42 26.41 ?  160 LEU   A HB3  1 
ATOM   3569 H HB3  T LEU   A 1 160 ? 7.587  -2.591  0.697   0.30 20.72 ?  160 LEU   A HB3  1 
ATOM   3570 H HG   A LEU   A 1 160 ? 8.449  -4.610  0.307   0.28 20.52 ?  160 LEU   A HG   1 
ATOM   3571 H HG   B LEU   A 1 160 ? 9.060  -4.430  0.741   0.42 27.61 ?  160 LEU   A HG   1 
ATOM   3572 H HG   T LEU   A 1 160 ? 8.390  -4.757  0.228   0.30 20.83 ?  160 LEU   A HG   1 
ATOM   3573 H HD11 A LEU   A 1 160 ? 8.535  -5.387  -1.904  0.28 21.26 ?  160 LEU   A HD11 1 
ATOM   3574 H HD11 B LEU   A 1 160 ? 9.629  -5.156  -1.411  0.42 27.81 ?  160 LEU   A HD11 1 
ATOM   3575 H HD11 T LEU   A 1 160 ? 8.518  -5.456  -2.003  0.30 21.52 ?  160 LEU   A HD11 1 
ATOM   3576 H HD12 A LEU   A 1 160 ? 7.043  -5.322  -1.369  0.28 21.26 ?  160 LEU   A HD12 1 
ATOM   3577 H HD12 B LEU   A 1 160 ? 8.072  -5.288  -1.139  0.42 27.81 ?  160 LEU   A HD12 1 
ATOM   3578 H HD12 T LEU   A 1 160 ? 7.009  -5.349  -1.518  0.30 21.52 ?  160 LEU   A HD12 1 
ATOM   3579 H HD13 A LEU   A 1 160 ? 7.588  -4.189  -2.341  0.28 21.26 ?  160 LEU   A HD13 1 
ATOM   3580 H HD13 B LEU   A 1 160 ? 8.626  -4.083  -2.016  0.42 27.81 ?  160 LEU   A HD13 1 
ATOM   3581 H HD13 T LEU   A 1 160 ? 7.634  -4.206  -2.427  0.30 21.52 ?  160 LEU   A HD13 1 
ATOM   3582 H HD21 A LEU   A 1 160 ? 10.261 -3.964  -0.980  0.28 20.54 ?  160 LEU   A HD21 1 
ATOM   3583 H HD21 B LEU   A 1 160 ? 10.995 -3.542  -0.191  0.42 28.07 ?  160 LEU   A HD21 1 
ATOM   3584 H HD21 T LEU   A 1 160 ? 10.249 -4.077  -0.999  0.30 20.64 ?  160 LEU   A HD21 1 
ATOM   3585 H HD22 A LEU   A 1 160 ? 9.467  -2.672  -1.453  0.28 20.54 ?  160 LEU   A HD22 1 
ATOM   3586 H HD22 B LEU   A 1 160 ? 10.152 -2.363  -0.843  0.42 28.07 ?  160 LEU   A HD22 1 
ATOM   3587 H HD22 T LEU   A 1 160 ? 9.481  -2.752  -1.423  0.30 20.64 ?  160 LEU   A HD22 1 
ATOM   3588 H HD23 A LEU   A 1 160 ? 9.897  -2.827  0.068   0.28 20.54 ?  160 LEU   A HD23 1 
ATOM   3589 H HD23 B LEU   A 1 160 ? 10.305 -2.451  0.736   0.42 28.07 ?  160 LEU   A HD23 1 
ATOM   3590 H HD23 T LEU   A 1 160 ? 9.880  -2.987  0.096   0.30 20.64 ?  160 LEU   A HD23 1 
ATOM   3591 N N    A TYR   A 1 161 ? 6.190  -4.433  2.615   0.58 17.30 ?  161 TYR   A N    1 
ATOM   3592 N N    B TYR   A 1 161 ? 6.435  -4.451  2.527   0.42 18.47 ?  161 TYR   A N    1 
ATOM   3593 C CA   A TYR   A 1 161 ? 6.341  -5.484  3.614   0.58 17.25 ?  161 TYR   A CA   1 
ATOM   3594 C CA   B TYR   A 1 161 ? 6.443  -5.468  3.575   0.42 17.99 ?  161 TYR   A CA   1 
ATOM   3595 C C    A TYR   A 1 161 ? 5.201  -6.491  3.534   0.58 17.83 ?  161 TYR   A C    1 
ATOM   3596 C C    B TYR   A 1 161 ? 5.215  -6.364  3.483   0.42 18.60 ?  161 TYR   A C    1 
ATOM   3597 O O    A TYR   A 1 161 ? 5.433  -7.705  3.467   0.58 17.34 ?  161 TYR   A O    1 
ATOM   3598 O O    B TYR   A 1 161 ? 5.318  -7.589  3.619   0.42 18.34 ?  161 TYR   A O    1 
ATOM   3599 C CB   A TYR   A 1 161 ? 6.420  -4.882  5.017   0.58 17.46 ?  161 TYR   A CB   1 
ATOM   3600 C CB   B TYR   A 1 161 ? 6.522  -4.808  4.955   0.42 17.46 ?  161 TYR   A CB   1 
ATOM   3601 C CG   A TYR   A 1 161 ? 6.350  -5.938  6.087   0.58 16.83 ?  161 TYR   A CG   1 
ATOM   3602 C CG   B TYR   A 1 161 ? 6.395  -5.780  6.117   0.42 16.42 ?  161 TYR   A CG   1 
ATOM   3603 C CD1  A TYR   A 1 161 ? 7.464  -6.697  6.410   0.58 16.97 ?  161 TYR   A CD1  1 
ATOM   3604 C CD1  B TYR   A 1 161 ? 7.513  -6.416  6.647   0.42 15.93 ?  161 TYR   A CD1  1 
ATOM   3605 C CD2  A TYR   A 1 161 ? 5.159  -6.197  6.757   0.58 16.77 ?  161 TYR   A CD2  1 
ATOM   3606 C CD2  B TYR   A 1 161 ? 5.158  -6.037  6.705   0.42 16.62 ?  161 TYR   A CD2  1 
ATOM   3607 C CE1  A TYR   A 1 161 ? 7.399  -7.675  7.374   0.58 16.32 ?  161 TYR   A CE1  1 
ATOM   3608 C CE1  B TYR   A 1 161 ? 7.400  -7.301  7.712   0.42 15.79 ?  161 TYR   A CE1  1 
ATOM   3609 C CE2  A TYR   A 1 161 ? 5.086  -7.177  7.724   0.58 16.38 ?  161 TYR   A CE2  1 
ATOM   3610 C CE2  B TYR   A 1 161 ? 5.038  -6.918  7.772   0.42 16.66 ?  161 TYR   A CE2  1 
ATOM   3611 C CZ   A TYR   A 1 161 ? 6.208  -7.912  8.029   0.58 16.20 ?  161 TYR   A CZ   1 
ATOM   3612 C CZ   B TYR   A 1 161 ? 6.160  -7.541  8.272   0.42 16.49 ?  161 TYR   A CZ   1 
ATOM   3613 O OH   A TYR   A 1 161 ? 6.149  -8.890  8.992   0.58 15.93 ?  161 TYR   A OH   1 
ATOM   3614 O OH   B TYR   A 1 161 ? 6.047  -8.419  9.328   0.42 17.61 ?  161 TYR   A OH   1 
ATOM   3615 H H    A TYR   A 1 161 ? 6.177  -3.637  2.937   0.58 20.73 ?  161 TYR   A H    1 
ATOM   3616 H H    B TYR   A 1 161 ? 6.492  -3.643  2.812   0.42 22.14 ?  161 TYR   A H    1 
ATOM   3617 H HA   A TYR   A 1 161 ? 7.162  -5.963  3.451   0.58 20.68 ?  161 TYR   A HA   1 
ATOM   3618 H HA   B TYR   A 1 161 ? 7.226  -6.023  3.465   0.42 21.56 ?  161 TYR   A HA   1 
ATOM   3619 H HB2  A TYR   A 1 161 ? 7.265  -4.414  5.114   0.58 20.92 ?  161 TYR   A HB2  1 
ATOM   3620 H HB2  B TYR   A 1 161 ? 7.379  -4.360  5.038   0.42 20.93 ?  161 TYR   A HB2  1 
ATOM   3621 H HB3  A TYR   A 1 161 ? 5.681  -4.268  5.149   0.58 20.92 ?  161 TYR   A HB3  1 
ATOM   3622 H HB3  B TYR   A 1 161 ? 5.806  -4.157  5.035   0.42 20.93 ?  161 TYR   A HB3  1 
ATOM   3623 H HD1  A TYR   A 1 161 ? 8.266  -6.545  5.968   0.58 20.33 ?  161 TYR   A HD1  1 
ATOM   3624 H HD1  B TYR   A 1 161 ? 8.349  -6.256  6.278   0.42 19.09 ?  161 TYR   A HD1  1 
ATOM   3625 H HD2  A TYR   A 1 161 ? 4.397  -5.703  6.553   0.58 20.10 ?  161 TYR   A HD2  1 
ATOM   3626 H HD2  B TYR   A 1 161 ? 4.396  -5.618  6.379   0.42 19.92 ?  161 TYR   A HD2  1 
ATOM   3627 H HE1  A TYR   A 1 161 ? 8.153  -8.181  7.580   0.58 19.56 ?  161 TYR   A HE1  1 
ATOM   3628 H HE1  B TYR   A 1 161 ? 8.157  -7.724  8.055   0.42 18.93 ?  161 TYR   A HE1  1 
ATOM   3629 H HE2  A TYR   A 1 161 ? 4.280  -7.341  8.166   0.58 19.63 ?  161 TYR   A HE2  1 
ATOM   3630 H HE2  B TYR   A 1 161 ? 4.203  -7.085  8.154   0.42 19.97 ?  161 TYR   A HE2  1 
ATOM   3631 H HH   A TYR   A 1 161 ? 5.365  -8.930  9.311   0.58 19.09 ?  161 TYR   A HH   1 
ATOM   3632 H HH   B TYR   A 1 161 ? 5.250  -8.435  9.614   0.42 21.11 ?  161 TYR   A HH   1 
ATOM   3633 N N    A ASP   A 1 162 ? 3.955  -6.005  3.552   0.58 18.42 ?  162 ASP   A N    1 
ATOM   3634 N N    B ASP   A 1 162 ? 4.042  -5.769  3.255   0.42 19.13 ?  162 ASP   A N    1 
ATOM   3635 C CA   A ASP   A 1 162 ? 2.812  -6.910  3.461   0.58 18.90 ?  162 ASP   A CA   1 
ATOM   3636 C CA   B ASP   A 1 162 ? 2.814  -6.555  3.197   0.42 20.03 ?  162 ASP   A CA   1 
ATOM   3637 C C    A ASP   A 1 162 ? 2.858  -7.711  2.170   0.58 19.39 ?  162 ASP   A C    1 
ATOM   3638 C C    B ASP   A 1 162 ? 2.857  -7.585  2.072   0.42 20.92 ?  162 ASP   A C    1 
ATOM   3639 O O    A ASP   A 1 162 ? 2.531  -8.904  2.157   0.58 20.19 ?  162 ASP   A O    1 
ATOM   3640 O O    B ASP   A 1 162 ? 2.437  -8.733  2.258   0.42 21.23 ?  162 ASP   A O    1 
ATOM   3641 C CB   A ASP   A 1 162 ? 1.497  -6.132  3.550   0.58 19.23 ?  162 ASP   A CB   1 
ATOM   3642 C CB   B ASP   A 1 162 ? 1.607  -5.627  3.050   0.42 20.40 ?  162 ASP   A CB   1 
ATOM   3643 C CG   A ASP   A 1 162 ? 1.247  -5.543  4.922   0.58 20.37 ?  162 ASP   A CG   1 
ATOM   3644 C CG   B ASP   A 1 162 ? 1.230  -4.954  4.352   0.42 20.86 ?  162 ASP   A CG   1 
ATOM   3645 O OD1  A ASP   A 1 162 ? 1.897  -5.971  5.896   0.58 20.74 ?  162 ASP   A OD1  1 
ATOM   3646 O OD1  B ASP   A 1 162 ? 1.777  -5.336  5.410   0.42 21.06 ?  162 ASP   A OD1  1 
ATOM   3647 O OD2  A ASP   A 1 162 ? 0.373  -4.656  5.023   0.58 20.80 -1 162 ASP   A OD2  1 
ATOM   3648 O OD2  B ASP   A 1 162 ? 0.383  -4.037  4.320   0.42 21.38 -1 162 ASP   A OD2  1 
ATOM   3649 H H    A ASP   A 1 162 ? 3.744  -5.172  3.609   0.58 22.08 ?  162 ASP   A H    1 
ATOM   3650 H H    B ASP   A 1 162 ? 3.935  -4.920  3.145   0.42 22.94 ?  162 ASP   A H    1 
ATOM   3651 H HA   A ASP   A 1 162 ? 2.836  -7.538  4.198   0.58 22.66 ?  162 ASP   A HA   1 
ATOM   3652 H HA   B ASP   A 1 162 ? 2.711  -7.030  4.034   0.42 24.01 ?  162 ASP   A HA   1 
ATOM   3653 H HB2  A ASP   A 1 162 ? 1.511  -5.402  2.916   0.58 23.06 ?  162 ASP   A HB2  1 
ATOM   3654 H HB2  B ASP   A 1 162 ? 1.806  -4.937  2.393   0.42 24.45 ?  162 ASP   A HB2  1 
ATOM   3655 H HB3  A ASP   A 1 162 ? 0.755  -6.730  3.353   0.58 23.06 ?  162 ASP   A HB3  1 
ATOM   3656 H HB3  B ASP   A 1 162 ? 0.837  -6.139  2.770   0.42 24.45 ?  162 ASP   A HB3  1 
ATOM   3657 N N    A LYS   A 1 163 ? 3.257  -7.071  1.068   0.58 20.17 ?  163 LYS   A N    1 
ATOM   3658 N N    B LYS   A 1 163 ? 3.365  -7.199  0.898   0.42 21.97 ?  163 LYS   A N    1 
ATOM   3659 C CA   A LYS   A 1 163 ? 3.390  -7.805  -0.186  0.58 20.85 ?  163 LYS   A CA   1 
ATOM   3660 C CA   B LYS   A 1 163 ? 3.389  -8.134  -0.225  0.42 22.70 ?  163 LYS   A CA   1 
ATOM   3661 C C    A LYS   A 1 163 ? 4.487  -8.859  -0.092  0.58 19.72 ?  163 LYS   A C    1 
ATOM   3662 C C    B LYS   A 1 163 ? 4.426  -9.235  -0.014  0.42 21.78 ?  163 LYS   A C    1 
ATOM   3663 O O    A LYS   A 1 163 ? 4.353  -9.954  -0.649  0.58 19.03 ?  163 LYS   A O    1 
ATOM   3664 O O    B LYS   A 1 163 ? 4.160  -10.409 -0.299  0.42 21.77 ?  163 LYS   A O    1 
ATOM   3665 C CB   A LYS   A 1 163 ? 3.662  -6.848  -1.349  0.58 23.24 ?  163 LYS   A CB   1 
ATOM   3666 C CB   B LYS   A 1 163 ? 3.654  -7.387  -1.534  0.42 24.83 ?  163 LYS   A CB   1 
ATOM   3667 C CG   A LYS   A 1 163 ? 3.746  -7.568  -2.689  0.58 25.86 ?  163 LYS   A CG   1 
ATOM   3668 C CG   B LYS   A 1 163 ? 3.276  -8.183  -2.779  0.42 27.11 ?  163 LYS   A CG   1 
ATOM   3669 C CD   A LYS   A 1 163 ? 4.196  -6.659  -3.815  0.58 28.55 ?  163 LYS   A CD   1 
ATOM   3670 C CD   B LYS   A 1 163 ? 4.139  -7.821  -3.980  0.42 29.06 ?  163 LYS   A CD   1 
ATOM   3671 C CE   A LYS   A 1 163 ? 4.144  -7.392  -5.148  0.58 30.55 ?  163 LYS   A CE   1 
ATOM   3672 C CE   B LYS   A 1 163 ? 3.899  -6.399  -4.467  0.42 30.63 ?  163 LYS   A CE   1 
ATOM   3673 N NZ   A LYS   A 1 163 ? 4.818  -6.638  -6.240  0.58 31.87 ?  163 LYS   A NZ   1 
ATOM   3674 N NZ   B LYS   A 1 163 ? 4.745  -6.084  -5.655  0.42 31.54 ?  163 LYS   A NZ   1 
ATOM   3675 H H    A LYS   A 1 163 ? 3.449  -6.229  1.023   0.58 24.18 ?  163 LYS   A H    1 
ATOM   3676 H H    B LYS   A 1 163 ? 3.686  -6.416  0.729   0.42 26.34 ?  163 LYS   A H    1 
ATOM   3677 H HA   A LYS   A 1 163 ? 2.555  -8.257  -0.369  0.58 24.99 ?  163 LYS   A HA   1 
ATOM   3678 H HA   B LYS   A 1 163 ? 2.520  -8.554  -0.297  0.42 27.22 ?  163 LYS   A HA   1 
ATOM   3679 H HB2  A LYS   A 1 163 ? 2.937  -6.199  -1.405  0.58 27.86 ?  163 LYS   A HB2  1 
ATOM   3680 H HB2  B LYS   A 1 163 ? 3.134  -6.567  -1.540  0.42 29.77 ?  163 LYS   A HB2  1 
ATOM   3681 H HB3  A LYS   A 1 163 ? 4.501  -6.390  -1.198  0.58 27.86 ?  163 LYS   A HB3  1 
ATOM   3682 H HB3  B LYS   A 1 163 ? 4.598  -7.177  -1.592  0.42 29.77 ?  163 LYS   A HB3  1 
ATOM   3683 H HG2  A LYS   A 1 163 ? 4.386  -8.294  -2.624  0.58 31.01 ?  163 LYS   A HG2  1 
ATOM   3684 H HG2  B LYS   A 1 163 ? 3.391  -9.129  -2.600  0.42 32.51 ?  163 LYS   A HG2  1 
ATOM   3685 H HG3  A LYS   A 1 163 ? 2.870  -7.918  -2.915  0.58 31.01 ?  163 LYS   A HG3  1 
ATOM   3686 H HG3  B LYS   A 1 163 ? 2.350  -7.998  -3.007  0.42 32.51 ?  163 LYS   A HG3  1 
ATOM   3687 H HD2  A LYS   A 1 163 ? 3.607  -5.892  -3.864  0.58 34.24 ?  163 LYS   A HD2  1 
ATOM   3688 H HD2  B LYS   A 1 163 ? 5.074  -7.900  -3.735  0.42 34.84 ?  163 LYS   A HD2  1 
ATOM   3689 H HD3  A LYS   A 1 163 ? 5.110  -6.377  -3.655  0.58 34.24 ?  163 LYS   A HD3  1 
ATOM   3690 H HD3  B LYS   A 1 163 ? 3.935  -8.425  -4.711  0.42 34.84 ?  163 LYS   A HD3  1 
ATOM   3691 H HE2  A LYS   A 1 163 ? 4.574  -8.256  -5.055  0.58 36.63 ?  163 LYS   A HE2  1 
ATOM   3692 H HE2  B LYS   A 1 163 ? 2.968  -6.298  -4.721  0.42 36.73 ?  163 LYS   A HE2  1 
ATOM   3693 H HE3  A LYS   A 1 163 ? 3.217  -7.515  -5.401  0.58 36.63 ?  163 LYS   A HE3  1 
ATOM   3694 H HE3  B LYS   A 1 163 ? 4.124  -5.774  -3.760  0.42 36.73 ?  163 LYS   A HE3  1 
ATOM   3695 H HZ1  A LYS   A 1 163 ? 4.768  -7.096  -7.002  0.58 38.22 ?  163 LYS   A HZ1  1 
ATOM   3696 H HZ1  B LYS   A 1 163 ? 4.595  -5.251  -5.927  0.42 37.83 ?  163 LYS   A HZ1  1 
ATOM   3697 H HZ2  A LYS   A 1 163 ? 4.423  -5.848  -6.351  0.58 38.22 ?  163 LYS   A HZ2  1 
ATOM   3698 H HZ2  B LYS   A 1 163 ? 5.608  -6.168  -5.446  0.42 37.83 ?  163 LYS   A HZ2  1 
ATOM   3699 H HZ3  A LYS   A 1 163 ? 5.674  -6.507  -6.036  0.58 38.22 ?  163 LYS   A HZ3  1 
ATOM   3700 H HZ3  B LYS   A 1 163 ? 4.556  -6.645  -6.321  0.42 37.83 ?  163 LYS   A HZ3  1 
ATOM   3701 N N    A LEU   A 1 164 ? 5.587  -8.544  0.596   0.58 17.75 ?  164 LEU   A N    1 
ATOM   3702 N N    B LEU   A 1 164 ? 5.614  -8.875  0.476   0.42 20.44 ?  164 LEU   A N    1 
ATOM   3703 C CA   A LEU   A 1 164 ? 6.673  -9.513  0.731   0.58 16.73 ?  164 LEU   A CA   1 
ATOM   3704 C CA   B LEU   A 1 164 ? 6.653  -9.875  0.712   0.42 20.06 ?  164 LEU   A CA   1 
ATOM   3705 C C    A LEU   A 1 164 ? 6.232  -10.724 1.545   0.58 16.56 ?  164 LEU   A C    1 
ATOM   3706 C C    B LEU   A 1 164 ? 6.205  -10.894 1.747   0.42 20.61 ?  164 LEU   A C    1 
ATOM   3707 O O    A LEU   A 1 164 ? 6.524  -11.868 1.177   0.58 16.12 ?  164 LEU   A O    1 
ATOM   3708 O O    B LEU   A 1 164 ? 6.474  -12.092 1.610   0.42 20.13 ?  164 LEU   A O    1 
ATOM   3709 C CB   A LEU   A 1 164 ? 7.885  -8.845  1.380   0.58 16.25 ?  164 LEU   A CB   1 
ATOM   3710 C CB   B LEU   A 1 164 ? 7.931  -9.187  1.187   0.42 19.48 ?  164 LEU   A CB   1 
ATOM   3711 C CG   A LEU   A 1 164 ? 8.711  -7.903  0.498   0.58 15.93 ?  164 LEU   A CG   1 
ATOM   3712 C CG   B LEU   A 1 164 ? 8.658  -8.305  0.176   0.42 19.18 ?  164 LEU   A CG   1 
ATOM   3713 C CD1  A LEU   A 1 164 ? 9.617  -7.038  1.356   0.58 15.95 ?  164 LEU   A CD1  1 
ATOM   3714 C CD1  B LEU   A 1 164 ? 9.762  -7.532  0.871   0.42 18.67 ?  164 LEU   A CD1  1 
ATOM   3715 C CD2  A LEU   A 1 164 ? 9.538  -8.674  -0.529  0.58 15.57 ?  164 LEU   A CD2  1 
ATOM   3716 C CD2  B LEU   A 1 164 ? 9.219  -9.160  -0.940  0.42 19.58 ?  164 LEU   A CD2  1 
ATOM   3717 H H    A LEU   A 1 164 ? 5.731  -7.778  0.981   0.58 21.28 ?  164 LEU   A H    1 
ATOM   3718 H H    B LEU   A 1 164 ? 5.838  -8.073  0.685   0.42 24.50 ?  164 LEU   A H    1 
ATOM   3719 H HA   A LEU   A 1 164 ? 6.933  -9.812  -0.153  0.58 20.06 ?  164 LEU   A HA   1 
ATOM   3720 H HA   B LEU   A 1 164 ? 6.845  -10.344 -0.115  0.42 24.04 ?  164 LEU   A HA   1 
ATOM   3721 H HB2  A LEU   A 1 164 ? 7.576  -8.322  2.137   0.58 19.48 ?  164 LEU   A HB2  1 
ATOM   3722 H HB2  B LEU   A 1 164 ? 7.710  -8.626  1.944   0.42 23.35 ?  164 LEU   A HB2  1 
ATOM   3723 H HB3  A LEU   A 1 164 ? 8.483  -9.538  1.688   0.58 19.48 ?  164 LEU   A HB3  1 
ATOM   3724 H HB3  B LEU   A 1 164 ? 8.559  -9.871  1.466   0.42 23.35 ?  164 LEU   A HB3  1 
ATOM   3725 H HG   A LEU   A 1 164 ? 8.113  -7.309  0.015   0.58 19.09 ?  164 LEU   A HG   1 
ATOM   3726 H HG   B LEU   A 1 164 ? 8.035  -7.666  -0.208  0.42 22.99 ?  164 LEU   A HG   1 
ATOM   3727 H HD11 A LEU   A 1 164 ? 10.139 -6.454  0.782   0.58 19.12 ?  164 LEU   A HD11 1 
ATOM   3728 H HD11 B LEU   A 1 164 ? 10.221 -6.979  0.220   0.42 22.38 ?  164 LEU   A HD11 1 
ATOM   3729 H HD12 A LEU   A 1 164 ? 9.071  -6.505  1.957   0.58 19.12 ?  164 LEU   A HD12 1 
ATOM   3730 H HD12 B LEU   A 1 164 ? 9.372  -6.976  1.563   0.42 22.38 ?  164 LEU   A HD12 1 
ATOM   3731 H HD13 A LEU   A 1 164 ? 10.208 -7.611  1.869   0.58 19.12 ?  164 LEU   A HD13 1 
ATOM   3732 H HD13 B LEU   A 1 164 ? 10.386 -8.163  1.267   0.42 22.38 ?  164 LEU   A HD13 1 
ATOM   3733 H HD21 A LEU   A 1 164 ? 10.067 -8.045  -1.047  0.58 18.66 ?  164 LEU   A HD21 1 
ATOM   3734 H HD21 B LEU   A 1 164 ? 9.770  -8.608  -1.514  0.42 23.47 ?  164 LEU   A HD21 1 
ATOM   3735 H HD22 A LEU   A 1 164 ? 10.121 -9.291  -0.063  0.58 18.66 ?  164 LEU   A HD22 1 
ATOM   3736 H HD22 B LEU   A 1 164 ? 9.752  -9.871  -0.551  0.42 23.47 ?  164 LEU   A HD22 1 
ATOM   3737 H HD23 A LEU   A 1 164 ? 8.937  -9.160  -1.113  0.58 18.66 ?  164 LEU   A HD23 1 
ATOM   3738 H HD23 B LEU   A 1 164 ? 8.483  -9.537  -1.447  0.42 23.47 ?  164 LEU   A HD23 1 
ATOM   3739 N N    A VAL   A 1 165 ? 5.529  -10.486 2.653   0.58 15.80 ?  165 VAL   A N    1 
ATOM   3740 N N    B VAL   A 1 165 ? 5.526  -10.429 2.797   0.42 21.63 ?  165 VAL   A N    1 
ATOM   3741 C CA   A VAL   A 1 165 ? 5.063  -11.576 3.505   0.58 15.43 ?  165 VAL   A CA   1 
ATOM   3742 C CA   B VAL   A 1 165 ? 5.082  -11.320 3.861   0.42 23.06 ?  165 VAL   A CA   1 
ATOM   3743 C C    A VAL   A 1 165 ? 4.031  -12.424 2.776   0.58 15.43 ?  165 VAL   A C    1 
ATOM   3744 C C    B VAL   A 1 165 ? 3.960  -12.233 3.380   0.42 24.00 ?  165 VAL   A C    1 
ATOM   3745 O O    A VAL   A 1 165 ? 4.136  -13.654 2.734   0.58 14.80 ?  165 VAL   A O    1 
ATOM   3746 O O    B VAL   A 1 165 ? 3.864  -13.389 3.810   0.42 24.80 ?  165 VAL   A O    1 
ATOM   3747 C CB   A VAL   A 1 165 ? 4.508  -11.010 4.824   0.58 16.28 ?  165 VAL   A CB   1 
ATOM   3748 C CB   B VAL   A 1 165 ? 4.689  -10.481 5.092   0.42 23.73 ?  165 VAL   A CB   1 
ATOM   3749 C CG1  A VAL   A 1 165 ? 3.734  -12.078 5.594   0.58 16.43 ?  165 VAL   A CG1  1 
ATOM   3750 C CG1  B VAL   A 1 165 ? 3.911  -11.306 6.074   0.42 24.28 ?  165 VAL   A CG1  1 
ATOM   3751 C CG2  A VAL   A 1 165 ? 5.638  -10.433 5.662   0.58 16.39 ?  165 VAL   A CG2  1 
ATOM   3752 C CG2  B VAL   A 1 165 ? 5.929  -9.907  5.754   0.42 23.73 ?  165 VAL   A CG2  1 
ATOM   3753 H H    A VAL   A 1 165 ? 5.311  -9.701  2.928   0.58 18.93 ?  165 VAL   A H    1 
ATOM   3754 H H    B VAL   A 1 165 ? 5.316  -9.604  2.912   0.42 25.93 ?  165 VAL   A H    1 
ATOM   3755 H HA   A VAL   A 1 165 ? 5.816  -12.146 3.715   0.58 18.49 ?  165 VAL   A HA   1 
ATOM   3756 H HA   B VAL   A 1 165 ? 5.822  -11.884 4.123   0.42 27.65 ?  165 VAL   A HA   1 
ATOM   3757 H HB   A VAL   A 1 165 ? 3.894  -10.289 4.617   0.58 19.51 ?  165 VAL   A HB   1 
ATOM   3758 H HB   B VAL   A 1 165 ? 4.123  -9.740  4.810   0.42 28.45 ?  165 VAL   A HB   1 
ATOM   3759 H HG11 A VAL   A 1 165 ? 3.636  -11.789 6.514   0.58 19.69 ?  165 VAL   A HG11 1 
ATOM   3760 H HG11 B VAL   A 1 165 ? 3.905  -10.864 6.940   0.42 29.11 ?  165 VAL   A HG11 1 
ATOM   3761 H HG12 A VAL   A 1 165 ? 2.858  -12.189 5.190   0.58 19.69 ?  165 VAL   A HG12 1 
ATOM   3762 H HG12 B VAL   A 1 165 ? 3.012  -11.368 5.730   0.42 29.11 ?  165 VAL   A HG12 1 
ATOM   3763 H HG13 A VAL   A 1 165 ? 4.226  -12.912 5.560   0.58 19.69 ?  165 VAL   A HG13 1 
ATOM   3764 H HG13 B VAL   A 1 165 ? 4.311  -12.186 6.149   0.42 29.11 ?  165 VAL   A HG13 1 
ATOM   3765 H HG21 A VAL   A 1 165 ? 5.273  -10.108 6.499   0.58 19.64 ?  165 VAL   A HG21 1 
ATOM   3766 H HG21 B VAL   A 1 165 ? 5.683  -9.552  6.621   0.42 28.45 ?  165 VAL   A HG21 1 
ATOM   3767 H HG22 A VAL   A 1 165 ? 6.292  -11.129 5.832   0.58 19.64 ?  165 VAL   A HG22 1 
ATOM   3768 H HG22 B VAL   A 1 165 ? 6.582  -10.614 5.860   0.42 28.45 ?  165 VAL   A HG22 1 
ATOM   3769 H HG23 A VAL   A 1 165 ? 6.052  -9.703  5.174   0.58 19.64 ?  165 VAL   A HG23 1 
ATOM   3770 H HG23 B VAL   A 1 165 ? 6.289  -9.203  5.194   0.42 28.45 ?  165 VAL   A HG23 1 
ATOM   3771 N N    A SER   A 1 166 ? 3.032  -11.777 2.171   0.58 15.75 ?  166 SER   A N    1 
ATOM   3772 N N    B SER   A 1 166 ? 3.108  -11.749 2.480   0.42 24.14 ?  166 SER   A N    1 
ATOM   3773 C CA   A SER   A 1 166 ? 1.919  -12.516 1.579   0.58 16.72 ?  166 SER   A CA   1 
ATOM   3774 C CA   B SER   A 1 166 ? 2.000  -12.535 1.956   0.42 24.48 ?  166 SER   A CA   1 
ATOM   3775 C C    A SER   A 1 166 ? 2.365  -13.360 0.395   0.58 17.15 ?  166 SER   A C    1 
ATOM   3776 C C    B SER   A 1 166 ? 2.372  -13.315 0.700   0.42 25.65 ?  166 SER   A C    1 
ATOM   3777 O O    A SER   A 1 166 ? 1.717  -14.365 0.078   0.58 18.75 ?  166 SER   A O    1 
ATOM   3778 O O    B SER   A 1 166 ? 1.478  -13.808 0.004   0.42 25.71 ?  166 SER   A O    1 
ATOM   3779 C CB   A SER   A 1 166 ? 0.810  -11.552 1.148   0.58 17.62 ?  166 SER   A CB   1 
ATOM   3780 C CB   B SER   A 1 166 ? 0.805  -11.625 1.665   0.42 24.15 ?  166 SER   A CB   1 
ATOM   3781 O OG   A SER   A 1 166 ? 0.199  -10.934 2.270   0.58 19.37 ?  166 SER   A OG   1 
ATOM   3782 O OG   B SER   A 1 166 ? 1.077  -10.783 0.559   0.42 24.03 ?  166 SER   A OG   1 
ATOM   3783 H H    A SER   A 1 166 ? 2.969  -10.926 2.089   0.58 18.87 ?  166 SER   A H    1 
ATOM   3784 H H    B SER   A 1 166 ? 3.153  -10.953 2.153   0.42 28.94 ?  166 SER   A H    1 
ATOM   3785 H HA   A SER   A 1 166 ? 1.547  -13.118 2.236   0.58 20.04 ?  166 SER   A HA   1 
ATOM   3786 H HA   B SER   A 1 166 ? 1.726  -13.173 2.628   0.42 29.36 ?  166 SER   A HA   1 
ATOM   3787 H HB2  A SER   A 1 166 ? 1.189  -10.871 0.567   0.58 21.12 ?  166 SER   A HB2  1 
ATOM   3788 H HB2  B SER   A 1 166 ? 0.030  -12.173 1.464   0.42 28.96 ?  166 SER   A HB2  1 
ATOM   3789 H HB3  A SER   A 1 166 ? 0.126  -12.047 0.664   0.58 21.12 ?  166 SER   A HB3  1 
ATOM   3790 H HB3  B SER   A 1 166 ? 0.626  -11.076 2.449   0.42 28.96 ?  166 SER   A HB3  1 
ATOM   3791 H HG   A SER   A 1 166 ? -0.392 -10.394 2.016   0.58 23.22 ?  166 SER   A HG   1 
ATOM   3792 H HG   B SER   A 1 166 ? 1.749  -10.305 0.725   0.42 28.82 ?  166 SER   A HG   1 
ATOM   3793 N N    A SER   A 1 167 ? 3.448  -12.969 -0.276  0.58 16.04 ?  167 SER   A N    1 
ATOM   3794 N N    B SER   A 1 167 ? 3.662  -13.445 0.403   0.42 27.25 ?  167 SER   A N    1 
ATOM   3795 C CA   A SER   A 1 167 ? 3.938  -13.693 -1.439  0.58 16.45 ?  167 SER   A CA   1 
ATOM   3796 C CA   B SER   A 1 167 ? 4.139  -14.110 -0.799  0.42 28.95 ?  167 SER   A CA   1 
ATOM   3797 C C    A SER   A 1 167 ? 5.088  -14.641 -1.116  0.58 15.87 ?  167 SER   A C    1 
ATOM   3798 C C    B SER   A 1 167 ? 4.821  -15.423 -0.437  0.42 30.13 ?  167 SER   A C    1 
ATOM   3799 O O    A SER   A 1 167 ? 5.605  -15.293 -2.029  0.58 16.96 ?  167 SER   A O    1 
ATOM   3800 O O    B SER   A 1 167 ? 5.366  -15.577 0.659   0.42 29.91 ?  167 SER   A O    1 
ATOM   3801 C CB   A SER   A 1 167 ? 4.372  -12.712 -2.537  0.58 17.05 ?  167 SER   A CB   1 
ATOM   3802 C CB   B SER   A 1 167 ? 5.136  -13.225 -1.549  0.42 29.57 ?  167 SER   A CB   1 
ATOM   3803 O OG   A SER   A 1 167 ? 5.441  -11.898 -2.084  0.58 17.75 ?  167 SER   A OG   1 
ATOM   3804 O OG   B SER   A 1 167 ? 6.223  -12.874 -0.711  0.42 30.19 ?  167 SER   A OG   1 
ATOM   3805 H H    A SER   A 1 167 ? 3.910  -12.266 -0.083  0.58 19.23 ?  167 SER   A H    1 
ATOM   3806 H H    B SER   A 1 167 ? 4.296  -13.148 0.904   0.42 32.67 ?  167 SER   A H    1 
ATOM   3807 H HA   A SER   A 1 167 ? 3.218  -14.220 -1.804  0.58 19.71 ?  167 SER   A HA   1 
ATOM   3808 H HA   B SER   A 1 167 ? 3.391  -14.298 -1.385  0.42 34.71 ?  167 SER   A HA   1 
ATOM   3809 H HB2  A SER   A 1 167 ? 4.670  -13.211 -3.316  0.58 20.44 ?  167 SER   A HB2  1 
ATOM   3810 H HB2  B SER   A 1 167 ? 5.477  -13.714 -2.314  0.42 35.46 ?  167 SER   A HB2  1 
ATOM   3811 H HB3  A SER   A 1 167 ? 3.613  -12.151 -2.785  0.58 20.44 ?  167 SER   A HB3  1 
ATOM   3812 H HB3  B SER   A 1 167 ? 4.686  -12.419 -1.843  0.42 35.46 ?  167 SER   A HB3  1 
ATOM   3813 H HG   A SER   A 1 167 ? 5.181  -11.427 -1.435  0.58 21.27 ?  167 SER   A HG   1 
ATOM   3814 H HG   B SER   A 1 167 ? 5.938  -12.633 0.042   0.42 36.20 ?  167 SER   A HG   1 
ATOM   3815 N N    A PHE   A 1 168 ? 5.502  -14.735 0.147   0.58 15.80 ?  168 PHE   A N    1 
ATOM   3816 N N    B PHE   A 1 168 ? 4.792  -16.366 -1.375  0.42 31.69 ?  168 PHE   A N    1 
ATOM   3817 C CA   A PHE   A 1 168 ? 6.671  -15.540 0.480   0.58 16.00 ?  168 PHE   A CA   1 
ATOM   3818 C CA   B PHE   A 1 168 ? 5.349  -17.699 -1.172  0.42 33.52 ?  168 PHE   A CA   1 
ATOM   3819 C C    A PHE   A 1 168 ? 6.361  -17.024 0.375   0.58 17.53 ?  168 PHE   A C    1 
ATOM   3820 C C    B PHE   A 1 168 ? 6.740  -17.764 -1.802  0.42 34.71 ?  168 PHE   A C    1 
ATOM   3821 O O    A PHE   A 1 168 ? 5.378  -17.508 0.942   0.58 19.89 ?  168 PHE   A O    1 
ATOM   3822 O O    B PHE   A 1 168 ? 6.892  -17.579 -3.014  0.42 34.89 ?  168 PHE   A O    1 
ATOM   3823 C CB   A PHE   A 1 168 ? 7.168  -15.245 1.892   0.58 15.73 ?  168 PHE   A CB   1 
ATOM   3824 C CB   B PHE   A 1 168 ? 4.377  -18.765 -1.696  0.42 34.16 ?  168 PHE   A CB   1 
ATOM   3825 C CG   A PHE   A 1 168 ? 8.441  -15.972 2.222   0.58 15.34 ?  168 PHE   A CG   1 
ATOM   3826 C CG   B PHE   A 1 168 ? 4.978  -19.771 -2.639  0.42 34.83 ?  168 PHE   A CG   1 
ATOM   3827 C CD1  A PHE   A 1 168 ? 9.622  -15.599 1.613   0.58 15.50 ?  168 PHE   A CD1  1 
ATOM   3828 C CD1  B PHE   A 1 168 ? 5.795  -20.791 -2.175  0.42 35.12 ?  168 PHE   A CD1  1 
ATOM   3829 C CD2  A PHE   A 1 168 ? 8.460  -17.045 3.103   0.58 14.79 ?  168 PHE   A CD2  1 
ATOM   3830 C CD2  B PHE   A 1 168 ? 4.665  -19.734 -3.988  0.42 35.10 ?  168 PHE   A CD2  1 
ATOM   3831 C CE1  A PHE   A 1 168 ? 10.798 -16.264 1.885   0.58 15.65 ?  168 PHE   A CE1  1 
ATOM   3832 C CE1  B PHE   A 1 168 ? 6.320  -21.728 -3.050  0.42 35.23 ?  168 PHE   A CE1  1 
ATOM   3833 C CE2  A PHE   A 1 168 ? 9.640  -17.711 3.381   0.58 15.41 ?  168 PHE   A CE2  1 
ATOM   3834 C CE2  B PHE   A 1 168 ? 5.184  -20.667 -4.865  0.42 35.27 ?  168 PHE   A CE2  1 
ATOM   3835 C CZ   A PHE   A 1 168 ? 10.804 -17.318 2.771   0.58 15.45 ?  168 PHE   A CZ   1 
ATOM   3836 C CZ   B PHE   A 1 168 ? 6.011  -21.665 -4.396  0.42 35.32 ?  168 PHE   A CZ   1 
ATOM   3837 H H    A PHE   A 1 168 ? 5.136  -14.336 0.816   0.58 18.94 ?  168 PHE   A H    1 
ATOM   3838 H H    B PHE   A 1 168 ? 4.442  -16.251 -2.153  0.42 38.00 ?  168 PHE   A H    1 
ATOM   3839 H HA   A PHE   A 1 168 ? 7.386  -15.331 -0.143  0.58 19.18 ?  168 PHE   A HA   1 
ATOM   3840 H HA   B PHE   A 1 168 ? 5.450  -17.848 -0.218  0.42 40.19 ?  168 PHE   A HA   1 
ATOM   3841 H HB2  A PHE   A 1 168 ? 7.334  -14.295 1.978   0.58 18.85 ?  168 PHE   A HB2  1 
ATOM   3842 H HB2  B PHE   A 1 168 ? 4.015  -19.253 -0.938  0.42 40.97 ?  168 PHE   A HB2  1 
ATOM   3843 H HB3  A PHE   A 1 168 ? 6.491  -15.525 2.528   0.58 18.85 ?  168 PHE   A HB3  1 
ATOM   3844 H HB3  B PHE   A 1 168 ? 3.656  -18.320 -2.167  0.42 40.97 ?  168 PHE   A HB3  1 
ATOM   3845 H HD1  A PHE   A 1 168 ? 9.628  -14.886 1.011   0.58 18.57 ?  168 PHE   A HD1  1 
ATOM   3846 H HD1  B PHE   A 1 168 ? 6.007  -20.838 -1.271  0.42 42.12 ?  168 PHE   A HD1  1 
ATOM   3847 H HD2  A PHE   A 1 168 ? 7.672  -17.313 3.517   0.58 17.73 ?  168 PHE   A HD2  1 
ATOM   3848 H HD2  B PHE   A 1 168 ? 4.106  -19.064 -4.310  0.42 42.09 ?  168 PHE   A HD2  1 
ATOM   3849 H HE1  A PHE   A 1 168 ? 11.594 -15.996 1.473   0.58 18.76 ?  168 PHE   A HE1  1 
ATOM   3850 H HE1  B PHE   A 1 168 ? 6.876  -22.402 -2.732  0.42 42.25 ?  168 PHE   A HE1  1 
ATOM   3851 H HE2  A PHE   A 1 168 ? 9.644  -18.423 3.977   0.58 18.46 ?  168 PHE   A HE2  1 
ATOM   3852 H HE2  B PHE   A 1 168 ? 4.971  -20.622 -5.770  0.42 42.31 ?  168 PHE   A HE2  1 
ATOM   3853 H HZ   A PHE   A 1 168 ? 11.602 -17.762 2.954   0.58 18.51 ?  168 PHE   A HZ   1 
ATOM   3854 H HZ   B PHE   A 1 168 ? 6.361  -22.295 -4.986  0.42 42.36 ?  168 PHE   A HZ   1 
ATOM   3855 N N    A LEU   A 1 169 ? 7.237  -17.755 -0.306  0.58 18.37 ?  169 LEU   A N    1 
ATOM   3856 N N    B LEU   A 1 169 ? 7.737  -18.027 -0.956  0.42 35.66 ?  169 LEU   A N    1 
ATOM   3857 C CA   A LEU   A 1 169 ? 7.045  -19.184 -0.474  0.58 21.38 ?  169 LEU   A CA   1 
ATOM   3858 C CA   B LEU   A 1 169 ? 9.180  -17.858 -1.202  0.42 36.52 ?  169 LEU   A CA   1 
ATOM   3859 C C    A LEU   A 1 169 ? 7.874  -19.947 0.548   0.58 21.48 ?  169 LEU   A C    1 
ATOM   3860 C C    B LEU   A 1 169 ? 9.636  -16.463 -0.780  0.42 36.99 ?  169 LEU   A C    1 
ATOM   3861 O O    A LEU   A 1 169 ? 7.317  -20.462 1.520   0.58 21.72 ?  169 LEU   A O    1 
ATOM   3862 O O    B LEU   A 1 169 ? 9.678  -15.533 -1.583  0.42 37.21 ?  169 LEU   A O    1 
ATOM   3863 C CB   A LEU   A 1 169 ? 7.397  -19.614 -1.901  0.58 23.18 ?  169 LEU   A CB   1 
ATOM   3864 C CB   B LEU   A 1 169 ? 9.616  -18.142 -2.646  0.42 36.90 ?  169 LEU   A CB   1 
ATOM   3865 C CG   A LEU   A 1 169 ? 7.110  -21.076 -2.255  0.58 25.17 ?  169 LEU   A CG   1 
ATOM   3866 C CG   B LEU   A 1 169 ? 9.484  -19.579 -3.152  0.42 37.25 ?  169 LEU   A CG   1 
ATOM   3867 C CD1  A LEU   A 1 169 ? 5.690  -21.461 -1.870  0.58 26.04 ?  169 LEU   A CD1  1 
ATOM   3868 C CD1  B LEU   A 1 169 ? 10.470 -19.832 -4.288  0.42 37.35 ?  169 LEU   A CD1  1 
ATOM   3869 C CD2  A LEU   A 1 169 ? 7.347  -21.322 -3.738  0.58 25.90 ?  169 LEU   A CD2  1 
ATOM   3870 C CD2  B LEU   A 1 169 ? 9.687  -20.580 -2.024  0.42 37.32 ?  169 LEU   A CD2  1 
ATOM   3871 O OXT  A LEU   A 1 169 ? 9.097  -20.052 0.437   0.58 21.22 -1 169 LEU   A OXT  1 
ATOM   3872 O OXT  B LEU   A 1 169 ? 9.982  -16.242 0.381   0.42 37.12 -1 169 LEU   A OXT  1 
ATOM   3873 H H    A LEU   A 1 169 ? 7.953  -17.447 -0.675  0.58 22.02 ?  169 LEU   A H    1 
ATOM   3874 H H    B LEU   A 1 169 ? 7.589  -18.323 -0.172  0.42 42.76 ?  169 LEU   A H    1 
ATOM   3875 H HA   A LEU   A 1 169 ? 6.120  -19.400 -0.310  0.58 25.63 ?  169 LEU   A HA   1 
ATOM   3876 H HA   B LEU   A 1 169 ? 9.642  -18.488 -0.632  0.42 43.80 ?  169 LEU   A HA   1 
ATOM   3877 H HB2  A LEU   A 1 169 ? 6.886  -19.066 -2.518  0.58 27.79 ?  169 LEU   A HB2  1 
ATOM   3878 H HB2  B LEU   A 1 169 ? 9.120  -17.571 -3.243  0.42 44.26 ?  169 LEU   A HB2  1 
ATOM   3879 H HB3  A LEU   A 1 169 ? 8.343  -19.464 -2.046  0.58 27.79 ?  169 LEU   A HB3  1 
ATOM   3880 H HB3  B LEU   A 1 169 ? 10.562 -17.914 -2.714  0.42 44.26 ?  169 LEU   A HB3  1 
ATOM   3881 H HG   A LEU   A 1 169 ? 7.719  -21.647 -1.760  0.58 30.18 ?  169 LEU   A HG   1 
ATOM   3882 H HG   B LEU   A 1 169 ? 8.591  -19.702 -3.503  0.42 44.68 ?  169 LEU   A HG   1 
ATOM   3883 H HD11 A LEU   A 1 169 ? 5.469  -22.310 -2.283  0.58 31.22 ?  169 LEU   A HD11 1 
ATOM   3884 H HD11 B LEU   A 1 169 ? 10.369 -20.746 -4.596  0.42 44.80 ?  169 LEU   A HD11 1 
ATOM   3885 H HD12 A LEU   A 1 169 ? 5.633  -21.538 -0.905  0.58 31.22 ?  169 LEU   A HD12 1 
ATOM   3886 H HD12 B LEU   A 1 169 ? 10.281 -19.217 -5.014  0.42 44.80 ?  169 LEU   A HD12 1 
ATOM   3887 H HD13 A LEU   A 1 169 ? 5.081  -20.773 -2.185  0.58 31.22 ?  169 LEU   A HD13 1 
ATOM   3888 H HD13 B LEU   A 1 169 ? 11.374 -19.692 -3.962  0.42 44.80 ?  169 LEU   A HD13 1 
ATOM   3889 H HD21 A LEU   A 1 169 ? 7.165  -22.254 -3.938  0.58 31.05 ?  169 LEU   A HD21 1 
ATOM   3890 H HD21 B LEU   A 1 169 ? 9.752  -21.468 -2.400  0.42 44.76 ?  169 LEU   A HD21 1 
ATOM   3891 H HD22 A LEU   A 1 169 ? 6.750  -20.753 -4.251  0.58 31.05 ?  169 LEU   A HD22 1 
ATOM   3892 H HD22 B LEU   A 1 169 ? 10.505 -20.360 -1.550  0.42 44.76 ?  169 LEU   A HD22 1 
ATOM   3893 H HD23 A LEU   A 1 169 ? 8.269  -21.111 -3.951  0.58 31.05 ?  169 LEU   A HD23 1 
ATOM   3894 H HD23 B LEU   A 1 169 ? 8.930  -20.530 -1.418  0.42 44.76 ?  169 LEU   A HD23 1 
ATOM   3895 N N    A SER   B 1 1   ? 50.851 -9.284  -23.714 0.58 28.47 ?  1   SER   B N    1 
ATOM   3896 N N    B SER   B 1 1   ? 50.828 -9.654  -23.618 0.42 20.62 ?  1   SER   B N    1 
ATOM   3897 C CA   A SER   B 1 1   ? 51.386 -10.335 -22.824 0.58 28.73 ?  1   SER   B CA   1 
ATOM   3898 C CA   B SER   B 1 1   ? 51.309 -10.610 -22.587 0.42 19.92 ?  1   SER   B CA   1 
ATOM   3899 C C    A SER   B 1 1   ? 50.337 -11.408 -22.582 0.58 27.87 ?  1   SER   B C    1 
ATOM   3900 C C    B SER   B 1 1   ? 50.337 -11.784 -22.418 0.42 18.31 ?  1   SER   B C    1 
ATOM   3901 O O    A SER   B 1 1   ? 49.144 -11.202 -22.822 0.58 28.19 ?  1   SER   B O    1 
ATOM   3902 O O    B SER   B 1 1   ? 49.119 -11.646 -22.598 0.42 19.29 ?  1   SER   B O    1 
ATOM   3903 C CB   A SER   B 1 1   ? 51.828 -9.742  -21.491 0.58 29.53 ?  1   SER   B CB   1 
ATOM   3904 C CB   B SER   B 1 1   ? 51.506 -9.893  -21.254 0.42 21.01 ?  1   SER   B CB   1 
ATOM   3905 O OG   A SER   B 1 1   ? 50.726 -9.571  -20.622 0.58 30.96 ?  1   SER   B OG   1 
ATOM   3906 O OG   B SER   B 1 1   ? 50.262 -9.466  -20.725 0.42 22.64 ?  1   SER   B OG   1 
ATOM   3907 H H1   A SER   B 1 1   ? 50.572 -9.658  -24.471 0.58 34.14 ?  1   SER   B H1   1 
ATOM   3908 H H1   B SER   B 1 1   ? 51.286 -9.779  -24.370 0.42 24.72 ?  1   SER   B H1   1 
ATOM   3909 H H2   A SER   B 1 1   ? 50.174 -8.880  -23.309 0.58 34.14 ?  1   SER   B H2   1 
ATOM   3910 H H2   B SER   B 1 1   ? 49.965 -9.796  -23.765 0.42 24.72 ?  1   SER   B H2   1 
ATOM   3911 H H3   A SER   B 1 1   ? 51.497 -8.702  -23.885 0.58 34.14 ?  1   SER   B H3   1 
ATOM   3912 H H3   B SER   B 1 1   ? 50.953 -8.825  -23.326 0.42 24.72 ?  1   SER   B H3   1 
ATOM   3913 H HA   A SER   B 1 1   ? 52.149 -10.739 -23.256 0.58 34.45 ?  1   SER   B HA   1 
ATOM   3914 H HA   B SER   B 1 1   ? 52.165 -10.951 -22.885 0.42 23.87 ?  1   SER   B HA   1 
ATOM   3915 H HB2  A SER   B 1 1   ? 52.457 -10.350 -21.080 0.58 35.41 ?  1   SER   B HB2  1 
ATOM   3916 H HB2  B SER   B 1 1   ? 51.911 -10.513 -20.635 0.42 25.19 ?  1   SER   B HB2  1 
ATOM   3917 H HB3  A SER   B 1 1   ? 52.244 -8.883  -21.653 0.58 35.41 ?  1   SER   B HB3  1 
ATOM   3918 H HB3  B SER   B 1 1   ? 52.089 -9.127  -21.391 0.42 25.19 ?  1   SER   B HB3  1 
ATOM   3919 H HG   A SER   B 1 1   ? 50.979 -9.225  -19.902 0.58 37.13 ?  1   SER   B HG   1 
ATOM   3920 H HG   B SER   B 1 1   ? 50.394 -9.059  -19.998 0.42 27.14 ?  1   SER   B HG   1 
ATOM   3921 N N    A MET   B 1 2   ? 50.801 -12.553 -22.095 0.58 27.05 ?  2   MET   B N    1 
ATOM   3922 N N    B MET   B 1 2   ? 50.884 -12.952 -22.084 0.42 16.56 ?  2   MET   B N    1 
ATOM   3923 C CA   A MET   B 1 2   ? 49.971 -13.734 -21.906 0.58 26.84 ?  2   MET   B CA   1 
ATOM   3924 C CA   B MET   B 1 2   ? 50.107 -14.193 -22.030 0.42 16.00 ?  2   MET   B CA   1 
ATOM   3925 C C    A MET   B 1 2   ? 49.671 -13.881 -20.419 0.58 24.07 ?  2   MET   B C    1 
ATOM   3926 C C    B MET   B 1 2   ? 49.735 -14.530 -20.592 0.42 15.88 ?  2   MET   B C    1 
ATOM   3927 O O    A MET   B 1 2   ? 50.576 -14.142 -19.621 0.58 23.20 ?  2   MET   B O    1 
ATOM   3928 O O    B MET   B 1 2   ? 50.428 -15.286 -19.908 0.42 17.29 ?  2   MET   B O    1 
ATOM   3929 C CB   A MET   B 1 2   ? 50.709 -14.957 -22.441 0.58 30.54 ?  2   MET   B CB   1 
ATOM   3930 C CB   B MET   B 1 2   ? 50.890 -15.320 -22.661 0.42 17.58 ?  2   MET   B CB   1 
ATOM   3931 C CG   A MET   B 1 2   ? 49.836 -16.177 -22.663 0.58 34.22 ?  2   MET   B CG   1 
ATOM   3932 C CG   B MET   B 1 2   ? 50.052 -16.581 -22.939 0.42 19.54 ?  2   MET   B CG   1 
ATOM   3933 S SD   A MET   B 1 2   ? 50.682 -17.387 -23.688 0.58 37.80 ?  2   MET   B SD   1 
ATOM   3934 S SD   B MET   B 1 2   ? 50.793 -17.599 -24.242 0.42 21.07 ?  2   MET   B SD   1 
ATOM   3935 C CE   A MET   B 1 2   ? 51.170 -16.366 -25.069 0.58 38.28 ?  2   MET   B CE   1 
ATOM   3936 C CE   B MET   B 1 2   ? 51.543 -16.279 -25.155 0.42 22.25 ?  2   MET   B CE   1 
ATOM   3937 H H    A MET   B 1 2   ? 51.620 -12.678 -21.866 0.58 32.43 ?  2   MET   B H    1 
ATOM   3938 H H    B MET   B 1 2   ? 51.722 -13.046 -21.904 0.42 19.85 ?  2   MET   B H    1 
ATOM   3939 H HA   A MET   B 1 2   ? 49.144 -13.648 -22.403 0.58 32.18 ?  2   MET   B HA   1 
ATOM   3940 H HA   B MET   B 1 2   ? 49.298 -14.069 -22.546 0.42 19.18 ?  2   MET   B HA   1 
ATOM   3941 H HB2  A MET   B 1 2   ? 51.119 -14.712 -23.283 0.58 36.63 ?  2   MET   B HB2  1 
ATOM   3942 H HB2  B MET   B 1 2   ? 51.259 -14.905 -23.443 0.42 21.07 ?  2   MET   B HB2  1 
ATOM   3943 H HB3  A MET   B 1 2   ? 51.397 -15.222 -21.815 0.58 36.63 ?  2   MET   B HB3  1 
ATOM   3944 H HB3  B MET   B 1 2   ? 51.603 -15.592 -22.082 0.42 21.07 ?  2   MET   B HB3  1 
ATOM   3945 H HG2  A MET   B 1 2   ? 49.635 -16.596 -21.809 0.58 41.04 ?  2   MET   B HG2  1 
ATOM   3946 H HG2  B MET   B 1 2   ? 49.992 -17.102 -22.109 0.42 23.43 ?  2   MET   B HG2  1 
ATOM   3947 H HG3  A MET   B 1 2   ? 49.016 -15.921 -23.113 0.58 41.04 ?  2   MET   B HG3  1 
ATOM   3948 H HG3  B MET   B 1 2   ? 49.155 -16.317 -23.214 0.42 23.43 ?  2   MET   B HG3  1 
ATOM   3949 H HE1  A MET   B 1 2   ? 51.260 -16.915 -25.857 0.58 45.91 ?  2   MET   B HE1  1 
ATOM   3950 H HE1  B MET   B 1 2   ? 51.651 -16.639 -26.004 0.42 26.67 ?  2   MET   B HE1  1 
ATOM   3951 H HE2  A MET   B 1 2   ? 50.489 -15.688 -25.209 0.58 45.91 ?  2   MET   B HE2  1 
ATOM   3952 H HE2  B MET   B 1 2   ? 50.940 -15.511 -25.224 0.42 26.67 ?  2   MET   B HE2  1 
ATOM   3953 H HE3  A MET   B 1 2   ? 52.017 -15.943 -24.855 0.58 45.91 ?  2   MET   B HE3  1 
ATOM   3954 H HE3  B MET   B 1 2   ? 52.407 -16.012 -24.755 0.42 26.67 ?  2   MET   B HE3  1 
ATOM   3955 N N    A VAL   B 1 3   ? 48.404 -13.711 -20.049 0.58 21.50 ?  3   VAL   B N    1 
ATOM   3956 N N    B VAL   B 1 3   ? 48.599 -14.005 -20.159 0.42 15.15 ?  3   VAL   B N    1 
ATOM   3957 C CA   A VAL   B 1 3   ? 47.959 -13.903 -18.673 0.58 19.95 ?  3   VAL   B CA   1 
ATOM   3958 C CA   B VAL   B 1 3   ? 48.137 -14.164 -18.789 0.42 14.97 ?  3   VAL   B CA   1 
ATOM   3959 C C    A VAL   B 1 3   ? 46.709 -14.771 -18.666 0.58 17.66 ?  3   VAL   B C    1 
ATOM   3960 C C    B VAL   B 1 3   ? 46.885 -15.030 -18.781 0.42 14.07 ?  3   VAL   B C    1 
ATOM   3961 O O    A VAL   B 1 3   ? 45.902 -14.744 -19.599 0.58 18.00 ?  3   VAL   B O    1 
ATOM   3962 O O    B VAL   B 1 3   ? 46.218 -15.219 -19.805 0.42 12.53 ?  3   VAL   B O    1 
ATOM   3963 C CB   A VAL   B 1 3   ? 47.701 -12.572 -17.931 0.58 21.02 ?  3   VAL   B CB   1 
ATOM   3964 C CB   B VAL   B 1 3   ? 47.866 -12.805 -18.117 0.42 16.24 ?  3   VAL   B CB   1 
ATOM   3965 C CG1  A VAL   B 1 3   ? 48.986 -11.748 -17.837 0.58 21.59 ?  3   VAL   B CG1  1 
ATOM   3966 C CG1  B VAL   B 1 3   ? 49.150 -11.986 -18.026 0.42 16.86 ?  3   VAL   B CG1  1 
ATOM   3967 C CG2  A VAL   B 1 3   ? 46.583 -11.783 -18.599 0.58 21.37 ?  3   VAL   B CG2  1 
ATOM   3968 C CG2  B VAL   B 1 3   ? 46.786 -12.043 -18.874 0.42 16.62 ?  3   VAL   B CG2  1 
ATOM   3969 H H    A VAL   B 1 3   ? 47.769 -13.502 -20.596 0.58 25.78 ?  3   VAL   B H    1 
ATOM   3970 H H    B VAL   B 1 3   ? 48.058 -13.563 -20.665 0.42 18.16 ?  3   VAL   B H    1 
ATOM   3971 H HA   A VAL   B 1 3   ? 48.644 -14.384 -18.193 0.58 23.92 ?  3   VAL   B HA   1 
ATOM   3972 H HA   B VAL   B 1 3   ? 48.824 -14.624 -18.282 0.42 17.95 ?  3   VAL   B HA   1 
ATOM   3973 H HB   A VAL   B 1 3   ? 47.417 -12.778 -17.028 0.58 25.20 ?  3   VAL   B HB   1 
ATOM   3974 H HB   B VAL   B 1 3   ? 47.550 -12.968 -17.215 0.42 19.46 ?  3   VAL   B HB   1 
ATOM   3975 H HG11 A VAL   B 1 3   ? 48.795 -10.927 -17.360 0.58 25.89 ?  3   VAL   B HG11 1 
ATOM   3976 H HG11 B VAL   B 1 3   ? 48.953 -11.150 -17.577 0.42 20.21 ?  3   VAL   B HG11 1 
ATOM   3977 H HG12 A VAL   B 1 3   ? 49.654 -12.264 -17.359 0.58 25.89 ?  3   VAL   B HG12 1 
ATOM   3978 H HG12 B VAL   B 1 3   ? 49.808 -12.488 -17.520 0.42 20.21 ?  3   VAL   B HG12 1 
ATOM   3979 H HG13 A VAL   B 1 3   ? 49.297 -11.549 -18.733 0.58 25.89 ?  3   VAL   B HG13 1 
ATOM   3980 H HG13 B VAL   B 1 3   ? 49.478 -11.816 -18.921 0.42 20.21 ?  3   VAL   B HG13 1 
ATOM   3981 H HG21 A VAL   B 1 3   ? 46.544 -10.900 -18.203 0.58 25.62 ?  3   VAL   B HG21 1 
ATOM   3982 H HG21 B VAL   B 1 3   ? 46.690 -11.166 -18.479 0.42 19.92 ?  3   VAL   B HG21 1 
ATOM   3983 H HG22 A VAL   B 1 3   ? 46.766 -11.715 -19.548 0.58 25.62 ?  3   VAL   B HG22 1 
ATOM   3984 H HG22 B VAL   B 1 3   ? 47.046 -11.961 -19.804 0.42 19.92 ?  3   VAL   B HG22 1 
ATOM   3985 H HG23 A VAL   B 1 3   ? 45.740 -12.246 -18.458 0.58 25.62 ?  3   VAL   B HG23 1 
ATOM   3986 H HG23 B VAL   B 1 3   ? 45.948 -12.529 -18.807 0.42 19.92 ?  3   VAL   B HG23 1 
ATOM   3987 N N    . ASN   B 1 4   ? 46.558 -15.553 -17.598 1.00 15.22 ?  4   ASN   B N    1 
ATOM   3988 C CA   . ASN   B 1 4   ? 45.406 -16.437 -17.431 1.00 15.06 ?  4   ASN   B CA   1 
ATOM   3989 C C    . ASN   B 1 4   ? 45.325 -17.424 -18.594 1.00 15.61 ?  4   ASN   B C    1 
ATOM   3990 O O    . ASN   B 1 4   ? 44.267 -17.645 -19.177 1.00 16.00 ?  4   ASN   B O    1 
ATOM   3991 C CB   . ASN   B 1 4   ? 44.100 -15.646 -17.280 1.00 14.78 ?  4   ASN   B CB   1 
ATOM   3992 C CG   . ASN   B 1 4   ? 44.046 -14.854 -15.983 1.00 14.31 ?  4   ASN   B CG   1 
ATOM   3993 O OD1  . ASN   B 1 4   ? 44.327 -15.380 -14.909 1.00 14.03 ?  4   ASN   B OD1  1 
ATOM   3994 N ND2  . ASN   B 1 4   ? 43.706 -13.571 -16.084 1.00 15.54 ?  4   ASN   B ND2  1 
ATOM   3995 H H    A ASN   B 1 4   ? 47.130 -15.597 -16.957 0.58 18.23 ?  4   ASN   B H    1 
ATOM   3996 H H    B ASN   B 1 4   ? 47.002 -15.414 -16.877 0.42 18.23 ?  4   ASN   B H    1 
ATOM   3997 H HA   . ASN   B 1 4   ? 45.538 -16.953 -16.615 1.00 18.05 ?  4   ASN   B HA   1 
ATOM   3998 H HB2  . ASN   B 1 4   ? 44.021 -15.027 -18.020 1.00 17.71 ?  4   ASN   B HB2  1 
ATOM   3999 H HB3  . ASN   B 1 4   ? 43.357 -16.270 -17.285 1.00 17.71 ?  4   ASN   B HB3  1 
ATOM   4000 H HD21 . ASN   B 1 4   ? 43.659 -13.079 -15.378 1.00 18.62 ?  4   ASN   B HD21 1 
ATOM   4001 H HD22 . ASN   B 1 4   ? 43.517 -13.233 -16.852 1.00 18.62 ?  4   ASN   B HD22 1 
ATOM   4002 N N    . SER   B 1 5   ? 46.474 -18.012 -18.946 1.00 16.30 ?  5   SER   B N    1 
ATOM   4003 C CA   . SER   B 1 5   ? 46.564 -18.944 -20.071 1.00 18.47 ?  5   SER   B CA   1 
ATOM   4004 C C    . SER   B 1 5   ? 46.584 -20.352 -19.490 1.00 20.05 ?  5   SER   B C    1 
ATOM   4005 O O    . SER   B 1 5   ? 47.634 -20.945 -19.250 1.00 21.80 ?  5   SER   B O    1 
ATOM   4006 C CB   . SER   B 1 5   ? 47.807 -18.653 -20.910 1.00 20.31 ?  5   SER   B CB   1 
ATOM   4007 O OG   . SER   B 1 5   ? 48.987 -18.843 -20.152 1.00 24.10 ?  5   SER   B OG   1 
ATOM   4008 H H    . SER   B 1 5   ? 47.227 -17.894 -18.544 1.00 19.53 ?  5   SER   B H    1 
ATOM   4009 H HA   . SER   B 1 5   ? 45.782 -18.856 -20.636 1.00 22.14 ?  5   SER   B HA   1 
ATOM   4010 H HB2  . SER   B 1 5   ? 47.819 -19.254 -21.677 1.00 24.35 ?  5   SER   B HB2  1 
ATOM   4011 H HB3  . SER   B 1 5   ? 47.770 -17.735 -21.217 1.00 24.35 ?  5   SER   B HB3  1 
ATOM   4012 H HG   . SER   B 1 5   ? 49.057 -19.648 -19.923 1.00 28.90 ?  5   SER   B HG   1 
ATOM   4013 N N    . PHE   B 1 6   ? 45.388 -20.861 -19.213 1.00 21.52 ?  6   PHE   B N    1 
ATOM   4014 C CA   . PHE   B 1 6   ? 45.204 -22.183 -18.634 1.00 21.10 ?  6   PHE   B CA   1 
ATOM   4015 C C    . PHE   B 1 6   ? 45.124 -23.199 -19.763 1.00 25.62 ?  6   PHE   B C    1 
ATOM   4016 O O    . PHE   B 1 6   ? 44.369 -23.011 -20.720 1.00 28.50 ?  6   PHE   B O    1 
ATOM   4017 C CB   . PHE   B 1 6   ? 43.914 -22.222 -17.810 1.00 19.13 ?  6   PHE   B CB   1 
ATOM   4018 C CG   . PHE   B 1 6   ? 43.927 -21.317 -16.606 1.00 17.75 ?  6   PHE   B CG   1 
ATOM   4019 C CD1  . PHE   B 1 6   ? 44.427 -21.762 -15.395 1.00 16.56 ?  6   PHE   B CD1  1 
ATOM   4020 C CD2  . PHE   B 1 6   ? 43.426 -20.028 -16.684 1.00 17.31 ?  6   PHE   B CD2  1 
ATOM   4021 C CE1  . PHE   B 1 6   ? 44.426 -20.937 -14.279 1.00 16.15 ?  6   PHE   B CE1  1 
ATOM   4022 C CE2  . PHE   B 1 6   ? 43.440 -19.189 -15.582 1.00 17.43 ?  6   PHE   B CE2  1 
ATOM   4023 C CZ   . PHE   B 1 6   ? 43.944 -19.637 -14.380 1.00 16.60 ?  6   PHE   B CZ   1 
ATOM   4024 H H    . PHE   B 1 6   ? 44.649 -20.449 -19.358 1.00 25.80 ?  6   PHE   B H    1 
ATOM   4025 H HA   . PHE   B 1 6   ? 45.950 -22.408 -18.060 1.00 25.29 ?  6   PHE   B HA   1 
ATOM   4026 H HB2  . PHE   B 1 6   ? 43.172 -21.951 -18.376 1.00 22.93 ?  6   PHE   B HB2  1 
ATOM   4027 H HB3  . PHE   B 1 6   ? 43.769 -23.130 -17.496 1.00 22.93 ?  6   PHE   B HB3  1 
ATOM   4028 H HD1  . PHE   B 1 6   ? 44.764 -22.628 -15.326 1.00 19.85 ?  6   PHE   B HD1  1 
ATOM   4029 H HD2  . PHE   B 1 6   ? 43.087 -19.720 -17.492 1.00 20.75 ?  6   PHE   B HD2  1 
ATOM   4030 H HE1  . PHE   B 1 6   ? 44.778 -21.241 -13.472 1.00 19.36 ?  6   PHE   B HE1  1 
ATOM   4031 H HE2  . PHE   B 1 6   ? 43.096 -18.330 -15.652 1.00 20.90 ?  6   PHE   B HE2  1 
ATOM   4032 H HZ   . PHE   B 1 6   ? 43.941 -19.083 -13.636 1.00 19.90 ?  6   PHE   B HZ   1 
ATOM   4033 N N    A SER   B 1 7   ? 45.903 -24.271 -19.651 0.58 26.01 ?  7   SER   B N    1 
ATOM   4034 N N    B SER   B 1 7   ? 45.908 -24.268 -19.650 0.42 26.80 ?  7   SER   B N    1 
ATOM   4035 C CA   A SER   B 1 7   ? 45.981 -25.274 -20.702 0.58 28.16 ?  7   SER   B CA   1 
ATOM   4036 C CA   B SER   B 1 7   ? 46.008 -25.265 -20.705 0.42 28.86 ?  7   SER   B CA   1 
ATOM   4037 C C    A SER   B 1 7   ? 45.904 -26.669 -20.099 0.58 27.39 ?  7   SER   B C    1 
ATOM   4038 C C    B SER   B 1 7   ? 45.942 -26.659 -20.100 0.42 28.38 ?  7   SER   B C    1 
ATOM   4039 O O    A SER   B 1 7   ? 46.498 -26.942 -19.051 0.58 27.95 ?  7   SER   B O    1 
ATOM   4040 O O    B SER   B 1 7   ? 46.558 -26.927 -19.065 0.42 28.88 ?  7   SER   B O    1 
ATOM   4041 C CB   A SER   B 1 7   ? 47.276 -25.115 -21.511 0.58 30.86 ?  7   SER   B CB   1 
ATOM   4042 C CB   B SER   B 1 7   ? 47.317 -25.098 -21.487 0.42 31.01 ?  7   SER   B CB   1 
ATOM   4043 O OG   A SER   B 1 7   ? 47.267 -25.945 -22.660 0.58 32.72 ?  7   SER   B OG   1 
ATOM   4044 O OG   B SER   B 1 7   ? 47.332 -25.923 -22.639 0.42 32.34 ?  7   SER   B OG   1 
ATOM   4045 H H    A SER   B 1 7   ? 46.402 -24.439 -18.968 0.58 31.19 ?  7   SER   B H    1 
ATOM   4046 H H    B SER   B 1 7   ? 46.398 -24.436 -18.964 0.42 32.14 ?  7   SER   B H    1 
ATOM   4047 H HA   A SER   B 1 7   ? 45.232 -25.165 -21.306 0.58 33.76 ?  7   SER   B HA   1 
ATOM   4048 H HA   B SER   B 1 7   ? 45.268 -25.165 -21.322 0.42 34.61 ?  7   SER   B HA   1 
ATOM   4049 H HB2  A SER   B 1 7   ? 47.361 -24.187 -21.792 0.58 37.01 ?  7   SER   B HB2  1 
ATOM   4050 H HB2  B SER   B 1 7   ? 47.405 -24.169 -21.759 0.42 37.19 ?  7   SER   B HB2  1 
ATOM   4051 H HB3  A SER   B 1 7   ? 48.030 -25.359 -20.955 0.58 37.01 ?  7   SER   B HB3  1 
ATOM   4052 H HB3  B SER   B 1 7   ? 48.061 -25.345 -20.917 0.42 37.19 ?  7   SER   B HB3  1 
ATOM   4053 H HG   A SER   B 1 7   ? 47.980 -25.840 -23.095 0.58 39.24 ?  7   SER   B HG   1 
ATOM   4054 H HG   B SER   B 1 7   ? 48.051 -25.813 -23.060 0.42 38.79 ?  7   SER   B HG   1 
ATOM   4055 N N    A GLY   B 1 8   ? 45.159 -27.546 -20.766 0.58 27.04 ?  8   GLY   B N    1 
ATOM   4056 N N    B GLY   B 1 8   ? 45.189 -27.541 -20.755 0.42 27.87 ?  8   GLY   B N    1 
ATOM   4057 C CA   A GLY   B 1 8   ? 45.097 -28.935 -20.368 0.58 26.52 ?  8   GLY   B CA   1 
ATOM   4058 C CA   B GLY   B 1 8   ? 45.122 -28.926 -20.342 0.42 27.07 ?  8   GLY   B CA   1 
ATOM   4059 C C    A GLY   B 1 8   ? 44.141 -29.241 -19.244 0.58 25.30 ?  8   GLY   B C    1 
ATOM   4060 C C    B GLY   B 1 8   ? 44.174 -29.216 -19.205 0.42 25.73 ?  8   GLY   B C    1 
ATOM   4061 O O    A GLY   B 1 8   ? 44.262 -30.303 -18.622 0.58 25.93 ?  8   GLY   B O    1 
ATOM   4062 O O    B GLY   B 1 8   ? 44.337 -30.239 -18.530 0.42 26.37 ?  8   GLY   B O    1 
ATOM   4063 H H    A GLY   B 1 8   ? 44.682 -27.351 -21.452 0.58 32.43 ?  8   GLY   B H    1 
ATOM   4064 H H    B GLY   B 1 8   ? 44.710 -27.354 -21.443 0.42 33.42 ?  8   GLY   B H    1 
ATOM   4065 H HA2  A GLY   B 1 8   ? 44.827 -29.466 -21.131 0.58 31.81 ?  8   GLY   B HA2  1 
ATOM   4066 H HA2  B GLY   B 1 8   ? 44.850 -29.467 -21.100 0.42 32.45 ?  8   GLY   B HA2  1 
ATOM   4067 H HA3  A GLY   B 1 8   ? 45.976 -29.225 -20.091 0.58 31.81 ?  8   GLY   B HA3  1 
ATOM   4068 H HA3  B GLY   B 1 8   ? 46.002 -29.219 -20.066 0.42 32.45 ?  8   GLY   B HA3  1 
ATOM   4069 N N    . TYR   B 1 9   ? 43.176 -28.366 -18.975 1.00 24.24 ?  9   TYR   B N    1 
ATOM   4070 C CA   . TYR   B 1 9   ? 42.211 -28.599 -17.912 1.00 21.81 ?  9   TYR   B CA   1 
ATOM   4071 C C    . TYR   B 1 9   ? 41.013 -29.376 -18.426 1.00 21.18 ?  9   TYR   B C    1 
ATOM   4072 O O    . TYR   B 1 9   ? 40.595 -29.236 -19.580 1.00 22.97 ?  9   TYR   B O    1 
ATOM   4073 C CB   . TYR   B 1 9   ? 41.726 -27.291 -17.292 1.00 21.38 ?  9   TYR   B CB   1 
ATOM   4074 C CG   . TYR   B 1 9   ? 42.750 -26.680 -16.366 1.00 20.27 ?  9   TYR   B CG   1 
ATOM   4075 C CD1  . TYR   B 1 9   ? 43.865 -26.028 -16.871 1.00 20.87 ?  9   TYR   B CD1  1 
ATOM   4076 C CD2  . TYR   B 1 9   ? 42.611 -26.768 -14.988 1.00 19.40 ?  9   TYR   B CD2  1 
ATOM   4077 C CE1  . TYR   B 1 9   ? 44.815 -25.477 -16.033 1.00 20.64 ?  9   TYR   B CE1  1 
ATOM   4078 C CE2  . TYR   B 1 9   ? 43.559 -26.217 -14.137 1.00 19.46 ?  9   TYR   B CE2  1 
ATOM   4079 C CZ   . TYR   B 1 9   ? 44.661 -25.567 -14.670 1.00 20.54 ?  9   TYR   B CZ   1 
ATOM   4080 O OH   . TYR   B 1 9   ? 45.615 -25.025 -13.846 1.00 21.35 ?  9   TYR   B OH   1 
ATOM   4081 H H    A TYR   B 1 9   ? 43.038 -27.639 -19.412 0.58 29.06 ?  9   TYR   B H    1 
ATOM   4082 H H    B TYR   B 1 9   ? 43.020 -27.655 -19.433 0.42 29.06 ?  9   TYR   B H    1 
ATOM   4083 H HA   . TYR   B 1 9   ? 42.621 -29.119 -17.210 1.00 26.14 ?  9   TYR   B HA   1 
ATOM   4084 H HB2  . TYR   B 1 9   ? 41.533 -26.645 -17.994 1.00 25.63 ?  9   TYR   B HB2  1 
ATOM   4085 H HB3  . TYR   B 1 9   ? 40.928 -27.468 -16.775 1.00 25.63 ?  9   TYR   B HB3  1 
ATOM   4086 H HD1  . TYR   B 1 9   ? 43.975 -25.966 -17.792 1.00 25.02 ?  9   TYR   B HD1  1 
ATOM   4087 H HD2  . TYR   B 1 9   ? 41.864 -27.206 -14.630 1.00 23.26 ?  9   TYR   B HD2  1 
ATOM   4088 H HE1  . TYR   B 1 9   ? 45.551 -25.049 -16.389 1.00 24.74 ?  9   TYR   B HE1  1 
ATOM   4089 H HE2  . TYR   B 1 9   ? 43.440 -26.289 -13.215 1.00 23.32 ?  9   TYR   B HE2  1 
ATOM   4090 H HH   . TYR   B 1 9   ? 46.208 -24.671 -14.309 1.00 25.59 ?  9   TYR   B HH   1 
ATOM   4091 N N    . LEU   B 1 10  ? 40.470 -30.211 -17.546 1.00 18.99 ?  10  LEU   B N    1 
ATOM   4092 C CA   . LEU   B 1 10  ? 39.260 -30.966 -17.821 1.00 19.00 ?  10  LEU   B CA   1 
ATOM   4093 C C    . LEU   B 1 10  ? 38.073 -30.185 -17.274 1.00 18.66 ?  10  LEU   B C    1 
ATOM   4094 O O    . LEU   B 1 10  ? 38.082 -29.763 -16.115 1.00 18.02 ?  10  LEU   B O    1 
ATOM   4095 C CB   . LEU   B 1 10  ? 39.350 -32.329 -17.134 1.00 19.95 ?  10  LEU   B CB   1 
ATOM   4096 C CG   . LEU   B 1 10  ? 38.217 -33.293 -17.471 1.00 21.54 ?  10  LEU   B CG   1 
ATOM   4097 C CD1  . LEU   B 1 10  ? 38.349 -33.794 -18.906 1.00 22.79 ?  10  LEU   B CD1  1 
ATOM   4098 C CD2  . LEU   B 1 10  ? 38.173 -34.455 -16.491 1.00 22.66 ?  10  LEU   B CD2  1 
ATOM   4099 H H    . LEU   B 1 10  ? 40.784 -30.355 -16.751 1.00 22.77 ?  10  LEU   B H    1 
ATOM   4100 H HA   . LEU   B 1 10  ? 39.147 -31.094 -18.770 1.00 22.77 ?  10  LEU   B HA   1 
ATOM   4101 H HB2  . LEU   B 1 10  ? 40.183 -32.754 -17.397 1.00 23.91 ?  10  LEU   B HB2  1 
ATOM   4102 H HB3  . LEU   B 1 10  ? 39.344 -32.200 -16.171 1.00 23.91 ?  10  LEU   B HB3  1 
ATOM   4103 H HG   . LEU   B 1 10  ? 37.374 -32.821 -17.403 1.00 25.83 ?  10  LEU   B HG   1 
ATOM   4104 H HD11 . LEU   B 1 10  ? 37.663 -34.457 -19.073 1.00 27.33 ?  10  LEU   B HD11 1 
ATOM   4105 H HD12 . LEU   B 1 10  ? 38.238 -33.043 -19.512 1.00 27.33 ?  10  LEU   B HD12 1 
ATOM   4106 H HD13 . LEU   B 1 10  ? 39.227 -34.187 -19.023 1.00 27.33 ?  10  LEU   B HD13 1 
ATOM   4107 H HD21 . LEU   B 1 10  ? 37.443 -35.045 -16.738 1.00 27.16 ?  10  LEU   B HD21 1 
ATOM   4108 H HD22 . LEU   B 1 10  ? 39.014 -34.931 -16.529 1.00 27.16 ?  10  LEU   B HD22 1 
ATOM   4109 H HD23 . LEU   B 1 10  ? 38.027 -34.104 -15.598 1.00 27.16 ?  10  LEU   B HD23 1 
ATOM   4110 N N    . LYS   B 1 11  ? 37.054 -30.002 -18.106 1.00 19.78 ?  11  LYS   B N    1 
ATOM   4111 C CA   . LYS   B 1 11  ? 35.854 -29.295 -17.689 1.00 21.73 ?  11  LYS   B CA   1 
ATOM   4112 C C    . LYS   B 1 11  ? 34.985 -30.225 -16.844 1.00 20.57 ?  11  LYS   B C    1 
ATOM   4113 O O    . LYS   B 1 11  ? 34.633 -31.327 -17.286 1.00 22.49 ?  11  LYS   B O    1 
ATOM   4114 C CB   . LYS   B 1 11  ? 35.099 -28.830 -18.932 1.00 26.08 ?  11  LYS   B CB   1 
ATOM   4115 C CG   . LYS   B 1 11  ? 33.918 -27.922 -18.671 1.00 29.72 ?  11  LYS   B CG   1 
ATOM   4116 C CD   . LYS   B 1 11  ? 33.198 -27.607 -19.977 1.00 32.92 ?  11  LYS   B CD   1 
ATOM   4117 C CE   . LYS   B 1 11  ? 32.197 -26.480 -19.811 1.00 35.31 ?  11  LYS   B CE   1 
ATOM   4118 N NZ   . LYS   B 1 11  ? 32.869 -25.180 -19.545 1.00 36.43 ?  11  LYS   B NZ   1 
ATOM   4119 H H    . LYS   B 1 11  ? 37.028 -30.289 -18.917 1.00 23.71 ?  11  LYS   B H    1 
ATOM   4120 H HA   . LYS   B 1 11  ? 36.096 -28.521 -17.158 1.00 26.05 ?  11  LYS   B HA   1 
ATOM   4121 H HB2  . LYS   B 1 11  ? 35.718 -28.344 -19.501 1.00 31.27 ?  11  LYS   B HB2  1 
ATOM   4122 H HB3  . LYS   B 1 11  ? 34.769 -29.609 -19.403 1.00 31.27 ?  11  LYS   B HB3  1 
ATOM   4123 H HG2  . LYS   B 1 11  ? 33.294 -28.365 -18.076 1.00 35.63 ?  11  LYS   B HG2  1 
ATOM   4124 H HG3  . LYS   B 1 11  ? 34.228 -27.090 -18.282 1.00 35.63 ?  11  LYS   B HG3  1 
ATOM   4125 H HD2  . LYS   B 1 11  ? 33.851 -27.340 -20.644 1.00 39.48 ?  11  LYS   B HD2  1 
ATOM   4126 H HD3  . LYS   B 1 11  ? 32.721 -28.398 -20.277 1.00 39.48 ?  11  LYS   B HD3  1 
ATOM   4127 H HE2  . LYS   B 1 11  ? 31.677 -26.392 -20.624 1.00 42.35 ?  11  LYS   B HE2  1 
ATOM   4128 H HE3  . LYS   B 1 11  ? 31.616 -26.684 -19.062 1.00 42.35 ?  11  LYS   B HE3  1 
ATOM   4129 H HZ1  . LYS   B 1 11  ? 32.264 -24.528 -19.502 1.00 43.69 ?  11  LYS   B HZ1  1 
ATOM   4130 H HZ2  . LYS   B 1 11  ? 33.310 -25.216 -18.773 1.00 43.69 ?  11  LYS   B HZ2  1 
ATOM   4131 H HZ3  . LYS   B 1 11  ? 33.445 -24.996 -20.199 1.00 43.69 ?  11  LYS   B HZ3  1 
ATOM   4132 N N    . LEU   B 1 12  ? 34.643 -29.790 -15.629 1.00 19.09 ?  12  LEU   B N    1 
ATOM   4133 C CA   . LEU   B 1 12  ? 33.685 -30.497 -14.784 1.00 18.73 ?  12  LEU   B CA   1 
ATOM   4134 C C    . LEU   B 1 12  ? 32.298 -29.882 -14.869 1.00 18.64 ?  12  LEU   B C    1 
ATOM   4135 O O    . LEU   B 1 12  ? 31.306 -30.594 -15.033 1.00 19.39 ?  12  LEU   B O    1 
ATOM   4136 C CB   . LEU   B 1 12  ? 34.145 -30.517 -13.320 1.00 18.28 ?  12  LEU   B CB   1 
ATOM   4137 C CG   . LEU   B 1 12  ? 35.488 -31.191 -13.043 1.00 18.03 ?  12  LEU   B CG   1 
ATOM   4138 C CD1  . LEU   B 1 12  ? 35.852 -31.129 -11.565 1.00 17.88 ?  12  LEU   B CD1  1 
ATOM   4139 C CD2  . LEU   B 1 12  ? 35.495 -32.631 -13.536 1.00 18.45 ?  12  LEU   B CD2  1 
ATOM   4140 H H    . LEU   B 1 12  ? 34.950 -29.069 -15.269 1.00 22.89 ?  12  LEU   B H    1 
ATOM   4141 H HA   . LEU   B 1 12  ? 33.611 -31.412 -15.090 1.00 22.46 ?  12  LEU   B HA   1 
ATOM   4142 H HB2  . LEU   B 1 12  ? 34.206 -29.603 -13.007 1.00 21.92 ?  12  LEU   B HB2  1 
ATOM   4143 H HB3  . LEU   B 1 12  ? 33.472 -30.990 -12.799 1.00 21.92 ?  12  LEU   B HB3  1 
ATOM   4144 H HG   . LEU   B 1 12  ? 36.173 -30.710 -13.530 1.00 21.61 ?  12  LEU   B HG   1 
ATOM   4145 H HD11 . LEU   B 1 12  ? 36.713 -31.561 -11.434 1.00 21.44 ?  12  LEU   B HD11 1 
ATOM   4146 H HD12 . LEU   B 1 12  ? 35.906 -30.200 -11.288 1.00 21.44 ?  12  LEU   B HD12 1 
ATOM   4147 H HD13 . LEU   B 1 12  ? 35.172 -31.589 -11.049 1.00 21.44 ?  12  LEU   B HD13 1 
ATOM   4148 H HD21 . LEU   B 1 12  ? 36.310 -33.061 -13.236 1.00 22.11 ?  12  LEU   B HD21 1 
ATOM   4149 H HD22 . LEU   B 1 12  ? 34.723 -33.092 -13.174 1.00 22.11 ?  12  LEU   B HD22 1 
ATOM   4150 H HD23 . LEU   B 1 12  ? 35.457 -32.632 -14.505 1.00 22.11 ?  12  LEU   B HD23 1 
ATOM   4151 N N    . THR   B 1 13  ? 32.215 -28.565 -14.751 1.00 18.40 ?  13  THR   B N    1 
ATOM   4152 C CA   . THR   B 1 13  ? 30.993 -27.813 -14.976 1.00 18.59 ?  13  THR   B CA   1 
ATOM   4153 C C    . THR   B 1 13  ? 31.337 -26.627 -15.869 1.00 20.74 ?  13  THR   B C    1 
ATOM   4154 O O    . THR   B 1 13  ? 32.486 -26.442 -16.282 1.00 21.65 ?  13  THR   B O    1 
ATOM   4155 C CB   . THR   B 1 13  ? 30.385 -27.321 -13.657 1.00 18.17 ?  13  THR   B CB   1 
ATOM   4156 O OG1  . THR   B 1 13  ? 31.221 -26.287 -13.120 1.00 17.72 ?  13  THR   B OG1  1 
ATOM   4157 C CG2  . THR   B 1 13  ? 30.261 -28.461 -12.648 1.00 18.62 ?  13  THR   B CG2  1 
ATOM   4158 H H    . THR   B 1 13  ? 32.879 -28.066 -14.525 1.00 22.06 ?  13  THR   B H    1 
ATOM   4159 H HA   . THR   B 1 13  ? 30.340 -28.376 -15.423 1.00 22.28 ?  13  THR   B HA   1 
ATOM   4160 H HB   . THR   B 1 13  ? 29.492 -26.966 -13.825 1.00 21.77 ?  13  THR   B HB   1 
ATOM   4161 H HG1  . THR   B 1 13  ? 30.878 -25.528 -13.288 1.00 21.24 ?  13  THR   B HG1  1 
ATOM   4162 H HG21 . THR   B 1 13  ? 29.744 -28.171 -11.879 1.00 22.33 ?  13  THR   B HG21 1 
ATOM   4163 H HG22 . THR   B 1 13  ? 29.813 -29.219 -13.057 1.00 22.33 ?  13  THR   B HG22 1 
ATOM   4164 H HG23 . THR   B 1 13  ? 31.140 -28.737 -12.351 1.00 22.33 ?  13  THR   B HG23 1 
ATOM   4165 N N    A ASP   B 1 14  ? 30.328 -25.805 -16.153 0.58 21.32 ?  14  ASP   B N    1 
ATOM   4166 N N    B ASP   B 1 14  ? 30.332 -25.799 -16.157 0.42 21.27 ?  14  ASP   B N    1 
ATOM   4167 C CA   A ASP   B 1 14  ? 30.548 -24.645 -17.006 0.58 22.71 ?  14  ASP   B CA   1 
ATOM   4168 C CA   B ASP   B 1 14  ? 30.555 -24.643 -17.018 0.42 22.33 ?  14  ASP   B CA   1 
ATOM   4169 C C    A ASP   B 1 14  ? 31.650 -23.742 -16.465 0.58 20.91 ?  14  ASP   B C    1 
ATOM   4170 C C    B ASP   B 1 14  ? 31.582 -23.672 -16.453 0.42 20.64 ?  14  ASP   B C    1 
ATOM   4171 O O    A ASP   B 1 14  ? 32.336 -23.076 -17.250 0.58 22.19 ?  14  ASP   B O    1 
ATOM   4172 O O    B ASP   B 1 14  ? 32.118 -22.856 -17.211 0.42 21.42 ?  14  ASP   B O    1 
ATOM   4173 C CB   A ASP   B 1 14  ? 29.247 -23.860 -17.172 0.58 26.11 ?  14  ASP   B CB   1 
ATOM   4174 C CB   B ASP   B 1 14  ? 29.248 -23.891 -17.262 0.42 25.19 ?  14  ASP   B CB   1 
ATOM   4175 C CG   A ASP   B 1 14  ? 28.241 -24.567 -18.061 0.58 29.46 ?  14  ASP   B CG   1 
ATOM   4176 C CG   B ASP   B 1 14  ? 28.374 -24.564 -18.301 0.42 27.95 ?  14  ASP   B CG   1 
ATOM   4177 O OD1  A ASP   B 1 14  ? 28.594 -25.579 -18.707 0.58 30.33 ?  14  ASP   B OD1  1 
ATOM   4178 O OD1  B ASP   B 1 14  ? 28.925 -25.247 -19.191 0.42 28.82 ?  14  ASP   B OD1  1 
ATOM   4179 O OD2  A ASP   B 1 14  ? 27.080 -24.111 -18.101 0.58 31.05 -1 14  ASP   B OD2  1 
ATOM   4180 O OD2  B ASP   B 1 14  ? 27.137 -24.413 -18.233 0.42 29.12 -1 14  ASP   B OD2  1 
ATOM   4181 H H    A ASP   B 1 14  ? 29.524 -25.893 -15.863 0.58 25.56 ?  14  ASP   B H    1 
ATOM   4182 H H    B ASP   B 1 14  ? 29.526 -25.887 -15.874 0.42 25.50 ?  14  ASP   B H    1 
ATOM   4183 H HA   A ASP   B 1 14  ? 30.830 -24.943 -17.880 0.58 27.23 ?  14  ASP   B HA   1 
ATOM   4184 H HA   B ASP   B 1 14  ? 30.884 -24.954 -17.874 0.42 26.77 ?  14  ASP   B HA   1 
ATOM   4185 H HB2  A ASP   B 1 14  ? 28.823 -23.755 -16.309 0.58 31.30 ?  14  ASP   B HB2  1 
ATOM   4186 H HB2  B ASP   B 1 14  ? 28.755 -23.841 -16.428 0.42 30.20 ?  14  ASP   B HB2  1 
ATOM   4187 H HB3  A ASP   B 1 14  ? 29.447 -22.990 -17.555 0.58 31.30 ?  14  ASP   B HB3  1 
ATOM   4188 H HB3  B ASP   B 1 14  ? 29.459 -22.994 -17.574 0.42 30.20 ?  14  ASP   B HB3  1 
ATOM   4189 N N    . ASN   B 1 15  ? 31.852 -23.717 -15.144 1.00 18.90 ?  15  ASN   B N    1 
ATOM   4190 C CA   . ASN   B 1 15  ? 32.813 -22.802 -14.533 1.00 16.60 ?  15  ASN   B CA   1 
ATOM   4191 C C    . ASN   B 1 15  ? 33.899 -23.456 -13.691 1.00 15.00 ?  15  ASN   B C    1 
ATOM   4192 O O    . ASN   B 1 15  ? 34.742 -22.729 -13.160 1.00 15.09 ?  15  ASN   B O    1 
ATOM   4193 C CB   . ASN   B 1 15  ? 32.100 -21.742 -13.679 1.00 16.73 ?  15  ASN   B CB   1 
ATOM   4194 C CG   . ASN   B 1 15  ? 31.467 -22.335 -12.436 1.00 16.32 ?  15  ASN   B CG   1 
ATOM   4195 O OD1  . ASN   B 1 15  ? 30.524 -23.130 -12.527 1.00 18.15 ?  15  ASN   B OD1  1 
ATOM   4196 N ND2  . ASN   B 1 15  ? 31.985 -21.977 -11.272 1.00 15.01 ?  15  ASN   B ND2  1 
ATOM   4197 H H    A ASN   B 1 15  ? 31.443 -24.228 -14.579 0.58 22.65 ?  15  ASN   B H    1 
ATOM   4198 H H    B ASN   B 1 15  ? 31.467 -24.251 -14.584 0.42 22.65 ?  15  ASN   B H    1 
ATOM   4199 H HA   . ASN   B 1 15  ? 33.273 -22.327 -15.232 1.00 19.90 ?  15  ASN   B HA   1 
ATOM   4200 H HB2  . ASN   B 1 15  ? 32.748 -21.067 -13.400 1.00 20.05 ?  15  ASN   B HB2  1 
ATOM   4201 H HB3  . ASN   B 1 15  ? 31.401 -21.322 -14.205 1.00 20.05 ?  15  ASN   B HB3  1 
ATOM   4202 H HD21 . ASN   B 1 15  ? 31.655 -22.283 -10.536 1.00 17.98 ?  15  ASN   B HD21 1 
ATOM   4203 H HD22 . ASN   B 1 15  ? 32.651 -21.426 -11.238 1.00 17.98 ?  15  ASN   B HD22 1 
ATOM   4204 N N    . VAL   B 1 16  ? 33.917 -24.780 -13.547 1.00 14.48 ?  16  VAL   B N    1 
ATOM   4205 C CA   . VAL   B 1 16  ? 34.914 -25.473 -12.735 1.00 14.31 ?  16  VAL   B CA   1 
ATOM   4206 C C    . VAL   B 1 16  ? 35.701 -26.414 -13.631 1.00 14.65 ?  16  VAL   B C    1 
ATOM   4207 O O    . VAL   B 1 16  ? 35.119 -27.293 -14.287 1.00 15.74 ?  16  VAL   B O    1 
ATOM   4208 C CB   . VAL   B 1 16  ? 34.281 -26.229 -11.555 1.00 15.06 ?  16  VAL   B CB   1 
ATOM   4209 C CG1  . VAL   B 1 16  ? 35.351 -26.971 -10.746 1.00 15.28 ?  16  VAL   B CG1  1 
ATOM   4210 C CG2  . VAL   B 1 16  ? 33.486 -25.270 -10.671 1.00 15.97 ?  16  VAL   B CG2  1 
ATOM   4211 H H    . VAL   B 1 16  ? 33.343 -25.315 -13.908 1.00 17.35 ?  16  VAL   B H    1 
ATOM   4212 H HA   . VAL   B 1 16  ? 35.529 -24.826 -12.365 1.00 17.15 ?  16  VAL   B HA   1 
ATOM   4213 H HB   . VAL   B 1 16  ? 33.662 -26.897 -11.898 1.00 18.05 ?  16  VAL   B HB   1 
ATOM   4214 H HG11 . VAL   B 1 16  ? 34.958 -27.286 -9.914  1.00 18.31 ?  16  VAL   B HG11 1 
ATOM   4215 H HG12 . VAL   B 1 16  ? 35.674 -27.728 -11.260 1.00 18.31 ?  16  VAL   B HG12 1 
ATOM   4216 H HG13 . VAL   B 1 16  ? 36.079 -26.362 -10.554 1.00 18.31 ?  16  VAL   B HG13 1 
ATOM   4217 H HG21 . VAL   B 1 16  ? 33.155 -25.752 -9.895  1.00 19.15 ?  16  VAL   B HG21 1 
ATOM   4218 H HG22 . VAL   B 1 16  ? 34.068 -24.549 -10.388 1.00 19.15 ?  16  VAL   B HG22 1 
ATOM   4219 H HG23 . VAL   B 1 16  ? 32.743 -24.915 -11.182 1.00 19.15 ?  16  VAL   B HG23 1 
ATOM   4220 N N    . TYR   B 1 17  ? 37.025 -26.248 -13.619 1.00 14.98 ?  17  TYR   B N    1 
ATOM   4221 C CA   . TYR   B 1 17  ? 37.971 -27.008 -14.421 1.00 15.19 ?  17  TYR   B CA   1 
ATOM   4222 C C    . TYR   B 1 17  ? 39.019 -27.613 -13.497 1.00 14.16 ?  17  TYR   B C    1 
ATOM   4223 O O    . TYR   B 1 17  ? 39.291 -27.079 -12.420 1.00 14.45 ?  17  TYR   B O    1 
ATOM   4224 C CB   . TYR   B 1 17  ? 38.679 -26.090 -15.431 1.00 17.92 ?  17  TYR   B CB   1 
ATOM   4225 C CG   . TYR   B 1 17  ? 37.757 -25.312 -16.337 1.00 21.25 ?  17  TYR   B CG   1 
ATOM   4226 C CD1  . TYR   B 1 17  ? 37.201 -24.106 -15.931 1.00 22.94 ?  17  TYR   B CD1  1 
ATOM   4227 C CD2  . TYR   B 1 17  ? 37.447 -25.782 -17.604 1.00 23.35 ?  17  TYR   B CD2  1 
ATOM   4228 C CE1  . TYR   B 1 17  ? 36.356 -23.390 -16.763 1.00 24.60 ?  17  TYR   B CE1  1 
ATOM   4229 C CE2  . TYR   B 1 17  ? 36.609 -25.075 -18.444 1.00 24.86 ?  17  TYR   B CE2  1 
ATOM   4230 C CZ   . TYR   B 1 17  ? 36.065 -23.882 -18.016 1.00 25.63 ?  17  TYR   B CZ   1 
ATOM   4231 O OH   . TYR   B 1 17  ? 35.232 -23.176 -18.849 1.00 27.14 ?  17  TYR   B OH   1 
ATOM   4232 H H    . TYR   B 1 17  ? 37.416 -25.664 -13.117 1.00 17.96 ?  17  TYR   B H    1 
ATOM   4233 H HA   . TYR   B 1 17  ? 37.504 -27.716 -14.899 1.00 18.20 ?  17  TYR   B HA   1 
ATOM   4234 H HB2  . TYR   B 1 17  ? 39.225 -25.455 -14.946 1.00 21.48 ?  17  TYR   B HB2  1 
ATOM   4235 H HB3  . TYR   B 1 17  ? 39.234 -26.640 -15.998 1.00 21.48 ?  17  TYR   B HB3  1 
ATOM   4236 H HD1  . TYR   B 1 17  ? 37.396 -23.773 -15.086 1.00 27.51 ?  17  TYR   B HD1  1 
ATOM   4237 H HD2  . TYR   B 1 17  ? 37.807 -26.587 -17.897 1.00 27.99 ?  17  TYR   B HD2  1 
ATOM   4238 H HE1  . TYR   B 1 17  ? 35.990 -22.582 -16.480 1.00 29.49 ?  17  TYR   B HE1  1 
ATOM   4239 H HE2  . TYR   B 1 17  ? 36.403 -25.403 -19.293 1.00 29.81 ?  17  TYR   B HE2  1 
ATOM   4240 H HH   . TYR   B 1 17  ? 35.134 -23.580 -19.580 1.00 32.54 ?  17  TYR   B HH   1 
ATOM   4241 N N    . ILE   B 1 18  ? 39.637 -28.717 -13.920 1.00 14.45 ?  18  ILE   B N    1 
ATOM   4242 C CA   . ILE   B 1 18  ? 40.558 -29.437 -13.047 1.00 14.47 ?  18  ILE   B CA   1 
ATOM   4243 C C    . ILE   B 1 18  ? 41.720 -30.002 -13.855 1.00 14.72 ?  18  ILE   B C    1 
ATOM   4244 O O    . ILE   B 1 18  ? 41.566 -30.397 -15.014 1.00 16.15 ?  18  ILE   B O    1 
ATOM   4245 C CB   . ILE   B 1 18  ? 39.799 -30.534 -12.245 1.00 14.80 ?  18  ILE   B CB   1 
ATOM   4246 C CG1  . ILE   B 1 18  ? 40.657 -31.086 -11.098 1.00 15.08 ?  18  ILE   B CG1  1 
ATOM   4247 C CG2  . ILE   B 1 18  ? 39.287 -31.658 -13.169 1.00 15.50 ?  18  ILE   B CG2  1 
ATOM   4248 C CD1  . ILE   B 1 18  ? 39.852 -31.882 -10.071 1.00 16.52 ?  18  ILE   B CD1  1 
ATOM   4249 H H    . ILE   B 1 18  ? 39.539 -29.064 -14.697 1.00 17.31 ?  18  ILE   B H    1 
ATOM   4250 H HA   . ILE   B 1 18  ? 40.916 -28.816 -12.393 1.00 17.34 ?  18  ILE   B HA   1 
ATOM   4251 H HB   . ILE   B 1 18  ? 39.016 -30.127 -11.839 1.00 17.74 ?  18  ILE   B HB   1 
ATOM   4252 H HG12 . ILE   B 1 18  ? 41.332 -31.672 -11.463 1.00 18.07 ?  18  ILE   B HG12 1 
ATOM   4253 H HG13 . ILE   B 1 18  ? 41.069 -30.343 -10.634 1.00 18.07 ?  18  ILE   B HG13 1 
ATOM   4254 H HG21 . ILE   B 1 18  ? 38.709 -32.253 -12.661 1.00 18.58 ?  18  ILE   B HG21 1 
ATOM   4255 H HG22 . ILE   B 1 18  ? 38.787 -31.258 -13.898 1.00 18.58 ?  18  ILE   B HG22 1 
ATOM   4256 H HG23 . ILE   B 1 18  ? 40.044 -32.152 -13.517 1.00 18.58 ?  18  ILE   B HG23 1 
ATOM   4257 H HD11 . ILE   B 1 18  ? 40.444 -32.170 -9.357  1.00 19.80 ?  18  ILE   B HD11 1 
ATOM   4258 H HD12 . ILE   B 1 18  ? 39.149 -31.320 -9.708  1.00 19.80 ?  18  ILE   B HD12 1 
ATOM   4259 H HD13 . ILE   B 1 18  ? 39.461 -32.659 -10.505 1.00 19.80 ?  18  ILE   B HD13 1 
ATOM   4260 N N    . LYS   B 1 19  ? 42.897 -30.041 -13.227 1.00 15.35 ?  19  LYS   B N    1 
ATOM   4261 C CA   . LYS   B 1 19  ? 44.106 -30.523 -13.881 1.00 16.13 ?  19  LYS   B CA   1 
ATOM   4262 C C    . LYS   B 1 19  ? 45.002 -31.202 -12.856 1.00 15.88 ?  19  LYS   B C    1 
ATOM   4263 O O    . LYS   B 1 19  ? 45.093 -30.757 -11.710 1.00 15.41 ?  19  LYS   B O    1 
ATOM   4264 C CB   . LYS   B 1 19  ? 44.876 -29.359 -14.522 1.00 17.71 ?  19  LYS   B CB   1 
ATOM   4265 C CG   . LYS   B 1 19  ? 46.081 -29.771 -15.352 1.00 19.80 ?  19  LYS   B CG   1 
ATOM   4266 C CD   . LYS   B 1 19  ? 46.823 -28.549 -15.893 1.00 21.16 ?  19  LYS   B CD   1 
ATOM   4267 C CE   . LYS   B 1 19  ? 48.000 -28.941 -16.773 1.00 22.79 ?  19  LYS   B CE   1 
ATOM   4268 N NZ   . LYS   B 1 19  ? 48.777 -27.764 -17.252 1.00 23.64 ?  19  LYS   B NZ   1 
ATOM   4269 H H    . LYS   B 1 19  ? 43.006 -29.793 -12.411 1.00 18.39 ?  19  LYS   B H    1 
ATOM   4270 H HA   . LYS   B 1 19  ? 43.863 -31.163 -14.570 1.00 19.33 ?  19  LYS   B HA   1 
ATOM   4271 H HB2  . LYS   B 1 19  ? 44.267 -28.876 -15.102 1.00 21.22 ?  19  LYS   B HB2  1 
ATOM   4272 H HB3  . LYS   B 1 19  ? 45.183 -28.771 -13.812 1.00 21.22 ?  19  LYS   B HB3  1 
ATOM   4273 H HG2  . LYS   B 1 19  ? 46.687 -30.284 -14.798 1.00 23.74 ?  19  LYS   B HG2  1 
ATOM   4274 H HG3  . LYS   B 1 19  ? 45.775 -30.307 -16.102 1.00 23.74 ?  19  LYS   B HG3  1 
ATOM   4275 H HD2  . LYS   B 1 19  ? 46.208 -28.014 -16.422 1.00 25.37 ?  19  LYS   B HD2  1 
ATOM   4276 H HD3  . LYS   B 1 19  ? 47.158 -28.028 -15.146 1.00 25.37 ?  19  LYS   B HD3  1 
ATOM   4277 H HE2  . LYS   B 1 19  ? 48.595 -29.514 -16.264 1.00 27.32 ?  19  LYS   B HE2  1 
ATOM   4278 H HE3  . LYS   B 1 19  ? 47.664 -29.422 -17.548 1.00 27.32 ?  19  LYS   B HE3  1 
ATOM   4279 H HZ1  . LYS   B 1 19  ? 49.421 -28.030 -17.806 1.00 28.34 ?  19  LYS   B HZ1  1 
ATOM   4280 H HZ2  . LYS   B 1 19  ? 48.239 -27.201 -17.685 1.00 28.34 ?  19  LYS   B HZ2  1 
ATOM   4281 H HZ3  . LYS   B 1 19  ? 49.144 -27.341 -16.562 1.00 28.34 ?  19  LYS   B HZ3  1 
ATOM   4282 N N    . ASN   B 1 20  ? 45.689 -32.257 -13.283 1.00 16.74 ?  20  ASN   B N    1 
ATOM   4283 C CA   . ASN   B 1 20  ? 46.723 -32.889 -12.464 1.00 17.86 ?  20  ASN   B CA   1 
ATOM   4284 C C    . ASN   B 1 20  ? 47.991 -32.066 -12.659 1.00 18.35 ?  20  ASN   B C    1 
ATOM   4285 O O    . ASN   B 1 20  ? 48.631 -32.135 -13.714 1.00 20.29 ?  20  ASN   B O    1 
ATOM   4286 C CB   . ASN   B 1 20  ? 46.900 -34.345 -12.894 1.00 19.87 ?  20  ASN   B CB   1 
ATOM   4287 C CG   . ASN   B 1 20  ? 48.065 -35.048 -12.205 1.00 21.64 ?  20  ASN   B CG   1 
ATOM   4288 O OD1  . ASN   B 1 20  ? 48.747 -35.879 -12.819 1.00 23.97 ?  20  ASN   B OD1  1 
ATOM   4289 N ND2  . ASN   B 1 20  ? 48.284 -34.746 -10.933 1.00 21.29 ?  20  ASN   B ND2  1 
ATOM   4290 H H    . ASN   B 1 20  ? 45.571 -32.628 -14.049 1.00 20.06 ?  20  ASN   B H    1 
ATOM   4291 H HA   . ASN   B 1 20  ? 46.452 -32.863 -11.531 1.00 21.41 ?  20  ASN   B HA   1 
ATOM   4292 H HB2  . ASN   B 1 20  ? 46.088 -34.835 -12.683 1.00 23.82 ?  20  ASN   B HB2  1 
ATOM   4293 H HB3  . ASN   B 1 20  ? 47.058 -34.368 -13.849 1.00 23.82 ?  20  ASN   B HB3  1 
ATOM   4294 H HD21 . ASN   B 1 20  ? 48.931 -35.116 -10.507 1.00 25.53 ?  20  ASN   B HD21 1 
ATOM   4295 H HD22 . ASN   B 1 20  ? 47.782 -34.170 -10.528 1.00 25.53 ?  20  ASN   B HD22 1 
ATOM   4296 N N    . ALA   B 1 21  ? 48.350 -31.261 -11.655 1.00 18.00 ?  21  ALA   B N    1 
ATOM   4297 C CA   . ALA   B 1 21  ? 49.470 -30.344 -11.808 1.00 18.86 ?  21  ALA   B CA   1 
ATOM   4298 C C    . ALA   B 1 21  ? 49.928 -29.840 -10.447 1.00 17.70 ?  21  ALA   B C    1 
ATOM   4299 O O    . ALA   B 1 21  ? 49.183 -29.866 -9.464  1.00 17.15 ?  21  ALA   B O    1 
ATOM   4300 C CB   . ALA   B 1 21  ? 49.094 -29.168 -12.710 1.00 20.45 ?  21  ALA   B CB   1 
ATOM   4301 H H    . ALA   B 1 21  ? 47.964 -31.233 -10.879 1.00 21.58 ?  21  ALA   B H    1 
ATOM   4302 H HA   . ALA   B 1 21  ? 50.207 -30.821 -12.216 1.00 22.61 ?  21  ALA   B HA   1 
ATOM   4303 H HB1  . ALA   B 1 21  ? 49.883 -28.628 -12.852 1.00 24.52 ?  21  ALA   B HB1  1 
ATOM   4304 H HB2  . ALA   B 1 21  ? 48.771 -29.517 -13.555 1.00 24.52 ?  21  ALA   B HB2  1 
ATOM   4305 H HB3  . ALA   B 1 21  ? 48.399 -28.649 -12.278 1.00 24.52 ?  21  ALA   B HB3  1 
ATOM   4306 N N    . ASP   B 1 22  ? 51.184 -29.396 -10.422 1.00 16.93 ?  22  ASP   B N    1 
ATOM   4307 C CA   . ASP   B 1 22  ? 51.795 -28.697 -9.294  1.00 16.10 ?  22  ASP   B CA   1 
ATOM   4308 C C    . ASP   B 1 22  ? 51.389 -27.224 -9.378  1.00 14.41 ?  22  ASP   B C    1 
ATOM   4309 O O    . ASP   B 1 22  ? 51.689 -26.554 -10.369 1.00 14.99 ?  22  ASP   B O    1 
ATOM   4310 C CB   . ASP   B 1 22  ? 53.313 -28.877 -9.446  1.00 17.33 ?  22  ASP   B CB   1 
ATOM   4311 C CG   . ASP   B 1 22  ? 54.142 -28.106 -8.426  1.00 19.34 ?  22  ASP   B CG   1 
ATOM   4312 O OD1  . ASP   B 1 22  ? 53.792 -26.980 -8.039  1.00 19.29 ?  22  ASP   B OD1  1 
ATOM   4313 O OD2  . ASP   B 1 22  ? 55.209 -28.626 -8.040  1.00 21.75 -1 22  ASP   B OD2  1 
ATOM   4314 H H    . ASP   B 1 22  ? 51.728 -29.485 -11.086 1.00 20.30 ?  22  ASP   B H    1 
ATOM   4315 H HA   . ASP   B 1 22  ? 51.503 -29.083 -8.449  1.00 19.29 ?  22  ASP   B HA   1 
ATOM   4316 H HB2  . ASP   B 1 22  ? 53.533 -29.815 -9.353  1.00 20.77 ?  22  ASP   B HB2  1 
ATOM   4317 H HB3  . ASP   B 1 22  ? 53.578 -28.560 -10.323 1.00 20.77 ?  22  ASP   B HB3  1 
ATOM   4318 N N    . ILE   B 1 23  ? 50.678 -26.726 -8.358  1.00 13.66 ?  23  ILE   B N    1 
ATOM   4319 C CA   . ILE   B 1 23  ? 50.087 -25.386 -8.439  1.00 13.04 ?  23  ILE   B CA   1 
ATOM   4320 C C    . ILE   B 1 23  ? 51.146 -24.298 -8.579  1.00 13.00 ?  23  ILE   B C    1 
ATOM   4321 O O    . ILE   B 1 23  ? 50.882 -23.255 -9.187  1.00 12.58 ?  23  ILE   B O    1 
ATOM   4322 C CB   . ILE   B 1 23  ? 49.136 -25.131 -7.253  1.00 13.73 ?  23  ILE   B CB   1 
ATOM   4323 C CG1  . ILE   B 1 23  ? 48.337 -23.845 -7.460  1.00 14.44 ?  23  ILE   B CG1  1 
ATOM   4324 C CG2  . ILE   B 1 23  ? 49.883 -25.122 -5.935  1.00 14.56 ?  23  ILE   B CG2  1 
ATOM   4325 C CD1  . ILE   B 1 23  ? 47.186 -23.686 -6.482  1.00 15.22 ?  23  ILE   B CD1  1 
ATOM   4326 H H    . ILE   B 1 23  ? 50.530 -27.142 -7.619  1.00 16.37 ?  23  ILE   B H    1 
ATOM   4327 H HA   . ILE   B 1 23  ? 49.551 -25.357 -9.242  1.00 15.63 ?  23  ILE   B HA   1 
ATOM   4328 H HB   . ILE   B 1 23  ? 48.502 -25.865 -7.229  1.00 16.46 ?  23  ILE   B HB   1 
ATOM   4329 H HG12 . ILE   B 1 23  ? 48.940 -23.087 -7.344  1.00 17.30 ?  23  ILE   B HG12 1 
ATOM   4330 H HG13 . ILE   B 1 23  ? 47.980 -23.839 -8.362  1.00 17.30 ?  23  ILE   B HG13 1 
ATOM   4331 H HG21 . ILE   B 1 23  ? 49.240 -25.089 -5.213  1.00 17.45 ?  23  ILE   B HG21 1 
ATOM   4332 H HG22 . ILE   B 1 23  ? 50.412 -25.934 -5.870  1.00 17.45 ?  23  ILE   B HG22 1 
ATOM   4333 H HG23 . ILE   B 1 23  ? 50.461 -24.347 -5.908  1.00 17.45 ?  23  ILE   B HG23 1 
ATOM   4334 H HD11 . ILE   B 1 23  ? 46.681 -22.895 -6.724  1.00 18.25 ?  23  ILE   B HD11 1 
ATOM   4335 H HD12 . ILE   B 1 23  ? 46.621 -24.472 -6.542  1.00 18.25 ?  23  ILE   B HD12 1 
ATOM   4336 H HD13 . ILE   B 1 23  ? 47.542 -23.596 -5.589  1.00 18.25 ?  23  ILE   B HD13 1 
ATOM   4337 N N    . VAL   B 1 24  ? 52.343 -24.501 -8.021  1.00 13.17 ?  24  VAL   B N    1 
ATOM   4338 C CA   . VAL   B 1 24  ? 53.414 -23.518 -8.182  1.00 13.80 ?  24  VAL   B CA   1 
ATOM   4339 C C    . VAL   B 1 24  ? 53.878 -23.475 -9.629  1.00 14.05 ?  24  VAL   B C    1 
ATOM   4340 O O    . VAL   B 1 24  ? 54.017 -22.399 -10.228 1.00 14.83 ?  24  VAL   B O    1 
ATOM   4341 C CB   . VAL   B 1 24  ? 54.584 -23.829 -7.226  1.00 14.60 ?  24  VAL   B CB   1 
ATOM   4342 C CG1  . VAL   B 1 24  ? 55.800 -22.956 -7.549  1.00 15.53 ?  24  VAL   B CG1  1 
ATOM   4343 C CG2  . VAL   B 1 24  ? 54.159 -23.629 -5.794  1.00 15.68 ?  24  VAL   B CG2  1 
ATOM   4344 H H    . VAL   B 1 24  ? 52.559 -25.189 -7.552  1.00 15.79 ?  24  VAL   B H    1 
ATOM   4345 H HA   . VAL   B 1 24  ? 53.076 -22.642 -7.954  1.00 16.53 ?  24  VAL   B HA   1 
ATOM   4346 H HB   . VAL   B 1 24  ? 54.847 -24.758 -7.332  1.00 17.49 ?  24  VAL   B HB   1 
ATOM   4347 H HG11 . VAL   B 1 24  ? 56.403 -22.962 -6.789  1.00 18.62 ?  24  VAL   B HG11 1 
ATOM   4348 H HG12 . VAL   B 1 24  ? 56.250 -23.314 -8.330  1.00 18.62 ?  24  VAL   B HG12 1 
ATOM   4349 H HG13 . VAL   B 1 24  ? 55.499 -22.050 -7.723  1.00 18.62 ?  24  VAL   B HG13 1 
ATOM   4350 H HG21 . VAL   B 1 24  ? 54.882 -23.896 -5.208  1.00 18.79 ?  24  VAL   B HG21 1 
ATOM   4351 H HG22 . VAL   B 1 24  ? 53.952 -22.690 -5.659  1.00 18.79 ?  24  VAL   B HG22 1 
ATOM   4352 H HG23 . VAL   B 1 24  ? 53.373 -24.170 -5.620  1.00 18.79 ?  24  VAL   B HG23 1 
ATOM   4353 N N    . GLU   B 1 25  ? 54.142 -24.650 -10.210 1.00 15.21 ?  25  GLU   B N    1 
ATOM   4354 C CA   . GLU   B 1 25  ? 54.537 -24.695 -11.612 1.00 16.60 ?  25  GLU   B CA   1 
ATOM   4355 C C    . GLU   B 1 25  ? 53.431 -24.155 -12.503 1.00 15.29 ?  25  GLU   B C    1 
ATOM   4356 O O    . GLU   B 1 25  ? 53.696 -23.429 -13.469 1.00 16.17 ?  25  GLU   B O    1 
ATOM   4357 C CB   . GLU   B 1 25  ? 54.927 -26.119 -12.005 1.00 20.68 ?  25  GLU   B CB   1 
ATOM   4358 C CG   . GLU   B 1 25  ? 56.227 -26.569 -11.355 1.00 27.06 ?  25  GLU   B CG   1 
ATOM   4359 C CD   . GLU   B 1 25  ? 57.343 -25.537 -11.455 1.00 33.14 ?  25  GLU   B CD   1 
ATOM   4360 O OE1  . GLU   B 1 25  ? 57.741 -25.190 -12.588 1.00 35.01 ?  25  GLU   B OE1  1 
ATOM   4361 O OE2  . GLU   B 1 25  ? 57.813 -25.056 -10.397 1.00 34.77 -1 25  GLU   B OE2  1 
ATOM   4362 H H    . GLU   B 1 25  ? 54.103 -25.415 -9.820  1.00 18.23 ?  25  GLU   B H    1 
ATOM   4363 H HA   . GLU   B 1 25  ? 55.298 -24.111 -11.740 1.00 19.90 ?  25  GLU   B HA   1 
ATOM   4364 H HB2  . GLU   B 1 25  ? 54.223 -26.728 -11.723 1.00 24.79 ?  25  GLU   B HB2  1 
ATOM   4365 H HB3  . GLU   B 1 25  ? 55.034 -26.163 -12.969 1.00 24.79 ?  25  GLU   B HB3  1 
ATOM   4366 H HG2  . GLU   B 1 25  ? 56.071 -26.725 -10.417 1.00 32.44 ?  25  GLU   B HG2  1 
ATOM   4367 H HG3  . GLU   B 1 25  ? 56.531 -27.377 -11.793 1.00 32.44 ?  25  GLU   B HG3  1 
ATOM   4368 N N    . GLU   B 1 26  ? 52.180 -24.478 -12.177 1.00 14.24 ?  26  GLU   B N    1 
ATOM   4369 C CA   . GLU   B 1 26  ? 51.059 -23.946 -12.945 1.00 14.71 ?  26  GLU   B CA   1 
ATOM   4370 C C    . GLU   B 1 26  ? 51.009 -22.427 -12.869 1.00 13.75 ?  26  GLU   B C    1 
ATOM   4371 O O    . GLU   B 1 26  ? 50.811 -21.753 -13.884 1.00 15.43 ?  26  GLU   B O    1 
ATOM   4372 C CB   . GLU   B 1 26  ? 49.740 -24.531 -12.440 1.00 16.47 ?  26  GLU   B CB   1 
ATOM   4373 C CG   . GLU   B 1 26  ? 49.324 -25.822 -13.105 1.00 20.45 ?  26  GLU   B CG   1 
ATOM   4374 C CD   . GLU   B 1 26  ? 49.103 -25.692 -14.611 1.00 22.00 ?  26  GLU   B CD   1 
ATOM   4375 O OE1  . GLU   B 1 26  ? 48.140 -25.031 -15.061 1.00 21.96 ?  26  GLU   B OE1  1 
ATOM   4376 O OE2  . GLU   B 1 26  ? 49.895 -26.289 -15.345 1.00 24.83 -1 26  GLU   B OE2  1 
ATOM   4377 H H    . GLU   B 1 26  ? 51.952 -24.993 -11.523 1.00 17.06 ?  26  GLU   B H    1 
ATOM   4378 H HA   . GLU   B 1 26  ? 51.165 -24.195 -13.872 1.00 17.63 ?  26  GLU   B HA   1 
ATOM   4379 H HB2  . GLU   B 1 26  ? 49.818 -24.705 -11.485 1.00 19.74 ?  26  GLU   B HB2  1 
ATOM   4380 H HB3  . GLU   B 1 26  ? 49.032 -23.881 -12.589 1.00 19.74 ?  26  GLU   B HB3  1 
ATOM   4381 H HG2  . GLU   B 1 26  ? 50.026 -26.470 -12.974 1.00 24.51 ?  26  GLU   B HG2  1 
ATOM   4382 H HG3  . GLU   B 1 26  ? 48.497 -26.130 -12.704 1.00 24.51 ?  26  GLU   B HG3  1 
ATOM   4383 N N    . ALA   B 1 27  ? 51.150 -21.871 -11.664 1.00 13.14 ?  27  ALA   B N    1 
ATOM   4384 C CA   . ALA   B 1 27  ? 51.098 -20.422 -11.531 1.00 13.52 ?  27  ALA   B CA   1 
ATOM   4385 C C    . ALA   B 1 27  ? 52.164 -19.759 -12.395 1.00 14.03 ?  27  ALA   B C    1 
ATOM   4386 O O    . ALA   B 1 27  ? 51.895 -18.767 -13.092 1.00 15.09 ?  27  ALA   B O    1 
ATOM   4387 C CB   . ALA   B 1 27  ? 51.238 -20.025 -10.061 1.00 13.73 ?  27  ALA   B CB   1 
ATOM   4388 H H    . ALA   B 1 27  ? 51.266 -22.305 -10.923 1.00 15.74 ?  27  ALA   B H    1 
ATOM   4389 H HA   . ALA   B 1 27  ? 50.236 -20.112 -11.837 1.00 16.20 ?  27  ALA   B HA   1 
ATOM   4390 H HB1  . ALA   B 1 27  ? 51.192 -19.058 -9.989  1.00 16.45 ?  27  ALA   B HB1  1 
ATOM   4391 H HB2  . ALA   B 1 27  ? 50.509 -20.424 -9.554  1.00 16.45 ?  27  ALA   B HB2  1 
ATOM   4392 H HB3  . ALA   B 1 27  ? 52.087 -20.343 -9.721  1.00 16.45 ?  27  ALA   B HB3  1 
ATOM   4393 N N    . LYS   B 1 28  ? 53.380 -20.301 -12.379 1.00 15.28 ?  28  LYS   B N    1 
ATOM   4394 C CA   . LYS   B 1 28  ? 54.452 -19.686 -13.153 1.00 17.29 ?  28  LYS   B CA   1 
ATOM   4395 C C    . LYS   B 1 28  ? 54.193 -19.774 -14.653 1.00 17.27 ?  28  LYS   B C    1 
ATOM   4396 O O    . LYS   B 1 28  ? 54.577 -18.864 -15.398 1.00 18.60 ?  28  LYS   B O    1 
ATOM   4397 C CB   . LYS   B 1 28  ? 55.810 -20.280 -12.758 1.00 20.80 ?  28  LYS   B CB   1 
ATOM   4398 C CG   . LYS   B 1 28  ? 56.202 -19.945 -11.319 1.00 24.63 ?  28  LYS   B CG   1 
ATOM   4399 C CD   . LYS   B 1 28  ? 57.625 -20.354 -10.969 1.00 30.08 ?  28  LYS   B CD   1 
ATOM   4400 C CE   . LYS   B 1 28  ? 57.751 -21.842 -10.763 1.00 34.35 ?  28  LYS   B CE   1 
ATOM   4401 N NZ   . LYS   B 1 28  ? 59.097 -22.196 -10.224 1.00 37.14 ?  28  LYS   B NZ   1 
ATOM   4402 H H    . LYS   B 1 28  ? 53.609 -21.003 -11.934 1.00 18.31 ?  28  LYS   B H    1 
ATOM   4403 H HA   . LYS   B 1 28  ? 54.487 -18.745 -12.930 1.00 20.73 ?  28  LYS   B HA   1 
ATOM   4404 H HB2  . LYS   B 1 28  ? 55.779 -21.246 -12.836 1.00 24.94 ?  28  LYS   B HB2  1 
ATOM   4405 H HB3  . LYS   B 1 28  ? 56.502 -19.923 -13.341 1.00 24.94 ?  28  LYS   B HB3  1 
ATOM   4406 H HG2  . LYS   B 1 28  ? 56.125 -18.985 -11.192 1.00 29.54 ?  28  LYS   B HG2  1 
ATOM   4407 H HG3  . LYS   B 1 28  ? 55.600 -20.407 -10.717 1.00 29.54 ?  28  LYS   B HG3  1 
ATOM   4408 H HD2  . LYS   B 1 28  ? 58.216 -20.094 -11.694 1.00 36.07 ?  28  LYS   B HD2  1 
ATOM   4409 H HD3  . LYS   B 1 28  ? 57.888 -19.907 -10.149 1.00 36.07 ?  28  LYS   B HD3  1 
ATOM   4410 H HE2  . LYS   B 1 28  ? 57.080 -22.137 -10.126 1.00 41.20 ?  28  LYS   B HE2  1 
ATOM   4411 H HE3  . LYS   B 1 28  ? 57.632 -22.297 -11.611 1.00 41.20 ?  28  LYS   B HE3  1 
ATOM   4412 H HZ1  . LYS   B 1 28  ? 59.157 -23.075 -10.107 1.00 44.55 ?  28  LYS   B HZ1  1 
ATOM   4413 H HZ2  . LYS   B 1 28  ? 59.729 -21.935 -10.794 1.00 44.55 ?  28  LYS   B HZ2  1 
ATOM   4414 H HZ3  . LYS   B 1 28  ? 59.228 -21.790 -9.443  1.00 44.55 ?  28  LYS   B HZ3  1 
ATOM   4415 N N    . LYS   B 1 29  ? 53.522 -20.836 -15.108 1.00 18.16 ?  29  LYS   B N    1 
ATOM   4416 C CA   . LYS   B 1 29  ? 53.245 -21.007 -16.534 1.00 20.92 ?  29  LYS   B CA   1 
ATOM   4417 C C    . LYS   B 1 29  ? 51.995 -20.254 -16.988 1.00 19.53 ?  29  LYS   B C    1 
ATOM   4418 O O    . LYS   B 1 29  ? 51.983 -19.674 -18.080 1.00 21.22 ?  29  LYS   B O    1 
ATOM   4419 C CB   . LYS   B 1 29  ? 53.097 -22.494 -16.858 1.00 26.05 ?  29  LYS   B CB   1 
ATOM   4420 C CG   . LYS   B 1 29  ? 52.909 -22.778 -18.339 1.00 31.07 ?  29  LYS   B CG   1 
ATOM   4421 C CD   . LYS   B 1 29  ? 53.131 -24.248 -18.666 1.00 35.04 ?  29  LYS   B CD   1 
ATOM   4422 C CE   . LYS   B 1 29  ? 52.035 -25.128 -18.091 1.00 37.82 ?  29  LYS   B CE   1 
ATOM   4423 N NZ   . LYS   B 1 29  ? 52.294 -26.574 -18.348 1.00 39.31 ?  29  LYS   B NZ   1 
ATOM   4424 H H    . LYS   B 1 29  ? 53.222 -21.471 -14.608 1.00 21.77 ?  29  LYS   B H    1 
ATOM   4425 H HA   . LYS   B 1 29  ? 53.995 -20.666 -17.037 1.00 25.08 ?  29  LYS   B HA   1 
ATOM   4426 H HB2  . LYS   B 1 29  ? 53.897 -22.959 -16.566 1.00 31.23 ?  29  LYS   B HB2  1 
ATOM   4427 H HB3  . LYS   B 1 29  ? 52.323 -22.843 -16.388 1.00 31.23 ?  29  LYS   B HB3  1 
ATOM   4428 H HG2  . LYS   B 1 29  ? 52.003 -22.545 -18.596 1.00 37.26 ?  29  LYS   B HG2  1 
ATOM   4429 H HG3  . LYS   B 1 29  ? 53.547 -22.254 -18.848 1.00 37.26 ?  29  LYS   B HG3  1 
ATOM   4430 H HD2  . LYS   B 1 29  ? 53.139 -24.364 -19.629 1.00 42.03 ?  29  LYS   B HD2  1 
ATOM   4431 H HD3  . LYS   B 1 29  ? 53.978 -24.536 -18.288 1.00 42.03 ?  29  LYS   B HD3  1 
ATOM   4432 H HE2  . LYS   B 1 29  ? 51.985 -24.995 -17.132 1.00 45.36 ?  29  LYS   B HE2  1 
ATOM   4433 H HE3  . LYS   B 1 29  ? 51.189 -24.893 -18.506 1.00 45.36 ?  29  LYS   B HE3  1 
ATOM   4434 H HZ1  . LYS   B 1 29  ? 51.638 -27.067 -18.003 1.00 47.14 ?  29  LYS   B HZ1  1 
ATOM   4435 H HZ2  . LYS   B 1 29  ? 52.338 -26.726 -19.224 1.00 47.14 ?  29  LYS   B HZ2  1 
ATOM   4436 H HZ3  . LYS   B 1 29  ? 53.065 -26.816 -17.974 1.00 47.14 ?  29  LYS   B HZ3  1 
ATOM   4437 N N    . VAL   B 1 30  ? 50.928 -20.287 -16.185 1.00 17.56 ?  30  VAL   B N    1 
ATOM   4438 C CA   . VAL   B 1 30  ? 49.637 -19.716 -16.578 1.00 17.85 ?  30  VAL   B CA   1 
ATOM   4439 C C    . VAL   B 1 30  ? 49.621 -18.206 -16.439 1.00 16.45 ?  30  VAL   B C    1 
ATOM   4440 O O    . VAL   B 1 30  ? 48.873 -17.515 -17.148 1.00 17.41 ?  30  VAL   B O    1 
ATOM   4441 C CB   . VAL   B 1 30  ? 48.541 -20.324 -15.682 1.00 20.28 ?  30  VAL   B CB   1 
ATOM   4442 C CG1  . VAL   B 1 30  ? 47.249 -19.526 -15.768 1.00 21.74 ?  30  VAL   B CG1  1 
ATOM   4443 C CG2  . VAL   B 1 30  ? 48.317 -21.796 -16.027 1.00 21.35 ?  30  VAL   B CG2  1 
ATOM   4444 H H    . VAL   B 1 30  ? 50.918 -20.660 -15.403 1.00 21.05 ?  30  VAL   B H    1 
ATOM   4445 H HA   . VAL   B 1 30  ? 49.442 -19.959 -17.498 1.00 21.40 ?  30  VAL   B HA   1 
ATOM   4446 H HB   . VAL   B 1 30  ? 48.840 -20.296 -14.759 1.00 24.31 ?  30  VAL   B HB   1 
ATOM   4447 H HG11 . VAL   B 1 30  ? 46.513 -20.109 -15.525 1.00 26.07 ?  30  VAL   B HG11 1 
ATOM   4448 H HG12 . VAL   B 1 30  ? 47.292 -18.781 -15.152 1.00 26.07 ?  30  VAL   B HG12 1 
ATOM   4449 H HG13 . VAL   B 1 30  ? 47.125 -19.217 -16.674 1.00 26.07 ?  30  VAL   B HG13 1 
ATOM   4450 H HG21 . VAL   B 1 30  ? 47.630 -22.164 -15.440 1.00 25.60 ?  30  VAL   B HG21 1 
ATOM   4451 H HG22 . VAL   B 1 30  ? 48.023 -21.867 -16.951 1.00 25.60 ?  30  VAL   B HG22 1 
ATOM   4452 H HG23 . VAL   B 1 30  ? 49.144 -22.286 -15.905 1.00 25.60 ?  30  VAL   B HG23 1 
ATOM   4453 N N    A LYS   B 1 31  ? 50.410 -17.672 -15.516 0.58 16.21 ?  31  LYS   B N    1 
ATOM   4454 N N    B LYS   B 1 31  ? 50.430 -17.681 -15.527 0.42 16.49 ?  31  LYS   B N    1 
ATOM   4455 C CA   A LYS   B 1 31  ? 50.437 -16.251 -15.185 0.58 16.38 ?  31  LYS   B CA   1 
ATOM   4456 C CA   B LYS   B 1 31  ? 50.437 -16.265 -15.182 0.42 16.82 ?  31  LYS   B CA   1 
ATOM   4457 C C    A LYS   B 1 31  ? 49.044 -15.759 -14.789 0.58 14.74 ?  31  LYS   B C    1 
ATOM   4458 C C    B LYS   B 1 31  ? 49.042 -15.768 -14.792 0.42 15.09 ?  31  LYS   B C    1 
ATOM   4459 O O    A LYS   B 1 31  ? 48.502 -14.841 -15.418 0.58 15.36 ?  31  LYS   B O    1 
ATOM   4460 O O    B LYS   B 1 31  ? 48.494 -14.867 -15.438 0.42 15.50 ?  31  LYS   B O    1 
ATOM   4461 C CB   A LYS   B 1 31  ? 51.065 -15.450 -16.332 0.58 18.64 ?  31  LYS   B CB   1 
ATOM   4462 C CB   B LYS   B 1 31  ? 51.044 -15.428 -16.299 0.42 19.10 ?  31  LYS   B CB   1 
ATOM   4463 C CG   A LYS   B 1 31  ? 52.522 -15.835 -16.609 0.58 21.37 ?  31  LYS   B CG   1 
ATOM   4464 C CG   B LYS   B 1 31  ? 52.484 -15.841 -16.608 0.42 21.42 ?  31  LYS   B CG   1 
ATOM   4465 C CD   A LYS   B 1 31  ? 53.141 -14.986 -17.704 0.58 24.33 ?  31  LYS   B CD   1 
ATOM   4466 C CD   B LYS   B 1 31  ? 53.072 -15.081 -17.779 0.42 23.66 ?  31  LYS   B CD   1 
ATOM   4467 C CE   A LYS   B 1 31  ? 54.629 -15.251 -17.830 0.58 26.62 ?  31  LYS   B CE   1 
ATOM   4468 C CE   B LYS   B 1 31  ? 54.575 -15.290 -17.864 0.42 25.42 ?  31  LYS   B CE   1 
ATOM   4469 N NZ   A LYS   B 1 31  ? 55.356 -14.886 -16.581 0.58 27.80 ?  31  LYS   B NZ   1 
ATOM   4470 N NZ   B LYS   B 1 31  ? 55.273 -14.787 -16.644 0.42 26.24 ?  31  LYS   B NZ   1 
ATOM   4471 H H    A LYS   B 1 31  ? 50.971 -18.140 -15.057 0.58 19.43 ?  31  LYS   B H    1 
ATOM   4472 H H    B LYS   B 1 31  ? 51.009 -18.145 -15.089 0.42 19.76 ?  31  LYS   B H    1 
ATOM   4473 H HA   A LYS   B 1 31  ? 51.006 -16.143 -14.414 0.58 19.63 ?  31  LYS   B HA   1 
ATOM   4474 H HA   B LYS   B 1 31  ? 51.002 -16.159 -14.409 0.42 20.16 ?  31  LYS   B HA   1 
ATOM   4475 H HB2  A LYS   B 1 31  ? 50.558 -15.602 -17.144 0.58 22.34 ?  31  LYS   B HB2  1 
ATOM   4476 H HB2  B LYS   B 1 31  ? 50.521 -15.537 -17.106 0.42 22.89 ?  31  LYS   B HB2  1 
ATOM   4477 H HB3  A LYS   B 1 31  ? 51.046 -14.510 -16.099 0.58 22.34 ?  31  LYS   B HB3  1 
ATOM   4478 H HB3  B LYS   B 1 31  ? 51.051 -14.497 -16.025 0.42 22.89 ?  31  LYS   B HB3  1 
ATOM   4479 H HG2  A LYS   B 1 31  ? 53.040 -15.714 -15.798 0.58 25.62 ?  31  LYS   B HG2  1 
ATOM   4480 H HG2  B LYS   B 1 31  ? 53.034 -15.671 -15.827 0.42 25.68 ?  31  LYS   B HG2  1 
ATOM   4481 H HG3  A LYS   B 1 31  ? 52.557 -16.763 -16.891 0.58 25.62 ?  31  LYS   B HG3  1 
ATOM   4482 H HG3  B LYS   B 1 31  ? 52.503 -16.787 -16.826 0.42 25.68 ?  31  LYS   B HG3  1 
ATOM   4483 H HD2  A LYS   B 1 31  ? 52.719 -15.199 -18.550 0.58 29.17 ?  31  LYS   B HD2  1 
ATOM   4484 H HD2  B LYS   B 1 31  ? 52.672 -15.403 -18.602 0.42 28.37 ?  31  LYS   B HD2  1 
ATOM   4485 H HD3  A LYS   B 1 31  ? 53.014 -14.049 -17.489 0.58 29.17 ?  31  LYS   B HD3  1 
ATOM   4486 H HD3  B LYS   B 1 31  ? 52.900 -14.135 -17.665 0.42 28.37 ?  31  LYS   B HD3  1 
ATOM   4487 H HE2  A LYS   B 1 31  ? 54.774 -16.196 -18.001 0.58 31.92 ?  31  LYS   B HE2  1 
ATOM   4488 H HE2  B LYS   B 1 31  ? 54.764 -16.239 -17.952 0.42 30.48 ?  31  LYS   B HE2  1 
ATOM   4489 H HE3  A LYS   B 1 31  ? 54.989 -14.720 -18.557 0.58 31.92 ?  31  LYS   B HE3  1 
ATOM   4490 H HE3  B LYS   B 1 31  ? 54.923 -14.808 -18.631 0.42 30.48 ?  31  LYS   B HE3  1 
ATOM   4491 H HZ1  A LYS   B 1 31  ? 56.234 -14.961 -16.706 0.58 33.34 ?  31  LYS   B HZ1  1 
ATOM   4492 H HZ1  B LYS   B 1 31  ? 56.154 -14.799 -16.768 0.42 31.47 ?  31  LYS   B HZ1  1 
ATOM   4493 H HZ2  A LYS   B 1 31  ? 55.166 -14.048 -16.353 0.58 33.34 ?  31  LYS   B HZ2  1 
ATOM   4494 H HZ2  B LYS   B 1 31  ? 55.016 -13.954 -16.468 0.42 31.47 ?  31  LYS   B HZ2  1 
ATOM   4495 H HZ3  A LYS   B 1 31  ? 55.113 -15.428 -15.917 0.58 33.34 ?  31  LYS   B HZ3  1 
ATOM   4496 H HZ3  B LYS   B 1 31  ? 55.075 -15.303 -15.944 0.42 31.47 ?  31  LYS   B HZ3  1 
ATOM   4497 N N    . PRO   B 1 32  ? 48.453 -16.326 -13.733 1.00 13.99 ?  32  PRO   B N    1 
ATOM   4498 C CA   . PRO   B 1 32  ? 47.079 -15.963 -13.362 1.00 13.67 ?  32  PRO   B CA   1 
ATOM   4499 C C    . PRO   B 1 32  ? 47.009 -14.620 -12.652 1.00 13.70 ?  32  PRO   B C    1 
ATOM   4500 O O    . PRO   B 1 32  ? 47.941 -14.202 -11.958 1.00 14.73 ?  32  PRO   B O    1 
ATOM   4501 C CB   . PRO   B 1 32  ? 46.689 -17.077 -12.383 1.00 13.77 ?  32  PRO   B CB   1 
ATOM   4502 C CG   . PRO   B 1 32  ? 48.004 -17.411 -11.706 1.00 13.75 ?  32  PRO   B CG   1 
ATOM   4503 C CD   . PRO   B 1 32  ? 49.050 -17.286 -12.781 1.00 14.27 ?  32  PRO   B CD   1 
ATOM   4504 H HA   . PRO   B 1 32  ? 46.491 -15.976 -14.140 1.00 16.38 ?  32  PRO   B HA   1 
ATOM   4505 H HB2  . PRO   B 1 32  ? 46.039 -16.741 -11.743 1.00 16.50 ?  32  PRO   B HB2  1 
ATOM   4506 H HB3  . PRO   B 1 32  ? 46.339 -17.841 -12.866 1.00 16.50 ?  32  PRO   B HB3  1 
ATOM   4507 H HG2  . PRO   B 1 32  ? 48.174 -16.776 -10.988 1.00 16.48 ?  32  PRO   B HG2  1 
ATOM   4508 H HG3  . PRO   B 1 32  ? 47.976 -18.316 -11.359 1.00 16.48 ?  32  PRO   B HG3  1 
ATOM   4509 H HD2  . PRO   B 1 32  ? 49.867 -16.924 -12.408 1.00 17.11 ?  32  PRO   B HD2  1 
ATOM   4510 H HD3  . PRO   B 1 32  ? 49.193 -18.141 -13.203 1.00 17.11 ?  32  PRO   B HD3  1 
ATOM   4511 N N    . THR   B 1 33  ? 45.859 -13.954 -12.812 1.00 13.23 ?  33  THR   B N    1 
ATOM   4512 C CA   . THR   B 1 33  ? 45.578 -12.780 -11.992 1.00 13.18 ?  33  THR   B CA   1 
ATOM   4513 C C    . THR   B 1 33  ? 45.535 -13.141 -10.513 1.00 13.03 ?  33  THR   B C    1 
ATOM   4514 O O    . THR   B 1 33  ? 46.014 -12.373 -9.667  1.00 14.22 ?  33  THR   B O    1 
ATOM   4515 C CB   . THR   B 1 33  ? 44.256 -12.138 -12.423 1.00 13.89 ?  33  THR   B CB   1 
ATOM   4516 O OG1  . THR   B 1 33  ? 44.273 -11.886 -13.832 1.00 13.96 ?  33  THR   B OG1  1 
ATOM   4517 C CG2  . THR   B 1 33  ? 44.029 -10.833 -11.677 1.00 15.27 ?  33  THR   B CG2  1 
ATOM   4518 H H    . THR   B 1 33  ? 45.239 -14.164 -13.379 1.00 15.86 ?  33  THR   B H    1 
ATOM   4519 H HA   . THR   B 1 33  ? 46.283 -12.132 -12.133 1.00 15.80 ?  33  THR   B HA   1 
ATOM   4520 H HB   . THR   B 1 33  ? 43.522 -12.744 -12.223 1.00 16.64 ?  33  THR   B HB   1 
ATOM   4521 H HG1  . THR   B 1 33  ? 43.552 -11.519 -14.073 1.00 16.73 ?  33  THR   B HG1  1 
ATOM   4522 H HG21 . THR   B 1 33  ? 43.271 -10.367 -12.052 1.00 18.30 ?  33  THR   B HG21 1 
ATOM   4523 H HG22 . THR   B 1 33  ? 43.859 -11.018 -10.740 1.00 18.30 ?  33  THR   B HG22 1 
ATOM   4524 H HG23 . THR   B 1 33  ? 44.818 -10.274 -11.751 1.00 18.30 ?  33  THR   B HG23 1 
ATOM   4525 N N    . VAL   B 1 34  ? 44.969 -14.304 -10.176 1.00 12.33 ?  34  VAL   B N    1 
ATOM   4526 C CA   . VAL   B 1 34  ? 44.762 -14.692 -8.784  1.00 11.91 ?  34  VAL   B CA   1 
ATOM   4527 C C    . VAL   B 1 34  ? 45.174 -16.143 -8.606  1.00 11.05 ?  34  VAL   B C    1 
ATOM   4528 O O    . VAL   B 1 34  ? 44.656 -17.028 -9.298  1.00 12.01 ?  34  VAL   B O    1 
ATOM   4529 C CB   . VAL   B 1 34  ? 43.284 -14.535 -8.363  1.00 13.22 ?  34  VAL   B CB   1 
ATOM   4530 C CG1  . VAL   B 1 34  ? 43.081 -14.988 -6.925  1.00 14.02 ?  34  VAL   B CG1  1 
ATOM   4531 C CG2  . VAL   B 1 34  ? 42.806 -13.106 -8.557  1.00 14.46 ?  34  VAL   B CG2  1 
ATOM   4532 H H    . VAL   B 1 34  ? 44.706 -14.895 -10.747 1.00 14.77 ?  34  VAL   B H    1 
ATOM   4533 H HA   . VAL   B 1 34  ? 45.315 -14.144 -8.208  1.00 14.27 ?  34  VAL   B HA   1 
ATOM   4534 H HB   . VAL   B 1 34  ? 42.743 -15.102 -8.935  1.00 15.84 ?  34  VAL   B HB   1 
ATOM   4535 H HG11 . VAL   B 1 34  ? 42.217 -14.671 -6.617  1.00 16.81 ?  34  VAL   B HG11 1 
ATOM   4536 H HG12 . VAL   B 1 34  ? 43.105 -15.958 -6.891  1.00 16.81 ?  34  VAL   B HG12 1 
ATOM   4537 H HG13 . VAL   B 1 34  ? 43.785 -14.617 -6.374  1.00 16.81 ?  34  VAL   B HG13 1 
ATOM   4538 H HG21 . VAL   B 1 34  ? 41.884 -13.038 -8.266  1.00 17.33 ?  34  VAL   B HG21 1 
ATOM   4539 H HG22 . VAL   B 1 34  ? 43.365 -12.509 -8.036  1.00 17.33 ?  34  VAL   B HG22 1 
ATOM   4540 H HG23 . VAL   B 1 34  ? 42.869 -12.872 -9.501  1.00 17.33 ?  34  VAL   B HG23 1 
ATOM   4541 N N    . VAL   B 1 35  ? 46.057 -16.399 -7.642  1.00 10.52 ?  35  VAL   B N    1 
ATOM   4542 C CA   . VAL   B 1 35  ? 46.282 -17.746 -7.125  1.00 10.59 ?  35  VAL   B CA   1 
ATOM   4543 C C    . VAL   B 1 35  ? 45.740 -17.793 -5.708  1.00 10.29 ?  35  VAL   B C    1 
ATOM   4544 O O    . VAL   B 1 35  ? 45.951 -16.865 -4.923  1.00 10.54 ?  35  VAL   B O    1 
ATOM   4545 C CB   . VAL   B 1 35  ? 47.768 -18.172 -7.189  1.00 11.41 ?  35  VAL   B CB   1 
ATOM   4546 C CG1  . VAL   B 1 35  ? 48.660 -17.322 -6.270  1.00 12.44 ?  35  VAL   B CG1  1 
ATOM   4547 C CG2  . VAL   B 1 35  ? 47.909 -19.665 -6.867  1.00 12.15 ?  35  VAL   B CG2  1 
ATOM   4548 H H    . VAL   B 1 35  ? 46.544 -15.796 -7.267  1.00 12.60 ?  35  VAL   B H    1 
ATOM   4549 H HA   . VAL   B 1 35  ? 45.773 -18.374 -7.653  1.00 12.69 ?  35  VAL   B HA   1 
ATOM   4550 H HB   . VAL   B 1 35  ? 48.082 -18.047 -8.099  1.00 13.67 ?  35  VAL   B HB   1 
ATOM   4551 H HG11 . VAL   B 1 35  ? 49.586 -17.548 -6.443  1.00 14.90 ?  35  VAL   B HG11 1 
ATOM   4552 H HG12 . VAL   B 1 35  ? 48.500 -16.389 -6.460  1.00 14.90 ?  35  VAL   B HG12 1 
ATOM   4553 H HG13 . VAL   B 1 35  ? 48.435 -17.522 -5.348  1.00 14.90 ?  35  VAL   B HG13 1 
ATOM   4554 H HG21 . VAL   B 1 35  ? 48.836 -19.930 -6.962  1.00 14.55 ?  35  VAL   B HG21 1 
ATOM   4555 H HG22 . VAL   B 1 35  ? 47.615 -19.824 -5.951  1.00 14.55 ?  35  VAL   B HG22 1 
ATOM   4556 H HG23 . VAL   B 1 35  ? 47.354 -20.181 -7.478  1.00 14.55 ?  35  VAL   B HG23 1 
ATOM   4557 N N    . VAL   B 1 36  ? 45.026 -18.873 -5.385  1.00 10.37 ?  36  VAL   B N    1 
ATOM   4558 C CA   . VAL   B 1 36  ? 44.477 -19.073 -4.058  1.00 9.90  ?  36  VAL   B CA   1 
ATOM   4559 C C    . VAL   B 1 36  ? 45.478 -19.833 -3.197  1.00 9.89  ?  36  VAL   B C    1 
ATOM   4560 O O    . VAL   B 1 36  ? 46.024 -20.870 -3.616  1.00 10.85 ?  36  VAL   B O    1 
ATOM   4561 C CB   . VAL   B 1 36  ? 43.140 -19.834 -4.132  1.00 10.50 ?  36  VAL   B CB   1 
ATOM   4562 C CG1  . VAL   B 1 36  ? 42.636 -20.188 -2.739  1.00 11.27 ?  36  VAL   B CG1  1 
ATOM   4563 C CG2  . VAL   B 1 36  ? 42.112 -19.010 -4.879  1.00 11.19 ?  36  VAL   B CG2  1 
ATOM   4564 H H    . VAL   B 1 36  ? 44.852 -19.514 -5.935  1.00 12.42 ?  36  VAL   B H    1 
ATOM   4565 H HA   . VAL   B 1 36  ? 44.310 -18.213 -3.644  1.00 11.85 ?  36  VAL   B HA   1 
ATOM   4566 H HB   . VAL   B 1 36  ? 43.269 -20.659 -4.622  1.00 12.58 ?  36  VAL   B HB   1 
ATOM   4567 H HG11 . VAL   B 1 36  ? 41.694 -20.417 -2.788  1.00 13.50 ?  36  VAL   B HG11 1 
ATOM   4568 H HG12 . VAL   B 1 36  ? 43.140 -20.942 -2.397  1.00 13.50 ?  36  VAL   B HG12 1 
ATOM   4569 H HG13 . VAL   B 1 36  ? 42.753 -19.418 -2.154  1.00 13.50 ?  36  VAL   B HG13 1 
ATOM   4570 H HG21 . VAL   B 1 36  ? 41.271 -19.491 -4.898  1.00 13.40 ?  36  VAL   B HG21 1 
ATOM   4571 H HG22 . VAL   B 1 36  ? 41.997 -18.159 -4.425  1.00 13.40 ?  36  VAL   B HG22 1 
ATOM   4572 H HG23 . VAL   B 1 36  ? 42.426 -18.858 -5.785  1.00 13.40 ?  36  VAL   B HG23 1 
ATOM   4573 N N    . ASN   B 1 37  ? 45.688 -19.340 -1.982  1.00 9.98  ?  37  ASN   B N    1 
ATOM   4574 C CA   . ASN   B 1 37  ? 46.431 -20.059 -0.962  1.00 10.27 ?  37  ASN   B CA   1 
ATOM   4575 C C    . ASN   B 1 37  ? 45.478 -20.737 0.013   1.00 10.67 ?  37  ASN   B C    1 
ATOM   4576 O O    . ASN   B 1 37  ? 44.471 -20.159 0.424   1.00 11.04 ?  37  ASN   B O    1 
ATOM   4577 C CB   . ASN   B 1 37  ? 47.358 -19.112 -0.194  1.00 10.32 ?  37  ASN   B CB   1 
ATOM   4578 C CG   . ASN   B 1 37  ? 48.205 -19.830 0.821   1.00 10.84 ?  37  ASN   B CG   1 
ATOM   4579 O OD1  . ASN   B 1 37  ? 48.553 -21.007 0.643   1.00 11.60 ?  37  ASN   B OD1  1 
ATOM   4580 N ND2  . ASN   B 1 37  ? 48.549 -19.137 1.899   1.00 11.04 ?  37  ASN   B ND2  1 
ATOM   4581 H H    . ASN   B 1 37  ? 45.397 -18.570 -1.713  1.00 11.95 ?  37  ASN   B H    1 
ATOM   4582 H HA   . ASN   B 1 37  ? 46.972 -20.745 -1.373  1.00 12.31 ?  37  ASN   B HA   1 
ATOM   4583 H HB2  . ASN   B 1 37  ? 47.954 -18.676 -0.819  1.00 12.37 ?  37  ASN   B HB2  1 
ATOM   4584 H HB3  . ASN   B 1 37  ? 46.827 -18.452 0.279   1.00 12.37 ?  37  ASN   B HB3  1 
ATOM   4585 H HD21 . ASN   B 1 37  ? 49.043 -19.498 2.509   1.00 13.23 ?  37  ASN   B HD21 1 
ATOM   4586 H HD22 . ASN   B 1 37  ? 48.298 -18.324 1.993   1.00 13.23 ?  37  ASN   B HD22 1 
ATOM   4587 N N    . ALA   B 1 38  ? 45.829 -21.970 0.391   1.00 10.97 ?  38  ALA   B N    1 
ATOM   4588 C CA   . ALA   B 1 38  ? 45.174 -22.711 1.473   1.00 11.07 ?  38  ALA   B CA   1 
ATOM   4589 C C    . ALA   B 1 38  ? 45.763 -22.231 2.800   1.00 11.13 ?  38  ALA   B C    1 
ATOM   4590 O O    . ALA   B 1 38  ? 46.661 -22.843 3.388   1.00 12.06 ?  38  ALA   B O    1 
ATOM   4591 C CB   . ALA   B 1 38  ? 45.393 -24.206 1.284   1.00 12.46 ?  38  ALA   B CB   1 
ATOM   4592 H H    . ALA   B 1 38  ? 46.475 -22.407 0.034   1.00 13.14 ?  38  ALA   B H    1 
ATOM   4593 H HA   . ALA   B 1 38  ? 44.220 -22.531 1.468   1.00 13.26 ?  38  ALA   B HA   1 
ATOM   4594 H HB1  . ALA   B 1 38  ? 44.947 -24.685 2.009   1.00 14.93 ?  38  ALA   B HB1  1 
ATOM   4595 H HB2  . ALA   B 1 38  ? 45.012 -24.478 0.435   1.00 14.93 ?  38  ALA   B HB2  1 
ATOM   4596 H HB3  . ALA   B 1 38  ? 46.340 -24.395 1.303   1.00 14.93 ?  38  ALA   B HB3  1 
ATOM   4597 N N    . ALA   B 1 39  ? 45.242 -21.093 3.267   1.00 10.93 ?  39  ALA   B N    1 
ATOM   4598 C CA   . ALA   B 1 39  ? 45.782 -20.368 4.405   1.00 11.21 ?  39  ALA   B CA   1 
ATOM   4599 C C    . ALA   B 1 39  ? 45.163 -20.817 5.727   1.00 10.78 ?  39  ALA   B C    1 
ATOM   4600 O O    . ALA   B 1 39  ? 44.128 -21.487 5.774   1.00 12.52 ?  39  ALA   B O    1 
ATOM   4601 C CB   . ALA   B 1 39  ? 45.557 -18.863 4.214   1.00 11.78 ?  39  ALA   B CB   1 
ATOM   4602 H H    . ALA   B 1 39  ? 44.551 -20.714 2.919   1.00 13.09 ?  39  ALA   B H    1 
ATOM   4603 H HA   . ALA   B 1 39  ? 46.737 -20.521 4.450   1.00 13.43 ?  39  ALA   B HA   1 
ATOM   4604 H HB1  . ALA   B 1 39  ? 45.921 -18.390 4.976   1.00 14.11 ?  39  ALA   B HB1  1 
ATOM   4605 H HB2  . ALA   B 1 39  ? 46.004 -18.576 3.400   1.00 14.11 ?  39  ALA   B HB2  1 
ATOM   4606 H HB3  . ALA   B 1 39  ? 44.604 -18.692 4.141   1.00 14.11 ?  39  ALA   B HB3  1 
ATOM   4607 N N    . ASN   B 1 40  ? 45.807 -20.402 6.813   1.00 11.52 ?  40  ASN   B N    1 
ATOM   4608 C CA   . ASN   B 1 40  ? 45.243 -20.459 8.149   1.00 12.31 ?  40  ASN   B CA   1 
ATOM   4609 C C    . ASN   B 1 40  ? 45.058 -19.034 8.678   1.00 12.53 ?  40  ASN   B C    1 
ATOM   4610 O O    . ASN   B 1 40  ? 45.472 -18.049 8.054   1.00 12.42 ?  40  ASN   B O    1 
ATOM   4611 C CB   . ASN   B 1 40  ? 46.099 -21.336 9.080   1.00 13.35 ?  40  ASN   B CB   1 
ATOM   4612 C CG   . ASN   B 1 40  ? 47.553 -20.921 9.110   1.00 14.35 ?  40  ASN   B CG   1 
ATOM   4613 O OD1  . ASN   B 1 40  ? 47.871 -19.733 9.176   1.00 16.40 ?  40  ASN   B OD1  1 
ATOM   4614 N ND2  . ASN   B 1 40  ? 48.444 -21.893 9.066   1.00 14.70 ?  40  ASN   B ND2  1 
ATOM   4615 H H    . ASN   B 1 40  ? 46.606 -20.083 6.793   1.00 13.80 ?  40  ASN   B H    1 
ATOM   4616 H HA   . ASN   B 1 40  ? 44.360 -20.856 8.097   1.00 14.74 ?  40  ASN   B HA   1 
ATOM   4617 H HB2  . ASN   B 1 40  ? 45.741 -21.273 9.981   1.00 15.99 ?  40  ASN   B HB2  1 
ATOM   4618 H HB3  . ASN   B 1 40  ? 46.051 -22.252 8.769   1.00 15.99 ?  40  ASN   B HB3  1 
ATOM   4619 H HD21 . ASN   B 1 40  ? 49.281 -21.709 9.089   1.00 17.62 ?  40  ASN   B HD21 1 
ATOM   4620 H HD22 . ASN   B 1 40  ? 48.181 -22.711 9.018   1.00 17.62 ?  40  ASN   B HD22 1 
ATOM   4621 N N    . VAL   B 1 41  ? 44.396 -18.915 9.832   1.00 12.77 ?  41  VAL   B N    1 
ATOM   4622 C CA   . VAL   B 1 41  ? 43.931 -17.599 10.283  1.00 13.48 ?  41  VAL   B CA   1 
ATOM   4623 C C    . VAL   B 1 41  ? 45.077 -16.640 10.574  1.00 13.44 ?  41  VAL   B C    1 
ATOM   4624 O O    . VAL   B 1 41  ? 44.907 -15.419 10.460  1.00 13.82 ?  41  VAL   B O    1 
ATOM   4625 C CB   . VAL   B 1 41  ? 42.958 -17.688 11.478  1.00 15.24 ?  41  VAL   B CB   1 
ATOM   4626 C CG1  . VAL   B 1 41  ? 41.648 -18.358 11.070  1.00 15.53 ?  41  VAL   B CG1  1 
ATOM   4627 C CG2  . VAL   B 1 41  ? 43.614 -18.377 12.673  1.00 16.30 ?  41  VAL   B CG2  1 
ATOM   4628 H H    . VAL   B 1 41  ? 44.205 -19.562 10.356  1.00 15.29 ?  41  VAL   B H    1 
ATOM   4629 H HA   . VAL   B 1 41  ? 43.426 -17.202 9.558   1.00 16.15 ?  41  VAL   B HA   1 
ATOM   4630 H HB   . VAL   B 1 41  ? 42.736 -16.784 11.759  1.00 18.26 ?  41  VAL   B HB   1 
ATOM   4631 H HG11 . VAL   B 1 41  ? 41.043 -18.360 11.830  1.00 18.61 ?  41  VAL   B HG11 1 
ATOM   4632 H HG12 . VAL   B 1 41  ? 41.254 -17.861 10.336  1.00 18.61 ?  41  VAL   B HG12 1 
ATOM   4633 H HG13 . VAL   B 1 41  ? 41.834 -19.268 10.793  1.00 18.61 ?  41  VAL   B HG13 1 
ATOM   4634 H HG21 . VAL   B 1 41  ? 42.977 -18.416 13.405  1.00 19.54 ?  41  VAL   B HG21 1 
ATOM   4635 H HG22 . VAL   B 1 41  ? 43.870 -19.279 12.415  1.00 19.54 ?  41  VAL   B HG22 1 
ATOM   4636 H HG23 . VAL   B 1 41  ? 44.395 -17.875 12.941  1.00 19.54 ?  41  VAL   B HG23 1 
ATOM   4637 N N    A TYR   B 1 42  ? 46.243 -17.155 10.966  0.58 13.63 ?  42  TYR   B N    1 
ATOM   4638 N N    B TYR   B 1 42  ? 46.241 -17.156 10.963  0.42 13.52 ?  42  TYR   B N    1 
ATOM   4639 C CA   A TYR   B 1 42  ? 47.396 -16.310 11.246  0.58 13.67 ?  42  TYR   B CA   1 
ATOM   4640 C CA   B TYR   B 1 42  ? 47.391 -16.311 11.249  0.42 13.47 ?  42  TYR   B CA   1 
ATOM   4641 C C    A TYR   B 1 42  ? 48.363 -16.214 10.066  0.58 13.03 ?  42  TYR   B C    1 
ATOM   4642 C C    B TYR   B 1 42  ? 48.365 -16.223 10.073  0.42 12.98 ?  42  TYR   B C    1 
ATOM   4643 O O    A TYR   B 1 42  ? 49.442 -15.629 10.204  0.58 14.30 ?  42  TYR   B O    1 
ATOM   4644 O O    B TYR   B 1 42  ? 49.456 -15.664 10.222  0.42 13.91 ?  42  TYR   B O    1 
ATOM   4645 C CB   A TYR   B 1 42  ? 48.084 -16.736 12.550  0.58 15.10 ?  42  TYR   B CB   1 
ATOM   4646 C CB   B TYR   B 1 42  ? 48.076 -16.751 12.550  0.42 14.41 ?  42  TYR   B CB   1 
ATOM   4647 C CG   A TYR   B 1 42  ? 47.518 -16.025 13.775  0.58 14.78 ?  42  TYR   B CG   1 
ATOM   4648 C CG   B TYR   B 1 42  ? 47.590 -15.988 13.780  0.42 13.79 ?  42  TYR   B CG   1 
ATOM   4649 C CD1  A TYR   B 1 42  ? 47.749 -14.667 13.974  0.58 13.95 ?  42  TYR   B CD1  1 
ATOM   4650 C CD1  B TYR   B 1 42  ? 47.880 -14.639 13.931  0.42 13.35 ?  42  TYR   B CD1  1 
ATOM   4651 C CD2  A TYR   B 1 42  ? 46.754 -16.696 14.720  0.58 15.99 ?  42  TYR   B CD2  1 
ATOM   4652 C CD2  B TYR   B 1 42  ? 46.856 -16.609 14.788  0.42 13.95 ?  42  TYR   B CD2  1 
ATOM   4653 C CE1  A TYR   B 1 42  ? 47.244 -14.001 15.075  0.58 14.57 ?  42  TYR   B CE1  1 
ATOM   4654 C CE1  B TYR   B 1 42  ? 47.455 -13.926 15.036  0.42 13.25 ?  42  TYR   B CE1  1 
ATOM   4655 C CE2  A TYR   B 1 42  ? 46.246 -16.037 15.830  0.58 15.94 ?  42  TYR   B CE2  1 
ATOM   4656 C CE2  B TYR   B 1 42  ? 46.427 -15.898 15.911  0.42 13.58 ?  42  TYR   B CE2  1 
ATOM   4657 C CZ   A TYR   B 1 42  ? 46.494 -14.687 16.001  0.58 15.99 ?  42  TYR   B CZ   1 
ATOM   4658 C CZ   B TYR   B 1 42  ? 46.732 -14.551 16.026  0.42 13.31 ?  42  TYR   B CZ   1 
ATOM   4659 O OH   A TYR   B 1 42  ? 45.992 -14.014 17.098  0.58 18.52 ?  42  TYR   B OH   1 
ATOM   4660 O OH   B TYR   B 1 42  ? 46.333 -13.807 17.126  0.42 13.65 ?  42  TYR   B OH   1 
ATOM   4661 H H    A TYR   B 1 42  ? 46.389 -18.003 11.066  0.58 16.34 ?  42  TYR   B H    1 
ATOM   4662 H H    B TYR   B 1 42  ? 46.389 -18.003 11.059  0.42 16.19 ?  42  TYR   B H    1 
ATOM   4663 H HA   A TYR   B 1 42  ? 47.064 -15.418 11.396  0.58 16.38 ?  42  TYR   B HA   1 
ATOM   4664 H HA   B TYR   B 1 42  ? 47.060 -15.418 11.403  0.42 16.15 ?  42  TYR   B HA   1 
ATOM   4665 H HB2  A TYR   B 1 42  ? 47.963 -17.690 12.682  0.58 18.09 ?  42  TYR   B HB2  1 
ATOM   4666 H HB2  B TYR   B 1 42  ? 47.901 -17.692 12.699  0.42 17.27 ?  42  TYR   B HB2  1 
ATOM   4667 H HB3  A TYR   B 1 42  ? 49.028 -16.526 12.494  0.58 18.09 ?  42  TYR   B HB3  1 
ATOM   4668 H HB3  B TYR   B 1 42  ? 49.031 -16.601 12.466  0.42 17.27 ?  42  TYR   B HB3  1 
ATOM   4669 H HD1  A TYR   B 1 42  ? 48.260 -14.196 13.350  0.58 16.72 ?  42  TYR   B HD1  1 
ATOM   4670 H HD1  B TYR   B 1 42  ? 48.375 -14.202 13.272  0.42 16.00 ?  42  TYR   B HD1  1 
ATOM   4671 H HD2  A TYR   B 1 42  ? 46.585 -17.602 14.611  0.58 19.17 ?  42  TYR   B HD2  1 
ATOM   4672 H HD2  B TYR   B 1 42  ? 46.652 -17.513 14.712  0.42 16.71 ?  42  TYR   B HD2  1 
ATOM   4673 H HE1  A TYR   B 1 42  ? 47.417 -13.089 15.187  0.58 17.46 ?  42  TYR   B HE1  1 
ATOM   4674 H HE1  B TYR   B 1 42  ? 47.670 -13.021 15.119  0.42 15.88 ?  42  TYR   B HE1  1 
ATOM   4675 H HE2  A TYR   B 1 42  ? 45.736 -16.497 16.459  0.58 19.11 ?  42  TYR   B HE2  1 
ATOM   4676 H HE2  B TYR   B 1 42  ? 45.938 -16.325 16.579  0.42 16.27 ?  42  TYR   B HE2  1 
ATOM   4677 H HH   A TYR   B 1 42  ? 46.226 -13.205 17.075  0.58 22.20 ?  42  TYR   B HH   1 
ATOM   4678 H HH   B TYR   B 1 42  ? 45.897 -14.299 17.658  0.42 16.36 ?  42  TYR   B HH   1 
ATOM   4679 N N    . LEU   B 1 43  ? 47.977 -16.727 8.902   1.00 12.52 ?  43  LEU   B N    1 
ATOM   4680 C CA   . LEU   B 1 43  ? 48.798 -16.646 7.693   1.00 12.27 ?  43  LEU   B CA   1 
ATOM   4681 C C    . LEU   B 1 43  ? 50.212 -17.154 7.941   1.00 12.52 ?  43  LEU   B C    1 
ATOM   4682 O O    . LEU   B 1 43  ? 51.192 -16.559 7.486   1.00 13.33 ?  43  LEU   B O    1 
ATOM   4683 C CB   . LEU   B 1 43  ? 48.809 -15.240 7.086   1.00 12.45 ?  43  LEU   B CB   1 
ATOM   4684 C CG   . LEU   B 1 43  ? 47.448 -14.631 6.730   1.00 12.92 ?  43  LEU   B CG   1 
ATOM   4685 C CD1  . LEU   B 1 43  ? 47.646 -13.226 6.157   1.00 14.37 ?  43  LEU   B CD1  1 
ATOM   4686 C CD2  . LEU   B 1 43  ? 46.681 -15.503 5.754   1.00 13.11 ?  43  LEU   B CD2  1 
ATOM   4687 H H    A LEU   B 1 43  ? 47.234 -17.140 8.783   0.58 14.99 ?  43  LEU   B H    1 
ATOM   4688 H H    B LEU   B 1 43  ? 47.236 -17.143 8.782   0.42 14.99 ?  43  LEU   B H    1 
ATOM   4689 H HA   . LEU   B 1 43  ? 48.403 -17.233 7.030   1.00 14.70 ?  43  LEU   B HA   1 
ATOM   4690 H HB2  . LEU   B 1 43  ? 49.240 -14.641 7.715   1.00 14.92 ?  43  LEU   B HB2  1 
ATOM   4691 H HB3  . LEU   B 1 43  ? 49.330 -15.271 6.267   1.00 14.92 ?  43  LEU   B HB3  1 
ATOM   4692 H HG   . LEU   B 1 43  ? 46.924 -14.543 7.540   1.00 15.49 ?  43  LEU   B HG   1 
ATOM   4693 H HD11 . LEU   B 1 43  ? 46.776 -12.849 5.939   1.00 17.22 ?  43  LEU   B HD11 1 
ATOM   4694 H HD12 . LEU   B 1 43  ? 48.086 -12.668 6.820   1.00 17.22 ?  43  LEU   B HD12 1 
ATOM   4695 H HD13 . LEU   B 1 43  ? 48.190 -13.280 5.357   1.00 17.22 ?  43  LEU   B HD13 1 
ATOM   4696 H HD21 . LEU   B 1 43  ? 45.869 -15.037 5.489   1.00 15.71 ?  43  LEU   B HD21 1 
ATOM   4697 H HD22 . LEU   B 1 43  ? 47.232 -15.674 4.979   1.00 15.71 ?  43  LEU   B HD22 1 
ATOM   4698 H HD23 . LEU   B 1 43  ? 46.451 -16.336 6.194   1.00 15.71 ?  43  LEU   B HD23 1 
ATOM   4699 N N    . LYS   B 1 44  ? 50.314 -18.276 8.660   1.00 12.64 ?  44  LYS   B N    1 
ATOM   4700 C CA   . LYS   B 1 44  ? 51.580 -18.957 8.896   1.00 12.99 ?  44  LYS   B CA   1 
ATOM   4701 C C    . LYS   B 1 44  ? 51.703 -20.082 7.876   1.00 12.80 ?  44  LYS   B C    1 
ATOM   4702 O O    . LYS   B 1 44  ? 51.009 -21.100 7.967   1.00 13.93 ?  44  LYS   B O    1 
ATOM   4703 C CB   . LYS   B 1 44  ? 51.639 -19.472 10.332  1.00 14.36 ?  44  LYS   B CB   1 
ATOM   4704 C CG   . LYS   B 1 44  ? 51.849 -18.363 11.345  1.00 17.22 ?  44  LYS   B CG   1 
ATOM   4705 C CD   . LYS   B 1 44  ? 53.009 -17.471 10.875  1.00 21.17 ?  44  LYS   B CD   1 
ATOM   4706 C CE   . LYS   B 1 44  ? 53.760 -16.781 11.990  1.00 24.51 ?  44  LYS   B CE   1 
ATOM   4707 N NZ   . LYS   B 1 44  ? 54.759 -15.804 11.516  1.00 25.42 ?  44  LYS   B NZ   1 
ATOM   4708 H H    . LYS   B 1 44  ? 49.641 -18.671 9.025   1.00 15.14 ?  44  LYS   B H    1 
ATOM   4709 H HA   . LYS   B 1 44  ? 52.308 -18.344 8.722   1.00 15.56 ?  44  LYS   B HA   1 
ATOM   4710 H HB2  . LYS   B 1 44  ? 50.794 -19.910 10.542  1.00 17.21 ?  44  LYS   B HB2  1 
ATOM   4711 H HB3  . LYS   B 1 44  ? 52.367 -20.100 10.416  1.00 17.21 ?  44  LYS   B HB3  1 
ATOM   4712 H HG2  . LYS   B 1 44  ? 51.045 -17.827 11.418  1.00 20.64 ?  44  LYS   B HG2  1 
ATOM   4713 H HG3  . LYS   B 1 44  ? 52.084 -18.751 12.205  1.00 20.64 ?  44  LYS   B HG3  1 
ATOM   4714 H HD2  . LYS   B 1 44  ? 53.642 -18.029 10.386  1.00 25.38 ?  44  LYS   B HD2  1 
ATOM   4715 H HD3  . LYS   B 1 44  ? 52.647 -16.792 10.279  1.00 25.38 ?  44  LYS   B HD3  1 
ATOM   4716 H HE2  . LYS   B 1 44  ? 53.144 -16.256 12.487  1.00 29.39 ?  44  LYS   B HE2  1 
ATOM   4717 H HE3  . LYS   B 1 44  ? 54.190 -17.448 12.554  1.00 29.39 ?  44  LYS   B HE3  1 
ATOM   4718 H HZ1  . LYS   B 1 44  ? 55.165 -15.426 12.211  1.00 30.48 ?  44  LYS   B HZ1  1 
ATOM   4719 H HZ2  . LYS   B 1 44  ? 55.364 -16.202 11.004  1.00 30.48 ?  44  LYS   B HZ2  1 
ATOM   4720 H HZ3  . LYS   B 1 44  ? 54.353 -15.164 11.040  1.00 30.48 ?  44  LYS   B HZ3  1 
ATOM   4721 N N    . HIS   B 1 45  ? 52.558 -19.867 6.879   1.00 12.36 ?  45  HIS   B N    1 
ATOM   4722 C CA   . HIS   B 1 45  ? 52.588 -20.694 5.674   1.00 12.67 ?  45  HIS   B CA   1 
ATOM   4723 C C    . HIS   B 1 45  ? 53.612 -21.813 5.832   1.00 14.53 ?  45  HIS   B C    1 
ATOM   4724 O O    . HIS   B 1 45  ? 54.671 -21.827 5.212   1.00 17.42 ?  45  HIS   B O    1 
ATOM   4725 C CB   . HIS   B 1 45  ? 52.901 -19.835 4.460   1.00 12.86 ?  45  HIS   B CB   1 
ATOM   4726 C CG   . HIS   B 1 45  ? 52.030 -18.631 4.353   1.00 12.30 ?  45  HIS   B CG   1 
ATOM   4727 N ND1  . HIS   B 1 45  ? 50.652 -18.707 4.326   1.00 12.36 ?  45  HIS   B ND1  1 
ATOM   4728 C CD2  . HIS   B 1 45  ? 52.345 -17.318 4.276   1.00 13.02 ?  45  HIS   B CD2  1 
ATOM   4729 C CE1  . HIS   B 1 45  ? 50.163 -17.484 4.225   1.00 11.99 ?  45  HIS   B CE1  1 
ATOM   4730 N NE2  . HIS   B 1 45  ? 51.166 -16.624 4.197   1.00 12.67 ?  45  HIS   B NE2  1 
ATOM   4731 H H    . HIS   B 1 45  ? 53.128 -19.225 6.870   1.00 14.81 ?  45  HIS   B H    1 
ATOM   4732 H HA   . HIS   B 1 45  ? 51.712 -21.096 5.537   1.00 15.18 ?  45  HIS   B HA   1 
ATOM   4733 H HB2  . HIS   B 1 45  ? 53.821 -19.536 4.513   1.00 15.40 ?  45  HIS   B HB2  1 
ATOM   4734 H HB3  . HIS   B 1 45  ? 52.775 -20.368 3.654   1.00 15.40 ?  45  HIS   B HB3  1 
ATOM   4735 H HD2  . HIS   B 1 45  ? 53.201 -16.949 4.284   1.00 15.59 ?  45  HIS   B HD2  1 
ATOM   4736 H HE1  . HIS   B 1 45  ? 49.258 -17.268 4.177   1.00 14.36 ?  45  HIS   B HE1  1 
ATOM   4737 H HE2  . HIS   B 1 45  ? 51.086 -15.769 4.144   1.00 15.17 ?  45  HIS   B HE2  1 
ATOM   4738 N N    A GLY   B 1 46  ? 53.254 -22.781 6.672   0.58 15.86 ?  46  GLY   B N    1 
ATOM   4739 N N    B GLY   B 1 46  ? 53.265 -22.766 6.689   0.42 15.78 ?  46  GLY   B N    1 
ATOM   4740 C CA   A GLY   B 1 46  ? 54.180 -23.832 7.055   0.58 17.65 ?  46  GLY   B CA   1 
ATOM   4741 C CA   B GLY   B 1 46  ? 54.185 -23.832 7.022   0.42 17.25 ?  46  GLY   B CA   1 
ATOM   4742 C C    A GLY   B 1 46  ? 54.225 -25.064 6.169   0.58 19.48 ?  46  GLY   B C    1 
ATOM   4743 C C    B GLY   B 1 46  ? 54.206 -24.973 6.025   0.42 18.79 ?  46  GLY   B C    1 
ATOM   4744 O O    A GLY   B 1 46  ? 55.310 -25.517 5.788   0.58 22.27 ?  46  GLY   B O    1 
ATOM   4745 O O    B GLY   B 1 46  ? 55.232 -25.240 5.391   0.42 20.11 ?  46  GLY   B O    1 
ATOM   4746 H H    A GLY   B 1 46  ? 52.478 -22.836 7.046   0.58 19.01 ?  46  GLY   B H    1 
ATOM   4747 H H    B GLY   B 1 46  ? 52.502 -22.808 7.092   0.42 18.91 ?  46  GLY   B H    1 
ATOM   4748 H HA2  A GLY   B 1 46  ? 55.073 -23.457 7.090   0.58 21.16 ?  46  GLY   B HA2  1 
ATOM   4749 H HA2  B GLY   B 1 46  ? 55.080 -23.463 7.080   0.42 20.67 ?  46  GLY   B HA2  1 
ATOM   4750 H HA3  A GLY   B 1 46  ? 53.951 -24.134 7.947   0.58 21.16 ?  46  GLY   B HA3  1 
ATOM   4751 H HA3  B GLY   B 1 46  ? 53.949 -24.185 7.895   0.42 20.67 ?  46  GLY   B HA3  1 
ATOM   4752 N N    . GLY   B 1 47  ? 53.066 -25.640 5.852   1.00 18.99 ?  47  GLY   B N    1 
ATOM   4753 C CA   . GLY   B 1 47  ? 53.008 -26.906 5.151   1.00 17.09 ?  47  GLY   B CA   1 
ATOM   4754 C C    . GLY   B 1 47  ? 52.093 -26.879 3.942   1.00 14.39 ?  47  GLY   B C    1 
ATOM   4755 O O    . GLY   B 1 47  ? 51.443 -25.875 3.650   1.00 14.42 ?  47  GLY   B O    1 
ATOM   4756 H H    A GLY   B 1 47  ? 52.293 -25.321 6.059   0.58 22.77 ?  47  GLY   B H    1 
ATOM   4757 H H    B GLY   B 1 47  ? 52.300 -25.367 6.139   0.42 22.77 ?  47  GLY   B H    1 
ATOM   4758 H HA2  . GLY   B 1 47  ? 53.896 -27.155 4.850   1.00 20.49 ?  47  GLY   B HA2  1 
ATOM   4759 H HA3  . GLY   B 1 47  ? 52.690 -27.592 5.758   1.00 20.49 ?  47  GLY   B HA3  1 
ATOM   4760 N N    . GLY   B 1 48  ? 52.046 -28.018 3.251   1.00 13.57 ?  48  GLY   B N    1 
ATOM   4761 C CA   . GLY   B 1 48  ? 51.123 -28.164 2.142   1.00 13.49 ?  48  GLY   B CA   1 
ATOM   4762 C C    . GLY   B 1 48  ? 51.271 -27.059 1.123   1.00 12.69 ?  48  GLY   B C    1 
ATOM   4763 O O    . GLY   B 1 48  ? 52.377 -26.597 0.819   1.00 13.34 ?  48  GLY   B O    1 
ATOM   4764 H H    . GLY   B 1 48  ? 52.542 -28.699 3.396   1.00 16.26 ?  48  GLY   B H    1 
ATOM   4765 H HA2  . GLY   B 1 48  ? 51.279 -29.014 1.699   1.00 16.16 ?  48  GLY   B HA2  1 
ATOM   4766 H HA3  . GLY   B 1 48  ? 50.212 -28.153 2.471   1.00 16.16 ?  48  GLY   B HA3  1 
ATOM   4767 N N    . VAL   B 1 49  ? 50.129 -26.627 0.587   1.00 12.76 ?  49  VAL   B N    1 
ATOM   4768 C CA   . VAL   B 1 49  ? 50.110 -25.605 -0.456  1.00 12.85 ?  49  VAL   B CA   1 
ATOM   4769 C C    . VAL   B 1 49  ? 50.768 -24.318 0.031   1.00 11.53 ?  49  VAL   B C    1 
ATOM   4770 O O    . VAL   B 1 49  ? 51.559 -23.699 -0.689  1.00 12.49 ?  49  VAL   B O    1 
ATOM   4771 C CB   . VAL   B 1 49  ? 48.663 -25.352 -0.929  1.00 13.84 ?  49  VAL   B CB   1 
ATOM   4772 C CG1  . VAL   B 1 49  ? 48.583 -24.105 -1.801  1.00 14.03 ?  49  VAL   B CG1  1 
ATOM   4773 C CG2  . VAL   B 1 49  ? 48.128 -26.565 -1.685  1.00 15.55 ?  49  VAL   B CG2  1 
ATOM   4774 H H    . VAL   B 1 49  ? 49.343 -26.909 0.811   1.00 15.29 ?  49  VAL   B H    1 
ATOM   4775 H HA   . VAL   B 1 49  ? 50.608 -25.925 -1.221  1.00 15.40 ?  49  VAL   B HA   1 
ATOM   4776 H HB   . VAL   B 1 49  ? 48.093 -25.211 -0.155  1.00 16.58 ?  49  VAL   B HB   1 
ATOM   4777 H HG11 . VAL   B 1 49  ? 47.752 -24.120 -2.300  1.00 16.81 ?  49  VAL   B HG11 1 
ATOM   4778 H HG12 . VAL   B 1 49  ? 48.610 -23.318 -1.232  1.00 16.81 ?  49  VAL   B HG12 1 
ATOM   4779 H HG13 . VAL   B 1 49  ? 49.335 -24.100 -2.412  1.00 16.81 ?  49  VAL   B HG13 1 
ATOM   4780 H HG21 . VAL   B 1 49  ? 47.217 -26.386 -1.969  1.00 18.63 ?  49  VAL   B HG21 1 
ATOM   4781 H HG22 . VAL   B 1 49  ? 48.690 -26.724 -2.460  1.00 18.63 ?  49  VAL   B HG22 1 
ATOM   4782 H HG23 . VAL   B 1 49  ? 48.147 -27.335 -1.098  1.00 18.63 ?  49  VAL   B HG23 1 
ATOM   4783 N N    . ALA   B 1 50  ? 50.420 -23.872 1.238   1.00 11.31 ?  50  ALA   B N    1 
ATOM   4784 C CA   . ALA   B 1 50  ? 50.938 -22.595 1.716   1.00 11.35 ?  50  ALA   B CA   1 
ATOM   4785 C C    . ALA   B 1 50  ? 52.457 -22.625 1.830   1.00 11.67 ?  50  ALA   B C    1 
ATOM   4786 O O    . ALA   B 1 50  ? 53.135 -21.657 1.468   1.00 11.68 ?  50  ALA   B O    1 
ATOM   4787 C CB   . ALA   B 1 50  ? 50.305 -22.240 3.057   1.00 11.93 ?  50  ALA   B CB   1 
ATOM   4788 H H    . ALA   B 1 50  ? 49.898 -24.278 1.787   1.00 13.55 ?  50  ALA   B H    1 
ATOM   4789 H HA   . ALA   B 1 50  ? 50.708 -21.900 1.082   1.00 13.60 ?  50  ALA   B HA   1 
ATOM   4790 H HB1  . ALA   B 1 50  ? 50.662 -21.386 3.360   1.00 14.29 ?  50  ALA   B HB1  1 
ATOM   4791 H HB2  . ALA   B 1 50  ? 49.346 -22.173 2.946   1.00 14.29 ?  50  ALA   B HB2  1 
ATOM   4792 H HB3  . ALA   B 1 50  ? 50.520 -22.931 3.702   1.00 14.29 ?  50  ALA   B HB3  1 
ATOM   4793 N N    . GLY   B 1 51  ? 53.008 -23.718 2.349   1.00 12.29 ?  51  GLY   B N    1 
ATOM   4794 C CA   . GLY   B 1 51  ? 54.453 -23.824 2.422   1.00 12.93 ?  51  GLY   B CA   1 
ATOM   4795 C C    . GLY   B 1 51  ? 55.105 -23.775 1.056   1.00 12.92 ?  51  GLY   B C    1 
ATOM   4796 O O    . GLY   B 1 51  ? 56.151 -23.143 0.881   1.00 13.62 ?  51  GLY   B O    1 
ATOM   4797 H H    . GLY   B 1 51  ? 52.580 -24.400 2.651   1.00 14.72 ?  51  GLY   B H    1 
ATOM   4798 H HA2  . GLY   B 1 51  ? 54.806 -23.091 2.952   1.00 15.49 ?  51  GLY   B HA2  1 
ATOM   4799 H HA3  . GLY   B 1 51  ? 54.700 -24.659 2.847   1.00 15.49 ?  51  GLY   B HA3  1 
ATOM   4800 N N    . ALA   B 1 52  ? 54.504 -24.442 0.071   1.00 12.34 ?  52  ALA   B N    1 
ATOM   4801 C CA   . ALA   B 1 52  ? 55.069 -24.450 -1.272  1.00 12.70 ?  52  ALA   B CA   1 
ATOM   4802 C C    . ALA   B 1 52  ? 54.988 -23.072 -1.922  1.00 12.23 ?  52  ALA   B C    1 
ATOM   4803 O O    . ALA   B 1 52  ? 55.963 -22.613 -2.536  1.00 12.94 ?  52  ALA   B O    1 
ATOM   4804 C CB   . ALA   B 1 52  ? 54.355 -25.484 -2.136  1.00 13.29 ?  52  ALA   B CB   1 
ATOM   4805 H H    . ALA   B 1 52  ? 53.768 -24.884 0.150   1.00 14.79 ?  52  ALA   B H    1 
ATOM   4806 H HA   . ALA   B 1 52  ? 56.002 -24.697 -1.217  1.00 15.22 ?  52  ALA   B HA   1 
ATOM   4807 H HB1  . ALA   B 1 52  ? 54.750 -25.476 -3.026  1.00 15.92 ?  52  ALA   B HB1  1 
ATOM   4808 H HB2  . ALA   B 1 52  ? 54.471 -26.360 -1.736  1.00 15.92 ?  52  ALA   B HB2  1 
ATOM   4809 H HB3  . ALA   B 1 52  ? 53.416 -25.263 -2.190  1.00 15.92 ?  52  ALA   B HB3  1 
ATOM   4810 N N    . LEU   B 1 53  ? 53.842 -22.390 -1.800  1.00 11.88 ?  53  LEU   B N    1 
ATOM   4811 C CA   . LEU   B 1 53  ? 53.729 -21.044 -2.363  1.00 12.02 ?  53  LEU   B CA   1 
ATOM   4812 C C    . LEU   B 1 53  ? 54.737 -20.105 -1.713  1.00 11.87 ?  53  LEU   B C    1 
ATOM   4813 O O    . LEU   B 1 53  ? 55.444 -19.357 -2.401  1.00 12.77 ?  53  LEU   B O    1 
ATOM   4814 C CB   . LEU   B 1 53  ? 52.303 -20.500 -2.205  1.00 12.57 ?  53  LEU   B CB   1 
ATOM   4815 C CG   . LEU   B 1 53  ? 51.168 -21.233 -2.931  1.00 12.66 ?  53  LEU   B CG   1 
ATOM   4816 C CD1  . LEU   B 1 53  ? 49.820 -20.624 -2.592  1.00 14.30 ?  53  LEU   B CD1  1 
ATOM   4817 C CD2  . LEU   B 1 53  ? 51.389 -21.235 -4.442  1.00 14.54 ?  53  LEU   B CD2  1 
ATOM   4818 H H    . LEU   B 1 53  ? 53.138 -22.675 -1.402  1.00 14.24 ?  53  LEU   B H    1 
ATOM   4819 H HA   . LEU   B 1 53  ? 53.934 -21.088 -3.314  1.00 14.40 ?  53  LEU   B HA   1 
ATOM   4820 H HB2  . LEU   B 1 53  ? 52.087 -20.508 -1.262  1.00 15.06 ?  53  LEU   B HB2  1 
ATOM   4821 H HB3  . LEU   B 1 53  ? 52.299 -19.585 -2.526  1.00 15.06 ?  53  LEU   B HB3  1 
ATOM   4822 H HG   . LEU   B 1 53  ? 51.154 -22.156 -2.636  1.00 15.17 ?  53  LEU   B HG   1 
ATOM   4823 H HD11 . LEU   B 1 53  ? 49.126 -21.116 -3.065  1.00 17.13 ?  53  LEU   B HD11 1 
ATOM   4824 H HD12 . LEU   B 1 53  ? 49.675 -20.697 -1.634  1.00 17.13 ?  53  LEU   B HD12 1 
ATOM   4825 H HD13 . LEU   B 1 53  ? 49.812 -19.697 -2.861  1.00 17.13 ?  53  LEU   B HD13 1 
ATOM   4826 H HD21 . LEU   B 1 53  ? 50.721 -21.805 -4.858  1.00 17.43 ?  53  LEU   B HD21 1 
ATOM   4827 H HD22 . LEU   B 1 53  ? 51.302 -20.331 -4.777  1.00 17.43 ?  53  LEU   B HD22 1 
ATOM   4828 H HD23 . LEU   B 1 53  ? 52.275 -21.580 -4.638  1.00 17.43 ?  53  LEU   B HD23 1 
ATOM   4829 N N    . ASN   B 1 54  ? 54.827 -20.136 -0.385  1.00 11.71 ?  54  ASN   B N    1 
ATOM   4830 C CA   . ASN   B 1 54  ? 55.739 -19.223 0.291   1.00 12.33 ?  54  ASN   B CA   1 
ATOM   4831 C C    . ASN   B 1 54  ? 57.186 -19.501 -0.098  1.00 12.91 ?  54  ASN   B C    1 
ATOM   4832 O O    . ASN   B 1 54  ? 57.960 -18.566 -0.341  1.00 13.12 ?  54  ASN   B O    1 
ATOM   4833 C CB   . ASN   B 1 54  ? 55.566 -19.295 1.800   1.00 13.25 ?  54  ASN   B CB   1 
ATOM   4834 C CG   . ASN   B 1 54  ? 56.543 -18.387 2.511   1.00 13.19 ?  54  ASN   B CG   1 
ATOM   4835 O OD1  . ASN   B 1 54  ? 56.568 -17.173 2.270   1.00 13.95 ?  54  ASN   B OD1  1 
ATOM   4836 N ND2  . ASN   B 1 54  ? 57.387 -18.964 3.359   1.00 14.75 ?  54  ASN   B ND2  1 
ATOM   4837 H H    . ASN   B 1 54  ? 54.382 -20.663 0.128   1.00 14.03 ?  54  ASN   B H    1 
ATOM   4838 H HA   . ASN   B 1 54  ? 55.525 -18.318 0.012   1.00 14.77 ?  54  ASN   B HA   1 
ATOM   4839 H HB2  . ASN   B 1 54  ? 54.665 -19.016 2.036   1.00 15.88 ?  54  ASN   B HB2  1 
ATOM   4840 H HB3  . ASN   B 1 54  ? 55.722 -20.205 2.099   1.00 15.88 ?  54  ASN   B HB3  1 
ATOM   4841 H HD21 . ASN   B 1 54  ? 57.969 -18.489 3.781   1.00 17.68 ?  54  ASN   B HD21 1 
ATOM   4842 H HD22 . ASN   B 1 54  ? 57.354 -19.815 3.491   1.00 17.68 ?  54  ASN   B HD22 1 
ATOM   4843 N N    . LYS   B 1 55  ? 57.569 -20.780 -0.166  1.00 13.30 ?  55  LYS   B N    1 
ATOM   4844 C CA   . LYS   B 1 55  ? 58.925 -21.123 -0.578  1.00 14.24 ?  55  LYS   B CA   1 
ATOM   4845 C C    . LYS   B 1 55  ? 59.228 -20.583 -1.968  1.00 14.04 ?  55  LYS   B C    1 
ATOM   4846 O O    . LYS   B 1 55  ? 60.328 -20.073 -2.216  1.00 14.85 ?  55  LYS   B O    1 
ATOM   4847 C CB   . LYS   B 1 55  ? 59.124 -22.638 -0.517  1.00 16.35 ?  55  LYS   B CB   1 
ATOM   4848 C CG   . LYS   B 1 55  ? 60.508 -23.095 -0.934  1.00 20.49 ?  55  LYS   B CG   1 
ATOM   4849 C CD   . LYS   B 1 55  ? 60.679 -24.593 -0.755  1.00 24.12 ?  55  LYS   B CD   1 
ATOM   4850 C CE   . LYS   B 1 55  ? 60.846 -24.976 0.714   1.00 26.95 ?  55  LYS   B CE   1 
ATOM   4851 N NZ   . LYS   B 1 55  ? 61.147 -26.421 0.878   1.00 28.77 ?  55  LYS   B NZ   1 
ATOM   4852 H H    . LYS   B 1 55  ? 57.063 -21.454 0.012   1.00 15.93 ?  55  LYS   B H    1 
ATOM   4853 H HA   . LYS   B 1 55  ? 59.548 -20.715 0.036   1.00 17.07 ?  55  LYS   B HA   1 
ATOM   4854 H HB2  . LYS   B 1 55  ? 58.975 -22.931 0.398   1.00 19.60 ?  55  LYS   B HB2  1 
ATOM   4855 H HB3  . LYS   B 1 55  ? 58.479 -23.064 -1.104  1.00 19.60 ?  55  LYS   B HB3  1 
ATOM   4856 H HG2  . LYS   B 1 55  ? 60.644 -22.885 -1.871  1.00 24.56 ?  55  LYS   B HG2  1 
ATOM   4857 H HG3  . LYS   B 1 55  ? 61.170 -22.644 -0.388  1.00 24.56 ?  55  LYS   B HG3  1 
ATOM   4858 H HD2  . LYS   B 1 55  ? 59.896 -25.052 -1.098  1.00 28.92 ?  55  LYS   B HD2  1 
ATOM   4859 H HD3  . LYS   B 1 55  ? 61.472 -24.885 -1.234  1.00 28.92 ?  55  LYS   B HD3  1 
ATOM   4860 H HE2  . LYS   B 1 55  ? 61.581 -24.464 1.092   1.00 32.32 ?  55  LYS   B HE2  1 
ATOM   4861 H HE3  . LYS   B 1 55  ? 60.024 -24.777 1.189   1.00 32.32 ?  55  LYS   B HE3  1 
ATOM   4862 H HZ1  . LYS   B 1 55  ? 61.199 -26.622 1.743   1.00 34.50 ?  55  LYS   B HZ1  1 
ATOM   4863 H HZ2  . LYS   B 1 55  ? 60.501 -26.906 0.505   1.00 34.50 ?  55  LYS   B HZ2  1 
ATOM   4864 H HZ3  . LYS   B 1 55  ? 61.920 -26.616 0.486   1.00 34.50 ?  55  LYS   B HZ3  1 
ATOM   4865 N N    . ALA   B 1 56  ? 58.263 -20.678 -2.891  1.00 13.36 ?  56  ALA   B N    1 
ATOM   4866 C CA   . ALA   B 1 56  ? 58.484 -20.173 -4.240  1.00 14.31 ?  56  ALA   B CA   1 
ATOM   4867 C C    . ALA   B 1 56  ? 58.761 -18.676 -4.243  1.00 14.03 ?  56  ALA   B C    1 
ATOM   4868 O O    . ALA   B 1 56  ? 59.500 -18.186 -5.107  1.00 15.15 ?  56  ALA   B O    1 
ATOM   4869 C CB   . ALA   B 1 56  ? 57.291 -20.503 -5.139  1.00 15.07 ?  56  ALA   B CB   1 
ATOM   4870 H H    . ALA   B 1 56  ? 57.478 -21.012 -2.761  1.00 16.01 ?  56  ALA   B H    1 
ATOM   4871 H HA   . ALA   B 1 56  ? 59.262 -20.605 -4.613  1.00 17.14 ?  56  ALA   B HA   1 
ATOM   4872 H HB1  . ALA   B 1 56  ? 57.463 -20.159 -6.034  1.00 18.06 ?  56  ALA   B HB1  1 
ATOM   4873 H HB2  . ALA   B 1 56  ? 57.182 -21.465 -5.174  1.00 18.06 ?  56  ALA   B HB2  1 
ATOM   4874 H HB3  . ALA   B 1 56  ? 56.493 -20.090 -4.778  1.00 18.06 ?  56  ALA   B HB3  1 
ATOM   4875 N N    . THR   B 1 57  ? 58.190 -17.936 -3.289  1.00 13.90 ?  57  THR   B N    1 
ATOM   4876 C CA   . THR   B 1 57  ? 58.427 -16.501 -3.167  1.00 14.29 ?  57  THR   B CA   1 
ATOM   4877 C C    . THR   B 1 57  ? 59.674 -16.170 -2.356  1.00 15.05 ?  57  THR   B C    1 
ATOM   4878 O O    . THR   B 1 57  ? 59.904 -14.994 -2.051  1.00 15.40 ?  57  THR   B O    1 
ATOM   4879 C CB   . THR   B 1 57  ? 57.224 -15.771 -2.539  1.00 13.14 ?  57  THR   B CB   1 
ATOM   4880 O OG1  . THR   B 1 57  ? 57.191 -15.989 -1.121  1.00 13.94 ?  57  THR   B OG1  1 
ATOM   4881 C CG2  . THR   B 1 57  ? 55.903 -16.177 -3.196  1.00 13.40 ?  57  THR   B CG2  1 
ATOM   4882 H H    . THR   B 1 57  ? 57.644 -18.244 -2.693  1.00 16.66 ?  57  THR   B H    1 
ATOM   4883 H HA   . THR   B 1 57  ? 58.547 -16.132 -4.056  1.00 17.12 ?  57  THR   B HA   1 
ATOM   4884 H HB   . THR   B 1 57  ? 57.331 -14.817 -2.693  1.00 15.75 ?  57  THR   B HB   1 
ATOM   4885 H HG1  . THR   B 1 57  ? 57.109 -16.811 -0.960  1.00 16.70 ?  57  THR   B HG1  1 
ATOM   4886 H HG21 . THR   B 1 57  ? 55.173 -15.655 -2.831  1.00 16.06 ?  57  THR   B HG21 1 
ATOM   4887 H HG22 . THR   B 1 57  ? 55.950 -16.031 -4.153  1.00 16.06 ?  57  THR   B HG22 1 
ATOM   4888 H HG23 . THR   B 1 57  ? 55.728 -17.118 -3.032  1.00 16.06 ?  57  THR   B HG23 1 
ATOM   4889 N N    . ASN   B 1 58  ? 60.467 -17.171 -1.985  1.00 15.71 ?  58  ASN   B N    1 
ATOM   4890 C CA   . ASN   B 1 58  ? 61.658 -16.951 -1.171  1.00 18.34 ?  58  ASN   B CA   1 
ATOM   4891 C C    . ASN   B 1 58  ? 61.314 -16.237 0.136   1.00 16.23 ?  58  ASN   B C    1 
ATOM   4892 O O    . ASN   B 1 58  ? 62.046 -15.362 0.603   1.00 17.38 ?  58  ASN   B O    1 
ATOM   4893 C CB   . ASN   B 1 58  ? 62.750 -16.205 -1.947  1.00 24.86 ?  58  ASN   B CB   1 
ATOM   4894 C CG   . ASN   B 1 58  ? 64.115 -16.329 -1.297  1.00 32.74 ?  58  ASN   B CG   1 
ATOM   4895 O OD1  . ASN   B 1 58  ? 64.418 -17.333 -0.654  1.00 35.17 ?  58  ASN   B OD1  1 
ATOM   4896 N ND2  . ASN   B 1 58  ? 64.944 -15.305 -1.459  1.00 37.75 ?  58  ASN   B ND2  1 
ATOM   4897 H H    . ASN   B 1 58  ? 60.332 -17.996 -2.192  1.00 18.83 ?  58  ASN   B H    1 
ATOM   4898 H HA   . ASN   B 1 58  ? 62.022 -17.822 -0.944  1.00 21.98 ?  58  ASN   B HA   1 
ATOM   4899 H HB2  . ASN   B 1 58  ? 62.810 -16.571 -2.847  1.00 29.80 ?  58  ASN   B HB2  1 
ATOM   4900 H HB3  . ASN   B 1 58  ? 62.525 -15.264 -1.988  1.00 29.80 ?  58  ASN   B HB3  1 
ATOM   4901 H HD21 . ASN   B 1 58  ? 65.731 -15.330 -1.110  1.00 45.27 ?  58  ASN   B HD21 1 
ATOM   4902 H HD22 . ASN   B 1 58  ? 64.696 -14.618 -1.912  1.00 45.27 ?  58  ASN   B HD22 1 
ATOM   4903 N N    . ASN   B 1 59  ? 60.185 -16.622 0.736   1.00 14.95 ?  59  ASN   B N    1 
ATOM   4904 C CA   . ASN   B 1 59  ? 59.701 -16.148 2.033   1.00 15.04 ?  59  ASN   B CA   1 
ATOM   4905 C C    . ASN   B 1 59  ? 59.106 -14.742 1.971   1.00 14.31 ?  59  ASN   B C    1 
ATOM   4906 O O    . ASN   B 1 59  ? 58.677 -14.234 3.008   1.00 14.40 ?  59  ASN   B O    1 
ATOM   4907 C CB   . ASN   B 1 59  ? 60.771 -16.198 3.139   1.00 16.02 ?  59  ASN   B CB   1 
ATOM   4908 C CG   . ASN   B 1 59  ? 60.182 -16.373 4.521   1.00 17.22 ?  59  ASN   B CG   1 
ATOM   4909 O OD1  . ASN   B 1 59  ? 59.357 -17.262 4.750   1.00 17.45 ?  59  ASN   B OD1  1 
ATOM   4910 N ND2  . ASN   B 1 59  ? 60.615 -15.537 5.459   1.00 17.78 ?  59  ASN   B ND2  1 
ATOM   4911 H H    . ASN   B 1 59  ? 59.648 -17.199 0.385   1.00 17.92 ?  59  ASN   B H    1 
ATOM   4912 H HA   . ASN   B 1 59  ? 58.992 -16.748 2.315   1.00 18.02 ?  59  ASN   B HA   1 
ATOM   4913 H HB2  . ASN   B 1 59  ? 61.367 -16.947 2.982   1.00 19.20 ?  59  ASN   B HB2  1 
ATOM   4914 H HB3  . ASN   B 1 59  ? 61.272 -15.369 3.140   1.00 19.20 ?  59  ASN   B HB3  1 
ATOM   4915 H HD21 . ASN   B 1 59  ? 60.311 -15.594 6.264   1.00 21.31 ?  59  ASN   B HD21 1 
ATOM   4916 H HD22 . ASN   B 1 59  ? 61.192 -14.930 5.264   1.00 21.31 ?  59  ASN   B HD22 1 
ATOM   4917 N N    . ALA   B 1 60  ? 59.053 -14.102 0.799   1.00 14.06 ?  60  ALA   B N    1 
ATOM   4918 C CA   . ALA   B 1 60  ? 58.454 -12.771 0.723   1.00 14.13 ?  60  ALA   B CA   1 
ATOM   4919 C C    . ALA   B 1 60  ? 56.983 -12.803 1.121   1.00 13.23 ?  60  ALA   B C    1 
ATOM   4920 O O    . ALA   B 1 60  ? 56.471 -11.851 1.723   1.00 14.27 ?  60  ALA   B O    1 
ATOM   4921 C CB   . ALA   B 1 60  ? 58.615 -12.193 -0.682  1.00 15.31 ?  60  ALA   B CB   1 
ATOM   4922 H H    . ALA   B 1 60  ? 59.357 -14.413 0.057   1.00 16.85 ?  60  ALA   B H    1 
ATOM   4923 H HA   . ALA   B 1 60  ? 58.915 -12.189 1.345   1.00 16.93 ?  60  ALA   B HA   1 
ATOM   4924 H HB1  . ALA   B 1 60  ? 58.212 -11.313 -0.705  1.00 18.34 ?  60  ALA   B HB1  1 
ATOM   4925 H HB2  . ALA   B 1 60  ? 59.562 -12.130 -0.890  1.00 18.34 ?  60  ALA   B HB2  1 
ATOM   4926 H HB3  . ALA   B 1 60  ? 58.176 -12.779 -1.317  1.00 18.34 ?  60  ALA   B HB3  1 
ATOM   4927 N N    . MET   B 1 61  ? 56.280 -13.884 0.781   1.00 12.92 ?  61  MET   B N    1 
ATOM   4928 C CA   . MET   B 1 61  ? 54.882 -14.007 1.170   1.00 12.56 ?  61  MET   B CA   1 
ATOM   4929 C C    . MET   B 1 61  ? 54.734 -14.011 2.689   1.00 12.67 ?  61  MET   B C    1 
ATOM   4930 O O    . MET   B 1 61  ? 53.826 -13.367 3.236   1.00 12.68 ?  61  MET   B O    1 
ATOM   4931 C CB   . MET   B 1 61  ? 54.309 -15.284 0.549   1.00 12.45 ?  61  MET   B CB   1 
ATOM   4932 C CG   . MET   B 1 61  ? 52.861 -15.572 0.945   1.00 12.04 ?  61  MET   B CG   1 
ATOM   4933 S SD   . MET   B 1 61  ? 52.222 -17.083 0.181   1.00 12.97 ?  61  MET   B SD   1 
ATOM   4934 C CE   . MET   B 1 61  ? 51.977 -16.501 -1.495  1.00 13.94 ?  61  MET   B CE   1 
ATOM   4935 H H    . MET   B 1 61  ? 56.590 -14.557 0.331   1.00 15.48 ?  61  MET   B H    1 
ATOM   4936 H HA   . MET   B 1 61  ? 54.391 -13.259 0.804   1.00 15.05 ?  61  MET   B HA   1 
ATOM   4937 H HB2  . MET   B 1 61  ? 54.339 -15.203 -0.419  1.00 14.92 ?  61  MET   B HB2  1 
ATOM   4938 H HB3  . MET   B 1 61  ? 54.850 -16.040 0.829   1.00 14.92 ?  61  MET   B HB3  1 
ATOM   4939 H HG2  . MET   B 1 61  ? 52.810 -15.684 1.910   1.00 14.43 ?  61  MET   B HG2  1 
ATOM   4940 H HG3  . MET   B 1 61  ? 52.302 -14.829 0.670   1.00 14.43 ?  61  MET   B HG3  1 
ATOM   4941 H HE1  . MET   B 1 61  ? 51.600 -17.221 -2.027  1.00 16.70 ?  61  MET   B HE1  1 
ATOM   4942 H HE2  . MET   B 1 61  ? 51.363 -15.745 -1.486  1.00 16.70 ?  61  MET   B HE2  1 
ATOM   4943 H HE3  . MET   B 1 61  ? 52.829 -16.227 -1.865  1.00 16.70 ?  61  MET   B HE3  1 
ATOM   4944 N N    . GLN   B 1 62  ? 55.617 -14.725 3.393   1.00 12.10 ?  62  GLN   B N    1 
ATOM   4945 C CA   . GLN   B 1 62  ? 55.507 -14.786 4.845   1.00 12.78 ?  62  GLN   B CA   1 
ATOM   4946 C C    . GLN   B 1 62  ? 55.782 -13.429 5.480   1.00 12.90 ?  62  GLN   B C    1 
ATOM   4947 O O    . GLN   B 1 62  ? 55.091 -13.031 6.425   1.00 13.64 ?  62  GLN   B O    1 
ATOM   4948 C CB   . GLN   B 1 62  ? 56.453 -15.846 5.415   1.00 13.21 ?  62  GLN   B CB   1 
ATOM   4949 C CG   . GLN   B 1 62  ? 56.218 -16.101 6.895   1.00 13.52 ?  62  GLN   B CG   1 
ATOM   4950 C CD   . GLN   B 1 62  ? 54.843 -16.696 7.140   1.00 13.24 ?  62  GLN   B CD   1 
ATOM   4951 O OE1  . GLN   B 1 62  ? 54.588 -17.849 6.789   1.00 13.57 ?  62  GLN   B OE1  1 
ATOM   4952 N NE2  . GLN   B 1 62  ? 53.935 -15.903 7.703   1.00 13.22 ?  62  GLN   B NE2  1 
ATOM   4953 H H    . GLN   B 1 62  ? 56.268 -15.180 3.057   1.00 14.49 ?  62  GLN   B H    1 
ATOM   4954 H HA   . GLN   B 1 62  ? 54.601 -15.045 5.076   1.00 15.31 ?  62  GLN   B HA   1 
ATOM   4955 H HB2  . GLN   B 1 62  ? 56.319 -16.686 4.944   1.00 15.83 ?  62  GLN   B HB2  1 
ATOM   4956 H HB3  . GLN   B 1 62  ? 57.371 -15.550 5.305   1.00 15.83 ?  62  GLN   B HB3  1 
ATOM   4957 H HG2  . GLN   B 1 62  ? 56.883 -16.728 7.222   1.00 16.20 ?  62  GLN   B HG2  1 
ATOM   4958 H HG3  . GLN   B 1 62  ? 56.279 -15.264 7.382   1.00 16.20 ?  62  GLN   B HG3  1 
ATOM   4959 H HE21 . GLN   B 1 62  ? 54.145 -15.100 7.925   1.00 15.84 ?  62  GLN   B HE21 1 
ATOM   4960 H HE22 . GLN   B 1 62  ? 53.142 -16.199 7.852   1.00 15.84 ?  62  GLN   B HE22 1 
ATOM   4961 N N    . VAL   B 1 63  ? 56.795 -12.712 4.990   1.00 13.69 ?  63  VAL   B N    1 
ATOM   4962 C CA   . VAL   B 1 63  ? 57.093 -11.391 5.538   1.00 14.52 ?  63  VAL   B CA   1 
ATOM   4963 C C    . VAL   B 1 63  ? 55.898 -10.462 5.356   1.00 13.85 ?  63  VAL   B C    1 
ATOM   4964 O O    . VAL   B 1 63  ? 55.475 -9.765  6.289   1.00 14.62 ?  63  VAL   B O    1 
ATOM   4965 C CB   . VAL   B 1 63  ? 58.380 -10.828 4.907   1.00 15.83 ?  63  VAL   B CB   1 
ATOM   4966 C CG1  . VAL   B 1 63  ? 58.604 -9.380  5.343   1.00 16.51 ?  63  VAL   B CG1  1 
ATOM   4967 C CG2  . VAL   B 1 63  ? 59.578 -11.695 5.291   1.00 16.60 ?  63  VAL   B CG2  1 
ATOM   4968 H H    . VAL   B 1 63  ? 57.307 -12.965 4.341   1.00 16.40 ?  63  VAL   B H    1 
ATOM   4969 H HA   . VAL   B 1 63  ? 57.253 -11.487 6.486   1.00 17.40 ?  63  VAL   B HA   1 
ATOM   4970 H HB   . VAL   B 1 63  ? 58.301 -10.848 3.940   1.00 18.97 ?  63  VAL   B HB   1 
ATOM   4971 H HG11 . VAL   B 1 63  ? 59.519 -9.129  5.141   1.00 19.79 ?  63  VAL   B HG11 1 
ATOM   4972 H HG12 . VAL   B 1 63  ? 57.990 -8.807  4.861   1.00 19.79 ?  63  VAL   B HG12 1 
ATOM   4973 H HG13 . VAL   B 1 63  ? 58.447 -9.313  6.298   1.00 19.79 ?  63  VAL   B HG13 1 
ATOM   4974 H HG21 . VAL   B 1 63  ? 60.382 -11.315 4.901   1.00 19.90 ?  63  VAL   B HG21 1 
ATOM   4975 H HG22 . VAL   B 1 63  ? 59.658 -11.711 6.259   1.00 19.90 ?  63  VAL   B HG22 1 
ATOM   4976 H HG23 . VAL   B 1 63  ? 59.442 -12.594 4.956   1.00 19.90 ?  63  VAL   B HG23 1 
ATOM   4977 N N    . GLU   B 1 64  ? 55.324 -10.455 4.151   1.00 13.43 ?  64  GLU   B N    1 
ATOM   4978 C CA   . GLU   B 1 64  ? 54.164 -9.616  3.876   1.00 13.20 ?  64  GLU   B CA   1 
ATOM   4979 C C    . GLU   B 1 64  ? 52.979 -10.023 4.746   1.00 12.93 ?  64  GLU   B C    1 
ATOM   4980 O O    . GLU   B 1 64  ? 52.230 -9.167  5.244   1.00 13.38 ?  64  GLU   B O    1 
ATOM   4981 C CB   . GLU   B 1 64  ? 53.814 -9.760  2.394   1.00 13.79 ?  64  GLU   B CB   1 
ATOM   4982 C CG   . GLU   B 1 64  ? 52.564 -9.014  1.947   1.00 13.79 ?  64  GLU   B CG   1 
ATOM   4983 C CD   . GLU   B 1 64  ? 52.033 -9.515  0.613   1.00 14.76 ?  64  GLU   B CD   1 
ATOM   4984 O OE1  . GLU   B 1 64  ? 52.212 -10.728 0.303   1.00 15.49 ?  64  GLU   B OE1  1 
ATOM   4985 O OE2  . GLU   B 1 64  ? 51.409 -8.699  -0.111  1.00 15.20 -1 64  GLU   B OE2  1 
ATOM   4986 H H    . GLU   B 1 64  ? 55.590 -10.929 3.475   1.00 16.10 ?  64  GLU   B H    1 
ATOM   4987 H HA   . GLU   B 1 64  ? 54.383 -8.689  4.054   1.00 15.82 ?  64  GLU   B HA   1 
ATOM   4988 H HB2  . GLU   B 1 64  ? 54.552 -9.419  1.862   1.00 16.53 ?  64  GLU   B HB2  1 
ATOM   4989 H HB3  . GLU   B 1 64  ? 53.677 -10.697 2.196   1.00 16.53 ?  64  GLU   B HB3  1 
ATOM   4990 H HG2  . GLU   B 1 64  ? 51.857 -9.130  2.604   1.00 16.52 ?  64  GLU   B HG2  1 
ATOM   4991 H HG3  . GLU   B 1 64  ? 52.771 -8.069  1.855   1.00 16.52 ?  64  GLU   B HG3  1 
ATOM   4992 N N    . SER   B 1 65  ? 52.800 -11.331 4.940   1.00 12.80 ?  65  SER   B N    1 
ATOM   4993 C CA   . SER   B 1 65  ? 51.689 -11.842 5.737   1.00 12.79 ?  65  SER   B CA   1 
ATOM   4994 C C    . SER   B 1 65  ? 51.815 -11.442 7.202   1.00 13.09 ?  65  SER   B C    1 
ATOM   4995 O O    . SER   B 1 65  ? 50.816 -11.072 7.837   1.00 12.79 ?  65  SER   B O    1 
ATOM   4996 C CB   . SER   B 1 65  ? 51.617 -13.363 5.610   1.00 13.08 ?  65  SER   B CB   1 
ATOM   4997 O OG   . SER   B 1 65  ? 51.252 -13.768 4.302   1.00 13.18 ?  65  SER   B OG   1 
ATOM   4998 H H    . SER   B 1 65  ? 53.312 -11.950 4.623   1.00 15.34 ?  65  SER   B H    1 
ATOM   4999 H HA   . SER   B 1 65  ? 50.858 -11.473 5.398   1.00 15.32 ?  65  SER   B HA   1 
ATOM   5000 H HB2  . SER   B 1 65  ? 52.483 -13.736 5.821   1.00 15.67 ?  65  SER   B HB2  1 
ATOM   5001 H HB3  . SER   B 1 65  ? 50.952 -13.695 6.238   1.00 15.67 ?  65  SER   B HB3  1 
ATOM   5002 H HG   . SER   B 1 65  ? 51.812 -13.476 3.743   1.00 15.79 ?  65  SER   B HG   1 
ATOM   5003 N N    . ASP   B 1 66  ? 53.021 -11.535 7.768   1.00 13.35 ?  66  ASP   B N    1 
ATOM   5004 C CA   . ASP   B 1 66  ? 53.209 -11.138 9.161   1.00 13.34 ?  66  ASP   B CA   1 
ATOM   5005 C C    . ASP   B 1 66  ? 52.900 -9.658  9.360   1.00 13.54 ?  66  ASP   B C    1 
ATOM   5006 O O    . ASP   B 1 66  ? 52.328 -9.265  10.384  1.00 14.18 ?  66  ASP   B O    1 
ATOM   5007 C CB   . ASP   B 1 66  ? 54.637 -11.449 9.619   1.00 14.73 ?  66  ASP   B CB   1 
ATOM   5008 C CG   . ASP   B 1 66  ? 54.901 -12.946 9.781   1.00 16.56 ?  66  ASP   B CG   1 
ATOM   5009 O OD1  . ASP   B 1 66  ? 53.945 -13.752 9.721   1.00 17.21 ?  66  ASP   B OD1  1 
ATOM   5010 O OD2  . ASP   B 1 66  ? 56.079 -13.318 9.985   1.00 19.42 -1 66  ASP   B OD2  1 
ATOM   5011 H H    . ASP   B 1 66  ? 53.729 -11.825 7.382   1.00 15.99 ?  66  ASP   B H    1 
ATOM   5012 H HA   . ASP   B 1 66  ? 52.604 -11.638 9.727   1.00 15.98 ?  66  ASP   B HA   1 
ATOM   5013 H HB2  . ASP   B 1 66  ? 55.264 -11.104 8.963   1.00 17.66 ?  66  ASP   B HB2  1 
ATOM   5014 H HB3  . ASP   B 1 66  ? 54.798 -11.023 10.480  1.00 17.66 ?  66  ASP   B HB3  1 
ATOM   5015 N N    . ASP   B 1 67  ? 53.281 -8.818  8.398   1.00 13.28 ?  67  ASP   B N    1 
ATOM   5016 C CA   . ASP   B 1 67  ? 52.929 -7.408  8.475   1.00 14.00 ?  67  ASP   B CA   1 
ATOM   5017 C C    . ASP   B 1 67  ? 51.415 -7.202  8.394   1.00 14.05 ?  67  ASP   B C    1 
ATOM   5018 O O    . ASP   B 1 67  ? 50.855 -6.379  9.126   1.00 14.42 ?  67  ASP   B O    1 
ATOM   5019 C CB   . ASP   B 1 67  ? 53.640 -6.647  7.363   1.00 14.99 ?  67  ASP   B CB   1 
ATOM   5020 C CG   . ASP   B 1 67  ? 53.212 -5.206  7.306   1.00 16.83 ?  67  ASP   B CG   1 
ATOM   5021 O OD1  . ASP   B 1 67  ? 53.686 -4.401  8.138   1.00 18.19 ?  67  ASP   B OD1  1 
ATOM   5022 O OD2  . ASP   B 1 67  ? 52.373 -4.894  6.451   1.00 17.82 -1 67  ASP   B OD2  1 
ATOM   5023 H H    . ASP   B 1 67  ? 53.743 -9.037  7.707   1.00 15.91 ?  67  ASP   B H    1 
ATOM   5024 H HA   . ASP   B 1 67  ? 53.237 -7.048  9.324   1.00 16.77 ?  67  ASP   B HA   1 
ATOM   5025 H HB2  . ASP   B 1 67  ? 54.598 -6.675  7.519   1.00 17.96 ?  67  ASP   B HB2  1 
ATOM   5026 H HB3  . ASP   B 1 67  ? 53.433 -7.068  6.510   1.00 17.96 ?  67  ASP   B HB3  1 
ATOM   5027 N N    . TYR   B 1 68  ? 50.734 -7.941  7.511   1.00 13.83 ?  68  TYR   B N    1 
ATOM   5028 C CA   . TYR   B 1 68  ? 49.276 -7.859  7.440   1.00 14.44 ?  68  TYR   B CA   1 
ATOM   5029 C C    . TYR   B 1 68  ? 48.641 -8.191  8.788   1.00 13.86 ?  68  TYR   B C    1 
ATOM   5030 O O    . TYR   B 1 68  ? 47.709 -7.505  9.232   1.00 14.65 ?  68  TYR   B O    1 
ATOM   5031 C CB   . TYR   B 1 68  ? 48.740 -8.791  6.343   1.00 15.35 ?  68  TYR   B CB   1 
ATOM   5032 C CG   . TYR   B 1 68  ? 47.231 -8.950  6.395   1.00 16.11 ?  68  TYR   B CG   1 
ATOM   5033 C CD1  . TYR   B 1 68  ? 46.643 -9.885  7.241   1.00 16.63 ?  68  TYR   B CD1  1 
ATOM   5034 C CD2  . TYR   B 1 68  ? 46.398 -8.133  5.645   1.00 16.99 ?  68  TYR   B CD2  1 
ATOM   5035 C CE1  . TYR   B 1 68  ? 45.278 -10.013 7.329   1.00 17.42 ?  68  TYR   B CE1  1 
ATOM   5036 C CE2  . TYR   B 1 68  ? 45.009 -8.263  5.724   1.00 17.12 ?  68  TYR   B CE2  1 
ATOM   5037 C CZ   . TYR   B 1 68  ? 44.474 -9.203  6.574   1.00 17.57 ?  68  TYR   B CZ   1 
ATOM   5038 O OH   . TYR   B 1 68  ? 43.112 -9.337  6.680   1.00 18.61 ?  68  TYR   B OH   1 
ATOM   5039 H H    . TYR   B 1 68  ? 51.092 -8.500  6.960   1.00 16.57 ?  68  TYR   B H    1 
ATOM   5040 H HA   . TYR   B 1 68  ? 49.032 -6.952  7.213   1.00 17.30 ?  68  TYR   B HA   1 
ATOM   5041 H HB2  . TYR   B 1 68  ? 48.970 -8.419  5.478   1.00 18.40 ?  68  TYR   B HB2  1 
ATOM   5042 H HB3  . TYR   B 1 68  ? 49.137 -9.667  6.449   1.00 18.40 ?  68  TYR   B HB3  1 
ATOM   5043 H HD1  . TYR   B 1 68  ? 47.186 -10.435 7.760   1.00 19.93 ?  68  TYR   B HD1  1 
ATOM   5044 H HD2  . TYR   B 1 68  ? 46.770 -7.488  5.087   1.00 20.36 ?  68  TYR   B HD2  1 
ATOM   5045 H HE1  . TYR   B 1 68  ? 44.901 -10.654 7.891   1.00 20.88 ?  68  TYR   B HE1  1 
ATOM   5046 H HE2  . TYR   B 1 68  ? 44.454 -7.712  5.221   1.00 20.52 ?  68  TYR   B HE2  1 
ATOM   5047 H HH   . TYR   B 1 68  ? 42.715 -8.800  6.160   1.00 22.31 ?  68  TYR   B HH   1 
ATOM   5048 N N    . ILE   B 1 69  ? 49.124 -9.252  9.443   1.00 13.49 ?  69  ILE   B N    1 
ATOM   5049 C CA   . ILE   B 1 69  ? 48.571 -9.666  10.731  1.00 14.04 ?  69  ILE   B CA   1 
ATOM   5050 C C    . ILE   B 1 69  ? 48.829 -8.608  11.792  1.00 13.49 ?  69  ILE   B C    1 
ATOM   5051 O O    . ILE   B 1 69  ? 47.962 -8.311  12.620  1.00 13.73 ?  69  ILE   B O    1 
ATOM   5052 C CB   . ILE   B 1 69  ? 49.153 -11.035 11.138  1.00 14.47 ?  69  ILE   B CB   1 
ATOM   5053 C CG1  . ILE   B 1 69  ? 48.644 -12.155 10.216  1.00 14.78 ?  69  ILE   B CG1  1 
ATOM   5054 C CG2  . ILE   B 1 69  ? 48.866 -11.338 12.599  1.00 15.17 ?  69  ILE   B CG2  1 
ATOM   5055 C CD1  . ILE   B 1 69  ? 47.170 -12.498 10.360  1.00 14.68 ?  69  ILE   B CD1  1 
ATOM   5056 H H    . ILE   B 1 69  ? 49.763 -9.753  9.160   1.00 16.16 ?  69  ILE   B H    1 
ATOM   5057 H HA   . ILE   B 1 69  ? 47.612 -9.772  10.642  1.00 16.83 ?  69  ILE   B HA   1 
ATOM   5058 H HB   . ILE   B 1 69  ? 50.119 -10.988 11.033  1.00 17.34 ?  69  ILE   B HB   1 
ATOM   5059 H HG12 . ILE   B 1 69  ? 48.793 -11.885 9.295   1.00 17.71 ?  69  ILE   B HG12 1 
ATOM   5060 H HG13 . ILE   B 1 69  ? 49.153 -12.961 10.400  1.00 17.71 ?  69  ILE   B HG13 1 
ATOM   5061 H HG21 . ILE   B 1 69  ? 49.017 -12.283 12.758  1.00 18.17 ?  69  ILE   B HG21 1 
ATOM   5062 H HG22 . ILE   B 1 69  ? 49.468 -10.815 13.156  1.00 18.17 ?  69  ILE   B HG22 1 
ATOM   5063 H HG23 . ILE   B 1 69  ? 47.947 -11.111 12.794  1.00 18.17 ?  69  ILE   B HG23 1 
ATOM   5064 H HD11 . ILE   B 1 69  ? 46.956 -13.216 9.739   1.00 17.60 ?  69  ILE   B HD11 1 
ATOM   5065 H HD12 . ILE   B 1 69  ? 47.000 -12.791 11.268  1.00 17.60 ?  69  ILE   B HD12 1 
ATOM   5066 H HD13 . ILE   B 1 69  ? 46.640 -11.717 10.154  1.00 17.60 ?  69  ILE   B HD13 1 
ATOM   5067 N N    . ALA   B 1 70  ? 50.027 -8.027  11.798  1.00 13.49 ?  70  ALA   B N    1 
ATOM   5068 C CA   . ALA   B 1 70  ? 50.323 -6.987  12.777  1.00 13.29 ?  70  ALA   B CA   1 
ATOM   5069 C C    . ALA   B 1 70  ? 49.330 -5.838  12.678  1.00 13.97 ?  70  ALA   B C    1 
ATOM   5070 O O    . ALA   B 1 70  ? 48.942 -5.259  13.695  1.00 14.08 ?  70  ALA   B O    1 
ATOM   5071 C CB   . ALA   B 1 70  ? 51.750 -6.476  12.586  1.00 14.38 ?  70  ALA   B CB   1 
ATOM   5072 H H    . ALA   B 1 70  ? 50.665 -8.212  11.259  1.00 16.17 ?  70  ALA   B H    1 
ATOM   5073 H HA   . ALA   B 1 70  ? 50.259 -7.364  13.668  1.00 15.93 ?  70  ALA   B HA   1 
ATOM   5074 H HB1  . ALA   B 1 70  ? 51.945 -5.811  13.267  1.00 17.23 ?  70  ALA   B HB1  1 
ATOM   5075 H HB2  . ALA   B 1 70  ? 52.370 -7.221  12.673  1.00 17.23 ?  70  ALA   B HB2  1 
ATOM   5076 H HB3  . ALA   B 1 70  ? 51.835 -6.082  11.704  1.00 17.23 ?  70  ALA   B HB3  1 
ATOM   5077 N N    . THR   B 1 71  ? 48.908 -5.494  11.465  1.00 14.57 ?  71  THR   B N    1 
ATOM   5078 C CA   . THR   B 1 71  ? 47.986 -4.378  11.279  1.00 15.65 ?  71  THR   B CA   1 
ATOM   5079 C C    . THR   B 1 71  ? 46.529 -4.776  11.506  1.00 15.88 ?  71  THR   B C    1 
ATOM   5080 O O    . THR   B 1 71  ? 45.749 -3.990  12.062  1.00 17.47 ?  71  THR   B O    1 
ATOM   5081 C CB   . THR   B 1 71  ? 48.176 -3.789  9.879   1.00 17.70 ?  71  THR   B CB   1 
ATOM   5082 O OG1  . THR   B 1 71  ? 49.490 -3.227  9.769   1.00 20.34 ?  71  THR   B OG1  1 
ATOM   5083 C CG2  . THR   B 1 71  ? 47.125 -2.723  9.580   1.00 18.84 ?  71  THR   B CG2  1 
ATOM   5084 H H    . THR   B 1 71  ? 49.138 -5.892  10.739  1.00 17.46 ?  71  THR   B H    1 
ATOM   5085 H HA   . THR   B 1 71  ? 48.200 -3.687  11.919  1.00 18.76 ?  71  THR   B HA   1 
ATOM   5086 H HB   . THR   B 1 71  ? 48.089 -4.489  9.215   1.00 21.21 ?  71  THR   B HB   1 
ATOM   5087 H HG1  . THR   B 1 71  ? 49.594 -2.875  9.010   1.00 24.39 ?  71  THR   B HG1  1 
ATOM   5088 H HG21 . THR   B 1 71  ? 47.404 -2.184  8.821   1.00 22.58 ?  71  THR   B HG21 1 
ATOM   5089 H HG22 . THR   B 1 71  ? 46.274 -3.138  9.373   1.00 22.58 ?  71  THR   B HG22 1 
ATOM   5090 H HG23 . THR   B 1 71  ? 47.015 -2.140  10.350  1.00 22.58 ?  71  THR   B HG23 1 
ATOM   5091 N N    . ASN   B 1 72  ? 46.146 -5.988  11.091  1.00 15.88 ?  72  ASN   B N    1 
ATOM   5092 C CA   . ASN   B 1 72  ? 44.746 -6.364  10.964  1.00 16.55 ?  72  ASN   B CA   1 
ATOM   5093 C C    . ASN   B 1 72  ? 44.289 -7.461  11.918  1.00 17.06 ?  72  ASN   B C    1 
ATOM   5094 O O    . ASN   B 1 72  ? 43.079 -7.624  12.105  1.00 18.55 ?  72  ASN   B O    1 
ATOM   5095 C CB   . ASN   B 1 72  ? 44.457 -6.797  9.518   1.00 17.64 ?  72  ASN   B CB   1 
ATOM   5096 C CG   . ASN   B 1 72  ? 44.718 -5.688  8.520   1.00 18.58 ?  72  ASN   B CG   1 
ATOM   5097 O OD1  . ASN   B 1 72  ? 45.722 -5.693  7.802   1.00 20.12 ?  72  ASN   B OD1  1 
ATOM   5098 N ND2  . ASN   B 1 72  ? 43.838 -4.706  8.499   1.00 20.25 ?  72  ASN   B ND2  1 
ATOM   5099 H H    . ASN   B 1 72  ? 46.695 -6.628  10.885  1.00 19.03 ?  72  ASN   B H    1 
ATOM   5100 H HA   . ASN   B 1 72  ? 44.207 -5.584  11.143  1.00 19.83 ?  72  ASN   B HA   1 
ATOM   5101 H HB2  . ASN   B 1 72  ? 45.033 -7.548  9.288   1.00 21.14 ?  72  ASN   B HB2  1 
ATOM   5102 H HB3  . ASN   B 1 72  ? 43.530 -7.054  9.440   1.00 21.14 ?  72  ASN   B HB3  1 
ATOM   5103 H HD21 . ASN   B 1 72  ? 43.938 -4.048  7.954   1.00 24.27 ?  72  ASN   B HD21 1 
ATOM   5104 H HD22 . ASN   B 1 72  ? 43.151 -4.736  9.015   1.00 24.27 ?  72  ASN   B HD22 1 
ATOM   5105 N N    . GLY   B 1 73  ? 45.205 -8.218  12.514  1.00 16.09 ?  73  GLY   B N    1 
ATOM   5106 C CA   . GLY   B 1 73  ? 44.826 -9.375  13.290  1.00 15.42 ?  73  GLY   B CA   1 
ATOM   5107 C C    . GLY   B 1 73  ? 44.468 -10.552 12.408  1.00 14.12 ?  73  GLY   B C    1 
ATOM   5108 O O    . GLY   B 1 73  ? 44.433 -10.444 11.179  1.00 14.37 ?  73  GLY   B O    1 
ATOM   5109 H H    . GLY   B 1 73  ? 46.052 -8.087  12.472  1.00 19.29 ?  73  GLY   B H    1 
ATOM   5110 H HA2  . GLY   B 1 73  ? 45.560 -9.634  13.868  1.00 18.48 ?  73  GLY   B HA2  1 
ATOM   5111 H HA3  . GLY   B 1 73  ? 44.058 -9.158  13.842  1.00 18.48 ?  73  GLY   B HA3  1 
ATOM   5112 N N    . PRO   B 1 74  ? 44.179 -11.692 13.033  1.00 14.33 ?  74  PRO   B N    1 
ATOM   5113 C CA   . PRO   B 1 74  ? 43.921 -12.916 12.271  1.00 13.59 ?  74  PRO   B CA   1 
ATOM   5114 C C    . PRO   B 1 74  ? 42.611 -12.849 11.501  1.00 12.94 ?  74  PRO   B C    1 
ATOM   5115 O O    . PRO   B 1 74  ? 41.680 -12.104 11.832  1.00 14.64 ?  74  PRO   B O    1 
ATOM   5116 C CB   . PRO   B 1 74  ? 43.864 -13.999 13.357  1.00 14.81 ?  74  PRO   B CB   1 
ATOM   5117 C CG   . PRO   B 1 74  ? 43.421 -13.274 14.583  1.00 16.00 ?  74  PRO   B CG   1 
ATOM   5118 C CD   . PRO   B 1 74  ? 44.074 -11.918 14.484  1.00 15.74 ?  74  PRO   B CD   1 
ATOM   5119 H HA   . PRO   B 1 74  ? 44.655 -13.097 11.659  1.00 16.28 ?  74  PRO   B HA   1 
ATOM   5120 H HB2  . PRO   B 1 74  ? 43.219 -14.680 13.102  1.00 17.75 ?  74  PRO   B HB2  1 
ATOM   5121 H HB3  . PRO   B 1 74  ? 44.744 -14.386 13.479  1.00 17.75 ?  74  PRO   B HB3  1 
ATOM   5122 H HG2  . PRO   B 1 74  ? 42.453 -13.191 14.580  1.00 19.18 ?  74  PRO   B HG2  1 
ATOM   5123 H HG3  . PRO   B 1 74  ? 43.724 -13.749 15.369  1.00 19.18 ?  74  PRO   B HG3  1 
ATOM   5124 H HD2  . PRO   B 1 74  ? 43.510 -11.242 14.898  1.00 18.86 ?  74  PRO   B HD2  1 
ATOM   5125 H HD3  . PRO   B 1 74  ? 44.956 -11.938 14.885  1.00 18.86 ?  74  PRO   B HD3  1 
ATOM   5126 N N    . LEU   B 1 75  ? 42.565 -13.650 10.443  1.00 12.52 ?  75  LEU   B N    1 
ATOM   5127 C CA   . LEU   B 1 75  ? 41.349 -13.852 9.678   1.00 12.78 ?  75  LEU   B CA   1 
ATOM   5128 C C    . LEU   B 1 75  ? 40.366 -14.705 10.478  1.00 13.36 ?  75  LEU   B C    1 
ATOM   5129 O O    . LEU   B 1 75  ? 40.708 -15.291 11.502  1.00 14.59 ?  75  LEU   B O    1 
ATOM   5130 C CB   . LEU   B 1 75  ? 41.669 -14.566 8.361   1.00 12.91 ?  75  LEU   B CB   1 
ATOM   5131 C CG   . LEU   B 1 75  ? 42.512 -13.801 7.333   1.00 15.14 ?  75  LEU   B CG   1 
ATOM   5132 C CD1  . LEU   B 1 75  ? 42.697 -14.612 6.054   1.00 16.59 ?  75  LEU   B CD1  1 
ATOM   5133 C CD2  . LEU   B 1 75  ? 41.915 -12.460 7.011   1.00 18.51 ?  75  LEU   B CD2  1 
ATOM   5134 H H    . LEU   B 1 75  ? 43.234 -14.098 10.143  1.00 15.00 ?  75  LEU   B H    1 
ATOM   5135 H HA   . LEU   B 1 75  ? 40.930 -13.002 9.477   1.00 15.31 ?  75  LEU   B HA   1 
ATOM   5136 H HB2  . LEU   B 1 75  ? 42.150 -15.385 8.565   1.00 15.47 ?  75  LEU   B HB2  1 
ATOM   5137 H HB3  . LEU   B 1 75  ? 40.832 -14.795 7.922   1.00 15.47 ?  75  LEU   B HB3  1 
ATOM   5138 H HG   . LEU   B 1 75  ? 43.393 -13.648 7.709   1.00 18.14 ?  75  LEU   B HG   1 
ATOM   5139 H HD11 . LEU   B 1 75  ? 43.244 -14.100 5.430   1.00 19.89 ?  75  LEU   B HD11 1 
ATOM   5140 H HD12 . LEU   B 1 75  ? 43.142 -15.447 6.267   1.00 19.89 ?  75  LEU   B HD12 1 
ATOM   5141 H HD13 . LEU   B 1 75  ? 41.830 -14.788 5.659   1.00 19.89 ?  75  LEU   B HD13 1 
ATOM   5142 H HD21 . LEU   B 1 75  ? 42.403 -12.065 6.272   1.00 22.19 ?  75  LEU   B HD21 1 
ATOM   5143 H HD22 . LEU   B 1 75  ? 40.985 -12.580 6.769   1.00 22.19 ?  75  LEU   B HD22 1 
ATOM   5144 H HD23 . LEU   B 1 75  ? 41.983 -11.889 7.794   1.00 22.19 ?  75  LEU   B HD23 1 
ATOM   5145 N N    . LYS   B 1 76  ? 39.129 -14.777 9.978   1.00 15.33 ?  76  LYS   B N    1 
ATOM   5146 C CA   . LYS   B 1 76  ? 38.139 -15.734 10.449  1.00 16.46 ?  76  LYS   B CA   1 
ATOM   5147 C C    . LYS   B 1 76  ? 38.244 -17.006 9.613   1.00 14.69 ?  76  LYS   B C    1 
ATOM   5148 O O    . LYS   B 1 76  ? 38.529 -16.947 8.416   1.00 14.37 ?  76  LYS   B O    1 
ATOM   5149 C CB   . LYS   B 1 76  ? 36.723 -15.169 10.255  1.00 18.58 ?  76  LYS   B CB   1 
ATOM   5150 C CG   . LYS   B 1 76  ? 36.448 -13.797 10.894  1.00 20.54 ?  76  LYS   B CG   1 
ATOM   5151 C CD   . LYS   B 1 76  ? 35.051 -13.255 10.529  1.00 21.50 ?  76  LYS   B CD   1 
ATOM   5152 C CE   . LYS   B 1 76  ? 34.789 -11.893 11.160  1.00 23.75 ?  76  LYS   B CE   1 
ATOM   5153 N NZ   . LYS   B 1 76  ? 33.507 -11.277 10.716  1.00 24.41 ?  76  LYS   B NZ   1 
ATOM   5154 H H    . LYS   B 1 76  ? 38.839 -14.277 9.341   1.00 18.38 ?  76  LYS   B H    1 
ATOM   5155 H HA   . LYS   B 1 76  ? 38.285 -15.951 11.384  1.00 19.73 ?  76  LYS   B HA   1 
ATOM   5156 H HB2  . LYS   B 1 76  ? 36.560 -15.084 9.302   1.00 22.27 ?  76  LYS   B HB2  1 
ATOM   5157 H HB3  . LYS   B 1 76  ? 36.090 -15.798 10.635  1.00 22.27 ?  76  LYS   B HB3  1 
ATOM   5158 H HG2  . LYS   B 1 76  ? 36.499 -13.879 11.858  1.00 24.62 ?  76  LYS   B HG2  1 
ATOM   5159 H HG3  . LYS   B 1 76  ? 37.111 -13.161 10.578  1.00 24.62 ?  76  LYS   B HG3  1 
ATOM   5160 H HD2  . LYS   B 1 76  ? 34.987 -13.161 9.564   1.00 25.77 ?  76  LYS   B HD2  1 
ATOM   5161 H HD3  . LYS   B 1 76  ? 34.376 -13.873 10.849  1.00 25.77 ?  76  LYS   B HD3  1 
ATOM   5162 H HE2  . LYS   B 1 76  ? 34.756 -11.994 12.122  1.00 28.47 ?  76  LYS   B HE2  1 
ATOM   5163 H HE3  . LYS   B 1 76  ? 35.510 -11.291 10.915  1.00 28.47 ?  76  LYS   B HE3  1 
ATOM   5164 H HZ1  . LYS   B 1 76  ? 33.396 -10.483 11.108  1.00 29.26 ?  76  LYS   B HZ1  1 
ATOM   5165 H HZ2  . LYS   B 1 76  ? 33.510 -11.160 9.832   1.00 29.26 ?  76  LYS   B HZ2  1 
ATOM   5166 H HZ3  . LYS   B 1 76  ? 32.821 -11.802 10.934  1.00 29.26 ?  76  LYS   B HZ3  1 
ATOM   5167 N N    . VAL   B 1 77  ? 38.002 -18.162 10.243  1.00 15.61 ?  77  VAL   B N    1 
ATOM   5168 C CA   . VAL   B 1 77  ? 37.797 -19.374 9.458   1.00 15.64 ?  77  VAL   B CA   1 
ATOM   5169 C C    . VAL   B 1 77  ? 36.606 -19.143 8.542   1.00 14.36 ?  77  VAL   B C    1 
ATOM   5170 O O    . VAL   B 1 77  ? 35.546 -18.689 8.987   1.00 14.53 ?  77  VAL   B O    1 
ATOM   5171 C CB   . VAL   B 1 77  ? 37.597 -20.597 10.368  1.00 17.66 ?  77  VAL   B CB   1 
ATOM   5172 C CG1  . VAL   B 1 77  ? 37.337 -21.839 9.524   1.00 17.86 ?  77  VAL   B CG1  1 
ATOM   5173 C CG2  . VAL   B 1 77  ? 38.818 -20.808 11.268  1.00 19.06 ?  77  VAL   B CG2  1 
ATOM   5174 H H    . VAL   B 1 77  ? 37.953 -18.267 11.093  1.00 18.71 ?  77  VAL   B H    1 
ATOM   5175 H HA   . VAL   B 1 77  ? 38.571 -19.534 8.903   1.00 18.75 ?  77  VAL   B HA   1 
ATOM   5176 H HB   . VAL   B 1 77  ? 36.821 -20.453 10.934  1.00 21.17 ?  77  VAL   B HB   1 
ATOM   5177 H HG11 . VAL   B 1 77  ? 37.382 -22.622 10.096  1.00 21.41 ?  77  VAL   B HG11 1 
ATOM   5178 H HG12 . VAL   B 1 77  ? 36.454 -21.776 9.124   1.00 21.41 ?  77  VAL   B HG12 1 
ATOM   5179 H HG13 . VAL   B 1 77  ? 38.011 -21.897 8.831   1.00 21.41 ?  77  VAL   B HG13 1 
ATOM   5180 H HG21 . VAL   B 1 77  ? 38.686 -21.612 11.792  1.00 22.84 ?  77  VAL   B HG21 1 
ATOM   5181 H HG22 . VAL   B 1 77  ? 39.605 -20.897 10.711  1.00 22.84 ?  77  VAL   B HG22 1 
ATOM   5182 H HG23 . VAL   B 1 77  ? 38.909 -20.041 11.854  1.00 22.84 ?  77  VAL   B HG23 1 
ATOM   5183 N N    . GLY   B 1 78  ? 36.787 -19.414 7.250   1.00 13.62 ?  78  GLY   B N    1 
ATOM   5184 C CA   . GLY   B 1 78  ? 35.812 -19.089 6.233   1.00 12.77 ?  78  GLY   B CA   1 
ATOM   5185 C C    . GLY   B 1 78  ? 36.064 -17.772 5.530   1.00 12.57 ?  78  GLY   B C    1 
ATOM   5186 O O    . GLY   B 1 78  ? 35.384 -17.484 4.541   1.00 13.28 ?  78  GLY   B O    1 
ATOM   5187 H H    . GLY   B 1 78  ? 37.485 -19.803 6.935   1.00 16.32 ?  78  GLY   B H    1 
ATOM   5188 H HA2  . GLY   B 1 78  ? 35.801 -19.784 5.562   1.00 15.31 ?  78  GLY   B HA2  1 
ATOM   5189 H HA3  . GLY   B 1 78  ? 34.930 -19.044 6.638   1.00 15.31 ?  78  GLY   B HA3  1 
ATOM   5190 N N    . GLY   B 1 79  ? 37.014 -16.966 6.018   1.00 13.00 ?  79  GLY   B N    1 
ATOM   5191 C CA   . GLY   B 1 79  ? 37.313 -15.673 5.437   1.00 12.68 ?  79  GLY   B CA   1 
ATOM   5192 C C    . GLY   B 1 79  ? 38.558 -15.695 4.558   1.00 11.98 ?  79  GLY   B C    1 
ATOM   5193 O O    . GLY   B 1 79  ? 39.175 -16.730 4.319   1.00 12.68 ?  79  GLY   B O    1 
ATOM   5194 H H    . GLY   B 1 79  ? 37.506 -17.156 6.691   1.00 15.57 ?  79  GLY   B H    1 
ATOM   5195 H HA2  . GLY   B 1 79  ? 36.562 -15.375 4.896   1.00 15.19 ?  79  GLY   B HA2  1 
ATOM   5196 H HA3  . GLY   B 1 79  ? 37.458 -15.026 6.141   1.00 15.19 ?  79  GLY   B HA3  1 
ATOM   5197 N N    . SER   B 1 80  ? 38.923 -14.507 4.070   1.00 12.14 ?  80  SER   B N    1 
ATOM   5198 C CA   . SER   B 1 80  ? 40.035 -14.376 3.140   1.00 12.14 ?  80  SER   B CA   1 
ATOM   5199 C C    . SER   B 1 80  ? 40.612 -12.969 3.200   1.00 12.12 ?  80  SER   B C    1 
ATOM   5200 O O    . SER   B 1 80  ? 39.990 -12.033 3.709   1.00 13.27 ?  80  SER   B O    1 
ATOM   5201 C CB   . SER   B 1 80  ? 39.601 -14.665 1.701   1.00 12.44 ?  80  SER   B CB   1 
ATOM   5202 O OG   . SER   B 1 80  ? 38.756 -13.643 1.211   1.00 13.42 ?  80  SER   B OG   1 
ATOM   5203 H H    . SER   B 1 80  ? 38.540 -13.764 4.262   1.00 14.54 ?  80  SER   B H    1 
ATOM   5204 H HA   . SER   B 1 80  ? 40.726 -15.008 3.390   1.00 14.55 ?  80  SER   B HA   1 
ATOM   5205 H HB2  . SER   B 1 80  ? 40.391 -14.711 1.134   1.00 14.90 ?  80  SER   B HB2  1 
ATOM   5206 H HB3  . SER   B 1 80  ? 39.129 -15.512 1.673   1.00 14.90 ?  80  SER   B HB3  1 
ATOM   5207 H HG   . SER   B 1 80  ? 38.060 -13.594 1.691   1.00 16.09 ?  80  SER   B HG   1 
ATOM   5208 N N    . CYS   B 1 81  ? 41.804 -12.827 2.626   1.00 11.89 ?  81  CYS   B N    1 
ATOM   5209 C CA   . CYS   B 1 81  ? 42.353 -11.515 2.313   1.00 11.96 ?  81  CYS   B CA   1 
ATOM   5210 C C    . CYS   B 1 81  ? 43.126 -11.597 1.007   1.00 11.25 ?  81  CYS   B C    1 
ATOM   5211 O O    . CYS   B 1 81  ? 43.642 -12.658 0.640   1.00 12.06 ?  81  CYS   B O    1 
ATOM   5212 C CB   . CYS   B 1 81  ? 43.247 -10.957 3.432   1.00 12.95 ?  81  CYS   B CB   1 
ATOM   5213 S SG   . CYS   B 1 81  ? 44.764 -11.899 3.691   1.00 13.15 ?  81  CYS   B SG   1 
ATOM   5214 H H    . CYS   B 1 81  ? 42.318 -13.483 2.403   1.00 14.25 ?  81  CYS   B H    1 
ATOM   5215 H HA   . CYS   B 1 81  ? 41.619 -10.894 2.183   1.00 14.32 ?  81  CYS   B HA   1 
ATOM   5216 H HB2  . CYS   B 1 81  ? 43.499 -10.047 3.209   1.00 15.51 ?  81  CYS   B HB2  1 
ATOM   5217 H HB3  . CYS   B 1 81  ? 42.744 -10.960 4.265   1.00 15.51 ?  81  CYS   B HB3  1 
ATOM   5218 H HG   . CYS   B 1 81  ? 45.385 -11.389 4.589   1.00 15.76 ?  81  CYS   B HG   1 
ATOM   5219 N N    . VAL   B 1 82  ? 43.235 -10.453 0.331   1.00 11.53 ?  82  VAL   B N    1 
ATOM   5220 C CA   . VAL   B 1 82  ? 44.009 -10.331 -0.902  1.00 11.62 ?  82  VAL   B CA   1 
ATOM   5221 C C    . VAL   B 1 82  ? 45.350 -9.689  -0.579  1.00 12.22 ?  82  VAL   B C    1 
ATOM   5222 O O    . VAL   B 1 82  ? 45.404 -8.573  -0.039  1.00 13.06 ?  82  VAL   B O    1 
ATOM   5223 C CB   . VAL   B 1 82  ? 43.268 -9.501  -1.962  1.00 12.74 ?  82  VAL   B CB   1 
ATOM   5224 C CG1  . VAL   B 1 82  ? 44.118 -9.354  -3.218  1.00 14.16 ?  82  VAL   B CG1  1 
ATOM   5225 C CG2  . VAL   B 1 82  ? 41.926 -10.117 -2.288  1.00 13.61 ?  82  VAL   B CG2  1 
ATOM   5226 H H    . VAL   B 1 82  ? 42.854 -9.715  0.567   1.00 13.81 ?  82  VAL   B H    1 
ATOM   5227 H HA   . VAL   B 1 82  ? 44.173 -11.213 -1.266  1.00 13.92 ?  82  VAL   B HA   1 
ATOM   5228 H HB   . VAL   B 1 82  ? 43.108 -8.615  -1.611  1.00 15.26 ?  82  VAL   B HB   1 
ATOM   5229 H HG11 . VAL   B 1 82  ? 43.559 -9.033  -3.942  1.00 16.96 ?  82  VAL   B HG11 1 
ATOM   5230 H HG12 . VAL   B 1 82  ? 44.832 -8.718  -3.046  1.00 16.96 ?  82  VAL   B HG12 1 
ATOM   5231 H HG13 . VAL   B 1 82  ? 44.494 -10.218 -3.450  1.00 16.96 ?  82  VAL   B HG13 1 
ATOM   5232 H HG21 . VAL   B 1 82  ? 41.495 -9.597  -2.986  1.00 16.30 ?  82  VAL   B HG21 1 
ATOM   5233 H HG22 . VAL   B 1 82  ? 42.056 -11.031 -2.594  1.00 16.30 ?  82  VAL   B HG22 1 
ATOM   5234 H HG23 . VAL   B 1 82  ? 41.371 -10.116 -1.490  1.00 16.30 ?  82  VAL   B HG23 1 
ATOM   5235 N N    . LEU   B 1 83  ? 46.428 -10.376 -0.948  1.00 11.44 ?  83  LEU   B N    1 
ATOM   5236 C CA   . LEU   B 1 83  ? 47.784 -9.859  -0.830  1.00 11.36 ?  83  LEU   B CA   1 
ATOM   5237 C C    . LEU   B 1 83  ? 48.486 -10.001 -2.180  1.00 11.28 ?  83  LEU   B C    1 
ATOM   5238 O O    . LEU   B 1 83  ? 47.891 -10.426 -3.172  1.00 11.67 ?  83  LEU   B O    1 
ATOM   5239 C CB   . LEU   B 1 83  ? 48.539 -10.541 0.321   1.00 11.95 ?  83  LEU   B CB   1 
ATOM   5240 C CG   . LEU   B 1 83  ? 48.025 -10.178 1.719   1.00 13.25 ?  83  LEU   B CG   1 
ATOM   5241 C CD1  . LEU   B 1 83  ? 48.646 -11.038 2.803   1.00 13.90 ?  83  LEU   B CD1  1 
ATOM   5242 C CD2  . LEU   B 1 83  ? 48.222 -8.684  2.031   1.00 14.45 ?  83  LEU   B CD2  1 
ATOM   5243 H H    . LEU   B 1 83  ? 46.392 -11.176 -1.278  1.00 13.70 ?  83  LEU   B H    1 
ATOM   5244 H HA   . LEU   B 1 83  ? 47.732 -8.917  -0.633  1.00 13.61 ?  83  LEU   B HA   1 
ATOM   5245 H HB2  . LEU   B 1 83  ? 48.463 -11.501 0.220   1.00 14.31 ?  83  LEU   B HB2  1 
ATOM   5246 H HB3  . LEU   B 1 83  ? 49.473 -10.280 0.272   1.00 14.31 ?  83  LEU   B HB3  1 
ATOM   5247 H HG   . LEU   B 1 83  ? 47.074 -10.345 1.737   1.00 15.87 ?  83  LEU   B HG   1 
ATOM   5248 H HD11 . LEU   B 1 83  ? 48.283 -10.774 3.665   1.00 16.65 ?  83  LEU   B HD11 1 
ATOM   5249 H HD12 . LEU   B 1 83  ? 48.429 -11.970 2.630   1.00 16.65 ?  83  LEU   B HD12 1 
ATOM   5250 H HD13 . LEU   B 1 83  ? 49.607 -10.918 2.800   1.00 16.65 ?  83  LEU   B HD13 1 
ATOM   5251 H HD21 . LEU   B 1 83  ? 48.031 -8.528  2.969   1.00 17.32 ?  83  LEU   B HD21 1 
ATOM   5252 H HD22 . LEU   B 1 83  ? 49.137 -8.433  1.832   1.00 17.32 ?  83  LEU   B HD22 1 
ATOM   5253 H HD23 . LEU   B 1 83  ? 47.611 -8.163  1.481   1.00 17.32 ?  83  LEU   B HD23 1 
ATOM   5254 N N    . SER   B 1 84  ? 49.763 -9.624  -2.233  1.00 12.39 ?  84  SER   B N    1 
ATOM   5255 C CA   . SER   B 1 84  ? 50.499 -9.759  -3.481  1.00 12.44 ?  84  SER   B CA   1 
ATOM   5256 C C    . SER   B 1 84  ? 50.667 -11.225 -3.873  1.00 11.24 ?  84  SER   B C    1 
ATOM   5257 O O    . SER   B 1 84  ? 50.790 -12.111 -3.028  1.00 11.82 ?  84  SER   B O    1 
ATOM   5258 C CB   . SER   B 1 84  ? 51.889 -9.139  -3.350  1.00 14.36 ?  84  SER   B CB   1 
ATOM   5259 O OG   . SER   B 1 84  ? 52.628 -9.364  -4.537  1.00 16.06 ?  84  SER   B OG   1 
ATOM   5260 H H    . SER   B 1 84  ? 50.206 -9.286  -1.582  1.00 14.85 ?  84  SER   B H    1 
ATOM   5261 H HA   . SER   B 1 84  ? 50.025 -9.306  -4.193  1.00 14.90 ?  84  SER   B HA   1 
ATOM   5262 H HB2  . SER   B 1 84  ? 51.800 -8.183  -3.202  1.00 17.21 ?  84  SER   B HB2  1 
ATOM   5263 H HB3  . SER   B 1 84  ? 52.356 -9.548  -2.604  1.00 17.21 ?  84  SER   B HB3  1 
ATOM   5264 H HG   . SER   B 1 84  ? 53.398 -9.013  -4.467  1.00 19.25 ?  84  SER   B HG   1 
ATOM   5265 N N    . GLY   B 1 85  ? 50.735 -11.462 -5.174  1.00 12.77 ?  85  GLY   B N    1 
ATOM   5266 C CA   . GLY   B 1 85  ? 51.087 -12.758 -5.703  1.00 13.78 ?  85  GLY   B CA   1 
ATOM   5267 C C    . GLY   B 1 85  ? 52.559 -12.941 -6.011  1.00 12.74 ?  85  GLY   B C    1 
ATOM   5268 O O    . GLY   B 1 85  ? 52.944 -14.018 -6.466  1.00 13.31 ?  85  GLY   B O    1 
ATOM   5269 H H    . GLY   B 1 85  ? 50.577 -10.882 -5.782  1.00 15.30 ?  85  GLY   B H    1 
ATOM   5270 H HA2  . GLY   B 1 85  ? 50.832 -13.447 -5.066  1.00 16.51 ?  85  GLY   B HA2  1 
ATOM   5271 H HA3  . GLY   B 1 85  ? 50.596 -12.917 -6.523  1.00 16.51 ?  85  GLY   B HA3  1 
ATOM   5272 N N    . HIS   B 1 86  ? 53.409 -11.936 -5.791  1.00 12.55 ?  86  HIS   B N    1 
ATOM   5273 C CA   . HIS   B 1 86  ? 54.877 -12.085 -5.881  1.00 12.53 ?  86  HIS   B CA   1 
ATOM   5274 C C    . HIS   B 1 86  ? 55.250 -12.604 -7.268  1.00 12.96 ?  86  HIS   B C    1 
ATOM   5275 O O    . HIS   B 1 86  ? 54.850 -11.998 -8.274  1.00 13.98 ?  86  HIS   B O    1 
ATOM   5276 C CB   . HIS   B 1 86  ? 55.382 -12.913 -4.704  1.00 12.89 ?  86  HIS   B CB   1 
ATOM   5277 C CG   . HIS   B 1 86  ? 55.051 -12.312 -3.381  1.00 13.46 ?  86  HIS   B CG   1 
ATOM   5278 N ND1  . HIS   B 1 86  ? 55.864 -11.391 -2.760  1.00 15.07 ?  86  HIS   B ND1  1 
ATOM   5279 C CD2  . HIS   B 1 86  ? 53.967 -12.462 -2.583  1.00 13.97 ?  86  HIS   B CD2  1 
ATOM   5280 C CE1  . HIS   B 1 86  ? 55.300 -11.008 -1.629  1.00 14.93 ?  86  HIS   B CE1  1 
ATOM   5281 N NE2  . HIS   B 1 86  ? 54.144 -11.635 -1.502  1.00 14.44 ?  86  HIS   B NE2  1 
ATOM   5282 H H    . HIS   B 1 86  ? 53.165 -11.139 -5.580  1.00 15.03 ?  86  HIS   B H    1 
ATOM   5283 H HA   . HIS   B 1 86  ? 55.278 -11.210 -5.792  1.00 15.01 ?  86  HIS   B HA   1 
ATOM   5284 H HB2  . HIS   B 1 86  ? 54.987 -13.798 -4.742  1.00 15.44 ?  86  HIS   B HB2  1 
ATOM   5285 H HB3  . HIS   B 1 86  ? 56.352 -12.986 -4.760  1.00 15.44 ?  86  HIS   B HB3  1 
ATOM   5286 H HD2  . HIS   B 1 86  ? 53.230 -13.014 -2.745  1.00 16.75 ?  86  HIS   B HD2  1 
ATOM   5287 H HE1  . HIS   B 1 86  ? 55.658 -10.410 -1.019  1.00 17.89 ?  86  HIS   B HE1  1 
ATOM   5288 H HE2  . HIS   B 1 86  ? 53.600 -11.562 -0.837  1.00 17.31 ?  86  HIS   B HE2  1 
ATOM   5289 N N    . ASN   B 1 87  ? 56.019 -13.688 -7.372  1.00 13.37 ?  87  ASN   B N    1 
ATOM   5290 C CA   . ASN   B 1 87  ? 56.419 -14.264 -8.646  1.00 14.15 ?  87  ASN   B CA   1 
ATOM   5291 C C    . ASN   B 1 87  ? 55.436 -15.310 -9.153  1.00 13.73 ?  87  ASN   B C    1 
ATOM   5292 O O    . ASN   B 1 87  ? 55.762 -16.018 -10.114 1.00 15.88 ?  87  ASN   B O    1 
ATOM   5293 C CB   . ASN   B 1 87  ? 57.814 -14.893 -8.527  1.00 15.97 ?  87  ASN   B CB   1 
ATOM   5294 C CG   . ASN   B 1 87  ? 57.873 -15.998 -7.478  1.00 16.67 ?  87  ASN   B CG   1 
ATOM   5295 O OD1  . ASN   B 1 87  ? 57.239 -15.906 -6.422  1.00 16.03 ?  87  ASN   B OD1  1 
ATOM   5296 N ND2  . ASN   B 1 87  ? 58.625 -17.066 -7.778  1.00 19.20 ?  87  ASN   B ND2  1 
ATOM   5297 H H    . ASN   B 1 87  ? 56.321 -14.124 -6.697  1.00 16.02 ?  87  ASN   B H    1 
ATOM   5298 H HA   . ASN   B 1 87  ? 56.461 -13.565 -9.309  1.00 16.95 ?  87  ASN   B HA   1 
ATOM   5299 H HB2  . ASN   B 1 87  ? 58.064 -15.276 -9.385  1.00 19.14 ?  87  ASN   B HB2  1 
ATOM   5300 H HB3  . ASN   B 1 87  ? 58.446 -14.205 -8.274  1.00 19.14 ?  87  ASN   B HB3  1 
ATOM   5301 H HD21 . ASN   B 1 87  ? 58.695 -17.717 -7.220  1.00 23.02 ?  87  ASN   B HD21 1 
ATOM   5302 H HD22 . ASN   B 1 87  ? 59.049 -17.101 -8.530  1.00 23.02 ?  87  ASN   B HD22 1 
ATOM   5303 N N    . LEU   B 1 88  ? 54.251 -15.421 -8.537  1.00 12.84 ?  88  LEU   B N    1 
ATOM   5304 C CA   . LEU   B 1 88  ? 53.270 -16.451 -8.862  1.00 13.28 ?  88  LEU   B CA   1 
ATOM   5305 C C    . LEU   B 1 88  ? 52.039 -15.931 -9.585  1.00 12.94 ?  88  LEU   B C    1 
ATOM   5306 O O    . LEU   B 1 88  ? 51.448 -16.673 -10.376 1.00 14.68 ?  88  LEU   B O    1 
ATOM   5307 C CB   . LEU   B 1 88  ? 52.804 -17.137 -7.575  1.00 14.58 ?  88  LEU   B CB   1 
ATOM   5308 C CG   . LEU   B 1 88  ? 53.943 -17.790 -6.797  1.00 16.89 ?  88  LEU   B CG   1 
ATOM   5309 C CD1  . LEU   B 1 88  ? 53.467 -18.292 -5.446  1.00 18.60 ?  88  LEU   B CD1  1 
ATOM   5310 C CD2  . LEU   B 1 88  ? 54.552 -18.914 -7.619  1.00 20.33 ?  88  LEU   B CD2  1 
ATOM   5311 H H    . LEU   B 1 88  ? 53.988 -14.889 -7.908  1.00 15.39 ?  88  LEU   B H    1 
ATOM   5312 H HA   . LEU   B 1 88  ? 53.680 -17.113 -9.425  1.00 15.91 ?  88  LEU   B HA   1 
ATOM   5313 H HB2  . LEU   B 1 88  ? 52.383 -16.482 -6.993  1.00 17.47 ?  88  LEU   B HB2  1 
ATOM   5314 H HB3  . LEU   B 1 88  ? 52.160 -17.831 -7.801  1.00 17.47 ?  88  LEU   B HB3  1 
ATOM   5315 H HG   . LEU   B 1 88  ? 54.631 -17.127 -6.642  1.00 20.24 ?  88  LEU   B HG   1 
ATOM   5316 H HD11 . LEU   B 1 88  ? 54.219 -18.677 -4.971  1.00 22.30 ?  88  LEU   B HD11 1 
ATOM   5317 H HD12 . LEU   B 1 88  ? 53.099 -17.549 -4.944  1.00 22.30 ?  88  LEU   B HD12 1 
ATOM   5318 H HD13 . LEU   B 1 88  ? 52.784 -18.967 -5.588  1.00 22.30 ?  88  LEU   B HD13 1 
ATOM   5319 H HD21 . LEU   B 1 88  ? 55.132 -19.437 -7.048  1.00 24.37 ?  88  LEU   B HD21 1 
ATOM   5320 H HD22 . LEU   B 1 88  ? 53.839 -19.469 -7.970  1.00 24.37 ?  88  LEU   B HD22 1 
ATOM   5321 H HD23 . LEU   B 1 88  ? 55.063 -18.529 -8.349  1.00 24.37 ?  88  LEU   B HD23 1 
ATOM   5322 N N    . ALA   B 1 89  ? 51.629 -14.698 -9.317  1.00 12.36 ?  89  ALA   B N    1 
ATOM   5323 C CA   . ALA   B 1 89  ? 50.350 -14.190 -9.786  1.00 11.95 ?  89  ALA   B CA   1 
ATOM   5324 C C    . ALA   B 1 89  ? 50.329 -12.703 -9.488  1.00 12.05 ?  89  ALA   B C    1 
ATOM   5325 O O    . ALA   B 1 89  ? 51.149 -12.201 -8.719  1.00 13.18 ?  89  ALA   B O    1 
ATOM   5326 C CB   . ALA   B 1 89  ? 49.192 -14.856 -9.054  1.00 12.21 ?  89  ALA   B CB   1 
ATOM   5327 H H    . ALA   B 1 89  ? 52.075 -14.123 -8.859  1.00 14.81 ?  89  ALA   B H    1 
ATOM   5328 H HA   . ALA   B 1 89  ? 50.254 -14.329 -10.749 1.00 14.31 ?  89  ALA   B HA   1 
ATOM   5329 H HB1  . ALA   B 1 89  ? 48.356 -14.508 -9.410  1.00 14.63 ?  89  ALA   B HB1  1 
ATOM   5330 H HB2  . ALA   B 1 89  ? 49.241 -15.811 -9.199  1.00 14.63 ?  89  ALA   B HB2  1 
ATOM   5331 H HB3  . ALA   B 1 89  ? 49.265 -14.651 -8.114  1.00 14.63 ?  89  ALA   B HB3  1 
ATOM   5332 N N    . LYS   B 1 90  ? 49.361 -11.996 -10.068 1.00 13.07 ?  90  LYS   B N    1 
ATOM   5333 C CA   . LYS   B 1 90  ? 49.182 -10.608 -9.656  1.00 13.25 ?  90  LYS   B CA   1 
ATOM   5334 C C    . LYS   B 1 90  ? 48.836 -10.535 -8.172  1.00 12.55 ?  90  LYS   B C    1 
ATOM   5335 O O    . LYS   B 1 90  ? 49.472 -9.795  -7.410  1.00 13.74 ?  90  LYS   B O    1 
ATOM   5336 C CB   . LYS   B 1 90  ? 48.134 -9.924  -10.529 1.00 14.77 ?  90  LYS   B CB   1 
ATOM   5337 C CG   . LYS   B 1 90  ? 47.807 -8.498  -10.113 1.00 14.63 ?  90  LYS   B CG   1 
ATOM   5338 C CD   . LYS   B 1 90  ? 49.003 -7.582  -10.140 1.00 16.92 ?  90  LYS   B CD   1 
ATOM   5339 C CE   . LYS   B 1 90  ? 48.524 -6.178  -9.831  1.00 18.94 ?  90  LYS   B CE   1 
ATOM   5340 N NZ   . LYS   B 1 90  ? 49.643 -5.209  -9.809  1.00 18.67 ?  90  LYS   B NZ   1 
ATOM   5341 H H    . LYS   B 1 90  ? 48.821 -12.285 -10.673 1.00 15.67 ?  90  LYS   B H    1 
ATOM   5342 H HA   . LYS   B 1 90  ? 50.019 -10.142 -9.785  1.00 15.87 ?  90  LYS   B HA   1 
ATOM   5343 H HB2  . LYS   B 1 90  ? 48.461 -9.896  -11.444 1.00 17.70 ?  90  LYS   B HB2  1 
ATOM   5344 H HB3  . LYS   B 1 90  ? 47.313 -10.439 -10.496 1.00 17.70 ?  90  LYS   B HB3  1 
ATOM   5345 H HG2  . LYS   B 1 90  ? 47.143 -8.137  -10.723 1.00 17.53 ?  90  LYS   B HG2  1 
ATOM   5346 H HG3  . LYS   B 1 90  ? 47.450 -8.502  -9.210  1.00 17.53 ?  90  LYS   B HG3  1 
ATOM   5347 H HD2  . LYS   B 1 90  ? 49.645 -7.846  -9.461  1.00 20.28 ?  90  LYS   B HD2  1 
ATOM   5348 H HD3  . LYS   B 1 90  ? 49.409 -7.585  -11.021 1.00 20.28 ?  90  LYS   B HD3  1 
ATOM   5349 H HE2  . LYS   B 1 90  ? 47.893 -5.890  -10.512 1.00 22.71 ?  90  LYS   B HE2  1 
ATOM   5350 H HE3  . LYS   B 1 90  ? 48.099 -6.161  -8.957  1.00 22.71 ?  90  LYS   B HE3  1 
ATOM   5351 H HZ1  . LYS   B 1 90  ? 49.341 -4.390  -9.629  1.00 22.38 ?  90  LYS   B HZ1  1 
ATOM   5352 H HZ2  . LYS   B 1 90  ? 50.237 -5.440  -9.189  1.00 22.38 ?  90  LYS   B HZ2  1 
ATOM   5353 H HZ3  . LYS   B 1 90  ? 50.049 -5.194  -10.604 1.00 22.38 ?  90  LYS   B HZ3  1 
ATOM   5354 N N    . HIS   B 1 91  ? 47.865 -11.344 -7.736  1.00 11.48 ?  91  HIS   B N    1 
ATOM   5355 C CA   . HIS   B 1 91  ? 47.381 -11.363 -6.367  1.00 11.41 ?  91  HIS   B CA   1 
ATOM   5356 C C    . HIS   B 1 91  ? 47.377 -12.790 -5.842  1.00 10.98 ?  91  HIS   B C    1 
ATOM   5357 O O    . HIS   B 1 91  ? 47.152 -13.740 -6.597  1.00 11.44 ?  91  HIS   B O    1 
ATOM   5358 C CB   . HIS   B 1 91  ? 45.918 -10.893 -6.278  1.00 12.97 ?  91  HIS   B CB   1 
ATOM   5359 C CG   . HIS   B 1 91  ? 45.712 -9.478  -6.696  1.00 16.69 ?  91  HIS   B CG   1 
ATOM   5360 N ND1  . HIS   B 1 91  ? 46.340 -8.415  -6.084  1.00 19.26 ?  91  HIS   B ND1  1 
ATOM   5361 C CD2  . HIS   B 1 91  ? 44.926 -8.948  -7.658  1.00 19.21 ?  91  HIS   B CD2  1 
ATOM   5362 C CE1  . HIS   B 1 91  ? 45.960 -7.288  -6.662  1.00 20.33 ?  91  HIS   B CE1  1 
ATOM   5363 N NE2  . HIS   B 1 91  ? 45.093 -7.585  -7.614  1.00 20.56 ?  91  HIS   B NE2  1 
ATOM   5364 H H    . HIS   B 1 91  ? 47.452 -11.906 -8.240  1.00 13.75 ?  91  HIS   B H    1 
ATOM   5365 H HA   . HIS   B 1 91  ? 47.933 -10.798 -5.795  1.00 13.67 ?  91  HIS   B HA   1 
ATOM   5366 H HB2  . HIS   B 1 91  ? 45.376 -11.455 -6.857  1.00 15.54 ?  91  HIS   B HB2  1 
ATOM   5367 H HB3  . HIS   B 1 91  ? 45.612 -10.981 -5.361  1.00 15.54 ?  91  HIS   B HB3  1 
ATOM   5368 H HD1  . HIS   B 1 91  ? 46.900 -8.479  -5.431  1.00 23.09 ?  91  HIS   B HD1  1 
ATOM   5369 H HD2  . HIS   B 1 91  ? 44.372 -9.412  -8.241  1.00 23.03 ?  91  HIS   B HD2  1 
ATOM   5370 H HE1  . HIS   B 1 91  ? 46.247 -6.436  -6.427  1.00 24.37 ?  91  HIS   B HE1  1 
ATOM   5371 N N    . CYS   B 1 92  ? 47.570 -12.924 -4.536  1.00 10.86 ?  92  CYS   B N    1 
ATOM   5372 C CA   . CYS   B 1 92  ? 47.260 -14.158 -3.825  1.00 10.61 ?  92  CYS   B CA   1 
ATOM   5373 C C    . CYS   B 1 92  ? 46.035 -13.922 -2.951  1.00 10.25 ?  92  CYS   B C    1 
ATOM   5374 O O    . CYS   B 1 92  ? 46.035 -13.027 -2.097  1.00 11.09 ?  92  CYS   B O    1 
ATOM   5375 C CB   . CYS   B 1 92  ? 48.431 -14.617 -2.961  1.00 11.47 ?  92  CYS   B CB   1 
ATOM   5376 S SG   . CYS   B 1 92  ? 48.077 -16.161 -2.068  1.00 11.48 ?  92  CYS   B SG   1 
ATOM   5377 H H    . CYS   B 1 92  ? 47.897 -12.306 -4.029  1.00 13.00 ?  92  CYS   B H    1 
ATOM   5378 H HA   . CYS   B 1 92  ? 47.062 -14.857 -4.468  1.00 12.71 ?  92  CYS   B HA   1 
ATOM   5379 H HB2  . CYS   B 1 92  ? 49.202 -14.759 -3.525  1.00 13.74 ?  92  CYS   B HB2  1 
ATOM   5380 H HB3  . CYS   B 1 92  ? 48.618 -13.925 -2.304  1.00 13.74 ?  92  CYS   B HB3  1 
ATOM   5381 H HG   . CYS   B 1 92  ? 49.049 -16.465 -1.433  1.00 13.76 ?  92  CYS   B HG   1 
ATOM   5382 N N    . LEU   B 1 93  ? 44.997 -14.732 -3.163  1.00 10.28 ?  93  LEU   B N    1 
ATOM   5383 C CA   . LEU   B 1 93  ? 43.821 -14.751 -2.303  1.00 10.32 ?  93  LEU   B CA   1 
ATOM   5384 C C    . LEU   B 1 93  ? 44.045 -15.814 -1.230  1.00 9.85  ?  93  LEU   B C    1 
ATOM   5385 O O    . LEU   B 1 93  ? 43.991 -17.019 -1.513  1.00 10.86 ?  93  LEU   B O    1 
ATOM   5386 C CB   . LEU   B 1 93  ? 42.557 -15.046 -3.111  1.00 10.99 ?  93  LEU   B CB   1 
ATOM   5387 C CG   . LEU   B 1 93  ? 41.255 -15.059 -2.307  1.00 11.89 ?  93  LEU   B CG   1 
ATOM   5388 C CD1  . LEU   B 1 93  ? 40.896 -13.666 -1.830  1.00 12.46 ?  93  LEU   B CD1  1 
ATOM   5389 C CD2  . LEU   B 1 93  ? 40.123 -15.650 -3.123  1.00 12.13 ?  93  LEU   B CD2  1 
ATOM   5390 H H    . LEU   B 1 93  ? 44.952 -15.295 -3.822  1.00 12.31 ?  93  LEU   B H    1 
ATOM   5391 H HA   . LEU   B 1 93  ? 43.724 -13.888 -1.875  1.00 12.36 ?  93  LEU   B HA   1 
ATOM   5392 H HB2  . LEU   B 1 93  ? 42.467 -14.364 -3.798  1.00 13.16 ?  93  LEU   B HB2  1 
ATOM   5393 H HB3  . LEU   B 1 93  ? 42.650 -15.914 -3.525  1.00 13.16 ?  93  LEU   B HB3  1 
ATOM   5394 H HG   . LEU   B 1 93  ? 41.375 -15.610 -1.522  1.00 14.25 ?  93  LEU   B HG   1 
ATOM   5395 H HD11 . LEU   B 1 93  ? 40.043 -13.695 -1.375  1.00 14.92 ?  93  LEU   B HD11 1 
ATOM   5396 H HD12 . LEU   B 1 93  ? 41.586 -13.347 -1.229  1.00 14.92 ?  93  LEU   B HD12 1 
ATOM   5397 H HD13 . LEU   B 1 93  ? 40.836 -13.074 -2.603  1.00 14.92 ?  93  LEU   B HD13 1 
ATOM   5398 H HD21 . LEU   B 1 93  ? 39.312 -15.641 -2.591  1.00 14.53 ?  93  LEU   B HD21 1 
ATOM   5399 H HD22 . LEU   B 1 93  ? 39.999 -15.119 -3.925  1.00 14.53 ?  93  LEU   B HD22 1 
ATOM   5400 H HD23 . LEU   B 1 93  ? 40.352 -16.562 -3.362  1.00 14.53 ?  93  LEU   B HD23 1 
ATOM   5401 N N    . HIS   B 1 94  ? 44.311 -15.378 -0.005  1.00 10.16 ?  94  HIS   B N    1 
ATOM   5402 C CA   . HIS   B 1 94  ? 44.528 -16.284 1.115   1.00 10.41 ?  94  HIS   B CA   1 
ATOM   5403 C C    . HIS   B 1 94  ? 43.166 -16.636 1.691   1.00 10.80 ?  94  HIS   B C    1 
ATOM   5404 O O    . HIS   B 1 94  ? 42.499 -15.758 2.243   1.00 12.18 ?  94  HIS   B O    1 
ATOM   5405 C CB   . HIS   B 1 94  ? 45.400 -15.608 2.174   1.00 10.72 ?  94  HIS   B CB   1 
ATOM   5406 C CG   . HIS   B 1 94  ? 46.784 -15.306 1.711   1.00 10.76 ?  94  HIS   B CG   1 
ATOM   5407 N ND1  . HIS   B 1 94  ? 47.807 -16.225 1.796   1.00 10.88 ?  94  HIS   B ND1  1 
ATOM   5408 C CD2  . HIS   B 1 94  ? 47.292 -14.200 1.117   1.00 11.02 ?  94  HIS   B CD2  1 
ATOM   5409 C CE1  . HIS   B 1 94  ? 48.899 -15.674 1.293   1.00 11.29 ?  94  HIS   B CE1  1 
ATOM   5410 N NE2  . HIS   B 1 94  ? 48.615 -14.451 0.874   1.00 11.32 ?  94  HIS   B NE2  1 
ATOM   5411 H H    . HIS   B 1 94  ? 44.383 -14.540 0.198   1.00 12.16 ?  94  HIS   B H    1 
ATOM   5412 H HA   . HIS   B 1 94  ? 44.966 -17.090 0.803   1.00 12.47 ?  94  HIS   B HA   1 
ATOM   5413 H HB2  . HIS   B 1 94  ? 44.986 -14.773 2.430   1.00 12.84 ?  94  HIS   B HB2  1 
ATOM   5414 H HB3  . HIS   B 1 94  ? 45.463 -16.199 2.938   1.00 12.84 ?  94  HIS   B HB3  1 
ATOM   5415 H HD2  . HIS   B 1 94  ? 46.839 -13.420 0.922   1.00 13.20 ?  94  HIS   B HD2  1 
ATOM   5416 H HE1  . HIS   B 1 94  ? 49.730 -16.099 1.236   1.00 13.52 ?  94  HIS   B HE1  1 
ATOM   5417 H HE2  . HIS   B 1 94  ? 49.176 -13.917 0.510   1.00 13.56 ?  94  HIS   B HE2  1 
ATOM   5418 N N    . VAL   B 1 95  ? 42.736 -17.893 1.545   1.00 10.55 ?  95  VAL   B N    1 
ATOM   5419 C CA   . VAL   B 1 95  ? 41.407 -18.338 1.973   1.00 10.83 ?  95  VAL   B CA   1 
ATOM   5420 C C    . VAL   B 1 95  ? 41.566 -19.371 3.074   1.00 11.02 ?  95  VAL   B C    1 
ATOM   5421 O O    . VAL   B 1 95  ? 42.340 -20.323 2.922   1.00 11.57 ?  95  VAL   B O    1 
ATOM   5422 C CB   . VAL   B 1 95  ? 40.595 -18.943 0.810   1.00 11.02 ?  95  VAL   B CB   1 
ATOM   5423 C CG1  . VAL   B 1 95  ? 39.206 -19.387 1.285   1.00 12.29 ?  95  VAL   B CG1  1 
ATOM   5424 C CG2  . VAL   B 1 95  ? 40.486 -17.962 -0.335  1.00 11.21 ?  95  VAL   B CG2  1 
ATOM   5425 H H    . VAL   B 1 95  ? 43.203 -18.521 1.187   1.00 12.64 ?  95  VAL   B H    1 
ATOM   5426 H HA   . VAL   B 1 95  ? 40.910 -17.580 2.329   1.00 12.98 ?  95  VAL   B HA   1 
ATOM   5427 H HB   . VAL   B 1 95  ? 41.054 -19.725 0.485   1.00 13.20 ?  95  VAL   B HB   1 
ATOM   5428 H HG11 . VAL   B 1 95  ? 38.656 -19.597 0.507   1.00 14.72 ?  95  VAL   B HG11 1 
ATOM   5429 H HG12 . VAL   B 1 95  ? 39.290 -20.173 1.843   1.00 14.72 ?  95  VAL   B HG12 1 
ATOM   5430 H HG13 . VAL   B 1 95  ? 38.788 -18.666 1.786   1.00 14.72 ?  95  VAL   B HG13 1 
ATOM   5431 H HG21 . VAL   B 1 95  ? 39.916 -18.345 -1.021  1.00 13.43 ?  95  VAL   B HG21 1 
ATOM   5432 H HG22 . VAL   B 1 95  ? 40.104 -17.135 -0.008  1.00 13.43 ?  95  VAL   B HG22 1 
ATOM   5433 H HG23 . VAL   B 1 95  ? 41.373 -17.804 -0.692  1.00 13.43 ?  95  VAL   B HG23 1 
ATOM   5434 N N    . VAL   B 1 96  ? 40.839 -19.191 4.171   1.00 11.40 ?  96  VAL   B N    1 
ATOM   5435 C CA   . VAL   B 1 96  ? 40.912 -20.111 5.307   1.00 11.77 ?  96  VAL   B CA   1 
ATOM   5436 C C    . VAL   B 1 96  ? 39.721 -21.068 5.252   1.00 12.42 ?  96  VAL   B C    1 
ATOM   5437 O O    . VAL   B 1 96  ? 38.602 -20.714 5.631   1.00 12.86 ?  96  VAL   B O    1 
ATOM   5438 C CB   . VAL   B 1 96  ? 40.955 -19.371 6.645   1.00 12.49 ?  96  VAL   B CB   1 
ATOM   5439 C CG1  . VAL   B 1 96  ? 41.140 -20.364 7.796   1.00 13.34 ?  96  VAL   B CG1  1 
ATOM   5440 C CG2  . VAL   B 1 96  ? 42.055 -18.322 6.655   1.00 13.09 ?  96  VAL   B CG2  1 
ATOM   5441 H H    . VAL   B 1 96  ? 40.283 -18.547 4.286   1.00 13.66 ?  96  VAL   B H    1 
ATOM   5442 H HA   . VAL   B 1 96  ? 41.723 -20.641 5.235   1.00 14.10 ?  96  VAL   B HA   1 
ATOM   5443 H HB   . VAL   B 1 96  ? 40.109 -18.918 6.782   1.00 14.96 ?  96  VAL   B HB   1 
ATOM   5444 H HG11 . VAL   B 1 96  ? 41.304 -19.869 8.617   1.00 15.98 ?  96  VAL   B HG11 1 
ATOM   5445 H HG12 . VAL   B 1 96  ? 40.338 -20.899 7.891   1.00 15.98 ?  96  VAL   B HG12 1 
ATOM   5446 H HG13 . VAL   B 1 96  ? 41.901 -20.936 7.603   1.00 15.98 ?  96  VAL   B HG13 1 
ATOM   5447 H HG21 . VAL   B 1 96  ? 42.107 -17.922 7.538   1.00 15.69 ?  96  VAL   B HG21 1 
ATOM   5448 H HG22 . VAL   B 1 96  ? 42.898 -18.740 6.429   1.00 15.69 ?  96  VAL   B HG22 1 
ATOM   5449 H HG23 . VAL   B 1 96  ? 41.841 -17.634 5.999   1.00 15.69 ?  96  VAL   B HG23 1 
ATOM   5450 N N    . GLY   B 1 97  ? 39.959 -22.302 4.817   1.00 12.41 ?  97  GLY   B N    1 
ATOM   5451 C CA   . GLY   B 1 97  ? 38.976 -23.351 4.972   1.00 13.16 ?  97  GLY   B CA   1 
ATOM   5452 C C    . GLY   B 1 97  ? 39.096 -23.969 6.351   1.00 14.28 ?  97  GLY   B C    1 
ATOM   5453 O O    . GLY   B 1 97  ? 40.129 -23.835 7.018   1.00 15.08 ?  97  GLY   B O    1 
ATOM   5454 H H    . GLY   B 1 97  ? 40.691 -22.551 4.425   1.00 14.86 ?  97  GLY   B H    1 
ATOM   5455 H HA2  . GLY   B 1 97  ? 38.085 -22.975 4.853   1.00 15.76 ?  97  GLY   B HA2  1 
ATOM   5456 H HA3  . GLY   B 1 97  ? 39.113 -24.034 4.293   1.00 15.76 ?  97  GLY   B HA3  1 
ATOM   5457 N N    . PRO   B 1 98  ? 38.051 -24.658 6.810   1.00 15.06 ?  98  PRO   B N    1 
ATOM   5458 C CA   . PRO   B 1 98  ? 38.149 -25.352 8.098   1.00 16.30 ?  98  PRO   B CA   1 
ATOM   5459 C C    . PRO   B 1 98  ? 39.166 -26.481 8.053   1.00 15.96 ?  98  PRO   B C    1 
ATOM   5460 O O    . PRO   B 1 98  ? 39.267 -27.213 7.070   1.00 16.19 ?  98  PRO   B O    1 
ATOM   5461 C CB   . PRO   B 1 98  ? 36.732 -25.895 8.315   1.00 16.55 ?  98  PRO   B CB   1 
ATOM   5462 C CG   . PRO   B 1 98  ? 36.157 -26.018 6.948   1.00 16.17 ?  98  PRO   B CG   1 
ATOM   5463 C CD   . PRO   B 1 98  ? 36.727 -24.846 6.184   1.00 15.33 ?  98  PRO   B CD   1 
ATOM   5464 H HA   . PRO   B 1 98  ? 38.380 -24.730 8.798   1.00 19.53 ?  98  PRO   B HA   1 
ATOM   5465 H HB2  . PRO   B 1 98  ? 36.782 -26.763 8.752   1.00 19.84 ?  98  PRO   B HB2  1 
ATOM   5466 H HB3  . PRO   B 1 98  ? 36.223 -25.270 8.848   1.00 19.84 ?  98  PRO   B HB3  1 
ATOM   5467 H HG2  . PRO   B 1 98  ? 36.441 -26.864 6.551   1.00 19.38 ?  98  PRO   B HG2  1 
ATOM   5468 H HG3  . PRO   B 1 98  ? 35.191 -25.974 6.995   1.00 19.38 ?  98  PRO   B HG3  1 
ATOM   5469 H HD2  . PRO   B 1 98  ? 36.813 -25.069 5.239   1.00 18.37 ?  98  PRO   B HD2  1 
ATOM   5470 H HD3  . PRO   B 1 98  ? 36.175 -24.060 6.313   1.00 18.37 ?  98  PRO   B HD3  1 
ATOM   5471 N N    . ASN   B 1 99  ? 39.921 -26.617 9.140   1.00 17.07 ?  99  ASN   B N    1 
ATOM   5472 C CA   . ASN   B 1 99  ? 40.898 -27.694 9.300   1.00 18.05 ?  99  ASN   B CA   1 
ATOM   5473 C C    . ASN   B 1 99  ? 40.266 -28.778 10.172  1.00 20.21 ?  99  ASN   B C    1 
ATOM   5474 O O    . ASN   B 1 99  ? 40.181 -28.637 11.394  1.00 20.81 ?  99  ASN   B O    1 
ATOM   5475 C CB   . ASN   B 1 99  ? 42.171 -27.140 9.925   1.00 18.35 ?  99  ASN   B CB   1 
ATOM   5476 C CG   . ASN   B 1 99  ? 43.309 -28.142 9.922   1.00 19.43 ?  99  ASN   B CG   1 
ATOM   5477 O OD1  . ASN   B 1 99  ? 43.093 -29.333 10.095  1.00 20.23 ?  99  ASN   B OD1  1 
ATOM   5478 N ND2  . ASN   B 1 99  ? 44.524 -27.663 9.719   1.00 19.38 ?  99  ASN   B ND2  1 
ATOM   5479 H H    . ASN   B 1 99  ? 39.886 -26.083 9.809   1.00 20.46 ?  99  ASN   B H    1 
ATOM   5480 H HA   . ASN   B 1 99  ? 41.112 -28.079 8.435   1.00 21.64 ?  99  ASN   B HA   1 
ATOM   5481 H HB2  . ASN   B 1 99  ? 42.452 -26.362 9.428   1.00 21.99 ?  99  ASN   B HB2  1 
ATOM   5482 H HB3  . ASN   B 1 99  ? 41.983 -26.900 10.848  1.00 21.99 ?  99  ASN   B HB3  1 
ATOM   5483 H HD21 . ASN   B 1 99  ? 45.199 -28.193 9.707   1.00 23.24 ?  99  ASN   B HD21 1 
ATOM   5484 H HD22 . ASN   B 1 99  ? 44.633 -26.819 9.602   1.00 23.24 ?  99  ASN   B HD22 1 
ATOM   5485 N N    A VAL   B 1 100 ? 39.793 -29.853 9.535   0.58 22.59 ?  100 VAL   B N    1 
ATOM   5486 N N    B VAL   B 1 100 ? 39.813 -29.859 9.529   0.42 22.49 ?  100 VAL   B N    1 
ATOM   5487 C CA   A VAL   B 1 100 ? 39.174 -30.944 10.288  0.58 25.26 ?  100 VAL   B CA   1 
ATOM   5488 C CA   B VAL   B 1 100 ? 39.181 -30.959 10.254  0.42 24.92 ?  100 VAL   B CA   1 
ATOM   5489 C C    A VAL   B 1 100 ? 40.181 -31.616 11.214  0.58 25.85 ?  100 VAL   B C    1 
ATOM   5490 C C    B VAL   B 1 100 ? 40.175 -31.643 11.186  0.42 25.61 ?  100 VAL   B C    1 
ATOM   5491 O O    A VAL   B 1 100 ? 39.810 -32.129 12.278  0.58 26.52 ?  100 VAL   B O    1 
ATOM   5492 O O    B VAL   B 1 100 ? 39.786 -32.187 12.227  0.42 25.95 ?  100 VAL   B O    1 
ATOM   5493 C CB   A VAL   B 1 100 ? 38.499 -31.949 9.332   0.58 27.44 ?  100 VAL   B CB   1 
ATOM   5494 C CB   B VAL   B 1 100 ? 38.538 -31.947 9.262   0.42 26.72 ?  100 VAL   B CB   1 
ATOM   5495 C CG1  A VAL   B 1 100 ? 37.961 -33.147 10.104  0.58 28.47 ?  100 VAL   B CG1  1 
ATOM   5496 C CG1  B VAL   B 1 100 ? 37.978 -33.161 9.993   0.42 27.54 ?  100 VAL   B CG1  1 
ATOM   5497 C CG2  A VAL   B 1 100 ? 37.376 -31.270 8.563   0.58 28.01 ?  100 VAL   B CG2  1 
ATOM   5498 C CG2  B VAL   B 1 100 ? 37.443 -31.254 8.466   0.42 27.25 ?  100 VAL   B CG2  1 
ATOM   5499 H H    A VAL   B 1 100 ? 39.802 -29.963 8.681   0.58 27.08 ?  100 VAL   B H    1 
ATOM   5500 H H    B VAL   B 1 100 ? 39.854 -29.974 8.678   0.42 26.96 ?  100 VAL   B H    1 
ATOM   5501 H HA   A VAL   B 1 100 ? 38.469 -30.568 10.842  0.58 30.29 ?  100 VAL   B HA   1 
ATOM   5502 H HA   B VAL   B 1 100 ? 38.468 -30.597 10.803  0.42 29.88 ?  100 VAL   B HA   1 
ATOM   5503 H HB   A VAL   B 1 100 ? 39.154 -32.273 8.697   0.58 32.91 ?  100 VAL   B HB   1 
ATOM   5504 H HB   B VAL   B 1 100 ? 39.213 -32.260 8.641   0.42 32.04 ?  100 VAL   B HB   1 
ATOM   5505 H HG11 A VAL   B 1 100 ? 37.376 -33.659 9.522   0.58 34.13 ?  100 VAL   B HG11 1 
ATOM   5506 H HG11 B VAL   B 1 100 ? 37.413 -33.662 9.383   0.42 33.03 ?  100 VAL   B HG11 1 
ATOM   5507 H HG12 A VAL   B 1 100 ? 38.702 -33.702 10.394  0.58 34.13 ?  100 VAL   B HG12 1 
ATOM   5508 H HG12 B VAL   B 1 100 ? 38.711 -33.719 10.295  0.42 33.03 ?  100 VAL   B HG12 1 
ATOM   5509 H HG13 A VAL   B 1 100 ? 37.462 -32.831 10.874  0.58 34.13 ?  100 VAL   B HG13 1 
ATOM   5510 H HG13 B VAL   B 1 100 ? 37.455 -32.860 10.752  0.42 33.03 ?  100 VAL   B HG13 1 
ATOM   5511 H HG21 A VAL   B 1 100 ? 36.944 -31.925 7.992   0.58 33.58 ?  100 VAL   B HG21 1 
ATOM   5512 H HG21 B VAL   B 1 100 ? 37.020 -31.902 7.881   0.42 32.68 ?  100 VAL   B HG21 1 
ATOM   5513 H HG22 A VAL   B 1 100 ? 36.733 -30.909 9.195   0.58 33.58 ?  100 VAL   B HG22 1 
ATOM   5514 H HG22 B VAL   B 1 100 ? 36.789 -30.889 9.083   0.42 32.68 ?  100 VAL   B HG22 1 
ATOM   5515 H HG23 A VAL   B 1 100 ? 37.749 -30.556 8.025   0.58 33.58 ?  100 VAL   B HG23 1 
ATOM   5516 H HG23 B VAL   B 1 100 ? 37.839 -30.542 7.941   0.42 32.68 ?  100 VAL   B HG23 1 
ATOM   5517 N N    . ASN   B 1 101 ? 41.460 -31.647 10.828  1.00 26.08 ?  101 ASN   B N    1 
ATOM   5518 C CA   . ASN   B 1 101 ? 42.492 -32.188 11.711  1.00 27.48 ?  101 ASN   B CA   1 
ATOM   5519 C C    . ASN   B 1 101 ? 42.673 -31.361 12.978  1.00 29.60 ?  101 ASN   B C    1 
ATOM   5520 O O    . ASN   B 1 101 ? 43.307 -31.841 13.926  1.00 31.12 ?  101 ASN   B O    1 
ATOM   5521 C CB   . ASN   B 1 101 ? 43.829 -32.308 10.972  1.00 27.73 ?  101 ASN   B CB   1 
ATOM   5522 C CG   . ASN   B 1 101 ? 43.852 -33.465 9.988   1.00 27.19 ?  101 ASN   B CG   1 
ATOM   5523 O OD1  . ASN   B 1 101 ? 43.199 -34.480 10.199  1.00 27.90 ?  101 ASN   B OD1  1 
ATOM   5524 N ND2  . ASN   B 1 101 ? 44.602 -33.310 8.906   1.00 26.50 ?  101 ASN   B ND2  1 
ATOM   5525 H H    A ASN   B 1 101 ? 41.746 -31.381 10.061  0.58 31.27 ?  101 ASN   B H    1 
ATOM   5526 H H    B ASN   B 1 101 ? 41.754 -31.355 10.073  0.42 31.27 ?  101 ASN   B H    1 
ATOM   5527 H HA   . ASN   B 1 101 ? 42.227 -33.077 11.981  1.00 32.95 ?  101 ASN   B HA   1 
ATOM   5528 H HB2  . ASN   B 1 101 ? 43.999 -31.494 10.476  1.00 33.25 ?  101 ASN   B HB2  1 
ATOM   5529 H HB3  . ASN   B 1 101 ? 44.535 -32.454 11.622  1.00 33.25 ?  101 ASN   B HB3  1 
ATOM   5530 H HD21 . ASN   B 1 101 ? 44.646 -33.941 8.324   1.00 31.77 ?  101 ASN   B HD21 1 
ATOM   5531 H HD22 . ASN   B 1 101 ? 45.043 -32.583 8.790   1.00 31.77 ?  101 ASN   B HD22 1 
ATOM   5532 N N    . LYS   B 1 102 ? 42.148 -30.135 13.008  1.00 31.79 ?  102 LYS   B N    1 
ATOM   5533 C CA   . LYS   B 1 102 ? 42.090 -29.316 14.211  1.00 34.26 ?  102 LYS   B CA   1 
ATOM   5534 C C    . LYS   B 1 102 ? 40.692 -29.278 14.816  1.00 34.27 ?  102 LYS   B C    1 
ATOM   5535 O O    . LYS   B 1 102 ? 40.439 -28.471 15.715  1.00 34.95 ?  102 LYS   B O    1 
ATOM   5536 C CB   . LYS   B 1 102 ? 42.539 -27.886 13.904  1.00 36.93 ?  102 LYS   B CB   1 
ATOM   5537 C CG   . LYS   B 1 102 ? 43.999 -27.734 13.513  1.00 39.63 ?  102 LYS   B CG   1 
ATOM   5538 C CD   . LYS   B 1 102 ? 44.264 -26.312 13.043  1.00 42.22 ?  102 LYS   B CD   1 
ATOM   5539 C CE   . LYS   B 1 102 ? 45.738 -26.050 12.801  1.00 44.19 ?  102 LYS   B CE   1 
ATOM   5540 N NZ   . LYS   B 1 102 ? 45.963 -24.650 12.336  1.00 45.45 ?  102 LYS   B NZ   1 
ATOM   5541 H H    . LYS   B 1 102 ? 41.804 -29.748 12.322  1.00 38.12 ?  102 LYS   B H    1 
ATOM   5542 H HA   . LYS   B 1 102 ? 42.697 -29.681 14.872  1.00 41.08 ?  102 LYS   B HA   1 
ATOM   5543 H HB2  . LYS   B 1 102 ? 42.004 -27.544 13.172  1.00 44.30 ?  102 LYS   B HB2  1 
ATOM   5544 H HB3  . LYS   B 1 102 ? 42.393 -27.340 14.694  1.00 44.30 ?  102 LYS   B HB3  1 
ATOM   5545 H HG2  . LYS   B 1 102 ? 44.563 -27.915 14.281  1.00 47.53 ?  102 LYS   B HG2  1 
ATOM   5546 H HG3  . LYS   B 1 102 ? 44.206 -28.343 12.787  1.00 47.53 ?  102 LYS   B HG3  1 
ATOM   5547 H HD2  . LYS   B 1 102 ? 43.789 -26.160 12.210  1.00 50.64 ?  102 LYS   B HD2  1 
ATOM   5548 H HD3  . LYS   B 1 102 ? 43.954 -25.691 13.721  1.00 50.64 ?  102 LYS   B HD3  1 
ATOM   5549 H HE2  . LYS   B 1 102 ? 46.229 -26.180 13.628  1.00 53.00 ?  102 LYS   B HE2  1 
ATOM   5550 H HE3  . LYS   B 1 102 ? 46.065 -26.655 12.117  1.00 53.00 ?  102 LYS   B HE3  1 
ATOM   5551 H HZ1  . LYS   B 1 102 ? 46.831 -24.511 12.198  1.00 54.51 ?  102 LYS   B HZ1  1 
ATOM   5552 H HZ2  . LYS   B 1 102 ? 45.523 -24.508 11.575  1.00 54.51 ?  102 LYS   B HZ2  1 
ATOM   5553 H HZ3  . LYS   B 1 102 ? 45.672 -24.075 12.950  1.00 54.51 ?  102 LYS   B HZ3  1 
ATOM   5554 N N    . GLY   B 1 103 ? 39.774 -30.111 14.330  1.00 33.94 ?  103 GLY   B N    1 
ATOM   5555 C CA   . GLY   B 1 103 ? 38.434 -30.169 14.877  1.00 33.87 ?  103 GLY   B CA   1 
ATOM   5556 C C    . GLY   B 1 103 ? 37.504 -29.064 14.431  1.00 33.05 ?  103 GLY   B C    1 
ATOM   5557 O O    . GLY   B 1 103 ? 36.413 -28.930 14.999  1.00 33.49 ?  103 GLY   B O    1 
ATOM   5558 H H    . GLY   B 1 103 ? 39.907 -30.650 13.676  1.00 40.70 ?  103 GLY   B H    1 
ATOM   5559 H HA2  . GLY   B 1 103 ? 38.031 -31.015 14.629  1.00 40.62 ?  103 GLY   B HA2  1 
ATOM   5560 H HA3  . GLY   B 1 103 ? 38.487 -30.136 15.845  1.00 40.62 ?  103 GLY   B HA3  1 
ATOM   5561 N N    A GLU   B 1 104 ? 37.904 -28.259 13.450  0.58 32.09 ?  104 GLU   B N    1 
ATOM   5562 N N    B GLU   B 1 104 ? 37.878 -28.285 13.422  0.42 32.22 ?  104 GLU   B N    1 
ATOM   5563 C CA   A GLU   B 1 104 ? 37.083 -27.142 13.012  0.58 31.01 ?  104 GLU   B CA   1 
ATOM   5564 C CA   B GLU   B 1 104 ? 37.036 -27.188 12.971  0.42 31.21 ?  104 GLU   B CA   1 
ATOM   5565 C C    A GLU   B 1 104 ? 35.895 -27.635 12.190  0.58 31.13 ?  104 GLU   B C    1 
ATOM   5566 C C    B GLU   B 1 104 ? 35.869 -27.704 12.134  0.42 31.30 ?  104 GLU   B C    1 
ATOM   5567 O O    A GLU   B 1 104 ? 35.930 -28.709 11.583  0.58 31.40 ?  104 GLU   B O    1 
ATOM   5568 O O    B GLU   B 1 104 ? 35.935 -28.775 11.523  0.42 31.56 ?  104 GLU   B O    1 
ATOM   5569 C CB   A GLU   B 1 104 ? 37.932 -26.144 12.221  0.58 30.08 ?  104 GLU   B CB   1 
ATOM   5570 C CB   B GLU   B 1 104 ? 37.870 -26.169 12.195  0.42 30.25 ?  104 GLU   B CB   1 
ATOM   5571 C CG   A GLU   B 1 104 ? 39.033 -25.514 13.070  0.58 29.10 ?  104 GLU   B CG   1 
ATOM   5572 C CG   B GLU   B 1 104 ? 38.952 -25.536 13.060  0.42 29.29 ?  104 GLU   B CG   1 
ATOM   5573 C CD   A GLU   B 1 104 ? 39.967 -24.619 12.287  0.58 27.91 ?  104 GLU   B CD   1 
ATOM   5574 C CD   B GLU   B 1 104 ? 39.921 -24.671 12.281  0.42 28.26 ?  104 GLU   B CD   1 
ATOM   5575 O OE1  A GLU   B 1 104 ? 39.955 -24.663 11.039  0.58 26.58 ?  104 GLU   B OE1  1 
ATOM   5576 O OE1  B GLU   B 1 104 ? 39.869 -24.671 11.033  0.42 27.45 ?  104 GLU   B OE1  1 
ATOM   5577 O OE2  A GLU   B 1 104 ? 40.724 -23.867 12.934  0.58 27.65 -1 104 GLU   B OE2  1 
ATOM   5578 O OE2  B GLU   B 1 104 ? 40.741 -23.988 12.928  0.42 27.93 -1 104 GLU   B OE2  1 
ATOM   5579 H H    A GLU   B 1 104 ? 38.649 -28.336 13.031  0.58 38.48 ?  104 GLU   B H    1 
ATOM   5580 H H    B GLU   B 1 104 ? 38.615 -28.367 12.987  0.42 38.65 ?  104 GLU   B H    1 
ATOM   5581 H HA   A GLU   B 1 104 ? 36.738 -26.680 13.791  0.58 37.19 ?  104 GLU   B HA   1 
ATOM   5582 H HA   B GLU   B 1 104 ? 36.669 -26.741 13.746  0.42 37.43 ?  104 GLU   B HA   1 
ATOM   5583 H HB2  A GLU   B 1 104 ? 38.354 -26.601 11.478  0.58 36.07 ?  104 GLU   B HB2  1 
ATOM   5584 H HB2  B GLU   B 1 104 ? 38.301 -26.610 11.447  0.42 36.27 ?  104 GLU   B HB2  1 
ATOM   5585 H HB3  A GLU   B 1 104 ? 37.363 -25.429 11.893  0.58 36.07 ?  104 GLU   B HB3  1 
ATOM   5586 H HB3  B GLU   B 1 104 ? 37.288 -25.461 11.874  0.42 36.27 ?  104 GLU   B HB3  1 
ATOM   5587 H HG2  A GLU   B 1 104 ? 38.628 -24.975 13.769  0.58 34.90 ?  104 GLU   B HG2  1 
ATOM   5588 H HG2  B GLU   B 1 104 ? 38.531 -24.976 13.732  0.42 35.12 ?  104 GLU   B HG2  1 
ATOM   5589 H HG3  A GLU   B 1 104 ? 39.572 -26.215 13.467  0.58 34.90 ?  104 GLU   B HG3  1 
ATOM   5590 H HG3  B GLU   B 1 104 ? 39.463 -26.238 13.493  0.42 35.12 ?  104 GLU   B HG3  1 
ATOM   5591 N N    A ASP   B 1 105 ? 34.831 -26.836 12.187  0.58 30.82 ?  105 ASP   B N    1 
ATOM   5592 N N    B ASP   B 1 105 ? 34.788 -26.925 12.120  0.42 30.96 ?  105 ASP   B N    1 
ATOM   5593 C CA   A ASP   B 1 105 ? 33.555 -27.268 11.629  0.58 31.41 ?  105 ASP   B CA   1 
ATOM   5594 C CA   B ASP   B 1 105 ? 33.521 -27.378 11.556  0.42 31.15 ?  105 ASP   B CA   1 
ATOM   5595 C C    A ASP   B 1 105 ? 33.624 -27.315 10.108  0.58 29.65 ?  105 ASP   B C    1 
ATOM   5596 C C    B ASP   B 1 105 ? 33.592 -27.392 10.033  0.42 29.85 ?  105 ASP   B C    1 
ATOM   5597 O O    A ASP   B 1 105 ? 33.802 -26.284 9.453   0.58 28.86 ?  105 ASP   B O    1 
ATOM   5598 O O    B ASP   B 1 105 ? 33.787 -26.348 9.402   0.42 29.26 ?  105 ASP   B O    1 
ATOM   5599 C CB   A ASP   B 1 105 ? 32.452 -26.311 12.077  0.58 34.10 ?  105 ASP   B CB   1 
ATOM   5600 C CB   B ASP   B 1 105 ? 32.392 -26.465 12.029  0.42 32.68 ?  105 ASP   B CB   1 
ATOM   5601 C CG   A ASP   B 1 105 ? 31.073 -26.761 11.637  0.58 36.61 ?  105 ASP   B CG   1 
ATOM   5602 C CG   B ASP   B 1 105 ? 31.016 -27.020 11.701  0.42 34.12 ?  105 ASP   B CG   1 
ATOM   5603 O OD1  A ASP   B 1 105 ? 30.949 -27.884 11.107  0.58 37.04 ?  105 ASP   B OD1  1 
ATOM   5604 O OD1  B ASP   B 1 105 ? 30.936 -28.010 10.943  0.42 34.50 ?  105 ASP   B OD1  1 
ATOM   5605 O OD2  A ASP   B 1 105 ? 30.110 -25.983 11.816  0.58 38.00 -1 105 ASP   B OD2  1 
ATOM   5606 O OD2  B ASP   B 1 105 ? 30.014 -26.474 12.210  0.42 34.52 -1 105 ASP   B OD2  1 
ATOM   5607 H H    A ASP   B 1 105 ? 34.825 -26.036 12.505  0.58 36.96 ?  105 ASP   B H    1 
ATOM   5608 H H    B ASP   B 1 105 ? 34.765 -26.126 12.432  0.42 37.13 ?  105 ASP   B H    1 
ATOM   5609 H HA   A ASP   B 1 105 ? 33.344 -28.156 11.957  0.58 37.67 ?  105 ASP   B HA   1 
ATOM   5610 H HA   B ASP   B 1 105 ? 33.329 -28.278 11.861  0.42 37.36 ?  105 ASP   B HA   1 
ATOM   5611 H HB2  A ASP   B 1 105 ? 32.469 -26.240 13.046  0.58 40.90 ?  105 ASP   B HB2  1 
ATOM   5612 H HB2  B ASP   B 1 105 ? 32.448 -26.361 12.992  0.42 39.20 ?  105 ASP   B HB2  1 
ATOM   5613 H HB3  A ASP   B 1 105 ? 32.604 -25.443 11.677  0.58 40.90 ?  105 ASP   B HB3  1 
ATOM   5614 H HB3  B ASP   B 1 105 ? 32.483 -25.598 11.599  0.42 39.20 ?  105 ASP   B HB3  1 
ATOM   5615 N N    A ILE   B 1 106 ? 33.448 -28.515 9.547   0.58 29.07 ?  106 ILE   B N    1 
ATOM   5616 N N    B ILE   B 1 106 ? 33.412 -28.578 9.445   0.42 29.24 ?  106 ILE   B N    1 
ATOM   5617 C CA   A ILE   B 1 106 ? 33.456 -28.696 8.100   0.58 28.20 ?  106 ILE   B CA   1 
ATOM   5618 C CA   B ILE   B 1 106 ? 33.429 -28.727 7.994   0.42 28.67 ?  106 ILE   B CA   1 
ATOM   5619 C C    A ILE   B 1 106 ? 32.368 -27.875 7.418   0.58 26.86 ?  106 ILE   B C    1 
ATOM   5620 C C    B ILE   B 1 106 ? 32.342 -27.895 7.326   0.42 27.72 ?  106 ILE   B C    1 
ATOM   5621 O O    A ILE   B 1 106 ? 32.474 -27.578 6.222   0.58 26.26 ?  106 ILE   B O    1 
ATOM   5622 O O    B ILE   B 1 106 ? 32.437 -27.598 6.130   0.42 27.21 ?  106 ILE   B O    1 
ATOM   5623 C CB   A ILE   B 1 106 ? 33.345 -30.203 7.771   0.58 28.88 ?  106 ILE   B CB   1 
ATOM   5624 C CB   B ILE   B 1 106 ? 33.324 -30.226 7.627   0.42 29.16 ?  106 ILE   B CB   1 
ATOM   5625 C CG1  A ILE   B 1 106 ? 33.594 -30.461 6.284   0.58 29.11 ?  106 ILE   B CG1  1 
ATOM   5626 C CG1  B ILE   B 1 106 ? 33.639 -30.454 6.147   0.42 29.37 ?  106 ILE   B CG1  1 
ATOM   5627 C CG2  A ILE   B 1 106 ? 31.981 -30.745 8.184   0.58 29.43 ?  106 ILE   B CG2  1 
ATOM   5628 C CG2  B ILE   B 1 106 ? 31.939 -30.767 7.960   0.42 29.54 ?  106 ILE   B CG2  1 
ATOM   5629 C CD1  A ILE   B 1 106 ? 34.968 -30.045 5.821   0.58 28.79 ?  106 ILE   B CD1  1 
ATOM   5630 C CD1  B ILE   B 1 106 ? 35.022 -30.002 5.747   0.42 29.31 ?  106 ILE   B CD1  1 
ATOM   5631 H H    A ILE   B 1 106 ? 33.321 -29.239 9.991   0.58 34.85 ?  106 ILE   B H    1 
ATOM   5632 H H    B ILE   B 1 106 ? 33.281 -29.312 9.870   0.42 35.07 ?  106 ILE   B H    1 
ATOM   5633 H HA   A ILE   B 1 106 ? 34.305 -28.383 7.763   0.58 33.81 ?  106 ILE   B HA   1 
ATOM   5634 H HA   B ILE   B 1 106 ? 34.278 -28.401 7.669   0.42 34.38 ?  106 ILE   B HA   1 
ATOM   5635 H HB   A ILE   B 1 106 ? 34.022 -30.676 8.280   0.58 34.64 ?  106 ILE   B HB   1 
ATOM   5636 H HB   B ILE   B 1 106 ? 33.974 -30.715 8.155   0.42 34.96 ?  106 ILE   B HB   1 
ATOM   5637 H HG12 A ILE   B 1 106 ? 33.503 -31.413 6.114   0.58 34.90 ?  106 ILE   B HG12 1 
ATOM   5638 H HG12 B ILE   B 1 106 ? 33.574 -31.405 5.956   0.42 35.22 ?  106 ILE   B HG12 1 
ATOM   5639 H HG13 A ILE   B 1 106 ? 32.942 -29.972 5.763   0.58 34.90 ?  106 ILE   B HG13 1 
ATOM   5640 H HG13 B ILE   B 1 106 ? 32.998 -29.968 5.608   0.42 35.22 ?  106 ILE   B HG13 1 
ATOM   5641 H HG21 A ILE   B 1 106 ? 31.987 -31.711 8.098   0.58 35.29 ?  106 ILE   B HG21 1 
ATOM   5642 H HG21 B ILE   B 1 106 ? 31.954 -31.735 7.893   0.42 35.42 ?  106 ILE   B HG21 1 
ATOM   5643 H HG22 A ILE   B 1 106 ? 31.808 -30.497 9.107   0.58 35.29 ?  106 ILE   B HG22 1 
ATOM   5644 H HG22 B ILE   B 1 106 ? 31.706 -30.502 8.864   0.42 35.42 ?  106 ILE   B HG22 1 
ATOM   5645 H HG23 A ILE   B 1 106 ? 31.300 -30.366 7.607   0.58 35.29 ?  106 ILE   B HG23 1 
ATOM   5646 H HG23 B ILE   B 1 106 ? 31.296 -30.402 7.332   0.42 35.42 ?  106 ILE   B HG23 1 
ATOM   5647 H HD11 A ILE   B 1 106 ? 35.143 -30.443 4.955   0.58 34.52 ?  106 ILE   B HD11 1 
ATOM   5648 H HD11 B ILE   B 1 106 ? 35.252 -30.408 4.898   0.42 35.15 ?  106 ILE   B HD11 1 
ATOM   5649 H HD12 A ILE   B 1 106 ? 35.000 -29.077 5.752   0.58 34.52 ?  106 ILE   B HD12 1 
ATOM   5650 H HD12 B ILE   B 1 106 ? 35.025 -29.035 5.663   0.42 35.15 ?  106 ILE   B HD12 1 
ATOM   5651 H HD13 A ILE   B 1 106 ? 35.626 -30.353 6.465   0.58 34.52 ?  106 ILE   B HD13 1 
ATOM   5652 H HD13 B ILE   B 1 106 ? 35.654 -30.278 6.429   0.42 35.15 ?  106 ILE   B HD13 1 
ATOM   5653 N N    A GLN   B 1 107 ? 31.323 -27.484 8.153   0.58 27.09 ?  107 GLN   B N    1 
ATOM   5654 N N    B GLN   B 1 107 ? 31.307 -27.503 8.073   0.42 27.83 ?  107 GLN   B N    1 
ATOM   5655 C CA   A GLN   B 1 107 ? 30.246 -26.700 7.557   0.58 27.54 ?  107 GLN   B CA   1 
ATOM   5656 C CA   B GLN   B 1 107 ? 30.236 -26.696 7.500   0.42 27.99 ?  107 GLN   B CA   1 
ATOM   5657 C C    A GLN   B 1 107 ? 30.734 -25.352 7.039   0.58 25.43 ?  107 GLN   B C    1 
ATOM   5658 C C    B GLN   B 1 107 ? 30.723 -25.326 7.039   0.42 25.68 ?  107 GLN   B C    1 
ATOM   5659 O O    A GLN   B 1 107 ? 30.101 -24.780 6.147   0.58 25.86 ?  107 GLN   B O    1 
ATOM   5660 O O    B GLN   B 1 107 ? 30.073 -24.707 6.191   0.42 26.03 ?  107 GLN   B O    1 
ATOM   5661 C CB   A GLN   B 1 107 ? 29.125 -26.496 8.580   0.58 31.25 ?  107 GLN   B CB   1 
ATOM   5662 C CB   B GLN   B 1 107 ? 29.100 -26.547 8.516   0.42 31.05 ?  107 GLN   B CB   1 
ATOM   5663 C CG   A GLN   B 1 107 ? 27.810 -25.989 7.995   0.58 34.74 ?  107 GLN   B CG   1 
ATOM   5664 C CG   B GLN   B 1 107 ? 27.777 -26.069 7.928   0.42 33.94 ?  107 GLN   B CG   1 
ATOM   5665 C CD   A GLN   B 1 107 ? 27.750 -24.475 7.890   0.58 37.42 ?  107 GLN   B CD   1 
ATOM   5666 C CD   B GLN   B 1 107 ? 27.653 -24.556 7.904   0.42 36.19 ?  107 GLN   B CD   1 
ATOM   5667 O OE1  A GLN   B 1 107 ? 28.581 -23.765 8.460   0.58 38.38 ?  107 GLN   B OE1  1 
ATOM   5668 O OE1  B GLN   B 1 107 ? 28.451 -23.844 8.515   0.42 37.00 ?  107 GLN   B OE1  1 
ATOM   5669 N NE2  A GLN   B 1 107 ? 26.759 -23.973 7.159   0.58 38.32 ?  107 GLN   B NE2  1 
ATOM   5670 N NE2  B GLN   B 1 107 ? 26.643 -24.057 7.200   0.42 36.95 ?  107 GLN   B NE2  1 
ATOM   5671 H H    A GLN   B 1 107 ? 31.221 -27.649 8.989   0.58 32.49 ?  107 GLN   B H    1 
ATOM   5672 H H    B GLN   B 1 107 ? 31.202 -27.692 8.903   0.42 33.38 ?  107 GLN   B H    1 
ATOM   5673 H HA   A GLN   B 1 107 ? 29.877 -27.196 6.809   0.58 33.02 ?  107 GLN   B HA   1 
ATOM   5674 H HA   B GLN   B 1 107 ? 29.878 -27.160 6.727   0.42 33.56 ?  107 GLN   B HA   1 
ATOM   5675 H HB2  A GLN   B 1 107 ? 28.944 -27.343 9.010   0.58 37.47 ?  107 GLN   B HB2  1 
ATOM   5676 H HB2  B GLN   B 1 107 ? 28.939 -27.409 8.926   0.42 37.24 ?  107 GLN   B HB2  1 
ATOM   5677 H HB3  A GLN   B 1 107 ? 29.422 -25.851 9.241   0.58 37.47 ?  107 GLN   B HB3  1 
ATOM   5678 H HB3  B GLN   B 1 107 ? 29.370 -25.910 9.195   0.42 37.24 ?  107 GLN   B HB3  1 
ATOM   5679 H HG2  A GLN   B 1 107 ? 27.697 -26.353 7.104   0.58 41.66 ?  107 GLN   B HG2  1 
ATOM   5680 H HG2  B GLN   B 1 107 ? 27.701 -26.388 7.015   0.42 40.71 ?  107 GLN   B HG2  1 
ATOM   5681 H HG3  A GLN   B 1 107 ? 27.078 -26.282 8.565   0.58 41.66 ?  107 GLN   B HG3  1 
ATOM   5682 H HG3  B GLN   B 1 107 ? 27.046 -26.425 8.462   0.42 40.71 ?  107 GLN   B HG3  1 
ATOM   5683 H HE21 A GLN   B 1 107 ? 26.198 -24.500 6.773   0.58 45.96 ?  107 GLN   B HE21 1 
ATOM   5684 H HE21 B GLN   B 1 107 ? 26.104 -24.583 6.784   0.42 44.32 ?  107 GLN   B HE21 1 
ATOM   5685 H HE22 A GLN   B 1 107 ? 26.677 -23.121 7.071   0.58 45.96 ?  107 GLN   B HE22 1 
ATOM   5686 H HE22 B GLN   B 1 107 ? 26.527 -23.206 7.159   0.42 44.32 ?  107 GLN   B HE22 1 
ATOM   5687 N N    . LEU   B 1 108 ? 31.853 -24.843 7.562   1.00 23.29 ?  108 LEU   B N    1 
ATOM   5688 C CA   . LEU   B 1 108 ? 32.401 -23.550 7.150   1.00 19.99 ?  108 LEU   B CA   1 
ATOM   5689 C C    . LEU   B 1 108 ? 33.065 -23.580 5.781   1.00 17.40 ?  108 LEU   B C    1 
ATOM   5690 O O    . LEU   B 1 108 ? 33.512 -22.529 5.301   1.00 16.30 ?  108 LEU   B O    1 
ATOM   5691 C CB   . LEU   B 1 108 ? 33.397 -23.049 8.194   1.00 20.33 ?  108 LEU   B CB   1 
ATOM   5692 C CG   . LEU   B 1 108 ? 32.771 -22.564 9.499   1.00 21.73 ?  108 LEU   B CG   1 
ATOM   5693 C CD1  . LEU   B 1 108 ? 33.793 -22.547 10.616  1.00 21.97 ?  108 LEU   B CD1  1 
ATOM   5694 C CD2  . LEU   B 1 108 ? 32.182 -21.176 9.306   1.00 22.87 ?  108 LEU   B CD2  1 
ATOM   5695 H H    A LEU   B 1 108 ? 32.308 -25.233 8.176   0.58 27.93 ?  108 LEU   B H    1 
ATOM   5696 H H    B LEU   B 1 108 ? 32.313 -25.246 8.164   0.42 27.93 ?  108 LEU   B H    1 
ATOM   5697 H HA   . LEU   B 1 108 ? 31.674 -22.913 7.107   1.00 23.96 ?  108 LEU   B HA   1 
ATOM   5698 H HB2  . LEU   B 1 108 ? 34.001 -23.771 8.417   1.00 24.37 ?  108 LEU   B HB2  1 
ATOM   5699 H HB3  . LEU   B 1 108 ? 33.891 -22.308 7.818   1.00 24.37 ?  108 LEU   B HB3  1 
ATOM   5700 H HG   . LEU   B 1 108 ? 32.048 -23.162 9.757   1.00 26.05 ?  108 LEU   B HG   1 
ATOM   5701 H HD11 . LEU   B 1 108 ? 33.364 -22.248 11.435  1.00 26.34 ?  108 LEU   B HD11 1 
ATOM   5702 H HD12 . LEU   B 1 108 ? 34.145 -23.441 10.735  1.00 26.34 ?  108 LEU   B HD12 1 
ATOM   5703 H HD13 . LEU   B 1 108 ? 34.508 -21.935 10.378  1.00 26.34 ?  108 LEU   B HD13 1 
ATOM   5704 H HD21 . LEU   B 1 108 ? 31.808 -20.869 10.147  1.00 27.43 ?  108 LEU   B HD21 1 
ATOM   5705 H HD22 . LEU   B 1 108 ? 32.885 -20.573 9.018   1.00 27.43 ?  108 LEU   B HD22 1 
ATOM   5706 H HD23 . LEU   B 1 108 ? 31.485 -21.217 8.632   1.00 27.43 ?  108 LEU   B HD23 1 
ATOM   5707 N N    . LEU   B 1 109 ? 33.131 -24.747 5.148   1.00 15.85 ?  109 LEU   B N    1 
ATOM   5708 C CA   . LEU   B 1 109 ? 33.766 -24.865 3.844   1.00 14.88 ?  109 LEU   B CA   1 
ATOM   5709 C C    . LEU   B 1 109 ? 33.000 -24.091 2.776   1.00 14.08 ?  109 LEU   B C    1 
ATOM   5710 O O    . LEU   B 1 109 ? 33.612 -23.506 1.876   1.00 13.79 ?  109 LEU   B O    1 
ATOM   5711 C CB   . LEU   B 1 109 ? 33.892 -26.343 3.479   1.00 14.98 ?  109 LEU   B CB   1 
ATOM   5712 C CG   . LEU   B 1 109 ? 34.671 -26.699 2.216   1.00 14.87 ?  109 LEU   B CG   1 
ATOM   5713 C CD1  . LEU   B 1 109 ? 36.040 -26.046 2.204   1.00 14.80 ?  109 LEU   B CD1  1 
ATOM   5714 C CD2  . LEU   B 1 109 ? 34.827 -28.210 2.102   1.00 15.48 ?  109 LEU   B CD2  1 
ATOM   5715 H H    . LEU   B 1 109 ? 32.822 -25.486 5.452   1.00 19.00 ?  109 LEU   B H    1 
ATOM   5716 H HA   . LEU   B 1 109 ? 34.659 -24.491 3.890   1.00 17.83 ?  109 LEU   B HA   1 
ATOM   5717 H HB2  . LEU   B 1 109 ? 34.330 -26.796 4.214   1.00 17.96 ?  109 LEU   B HB2  1 
ATOM   5718 H HB3  . LEU   B 1 109 ? 32.999 -26.704 3.368   1.00 17.96 ?  109 LEU   B HB3  1 
ATOM   5719 H HG   . LEU   B 1 109 ? 34.180 -26.398 1.434   1.00 17.82 ?  109 LEU   B HG   1 
ATOM   5720 H HD11 . LEU   B 1 109 ? 36.557 -26.412 1.466   1.00 17.74 ?  109 LEU   B HD11 1 
ATOM   5721 H HD12 . LEU   B 1 109 ? 35.929 -25.093 2.089   1.00 17.74 ?  109 LEU   B HD12 1 
ATOM   5722 H HD13 . LEU   B 1 109 ? 36.485 -26.237 3.043   1.00 17.74 ?  109 LEU   B HD13 1 
ATOM   5723 H HD21 . LEU   B 1 109 ? 35.375 -28.420 1.326   1.00 18.55 ?  109 LEU   B HD21 1 
ATOM   5724 H HD22 . LEU   B 1 109 ? 35.256 -28.548 2.904   1.00 18.55 ?  109 LEU   B HD22 1 
ATOM   5725 H HD23 . LEU   B 1 109 ? 33.951 -28.618 2.002   1.00 18.55 ?  109 LEU   B HD23 1 
ATOM   5726 N N    . LYS   B 1 110 ? 31.666 -24.052 2.861   1.00 14.02 ?  110 LYS   B N    1 
ATOM   5727 C CA   . LYS   B 1 110 ? 30.912 -23.287 1.873   1.00 13.63 ?  110 LYS   B CA   1 
ATOM   5728 C C    . LYS   B 1 110 ? 31.255 -21.799 1.957   1.00 13.42 ?  110 LYS   B C    1 
ATOM   5729 O O    . LYS   B 1 110 ? 31.500 -21.150 0.934   1.00 13.47 ?  110 LYS   B O    1 
ATOM   5730 C CB   . LYS   B 1 110 ? 29.405 -23.532 2.023   1.00 14.57 ?  110 LYS   B CB   1 
ATOM   5731 C CG   . LYS   B 1 110 ? 28.600 -22.919 0.880   1.00 15.13 ?  110 LYS   B CG   1 
ATOM   5732 C CD   . LYS   B 1 110 ? 27.130 -23.347 0.903   1.00 15.38 ?  110 LYS   B CD   1 
ATOM   5733 C CE   . LYS   B 1 110 ? 26.369 -22.826 -0.321  1.00 16.16 ?  110 LYS   B CE   1 
ATOM   5734 N NZ   . LYS   B 1 110 ? 26.705 -23.546 -1.575  1.00 16.44 ?  110 LYS   B NZ   1 
ATOM   5735 H H    . LYS   B 1 110 ? 31.194 -24.448 3.454   1.00 16.80 ?  110 LYS   B H    1 
ATOM   5736 H HA   . LYS   B 1 110 ? 31.163 -23.592 0.983   1.00 16.34 ?  110 LYS   B HA   1 
ATOM   5737 H HB2  . LYS   B 1 110 ? 29.236 -24.490 2.030   1.00 17.46 ?  110 LYS   B HB2  1 
ATOM   5738 H HB3  . LYS   B 1 110 ? 29.098 -23.136 2.853   1.00 17.46 ?  110 LYS   B HB3  1 
ATOM   5739 H HG2  . LYS   B 1 110 ? 28.628 -21.955 0.953   1.00 18.14 ?  110 LYS   B HG2  1 
ATOM   5740 H HG3  . LYS   B 1 110 ? 28.979 -23.205 0.036   1.00 18.14 ?  110 LYS   B HG3  1 
ATOM   5741 H HD2  . LYS   B 1 110 ? 27.073 -24.320 0.901   1.00 18.43 ?  110 LYS   B HD2  1 
ATOM   5742 H HD3  . LYS   B 1 110 ? 26.698 -22.993 1.697   1.00 18.43 ?  110 LYS   B HD3  1 
ATOM   5743 H HE2  . LYS   B 1 110 ? 25.418 -22.925 -0.171  1.00 19.37 ?  110 LYS   B HE2  1 
ATOM   5744 H HE3  . LYS   B 1 110 ? 26.591 -21.892 -0.450  1.00 19.37 ?  110 LYS   B HE3  1 
ATOM   5745 H HZ1  . LYS   B 1 110 ? 26.247 -23.210 -2.256  1.00 19.71 ?  110 LYS   B HZ1  1 
ATOM   5746 H HZ2  . LYS   B 1 110 ? 27.579 -23.470 -1.747  1.00 19.71 ?  110 LYS   B HZ2  1 
ATOM   5747 H HZ3  . LYS   B 1 110 ? 26.509 -24.413 -1.492  1.00 19.71 ?  110 LYS   B HZ3  1 
ATOM   5748 N N    . SER   B 1 111 ? 31.279 -21.248 3.177   1.00 13.72 ?  111 SER   B N    1 
ATOM   5749 C CA   . SER   B 1 111 ? 31.670 -19.850 3.356   1.00 13.47 ?  111 SER   B CA   1 
ATOM   5750 C C    . SER   B 1 111 ? 33.050 -19.594 2.769   1.00 13.26 ?  111 SER   B C    1 
ATOM   5751 O O    . SER   B 1 111 ? 33.280 -18.565 2.120   1.00 13.59 ?  111 SER   B O    1 
ATOM   5752 C CB   . SER   B 1 111 ? 31.669 -19.497 4.842   1.00 14.99 ?  111 SER   B CB   1 
ATOM   5753 O OG   . SER   B 1 111 ? 30.367 -19.494 5.387   1.00 16.64 ?  111 SER   B OG   1 
ATOM   5754 H H    . SER   B 1 111 ? 31.090 -21.673 3.903   1.00 16.45 ?  111 SER   B H    1 
ATOM   5755 H HA   . SER   B 1 111 ? 31.032 -19.287 2.903   1.00 16.14 ?  111 SER   B HA   1 
ATOM   5756 H HB2  . SER   B 1 111 ? 32.199 -20.157 5.323   1.00 17.96 ?  111 SER   B HB2  1 
ATOM   5757 H HB3  . SER   B 1 111 ? 32.057 -18.621 4.953   1.00 17.96 ?  111 SER   B HB3  1 
ATOM   5758 H HG   . SER   B 1 111 ? 30.400 -19.289 6.212   1.00 19.94 ?  111 SER   B HG   1 
ATOM   5759 N N    . ALA   B 1 112 ? 33.985 -20.520 2.985   1.00 13.29 ?  112 ALA   B N    1 
ATOM   5760 C CA   . ALA   B 1 112 ? 35.333 -20.346 2.448   1.00 12.88 ?  112 ALA   B CA   1 
ATOM   5761 C C    . ALA   B 1 112 ? 35.307 -20.252 0.922   1.00 12.54 ?  112 ALA   B C    1 
ATOM   5762 O O    . ALA   B 1 112 ? 35.928 -19.358 0.330   1.00 12.52 ?  112 ALA   B O    1 
ATOM   5763 C CB   . ALA   B 1 112 ? 36.244 -21.476 2.939   1.00 13.45 ?  112 ALA   B CB   1 
ATOM   5764 H H    . ALA   B 1 112 ? 33.868 -21.247 3.438   1.00 15.92 ?  112 ALA   B H    1 
ATOM   5765 H HA   . ALA   B 1 112 ? 35.691 -19.511 2.787   1.00 15.43 ?  112 ALA   B HA   1 
ATOM   5766 H HB1  . ALA   B 1 112 ? 37.135 -21.336 2.576   1.00 16.11 ?  112 ALA   B HB1  1 
ATOM   5767 H HB2  . ALA   B 1 112 ? 36.281 -21.449 3.911   1.00 16.11 ?  112 ALA   B HB2  1 
ATOM   5768 H HB3  . ALA   B 1 112 ? 35.891 -22.322 2.642   1.00 16.11 ?  112 ALA   B HB3  1 
ATOM   5769 N N    . TYR   B 1 113 ? 34.577 -21.158 0.264   1.00 12.20 ?  113 TYR   B N    1 
ATOM   5770 C CA   . TYR   B 1 113 ? 34.496 -21.110 -1.191  1.00 11.94 ?  113 TYR   B CA   1 
ATOM   5771 C C    . TYR   B 1 113 ? 33.787 -19.857 -1.703  1.00 11.41 ?  113 TYR   B C    1 
ATOM   5772 O O    . TYR   B 1 113 ? 34.061 -19.424 -2.827  1.00 11.89 ?  113 TYR   B O    1 
ATOM   5773 C CB   . TYR   B 1 113 ? 33.821 -22.370 -1.739  1.00 12.10 ?  113 TYR   B CB   1 
ATOM   5774 C CG   . TYR   B 1 113 ? 34.783 -23.520 -1.987  1.00 12.37 ?  113 TYR   B CG   1 
ATOM   5775 C CD1  . TYR   B 1 113 ? 35.786 -23.414 -2.945  1.00 12.97 ?  113 TYR   B CD1  1 
ATOM   5776 C CD2  . TYR   B 1 113 ? 34.676 -24.710 -1.284  1.00 13.02 ?  113 TYR   B CD2  1 
ATOM   5777 C CE1  . TYR   B 1 113 ? 36.670 -24.448 -3.182  1.00 13.02 ?  113 TYR   B CE1  1 
ATOM   5778 C CE2  . TYR   B 1 113 ? 35.550 -25.762 -1.519  1.00 13.06 ?  113 TYR   B CE2  1 
ATOM   5779 C CZ   . TYR   B 1 113 ? 36.540 -25.630 -2.473  1.00 13.07 ?  113 TYR   B CZ   1 
ATOM   5780 O OH   . TYR   B 1 113 ? 37.428 -26.653 -2.737  1.00 14.07 ?  113 TYR   B OH   1 
ATOM   5781 H H    . TYR   B 1 113 ? 34.119 -21.792 0.635   1.00 14.61 ?  113 TYR   B H    1 
ATOM   5782 H HA   . TYR   B 1 113 ? 35.397 -21.089 -1.532  1.00 14.31 ?  113 TYR   B HA   1 
ATOM   5783 H HB2  . TYR   B 1 113 ? 33.157 -22.677 -1.101  1.00 14.50 ?  113 TYR   B HB2  1 
ATOM   5784 H HB3  . TYR   B 1 113 ? 33.392 -22.153 -2.580  1.00 14.50 ?  113 TYR   B HB3  1 
ATOM   5785 H HD1  . TYR   B 1 113 ? 35.876 -22.621 -3.425  1.00 15.54 ?  113 TYR   B HD1  1 
ATOM   5786 H HD2  . TYR   B 1 113 ? 34.004 -24.807 -0.650  1.00 15.60 ?  113 TYR   B HD2  1 
ATOM   5787 H HE1  . TYR   B 1 113 ? 37.338 -24.360 -3.826  1.00 15.60 ?  113 TYR   B HE1  1 
ATOM   5788 H HE2  . TYR   B 1 113 ? 35.464 -26.561 -1.044  1.00 15.65 ?  113 TYR   B HE2  1 
ATOM   5789 H HH   . TYR   B 1 113 ? 37.245 -27.315 -2.253  1.00 16.86 ?  113 TYR   B HH   1 
ATOM   5790 N N    . GLU   B 1 114 ? 32.858 -19.288 -0.924  1.00 11.79 ?  114 GLU   B N    1 
ATOM   5791 C CA   . GLU   B 1 114 ? 32.180 -18.069 -1.366  1.00 11.99 ?  114 GLU   B CA   1 
ATOM   5792 C C    . GLU   B 1 114 ? 33.171 -16.954 -1.672  1.00 12.01 ?  114 GLU   B C    1 
ATOM   5793 O O    . GLU   B 1 114 ? 32.895 -16.096 -2.514  1.00 12.34 ?  114 GLU   B O    1 
ATOM   5794 C CB   . GLU   B 1 114 ? 31.135 -17.641 -0.337  1.00 12.73 ?  114 GLU   B CB   1 
ATOM   5795 C CG   . GLU   B 1 114 ? 29.898 -18.553 -0.417  1.00 12.65 ?  114 GLU   B CG   1 
ATOM   5796 C CD   . GLU   B 1 114 ? 28.876 -18.363 0.693   1.00 12.81 ?  114 GLU   B CD   1 
ATOM   5797 O OE1  . GLU   B 1 114 ? 29.168 -17.748 1.739   1.00 13.10 ?  114 GLU   B OE1  1 
ATOM   5798 O OE2  . GLU   B 1 114 ? 27.755 -18.902 0.530   1.00 13.70 -1 114 GLU   B OE2  1 
ATOM   5799 H H    . GLU   B 1 114 ? 32.600 -19.593 -0.159  1.00 14.12 ?  114 GLU   B H    1 
ATOM   5800 H HA   . GLU   B 1 114 ? 31.711 -18.263 -2.185  1.00 14.36 ?  114 GLU   B HA   1 
ATOM   5801 H HB2  . GLU   B 1 114 ? 31.512 -17.712 0.558   1.00 15.26 ?  114 GLU   B HB2  1 
ATOM   5802 H HB3  . GLU   B 1 114 ? 30.860 -16.731 -0.515  1.00 15.26 ?  114 GLU   B HB3  1 
ATOM   5803 H HG2  . GLU   B 1 114 ? 29.449 -18.383 -1.256  1.00 15.15 ?  114 GLU   B HG2  1 
ATOM   5804 H HG3  . GLU   B 1 114 ? 30.196 -19.476 -0.387  1.00 15.15 ?  114 GLU   B HG3  1 
ATOM   5805 N N    . ASN   B 1 115 ? 34.341 -16.950 -1.023  1.00 11.67 ?  115 ASN   B N    1 
ATOM   5806 C CA   . ASN   B 1 115 ? 35.331 -15.913 -1.318  1.00 11.37 ?  115 ASN   B CA   1 
ATOM   5807 C C    . ASN   B 1 115 ? 35.746 -15.937 -2.782  1.00 11.64 ?  115 ASN   B C    1 
ATOM   5808 O O    . ASN   B 1 115 ? 36.141 -14.903 -3.335  1.00 12.19 ?  115 ASN   B O    1 
ATOM   5809 C CB   . ASN   B 1 115 ? 36.570 -16.088 -0.428  1.00 12.47 ?  115 ASN   B CB   1 
ATOM   5810 C CG   . ASN   B 1 115 ? 36.291 -15.824 1.032   1.00 12.73 ?  115 ASN   B CG   1 
ATOM   5811 O OD1  . ASN   B 1 115 ? 36.283 -14.674 1.471   1.00 14.89 ?  115 ASN   B OD1  1 
ATOM   5812 N ND2  . ASN   B 1 115 ? 36.120 -16.888 1.808   1.00 13.18 ?  115 ASN   B ND2  1 
ATOM   5813 H H    . ASN   B 1 115 ? 34.579 -17.511 -0.409  1.00 13.97 ?  115 ASN   B H    1 
ATOM   5814 H HA   . ASN   B 1 115 ? 34.956 -15.042 -1.129  1.00 13.63 ?  115 ASN   B HA   1 
ATOM   5815 H HB2  . ASN   B 1 115 ? 36.898 -16.999 -0.512  1.00 14.93 ?  115 ASN   B HB2  1 
ATOM   5816 H HB3  . ASN   B 1 115 ? 37.259 -15.465 -0.711  1.00 14.93 ?  115 ASN   B HB3  1 
ATOM   5817 H HD21 . ASN   B 1 115 ? 35.969 -16.790 2.651   1.00 15.79 ?  115 ASN   B HD21 1 
ATOM   5818 H HD22 . ASN   B 1 115 ? 36.145 -17.680 1.469   1.00 15.79 ?  115 ASN   B HD22 1 
ATOM   5819 N N    . PHE   B 1 116 ? 35.714 -17.113 -3.416  1.00 11.46 ?  116 PHE   B N    1 
ATOM   5820 C CA   . PHE   B 1 116 ? 36.149 -17.208 -4.805  1.00 11.45 ?  116 PHE   B CA   1 
ATOM   5821 C C    . PHE   B 1 116 ? 35.254 -16.384 -5.723  1.00 11.05 ?  116 PHE   B C    1 
ATOM   5822 O O    . PHE   B 1 116 ? 35.695 -15.953 -6.797  1.00 12.22 ?  116 PHE   B O    1 
ATOM   5823 C CB   . PHE   B 1 116 ? 36.115 -18.656 -5.327  1.00 11.21 ?  116 PHE   B CB   1 
ATOM   5824 C CG   . PHE   B 1 116 ? 37.186 -19.618 -4.779  1.00 10.80 ?  116 PHE   B CG   1 
ATOM   5825 C CD1  . PHE   B 1 116 ? 37.832 -19.433 -3.570  1.00 11.62 ?  116 PHE   B CD1  1 
ATOM   5826 C CD2  . PHE   B 1 116 ? 37.490 -20.760 -5.512  1.00 11.48 ?  116 PHE   B CD2  1 
ATOM   5827 C CE1  . PHE   B 1 116 ? 38.755 -20.368 -3.113  1.00 11.93 ?  116 PHE   B CE1  1 
ATOM   5828 C CE2  . PHE   B 1 116 ? 38.416 -21.694 -5.064  1.00 11.60 ?  116 PHE   B CE2  1 
ATOM   5829 C CZ   . PHE   B 1 116 ? 39.039 -21.501 -3.868  1.00 11.76 ?  116 PHE   B CZ   1 
ATOM   5830 H H    . PHE   B 1 116 ? 35.439 -17.859 -3.071  1.00 13.73 ?  116 PHE   B H    1 
ATOM   5831 H HA   . PHE   B 1 116 ? 37.055 -16.883 -4.881  1.00 13.72 ?  116 PHE   B HA   1 
ATOM   5832 H HB2  . PHE   B 1 116 ? 35.242 -19.039 -5.110  1.00 13.43 ?  116 PHE   B HB2  1 
ATOM   5833 H HB3  . PHE   B 1 116 ? 36.212 -18.636 -6.293  1.00 13.43 ?  116 PHE   B HB3  1 
ATOM   5834 H HD1  . PHE   B 1 116 ? 37.632 -18.686 -3.052  1.00 13.93 ?  116 PHE   B HD1  1 
ATOM   5835 H HD2  . PHE   B 1 116 ? 37.051 -20.908 -6.320  1.00 13.76 ?  116 PHE   B HD2  1 
ATOM   5836 H HE1  . PHE   B 1 116 ? 39.191 -20.234 -2.304  1.00 14.30 ?  116 PHE   B HE1  1 
ATOM   5837 H HE2  . PHE   B 1 116 ? 38.601 -22.445 -5.577  1.00 13.90 ?  116 PHE   B HE2  1 
ATOM   5838 H HZ   . PHE   B 1 116 ? 39.671 -22.111 -3.570  1.00 14.08 ?  116 PHE   B HZ   1 
ATOM   5839 N N    . ASN   B 1 117 ? 33.984 -16.187 -5.345  1.00 11.71 ?  117 ASN   B N    1 
ATOM   5840 C CA   . ASN   B 1 117 ? 33.046 -15.482 -6.215  1.00 12.28 ?  117 ASN   B CA   1 
ATOM   5841 C C    . ASN   B 1 117 ? 33.367 -14.004 -6.374  1.00 12.40 ?  117 ASN   B C    1 
ATOM   5842 O O    . ASN   B 1 117 ? 32.778 -13.353 -7.240  1.00 13.42 ?  117 ASN   B O    1 
ATOM   5843 C CB   . ASN   B 1 117 ? 31.619 -15.701 -5.723  1.00 12.55 ?  117 ASN   B CB   1 
ATOM   5844 C CG   . ASN   B 1 117 ? 31.161 -17.105 -5.978  1.00 12.50 ?  117 ASN   B CG   1 
ATOM   5845 O OD1  . ASN   B 1 117 ? 31.514 -17.698 -7.001  1.00 13.59 ?  117 ASN   B OD1  1 
ATOM   5846 N ND2  . ASN   B 1 117 ? 30.422 -17.673 -5.038  1.00 12.63 ?  117 ASN   B ND2  1 
ATOM   5847 H H    . ASN   B 1 117 ? 33.653 -16.449 -4.592  1.00 14.03 ?  117 ASN   B H    1 
ATOM   5848 H HA   . ASN   B 1 117 ? 33.108 -15.886 -7.093  1.00 14.72 ?  117 ASN   B HA   1 
ATOM   5849 H HB2  . ASN   B 1 117 ? 31.581 -15.538 -4.765  1.00 15.03 ?  117 ASN   B HB2  1 
ATOM   5850 H HB3  . ASN   B 1 117 ? 31.026 -15.090 -6.189  1.00 15.03 ?  117 ASN   B HB3  1 
ATOM   5851 H HD21 . ASN   B 1 117 ? 30.132 -18.478 -5.146  1.00 15.13 ?  117 ASN   B HD21 1 
ATOM   5852 H HD22 . ASN   B 1 117 ? 30.202 -17.231 -4.334  1.00 15.13 ?  117 ASN   B HD22 1 
ATOM   5853 N N    . GLN   B 1 118 ? 34.294 -13.473 -5.586  1.00 12.03 ?  118 GLN   B N    1 
ATOM   5854 C CA   . GLN   B 1 118 ? 34.720 -12.085 -5.725  1.00 12.64 ?  118 GLN   B CA   1 
ATOM   5855 C C    . GLN   B 1 118 ? 35.792 -11.897 -6.793  1.00 12.81 ?  118 GLN   B C    1 
ATOM   5856 O O    . GLN   B 1 118 ? 36.268 -10.770 -6.973  1.00 14.26 ?  118 GLN   B O    1 
ATOM   5857 C CB   . GLN   B 1 118 ? 35.197 -11.550 -4.371  1.00 13.26 ?  118 GLN   B CB   1 
ATOM   5858 C CG   . GLN   B 1 118 ? 34.113 -11.598 -3.304  1.00 13.44 ?  118 GLN   B CG   1 
ATOM   5859 C CD   . GLN   B 1 118 ? 32.945 -10.687 -3.629  1.00 13.48 ?  118 GLN   B CD   1 
ATOM   5860 O OE1  . GLN   B 1 118 ? 33.139 -9.543  -4.053  1.00 14.01 ?  118 GLN   B OE1  1 
ATOM   5861 N NE2  . GLN   B 1 118 ? 31.730 -11.180 -3.439  1.00 13.92 ?  118 GLN   B NE2  1 
ATOM   5862 H H    . GLN   B 1 118 ? 34.710 -13.897 -4.966  1.00 14.41 ?  118 GLN   B H    1 
ATOM   5863 H HA   . GLN   B 1 118 ? 33.960 -11.555 -6.001  1.00 15.15 ?  118 GLN   B HA   1 
ATOM   5864 H HB2  . GLN   B 1 118 ? 35.945 -12.081 -4.067  1.00 15.89 ?  118 GLN   B HB2  1 
ATOM   5865 H HB3  . GLN   B 1 118 ? 35.469 -10.622 -4.477  1.00 15.89 ?  118 GLN   B HB3  1 
ATOM   5866 H HG2  . GLN   B 1 118 ? 33.778 -12.507 -3.236  1.00 16.11 ?  118 GLN   B HG2  1 
ATOM   5867 H HG3  . GLN   B 1 118 ? 34.490 -11.317 -2.459  1.00 16.11 ?  118 GLN   B HG3  1 
ATOM   5868 H HE21 . GLN   B 1 118 ? 31.637 -11.983 -3.140  1.00 16.68 ?  118 GLN   B HE21 1 
ATOM   5869 H HE22 . GLN   B 1 118 ? 31.043 -10.701 -3.612  1.00 16.68 ?  118 GLN   B HE22 1 
ATOM   5870 N N    . HIS   B 1 119 ? 36.152 -12.953 -7.529  1.00 12.06 ?  119 HIS   B N    1 
ATOM   5871 C CA   . HIS   B 1 119 ? 37.201 -12.904 -8.540  1.00 12.54 ?  119 HIS   B CA   1 
ATOM   5872 C C    . HIS   B 1 119 ? 36.725 -13.639 -9.779  1.00 12.50 ?  119 HIS   B C    1 
ATOM   5873 O O    . HIS   B 1 119 ? 36.210 -14.753 -9.677  1.00 13.28 ?  119 HIS   B O    1 
ATOM   5874 C CB   . HIS   B 1 119 ? 38.475 -13.546 -7.988  1.00 12.92 ?  119 HIS   B CB   1 
ATOM   5875 C CG   . HIS   B 1 119 ? 38.961 -12.854 -6.763  1.00 14.38 ?  119 HIS   B CG   1 
ATOM   5876 N ND1  . HIS   B 1 119 ? 39.774 -11.741 -6.814  1.00 15.94 ?  119 HIS   B ND1  1 
ATOM   5877 C CD2  . HIS   B 1 119 ? 38.655 -13.042 -5.458  1.00 15.36 ?  119 HIS   B CD2  1 
ATOM   5878 C CE1  . HIS   B 1 119 ? 39.981 -11.302 -5.587  1.00 17.23 ?  119 HIS   B CE1  1 
ATOM   5879 N NE2  . HIS   B 1 119 ? 39.308 -12.066 -4.747  1.00 16.83 ?  119 HIS   B NE2  1 
ATOM   5880 H H    . HIS   B 1 119 ? 35.783 -13.732 -7.466  1.00 14.45 ?  119 HIS   B H    1 
ATOM   5881 H HA   . HIS   B 1 119 ? 37.386 -11.979 -8.775  1.00 15.02 ?  119 HIS   B HA   1 
ATOM   5882 H HB2  . HIS   B 1 119 ? 38.291 -14.473 -7.772  1.00 15.49 ?  119 HIS   B HB2  1 
ATOM   5883 H HB3  . HIS   B 1 119 ? 39.169 -13.496 -8.668  1.00 15.49 ?  119 HIS   B HB3  1 
ATOM   5884 H HD2  . HIS   B 1 119 ? 38.107 -13.712 -5.113  1.00 18.41 ?  119 HIS   B HD2  1 
ATOM   5885 H HE1  . HIS   B 1 119 ? 40.521 -10.586 -5.356  1.00 20.65 ?  119 HIS   B HE1  1 
ATOM   5886 H HE2  . HIS   B 1 119 ? 39.306 -11.990 -3.892  1.00 20.17 ?  119 HIS   B HE2  1 
ATOM   5887 N N    . GLU   B 1 120 ? 36.893 -13.026 -10.950 1.00 12.90 ?  120 GLU   B N    1 
ATOM   5888 C CA   . GLU   B 1 120 ? 36.306 -13.603 -12.155 1.00 14.05 ?  120 GLU   B CA   1 
ATOM   5889 C C    . GLU   B 1 120 ? 36.981 -14.903 -12.573 1.00 12.94 ?  120 GLU   B C    1 
ATOM   5890 O O    . GLU   B 1 120 ? 36.316 -15.777 -13.143 1.00 13.53 ?  120 GLU   B O    1 
ATOM   5891 C CB   . GLU   B 1 120 ? 36.324 -12.586 -13.296 1.00 18.53 ?  120 GLU   B CB   1 
ATOM   5892 C CG   . GLU   B 1 120 ? 35.356 -11.433 -13.088 1.00 25.10 ?  120 GLU   B CG   1 
ATOM   5893 C CD   . GLU   B 1 120 ? 35.218 -10.539 -14.306 1.00 30.96 ?  120 GLU   B CD   1 
ATOM   5894 O OE1  . GLU   B 1 120 ? 36.233 -10.314 -15.001 1.00 33.12 ?  120 GLU   B OE1  1 
ATOM   5895 O OE2  . GLU   B 1 120 ? 34.094 -10.057 -14.562 1.00 33.72 -1 120 GLU   B OE2  1 
ATOM   5896 H H    . GLU   B 1 120 ? 37.328 -12.287 -11.073 1.00 15.46 ?  120 GLU   B H    1 
ATOM   5897 H HA   . GLU   B 1 120 ? 35.381 -13.810 -11.968 1.00 16.83 ?  120 GLU   B HA   1 
ATOM   5898 H HB2  . GLU   B 1 120 ? 37.212 -12.214 -13.380 1.00 22.21 ?  120 GLU   B HB2  1 
ATOM   5899 H HB3  . GLU   B 1 120 ? 36.072 -13.036 -14.121 1.00 22.21 ?  120 GLU   B HB3  1 
ATOM   5900 H HG2  . GLU   B 1 120 ? 34.476 -11.788 -12.880 1.00 30.09 ?  120 GLU   B HG2  1 
ATOM   5901 H HG3  . GLU   B 1 120 ? 35.672 -10.879 -12.361 1.00 30.09 ?  120 GLU   B HG3  1 
ATOM   5902 N N    . VAL   B 1 121 ? 38.281 -15.046 -12.315 1.00 12.65 ?  121 VAL   B N    1 
ATOM   5903 C CA   . VAL   B 1 121 ? 39.025 -16.258 -12.655 1.00 12.61 ?  121 VAL   B CA   1 
ATOM   5904 C C    . VAL   B 1 121 ? 40.131 -16.462 -11.630 1.00 12.09 ?  121 VAL   B C    1 
ATOM   5905 O O    . VAL   B 1 121 ? 40.819 -15.509 -11.244 1.00 12.83 ?  121 VAL   B O    1 
ATOM   5906 C CB   . VAL   B 1 121 ? 39.545 -16.227 -14.113 1.00 14.31 ?  121 VAL   B CB   1 
ATOM   5907 C CG1  . VAL   B 1 121 ? 40.411 -14.998 -14.380 1.00 15.93 ?  121 VAL   B CG1  1 
ATOM   5908 C CG2  . VAL   B 1 121 ? 40.282 -17.520 -14.459 1.00 15.95 ?  121 VAL   B CG2  1 
ATOM   5909 H H    . VAL   B 1 121 ? 38.772 -14.436 -11.956 1.00 15.16 ?  121 VAL   B H    1 
ATOM   5910 H HA   . VAL   B 1 121 ? 38.414 -17.009 -12.589 1.00 15.11 ?  121 VAL   B HA   1 
ATOM   5911 H HB   . VAL   B 1 121 ? 38.779 -16.174 -14.711 1.00 17.15 ?  121 VAL   B HB   1 
ATOM   5912 H HG11 . VAL   B 1 121 ? 40.726 -15.025 -15.298 1.00 19.09 ?  121 VAL   B HG11 1 
ATOM   5913 H HG12 . VAL   B 1 121 ? 39.876 -14.201 -14.239 1.00 19.09 ?  121 VAL   B HG12 1 
ATOM   5914 H HG13 . VAL   B 1 121 ? 41.164 -15.005 -13.771 1.00 19.09 ?  121 VAL   B HG13 1 
ATOM   5915 H HG21 . VAL   B 1 121 ? 40.491 -17.525 -15.408 1.00 19.11 ?  121 VAL   B HG21 1 
ATOM   5916 H HG22 . VAL   B 1 121 ? 41.103 -17.566 -13.943 1.00 19.11 ?  121 VAL   B HG22 1 
ATOM   5917 H HG23 . VAL   B 1 121 ? 39.715 -18.279 -14.245 1.00 19.11 ?  121 VAL   B HG23 1 
ATOM   5918 N N    . LEU   B 1 122 ? 40.307 -17.716 -11.197 1.00 11.73 ?  122 LEU   B N    1 
ATOM   5919 C CA   . LEU   B 1 122 ? 41.284 -18.072 -10.175 1.00 11.38 ?  122 LEU   B CA   1 
ATOM   5920 C C    . LEU   B 1 122 ? 41.938 -19.405 -10.496 1.00 11.37 ?  122 LEU   B C    1 
ATOM   5921 O O    . LEU   B 1 122 ? 41.281 -20.326 -10.994 1.00 12.48 ?  122 LEU   B O    1 
ATOM   5922 C CB   . LEU   B 1 122 ? 40.639 -18.298 -8.796  1.00 13.52 ?  122 LEU   B CB   1 
ATOM   5923 C CG   . LEU   B 1 122 ? 39.600 -17.281 -8.319  1.00 13.95 ?  122 LEU   B CG   1 
ATOM   5924 C CD1  . LEU   B 1 122 ? 38.209 -17.665 -8.788  1.00 14.69 ?  122 LEU   B CD1  1 
ATOM   5925 C CD2  . LEU   B 1 122 ? 39.645 -17.162 -6.812  1.00 12.91 ?  122 LEU   B CD2  1 
ATOM   5926 H H    . LEU   B 1 122 ? 39.863 -18.395 -11.490 1.00 14.05 ?  122 LEU   B H    1 
ATOM   5927 H HA   . LEU   B 1 122 ? 41.964 -17.382 -10.101 1.00 13.63 ?  122 LEU   B HA   1 
ATOM   5928 H HB2  . LEU   B 1 122 ? 40.200 -19.160 -8.809  1.00 16.20 ?  122 LEU   B HB2  1 
ATOM   5929 H HB3  . LEU   B 1 122 ? 41.345 -18.308 -8.132  1.00 16.20 ?  122 LEU   B HB3  1 
ATOM   5930 H HG   . LEU   B 1 122 ? 39.815 -16.410 -8.693  1.00 16.71 ?  122 LEU   B HG   1 
ATOM   5931 H HD11 . LEU   B 1 122 ? 37.571 -17.019 -8.443  1.00 17.61 ?  122 LEU   B HD11 1 
ATOM   5932 H HD12 . LEU   B 1 122 ? 38.189 -17.659 -9.758  1.00 17.61 ?  122 LEU   B HD12 1 
ATOM   5933 H HD13 . LEU   B 1 122 ? 37.997 -18.549 -8.457  1.00 17.61 ?  122 LEU   B HD13 1 
ATOM   5934 H HD21 . LEU   B 1 122 ? 38.959 -16.540 -6.522  1.00 15.46 ?  122 LEU   B HD21 1 
ATOM   5935 H HD22 . LEU   B 1 122 ? 39.490 -18.034 -6.420  1.00 15.46 ?  122 LEU   B HD22 1 
ATOM   5936 H HD23 . LEU   B 1 122 ? 40.521 -16.831 -6.546  1.00 15.46 ?  122 LEU   B HD23 1 
ATOM   5937 N N    . LEU   B 1 123 ? 43.220 -19.515 -10.128 1.00 10.81 ?  123 LEU   B N    1 
ATOM   5938 C CA   . LEU   B 1 123 ? 43.928 -20.788 -10.012 1.00 11.42 ?  123 LEU   B CA   1 
ATOM   5939 C C    . LEU   B 1 123 ? 43.897 -21.183 -8.539  1.00 11.02 ?  123 LEU   B C    1 
ATOM   5940 O O    . LEU   B 1 123 ? 44.256 -20.361 -7.688  1.00 11.35 ?  123 LEU   B O    1 
ATOM   5941 C CB   . LEU   B 1 123 ? 45.380 -20.606 -10.466 1.00 11.61 ?  123 LEU   B CB   1 
ATOM   5942 C CG   . LEU   B 1 123 ? 46.319 -21.792 -10.228 1.00 11.80 ?  123 LEU   B CG   1 
ATOM   5943 C CD1  . LEU   B 1 123 ? 45.890 -23.038 -10.992 1.00 12.52 ?  123 LEU   B CD1  1 
ATOM   5944 C CD2  . LEU   B 1 123 ? 47.739 -21.404 -10.608 1.00 12.75 ?  123 LEU   B CD2  1 
ATOM   5945 H H    . LEU   B 1 123 ? 43.713 -18.835 -9.923  1.00 12.95 ?  123 LEU   B H    1 
ATOM   5946 H HA   . LEU   B 1 123 ? 43.491 -21.470 -10.541 1.00 13.69 ?  123 LEU   B HA   1 
ATOM   5947 H HB2  . LEU   B 1 123 ? 45.375 -20.428 -11.419 1.00 13.90 ?  123 LEU   B HB2  1 
ATOM   5948 H HB3  . LEU   B 1 123 ? 45.751 -19.843 -9.997  1.00 13.90 ?  123 LEU   B HB3  1 
ATOM   5949 H HG   . LEU   B 1 123 ? 46.319 -22.012 -9.281  1.00 14.13 ?  123 LEU   B HG   1 
ATOM   5950 H HD11 . LEU   B 1 123 ? 46.527 -23.748 -10.817 1.00 15.00 ?  123 LEU   B HD11 1 
ATOM   5951 H HD12 . LEU   B 1 123 ? 45.007 -23.304 -10.690 1.00 15.00 ?  123 LEU   B HD12 1 
ATOM   5952 H HD13 . LEU   B 1 123 ? 45.871 -22.834 -11.938 1.00 15.00 ?  123 LEU   B HD13 1 
ATOM   5953 H HD21 . LEU   B 1 123 ? 48.324 -22.161 -10.455 1.00 15.28 ?  123 LEU   B HD21 1 
ATOM   5954 H HD22 . LEU   B 1 123 ? 47.754 -21.157 -11.547 1.00 15.28 ?  123 LEU   B HD22 1 
ATOM   5955 H HD23 . LEU   B 1 123 ? 48.016 -20.652 -10.063 1.00 15.28 ?  123 LEU   B HD23 1 
ATOM   5956 N N    . ALA   B 1 124 ? 43.463 -22.412 -8.226  1.00 10.73 ?  124 ALA   B N    1 
ATOM   5957 C CA   . ALA   B 1 124 ? 43.201 -22.720 -6.827  1.00 10.94 ?  124 ALA   B CA   1 
ATOM   5958 C C    . ALA   B 1 124 ? 43.471 -24.182 -6.498  1.00 10.47 ?  124 ALA   B C    1 
ATOM   5959 O O    . ALA   B 1 124 ? 43.344 -25.058 -7.362  1.00 11.14 ?  124 ALA   B O    1 
ATOM   5960 C CB   . ALA   B 1 124 ? 41.748 -22.414 -6.462  1.00 11.15 ?  124 ALA   B CB   1 
ATOM   5961 H H    . ALA   B 1 124 ? 43.305 -23.051 -8.788  1.00 12.86 ?  124 ALA   B H    1 
ATOM   5962 H HA   . ALA   B 1 124 ? 43.778 -22.171 -6.283  1.00 13.11 ?  124 ALA   B HA   1 
ATOM   5963 H HB1  . ALA   B 1 124 ? 41.603 -22.630 -5.530  1.00 13.36 ?  124 ALA   B HB1  1 
ATOM   5964 H HB2  . ALA   B 1 124 ? 41.581 -21.469 -6.615  1.00 13.36 ?  124 ALA   B HB2  1 
ATOM   5965 H HB3  . ALA   B 1 124 ? 41.161 -22.947 -7.022  1.00 13.36 ?  124 ALA   B HB3  1 
ATOM   5966 N N    . PRO   B 1 125 ? 43.766 -24.476 -5.234  1.00 10.87 ?  125 PRO   B N    1 
ATOM   5967 C CA   . PRO   B 1 125 ? 43.700 -25.841 -4.712  1.00 11.33 ?  125 PRO   B CA   1 
ATOM   5968 C C    . PRO   B 1 125 ? 42.297 -26.111 -4.169  1.00 11.49 ?  125 PRO   B C    1 
ATOM   5969 O O    . PRO   B 1 125 ? 41.504 -25.192 -3.949  1.00 12.14 ?  125 PRO   B O    1 
ATOM   5970 C CB   . PRO   B 1 125 ? 44.687 -25.770 -3.541  1.00 13.04 ?  125 PRO   B CB   1 
ATOM   5971 C CG   . PRO   B 1 125 ? 44.427 -24.377 -2.968  1.00 12.79 ?  125 PRO   B CG   1 
ATOM   5972 C CD   . PRO   B 1 125 ? 44.095 -23.506 -4.174  1.00 11.65 ?  125 PRO   B CD   1 
ATOM   5973 H HA   . PRO   B 1 125 ? 43.974 -26.509 -5.365  1.00 13.57 ?  125 PRO   B HA   1 
ATOM   5974 H HB2  . PRO   B 1 125 ? 44.481 -26.460 -2.886  1.00 15.62 ?  125 PRO   B HB2  1 
ATOM   5975 H HB3  . PRO   B 1 125 ? 45.597 -25.852 -3.859  1.00 15.62 ?  125 PRO   B HB3  1 
ATOM   5976 H HG2  . PRO   B 1 125 ? 43.670 -24.406 -2.354  1.00 15.33 ?  125 PRO   B HG2  1 
ATOM   5977 H HG3  . PRO   B 1 125 ? 45.219 -24.052 -2.511  1.00 15.33 ?  125 PRO   B HG3  1 
ATOM   5978 H HD2  . PRO   B 1 125 ? 43.338 -22.936 -3.988  1.00 13.96 ?  125 PRO   B HD2  1 
ATOM   5979 H HD3  . PRO   B 1 125 ? 44.879 -22.982 -4.430  1.00 13.96 ?  125 PRO   B HD3  1 
ATOM   5980 N N    . LEU   B 1 126 ? 42.027 -27.388 -3.890  1.00 12.49 ?  126 LEU   B N    1 
ATOM   5981 C CA   . LEU   B 1 126 ? 40.809 -27.755 -3.175  1.00 13.07 ?  126 LEU   B CA   1 
ATOM   5982 C C    . LEU   B 1 126 ? 40.915 -27.356 -1.707  1.00 13.13 ?  126 LEU   B C    1 
ATOM   5983 O O    . LEU   B 1 126 ? 41.805 -27.812 -0.987  1.00 15.18 ?  126 LEU   B O    1 
ATOM   5984 C CB   . LEU   B 1 126 ? 40.562 -29.254 -3.293  1.00 14.57 ?  126 LEU   B CB   1 
ATOM   5985 C CG   . LEU   B 1 126 ? 40.022 -29.745 -4.636  1.00 15.67 ?  126 LEU   B CG   1 
ATOM   5986 C CD1  . LEU   B 1 126 ? 40.067 -31.256 -4.698  1.00 17.62 ?  126 LEU   B CD1  1 
ATOM   5987 C CD2  . LEU   B 1 126 ? 38.601 -29.259 -4.871  1.00 15.81 ?  126 LEU   B CD2  1 
ATOM   5988 H H    . LEU   B 1 126 ? 42.539 -28.052 -4.089  1.00 14.96 ?  126 LEU   B H    1 
ATOM   5989 H HA   . LEU   B 1 126 ? 40.059 -27.284 -3.566  1.00 15.66 ?  126 LEU   B HA   1 
ATOM   5990 H HB2  . LEU   B 1 126 ? 41.394 -29.716 -3.132  1.00 17.47 ?  126 LEU   B HB2  1 
ATOM   5991 H HB3  . LEU   B 1 126 ? 39.912 -29.506 -2.616  1.00 17.47 ?  126 LEU   B HB3  1 
ATOM   5992 H HG   . LEU   B 1 126 ? 40.582 -29.392 -5.350  1.00 18.79 ?  126 LEU   B HG   1 
ATOM   5993 H HD11 . LEU   B 1 126 ? 39.720 -31.546 -5.555  1.00 21.12 ?  126 LEU   B HD11 1 
ATOM   5994 H HD12 . LEU   B 1 126 ? 40.983 -31.548 -4.591  1.00 21.12 ?  126 LEU   B HD12 1 
ATOM   5995 H HD13 . LEU   B 1 126 ? 39.518 -31.613 -3.981  1.00 21.12 ?  126 LEU   B HD13 1 
ATOM   5996 H HD21 . LEU   B 1 126 ? 38.257 -29.669 -5.681  1.00 18.95 ?  126 LEU   B HD21 1 
ATOM   5997 H HD22 . LEU   B 1 126 ? 38.052 -29.511 -4.114  1.00 18.95 ?  126 LEU   B HD22 1 
ATOM   5998 H HD23 . LEU   B 1 126 ? 38.604 -28.292 -4.970  1.00 18.95 ?  126 LEU   B HD23 1 
ATOM   5999 N N    . LEU   B 1 127 ? 39.986 -26.527 -1.249  1.00 12.86 ?  127 LEU   B N    1 
ATOM   6000 C CA   . LEU   B 1 127 ? 40.039 -26.043 0.119   1.00 13.10 ?  127 LEU   B CA   1 
ATOM   6001 C C    . LEU   B 1 127 ? 39.769 -27.163 1.115   1.00 13.12 ?  127 LEU   B C    1 
ATOM   6002 O O    . LEU   B 1 127 ? 38.950 -28.060 0.890   1.00 13.66 ?  127 LEU   B O    1 
ATOM   6003 C CB   . LEU   B 1 127 ? 39.025 -24.920 0.333   1.00 14.13 ?  127 LEU   B CB   1 
ATOM   6004 C CG   . LEU   B 1 127 ? 39.201 -23.660 -0.518  1.00 14.30 ?  127 LEU   B CG   1 
ATOM   6005 C CD1  . LEU   B 1 127 ? 38.077 -22.690 -0.203  1.00 14.99 ?  127 LEU   B CD1  1 
ATOM   6006 C CD2  . LEU   B 1 127 ? 40.558 -22.998 -0.291  1.00 15.19 ?  127 LEU   B CD2  1 
ATOM   6007 H H    . LEU   B 1 127 ? 39.321 -26.220 -1.711  1.00 15.41 ?  127 LEU   B H    1 
ATOM   6008 H HA   . LEU   B 1 127 ? 40.928 -25.683 0.292   1.00 15.70 ?  127 LEU   B HA   1 
ATOM   6009 H HB2  . LEU   B 1 127 ? 38.141 -25.272 0.147   1.00 16.94 ?  127 LEU   B HB2  1 
ATOM   6010 H HB3  . LEU   B 1 127 ? 39.071 -24.645 1.263   1.00 16.94 ?  127 LEU   B HB3  1 
ATOM   6011 H HG   . LEU   B 1 127 ? 39.128 -23.897 -1.454  1.00 17.14 ?  127 LEU   B HG   1 
ATOM   6012 H HD11 . LEU   B 1 127 ? 38.191 -21.887 -0.739  1.00 17.96 ?  127 LEU   B HD11 1 
ATOM   6013 H HD12 . LEU   B 1 127 ? 37.225 -23.105 -0.409  1.00 17.96 ?  127 LEU   B HD12 1 
ATOM   6014 H HD13 . LEU   B 1 127 ? 38.111 -22.459 0.741   1.00 17.96 ?  127 LEU   B HD13 1 
ATOM   6015 H HD21 . LEU   B 1 127 ? 40.588 -22.162 -0.782  1.00 18.21 ?  127 LEU   B HD21 1 
ATOM   6016 H HD22 . LEU   B 1 127 ? 40.671 -22.827 0.658   1.00 18.21 ?  127 LEU   B HD22 1 
ATOM   6017 H HD23 . LEU   B 1 127 ? 41.254 -23.593 -0.606  1.00 18.21 ?  127 LEU   B HD23 1 
ATOM   6018 N N    . SER   B 1 128 ? 40.451 -27.074 2.245   1.00 13.25 ?  128 SER   B N    1 
ATOM   6019 C CA   . SER   B 1 128 ? 40.330 -27.988 3.367   1.00 14.10 ?  128 SER   B CA   1 
ATOM   6020 C C    . SER   B 1 128 ? 40.820 -29.397 3.050   1.00 15.27 ?  128 SER   B C    1 
ATOM   6021 O O    . SER   B 1 128 ? 40.713 -30.274 3.904   1.00 16.99 ?  128 SER   B O    1 
ATOM   6022 C CB   . SER   B 1 128 ? 38.922 -27.994 3.980   1.00 14.39 ?  128 SER   B CB   1 
ATOM   6023 O OG   . SER   B 1 128 ? 38.608 -26.714 4.527   1.00 14.98 ?  128 SER   B OG   1 
ATOM   6024 H H    . SER   B 1 128 ? 41.021 -26.446 2.393   1.00 15.87 ?  128 SER   B H    1 
ATOM   6025 H HA   . SER   B 1 128 ? 40.909 -27.655 4.058   1.00 16.90 ?  128 SER   B HA   1 
ATOM   6026 H HB2  . SER   B 1 128 ? 38.267 -28.218 3.296   1.00 17.24 ?  128 SER   B HB2  1 
ATOM   6027 H HB3  . SER   B 1 128 ? 38.887 -28.661 4.693   1.00 17.24 ?  128 SER   B HB3  1 
ATOM   6028 H HG   . SER   B 1 128 ? 39.170 -26.517 5.120   1.00 17.96 ?  128 SER   B HG   1 
ATOM   6029 N N    . ALA   B 1 129 ? 41.403 -29.620 1.870   1.00 16.36 ?  129 ALA   B N    1 
ATOM   6030 C CA   . ALA   B 1 129 ? 41.948 -30.919 1.512   1.00 17.07 ?  129 ALA   B CA   1 
ATOM   6031 C C    . ALA   B 1 129 ? 43.336 -31.099 2.111   1.00 16.32 ?  129 ALA   B C    1 
ATOM   6032 O O    . ALA   B 1 129 ? 43.897 -30.207 2.761   1.00 15.67 ?  129 ALA   B O    1 
ATOM   6033 C CB   . ALA   B 1 129 ? 42.012 -31.076 -0.006  1.00 19.19 ?  129 ALA   B CB   1 
ATOM   6034 H H    . ALA   B 1 129 ? 41.496 -29.023 1.254   1.00 19.61 ?  129 ALA   B H    1 
ATOM   6035 H HA   . ALA   B 1 129 ? 41.375 -31.613 1.864   1.00 20.46 ?  129 ALA   B HA   1 
ATOM   6036 H HB1  . ALA   B 1 129 ? 42.368 -31.954 -0.219  1.00 23.00 ?  129 ALA   B HB1  1 
ATOM   6037 H HB2  . ALA   B 1 129 ? 41.121 -30.983 -0.371  1.00 23.00 ?  129 ALA   B HB2  1 
ATOM   6038 H HB3  . ALA   B 1 129 ? 42.594 -30.388 -0.372  1.00 23.00 ?  129 ALA   B HB3  1 
ATOM   6039 N N    . GLY   B 1 130 ? 43.893 -32.285 1.883   1.00 16.26 ?  130 GLY   B N    1 
ATOM   6040 C CA   . GLY   B 1 130 ? 45.282 -32.522 2.233   1.00 17.09 ?  130 GLY   B CA   1 
ATOM   6041 C C    . GLY   B 1 130 ? 45.501 -32.423 3.725   1.00 16.76 ?  130 GLY   B C    1 
ATOM   6042 O O    . GLY   B 1 130 ? 44.806 -33.067 4.523   1.00 17.89 ?  130 GLY   B O    1 
ATOM   6043 H H    . GLY   B 1 130 ? 43.493 -32.960 1.527   1.00 19.49 ?  130 GLY   B H    1 
ATOM   6044 H HA2  . GLY   B 1 130 ? 45.545 -33.414 1.945   1.00 20.48 ?  130 GLY   B HA2  1 
ATOM   6045 H HA3  . GLY   B 1 130 ? 45.849 -31.876 1.793   1.00 20.48 ?  130 GLY   B HA3  1 
ATOM   6046 N N    . ILE   B 1 131 ? 46.480 -31.598 4.113   1.00 17.31 ?  131 ILE   B N    1 
ATOM   6047 C CA   . ILE   B 1 131 ? 46.843 -31.463 5.514   1.00 18.46 ?  131 ILE   B CA   1 
ATOM   6048 C C    . ILE   B 1 131 ? 45.721 -30.875 6.354   1.00 17.50 ?  131 ILE   B C    1 
ATOM   6049 O O    . ILE   B 1 131 ? 45.782 -30.957 7.582   1.00 19.24 ?  131 ILE   B O    1 
ATOM   6050 C CB   . ILE   B 1 131 ? 48.163 -30.672 5.699   1.00 20.37 ?  131 ILE   B CB   1 
ATOM   6051 C CG1  . ILE   B 1 131 ? 47.976 -29.193 5.332   1.00 21.74 ?  131 ILE   B CG1  1 
ATOM   6052 C CG2  . ILE   B 1 131 ? 49.285 -31.302 4.876   1.00 21.51 ?  131 ILE   B CG2  1 
ATOM   6053 C CD1  . ILE   B 1 131 ? 49.185 -28.325 5.637   1.00 22.96 ?  131 ILE   B CD1  1 
ATOM   6054 H H    . ILE   B 1 131 ? 46.938 -31.104 3.582   1.00 20.75 ?  131 ILE   B H    1 
ATOM   6055 H HA   . ILE   B 1 131 ? 47.000 -32.350 5.862   1.00 22.13 ?  131 ILE   B HA   1 
ATOM   6056 H HB   . ILE   B 1 131 ? 48.409 -30.721 6.636   1.00 24.42 ?  131 ILE   B HB   1 
ATOM   6057 H HG12 . ILE   B 1 131 ? 47.792 -29.130 4.383   1.00 26.06 ?  131 ILE   B HG12 1 
ATOM   6058 H HG13 . ILE   B 1 131 ? 47.226 -28.831 5.834   1.00 26.06 ?  131 ILE   B HG13 1 
ATOM   6059 H HG21 . ILE   B 1 131 ? 50.123 -30.886 5.121   1.00 25.79 ?  131 ILE   B HG21 1 
ATOM   6060 H HG22 . ILE   B 1 131 ? 49.312 -32.251 5.062   1.00 25.79 ?  131 ILE   B HG22 1 
ATOM   6061 H HG23 . ILE   B 1 131 ? 49.100 -31.152 3.934   1.00 25.79 ?  131 ILE   B HG23 1 
ATOM   6062 H HD11 . ILE   B 1 131 ? 48.953 -27.399 5.473   1.00 27.53 ?  131 ILE   B HD11 1 
ATOM   6063 H HD12 . ILE   B 1 131 ? 49.431 -28.447 6.567   1.00 27.53 ?  131 ILE   B HD12 1 
ATOM   6064 H HD13 . ILE   B 1 131 ? 49.915 -28.594 5.061   1.00 27.53 ?  131 ILE   B HD13 1 
ATOM   6065 N N    . PHE   B 1 132 ? 44.696 -30.288 5.724   1.00 16.16 ?  132 PHE   B N    1 
ATOM   6066 C CA   . PHE   B 1 132 ? 43.529 -29.792 6.449   1.00 16.62 ?  132 PHE   B CA   1 
ATOM   6067 C C    . PHE   B 1 132 ? 42.507 -30.885 6.763   1.00 18.00 ?  132 PHE   B C    1 
ATOM   6068 O O    . PHE   B 1 132 ? 41.598 -30.641 7.563   1.00 19.51 ?  132 PHE   B O    1 
ATOM   6069 C CB   . PHE   B 1 132 ? 42.850 -28.659 5.666   1.00 15.78 ?  132 PHE   B CB   1 
ATOM   6070 C CG   . PHE   B 1 132 ? 43.544 -27.315 5.776   1.00 15.49 ?  132 PHE   B CG   1 
ATOM   6071 C CD1  . PHE   B 1 132 ? 44.831 -27.130 5.297   1.00 16.66 ?  132 PHE   B CD1  1 
ATOM   6072 C CD2  . PHE   B 1 132 ? 42.871 -26.219 6.305   1.00 14.87 ?  132 PHE   B CD2  1 
ATOM   6073 C CE1  . PHE   B 1 132 ? 45.450 -25.885 5.387   1.00 17.26 ?  132 PHE   B CE1  1 
ATOM   6074 C CE2  . PHE   B 1 132 ? 43.481 -24.974 6.393   1.00 15.95 ?  132 PHE   B CE2  1 
ATOM   6075 C CZ   . PHE   B 1 132 ? 44.767 -24.807 5.933   1.00 16.97 ?  132 PHE   B CZ   1 
ATOM   6076 H H    . PHE   B 1 132 ? 44.654 -30.165 4.873   1.00 19.37 ?  132 PHE   B H    1 
ATOM   6077 H HA   . PHE   B 1 132 ? 43.826 -29.419 7.293   1.00 19.92 ?  132 PHE   B HA   1 
ATOM   6078 H HB2  . PHE   B 1 132 ? 42.834 -28.899 4.729   1.00 18.91 ?  132 PHE   B HB2  1 
ATOM   6079 H HB3  . PHE   B 1 132 ? 41.945 -28.548 5.996   1.00 18.91 ?  132 PHE   B HB3  1 
ATOM   6080 H HD1  . PHE   B 1 132 ? 45.297 -27.852 4.935   1.00 19.97 ?  132 PHE   B HD1  1 
ATOM   6081 H HD2  . PHE   B 1 132 ? 42.003 -26.330 6.621   1.00 17.82 ?  132 PHE   B HD2  1 
ATOM   6082 H HE1  . PHE   B 1 132 ? 46.322 -25.777 5.078   1.00 20.69 ?  132 PHE   B HE1  1 
ATOM   6083 H HE2  . PHE   B 1 132 ? 43.021 -24.256 6.766   1.00 19.12 ?  132 PHE   B HE2  1 
ATOM   6084 H HZ   . PHE   B 1 132 ? 45.183 -23.974 5.998   1.00 20.35 ?  132 PHE   B HZ   1 
ATOM   6085 N N    . GLY   B 1 133 ? 42.607 -32.068 6.148   1.00 17.60 ?  133 GLY   B N    1 
ATOM   6086 C CA   . GLY   B 1 133 ? 41.905 -33.241 6.634   1.00 18.61 ?  133 GLY   B CA   1 
ATOM   6087 C C    . GLY   B 1 133 ? 40.491 -33.483 6.134   1.00 19.21 ?  133 GLY   B C    1 
ATOM   6088 O O    . GLY   B 1 133 ? 39.897 -34.490 6.523   1.00 21.06 ?  133 GLY   B O    1 
ATOM   6089 H H    . GLY   B 1 133 ? 43.088 -32.209 5.447   1.00 21.09 ?  133 GLY   B H    1 
ATOM   6090 H HA2  . GLY   B 1 133 ? 42.431 -34.021 6.406   1.00 22.31 ?  133 GLY   B HA2  1 
ATOM   6091 H HA3  . GLY   B 1 133 ? 41.868 -33.187 7.603   1.00 22.31 ?  133 GLY   B HA3  1 
ATOM   6092 N N    . ALA   B 1 134 ? 39.925 -32.616 5.300   1.00 18.41 ?  134 ALA   B N    1 
ATOM   6093 C CA   . ALA   B 1 134 ? 38.598 -32.898 4.772   1.00 18.68 ?  134 ALA   B CA   1 
ATOM   6094 C C    . ALA   B 1 134 ? 38.680 -33.892 3.618   1.00 18.25 ?  134 ALA   B C    1 
ATOM   6095 O O    . ALA   B 1 134 ? 39.734 -34.084 3.003   1.00 19.26 ?  134 ALA   B O    1 
ATOM   6096 C CB   . ALA   B 1 134 ? 37.928 -31.615 4.289   1.00 19.02 ?  134 ALA   B CB   1 
ATOM   6097 H H    . ALA   B 1 134 ? 40.277 -31.876 5.037   1.00 22.07 ?  134 ALA   B H    1 
ATOM   6098 H HA   . ALA   B 1 134 ? 38.051 -33.284 5.475   1.00 22.39 ?  134 ALA   B HA   1 
ATOM   6099 H HB1  . ALA   B 1 134 ? 37.040 -31.831 3.962   1.00 22.80 ?  134 ALA   B HB1  1 
ATOM   6100 H HB2  . ALA   B 1 134 ? 37.865 -30.992 5.029   1.00 22.80 ?  134 ALA   B HB2  1 
ATOM   6101 H HB3  . ALA   B 1 134 ? 38.459 -31.231 3.575   1.00 22.80 ?  134 ALA   B HB3  1 
ATOM   6102 N N    . ASP   B 1 135 ? 37.541 -34.514 3.324   1.00 18.33 ?  135 ASP   B N    1 
ATOM   6103 C CA   . ASP   B 1 135 ? 37.440 -35.404 2.177   1.00 18.92 ?  135 ASP   B CA   1 
ATOM   6104 C C    . ASP   B 1 135 ? 37.552 -34.568 0.909   1.00 17.66 ?  135 ASP   B C    1 
ATOM   6105 O O    . ASP   B 1 135 ? 36.701 -33.699 0.677   1.00 17.71 ?  135 ASP   B O    1 
ATOM   6106 C CB   . ASP   B 1 135 ? 36.093 -36.125 2.220   1.00 20.75 ?  135 ASP   B CB   1 
ATOM   6107 C CG   . ASP   B 1 135 ? 35.926 -37.141 1.106   1.00 22.81 ?  135 ASP   B CG   1 
ATOM   6108 O OD1  . ASP   B 1 135 ? 36.795 -37.205 0.210   1.00 22.80 ?  135 ASP   B OD1  1 
ATOM   6109 O OD2  . ASP   B 1 135 ? 34.925 -37.895 1.141   1.00 25.65 -1 135 ASP   B OD2  1 
ATOM   6110 H H    . ASP   B 1 135 ? 36.813 -34.431 3.771   1.00 21.97 ?  135 ASP   B H    1 
ATOM   6111 H HA   . ASP   B 1 135 ? 38.153 -36.060 2.208   1.00 22.68 ?  135 ASP   B HA   1 
ATOM   6112 H HB2  . ASP   B 1 135 ? 36.021 -36.598 3.060   1.00 24.88 ?  135 ASP   B HB2  1 
ATOM   6113 H HB3  . ASP   B 1 135 ? 35.387 -35.469 2.139   1.00 24.88 ?  135 ASP   B HB3  1 
ATOM   6114 N N    . PRO   B 1 136 ? 38.566 -34.776 0.068   1.00 17.77 ?  136 PRO   B N    1 
ATOM   6115 C CA   . PRO   B 1 136 ? 38.665 -33.960 -1.153  1.00 16.81 ?  136 PRO   B CA   1 
ATOM   6116 C C    . PRO   B 1 136 ? 37.470 -34.113 -2.076  1.00 15.98 ?  136 PRO   B C    1 
ATOM   6117 O O    . PRO   B 1 136 ? 37.147 -33.172 -2.810  1.00 15.53 ?  136 PRO   B O    1 
ATOM   6118 C CB   . PRO   B 1 136 ? 39.974 -34.441 -1.799  1.00 17.98 ?  136 PRO   B CB   1 
ATOM   6119 C CG   . PRO   B 1 136 ? 40.188 -35.825 -1.236  1.00 19.70 ?  136 PRO   B CG   1 
ATOM   6120 C CD   . PRO   B 1 136 ? 39.652 -35.764 0.163   1.00 19.09 ?  136 PRO   B CD   1 
ATOM   6121 H HA   . PRO   B 1 136 ? 38.756 -33.022 -0.924  1.00 20.14 ?  136 PRO   B HA   1 
ATOM   6122 H HB2  . PRO   B 1 136 ? 39.878 -34.472 -2.767  1.00 21.55 ?  136 PRO   B HB2  1 
ATOM   6123 H HB3  . PRO   B 1 136 ? 40.701 -33.848 -1.549  1.00 21.55 ?  136 PRO   B HB3  1 
ATOM   6124 H HG2  . PRO   B 1 136 ? 39.695 -36.476 -1.761  1.00 23.61 ?  136 PRO   B HG2  1 
ATOM   6125 H HG3  . PRO   B 1 136 ? 41.135 -36.036 -1.228  1.00 23.61 ?  136 PRO   B HG3  1 
ATOM   6126 H HD2  . PRO   B 1 136 ? 39.303 -36.627 0.431   1.00 22.88 ?  136 PRO   B HD2  1 
ATOM   6127 H HD3  . PRO   B 1 136 ? 40.334 -35.447 0.778   1.00 22.88 ?  136 PRO   B HD3  1 
ATOM   6128 N N    . ILE   B 1 137 ? 36.808 -35.275 -2.072  1.00 16.58 ?  137 ILE   B N    1 
ATOM   6129 C CA   . ILE   B 1 137 ? 35.596 -35.447 -2.868  1.00 16.69 ?  137 ILE   B CA   1 
ATOM   6130 C C    . ILE   B 1 137 ? 34.519 -34.473 -2.401  1.00 16.54 ?  137 ILE   B C    1 
ATOM   6131 O O    . ILE   B 1 137 ? 33.811 -33.857 -3.210  1.00 16.29 ?  137 ILE   B O    1 
ATOM   6132 C CB   . ILE   B 1 137 ? 35.124 -36.916 -2.802  1.00 18.90 ?  137 ILE   B CB   1 
ATOM   6133 C CG1  . ILE   B 1 137 ? 36.133 -37.829 -3.502  1.00 21.06 ?  137 ILE   B CG1  1 
ATOM   6134 C CG2  . ILE   B 1 137 ? 33.744 -37.069 -3.424  1.00 19.36 ?  137 ILE   B CG2  1 
ATOM   6135 C CD1  . ILE   B 1 137 ? 35.801 -39.309 -3.410  1.00 23.46 ?  137 ILE   B CD1  1 
ATOM   6136 H H    . ILE   B 1 137 ? 37.042 -35.972 -1.629  1.00 19.87 ?  137 ILE   B H    1 
ATOM   6137 H HA   . ILE   B 1 137 ? 35.792 -35.245 -3.798  1.00 20.00 ?  137 ILE   B HA   1 
ATOM   6138 H HB   . ILE   B 1 137 ? 35.067 -37.178 -1.874  1.00 22.66 ?  137 ILE   B HB   1 
ATOM   6139 H HG12 . ILE   B 1 137 ? 36.170 -37.597 -4.443  1.00 25.25 ?  137 ILE   B HG12 1 
ATOM   6140 H HG13 . ILE   B 1 137 ? 37.004 -37.700 -3.097  1.00 25.25 ?  137 ILE   B HG13 1 
ATOM   6141 H HG21 . ILE   B 1 137 ? 33.487 -38.006 -3.414  1.00 23.21 ?  137 ILE   B HG21 1 
ATOM   6142 H HG22 . ILE   B 1 137 ? 33.100 -36.562 -2.910  1.00 23.21 ?  137 ILE   B HG22 1 
ATOM   6143 H HG23 . ILE   B 1 137 ? 33.770 -36.747 -4.338  1.00 23.21 ?  137 ILE   B HG23 1 
ATOM   6144 H HD11 . ILE   B 1 137 ? 36.498 -39.802 -3.863  1.00 28.13 ?  137 ILE   B HD11 1 
ATOM   6145 H HD12 . ILE   B 1 137 ? 35.759 -39.568 -2.475  1.00 28.13 ?  137 ILE   B HD12 1 
ATOM   6146 H HD13 . ILE   B 1 137 ? 34.950 -39.481 -3.842  1.00 28.13 ?  137 ILE   B HD13 1 
ATOM   6147 N N    . HIS   B 1 138 ? 34.381 -34.320 -1.086  1.00 16.81 ?  138 HIS   B N    1 
ATOM   6148 C CA   . HIS   B 1 138 ? 33.430 -33.352 -0.558  1.00 17.22 ?  138 HIS   B CA   1 
ATOM   6149 C C    . HIS   B 1 138 ? 33.854 -31.925 -0.879  1.00 16.33 ?  138 HIS   B C    1 
ATOM   6150 O O    . HIS   B 1 138 ? 33.009 -31.075 -1.176  1.00 16.75 ?  138 HIS   B O    1 
ATOM   6151 C CB   . HIS   B 1 138 ? 33.299 -33.524 0.949   1.00 18.84 ?  138 HIS   B CB   1 
ATOM   6152 C CG   . HIS   B 1 138 ? 32.363 -32.542 1.575   1.00 19.72 ?  138 HIS   B CG   1 
ATOM   6153 N ND1  . HIS   B 1 138 ? 31.027 -32.475 1.242   1.00 21.16 ?  138 HIS   B ND1  1 
ATOM   6154 C CD2  . HIS   B 1 138 ? 32.575 -31.562 2.485   1.00 20.40 ?  138 HIS   B CD2  1 
ATOM   6155 C CE1  . HIS   B 1 138 ? 30.451 -31.511 1.937   1.00 21.15 ?  138 HIS   B CE1  1 
ATOM   6156 N NE2  . HIS   B 1 138 ? 31.368 -30.944 2.702   1.00 20.49 ?  138 HIS   B NE2  1 
ATOM   6157 H H    . HIS   B 1 138 ? 34.819 -34.758 -0.491  1.00 20.14 ?  138 HIS   B H    1 
ATOM   6158 H HA   . HIS   B 1 138 ? 32.559 -33.511 -0.958  1.00 20.64 ?  138 HIS   B HA   1 
ATOM   6159 H HB2  . HIS   B 1 138 ? 32.960 -34.413 1.137   1.00 22.58 ?  138 HIS   B HB2  1 
ATOM   6160 H HB3  . HIS   B 1 138 ? 34.168 -33.406 1.357   1.00 22.58 ?  138 HIS   B HB3  1 
ATOM   6161 H HD1  . HIS   B 1 138 ? 30.628 -32.989 0.676   1.00 25.37 ?  138 HIS   B HD1  1 
ATOM   6162 H HD2  . HIS   B 1 138 ? 33.375 -31.355 2.904   1.00 24.46 ?  138 HIS   B HD2  1 
ATOM   6163 H HE1  . HIS   B 1 138 ? 29.547 -31.277 1.895   1.00 25.36 ?  138 HIS   B HE1  1 
ATOM   6164 N N    . SER   B 1 139 ? 35.154 -31.631 -0.809  1.00 15.63 ?  139 SER   B N    1 
ATOM   6165 C CA   . SER   B 1 139 ? 35.603 -30.284 -1.130  1.00 14.84 ?  139 SER   B CA   1 
ATOM   6166 C C    . SER   B 1 139 ? 35.266 -29.932 -2.567  1.00 13.83 ?  139 SER   B C    1 
ATOM   6167 O O    . SER   B 1 139 ? 34.810 -28.817 -2.841  1.00 14.33 ?  139 SER   B O    1 
ATOM   6168 C CB   . SER   B 1 139 ? 37.099 -30.143 -0.861  1.00 15.47 ?  139 SER   B CB   1 
ATOM   6169 O OG   . SER   B 1 139 ? 37.500 -28.805 -1.093  1.00 15.25 ?  139 SER   B OG   1 
ATOM   6170 H H    . SER   B 1 139 ? 35.772 -32.182 -0.594  1.00 18.73 ?  139 SER   B H    1 
ATOM   6171 H HA   . SER   B 1 139 ? 35.134 -29.657 -0.568  1.00 17.78 ?  139 SER   B HA   1 
ATOM   6172 H HB2  . SER   B 1 139 ? 37.272 -30.383 0.066   1.00 18.54 ?  139 SER   B HB2  1 
ATOM   6173 H HB3  . SER   B 1 139 ? 37.591 -30.729 -1.454  1.00 18.54 ?  139 SER   B HB3  1 
ATOM   6174 H HG   . SER   B 1 139 ? 38.324 -28.720 -0.925  1.00 18.28 ?  139 SER   B HG   1 
ATOM   6175 N N    . LEU   B 1 140 ? 35.464 -30.871 -3.496  1.00 13.54 ?  140 LEU   B N    1 
ATOM   6176 C CA   . LEU   B 1 140 ? 35.097 -30.625 -4.886  1.00 14.00 ?  140 LEU   B CA   1 
ATOM   6177 C C    . LEU   B 1 140 ? 33.592 -30.398 -5.029  1.00 13.84 ?  140 LEU   B C    1 
ATOM   6178 O O    . LEU   B 1 140 ? 33.164 -29.516 -5.779  1.00 14.17 ?  140 LEU   B O    1 
ATOM   6179 C CB   . LEU   B 1 140 ? 35.571 -31.787 -5.762  1.00 14.27 ?  140 LEU   B CB   1 
ATOM   6180 C CG   . LEU   B 1 140 ? 35.204 -31.680 -7.233  1.00 14.49 ?  140 LEU   B CG   1 
ATOM   6181 C CD1  . LEU   B 1 140 ? 35.772 -30.409 -7.832  1.00 15.37 ?  140 LEU   B CD1  1 
ATOM   6182 C CD2  . LEU   B 1 140 ? 35.693 -32.909 -7.974  1.00 15.64 ?  140 LEU   B CD2  1 
ATOM   6183 H H    . LEU   B 1 140 ? 35.802 -31.652 -3.355  1.00 16.23 ?  140 LEU   B H    1 
ATOM   6184 H HA   . LEU   B 1 140 ? 35.553 -29.828 -5.196  1.00 16.77 ?  140 LEU   B HA   1 
ATOM   6185 H HB2  . LEU   B 1 140 ? 36.539 -31.846 -5.714  1.00 17.10 ?  140 LEU   B HB2  1 
ATOM   6186 H HB3  . LEU   B 1 140 ? 35.180 -32.612 -5.430  1.00 17.10 ?  140 LEU   B HB3  1 
ATOM   6187 H HG   . LEU   B 1 140 ? 34.236 -31.641 -7.316  1.00 17.36 ?  140 LEU   B HG   1 
ATOM   6188 H HD11 . LEU   B 1 140 ? 35.664 -30.441 -8.792  1.00 18.42 ?  140 LEU   B HD11 1 
ATOM   6189 H HD12 . LEU   B 1 140 ? 35.294 -29.646 -7.467  1.00 18.42 ?  140 LEU   B HD12 1 
ATOM   6190 H HD13 . LEU   B 1 140 ? 36.713 -30.351 -7.603  1.00 18.42 ?  140 LEU   B HD13 1 
ATOM   6191 H HD21 . LEU   B 1 140 ? 35.445 -32.825 -8.909  1.00 18.74 ?  140 LEU   B HD21 1 
ATOM   6192 H HD22 . LEU   B 1 140 ? 36.651 -32.966 -7.884  1.00 18.74 ?  140 LEU   B HD22 1 
ATOM   6193 H HD23 . LEU   B 1 140 ? 35.268 -33.691 -7.589  1.00 18.74 ?  140 LEU   B HD23 1 
ATOM   6194 N N    . ARG   B 1 141 ? 32.781 -31.187 -4.318  1.00 14.25 ?  141 ARG   B N    1 
ATOM   6195 C CA   . ARG   B 1 141 ? 31.330 -31.006 -4.299  1.00 15.49 ?  141 ARG   B CA   1 
ATOM   6196 C C    . ARG   B 1 141 ? 30.953 -29.591 -3.874  1.00 15.11 ?  141 ARG   B C    1 
ATOM   6197 O O    . ARG   B 1 141 ? 30.151 -28.917 -4.537  1.00 15.24 ?  141 ARG   B O    1 
ATOM   6198 C CB   . ARG   B 1 141 ? 30.744 -32.038 -3.329  1.00 17.12 ?  141 ARG   B CB   1 
ATOM   6199 C CG   . ARG   B 1 141 ? 29.292 -31.891 -2.971  1.00 19.39 ?  141 ARG   B CG   1 
ATOM   6200 C CD   . ARG   B 1 141 ? 28.467 -32.539 -4.006  1.00 21.18 ?  141 ARG   B CD   1 
ATOM   6201 N NE   . ARG   B 1 141 ? 28.203 -31.647 -5.122  1.00 21.62 ?  141 ARG   B NE   1 
ATOM   6202 C CZ   . ARG   B 1 141 ? 28.228 -32.004 -6.399  1.00 20.96 ?  141 ARG   B CZ   1 
ATOM   6203 N NH1  . ARG   B 1 141 ? 28.680 -33.190 -6.781  1.00 20.47 ?  141 ARG   B NH1  1 
ATOM   6204 N NH2  . ARG   B 1 141 ? 27.792 -31.146 -7.316  1.00 21.89 ?  141 ARG   B NH2  1 
ATOM   6205 H H    . ARG   B 1 141 ? 33.059 -31.834 -3.833  1.00 17.08 ?  141 ARG   B H    1 
ATOM   6206 H HA   . ARG   B 1 141 ? 30.972 -31.165 -5.182  1.00 18.56 ?  141 ARG   B HA   1 
ATOM   6207 H HB2  . ARG   B 1 141 ? 30.871 -32.919 -3.718  1.00 20.52 ?  141 ARG   B HB2  1 
ATOM   6208 H HB3  . ARG   B 1 141 ? 31.247 -31.990 -2.503  1.00 20.52 ?  141 ARG   B HB3  1 
ATOM   6209 H HG2  . ARG   B 1 141 ? 29.132 -32.323 -2.121  1.00 23.24 ?  141 ARG   B HG2  1 
ATOM   6210 H HG3  . ARG   B 1 141 ? 29.050 -30.949 -2.919  1.00 23.24 ?  141 ARG   B HG3  1 
ATOM   6211 H HD2  . ARG   B 1 141 ? 28.925 -33.334 -4.332  1.00 25.39 ?  141 ARG   B HD2  1 
ATOM   6212 H HD3  . ARG   B 1 141 ? 27.625 -32.791 -3.612  1.00 25.39 ?  141 ARG   B HD3  1 
ATOM   6213 H HE   . ARG   B 1 141 ? 27.996 -30.831 -4.939  1.00 25.93 ?  141 ARG   B HE   1 
ATOM   6214 H HH11 . ARG   B 1 141 ? 28.956 -33.761 -6.201  1.00 24.54 ?  141 ARG   B HH11 1 
ATOM   6215 H HH12 . ARG   B 1 141 ? 28.692 -33.391 -7.615  1.00 24.54 ?  141 ARG   B HH12 1 
ATOM   6216 H HH21 . ARG   B 1 141 ? 27.506 -30.368 -7.079  1.00 26.25 ?  141 ARG   B HH21 1 
ATOM   6217 H HH22 . ARG   B 1 141 ? 27.821 -31.354 -8.150  1.00 26.25 ?  141 ARG   B HH22 1 
ATOM   6218 N N    . VAL   B 1 142 ? 31.492 -29.141 -2.742  1.00 14.74 ?  142 VAL   B N    1 
ATOM   6219 C CA   . VAL   B 1 142 ? 31.164 -27.804 -2.260  1.00 14.40 ?  142 VAL   B CA   1 
ATOM   6220 C C    . VAL   B 1 142 ? 31.647 -26.751 -3.248  1.00 14.01 ?  142 VAL   B C    1 
ATOM   6221 O O    . VAL   B 1 142 ? 30.953 -25.764 -3.507  1.00 14.91 ?  142 VAL   B O    1 
ATOM   6222 C CB   . VAL   B 1 142 ? 31.717 -27.586 -0.838  1.00 15.07 ?  142 VAL   B CB   1 
ATOM   6223 C CG1  . VAL   B 1 142 ? 31.421 -26.162 -0.362  1.00 15.32 ?  142 VAL   B CG1  1 
ATOM   6224 C CG2  . VAL   B 1 142 ? 31.118 -28.604 0.121   1.00 15.83 ?  142 VAL   B CG2  1 
ATOM   6225 H H    . VAL   B 1 142 ? 32.038 -29.582 -2.242  1.00 17.67 ?  142 VAL   B H    1 
ATOM   6226 H HA   . VAL   B 1 142 ? 30.205 -27.728 -2.205  1.00 17.26 ?  142 VAL   B HA   1 
ATOM   6227 H HB   . VAL   B 1 142 ? 32.680 -27.710 -0.846  1.00 18.06 ?  142 VAL   B HB   1 
ATOM   6228 H HG11 . VAL   B 1 142 ? 31.626 -26.102 0.583   1.00 18.36 ?  142 VAL   B HG11 1 
ATOM   6229 H HG12 . VAL   B 1 142 ? 31.981 -25.542 -0.860  1.00 18.36 ?  142 VAL   B HG12 1 
ATOM   6230 H HG13 . VAL   B 1 142 ? 30.488 -25.967 -0.516  1.00 18.36 ?  142 VAL   B HG13 1 
ATOM   6231 H HG21 . VAL   B 1 142 ? 31.436 -28.421 1.017   1.00 18.97 ?  142 VAL   B HG21 1 
ATOM   6232 H HG22 . VAL   B 1 142 ? 30.151 -28.535 0.089   1.00 18.97 ?  142 VAL   B HG22 1 
ATOM   6233 H HG23 . VAL   B 1 142 ? 31.393 -29.496 -0.153  1.00 18.97 ?  142 VAL   B HG23 1 
ATOM   6234 N N    . CYS   B 1 143 ? 32.833 -26.950 -3.826  1.00 13.65 ?  143 CYS   B N    1 
ATOM   6235 C CA   . CYS   B 1 143 ? 33.330 -26.017 -4.833  1.00 13.90 ?  143 CYS   B CA   1 
ATOM   6236 C C    . CYS   B 1 143 ? 32.335 -25.871 -5.978  1.00 13.83 ?  143 CYS   B C    1 
ATOM   6237 O O    . CYS   B 1 143 ? 31.931 -24.759 -6.334  1.00 13.99 ?  143 CYS   B O    1 
ATOM   6238 C CB   . CYS   B 1 143 ? 34.687 -26.500 -5.358  1.00 14.30 ?  143 CYS   B CB   1 
ATOM   6239 S SG   . CYS   B 1 143 ? 35.447 -25.406 -6.580  1.00 14.07 ?  143 CYS   B SG   1 
ATOM   6240 H H    . CYS   B 1 143 ? 33.366 -27.600 -3.656  1.00 16.36 ?  143 CYS   B H    1 
ATOM   6241 H HA   . CYS   B 1 143 ? 33.462 -25.141 -4.433  1.00 16.66 ?  143 CYS   B HA   1 
ATOM   6242 H HB2  . CYS   B 1 143 ? 35.308 -26.580 -4.615  1.00 17.14 ?  143 CYS   B HB2  1 
ATOM   6243 H HB3  . CYS   B 1 143 ? 34.573 -27.367 -5.775  1.00 17.14 ?  143 CYS   B HB3  1 
ATOM   6244 H HG   . CYS   B 1 143 ? 36.528 -25.841 -6.885  1.00 16.86 ?  143 CYS   B HG   1 
ATOM   6245 N N    . VAL   B 1 144 ? 31.926 -26.990 -6.569  1.00 14.52 ?  144 VAL   B N    1 
ATOM   6246 C CA   . VAL   B 1 144 ? 31.024 -26.932 -7.714  1.00 15.51 ?  144 VAL   B CA   1 
ATOM   6247 C C    . VAL   B 1 144 ? 29.682 -26.317 -7.344  1.00 15.60 ?  144 VAL   B C    1 
ATOM   6248 O O    . VAL   B 1 144 ? 29.069 -25.615 -8.156  1.00 17.00 ?  144 VAL   B O    1 
ATOM   6249 C CB   . VAL   B 1 144 ? 30.862 -28.349 -8.280  1.00 18.16 ?  144 VAL   B CB   1 
ATOM   6250 C CG1  . VAL   B 1 144 ? 29.585 -28.477 -9.116  1.00 20.89 ?  144 VAL   B CG1  1 
ATOM   6251 C CG2  . VAL   B 1 144 ? 32.107 -28.757 -9.064  1.00 18.01 ?  144 VAL   B CG2  1 
ATOM   6252 H H    . VAL   B 1 144 ? 32.155 -27.784 -6.332  1.00 17.40 ?  144 VAL   B H    1 
ATOM   6253 H HA   . VAL   B 1 144 ? 31.418 -26.380 -8.405  1.00 18.58 ?  144 VAL   B HA   1 
ATOM   6254 H HB   . VAL   B 1 144 ? 30.781 -28.969 -7.537  1.00 21.77 ?  144 VAL   B HB   1 
ATOM   6255 H HG11 . VAL   B 1 144 ? 29.662 -29.269 -9.680  1.00 25.05 ?  144 VAL   B HG11 1 
ATOM   6256 H HG12 . VAL   B 1 144 ? 28.827 -28.577 -8.521  1.00 25.05 ?  144 VAL   B HG12 1 
ATOM   6257 H HG13 . VAL   B 1 144 ? 29.485 -27.691 -9.667  1.00 25.05 ?  144 VAL   B HG13 1 
ATOM   6258 H HG21 . VAL   B 1 144 ? 31.984 -29.655 -9.408  1.00 21.59 ?  144 VAL   B HG21 1 
ATOM   6259 H HG22 . VAL   B 1 144 ? 32.230 -28.135 -9.800  1.00 21.59 ?  144 VAL   B HG22 1 
ATOM   6260 H HG23 . VAL   B 1 144 ? 32.873 -28.727 -8.474  1.00 21.59 ?  144 VAL   B HG23 1 
ATOM   6261 N N    . ASP   B 1 145 ? 29.207 -26.562 -6.128  1.00 15.62 ?  145 ASP   B N    1 
ATOM   6262 C CA   . ASP   B 1 145 ? 27.902 -26.086 -5.691  1.00 16.48 ?  145 ASP   B CA   1 
ATOM   6263 C C    . ASP   B 1 145 ? 27.938 -24.664 -5.148  1.00 16.01 ?  145 ASP   B C    1 
ATOM   6264 O O    . ASP   B 1 145 ? 26.878 -24.110 -4.830  1.00 17.83 ?  145 ASP   B O    1 
ATOM   6265 C CB   . ASP   B 1 145 ? 27.338 -27.005 -4.599  1.00 17.96 ?  145 ASP   B CB   1 
ATOM   6266 C CG   . ASP   B 1 145 ? 26.946 -28.375 -5.112  1.00 19.42 ?  145 ASP   B CG   1 
ATOM   6267 O OD1  . ASP   B 1 145 ? 26.854 -28.580 -6.343  1.00 19.66 ?  145 ASP   B OD1  1 
ATOM   6268 O OD2  . ASP   B 1 145 ? 26.734 -29.259 -4.259  1.00 21.54 -1 145 ASP   B OD2  1 
ATOM   6269 H H    . ASP   B 1 145 ? 29.638 -26.991 -5.527  1.00 18.72 ?  145 ASP   B H    1 
ATOM   6270 H HA   . ASP   B 1 145 ? 27.296 -26.089 -6.444  1.00 19.76 ?  145 ASP   B HA   1 
ATOM   6271 H HB2  . ASP   B 1 145 ? 28.011 -27.138 -3.920  1.00 21.53 ?  145 ASP   B HB2  1 
ATOM   6272 H HB3  . ASP   B 1 145 ? 26.549 -26.592 -4.218  1.00 21.53 ?  145 ASP   B HB3  1 
ATOM   6273 N N    . THR   B 1 146 ? 29.121 -24.059 -5.034  1.00 14.11 ?  146 THR   B N    1 
ATOM   6274 C CA   . THR   B 1 146 ? 29.259 -22.732 -4.433  1.00 13.57 ?  146 THR   B CA   1 
ATOM   6275 C C    . THR   B 1 146 ? 29.890 -21.705 -5.355  1.00 13.54 ?  146 THR   B C    1 
ATOM   6276 O O    . THR   B 1 146 ? 29.437 -20.546 -5.400  1.00 13.75 ?  146 THR   B O    1 
ATOM   6277 C CB   . THR   B 1 146 ? 30.084 -22.834 -3.144  1.00 14.15 ?  146 THR   B CB   1 
ATOM   6278 O OG1  . THR   B 1 146 ? 29.500 -23.819 -2.279  1.00 14.28 ?  146 THR   B OG1  1 
ATOM   6279 C CG2  . THR   B 1 146 ? 30.158 -21.484 -2.437  1.00 14.32 ?  146 THR   B CG2  1 
ATOM   6280 H H    . THR   B 1 146 ? 29.869 -24.387 -5.307  1.00 16.91 ?  146 THR   B H    1 
ATOM   6281 H HA   . THR   B 1 146 ? 28.385 -22.400 -4.192  1.00 16.26 ?  146 THR   B HA   1 
ATOM   6282 H HB   . THR   B 1 146 ? 30.994 -23.096 -3.367  1.00 16.95 ?  146 THR   B HB   1 
ATOM   6283 H HG1  . THR   B 1 146 ? 29.530 -24.575 -2.649  1.00 17.11 ?  146 THR   B HG1  1 
ATOM   6284 H HG21 . THR   B 1 146 ? 30.498 -21.601 -1.538  1.00 17.16 ?  146 THR   B HG21 1 
ATOM   6285 H HG22 . THR   B 1 146 ? 30.754 -20.886 -2.921  1.00 17.16 ?  146 THR   B HG22 1 
ATOM   6286 H HG23 . THR   B 1 146 ? 29.278 -21.086 -2.396  1.00 17.16 ?  146 THR   B HG23 1 
ATOM   6287 N N    . VAL   B 1 147 ? 30.951 -22.079 -6.054  1.00 13.31 ?  147 VAL   B N    1 
ATOM   6288 C CA   . VAL   B 1 147 ? 31.676 -21.136 -6.887  1.00 13.32 ?  147 VAL   B CA   1 
ATOM   6289 C C    . VAL   B 1 147 ? 30.948 -21.001 -8.211  1.00 13.52 ?  147 VAL   B C    1 
ATOM   6290 O O    . VAL   B 1 147 ? 30.584 -22.001 -8.843  1.00 14.30 ?  147 VAL   B O    1 
ATOM   6291 C CB   . VAL   B 1 147 ? 33.131 -21.590 -7.090  1.00 13.50 ?  147 VAL   B CB   1 
ATOM   6292 C CG1  . VAL   B 1 147 ? 33.896 -20.560 -7.897  1.00 13.34 ?  147 VAL   B CG1  1 
ATOM   6293 C CG2  . VAL   B 1 147 ? 33.814 -21.805 -5.753  1.00 13.34 ?  147 VAL   B CG2  1 
ATOM   6294 H H    . VAL   B 1 147 ? 31.271 -22.881 -6.071  1.00 15.95 ?  147 VAL   B H    1 
ATOM   6295 H HA   . VAL   B 1 147 ? 31.694 -20.270 -6.455  1.00 15.96 ?  147 VAL   B HA   1 
ATOM   6296 H HB   . VAL   B 1 147 ? 33.147 -22.433 -7.581  1.00 16.18 ?  147 VAL   B HB   1 
ATOM   6297 H HG11 . VAL   B 1 147 ? 34.840 -20.787 -7.892  1.00 15.98 ?  147 VAL   B HG11 1 
ATOM   6298 H HG12 . VAL   B 1 147 ? 33.564 -20.550 -8.807  1.00 15.98 ?  147 VAL   B HG12 1 
ATOM   6299 H HG13 . VAL   B 1 147 ? 33.769 -19.686 -7.489  1.00 15.98 ?  147 VAL   B HG13 1 
ATOM   6300 H HG21 . VAL   B 1 147 ? 34.752 -22.009 -5.901  1.00 15.98 ?  147 VAL   B HG21 1 
ATOM   6301 H HG22 . VAL   B 1 147 ? 33.731 -20.997 -5.224  1.00 15.98 ?  147 VAL   B HG22 1 
ATOM   6302 H HG23 . VAL   B 1 147 ? 33.387 -22.546 -5.292  1.00 15.98 ?  147 VAL   B HG23 1 
ATOM   6303 N N    . ARG   B 1 148 ? 30.746 -19.752 -8.633  1.00 13.39 ?  148 ARG   B N    1 
ATOM   6304 C CA   . ARG   B 1 148 ? 30.122 -19.429 -9.906  1.00 13.42 ?  148 ARG   B CA   1 
ATOM   6305 C C    . ARG   B 1 148 ? 31.080 -18.758 -10.880 1.00 13.36 ?  148 ARG   B C    1 
ATOM   6306 O O    . ARG   B 1 148 ? 30.790 -18.722 -12.079 1.00 15.13 ?  148 ARG   B O    1 
ATOM   6307 C CB   . ARG   B 1 148 ? 28.888 -18.537 -9.686  1.00 13.89 ?  148 ARG   B CB   1 
ATOM   6308 C CG   . ARG   B 1 148 ? 27.812 -19.239 -8.865  1.00 14.68 ?  148 ARG   B CG   1 
ATOM   6309 C CD   . ARG   B 1 148 ? 26.604 -18.346 -8.568  1.00 15.67 ?  148 ARG   B CD   1 
ATOM   6310 N NE   . ARG   B 1 148 ? 26.981 -17.142 -7.839  1.00 15.71 ?  148 ARG   B NE   1 
ATOM   6311 C CZ   . ARG   B 1 148 ? 27.285 -17.106 -6.548  1.00 15.01 ?  148 ARG   B CZ   1 
ATOM   6312 N NH1  . ARG   B 1 148 ? 27.210 -18.189 -5.785  1.00 14.95 ?  148 ARG   B NH1  1 
ATOM   6313 N NH2  . ARG   B 1 148 ? 27.689 -15.957 -6.013  1.00 14.79 ?  148 ARG   B NH2  1 
ATOM   6314 H H    . ARG   B 1 148 ? 30.987 -19.048 -8.186  1.00 16.05 ?  148 ARG   B H    1 
ATOM   6315 H HA   . ARG   B 1 148 ? 29.818 -20.247 -10.316 1.00 16.08 ?  148 ARG   B HA   1 
ATOM   6316 H HB2  . ARG   B 1 148 ? 29.151 -17.732 -9.212  1.00 16.64 ?  148 ARG   B HB2  1 
ATOM   6317 H HB3  . ARG   B 1 148 ? 28.505 -18.304 -10.548 1.00 16.64 ?  148 ARG   B HB3  1 
ATOM   6318 H HG2  . ARG   B 1 148 ? 27.500 -20.017 -9.359  1.00 17.59 ?  148 ARG   B HG2  1 
ATOM   6319 H HG3  . ARG   B 1 148 ? 28.197 -19.521 -8.020  1.00 17.59 ?  148 ARG   B HG3  1 
ATOM   6320 H HD2  . ARG   B 1 148 ? 26.195 -18.083 -9.404  1.00 18.78 ?  148 ARG   B HD2  1 
ATOM   6321 H HD3  . ARG   B 1 148 ? 25.971 -18.847 -8.028  1.00 18.78 ?  148 ARG   B HD3  1 
ATOM   6322 H HE   . ARG   B 1 148 ? 27.017 -16.409 -8.279  1.00 18.82 ?  148 ARG   B HE   1 
ATOM   6323 H HH11 . ARG   B 1 148 ? 26.950 -18.941 -6.117  1.00 17.92 ?  148 ARG   B HH11 1 
ATOM   6324 H HH12 . ARG   B 1 148 ? 27.407 -18.141 -4.947  1.00 17.92 ?  148 ARG   B HH12 1 
ATOM   6325 H HH21 . ARG   B 1 148 ? 27.744 -15.253 -6.503  1.00 17.72 ?  148 ARG   B HH21 1 
ATOM   6326 H HH22 . ARG   B 1 148 ? 27.887 -15.916 -5.179  1.00 17.72 ?  148 ARG   B HH22 1 
ATOM   6327 N N    . THR   B 1 149 ? 32.194 -18.217 -10.393 1.00 13.24 ?  149 THR   B N    1 
ATOM   6328 C CA   . THR   B 1 149 ? 33.235 -17.648 -11.236 1.00 13.22 ?  149 THR   B CA   1 
ATOM   6329 C C    . THR   B 1 149 ? 34.119 -18.785 -11.746 1.00 12.99 ?  149 THR   B C    1 
ATOM   6330 O O    . THR   B 1 149 ? 33.922 -19.955 -11.408 1.00 13.31 ?  149 THR   B O    1 
ATOM   6331 C CB   . THR   B 1 149 ? 34.005 -16.595 -10.451 1.00 13.52 ?  149 THR   B CB   1 
ATOM   6332 O OG1  . THR   B 1 149 ? 34.468 -17.194 -9.239  1.00 13.62 ?  149 THR   B OG1  1 
ATOM   6333 C CG2  . THR   B 1 149 ? 33.107 -15.396 -10.148 1.00 14.33 ?  149 THR   B CG2  1 
ATOM   6334 H H    . THR   B 1 149 ? 32.366 -18.164 -9.552  1.00 15.87 ?  149 THR   B H    1 
ATOM   6335 H HA   . THR   B 1 149 ? 32.823 -17.216 -11.999 1.00 15.84 ?  149 THR   B HA   1 
ATOM   6336 H HB   . THR   B 1 149 ? 34.762 -16.297 -10.970 1.00 16.20 ?  149 THR   B HB   1 
ATOM   6337 H HG1  . THR   B 1 149 ? 34.888 -16.621 -8.779  1.00 16.32 ?  149 THR   B HG1  1 
ATOM   6338 H HG21 . THR   B 1 149 ? 33.609 -14.723 -9.663  1.00 17.17 ?  149 THR   B HG21 1 
ATOM   6339 H HG22 . THR   B 1 149 ? 32.781 -15.010 -10.976 1.00 17.17 ?  149 THR   B HG22 1 
ATOM   6340 H HG23 . THR   B 1 149 ? 32.349 -15.673 -9.610  1.00 17.17 ?  149 THR   B HG23 1 
ATOM   6341 N N    . ASN   B 1 150 ? 35.089 -18.464 -12.592 1.00 13.08 ?  150 ASN   B N    1 
ATOM   6342 C CA   . ASN   B 1 150 ? 35.856 -19.496 -13.284 1.00 13.54 ?  150 ASN   B CA   1 
ATOM   6343 C C    . ASN   B 1 150 ? 37.018 -19.948 -12.409 1.00 13.08 ?  150 ASN   B C    1 
ATOM   6344 O O    . ASN   B 1 150 ? 37.945 -19.177 -12.148 1.00 13.83 ?  150 ASN   B O    1 
ATOM   6345 C CB   . ASN   B 1 150 ? 36.335 -18.970 -14.628 1.00 15.24 ?  150 ASN   B CB   1 
ATOM   6346 C CG   . ASN   B 1 150 ? 35.195 -18.744 -15.576 1.00 18.12 ?  150 ASN   B CG   1 
ATOM   6347 O OD1  . ASN   B 1 150 ? 34.286 -19.562 -15.657 1.00 18.65 ?  150 ASN   B OD1  1 
ATOM   6348 N ND2  . ASN   B 1 150 ? 35.205 -17.617 -16.266 1.00 20.08 ?  150 ASN   B ND2  1 
ATOM   6349 H H    . ASN   B 1 150 ? 35.328 -17.660 -12.774 1.00 15.68 ?  150 ASN   B H    1 
ATOM   6350 H HA   . ASN   B 1 150 ? 35.278 -20.264 -13.445 1.00 16.22 ?  150 ASN   B HA   1 
ATOM   6351 H HB2  . ASN   B 1 150 ? 36.788 -18.123 -14.488 1.00 18.26 ?  150 ASN   B HB2  1 
ATOM   6352 H HB3  . ASN   B 1 150 ? 36.937 -19.614 -15.024 1.00 18.26 ?  150 ASN   B HB3  1 
ATOM   6353 H HD21 . ASN   B 1 150 ? 34.572 -17.442 -16.821 1.00 24.07 ?  150 ASN   B HD21 1 
ATOM   6354 H HD22 . ASN   B 1 150 ? 35.860 -17.063 -16.176 1.00 24.07 ?  150 ASN   B HD22 1 
ATOM   6355 N N    . VAL   B 1 151 ? 36.975 -21.199 -11.960 1.00 12.78 ?  151 VAL   B N    1 
ATOM   6356 C CA   . VAL   B 1 151 ? 37.986 -21.737 -11.065 1.00 12.65 ?  151 VAL   B CA   1 
ATOM   6357 C C    . VAL   B 1 151 ? 38.689 -22.903 -11.740 1.00 12.31 ?  151 VAL   B C    1 
ATOM   6358 O O    . VAL   B 1 151 ? 38.046 -23.838 -12.237 1.00 14.11 ?  151 VAL   B O    1 
ATOM   6359 C CB   . VAL   B 1 151 ? 37.425 -22.076 -9.670  1.00 14.05 ?  151 VAL   B CB   1 
ATOM   6360 C CG1  . VAL   B 1 151 ? 36.262 -23.062 -9.751  1.00 15.57 ?  151 VAL   B CG1  1 
ATOM   6361 C CG2  . VAL   B 1 151 ? 38.537 -22.582 -8.761  1.00 14.54 ?  151 VAL   B CG2  1 
ATOM   6362 H H    . VAL   B 1 151 ? 36.360 -21.770 -12.174 1.00 15.32 ?  151 VAL   B H    1 
ATOM   6363 H HA   . VAL   B 1 151 ? 38.652 -21.043 -10.930 1.00 15.15 ?  151 VAL   B HA   1 
ATOM   6364 H HB   . VAL   B 1 151 ? 37.081 -21.257 -9.273  1.00 16.84 ?  151 VAL   B HB   1 
ATOM   6365 H HG11 . VAL   B 1 151 ? 35.940 -23.249 -8.854  1.00 18.66 ?  151 VAL   B HG11 1 
ATOM   6366 H HG12 . VAL   B 1 151 ? 35.547 -22.672 -10.281 1.00 18.66 ?  151 VAL   B HG12 1 
ATOM   6367 H HG13 . VAL   B 1 151 ? 36.570 -23.883 -10.167 1.00 18.66 ?  151 VAL   B HG13 1 
ATOM   6368 H HG21 . VAL   B 1 151 ? 38.193 -22.647 -7.855  1.00 17.42 ?  151 VAL   B HG21 1 
ATOM   6369 H HG22 . VAL   B 1 151 ? 38.821 -23.456 -9.069  1.00 17.42 ?  151 VAL   B HG22 1 
ATOM   6370 H HG23 . VAL   B 1 151 ? 39.277 -21.959 -8.789  1.00 17.42 ?  151 VAL   B HG23 1 
ATOM   6371 N N    . TYR   B 1 152 ? 40.017 -22.813 -11.762 1.00 12.16 ?  152 TYR   B N    1 
ATOM   6372 C CA   . TYR   B 1 152 ? 40.922 -23.798 -12.336 1.00 11.95 ?  152 TYR   B CA   1 
ATOM   6373 C C    . TYR   B 1 152 ? 41.642 -24.476 -11.176 1.00 11.48 ?  152 TYR   B C    1 
ATOM   6374 O O    . TYR   B 1 152 ? 42.497 -23.860 -10.532 1.00 12.31 ?  152 TYR   B O    1 
ATOM   6375 C CB   . TYR   B 1 152 ? 41.896 -23.099 -13.286 1.00 12.97 ?  152 TYR   B CB   1 
ATOM   6376 C CG   . TYR   B 1 152 ? 41.218 -22.635 -14.554 1.00 13.60 ?  152 TYR   B CG   1 
ATOM   6377 C CD1  . TYR   B 1 152 ? 40.566 -21.403 -14.623 1.00 13.90 ?  152 TYR   B CD1  1 
ATOM   6378 C CD2  . TYR   B 1 152 ? 41.205 -23.445 -15.676 1.00 14.66 ?  152 TYR   B CD2  1 
ATOM   6379 C CE1  . TYR   B 1 152 ? 39.932 -20.999 -15.779 1.00 15.72 ?  152 TYR   B CE1  1 
ATOM   6380 C CE2  . TYR   B 1 152 ? 40.569 -23.055 -16.834 1.00 15.52 ?  152 TYR   B CE2  1 
ATOM   6381 C CZ   . TYR   B 1 152 ? 39.933 -21.827 -16.883 1.00 16.09 ?  152 TYR   B CZ   1 
ATOM   6382 O OH   . TYR   B 1 152 ? 39.304 -21.436 -18.040 1.00 19.03 ?  152 TYR   B OH   1 
ATOM   6383 H H    . TYR   B 1 152 ? 40.445 -22.138 -11.423 1.00 14.57 ?  152 TYR   B H    1 
ATOM   6384 H HA   . TYR   B 1 152 ? 40.413 -24.458 -12.831 1.00 14.31 ?  152 TYR   B HA   1 
ATOM   6385 H HB2  . TYR   B 1 152 ? 42.272 -22.322 -12.841 1.00 15.54 ?  152 TYR   B HB2  1 
ATOM   6386 H HB3  . TYR   B 1 152 ? 42.602 -23.717 -13.529 1.00 15.54 ?  152 TYR   B HB3  1 
ATOM   6387 H HD1  . TYR   B 1 152 ? 40.558 -20.843 -13.878 1.00 16.66 ?  152 TYR   B HD1  1 
ATOM   6388 H HD2  . TYR   B 1 152 ? 41.627 -24.277 -15.646 1.00 17.57 ?  152 TYR   B HD2  1 
ATOM   6389 H HE1  . TYR   B 1 152 ? 39.502 -20.175 -15.819 1.00 18.84 ?  152 TYR   B HE1  1 
ATOM   6390 H HE2  . TYR   B 1 152 ? 40.574 -23.612 -17.583 1.00 18.60 ?  152 TYR   B HE2  1 
ATOM   6391 H HH   . TYR   B 1 152 ? 39.389 -22.027 -18.630 1.00 22.81 ?  152 TYR   B HH   1 
ATOM   6392 N N    . LEU   B 1 153 ? 41.269 -25.728 -10.901 1.00 11.94 ?  153 LEU   B N    1 
ATOM   6393 C CA   . LEU   B 1 153 ? 41.780 -26.476 -9.762  1.00 11.81 ?  153 LEU   B CA   1 
ATOM   6394 C C    . LEU   B 1 153 ? 43.009 -27.284 -10.153 1.00 11.99 ?  153 LEU   B C    1 
ATOM   6395 O O    . LEU   B 1 153 ? 42.990 -28.012 -11.145 1.00 12.97 ?  153 LEU   B O    1 
ATOM   6396 C CB   . LEU   B 1 153 ? 40.699 -27.426 -9.239  1.00 11.90 ?  153 LEU   B CB   1 
ATOM   6397 C CG   . LEU   B 1 153 ? 39.439 -26.770 -8.663  1.00 13.16 ?  153 LEU   B CG   1 
ATOM   6398 C CD1  . LEU   B 1 153 ? 38.308 -27.794 -8.527  1.00 14.23 ?  153 LEU   B CD1  1 
ATOM   6399 C CD2  . LEU   B 1 153 ? 39.734 -26.108 -7.317  1.00 13.95 ?  153 LEU   B CD2  1 
ATOM   6400 H H    . LEU   B 1 153 ? 40.698 -26.175 -11.378 1.00 14.31 ?  153 LEU   B H    1 
ATOM   6401 H HA   . LEU   B 1 153 ? 42.015 -25.858 -9.057  1.00 14.15 ?  153 LEU   B HA   1 
ATOM   6402 H HB2  . LEU   B 1 153 ? 40.416 -28.001 -9.963  1.00 14.26 ?  153 LEU   B HB2  1 
ATOM   6403 H HB3  . LEU   B 1 153 ? 41.088 -27.966 -8.530  1.00 14.26 ?  153 LEU   B HB3  1 
ATOM   6404 H HG   . LEU   B 1 153 ? 39.140 -26.071 -9.270  1.00 15.77 ?  153 LEU   B HG   1 
ATOM   6405 H HD11 . LEU   B 1 153 ? 37.502 -27.333 -8.238  1.00 17.05 ?  153 LEU   B HD11 1 
ATOM   6406 H HD12 . LEU   B 1 153 ? 38.160 -28.206 -9.389  1.00 17.05 ?  153 LEU   B HD12 1 
ATOM   6407 H HD13 . LEU   B 1 153 ? 38.564 -28.456 -7.873  1.00 17.05 ?  153 LEU   B HD13 1 
ATOM   6408 H HD21 . LEU   B 1 153 ? 38.921 -25.720 -6.964  1.00 16.72 ?  153 LEU   B HD21 1 
ATOM   6409 H HD22 . LEU   B 1 153 ? 40.075 -26.780 -6.705  1.00 16.72 ?  153 LEU   B HD22 1 
ATOM   6410 H HD23 . LEU   B 1 153 ? 40.404 -25.414 -7.445  1.00 16.72 ?  153 LEU   B HD23 1 
ATOM   6411 N N    . ALA   B 1 154 ? 44.063 -27.166 -9.352  1.00 12.10 ?  154 ALA   B N    1 
ATOM   6412 C CA   . ALA   B 1 154 ? 45.292 -27.933 -9.522  1.00 13.10 ?  154 ALA   B CA   1 
ATOM   6413 C C    . ALA   B 1 154 ? 45.359 -29.005 -8.438  1.00 13.64 ?  154 ALA   B C    1 
ATOM   6414 O O    . ALA   B 1 154 ? 45.292 -28.699 -7.240  1.00 15.13 ?  154 ALA   B O    1 
ATOM   6415 C CB   . ALA   B 1 154 ? 46.517 -27.022 -9.463  1.00 13.88 ?  154 ALA   B CB   1 
ATOM   6416 H H    . ALA   B 1 154 ? 44.082 -26.625 -8.680  1.00 14.50 ?  154 ALA   B H    1 
ATOM   6417 H HA   . ALA   B 1 154 ? 45.277 -28.370 -10.384 1.00 15.69 ?  154 ALA   B HA   1 
ATOM   6418 H HB1  . ALA   B 1 154 ? 47.315 -27.559 -9.579  1.00 16.64 ?  154 ALA   B HB1  1 
ATOM   6419 H HB2  . ALA   B 1 154 ? 46.456 -26.363 -10.176 1.00 16.64 ?  154 ALA   B HB2  1 
ATOM   6420 H HB3  . ALA   B 1 154 ? 46.540 -26.573 -8.603  1.00 16.64 ?  154 ALA   B HB3  1 
ATOM   6421 N N    . VAL   B 1 155 ? 45.472 -30.259 -8.862  1.00 13.28 ?  155 VAL   B N    1 
ATOM   6422 C CA   . VAL   B 1 155 ? 45.578 -31.406 -7.969  1.00 13.75 ?  155 VAL   B CA   1 
ATOM   6423 C C    . VAL   B 1 155 ? 46.917 -32.079 -8.247  1.00 13.15 ?  155 VAL   B C    1 
ATOM   6424 O O    . VAL   B 1 155 ? 47.148 -32.584 -9.355  1.00 15.12 ?  155 VAL   B O    1 
ATOM   6425 C CB   . VAL   B 1 155 ? 44.417 -32.399 -8.171  1.00 15.09 ?  155 VAL   B CB   1 
ATOM   6426 C CG1  . VAL   B 1 155 ? 44.592 -33.599 -7.252  1.00 15.54 ?  155 VAL   B CG1  1 
ATOM   6427 C CG2  . VAL   B 1 155 ? 43.070 -31.712 -7.934  1.00 16.03 ?  155 VAL   B CG2  1 
ATOM   6428 H H    . VAL   B 1 155 ? 45.505 -30.474 -9.694  1.00 15.91 ?  155 VAL   B H    1 
ATOM   6429 H HA   . VAL   B 1 155 ? 45.567 -31.105 -7.045  1.00 16.48 ?  155 VAL   B HA   1 
ATOM   6430 H HB   . VAL   B 1 155 ? 44.431 -32.713 -9.088  1.00 18.09 ?  155 VAL   B HB   1 
ATOM   6431 H HG11 . VAL   B 1 155 ? 43.763 -34.105 -7.230  1.00 18.62 ?  155 VAL   B HG11 1 
ATOM   6432 H HG12 . VAL   B 1 155 ? 45.307 -34.162 -7.592  1.00 18.62 ?  155 VAL   B HG12 1 
ATOM   6433 H HG13 . VAL   B 1 155 ? 44.810 -33.290 -6.359  1.00 18.62 ?  155 VAL   B HG13 1 
ATOM   6434 H HG21 . VAL   B 1 155 ? 42.363 -32.372 -8.027  1.00 19.21 ?  155 VAL   B HG21 1 
ATOM   6435 H HG22 . VAL   B 1 155 ? 43.060 -31.341 -7.039  1.00 19.21 ?  155 VAL   B HG22 1 
ATOM   6436 H HG23 . VAL   B 1 155 ? 42.953 -31.007 -8.588  1.00 19.21 ?  155 VAL   B HG23 1 
ATOM   6437 N N    . PHE   B 1 156 ? 47.783 -32.115 -7.234  1.00 13.58 ?  156 PHE   B N    1 
ATOM   6438 C CA   . PHE   B 1 156 ? 49.157 -32.581 -7.433  1.00 15.00 ?  156 PHE   B CA   1 
ATOM   6439 C C    . PHE   B 1 156 ? 49.242 -34.083 -7.707  1.00 16.35 ?  156 PHE   B C    1 
ATOM   6440 O O    . PHE   B 1 156 ? 49.959 -34.516 -8.619  1.00 18.26 ?  156 PHE   B O    1 
ATOM   6441 C CB   . PHE   B 1 156 ? 49.994 -32.211 -6.211  1.00 14.89 ?  156 PHE   B CB   1 
ATOM   6442 C CG   . PHE   B 1 156 ? 51.420 -32.676 -6.280  1.00 15.46 ?  156 PHE   B CG   1 
ATOM   6443 C CD1  . PHE   B 1 156 ? 52.292 -32.142 -7.210  1.00 17.16 ?  156 PHE   B CD1  1 
ATOM   6444 C CD2  . PHE   B 1 156 ? 51.888 -33.634 -5.404  1.00 16.12 ?  156 PHE   B CD2  1 
ATOM   6445 C CE1  . PHE   B 1 156 ? 53.613 -32.560 -7.269  1.00 18.43 ?  156 PHE   B CE1  1 
ATOM   6446 C CE2  . PHE   B 1 156 ? 53.203 -34.056 -5.458  1.00 17.37 ?  156 PHE   B CE2  1 
ATOM   6447 C CZ   . PHE   B 1 156 ? 54.060 -33.518 -6.396  1.00 18.44 ?  156 PHE   B CZ   1 
ATOM   6448 H H    . PHE   B 1 156 ? 47.600 -31.882 -6.426  1.00 16.27 ?  156 PHE   B H    1 
ATOM   6449 H HA   . PHE   B 1 156 ? 49.529 -32.121 -8.198  1.00 17.97 ?  156 PHE   B HA   1 
ATOM   6450 H HB2  . PHE   B 1 156 ? 50.003 -31.245 -6.126  1.00 17.85 ?  156 PHE   B HB2  1 
ATOM   6451 H HB3  . PHE   B 1 156 ? 49.594 -32.608 -5.424  1.00 17.85 ?  156 PHE   B HB3  1 
ATOM   6452 H HD1  . PHE   B 1 156 ? 51.991 -31.489 -7.806  1.00 20.57 ?  156 PHE   B HD1  1 
ATOM   6453 H HD2  . PHE   B 1 156 ? 51.308 -34.001 -4.774  1.00 19.32 ?  156 PHE   B HD2  1 
ATOM   6454 H HE1  . PHE   B 1 156 ? 54.194 -32.196 -7.902  1.00 22.09 ?  156 PHE   B HE1  1 
ATOM   6455 H HE2  . PHE   B 1 156 ? 53.507 -34.709 -4.867  1.00 20.82 ?  156 PHE   B HE2  1 
ATOM   6456 H HZ   . PHE   B 1 156 ? 54.947 -33.805 -6.432  1.00 22.10 ?  156 PHE   B HZ   1 
ATOM   6457 N N    . ASP   B 1 157 ? 48.575 -34.898 -6.900  1.00 17.10 ?  157 ASP   B N    1 
ATOM   6458 C CA   . ASP   B 1 157 ? 48.716 -36.350 -6.994  1.00 18.49 ?  157 ASP   B CA   1 
ATOM   6459 C C    . ASP   B 1 157 ? 47.803 -36.899 -8.087  1.00 18.69 ?  157 ASP   B C    1 
ATOM   6460 O O    . ASP   B 1 157 ? 46.578 -36.786 -7.986  1.00 18.13 ?  157 ASP   B O    1 
ATOM   6461 C CB   . ASP   B 1 157 ? 48.341 -36.955 -5.648  1.00 19.81 ?  157 ASP   B CB   1 
ATOM   6462 C CG   . ASP   B 1 157 ? 48.482 -38.467 -5.617  1.00 22.13 ?  157 ASP   B CG   1 
ATOM   6463 O OD1  . ASP   B 1 157 ? 48.828 -39.086 -6.653  1.00 22.76 ?  157 ASP   B OD1  1 
ATOM   6464 O OD2  . ASP   B 1 157 ? 48.255 -39.033 -4.533  1.00 23.86 -1 157 ASP   B OD2  1 
ATOM   6465 H H    . ASP   B 1 157 ? 48.040 -34.638 -6.283  1.00 20.49 ?  157 ASP   B H    1 
ATOM   6466 H HA   . ASP   B 1 157 ? 49.637 -36.585 -7.200  1.00 22.16 ?  157 ASP   B HA   1 
ATOM   6467 H HB2  . ASP   B 1 157 ? 48.904 -36.566 -4.963  1.00 23.75 ?  157 ASP   B HB2  1 
ATOM   6468 H HB3  . ASP   B 1 157 ? 47.409 -36.743 -5.463  1.00 23.75 ?  157 ASP   B HB3  1 
ATOM   6469 N N    . LYS   B 1 158 ? 48.399 -37.513 -9.118  1.00 20.00 ?  158 LYS   B N    1 
ATOM   6470 C CA   . LYS   B 1 158 ? 47.624 -38.135 -10.198 1.00 21.12 ?  158 LYS   B CA   1 
ATOM   6471 C C    . LYS   B 1 158 ? 46.559 -39.094 -9.665  1.00 20.96 ?  158 LYS   B C    1 
ATOM   6472 O O    . LYS   B 1 158 ? 45.452 -39.175 -10.213 1.00 20.82 ?  158 LYS   B O    1 
ATOM   6473 C CB   . LYS   B 1 158 ? 48.568 -38.871 -11.158 1.00 22.98 ?  158 LYS   B CB   1 
ATOM   6474 C CG   . LYS   B 1 158 ? 47.880 -39.751 -12.195 1.00 25.13 ?  158 LYS   B CG   1 
ATOM   6475 C CD   . LYS   B 1 158 ? 47.053 -38.947 -13.179 1.00 27.27 ?  158 LYS   B CD   1 
ATOM   6476 C CE   . LYS   B 1 158 ? 46.448 -39.857 -14.238 1.00 29.13 ?  158 LYS   B CE   1 
ATOM   6477 N NZ   . LYS   B 1 158 ? 45.374 -39.186 -15.023 1.00 29.68 ?  158 LYS   B NZ   1 
ATOM   6478 H H    . LYS   B 1 158 ? 49.253 -37.582 -9.218  1.00 23.97 ?  158 LYS   B H    1 
ATOM   6479 H HA   . LYS   B 1 158 ? 47.177 -37.437 -10.707 1.00 25.33 ?  158 LYS   B HA   1 
ATOM   6480 H HB2  . LYS   B 1 158 ? 49.095 -38.213 -11.645 1.00 27.56 ?  158 LYS   B HB2  1 
ATOM   6481 H HB3  . LYS   B 1 158 ? 49.159 -39.437 -10.641 1.00 27.56 ?  158 LYS   B HB3  1 
ATOM   6482 H HG2  . LYS   B 1 158 ? 48.559 -40.226 -12.700 1.00 30.13 ?  158 LYS   B HG2  1 
ATOM   6483 H HG3  . LYS   B 1 158 ? 47.298 -40.392 -11.756 1.00 30.13 ?  158 LYS   B HG3  1 
ATOM   6484 H HD2  . LYS   B 1 158 ? 46.332 -38.501 -12.710 1.00 32.70 ?  158 LYS   B HD2  1 
ATOM   6485 H HD3  . LYS   B 1 158 ? 47.621 -38.298 -13.624 1.00 32.70 ?  158 LYS   B HD3  1 
ATOM   6486 H HE2  . LYS   B 1 158 ? 47.142 -40.132 -14.855 1.00 34.93 ?  158 LYS   B HE2  1 
ATOM   6487 H HE3  . LYS   B 1 158 ? 46.061 -40.634 -13.805 1.00 34.93 ?  158 LYS   B HE3  1 
ATOM   6488 H HZ1  . LYS   B 1 158 ? 45.044 -39.747 -15.629 1.00 35.59 ?  158 LYS   B HZ1  1 
ATOM   6489 H HZ2  . LYS   B 1 158 ? 44.717 -38.926 -14.481 1.00 35.59 ?  158 LYS   B HZ2  1 
ATOM   6490 H HZ3  . LYS   B 1 158 ? 45.704 -38.471 -15.439 1.00 35.59 ?  158 LYS   B HZ3  1 
ATOM   6491 N N    . ASN   B 1 159 ? 46.877 -39.847 -8.613  1.00 21.22 ?  159 ASN   B N    1 
ATOM   6492 C CA   . ASN   B 1 159 ? 45.922 -40.828 -8.109  1.00 21.64 ?  159 ASN   B CA   1 
ATOM   6493 C C    . ASN   B 1 159 ? 44.725 -40.153 -7.438  1.00 20.08 ?  159 ASN   B C    1 
ATOM   6494 O O    . ASN   B 1 159 ? 43.593 -40.644 -7.541  1.00 20.61 ?  159 ASN   B O    1 
ATOM   6495 C CB   . ASN   B 1 159 ? 46.626 -41.802 -7.167  1.00 23.22 ?  159 ASN   B CB   1 
ATOM   6496 C CG   . ASN   B 1 159 ? 47.653 -42.658 -7.881  1.00 25.09 ?  159 ASN   B CG   1 
ATOM   6497 O OD1  . ASN   B 1 159 ? 47.413 -43.139 -8.996  1.00 25.72 ?  159 ASN   B OD1  1 
ATOM   6498 N ND2  . ASN   B 1 159 ? 48.803 -42.859 -7.243  1.00 25.88 ?  159 ASN   B ND2  1 
ATOM   6499 H H    . ASN   B 1 159 ? 47.623 -39.801 -8.188  1.00 25.44 ?  159 ASN   B H    1 
ATOM   6500 H HA   . ASN   B 1 159 ? 45.590 -41.337 -8.867  1.00 25.94 ?  159 ASN   B HA   1 
ATOM   6501 H HB2  . ASN   B 1 159 ? 47.079 -41.302 -6.474  1.00 27.85 ?  159 ASN   B HB2  1 
ATOM   6502 H HB3  . ASN   B 1 159 ? 45.965 -42.394 -6.783  1.00 27.85 ?  159 ASN   B HB3  1 
ATOM   6503 H HD21 . ASN   B 1 159 ? 49.422 -43.340 -7.603  1.00 31.04 ?  159 ASN   B HD21 1 
ATOM   6504 H HD22 . ASN   B 1 159 ? 48.927 -42.523 -6.460  1.00 31.04 ?  159 ASN   B HD22 1 
ATOM   6505 N N    . LEU   B 1 160 ? 44.940 -39.029 -6.750  1.00 19.12 ?  160 LEU   B N    1 
ATOM   6506 C CA   . LEU   B 1 160 ? 43.806 -38.294 -6.206  1.00 17.94 ?  160 LEU   B CA   1 
ATOM   6507 C C    . LEU   B 1 160 ? 43.020 -37.621 -7.320  1.00 16.77 ?  160 LEU   B C    1 
ATOM   6508 O O    . LEU   B 1 160 ? 41.782 -37.617 -7.304  1.00 16.61 ?  160 LEU   B O    1 
ATOM   6509 C CB   . LEU   B 1 160 ? 44.280 -37.262 -5.184  1.00 17.59 ?  160 LEU   B CB   1 
ATOM   6510 C CG   . LEU   B 1 160 ? 43.151 -36.360 -4.667  1.00 17.42 ?  160 LEU   B CG   1 
ATOM   6511 C CD1  . LEU   B 1 160 ? 42.046 -37.195 -4.035  1.00 18.72 ?  160 LEU   B CD1  1 
ATOM   6512 C CD2  . LEU   B 1 160 ? 43.698 -35.339 -3.676  1.00 17.33 ?  160 LEU   B CD2  1 
ATOM   6513 H H    . LEU   B 1 160 ? 45.713 -38.684 -6.594  1.00 22.92 ?  160 LEU   B H    1 
ATOM   6514 H HA   . LEU   B 1 160 ? 43.216 -38.919 -5.760  1.00 21.50 ?  160 LEU   B HA   1 
ATOM   6515 H HB2  . LEU   B 1 160 ? 44.665 -37.729 -4.426  1.00 21.08 ?  160 LEU   B HB2  1 
ATOM   6516 H HB3  . LEU   B 1 160 ? 44.954 -36.697 -5.600  1.00 21.08 ?  160 LEU   B HB3  1 
ATOM   6517 H HG   . LEU   B 1 160 ? 42.770 -35.870 -5.413  1.00 20.89 ?  160 LEU   B HG   1 
ATOM   6518 H HD11 . LEU   B 1 160 ? 41.430 -36.606 -3.580  1.00 22.44 ?  160 LEU   B HD11 1 
ATOM   6519 H HD12 . LEU   B 1 160 ? 41.581 -37.690 -4.730  1.00 22.44 ?  160 LEU   B HD12 1 
ATOM   6520 H HD13 . LEU   B 1 160 ? 42.444 -37.816 -3.401  1.00 22.44 ?  160 LEU   B HD13 1 
ATOM   6521 H HD21 . LEU   B 1 160 ? 42.973 -34.766 -3.388  1.00 20.77 ?  160 LEU   B HD21 1 
ATOM   6522 H HD22 . LEU   B 1 160 ? 44.074 -35.810 -2.917  1.00 20.77 ?  160 LEU   B HD22 1 
ATOM   6523 H HD23 . LEU   B 1 160 ? 44.386 -34.813 -4.113  1.00 20.77 ?  160 LEU   B HD23 1 
ATOM   6524 N N    . TYR   B 1 161 ? 43.722 -37.052 -8.302  1.00 17.13 ?  161 TYR   B N    1 
ATOM   6525 C CA   . TYR   B 1 161 ? 43.055 -36.486 -9.469  1.00 17.09 ?  161 TYR   B CA   1 
ATOM   6526 C C    . TYR   B 1 161 ? 42.106 -37.503 -10.090 1.00 16.85 ?  161 TYR   B C    1 
ATOM   6527 O O    . TYR   B 1 161 ? 40.932 -37.208 -10.336 1.00 16.77 ?  161 TYR   B O    1 
ATOM   6528 C CB   . TYR   B 1 161 ? 44.100 -36.009 -10.488 1.00 17.73 ?  161 TYR   B CB   1 
ATOM   6529 C CG   . TYR   B 1 161 ? 43.523 -35.541 -11.806 1.00 18.33 ?  161 TYR   B CG   1 
ATOM   6530 C CD1  . TYR   B 1 161 ? 43.132 -34.218 -11.978 1.00 18.70 ?  161 TYR   B CD1  1 
ATOM   6531 C CD2  . TYR   B 1 161 ? 43.359 -36.418 -12.875 1.00 19.01 ?  161 TYR   B CD2  1 
ATOM   6532 C CE1  . TYR   B 1 161 ? 42.608 -33.783 -13.169 1.00 19.41 ?  161 TYR   B CE1  1 
ATOM   6533 C CE2  . TYR   B 1 161 ? 42.829 -35.990 -14.069 1.00 20.10 ?  161 TYR   B CE2  1 
ATOM   6534 C CZ   . TYR   B 1 161 ? 42.456 -34.670 -14.212 1.00 20.35 ?  161 TYR   B CZ   1 
ATOM   6535 O OH   . TYR   B 1 161 ? 41.924 -34.235 -15.401 1.00 22.56 ?  161 TYR   B OH   1 
ATOM   6536 H H    . TYR   B 1 161 ? 44.579 -36.990 -8.319  1.00 20.53 ?  161 TYR   B H    1 
ATOM   6537 H HA   . TYR   B 1 161 ? 42.534 -35.716 -9.195  1.00 20.48 ?  161 TYR   B HA   1 
ATOM   6538 H HB2  . TYR   B 1 161 ? 44.591 -35.263 -10.106 1.00 21.25 ?  161 TYR   B HB2  1 
ATOM   6539 H HB3  . TYR   B 1 161 ? 44.709 -36.737 -10.680 1.00 21.25 ?  161 TYR   B HB3  1 
ATOM   6540 H HD1  . TYR   B 1 161 ? 43.239 -33.609 -11.280 1.00 22.41 ?  161 TYR   B HD1  1 
ATOM   6541 H HD2  . TYR   B 1 161 ? 43.607 -37.309 -12.782 1.00 22.78 ?  161 TYR   B HD2  1 
ATOM   6542 H HE1  . TYR   B 1 161 ? 42.356 -32.890 -13.267 1.00 23.27 ?  161 TYR   B HE1  1 
ATOM   6543 H HE2  . TYR   B 1 161 ? 42.720 -36.586 -14.776 1.00 24.10 ?  161 TYR   B HE2  1 
ATOM   6544 H HH   . TYR   B 1 161 ? 41.881 -34.873 -15.947 1.00 27.05 ?  161 TYR   B HH   1 
ATOM   6545 N N    . ASP   B 1 162 ? 42.598 -38.722 -10.325 1.00 17.60 ?  162 ASP   B N    1 
ATOM   6546 C CA   . ASP   B 1 162 ? 41.769 -39.758 -10.937 1.00 18.09 ?  162 ASP   B CA   1 
ATOM   6547 C C    . ASP   B 1 162 ? 40.563 -40.098 -10.067 1.00 17.19 ?  162 ASP   B C    1 
ATOM   6548 O O    . ASP   B 1 162 ? 39.456 -40.309 -10.583 1.00 17.47 ?  162 ASP   B O    1 
ATOM   6549 C CB   . ASP   B 1 162 ? 42.600 -41.017 -11.192 1.00 19.65 ?  162 ASP   B CB   1 
ATOM   6550 C CG   . ASP   B 1 162 ? 43.605 -40.851 -12.319 1.00 21.20 ?  162 ASP   B CG   1 
ATOM   6551 O OD1  . ASP   B 1 162 ? 43.463 -39.915 -13.129 1.00 21.79 ?  162 ASP   B OD1  1 
ATOM   6552 O OD2  . ASP   B 1 162 ? 44.528 -41.691 -12.413 1.00 23.16 -1 162 ASP   B OD2  1 
ATOM   6553 H H    . ASP   B 1 162 ? 43.401 -38.965 -10.150 1.00 21.10 ?  162 ASP   B H    1 
ATOM   6554 H HA   . ASP   B 1 162 ? 41.440 -39.440 -11.790 1.00 21.68 ?  162 ASP   B HA   1 
ATOM   6555 H HB2  . ASP   B 1 162 ? 43.097 -41.241 -10.391 1.00 23.56 ?  162 ASP   B HB2  1 
ATOM   6556 H HB3  . ASP   B 1 162 ? 42.005 -41.747 -11.430 1.00 23.56 ?  162 ASP   B HB3  1 
ATOM   6557 N N    A LYS   B 1 163 ? 40.757 -40.179 -8.749  0.58 16.63 ?  163 LYS   B N    1 
ATOM   6558 N N    B LYS   B 1 163 ? 40.754 -40.164 -8.747  0.42 17.20 ?  163 LYS   B N    1 
ATOM   6559 C CA   A LYS   B 1 163 ? 39.629 -40.449 -7.862  0.58 17.40 ?  163 LYS   B CA   1 
ATOM   6560 C CA   B LYS   B 1 163 ? 39.631 -40.448 -7.857  0.42 18.02 ?  163 LYS   B CA   1 
ATOM   6561 C C    A LYS   B 1 163 ? 38.593 -39.332 -7.932  0.58 16.30 ?  163 LYS   B C    1 
ATOM   6562 C C    B LYS   B 1 163 ? 38.595 -39.330 -7.896  0.42 16.60 ?  163 LYS   B C    1 
ATOM   6563 O O    A LYS   B 1 163 ? 37.381 -39.596 -7.942  0.58 16.68 ?  163 LYS   B O    1 
ATOM   6564 O O    B LYS   B 1 163 ? 37.385 -39.593 -7.845  0.42 16.87 ?  163 LYS   B O    1 
ATOM   6565 C CB   A LYS   B 1 163 ? 40.110 -40.634 -6.424  0.58 20.42 ?  163 LYS   B CB   1 
ATOM   6566 C CB   B LYS   B 1 163 ? 40.128 -40.657 -6.429  0.42 20.99 ?  163 LYS   B CB   1 
ATOM   6567 C CG   A LYS   B 1 163 ? 39.031 -41.189 -5.513  0.58 25.16 ?  163 LYS   B CG   1 
ATOM   6568 C CG   B LYS   B 1 163 ? 39.046 -41.151 -5.489  0.42 24.98 ?  163 LYS   B CG   1 
ATOM   6569 C CD   A LYS   B 1 163 ? 39.432 -41.182 -4.051  0.58 29.08 ?  163 LYS   B CD   1 
ATOM   6570 C CD   B LYS   B 1 163 ? 39.558 -41.366 -4.077  0.42 28.45 ?  163 LYS   B CD   1 
ATOM   6571 C CE   A LYS   B 1 163 ? 38.361 -41.860 -3.207  0.58 31.82 ?  163 LYS   B CE   1 
ATOM   6572 C CE   B LYS   B 1 163 ? 38.492 -42.044 -3.230  0.42 30.89 ?  163 LYS   B CE   1 
ATOM   6573 N NZ   A LYS   B 1 163 ? 38.445 -41.489 -1.769  0.58 33.45 ?  163 LYS   B NZ   1 
ATOM   6574 N NZ   B LYS   B 1 163 ? 38.675 -41.797 -1.774  0.42 32.19 ?  163 LYS   B NZ   1 
ATOM   6575 H H    A LYS   B 1 163 ? 41.518 -40.089 -8.355  0.58 19.93 ?  163 LYS   B H    1 
ATOM   6576 H H    B LYS   B 1 163 ? 41.510 -40.055 -8.351  0.42 20.61 ?  163 LYS   B H    1 
ATOM   6577 H HA   A LYS   B 1 163 ? 39.201 -41.271 -8.143  0.58 20.85 ?  163 LYS   B HA   1 
ATOM   6578 H HA   B LYS   B 1 163 ? 39.198 -41.265 -8.147  0.42 21.59 ?  163 LYS   B HA   1 
ATOM   6579 H HB2  A LYS   B 1 163 ? 40.856 -41.257 -6.418  0.58 24.48 ?  163 LYS   B HB2  1 
ATOM   6580 H HB2  B LYS   B 1 163 ? 40.840 -41.317 -6.436  0.42 25.16 ?  163 LYS   B HB2  1 
ATOM   6581 H HB3  A LYS   B 1 163 ? 40.391 -39.778 -6.069  0.58 24.48 ?  163 LYS   B HB3  1 
ATOM   6582 H HB3  B LYS   B 1 163 ? 40.461 -39.815 -6.083  0.42 25.16 ?  163 LYS   B HB3  1 
ATOM   6583 H HG2  A LYS   B 1 163 ? 38.229 -40.652 -5.603  0.58 30.16 ?  163 LYS   B HG2  1 
ATOM   6584 H HG2  B LYS   B 1 163 ? 38.332 -40.496 -5.450  0.42 29.95 ?  163 LYS   B HG2  1 
ATOM   6585 H HG3  A LYS   B 1 163 ? 38.843 -42.108 -5.766  0.58 30.16 ?  163 LYS   B HG3  1 
ATOM   6586 H HG3  B LYS   B 1 163 ? 38.703 -41.998 -5.816  0.42 29.95 ?  163 LYS   B HG3  1 
ATOM   6587 H HD2  A LYS   B 1 163 ? 40.264 -41.671 -3.940  0.58 34.87 ?  163 LYS   B HD2  1 
ATOM   6588 H HD2  B LYS   B 1 163 ? 40.343 -41.938 -4.100  0.42 34.11 ?  163 LYS   B HD2  1 
ATOM   6589 H HD3  A LYS   B 1 163 ? 39.532 -40.267 -3.746  0.58 34.87 ?  163 LYS   B HD3  1 
ATOM   6590 H HD3  B LYS   B 1 163 ? 39.774 -40.510 -3.676  0.42 34.11 ?  163 LYS   B HD3  1 
ATOM   6591 H HE2  A LYS   B 1 163 ? 37.484 -41.613 -3.539  0.58 38.16 ?  163 LYS   B HE2  1 
ATOM   6592 H HE2  B LYS   B 1 163 ? 37.620 -41.706 -3.488  0.42 37.04 ?  163 LYS   B HE2  1 
ATOM   6593 H HE3  A LYS   B 1 163 ? 38.475 -42.820 -3.274  0.58 38.16 ?  163 LYS   B HE3  1 
ATOM   6594 H HE3  B LYS   B 1 163 ? 38.533 -43.002 -3.379  0.42 37.04 ?  163 LYS   B HE3  1 
ATOM   6595 H HZ1  A LYS   B 1 163 ? 37.804 -41.903 -1.311  0.58 40.11 ?  163 LYS   B HZ1  1 
ATOM   6596 H HZ1  B LYS   B 1 163 ? 38.033 -42.207 -1.314  0.42 38.60 ?  163 LYS   B HZ1  1 
ATOM   6597 H HZ2  A LYS   B 1 163 ? 39.236 -41.730 -1.440  0.58 40.11 ?  163 LYS   B HZ2  1 
ATOM   6598 H HZ2  B LYS   B 1 163 ? 39.465 -42.107 -1.510  0.42 38.60 ?  163 LYS   B HZ2  1 
ATOM   6599 H HZ3  A LYS   B 1 163 ? 38.347 -40.610 -1.674  0.58 40.11 ?  163 LYS   B HZ3  1 
ATOM   6600 H HZ3  B LYS   B 1 163 ? 38.636 -40.923 -1.608  0.42 38.60 ?  163 LYS   B HZ3  1 
ATOM   6601 N N    . LEU   B 1 164 ? 39.053 -38.077 -7.975  1.00 15.13 ?  164 LEU   B N    1 
ATOM   6602 C CA   . LEU   B 1 164 ? 38.141 -36.939 -8.030  1.00 14.87 ?  164 LEU   B CA   1 
ATOM   6603 C C    . LEU   B 1 164 ? 37.358 -36.920 -9.339  1.00 15.13 ?  164 LEU   B C    1 
ATOM   6604 O O    . LEU   B 1 164 ? 36.134 -36.720 -9.342  1.00 16.73 ?  164 LEU   B O    1 
ATOM   6605 C CB   . LEU   B 1 164 ? 38.945 -35.647 -7.864  1.00 14.10 ?  164 LEU   B CB   1 
ATOM   6606 C CG   . LEU   B 1 164 ? 39.473 -35.355 -6.464  1.00 14.83 ?  164 LEU   B CG   1 
ATOM   6607 C CD1  . LEU   B 1 164 ? 40.564 -34.297 -6.534  1.00 14.77 ?  164 LEU   B CD1  1 
ATOM   6608 C CD2  . LEU   B 1 164 ? 38.358 -34.906 -5.536  1.00 16.94 ?  164 LEU   B CD2  1 
ATOM   6609 H H    A LEU   B 1 164 ? 39.891 -37.862 -7.975  0.58 18.14 ?  164 LEU   B H    1 
ATOM   6610 H H    B LEU   B 1 164 ? 39.891 -37.863 -8.001  0.42 18.14 ?  164 LEU   B H    1 
ATOM   6611 H HA   . LEU   B 1 164 ? 37.514 -37.000 -7.305  1.00 17.82 ?  164 LEU   B HA   1 
ATOM   6612 H HB2  . LEU   B 1 164 ? 39.717 -35.686 -8.458  1.00 16.90 ?  164 LEU   B HB2  1 
ATOM   6613 H HB3  . LEU   B 1 164 ? 38.384 -34.903 -8.120  1.00 16.90 ?  164 LEU   B HB3  1 
ATOM   6614 H HG   . LEU   B 1 164 ? 39.870 -36.159 -6.099  1.00 17.77 ?  164 LEU   B HG   1 
ATOM   6615 H HD11 . LEU   B 1 164 ? 40.890 -34.108 -5.635  1.00 17.70 ?  164 LEU   B HD11 1 
ATOM   6616 H HD12 . LEU   B 1 164 ? 41.303 -34.626 -7.078  1.00 17.70 ?  164 LEU   B HD12 1 
ATOM   6617 H HD13 . LEU   B 1 164 ? 40.208 -33.485 -6.928  1.00 17.70 ?  164 LEU   B HD13 1 
ATOM   6618 H HD21 . LEU   B 1 164 ? 38.734 -34.677 -4.673  1.00 20.30 ?  164 LEU   B HD21 1 
ATOM   6619 H HD22 . LEU   B 1 164 ? 37.916 -34.133 -5.921  1.00 20.30 ?  164 LEU   B HD22 1 
ATOM   6620 H HD23 . LEU   B 1 164 ? 37.723 -35.634 -5.438  1.00 20.30 ?  164 LEU   B HD23 1 
ATOM   6621 N N    . VAL   B 1 165 ? 38.051 -37.103 -10.465 1.00 16.76 ?  165 VAL   B N    1 
ATOM   6622 C CA   . VAL   B 1 165 ? 37.390 -37.040 -11.764 1.00 18.29 ?  165 VAL   B CA   1 
ATOM   6623 C C    . VAL   B 1 165 ? 36.464 -38.234 -11.942 1.00 20.16 ?  165 VAL   B C    1 
ATOM   6624 O O    . VAL   B 1 165 ? 35.304 -38.093 -12.351 1.00 21.22 ?  165 VAL   B O    1 
ATOM   6625 C CB   . VAL   B 1 165 ? 38.432 -36.961 -12.897 1.00 19.35 ?  165 VAL   B CB   1 
ATOM   6626 C CG1  . VAL   B 1 165 ? 37.759 -37.071 -14.247 1.00 20.80 ?  165 VAL   B CG1  1 
ATOM   6627 C CG2  . VAL   B 1 165 ? 39.227 -35.672 -12.808 1.00 19.32 ?  165 VAL   B CG2  1 
ATOM   6628 H H    . VAL   B 1 165 ? 38.902 -37.257 -10.506 1.00 20.09 ?  165 VAL   B H    1 
ATOM   6629 H HA   . VAL   B 1 165 ? 36.853 -36.237 -11.807 1.00 21.92 ?  165 VAL   B HA   1 
ATOM   6630 H HB   . VAL   B 1 165 ? 39.059 -37.697 -12.809 1.00 23.19 ?  165 VAL   B HB   1 
ATOM   6631 H HG11 . VAL   B 1 165 ? 38.376 -36.778 -14.934 1.00 24.94 ?  165 VAL   B HG11 1 
ATOM   6632 H HG12 . VAL   B 1 165 ? 37.518 -38.000 -14.402 1.00 24.94 ?  165 VAL   B HG12 1 
ATOM   6633 H HG13 . VAL   B 1 165 ? 36.966 -36.518 -14.252 1.00 24.94 ?  165 VAL   B HG13 1 
ATOM   6634 H HG21 . VAL   B 1 165 ? 39.862 -35.635 -13.544 1.00 23.17 ?  165 VAL   B HG21 1 
ATOM   6635 H HG22 . VAL   B 1 165 ? 38.615 -34.917 -12.869 1.00 23.17 ?  165 VAL   B HG22 1 
ATOM   6636 H HG23 . VAL   B 1 165 ? 39.700 -35.643 -11.963 1.00 23.17 ?  165 VAL   B HG23 1 
ATOM   6637 N N    . SER   B 1 166 ? 36.968 -39.435 -11.637 1.00 21.02 ?  166 SER   B N    1 
ATOM   6638 C CA   . SER   B 1 166 ? 36.209 -40.647 -11.919 1.00 22.18 ?  166 SER   B CA   1 
ATOM   6639 C C    . SER   B 1 166 ? 34.948 -40.728 -11.072 1.00 22.52 ?  166 SER   B C    1 
ATOM   6640 O O    . SER   B 1 166 ? 33.977 -41.360 -11.491 1.00 23.84 ?  166 SER   B O    1 
ATOM   6641 C CB   . SER   B 1 166 ? 37.073 -41.903 -11.740 1.00 23.46 ?  166 SER   B CB   1 
ATOM   6642 O OG   . SER   B 1 166 ? 37.433 -42.105 -10.386 1.00 23.80 ?  166 SER   B OG   1 
ATOM   6643 H H    . SER   B 1 166 ? 37.746 -39.569 -11.277 1.00 25.20 ?  166 SER   B H    1 
ATOM   6644 H HA   . SER   B 1 166 ? 35.943 -40.625 -12.848 1.00 26.59 ?  166 SER   B HA   1 
ATOM   6645 H HB2  . SER   B 1 166 ? 36.573 -42.675 -12.046 1.00 28.13 ?  166 SER   B HB2  1 
ATOM   6646 H HB3  . SER   B 1 166 ? 37.884 -41.811 -12.273 1.00 28.13 ?  166 SER   B HB3  1 
ATOM   6647 H HG   . SER   B 1 166 ? 37.891 -41.453 -10.112 1.00 28.53 ?  166 SER   B HG   1 
ATOM   6648 N N    . SER   B 1 167 ? 34.931 -40.111 -9.893  1.00 21.28 ?  167 SER   B N    1 
ATOM   6649 C CA   . SER   B 1 167 ? 33.774 -40.163 -9.004  1.00 21.03 ?  167 SER   B CA   1 
ATOM   6650 C C    . SER   B 1 167 ? 32.859 -38.939 -9.107  1.00 20.27 ?  167 SER   B C    1 
ATOM   6651 O O    . SER   B 1 167 ? 31.775 -38.938 -8.508  1.00 20.40 ?  167 SER   B O    1 
ATOM   6652 C CB   . SER   B 1 167 ? 34.224 -40.349 -7.549  1.00 21.17 ?  167 SER   B CB   1 
ATOM   6653 O OG   . SER   B 1 167 ? 34.894 -39.188 -7.075  1.00 21.11 ?  167 SER   B OG   1 
ATOM   6654 H H    . SER   B 1 167 ? 35.590 -39.667 -9.580  1.00 25.51 ?  167 SER   B H    1 
ATOM   6655 H HA   . SER   B 1 167 ? 33.246 -40.942 -9.240  1.00 25.21 ?  167 SER   B HA   1 
ATOM   6656 H HB2  . SER   B 1 167 ? 33.446 -40.516 -6.996  1.00 25.38 ?  167 SER   B HB2  1 
ATOM   6657 H HB3  . SER   B 1 167 ? 34.830 -41.112 -7.499  1.00 25.38 ?  167 SER   B HB3  1 
ATOM   6658 H HG   . SER   B 1 167 ? 35.579 -39.044 -7.540  1.00 25.31 ?  167 SER   B HG   1 
ATOM   6659 N N    . PHE   B 1 168 ? 33.249 -37.904 -9.856  1.00 19.90 ?  168 PHE   B N    1 
ATOM   6660 C CA   . PHE   B 1 168 ? 32.422 -36.699 -9.940  1.00 18.88 ?  168 PHE   B CA   1 
ATOM   6661 C C    . PHE   B 1 168 ? 31.109 -36.969 -10.669 1.00 16.60 ?  168 PHE   B C    1 
ATOM   6662 O O    . PHE   B 1 168 ? 30.066 -36.373 -10.339 1.00 17.16 ?  168 PHE   B O    1 
ATOM   6663 C CB   . PHE   B 1 168 ? 33.191 -35.578 -10.639 1.00 19.88 ?  168 PHE   B CB   1 
ATOM   6664 C CG   . PHE   B 1 168 ? 32.391 -34.326 -10.797 1.00 19.77 ?  168 PHE   B CG   1 
ATOM   6665 C CD1  . PHE   B 1 168 ? 32.059 -33.571 -9.684  1.00 21.14 ?  168 PHE   B CD1  1 
ATOM   6666 C CD2  . PHE   B 1 168 ? 31.942 -33.915 -12.039 1.00 19.37 ?  168 PHE   B CD2  1 
ATOM   6667 C CE1  . PHE   B 1 168 ? 31.302 -32.421 -9.802  1.00 21.62 ?  168 PHE   B CE1  1 
ATOM   6668 C CE2  . PHE   B 1 168 ? 31.196 -32.751 -12.172 1.00 20.31 ?  168 PHE   B CE2  1 
ATOM   6669 C CZ   . PHE   B 1 168 ? 30.867 -32.005 -11.046 1.00 20.75 ?  168 PHE   B CZ   1 
ATOM   6670 H H    . PHE   B 1 168 ? 33.977 -37.874 -10.311 1.00 23.85 ?  168 PHE   B H    1 
ATOM   6671 H HA   . PHE   B 1 168 ? 32.203 -36.403 -9.047  1.00 22.64 ?  168 PHE   B HA   1 
ATOM   6672 H HB2  . PHE   B 1 168 ? 33.977 -35.367 -10.114 1.00 23.84 ?  168 PHE   B HB2  1 
ATOM   6673 H HB3  . PHE   B 1 168 ? 33.452 -35.879 -11.523 1.00 23.84 ?  168 PHE   B HB3  1 
ATOM   6674 H HD1  . PHE   B 1 168 ? 32.344 -33.851 -8.845  1.00 25.35 ?  168 PHE   B HD1  1 
ATOM   6675 H HD2  . PHE   B 1 168 ? 32.157 -34.409 -12.795 1.00 23.22 ?  168 PHE   B HD2  1 
ATOM   6676 H HE1  . PHE   B 1 168 ? 31.088 -31.927 -9.045  1.00 25.92 ?  168 PHE   B HE1  1 
ATOM   6677 H HE2  . PHE   B 1 168 ? 30.898 -32.479 -13.013 1.00 24.35 ?  168 PHE   B HE2  1 
ATOM   6678 H HZ   . PHE   B 1 168 ? 30.359 -31.230 -11.133 1.00 24.88 ?  168 PHE   B HZ   1 
ATOM   6679 N N    . LEU   B 1 169 ? 31.146 -37.838 -11.678 1.00 16.89 ?  169 LEU   B N    1 
ATOM   6680 C CA   . LEU   B 1 169 ? 29.970 -38.159 -12.478 1.00 18.92 ?  169 LEU   B CA   1 
ATOM   6681 C C    . LEU   B 1 169 ? 29.975 -39.596 -12.981 1.00 21.80 ?  169 LEU   B C    1 
ATOM   6682 O O    . LEU   B 1 169 ? 29.079 -40.002 -13.724 1.00 24.37 ?  169 LEU   B O    1 
ATOM   6683 C CB   . LEU   B 1 169 ? 29.894 -37.230 -13.686 1.00 20.98 ?  169 LEU   B CB   1 
ATOM   6684 C CG   . LEU   B 1 169 ? 28.636 -36.372 -13.808 1.00 24.23 ?  169 LEU   B CG   1 
ATOM   6685 C CD1  . LEU   B 1 169 ? 28.585 -35.768 -15.190 1.00 25.28 ?  169 LEU   B CD1  1 
ATOM   6686 C CD2  . LEU   B 1 169 ? 27.371 -37.166 -13.522 1.00 24.17 ?  169 LEU   B CD2  1 
ATOM   6687 O OXT  . LEU   B 1 169 ? 30.877 -40.371 -12.683 1.00 22.56 -1 169 LEU   B OXT  1 
ATOM   6688 H H    . LEU   B 1 169 ? 31.855 -38.254 -11.933 1.00 20.25 ?  169 LEU   B H    1 
ATOM   6689 H HA   . LEU   B 1 169 ? 29.183 -38.021 -11.935 1.00 22.67 ?  169 LEU   B HA   1 
ATOM   6690 H HB2  . LEU   B 1 169 ? 30.651 -36.625 -13.659 1.00 25.16 ?  169 LEU   B HB2  1 
ATOM   6691 H HB3  . LEU   B 1 169 ? 29.946 -37.769 -14.493 1.00 25.16 ?  169 LEU   B HB3  1 
ATOM   6692 H HG   . LEU   B 1 169 ? 28.684 -35.644 -13.168 1.00 29.05 ?  169 LEU   B HG   1 
ATOM   6693 H HD11 . LEU   B 1 169 ? 27.806 -35.194 -15.254 1.00 30.31 ?  169 LEU   B HD11 1 
ATOM   6694 H HD12 . LEU   B 1 169 ? 29.391 -35.252 -15.336 1.00 30.31 ?  169 LEU   B HD12 1 
ATOM   6695 H HD13 . LEU   B 1 169 ? 28.524 -36.483 -15.841 1.00 30.31 ?  169 LEU   B HD13 1 
ATOM   6696 H HD21 . LEU   B 1 169 ? 26.620 -36.739 -13.957 1.00 28.98 ?  169 LEU   B HD21 1 
ATOM   6697 H HD22 . LEU   B 1 169 ? 27.484 -38.069 -13.866 1.00 28.98 ?  169 LEU   B HD22 1 
ATOM   6698 H HD23 . LEU   B 1 169 ? 27.230 -37.196 -12.564 1.00 28.98 ?  169 LEU   B HD23 1 
HETATM 6699 C C1   T TFA   C 2 .   ? 12.125 -1.289  1.388   0.30 10.62 ?  201 TFA   A C1   1 
HETATM 6700 C C2   T TFA   C 2 .   ? 12.749 -1.743  0.045   0.30 13.02 ?  201 TFA   A C2   1 
HETATM 6701 O O    T TFA   C 2 .   ? 12.830 -1.572  2.360   0.30 9.19  ?  201 TFA   A O    1 
HETATM 6702 F F1   T TFA   C 2 .   ? 12.808 -3.084  -0.004  0.30 14.57 ?  201 TFA   A F1   1 
HETATM 6703 F F2   T TFA   C 2 .   ? 12.055 -1.345  -1.034  0.30 13.09 ?  201 TFA   A F2   1 
HETATM 6704 F F3   T TFA   C 2 .   ? 13.995 -1.297  -0.133  0.30 14.77 ?  201 TFA   A F3   1 
HETATM 6705 O OXT  T TFA   C 2 .   ? 11.033 -0.718  1.317   0.30 10.84 ?  201 TFA   A OXT  1 
HETATM 6706 N N2   B A1A61 D 3 .   ? 14.941 -0.251  4.208   0.42 17.20 ?  202 A1A61 A N2   1 
HETATM 6707 C C3   B A1A61 D 3 .   ? 14.085 -0.353  -0.089  0.42 21.74 ?  202 A1A61 A C3   1 
HETATM 6708 C C6   B A1A61 D 3 .   ? 12.526 1.044   -2.372  0.42 24.40 ?  202 A1A61 A C6   1 
HETATM 6709 C C9   B A1A61 D 3 .   ? 14.716 1.710   0.951   0.42 20.83 ?  202 A1A61 A C9   1 
HETATM 6710 C C12  B A1A61 D 3 .   ? 15.406 2.105   5.397   0.42 14.82 ?  202 A1A61 A C12  1 
HETATM 6711 C C14  B A1A61 D 3 .   ? 15.649 3.505   3.590   0.42 14.99 ?  202 A1A61 A C14  1 
HETATM 6712 C C1   B A1A61 D 3 .   ? 15.471 -1.918  1.564   0.42 20.44 ?  202 A1A61 A C1   1 
HETATM 6713 C C10  B A1A61 D 3 .   ? 15.132 0.819   3.357   0.42 17.43 ?  202 A1A61 A C10  1 
HETATM 6714 C C11  B A1A61 D 3 .   ? 14.993 -0.102  5.586   0.42 16.77 ?  202 A1A61 A C11  1 
HETATM 6715 C C13  B A1A61 D 3 .   ? 15.381 2.112   3.964   0.42 15.67 ?  202 A1A61 A C13  1 
HETATM 6716 C C15  B A1A61 D 3 .   ? 15.804 4.236   4.774   0.42 14.06 ?  202 A1A61 A C15  1 
HETATM 6717 C C2   B A1A61 D 3 .   ? 14.448 -0.677  1.406   0.42 20.78 ?  202 A1A61 A C2   1 
HETATM 6718 C C4   B A1A61 D 3 .   ? 13.637 1.131   -0.065  0.42 22.37 ?  202 A1A61 A C4   1 
HETATM 6719 C C5   B A1A61 D 3 .   ? 13.620 1.708   -1.493  0.42 23.60 ?  202 A1A61 A C5   1 
HETATM 6720 C C7   B A1A61 D 3 .   ? 11.146 1.675   -0.537  0.42 23.66 ?  202 A1A61 A C7   1 
HETATM 6721 C C8   B A1A61 D 3 .   ? 12.235 1.448   0.524   0.42 23.23 ?  202 A1A61 A C8   1 
HETATM 6722 N N1   B A1A61 D 3 .   ? 15.059 0.601   1.958   0.42 19.72 ?  202 A1A61 A N1   1 
HETATM 6723 N N3   B A1A61 D 3 .   ? 15.214 1.038   6.213   0.42 15.96 ?  202 A1A61 A N3   1 
HETATM 6724 N N4   B A1A61 D 3 .   ? 15.655 3.368   5.793   0.42 13.71 ?  202 A1A61 A N4   1 
HETATM 6725 O O1   B A1A61 D 3 .   ? 15.203 -2.646  2.764   0.42 19.98 ?  202 A1A61 A O1   1 
HETATM 6726 O O2   B A1A61 D 3 .   ? 11.316 0.826   -1.656  0.42 24.85 ?  202 A1A61 A O2   1 
HETATM 6727 H H5   B A1A61 D 3 .   ? 14.975 -0.538  -0.760  0.42 26.07 ?  202 A1A61 A H5   1 
HETATM 6728 H H6   B A1A61 D 3 .   ? 13.303 -1.059  -0.478  0.42 26.07 ?  202 A1A61 A H6   1 
HETATM 6729 H H9   B A1A61 D 3 .   ? 12.340 1.589   -3.302  0.42 29.26 ?  202 A1A61 A H9   1 
HETATM 6730 H H10  B A1A61 D 3 .   ? 12.877 0.050   -2.740  0.42 29.26 ?  202 A1A61 A H10  1 
HETATM 6731 H H16  B A1A61 D 3 .   ? 14.353 2.652   1.426   0.42 24.97 ?  202 A1A61 A H16  1 
HETATM 6732 H H15  B A1A61 D 3 .   ? 15.640 1.990   0.391   0.42 24.97 ?  202 A1A61 A H15  1 
HETATM 6733 H H18  B A1A61 D 3 .   ? 15.704 3.946   2.608   0.42 17.97 ?  202 A1A61 A H18  1 
HETATM 6734 H H4   B A1A61 D 3 .   ? 16.520 -1.541  1.583   0.42 24.50 ?  202 A1A61 A H4   1 
HETATM 6735 H H3   B A1A61 D 3 .   ? 15.368 -2.578  0.675   0.42 24.50 ?  202 A1A61 A H3   1 
HETATM 6736 H H17  B A1A61 D 3 .   ? 14.823 -1.001  6.247   0.42 20.09 ?  202 A1A61 A H17  1 
HETATM 6737 H H19  B A1A61 D 3 .   ? 16.006 5.286   5.016   0.42 16.84 ?  202 A1A61 A H19  1 
HETATM 6738 H H1   B A1A61 D 3 .   ? 13.502 -0.899  1.968   0.42 24.91 ?  202 A1A61 A H1   1 
HETATM 6739 H H8   B A1A61 D 3 .   ? 13.498 2.826   -1.481  0.42 28.29 ?  202 A1A61 A H8   1 
HETATM 6740 H H7   B A1A61 D 3 .   ? 14.588 1.529   -2.003  0.42 28.29 ?  202 A1A61 A H7   1 
HETATM 6741 H H11  B A1A61 D 3 .   ? 10.113 1.543   -0.116  0.42 28.36 ?  202 A1A61 A H11  1 
HETATM 6742 H H12  B A1A61 D 3 .   ? 11.143 2.751   -0.875  0.42 28.36 ?  202 A1A61 A H12  1 
HETATM 6743 H H14  B A1A61 D 3 .   ? 11.914 0.579   1.151   0.42 27.86 ?  202 A1A61 A H14  1 
HETATM 6744 H H13  B A1A61 D 3 .   ? 12.271 2.314   1.251   0.42 27.86 ?  202 A1A61 A H13  1 
HETATM 6745 H H20  B A1A61 D 3 .   ? 15.732 3.679   6.812   0.42 16.43 ?  202 A1A61 A H20  1 
HETATM 6746 H H2   B A1A61 D 3 .   ? 14.336 -3.107  2.703   0.42 23.95 ?  202 A1A61 A H2   1 
HETATM 6747 O O    . HOH   E 4 .   ? 4.753  3.732   0.395   1.00 27.14 ?  301 HOH   A O    1 
HETATM 6748 O O    A HOH   E 4 .   ? 14.750 -4.592  20.357  0.58 36.16 ?  302 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 11.937 0.318   14.655  1.00 32.03 ?  303 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 14.499 -0.478  -12.329 1.00 30.79 ?  304 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 3.765  -9.169  9.835   1.00 33.21 ?  305 HOH   A O    1 
HETATM 6752 O O    . HOH   E 4 .   ? 34.385 -1.847  12.504  1.00 38.97 ?  306 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 29.012 0.443   -9.762  1.00 22.98 ?  307 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 11.792 -10.801 -10.083 1.00 53.50 ?  308 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 0.785  -4.269  -0.010  1.00 33.57 ?  309 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 14.953 -12.152 18.560  1.00 42.49 ?  310 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 6.836  -8.016  11.719  1.00 20.01 ?  311 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 14.634 -13.866 16.661  1.00 28.40 ?  312 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 42.472 10.494  5.004   1.00 20.00 ?  313 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? 9.214  -10.035 19.287  1.00 40.59 ?  314 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 28.081 -6.242  19.608  1.00 44.28 ?  315 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 31.019 6.174   -12.275 1.00 28.24 ?  316 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 38.270 10.298  7.069   1.00 46.87 ?  317 HOH   A O    1 
HETATM 6764 O O    A HOH   E 4 .   ? 14.131 -4.565  -11.799 0.58 25.44 ?  318 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 22.290 5.370   18.983  1.00 41.09 ?  319 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 30.271 -13.315 -8.585  1.00 22.83 ?  320 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 42.587 4.236   5.536   1.00 35.71 ?  321 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 15.019 4.030   17.581  1.00 39.43 ?  322 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? -0.672 -8.444  2.058   1.00 43.68 ?  323 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 23.930 -15.742 -9.252  1.00 36.88 ?  324 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 22.534 -11.987 21.806  1.00 50.05 ?  325 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 13.571 -15.229 -7.762  1.00 29.06 ?  326 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 26.497 -19.329 -1.828  1.00 15.31 ?  327 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 22.740 12.485  1.571   1.00 15.85 ?  328 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 31.010 -18.115 7.764   1.00 20.47 ?  329 HOH   A O    1 
HETATM 6776 O O    A HOH   E 4 .   ? 28.292 -0.190  -13.360 0.58 26.13 ?  330 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 37.526 2.775   10.275  1.00 28.48 ?  331 HOH   A O    1 
HETATM 6778 O O    A HOH   E 4 .   ? 14.651 -3.639  3.033   0.58 14.94 ?  332 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 44.367 7.160   6.462   1.00 27.61 ?  333 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 19.986 -12.576 -8.840  1.00 28.44 ?  334 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 27.336 13.831  2.884   1.00 33.64 ?  335 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 36.220 -5.117  -0.522  1.00 33.75 ?  336 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 17.095 -17.997 14.902  1.00 29.66 ?  337 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 8.008  -21.450 3.920   1.00 46.68 ?  338 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 15.215 -8.056  -9.946  1.00 31.22 ?  339 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 34.059 -1.012  -8.896  1.00 28.17 ?  340 HOH   A O    1 
HETATM 6787 O O    A HOH   E 4 .   ? 14.284 0.588   6.737   0.58 16.65 ?  341 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 18.906 -21.966 6.938   1.00 37.74 ?  342 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 13.233 -1.469  -6.709  1.00 20.65 ?  343 HOH   A O    1 
HETATM 6790 O O    A HOH   E 4 .   ? 8.014  -12.572 -0.969  0.58 18.56 ?  344 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 14.345 -21.166 -4.283  1.00 33.27 ?  345 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 10.938 1.713   12.419  1.00 24.61 ?  346 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 27.967 0.822   -7.173  1.00 15.00 ?  347 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 22.133 -19.348 11.331  1.00 37.52 ?  348 HOH   A O    1 
HETATM 6795 O O    A HOH   E 4 .   ? -0.461 -3.058  2.990   0.58 29.06 ?  349 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 21.298 -2.253  -2.428  1.00 17.55 ?  350 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 20.676 -19.715 -5.163  1.00 30.26 ?  351 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 25.781 -0.741  -7.375  1.00 18.90 ?  352 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 39.805 -1.059  -5.102  1.00 20.87 ?  353 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 38.558 4.943   7.075   1.00 16.06 ?  354 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 18.563 9.488   8.957   1.00 22.36 ?  355 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 24.062 -2.096  -2.135  1.00 11.86 ?  356 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 26.910 11.458  1.639   1.00 17.95 ?  357 HOH   A O    1 
HETATM 6804 O O    A HOH   E 4 .   ? 24.635 2.049   -7.018  0.58 16.14 ?  358 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 31.699 8.199   14.889  1.00 26.06 ?  359 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 31.104 -13.945 -2.512  1.00 14.24 ?  360 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 18.618 -19.369 13.563  1.00 37.16 ?  361 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 7.555  -6.056  -6.770  1.00 46.31 ?  362 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 35.773 -12.660 6.835   1.00 16.32 ?  363 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 24.402 3.638   -1.805  1.00 17.34 ?  364 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 31.914 -9.324  -6.647  1.00 22.88 ?  365 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 21.846 -21.889 8.419   1.00 30.11 ?  366 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 30.816 3.091   8.289   1.00 12.80 ?  367 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 37.320 11.959  4.975   1.00 29.17 ?  368 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 24.661 -17.459 12.735  1.00 26.71 ?  369 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 13.840 -4.835  17.319  1.00 28.58 ?  370 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 27.398 -10.565 14.085  1.00 19.08 ?  371 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 21.309 3.032   -0.266  1.00 14.72 ?  372 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 21.219 10.323  15.007  1.00 35.26 ?  373 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 9.881  -21.349 5.610   1.00 22.34 ?  374 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 16.506 -22.070 0.930   1.00 30.46 ?  375 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 33.519 -16.963 8.090   1.00 19.91 ?  376 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 43.438 7.752   2.806   1.00 40.65 ?  377 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 33.650 -7.133  4.326   1.00 17.11 ?  378 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 21.784 -13.781 -8.238  1.00 44.61 ?  379 HOH   A O    1 
HETATM 6826 O O    A HOH   E 4 .   ? 17.522 -1.700  0.388   0.58 17.02 ?  380 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 16.996 -19.252 4.868   1.00 16.92 ?  381 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 31.886 -7.327  -9.828  1.00 22.42 ?  382 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 23.495 11.390  4.060   1.00 13.27 ?  383 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 37.560 -2.095  5.889   1.00 28.05 ?  384 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 17.158 -17.762 -5.165  1.00 32.06 ?  385 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 37.246 -2.935  9.762   1.00 46.58 ?  386 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 24.153 -7.723  14.423  1.00 17.98 ?  387 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 8.821  -12.099 17.045  1.00 42.09 ?  388 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 29.791 -1.953  -12.794 1.00 45.95 ?  389 HOH   A O    1 
HETATM 6836 O O    T HOH   E 4 .   ? 15.428 -0.407  2.326   0.30 13.11 ?  390 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 18.877 -0.701  -1.684  1.00 16.74 ?  391 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 30.614 1.919   16.717  1.00 22.55 ?  392 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 43.710 8.404   -3.161  1.00 31.04 ?  393 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 5.347  2.843   4.765   1.00 33.43 ?  394 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 32.757 -9.279  5.937   1.00 20.41 ?  395 HOH   A O    1 
HETATM 6842 O O    . HOH   E 4 .   ? 6.372  -5.464  10.945  1.00 19.54 ?  396 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 20.560 -20.023 2.752   1.00 20.70 ?  397 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 27.662 -6.289  -14.060 1.00 42.35 ?  398 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 27.175 2.391   18.711  1.00 31.84 ?  399 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 6.653  -3.268  12.684  1.00 29.99 ?  400 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 30.035 -10.097 13.026  1.00 23.19 ?  401 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 15.159 -21.510 14.201  1.00 19.26 ?  402 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 15.518 11.718  7.864   1.00 47.96 ?  403 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 38.149 -1.377  -1.871  1.00 19.72 ?  404 HOH   A O    1 
HETATM 6851 O O    A HOH   E 4 .   ? 10.410 -13.703 -1.756  0.58 15.05 ?  405 HOH   A O    1 
HETATM 6852 O O    . HOH   E 4 .   ? 15.791 2.157   24.599  1.00 53.82 ?  406 HOH   A O    1 
HETATM 6853 O O    A HOH   E 4 .   ? 15.812 -0.932  5.211   0.58 18.44 ?  407 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 23.951 -20.277 -1.395  1.00 18.49 ?  408 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 14.032 -23.060 7.413   1.00 19.55 ?  409 HOH   A O    1 
HETATM 6856 O O    A HOH   E 4 .   ? 11.090 -0.360  1.860   0.70 32.28 ?  410 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 24.070 3.994   -4.835  1.00 24.45 ?  411 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 26.956 4.176   -0.682  1.00 13.18 ?  412 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 35.055 -5.253  -3.068  1.00 19.02 ?  413 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 28.723 -10.638 -14.048 1.00 43.81 ?  414 HOH   A O    1 
HETATM 6861 O O    A HOH   E 4 .   ? 20.155 4.557   -7.589  0.58 16.07 ?  415 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 40.999 -8.330  -6.758  1.00 38.53 ?  416 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 14.437 -24.606 11.494  1.00 43.86 ?  417 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 30.296 -12.907 13.521  1.00 21.24 ?  418 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 41.579 1.493   5.090   1.00 39.38 ?  419 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 16.242 16.669  8.569   1.00 39.03 ?  420 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 32.755 -4.304  -9.892  1.00 30.57 ?  421 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 15.987 6.847   2.887   1.00 19.22 ?  422 HOH   A O    1 
HETATM 6869 O O    . HOH   E 4 .   ? 16.174 -14.165 20.198  1.00 53.90 ?  423 HOH   A O    1 
HETATM 6870 O O    . HOH   E 4 .   ? 32.555 -10.630 3.214   1.00 33.04 ?  424 HOH   A O    1 
HETATM 6871 O O    . HOH   E 4 .   ? 36.705 -5.017  5.422   1.00 25.62 ?  425 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? -1.447 -4.919  7.343   1.00 49.64 ?  426 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 44.980 -0.743  3.099   1.00 40.56 ?  427 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 26.996 -3.177  19.505  1.00 39.36 ?  428 HOH   A O    1 
HETATM 6875 O O    A HOH   E 4 .   ? 18.648 -2.443  -16.389 0.58 35.66 ?  429 HOH   A O    1 
HETATM 6876 O O    . HOH   E 4 .   ? 16.274 2.882   -1.602  1.00 17.60 ?  430 HOH   A O    1 
HETATM 6877 O O    A HOH   E 4 .   ? 18.514 4.862   -15.076 0.58 36.12 ?  431 HOH   A O    1 
HETATM 6878 O O    . HOH   E 4 .   ? 11.614 -10.665 16.878  1.00 26.76 ?  432 HOH   A O    1 
HETATM 6879 O O    . HOH   E 4 .   ? 22.573 8.170   18.368  1.00 50.92 ?  433 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 23.405 -20.918 1.286   1.00 20.34 ?  434 HOH   A O    1 
HETATM 6881 O O    . HOH   E 4 .   ? 18.795 1.970   -0.752  1.00 15.30 ?  435 HOH   A O    1 
HETATM 6882 O O    . HOH   E 4 .   ? 23.246 7.412   -3.177  1.00 37.34 ?  436 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 37.778 -8.854  -3.470  1.00 24.77 ?  437 HOH   A O    1 
HETATM 6884 O O    . HOH   E 4 .   ? 23.480 -8.059  17.076  1.00 23.66 ?  438 HOH   A O    1 
HETATM 6885 O O    . HOH   E 4 .   ? 34.415 -8.104  -0.529  1.00 31.45 ?  439 HOH   A O    1 
HETATM 6886 O O    . HOH   E 4 .   ? 21.448 -14.744 17.845  1.00 54.22 ?  440 HOH   A O    1 
HETATM 6887 O O    . HOH   E 4 .   ? 18.373 -15.954 16.250  1.00 38.68 ?  441 HOH   A O    1 
HETATM 6888 O O    A HOH   E 4 .   ? 10.519 -22.156 -1.346  0.58 32.31 ?  442 HOH   A O    1 
HETATM 6889 O O    . HOH   E 4 .   ? 21.270 -9.095  21.231  1.00 52.88 ?  443 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 30.610 14.766  2.767   1.00 19.33 ?  444 HOH   A O    1 
HETATM 6891 O O    . HOH   E 4 .   ? 31.352 -12.793 -0.043  1.00 21.07 ?  445 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 20.495 -17.702 24.823  1.00 61.37 ?  446 HOH   A O    1 
HETATM 6893 O O    A HOH   E 4 .   ? 9.403  -16.302 -2.069  0.58 36.84 ?  447 HOH   A O    1 
HETATM 6894 O O    A HOH   E 4 .   ? 14.045 -0.322  3.397   0.28 28.00 ?  448 HOH   A O    1 
HETATM 6895 O O    . HOH   E 4 .   ? 18.931 -10.771 24.042  1.00 82.26 ?  449 HOH   A O    1 
HETATM 6896 O O    . HOH   E 4 .   ? 29.736 -16.029 10.669  1.00 34.42 ?  450 HOH   A O    1 
HETATM 6897 O O    B HOH   E 4 .   ? 16.694 5.992   -2.673  0.42 34.11 ?  451 HOH   A O    1 
HETATM 6898 O O    . HOH   E 4 .   ? 32.394 -15.906 10.827  1.00 31.84 ?  452 HOH   A O    1 
HETATM 6899 O O    . HOH   E 4 .   ? 25.448 8.246   -4.826  1.00 39.97 ?  453 HOH   A O    1 
HETATM 6900 O O    . HOH   E 4 .   ? 24.804 5.644   20.692  1.00 56.87 ?  454 HOH   A O    1 
HETATM 6901 O O    . HOH   E 4 .   ? 19.920 -17.351 -5.116  1.00 29.53 ?  455 HOH   A O    1 
HETATM 6902 O O    . HOH   E 4 .   ? 27.931 7.122   -6.601  1.00 40.06 ?  456 HOH   A O    1 
HETATM 6903 O O    . HOH   E 4 .   ? 23.183 -22.345 -3.340  1.00 37.62 ?  457 HOH   A O    1 
HETATM 6904 O O    . HOH   E 4 .   ? 24.701 14.688  7.715   1.00 36.02 ?  458 HOH   A O    1 
HETATM 6905 O O    . HOH   E 4 .   ? 16.113 -6.746  -12.040 1.00 46.91 ?  459 HOH   A O    1 
HETATM 6906 O O    . HOH   E 4 .   ? 15.782 -21.553 3.683   1.00 26.29 ?  460 HOH   A O    1 
HETATM 6907 O O    . HOH   E 4 .   ? 18.753 10.974  11.205  1.00 33.13 ?  461 HOH   A O    1 
HETATM 6908 O O    . HOH   E 4 .   ? 28.659 -4.707  -12.290 1.00 42.76 ?  462 HOH   A O    1 
HETATM 6909 O O    . HOH   E 4 .   ? 12.330 1.617   17.163  1.00 42.90 ?  463 HOH   A O    1 
HETATM 6910 O O    A HOH   E 4 .   ? 22.017 5.278   -5.873  0.58 27.25 ?  464 HOH   A O    1 
HETATM 6911 O O    . HOH   E 4 .   ? 26.973 11.688  -1.408  1.00 35.81 ?  465 HOH   A O    1 
HETATM 6912 O O    . HOH   E 4 .   ? 27.432 -11.455 16.599  1.00 38.14 ?  466 HOH   A O    1 
HETATM 6913 O O    . HOH   E 4 .   ? 39.698 -7.087  -3.403  1.00 48.14 ?  467 HOH   A O    1 
HETATM 6914 O O    . HOH   E 4 .   ? 11.940 -13.396 16.236  1.00 52.51 ?  468 HOH   A O    1 
HETATM 6915 O O    A HOH   E 4 .   ? 11.196 -14.832 -6.218  0.58 28.77 ?  469 HOH   A O    1 
HETATM 6916 O O    . HOH   E 4 .   ? 23.486 13.746  5.492   1.00 19.55 ?  470 HOH   A O    1 
HETATM 6917 O O    . HOH   E 4 .   ? 18.143 -16.149 -8.820  1.00 46.56 ?  471 HOH   A O    1 
HETATM 6918 O O    . HOH   E 4 .   ? 13.956 -10.387 -10.989 1.00 34.68 ?  472 HOH   A O    1 
HETATM 6919 O O    . HOH   E 4 .   ? 25.826 10.841  -3.787  1.00 29.65 ?  473 HOH   A O    1 
HETATM 6920 O O    . HOH   E 4 .   ? 15.819 -17.106 -7.045  1.00 37.41 ?  474 HOH   A O    1 
HETATM 6921 O O    . HOH   E 4 .   ? 28.897 8.976   17.579  1.00 42.21 ?  475 HOH   A O    1 
HETATM 6922 O O    . HOH   E 4 .   ? 41.759 9.158   -3.740  1.00 39.95 ?  476 HOH   A O    1 
HETATM 6923 O O    . HOH   E 4 .   ? 17.376 -18.694 19.786  1.00 53.90 ?  477 HOH   A O    1 
HETATM 6924 O O    . HOH   E 4 .   ? 23.160 11.877  -4.128  1.00 21.38 ?  478 HOH   A O    1 
HETATM 6925 O O    B HOH   E 4 .   ? 18.297 7.908   -3.845  0.42 34.76 ?  479 HOH   A O    1 
HETATM 6926 O O    . HOH   E 4 .   ? 35.185 7.506   12.225  1.00 53.43 ?  480 HOH   A O    1 
HETATM 6927 O O    . HOH   E 4 .   ? 44.241 10.249  -1.992  1.00 41.42 ?  481 HOH   A O    1 
HETATM 6928 O O    . HOH   E 4 .   ? 41.044 -3.997  -0.401  1.00 40.98 ?  482 HOH   A O    1 
HETATM 6929 O O    . HOH   E 4 .   ? 28.773 -8.003  -15.284 1.00 50.88 ?  483 HOH   A O    1 
HETATM 6930 O O    . HOH   E 4 .   ? 30.801 0.726   19.180  1.00 41.05 ?  484 HOH   A O    1 
HETATM 6931 O O    . HOH   E 4 .   ? 16.793 -20.460 16.133  1.00 33.23 ?  485 HOH   A O    1 
HETATM 6932 O O    . HOH   E 4 .   ? 20.581 -15.977 -7.502  1.00 30.18 ?  486 HOH   A O    1 
HETATM 6933 O O    . HOH   E 4 .   ? 23.184 -12.773 19.317  1.00 49.03 ?  487 HOH   A O    1 
HETATM 6934 O O    . HOH   E 4 .   ? 39.229 2.349   7.254   1.00 34.24 ?  488 HOH   A O    1 
HETATM 6935 O O    . HOH   E 4 .   ? 31.570 -0.598  -10.571 1.00 31.40 ?  489 HOH   A O    1 
HETATM 6936 O O    . HOH   E 4 .   ? 8.055  -3.213  -5.864  1.00 50.61 ?  490 HOH   A O    1 
HETATM 6937 O O    . HOH   E 4 .   ? 13.755 -25.151 8.949   1.00 36.05 ?  491 HOH   A O    1 
HETATM 6938 O O    . HOH   E 4 .   ? 18.358 -23.242 1.873   1.00 43.08 ?  492 HOH   A O    1 
HETATM 6939 O O    . HOH   E 4 .   ? 40.780 -0.187  -7.666  1.00 35.63 ?  493 HOH   A O    1 
HETATM 6940 O O    . HOH   E 4 .   ? 30.817 5.810   -14.711 1.00 36.50 ?  494 HOH   A O    1 
HETATM 6941 O O    . HOH   E 4 .   ? 20.068 -22.356 4.205   1.00 32.45 ?  495 HOH   A O    1 
HETATM 6942 O O    . HOH   E 4 .   ? 16.205 -23.401 5.760   1.00 29.95 ?  496 HOH   A O    1 
HETATM 6943 O O    . HOH   E 4 .   ? 30.794 -5.834  -11.862 1.00 50.20 ?  497 HOH   A O    1 
HETATM 6944 O O    . HOH   E 4 .   ? 23.243 -23.781 1.621   1.00 32.39 ?  498 HOH   A O    1 
HETATM 6945 O O    . HOH   E 4 .   ? 37.358 -6.655  7.624   1.00 28.85 ?  499 HOH   A O    1 
HETATM 6946 O O    . HOH   E 4 .   ? 39.528 -0.053  6.695   1.00 32.60 ?  500 HOH   A O    1 
HETATM 6947 O O    . HOH   E 4 .   ? 38.009 13.926  6.689   1.00 27.69 ?  501 HOH   A O    1 
HETATM 6948 O O    . HOH   E 4 .   ? 29.013 14.467  0.856   1.00 49.21 ?  502 HOH   A O    1 
HETATM 6949 O O    . HOH   E 4 .   ? 14.782 8.238   4.927   1.00 41.14 ?  503 HOH   A O    1 
HETATM 6950 O O    . HOH   E 4 .   ? 22.076 -24.026 4.462   1.00 27.95 ?  504 HOH   A O    1 
HETATM 6951 O O    . HOH   E 4 .   ? 36.436 -6.480  10.189  1.00 49.17 ?  505 HOH   A O    1 
HETATM 6952 O O    A HOH   E 4 .   ? 17.549 -6.499  -14.236 0.58 33.60 ?  506 HOH   A O    1 
HETATM 6953 O O    T HOH   E 4 .   ? 11.959 -2.127  -3.726  0.30 13.24 ?  507 HOH   A O    1 
HETATM 6954 O O    . HOH   E 4 .   ? 24.129 9.053   -7.174  1.00 41.74 ?  508 HOH   A O    1 
HETATM 6955 O O    . HOH   E 4 .   ? 15.768 -12.318 27.330  1.00 47.42 ?  509 HOH   A O    1 
HETATM 6956 O O    . HOH   E 4 .   ? 16.313 -21.146 18.666  1.00 41.69 ?  510 HOH   A O    1 
HETATM 6957 O O    . HOH   E 4 .   ? 14.723 -22.724 19.835  1.00 37.23 ?  511 HOH   A O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 29.850 -22.422 5.466   1.00 21.78 ?  201 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 27.701 -29.177 -1.887  1.00 33.28 ?  202 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 41.808 -36.041 -17.245 1.00 32.14 ?  203 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 37.942 -39.486 -0.187  1.00 41.62 ?  204 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 29.982 -26.304 4.059   1.00 30.53 ?  205 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 47.403 -7.433  -3.904  1.00 41.49 ?  206 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 27.884 -41.836 -15.167 1.00 35.95 ?  207 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 59.128 -18.765 6.896   1.00 35.02 ?  208 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 58.197 -12.981 8.460   1.00 30.31 ?  209 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 30.243 -41.035 -8.069  1.00 17.68 ?  210 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 49.559 -22.679 -19.764 1.00 49.17 ?  211 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 57.754 -24.524 5.035   1.00 37.63 ?  212 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 30.900 -28.772 4.321   1.00 30.18 ?  213 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 54.534 -9.395  -8.657  1.00 20.16 ?  214 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 56.385 -19.704 7.399   1.00 34.35 ?  215 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 50.128 -3.376  7.192   1.00 36.29 ?  216 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 56.742 -30.791 -7.802  1.00 29.78 ?  217 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 41.275 -7.855  5.445   1.00 39.76 ?  218 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 29.722 -34.137 -0.400  1.00 33.61 ?  219 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 53.062 -13.531 -20.432 1.00 43.64 ?  220 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 41.518 -39.204 -14.848 1.00 23.65 ?  221 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 50.714 -6.111  0.164   1.00 28.14 ?  222 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 44.521 -7.289  2.159   1.00 34.28 ?  223 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 37.199 -19.756 -18.142 1.00 37.80 ?  224 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 34.574 -36.394 -7.162  1.00 18.91 ?  225 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 57.381 -16.277 -12.269 1.00 18.04 ?  226 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 46.337 -1.699  13.404  1.00 29.89 ?  227 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 32.863 -43.834 -11.298 1.00 21.32 ?  228 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 36.021 -43.319 -8.398  1.00 36.68 ?  229 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 48.176 -24.623 -17.755 1.00 30.36 ?  230 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 35.126 -8.014  -2.983  1.00 18.94 ?  231 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 51.650 -6.512  4.378   1.00 20.20 ?  232 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 50.776 -13.003 -0.446  1.00 12.57 ?  233 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 57.276 -26.887 -7.628  1.00 45.24 ?  234 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 44.943 -43.621 -10.522 1.00 29.25 ?  235 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 34.863 -24.668 13.853  1.00 31.33 ?  236 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 44.524 -27.735 -0.699  1.00 23.46 ?  237 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 41.401 -9.692  13.093  1.00 22.77 ?  238 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 40.727 -16.066 14.131  1.00 21.94 ?  239 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 25.385 -25.933 -1.290  1.00 34.41 ?  240 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 28.488 -19.702 -13.219 1.00 26.34 ?  241 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 42.593 -25.392 2.640   1.00 15.61 ?  242 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 45.141 -34.972 6.779   1.00 43.29 ?  243 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 38.534 -11.108 -2.284  1.00 19.47 ?  244 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 39.298 -10.931 6.136   1.00 25.18 ?  245 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 34.208 -18.469 11.389  1.00 25.23 ?  246 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 50.968 -39.977 -8.148  1.00 32.90 ?  247 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 42.654 -22.893 3.874   1.00 12.52 ?  248 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 55.240 -16.399 -14.277 1.00 28.00 ?  249 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 57.667 -24.385 -3.793  1.00 21.87 ?  250 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 43.096 -43.281 -8.207  1.00 30.66 ?  251 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 47.909 -6.942  15.636  1.00 35.30 ?  252 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 40.417 -12.779 -11.526 1.00 15.49 ?  253 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 39.537 -11.135 0.312   1.00 17.25 ?  254 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 27.152 -31.853 -9.924  1.00 22.07 ?  255 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 58.210 -10.649 -4.056  1.00 21.08 ?  256 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 29.768 -25.233 -10.821 1.00 18.22 ?  257 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 31.818 -17.893 -14.528 1.00 29.54 ?  258 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 47.995 -22.786 5.837   1.00 18.80 ?  259 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 43.234 -32.421 -17.073 1.00 23.82 ?  260 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 48.605 -36.588 -15.518 1.00 46.53 ?  261 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 41.878 -23.599 9.312   1.00 18.89 ?  262 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 30.879 -15.737 2.659   1.00 14.62 ?  263 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 57.461 -9.244  1.443   1.00 20.62 ?  264 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 49.370 -28.731 -6.893  1.00 15.84 ?  265 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 49.588 -0.465  10.282  1.00 30.49 ?  266 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 28.520 -30.892 -14.755 1.00 30.45 ?  267 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 56.239 -23.640 -14.671 1.00 27.33 ?  268 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 34.510 -12.790 2.602   1.00 23.67 ?  269 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 43.451 -15.814 -12.225 1.00 14.70 ?  270 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 30.622 -42.304 -10.633 1.00 30.90 ?  271 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 42.304 -9.948  9.381   1.00 21.27 ?  272 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 48.569 -12.117 -14.647 1.00 26.27 ?  273 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 56.925 -8.630  8.442   1.00 20.08 ?  274 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 51.489 -13.864 11.134  1.00 26.47 ?  275 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 46.648 -31.269 -4.775  1.00 22.21 ?  276 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 42.391 -34.725 3.770   1.00 28.28 ?  277 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 38.909 -11.969 12.439  1.00 35.40 ?  278 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 27.997 -22.874 -8.030  1.00 18.85 ?  279 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 53.728 -12.739 -22.196 1.00 35.06 ?  280 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 45.936 -40.428 -3.607  1.00 29.76 ?  281 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 28.267 -34.365 -9.380  1.00 19.24 ?  282 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 50.023 -24.637 5.807   1.00 34.86 ?  283 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 48.435 -25.078 3.132   1.00 14.10 ?  284 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 34.988 -33.423 -19.210 1.00 26.85 ?  285 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 36.827 -12.788 -1.519  1.00 26.15 ?  286 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 46.893 -29.561 9.836   1.00 31.46 ?  287 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 33.598 -15.297 -13.947 1.00 22.07 ?  288 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 47.098 -34.008 -4.593  1.00 18.28 ?  289 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 57.131 -12.123 12.387  1.00 38.48 ?  290 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 45.370 -33.465 -15.880 1.00 24.16 ?  291 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 48.733 -20.083 5.981   1.00 14.48 ?  292 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 27.619 -26.647 -15.615 1.00 33.33 ?  293 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 52.605 -35.697 -8.647  1.00 29.97 ?  294 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 43.028 -20.156 -20.746 1.00 32.41 ?  295 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 52.444 -10.388 13.061  1.00 25.03 ?  296 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 59.769 -15.273 8.226   1.00 32.46 ?  297 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 51.265 -37.636 -9.592  1.00 28.36 ?  298 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 52.891 -15.870 -12.776 1.00 22.47 ?  299 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 43.056 -12.028 -18.472 1.00 22.38 ?  300 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 35.062 -33.584 4.550   1.00 30.90 ?  301 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 40.344 -10.873 -9.542  1.00 17.81 ?  302 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 37.433 -18.144 13.107  1.00 30.75 ?  303 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 44.655 -27.483 2.021   1.00 16.42 ?  304 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 41.178 -5.495  11.472  1.00 47.81 ?  305 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 44.030 -29.371 -4.686  1.00 24.37 ?  306 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 62.692 -13.574 4.780   1.00 28.91 ?  307 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 51.743 -5.931  -7.881  1.00 44.23 ?  308 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 37.301 -35.714 7.185   1.00 34.04 ?  309 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 37.926 -10.272 -10.773 1.00 18.56 ?  310 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 53.486 -30.240 4.547   1.00 19.68 ?  311 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 52.603 -29.292 -13.014 1.00 25.40 ?  312 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 37.137 -30.665 -20.989 1.00 33.57 ?  313 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 43.194 -21.494 10.662  1.00 17.19 ?  314 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 25.977 -21.473 -3.566  1.00 17.93 ?  315 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 42.429 -9.820  -14.897 1.00 37.97 ?  316 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 60.069 -17.162 -10.370 1.00 36.80 ?  317 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 41.799 -8.095  1.427   1.00 25.69 ?  318 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 38.455 -9.366  -13.272 1.00 29.29 ?  319 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 41.243 -24.579 15.796  1.00 47.30 ?  320 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 32.832 -34.619 -5.910  1.00 17.54 ?  321 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 38.328 -12.739 7.950   1.00 19.17 ?  322 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 26.383 -21.039 -6.271  1.00 17.45 ?  323 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 44.596 -24.657 9.582   1.00 22.96 ?  324 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 62.958 -20.192 -0.750  1.00 38.73 ?  325 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 48.138 -32.719 -16.629 1.00 44.54 ?  326 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 44.075 -1.809  7.703   1.00 48.29 ?  327 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 27.857 -14.763 -9.485  1.00 36.27 ?  328 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 51.445 -32.948 -10.734 1.00 39.94 ?  329 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 36.733 -12.429 4.284   1.00 18.55 ?  330 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 57.638 -22.071 3.324   1.00 32.87 ?  331 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 33.540 -31.160 11.087  1.00 36.73 ?  332 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 47.200 -24.549 8.184   1.00 28.36 ?  333 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 43.121 -34.676 0.085   1.00 20.95 ?  334 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 43.496 -15.457 18.211  1.00 27.63 ?  335 HOH   B O    1 
HETATM 7093 O O    . HOH   F 4 .   ? 37.115 -15.203 -16.544 1.00 41.69 ?  336 HOH   B O    1 
HETATM 7094 O O    . HOH   F 4 .   ? 45.687 -36.302 -16.090 1.00 35.57 ?  337 HOH   B O    1 
HETATM 7095 O O    . HOH   F 4 .   ? 42.948 -43.517 -14.364 1.00 45.66 ?  338 HOH   B O    1 
HETATM 7096 O O    . HOH   F 4 .   ? 39.579 -23.522 -20.331 1.00 35.18 ?  339 HOH   B O    1 
HETATM 7097 O O    . HOH   F 4 .   ? 47.503 -27.475 2.032   1.00 15.68 ?  340 HOH   B O    1 
HETATM 7098 O O    . HOH   F 4 .   ? 28.914 -42.896 -12.380 1.00 41.42 ?  341 HOH   B O    1 
HETATM 7099 O O    . HOH   F 4 .   ? 37.122 -45.244 -9.760  1.00 37.65 ?  342 HOH   B O    1 
HETATM 7100 O O    . HOH   F 4 .   ? 46.743 -20.016 12.364  1.00 27.76 ?  343 HOH   B O    1 
HETATM 7101 O O    . HOH   F 4 .   ? 38.588 -22.485 14.989  1.00 44.00 ?  344 HOH   B O    1 
HETATM 7102 O O    . HOH   F 4 .   ? 32.993 -14.710 1.029   1.00 20.16 ?  345 HOH   B O    1 
HETATM 7103 O O    . HOH   F 4 .   ? 38.671 -12.228 -16.240 1.00 41.13 ?  346 HOH   B O    1 
HETATM 7104 O O    . HOH   F 4 .   ? 34.534 -10.353 7.672   1.00 24.79 ?  347 HOH   B O    1 
HETATM 7105 O O    . HOH   F 4 .   ? 40.422 -43.513 -9.117  1.00 26.85 ?  348 HOH   B O    1 
HETATM 7106 O O    . HOH   F 4 .   ? 39.804 -44.398 -11.199 1.00 41.10 ?  349 HOH   B O    1 
HETATM 7107 O O    . HOH   F 4 .   ? 33.829 -9.356  -8.872  1.00 31.75 ?  350 HOH   B O    1 
HETATM 7108 O O    . HOH   F 4 .   ? 44.216 -37.398 -17.738 1.00 34.06 ?  351 HOH   B O    1 
HETATM 7109 O O    . HOH   F 4 .   ? 23.231 -23.644 6.794   1.00 36.09 ?  352 HOH   B O    1 
HETATM 7110 O O    . HOH   F 4 .   ? 62.607 -20.090 -4.828  1.00 51.12 ?  353 HOH   B O    1 
HETATM 7111 O O    . HOH   F 4 .   ? 27.787 -26.682 -0.509  1.00 30.72 ?  354 HOH   B O    1 
HETATM 7112 O O    . HOH   F 4 .   ? 55.670 -8.275  10.887  1.00 25.32 ?  355 HOH   B O    1 
HETATM 7113 O O    . HOH   F 4 .   ? 36.222 -8.555  -9.684  1.00 35.70 ?  356 HOH   B O    1 
HETATM 7114 O O    . HOH   F 4 .   ? 56.511 -7.253  3.149   1.00 29.60 ?  357 HOH   B O    1 
HETATM 7115 O O    . HOH   F 4 .   ? 43.269 -12.851 -21.193 1.00 28.23 ?  358 HOH   B O    1 
HETATM 7116 O O    . HOH   F 4 .   ? 34.088 -7.770  11.462  1.00 41.39 ?  359 HOH   B O    1 
HETATM 7117 O O    . HOH   F 4 .   ? 61.504 -19.902 1.842   1.00 37.65 ?  360 HOH   B O    1 
HETATM 7118 O O    . HOH   F 4 .   ? 56.973 -21.665 -16.351 1.00 41.70 ?  361 HOH   B O    1 
HETATM 7119 O O    . HOH   F 4 .   ? 40.269 -8.859  9.866   1.00 39.13 ?  362 HOH   B O    1 
HETATM 7120 O O    . HOH   F 4 .   ? 27.197 -25.928 -11.506 1.00 35.32 ?  363 HOH   B O    1 
HETATM 7121 O O    . HOH   F 4 .   ? 40.405 -11.320 -14.008 1.00 30.90 ?  364 HOH   B O    1 
HETATM 7122 O O    . HOH   F 4 .   ? 54.199 -5.736  3.065   1.00 35.48 ?  365 HOH   B O    1 
HETATM 7123 O O    . HOH   F 4 .   ? 48.284 -26.579 8.873   1.00 44.59 ?  366 HOH   B O    1 
HETATM 7124 O O    . HOH   F 4 .   ? 32.553 -23.679 14.091  1.00 42.11 ?  367 HOH   B O    1 
HETATM 7125 O O    . HOH   F 4 .   ? 36.141 -8.625  9.039   1.00 40.91 ?  368 HOH   B O    1 
HETATM 7126 O O    . HOH   F 4 .   ? 39.858 -7.072  7.773   1.00 40.06 ?  369 HOH   B O    1 
HETATM 7127 O O    . HOH   F 4 .   ? 58.911 -10.380 9.295   1.00 39.24 ?  370 HOH   B O    1 
HETATM 7128 O O    . HOH   F 4 .   ? 56.113 -7.835  -0.572  1.00 33.98 ?  371 HOH   B O    1 
HETATM 7129 O O    . HOH   F 4 .   ? 62.990 -12.452 7.018   1.00 39.51 ?  372 HOH   B O    1 
HETATM 7130 O O    . HOH   F 4 .   ? 41.927 -9.977  -17.407 1.00 58.34 ?  373 HOH   B O    1 
HETATM 7131 O O    . HOH   F 4 .   ? 41.990 -6.671  -4.871  1.00 47.26 ?  374 HOH   B O    1 
HETATM 7132 O O    . HOH   F 4 .   ? 52.023 -12.981 13.461  1.00 26.43 ?  375 HOH   B O    1 
HETATM 7133 O O    . HOH   F 4 .   ? 36.567 -22.901 13.290  1.00 28.62 ?  376 HOH   B O    1 
HETATM 7134 O O    . HOH   F 4 .   ? 38.038 -10.609 10.065  1.00 28.77 ?  377 HOH   B O    1 
HETATM 7135 O O    . HOH   F 4 .   ? 40.153 -7.750  3.192   1.00 41.63 ?  378 HOH   B O    1 
HETATM 7136 O O    . HOH   F 4 .   ? 42.778 -17.084 -23.227 1.00 39.96 ?  379 HOH   B O    1 
HETATM 7137 O O    . HOH   F 4 .   ? 44.195 -5.667  -3.472  1.00 44.27 ?  380 HOH   B O    1 
HETATM 7138 O O    . HOH   F 4 .   ? 52.896 -29.911 7.260   1.00 23.62 ?  381 HOH   B O    1 
HETATM 7139 O O    . HOH   F 4 .   ? 46.693 -5.435  2.929   1.00 37.37 ?  382 HOH   B O    1 
HETATM 7140 O O    . HOH   F 4 .   ? 60.472 -22.334 2.920   1.00 43.35 ?  383 HOH   B O    1 
HETATM 7141 O O    . HOH   F 4 .   ? 39.656 -14.064 15.732  1.00 43.03 ?  384 HOH   B O    1 
HETATM 7142 O O    . HOH   F 4 .   ? 25.808 -18.888 -11.927 1.00 42.10 ?  385 HOH   B O    1 
HETATM 7143 O O    . HOH   F 4 .   ? 35.368 -33.787 7.311   1.00 43.91 ?  386 HOH   B O    1 
HETATM 7144 O O    . HOH   F 4 .   ? 41.098 -9.834  15.903  1.00 40.07 ?  387 HOH   B O    1 
HETATM 7145 O O    . HOH   F 4 .   ? 23.947 -20.854 -7.648  1.00 29.90 ?  388 HOH   B O    1 
HETATM 7146 O O    . HOH   F 4 .   ? 35.325 -20.339 13.303  1.00 31.03 ?  389 HOH   B O    1 
HETATM 7147 O O    . HOH   F 4 .   ? 40.737 -6.637  -0.897  1.00 26.48 ?  390 HOH   B O    1 
HETATM 7148 O O    . HOH   F 4 .   ? 44.159 -31.777 -3.756  1.00 38.36 ?  391 HOH   B O    1 
HETATM 7149 O O    . HOH   F 4 .   ? 26.678 -28.017 -13.591 1.00 34.75 ?  392 HOH   B O    1 
HETATM 7150 O O    . HOH   F 4 .   ? 27.921 -27.114 2.140   1.00 32.39 ?  393 HOH   B O    1 
HETATM 7151 O O    . HOH   F 4 .   ? 24.662 -20.590 -10.538 1.00 39.33 ?  394 HOH   B O    1 
HETATM 7152 O O    . HOH   F 4 .   ? 34.356 -33.480 9.616   1.00 37.36 ?  395 HOH   B O    1 
HETATM 7153 O O    . HOH   F 4 .   ? 50.666 -30.817 8.736   1.00 30.59 ?  396 HOH   B O    1 
HETATM 7154 O O    . HOH   F 4 .   ? 26.857 -30.679 -12.600 1.00 29.60 ?  397 HOH   B O    1 
HETATM 7155 O O    . HOH   F 4 .   ? 57.741 -6.555  -2.324  1.00 34.96 ?  398 HOH   B O    1 
HETATM 7156 O O    . HOH   F 4 .   ? 45.796 -20.249 15.229  1.00 47.84 ?  399 HOH   B O    1 
HETATM 7157 O O    . HOH   F 4 .   ? 41.060 -11.860 -22.394 1.00 35.23 ?  400 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   ? 0.6439 0.6597 0.7504 0.0015  -0.0101 0.0829  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6332 0.6410 0.7319 -0.0049 -0.0100 0.0606  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6407 0.6568 0.7397 -0.0007 -0.0097 0.0826  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6302 0.6379 0.7217 -0.0064 -0.0098 0.0607  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6250 0.6453 0.7048 -0.0094 -0.0152 0.0853  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6146 0.6252 0.6884 -0.0131 -0.0143 0.0621  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6281 0.6479 0.7186 -0.0079 -0.0169 0.0879  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6177 0.6284 0.7009 -0.0123 -0.0156 0.0639  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6502 0.6634 0.7549 0.0036  -0.0046 0.0801  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6399 0.6454 0.7366 -0.0028 -0.0056 0.0595  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6535 0.6653 0.7582 0.0052  -0.0029 0.0793  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6432 0.6476 0.7407 -0.0015 -0.0042 0.0591  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6532 0.6656 0.7593 0.0050  -0.0030 0.0799  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6430 0.6479 0.7411 -0.0015 -0.0042 0.0595  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6034 0.6290 0.6456 -0.0202 -0.0184 0.0848  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.5931 0.6069 0.6329 -0.0211 -0.0172 0.0611  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.5786 0.6100 0.5798 -0.0317 -0.0220 0.0820  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.5687 0.5862 0.5716 -0.0298 -0.0204 0.0584  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5410 0.5836 0.5407 -0.0468 -0.0141 0.0597  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5330 0.5587 0.5322 -0.0425 -0.0135 0.0442  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5435 0.5857 0.5392 -0.0466 -0.0169 0.0602  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5351 0.5607 0.5319 -0.0423 -0.0155 0.0458  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.5880 0.6153 0.5476 -0.0290 -0.0316 0.1013  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.5770 0.5910 0.5455 -0.0270 -0.0292 0.0701  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.5949 0.6186 0.5166 -0.0274 -0.0398 0.1189  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.5830 0.5940 0.5210 -0.0252 -0.0369 0.0805  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.5980 0.6199 0.5049 -0.0273 -0.0434 0.1262  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.5855 0.5949 0.5122 -0.0246 -0.0407 0.0847  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.5965 0.6194 0.5082 -0.0267 -0.0425 0.1258  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.5843 0.5947 0.5144 -0.0243 -0.0390 0.0851  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.4981 0.5527 0.4980 -0.0639 -0.0024 0.0372  5   SER   A N   
60   N N   B SER   A 5   ? 0.4931 0.5271 0.4891 -0.0565 -0.0040 0.0283  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4532 0.5208 0.4549 -0.0804 0.0141  0.0173  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4518 0.4947 0.4459 -0.0703 0.0088  0.0141  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4031 0.4818 0.4047 -0.0950 0.0343  0.0112  5   SER   A C   
64   C C   B SER   A 5   ? 0.4072 0.4568 0.3966 -0.0830 0.0257  0.0091  5   SER   A C   
65   O O   A SER   A 5   ? 0.4066 0.4850 0.4052 -0.0916 0.0343  0.0029  5   SER   A O   
66   O O   B SER   A 5   ? 0.4099 0.4600 0.3947 -0.0805 0.0264  0.0018  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4587 0.5268 0.4654 -0.0822 0.0139  0.0067  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4555 0.4993 0.4537 -0.0711 0.0068  0.0066  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4623 0.5301 0.4704 -0.0831 0.0140  0.0003  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4578 0.5016 0.4570 -0.0715 0.0052  0.0021  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3470 0.4389 0.3414 -0.1122 0.0551  0.0178  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3581 0.4161 0.3400 -0.0977 0.0418  0.0135  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2972 0.3949 0.2854 -0.1223 0.0650  0.0301  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3113 0.3745 0.2897 -0.1078 0.0501  0.0212  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2910 0.3882 0.2879 -0.1253 0.0771  0.0295  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.2997 0.3641 0.2894 -0.1100 0.0617  0.0189  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2960 0.3941 0.3251 -0.1276 0.0792  0.0383  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3041 0.3676 0.3154 -0.1092 0.0649  0.0258  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2687 0.3599 0.2467 -0.1181 0.0488  0.0356  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2859 0.3462 0.2555 -0.1076 0.0404  0.0273  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2470 0.3319 0.2272 -0.1048 0.0393  0.0333  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2663 0.3246 0.2379 -0.0992 0.0315  0.0272  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2362 0.3157 0.2251 -0.1000 0.0252  0.0267  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2567 0.3123 0.2330 -0.0966 0.0235  0.0244  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2515 0.3244 0.2446 -0.0872 0.0372  0.0284  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2659 0.3184 0.2492 -0.0888 0.0272  0.0245  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2356 0.3089 0.2336 -0.0920 0.0318  0.0258  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2545 0.3067 0.2372 -0.0924 0.0249  0.0242  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2474 0.3178 0.2580 -0.0803 0.0386  0.0245  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2609 0.3134 0.2572 -0.0846 0.0252  0.0224  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2414 0.3116 0.2444 -0.0836 0.0337  0.0211  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2570 0.3085 0.2449 -0.0873 0.0229  0.0205  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2815 0.3755 0.2694 -0.1216 0.0799  0.0186  7   SER   A N   
122  N N   B SER   A 7   ? 0.2853 0.3500 0.2734 -0.1096 0.0654  0.0099  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2817 0.3666 0.2742 -0.1056 0.0735  0.0010  7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2777 0.3400 0.2745 -0.0982 0.0605  -0.0042 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2621 0.3343 0.2454 -0.0965 0.0752  0.0029  7   SER   A C   
126  C C   B SER   A 7   ? 0.2548 0.3145 0.2429 -0.0907 0.0641  -0.0032 7   SER   A C   
127  O O   A SER   A 7   ? 0.2737 0.3303 0.2479 -0.0932 0.0711  0.0007  7   SER   A O   
128  O O   B SER   A 7   ? 0.2602 0.3104 0.2375 -0.0921 0.0673  -0.0027 7   SER   A O   
129  C CB  A SER   A 7   ? 0.3034 0.3883 0.3091 -0.0928 0.0736  -0.0082 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2945 0.3551 0.3087 -0.0900 0.0588  -0.0108 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.3230 0.4007 0.3429 -0.0830 0.0677  -0.0148 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3107 0.3656 0.3434 -0.0828 0.0523  -0.0192 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2345 0.3044 0.2338 -0.0865 0.0695  -0.0022 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2279 0.2919 0.2290 -0.0799 0.0588  -0.0051 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2152 0.2792 0.2396 -0.0632 0.0625  -0.0002 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2098 0.2726 0.2328 -0.0595 0.0522  -0.0015 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1903 0.2601 0.2300 -0.0427 0.0502  0.0007  8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1876 0.2579 0.2257 -0.0408 0.0468  0.0029  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1944 0.2624 0.2565 -0.0264 0.0463  -0.0162 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1894 0.2608 0.2437 -0.0261 0.0443  -0.0092 8   GLY   A O   
157  N N   . TYR   A 9   ? 0.1735 0.2428 0.2253 -0.0317 0.0476  0.0196  9   TYR   A N   
158  C CA  . TYR   A 9   ? 0.1626 0.2207 0.2058 -0.0308 0.0340  0.0353  9   TYR   A CA  
159  C C   . TYR   A 9   ? 0.1592 0.2022 0.2060 -0.0257 0.0314  0.0435  9   TYR   A C   
160  O O   . TYR   A 9   ? 0.1856 0.2210 0.2176 -0.0249 0.0296  0.0425  9   TYR   A O   
161  C CB  . TYR   A 9   ? 0.1558 0.2320 0.2067 -0.0247 0.0236  0.0299  9   TYR   A CB  
162  C CG  . TYR   A 9   ? 0.1541 0.2403 0.1994 -0.0186 0.0365  0.0126  9   TYR   A CG  
163  C CD1 . TYR   A 9   ? 0.1613 0.2519 0.2018 -0.0360 0.0361  0.0057  9   TYR   A CD1 
164  C CD2 . TYR   A 9   ? 0.1591 0.2346 0.1880 -0.0153 0.0384  0.0214  9   TYR   A CD2 
165  C CE1 . TYR   A 9   ? 0.1744 0.2542 0.2244 -0.0437 0.0401  -0.0007 9   TYR   A CE1 
166  C CE2 . TYR   A 9   ? 0.1659 0.2432 0.2001 -0.0224 0.0350  0.0153  9   TYR   A CE2 
167  C CZ  . TYR   A 9   ? 0.1670 0.2521 0.2251 -0.0440 0.0534  0.0035  9   TYR   A CZ  
168  O OH  . TYR   A 9   ? 0.1732 0.2709 0.2678 -0.0577 0.0577  -0.0041 9   TYR   A OH  
179  N N   . LEU   A 10  ? 0.1592 0.1901 0.2016 -0.0271 0.0130  0.0439  10  LEU   A N   
180  C CA  . LEU   A 10  ? 0.1517 0.1838 0.2080 -0.0268 0.0088  0.0586  10  LEU   A CA  
181  C C   . LEU   A 10  ? 0.1517 0.1731 0.2077 -0.0287 0.0009  0.0604  10  LEU   A C   
182  O O   . LEU   A 10  ? 0.1617 0.1605 0.2119 -0.0277 0.0237  0.0548  10  LEU   A O   
183  C CB  . LEU   A 10  ? 0.1605 0.1905 0.2359 -0.0257 0.0016  0.0699  10  LEU   A CB  
184  C CG  . LEU   A 10  ? 0.1824 0.2007 0.2945 -0.0091 -0.0375 0.0832  10  LEU   A CG  
185  C CD1 . LEU   A 10  ? 0.2041 0.2090 0.3333 -0.0204 -0.0301 0.0792  10  LEU   A CD1 
186  C CD2 . LEU   A 10  ? 0.2159 0.2269 0.3317 -0.0076 -0.0240 0.0733  10  LEU   A CD2 
198  N N   . LYS   A 11  ? 0.1548 0.1833 0.2198 -0.0355 0.0018  0.0685  11  LYS   A N   
199  C CA  . LYS   A 11  ? 0.1604 0.1796 0.2134 -0.0416 0.0045  0.0672  11  LYS   A CA  
200  C C   . LYS   A 11  ? 0.1579 0.1862 0.2083 -0.0453 0.0053  0.0502  11  LYS   A C   
201  O O   . LYS   A 11  ? 0.1697 0.2342 0.2444 -0.0699 0.0164  0.0304  11  LYS   A O   
202  C CB  . LYS   A 11  ? 0.1695 0.1699 0.2077 -0.0379 -0.0018 0.0465  11  LYS   A CB  
203  C CG  . LYS   A 11  ? 0.1846 0.1690 0.2078 -0.0355 0.0029  0.0449  11  LYS   A CG  
204  C CD  . LYS   A 11  ? 0.2035 0.1744 0.2048 -0.0282 0.0081  0.0388  11  LYS   A CD  
205  C CE  . LYS   A 11  ? 0.2108 0.1791 0.1970 -0.0287 0.0083  0.0417  11  LYS   A CE  
206  N NZ  . LYS   A 11  ? 0.2149 0.1761 0.2068 -0.0187 0.0001  0.0531  11  LYS   A NZ  
220  N N   . LEU   A 12  ? 0.1473 0.1768 0.2013 -0.0347 -0.0003 0.0488  12  LEU   A N   
221  C CA  . LEU   A 12  ? 0.1512 0.1919 0.1898 -0.0222 -0.0057 0.0598  12  LEU   A CA  
222  C C   . LEU   A 12  ? 0.1643 0.1852 0.2037 -0.0298 0.0042  0.0529  12  LEU   A C   
223  O O   . LEU   A 12  ? 0.1652 0.1926 0.2147 -0.0294 -0.0006 0.0425  12  LEU   A O   
224  C CB  . LEU   A 12  ? 0.1611 0.1962 0.2003 -0.0220 0.0016  0.0640  12  LEU   A CB  
225  C CG  . LEU   A 12  ? 0.1739 0.2024 0.2360 -0.0164 0.0124  0.0638  12  LEU   A CG  
226  C CD1 . LEU   A 12  ? 0.1905 0.2070 0.2323 -0.0024 0.0251  0.0661  12  LEU   A CD1 
227  C CD2 . LEU   A 12  ? 0.1728 0.2041 0.2714 -0.0139 0.0002  0.0681  12  LEU   A CD2 
239  N N   . THR   A 13  ? 0.1544 0.1731 0.2199 -0.0310 0.0061  0.0515  13  THR   A N   
240  C CA  . THR   A 13  ? 0.1601 0.1740 0.2232 -0.0338 0.0133  0.0443  13  THR   A CA  
241  C C   . THR   A 13  ? 0.1576 0.1643 0.2455 -0.0320 -0.0005 0.0523  13  THR   A C   
242  O O   . THR   A 13  ? 0.1630 0.1681 0.2361 -0.0293 0.0076  0.0507  13  THR   A O   
243  C CB  . THR   A 13  ? 0.1628 0.1878 0.2323 -0.0285 0.0012  0.0416  13  THR   A CB  
244  O OG1 . THR   A 13  ? 0.1588 0.1929 0.2513 -0.0373 0.0021  0.0490  13  THR   A OG1 
245  C CG2 . THR   A 13  ? 0.1814 0.2054 0.2404 -0.0231 0.0076  0.0321  13  THR   A CG2 
253  N N   . ASP   A 14  ? 0.1586 0.1646 0.2609 -0.0391 -0.0011 0.0626  14  ASP   A N   
254  C CA  . ASP   A 14  ? 0.1636 0.1791 0.2744 -0.0300 -0.0085 0.0729  14  ASP   A CA  
255  C C   . ASP   A 14  ? 0.1583 0.1829 0.2452 -0.0327 -0.0203 0.0722  14  ASP   A C   
256  O O   . ASP   A 14  ? 0.1822 0.1978 0.2499 -0.0482 -0.0289 0.0793  14  ASP   A O   
257  C CB  . ASP   A 14  ? 0.1923 0.2026 0.3402 -0.0301 -0.0166 0.0830  14  ASP   A CB  
258  C CG  . ASP   A 14  ? 0.2259 0.2559 0.4198 -0.0311 -0.0061 0.0786  14  ASP   A CG  
259  O OD1 . ASP   A 14  ? 0.2442 0.2779 0.4475 -0.0118 -0.0107 0.0792  14  ASP   A OD1 
260  O OD2 . ASP   A 14  ? 0.2472 0.2987 0.4613 -0.0163 -0.0179 0.0585  14  ASP   A OD2 
265  N N   . ASN   A 15  ? 0.1440 0.1672 0.2407 -0.0315 -0.0076 0.0689  15  ASN   A N   
266  C CA  . ASN   A 15  ? 0.1479 0.1645 0.2558 -0.0222 -0.0074 0.0526  15  ASN   A CA  
267  C C   . ASN   A 15  ? 0.1477 0.1575 0.2752 -0.0242 0.0002  0.0505  15  ASN   A C   
268  O O   . ASN   A 15  ? 0.1560 0.1586 0.3039 -0.0256 -0.0167 0.0451  15  ASN   A O   
269  C CB  . ASN   A 15  ? 0.1496 0.1647 0.2520 -0.0185 -0.0097 0.0522  15  ASN   A CB  
270  C CG  . ASN   A 15  ? 0.1552 0.1658 0.2592 -0.0128 0.0015  0.0287  15  ASN   A CG  
271  O OD1 . ASN   A 15  ? 0.1701 0.1719 0.2781 -0.0322 -0.0001 0.0332  15  ASN   A OD1 
272  N ND2 . ASN   A 15  ? 0.1623 0.1762 0.2510 -0.0149 0.0120  0.0290  15  ASN   A ND2 
279  N N   . VAL   A 16  ? 0.1477 0.1596 0.2550 -0.0279 0.0051  0.0524  16  VAL   A N   
280  C CA  . VAL   A 16  ? 0.1518 0.1659 0.2428 -0.0206 -0.0007 0.0588  16  VAL   A CA  
281  C C   . VAL   A 16  ? 0.1449 0.1628 0.2244 -0.0305 -0.0019 0.0508  16  VAL   A C   
282  O O   . VAL   A 16  ? 0.1435 0.1562 0.2263 -0.0250 0.0066  0.0401  16  VAL   A O   
283  C CB  . VAL   A 16  ? 0.1643 0.1720 0.2420 -0.0021 0.0232  0.0644  16  VAL   A CB  
284  C CG1 . VAL   A 16  ? 0.1814 0.1830 0.2542 0.0059  0.0281  0.0668  16  VAL   A CG1 
285  C CG2 . VAL   A 16  ? 0.1694 0.1843 0.2560 0.0038  0.0389  0.0567  16  VAL   A CG2 
295  N N   . TYR   A 17  ? 0.1333 0.1622 0.2282 -0.0276 0.0023  0.0532  17  TYR   A N   
296  C CA  . TYR   A 17  ? 0.1404 0.1637 0.2152 -0.0317 0.0027  0.0558  17  TYR   A CA  
297  C C   . TYR   A 17  ? 0.1497 0.1546 0.2219 -0.0229 0.0109  0.0450  17  TYR   A C   
298  O O   . TYR   A 17  ? 0.1471 0.1573 0.2318 -0.0275 0.0159  0.0562  17  TYR   A O   
299  C CB  . TYR   A 17  ? 0.1603 0.1623 0.2263 -0.0387 -0.0122 0.0504  17  TYR   A CB  
300  C CG  . TYR   A 17  ? 0.1934 0.1743 0.2260 -0.0378 -0.0229 0.0442  17  TYR   A CG  
301  C CD1 . TYR   A 17  ? 0.2094 0.1837 0.2371 -0.0216 -0.0287 0.0424  17  TYR   A CD1 
302  C CD2 . TYR   A 17  ? 0.2143 0.1811 0.2047 -0.0549 -0.0256 0.0501  17  TYR   A CD2 
303  C CE1 . TYR   A 17  ? 0.2248 0.1841 0.2413 -0.0257 -0.0329 0.0431  17  TYR   A CE1 
304  C CE2 . TYR   A 17  ? 0.2336 0.1837 0.2161 -0.0501 -0.0348 0.0323  17  TYR   A CE2 
305  C CZ  . TYR   A 17  ? 0.2427 0.1780 0.2233 -0.0390 -0.0384 0.0437  17  TYR   A CZ  
306  O OH  . TYR   A 17  ? 0.2665 0.1844 0.2438 -0.0284 -0.0385 0.0443  17  TYR   A OH  
316  N N   . ILE   A 18  ? 0.1556 0.1569 0.2180 -0.0179 0.0176  0.0615  18  ILE   A N   
317  C CA  . ILE   A 18  ? 0.1563 0.1635 0.2105 -0.0150 0.0195  0.0490  18  ILE   A CA  
318  C C   . ILE   A 18  ? 0.1560 0.1766 0.2162 -0.0222 0.0257  0.0620  18  ILE   A C   
319  O O   . ILE   A 18  ? 0.1566 0.1881 0.2187 -0.0261 0.0320  0.0632  18  ILE   A O   
320  C CB  . ILE   A 18  ? 0.1579 0.1704 0.1984 -0.0094 0.0144  0.0573  18  ILE   A CB  
321  C CG1 . ILE   A 18  ? 0.1769 0.1935 0.2081 -0.0064 0.0076  0.0685  18  ILE   A CG1 
322  C CG2 . ILE   A 18  ? 0.1721 0.1840 0.2016 -0.0114 0.0154  0.0669  18  ILE   A CG2 
323  C CD1 . ILE   A 18  ? 0.1989 0.2159 0.2327 -0.0029 -0.0029 0.0678  18  ILE   A CD1 
335  N N   A LYS   A 19  ? 0.1547 0.1729 0.2286 -0.0150 0.0473  0.0604  19  LYS   A N   
336  N N   B LYS   A 19  ? 0.1588 0.1831 0.2207 -0.0105 0.0378  0.0514  19  LYS   A N   
337  C CA  A LYS   A 19  ? 0.1672 0.1844 0.2362 -0.0090 0.0532  0.0511  19  LYS   A CA  
338  C CA  B LYS   A 19  ? 0.1710 0.2000 0.2243 -0.0024 0.0384  0.0398  19  LYS   A CA  
339  C C   A LYS   A 19  ? 0.1655 0.1725 0.2401 -0.0057 0.0626  0.0438  19  LYS   A C   
340  C C   B LYS   A 19  ? 0.1679 0.1968 0.2269 0.0005  0.0354  0.0413  19  LYS   A C   
341  O O   A LYS   A 19  ? 0.1570 0.1699 0.2370 -0.0029 0.0605  0.0592  19  LYS   A O   
342  O O   B LYS   A 19  ? 0.1652 0.1927 0.2252 -0.0060 0.0239  0.0489  19  LYS   A O   
343  C CB  A LYS   A 19  ? 0.1798 0.2038 0.2241 -0.0084 0.0570  0.0566  19  LYS   A CB  
344  C CB  B LYS   A 19  ? 0.1827 0.2172 0.2189 0.0027  0.0446  0.0331  19  LYS   A CB  
345  C CG  A LYS   A 19  ? 0.2114 0.2245 0.2322 -0.0081 0.0526  0.0530  19  LYS   A CG  
346  C CG  B LYS   A 19  ? 0.2060 0.2341 0.2226 0.0073  0.0416  0.0259  19  LYS   A CG  
347  C CD  A LYS   A 19  ? 0.2405 0.2443 0.2395 -0.0115 0.0545  0.0515  19  LYS   A CD  
348  C CD  B LYS   A 19  ? 0.2285 0.2513 0.2292 0.0098  0.0412  0.0202  19  LYS   A CD  
349  C CE  A LYS   A 19  ? 0.2570 0.2543 0.2550 -0.0223 0.0559  0.0424  19  LYS   A CE  
350  C CE  B LYS   A 19  ? 0.2420 0.2630 0.2448 0.0030  0.0426  0.0112  19  LYS   A CE  
351  N NZ  A LYS   A 19  ? 0.2662 0.2582 0.2617 -0.0329 0.0641  0.0332  19  LYS   A NZ  
352  N NZ  B LYS   A 19  ? 0.2486 0.2696 0.2499 -0.0012 0.0436  0.0044  19  LYS   A NZ  
379  N N   A ASN   A 20  ? 0.1731 0.1736 0.2509 -0.0096 0.0652  0.0475  20  ASN   A N   
380  N N   B ASN   A 20  ? 0.1678 0.2023 0.2417 0.0040  0.0394  0.0475  20  ASN   A N   
381  C CA  A ASN   A 20  ? 0.1869 0.1794 0.2550 0.0021  0.0647  0.0356  20  ASN   A CA  
382  C CA  B ASN   A 20  ? 0.1691 0.2110 0.2509 0.0182  0.0423  0.0438  20  ASN   A CA  
383  C C   A ASN   A 20  ? 0.1991 0.1839 0.2549 -0.0078 0.0734  0.0296  20  ASN   A C   
384  C C   B ASN   A 20  ? 0.1850 0.2087 0.2660 0.0178  0.0601  0.0391  20  ASN   A C   
385  O O   A ASN   A 20  ? 0.2113 0.1857 0.2482 -0.0191 0.0606  0.0238  20  ASN   A O   
386  O O   B ASN   A 20  ? 0.1893 0.2074 0.2734 0.0240  0.0535  0.0441  20  ASN   A O   
387  C CB  A ASN   A 20  ? 0.1984 0.1809 0.2709 0.0138  0.0589  0.0346  20  ASN   A CB  
388  C CB  B ASN   A 20  ? 0.1656 0.2213 0.2496 0.0246  0.0324  0.0467  20  ASN   A CB  
389  C CG  A ASN   A 20  ? 0.2133 0.1772 0.2936 0.0300  0.0683  0.0250  20  ASN   A CG  
390  C CG  B ASN   A 20  ? 0.1692 0.2256 0.2510 0.0336  0.0338  0.0508  20  ASN   A CG  
391  O OD1 A ASN   A 20  ? 0.2349 0.1906 0.3278 0.0341  0.0816  0.0231  20  ASN   A OD1 
392  O OD1 B ASN   A 20  ? 0.1716 0.2185 0.2440 0.0400  0.0335  0.0520  20  ASN   A OD1 
393  N ND2 A ASN   A 20  ? 0.2233 0.1696 0.3069 0.0395  0.0611  0.0389  20  ASN   A ND2 
394  N ND2 B ASN   A 20  ? 0.1829 0.2300 0.2615 0.0240  0.0269  0.0610  20  ASN   A ND2 
407  N N   A ALA   A 21  ? 0.2050 0.1821 0.2639 -0.0056 0.0722  0.0254  21  ALA   A N   
408  N N   B ALA   A 21  ? 0.1958 0.2021 0.2778 0.0122  0.0677  0.0257  21  ALA   A N   
409  C CA  A ALA   A 21  ? 0.2033 0.1837 0.2570 -0.0067 0.0629  0.0359  21  ALA   A CA  
410  C CA  B ALA   A 21  ? 0.2014 0.1950 0.2829 0.0047  0.0682  0.0188  21  ALA   A CA  
411  C C   A ALA   A 21  ? 0.1954 0.1840 0.2495 -0.0008 0.0492  0.0258  21  ALA   A C   
412  C C   B ALA   A 21  ? 0.1941 0.1769 0.2708 0.0005  0.0878  0.0141  21  ALA   A C   
413  O O   A ALA   A 21  ? 0.1967 0.1913 0.2498 0.0031  0.0452  0.0266  21  ALA   A O   
414  O O   B ALA   A 21  ? 0.1913 0.1631 0.2869 0.0101  0.0964  0.0035  21  ALA   A O   
415  C CB  A ALA   A 21  ? 0.2080 0.1867 0.2525 -0.0085 0.0688  0.0438  21  ALA   A CB  
416  C CB  B ALA   A 21  ? 0.2099 0.2030 0.2987 0.0085  0.0527  0.0072  21  ALA   A CB  
427  N N   A ASP   A 22  ? 0.1895 0.1763 0.2580 -0.0040 0.0418  0.0232  22  ASP   A N   
428  N N   B ASP   A 22  ? 0.1931 0.1691 0.2586 -0.0078 0.0964  0.0195  22  ASP   A N   
429  C CA  A ASP   A 22  ? 0.1845 0.1718 0.2503 0.0073  0.0317  0.0392  22  ASP   A CA  
430  C CA  B ASP   A 22  ? 0.1986 0.1655 0.2546 -0.0065 0.0899  0.0219  22  ASP   A CA  
431  C C   A ASP   A 22  ? 0.1805 0.1774 0.2215 0.0060  0.0255  0.0343  22  ASP   A C   
432  C C   B ASP   A 22  ? 0.1792 0.1674 0.2270 -0.0196 0.0901  0.0178  22  ASP   A C   
433  O O   A ASP   A 22  ? 0.1888 0.1826 0.2407 -0.0037 0.0141  0.0392  22  ASP   A O   
434  O O   B ASP   A 22  ? 0.1730 0.1716 0.2411 -0.0280 0.0850  -0.0040 22  ASP   A O   
435  C CB  A ASP   A 22  ? 0.1966 0.1772 0.2836 0.0083  0.0363  0.0356  22  ASP   A CB  
436  C CB  B ASP   A 22  ? 0.2274 0.1697 0.2848 0.0069  0.0890  0.0154  22  ASP   A CB  
437  C CG  A ASP   A 22  ? 0.2090 0.1895 0.3263 0.0019  0.0163  0.0376  22  ASP   A CG  
438  C CG  B ASP   A 22  ? 0.2484 0.1759 0.3032 0.0159  0.0889  0.0139  22  ASP   A CG  
439  O OD1 A ASP   A 22  ? 0.1968 0.1824 0.3535 -0.0126 -0.0043 0.0446  22  ASP   A OD1 
440  O OD1 B ASP   A 22  ? 0.2547 0.1739 0.2847 0.0104  0.0867  0.0093  22  ASP   A OD1 
441  O OD2 A ASP   A 22  ? 0.2305 0.2067 0.3519 0.0190  0.0179  0.0150  22  ASP   A OD2 
442  O OD2 B ASP   A 22  ? 0.2636 0.1928 0.3305 0.0207  0.1011  0.0154  22  ASP   A OD2 
451  N N   A ILE   A 23  ? 0.1847 0.1798 0.2038 0.0096  0.0277  0.0276  23  ILE   A N   
452  N N   B ILE   A 23  ? 0.1779 0.1631 0.2148 -0.0122 0.0760  0.0283  23  ILE   A N   
453  C CA  A ILE   A 23  ? 0.1820 0.1774 0.2016 0.0046  0.0330  0.0286  23  ILE   A CA  
454  C CA  B ILE   A 23  ? 0.1712 0.1651 0.1910 -0.0170 0.0585  0.0334  23  ILE   A CA  
455  C C   A ILE   A 23  ? 0.1782 0.1874 0.2064 0.0017  0.0539  0.0280  23  ILE   A C   
456  C C   B ILE   A 23  ? 0.1748 0.1773 0.1892 -0.0323 0.0642  0.0221  23  ILE   A C   
457  O O   A ILE   A 23  ? 0.1835 0.2016 0.2126 -0.0003 0.0399  0.0100  23  ILE   A O   
458  O O   B ILE   A 23  ? 0.1814 0.1775 0.1852 -0.0335 0.0492  0.0144  23  ILE   A O   
459  C CB  A ILE   A 23  ? 0.1842 0.1713 0.1841 0.0099  0.0242  0.0204  23  ILE   A CB  
460  C CB  B ILE   A 23  ? 0.1627 0.1540 0.1745 -0.0081 0.0382  0.0293  23  ILE   A CB  
461  C CG1 A ILE   A 23  ? 0.1877 0.1680 0.1715 0.0030  0.0220  0.0219  23  ILE   A CG1 
462  C CG1 B ILE   A 23  ? 0.1678 0.1513 0.1672 -0.0076 0.0256  0.0187  23  ILE   A CG1 
463  C CG2 A ILE   A 23  ? 0.1812 0.1781 0.1908 0.0172  0.0281  0.0298  23  ILE   A CG2 
464  C CG2 B ILE   A 23  ? 0.1592 0.1504 0.1878 -0.0004 0.0327  0.0291  23  ILE   A CG2 
465  C CD1 A ILE   A 23  ? 0.1918 0.1688 0.1813 -0.0042 0.0107  0.0151  23  ILE   A CD1 
466  C CD1 B ILE   A 23  ? 0.1652 0.1515 0.1852 -0.0017 0.0098  0.0036  23  ILE   A CD1 
489  N N   A VAL   A 24  ? 0.1871 0.1927 0.2191 -0.0048 0.0457  0.0202  24  VAL   A N   
490  N N   B VAL   A 24  ? 0.1869 0.1891 0.2167 -0.0422 0.0541  0.0068  24  VAL   A N   
491  C CA  A VAL   A 24  ? 0.1964 0.2034 0.2367 -0.0189 0.0417  0.0068  24  VAL   A CA  
492  C CA  B VAL   A 24  ? 0.1986 0.1970 0.2390 -0.0512 0.0492  0.0055  24  VAL   A CA  
493  C C   A VAL   A 24  ? 0.2011 0.2199 0.2385 -0.0243 0.0322  0.0011  24  VAL   A C   
494  C C   B VAL   A 24  ? 0.2035 0.2166 0.2400 -0.0491 0.0536  -0.0096 24  VAL   A C   
495  O O   A VAL   A 24  ? 0.2115 0.2294 0.2371 -0.0229 0.0340  0.0037  24  VAL   A O   
496  O O   B VAL   A 24  ? 0.2160 0.2261 0.2515 -0.0409 0.0543  -0.0029 24  VAL   A O   
497  C CB  A VAL   A 24  ? 0.2035 0.2013 0.2485 -0.0240 0.0423  0.0016  24  VAL   A CB  
498  C CB  B VAL   A 24  ? 0.2070 0.1979 0.2563 -0.0554 0.0389  0.0171  24  VAL   A CB  
499  C CG1 A VAL   A 24  ? 0.2090 0.2080 0.2464 -0.0132 0.0513  -0.0127 24  VAL   A CG1 
500  C CG1 B VAL   A 24  ? 0.2220 0.2074 0.2774 -0.0488 0.0271  0.0207  24  VAL   A CG1 
501  C CG2 A VAL   A 24  ? 0.2168 0.2043 0.2634 -0.0301 0.0484  0.0192  24  VAL   A CG2 
502  C CG2 B VAL   A 24  ? 0.2085 0.1969 0.2475 -0.0627 0.0330  0.0115  24  VAL   A CG2 
521  N N   A GLU   A 25  ? 0.2061 0.2359 0.2345 -0.0245 0.0397  -0.0114 25  GLU   A N   
522  N N   B GLU   A 25  ? 0.2047 0.2381 0.2366 -0.0445 0.0727  -0.0209 25  GLU   A N   
523  C CA  A GLU   A 25  ? 0.2234 0.2597 0.2374 -0.0182 0.0436  -0.0174 25  GLU   A CA  
524  C CA  B GLU   A 25  ? 0.2190 0.2614 0.2415 -0.0406 0.0811  -0.0211 25  GLU   A CA  
525  C C   A GLU   A 25  ? 0.2119 0.2652 0.2031 -0.0302 0.0460  -0.0175 25  GLU   A C   
526  C C   B GLU   A 25  ? 0.2171 0.2710 0.2134 -0.0439 0.0852  -0.0241 25  GLU   A C   
527  O O   A GLU   A 25  ? 0.2138 0.2783 0.2071 -0.0317 0.0392  -0.0246 25  GLU   A O   
528  O O   B GLU   A 25  ? 0.2231 0.2775 0.2179 -0.0446 0.0902  -0.0253 25  GLU   A O   
529  C CB  A GLU   A 25  ? 0.2517 0.2845 0.2796 -0.0100 0.0406  -0.0133 25  GLU   A CB  
530  C CB  B GLU   A 25  ? 0.2379 0.2739 0.2800 -0.0368 0.0803  -0.0192 25  GLU   A CB  
531  C CG  A GLU   A 25  ? 0.2850 0.3098 0.3404 -0.0109 0.0238  -0.0182 25  GLU   A CG  
532  C CG  B GLU   A 25  ? 0.2675 0.2936 0.3368 -0.0345 0.0669  -0.0181 25  GLU   A CG  
533  C CD  A GLU   A 25  ? 0.3136 0.3346 0.3886 -0.0076 0.0067  -0.0208 25  GLU   A CD  
534  C CD  B GLU   A 25  ? 0.2912 0.3123 0.3940 -0.0325 0.0480  -0.0190 25  GLU   A CD  
535  O OE1 A GLU   A 25  ? 0.3276 0.3450 0.3997 -0.0020 -0.0017 -0.0289 25  GLU   A OE1 
536  O OE1 B GLU   A 25  ? 0.3023 0.3221 0.4223 -0.0297 0.0400  -0.0186 25  GLU   A OE1 
537  O OE2 A GLU   A 25  ? 0.3188 0.3442 0.4124 -0.0106 -0.0072 -0.0277 25  GLU   A OE2 
538  O OE2 B GLU   A 25  ? 0.3015 0.3178 0.4166 -0.0329 0.0411  -0.0210 25  GLU   A OE2 
551  N N   A GLU   A 26  ? 0.2015 0.2572 0.2081 -0.0509 0.0520  -0.0192 26  GLU   A N   
552  N N   B GLU   A 26  ? 0.2131 0.2718 0.2046 -0.0515 0.0846  -0.0243 26  GLU   A N   
553  C CA  A GLU   A 26  ? 0.2148 0.2559 0.2014 -0.0591 0.0556  -0.0023 26  GLU   A CA  
554  C CA  B GLU   A 26  ? 0.2191 0.2741 0.1998 -0.0563 0.0732  -0.0109 26  GLU   A CA  
555  C C   A GLU   A 26  ? 0.2172 0.2451 0.1832 -0.0537 0.0479  0.0065  26  GLU   A C   
556  C C   B GLU   A 26  ? 0.2178 0.2534 0.1833 -0.0547 0.0662  -0.0025 26  GLU   A C   
557  O O   A GLU   A 26  ? 0.2250 0.2376 0.1859 -0.0656 0.0374  0.0108  26  GLU   A O   
558  O O   B GLU   A 26  ? 0.2237 0.2487 0.1690 -0.0644 0.0771  -0.0077 26  GLU   A O   
559  C CB  A GLU   A 26  ? 0.2343 0.2657 0.2411 -0.0728 0.0515  0.0039  26  GLU   A CB  
560  C CB  B GLU   A 26  ? 0.2296 0.2939 0.2185 -0.0608 0.0465  -0.0149 26  GLU   A CB  
561  C CG  A GLU   A 26  ? 0.2561 0.2811 0.3087 -0.0818 0.0610  -0.0040 26  GLU   A CG  
562  C CG  B GLU   A 26  ? 0.2391 0.3110 0.2332 -0.0666 0.0398  -0.0204 26  GLU   A CG  
563  C CD  A GLU   A 26  ? 0.2681 0.2878 0.3374 -0.0915 0.0850  -0.0090 26  GLU   A CD  
564  C CD  B GLU   A 26  ? 0.2412 0.3209 0.2192 -0.0759 0.0402  -0.0228 26  GLU   A CD  
565  O OE1 A GLU   A 26  ? 0.2632 0.2991 0.3408 -0.0870 0.1148  -0.0470 26  GLU   A OE1 
566  O OE1 B GLU   A 26  ? 0.2452 0.3358 0.2034 -0.0737 0.0473  -0.0305 26  GLU   A OE1 
567  O OE2 A GLU   A 26  ? 0.2820 0.2934 0.3454 -0.0911 0.0821  0.0053  26  GLU   A OE2 
568  O OE2 B GLU   A 26  ? 0.2372 0.3168 0.1971 -0.0830 0.0387  -0.0256 26  GLU   A OE2 
581  N N   . ALA   A 27  ? 0.2021 0.2353 0.1828 -0.0521 0.0501  0.0095  27  ALA   A N   
582  C CA  . ALA   A 27  ? 0.2081 0.2417 0.1892 -0.0426 0.0415  0.0038  27  ALA   A CA  
583  C C   . ALA   A 27  ? 0.2373 0.2643 0.1903 -0.0532 0.0519  -0.0158 27  ALA   A C   
584  O O   . ALA   A 27  ? 0.2370 0.2530 0.1899 -0.0627 0.0424  -0.0137 27  ALA   A O   
585  C CB  . ALA   A 27  ? 0.1929 0.2279 0.1977 -0.0420 0.0348  0.0032  27  ALA   A CB  
592  N N   A LYS   A 28  ? 0.2652 0.2841 0.2072 -0.0560 0.0449  -0.0479 28  LYS   A N   
593  N N   B LYS   A 28  ? 0.2648 0.2837 0.2131 -0.0479 0.0399  -0.0360 28  LYS   A N   
594  C CA  A LYS   A 28  ? 0.3051 0.3197 0.2459 -0.0433 0.0479  -0.0647 28  LYS   A CA  
595  C CA  B LYS   A 28  ? 0.3001 0.3139 0.2520 -0.0323 0.0338  -0.0473 28  LYS   A CA  
596  C C   A LYS   A 28  ? 0.3286 0.3459 0.2381 -0.0499 0.0646  -0.0531 28  LYS   A C   
597  C C   B LYS   A 28  ? 0.3222 0.3351 0.2537 -0.0312 0.0392  -0.0391 28  LYS   A C   
598  O O   A LYS   A 28  ? 0.3410 0.3550 0.2769 -0.0474 0.0430  -0.0498 28  LYS   A O   
599  O O   B LYS   A 28  ? 0.3306 0.3409 0.2773 -0.0310 0.0271  -0.0379 28  LYS   A O   
600  C CB  A LYS   A 28  ? 0.3252 0.3357 0.3104 -0.0265 0.0362  -0.0724 28  LYS   A CB  
601  C CB  B LYS   A 28  ? 0.3169 0.3275 0.3023 -0.0207 0.0229  -0.0537 28  LYS   A CB  
602  C CG  A LYS   A 28  ? 0.3446 0.3501 0.3684 -0.0129 0.0307  -0.0726 28  LYS   A CG  
603  C CG  B LYS   A 28  ? 0.3339 0.3405 0.3515 -0.0111 0.0169  -0.0542 28  LYS   A CG  
604  C CD  A LYS   A 28  ? 0.3614 0.3683 0.4282 -0.0019 0.0215  -0.0703 28  LYS   A CD  
605  C CD  B LYS   A 28  ? 0.3505 0.3566 0.4062 -0.0027 0.0091  -0.0530 28  LYS   A CD  
606  C CE  A LYS   A 28  ? 0.3730 0.3811 0.4718 0.0042  0.0158  -0.0708 28  LYS   A CE  
607  C CE  B LYS   A 28  ? 0.3632 0.3677 0.4491 0.0008  0.0049  -0.0544 28  LYS   A CE  
608  N NZ  A LYS   A 28  ? 0.3822 0.3874 0.4991 0.0086  0.0149  -0.0744 28  LYS   A NZ  
609  N NZ  B LYS   A 28  ? 0.3713 0.3731 0.4735 0.0038  0.0020  -0.0585 28  LYS   A NZ  
636  N N   A LYS   A 29  ? 0.3374 0.3630 0.2173 -0.0618 0.1022  -0.0328 29  LYS   A N   
637  N N   B LYS   A 29  ? 0.3335 0.3501 0.2489 -0.0320 0.0571  -0.0244 29  LYS   A N   
638  C CA  A LYS   A 29  ? 0.3526 0.3841 0.2309 -0.0689 0.1214  -0.0174 29  LYS   A CA  
639  C CA  B LYS   A 29  ? 0.3483 0.3683 0.2622 -0.0320 0.0676  -0.0113 29  LYS   A CA  
640  C C   A LYS   A 29  ? 0.3560 0.3776 0.2098 -0.0825 0.1104  -0.0085 29  LYS   A C   
641  C C   B LYS   A 29  ? 0.3495 0.3633 0.2394 -0.0366 0.0612  -0.0026 29  LYS   A C   
642  O O   A LYS   A 29  ? 0.3701 0.3902 0.2337 -0.0765 0.0966  -0.0137 29  LYS   A O   
643  O O   B LYS   A 29  ? 0.3560 0.3715 0.2497 -0.0344 0.0591  -0.0049 29  LYS   A O   
644  C CB  A LYS   A 29  ? 0.3650 0.4113 0.2857 -0.0585 0.1395  -0.0136 29  LYS   A CB  
645  C CB  B LYS   A 29  ? 0.3618 0.3905 0.3099 -0.0250 0.0794  -0.0081 29  LYS   A CB  
646  C CG  A LYS   A 29  ? 0.3839 0.4362 0.3571 -0.0462 0.1361  -0.0126 29  LYS   A CG  
647  C CG  B LYS   A 29  ? 0.3779 0.4101 0.3654 -0.0169 0.0821  -0.0065 29  LYS   A CG  
648  C CD  A LYS   A 29  ? 0.3996 0.4557 0.4251 -0.0371 0.1302  -0.0135 29  LYS   A CD  
649  C CD  B LYS   A 29  ? 0.3905 0.4252 0.4203 -0.0105 0.0823  -0.0053 29  LYS   A CD  
650  C CE  A LYS   A 29  ? 0.4103 0.4686 0.4673 -0.0302 0.1284  -0.0152 29  LYS   A CE  
651  C CE  B LYS   A 29  ? 0.3989 0.4353 0.4565 -0.0061 0.0837  -0.0063 29  LYS   A CE  
652  N NZ  A LYS   A 29  ? 0.4146 0.4755 0.4948 -0.0254 0.1256  -0.0177 29  LYS   A NZ  
653  N NZ  B LYS   A 29  ? 0.4026 0.4404 0.4805 -0.0034 0.0823  -0.0067 29  LYS   A NZ  
680  N N   A VAL   A 30  ? 0.3434 0.3551 0.1904 -0.0998 0.1111  0.0013  30  VAL   A N   
681  N N   B VAL   A 30  ? 0.3433 0.3492 0.2240 -0.0437 0.0597  0.0079  30  VAL   A N   
682  C CA  A VAL   A 30  ? 0.3375 0.3362 0.1973 -0.1120 0.0838  0.0115  30  VAL   A CA  
683  C CA  B VAL   A 30  ? 0.3371 0.3358 0.2237 -0.0503 0.0417  0.0215  30  VAL   A CA  
684  C C   A VAL   A 30  ? 0.3368 0.3174 0.1620 -0.1110 0.0700  0.0248  30  VAL   A C   
685  C C   B VAL   A 30  ? 0.3347 0.3284 0.2072 -0.0506 0.0280  0.0237  30  VAL   A C   
686  O O   A VAL   A 30  ? 0.3451 0.3173 0.1701 -0.1067 0.0541  0.0323  30  VAL   A O   
687  O O   B VAL   A 30  ? 0.3389 0.3292 0.2023 -0.0498 0.0192  0.0298  30  VAL   A O   
688  C CB  A VAL   A 30  ? 0.3314 0.3302 0.2401 -0.1285 0.0728  0.0139  30  VAL   A CB  
689  C CB  B VAL   A 30  ? 0.3339 0.3270 0.2461 -0.0585 0.0370  0.0302  30  VAL   A CB  
690  C CG1 A VAL   A 30  ? 0.3362 0.3262 0.2598 -0.1313 0.0595  0.0150  30  VAL   A CG1 
691  C CG1 B VAL   A 30  ? 0.3366 0.3241 0.2595 -0.0592 0.0289  0.0315  30  VAL   A CG1 
692  C CG2 A VAL   A 30  ? 0.3262 0.3317 0.2569 -0.1373 0.0793  0.0131  30  VAL   A CG2 
693  C CG2 B VAL   A 30  ? 0.3317 0.3247 0.2550 -0.0633 0.0404  0.0352  30  VAL   A CG2 
712  N N   A LYS   A 31  ? 0.3256 0.2981 0.1423 -0.1147 0.0513  0.0163  31  LYS   A N   
713  N N   B LYS   A 31  ? 0.3282 0.3200 0.2114 -0.0515 0.0129  0.0168  31  LYS   A N   
714  C CA  A LYS   A 31  ? 0.3358 0.2991 0.1671 -0.0957 0.0188  0.0170  31  LYS   A CA  
715  C CA  B LYS   A 31  ? 0.3282 0.3187 0.2320 -0.0439 -0.0047 0.0138  31  LYS   A CA  
716  C C   A LYS   A 31  ? 0.3155 0.2809 0.1160 -0.0804 0.0032  0.0493  31  LYS   A C   
717  C C   B LYS   A 31  ? 0.3004 0.3022 0.1903 -0.0338 -0.0100 0.0341  31  LYS   A C   
718  O O   A LYS   A 31  ? 0.3205 0.2923 0.1333 -0.0727 -0.0168 0.0563  31  LYS   A O   
719  O O   B LYS   A 31  ? 0.3066 0.3094 0.2009 -0.0303 -0.0160 0.0364  31  LYS   A O   
720  C CB  A LYS   A 31  ? 0.3706 0.3257 0.2820 -0.0840 -0.0030 -0.0086 31  LYS   A CB  
721  C CB  B LYS   A 31  ? 0.3565 0.3377 0.3165 -0.0441 -0.0187 -0.0082 31  LYS   A CB  
722  C CG  A LYS   A 31  ? 0.4062 0.3499 0.4047 -0.0699 -0.0233 -0.0213 31  LYS   A CG  
723  C CG  B LYS   A 31  ? 0.3842 0.3568 0.4099 -0.0422 -0.0325 -0.0224 31  LYS   A CG  
724  C CD  A LYS   A 31  ? 0.4356 0.3711 0.4969 -0.0567 -0.0415 -0.0340 31  LYS   A CD  
725  C CD  B LYS   A 31  ? 0.4054 0.3721 0.4831 -0.0389 -0.0459 -0.0356 31  LYS   A CD  
726  C CE  A LYS   A 31  ? 0.4552 0.3873 0.5594 -0.0457 -0.0532 -0.0421 31  LYS   A CE  
727  C CE  B LYS   A 31  ? 0.4196 0.3847 0.5355 -0.0362 -0.0545 -0.0432 31  LYS   A CE  
728  N NZ  A LYS   A 31  ? 0.4650 0.3938 0.5924 -0.0386 -0.0606 -0.0468 31  LYS   A NZ  
729  N NZ  B LYS   A 31  ? 0.4282 0.3913 0.5645 -0.0341 -0.0585 -0.0489 31  LYS   A NZ  
756  N N   A PRO   A 32  ? 0.2870 0.2546 0.1087 -0.0827 0.0067  0.0328  32  PRO   A N   
757  N N   B PRO   A 32  ? 0.2665 0.2783 0.1613 -0.0305 -0.0089 0.0355  32  PRO   A N   
758  C CA  A PRO   A 32  ? 0.2788 0.2393 0.1449 -0.0751 -0.0081 0.0473  32  PRO   A CA  
759  C CA  B PRO   A 32  ? 0.2526 0.2640 0.1638 -0.0228 -0.0146 0.0486  32  PRO   A CA  
760  C C   A PRO   A 32  ? 0.2757 0.2313 0.1579 -0.0629 -0.0131 0.0490  32  PRO   A C   
761  C C   B PRO   A 32  ? 0.2458 0.2515 0.1633 -0.0147 -0.0229 0.0538  32  PRO   A C   
762  O O   A PRO   A 32  ? 0.2712 0.2240 0.1520 -0.0718 -0.0192 0.0353  32  PRO   A O   
763  O O   B PRO   A 32  ? 0.2412 0.2498 0.1719 -0.0119 -0.0346 0.0484  32  PRO   A O   
764  C CB  A PRO   A 32  ? 0.2709 0.2400 0.1547 -0.0837 -0.0068 0.0374  32  PRO   A CB  
765  C CB  B PRO   A 32  ? 0.2473 0.2674 0.1711 -0.0265 -0.0102 0.0368  32  PRO   A CB  
766  C CG  A PRO   A 32  ? 0.2720 0.2455 0.1148 -0.0802 -0.0174 0.0236  32  PRO   A CG  
767  C CG  B PRO   A 32  ? 0.2488 0.2717 0.1508 -0.0269 -0.0158 0.0288  32  PRO   A CG  
768  C CD  A PRO   A 32  ? 0.2764 0.2483 0.1047 -0.0820 -0.0047 0.0274  32  PRO   A CD  
769  C CD  B PRO   A 32  ? 0.2546 0.2751 0.1487 -0.0293 -0.0127 0.0314  32  PRO   A CD  
784  N N   A THR   A 33  ? 0.2788 0.2305 0.1526 -0.0477 -0.0171 0.0483  33  THR   A N   
785  N N   B THR   A 33  ? 0.2486 0.2421 0.1589 -0.0140 -0.0238 0.0562  33  THR   A N   
786  C CA  A THR   A 33  ? 0.2755 0.2338 0.1634 -0.0374 -0.0277 0.0457  33  THR   A CA  
787  C CA  B THR   A 33  ? 0.2480 0.2336 0.1627 -0.0160 -0.0316 0.0588  33  THR   A CA  
788  C C   A THR   A 33  ? 0.2429 0.2181 0.1517 -0.0354 -0.0265 0.0324  33  THR   A C   
789  C C   B THR   A 33  ? 0.2262 0.2132 0.1578 -0.0265 -0.0237 0.0403  33  THR   A C   
790  O O   A THR   A 33  ? 0.2380 0.2142 0.1615 -0.0322 -0.0385 0.0342  33  THR   A O   
791  O O   B THR   A 33  ? 0.2193 0.2011 0.1720 -0.0265 -0.0258 0.0402  33  THR   A O   
792  C CB  A THR   A 33  ? 0.3024 0.2564 0.1858 -0.0293 -0.0338 0.0582  33  THR   A CB  
793  C CB  B THR   A 33  ? 0.2706 0.2507 0.1764 -0.0101 -0.0363 0.0768  33  THR   A CB  
794  O OG1 A THR   A 33  ? 0.3214 0.2700 0.2061 -0.0185 -0.0287 0.0656  33  THR   A OG1 
795  O OG1 B THR   A 33  ? 0.2854 0.2635 0.1853 -0.0021 -0.0400 0.0905  33  THR   A OG1 
796  C CG2 A THR   A 33  ? 0.3087 0.2654 0.2025 -0.0248 -0.0451 0.0544  33  THR   A CG2 
797  C CG2 B THR   A 33  ? 0.2753 0.2561 0.1928 -0.0066 -0.0388 0.0706  33  THR   A CG2 
812  N N   . VAL   A 34  ? 0.2127 0.2062 0.1401 -0.0380 -0.0140 0.0319  34  VAL   A N   
813  C CA  . VAL   A 34  ? 0.1890 0.1854 0.1264 -0.0321 -0.0080 0.0285  34  VAL   A CA  
814  C C   . VAL   A 34  ? 0.1806 0.1703 0.1369 -0.0279 -0.0032 0.0259  34  VAL   A C   
815  O O   . VAL   A 34  ? 0.1868 0.1695 0.1642 -0.0372 0.0012  0.0334  34  VAL   A O   
816  C CB  . VAL   A 34  ? 0.1864 0.1862 0.1523 -0.0339 0.0053  0.0216  34  VAL   A CB  
817  C CG1 . VAL   A 34  ? 0.1880 0.1864 0.1633 -0.0284 0.0148  0.0071  34  VAL   A CG1 
818  C CG2 . VAL   A 34  ? 0.1951 0.2000 0.1799 -0.0230 0.0015  0.0161  34  VAL   A CG2 
829  N N   . VAL   A 35  ? 0.1609 0.1617 0.1413 -0.0281 -0.0090 0.0253  35  VAL   A N   
830  C CA  . VAL   A 35  ? 0.1516 0.1591 0.1412 -0.0283 0.0020  0.0219  35  VAL   A CA  
831  C C   . VAL   A 35  ? 0.1508 0.1480 0.1376 -0.0221 0.0118  0.0176  35  VAL   A C   
832  O O   . VAL   A 35  ? 0.1501 0.1619 0.1496 -0.0253 0.0155  0.0101  35  VAL   A O   
833  C CB  . VAL   A 35  ? 0.1655 0.1651 0.1427 -0.0131 0.0111  0.0103  35  VAL   A CB  
834  C CG1 . VAL   A 35  ? 0.1818 0.1758 0.1660 -0.0125 0.0058  0.0037  35  VAL   A CG1 
835  C CG2 . VAL   A 35  ? 0.1668 0.1658 0.1604 -0.0060 0.0214  0.0064  35  VAL   A CG2 
845  N N   . VAL   A 36  ? 0.1397 0.1417 0.1308 -0.0224 0.0102  0.0207  36  VAL   A N   
846  C CA  . VAL   A 36  ? 0.1337 0.1330 0.1291 -0.0174 0.0067  0.0177  36  VAL   A CA  
847  C C   . VAL   A 36  ? 0.1330 0.1338 0.1379 -0.0141 0.0129  0.0118  36  VAL   A C   
848  O O   . VAL   A 36  ? 0.1411 0.1369 0.1589 -0.0116 0.0238  0.0147  36  VAL   A O   
849  C CB  . VAL   A 36  ? 0.1312 0.1311 0.1398 -0.0186 0.0101  0.0219  36  VAL   A CB  
850  C CG1 . VAL   A 36  ? 0.1360 0.1356 0.1502 -0.0195 0.0100  0.0082  36  VAL   A CG1 
851  C CG2 . VAL   A 36  ? 0.1468 0.1414 0.1599 -0.0103 -0.0010 0.0205  36  VAL   A CG2 
861  N N   . ASN   A 37  ? 0.1294 0.1269 0.1319 -0.0127 0.0070  0.0117  37  ASN   A N   
862  C CA  . ASN   A 37  ? 0.1277 0.1241 0.1330 -0.0019 -0.0011 0.0193  37  ASN   A CA  
863  C C   . ASN   A 37  ? 0.1224 0.1283 0.1321 -0.0058 0.0093  0.0231  37  ASN   A C   
864  O O   . ASN   A 37  ? 0.1385 0.1423 0.1251 0.0025  0.0102  0.0092  37  ASN   A O   
865  C CB  . ASN   A 37  ? 0.1281 0.1287 0.1482 0.0049  -0.0026 0.0209  37  ASN   A CB  
866  C CG  . ASN   A 37  ? 0.1285 0.1297 0.1524 0.0023  0.0063  0.0191  37  ASN   A CG  
867  O OD1 . ASN   A 37  ? 0.1272 0.1306 0.1672 0.0023  0.0049  0.0136  37  ASN   A OD1 
868  N ND2 . ASN   A 37  ? 0.1373 0.1281 0.1551 0.0005  0.0042  0.0361  37  ASN   A ND2 
875  N N   A ALA   A 38  ? 0.1216 0.1374 0.1365 -0.0056 0.0132  0.0144  38  ALA   A N   
876  N N   B ALA   A 38  ? 0.1265 0.1358 0.1556 -0.0012 0.0054  0.0185  38  ALA   A N   
877  C CA  A ALA   A 38  ? 0.1304 0.1314 0.1099 -0.0043 0.0033  0.0048  38  ALA   A CA  
878  C CA  B ALA   A 38  ? 0.1351 0.1374 0.1647 -0.0023 -0.0033 0.0162  38  ALA   A CA  
879  C C   A ALA   A 38  ? 0.1305 0.1378 0.1246 0.0016  -0.0051 -0.0004 38  ALA   A C   
880  C C   B ALA   A 38  ? 0.1306 0.1360 0.1669 0.0031  -0.0044 0.0123  38  ALA   A C   
881  O O   A ALA   A 38  ? 0.1268 0.1290 0.1100 0.0014  -0.0039 -0.0057 38  ALA   A O   
882  O O   B ALA   A 38  ? 0.1195 0.1277 0.1954 -0.0024 -0.0129 0.0182  38  ALA   A O   
883  C CB  A ALA   A 38  ? 0.1369 0.1421 0.1143 -0.0165 -0.0106 0.0006  38  ALA   A CB  
884  C CB  B ALA   A 38  ? 0.1421 0.1472 0.1812 -0.0135 -0.0090 0.0169  38  ALA   A CB  
895  N N   A ALA   A 39  ? 0.1230 0.1286 0.1373 0.0073  -0.0001 0.0056  39  ALA   A N   
896  N N   B ALA   A 39  ? 0.1333 0.1381 0.1575 0.0066  0.0037  0.0227  39  ALA   A N   
897  C CA  A ALA   A 39  ? 0.1155 0.1247 0.1230 0.0045  0.0032  0.0140  39  ALA   A CA  
898  C CA  B ALA   A 39  ? 0.1370 0.1364 0.1423 0.0041  -0.0086 0.0213  39  ALA   A CA  
899  C C   A ALA   A 39  ? 0.1182 0.1289 0.1212 -0.0046 0.0009  0.0017  39  ALA   A C   
900  C C   B ALA   A 39  ? 0.1320 0.1301 0.1365 0.0020  -0.0118 0.0123  39  ALA   A C   
901  O O   A ALA   A 39  ? 0.1334 0.1355 0.1278 -0.0131 -0.0030 0.0124  39  ALA   A O   
902  O O   B ALA   A 39  ? 0.1479 0.1343 0.1353 0.0029  -0.0152 0.0020  39  ALA   A O   
903  C CB  A ALA   A 39  ? 0.1168 0.1350 0.1418 0.0100  -0.0050 0.0063  39  ALA   A CB  
904  C CB  B ALA   A 39  ? 0.1492 0.1489 0.1585 0.0081  -0.0190 0.0129  39  ALA   A CB  
915  N N   A ASN   A 40  ? 0.1269 0.1328 0.1393 -0.0117 0.0096  0.0029  40  ASN   A N   
916  N N   B ASN   A 40  ? 0.1340 0.1294 0.1290 -0.0057 0.0108  0.0231  40  ASN   A N   
917  C CA  A ASN   A 40  ? 0.1302 0.1294 0.1365 -0.0051 -0.0022 0.0015  40  ASN   A CA  
918  C CA  B ASN   A 40  ? 0.1348 0.1281 0.1378 0.0012  0.0070  0.0269  40  ASN   A CA  
919  C C   A ASN   A 40  ? 0.1287 0.1283 0.1274 -0.0095 0.0004  0.0099  40  ASN   A C   
920  C C   B ASN   A 40  ? 0.1307 0.1223 0.1219 -0.0056 0.0099  0.0274  40  ASN   A C   
921  O O   A ASN   A 40  ? 0.1229 0.1369 0.1247 -0.0068 0.0033  0.0088  40  ASN   A O   
922  O O   B ASN   A 40  ? 0.1250 0.1248 0.1421 -0.0082 -0.0009 0.0248  40  ASN   A O   
923  C CB  A ASN   A 40  ? 0.1429 0.1389 0.1534 0.0002  -0.0139 -0.0030 40  ASN   A CB  
924  C CB  B ASN   A 40  ? 0.1444 0.1386 0.1481 0.0032  0.0031  0.0191  40  ASN   A CB  
925  C CG  A ASN   A 40  ? 0.1628 0.1443 0.1814 -0.0024 -0.0092 -0.0026 40  ASN   A CG  
926  C CG  B ASN   A 40  ? 0.1540 0.1437 0.1432 0.0013  0.0093  0.0196  40  ASN   A CG  
927  O OD1 A ASN   A 40  ? 0.1726 0.1490 0.1575 -0.0017 -0.0135 0.0084  40  ASN   A OD1 
928  O OD1 B ASN   A 40  ? 0.1599 0.1469 0.1340 -0.0023 0.0182  0.0194  40  ASN   A OD1 
929  N ND2 A ASN   A 40  ? 0.1674 0.1501 0.2012 -0.0042 -0.0096 -0.0137 40  ASN   A ND2 
930  N ND2 B ASN   A 40  ? 0.1577 0.1510 0.1638 0.0008  0.0079  0.0043  40  ASN   A ND2 
943  N N   A VAL   A 41  ? 0.1321 0.1296 0.1312 0.0016  -0.0018 0.0174  41  VAL   A N   
944  N N   B VAL   A 41  ? 0.1347 0.1298 0.1118 -0.0015 0.0095  0.0234  41  VAL   A N   
945  C CA  A VAL   A 41  ? 0.1338 0.1401 0.1451 0.0027  0.0032  0.0162  41  VAL   A CA  
946  C CA  B VAL   A 41  ? 0.1455 0.1356 0.1263 0.0041  0.0137  0.0297  41  VAL   A CA  
947  C C   A VAL   A 41  ? 0.1350 0.1408 0.1456 0.0064  0.0097  0.0168  41  VAL   A C   
948  C C   B VAL   A 41  ? 0.1497 0.1360 0.1188 0.0017  0.0235  0.0172  41  VAL   A C   
949  O O   A VAL   A 41  ? 0.1423 0.1344 0.1404 0.0099  -0.0034 0.0079  41  VAL   A O   
950  O O   B VAL   A 41  ? 0.1604 0.1257 0.1027 0.0042  0.0184  0.0209  41  VAL   A O   
951  C CB  A VAL   A 41  ? 0.1383 0.1456 0.1344 -0.0006 0.0076  0.0043  41  VAL   A CB  
952  C CB  B VAL   A 41  ? 0.1539 0.1503 0.1503 0.0048  0.0142  0.0278  41  VAL   A CB  
953  C CG1 A VAL   A 41  ? 0.1529 0.1499 0.1513 0.0036  0.0072  -0.0045 41  VAL   A CG1 
954  C CG1 B VAL   A 41  ? 0.1729 0.1553 0.1633 0.0059  0.0226  0.0180  41  VAL   A CG1 
955  C CG2 A VAL   A 41  ? 0.1358 0.1511 0.1213 0.0030  0.0171  0.0074  41  VAL   A CG2 
956  C CG2 B VAL   A 41  ? 0.1584 0.1651 0.1627 0.0025  0.0076  0.0301  41  VAL   A CG2 
975  N N   A TYR   A 42  ? 0.1318 0.1334 0.1611 -0.0020 0.0179  0.0210  42  TYR   A N   
976  N N   B TYR   A 42  ? 0.1407 0.1307 0.1541 0.0029  0.0303  0.0291  42  TYR   A N   
977  C CA  A TYR   A 42  ? 0.1414 0.1262 0.1668 -0.0077 0.0168  0.0224  42  TYR   A CA  
978  C CA  B TYR   A 42  ? 0.1401 0.1278 0.1598 0.0038  0.0286  0.0376  42  TYR   A CA  
979  C C   A TYR   A 42  ? 0.1379 0.1219 0.1610 -0.0038 0.0209  0.0257  42  TYR   A C   
980  C C   B TYR   A 42  ? 0.1387 0.1238 0.1549 -0.0048 0.0301  0.0376  42  TYR   A C   
981  O O   A TYR   A 42  ? 0.1379 0.1281 0.1685 -0.0095 0.0096  0.0046  42  TYR   A O   
982  O O   B TYR   A 42  ? 0.1291 0.1234 0.1684 -0.0163 0.0285  0.0357  42  TYR   A O   
983  C CB  A TYR   A 42  ? 0.1533 0.1427 0.1705 -0.0127 0.0289  0.0258  42  TYR   A CB  
984  C CB  B TYR   A 42  ? 0.1530 0.1425 0.1728 0.0078  0.0285  0.0457  42  TYR   A CB  
985  C CG  A TYR   A 42  ? 0.1585 0.1552 0.1654 -0.0088 0.0284  0.0316  42  TYR   A CG  
986  C CG  B TYR   A 42  ? 0.1629 0.1522 0.1743 0.0131  0.0089  0.0527  42  TYR   A CG  
987  C CD1 A TYR   A 42  ? 0.1635 0.1646 0.1765 -0.0144 0.0209  0.0289  42  TYR   A CD1 
988  C CD1 B TYR   A 42  ? 0.1642 0.1534 0.1740 0.0009  0.0187  0.0526  42  TYR   A CD1 
989  C CD2 A TYR   A 42  ? 0.1661 0.1717 0.1739 -0.0002 0.0241  0.0264  42  TYR   A CD2 
990  C CD2 B TYR   A 42  ? 0.1719 0.1662 0.1869 0.0183  0.0008  0.0499  42  TYR   A CD2 
991  C CE1 A TYR   A 42  ? 0.1716 0.1739 0.1802 -0.0103 0.0223  0.0159  42  TYR   A CE1 
992  C CE1 B TYR   A 42  ? 0.1633 0.1589 0.1717 0.0022  0.0221  0.0465  42  TYR   A CE1 
993  C CE2 A TYR   A 42  ? 0.1734 0.1792 0.1891 -0.0100 0.0183  0.0194  42  TYR   A CE2 
994  C CE2 B TYR   A 42  ? 0.1758 0.1736 0.1887 0.0130  0.0042  0.0460  42  TYR   A CE2 
995  C CZ  A TYR   A 42  ? 0.1768 0.1811 0.1762 -0.0127 0.0264  0.0183  42  TYR   A CZ  
996  C CZ  B TYR   A 42  ? 0.1722 0.1722 0.1792 0.0027  0.0166  0.0404  42  TYR   A CZ  
997  O OH  A TYR   A 42  ? 0.1876 0.1969 0.1982 -0.0122 0.0148  0.0075  42  TYR   A OH  
998  O OH  B TYR   A 42  ? 0.1739 0.1871 0.1892 -0.0033 0.0078  0.0330  42  TYR   A OH  
1017 N N   . LEU   A 43  ? 0.1404 0.1266 0.1538 -0.0056 0.0207  0.0112  43  LEU   A N   
1018 C CA  . LEU   A 43  ? 0.1291 0.1301 0.1474 -0.0087 0.0169  0.0058  43  LEU   A CA  
1019 C C   . LEU   A 43  ? 0.1284 0.1339 0.1444 -0.0037 0.0096  0.0025  43  LEU   A C   
1020 O O   . LEU   A 43  ? 0.1482 0.1370 0.1769 0.0023  -0.0044 -0.0009 43  LEU   A O   
1021 C CB  . LEU   A 43  ? 0.1282 0.1328 0.1663 -0.0089 0.0115  0.0035  43  LEU   A CB  
1022 C CG  . LEU   A 43  ? 0.1393 0.1282 0.1762 -0.0053 0.0091  0.0083  43  LEU   A CG  
1023 C CD1 . LEU   A 43  ? 0.1473 0.1360 0.2042 0.0007  0.0072  0.0178  43  LEU   A CD1 
1024 C CD2 . LEU   A 43  ? 0.1621 0.1247 0.1760 0.0020  0.0093  0.0375  43  LEU   A CD2 
1037 N N   A LYS   A 44  ? 0.1370 0.1336 0.1479 -0.0029 0.0067  0.0101  44  LYS   A N   
1038 N N   B LYS   A 44  ? 0.1398 0.1361 0.1570 0.0016  0.0076  0.0068  44  LYS   A N   
1039 C CA  A LYS   A 44  ? 0.1521 0.1372 0.1515 -0.0041 0.0177  0.0151  44  LYS   A CA  
1040 C CA  B LYS   A 44  ? 0.1560 0.1409 0.1719 0.0044  0.0158  0.0106  44  LYS   A CA  
1041 C C   A LYS   A 44  ? 0.1395 0.1323 0.1434 0.0054  0.0031  0.0080  44  LYS   A C   
1042 C C   B LYS   A 44  ? 0.1406 0.1346 0.1572 0.0063  0.0042  0.0082  44  LYS   A C   
1043 O O   A LYS   A 44  ? 0.1519 0.1483 0.1637 0.0082  -0.0041 -0.0100 44  LYS   A O   
1044 O O   B LYS   A 44  ? 0.1460 0.1451 0.1713 0.0051  -0.0004 -0.0035 44  LYS   A O   
1045 C CB  A LYS   A 44  ? 0.1824 0.1602 0.1811 -0.0131 0.0229  0.0254  44  LYS   A CB  
1046 C CB  B LYS   A 44  ? 0.1884 0.1618 0.2170 0.0053  0.0216  0.0159  44  LYS   A CB  
1047 C CG  A LYS   A 44  ? 0.2106 0.1875 0.2363 -0.0212 0.0365  0.0306  44  LYS   A CG  
1048 C CG  B LYS   A 44  ? 0.2177 0.1913 0.2828 0.0052  0.0286  0.0288  44  LYS   A CG  
1049 C CD  A LYS   A 44  ? 0.2519 0.2325 0.3216 -0.0121 0.0264  0.0288  44  LYS   A CD  
1050 C CD  B LYS   A 44  ? 0.2469 0.2221 0.3532 0.0061  0.0192  0.0347  44  LYS   A CD  
1051 C CE  A LYS   A 44  ? 0.2726 0.2595 0.3712 -0.0111 0.0245  0.0288  44  LYS   A CE  
1052 C CE  B LYS   A 44  ? 0.2635 0.2437 0.4036 0.0044  0.0127  0.0409  44  LYS   A CE  
1053 N NZ  A LYS   A 44  ? 0.2785 0.2730 0.3872 -0.0112 0.0210  0.0373  44  LYS   A NZ  
1054 N NZ  B LYS   A 44  ? 0.2721 0.2533 0.4261 -0.0002 0.0107  0.0461  44  LYS   A NZ  
1081 N N   . HIS   A 45  ? 0.1313 0.1284 0.1558 0.0005  0.0008  0.0169  45  HIS   A N   
1082 C CA  . HIS   A 45  ? 0.1326 0.1270 0.1662 -0.0036 -0.0006 0.0137  45  HIS   A CA  
1083 C C   . HIS   A 45  ? 0.1397 0.1402 0.1757 0.0062  -0.0009 0.0072  45  HIS   A C   
1084 O O   . HIS   A 45  ? 0.1707 0.1651 0.2080 0.0274  -0.0024 -0.0097 45  HIS   A O   
1085 C CB  . HIS   A 45  ? 0.1342 0.1317 0.1629 -0.0044 0.0045  0.0068  45  HIS   A CB  
1086 C CG  . HIS   A 45  ? 0.1269 0.1261 0.1540 -0.0106 0.0074  0.0077  45  HIS   A CG  
1087 N ND1 . HIS   A 45  ? 0.1244 0.1323 0.1608 -0.0045 -0.0002 0.0162  45  HIS   A ND1 
1088 C CD2 . HIS   A 45  ? 0.1271 0.1265 0.1631 -0.0078 0.0012  0.0170  45  HIS   A CD2 
1089 C CE1 . HIS   A 45  ? 0.1260 0.1353 0.1448 -0.0111 -0.0056 0.0147  45  HIS   A CE1 
1090 N NE2 . HIS   A 45  ? 0.1247 0.1346 0.1570 -0.0064 0.0023  0.0203  45  HIS   A NE2 
1099 N N   A GLY   A 46  ? 0.1414 0.1467 0.1943 0.0096  -0.0140 0.0215  46  GLY   A N   
1100 N N   B GLY   A 46  ? 0.1470 0.1382 0.1715 0.0090  -0.0088 0.0052  46  GLY   A N   
1101 C CA  A GLY   A 46  ? 0.1484 0.1594 0.2087 0.0151  -0.0092 0.0370  46  GLY   A CA  
1102 C CA  B GLY   A 46  ? 0.1478 0.1480 0.1673 0.0098  0.0017  0.0065  46  GLY   A CA  
1103 C C   A GLY   A 46  ? 0.1518 0.1572 0.1988 0.0234  -0.0148 0.0531  46  GLY   A C   
1104 C C   B GLY   A 46  ? 0.1459 0.1487 0.1487 0.0119  0.0086  0.0135  46  GLY   A C   
1105 O O   A GLY   A 46  ? 0.1537 0.1592 0.1974 0.0236  -0.0263 0.0592  46  GLY   A O   
1106 O O   B GLY   A 46  ? 0.1526 0.1623 0.1507 0.0085  -0.0043 0.0033  46  GLY   A O   
1113 N N   A GLY   A 47  ? 0.1524 0.1600 0.1931 0.0175  -0.0130 0.0394  47  GLY   A N   
1114 N N   B GLY   A 47  ? 0.1541 0.1527 0.1617 0.0098  0.0101  0.0017  47  GLY   A N   
1115 C CA  A GLY   A 47  ? 0.1567 0.1647 0.1679 0.0219  -0.0163 0.0415  47  GLY   A CA  
1116 C CA  B GLY   A 47  ? 0.1476 0.1582 0.1593 0.0023  0.0010  0.0102  47  GLY   A CA  
1117 C C   A GLY   A 47  ? 0.1433 0.1601 0.1514 0.0204  -0.0140 0.0307  47  GLY   A C   
1118 C C   B GLY   A 47  ? 0.1357 0.1467 0.1405 0.0077  0.0032  0.0043  47  GLY   A C   
1119 O O   A GLY   A 47  ? 0.1393 0.1467 0.1793 0.0154  -0.0151 0.0309  47  GLY   A O   
1120 O O   B GLY   A 47  ? 0.1299 0.1403 0.1323 0.0096  -0.0023 0.0194  47  GLY   A O   
1127 N N   A GLY   A 48  ? 0.1410 0.1629 0.1376 0.0244  -0.0127 0.0203  48  GLY   A N   
1128 N N   B GLY   A 48  ? 0.1317 0.1439 0.1418 0.0039  0.0019  -0.0009 48  GLY   A N   
1129 C CA  A GLY   A 48  ? 0.1398 0.1576 0.1355 0.0118  -0.0052 0.0022  48  GLY   A CA  
1130 C CA  B GLY   A 48  ? 0.1316 0.1304 0.1383 -0.0040 -0.0016 -0.0027 48  GLY   A CA  
1131 C C   A GLY   A 48  ? 0.1394 0.1498 0.1340 0.0045  0.0013  0.0099  48  GLY   A C   
1132 C C   B GLY   A 48  ? 0.1332 0.1268 0.1382 -0.0027 0.0010  0.0020  48  GLY   A C   
1133 O O   A GLY   A 48  ? 0.1583 0.1487 0.1280 0.0049  0.0021  0.0167  48  GLY   A O   
1134 O O   B GLY   A 48  ? 0.1418 0.1287 0.1263 0.0005  0.0141  -0.0068 48  GLY   A O   
1141 N N   A VAL   A 49  ? 0.1347 0.1460 0.1557 0.0043  -0.0104 0.0096  49  VAL   A N   
1142 N N   B VAL   A 49  ? 0.1224 0.1229 0.1562 -0.0069 -0.0098 -0.0068 49  VAL   A N   
1143 C CA  A VAL   A 49  ? 0.1411 0.1388 0.1688 -0.0000 -0.0034 0.0107  49  VAL   A CA  
1144 C CA  B VAL   A 49  ? 0.1222 0.1264 0.1516 -0.0101 -0.0041 -0.0018 49  VAL   A CA  
1145 C C   A VAL   A 49  ? 0.1308 0.1300 0.1428 -0.0044 -0.0020 0.0201  49  VAL   A C   
1146 C C   B VAL   A 49  ? 0.1223 0.1228 0.1316 -0.0063 0.0094  -0.0197 49  VAL   A C   
1147 O O   A VAL   A 49  ? 0.1303 0.1383 0.1440 -0.0041 -0.0175 0.0162  49  VAL   A O   
1148 O O   B VAL   A 49  ? 0.1270 0.1266 0.1349 0.0031  0.0276  -0.0059 49  VAL   A O   
1149 C CB  A VAL   A 49  ? 0.1399 0.1347 0.1960 -0.0010 -0.0079 0.0131  49  VAL   A CB  
1150 C CB  B VAL   A 49  ? 0.1165 0.1222 0.1616 -0.0033 -0.0068 0.0056  49  VAL   A CB  
1151 C CG1 A VAL   A 49  ? 0.1497 0.1299 0.2106 -0.0062 -0.0120 0.0150  49  VAL   A CG1 
1152 C CG1 B VAL   A 49  ? 0.1111 0.1205 0.1557 0.0129  0.0016  0.0094  49  VAL   A CG1 
1153 C CG2 A VAL   A 49  ? 0.1427 0.1455 0.2371 -0.0175 -0.0092 0.0157  49  VAL   A CG2 
1154 C CG2 B VAL   A 49  ? 0.1221 0.1221 0.1830 0.0018  -0.0084 0.0116  49  VAL   A CG2 
1173 N N   A ALA   A 50  ? 0.1268 0.1305 0.1382 -0.0049 -0.0139 0.0264  50  ALA   A N   
1174 N N   B ALA   A 50  ? 0.1263 0.1277 0.1257 -0.0014 0.0004  -0.0241 50  ALA   A N   
1175 C CA  A ALA   A 50  ? 0.1205 0.1221 0.1539 -0.0162 -0.0181 0.0280  50  ALA   A CA  
1176 C CA  B ALA   A 50  ? 0.1237 0.1261 0.1251 -0.0021 0.0059  -0.0286 50  ALA   A CA  
1177 C C   A ALA   A 50  ? 0.1127 0.1251 0.1512 -0.0150 -0.0130 0.0240  50  ALA   A C   
1178 C C   B ALA   A 50  ? 0.1276 0.1277 0.1066 -0.0023 0.0084  -0.0246 50  ALA   A C   
1179 O O   A ALA   A 50  ? 0.1172 0.1268 0.1653 -0.0057 -0.0090 0.0149  50  ALA   A O   
1180 O O   B ALA   A 50  ? 0.1334 0.1343 0.1073 0.0005  0.0162  -0.0219 50  ALA   A O   
1181 C CB  A ALA   A 50  ? 0.1269 0.1264 0.1673 -0.0111 -0.0129 0.0276  50  ALA   A CB  
1182 C CB  B ALA   A 50  ? 0.1259 0.1277 0.1269 0.0026  0.0203  -0.0358 50  ALA   A CB  
1193 N N   A GLY   A 51  ? 0.1220 0.1293 0.1617 -0.0030 -0.0136 0.0168  51  GLY   A N   
1194 N N   B GLY   A 51  ? 0.1353 0.1263 0.1282 0.0048  -0.0034 -0.0258 51  GLY   A N   
1195 C CA  A GLY   A 51  ? 0.1344 0.1289 0.1834 -0.0026 -0.0104 0.0153  51  GLY   A CA  
1196 C CA  B GLY   A 51  ? 0.1408 0.1219 0.1368 0.0033  -0.0173 -0.0226 51  GLY   A CA  
1197 C C   A GLY   A 51  ? 0.1254 0.1328 0.1845 -0.0008 0.0013  -0.0045 51  GLY   A C   
1198 C C   B GLY   A 51  ? 0.1356 0.1229 0.1372 0.0051  -0.0174 -0.0249 51  GLY   A C   
1199 O O   A GLY   A 51  ? 0.1285 0.1431 0.1914 -0.0040 0.0017  -0.0003 51  GLY   A O   
1200 O O   B GLY   A 51  ? 0.1391 0.1251 0.1446 0.0032  -0.0184 -0.0257 51  GLY   A O   
1207 N N   A ALA   A 52  ? 0.1271 0.1446 0.1874 -0.0042 0.0037  -0.0084 52  ALA   A N   
1208 N N   B ALA   A 52  ? 0.1340 0.1330 0.1270 0.0055  -0.0105 -0.0287 52  ALA   A N   
1209 C CA  A ALA   A 52  ? 0.1296 0.1546 0.1989 -0.0110 0.0020  -0.0104 52  ALA   A CA  
1210 C CA  B ALA   A 52  ? 0.1294 0.1402 0.1433 0.0025  -0.0034 -0.0210 52  ALA   A CA  
1211 C C   A ALA   A 52  ? 0.1285 0.1528 0.1850 -0.0131 0.0150  -0.0020 52  ALA   A C   
1212 C C   B ALA   A 52  ? 0.1314 0.1367 0.1373 -0.0061 0.0042  -0.0187 52  ALA   A C   
1213 O O   A ALA   A 52  ? 0.1323 0.1630 0.1941 -0.0110 0.0139  -0.0039 52  ALA   A O   
1214 O O   B ALA   A 52  ? 0.1381 0.1419 0.1482 -0.0087 0.0078  -0.0254 52  ALA   A O   
1215 C CB  A ALA   A 52  ? 0.1391 0.1690 0.2213 -0.0112 -0.0119 -0.0183 52  ALA   A CB  
1216 C CB  B ALA   A 52  ? 0.1320 0.1576 0.1537 0.0087  -0.0038 -0.0134 52  ALA   A CB  
1227 N N   A LEU   A 53  ? 0.1225 0.1487 0.1704 -0.0090 0.0069  -0.0008 53  LEU   A N   
1228 N N   B LEU   A 53  ? 0.1288 0.1347 0.1412 -0.0051 -0.0126 -0.0144 53  LEU   A N   
1229 C CA  A LEU   A 53  ? 0.1385 0.1497 0.1472 -0.0083 0.0080  0.0034  53  LEU   A CA  
1230 C CA  B LEU   A 53  ? 0.1395 0.1373 0.1382 -0.0054 -0.0099 -0.0080 53  LEU   A CA  
1231 C C   A LEU   A 53  ? 0.1362 0.1487 0.1169 -0.0050 0.0124  -0.0004 53  LEU   A C   
1232 C C   B LEU   A 53  ? 0.1373 0.1393 0.1202 -0.0017 -0.0071 0.0010  53  LEU   A C   
1233 O O   A LEU   A 53  ? 0.1391 0.1632 0.1398 -0.0160 0.0188  -0.0051 53  LEU   A O   
1234 O O   B LEU   A 53  ? 0.1430 0.1421 0.1303 -0.0018 -0.0101 0.0012  53  LEU   A O   
1235 C CB  A LEU   A 53  ? 0.1385 0.1539 0.1438 -0.0101 0.0091  0.0112  53  LEU   A CB  
1236 C CB  B LEU   A 53  ? 0.1392 0.1406 0.1493 -0.0077 -0.0037 -0.0117 53  LEU   A CB  
1237 C CG  A LEU   A 53  ? 0.1396 0.1526 0.1629 -0.0122 0.0049  0.0247  53  LEU   A CG  
1238 C CG  B LEU   A 53  ? 0.1349 0.1380 0.1528 -0.0121 -0.0079 -0.0176 53  LEU   A CG  
1239 C CD1 A LEU   A 53  ? 0.1371 0.1642 0.1483 -0.0040 0.0016  0.0319  53  LEU   A CD1 
1240 C CD1 B LEU   A 53  ? 0.1359 0.1405 0.1639 -0.0125 -0.0090 -0.0145 53  LEU   A CD1 
1241 C CD2 A LEU   A 53  ? 0.1368 0.1654 0.1801 -0.0203 -0.0072 0.0248  53  LEU   A CD2 
1242 C CD2 B LEU   A 53  ? 0.1301 0.1449 0.1556 -0.0165 -0.0028 -0.0117 53  LEU   A CD2 
1265 N N   . ASN   A 54  ? 0.1275 0.1360 0.1232 -0.0065 -0.0004 0.0076  54  ASN   A N   
1266 C CA  . ASN   A 54  ? 0.1212 0.1320 0.1404 -0.0064 0.0054  -0.0001 54  ASN   A CA  
1267 C C   . ASN   A 54  ? 0.1352 0.1369 0.1342 -0.0080 0.0031  -0.0073 54  ASN   A C   
1268 O O   . ASN   A 54  ? 0.1379 0.1486 0.1519 -0.0087 -0.0029 -0.0114 54  ASN   A O   
1269 C CB  . ASN   A 54  ? 0.1203 0.1361 0.1444 -0.0099 -0.0055 0.0011  54  ASN   A CB  
1270 C CG  . ASN   A 54  ? 0.1247 0.1433 0.1435 -0.0033 -0.0075 -0.0046 54  ASN   A CG  
1271 O OD1 . ASN   A 54  ? 0.1222 0.1425 0.1488 -0.0036 -0.0069 -0.0033 54  ASN   A OD1 
1272 N ND2 . ASN   A 54  ? 0.1377 0.1482 0.1659 -0.0143 -0.0170 0.0145  54  ASN   A ND2 
1280 N N   . LYS   A 55  ? 0.1335 0.1370 0.1591 -0.0023 -0.0011 -0.0097 55  LYS   A N   
1281 C CA  . LYS   A 55  ? 0.1453 0.1504 0.1650 0.0050  -0.0069 -0.0209 55  LYS   A CA  
1282 C C   . LYS   A 55  ? 0.1403 0.1560 0.1652 -0.0073 -0.0020 -0.0252 55  LYS   A C   
1283 O O   . LYS   A 55  ? 0.1496 0.1669 0.1711 -0.0025 0.0045  -0.0270 55  LYS   A O   
1284 C CB  . LYS   A 55  ? 0.1543 0.1628 0.1776 0.0211  -0.0076 -0.0276 55  LYS   A CB  
1285 C CG  . LYS   A 55  ? 0.1738 0.2003 0.2127 0.0401  -0.0246 -0.0347 55  LYS   A CG  
1286 C CD  . LYS   A 55  ? 0.1921 0.2353 0.2247 0.0573  -0.0185 -0.0327 55  LYS   A CD  
1287 C CE  . LYS   A 55  ? 0.2162 0.2727 0.2511 0.0658  -0.0223 -0.0333 55  LYS   A CE  
1288 N NZ  . LYS   A 55  ? 0.2251 0.2894 0.2495 0.0743  -0.0303 -0.0268 55  LYS   A NZ  
1302 N N   . ALA   A 56  ? 0.1475 0.1646 0.1704 -0.0140 0.0056  -0.0226 56  ALA   A N   
1303 C CA  . ALA   A 56  ? 0.1606 0.1862 0.1625 -0.0161 0.0150  -0.0211 56  ALA   A CA  
1304 C C   . ALA   A 56  ? 0.1620 0.1944 0.1264 -0.0092 0.0117  -0.0325 56  ALA   A C   
1305 O O   . ALA   A 56  ? 0.1646 0.2244 0.1473 -0.0022 0.0223  -0.0200 56  ALA   A O   
1306 C CB  . ALA   A 56  ? 0.1616 0.2087 0.1762 -0.0273 0.0154  -0.0084 56  ALA   A CB  
1312 N N   . THR   A 57  ? 0.1506 0.1777 0.1265 -0.0131 0.0137  -0.0206 57  THR   A N   
1313 C CA  . THR   A 57  ? 0.1477 0.1738 0.1324 -0.0186 0.0013  -0.0056 57  THR   A CA  
1314 C C   . THR   A 57  ? 0.1479 0.1796 0.1468 -0.0123 -0.0008 -0.0131 57  THR   A C   
1315 O O   . THR   A 57  ? 0.1449 0.1890 0.1755 -0.0146 -0.0105 -0.0264 57  THR   A O   
1316 C CB  . THR   A 57  ? 0.1485 0.1735 0.1378 -0.0122 0.0055  -0.0097 57  THR   A CB  
1317 O OG1 . THR   A 57  ? 0.1375 0.1638 0.1438 -0.0159 0.0075  -0.0164 57  THR   A OG1 
1318 C CG2 . THR   A 57  ? 0.1553 0.1657 0.1405 -0.0090 0.0054  0.0084  57  THR   A CG2 
1326 N N   . ASN   A 58  ? 0.1456 0.1694 0.1773 -0.0109 0.0134  -0.0315 58  ASN   A N   
1327 C CA  . ASN   A 58  ? 0.1720 0.1656 0.1916 -0.0157 0.0159  -0.0436 58  ASN   A CA  
1328 C C   . ASN   A 58  ? 0.1552 0.1524 0.1734 -0.0031 0.0050  -0.0281 58  ASN   A C   
1329 O O   . ASN   A 58  ? 0.1579 0.1637 0.1985 -0.0184 -0.0009 -0.0299 58  ASN   A O   
1330 C CB  . ASN   A 58  ? 0.2189 0.1794 0.2367 -0.0315 0.0489  -0.0537 58  ASN   A CB  
1331 C CG  . ASN   A 58  ? 0.2735 0.2070 0.3205 -0.0294 0.0550  -0.0353 58  ASN   A CG  
1332 O OD1 . ASN   A 58  ? 0.3007 0.2014 0.3674 0.0086  0.0873  -0.0268 58  ASN   A OD1 
1333 N ND2 . ASN   A 58  ? 0.2885 0.2189 0.3500 -0.0338 0.0403  -0.0389 58  ASN   A ND2 
1340 N N   . ASN   A 59  ? 0.1338 0.1448 0.1600 -0.0091 -0.0025 -0.0140 59  ASN   A N   
1341 C CA  . ASN   A 59  ? 0.1374 0.1345 0.1585 -0.0052 -0.0018 -0.0122 59  ASN   A CA  
1342 C C   . ASN   A 59  ? 0.1428 0.1387 0.1392 -0.0032 -0.0008 -0.0079 59  ASN   A C   
1343 O O   . ASN   A 59  ? 0.1405 0.1442 0.1382 -0.0090 0.0047  -0.0040 59  ASN   A O   
1344 C CB  . ASN   A 59  ? 0.1399 0.1388 0.1740 -0.0019 -0.0129 -0.0198 59  ASN   A CB  
1345 C CG  . ASN   A 59  ? 0.1436 0.1406 0.1758 -0.0062 -0.0266 0.0051  59  ASN   A CG  
1346 O OD1 . ASN   A 59  ? 0.1581 0.1442 0.1720 -0.0150 -0.0242 0.0069  59  ASN   A OD1 
1347 N ND2 . ASN   A 59  ? 0.1541 0.1485 0.1861 -0.0156 -0.0106 0.0057  59  ASN   A ND2 
1354 N N   . ALA   A 60  ? 0.1285 0.1460 0.1545 -0.0074 -0.0008 -0.0027 60  ALA   A N   
1355 C CA  . ALA   A 60  ? 0.1357 0.1439 0.1579 -0.0054 -0.0119 -0.0022 60  ALA   A CA  
1356 C C   . ALA   A 60  ? 0.1359 0.1426 0.1627 -0.0079 -0.0048 -0.0050 60  ALA   A C   
1357 O O   . ALA   A 60  ? 0.1253 0.1431 0.1826 -0.0076 -0.0080 -0.0160 60  ALA   A O   
1358 C CB  . ALA   A 60  ? 0.1476 0.1549 0.1636 -0.0058 -0.0185 -0.0197 60  ALA   A CB  
1364 N N   . MET   A 61  ? 0.1316 0.1348 0.1584 -0.0119 0.0022  -0.0102 61  MET   A N   
1365 C CA  . MET   A 61  ? 0.1280 0.1293 0.1644 -0.0100 0.0077  0.0054  61  MET   A CA  
1366 C C   . MET   A 61  ? 0.1231 0.1270 0.1630 -0.0105 -0.0087 0.0042  61  MET   A C   
1367 O O   . MET   A 61  ? 0.1259 0.1332 0.1678 -0.0040 0.0079  0.0070  61  MET   A O   
1368 C CB  . MET   A 61  ? 0.1408 0.1331 0.1546 -0.0137 0.0041  -0.0018 61  MET   A CB  
1369 C CG  . MET   A 61  ? 0.1378 0.1435 0.1656 -0.0093 0.0037  -0.0024 61  MET   A CG  
1370 S SD  . MET   A 61  ? 0.1387 0.1446 0.1934 -0.0129 0.0006  -0.0190 61  MET   A SD  
1371 C CE  . MET   A 61  ? 0.1615 0.1532 0.2183 -0.0161 0.0207  -0.0141 61  MET   A CE  
1381 N N   . GLN   A 62  ? 0.1279 0.1271 0.1678 -0.0110 0.0034  -0.0025 62  GLN   A N   
1382 C CA  . GLN   A 62  ? 0.1286 0.1258 0.1664 -0.0074 0.0030  0.0076  62  GLN   A CA  
1383 C C   . GLN   A 62  ? 0.1305 0.1121 0.1730 -0.0050 0.0084  -0.0001 62  GLN   A C   
1384 O O   . GLN   A 62  ? 0.1319 0.1288 0.1726 -0.0049 0.0045  -0.0069 62  GLN   A O   
1385 C CB  . GLN   A 62  ? 0.1247 0.1246 0.1780 -0.0124 0.0069  -0.0009 62  GLN   A CB  
1386 C CG  . GLN   A 62  ? 0.1301 0.1247 0.1745 -0.0078 0.0025  0.0128  62  GLN   A CG  
1387 C CD  . GLN   A 62  ? 0.1415 0.1277 0.1708 -0.0029 0.0034  0.0022  62  GLN   A CD  
1388 O OE1 . GLN   A 62  ? 0.1478 0.1389 0.1732 -0.0030 -0.0003 0.0007  62  GLN   A OE1 
1389 N NE2 . GLN   A 62  ? 0.1481 0.1351 0.1835 -0.0011 -0.0007 -0.0044 62  GLN   A NE2 
1398 N N   . VAL   A 63  ? 0.1241 0.1269 0.1851 -0.0058 0.0108  -0.0148 63  VAL   A N   
1399 C CA  . VAL   A 63  ? 0.1265 0.1365 0.1968 -0.0159 0.0055  -0.0229 63  VAL   A CA  
1400 C C   . VAL   A 63  ? 0.1182 0.1390 0.1812 -0.0171 -0.0041 -0.0138 63  VAL   A C   
1401 O O   . VAL   A 63  ? 0.1210 0.1362 0.2166 -0.0181 0.0015  -0.0101 63  VAL   A O   
1402 C CB  . VAL   A 63  ? 0.1424 0.1513 0.2405 -0.0131 0.0060  -0.0370 63  VAL   A CB  
1403 C CG1 . VAL   A 63  ? 0.1535 0.1737 0.2644 -0.0177 -0.0080 -0.0721 63  VAL   A CG1 
1404 C CG2 . VAL   A 63  ? 0.1546 0.1503 0.2439 -0.0099 0.0064  -0.0392 63  VAL   A CG2 
1414 N N   . GLU   A 64  ? 0.1223 0.1461 0.1777 -0.0069 -0.0007 -0.0049 64  GLU   A N   
1415 C CA  . GLU   A 64  ? 0.1259 0.1426 0.1927 -0.0076 -0.0153 0.0011  64  GLU   A CA  
1416 C C   . GLU   A 64  ? 0.1191 0.1342 0.1934 -0.0041 -0.0025 0.0123  64  GLU   A C   
1417 O O   . GLU   A 64  ? 0.1259 0.1394 0.1943 0.0006  0.0040  -0.0020 64  GLU   A O   
1418 C CB  . GLU   A 64  ? 0.1292 0.1565 0.1956 -0.0120 -0.0046 0.0060  64  GLU   A CB  
1419 C CG  . GLU   A 64  ? 0.1428 0.1575 0.2125 -0.0092 -0.0046 -0.0008 64  GLU   A CG  
1420 C CD  . GLU   A 64  ? 0.1518 0.1670 0.2116 -0.0150 0.0051  -0.0048 64  GLU   A CD  
1421 O OE1 . GLU   A 64  ? 0.1513 0.1763 0.2231 -0.0203 0.0115  0.0030  64  GLU   A OE1 
1422 O OE2 . GLU   A 64  ? 0.1734 0.1706 0.1993 -0.0258 -0.0114 0.0025  64  GLU   A OE2 
1429 N N   . SER   A 65  ? 0.1166 0.1318 0.1772 0.0000  0.0051  0.0067  65  SER   A N   
1430 C CA  . SER   A 65  ? 0.1327 0.1308 0.1613 -0.0044 0.0109  -0.0034 65  SER   A CA  
1431 C C   . SER   A 65  ? 0.1304 0.1412 0.1552 -0.0120 0.0083  -0.0000 65  SER   A C   
1432 O O   . SER   A 65  ? 0.1371 0.1460 0.1829 -0.0077 0.0251  -0.0129 65  SER   A O   
1433 C CB  . SER   A 65  ? 0.1299 0.1316 0.1767 -0.0063 0.0052  0.0101  65  SER   A CB  
1434 O OG  . SER   A 65  ? 0.1263 0.1408 0.1767 -0.0109 0.0031  0.0117  65  SER   A OG  
1440 N N   . ASP   A 66  ? 0.1268 0.1366 0.1733 -0.0084 0.0165  0.0053  66  ASP   A N   
1441 C CA  . ASP   A 66  ? 0.1370 0.1513 0.1953 -0.0036 0.0187  0.0157  66  ASP   A CA  
1442 C C   . ASP   A 66  ? 0.1361 0.1496 0.1867 -0.0104 0.0168  0.0136  66  ASP   A C   
1443 O O   . ASP   A 66  ? 0.1437 0.1561 0.1968 -0.0110 0.0266  0.0250  66  ASP   A O   
1444 C CB  . ASP   A 66  ? 0.1489 0.1630 0.2606 0.0055  0.0264  0.0470  66  ASP   A CB  
1445 C CG  . ASP   A 66  ? 0.1864 0.1797 0.2995 -0.0121 0.0101  0.0832  66  ASP   A CG  
1446 O OD1 . ASP   A 66  ? 0.1765 0.2259 0.2830 -0.0184 0.0087  0.0896  66  ASP   A OD1 
1447 O OD2 . ASP   A 66  ? 0.2072 0.1976 0.3783 0.0073  -0.0119 0.0471  66  ASP   A OD2 
1452 N N   . ASP   A 67  ? 0.1288 0.1453 0.1978 -0.0003 0.0106  0.0072  67  ASP   A N   
1453 C CA  . ASP   A 67  ? 0.1315 0.1578 0.2170 -0.0006 0.0063  0.0112  67  ASP   A CA  
1454 C C   . ASP   A 67  ? 0.1333 0.1561 0.2202 -0.0021 0.0247  0.0144  67  ASP   A C   
1455 O O   . ASP   A 67  ? 0.1308 0.1627 0.2523 -0.0007 0.0304  0.0264  67  ASP   A O   
1456 C CB  . ASP   A 67  ? 0.1410 0.1606 0.2444 -0.0041 -0.0092 0.0240  67  ASP   A CB  
1457 C CG  . ASP   A 67  ? 0.1359 0.1734 0.2766 -0.0142 -0.0144 0.0470  67  ASP   A CG  
1458 O OD1 . ASP   A 67  ? 0.1450 0.1868 0.3564 -0.0202 -0.0310 0.0522  67  ASP   A OD1 
1459 O OD2 . ASP   A 67  ? 0.1417 0.1823 0.2796 -0.0007 -0.0132 0.0393  67  ASP   A OD2 
1464 N N   . TYR   A 68  ? 0.1370 0.1449 0.2229 0.0036  0.0261  0.0233  68  TYR   A N   
1465 C CA  . TYR   A 68  ? 0.1428 0.1379 0.2244 -0.0019 0.0329  0.0189  68  TYR   A CA  
1466 C C   . TYR   A 68  ? 0.1363 0.1340 0.2243 -0.0025 0.0373  0.0050  68  TYR   A C   
1467 O O   . TYR   A 68  ? 0.1420 0.1362 0.2326 0.0018  0.0328  -0.0004 68  TYR   A O   
1468 C CB  . TYR   A 68  ? 0.1450 0.1354 0.2148 0.0035  0.0392  0.0141  68  TYR   A CB  
1469 C CG  . TYR   A 68  ? 0.1461 0.1508 0.2404 -0.0013 0.0413  0.0200  68  TYR   A CG  
1470 C CD1 . TYR   A 68  ? 0.1595 0.1612 0.2637 -0.0195 0.0418  -0.0076 68  TYR   A CD1 
1471 C CD2 . TYR   A 68  ? 0.1716 0.1540 0.2847 0.0056  0.0468  0.0238  68  TYR   A CD2 
1472 C CE1 . TYR   A 68  ? 0.1709 0.1707 0.2915 -0.0203 0.0481  -0.0163 68  TYR   A CE1 
1473 C CE2 . TYR   A 68  ? 0.1722 0.1580 0.2975 -0.0044 0.0637  0.0079  68  TYR   A CE2 
1474 C CZ  . TYR   A 68  ? 0.1729 0.1629 0.3138 -0.0225 0.0400  -0.0163 68  TYR   A CZ  
1475 O OH  . TYR   A 68  ? 0.1953 0.1678 0.3354 -0.0160 0.0258  -0.0371 68  TYR   A OH  
1485 N N   . ILE   A 69  ? 0.1311 0.1306 0.2150 -0.0037 0.0361  0.0138  69  ILE   A N   
1486 C CA  . ILE   A 69  ? 0.1401 0.1424 0.2115 0.0036  0.0303  0.0024  69  ILE   A CA  
1487 C C   . ILE   A 69  ? 0.1457 0.1410 0.2149 -0.0010 0.0397  -0.0047 69  ILE   A C   
1488 O O   . ILE   A 69  ? 0.1562 0.1487 0.2205 -0.0072 0.0454  -0.0020 69  ILE   A O   
1489 C CB  . ILE   A 69  ? 0.1503 0.1637 0.2054 0.0037  0.0317  0.0054  69  ILE   A CB  
1490 C CG1 . ILE   A 69  ? 0.1479 0.1632 0.2075 0.0041  0.0274  -0.0082 69  ILE   A CG1 
1491 C CG2 . ILE   A 69  ? 0.1762 0.1910 0.2246 0.0103  0.0277  0.0048  69  ILE   A CG2 
1492 C CD1 . ILE   A 69  ? 0.1463 0.1748 0.2091 -0.0050 0.0210  -0.0213 69  ILE   A CD1 
1504 N N   A ALA   A 70  ? 0.1582 0.1477 0.2389 -0.0084 0.0462  0.0078  70  ALA   A N   
1505 N N   B ALA   A 70  ? 0.1504 0.1420 0.2297 -0.0187 0.0395  -0.0150 70  ALA   A N   
1506 C CA  A ALA   A 70  ? 0.1633 0.1582 0.2692 -0.0199 0.0640  0.0128  70  ALA   A CA  
1507 C CA  B ALA   A 70  ? 0.1442 0.1513 0.2500 -0.0346 0.0401  -0.0215 70  ALA   A CA  
1508 C C   A ALA   A 70  ? 0.1611 0.1705 0.2661 -0.0200 0.0678  0.0091  70  ALA   A C   
1509 C C   B ALA   A 70  ? 0.1371 0.1672 0.2596 -0.0338 0.0302  -0.0375 70  ALA   A C   
1510 O O   A ALA   A 70  ? 0.1721 0.1935 0.2591 -0.0107 0.0790  0.0117  70  ALA   A O   
1511 O O   B ALA   A 70  ? 0.1463 0.1881 0.2692 -0.0262 0.0335  -0.0399 70  ALA   A O   
1512 C CB  A ALA   A 70  ? 0.1767 0.1612 0.2884 -0.0178 0.0634  0.0047  70  ALA   A CB  
1513 C CB  B ALA   A 70  ? 0.1557 0.1534 0.2606 -0.0378 0.0396  -0.0285 70  ALA   A CB  
1524 N N   A THR   A 71  ? 0.1566 0.1698 0.2659 -0.0069 0.0577  0.0144  71  THR   A N   
1525 N N   B THR   A 71  ? 0.1339 0.1724 0.2714 -0.0223 0.0280  -0.0340 71  THR   A N   
1526 C CA  A THR   A 71  ? 0.1656 0.1854 0.2876 0.0027  0.0454  0.0138  71  THR   A CA  
1527 C CA  B THR   A 71  ? 0.1402 0.1811 0.2963 -0.0116 0.0213  -0.0231 71  THR   A CA  
1528 C C   A THR   A 71  ? 0.1552 0.1766 0.2907 0.0042  0.0544  0.0133  71  THR   A C   
1529 C C   B THR   A 71  ? 0.1369 0.1687 0.2938 0.0030  0.0276  -0.0158 71  THR   A C   
1530 O O   A THR   A 71  ? 0.1652 0.1878 0.2939 0.0049  0.0609  0.0200  71  THR   A O   
1531 O O   B THR   A 71  ? 0.1279 0.1587 0.2971 0.0072  0.0228  -0.0201 71  THR   A O   
1532 C CB  A THR   A 71  ? 0.1939 0.2099 0.3133 0.0130  0.0150  0.0175  71  THR   A CB  
1533 C CB  B THR   A 71  ? 0.1675 0.2035 0.3299 -0.0108 -0.0008 -0.0172 71  THR   A CB  
1534 O OG1 A THR   A 71  ? 0.2204 0.2239 0.3360 0.0099  0.0056  0.0137  71  THR   A OG1 
1535 O OG1 B THR   A 71  ? 0.1861 0.2155 0.3491 -0.0149 -0.0133 -0.0201 71  THR   A OG1 
1536 C CG2 A THR   A 71  ? 0.2046 0.2234 0.3154 0.0162  -0.0037 0.0283  71  THR   A CG2 
1537 C CG2 B THR   A 71  ? 0.1766 0.2153 0.3368 -0.0116 -0.0111 -0.0084 71  THR   A CG2 
1552 N N   . ASN   A 72  ? 0.1497 0.1632 0.2838 -0.0008 0.0440  0.0057  72  ASN   A N   
1553 C CA  . ASN   A 72  ? 0.1493 0.1573 0.2888 0.0071  0.0456  0.0016  72  ASN   A CA  
1554 C C   . ASN   A 72  ? 0.1653 0.1679 0.2750 0.0027  0.0545  -0.0069 72  ASN   A C   
1555 O O   . ASN   A 72  ? 0.1826 0.1624 0.2863 0.0022  0.0537  -0.0162 72  ASN   A O   
1556 C CB  . ASN   A 72  ? 0.1683 0.1679 0.2887 0.0107  0.0461  0.0101  72  ASN   A CB  
1557 C CG  . ASN   A 72  ? 0.1923 0.1824 0.2953 0.0136  0.0442  0.0175  72  ASN   A CG  
1558 O OD1 . ASN   A 72  ? 0.2109 0.2199 0.3152 0.0184  0.0421  0.0157  72  ASN   A OD1 
1559 N ND2 . ASN   A 72  ? 0.2128 0.1796 0.3003 0.0431  0.0284  0.0169  72  ASN   A ND2 
1567 N N   . GLY   A 73  ? 0.1697 0.1646 0.2458 -0.0029 0.0626  -0.0018 73  GLY   A N   
1568 C CA  . GLY   A 73  ? 0.1748 0.1560 0.2387 -0.0098 0.0541  0.0082  73  GLY   A CA  
1569 C C   . GLY   A 73  ? 0.1705 0.1485 0.2184 -0.0018 0.0675  0.0150  73  GLY   A C   
1570 O O   . GLY   A 73  ? 0.1703 0.1505 0.2346 0.0066  0.0524  0.0200  73  GLY   A O   
1574 N N   . PRO   A 74  ? 0.1839 0.1545 0.2167 -0.0173 0.0626  0.0057  74  PRO   A N   
1575 C CA  . PRO   A 74  ? 0.1800 0.1524 0.2266 -0.0117 0.0470  0.0116  74  PRO   A CA  
1576 C C   . PRO   A 74  ? 0.1676 0.1370 0.2157 -0.0071 0.0427  0.0059  74  PRO   A C   
1577 O O   . PRO   A 74  ? 0.1731 0.1411 0.2457 -0.0014 0.0537  -0.0065 74  PRO   A O   
1578 C CB  . PRO   A 74  ? 0.1938 0.1722 0.2470 -0.0027 0.0567  0.0224  74  PRO   A CB  
1579 C CG  . PRO   A 74  ? 0.2227 0.2118 0.2849 -0.0254 0.0477  0.0071  74  PRO   A CG  
1580 C CD  . PRO   A 74  ? 0.1999 0.1839 0.2255 -0.0268 0.0540  -0.0088 74  PRO   A CD  
1588 N N   . LEU   A 75  ? 0.1666 0.1295 0.1955 -0.0025 0.0337  0.0015  75  LEU   A N   
1589 C CA  . LEU   A 75  ? 0.1580 0.1273 0.1799 0.0010  0.0122  0.0092  75  LEU   A CA  
1590 C C   . LEU   A 75  ? 0.1727 0.1366 0.1702 -0.0032 0.0138  0.0159  75  LEU   A C   
1591 O O   . LEU   A 75  ? 0.2054 0.1572 0.1722 0.0097  0.0103  0.0148  75  LEU   A O   
1592 C CB  . LEU   A 75  ? 0.1611 0.1302 0.1798 -0.0071 0.0099  0.0182  75  LEU   A CB  
1593 C CG  . LEU   A 75  ? 0.1844 0.1588 0.1843 -0.0330 0.0084  0.0091  75  LEU   A CG  
1594 C CD1 . LEU   A 75  ? 0.1972 0.2037 0.1968 -0.0422 0.0058  -0.0139 75  LEU   A CD1 
1595 C CD2 . LEU   A 75  ? 0.2136 0.1985 0.2400 -0.0144 0.0123  0.0110  75  LEU   A CD2 
1607 N N   . LYS   A 76  ? 0.1815 0.1386 0.1803 -0.0077 0.0083  -0.0015 76  LYS   A N   
1608 C CA  . LYS   A 76  ? 0.1807 0.1613 0.1806 -0.0090 0.0095  -0.0038 76  LYS   A CA  
1609 C C   . LYS   A 76  ? 0.1757 0.1489 0.1433 -0.0045 0.0094  0.0059  76  LYS   A C   
1610 O O   . LYS   A 76  ? 0.1785 0.1376 0.1566 -0.0039 0.0155  0.0139  76  LYS   A O   
1611 C CB  . LYS   A 76  ? 0.1779 0.1890 0.2150 0.0003  0.0207  -0.0343 76  LYS   A CB  
1612 C CG  . LYS   A 76  ? 0.1837 0.1842 0.2551 0.0048  0.0149  -0.0294 76  LYS   A CG  
1613 C CD  . LYS   A 76  ? 0.1937 0.1854 0.2995 0.0079  -0.0020 -0.0330 76  LYS   A CD  
1614 C CE  . LYS   A 76  ? 0.2118 0.2033 0.3602 0.0023  0.0094  -0.0489 76  LYS   A CE  
1615 N NZ  . LYS   A 76  ? 0.2138 0.1941 0.4059 -0.0172 0.0071  -0.0644 76  LYS   A NZ  
1629 N N   . VAL   A 77  ? 0.1888 0.1543 0.1471 -0.0056 0.0198  0.0201  77  VAL   A N   
1630 C CA  . VAL   A 77  ? 0.1824 0.1597 0.1546 0.0005  0.0131  0.0136  77  VAL   A CA  
1631 C C   . VAL   A 77  ? 0.1715 0.1513 0.1475 0.0049  0.0172  0.0080  77  VAL   A C   
1632 O O   . VAL   A 77  ? 0.1774 0.1578 0.1612 0.0063  0.0296  0.0010  77  VAL   A O   
1633 C CB  . VAL   A 77  ? 0.1988 0.1755 0.1623 -0.0055 0.0051  0.0285  77  VAL   A CB  
1634 C CG1 . VAL   A 77  ? 0.1994 0.1994 0.1759 0.0012  -0.0071 0.0122  77  VAL   A CG1 
1635 C CG2 . VAL   A 77  ? 0.2248 0.1853 0.1986 -0.0051 -0.0053 0.0313  77  VAL   A CG2 
1645 N N   . GLY   A 78  ? 0.1640 0.1420 0.1502 -0.0019 0.0192  0.0080  78  GLY   A N   
1646 C CA  . GLY   A 78  ? 0.1621 0.1422 0.1640 -0.0000 0.0232  0.0078  78  GLY   A CA  
1647 C C   . GLY   A 78  ? 0.1537 0.1332 0.1538 0.0040  0.0211  0.0128  78  GLY   A C   
1648 O O   . GLY   A 78  ? 0.1529 0.1454 0.1851 -0.0027 0.0145  0.0224  78  GLY   A O   
1652 N N   . GLY   A 79  ? 0.1573 0.1262 0.1527 0.0012  0.0185  0.0143  79  GLY   A N   
1653 C CA  . GLY   A 79  ? 0.1565 0.1399 0.1551 0.0006  0.0212  0.0103  79  GLY   A CA  
1654 C C   . GLY   A 79  ? 0.1406 0.1325 0.1496 -0.0045 0.0161  0.0096  79  GLY   A C   
1655 O O   . GLY   A 79  ? 0.1409 0.1451 0.1812 0.0140  0.0113  0.0044  79  GLY   A O   
1659 N N   . SER   A 80  ? 0.1374 0.1472 0.1744 -0.0027 0.0085  -0.0038 80  SER   A N   
1660 C CA  . SER   A 80  ? 0.1267 0.1360 0.1565 -0.0011 0.0077  0.0082  80  SER   A CA  
1661 C C   . SER   A 80  ? 0.1329 0.1349 0.1557 -0.0046 0.0109  0.0105  80  SER   A C   
1662 O O   . SER   A 80  ? 0.1314 0.1630 0.2073 0.0106  0.0073  -0.0066 80  SER   A O   
1663 C CB  . SER   A 80  ? 0.1460 0.1393 0.1919 0.0005  0.0101  0.0092  80  SER   A CB  
1664 O OG  . SER   A 80  ? 0.1707 0.1452 0.2417 -0.0036 -0.0029 0.0259  80  SER   A OG  
1670 N N   . CYS   A 81  ? 0.1283 0.1318 0.1630 -0.0016 -0.0020 0.0118  81  CYS   A N   
1671 C CA  . CYS   A 81  ? 0.1286 0.1471 0.1610 -0.0094 -0.0035 0.0239  81  CYS   A CA  
1672 C C   . CYS   A 81  ? 0.1339 0.1466 0.1368 -0.0095 -0.0050 0.0271  81  CYS   A C   
1673 O O   . CYS   A 81  ? 0.1260 0.1740 0.1758 0.0022  0.0031  0.0356  81  CYS   A O   
1674 C CB  . CYS   A 81  ? 0.1328 0.1481 0.1788 -0.0124 -0.0041 0.0218  81  CYS   A CB  
1675 S SG  . CYS   A 81  ? 0.1482 0.1418 0.1805 -0.0166 0.0012  0.0142  81  CYS   A SG  
1681 N N   . VAL   A 82  ? 0.1351 0.1449 0.1452 0.0004  -0.0170 0.0236  82  VAL   A N   
1682 C CA  . VAL   A 82  ? 0.1504 0.1543 0.1557 -0.0034 -0.0125 0.0332  82  VAL   A CA  
1683 C C   . VAL   A 82  ? 0.1435 0.1601 0.1653 -0.0090 -0.0081 0.0269  82  VAL   A C   
1684 O O   . VAL   A 82  ? 0.1364 0.1616 0.2016 -0.0043 -0.0080 0.0026  82  VAL   A O   
1685 C CB  . VAL   A 82  ? 0.1807 0.1736 0.1784 -0.0025 -0.0053 0.0323  82  VAL   A CB  
1686 C CG1 . VAL   A 82  ? 0.1988 0.1861 0.2005 -0.0042 -0.0035 0.0235  82  VAL   A CG1 
1687 C CG2 . VAL   A 82  ? 0.1771 0.1789 0.2109 -0.0141 -0.0121 0.0194  82  VAL   A CG2 
1697 N N   . LEU   A 83  ? 0.1336 0.1618 0.1660 -0.0182 -0.0074 0.0122  83  LEU   A N   
1698 C CA  . LEU   A 83  ? 0.1353 0.1581 0.1565 -0.0120 -0.0111 0.0163  83  LEU   A CA  
1699 C C   . LEU   A 83  ? 0.1385 0.1600 0.1592 -0.0143 -0.0115 0.0137  83  LEU   A C   
1700 O O   . LEU   A 83  ? 0.1498 0.1596 0.1781 -0.0218 -0.0113 0.0232  83  LEU   A O   
1701 C CB  . LEU   A 83  ? 0.1481 0.1711 0.1651 -0.0175 -0.0066 0.0176  83  LEU   A CB  
1702 C CG  . LEU   A 83  ? 0.1547 0.1715 0.1759 -0.0178 0.0011  0.0081  83  LEU   A CG  
1703 C CD1 . LEU   A 83  ? 0.1690 0.1749 0.1750 -0.0222 0.0006  0.0251  83  LEU   A CD1 
1704 C CD2 . LEU   A 83  ? 0.1570 0.1848 0.1993 -0.0089 0.0122  0.0159  83  LEU   A CD2 
1716 N N   . SER   A 84  ? 0.1571 0.1654 0.1674 -0.0219 -0.0113 0.0118  84  SER   A N   
1717 C CA  . SER   A 84  ? 0.1683 0.1693 0.1493 -0.0145 -0.0145 0.0095  84  SER   A CA  
1718 C C   . SER   A 84  ? 0.1737 0.1655 0.1313 -0.0240 -0.0028 0.0139  84  SER   A C   
1719 O O   . SER   A 84  ? 0.1695 0.1774 0.1373 -0.0162 -0.0099 0.0085  84  SER   A O   
1720 C CB  . SER   A 84  ? 0.1790 0.1842 0.1591 -0.0099 -0.0175 -0.0086 84  SER   A CB  
1721 O OG  . SER   A 84  ? 0.1875 0.2010 0.1776 -0.0107 -0.0211 -0.0159 84  SER   A OG  
1727 N N   . GLY   A 85  ? 0.1884 0.1798 0.1466 -0.0208 0.0122  0.0112  85  GLY   A N   
1728 C CA  . GLY   A 85  ? 0.1919 0.1834 0.1668 -0.0201 0.0073  -0.0057 85  GLY   A CA  
1729 C C   . GLY   A 85  ? 0.1869 0.1883 0.1537 -0.0196 -0.0076 -0.0017 85  GLY   A C   
1730 O O   . GLY   A 85  ? 0.1848 0.2001 0.1724 -0.0264 0.0064  -0.0199 85  GLY   A O   
1734 N N   . HIS   A 86  ? 0.1891 0.1876 0.1407 -0.0212 -0.0110 0.0013  86  HIS   A N   
1735 C CA  . HIS   A 86  ? 0.2058 0.1973 0.1281 -0.0264 -0.0074 0.0018  86  HIS   A CA  
1736 C C   . HIS   A 86  ? 0.2303 0.2055 0.1325 -0.0311 -0.0031 -0.0017 86  HIS   A C   
1737 O O   . HIS   A 86  ? 0.2460 0.2270 0.1521 -0.0249 0.0079  -0.0057 86  HIS   A O   
1738 C CB  . HIS   A 86  ? 0.2042 0.1862 0.1367 -0.0196 -0.0017 0.0053  86  HIS   A CB  
1739 C CG  . HIS   A 86  ? 0.1961 0.1822 0.1613 -0.0116 0.0001  0.0115  86  HIS   A CG  
1740 N ND1 . HIS   A 86  ? 0.2076 0.1800 0.1979 -0.0206 -0.0005 0.0096  86  HIS   A ND1 
1741 C CD2 . HIS   A 86  ? 0.1914 0.1807 0.1557 -0.0032 -0.0007 0.0124  86  HIS   A CD2 
1742 C CE1 . HIS   A 86  ? 0.1971 0.1805 0.1996 -0.0123 0.0183  0.0180  86  HIS   A CE1 
1743 N NE2 . HIS   A 86  ? 0.1920 0.1821 0.1729 0.0002  0.0125  0.0265  86  HIS   A NE2 
1751 N N   . ASN   A 87  ? 0.2417 0.2138 0.1583 -0.0176 0.0189  -0.0145 87  ASN   A N   
1752 C CA  . ASN   A 87  ? 0.2632 0.2278 0.1562 -0.0127 0.0423  -0.0170 87  ASN   A CA  
1753 C C   . ASN   A 87  ? 0.2589 0.2430 0.1933 -0.0263 0.0590  -0.0004 87  ASN   A C   
1754 O O   . ASN   A 87  ? 0.2866 0.2694 0.2363 -0.0400 0.0928  -0.0129 87  ASN   A O   
1755 C CB  . ASN   A 87  ? 0.2858 0.2366 0.1798 -0.0008 0.0404  -0.0174 87  ASN   A CB  
1756 C CG  . ASN   A 87  ? 0.3010 0.2498 0.1804 0.0063  0.0494  -0.0028 87  ASN   A CG  
1757 O OD1 . ASN   A 87  ? 0.3193 0.2494 0.1714 0.0205  0.0456  0.0129  87  ASN   A OD1 
1758 N ND2 . ASN   A 87  ? 0.3087 0.2766 0.1931 0.0054  0.0494  -0.0012 87  ASN   A ND2 
1765 N N   A LEU   A 88  ? 0.2385 0.2304 0.1864 -0.0308 0.0398  0.0056  88  LEU   A N   
1766 N N   B LEU   A 88  ? 0.2405 0.2334 0.1895 -0.0294 0.0460  0.0022  88  LEU   A N   
1767 C CA  A LEU   A 88  ? 0.2195 0.2290 0.1918 -0.0330 0.0377  0.0214  88  LEU   A CA  
1768 C CA  B LEU   A 88  ? 0.2228 0.2309 0.1924 -0.0307 0.0455  0.0132  88  LEU   A CA  
1769 C C   A LEU   A 88  ? 0.2107 0.2308 0.1895 -0.0307 0.0338  0.0248  88  LEU   A C   
1770 C C   B LEU   A 88  ? 0.2123 0.2307 0.1874 -0.0286 0.0406  0.0275  88  LEU   A C   
1771 O O   A LEU   A 88  ? 0.2107 0.2351 0.2163 -0.0253 0.0364  0.0366  88  LEU   A O   
1772 O O   B LEU   A 88  ? 0.2104 0.2331 0.2051 -0.0223 0.0492  0.0531  88  LEU   A O   
1773 C CB  A LEU   A 88  ? 0.2189 0.2345 0.2005 -0.0393 0.0086  0.0321  88  LEU   A CB  
1774 C CB  B LEU   A 88  ? 0.2224 0.2346 0.2005 -0.0351 0.0278  0.0086  88  LEU   A CB  
1775 C CG  A LEU   A 88  ? 0.2316 0.2464 0.2373 -0.0361 -0.0034 0.0399  88  LEU   A CG  
1776 C CG  B LEU   A 88  ? 0.2279 0.2405 0.2209 -0.0311 0.0244  0.0011  88  LEU   A CG  
1777 C CD1 A LEU   A 88  ? 0.2373 0.2533 0.2388 -0.0348 -0.0163 0.0363  88  LEU   A CD1 
1778 C CD1 B LEU   A 88  ? 0.2307 0.2427 0.2174 -0.0289 0.0173  -0.0106 88  LEU   A CD1 
1779 C CD2 A LEU   A 88  ? 0.2425 0.2552 0.2736 -0.0282 -0.0057 0.0331  88  LEU   A CD2 
1780 C CD2 B LEU   A 88  ? 0.2340 0.2468 0.2419 -0.0250 0.0226  -0.0050 88  LEU   A CD2 
1803 N N   . ALA   A 89  ? 0.2084 0.2260 0.1644 -0.0272 0.0296  0.0131  89  ALA   A N   
1804 C CA  . ALA   A 89  ? 0.2142 0.2296 0.1463 -0.0169 0.0097  0.0220  89  ALA   A CA  
1805 C C   . ALA   A 89  ? 0.2225 0.2294 0.1515 -0.0129 -0.0032 0.0209  89  ALA   A C   
1806 O O   . ALA   A 89  ? 0.2184 0.2236 0.2030 -0.0272 -0.0082 -0.0068 89  ALA   A O   
1807 C CB  . ALA   A 89  ? 0.1976 0.2280 0.1401 -0.0257 0.0059  0.0246  89  ALA   A CB  
1814 N N   . LYS   A 90  ? 0.2291 0.2398 0.1397 -0.0267 -0.0174 0.0225  90  LYS   A N   
1815 C CA  . LYS   A 90  ? 0.2399 0.2552 0.1589 -0.0167 -0.0291 0.0252  90  LYS   A CA  
1816 C C   . LYS   A 90  ? 0.2119 0.2343 0.1543 -0.0245 -0.0298 0.0072  90  LYS   A C   
1817 O O   . LYS   A 90  ? 0.2112 0.2436 0.2060 -0.0277 -0.0384 0.0037  90  LYS   A O   
1818 C CB  . LYS   A 90  ? 0.2690 0.2982 0.1986 -0.0182 -0.0463 0.0436  90  LYS   A CB  
1819 C CG  . LYS   A 90  ? 0.3229 0.3429 0.2935 -0.0173 -0.0393 0.0511  90  LYS   A CG  
1820 C CD  . LYS   A 90  ? 0.3756 0.3892 0.3976 -0.0223 -0.0218 0.0471  90  LYS   A CD  
1821 C CE  . LYS   A 90  ? 0.4159 0.4256 0.4774 -0.0254 -0.0085 0.0391  90  LYS   A CE  
1822 N NZ  . LYS   A 90  ? 0.4382 0.4448 0.5305 -0.0284 0.0001  0.0344  90  LYS   A NZ  
1836 N N   . HIS   A 91  ? 0.1947 0.2069 0.1302 -0.0268 -0.0325 0.0170  91  HIS   A N   
1837 C CA  . HIS   A 91  ? 0.1889 0.1842 0.1315 -0.0164 -0.0240 0.0167  91  HIS   A CA  
1838 C C   . HIS   A 91  ? 0.1686 0.1748 0.1208 -0.0203 -0.0137 0.0238  91  HIS   A C   
1839 O O   . HIS   A 91  ? 0.1650 0.1873 0.1469 -0.0282 0.0037  0.0209  91  HIS   A O   
1840 C CB  . HIS   A 91  ? 0.2021 0.2072 0.1906 -0.0010 -0.0390 0.0207  91  HIS   A CB  
1841 C CG  . HIS   A 91  ? 0.2508 0.2646 0.2548 0.0129  -0.0669 0.0112  91  HIS   A CG  
1842 N ND1 . HIS   A 91  ? 0.2618 0.2963 0.2977 0.0227  -0.0777 -0.0127 91  HIS   A ND1 
1843 C CD2 . HIS   A 91  ? 0.2765 0.2888 0.2801 0.0178  -0.0857 0.0202  91  HIS   A CD2 
1844 C CE1 . HIS   A 91  ? 0.2747 0.3044 0.3123 0.0238  -0.0825 0.0026  91  HIS   A CE1 
1845 N NE2 . HIS   A 91  ? 0.2865 0.3045 0.3072 0.0234  -0.0931 0.0097  91  HIS   A NE2 
1853 N N   . CYS   A 92  ? 0.1546 0.1661 0.1304 -0.0237 -0.0132 0.0206  92  CYS   A N   
1854 C CA  . CYS   A 92  ? 0.1490 0.1606 0.1334 -0.0141 0.0015  0.0176  92  CYS   A CA  
1855 C C   . CYS   A 92  ? 0.1480 0.1506 0.1300 -0.0177 -0.0006 0.0142  92  CYS   A C   
1856 O O   . CYS   A 92  ? 0.1429 0.1580 0.1605 -0.0191 0.0037  0.0151  92  CYS   A O   
1857 C CB  . CYS   A 92  ? 0.1493 0.1564 0.1589 -0.0080 0.0020  0.0147  92  CYS   A CB  
1858 S SG  . CYS   A 92  ? 0.1463 0.1459 0.1584 -0.0151 -0.0050 0.0124  92  CYS   A SG  
1864 N N   . LEU   A 93  ? 0.1421 0.1401 0.1397 -0.0092 0.0138  0.0117  93  LEU   A N   
1865 C CA  . LEU   A 93  ? 0.1315 0.1391 0.1371 -0.0123 -0.0022 0.0156  93  LEU   A CA  
1866 C C   . LEU   A 93  ? 0.1375 0.1292 0.1332 -0.0007 -0.0033 0.0099  93  LEU   A C   
1867 O O   . LEU   A 93  ? 0.1249 0.1376 0.1339 -0.0022 -0.0006 0.0126  93  LEU   A O   
1868 C CB  . LEU   A 93  ? 0.1325 0.1428 0.1570 -0.0084 -0.0036 0.0209  93  LEU   A CB  
1869 C CG  . LEU   A 93  ? 0.1459 0.1404 0.1636 -0.0069 0.0025  0.0216  93  LEU   A CG  
1870 C CD1 . LEU   A 93  ? 0.1471 0.1474 0.1973 0.0031  0.0067  0.0151  93  LEU   A CD1 
1871 C CD2 . LEU   A 93  ? 0.1516 0.1377 0.1900 -0.0240 -0.0028 0.0231  93  LEU   A CD2 
1883 N N   . HIS   A 94  ? 0.1327 0.1255 0.1332 -0.0074 0.0034  0.0200  94  HIS   A N   
1884 C CA  . HIS   A 94  ? 0.1274 0.1257 0.1367 -0.0058 0.0029  0.0153  94  HIS   A CA  
1885 C C   . HIS   A 94  ? 0.1218 0.1219 0.1523 -0.0082 -0.0003 0.0046  94  HIS   A C   
1886 O O   . HIS   A 94  ? 0.1229 0.1427 0.1799 -0.0026 0.0020  -0.0103 94  HIS   A O   
1887 C CB  . HIS   A 94  ? 0.1251 0.1242 0.1544 -0.0046 -0.0029 0.0161  94  HIS   A CB  
1888 C CG  . HIS   A 94  ? 0.1226 0.1239 0.1377 -0.0100 -0.0085 0.0183  94  HIS   A CG  
1889 N ND1 . HIS   A 94  ? 0.1254 0.1272 0.1501 -0.0041 -0.0030 0.0213  94  HIS   A ND1 
1890 C CD2 . HIS   A 94  ? 0.1292 0.1384 0.1494 -0.0085 -0.0056 0.0081  94  HIS   A CD2 
1891 C CE1 . HIS   A 94  ? 0.1300 0.1371 0.1434 -0.0116 -0.0188 0.0079  94  HIS   A CE1 
1892 N NE2 . HIS   A 94  ? 0.1310 0.1361 0.1512 -0.0122 -0.0024 -0.0038 94  HIS   A NE2 
1900 N N   . VAL   A 95  ? 0.1197 0.1262 0.1297 -0.0079 0.0015  0.0022  95  VAL   A N   
1901 C CA  . VAL   A 95  ? 0.1326 0.1305 0.1208 -0.0106 0.0110  0.0142  95  VAL   A CA  
1902 C C   . VAL   A 95  ? 0.1330 0.1256 0.1217 -0.0192 0.0044  0.0024  95  VAL   A C   
1903 O O   . VAL   A 95  ? 0.1347 0.1346 0.1406 0.0109  0.0090  0.0093  95  VAL   A O   
1904 C CB  . VAL   A 95  ? 0.1323 0.1291 0.1470 -0.0127 0.0054  0.0049  95  VAL   A CB  
1905 C CG1 . VAL   A 95  ? 0.1448 0.1291 0.1549 -0.0173 -0.0009 0.0062  95  VAL   A CG1 
1906 C CG2 . VAL   A 95  ? 0.1357 0.1277 0.1507 -0.0150 0.0019  0.0218  95  VAL   A CG2 
1916 N N   . VAL   A 96  ? 0.1354 0.1298 0.1181 -0.0040 0.0078  0.0153  96  VAL   A N   
1917 C CA  . VAL   A 96  ? 0.1423 0.1311 0.1341 -0.0030 0.0093  0.0201  96  VAL   A CA  
1918 C C   . VAL   A 96  ? 0.1415 0.1405 0.1468 0.0009  0.0069  0.0174  96  VAL   A C   
1919 O O   . VAL   A 96  ? 0.1543 0.1434 0.1715 -0.0043 0.0153  0.0004  96  VAL   A O   
1920 C CB  . VAL   A 96  ? 0.1438 0.1349 0.1435 -0.0060 0.0186  0.0175  96  VAL   A CB  
1921 C CG1 . VAL   A 96  ? 0.1539 0.1470 0.1423 -0.0069 0.0144  0.0186  96  VAL   A CG1 
1922 C CG2 . VAL   A 96  ? 0.1448 0.1428 0.1513 -0.0182 0.0186  0.0056  96  VAL   A CG2 
1932 N N   A GLY   A 97  ? 0.1422 0.1382 0.1550 0.0006  0.0043  0.0141  97  GLY   A N   
1933 N N   B GLY   A 97  ? 0.1486 0.1447 0.1388 -0.0044 0.0104  0.0175  97  GLY   A N   
1934 C CA  A GLY   A 97  ? 0.1500 0.1518 0.1609 -0.0036 -0.0051 0.0123  97  GLY   A CA  
1935 C CA  B GLY   A 97  ? 0.1584 0.1551 0.1318 -0.0118 0.0119  0.0263  97  GLY   A CA  
1936 C C   A GLY   A 97  ? 0.1450 0.1592 0.1482 -0.0020 -0.0023 -0.0010 97  GLY   A C   
1937 C C   B GLY   A 97  ? 0.1619 0.1615 0.1425 -0.0155 0.0095  0.0277  97  GLY   A C   
1938 O O   A GLY   A 97  ? 0.1514 0.1587 0.1443 -0.0002 0.0067  -0.0008 97  GLY   A O   
1939 O O   B GLY   A 97  ? 0.1610 0.1608 0.1618 -0.0241 0.0089  0.0380  97  GLY   A O   
1946 N N   A PRO   A 98  ? 0.1486 0.1617 0.1280 -0.0014 -0.0100 0.0031  98  PRO   A N   
1947 N N   B PRO   A 98  ? 0.1798 0.1621 0.1523 -0.0014 0.0009  0.0365  98  PRO   A N   
1948 C CA  A PRO   A 98  ? 0.1522 0.1716 0.1315 -0.0018 -0.0012 -0.0043 98  PRO   A CA  
1949 C CA  B PRO   A 98  ? 0.1971 0.1709 0.1696 0.0014  -0.0022 0.0240  98  PRO   A CA  
1950 C C   A PRO   A 98  ? 0.1522 0.1829 0.1131 -0.0156 0.0033  0.0048  98  PRO   A C   
1951 C C   B PRO   A 98  ? 0.2208 0.1760 0.1607 -0.0006 -0.0036 0.0369  98  PRO   A C   
1952 O O   A PRO   A 98  ? 0.1454 0.1700 0.1203 -0.0158 0.0052  0.0038  98  PRO   A O   
1953 O O   B PRO   A 98  ? 0.2183 0.1665 0.1813 0.0010  0.0055  0.0283  98  PRO   A O   
1954 C CB  A PRO   A 98  ? 0.1612 0.1792 0.1305 0.0133  0.0011  -0.0114 98  PRO   A CB  
1955 C CB  B PRO   A 98  ? 0.1989 0.1693 0.1666 0.0080  -0.0054 0.0193  98  PRO   A CB  
1956 C CG  A PRO   A 98  ? 0.1583 0.1745 0.1316 0.0144  0.0014  -0.0098 98  PRO   A CG  
1957 C CG  B PRO   A 98  ? 0.1996 0.1661 0.1712 0.0054  0.0014  0.0175  98  PRO   A CG  
1958 C CD  A PRO   A 98  ? 0.1491 0.1633 0.1273 0.0047  -0.0065 -0.0087 98  PRO   A CD  
1959 C CD  B PRO   A 98  ? 0.1864 0.1619 0.1551 0.0018  0.0023  0.0325  98  PRO   A CD  
1974 N N   A ASN   A 99  ? 0.1551 0.2044 0.1142 -0.0167 0.0054  0.0216  99  ASN   A N   
1975 N N   B ASN   A 99  ? 0.2482 0.1927 0.1608 -0.0001 -0.0117 0.0574  99  ASN   A N   
1976 C CA  A ASN   A 99  ? 0.1758 0.2184 0.0939 -0.0144 0.0042  0.0443  99  ASN   A CA  
1977 C CA  B ASN   A 99  ? 0.2768 0.2130 0.2005 -0.0021 -0.0137 0.0622  99  ASN   A CA  
1978 C C   A ASN   A 99  ? 0.1940 0.2520 0.0902 -0.0186 0.0025  0.0472  99  ASN   A C   
1979 C C   B ASN   A 99  ? 0.2932 0.2437 0.1975 -0.0026 -0.0176 0.0538  99  ASN   A C   
1980 O O   A ASN   A 99  ? 0.2005 0.2780 0.1124 -0.0136 -0.0074 0.0262  99  ASN   A O   
1981 O O   B ASN   A 99  ? 0.2933 0.2367 0.1726 0.0018  -0.0228 0.0719  99  ASN   A O   
1982 C CB  A ASN   A 99  ? 0.1736 0.2068 0.1333 -0.0097 -0.0101 0.0412  99  ASN   A CB  
1983 C CB  B ASN   A 99  ? 0.2873 0.2084 0.2438 -0.0048 -0.0154 0.0778  99  ASN   A CB  
1984 C CG  A ASN   A 99  ? 0.1758 0.2042 0.1665 -0.0010 -0.0131 0.0257  99  ASN   A CG  
1985 C CG  B ASN   A 99  ? 0.2983 0.2084 0.2786 -0.0074 -0.0173 0.0844  99  ASN   A CG  
1986 O OD1 A ASN   A 99  ? 0.1822 0.2106 0.1763 0.0089  -0.0067 0.0170  99  ASN   A OD1 
1987 O OD1 B ASN   A 99  ? 0.3077 0.2175 0.3339 -0.0131 -0.0155 0.0667  99  ASN   A OD1 
1988 N ND2 A ASN   A 99  ? 0.1768 0.2002 0.1875 -0.0006 -0.0064 0.0314  99  ASN   A ND2 
1989 N ND2 B ASN   A 99  ? 0.2957 0.2031 0.2592 0.0012  -0.0230 0.1023  99  ASN   A ND2 
2002 N N   A VAL   A 100 ? 0.2075 0.2606 0.1035 -0.0353 -0.0156 0.0482  100 VAL   A N   
2003 N N   B VAL   A 100 ? 0.3123 0.2823 0.2307 -0.0060 -0.0108 0.0314  100 VAL   A N   
2004 C CA  A VAL   A 100 ? 0.2283 0.2842 0.1408 -0.0464 -0.0178 0.0402  100 VAL   A CA  
2005 C CA  B VAL   A 100 ? 0.3343 0.3140 0.2734 -0.0046 -0.0107 0.0119  100 VAL   A CA  
2006 C C   A VAL   A 100 ? 0.2401 0.3038 0.1355 -0.0511 -0.0291 0.0593  100 VAL   A C   
2007 C C   B VAL   A 100 ? 0.3516 0.3375 0.3066 -0.0000 -0.0075 0.0086  100 VAL   A C   
2008 O O   A VAL   A 100 ? 0.2570 0.3168 0.1556 -0.0445 -0.0123 0.0706  100 VAL   A O   
2009 O O   B VAL   A 100 ? 0.3538 0.3456 0.3069 0.0000  -0.0100 0.0096  100 VAL   A O   
2010 C CB  A VAL   A 100 ? 0.2406 0.2832 0.1720 -0.0537 -0.0241 0.0199  100 VAL   A CB  
2011 C CB  B VAL   A 100 ? 0.3393 0.3199 0.2884 -0.0056 -0.0123 -0.0008 100 VAL   A CB  
2012 C CG1 A VAL   A 100 ? 0.2383 0.2898 0.1908 -0.0575 -0.0200 0.0140  100 VAL   A CG1 
2013 C CG1 B VAL   A 100 ? 0.3407 0.3242 0.2956 -0.0050 -0.0160 -0.0047 100 VAL   A CG1 
2014 C CG2 A VAL   A 100 ? 0.2538 0.2843 0.1863 -0.0503 -0.0205 0.0145  100 VAL   A CG2 
2015 C CG2 B VAL   A 100 ? 0.3432 0.3223 0.2946 -0.0070 -0.0121 -0.0044 100 VAL   A CG2 
2034 N N   A ASN   A 101 ? 0.2366 0.3061 0.1562 -0.0649 -0.0368 0.0818  101 ASN   A N   
2035 N N   B ASN   A 101 ? 0.3631 0.3488 0.3211 0.0075  -0.0048 0.0120  101 ASN   A N   
2036 C CA  A ASN   A 101 ? 0.2507 0.3148 0.1796 -0.0697 -0.0483 0.0932  101 ASN   A CA  
2037 C CA  B ASN   A 101 ? 0.3745 0.3555 0.3346 0.0136  -0.0041 0.0178  101 ASN   A CA  
2038 C C   A ASN   A 101 ? 0.2738 0.3399 0.1975 -0.0719 -0.0234 0.1112  101 ASN   A C   
2039 C C   B ASN   A 101 ? 0.3850 0.3588 0.3418 0.0117  0.0063  0.0154  101 ASN   A C   
2040 O O   A ASN   A 101 ? 0.2883 0.3437 0.2317 -0.0695 -0.0257 0.0967  101 ASN   A O   
2041 O O   B ASN   A 101 ? 0.3899 0.3624 0.3529 0.0121  0.0051  0.0183  101 ASN   A O   
2042 C CB  A ASN   A 101 ? 0.2509 0.3047 0.1866 -0.0696 -0.0640 0.0813  101 ASN   A CB  
2043 C CB  B ASN   A 101 ? 0.3762 0.3584 0.3343 0.0198  -0.0113 0.0286  101 ASN   A CB  
2044 C CG  A ASN   A 101 ? 0.2546 0.2957 0.1917 -0.0700 -0.0641 0.0594  101 ASN   A CG  
2045 C CG  B ASN   A 101 ? 0.3764 0.3566 0.3276 0.0254  -0.0168 0.0373  101 ASN   A CG  
2046 O OD1 A ASN   A 101 ? 0.2487 0.3010 0.1900 -0.0554 -0.0637 0.0367  101 ASN   A OD1 
2047 O OD1 B ASN   A 101 ? 0.3743 0.3585 0.3312 0.0264  -0.0282 0.0413  101 ASN   A OD1 
2048 N ND2 A ASN   A 101 ? 0.2610 0.2885 0.2093 -0.0790 -0.0603 0.0575  101 ASN   A ND2 
2049 N ND2 B ASN   A 101 ? 0.3770 0.3552 0.3197 0.0273  -0.0144 0.0424  101 ASN   A ND2 
2062 N N   A LYS   A 102 ? 0.2759 0.3652 0.2275 -0.0786 -0.0021 0.1088  102 LYS   A N   
2063 N N   B LYS   A 102 ? 0.3879 0.3580 0.3379 0.0109  0.0127  0.0052  102 LYS   A N   
2064 C CA  A LYS   A 102 ? 0.2853 0.3885 0.2362 -0.0781 0.0036  0.0945  102 LYS   A CA  
2065 C CA  B LYS   A 102 ? 0.3916 0.3583 0.3262 0.0078  0.0238  0.0027  102 LYS   A CA  
2066 C C   A LYS   A 102 ? 0.2966 0.4079 0.2345 -0.0672 0.0102  0.0848  102 LYS   A C   
2067 C C   B LYS   A 102 ? 0.3828 0.3431 0.2914 0.0160  0.0221  0.0132  102 LYS   A C   
2068 O O   A LYS   A 102 ? 0.3009 0.4211 0.2435 -0.0619 0.0172  0.0737  102 LYS   A O   
2069 O O   B LYS   A 102 ? 0.3823 0.3377 0.2934 0.0173  0.0269  0.0106  102 LYS   A O   
2070 C CB  A LYS   A 102 ? 0.2892 0.3914 0.2653 -0.0860 0.0000  0.0813  102 LYS   A CB  
2071 C CB  B LYS   A 102 ? 0.4013 0.3712 0.3577 -0.0004 0.0299  -0.0140 102 LYS   A CB  
2072 C CG  A LYS   A 102 ? 0.2935 0.3932 0.2855 -0.0904 -0.0036 0.0645  102 LYS   A CG  
2073 C CG  B LYS   A 102 ? 0.4092 0.3821 0.3897 -0.0082 0.0321  -0.0236 102 LYS   A CG  
2074 C CD  A LYS   A 102 ? 0.3044 0.3975 0.3176 -0.0900 -0.0074 0.0443  102 LYS   A CD  
2075 C CD  B LYS   A 102 ? 0.4158 0.3914 0.4196 -0.0145 0.0335  -0.0330 102 LYS   A CD  
2076 C CE  A LYS   A 102 ? 0.3151 0.4018 0.3453 -0.0836 -0.0091 0.0300  102 LYS   A CE  
2077 C CE  B LYS   A 102 ? 0.4195 0.3975 0.4412 -0.0183 0.0319  -0.0406 102 LYS   A CE  
2078 N NZ  A LYS   A 102 ? 0.3201 0.4034 0.3575 -0.0822 -0.0115 0.0173  102 LYS   A NZ  
2079 N NZ  B LYS   A 102 ? 0.4218 0.4003 0.4566 -0.0205 0.0317  -0.0441 102 LYS   A NZ  
2106 N N   A GLY   A 103 ? 0.3013 0.4165 0.2478 -0.0556 0.0019  0.0647  103 GLY   A N   
2107 N N   B GLY   A 103 ? 0.3723 0.3330 0.2726 0.0232  0.0095  0.0237  103 GLY   A N   
2108 C CA  A GLY   A 103 ? 0.3104 0.4229 0.2643 -0.0421 0.0029  0.0483  103 GLY   A CA  
2109 C CA  B GLY   A 103 ? 0.3587 0.3224 0.2608 0.0280  0.0008  0.0362  103 GLY   A CA  
2110 C C   A GLY   A 103 ? 0.3139 0.4287 0.2754 -0.0337 0.0140  0.0365  103 GLY   A C   
2111 C C   B GLY   A 103 ? 0.3434 0.3116 0.2445 0.0269  -0.0036 0.0472  103 GLY   A C   
2112 O O   A GLY   A 103 ? 0.3238 0.4355 0.2987 -0.0250 0.0133  0.0330  103 GLY   A O   
2113 O O   B GLY   A 103 ? 0.3476 0.3102 0.2506 0.0268  -0.0023 0.0414  103 GLY   A O   
2120 N N   A GLU   A 104 ? 0.3015 0.4246 0.2389 -0.0389 0.0338  0.0262  104 GLU   A N   
2121 N N   B GLU   A 104 ? 0.3243 0.3021 0.2246 0.0238  -0.0091 0.0549  104 GLU   A N   
2122 C CA  A GLU   A 104 ? 0.2891 0.4162 0.2118 -0.0478 0.0386  0.0146  104 GLU   A CA  
2123 C CA  B GLU   A 104 ? 0.3091 0.2962 0.2062 0.0151  -0.0058 0.0540  104 GLU   A CA  
2124 C C   A GLU   A 104 ? 0.2983 0.4225 0.2151 -0.0521 0.0394  -0.0059 104 GLU   A C   
2125 C C   B GLU   A 104 ? 0.2990 0.3012 0.2152 0.0145  -0.0009 0.0345  104 GLU   A C   
2126 O O   A GLU   A 104 ? 0.2926 0.4243 0.2189 -0.0563 0.0306  -0.0157 104 GLU   A O   
2127 O O   B GLU   A 104 ? 0.2976 0.3005 0.2263 0.0153  -0.0111 0.0349  104 GLU   A O   
2128 C CB  A GLU   A 104 ? 0.2636 0.3993 0.1755 -0.0540 0.0405  0.0278  104 GLU   A CB  
2129 C CB  B GLU   A 104 ? 0.3092 0.2878 0.2033 0.0019  -0.0018 0.0646  104 GLU   A CB  
2130 C CG  A GLU   A 104 ? 0.2469 0.3821 0.1605 -0.0546 0.0240  0.0295  104 GLU   A CG  
2131 C CG  B GLU   A 104 ? 0.3128 0.2872 0.2080 -0.0075 -0.0011 0.0674  104 GLU   A CG  
2132 C CD  A GLU   A 104 ? 0.2265 0.3625 0.1471 -0.0573 0.0169  0.0379  104 GLU   A CD  
2133 C CD  B GLU   A 104 ? 0.3187 0.2918 0.2137 -0.0143 -0.0052 0.0664  104 GLU   A CD  
2134 O OE1 A GLU   A 104 ? 0.2097 0.3478 0.1119 -0.0610 0.0020  0.0372  104 GLU   A OE1 
2135 O OE1 B GLU   A 104 ? 0.3225 0.2972 0.2125 -0.0126 -0.0104 0.0626  104 GLU   A OE1 
2136 O OE2 A GLU   A 104 ? 0.2396 0.3595 0.1600 -0.0549 0.0214  0.0495  104 GLU   A OE2 
2137 O OE2 B GLU   A 104 ? 0.3225 0.2920 0.2185 -0.0201 0.0005  0.0673  104 GLU   A OE2 
2150 N N   A ASP   A 105 ? 0.3126 0.4270 0.2266 -0.0499 0.0398  -0.0223 105 ASP   A N   
2151 N N   B ASP   A 105 ? 0.2958 0.3032 0.2278 0.0121  0.0012  0.0158  105 ASP   A N   
2152 C CA  A ASP   A 105 ? 0.3213 0.4299 0.2534 -0.0464 0.0423  -0.0459 105 ASP   A CA  
2153 C CA  B ASP   A 105 ? 0.2924 0.3070 0.2532 0.0080  0.0069  -0.0113 105 ASP   A CA  
2154 C C   A ASP   A 105 ? 0.3018 0.4184 0.2321 -0.0588 0.0277  -0.0666 105 ASP   A C   
2155 C C   B ASP   A 105 ? 0.2846 0.3032 0.2265 -0.0062 0.0025  -0.0271 105 ASP   A C   
2156 O O   A ASP   A 105 ? 0.2999 0.4204 0.2144 -0.0602 0.0230  -0.0826 105 ASP   A O   
2157 O O   B ASP   A 105 ? 0.2728 0.2917 0.1655 -0.0004 0.0006  -0.0364 105 ASP   A O   
2158 C CB  A ASP   A 105 ? 0.3466 0.4417 0.3062 -0.0316 0.0496  -0.0506 105 ASP   A CB  
2159 C CB  B ASP   A 105 ? 0.3007 0.3140 0.3003 0.0199  0.0171  -0.0262 105 ASP   A CB  
2160 C CG  A ASP   A 105 ? 0.3654 0.4511 0.3482 -0.0208 0.0519  -0.0576 105 ASP   A CG  
2161 C CG  B ASP   A 105 ? 0.3115 0.3216 0.3449 0.0309  0.0283  -0.0405 105 ASP   A CG  
2162 O OD1 A ASP   A 105 ? 0.3710 0.4556 0.3529 -0.0188 0.0486  -0.0715 105 ASP   A OD1 
2163 O OD1 B ASP   A 105 ? 0.3150 0.3223 0.3469 0.0290  0.0283  -0.0453 105 ASP   A OD1 
2164 O OD2 A ASP   A 105 ? 0.3760 0.4550 0.3813 -0.0173 0.0563  -0.0470 105 ASP   A OD2 
2165 O OD2 B ASP   A 105 ? 0.3158 0.3254 0.3753 0.0402  0.0334  -0.0474 105 ASP   A OD2 
2174 N N   A ILE   A 106 ? 0.2838 0.4008 0.2338 -0.0700 0.0015  -0.0769 106 ILE   A N   
2175 N N   B ILE   A 106 ? 0.2889 0.3160 0.2557 -0.0231 -0.0038 -0.0329 106 ILE   A N   
2176 C CA  A ILE   A 106 ? 0.2628 0.3798 0.2438 -0.0801 -0.0183 -0.0928 106 ILE   A CA  
2177 C CA  B ILE   A 106 ? 0.2934 0.3218 0.2812 -0.0443 -0.0094 -0.0445 106 ILE   A CA  
2178 C C   A ILE   A 106 ? 0.2466 0.3608 0.2576 -0.0948 -0.0117 -0.1031 106 ILE   A C   
2179 C C   B ILE   A 106 ? 0.2972 0.3184 0.2856 -0.0510 0.0077  -0.0420 106 ILE   A C   
2180 O O   A ILE   A 106 ? 0.2189 0.3502 0.2513 -0.1022 0.0026  -0.1133 106 ILE   A O   
2181 O O   B ILE   A 106 ? 0.2929 0.3216 0.2862 -0.0533 0.0210  -0.0334 106 ILE   A O   
2182 C CB  A ILE   A 106 ? 0.2664 0.3811 0.2731 -0.0700 -0.0363 -0.0681 106 ILE   A CB  
2183 C CB  B ILE   A 106 ? 0.2969 0.3331 0.2936 -0.0536 -0.0260 -0.0599 106 ILE   A CB  
2184 C CG1 A ILE   A 106 ? 0.2639 0.3768 0.2997 -0.0628 -0.0370 -0.0538 106 ILE   A CG1 
2185 C CG1 B ILE   A 106 ? 0.2931 0.3396 0.3035 -0.0551 -0.0309 -0.0652 106 ILE   A CG1 
2186 C CG2 A ILE   A 106 ? 0.2734 0.3830 0.2827 -0.0662 -0.0428 -0.0659 106 ILE   A CG2 
2187 C CG2 B ILE   A 106 ? 0.3032 0.3366 0.2951 -0.0559 -0.0284 -0.0637 106 ILE   A CG2 
2188 C CD1 A ILE   A 106 ? 0.2637 0.3733 0.3211 -0.0547 -0.0290 -0.0430 106 ILE   A CD1 
2189 C CD1 B ILE   A 106 ? 0.2914 0.3440 0.3153 -0.0568 -0.0295 -0.0666 106 ILE   A CD1 
2212 N N   A GLN   A 107 ? 0.2675 0.3484 0.2905 -0.0926 0.0031  -0.1109 107 GLN   A N   
2213 N N   B GLN   A 107 ? 0.3058 0.3104 0.2949 -0.0540 0.0174  -0.0496 107 GLN   A N   
2214 C CA  A GLN   A 107 ? 0.2894 0.3322 0.3479 -0.0799 0.0272  -0.1058 107 GLN   A CA  
2215 C CA  B GLN   A 107 ? 0.3154 0.3100 0.3400 -0.0572 0.0265  -0.0454 107 GLN   A CA  
2216 C C   A GLN   A 107 ? 0.2636 0.2926 0.3335 -0.0736 0.0525  -0.0814 107 GLN   A C   
2217 C C   B GLN   A 107 ? 0.2852 0.2833 0.3211 -0.0621 0.0471  -0.0546 107 GLN   A C   
2218 O O   A GLN   A 107 ? 0.2548 0.2858 0.3749 -0.0749 0.0799  -0.0824 107 GLN   A O   
2219 O O   B GLN   A 107 ? 0.2889 0.2829 0.3504 -0.0709 0.0532  -0.0571 107 GLN   A O   
2220 C CB  A GLN   A 107 ? 0.3329 0.3570 0.4342 -0.0794 0.0173  -0.1021 107 GLN   A CB  
2221 C CB  B GLN   A 107 ? 0.3484 0.3355 0.4013 -0.0604 0.0103  -0.0346 107 GLN   A CB  
2222 C CG  A GLN   A 107 ? 0.3741 0.3819 0.5247 -0.0751 0.0103  -0.0858 107 GLN   A CG  
2223 C CG  B GLN   A 107 ? 0.3771 0.3585 0.4644 -0.0620 -0.0056 -0.0166 107 GLN   A CG  
2224 C CD  A GLN   A 107 ? 0.4061 0.4003 0.6007 -0.0711 0.0056  -0.0678 107 GLN   A CD  
2225 C CD  B GLN   A 107 ? 0.4008 0.3794 0.5211 -0.0607 -0.0173 0.0009  107 GLN   A CD  
2226 O OE1 A GLN   A 107 ? 0.4195 0.4089 0.6332 -0.0679 0.0028  -0.0601 107 GLN   A OE1 
2227 O OE1 B GLN   A 107 ? 0.4094 0.3867 0.5394 -0.0601 -0.0213 0.0101  107 GLN   A OE1 
2228 N NE2 A GLN   A 107 ? 0.4170 0.4057 0.6256 -0.0710 0.0040  -0.0646 107 GLN   A NE2 
2229 N NE2 B GLN   A 107 ? 0.4084 0.3857 0.5383 -0.0596 -0.0252 0.0042  107 GLN   A NE2 
2246 N N   . LEU   A 108 ? 0.2506 0.2583 0.2798 -0.0625 0.0464  -0.0649 108 LEU   A N   
2247 C CA  . LEU   A 108 ? 0.2157 0.2084 0.2409 -0.0332 0.0412  -0.0320 108 LEU   A CA  
2248 C C   . LEU   A 108 ? 0.1860 0.1588 0.2209 -0.0134 0.0332  -0.0061 108 LEU   A C   
2249 O O   . LEU   A 108 ? 0.1815 0.1571 0.2344 0.0023  0.0362  -0.0018 108 LEU   A O   
2250 C CB  . LEU   A 108 ? 0.2167 0.2217 0.2169 -0.0311 0.0494  -0.0291 108 LEU   A CB  
2251 C CG  . LEU   A 108 ? 0.2310 0.2486 0.2456 -0.0268 0.0571  -0.0326 108 LEU   A CG  
2252 C CD1 . LEU   A 108 ? 0.2472 0.2604 0.2590 -0.0371 0.0628  -0.0262 108 LEU   A CD1 
2253 C CD2 . LEU   A 108 ? 0.2313 0.2675 0.2922 -0.0233 0.0562  -0.0267 108 LEU   A CD2 
2266 N N   . LEU   A 109 ? 0.1710 0.1536 0.2117 0.0012  0.0204  0.0013  109 LEU   A N   
2267 C CA  . LEU   A 109 ? 0.1651 0.1445 0.1945 -0.0001 0.0075  0.0062  109 LEU   A CA  
2268 C C   . LEU   A 109 ? 0.1505 0.1408 0.1826 -0.0084 0.0061  -0.0045 109 LEU   A C   
2269 O O   . LEU   A 109 ? 0.1559 0.1335 0.2032 -0.0038 -0.0036 -0.0019 109 LEU   A O   
2270 C CB  . LEU   A 109 ? 0.1667 0.1515 0.2077 0.0132  -0.0008 0.0165  109 LEU   A CB  
2271 C CG  . LEU   A 109 ? 0.1600 0.1640 0.2192 0.0096  0.0047  0.0177  109 LEU   A CG  
2272 C CD1 . LEU   A 109 ? 0.1615 0.1620 0.2187 0.0039  0.0168  0.0055  109 LEU   A CD1 
2273 C CD2 . LEU   A 109 ? 0.1578 0.1781 0.2425 0.0112  0.0029  0.0269  109 LEU   A CD2 
2285 N N   . LYS   A 110 ? 0.1556 0.1440 0.1800 -0.0067 -0.0071 -0.0059 110 LYS   A N   
2286 C CA  . LYS   A 110 ? 0.1494 0.1407 0.1856 -0.0177 -0.0081 0.0043  110 LYS   A CA  
2287 C C   . LYS   A 110 ? 0.1513 0.1317 0.1677 -0.0102 0.0019  -0.0048 110 LYS   A C   
2288 O O   . LYS   A 110 ? 0.1459 0.1293 0.1887 -0.0126 0.0092  -0.0051 110 LYS   A O   
2289 C CB  . LYS   A 110 ? 0.1614 0.1456 0.2192 -0.0140 -0.0156 -0.0029 110 LYS   A CB  
2290 C CG  . LYS   A 110 ? 0.1600 0.1413 0.2313 -0.0129 -0.0156 -0.0069 110 LYS   A CG  
2291 C CD  . LYS   A 110 ? 0.1604 0.1480 0.2485 -0.0160 -0.0042 -0.0151 110 LYS   A CD  
2292 C CE  . LYS   A 110 ? 0.1696 0.1519 0.2625 -0.0121 0.0073  -0.0132 110 LYS   A CE  
2293 N NZ  . LYS   A 110 ? 0.1690 0.1570 0.2698 -0.0187 0.0130  0.0039  110 LYS   A NZ  
2307 N N   . SER   A 111 ? 0.1534 0.1317 0.1774 -0.0064 -0.0046 -0.0017 111 SER   A N   
2308 C CA  . SER   A 111 ? 0.1453 0.1413 0.1811 -0.0012 0.0077  0.0019  111 SER   A CA  
2309 C C   . SER   A 111 ? 0.1319 0.1362 0.1810 -0.0059 0.0092  0.0076  111 SER   A C   
2310 O O   . SER   A 111 ? 0.1541 0.1243 0.1942 -0.0031 0.0077  0.0041  111 SER   A O   
2311 C CB  . SER   A 111 ? 0.1618 0.1622 0.1903 -0.0007 0.0250  -0.0146 111 SER   A CB  
2312 O OG  . SER   A 111 ? 0.2023 0.1824 0.2009 0.0047  0.0256  -0.0194 111 SER   A OG  
2318 N N   . ALA   A 112 ? 0.1410 0.1292 0.1961 -0.0030 0.0149  0.0050  112 ALA   A N   
2319 C CA  . ALA   A 112 ? 0.1435 0.1269 0.1719 -0.0042 0.0241  -0.0064 112 ALA   A CA  
2320 C C   . ALA   A 112 ? 0.1357 0.1217 0.1881 -0.0009 0.0107  -0.0029 112 ALA   A C   
2321 O O   . ALA   A 112 ? 0.1392 0.1211 0.2003 -0.0123 0.0123  0.0033  112 ALA   A O   
2322 C CB  . ALA   A 112 ? 0.1550 0.1309 0.1843 -0.0051 0.0123  -0.0034 112 ALA   A CB  
2328 N N   . TYR   A 113 ? 0.1274 0.1255 0.1959 -0.0073 0.0158  0.0037  113 TYR   A N   
2329 C CA  . TYR   A 113 ? 0.1266 0.1240 0.1880 -0.0017 0.0163  0.0069  113 TYR   A CA  
2330 C C   . TYR   A 113 ? 0.1268 0.1223 0.1763 -0.0116 0.0120  -0.0020 113 TYR   A C   
2331 O O   . TYR   A 113 ? 0.1351 0.1278 0.1942 -0.0058 0.0208  -0.0021 113 TYR   A O   
2332 C CB  . TYR   A 113 ? 0.1302 0.1356 0.1931 -0.0052 0.0031  0.0170  113 TYR   A CB  
2333 C CG  . TYR   A 113 ? 0.1328 0.1345 0.1708 -0.0084 0.0099  0.0195  113 TYR   A CG  
2334 C CD1 . TYR   A 113 ? 0.1366 0.1404 0.1717 -0.0006 0.0094  0.0205  113 TYR   A CD1 
2335 C CD2 . TYR   A 113 ? 0.1434 0.1383 0.1738 -0.0149 -0.0010 0.0154  113 TYR   A CD2 
2336 C CE1 . TYR   A 113 ? 0.1382 0.1508 0.1725 -0.0068 0.0071  0.0139  113 TYR   A CE1 
2337 C CE2 . TYR   A 113 ? 0.1408 0.1470 0.1778 -0.0053 -0.0048 0.0216  113 TYR   A CE2 
2338 C CZ  . TYR   A 113 ? 0.1336 0.1439 0.1744 -0.0016 0.0074  0.0181  113 TYR   A CZ  
2339 O OH  . TYR   A 113 ? 0.1364 0.1542 0.2005 0.0110  0.0023  0.0143  113 TYR   A OH  
2349 N N   . GLU   A 114 ? 0.1272 0.1250 0.1810 -0.0021 0.0148  0.0093  114 GLU   A N   
2350 C CA  . GLU   A 114 ? 0.1335 0.1200 0.1924 -0.0000 0.0076  0.0109  114 GLU   A CA  
2351 C C   . GLU   A 114 ? 0.1274 0.1254 0.1848 -0.0081 0.0076  0.0166  114 GLU   A C   
2352 O O   . GLU   A 114 ? 0.1402 0.1274 0.1842 -0.0034 0.0056  0.0121  114 GLU   A O   
2353 C CB  . GLU   A 114 ? 0.1285 0.1271 0.1994 -0.0043 0.0090  0.0096  114 GLU   A CB  
2354 C CG  . GLU   A 114 ? 0.1345 0.1257 0.2070 0.0023  0.0100  0.0020  114 GLU   A CG  
2355 C CD  . GLU   A 114 ? 0.1468 0.1195 0.2135 -0.0013 -0.0015 -0.0043 114 GLU   A CD  
2356 O OE1 . GLU   A 114 ? 0.1470 0.1254 0.2122 -0.0092 0.0135  -0.0040 114 GLU   A OE1 
2357 O OE2 . GLU   A 114 ? 0.1689 0.1392 0.2273 -0.0137 -0.0011 -0.0183 114 GLU   A OE2 
2364 N N   . ASN   A 115 ? 0.1347 0.1246 0.1732 -0.0105 0.0091  0.0048  115 ASN   A N   
2365 C CA  . ASN   A 115 ? 0.1434 0.1317 0.1789 -0.0101 0.0197  0.0101  115 ASN   A CA  
2366 C C   . ASN   A 115 ? 0.1401 0.1297 0.1739 -0.0158 0.0034  0.0082  115 ASN   A C   
2367 O O   . ASN   A 115 ? 0.1344 0.1414 0.1856 -0.0101 0.0120  0.0090  115 ASN   A O   
2368 C CB  . ASN   A 115 ? 0.1466 0.1347 0.1805 -0.0144 0.0178  0.0157  115 ASN   A CB  
2369 C CG  . ASN   A 115 ? 0.1447 0.1553 0.1884 -0.0147 0.0174  0.0150  115 ASN   A CG  
2370 O OD1 . ASN   A 115 ? 0.1457 0.2522 0.2188 -0.0083 0.0301  0.0276  115 ASN   A OD1 
2371 N ND2 . ASN   A 115 ? 0.1450 0.1383 0.1875 -0.0166 0.0233  0.0141  115 ASN   A ND2 
2378 N N   . PHE   A 116 ? 0.1272 0.1323 0.1777 -0.0072 0.0138  0.0104  116 PHE   A N   
2379 C CA  . PHE   A 116 ? 0.1303 0.1417 0.1685 -0.0043 0.0156  0.0089  116 PHE   A CA  
2380 C C   . PHE   A 116 ? 0.1274 0.1439 0.1811 -0.0089 0.0158  0.0196  116 PHE   A C   
2381 O O   . PHE   A 116 ? 0.1373 0.1484 0.1919 0.0001  0.0225  0.0271  116 PHE   A O   
2382 C CB  . PHE   A 116 ? 0.1255 0.1312 0.1855 -0.0027 0.0186  0.0146  116 PHE   A CB  
2383 C CG  . PHE   A 116 ? 0.1305 0.1271 0.1597 -0.0053 0.0202  0.0117  116 PHE   A CG  
2384 C CD1 . PHE   A 116 ? 0.1350 0.1277 0.1738 -0.0005 0.0139  0.0165  116 PHE   A CD1 
2385 C CD2 . PHE   A 116 ? 0.1421 0.1367 0.1677 -0.0078 0.0201  0.0124  116 PHE   A CD2 
2386 C CE1 . PHE   A 116 ? 0.1352 0.1340 0.1814 -0.0233 0.0084  0.0116  116 PHE   A CE1 
2387 C CE2 . PHE   A 116 ? 0.1395 0.1324 0.1902 -0.0073 0.0122  0.0088  116 PHE   A CE2 
2388 C CZ  . PHE   A 116 ? 0.1404 0.1217 0.1825 -0.0049 0.0048  0.0039  116 PHE   A CZ  
2398 N N   . ASN   A 117 ? 0.1315 0.1354 0.1947 -0.0103 0.0126  0.0264  117 ASN   A N   
2399 C CA  . ASN   A 117 ? 0.1340 0.1348 0.2058 -0.0070 0.0098  0.0250  117 ASN   A CA  
2400 C C   . ASN   A 117 ? 0.1397 0.1431 0.2172 -0.0004 0.0175  0.0248  117 ASN   A C   
2401 O O   . ASN   A 117 ? 0.1446 0.1477 0.2381 -0.0063 -0.0051 0.0355  117 ASN   A O   
2402 C CB  . ASN   A 117 ? 0.1375 0.1430 0.2107 -0.0066 0.0120  0.0322  117 ASN   A CB  
2403 C CG  . ASN   A 117 ? 0.1364 0.1392 0.2160 -0.0067 0.0111  0.0289  117 ASN   A CG  
2404 O OD1 . ASN   A 117 ? 0.1377 0.1618 0.2293 -0.0145 0.0137  0.0225  117 ASN   A OD1 
2405 N ND2 . ASN   A 117 ? 0.1287 0.1348 0.2106 -0.0053 0.0076  0.0270  117 ASN   A ND2 
2412 N N   . GLN   A 118 ? 0.1349 0.1415 0.2088 -0.0071 0.0016  0.0245  118 GLN   A N   
2413 C CA  . GLN   A 118 ? 0.1453 0.1540 0.2090 -0.0061 -0.0011 0.0256  118 GLN   A CA  
2414 C C   . GLN   A 118 ? 0.1498 0.1646 0.1973 -0.0024 -0.0029 0.0295  118 GLN   A C   
2415 O O   . GLN   A 118 ? 0.1412 0.1964 0.2279 0.0001  -0.0126 0.0124  118 GLN   A O   
2416 C CB  . GLN   A 118 ? 0.1439 0.1553 0.2272 -0.0023 0.0083  0.0230  118 GLN   A CB  
2417 C CG  . GLN   A 118 ? 0.1364 0.1614 0.2134 -0.0005 0.0036  0.0345  118 GLN   A CG  
2418 C CD  . GLN   A 118 ? 0.1348 0.1669 0.2403 0.0034  0.0065  0.0207  118 GLN   A CD  
2419 O OE1 . GLN   A 118 ? 0.1346 0.1794 0.2583 0.0094  0.0081  0.0152  118 GLN   A OE1 
2420 N NE2 . GLN   A 118 ? 0.1419 0.1647 0.2361 0.0058  0.0074  0.0293  118 GLN   A NE2 
2429 N N   . HIS   A 119 ? 0.1538 0.1563 0.1852 -0.0002 0.0070  0.0260  119 HIS   A N   
2430 C CA  . HIS   A 119 ? 0.1601 0.1658 0.1974 -0.0047 0.0101  0.0351  119 HIS   A CA  
2431 C C   . HIS   A 119 ? 0.1632 0.1721 0.1963 -0.0092 0.0164  0.0380  119 HIS   A C   
2432 O O   . HIS   A 119 ? 0.1576 0.1795 0.2042 -0.0269 0.0049  0.0375  119 HIS   A O   
2433 C CB  . HIS   A 119 ? 0.1631 0.1659 0.2151 -0.0027 0.0186  0.0395  119 HIS   A CB  
2434 C CG  . HIS   A 119 ? 0.1612 0.1673 0.2511 -0.0035 0.0129  0.0430  119 HIS   A CG  
2435 N ND1 . HIS   A 119 ? 0.1742 0.1841 0.3052 -0.0166 0.0129  0.0241  119 HIS   A ND1 
2436 C CD2 . HIS   A 119 ? 0.1695 0.1732 0.2711 0.0094  0.0272  0.0601  119 HIS   A CD2 
2437 C CE1 . HIS   A 119 ? 0.1769 0.1814 0.3176 -0.0159 0.0253  0.0431  119 HIS   A CE1 
2438 N NE2 . HIS   A 119 ? 0.1831 0.1791 0.3123 -0.0061 0.0362  0.0613  119 HIS   A NE2 
2446 N N   . GLU   A 120 ? 0.1721 0.1976 0.1891 -0.0088 0.0020  0.0617  120 GLU   A N   
2447 C CA  . GLU   A 120 ? 0.2019 0.2295 0.2286 0.0052  0.0032  0.1103  120 GLU   A CA  
2448 C C   . GLU   A 120 ? 0.1805 0.2173 0.2111 -0.0092 0.0102  0.0919  120 GLU   A C   
2449 O O   . GLU   A 120 ? 0.1763 0.2087 0.2199 -0.0138 -0.0006 0.0819  120 GLU   A O   
2450 C CB  . GLU   A 120 ? 0.2673 0.2928 0.2871 0.0242  0.0124  0.1556  120 GLU   A CB  
2451 C CG  . GLU   A 120 ? 0.3543 0.3653 0.3868 0.0402  0.0077  0.1573  120 GLU   A CG  
2452 C CD  . GLU   A 120 ? 0.4283 0.4243 0.4943 0.0537  0.0160  0.1421  120 GLU   A CD  
2453 O OE1 . GLU   A 120 ? 0.4534 0.4450 0.5142 0.0548  0.0212  0.1342  120 GLU   A OE1 
2454 O OE2 . GLU   A 120 ? 0.4682 0.4682 0.5478 0.0581  0.0163  0.1349  120 GLU   A OE2 
2461 N N   . VAL   A 121 ? 0.1760 0.2196 0.1937 -0.0094 0.0161  0.0676  121 VAL   A N   
2462 C CA  . VAL   A 121 ? 0.1804 0.2218 0.1715 -0.0125 0.0196  0.0705  121 VAL   A CA  
2463 C C   . VAL   A 121 ? 0.1660 0.2000 0.1568 -0.0256 0.0194  0.0525  121 VAL   A C   
2464 O O   . VAL   A 121 ? 0.1725 0.2012 0.1792 -0.0314 0.0035  0.0395  121 VAL   A O   
2465 C CB  . VAL   A 121 ? 0.2213 0.2604 0.2093 -0.0008 0.0278  0.0836  121 VAL   A CB  
2466 C CG1 . VAL   A 121 ? 0.2226 0.2747 0.2178 0.0087  0.0329  0.0733  121 VAL   A CG1 
2467 C CG2 . VAL   A 121 ? 0.2447 0.2819 0.2453 -0.0106 0.0152  0.0713  121 VAL   A CG2 
2477 N N   . LEU   A 122 ? 0.1543 0.1792 0.1765 -0.0284 0.0075  0.0403  122 LEU   A N   
2478 C CA  . LEU   A 122 ? 0.1660 0.1574 0.1777 -0.0226 0.0290  0.0391  122 LEU   A CA  
2479 C C   . LEU   A 122 ? 0.1599 0.1557 0.1750 -0.0297 0.0114  0.0321  122 LEU   A C   
2480 O O   . LEU   A 122 ? 0.1607 0.1636 0.2057 -0.0338 0.0087  0.0319  122 LEU   A O   
2481 C CB  . LEU   A 122 ? 0.1831 0.1614 0.2082 -0.0138 0.0179  0.0496  122 LEU   A CB  
2482 C CG  . LEU   A 122 ? 0.1840 0.1651 0.2068 -0.0158 0.0266  0.0271  122 LEU   A CG  
2483 C CD1 . LEU   A 122 ? 0.2044 0.1687 0.1979 -0.0280 0.0246  0.0259  122 LEU   A CD1 
2484 C CD2 . LEU   A 122 ? 0.1773 0.1610 0.2048 -0.0146 0.0322  0.0269  122 LEU   A CD2 
2496 N N   A LEU   A 123 ? 0.1570 0.1609 0.1773 -0.0272 0.0104  0.0326  123 LEU   A N   
2497 N N   B LEU   A 123 ? 0.1583 0.1558 0.1643 -0.0308 0.0071  0.0172  123 LEU   A N   
2498 C CA  A LEU   A 123 ? 0.1491 0.1613 0.1621 -0.0249 0.0152  0.0384  123 LEU   A CA  
2499 C CA  B LEU   A 123 ? 0.1557 0.1515 0.1533 -0.0288 0.0083  0.0082  123 LEU   A CA  
2500 C C   A LEU   A 123 ? 0.1420 0.1495 0.1711 -0.0194 0.0083  0.0356  123 LEU   A C   
2501 C C   B LEU   A 123 ? 0.1540 0.1409 0.1395 -0.0202 0.0168  0.0099  123 LEU   A C   
2502 O O   A LEU   A 123 ? 0.1283 0.1405 0.1829 -0.0216 0.0104  0.0215  123 LEU   A O   
2503 O O   B LEU   A 123 ? 0.1504 0.1366 0.1257 -0.0140 0.0166  -0.0031 123 LEU   A O   
2504 C CB  A LEU   A 123 ? 0.1621 0.1756 0.1625 -0.0251 0.0369  0.0432  123 LEU   A CB  
2505 C CB  B LEU   A 123 ? 0.1642 0.1609 0.1629 -0.0324 0.0031  0.0024  123 LEU   A CB  
2506 C CG  A LEU   A 123 ? 0.1611 0.1896 0.1724 -0.0174 0.0365  0.0247  123 LEU   A CG  
2507 C CG  B LEU   A 123 ? 0.1648 0.1705 0.1681 -0.0309 -0.0043 -0.0043 123 LEU   A CG  
2508 C CD1 A LEU   A 123 ? 0.1651 0.1999 0.1791 -0.0052 0.0375  0.0088  123 LEU   A CD1 
2509 C CD1 B LEU   A 123 ? 0.1698 0.1769 0.1766 -0.0236 -0.0024 -0.0149 123 LEU   A CD1 
2510 C CD2 A LEU   A 123 ? 0.1715 0.1928 0.1675 -0.0160 0.0267  0.0327  123 LEU   A CD2 
2511 C CD2 B LEU   A 123 ? 0.1736 0.1747 0.1739 -0.0308 -0.0165 -0.0071 123 LEU   A CD2 
2534 N N   A ALA   A 124 ? 0.1367 0.1394 0.1545 -0.0159 0.0035  0.0356  124 ALA   A N   
2535 N N   B ALA   A 124 ? 0.1517 0.1283 0.1492 -0.0208 0.0221  0.0043  124 ALA   A N   
2536 C CA  A ALA   A 124 ? 0.1299 0.1351 0.1380 -0.0028 -0.0019 0.0361  124 ALA   A CA  
2537 C CA  B ALA   A 124 ? 0.1528 0.1340 0.1614 -0.0263 0.0170  0.0156  124 ALA   A CA  
2538 C C   A ALA   A 124 ? 0.1237 0.1367 0.1445 -0.0060 0.0079  0.0382  124 ALA   A C   
2539 C C   B ALA   A 124 ? 0.1471 0.1270 0.1616 -0.0237 0.0149  0.0189  124 ALA   A C   
2540 O O   A ALA   A 124 ? 0.1274 0.1460 0.1688 -0.0045 0.0299  0.0363  124 ALA   A O   
2541 O O   B ALA   A 124 ? 0.1456 0.1311 0.1748 -0.0202 0.0194  0.0143  124 ALA   A O   
2542 C CB  A ALA   A 124 ? 0.1276 0.1353 0.1483 0.0017  -0.0024 0.0277  124 ALA   A CB  
2543 C CB  B ALA   A 124 ? 0.1581 0.1359 0.1774 -0.0298 0.0213  0.0199  124 ALA   A CB  
2554 N N   A PRO   A 125 ? 0.1221 0.1421 0.1574 -0.0107 0.0046  0.0372  125 PRO   A N   
2555 N N   B PRO   A 125 ? 0.1354 0.1195 0.1428 -0.0116 0.0066  0.0282  125 PRO   A N   
2556 C CA  A PRO   A 125 ? 0.1297 0.1484 0.1606 -0.0076 -0.0076 0.0240  125 PRO   A CA  
2557 C CA  B PRO   A 125 ? 0.1377 0.1298 0.1481 -0.0071 0.0032  0.0222  125 PRO   A CA  
2558 C C   A PRO   A 125 ? 0.1200 0.1414 0.1643 -0.0088 0.0027  0.0275  125 PRO   A C   
2559 C C   B PRO   A 125 ? 0.1479 0.1474 0.1680 -0.0043 0.0067  0.0068  125 PRO   A C   
2560 O O   A PRO   A 125 ? 0.1288 0.1374 0.1794 -0.0099 -0.0070 0.0251  125 PRO   A O   
2561 O O   B PRO   A 125 ? 0.1506 0.1500 0.1808 -0.0070 0.0052  0.0043  125 PRO   A O   
2562 C CB  A PRO   A 125 ? 0.1424 0.1531 0.1636 -0.0172 -0.0031 0.0225  125 PRO   A CB  
2563 C CB  B PRO   A 125 ? 0.1282 0.1164 0.1548 -0.0096 0.0051  0.0276  125 PRO   A CB  
2564 C CG  A PRO   A 125 ? 0.1460 0.1538 0.1566 -0.0161 -0.0100 0.0356  125 PRO   A CG  
2565 C CG  B PRO   A 125 ? 0.1204 0.1101 0.1567 -0.0046 0.0062  0.0282  125 PRO   A CG  
2566 C CD  A PRO   A 125 ? 0.1303 0.1482 0.1609 -0.0108 0.0056  0.0375  125 PRO   A CD  
2567 C CD  B PRO   A 125 ? 0.1193 0.1045 0.1525 -0.0063 0.0128  0.0264  125 PRO   A CD  
2582 N N   A LEU   A 126 ? 0.1130 0.1388 0.1762 -0.0023 0.0144  0.0196  126 LEU   A N   
2583 N N   B LEU   A 126 ? 0.1587 0.1583 0.1801 -0.0022 0.0016  -0.0005 126 LEU   A N   
2584 C CA  A LEU   A 126 ? 0.1261 0.1312 0.1737 -0.0065 0.0119  0.0227  126 LEU   A CA  
2585 C CA  B LEU   A 126 ? 0.1661 0.1535 0.1866 0.0014  0.0013  0.0097  126 LEU   A CA  
2586 C C   A LEU   A 126 ? 0.1397 0.1231 0.1645 -0.0095 -0.0021 0.0014  126 LEU   A C   
2587 C C   B LEU   A 126 ? 0.1596 0.1530 0.1924 0.0125  0.0074  0.0042  126 LEU   A C   
2588 O O   A LEU   A 126 ? 0.1535 0.1157 0.1616 -0.0110 0.0027  0.0055  126 LEU   A O   
2589 O O   B LEU   A 126 ? 0.1725 0.1439 0.2270 0.0048  0.0375  0.0002  126 LEU   A O   
2590 C CB  A LEU   A 126 ? 0.1318 0.1358 0.1683 -0.0048 0.0096  0.0131  126 LEU   A CB  
2591 C CB  B LEU   A 126 ? 0.1852 0.1696 0.2089 -0.0081 -0.0089 0.0090  126 LEU   A CB  
2592 C CG  A LEU   A 126 ? 0.1338 0.1623 0.1633 -0.0125 0.0110  0.0149  126 LEU   A CG  
2593 C CG  B LEU   A 126 ? 0.1959 0.1813 0.2380 -0.0087 -0.0144 0.0243  126 LEU   A CG  
2594 C CD1 A LEU   A 126 ? 0.1331 0.1713 0.1715 -0.0173 0.0055  0.0226  126 LEU   A CD1 
2595 C CD1 B LEU   A 126 ? 0.1995 0.1875 0.2523 -0.0041 -0.0197 0.0277  126 LEU   A CD1 
2596 C CD2 A LEU   A 126 ? 0.1461 0.1541 0.1431 -0.0192 0.0094  0.0248  126 LEU   A CD2 
2597 C CD2 B LEU   A 126 ? 0.2001 0.1832 0.2479 -0.0126 -0.0144 0.0302  126 LEU   A CD2 
2620 N N   A LEU   A 127 ? 0.1355 0.1362 0.1643 -0.0113 0.0105  0.0125  127 LEU   A N   
2621 N N   B LEU   A 127 ? 0.1480 0.1620 0.1757 0.0253  0.0011  0.0148  127 LEU   A N   
2622 C CA  A LEU   A 127 ? 0.1398 0.1399 0.1570 -0.0124 0.0116  0.0106  127 LEU   A CA  
2623 C CA  B LEU   A 127 ? 0.1512 0.1731 0.1720 0.0232  -0.0124 0.0231  127 LEU   A CA  
2624 C C   A LEU   A 127 ? 0.1403 0.1271 0.1549 -0.0153 -0.0041 0.0120  127 LEU   A C   
2625 C C   B LEU   A 127 ? 0.1594 0.1787 0.1802 0.0181  -0.0182 0.0122  127 LEU   A C   
2626 O O   A LEU   A 127 ? 0.1445 0.1275 0.1640 -0.0268 -0.0001 0.0088  127 LEU   A O   
2627 O O   B LEU   A 127 ? 0.1679 0.1777 0.1829 0.0149  -0.0130 0.0075  127 LEU   A O   
2628 C CB  A LEU   A 127 ? 0.1473 0.1496 0.1676 0.0066  0.0169  0.0038  127 LEU   A CB  
2629 C CB  B LEU   A 127 ? 0.1502 0.1798 0.1627 0.0245  -0.0155 0.0218  127 LEU   A CB  
2630 C CG  A LEU   A 127 ? 0.1534 0.1517 0.1817 0.0058  0.0058  0.0061  127 LEU   A CG  
2631 C CG  B LEU   A 127 ? 0.1464 0.1852 0.1646 0.0246  -0.0215 0.0226  127 LEU   A CG  
2632 C CD1 A LEU   A 127 ? 0.1550 0.1433 0.1875 -0.0073 0.0078  -0.0047 127 LEU   A CD1 
2633 C CD1 B LEU   A 127 ? 0.1464 0.1856 0.1782 0.0302  -0.0086 0.0293  127 LEU   A CD1 
2634 C CD2 A LEU   A 127 ? 0.1623 0.1537 0.2070 0.0139  -0.0032 0.0111  127 LEU   A CD2 
2635 C CD2 B LEU   A 127 ? 0.1512 0.1961 0.1666 0.0205  -0.0282 0.0151  127 LEU   A CD2 
2658 N N   A SER   A 128 ? 0.1423 0.1275 0.1516 -0.0154 -0.0086 0.0118  128 SER   A N   
2659 N N   B SER   A 128 ? 0.1605 0.1891 0.1863 0.0095  -0.0234 0.0144  128 SER   A N   
2660 C CA  A SER   A 128 ? 0.1496 0.1355 0.1448 -0.0077 0.0007  0.0129  128 SER   A CA  
2661 C CA  B SER   A 128 ? 0.1648 0.2022 0.1880 0.0095  -0.0253 0.0139  128 SER   A CA  
2662 C C   A SER   A 128 ? 0.1501 0.1325 0.1225 -0.0064 -0.0003 0.0168  128 SER   A C   
2663 C C   B SER   A 128 ? 0.1933 0.2153 0.2051 0.0110  -0.0320 0.0194  128 SER   A C   
2664 O O   A SER   A 128 ? 0.1708 0.1514 0.1427 -0.0009 0.0011  0.0096  128 SER   A O   
2665 O O   B SER   A 128 ? 0.1905 0.2099 0.2094 0.0084  -0.0271 0.0187  128 SER   A O   
2666 C CB  A SER   A 128 ? 0.1558 0.1432 0.1459 -0.0100 0.0098  0.0121  128 SER   A CB  
2667 C CB  B SER   A 128 ? 0.1473 0.2009 0.1701 0.0050  -0.0273 0.0154  128 SER   A CB  
2668 O OG  A SER   A 128 ? 0.1641 0.1550 0.1455 -0.0101 0.0175  0.0148  128 SER   A OG  
2669 O OG  B SER   A 128 ? 0.1319 0.2044 0.1680 -0.0035 -0.0255 0.0120  128 SER   A OG  
2680 N N   A ALA   A 129 ? 0.1375 0.1343 0.1229 -0.0035 0.0003  0.0305  129 ALA   A N   
2681 N N   B ALA   A 129 ? 0.2254 0.2403 0.2192 0.0202  -0.0397 0.0279  129 ALA   A N   
2682 C CA  A ALA   A 129 ? 0.1262 0.1368 0.1406 0.0015  0.0030  0.0376  129 ALA   A CA  
2683 C CA  B ALA   A 129 ? 0.2596 0.2640 0.2378 0.0303  -0.0462 0.0244  129 ALA   A CA  
2684 C C   A ALA   A 129 ? 0.1324 0.1405 0.1234 0.0037  0.0006  0.0103  129 ALA   A C   
2685 C C   B ALA   A 129 ? 0.2829 0.2757 0.2570 0.0413  -0.0517 0.0199  129 ALA   A C   
2686 O O   A ALA   A 129 ? 0.1327 0.1435 0.1234 -0.0033 0.0005  0.0165  129 ALA   A O   
2687 O O   B ALA   A 129 ? 0.2921 0.2774 0.2688 0.0426  -0.0457 0.0119  129 ALA   A O   
2688 C CB  A ALA   A 129 ? 0.1279 0.1410 0.1893 0.0020  0.0059  0.0463  129 ALA   A CB  
2689 C CB  B ALA   A 129 ? 0.2670 0.2717 0.2463 0.0273  -0.0441 0.0193  129 ALA   A CB  
2700 N N   A GLY   A 130 ? 0.1359 0.1337 0.1446 -0.0051 -0.0001 0.0153  130 GLY   A N   
2701 N N   B GLY   A 130 ? 0.2975 0.2895 0.2760 0.0468  -0.0545 0.0166  130 GLY   A N   
2702 C CA  A GLY   A 130 ? 0.1536 0.1316 0.1720 -0.0013 0.0045  0.0091  130 GLY   A CA  
2703 C CA  B GLY   A 130 ? 0.3117 0.2974 0.2846 0.0476  -0.0541 0.0135  130 GLY   A CA  
2704 C C   A GLY   A 130 ? 0.1550 0.1275 0.1723 0.0006  -0.0041 0.0024  130 GLY   A C   
2705 C C   B GLY   A 130 ? 0.3218 0.3020 0.2888 0.0497  -0.0593 0.0141  130 GLY   A C   
2706 O O   A GLY   A 130 ? 0.1471 0.1210 0.1603 -0.0063 -0.0198 0.0125  130 GLY   A O   
2707 O O   B GLY   A 130 ? 0.3253 0.3051 0.2727 0.0552  -0.0624 0.0077  130 GLY   A O   
2714 N N   A ILE   A 131 ? 0.1703 0.1207 0.1606 -0.0036 -0.0104 0.0153  131 ILE   A N   
2715 N N   B ILE   A 131 ? 0.3289 0.3025 0.3106 0.0440  -0.0597 0.0194  131 ILE   A N   
2716 C CA  A ILE   A 131 ? 0.1842 0.1360 0.1311 -0.0134 -0.0148 0.0140  131 ILE   A CA  
2717 C CA  B ILE   A 131 ? 0.3350 0.3034 0.3340 0.0367  -0.0558 0.0234  131 ILE   A CA  
2718 C C   A ILE   A 131 ? 0.1618 0.1375 0.1262 -0.0198 -0.0160 0.0264  131 ILE   A C   
2719 C C   B ILE   A 131 ? 0.3278 0.2981 0.3308 0.0332  -0.0559 0.0311  131 ILE   A C   
2720 O O   A ILE   A 131 ? 0.1653 0.1344 0.1485 -0.0148 -0.0166 0.0283  131 ILE   A O   
2721 O O   B ILE   A 131 ? 0.3305 0.2990 0.3397 0.0338  -0.0407 0.0317  131 ILE   A O   
2722 C CB  A ILE   A 131 ? 0.2144 0.1552 0.1375 -0.0303 -0.0224 -0.0038 131 ILE   A CB  
2723 C CB  B ILE   A 131 ? 0.3483 0.3114 0.3594 0.0337  -0.0502 0.0208  131 ILE   A CB  
2724 C CG1 A ILE   A 131 ? 0.2237 0.1818 0.1518 -0.0451 -0.0297 -0.0134 131 ILE   A CG1 
2725 C CG1 B ILE   A 131 ? 0.3534 0.3151 0.3765 0.0313  -0.0465 0.0198  131 ILE   A CG1 
2726 C CG2 A ILE   A 131 ? 0.2296 0.1506 0.1621 -0.0217 -0.0018 -0.0029 131 ILE   A CG2 
2727 C CG2 B ILE   A 131 ? 0.3529 0.3154 0.3637 0.0332  -0.0501 0.0204  131 ILE   A CG2 
2728 C CD1 A ILE   A 131 ? 0.2328 0.1964 0.1814 -0.0492 -0.0234 -0.0220 131 ILE   A CD1 
2729 C CD1 B ILE   A 131 ? 0.3551 0.3178 0.3853 0.0320  -0.0436 0.0183  131 ILE   A CD1 
2752 N N   A PHE   A 132 ? 0.1553 0.1371 0.1223 -0.0190 -0.0179 0.0332  132 PHE   A N   
2753 N N   B PHE   A 132 ? 0.3185 0.2920 0.3243 0.0286  -0.0685 0.0353  132 PHE   A N   
2754 C CA  A PHE   A 132 ? 0.1587 0.1488 0.1062 -0.0268 -0.0116 0.0113  132 PHE   A CA  
2755 C CA  B PHE   A 132 ? 0.3099 0.2847 0.3191 0.0202  -0.0717 0.0381  132 PHE   A CA  
2756 C C   A PHE   A 132 ? 0.1616 0.1666 0.1233 -0.0177 -0.0133 0.0096  132 PHE   A C   
2757 C C   B PHE   A 132 ? 0.3020 0.2833 0.2964 0.0211  -0.0675 0.0389  132 PHE   A C   
2758 O O   A PHE   A 132 ? 0.1635 0.1821 0.1276 -0.0190 -0.0120 0.0008  132 PHE   A O   
2759 O O   B PHE   A 132 ? 0.3027 0.2845 0.2890 0.0225  -0.0653 0.0389  132 PHE   A O   
2760 C CB  A PHE   A 132 ? 0.1562 0.1366 0.1114 -0.0221 -0.0083 0.0189  132 PHE   A CB  
2761 C CB  B PHE   A 132 ? 0.3078 0.2822 0.3425 0.0136  -0.0825 0.0357  132 PHE   A CB  
2762 C CG  A PHE   A 132 ? 0.1523 0.1357 0.1135 -0.0107 -0.0127 0.0182  132 PHE   A CG  
2763 C CG  B PHE   A 132 ? 0.3106 0.2826 0.3717 0.0047  -0.0823 0.0350  132 PHE   A CG  
2764 C CD1 A PHE   A 132 ? 0.1533 0.1462 0.1393 0.0023  -0.0116 -0.0008 132 PHE   A CD1 
2765 C CD1 B PHE   A 132 ? 0.3139 0.2855 0.3837 0.0003  -0.0781 0.0318  132 PHE   A CD1 
2766 C CD2 A PHE   A 132 ? 0.1567 0.1404 0.1304 -0.0080 -0.0092 0.0111  132 PHE   A CD2 
2767 C CD2 B PHE   A 132 ? 0.3099 0.2820 0.3763 -0.0003 -0.0874 0.0350  132 PHE   A CD2 
2768 C CE1 A PHE   A 132 ? 0.1536 0.1521 0.1400 0.0021  -0.0257 0.0052  132 PHE   A CE1 
2769 C CE1 B PHE   A 132 ? 0.3150 0.2854 0.3879 -0.0028 -0.0804 0.0251  132 PHE   A CE1 
2770 C CE2 A PHE   A 132 ? 0.1540 0.1476 0.1482 0.0020  -0.0189 0.0103  132 PHE   A CE2 
2771 C CE2 B PHE   A 132 ? 0.3109 0.2823 0.3831 -0.0049 -0.0881 0.0307  132 PHE   A CE2 
2772 C CZ  A PHE   A 132 ? 0.1523 0.1462 0.1437 -0.0057 -0.0333 0.0087  132 PHE   A CZ  
2773 C CZ  B PHE   A 132 ? 0.3124 0.2836 0.3851 -0.0055 -0.0891 0.0256  132 PHE   A CZ  
2792 N N   A GLY   A 133 ? 0.1614 0.1686 0.1178 -0.0209 -0.0243 0.0284  133 GLY   A N   
2793 N N   B GLY   A 133 ? 0.2963 0.2787 0.2902 0.0195  -0.0567 0.0372  133 GLY   A N   
2794 C CA  A GLY   A 133 ? 0.1727 0.1794 0.1366 -0.0225 -0.0246 0.0173  133 GLY   A CA  
2795 C CA  B GLY   A 133 ? 0.2889 0.2759 0.2832 0.0175  -0.0576 0.0278  133 GLY   A CA  
2796 C C   A GLY   A 133 ? 0.1775 0.1878 0.1385 -0.0261 -0.0406 -0.0025 133 GLY   A C   
2797 C C   B GLY   A 133 ? 0.2796 0.2737 0.2828 0.0119  -0.0584 0.0164  133 GLY   A C   
2798 O O   A GLY   A 133 ? 0.1930 0.1970 0.1479 -0.0192 -0.0547 -0.0174 133 GLY   A O   
2799 O O   B GLY   A 133 ? 0.2849 0.2821 0.2978 0.0134  -0.0607 0.0169  133 GLY   A O   
2806 N N   A ALA   A 134 ? 0.1794 0.1817 0.1491 -0.0286 -0.0302 -0.0120 134 ALA   A N   
2807 N N   B ALA   A 134 ? 0.2681 0.2632 0.2677 0.0048  -0.0551 0.0138  134 ALA   A N   
2808 C CA  A ALA   A 134 ? 0.1790 0.1825 0.1741 -0.0201 -0.0256 -0.0036 134 ALA   A CA  
2809 C CA  B ALA   A 134 ? 0.2587 0.2565 0.2546 -0.0043 -0.0533 0.0103  134 ALA   A CA  
2810 C C   A ALA   A 134 ? 0.1826 0.1881 0.1858 -0.0125 -0.0296 -0.0047 134 ALA   A C   
2811 C C   B ALA   A 134 ? 0.2548 0.2602 0.2575 -0.0078 -0.0503 0.0085  134 ALA   A C   
2812 O O   A ALA   A 134 ? 0.1889 0.1854 0.2096 0.0044  -0.0102 0.0036  134 ALA   A O   
2813 O O   B ALA   A 134 ? 0.2534 0.2621 0.2708 -0.0032 -0.0418 0.0119  134 ALA   A O   
2814 C CB  A ALA   A 134 ? 0.1767 0.1770 0.2010 -0.0190 -0.0332 -0.0063 134 ALA   A CB  
2815 C CB  B ALA   A 134 ? 0.2586 0.2496 0.2576 -0.0068 -0.0520 0.0083  134 ALA   A CB  
2826 N N   A ASP   A 135 ? 0.1906 0.1948 0.1970 -0.0234 -0.0354 0.0134  135 ASP   A N   
2827 N N   B ASP   A 135 ? 0.2521 0.2597 0.2504 -0.0116 -0.0548 0.0154  135 ASP   A N   
2828 C CA  A ASP   A 135 ? 0.1858 0.2076 0.2237 -0.0345 -0.0506 0.0269  135 ASP   A CA  
2829 C CA  B ASP   A 135 ? 0.2472 0.2627 0.2549 -0.0126 -0.0555 0.0220  135 ASP   A CA  
2830 C C   A ASP   A 135 ? 0.1690 0.1895 0.2102 -0.0246 -0.0349 0.0304  135 ASP   A C   
2831 C C   B ASP   A 135 ? 0.2340 0.2524 0.2318 -0.0081 -0.0433 0.0301  135 ASP   A C   
2832 O O   A ASP   A 135 ? 0.1620 0.1716 0.2011 -0.0341 -0.0314 0.0317  135 ASP   A O   
2833 O O   B ASP   A 135 ? 0.2302 0.2491 0.2292 -0.0096 -0.0415 0.0309  135 ASP   A O   
2834 C CB  A ASP   A 135 ? 0.2033 0.2383 0.2587 -0.0567 -0.0781 0.0285  135 ASP   A CB  
2835 C CB  B ASP   A 135 ? 0.2581 0.2755 0.2996 -0.0205 -0.0618 0.0195  135 ASP   A CB  
2836 C CG  A ASP   A 135 ? 0.2174 0.2620 0.3002 -0.0728 -0.0800 0.0322  135 ASP   A CG  
2837 C CG  B ASP   A 135 ? 0.2670 0.2852 0.3428 -0.0236 -0.0634 0.0190  135 ASP   A CG  
2838 O OD1 A ASP   A 135 ? 0.2092 0.2699 0.2951 -0.0814 -0.0884 0.0642  135 ASP   A OD1 
2839 O OD1 B ASP   A 135 ? 0.2759 0.2896 0.3669 -0.0217 -0.0535 0.0218  135 ASP   A OD1 
2840 O OD2 A ASP   A 135 ? 0.2491 0.2816 0.3556 -0.0677 -0.0476 0.0259  135 ASP   A OD2 
2841 O OD2 B ASP   A 135 ? 0.2634 0.2889 0.3566 -0.0331 -0.0753 0.0223  135 ASP   A OD2 
2850 N N   A PRO   A 136 ? 0.1611 0.1822 0.2171 -0.0050 -0.0217 0.0366  136 PRO   A N   
2851 N N   B PRO   A 136 ? 0.2274 0.2437 0.2301 0.0019  -0.0296 0.0400  136 PRO   A N   
2852 C CA  A PRO   A 136 ? 0.1441 0.1827 0.2330 -0.0056 -0.0072 0.0197  136 PRO   A CA  
2853 C CA  B PRO   A 136 ? 0.2185 0.2362 0.2289 0.0025  -0.0275 0.0318  136 PRO   A CA  
2854 C C   A PRO   A 136 ? 0.1235 0.1781 0.2144 -0.0055 -0.0021 0.0150  136 PRO   A C   
2855 C C   B PRO   A 136 ? 0.2094 0.2263 0.2280 0.0064  -0.0276 0.0240  136 PRO   A C   
2856 O O   A PRO   A 136 ? 0.1199 0.1677 0.1877 -0.0094 0.0080  0.0029  136 PRO   A O   
2857 O O   B PRO   A 136 ? 0.2058 0.2272 0.2196 0.0049  -0.0265 0.0272  136 PRO   A O   
2858 C CB  A PRO   A 136 ? 0.1610 0.1824 0.2579 0.0026  -0.0019 0.0190  136 PRO   A CB  
2859 C CB  B PRO   A 136 ? 0.2234 0.2369 0.2346 0.0048  -0.0208 0.0376  136 PRO   A CB  
2860 C CG  A PRO   A 136 ? 0.1634 0.1824 0.2572 0.0009  -0.0044 0.0351  136 PRO   A CG  
2861 C CG  B PRO   A 136 ? 0.2249 0.2380 0.2371 0.0075  -0.0192 0.0440  136 PRO   A CG  
2862 C CD  A PRO   A 136 ? 0.1680 0.1857 0.2456 0.0019  -0.0127 0.0406  136 PRO   A CD  
2863 C CD  B PRO   A 136 ? 0.2280 0.2426 0.2386 0.0049  -0.0218 0.0435  136 PRO   A CD  
2878 N N   A ILE   A 137 ? 0.1248 0.1847 0.2297 -0.0061 -0.0073 0.0228  137 ILE   A N   
2879 N N   B ILE   A 137 ? 0.2102 0.2224 0.2391 0.0072  -0.0242 0.0161  137 ILE   A N   
2880 C CA  A ILE   A 137 ? 0.1366 0.1962 0.2302 -0.0186 -0.0188 0.0244  137 ILE   A CA  
2881 C CA  B ILE   A 137 ? 0.2165 0.2276 0.2559 0.0023  -0.0237 0.0089  137 ILE   A CA  
2882 C C   A ILE   A 137 ? 0.1392 0.1853 0.1922 -0.0279 -0.0170 0.0220  137 ILE   A C   
2883 C C   B ILE   A 137 ? 0.2133 0.2224 0.2335 -0.0010 -0.0208 -0.0043 137 ILE   A C   
2884 O O   A ILE   A 137 ? 0.1429 0.1719 0.1891 -0.0321 -0.0046 0.0027  137 ILE   A O   
2885 O O   B ILE   A 137 ? 0.2173 0.2128 0.2349 -0.0011 -0.0122 -0.0089 137 ILE   A O   
2886 C CB  A ILE   A 137 ? 0.1427 0.2169 0.2642 -0.0208 -0.0254 0.0300  137 ILE   A CB  
2887 C CB  B ILE   A 137 ? 0.2311 0.2413 0.2942 0.0003  -0.0272 0.0126  137 ILE   A CB  
2888 C CG1 A ILE   A 137 ? 0.1454 0.2423 0.2937 -0.0202 -0.0233 0.0362  137 ILE   A CG1 
2889 C CG1 B ILE   A 137 ? 0.2463 0.2588 0.3193 0.0079  -0.0321 0.0141  137 ILE   A CG1 
2890 C CG2 A ILE   A 137 ? 0.1557 0.2187 0.2544 -0.0254 -0.0278 0.0239  137 ILE   A CG2 
2891 C CG2 B ILE   A 137 ? 0.2327 0.2419 0.2997 -0.0049 -0.0206 0.0141  137 ILE   A CG2 
2892 C CD1 A ILE   A 137 ? 0.1546 0.2527 0.3057 -0.0130 -0.0268 0.0302  137 ILE   A CD1 
2893 C CD1 B ILE   A 137 ? 0.2568 0.2649 0.3307 0.0111  -0.0307 0.0147  137 ILE   A CD1 
2916 N N   A HIS   A 138 ? 0.1444 0.2051 0.1838 -0.0171 -0.0185 0.0310  138 HIS   A N   
2917 N N   B HIS   A 138 ? 0.2096 0.2311 0.2237 -0.0032 -0.0200 -0.0111 138 HIS   A N   
2918 C CA  A HIS   A 138 ? 0.1452 0.2030 0.1636 -0.0184 -0.0146 0.0226  138 HIS   A CA  
2919 C CA  B HIS   A 138 ? 0.2038 0.2322 0.2119 -0.0094 -0.0106 -0.0134 138 HIS   A CA  
2920 C C   A HIS   A 138 ? 0.1335 0.1853 0.1561 -0.0116 -0.0101 0.0124  138 HIS   A C   
2921 C C   B HIS   A 138 ? 0.1854 0.2173 0.1897 -0.0114 -0.0075 -0.0107 138 HIS   A C   
2922 O O   A HIS   A 138 ? 0.1478 0.1824 0.1590 -0.0118 -0.0172 0.0058  138 HIS   A O   
2923 O O   B HIS   A 138 ? 0.1880 0.2173 0.1822 -0.0190 -0.0033 -0.0185 138 HIS   A O   
2924 C CB  A HIS   A 138 ? 0.1663 0.2218 0.1663 -0.0187 -0.0187 0.0256  138 HIS   A CB  
2925 C CB  B HIS   A 138 ? 0.2192 0.2487 0.2304 -0.0125 -0.0177 -0.0212 138 HIS   A CB  
2926 C CG  A HIS   A 138 ? 0.1820 0.2301 0.1767 -0.0354 -0.0079 0.0189  138 HIS   A CG  
2927 C CG  B HIS   A 138 ? 0.2278 0.2603 0.2586 -0.0212 -0.0153 -0.0330 138 HIS   A CG  
2928 N ND1 A HIS   A 138 ? 0.1850 0.2390 0.2019 -0.0476 0.0007  0.0061  138 HIS   A ND1 
2929 N ND1 B HIS   A 138 ? 0.2316 0.2679 0.2752 -0.0239 -0.0101 -0.0332 138 HIS   A ND1 
2930 C CD2 A HIS   A 138 ? 0.1848 0.2343 0.1805 -0.0352 -0.0085 0.0272  138 HIS   A CD2 
2931 C CD2 B HIS   A 138 ? 0.2289 0.2627 0.2741 -0.0201 -0.0181 -0.0335 138 HIS   A CD2 
2932 C CE1 A HIS   A 138 ? 0.1913 0.2387 0.2134 -0.0372 -0.0007 0.0056  138 HIS   A CE1 
2933 C CE1 B HIS   A 138 ? 0.2309 0.2671 0.2812 -0.0233 -0.0108 -0.0339 138 HIS   A CE1 
2934 N NE2 A HIS   A 138 ? 0.1918 0.2367 0.1912 -0.0376 -0.0013 0.0111  138 HIS   A NE2 
2935 N NE2 B HIS   A 138 ? 0.2299 0.2640 0.2809 -0.0240 -0.0175 -0.0381 138 HIS   A NE2 
2950 N N   A SER   A 139 ? 0.1347 0.1701 0.1522 -0.0087 -0.0099 0.0108  139 SER   A N   
2951 N N   B SER   A 139 ? 0.1680 0.1934 0.1700 -0.0073 -0.0016 -0.0027 139 SER   A N   
2952 C CA  A SER   A 139 ? 0.1334 0.1630 0.1509 -0.0053 0.0018  0.0079  139 SER   A CA  
2953 C CA  B SER   A 139 ? 0.1587 0.1696 0.1602 -0.0086 0.0015  0.0071  139 SER   A CA  
2954 C C   A SER   A 139 ? 0.1292 0.1543 0.1520 -0.0047 0.0085  -0.0028 139 SER   A C   
2955 C C   B SER   A 139 ? 0.1511 0.1637 0.1733 -0.0155 -0.0024 0.0098  139 SER   A C   
2956 O O   A SER   A 139 ? 0.1298 0.1427 0.1646 -0.0094 -0.0006 0.0052  139 SER   A O   
2957 O O   B SER   A 139 ? 0.1401 0.1592 0.1695 -0.0196 0.0023  -0.0001 139 SER   A O   
2958 C CB  A SER   A 139 ? 0.1297 0.1565 0.1773 -0.0035 -0.0020 0.0071  139 SER   A CB  
2959 C CB  B SER   A 139 ? 0.1446 0.1510 0.1464 -0.0018 0.0293  0.0030  139 SER   A CB  
2960 O OG  A SER   A 139 ? 0.1360 0.1514 0.1932 -0.0030 -0.0114 0.0007  139 SER   A OG  
2961 O OG  B SER   A 139 ? 0.1367 0.1347 0.1393 0.0065  0.0253  0.0023  139 SER   A OG  
2972 N N   A LEU   A 140 ? 0.1252 0.1570 0.1412 -0.0034 0.0060  0.0095  140 LEU   A N   
2973 N N   B LEU   A 140 ? 0.1496 0.1648 0.1753 -0.0134 -0.0045 0.0208  140 LEU   A N   
2974 C CA  A LEU   A 140 ? 0.1299 0.1494 0.1492 -0.0048 0.0124  0.0076  140 LEU   A CA  
2975 C CA  B LEU   A 140 ? 0.1519 0.1692 0.1849 -0.0214 -0.0068 0.0138  140 LEU   A CA  
2976 C C   A LEU   A 140 ? 0.1301 0.1600 0.1640 -0.0109 0.0077  0.0176  140 LEU   A C   
2977 C C   B LEU   A 140 ? 0.1516 0.1730 0.1943 -0.0223 -0.0045 0.0007  140 LEU   A C   
2978 O O   A LEU   A 140 ? 0.1353 0.1588 0.1715 -0.0024 0.0002  0.0316  140 LEU   A O   
2979 O O   B LEU   A 140 ? 0.1533 0.1696 0.2051 -0.0213 0.0036  0.0084  140 LEU   A O   
2980 C CB  A LEU   A 140 ? 0.1316 0.1561 0.1480 -0.0074 0.0084  0.0126  140 LEU   A CB  
2981 C CB  B LEU   A 140 ? 0.1567 0.1778 0.1956 -0.0217 0.0008  0.0189  140 LEU   A CB  
2982 C CG  A LEU   A 140 ? 0.1378 0.1654 0.1694 -0.0192 -0.0022 0.0313  140 LEU   A CG  
2983 C CG  B LEU   A 140 ? 0.1588 0.1862 0.2027 -0.0247 0.0078  0.0330  140 LEU   A CG  
2984 C CD1 A LEU   A 140 ? 0.1372 0.1620 0.1777 -0.0093 -0.0086 0.0462  140 LEU   A CD1 
2985 C CD1 B LEU   A 140 ? 0.1667 0.1839 0.2052 -0.0198 0.0121  0.0428  140 LEU   A CD1 
2986 C CD2 A LEU   A 140 ? 0.1456 0.1841 0.1659 -0.0153 -0.0015 0.0291  140 LEU   A CD2 
2987 C CD2 B LEU   A 140 ? 0.1571 0.2001 0.1934 -0.0210 0.0110  0.0294  140 LEU   A CD2 
3010 N N   A ARG   A 141 ? 0.1389 0.1614 0.1688 -0.0156 0.0031  0.0111  141 ARG   A N   
3011 N N   B ARG   A 141 ? 0.1631 0.1736 0.2080 -0.0141 -0.0198 -0.0147 141 ARG   A N   
3012 C CA  A ARG   A 141 ? 0.1505 0.1659 0.1892 -0.0221 -0.0005 -0.0049 141 ARG   A CA  
3013 C CA  B ARG   A 141 ? 0.1862 0.1805 0.2286 -0.0118 -0.0180 -0.0286 141 ARG   A CA  
3014 C C   A ARG   A 141 ? 0.1493 0.1567 0.1712 -0.0226 0.0004  -0.0033 141 ARG   A C   
3015 C C   B ARG   A 141 ? 0.1768 0.1669 0.2134 -0.0104 -0.0105 -0.0248 141 ARG   A C   
3016 O O   A ARG   A 141 ? 0.1418 0.1514 0.1695 -0.0193 0.0081  -0.0144 141 ARG   A O   
3017 O O   B ARG   A 141 ? 0.1745 0.1527 0.2091 -0.0052 0.0004  -0.0435 141 ARG   A O   
3018 C CB  A ARG   A 141 ? 0.1593 0.1758 0.2026 -0.0333 0.0033  -0.0242 141 ARG   A CB  
3019 C CB  B ARG   A 141 ? 0.2153 0.2048 0.2692 -0.0117 -0.0220 -0.0393 141 ARG   A CB  
3020 C CG  A ARG   A 141 ? 0.1821 0.2031 0.2263 -0.0419 0.0021  -0.0198 141 ARG   A CG  
3021 C CG  B ARG   A 141 ? 0.2503 0.2318 0.3152 -0.0102 -0.0169 -0.0368 141 ARG   A CG  
3022 C CD  A ARG   A 141 ? 0.2056 0.2266 0.2555 -0.0460 0.0074  -0.0223 141 ARG   A CD  
3023 C CD  B ARG   A 141 ? 0.2783 0.2537 0.3525 -0.0131 -0.0143 -0.0324 141 ARG   A CD  
3024 N NE  A ARG   A 141 ? 0.2052 0.2436 0.2728 -0.0500 0.0009  -0.0179 141 ARG   A NE  
3025 N NE  B ARG   A 141 ? 0.3014 0.2693 0.3824 -0.0144 -0.0115 -0.0318 141 ARG   A NE  
3026 C CZ  A ARG   A 141 ? 0.2062 0.2588 0.2784 -0.0588 0.0072  -0.0142 141 ARG   A CZ  
3027 C CZ  B ARG   A 141 ? 0.3192 0.2796 0.4051 -0.0145 -0.0093 -0.0388 141 ARG   A CZ  
3028 N NH1 A ARG   A 141 ? 0.1974 0.2608 0.2736 -0.0676 0.0182  -0.0284 141 ARG   A NH1 
3029 N NH1 B ARG   A 141 ? 0.3258 0.2850 0.4168 -0.0169 -0.0088 -0.0372 141 ARG   A NH1 
3030 N NH2 A ARG   A 141 ? 0.2116 0.2662 0.2976 -0.0529 -0.0009 -0.0031 141 ARG   A NH2 
3031 N NH2 B ARG   A 141 ? 0.3255 0.2841 0.4123 -0.0120 -0.0072 -0.0428 141 ARG   A NH2 
3058 N N   A VAL   A 142 ? 0.1437 0.1593 0.1794 -0.0196 0.0026  0.0056  142 VAL   A N   
3059 N N   B VAL   A 142 ? 0.1646 0.1692 0.2106 -0.0092 -0.0078 -0.0099 142 VAL   A N   
3060 C CA  A VAL   A 142 ? 0.1433 0.1597 0.2027 -0.0167 0.0173  0.0037  142 VAL   A CA  
3061 C CA  B VAL   A 142 ? 0.1568 0.1692 0.2121 -0.0075 0.0046  -0.0007 142 VAL   A CA  
3062 C C   A VAL   A 142 ? 0.1287 0.1563 0.2076 -0.0180 0.0059  0.0048  142 VAL   A C   
3063 C C   B VAL   A 142 ? 0.1406 0.1611 0.2061 -0.0129 -0.0006 0.0024  142 VAL   A C   
3064 O O   A VAL   A 142 ? 0.1370 0.1592 0.2180 -0.0037 0.0088  0.0146  142 VAL   A O   
3065 O O   B VAL   A 142 ? 0.1469 0.1634 0.2095 -0.0054 -0.0009 0.0096  142 VAL   A O   
3066 C CB  A VAL   A 142 ? 0.1527 0.1622 0.2087 -0.0160 0.0160  -0.0013 142 VAL   A CB  
3067 C CB  B VAL   A 142 ? 0.1650 0.1768 0.2122 -0.0020 0.0058  0.0043  142 VAL   A CB  
3068 C CG1 A VAL   A 142 ? 0.1536 0.1598 0.2146 -0.0242 0.0194  0.0062  142 VAL   A CG1 
3069 C CG1 B VAL   A 142 ? 0.1660 0.1768 0.2141 -0.0051 0.0087  0.0093  142 VAL   A CG1 
3070 C CG2 A VAL   A 142 ? 0.1637 0.1734 0.2245 -0.0116 0.0166  -0.0042 142 VAL   A CG2 
3071 C CG2 B VAL   A 142 ? 0.1714 0.1850 0.2195 0.0034  0.0048  0.0087  142 VAL   A CG2 
3090 N N   . CYS   A 143 ? 0.1361 0.1520 0.1964 -0.0151 0.0015  0.0055  143 CYS   A N   
3091 C CA  . CYS   A 143 ? 0.1334 0.1532 0.2070 -0.0217 -0.0016 0.0172  143 CYS   A CA  
3092 C C   . CYS   A 143 ? 0.1347 0.1522 0.2117 -0.0224 -0.0028 0.0273  143 CYS   A C   
3093 O O   . CYS   A 143 ? 0.1373 0.1560 0.2216 -0.0115 0.0024  0.0347  143 CYS   A O   
3094 C CB  . CYS   A 143 ? 0.1396 0.1542 0.2191 -0.0169 0.0091  0.0256  143 CYS   A CB  
3095 S SG  . CYS   A 143 ? 0.1651 0.1646 0.1929 -0.0014 0.0070  0.0158  143 CYS   A SG  
3102 N N   . VAL   A 144 ? 0.1420 0.1537 0.2323 -0.0190 0.0046  0.0346  144 VAL   A N   
3103 C CA  . VAL   A 144 ? 0.1450 0.1636 0.2725 -0.0157 0.0129  0.0372  144 VAL   A CA  
3104 C C   . VAL   A 144 ? 0.1466 0.1612 0.2754 -0.0225 -0.0193 0.0272  144 VAL   A C   
3105 O O   . VAL   A 144 ? 0.1629 0.1602 0.2868 -0.0070 -0.0143 0.0373  144 VAL   A O   
3106 C CB  . VAL   A 144 ? 0.1654 0.1891 0.3270 -0.0079 0.0293  0.0425  144 VAL   A CB  
3107 C CG1 . VAL   A 144 ? 0.1804 0.2054 0.3583 -0.0179 0.0154  0.0392  144 VAL   A CG1 
3108 C CG2 . VAL   A 144 ? 0.1545 0.1970 0.3303 -0.0098 0.0394  0.0517  144 VAL   A CG2 
3118 N N   . ASP   A 145 ? 0.1570 0.1490 0.2877 -0.0243 -0.0142 0.0166  145 ASP   A N   
3119 C CA  . ASP   A 145 ? 0.1669 0.1584 0.3012 -0.0249 -0.0093 0.0070  145 ASP   A CA  
3120 C C   . ASP   A 145 ? 0.1623 0.1530 0.2921 -0.0160 -0.0001 -0.0001 145 ASP   A C   
3121 O O   . ASP   A 145 ? 0.1716 0.1634 0.3507 -0.0193 -0.0035 -0.0466 145 ASP   A O   
3122 C CB  . ASP   A 145 ? 0.1791 0.1875 0.3330 -0.0311 -0.0239 0.0063  145 ASP   A CB  
3123 C CG  . ASP   A 145 ? 0.2022 0.2258 0.3629 -0.0475 -0.0474 0.0122  145 ASP   A CG  
3124 O OD1 . ASP   A 145 ? 0.2015 0.2381 0.3739 -0.0583 -0.0330 0.0163  145 ASP   A OD1 
3125 O OD2 . ASP   A 145 ? 0.2262 0.2512 0.3850 -0.0564 -0.0658 0.0087  145 ASP   A OD2 
3130 N N   . THR   A 146 ? 0.1409 0.1463 0.2359 -0.0210 0.0029  0.0070  146 THR   A N   
3131 C CA  . THR   A 146 ? 0.1405 0.1419 0.2173 -0.0158 -0.0021 0.0034  146 THR   A CA  
3132 C C   . THR   A 146 ? 0.1282 0.1375 0.2258 -0.0062 0.0088  0.0059  146 THR   A C   
3133 O O   . THR   A 146 ? 0.1438 0.1491 0.2557 -0.0010 -0.0012 0.0055  146 THR   A O   
3134 C CB  . THR   A 146 ? 0.1372 0.1465 0.2082 -0.0108 0.0006  0.0072  146 THR   A CB  
3135 O OG1 . THR   A 146 ? 0.1436 0.1625 0.2224 -0.0040 -0.0030 -0.0064 146 THR   A OG1 
3136 C CG2 . THR   A 146 ? 0.1379 0.1445 0.2223 -0.0134 0.0043  0.0181  146 THR   A CG2 
3144 N N   . VAL   A 147 ? 0.1289 0.1441 0.2179 -0.0035 0.0092  0.0125  147 VAL   A N   
3145 C CA  . VAL   A 147 ? 0.1313 0.1487 0.2170 -0.0106 0.0186  0.0235  147 VAL   A CA  
3146 C C   . VAL   A 147 ? 0.1362 0.1453 0.2470 -0.0172 0.0233  0.0312  147 VAL   A C   
3147 O O   . VAL   A 147 ? 0.1442 0.1453 0.2574 -0.0189 0.0131  0.0290  147 VAL   A O   
3148 C CB  . VAL   A 147 ? 0.1429 0.1476 0.2132 -0.0170 0.0150  0.0143  147 VAL   A CB  
3149 C CG1 . VAL   A 147 ? 0.1719 0.1539 0.2151 -0.0129 0.0135  0.0257  147 VAL   A CG1 
3150 C CG2 . VAL   A 147 ? 0.1514 0.1519 0.2145 -0.0141 0.0116  0.0149  147 VAL   A CG2 
3160 N N   . ARG   A 148 ? 0.1407 0.1494 0.2465 -0.0216 0.0198  0.0443  148 ARG   A N   
3161 C CA  . ARG   A 148 ? 0.1478 0.1501 0.2333 -0.0189 0.0097  0.0513  148 ARG   A CA  
3162 C C   . ARG   A 148 ? 0.1619 0.1469 0.2396 -0.0184 0.0082  0.0668  148 ARG   A C   
3163 O O   . ARG   A 148 ? 0.1875 0.1602 0.2648 -0.0217 0.0182  0.0622  148 ARG   A O   
3164 C CB  . ARG   A 148 ? 0.1564 0.1530 0.2438 -0.0161 0.0274  0.0407  148 ARG   A CB  
3165 C CG  . ARG   A 148 ? 0.1735 0.1516 0.2866 -0.0098 0.0391  0.0327  148 ARG   A CG  
3166 C CD  . ARG   A 148 ? 0.1866 0.1494 0.3039 -0.0032 0.0559  0.0438  148 ARG   A CD  
3167 N NE  . ARG   A 148 ? 0.1846 0.1555 0.3050 0.0093  0.0570  0.0490  148 ARG   A NE  
3168 C CZ  . ARG   A 148 ? 0.1777 0.1421 0.2864 0.0005  0.0474  0.0374  148 ARG   A CZ  
3169 N NH1 . ARG   A 148 ? 0.1816 0.1472 0.3011 -0.0085 0.0449  0.0167  148 ARG   A NH1 
3170 N NH2 . ARG   A 148 ? 0.1715 0.1669 0.2833 0.0095  0.0502  0.0422  148 ARG   A NH2 
3184 N N   . THR   A 149 ? 0.1574 0.1609 0.2333 -0.0164 0.0030  0.0512  149 THR   A N   
3185 C CA  . THR   A 149 ? 0.1568 0.1642 0.2273 -0.0181 0.0072  0.0509  149 THR   A CA  
3186 C C   . THR   A 149 ? 0.1560 0.1634 0.2240 -0.0232 0.0111  0.0528  149 THR   A C   
3187 O O   . THR   A 149 ? 0.1569 0.1704 0.2348 -0.0277 0.0079  0.0473  149 THR   A O   
3188 C CB  . THR   A 149 ? 0.1536 0.1805 0.2324 -0.0217 0.0036  0.0453  149 THR   A CB  
3189 O OG1 . THR   A 149 ? 0.1604 0.1638 0.2454 -0.0291 0.0094  0.0435  149 THR   A OG1 
3190 C CG2 . THR   A 149 ? 0.1540 0.1962 0.2329 -0.0110 -0.0171 0.0336  149 THR   A CG2 
3198 N N   . ASN   A 150 ? 0.1582 0.1727 0.2254 -0.0137 0.0053  0.0696  150 ASN   A N   
3199 C CA  . ASN   A 150 ? 0.1719 0.1825 0.2268 -0.0154 0.0131  0.0529  150 ASN   A CA  
3200 C C   . ASN   A 150 ? 0.1458 0.1670 0.2210 -0.0220 0.0072  0.0405  150 ASN   A C   
3201 O O   . ASN   A 150 ? 0.1566 0.1762 0.2461 -0.0179 -0.0077 0.0471  150 ASN   A O   
3202 C CB  . ASN   A 150 ? 0.2219 0.2081 0.2626 -0.0235 0.0350  0.0662  150 ASN   A CB  
3203 C CG  . ASN   A 150 ? 0.2806 0.2391 0.3268 -0.0203 0.0199  0.0716  150 ASN   A CG  
3204 O OD1 . ASN   A 150 ? 0.3066 0.2418 0.3497 -0.0231 0.0288  0.0870  150 ASN   A OD1 
3205 N ND2 . ASN   A 150 ? 0.3120 0.2662 0.3677 -0.0144 0.0070  0.0673  150 ASN   A ND2 
3212 N N   . VAL   A 151 ? 0.1503 0.1526 0.2084 -0.0247 0.0022  0.0402  151 VAL   A N   
3213 C CA  . VAL   A 151 ? 0.1564 0.1583 0.2080 -0.0210 0.0147  0.0484  151 VAL   A CA  
3214 C C   . VAL   A 151 ? 0.1560 0.1543 0.2243 -0.0360 0.0121  0.0386  151 VAL   A C   
3215 O O   . VAL   A 151 ? 0.1684 0.1627 0.2563 -0.0266 0.0116  0.0380  151 VAL   A O   
3216 C CB  . VAL   A 151 ? 0.1828 0.1786 0.2080 -0.0132 0.0127  0.0467  151 VAL   A CB  
3217 C CG1 . VAL   A 151 ? 0.1826 0.2020 0.2348 -0.0105 0.0007  0.0366  151 VAL   A CG1 
3218 C CG2 . VAL   A 151 ? 0.1953 0.1684 0.2071 -0.0104 0.0250  0.0325  151 VAL   A CG2 
3228 N N   . TYR   A 152 ? 0.1467 0.1553 0.2267 -0.0319 0.0055  0.0511  152 TYR   A N   
3229 C CA  . TYR   A 152 ? 0.1468 0.1647 0.2064 -0.0358 0.0047  0.0415  152 TYR   A CA  
3230 C C   . TYR   A 152 ? 0.1460 0.1560 0.1867 -0.0292 0.0215  0.0429  152 TYR   A C   
3231 O O   . TYR   A 152 ? 0.1616 0.1455 0.1895 -0.0238 0.0247  0.0339  152 TYR   A O   
3232 C CB  . TYR   A 152 ? 0.1671 0.1732 0.2191 -0.0287 0.0217  0.0482  152 TYR   A CB  
3233 C CG  . TYR   A 152 ? 0.1734 0.1996 0.2061 -0.0261 0.0277  0.0547  152 TYR   A CG  
3234 C CD1 . TYR   A 152 ? 0.1881 0.2223 0.2229 -0.0165 0.0351  0.0581  152 TYR   A CD1 
3235 C CD2 . TYR   A 152 ? 0.1819 0.2187 0.1969 -0.0389 0.0186  0.0549  152 TYR   A CD2 
3236 C CE1 . TYR   A 152 ? 0.2197 0.2392 0.2397 -0.0137 0.0198  0.0747  152 TYR   A CE1 
3237 C CE2 . TYR   A 152 ? 0.2070 0.2355 0.2030 -0.0441 0.0242  0.0659  152 TYR   A CE2 
3238 C CZ  . TYR   A 152 ? 0.2354 0.2377 0.2178 -0.0295 0.0185  0.0944  152 TYR   A CZ  
3239 O OH  . TYR   A 152 ? 0.2753 0.2639 0.2633 -0.0205 0.0182  0.1076  152 TYR   A OH  
3249 N N   . LEU   A 153 ? 0.1522 0.1569 0.1941 -0.0280 0.0180  0.0424  153 LEU   A N   
3250 C CA  . LEU   A 153 ? 0.1442 0.1482 0.2087 -0.0230 0.0193  0.0430  153 LEU   A CA  
3251 C C   . LEU   A 153 ? 0.1509 0.1556 0.2199 -0.0138 0.0304  0.0426  153 LEU   A C   
3252 O O   . LEU   A 153 ? 0.1542 0.1695 0.2332 -0.0094 0.0452  0.0447  153 LEU   A O   
3253 C CB  . LEU   A 153 ? 0.1425 0.1485 0.2188 -0.0166 0.0133  0.0369  153 LEU   A CB  
3254 C CG  . LEU   A 153 ? 0.1477 0.1505 0.2008 -0.0159 0.0112  0.0282  153 LEU   A CG  
3255 C CD1 . LEU   A 153 ? 0.1630 0.1504 0.1977 -0.0070 -0.0012 0.0303  153 LEU   A CD1 
3256 C CD2 . LEU   A 153 ? 0.1515 0.1560 0.2046 -0.0214 0.0233  0.0082  153 LEU   A CD2 
3268 N N   A ALA   A 154 ? 0.1509 0.1496 0.2133 -0.0059 0.0345  0.0402  154 ALA   A N   
3269 N N   B ALA   A 154 ? 0.1474 0.1526 0.2085 -0.0125 0.0437  0.0377  154 ALA   A N   
3270 C CA  A ALA   A 154 ? 0.1662 0.1521 0.2222 0.0034  0.0282  0.0358  154 ALA   A CA  
3271 C CA  B ALA   A 154 ? 0.1569 0.1554 0.2018 -0.0089 0.0452  0.0356  154 ALA   A CA  
3272 C C   A ALA   A 154 ? 0.1695 0.1540 0.2226 0.0120  0.0307  0.0414  154 ALA   A C   
3273 C C   B ALA   A 154 ? 0.1619 0.1557 0.1988 -0.0076 0.0480  0.0431  154 ALA   A C   
3274 O O   A ALA   A 154 ? 0.1740 0.1624 0.2432 0.0112  0.0385  0.0437  154 ALA   A O   
3275 O O   B ALA   A 154 ? 0.1696 0.1616 0.2153 -0.0178 0.0380  0.0407  154 ALA   A O   
3276 C CB  A ALA   A 154 ? 0.1793 0.1583 0.2354 0.0080  0.0259  0.0203  154 ALA   A CB  
3277 C CB  B ALA   A 154 ? 0.1621 0.1610 0.2014 -0.0058 0.0531  0.0257  154 ALA   A CB  
3288 N N   A VAL   A 155 ? 0.1607 0.1440 0.2008 0.0276  0.0206  0.0457  155 VAL   A N   
3289 N N   B VAL   A 155 ? 0.1507 0.1462 0.1774 0.0089  0.0611  0.0542  155 VAL   A N   
3290 C CA  A VAL   A 155 ? 0.1682 0.1540 0.2107 0.0241  0.0061  0.0441  155 VAL   A CA  
3291 C CA  B VAL   A 155 ? 0.1650 0.1546 0.2102 -0.0061 0.0565  0.0503  155 VAL   A CA  
3292 C CA  T VAL   A 155 ? 0.1947 0.1784 0.2282 -0.0009 0.0067  0.0377  155 VAL   A CA  
3293 C C   A VAL   A 155 ? 0.1755 0.1646 0.2256 0.0298  0.0059  0.0345  155 VAL   A C   
3294 C C   B VAL   A 155 ? 0.1731 0.1590 0.2095 -0.0045 0.0586  0.0438  155 VAL   A C   
3295 C C   T VAL   A 155 ? 0.1948 0.1769 0.2284 0.0113  0.0178  0.0332  155 VAL   A C   
3296 O O   A VAL   A 155 ? 0.1768 0.1767 0.2316 0.0308  0.0012  0.0279  155 VAL   A O   
3297 O O   B VAL   A 155 ? 0.1698 0.1687 0.2016 0.0007  0.0606  0.0373  155 VAL   A O   
3298 O O   T VAL   A 155 ? 0.1949 0.1887 0.2297 0.0152  0.0175  0.0261  155 VAL   A O   
3299 C CB  A VAL   A 155 ? 0.1593 0.1545 0.2049 0.0225  -0.0063 0.0452  155 VAL   A CB  
3300 C CB  B VAL   A 155 ? 0.1640 0.1488 0.2293 -0.0028 0.0430  0.0351  155 VAL   A CB  
3301 C CB  T VAL   A 155 ? 0.1882 0.1778 0.2215 -0.0077 -0.0068 0.0371  155 VAL   A CB  
3302 C CG1 A VAL   A 155 ? 0.1712 0.1616 0.2030 0.0167  -0.0107 0.0525  155 VAL   A CG1 
3303 C CG1 B VAL   A 155 ? 0.1770 0.1493 0.2426 0.0009  0.0342  0.0282  155 VAL   A CG1 
3304 C CG1 T VAL   A 155 ? 0.1984 0.1851 0.2239 -0.0100 -0.0108 0.0393  155 VAL   A CG1 
3305 C CG2 A VAL   A 155 ? 0.1534 0.1607 0.2175 0.0264  -0.0150 0.0316  155 VAL   A CG2 
3306 C CG2 B VAL   A 155 ? 0.1693 0.1559 0.2434 0.0109  0.0253  0.0182  155 VAL   A CG2 
3307 C CG2 T VAL   A 155 ? 0.1836 0.1821 0.2293 -0.0084 -0.0145 0.0276  155 VAL   A CG2 
3333 N N   A PHE   A 156 ? 0.1798 0.1678 0.2396 0.0316  0.0145  0.0326  156 PHE   A N   
3334 N N   B PHE   A 156 ? 0.1873 0.1620 0.2389 -0.0073 0.0510  0.0506  156 PHE   A N   
3335 N N   T PHE   A 156 ? 0.1945 0.1661 0.2317 0.0169  0.0293  0.0400  156 PHE   A N   
3336 C CA  A PHE   A 156 ? 0.1937 0.1736 0.2504 0.0405  0.0152  0.0323  156 PHE   A CA  
3337 C CA  B PHE   A 156 ? 0.2044 0.1770 0.2317 -0.0050 0.0411  0.0568  156 PHE   A CA  
3338 C CA  T PHE   A 156 ? 0.2084 0.1584 0.2208 0.0273  0.0373  0.0436  156 PHE   A CA  
3339 C C   A PHE   A 156 ? 0.1912 0.1850 0.2410 0.0432  0.0311  0.0371  156 PHE   A C   
3340 C C   B PHE   A 156 ? 0.2069 0.1982 0.2448 0.0008  0.0469  0.0601  156 PHE   A C   
3341 C C   T PHE   A 156 ? 0.2007 0.1684 0.2106 0.0267  0.0553  0.0559  156 PHE   A C   
3342 O O   A PHE   A 156 ? 0.2000 0.1886 0.2510 0.0382  0.0397  0.0291  156 PHE   A O   
3343 O O   B PHE   A 156 ? 0.2103 0.2023 0.2690 -0.0112 0.0461  0.0391  156 PHE   A O   
3344 O O   T PHE   A 156 ? 0.2054 0.1712 0.2189 0.0230  0.0722  0.0403  156 PHE   A O   
3345 C CB  A PHE   A 156 ? 0.2090 0.1805 0.2646 0.0362  0.0101  0.0318  156 PHE   A CB  
3346 C CB  B PHE   A 156 ? 0.2141 0.1822 0.2217 -0.0098 0.0322  0.0538  156 PHE   A CB  
3347 C CB  T PHE   A 156 ? 0.2224 0.1497 0.2179 0.0319  0.0352  0.0394  156 PHE   A CB  
3348 C CG  A PHE   A 156 ? 0.2252 0.1885 0.2789 0.0364  0.0021  0.0258  156 PHE   A CG  
3349 C CG  B PHE   A 156 ? 0.2295 0.1978 0.2342 -0.0082 0.0199  0.0453  156 PHE   A CG  
3350 C CG  T PHE   A 156 ? 0.2395 0.1487 0.2243 0.0385  0.0250  0.0384  156 PHE   A CG  
3351 C CD1 A PHE   A 156 ? 0.2309 0.1927 0.2803 0.0402  0.0115  0.0260  156 PHE   A CD1 
3352 C CD1 B PHE   A 156 ? 0.2387 0.2138 0.2654 -0.0036 0.0184  0.0287  156 PHE   A CD1 
3353 C CD1 T PHE   A 156 ? 0.2471 0.1474 0.2378 0.0451  0.0147  0.0383  156 PHE   A CD1 
3354 C CD2 A PHE   A 156 ? 0.2361 0.1992 0.2884 0.0369  -0.0051 0.0205  156 PHE   A CD2 
3355 C CD2 B PHE   A 156 ? 0.2391 0.2045 0.2530 -0.0074 0.0140  0.0429  156 PHE   A CD2 
3356 C CD2 T PHE   A 156 ? 0.2497 0.1556 0.2365 0.0390  0.0232  0.0433  156 PHE   A CD2 
3357 C CE1 A PHE   A 156 ? 0.2380 0.1969 0.2905 0.0400  0.0132  0.0215  156 PHE   A CE1 
3358 C CE1 B PHE   A 156 ? 0.2437 0.2207 0.2834 -0.0045 0.0169  0.0195  156 PHE   A CE1 
3359 C CE1 T PHE   A 156 ? 0.2552 0.1521 0.2492 0.0466  0.0082  0.0362  156 PHE   A CE1 
3360 C CE2 A PHE   A 156 ? 0.2427 0.2042 0.2915 0.0394  -0.0046 0.0135  156 PHE   A CE2 
3361 C CE2 B PHE   A 156 ? 0.2494 0.2141 0.2742 -0.0056 0.0086  0.0306  156 PHE   A CE2 
3362 C CE2 T PHE   A 156 ? 0.2588 0.1588 0.2466 0.0397  0.0153  0.0434  156 PHE   A CE2 
3363 C CZ  A PHE   A 156 ? 0.2428 0.2046 0.2943 0.0417  0.0094  0.0162  156 PHE   A CZ  
3364 C CZ  B PHE   A 156 ? 0.2477 0.2186 0.2903 -0.0087 0.0125  0.0223  156 PHE   A CZ  
3365 C CZ  T PHE   A 156 ? 0.2597 0.1542 0.2591 0.0392  0.0109  0.0401  156 PHE   A CZ  
3393 N N   A ASP   A 157 ? 0.1865 0.1963 0.2339 0.0460  0.0298  0.0365  157 ASP   A N   
3394 N N   B ASP   A 157 ? 0.2107 0.2268 0.2627 0.0141  0.0333  0.0742  157 ASP   A N   
3395 N N   T ASP   A 157 ? 0.1911 0.1805 0.2177 0.0313  0.0390  0.0690  157 ASP   A N   
3396 C CA  A ASP   A 157 ? 0.1940 0.2159 0.2355 0.0440  0.0225  0.0440  157 ASP   A CA  
3397 C CA  B ASP   A 157 ? 0.2205 0.2518 0.2669 0.0324  0.0204  0.0809  157 ASP   A CA  
3398 C CA  T ASP   A 157 ? 0.1845 0.1962 0.2224 0.0418  0.0262  0.0756  157 ASP   A CA  
3399 C C   A ASP   A 157 ? 0.1887 0.2307 0.2414 0.0455  0.0245  0.0557  157 ASP   A C   
3400 C C   B ASP   A 157 ? 0.2110 0.2706 0.2546 0.0472  0.0299  0.1020  157 ASP   A C   
3401 C C   T ASP   A 157 ? 0.1765 0.2162 0.2231 0.0484  0.0269  0.0846  157 ASP   A C   
3402 O O   A ASP   A 157 ? 0.1868 0.2333 0.2484 0.0438  0.0256  0.0495  157 ASP   A O   
3403 O O   B ASP   A 157 ? 0.1965 0.2760 0.2465 0.0451  0.0317  0.1038  157 ASP   A O   
3404 O O   T ASP   A 157 ? 0.1704 0.2189 0.2305 0.0447  0.0346  0.0818  157 ASP   A O   
3405 C CB  A ASP   A 157 ? 0.2071 0.2185 0.2386 0.0399  0.0175  0.0394  157 ASP   A CB  
3406 C CB  B ASP   A 157 ? 0.2383 0.2539 0.2775 0.0333  0.0056  0.0724  157 ASP   A CB  
3407 C CB  T ASP   A 157 ? 0.1842 0.1873 0.2215 0.0444  0.0250  0.0768  157 ASP   A CB  
3408 C CG  A ASP   A 157 ? 0.2173 0.2201 0.2521 0.0355  0.0128  0.0290  157 ASP   A CG  
3409 C CG  B ASP   A 157 ? 0.2505 0.2536 0.2913 0.0365  -0.0126 0.0582  157 ASP   A CG  
3410 C CG  T ASP   A 157 ? 0.1852 0.1800 0.2282 0.0459  0.0276  0.0665  157 ASP   A CG  
3411 O OD1 A ASP   A 157 ? 0.2207 0.2240 0.2724 0.0288  -0.0021 0.0170  157 ASP   A OD1 
3412 O OD1 B ASP   A 157 ? 0.2553 0.2544 0.3169 0.0376  -0.0232 0.0568  157 ASP   A OD1 
3413 O OD1 T ASP   A 157 ? 0.1862 0.1706 0.2473 0.0363  0.0333  0.0585  157 ASP   A OD1 
3414 O OD2 A ASP   A 157 ? 0.2176 0.2115 0.2420 0.0371  0.0259  0.0330  157 ASP   A OD2 
3415 O OD2 B ASP   A 157 ? 0.2517 0.2490 0.2814 0.0413  -0.0159 0.0534  157 ASP   A OD2 
3416 O OD2 T ASP   A 157 ? 0.1873 0.1762 0.2161 0.0532  0.0268  0.0601  157 ASP   A OD2 
3429 N N   A LYS   A 158 ? 0.1952 0.2442 0.2460 0.0425  0.0340  0.0628  158 LYS   A N   
3430 N N   B LYS   A 158 ? 0.2272 0.2899 0.2600 0.0562  0.0409  0.1044  158 LYS   A N   
3431 N N   T LYS   A 158 ? 0.1867 0.2359 0.2271 0.0462  0.0337  0.0792  158 LYS   A N   
3432 C CA  A LYS   A 158 ? 0.1980 0.2584 0.2607 0.0399  0.0440  0.0594  158 LYS   A CA  
3433 C CA  B LYS   A 158 ? 0.2480 0.3079 0.2587 0.0662  0.0444  0.1094  158 LYS   A CA  
3434 C CA  T LYS   A 158 ? 0.1944 0.2547 0.2392 0.0473  0.0344  0.0698  158 LYS   A CA  
3435 C C   A LYS   A 158 ? 0.1844 0.2665 0.2512 0.0409  0.0395  0.0665  158 LYS   A C   
3436 C C   B LYS   A 158 ? 0.2389 0.3145 0.2461 0.0721  0.0384  0.1092  158 LYS   A C   
3437 C C   T LYS   A 158 ? 0.1813 0.2558 0.2307 0.0462  0.0331  0.0660  158 LYS   A C   
3438 O O   A LYS   A 158 ? 0.1801 0.2715 0.2567 0.0340  0.0475  0.0629  158 LYS   A O   
3439 O O   B LYS   A 158 ? 0.2254 0.3181 0.2158 0.0683  0.0399  0.1139  158 LYS   A O   
3440 O O   T LYS   A 158 ? 0.1755 0.2579 0.2387 0.0431  0.0404  0.0546  158 LYS   A O   
3441 C CB  A LYS   A 158 ? 0.2152 0.2615 0.2861 0.0357  0.0632  0.0545  158 LYS   A CB  
3442 C CB  B LYS   A 158 ? 0.2768 0.3217 0.2864 0.0652  0.0465  0.1056  158 LYS   A CB  
3443 C CB  T LYS   A 158 ? 0.2171 0.2672 0.2697 0.0447  0.0468  0.0627  158 LYS   A CB  
3444 C CG  A LYS   A 158 ? 0.2317 0.2649 0.3115 0.0333  0.0738  0.0574  158 LYS   A CG  
3445 C CG  B LYS   A 158 ? 0.3045 0.3357 0.3196 0.0609  0.0495  0.1013  158 LYS   A CG  
3446 C CG  T LYS   A 158 ? 0.2394 0.2761 0.3054 0.0444  0.0513  0.0623  158 LYS   A CG  
3447 C CD  A LYS   A 158 ? 0.2455 0.2704 0.3330 0.0304  0.0831  0.0671  158 LYS   A CD  
3448 C CD  B LYS   A 158 ? 0.3276 0.3477 0.3543 0.0577  0.0533  0.0954  158 LYS   A CD  
3449 C CD  T LYS   A 158 ? 0.2607 0.2844 0.3443 0.0444  0.0516  0.0668  158 LYS   A CD  
3450 C CE  A LYS   A 158 ? 0.2556 0.2727 0.3479 0.0254  0.0916  0.0794  158 LYS   A CE  
3451 C CE  B LYS   A 158 ? 0.3422 0.3542 0.3770 0.0557  0.0594  0.0968  158 LYS   A CE  
3452 C CE  T LYS   A 158 ? 0.2788 0.2868 0.3737 0.0450  0.0483  0.0719  158 LYS   A CE  
3453 N NZ  A LYS   A 158 ? 0.2604 0.2719 0.3544 0.0200  0.0981  0.0890  158 LYS   A NZ  
3454 N NZ  B LYS   A 158 ? 0.3490 0.3600 0.3906 0.0529  0.0650  0.0958  158 LYS   A NZ  
3455 N NZ  T LYS   A 158 ? 0.2892 0.2880 0.3883 0.0470  0.0448  0.0739  158 LYS   A NZ  
3495 N N   A ASN   A 159 ? 0.1794 0.2683 0.2566 0.0436  0.0309  0.0691  159 ASN   A N   
3496 N N   B ASN   A 159 ? 0.2485 0.3181 0.2700 0.0786  0.0348  0.0925  159 ASN   A N   
3497 N N   T ASN   A 159 ? 0.1824 0.2557 0.2431 0.0441  0.0275  0.0646  159 ASN   A N   
3498 C CA  A ASN   A 159 ? 0.1742 0.2717 0.2576 0.0424  0.0222  0.0704  159 ASN   A CA  
3499 C CA  B ASN   A 159 ? 0.2625 0.3228 0.3059 0.0799  0.0324  0.0733  159 ASN   A CA  
3500 C CA  T ASN   A 159 ? 0.1872 0.2598 0.2512 0.0376  0.0229  0.0633  159 ASN   A CA  
3501 C C   A ASN   A 159 ? 0.1518 0.2691 0.2423 0.0429  0.0263  0.0755  159 ASN   A C   
3502 C C   B ASN   A 159 ? 0.2555 0.3202 0.2967 0.0816  0.0355  0.0725  159 ASN   A C   
3503 C C   T ASN   A 159 ? 0.1833 0.2614 0.2469 0.0264  0.0375  0.0575  159 ASN   A C   
3504 O O   A ASN   A 159 ? 0.1328 0.2661 0.2281 0.0540  0.0141  0.0595  159 ASN   A O   
3505 O O   B ASN   A 159 ? 0.2497 0.3265 0.3006 0.0874  0.0244  0.0789  159 ASN   A O   
3506 O O   T ASN   A 159 ? 0.1815 0.2602 0.2363 0.0253  0.0378  0.0368  159 ASN   A O   
3507 C CB  A ASN   A 159 ? 0.1845 0.2781 0.2818 0.0414  0.0112  0.0668  159 ASN   A CB  
3508 C CB  B ASN   A 159 ? 0.2802 0.3279 0.3543 0.0777  0.0353  0.0526  159 ASN   A CB  
3509 C CB  T ASN   A 159 ? 0.1912 0.2641 0.2743 0.0430  0.0048  0.0687  159 ASN   A CB  
3510 C CG  A ASN   A 159 ? 0.1971 0.2836 0.3086 0.0404  0.0043  0.0587  159 ASN   A CG  
3511 C CG  B ASN   A 159 ? 0.2964 0.3367 0.4085 0.0663  0.0408  0.0298  159 ASN   A CG  
3512 C CG  T ASN   A 159 ? 0.1978 0.2674 0.3015 0.0479  -0.0071 0.0676  159 ASN   A CG  
3513 O OD1 A ASN   A 159 ? 0.2073 0.2915 0.3257 0.0379  0.0113  0.0548  159 ASN   A OD1 
3514 O OD1 B ASN   A 159 ? 0.3059 0.3450 0.4359 0.0594  0.0450  0.0148  159 ASN   A OD1 
3515 O OD1 T ASN   A 159 ? 0.2043 0.2769 0.3214 0.0468  0.0026  0.0616  159 ASN   A OD1 
3516 N ND2 A ASN   A 159 ? 0.1989 0.2853 0.3212 0.0408  0.0008  0.0482  159 ASN   A ND2 
3517 N ND2 B ASN   A 159 ? 0.3000 0.3414 0.4267 0.0597  0.0403  0.0268  159 ASN   A ND2 
3518 N ND2 T ASN   A 159 ? 0.1982 0.2676 0.3138 0.0519  -0.0152 0.0623  159 ASN   A ND2 
3537 N N   A LEU   A 160 ? 0.1409 0.2611 0.2404 0.0369  0.0286  0.0935  160 LEU   A N   
3538 N N   B LEU   A 160 ? 0.2474 0.3079 0.2832 0.0719  0.0431  0.0802  160 LEU   A N   
3539 N N   T LEU   A 160 ? 0.1751 0.2564 0.2515 0.0170  0.0378  0.0686  160 LEU   A N   
3540 C CA  A LEU   A 160 ? 0.1348 0.2571 0.2322 0.0265  0.0319  0.1042  160 LEU   A CA  
3541 C CA  B LEU   A 160 ? 0.2417 0.2935 0.2666 0.0601  0.0451  0.0840  160 LEU   A CA  
3542 C CA  T LEU   A 160 ? 0.1707 0.2519 0.2463 0.0044  0.0362  0.0759  160 LEU   A CA  
3543 C C   A LEU   A 160 ? 0.1199 0.2575 0.2250 0.0204  0.0349  0.1067  160 LEU   A C   
3544 C C   B LEU   A 160 ? 0.2171 0.2805 0.2423 0.0452  0.0524  0.1014  160 LEU   A C   
3545 O O   A LEU   A 160 ? 0.1105 0.2640 0.2233 0.0130  0.0324  0.1089  160 LEU   A O   
3546 O O   B LEU   A 160 ? 0.2098 0.2814 0.2387 0.0395  0.0528  0.1063  160 LEU   A O   
3547 C CB  A LEU   A 160 ? 0.1408 0.2583 0.2323 0.0234  0.0242  0.1008  160 LEU   A CB  
3548 C CB  B LEU   A 160 ? 0.2622 0.2946 0.2803 0.0540  0.0396  0.0637  160 LEU   A CB  
3549 C CB  T LEU   A 160 ? 0.1655 0.2514 0.2398 -0.0068 0.0297  0.0744  160 LEU   A CB  
3550 C CG  A LEU   A 160 ? 0.1462 0.2617 0.2426 0.0204  0.0163  0.0831  160 LEU   A CG  
3551 C CG  B LEU   A 160 ? 0.2801 0.2960 0.2990 0.0462  0.0238  0.0375  160 LEU   A CG  
3552 C CG  T LEU   A 160 ? 0.1632 0.2534 0.2438 -0.0158 0.0229  0.0598  160 LEU   A CG  
3553 C CD1 A LEU   A 160 ? 0.1554 0.2662 0.2523 0.0162  0.0181  0.0773  160 LEU   A CD1 
3554 C CD1 B LEU   A 160 ? 0.2839 0.2974 0.2999 0.0446  0.0175  0.0320  160 LEU   A CD1 
3555 C CD1 T LEU   A 160 ? 0.1699 0.2580 0.2544 -0.0179 0.0250  0.0574  160 LEU   A CD1 
3556 C CD2 A LEU   A 160 ? 0.1456 0.2623 0.2432 0.0170  0.0140  0.0726  160 LEU   A CD2 
3557 C CD2 B LEU   A 160 ? 0.2883 0.2961 0.3051 0.0426  0.0177  0.0284  160 LEU   A CD2 
3558 C CD2 T LEU   A 160 ? 0.1598 0.2523 0.2422 -0.0234 0.0189  0.0498  160 LEU   A CD2 
3591 N N   A TYR   A 161 ? 0.1403 0.2539 0.2630 0.0179  0.0289  0.1002  161 TYR   A N   
3592 N N   B TYR   A 161 ? 0.2043 0.2667 0.2308 0.0327  0.0631  0.1078  161 TYR   A N   
3593 C CA  A TYR   A 161 ? 0.1467 0.2464 0.2623 0.0086  0.0285  0.0888  161 TYR   A CA  
3594 C CA  B TYR   A 161 ? 0.2005 0.2567 0.2264 0.0163  0.0516  0.1017  161 TYR   A CA  
3595 C C   A TYR   A 161 ? 0.1479 0.2630 0.2666 0.0106  0.0180  0.0872  161 TYR   A C   
3596 C C   B TYR   A 161 ? 0.2048 0.2732 0.2288 0.0109  0.0344  0.1004  161 TYR   A C   
3597 O O   A TYR   A 161 ? 0.1400 0.2684 0.2504 0.0106  0.0164  0.0769  161 TYR   A O   
3598 O O   B TYR   A 161 ? 0.2047 0.2750 0.2173 0.0076  0.0323  0.0972  161 TYR   A O   
3599 C CB  A TYR   A 161 ? 0.1596 0.2355 0.2682 0.0050  0.0209  0.0718  161 TYR   A CB  
3600 C CB  B TYR   A 161 ? 0.1958 0.2384 0.2292 0.0110  0.0498  0.0848  161 TYR   A CB  
3601 C CG  A TYR   A 161 ? 0.1560 0.2190 0.2644 0.0030  0.0140  0.0536  161 TYR   A CG  
3602 C CG  B TYR   A 161 ? 0.1816 0.2148 0.2273 0.0081  0.0507  0.0631  161 TYR   A CG  
3603 C CD1 A TYR   A 161 ? 0.1588 0.2123 0.2736 0.0047  0.0073  0.0447  161 TYR   A CD1 
3604 C CD1 B TYR   A 161 ? 0.1784 0.1992 0.2276 0.0084  0.0441  0.0489  161 TYR   A CD1 
3605 C CD2 A TYR   A 161 ? 0.1576 0.2151 0.2645 0.0076  -0.0035 0.0435  161 TYR   A CD2 
3606 C CD2 B TYR   A 161 ? 0.1799 0.2097 0.2420 0.0104  0.0450  0.0554  161 TYR   A CD2 
3607 C CE1 A TYR   A 161 ? 0.1644 0.1968 0.2587 0.0045  0.0017  0.0434  161 TYR   A CE1 
3608 C CE1 B TYR   A 161 ? 0.1776 0.1935 0.2290 0.0080  0.0450  0.0410  161 TYR   A CE1 
3609 C CE2 A TYR   A 161 ? 0.1651 0.2008 0.2564 0.0050  -0.0134 0.0487  161 TYR   A CE2 
3610 C CE2 B TYR   A 161 ? 0.1833 0.2019 0.2479 0.0032  0.0390  0.0549  161 TYR   A CE2 
3611 C CZ  A TYR   A 161 ? 0.1734 0.1913 0.2507 0.0008  -0.0121 0.0490  161 TYR   A CZ  
3612 C CZ  B TYR   A 161 ? 0.1862 0.1943 0.2460 0.0053  0.0424  0.0503  161 TYR   A CZ  
3613 O OH  A TYR   A 161 ? 0.1866 0.1782 0.2403 -0.0023 -0.0116 0.0526  161 TYR   A OH  
3614 O OH  B TYR   A 161 ? 0.1980 0.1967 0.2746 0.0067  0.0344  0.0535  161 TYR   A OH  
3633 N N   A ASP   A 162 ? 0.1489 0.2707 0.2801 0.0145  0.0306  0.1047  162 ASP   A N   
3634 N N   B ASP   A 162 ? 0.2041 0.2856 0.2373 0.0141  0.0329  0.1098  162 ASP   A N   
3635 C CA  A ASP   A 162 ? 0.1506 0.2892 0.2784 0.0102  0.0373  0.0996  162 ASP   A CA  
3636 C CA  B ASP   A 162 ? 0.2066 0.3018 0.2526 0.0179  0.0171  0.1056  162 ASP   A CA  
3637 C C   A ASP   A 162 ? 0.1538 0.3047 0.2782 0.0106  0.0288  0.0846  162 ASP   A C   
3638 C C   B ASP   A 162 ? 0.2148 0.3162 0.2640 0.0169  0.0051  0.0874  162 ASP   A C   
3639 O O   A ASP   A 162 ? 0.1593 0.3092 0.2987 0.0170  0.0271  0.0690  162 ASP   A O   
3640 O O   B ASP   A 162 ? 0.2186 0.3175 0.2705 0.0194  0.0022  0.0737  162 ASP   A O   
3641 C CB  A ASP   A 162 ? 0.1548 0.2980 0.2780 0.0181  0.0443  0.0978  162 ASP   A CB  
3642 C CB  B ASP   A 162 ? 0.2016 0.3041 0.2693 0.0231  0.0121  0.1179  162 ASP   A CB  
3643 C CG  A ASP   A 162 ? 0.1755 0.3127 0.2858 0.0270  0.0471  0.0938  162 ASP   A CG  
3644 C CG  B ASP   A 162 ? 0.2019 0.3054 0.2852 0.0281  0.0017  0.1339  162 ASP   A CG  
3645 O OD1 A ASP   A 162 ? 0.1904 0.3208 0.2767 0.0275  0.0507  0.0950  162 ASP   A OD1 
3646 O OD1 B ASP   A 162 ? 0.2061 0.3039 0.2901 0.0299  -0.0026 0.1441  162 ASP   A OD1 
3647 O OD2 A ASP   A 162 ? 0.1861 0.3132 0.2909 0.0353  0.0588  0.0910  162 ASP   A OD2 
3648 O OD2 B ASP   A 162 ? 0.2026 0.3120 0.2977 0.0367  0.0041  0.1345  162 ASP   A OD2 
3657 N N   A LYS   A 163 ? 0.1708 0.3169 0.2785 0.0095  0.0168  0.0678  163 LYS   A N   
3658 N N   B LYS   A 163 ? 0.2265 0.3305 0.2777 0.0131  -0.0020 0.0775  163 LYS   A N   
3659 C CA  A LYS   A 163 ? 0.1850 0.3247 0.2823 0.0113  0.0019  0.0559  163 LYS   A CA  
3660 C CA  B LYS   A 163 ? 0.2358 0.3398 0.2869 0.0063  -0.0067 0.0703  163 LYS   A CA  
3661 C C   A LYS   A 163 ? 0.1764 0.3090 0.2638 0.0032  0.0115  0.0607  163 LYS   A C   
3662 C C   B LYS   A 163 ? 0.2318 0.3298 0.2660 -0.0036 -0.0028 0.0715  163 LYS   A C   
3663 O O   A LYS   A 163 ? 0.1660 0.3058 0.2512 -0.0095 0.0209  0.0578  163 LYS   A O   
3664 O O   B LYS   A 163 ? 0.2329 0.3361 0.2581 -0.0041 -0.0024 0.0719  163 LYS   A O   
3665 C CB  A LYS   A 163 ? 0.2183 0.3455 0.3192 0.0212  -0.0053 0.0479  163 LYS   A CB  
3666 C CB  B LYS   A 163 ? 0.2562 0.3580 0.3292 0.0098  -0.0090 0.0617  163 LYS   A CB  
3667 C CG  A LYS   A 163 ? 0.2526 0.3632 0.3669 0.0217  -0.0008 0.0438  163 LYS   A CG  
3668 C CG  B LYS   A 163 ? 0.2790 0.3741 0.3772 0.0095  -0.0063 0.0531  163 LYS   A CG  
3669 C CD  A LYS   A 163 ? 0.2859 0.3787 0.4202 0.0234  -0.0009 0.0412  163 LYS   A CD  
3670 C CD  B LYS   A 163 ? 0.2981 0.3851 0.4209 0.0101  -0.0036 0.0460  163 LYS   A CD  
3671 C CE  A LYS   A 163 ? 0.3118 0.3892 0.4596 0.0219  0.0035  0.0393  163 LYS   A CE  
3672 C CE  B LYS   A 163 ? 0.3137 0.3938 0.4562 0.0095  -0.0032 0.0404  163 LYS   A CE  
3673 N NZ  A LYS   A 163 ? 0.3284 0.3973 0.4852 0.0196  0.0037  0.0363  163 LYS   A NZ  
3674 N NZ  B LYS   A 163 ? 0.3232 0.3995 0.4757 0.0075  -0.0012 0.0349  163 LYS   A NZ  
3701 N N   A LEU   A 164 ? 0.1571 0.2822 0.2351 -0.0024 0.0150  0.0658  164 LEU   A N   
3702 N N   B LEU   A 164 ? 0.2210 0.3100 0.2456 -0.0109 -0.0046 0.0740  164 LEU   A N   
3703 C CA  A LEU   A 164 ? 0.1633 0.2664 0.2061 -0.0098 0.0294  0.0511  164 LEU   A CA  
3704 C CA  B LEU   A 164 ? 0.2272 0.2978 0.2370 -0.0177 0.0063  0.0763  164 LEU   A CA  
3705 C C   A LEU   A 164 ? 0.1671 0.2636 0.1986 -0.0164 0.0269  0.0449  164 LEU   A C   
3706 C C   B LEU   A 164 ? 0.2406 0.3027 0.2397 -0.0209 -0.0021 0.0831  164 LEU   A C   
3707 O O   A LEU   A 164 ? 0.1669 0.2616 0.1841 -0.0229 0.0489  0.0324  164 LEU   A O   
3708 O O   B LEU   A 164 ? 0.2413 0.3021 0.2217 -0.0264 0.0077  0.0947  164 LEU   A O   
3709 C CB  A LEU   A 164 ? 0.1667 0.2510 0.1997 -0.0092 0.0339  0.0450  164 LEU   A CB  
3710 C CB  B LEU   A 164 ? 0.2236 0.2853 0.2313 -0.0212 0.0198  0.0687  164 LEU   A CB  
3711 C CG  A LEU   A 164 ? 0.1708 0.2347 0.1998 -0.0032 0.0257  0.0401  164 LEU   A CG  
3712 C CG  B LEU   A 164 ? 0.2231 0.2790 0.2266 -0.0188 0.0234  0.0564  164 LEU   A CG  
3713 C CD1 A LEU   A 164 ? 0.1624 0.2310 0.2127 0.0076  0.0302  0.0435  164 LEU   A CD1 
3714 C CD1 B LEU   A 164 ? 0.2171 0.2753 0.2170 -0.0194 0.0230  0.0481  164 LEU   A CD1 
3715 C CD2 A LEU   A 164 ? 0.1691 0.2244 0.1981 -0.0139 0.0203  0.0218  164 LEU   A CD2 
3716 C CD2 B LEU   A 164 ? 0.2311 0.2836 0.2293 -0.0137 0.0263  0.0493  164 LEU   A CD2 
3739 N N   A VAL   A 165 ? 0.1508 0.2593 0.1901 -0.0284 0.0230  0.0517  165 VAL   A N   
3740 N N   B VAL   A 165 ? 0.2501 0.3087 0.2631 -0.0228 -0.0152 0.0758  165 VAL   A N   
3741 C CA  A VAL   A 165 ? 0.1588 0.2584 0.1691 -0.0353 0.0228  0.0457  165 VAL   A CA  
3742 C CA  B VAL   A 165 ? 0.2666 0.3183 0.2911 -0.0210 -0.0295 0.0604  165 VAL   A CA  
3743 C C   A VAL   A 165 ? 0.1534 0.2719 0.1610 -0.0277 0.0235  0.0461  165 VAL   A C   
3744 C C   B VAL   A 165 ? 0.2724 0.3291 0.3103 -0.0173 -0.0422 0.0522  165 VAL   A C   
3745 O O   A VAL   A 165 ? 0.1399 0.2702 0.1523 -0.0251 0.0312  0.0478  165 VAL   A O   
3746 O O   B VAL   A 165 ? 0.2760 0.3336 0.3327 -0.0190 -0.0588 0.0537  165 VAL   A O   
3747 C CB  A VAL   A 165 ? 0.1793 0.2495 0.1898 -0.0458 0.0337  0.0425  165 VAL   A CB  
3748 C CB  B VAL   A 165 ? 0.2794 0.3193 0.3028 -0.0222 -0.0303 0.0529  165 VAL   A CB  
3749 C CG1 A VAL   A 165 ? 0.1830 0.2496 0.1916 -0.0472 0.0309  0.0272  165 VAL   A CG1 
3750 C CG1 B VAL   A 165 ? 0.2849 0.3229 0.3147 -0.0213 -0.0291 0.0465  165 VAL   A CG1 
3751 C CG2 A VAL   A 165 ? 0.1915 0.2481 0.1832 -0.0363 0.0311  0.0594  165 VAL   A CG2 
3752 C CG2 B VAL   A 165 ? 0.2826 0.3169 0.3020 -0.0233 -0.0329 0.0537  165 VAL   A CG2 
3771 N N   A SER   A 166 ? 0.1399 0.2782 0.1802 -0.0287 0.0271  0.0349  166 SER   A N   
3772 N N   B SER   A 166 ? 0.2725 0.3347 0.3100 -0.0131 -0.0397 0.0427  166 SER   A N   
3773 C CA  A SER   A 166 ? 0.1443 0.2877 0.2033 -0.0220 0.0215  0.0265  166 SER   A CA  
3774 C CA  B SER   A 166 ? 0.2785 0.3422 0.3095 -0.0107 -0.0359 0.0333  166 SER   A CA  
3775 C C   A SER   A 166 ? 0.1470 0.2925 0.2120 -0.0072 0.0074  0.0159  166 SER   A C   
3776 C C   B SER   A 166 ? 0.3003 0.3551 0.3191 -0.0082 -0.0327 0.0208  166 SER   A C   
3777 O O   A SER   A 166 ? 0.1701 0.3005 0.2419 -0.0067 0.0164  -0.0009 166 SER   A O   
3778 O O   B SER   A 166 ? 0.3027 0.3549 0.3192 -0.0069 -0.0357 0.0222  166 SER   A O   
3779 C CB  A SER   A 166 ? 0.1557 0.2949 0.2190 -0.0118 0.0141  0.0259  166 SER   A CB  
3780 C CB  B SER   A 166 ? 0.2657 0.3383 0.3135 -0.0081 -0.0392 0.0336  166 SER   A CB  
3781 O OG  A SER   A 166 ? 0.1770 0.3040 0.2550 -0.0045 0.0113  0.0314  166 SER   A OG  
3782 O OG  B SER   A 166 ? 0.2553 0.3363 0.3216 -0.0060 -0.0465 0.0404  166 SER   A OG  
3793 N N   A SER   A 167 ? 0.1431 0.2863 0.1802 0.0109  -0.0022 0.0296  167 SER   A N   
3794 N N   B SER   A 167 ? 0.3242 0.3702 0.3409 -0.0058 -0.0202 0.0107  167 SER   A N   
3795 C CA  A SER   A 167 ? 0.1667 0.2814 0.1768 0.0189  -0.0019 0.0328  167 SER   A CA  
3796 C CA  B SER   A 167 ? 0.3498 0.3844 0.3657 -0.0004 -0.0157 0.0015  167 SER   A CA  
3797 C C   A SER   A 167 ? 0.1660 0.2754 0.1615 0.0200  0.0241  0.0356  167 SER   A C   
3798 C C   B SER   A 167 ? 0.3679 0.3990 0.3780 0.0084  -0.0158 -0.0058 167 SER   A C   
3799 O O   A SER   A 167 ? 0.1862 0.2754 0.1826 0.0207  0.0138  0.0333  167 SER   A O   
3800 O O   B SER   A 167 ? 0.3669 0.3961 0.3734 0.0067  -0.0150 -0.0036 167 SER   A O   
3801 C CB  A SER   A 167 ? 0.1820 0.2787 0.1872 0.0233  0.0026  0.0463  167 SER   A CB  
3802 C CB  B SER   A 167 ? 0.3551 0.3861 0.3822 -0.0007 -0.0112 0.0003  167 SER   A CB  
3803 O OG  A SER   A 167 ? 0.1918 0.2819 0.2005 0.0204  0.0161  0.0492  167 SER   A OG  
3804 O OG  B SER   A 167 ? 0.3594 0.3880 0.3994 0.0000  -0.0087 0.0029  167 SER   A OG  
3815 N N   A PHE   A 168 ? 0.1627 0.2723 0.1654 0.0273  0.0241  0.0366  168 PHE   A N   
3816 N N   B PHE   A 168 ? 0.3893 0.4187 0.3960 0.0181  -0.0180 -0.0112 168 PHE   A N   
3817 C CA  A PHE   A 168 ? 0.1572 0.2713 0.1797 0.0196  0.0216  0.0398  168 PHE   A CA  
3818 C CA  B PHE   A 168 ? 0.4111 0.4380 0.4244 0.0258  -0.0171 -0.0141 168 PHE   A CA  
3819 C C   A PHE   A 168 ? 0.1626 0.2905 0.2131 0.0119  0.0457  0.0278  168 PHE   A C   
3820 C C   B PHE   A 168 ? 0.4268 0.4484 0.4436 0.0201  -0.0203 -0.0162 168 PHE   A C   
3821 O O   A PHE   A 168 ? 0.1762 0.3016 0.2779 0.0008  0.0508  0.0340  168 PHE   A O   
3822 O O   B PHE   A 168 ? 0.4290 0.4509 0.4457 0.0237  -0.0182 -0.0167 168 PHE   A O   
3823 C CB  A PHE   A 168 ? 0.1552 0.2606 0.1818 0.0049  0.0113  0.0422  168 PHE   A CB  
3824 C CB  B PHE   A 168 ? 0.4164 0.4467 0.4348 0.0400  -0.0154 -0.0132 168 PHE   A CB  
3825 C CG  A PHE   A 168 ? 0.1555 0.2566 0.1709 0.0023  0.0056  0.0439  168 PHE   A CG  
3826 C CG  B PHE   A 168 ? 0.4209 0.4551 0.4474 0.0528  -0.0128 -0.0126 168 PHE   A CG  
3827 C CD1 A PHE   A 168 ? 0.1579 0.2582 0.1727 -0.0030 0.0024  0.0471  168 PHE   A CD1 
3828 C CD1 B PHE   A 168 ? 0.4231 0.4582 0.4529 0.0582  -0.0110 -0.0116 168 PHE   A CD1 
3829 C CD2 A PHE   A 168 ? 0.1513 0.2511 0.1596 0.0009  0.0249  0.0455  168 PHE   A CD2 
3830 C CD2 B PHE   A 168 ? 0.4227 0.4582 0.4526 0.0591  -0.0093 -0.0126 168 PHE   A CD2 
3831 C CE1 A PHE   A 168 ? 0.1549 0.2569 0.1829 -0.0042 0.0005  0.0547  168 PHE   A CE1 
3832 C CE1 B PHE   A 168 ? 0.4240 0.4605 0.4540 0.0618  -0.0081 -0.0118 168 PHE   A CE1 
3833 C CE2 A PHE   A 168 ? 0.1619 0.2468 0.1766 0.0016  0.0150  0.0539  168 PHE   A CE2 
3834 C CE2 B PHE   A 168 ? 0.4239 0.4603 0.4561 0.0623  -0.0071 -0.0124 168 PHE   A CE2 
3835 C CZ  A PHE   A 168 ? 0.1549 0.2490 0.1830 -0.0009 0.0021  0.0536  168 PHE   A CZ  
3836 C CZ  B PHE   A 168 ? 0.4243 0.4610 0.4566 0.0638  -0.0073 -0.0119 168 PHE   A CZ  
3855 N N   A LEU   A 169 ? 0.1818 0.2992 0.2168 0.0068  0.0440  0.0051  169 LEU   A N   
3856 N N   B LEU   A 169 ? 0.4389 0.4560 0.4599 0.0092  -0.0246 -0.0172 169 LEU   A N   
3857 C CA  A LEU   A 169 ? 0.2222 0.3146 0.2754 0.0130  0.0194  0.0104  169 LEU   A CA  
3858 C CA  B LEU   A 169 ? 0.4522 0.4639 0.4713 -0.0001 -0.0234 -0.0155 169 LEU   A CA  
3859 C C   A LEU   A 169 ? 0.2246 0.3118 0.2797 0.0106  0.0190  0.0295  169 LEU   A C   
3860 C C   B LEU   A 169 ? 0.4575 0.4674 0.4806 -0.0031 -0.0302 -0.0109 169 LEU   A C   
3861 O O   A LEU   A 169 ? 0.2274 0.3120 0.2857 0.0129  0.0174  0.0217  169 LEU   A O   
3862 O O   B LEU   A 169 ? 0.4598 0.4696 0.4844 -0.0036 -0.0319 -0.0052 169 LEU   A O   
3863 C CB  A LEU   A 169 ? 0.2487 0.3280 0.3041 0.0153  0.0024  -0.0081 169 LEU   A CB  
3864 C CB  B LEU   A 169 ? 0.4595 0.4685 0.4742 -0.0060 -0.0136 -0.0163 169 LEU   A CB  
3865 C CG  A LEU   A 169 ? 0.2741 0.3419 0.3403 0.0139  -0.0133 -0.0298 169 LEU   A CG  
3866 C CG  B LEU   A 169 ? 0.4659 0.4729 0.4767 -0.0096 -0.0051 -0.0168 169 LEU   A CG  
3867 C CD1 A LEU   A 169 ? 0.2839 0.3446 0.3608 0.0169  -0.0218 -0.0331 169 LEU   A CD1 
3868 C CD1 B LEU   A 169 ? 0.4682 0.4748 0.4762 -0.0118 -0.0004 -0.0176 169 LEU   A CD1 
3869 C CD2 A LEU   A 169 ? 0.2822 0.3489 0.3529 0.0104  -0.0159 -0.0350 169 LEU   A CD2 
3870 C CD2 B LEU   A 169 ? 0.4681 0.4748 0.4751 -0.0119 -0.0046 -0.0153 169 LEU   A CD2 
3871 O OXT A LEU   A 169 ? 0.2184 0.3135 0.2744 0.0066  0.0218  0.0445  169 LEU   A OXT 
3872 O OXT B LEU   A 169 ? 0.4598 0.4678 0.4826 -0.0042 -0.0320 -0.0126 169 LEU   A OXT 
3895 N N   A SER   B 1   ? 0.3745 0.3701 0.3371 -0.1031 -0.0688 0.0182  1   SER   B N   
3896 N N   B SER   B 1   ? 0.2419 0.2352 0.3062 -0.0347 -0.0492 -0.0196 1   SER   B N   
3897 C CA  A SER   B 1   ? 0.3691 0.3731 0.3495 -0.1082 -0.0697 0.0186  1   SER   B CA  
3898 C CA  B SER   B 1   ? 0.2298 0.2343 0.2927 -0.0494 -0.0619 -0.0402 1   SER   B CA  
3899 C C   A SER   B 1   ? 0.3512 0.3696 0.3380 -0.1148 -0.0697 0.0436  1   SER   B C   
3900 C C   B SER   B 1   ? 0.2125 0.2230 0.2603 -0.0443 -0.0714 -0.0472 1   SER   B C   
3901 O O   A SER   B 1   ? 0.3582 0.3761 0.3367 -0.1127 -0.0577 0.0468  1   SER   B O   
3902 O O   B SER   B 1   ? 0.2179 0.2305 0.2847 -0.0513 -0.0723 -0.0504 1   SER   B O   
3903 C CB  A SER   B 1   ? 0.3779 0.3739 0.3702 -0.1069 -0.0626 -0.0010 1   SER   B CB  
3904 C CB  B SER   B 1   ? 0.2296 0.2386 0.3300 -0.0578 -0.0611 -0.0566 1   SER   B CB  
3905 O OG  A SER   B 1   ? 0.3861 0.3802 0.4100 -0.1054 -0.0508 -0.0102 1   SER   B OG  
3906 O OG  B SER   B 1   ? 0.2344 0.2504 0.3754 -0.0655 -0.0549 -0.0484 1   SER   B OG  
3921 N N   A MET   B 2   ? 0.3320 0.3579 0.3377 -0.1192 -0.0673 0.0831  2   MET   B N   
3922 N N   B MET   B 2   ? 0.2056 0.2096 0.2141 -0.0237 -0.0607 -0.0521 2   MET   B N   
3923 C CA  A MET   B 2   ? 0.3179 0.3487 0.3532 -0.1096 -0.0733 0.1056  2   MET   B CA  
3924 C CA  B MET   B 2   ? 0.2118 0.2021 0.1942 -0.0096 -0.0556 -0.0413 2   MET   B CA  
3925 C C   A MET   B 2   ? 0.2806 0.3140 0.3199 -0.0943 -0.0905 0.1229  2   MET   B C   
3926 C C   B MET   B 2   ? 0.2023 0.1982 0.2028 -0.0015 -0.0478 -0.0008 2   MET   B C   
3927 O O   A MET   B 2   ? 0.2706 0.3106 0.3005 -0.0959 -0.1152 0.1285  2   MET   B O   
3928 O O   B MET   B 2   ? 0.2171 0.2122 0.2277 0.0143  -0.0417 0.0129  2   MET   B O   
3929 C CB  A MET   B 2   ? 0.3478 0.3805 0.4322 -0.1001 -0.0565 0.0910  2   MET   B CB  
3930 C CB  B MET   B 2   ? 0.2434 0.2135 0.2110 -0.0074 -0.0298 -0.0705 2   MET   B CB  
3931 C CG  A MET   B 2   ? 0.3751 0.4099 0.5151 -0.0873 -0.0432 0.0791  2   MET   B CG  
3932 C CG  B MET   B 2   ? 0.2764 0.2327 0.2335 -0.0056 -0.0234 -0.0665 2   MET   B CG  
3933 S SD  A MET   B 2   ? 0.4025 0.4396 0.5940 -0.0729 -0.0303 0.0670  2   MET   B SD  
3934 S SD  B MET   B 2   ? 0.3090 0.2492 0.2426 0.0022  -0.0004 -0.0726 2   MET   B SD  
3935 C CE  A MET   B 2   ? 0.4064 0.4447 0.6032 -0.0713 -0.0234 0.0711  2   MET   B CE  
3936 C CE  B MET   B 2   ? 0.3122 0.2640 0.2691 -0.0044 -0.0006 -0.0704 2   MET   B CE  
3955 N N   A VAL   B 3   ? 0.2472 0.2751 0.2948 -0.0906 -0.0776 0.1384  3   VAL   B N   
3956 N N   B VAL   B 3   ? 0.1865 0.1786 0.2105 -0.0146 -0.0383 0.0232  3   VAL   B N   
3957 C CA  A VAL   B 3   ? 0.2254 0.2439 0.2888 -0.0697 -0.0746 0.1084  3   VAL   B CA  
3958 C CA  B VAL   B 3   ? 0.1859 0.1690 0.2141 -0.0240 -0.0432 0.0270  3   VAL   B CA  
3959 C C   A VAL   B 3   ? 0.1976 0.2190 0.2543 -0.0567 -0.0623 0.0896  3   VAL   B C   
3960 C C   B VAL   B 3   ? 0.1759 0.1613 0.1975 -0.0280 -0.0418 0.0235  3   VAL   B C   
3961 O O   A VAL   B 3   ? 0.1926 0.2283 0.2631 -0.0461 -0.0650 0.1022  3   VAL   B O   
3962 O O   B VAL   B 3   ? 0.1665 0.1335 0.1760 -0.0177 -0.0237 -0.0086 3   VAL   B O   
3963 C CB  A VAL   B 3   ? 0.2370 0.2348 0.3269 -0.0647 -0.0697 0.1006  3   VAL   B CB  
3964 C CB  B VAL   B 3   ? 0.1974 0.1706 0.2490 -0.0326 -0.0352 0.0113  3   VAL   B CB  
3965 C CG1 A VAL   B 3   ? 0.2414 0.2327 0.3464 -0.0680 -0.0614 0.0950  3   VAL   B CG1 
3966 C CG1 B VAL   B 3   ? 0.1998 0.1737 0.2672 -0.0406 -0.0342 0.0135  3   VAL   B CG1 
3967 C CG2 A VAL   B 3   ? 0.2433 0.2299 0.3388 -0.0573 -0.0604 0.1100  3   VAL   B CG2 
3968 C CG2 B VAL   B 3   ? 0.2067 0.1696 0.2552 -0.0239 -0.0190 0.0044  3   VAL   B CG2 
3987 N N   . ASN   B 4   ? 0.1787 0.1890 0.2104 -0.0458 -0.0575 0.0589  4   ASN   B N   
3988 C CA  . ASN   B 4   ? 0.1831 0.1942 0.1949 -0.0455 -0.0604 0.0339  4   ASN   B CA  
3989 C C   . ASN   B 4   ? 0.1996 0.2031 0.1904 -0.0456 -0.0443 0.0248  4   ASN   B C   
3990 O O   . ASN   B 4   ? 0.2010 0.2089 0.1978 -0.0453 -0.0427 0.0087  4   ASN   B O   
3991 C CB  . ASN   B 4   ? 0.1885 0.1944 0.1785 -0.0484 -0.0609 0.0250  4   ASN   B CB  
3992 C CG  . ASN   B 4   ? 0.1908 0.1798 0.1732 -0.0411 -0.0649 0.0272  4   ASN   B CG  
3993 O OD1 . ASN   B 4   ? 0.1967 0.1671 0.1693 -0.0371 -0.0543 0.0316  4   ASN   B OD1 
3994 N ND2 . ASN   B 4   ? 0.2096 0.1856 0.1951 -0.0216 -0.0442 0.0213  4   ASN   B ND2 
4002 N N   . SER   B 5   ? 0.2095 0.2100 0.1996 -0.0566 -0.0333 0.0249  5   SER   B N   
4003 C CA  . SER   B 5   ? 0.2367 0.2458 0.2194 -0.0496 -0.0186 0.0240  5   SER   B CA  
4004 C C   . SER   B 5   ? 0.2598 0.2508 0.2514 -0.0630 -0.0053 0.0365  5   SER   B C   
4005 O O   . SER   B 5   ? 0.2820 0.2374 0.3089 -0.0486 0.0257  0.0287  5   SER   B O   
4006 C CB  . SER   B 5   ? 0.2524 0.2684 0.2510 -0.0439 -0.0094 0.0333  5   SER   B CB  
4007 O OG  . SER   B 5   ? 0.2890 0.3015 0.3253 -0.0305 -0.0088 0.0369  5   SER   B OG  
4013 N N   . PHE   B 6   ? 0.2812 0.2859 0.2504 -0.0796 0.0107  0.0460  6   PHE   B N   
4014 C CA  . PHE   B 6   ? 0.2968 0.2975 0.2074 -0.1120 0.0187  0.0262  6   PHE   B CA  
4015 C C   . PHE   B 6   ? 0.3618 0.3465 0.2652 -0.1205 0.0607  -0.0105 6   PHE   B C   
4016 O O   . PHE   B 6   ? 0.3786 0.3971 0.3072 -0.1050 0.0478  -0.0222 6   PHE   B O   
4017 C CB  . PHE   B 6   ? 0.2639 0.2768 0.1861 -0.1016 -0.0091 0.0247  6   PHE   B CB  
4018 C CG  . PHE   B 6   ? 0.2297 0.2478 0.1971 -0.0890 -0.0150 0.0306  6   PHE   B CG  
4019 C CD1 . PHE   B 6   ? 0.2250 0.2206 0.1836 -0.0801 -0.0311 0.0218  6   PHE   B CD1 
4020 C CD2 . PHE   B 6   ? 0.2047 0.2474 0.2056 -0.0706 -0.0211 0.0522  6   PHE   B CD2 
4021 C CE1 . PHE   B 6   ? 0.2208 0.1989 0.1940 -0.0616 -0.0377 0.0250  6   PHE   B CE1 
4022 C CE2 . PHE   B 6   ? 0.2013 0.2274 0.2338 -0.0578 -0.0165 0.0557  6   PHE   B CE2 
4023 C CZ  . PHE   B 6   ? 0.2083 0.2053 0.2171 -0.0566 -0.0299 0.0368  6   PHE   B CZ  
4033 N N   A SER   B 7   ? 0.3922 0.3281 0.2680 -0.1426 0.0910  -0.0300 7   SER   B N   
4034 N N   B SER   B 7   ? 0.3892 0.3400 0.2892 -0.1302 0.0783  -0.0228 7   SER   B N   
4035 C CA  A SER   B 7   ? 0.4214 0.3342 0.3143 -0.1429 0.1073  -0.0433 7   SER   B CA  
4036 C CA  B SER   B 7   ? 0.4143 0.3475 0.3349 -0.1267 0.0873  -0.0308 7   SER   B CA  
4037 C C   A SER   B 7   ? 0.4262 0.3184 0.2960 -0.1448 0.1193  -0.0550 7   SER   B C   
4038 C C   B SER   B 7   ? 0.4207 0.3359 0.3219 -0.1265 0.0927  -0.0383 7   SER   B C   
4039 O O   A SER   B 7   ? 0.4329 0.3174 0.3116 -0.1457 0.1218  -0.0590 7   SER   B O   
4040 O O   B SER   B 7   ? 0.4261 0.3379 0.3333 -0.1264 0.0923  -0.0385 7   SER   B O   
4041 C CB  A SER   B 7   ? 0.4390 0.3520 0.3817 -0.1350 0.1163  -0.0391 7   SER   B CB  
4042 C CB  B SER   B 7   ? 0.4279 0.3611 0.3893 -0.1200 0.0933  -0.0285 7   SER   B CB  
4043 O OG  A SER   B 7   ? 0.4507 0.3606 0.4319 -0.1284 0.1162  -0.0347 7   SER   B OG  
4044 O OG  B SER   B 7   ? 0.4367 0.3665 0.4257 -0.1154 0.0932  -0.0257 7   SER   B OG  
4055 N N   A GLY   B 8   ? 0.4276 0.3107 0.2893 -0.1319 0.1243  -0.0675 8   GLY   B N   
4056 N N   B GLY   B 8   ? 0.4222 0.3246 0.3120 -0.1195 0.0976  -0.0490 8   GLY   B N   
4057 C CA  A GLY   B 8   ? 0.4203 0.2993 0.2882 -0.1252 0.1239  -0.0733 8   GLY   B CA  
4058 C CA  B GLY   B 8   ? 0.4170 0.3096 0.3017 -0.1163 0.1004  -0.0572 8   GLY   B CA  
4059 C C   A GLY   B 8   ? 0.4071 0.2783 0.2760 -0.1230 0.1262  -0.0660 8   GLY   B C   
4060 C C   B GLY   B 8   ? 0.4071 0.2869 0.2838 -0.1159 0.1055  -0.0580 8   GLY   B C   
4061 O O   A GLY   B 8   ? 0.4123 0.2780 0.2948 -0.1224 0.1346  -0.0738 8   GLY   B O   
4062 O O   B GLY   B 8   ? 0.4135 0.2922 0.2962 -0.1105 0.1068  -0.0617 8   GLY   B O   
4069 N N   . TYR   B 9   ? 0.3953 0.2615 0.2642 -0.1128 0.0991  -0.0674 9   TYR   B N   
4070 C CA  . TYR   B 9   ? 0.3701 0.2231 0.2354 -0.0913 0.0706  -0.0472 9   TYR   B CA  
4071 C C   . TYR   B 9   ? 0.3619 0.2276 0.2151 -0.0788 0.0434  -0.0383 9   TYR   B C   
4072 O O   . TYR   B 9   ? 0.3734 0.2472 0.2522 -0.0805 0.0456  -0.0270 9   TYR   B O   
4073 C CB  . TYR   B 9   ? 0.3653 0.1901 0.2568 -0.0776 0.0619  -0.0360 9   TYR   B CB  
4074 C CG  . TYR   B 9   ? 0.3520 0.1712 0.2472 -0.0818 0.0593  -0.0357 9   TYR   B CG  
4075 C CD1 . TYR   B 9   ? 0.3515 0.1763 0.2651 -0.0959 0.0605  -0.0360 9   TYR   B CD1 
4076 C CD2 . TYR   B 9   ? 0.3382 0.1681 0.2310 -0.0701 0.0545  -0.0388 9   TYR   B CD2 
4077 C CE1 . TYR   B 9   ? 0.3420 0.1836 0.2587 -0.0999 0.0689  -0.0491 9   TYR   B CE1 
4078 C CE2 . TYR   B 9   ? 0.3351 0.1655 0.2387 -0.0785 0.0593  -0.0345 9   TYR   B CE2 
4079 C CZ  . TYR   B 9   ? 0.3362 0.1820 0.2624 -0.0903 0.0638  -0.0598 9   TYR   B CZ  
4080 O OH  . TYR   B 9   ? 0.3298 0.1976 0.2838 -0.0996 0.0616  -0.0798 9   TYR   B OH  
4091 N N   . LEU   B 10  ? 0.3363 0.1999 0.1855 -0.0747 0.0235  -0.0426 10  LEU   B N   
4092 C CA  . LEU   B 10  ? 0.3291 0.1960 0.1967 -0.0847 -0.0118 -0.0359 10  LEU   B CA  
4093 C C   . LEU   B 10  ? 0.3088 0.1991 0.2010 -0.0844 -0.0251 -0.0251 10  LEU   B C   
4094 O O   . LEU   B 10  ? 0.2913 0.1985 0.1949 -0.0688 -0.0202 -0.0207 10  LEU   B O   
4095 C CB  . LEU   B 10  ? 0.3396 0.1960 0.2223 -0.0900 -0.0384 -0.0137 10  LEU   B CB  
4096 C CG  . LEU   B 10  ? 0.3554 0.2046 0.2586 -0.0818 -0.0699 0.0042  10  LEU   B CG  
4097 C CD1 . LEU   B 10  ? 0.3688 0.2147 0.2825 -0.0776 -0.0646 0.0085  10  LEU   B CD1 
4098 C CD2 . LEU   B 10  ? 0.3608 0.2097 0.2903 -0.0842 -0.0643 0.0276  10  LEU   B CD2 
4110 N N   . LYS   B 11  ? 0.3247 0.2228 0.2041 -0.0758 -0.0340 -0.0179 11  LYS   B N   
4111 C CA  . LYS   B 11  ? 0.3355 0.2481 0.2421 -0.0593 -0.0565 -0.0246 11  LYS   B CA  
4112 C C   . LYS   B 11  ? 0.3123 0.2234 0.2457 -0.0773 -0.0526 -0.0326 11  LYS   B C   
4113 O O   . LYS   B 11  ? 0.3312 0.2428 0.2804 -0.0910 -0.0509 -0.0619 11  LYS   B O   
4114 C CB  . LYS   B 11  ? 0.3708 0.3018 0.3182 -0.0246 -0.0584 -0.0152 11  LYS   B CB  
4115 C CG  . LYS   B 11  ? 0.3990 0.3364 0.3936 -0.0056 -0.0642 -0.0120 11  LYS   B CG  
4116 C CD  . LYS   B 11  ? 0.4226 0.3600 0.4683 0.0017  -0.0628 -0.0167 11  LYS   B CD  
4117 C CE  . LYS   B 11  ? 0.4391 0.3766 0.5259 0.0023  -0.0619 -0.0185 11  LYS   B CE  
4118 N NZ  . LYS   B 11  ? 0.4475 0.3852 0.5514 0.0009  -0.0635 -0.0159 11  LYS   B NZ  
4132 N N   . LEU   B 12  ? 0.2757 0.2032 0.2465 -0.0715 -0.0492 -0.0294 12  LEU   B N   
4133 C CA  . LEU   B 12  ? 0.2597 0.1857 0.2664 -0.0630 -0.0418 -0.0162 12  LEU   B CA  
4134 C C   . LEU   B 12  ? 0.2486 0.1899 0.2698 -0.0683 -0.0682 -0.0172 12  LEU   B C   
4135 O O   . LEU   B 12  ? 0.2470 0.1971 0.2928 -0.0776 -0.0752 -0.0124 12  LEU   B O   
4136 C CB  . LEU   B 12  ? 0.2565 0.1666 0.2716 -0.0515 -0.0299 -0.0227 12  LEU   B CB  
4137 C CG  . LEU   B 12  ? 0.2489 0.1647 0.2714 -0.0483 -0.0214 -0.0248 12  LEU   B CG  
4138 C CD1 . LEU   B 12  ? 0.2551 0.1656 0.2588 -0.0284 -0.0198 -0.0082 12  LEU   B CD1 
4139 C CD2 . LEU   B 12  ? 0.2481 0.1684 0.2845 -0.0470 -0.0128 -0.0367 12  LEU   B CD2 
4151 N N   . THR   B 13  ? 0.2406 0.1914 0.2671 -0.0644 -0.0720 -0.0259 13  THR   B N   
4152 C CA  . THR   B 13  ? 0.2397 0.2040 0.2625 -0.0663 -0.0846 -0.0134 13  THR   B CA  
4153 C C   . THR   B 13  ? 0.2766 0.2188 0.2928 -0.0700 -0.0949 -0.0025 13  THR   B C   
4154 O O   . THR   B 13  ? 0.2991 0.2110 0.3124 -0.0730 -0.0643 -0.0043 13  THR   B O   
4155 C CB  . THR   B 13  ? 0.2201 0.2065 0.2636 -0.0573 -0.0682 -0.0058 13  THR   B CB  
4156 O OG1 . THR   B 13  ? 0.2013 0.1966 0.2754 -0.0535 -0.0583 -0.0124 13  THR   B OG1 
4157 C CG2 . THR   B 13  ? 0.2254 0.2154 0.2668 -0.0533 -0.0556 -0.0010 13  THR   B CG2 
4165 N N   A ASP   B 14  ? 0.2818 0.2309 0.2973 -0.0802 -0.1219 0.0025  14  ASP   B N   
4166 N N   B ASP   B 14  ? 0.2821 0.2303 0.2958 -0.0745 -0.1079 0.0065  14  ASP   B N   
4167 C CA  A ASP   B 14  ? 0.2929 0.2459 0.3243 -0.0739 -0.1230 0.0213  14  ASP   B CA  
4168 C CA  B ASP   B 14  ? 0.2904 0.2429 0.3150 -0.0686 -0.1046 0.0232  14  ASP   B CA  
4169 C C   A ASP   B 14  ? 0.2831 0.2262 0.2853 -0.0779 -0.1097 0.0188  14  ASP   B C   
4170 C C   B ASP   B 14  ? 0.2795 0.2239 0.2806 -0.0730 -0.1046 0.0214  14  ASP   B C   
4171 O O   A ASP   B 14  ? 0.3093 0.2422 0.2916 -0.0771 -0.0969 0.0219  14  ASP   B O   
4172 O O   B ASP   B 14  ? 0.2994 0.2334 0.2810 -0.0725 -0.1030 0.0264  14  ASP   B O   
4173 C CB  A ASP   B 14  ? 0.3129 0.2775 0.4015 -0.0673 -0.1287 0.0196  14  ASP   B CB  
4174 C CB  B ASP   B 14  ? 0.3089 0.2723 0.3758 -0.0602 -0.0951 0.0253  14  ASP   B CB  
4175 C CG  A ASP   B 14  ? 0.3357 0.3070 0.4768 -0.0583 -0.1179 0.0033  14  ASP   B CG  
4176 C CG  B ASP   B 14  ? 0.3277 0.3004 0.4338 -0.0507 -0.0781 0.0158  14  ASP   B CG  
4177 O OD1 A ASP   B 14  ? 0.3483 0.3121 0.4919 -0.0670 -0.1165 -0.0098 14  ASP   B OD1 
4178 O OD1 B ASP   B 14  ? 0.3372 0.3109 0.4470 -0.0492 -0.0683 0.0133  14  ASP   B OD1 
4179 O OD2 A ASP   B 14  ? 0.3414 0.3238 0.5147 -0.0519 -0.1092 0.0022  14  ASP   B OD2 
4180 O OD2 B ASP   B 14  ? 0.3325 0.3129 0.4609 -0.0506 -0.0735 0.0125  14  ASP   B OD2 
4189 N N   . ASN   B 15  ? 0.2538 0.2004 0.2638 -0.0632 -0.1032 0.0191  15  ASN   B N   
4190 C CA  . ASN   B 15  ? 0.2083 0.1729 0.2496 -0.0415 -0.0755 0.0084  15  ASN   B CA  
4191 C C   . ASN   B 15  ? 0.1887 0.1573 0.2240 -0.0299 -0.0570 0.0063  15  ASN   B C   
4192 O O   . ASN   B 15  ? 0.1842 0.1485 0.2404 -0.0336 -0.0515 -0.0043 15  ASN   B O   
4193 C CB  . ASN   B 15  ? 0.2019 0.1679 0.2658 -0.0250 -0.0755 0.0205  15  ASN   B CB  
4194 C CG  . ASN   B 15  ? 0.1868 0.1643 0.2690 -0.0336 -0.0429 0.0189  15  ASN   B CG  
4195 O OD1 . ASN   B 15  ? 0.1933 0.1926 0.3037 -0.0534 -0.0412 0.0199  15  ASN   B OD1 
4196 N ND2 . ASN   B 15  ? 0.1813 0.1432 0.2456 -0.0178 -0.0089 -0.0010 15  ASN   B ND2 
4204 N N   . VAL   B 16  ? 0.1845 0.1468 0.2187 -0.0402 -0.0586 0.0032  16  VAL   B N   
4205 C CA  . VAL   B 16  ? 0.1918 0.1567 0.1953 -0.0320 -0.0533 -0.0190 16  VAL   B CA  
4206 C C   . VAL   B 16  ? 0.1945 0.1628 0.1994 -0.0408 -0.0510 -0.0107 16  VAL   B C   
4207 O O   . VAL   B 16  ? 0.1936 0.1728 0.2318 -0.0359 -0.0508 -0.0244 16  VAL   B O   
4208 C CB  . VAL   B 16  ? 0.1931 0.1539 0.2253 -0.0167 -0.0376 -0.0127 16  VAL   B CB  
4209 C CG1 . VAL   B 16  ? 0.1971 0.1508 0.2326 -0.0019 -0.0277 -0.0061 16  VAL   B CG1 
4210 C CG2 . VAL   B 16  ? 0.1976 0.1615 0.2479 -0.0076 -0.0311 -0.0132 16  VAL   B CG2 
4220 N N   . TYR   B 17  ? 0.2016 0.1745 0.1933 -0.0392 -0.0421 -0.0100 17  TYR   B N   
4221 C CA  . TYR   B 17  ? 0.2080 0.1856 0.1835 -0.0521 -0.0430 0.0028  17  TYR   B CA  
4222 C C   . TYR   B 17  ? 0.2023 0.1564 0.1795 -0.0529 -0.0342 -0.0061 17  TYR   B C   
4223 O O   . TYR   B 17  ? 0.1963 0.1603 0.1924 -0.0412 -0.0420 -0.0268 17  TYR   B O   
4224 C CB  . TYR   B 17  ? 0.2370 0.2294 0.2144 -0.0417 -0.0414 0.0406  17  TYR   B CB  
4225 C CG  . TYR   B 17  ? 0.2668 0.2774 0.2632 -0.0342 -0.0568 0.0552  17  TYR   B CG  
4226 C CD1 . TYR   B 17  ? 0.2808 0.2950 0.2960 -0.0277 -0.0722 0.0672  17  TYR   B CD1 
4227 C CD2 . TYR   B 17  ? 0.2901 0.3074 0.2895 -0.0218 -0.0709 0.0576  17  TYR   B CD2 
4228 C CE1 . TYR   B 17  ? 0.3000 0.3207 0.3140 -0.0185 -0.0847 0.0601  17  TYR   B CE1 
4229 C CE2 . TYR   B 17  ? 0.3062 0.3280 0.3105 -0.0074 -0.0858 0.0625  17  TYR   B CE2 
4230 C CZ  . TYR   B 17  ? 0.3159 0.3359 0.3222 -0.0060 -0.0925 0.0642  17  TYR   B CZ  
4231 O OH  . TYR   B 17  ? 0.3329 0.3560 0.3422 0.0047  -0.1021 0.0638  17  TYR   B OH  
4241 N N   . ILE   B 18  ? 0.2151 0.1573 0.1765 -0.0511 -0.0149 -0.0045 18  ILE   B N   
4242 C CA  . ILE   B 18  ? 0.2135 0.1551 0.1811 -0.0461 -0.0171 -0.0142 18  ILE   B CA  
4243 C C   . ILE   B 18  ? 0.2340 0.1645 0.1607 -0.0563 -0.0105 -0.0249 18  ILE   B C   
4244 O O   . ILE   B 18  ? 0.2534 0.1844 0.1758 -0.0553 -0.0053 -0.0289 18  ILE   B O   
4245 C CB  . ILE   B 18  ? 0.2136 0.1555 0.1933 -0.0468 -0.0208 -0.0141 18  ILE   B CB  
4246 C CG1 . ILE   B 18  ? 0.2120 0.1605 0.2004 -0.0452 -0.0120 -0.0044 18  ILE   B CG1 
4247 C CG2 . ILE   B 18  ? 0.2234 0.1645 0.2011 -0.0459 -0.0252 -0.0027 18  ILE   B CG2 
4248 C CD1 . ILE   B 18  ? 0.2176 0.1853 0.2247 -0.0469 -0.0099 0.0188  18  ILE   B CD1 
4260 N N   . LYS   B 19  ? 0.2342 0.1567 0.1922 -0.0331 0.0282  -0.0324 19  LYS   B N   
4261 C CA  . LYS   B 19  ? 0.2376 0.1608 0.2143 -0.0421 0.0310  -0.0401 19  LYS   B CA  
4262 C C   . LYS   B 19  ? 0.2120 0.1617 0.2296 -0.0392 0.0276  -0.0512 19  LYS   B C   
4263 O O   . LYS   B 19  ? 0.2007 0.1642 0.2205 -0.0298 0.0179  -0.0458 19  LYS   B O   
4264 C CB  . LYS   B 19  ? 0.2668 0.1817 0.2242 -0.0484 0.0416  -0.0309 19  LYS   B CB  
4265 C CG  . LYS   B 19  ? 0.2976 0.2024 0.2524 -0.0508 0.0484  -0.0258 19  LYS   B CG  
4266 C CD  . LYS   B 19  ? 0.3240 0.2267 0.2534 -0.0557 0.0561  -0.0290 19  LYS   B CD  
4267 C CE  . LYS   B 19  ? 0.3464 0.2504 0.2691 -0.0642 0.0441  -0.0312 19  LYS   B CE  
4268 N NZ  . LYS   B 19  ? 0.3652 0.2646 0.2683 -0.0695 0.0413  -0.0320 19  LYS   B NZ  
4282 N N   . ASN   B 20  ? 0.2102 0.1732 0.2527 -0.0350 0.0439  -0.0593 20  ASN   B N   
4283 C CA  . ASN   B 20  ? 0.2036 0.1920 0.2829 -0.0299 0.0435  -0.0813 20  ASN   B CA  
4284 C C   . ASN   B 20  ? 0.2058 0.2113 0.2801 -0.0358 0.0585  -0.0910 20  ASN   B C   
4285 O O   . ASN   B 20  ? 0.2289 0.2438 0.2982 -0.0471 0.0632  -0.0905 20  ASN   B O   
4286 C CB  . ASN   B 20  ? 0.2320 0.1975 0.3253 -0.0051 0.0307  -0.0825 20  ASN   B CB  
4287 C CG  . ASN   B 20  ? 0.2584 0.2041 0.3599 0.0301  0.0300  -0.0956 20  ASN   B CG  
4288 O OD1 . ASN   B 20  ? 0.2919 0.2316 0.3872 0.0425  0.0278  -0.0997 20  ASN   B OD1 
4289 N ND2 . ASN   B 20  ? 0.2467 0.2065 0.3558 0.0316  0.0133  -0.0852 20  ASN   B ND2 
4296 N N   . ALA   B 21  ? 0.2073 0.1914 0.2854 -0.0396 0.0595  -0.0713 21  ALA   B N   
4297 C CA  . ALA   B 21  ? 0.2160 0.1979 0.3027 -0.0404 0.0483  -0.0585 21  ALA   B CA  
4298 C C   . ALA   B 21  ? 0.2140 0.1726 0.2859 -0.0258 0.0475  -0.0433 21  ALA   B C   
4299 O O   . ALA   B 21  ? 0.2130 0.1677 0.2710 -0.0411 0.0357  -0.0335 21  ALA   B O   
4300 C CB  . ALA   B 21  ? 0.2329 0.2254 0.3188 -0.0614 0.0507  -0.0429 21  ALA   B CB  
4306 N N   . ASP   B 22  ? 0.2052 0.1594 0.2788 -0.0258 0.0352  -0.0313 22  ASP   B N   
4307 C CA  . ASP   B 22  ? 0.1957 0.1537 0.2622 -0.0180 0.0294  -0.0208 22  ASP   B CA  
4308 C C   . ASP   B 22  ? 0.1870 0.1500 0.2105 -0.0235 0.0172  -0.0130 22  ASP   B C   
4309 O O   . ASP   B 22  ? 0.1973 0.1543 0.2182 -0.0149 0.0127  -0.0108 22  ASP   B O   
4310 C CB  . ASP   B 22  ? 0.1998 0.1605 0.2980 -0.0074 0.0350  -0.0048 22  ASP   B CB  
4311 C CG  . ASP   B 22  ? 0.2037 0.1867 0.3446 -0.0000 0.0165  -0.0007 22  ASP   B CG  
4312 O OD1 . ASP   B 22  ? 0.2117 0.1767 0.3447 0.0030  -0.0120 0.0050  22  ASP   B OD1 
4313 O OD2 . ASP   B 22  ? 0.2125 0.2126 0.4011 0.0109  -0.0082 -0.0178 22  ASP   B OD2 
4318 N N   . ILE   B 23  ? 0.1873 0.1459 0.1858 -0.0134 -0.0011 0.0058  23  ILE   B N   
4319 C CA  . ILE   B 23  ? 0.1802 0.1434 0.1720 -0.0140 -0.0027 0.0023  23  ILE   B CA  
4320 C C   . ILE   B 23  ? 0.1717 0.1478 0.1743 -0.0073 -0.0179 0.0079  23  ILE   B C   
4321 O O   . ILE   B 23  ? 0.1621 0.1456 0.1705 -0.0138 -0.0093 0.0102  23  ILE   B O   
4322 C CB  . ILE   B 23  ? 0.1747 0.1556 0.1916 -0.0230 0.0017  0.0161  23  ILE   B CB  
4323 C CG1 . ILE   B 23  ? 0.1798 0.1617 0.2070 -0.0131 0.0102  0.0254  23  ILE   B CG1 
4324 C CG2 . ILE   B 23  ? 0.1833 0.1802 0.1899 -0.0207 0.0063  0.0138  23  ILE   B CG2 
4325 C CD1 . ILE   B 23  ? 0.1922 0.1720 0.2144 -0.0078 0.0005  0.0243  23  ILE   B CD1 
4337 N N   . VAL   B 24  ? 0.1738 0.1404 0.1863 -0.0109 -0.0159 0.0036  24  VAL   B N   
4338 C CA  . VAL   B 24  ? 0.1662 0.1489 0.2091 -0.0124 -0.0238 -0.0026 24  VAL   B CA  
4339 C C   . VAL   B 24  ? 0.1609 0.1520 0.2211 -0.0157 -0.0058 0.0008  24  VAL   B C   
4340 O O   . VAL   B 24  ? 0.1635 0.1664 0.2337 -0.0194 -0.0109 0.0121  24  VAL   B O   
4341 C CB  . VAL   B 24  ? 0.1760 0.1641 0.2146 -0.0045 -0.0263 -0.0030 24  VAL   B CB  
4342 C CG1 . VAL   B 24  ? 0.1762 0.1685 0.2455 -0.0143 -0.0291 -0.0030 24  VAL   B CG1 
4343 C CG2 . VAL   B 24  ? 0.1837 0.1967 0.2154 -0.0082 -0.0219 -0.0090 24  VAL   B CG2 
4353 N N   . GLU   B 25  ? 0.1874 0.1616 0.2291 -0.0157 0.0083  0.0036  25  GLU   B N   
4354 C CA  . GLU   B 25  ? 0.2035 0.1905 0.2368 -0.0082 0.0157  -0.0030 25  GLU   B CA  
4355 C C   . GLU   B 25  ? 0.1967 0.1809 0.2035 -0.0193 0.0135  -0.0064 25  GLU   B C   
4356 O O   . GLU   B 25  ? 0.2009 0.1965 0.2172 -0.0171 0.0123  0.0027  25  GLU   B O   
4357 C CB  . GLU   B 25  ? 0.2402 0.2441 0.3012 0.0114  0.0294  0.0032  25  GLU   B CB  
4358 C CG  . GLU   B 25  ? 0.2897 0.3147 0.4236 0.0211  0.0251  0.0021  25  GLU   B CG  
4359 C CD  . GLU   B 25  ? 0.3508 0.3829 0.5256 0.0191  0.0249  0.0007  25  GLU   B CD  
4360 O OE1 . GLU   B 25  ? 0.3647 0.4065 0.5591 0.0229  0.0312  0.0032  25  GLU   B OE1 
4361 O OE2 . GLU   B 25  ? 0.3616 0.4018 0.5577 0.0194  0.0190  -0.0053 25  GLU   B OE2 
4368 N N   . GLU   B 26  ? 0.1921 0.1655 0.1833 -0.0326 0.0190  -0.0042 26  GLU   B N   
4369 C CA  . GLU   B 26  ? 0.1905 0.1820 0.1865 -0.0402 -0.0007 0.0001  26  GLU   B CA  
4370 C C   . GLU   B 26  ? 0.1694 0.1805 0.1724 -0.0304 0.0041  0.0221  26  GLU   B C   
4371 O O   . GLU   B 26  ? 0.1978 0.2039 0.1845 -0.0228 0.0044  0.0246  26  GLU   B O   
4372 C CB  . GLU   B 26  ? 0.2239 0.2011 0.2007 -0.0479 0.0119  0.0147  26  GLU   B CB  
4373 C CG  . GLU   B 26  ? 0.2727 0.2433 0.2609 -0.0579 0.0206  -0.0142 26  GLU   B CG  
4374 C CD  . GLU   B 26  ? 0.3028 0.2667 0.2664 -0.0814 0.0284  -0.0543 26  GLU   B CD  
4375 O OE1 . GLU   B 26  ? 0.3236 0.2464 0.2643 -0.0908 0.0888  -0.0469 26  GLU   B OE1 
4376 O OE2 . GLU   B 26  ? 0.3125 0.3184 0.3126 -0.0752 0.0249  -0.0395 26  GLU   B OE2 
4383 N N   . ALA   B 27  ? 0.1579 0.1674 0.1740 -0.0311 0.0053  0.0252  27  ALA   B N   
4384 C CA  . ALA   B 27  ? 0.1639 0.1679 0.1818 -0.0172 -0.0004 0.0332  27  ALA   B CA  
4385 C C   . ALA   B 27  ? 0.1684 0.1696 0.1952 -0.0141 0.0077  0.0457  27  ALA   B C   
4386 O O   . ALA   B 27  ? 0.1677 0.1834 0.2222 -0.0047 0.0001  0.0472  27  ALA   B O   
4387 C CB  . ALA   B 27  ? 0.1802 0.1533 0.1882 -0.0148 -0.0007 0.0242  27  ALA   B CB  
4393 N N   . LYS   B 28  ? 0.1633 0.1763 0.2409 -0.0160 0.0089  0.0450  28  LYS   B N   
4394 C CA  . LYS   B 28  ? 0.1755 0.2084 0.2731 -0.0005 0.0355  0.0779  28  LYS   B CA  
4395 C C   . LYS   B 28  ? 0.1920 0.2190 0.2454 -0.0014 0.0435  0.0661  28  LYS   B C   
4396 O O   . LYS   B 28  ? 0.2190 0.2264 0.2614 -0.0087 0.0525  0.0569  28  LYS   B O   
4397 C CB  . LYS   B 28  ? 0.2033 0.2477 0.3393 0.0180  0.0610  0.1081  28  LYS   B CB  
4398 C CG  . LYS   B 28  ? 0.2367 0.3058 0.3934 0.0280  0.0735  0.1338  28  LYS   B CG  
4399 C CD  . LYS   B 28  ? 0.2983 0.3737 0.4707 0.0347  0.0881  0.1431  28  LYS   B CD  
4400 C CE  . LYS   B 28  ? 0.3511 0.4247 0.5294 0.0440  0.0914  0.1566  28  LYS   B CE  
4401 N NZ  . LYS   B 28  ? 0.4054 0.4501 0.5558 0.0530  0.0898  0.1700  28  LYS   B NZ  
4415 N N   . LYS   B 29  ? 0.2102 0.2412 0.2385 0.0113  0.0445  0.0529  29  LYS   B N   
4416 C CA  . LYS   B 29  ? 0.2556 0.2749 0.2643 0.0129  0.0375  0.0503  29  LYS   B CA  
4417 C C   . LYS   B 29  ? 0.2452 0.2695 0.2274 0.0081  0.0251  0.0542  29  LYS   B C   
4418 O O   . LYS   B 29  ? 0.2674 0.2956 0.2433 0.0194  0.0314  0.0646  29  LYS   B O   
4419 C CB  . LYS   B 29  ? 0.3213 0.3203 0.3481 0.0148  0.0375  0.0359  29  LYS   B CB  
4420 C CG  . LYS   B 29  ? 0.3775 0.3642 0.4387 0.0123  0.0382  0.0342  29  LYS   B CG  
4421 C CD  . LYS   B 29  ? 0.4246 0.3957 0.5112 0.0082  0.0498  0.0290  29  LYS   B CD  
4422 C CE  . LYS   B 29  ? 0.4586 0.4180 0.5602 0.0038  0.0611  0.0247  29  LYS   B CE  
4423 N NZ  . LYS   B 29  ? 0.4756 0.4304 0.5875 0.0022  0.0650  0.0211  29  LYS   B NZ  
4437 N N   . VAL   B 30  ? 0.2073 0.2415 0.2184 -0.0106 0.0060  0.0435  30  VAL   B N   
4438 C CA  . VAL   B 30  ? 0.2023 0.2311 0.2449 -0.0216 -0.0167 0.0499  30  VAL   B CA  
4439 C C   . VAL   B 30  ? 0.1872 0.2236 0.2142 -0.0218 -0.0173 0.0625  30  VAL   B C   
4440 O O   . VAL   B 30  ? 0.2045 0.2418 0.2152 -0.0161 -0.0214 0.0703  30  VAL   B O   
4441 C CB  . VAL   B 30  ? 0.2179 0.2338 0.3189 -0.0359 -0.0343 0.0637  30  VAL   B CB  
4442 C CG1 . VAL   B 30  ? 0.2340 0.2549 0.3372 -0.0220 -0.0257 0.0586  30  VAL   B CG1 
4443 C CG2 . VAL   B 30  ? 0.2359 0.2299 0.3455 -0.0475 -0.0435 0.0602  30  VAL   B CG2 
4453 N N   A LYS   B 31  ? 0.1780 0.2002 0.2378 -0.0327 -0.0198 0.0654  31  LYS   B N   
4454 N N   B LYS   B 31  ? 0.1876 0.2067 0.2322 -0.0277 -0.0245 0.0557  31  LYS   B N   
4455 C CA  A LYS   B 31  ? 0.1629 0.1977 0.2616 -0.0370 -0.0158 0.0680  31  LYS   B CA  
4456 C CA  B LYS   B 31  ? 0.1838 0.2037 0.2515 -0.0292 -0.0285 0.0507  31  LYS   B CA  
4457 C C   A LYS   B 31  ? 0.1617 0.1717 0.2268 -0.0327 -0.0370 0.0647  31  LYS   B C   
4458 C C   B LYS   B 31  ? 0.1754 0.1773 0.2208 -0.0296 -0.0425 0.0498  31  LYS   B C   
4459 O O   A LYS   B 31  ? 0.1656 0.1816 0.2363 -0.0298 -0.0258 0.0805  31  LYS   B O   
4460 O O   B LYS   B 31  ? 0.1798 0.1852 0.2240 -0.0285 -0.0371 0.0538  31  LYS   B O   
4461 C CB  A LYS   B 31  ? 0.1676 0.2333 0.3072 -0.0303 0.0120  0.0800  31  LYS   B CB  
4462 C CB  B LYS   B 31  ? 0.1979 0.2333 0.2945 -0.0224 -0.0164 0.0534  31  LYS   B CB  
4463 C CG  A LYS   B 31  ? 0.1893 0.2710 0.3517 -0.0277 0.0271  0.0856  31  LYS   B CG  
4464 C CG  B LYS   B 31  ? 0.2190 0.2607 0.3342 -0.0206 -0.0094 0.0518  31  LYS   B CG  
4465 C CD  A LYS   B 31  ? 0.2164 0.3103 0.3976 -0.0237 0.0224  0.0833  31  LYS   B CD  
4466 C CD  B LYS   B 31  ? 0.2396 0.2880 0.3716 -0.0187 -0.0111 0.0480  31  LYS   B CD  
4467 C CE  A LYS   B 31  ? 0.2369 0.3371 0.4374 -0.0169 0.0131  0.0763  31  LYS   B CE  
4468 C CE  B LYS   B 31  ? 0.2537 0.3061 0.4062 -0.0137 -0.0144 0.0429  31  LYS   B CE  
4469 N NZ  A LYS   B 31  ? 0.2545 0.3522 0.4497 -0.0042 0.0017  0.0693  31  LYS   B NZ  
4470 N NZ  B LYS   B 31  ? 0.2638 0.3163 0.4170 -0.0038 -0.0240 0.0369  31  LYS   B NZ  
4497 N N   . PRO   B 32  ? 0.1723 0.1573 0.2019 -0.0318 -0.0465 0.0500  32  PRO   B N   
4498 C CA  . PRO   B 32  ? 0.1847 0.1557 0.1790 -0.0329 -0.0390 0.0233  32  PRO   B CA  
4499 C C   . PRO   B 32  ? 0.1889 0.1470 0.1847 -0.0383 -0.0552 0.0282  32  PRO   B C   
4500 O O   . PRO   B 32  ? 0.1986 0.1394 0.2218 -0.0386 -0.0692 0.0239  32  PRO   B O   
4501 C CB  . PRO   B 32  ? 0.1961 0.1470 0.1800 -0.0376 -0.0314 0.0151  32  PRO   B CB  
4502 C CG  . PRO   B 32  ? 0.2114 0.1345 0.1765 -0.0208 -0.0557 0.0151  32  PRO   B CG  
4503 C CD  . PRO   B 32  ? 0.1960 0.1437 0.2027 -0.0241 -0.0575 0.0322  32  PRO   B CD  
4511 N N   . THR   B 33  ? 0.1925 0.1345 0.1757 -0.0338 -0.0522 0.0134  33  THR   B N   
4512 C CA  . THR   B 33  ? 0.1993 0.1477 0.1540 -0.0343 -0.0507 0.0219  33  THR   B CA  
4513 C C   . THR   B 33  ? 0.2003 0.1395 0.1555 -0.0323 -0.0474 0.0157  33  THR   B C   
4514 O O   . THR   B 33  ? 0.2270 0.1432 0.1701 -0.0416 -0.0543 0.0156  33  THR   B O   
4515 C CB  . THR   B 33  ? 0.2053 0.1617 0.1607 -0.0200 -0.0474 0.0282  33  THR   B CB  
4516 O OG1 . THR   B 33  ? 0.1879 0.1649 0.1777 -0.0188 -0.0493 0.0341  33  THR   B OG1 
4517 C CG2 . THR   B 33  ? 0.2248 0.1710 0.1844 -0.0117 -0.0387 0.0176  33  THR   B CG2 
4525 N N   . VAL   B 34  ? 0.1855 0.1350 0.1479 -0.0348 -0.0467 0.0192  34  VAL   B N   
4526 C CA  . VAL   B 34  ? 0.1729 0.1343 0.1453 -0.0304 -0.0400 0.0076  34  VAL   B CA  
4527 C C   . VAL   B 34  ? 0.1597 0.1251 0.1353 -0.0250 -0.0256 0.0090  34  VAL   B C   
4528 O O   . VAL   B 34  ? 0.1735 0.1352 0.1476 -0.0249 -0.0417 0.0044  34  VAL   B O   
4529 C CB  . VAL   B 34  ? 0.1852 0.1408 0.1765 -0.0081 -0.0313 0.0018  34  VAL   B CB  
4530 C CG1 . VAL   B 34  ? 0.1772 0.1613 0.1944 -0.0112 -0.0201 0.0002  34  VAL   B CG1 
4531 C CG2 . VAL   B 34  ? 0.1913 0.1491 0.2092 -0.0105 -0.0220 0.0055  34  VAL   B CG2 
4541 N N   . VAL   B 35  ? 0.1559 0.1274 0.1164 -0.0264 -0.0208 0.0107  35  VAL   B N   
4542 C CA  . VAL   B 35  ? 0.1536 0.1262 0.1228 -0.0203 -0.0089 0.0088  35  VAL   B CA  
4543 C C   . VAL   B 35  ? 0.1402 0.1210 0.1298 -0.0212 -0.0148 0.0065  35  VAL   B C   
4544 O O   . VAL   B 35  ? 0.1469 0.1343 0.1192 -0.0281 -0.0093 -0.0064 35  VAL   B O   
4545 C CB  . VAL   B 35  ? 0.1518 0.1435 0.1383 -0.0184 -0.0011 0.0036  35  VAL   B CB  
4546 C CG1 . VAL   B 35  ? 0.1503 0.1584 0.1639 -0.0284 -0.0050 0.0037  35  VAL   B CG1 
4547 C CG2 . VAL   B 35  ? 0.1537 0.1468 0.1610 -0.0112 -0.0129 -0.0021 35  VAL   B CG2 
4557 N N   . VAL   B 36  ? 0.1397 0.1275 0.1269 -0.0188 -0.0192 0.0101  36  VAL   B N   
4558 C CA  . VAL   B 36  ? 0.1369 0.1191 0.1200 -0.0144 -0.0120 0.0023  36  VAL   B CA  
4559 C C   . VAL   B 36  ? 0.1381 0.1245 0.1130 -0.0143 -0.0071 -0.0007 36  VAL   B C   
4560 O O   . VAL   B 36  ? 0.1446 0.1349 0.1326 -0.0141 -0.0070 -0.0047 36  VAL   B O   
4561 C CB  . VAL   B 36  ? 0.1399 0.1281 0.1311 -0.0172 -0.0026 0.0092  36  VAL   B CB  
4562 C CG1 . VAL   B 36  ? 0.1419 0.1397 0.1465 -0.0200 -0.0098 0.0015  36  VAL   B CG1 
4563 C CG2 . VAL   B 36  ? 0.1449 0.1399 0.1404 -0.0136 -0.0140 0.0136  36  VAL   B CG2 
4573 N N   . ASN   B 37  ? 0.1359 0.1228 0.1205 -0.0011 -0.0083 -0.0001 37  ASN   B N   
4574 C CA  . ASN   B 37  ? 0.1370 0.1275 0.1259 -0.0018 -0.0200 0.0032  37  ASN   B CA  
4575 C C   . ASN   B 37  ? 0.1360 0.1311 0.1383 -0.0000 -0.0152 0.0113  37  ASN   B C   
4576 O O   . ASN   B 37  ? 0.1465 0.1368 0.1362 0.0003  -0.0053 0.0083  37  ASN   B O   
4577 C CB  . ASN   B 37  ? 0.1385 0.1339 0.1199 -0.0053 -0.0199 0.0152  37  ASN   B CB  
4578 C CG  . ASN   B 37  ? 0.1459 0.1313 0.1346 -0.0043 -0.0076 0.0012  37  ASN   B CG  
4579 O OD1 . ASN   B 37  ? 0.1497 0.1366 0.1545 0.0069  -0.0139 0.0003  37  ASN   B OD1 
4580 N ND2 . ASN   B 37  ? 0.1568 0.1241 0.1387 0.0074  -0.0213 0.0010  37  ASN   B ND2 
4587 N N   . ALA   B 38  ? 0.1488 0.1318 0.1363 0.0049  0.0005  0.0054  38  ALA   B N   
4588 C CA  . ALA   B 38  ? 0.1556 0.1368 0.1281 -0.0008 0.0027  0.0080  38  ALA   B CA  
4589 C C   . ALA   B 38  ? 0.1575 0.1314 0.1340 -0.0029 -0.0008 0.0079  38  ALA   B C   
4590 O O   . ALA   B 38  ? 0.1732 0.1416 0.1433 0.0049  -0.0123 0.0099  38  ALA   B O   
4591 C CB  . ALA   B 38  ? 0.1774 0.1412 0.1549 -0.0023 0.0118  0.0029  38  ALA   B CB  
4597 N N   . ALA   B 39  ? 0.1566 0.1339 0.1247 0.0072  -0.0030 -0.0004 39  ALA   B N   
4598 C CA  . ALA   B 39  ? 0.1650 0.1421 0.1188 0.0129  -0.0141 -0.0010 39  ALA   B CA  
4599 C C   . ALA   B 39  ? 0.1679 0.1485 0.0931 0.0160  -0.0053 -0.0038 39  ALA   B C   
4600 O O   . ALA   B 39  ? 0.1684 0.1533 0.1542 -0.0016 -0.0066 0.0043  39  ALA   B O   
4601 C CB  . ALA   B 39  ? 0.1658 0.1450 0.1367 -0.0014 -0.0166 0.0005  39  ALA   B CB  
4607 N N   . ASN   B 40  ? 0.1711 0.1702 0.0965 0.0019  -0.0019 -0.0137 40  ASN   B N   
4608 C CA  . ASN   B 40  ? 0.1729 0.1750 0.1197 0.0058  -0.0118 -0.0171 40  ASN   B CA  
4609 C C   . ASN   B 40  ? 0.1762 0.1754 0.1244 0.0118  -0.0123 -0.0053 40  ASN   B C   
4610 O O   . ASN   B 40  ? 0.1840 0.1713 0.1168 0.0115  -0.0131 -0.0035 40  ASN   B O   
4611 C CB  . ASN   B 40  ? 0.1865 0.1734 0.1473 0.0139  -0.0143 -0.0024 40  ASN   B CB  
4612 C CG  . ASN   B 40  ? 0.1916 0.1752 0.1783 0.0081  -0.0236 0.0082  40  ASN   B CG  
4613 O OD1 . ASN   B 40  ? 0.1891 0.1659 0.2680 0.0097  -0.0391 0.0203  40  ASN   B OD1 
4614 N ND2 . ASN   B 40  ? 0.1938 0.1745 0.1902 0.0118  -0.0216 0.0146  40  ASN   B ND2 
4621 N N   . VAL   B 41  ? 0.1863 0.1720 0.1267 0.0220  0.0008  -0.0086 41  VAL   B N   
4622 C CA  . VAL   B 41  ? 0.1940 0.1801 0.1380 0.0196  -0.0072 -0.0074 41  VAL   B CA  
4623 C C   . VAL   B 41  ? 0.1911 0.1793 0.1403 0.0326  -0.0084 -0.0068 41  VAL   B C   
4624 O O   . VAL   B 41  ? 0.1867 0.1813 0.1571 0.0236  -0.0127 -0.0119 41  VAL   B O   
4625 C CB  . VAL   B 41  ? 0.2107 0.2023 0.1661 0.0027  0.0154  -0.0215 41  VAL   B CB  
4626 C CG1 . VAL   B 41  ? 0.2050 0.2034 0.1815 -0.0134 0.0236  -0.0262 41  VAL   B CG1 
4627 C CG2 . VAL   B 41  ? 0.2248 0.2223 0.1722 -0.0043 0.0161  -0.0196 41  VAL   B CG2 
4637 N N   A TYR   B 42  ? 0.1985 0.1795 0.1400 0.0337  -0.0169 -0.0083 42  TYR   B N   
4638 N N   B TYR   B 42  ? 0.1952 0.1760 0.1423 0.0274  -0.0193 -0.0105 42  TYR   B N   
4639 C CA  A TYR   B 42  ? 0.1975 0.1846 0.1373 0.0349  -0.0235 -0.0140 42  TYR   B CA  
4640 C CA  B TYR   B 42  ? 0.1932 0.1765 0.1423 0.0224  -0.0295 -0.0194 42  TYR   B CA  
4641 C C   A TYR   B 42  ? 0.1825 0.1663 0.1463 0.0333  -0.0298 -0.0116 42  TYR   B C   
4642 C C   B TYR   B 42  ? 0.1815 0.1647 0.1468 0.0223  -0.0301 -0.0169 42  TYR   B C   
4643 O O   A TYR   B 42  ? 0.1856 0.1723 0.1853 0.0266  -0.0283 -0.0141 42  TYR   B O   
4644 O O   B TYR   B 42  ? 0.1825 0.1710 0.1750 0.0154  -0.0296 -0.0206 42  TYR   B O   
4645 C CB  A TYR   B 42  ? 0.2098 0.2068 0.1570 0.0245  -0.0184 0.0066  42  TYR   B CB  
4646 C CB  B TYR   B 42  ? 0.2010 0.1871 0.1596 0.0078  -0.0363 -0.0105 42  TYR   B CB  
4647 C CG  A TYR   B 42  ? 0.2006 0.2205 0.1404 0.0101  -0.0056 0.0230  42  TYR   B CG  
4648 C CG  B TYR   B 42  ? 0.1901 0.1884 0.1454 -0.0120 -0.0460 -0.0104 42  TYR   B CG  
4649 C CD1 A TYR   B 42  ? 0.1918 0.2182 0.1201 0.0074  0.0117  0.0318  42  TYR   B CD1 
4650 C CD1 B TYR   B 42  ? 0.1825 0.1844 0.1405 -0.0212 -0.0512 -0.0096 42  TYR   B CD1 
4651 C CD2 A TYR   B 42  ? 0.2105 0.2254 0.1718 0.0095  0.0040  0.0230  42  TYR   B CD2 
4652 C CD2 B TYR   B 42  ? 0.1927 0.1847 0.1526 -0.0154 -0.0386 -0.0108 42  TYR   B CD2 
4653 C CE1 A TYR   B 42  ? 0.2018 0.2224 0.1296 0.0025  0.0166  0.0287  42  TYR   B CE1 
4654 C CE1 B TYR   B 42  ? 0.1850 0.1802 0.1384 -0.0295 -0.0414 -0.0104 42  TYR   B CE1 
4655 C CE2 A TYR   B 42  ? 0.2098 0.2290 0.1670 0.0061  0.0305  0.0308  42  TYR   B CE2 
4656 C CE2 B TYR   B 42  ? 0.1857 0.1840 0.1463 -0.0233 -0.0198 0.0043  42  TYR   B CE2 
4657 C CZ  A TYR   B 42  ? 0.2171 0.2333 0.1572 0.0125  0.0380  0.0200  42  TYR   B CZ  
4658 C CZ  B TYR   B 42  ? 0.1815 0.1804 0.1436 -0.0291 -0.0333 -0.0081 42  TYR   B CZ  
4659 O OH  A TYR   B 42  ? 0.2484 0.2581 0.1973 0.0170  0.0476  0.0232  42  TYR   B OH  
4660 O OH  B TYR   B 42  ? 0.1806 0.1802 0.1579 -0.0426 -0.0501 -0.0016 42  TYR   B OH  
4679 N N   . LEU   B 43  ? 0.1772 0.1568 0.1415 0.0168  -0.0245 -0.0182 43  LEU   B N   
4680 C CA  . LEU   B 43  ? 0.1766 0.1542 0.1355 0.0105  -0.0230 -0.0028 43  LEU   B CA  
4681 C C   . LEU   B 43  ? 0.1818 0.1611 0.1329 0.0083  -0.0269 0.0019  43  LEU   B C   
4682 O O   . LEU   B 43  ? 0.1766 0.1592 0.1706 0.0099  -0.0239 0.0006  43  LEU   B O   
4683 C CB  . LEU   B 43  ? 0.1716 0.1521 0.1494 0.0049  -0.0283 -0.0114 43  LEU   B CB  
4684 C CG  . LEU   B 43  ? 0.1785 0.1493 0.1633 0.0015  -0.0370 -0.0097 43  LEU   B CG  
4685 C CD1 . LEU   B 43  ? 0.1917 0.1570 0.1973 -0.0044 -0.0481 -0.0111 43  LEU   B CD1 
4686 C CD2 . LEU   B 43  ? 0.1809 0.1444 0.1730 -0.0014 -0.0319 -0.0060 43  LEU   B CD2 
4699 N N   . LYS   B 44  ? 0.1747 0.1590 0.1465 0.0115  -0.0150 -0.0081 44  LYS   B N   
4700 C CA  . LYS   B 44  ? 0.1828 0.1662 0.1445 0.0087  -0.0143 -0.0028 44  LYS   B CA  
4701 C C   . LYS   B 44  ? 0.1816 0.1622 0.1424 0.0091  -0.0154 0.0008  44  LYS   B C   
4702 O O   . LYS   B 44  ? 0.2009 0.1615 0.1668 0.0141  -0.0056 0.0011  44  LYS   B O   
4703 C CB  . LYS   B 44  ? 0.2050 0.1864 0.1543 0.0246  -0.0213 -0.0038 44  LYS   B CB  
4704 C CG  . LYS   B 44  ? 0.2414 0.2121 0.2008 0.0162  -0.0435 -0.0035 44  LYS   B CG  
4705 C CD  . LYS   B 44  ? 0.2792 0.2389 0.2864 -0.0022 -0.0504 -0.0161 44  LYS   B CD  
4706 C CE  . LYS   B 44  ? 0.3099 0.2693 0.3520 -0.0070 -0.0547 0.0019  44  LYS   B CE  
4707 N NZ  . LYS   B 44  ? 0.3172 0.2758 0.3730 -0.0074 -0.0675 0.0183  44  LYS   B NZ  
4721 N N   . HIS   B 45  ? 0.1683 0.1616 0.1398 -0.0017 -0.0166 0.0057  45  HIS   B N   
4722 C CA  . HIS   B 45  ? 0.1719 0.1620 0.1476 0.0087  -0.0117 -0.0091 45  HIS   B CA  
4723 C C   . HIS   B 45  ? 0.1956 0.1804 0.1761 0.0250  -0.0252 -0.0117 45  HIS   B C   
4724 O O   . HIS   B 45  ? 0.2115 0.2123 0.2379 0.0471  0.0036  -0.0070 45  HIS   B O   
4725 C CB  . HIS   B 45  ? 0.1651 0.1679 0.1554 0.0037  -0.0121 -0.0136 45  HIS   B CB  
4726 C CG  . HIS   B 45  ? 0.1645 0.1580 0.1448 -0.0064 -0.0181 -0.0059 45  HIS   B CG  
4727 N ND1 . HIS   B 45  ? 0.1719 0.1481 0.1497 0.0032  -0.0246 -0.0147 45  HIS   B ND1 
4728 C CD2 . HIS   B 45  ? 0.1776 0.1590 0.1579 -0.0100 -0.0186 -0.0043 45  HIS   B CD2 
4729 C CE1 . HIS   B 45  ? 0.1777 0.1364 0.1413 0.0046  -0.0339 -0.0101 45  HIS   B CE1 
4730 N NE2 . HIS   B 45  ? 0.1856 0.1509 0.1447 -0.0037 -0.0206 -0.0063 45  HIS   B NE2 
4738 N N   A GLY   B 46  ? 0.2156 0.1772 0.2098 0.0286  -0.0439 0.0052  46  GLY   B N   
4739 N N   B GLY   B 46  ? 0.2122 0.1846 0.2028 0.0268  -0.0412 0.0031  46  GLY   B N   
4740 C CA  A GLY   B 46  ? 0.2283 0.1886 0.2539 0.0210  -0.0488 0.0056  46  GLY   B CA  
4741 C CA  B GLY   B 46  ? 0.2238 0.1979 0.2337 0.0201  -0.0477 0.0088  46  GLY   B CA  
4742 C C   A GLY   B 46  ? 0.2306 0.2039 0.3056 0.0245  -0.0405 0.0059  46  GLY   B C   
4743 C C   B GLY   B 46  ? 0.2283 0.2137 0.2718 0.0217  -0.0433 0.0154  46  GLY   B C   
4744 O O   A GLY   B 46  ? 0.2416 0.2162 0.3885 0.0265  -0.0210 -0.0179 46  GLY   B O   
4745 O O   B GLY   B 46  ? 0.2361 0.2305 0.2975 0.0240  -0.0395 0.0243  46  GLY   B O   
4752 N N   . GLY   B 47  ? 0.2269 0.2132 0.2815 0.0076  -0.0280 0.0005  47  GLY   B N   
4753 C CA  . GLY   B 47  ? 0.2096 0.1878 0.2521 0.0035  -0.0182 -0.0061 47  GLY   B CA  
4754 C C   . GLY   B 47  ? 0.1823 0.1659 0.1986 0.0016  -0.0107 0.0027  47  GLY   B C   
4755 O O   . GLY   B 47  ? 0.1951 0.1516 0.2014 0.0040  -0.0169 0.0093  47  GLY   B O   
4760 N N   . GLY   B 48  ? 0.1623 0.1590 0.1944 -0.0019 -0.0173 0.0161  48  GLY   B N   
4761 C CA  . GLY   B 48  ? 0.1621 0.1570 0.1934 -0.0047 -0.0031 0.0070  48  GLY   B CA  
4762 C C   . GLY   B 48  ? 0.1554 0.1468 0.1799 0.0011  0.0032  0.0027  48  GLY   B C   
4763 O O   . GLY   B 48  ? 0.1521 0.1441 0.2105 0.0065  -0.0037 0.0093  48  GLY   B O   
4767 N N   . VAL   B 49  ? 0.1605 0.1474 0.1770 0.0119  0.0005  0.0075  49  VAL   B N   
4768 C CA  . VAL   B 49  ? 0.1642 0.1585 0.1658 0.0119  -0.0167 -0.0079 49  VAL   B CA  
4769 C C   . VAL   B 49  ? 0.1550 0.1444 0.1388 0.0129  -0.0121 -0.0040 49  VAL   B C   
4770 O O   . VAL   B 49  ? 0.1588 0.1477 0.1683 0.0036  -0.0042 -0.0003 49  VAL   B O   
4771 C CB  . VAL   B 49  ? 0.1639 0.1729 0.1892 0.0010  -0.0260 -0.0051 49  VAL   B CB  
4772 C CG1 . VAL   B 49  ? 0.1610 0.1838 0.1883 0.0078  -0.0355 0.0009  49  VAL   B CG1 
4773 C CG2 . VAL   B 49  ? 0.1859 0.1889 0.2160 -0.0081 -0.0318 -0.0095 49  VAL   B CG2 
4783 N N   . ALA   B 50  ? 0.1515 0.1469 0.1313 0.0024  -0.0028 0.0004  50  ALA   B N   
4784 C CA  . ALA   B 50  ? 0.1539 0.1368 0.1407 0.0071  -0.0062 -0.0008 50  ALA   B CA  
4785 C C   . ALA   B 50  ? 0.1536 0.1394 0.1506 0.0070  -0.0149 -0.0032 50  ALA   B C   
4786 O O   . ALA   B 50  ? 0.1538 0.1447 0.1455 0.0042  -0.0040 -0.0034 50  ALA   B O   
4787 C CB  . ALA   B 50  ? 0.1622 0.1383 0.1529 -0.0020 -0.0038 0.0149  50  ALA   B CB  
4793 N N   . GLY   B 51  ? 0.1493 0.1505 0.1671 0.0088  -0.0187 0.0069  51  GLY   B N   
4794 C CA  . GLY   B 51  ? 0.1487 0.1557 0.1867 0.0172  -0.0221 0.0049  51  GLY   B CA  
4795 C C   . GLY   B 51  ? 0.1532 0.1538 0.1838 0.0198  -0.0096 0.0023  51  GLY   B C   
4796 O O   . GLY   B 51  ? 0.1523 0.1692 0.1960 0.0127  -0.0115 -0.0075 51  GLY   B O   
4800 N N   . ALA   B 52  ? 0.1524 0.1544 0.1623 0.0147  -0.0105 0.0054  52  ALA   B N   
4801 C CA  . ALA   B 52  ? 0.1589 0.1588 0.1650 0.0122  -0.0057 -0.0008 52  ALA   B CA  
4802 C C   . ALA   B 52  ? 0.1482 0.1544 0.1620 0.0072  -0.0066 -0.0001 52  ALA   B C   
4803 O O   . ALA   B 52  ? 0.1449 0.1588 0.1880 0.0062  -0.0084 0.0030  52  ALA   B O   
4804 C CB  . ALA   B 52  ? 0.1780 0.1650 0.1619 0.0036  0.0032  -0.0052 52  ALA   B CB  
4810 N N   . LEU   B 53  ? 0.1449 0.1493 0.1572 0.0159  -0.0088 0.0030  53  LEU   B N   
4811 C CA  . LEU   B 53  ? 0.1471 0.1589 0.1509 0.0097  -0.0153 0.0049  53  LEU   B CA  
4812 C C   . LEU   B 53  ? 0.1498 0.1487 0.1527 0.0120  -0.0064 0.0059  53  LEU   B C   
4813 O O   . LEU   B 53  ? 0.1578 0.1587 0.1688 0.0009  -0.0002 0.0081  53  LEU   B O   
4814 C CB  . LEU   B 53  ? 0.1499 0.1654 0.1622 0.0141  -0.0114 0.0121  53  LEU   B CB  
4815 C CG  . LEU   B 53  ? 0.1456 0.1711 0.1644 0.0062  -0.0083 0.0223  53  LEU   B CG  
4816 C CD1 . LEU   B 53  ? 0.1523 0.1919 0.1990 0.0185  -0.0041 0.0061  53  LEU   B CD1 
4817 C CD2 . LEU   B 53  ? 0.1659 0.1914 0.1953 -0.0018 -0.0129 -0.0027 53  LEU   B CD2 
4829 N N   . ASN   B 54  ? 0.1547 0.1392 0.1510 0.0029  -0.0082 0.0047  54  ASN   B N   
4830 C CA  . ASN   B 54  ? 0.1588 0.1565 0.1531 0.0046  -0.0132 -0.0118 54  ASN   B CA  
4831 C C   . ASN   B 54  ? 0.1511 0.1570 0.1823 0.0078  -0.0002 -0.0076 54  ASN   B C   
4832 O O   . ASN   B 54  ? 0.1468 0.1605 0.1913 0.0037  0.0029  -0.0035 54  ASN   B O   
4833 C CB  . ASN   B 54  ? 0.1618 0.1689 0.1728 0.0035  -0.0133 -0.0052 54  ASN   B CB  
4834 C CG  . ASN   B 54  ? 0.1519 0.1809 0.1681 0.0066  -0.0132 -0.0079 54  ASN   B CG  
4835 O OD1 . ASN   B 54  ? 0.1481 0.1802 0.2016 0.0034  -0.0156 -0.0163 54  ASN   B OD1 
4836 N ND2 . ASN   B 54  ? 0.1656 0.2011 0.1938 0.0032  -0.0333 0.0057  54  ASN   B ND2 
4843 N N   . LYS   B 55  ? 0.1480 0.1679 0.1894 0.0136  -0.0071 -0.0086 55  LYS   B N   
4844 C CA  . LYS   B 55  ? 0.1512 0.1813 0.2086 0.0170  -0.0097 -0.0051 55  LYS   B CA  
4845 C C   . LYS   B 55  ? 0.1493 0.1824 0.2016 0.0163  0.0028  -0.0124 55  LYS   B C   
4846 O O   . LYS   B 55  ? 0.1476 0.1967 0.2199 0.0138  0.0012  -0.0081 55  LYS   B O   
4847 C CB  . LYS   B 55  ? 0.1687 0.1929 0.2598 0.0321  -0.0043 0.0063  55  LYS   B CB  
4848 C CG  . LYS   B 55  ? 0.2096 0.2252 0.3436 0.0414  0.0153  0.0217  55  LYS   B CG  
4849 C CD  . LYS   B 55  ? 0.2500 0.2504 0.4160 0.0558  0.0399  0.0265  55  LYS   B CD  
4850 C CE  . LYS   B 55  ? 0.2785 0.2686 0.4768 0.0510  0.0598  0.0267  55  LYS   B CE  
4851 N NZ  . LYS   B 55  ? 0.2925 0.2841 0.5165 0.0472  0.0429  0.0414  55  LYS   B NZ  
4865 N N   . ALA   B 56  ? 0.1486 0.1795 0.1794 0.0051  -0.0019 -0.0089 56  ALA   B N   
4866 C CA  . ALA   B 56  ? 0.1686 0.1988 0.1762 0.0009  -0.0051 -0.0060 56  ALA   B CA  
4867 C C   . ALA   B 56  ? 0.1669 0.2000 0.1662 0.0004  0.0082  -0.0032 56  ALA   B C   
4868 O O   . ALA   B 56  ? 0.1748 0.2070 0.1939 0.0055  0.0268  0.0037  56  ALA   B O   
4869 C CB  . ALA   B 56  ? 0.1806 0.2168 0.1752 -0.0106 -0.0002 -0.0014 56  ALA   B CB  
4875 N N   . THR   B 57  ? 0.1583 0.1889 0.1811 -0.0027 0.0182  -0.0012 57  THR   B N   
4876 C CA  . THR   B 57  ? 0.1639 0.1857 0.1933 -0.0029 0.0204  0.0016  57  THR   B CA  
4877 C C   . THR   B 57  ? 0.1576 0.1971 0.2170 -0.0043 0.0099  0.0014  57  THR   B C   
4878 O O   . THR   B 57  ? 0.1650 0.1983 0.2220 -0.0207 0.0053  -0.0119 57  THR   B O   
4879 C CB  . THR   B 57  ? 0.1677 0.1618 0.1697 -0.0094 0.0187  0.0069  57  THR   B CB  
4880 O OG1 . THR   B 57  ? 0.1697 0.1604 0.1996 -0.0106 0.0142  0.0014  57  THR   B OG1 
4881 C CG2 . THR   B 57  ? 0.1742 0.1612 0.1738 -0.0086 0.0175  -0.0007 57  THR   B CG2 
4889 N N   . ASN   B 58  ? 0.1483 0.2143 0.2343 -0.0115 0.0039  -0.0093 58  ASN   B N   
4890 C CA  . ASN   B 58  ? 0.1766 0.2497 0.2705 -0.0235 0.0249  -0.0067 58  ASN   B CA  
4891 C C   . ASN   B 58  ? 0.1579 0.2242 0.2345 -0.0184 -0.0047 -0.0078 58  ASN   B C   
4892 O O   . ASN   B 58  ? 0.1634 0.2392 0.2578 -0.0169 -0.0142 -0.0194 58  ASN   B O   
4893 C CB  . ASN   B 58  ? 0.2575 0.3185 0.3684 -0.0349 0.0548  0.0049  58  ASN   B CB  
4894 C CG  . ASN   B 58  ? 0.3591 0.3865 0.4983 -0.0365 0.0718  0.0285  58  ASN   B CG  
4895 O OD1 . ASN   B 58  ? 0.3808 0.4081 0.5476 -0.0369 0.0754  0.0372  58  ASN   B OD1 
4896 N ND2 . ASN   B 58  ? 0.4445 0.4445 0.5451 -0.0392 0.0797  0.0341  58  ASN   B ND2 
4903 N N   . ASN   B 59  ? 0.1556 0.2083 0.2041 -0.0098 -0.0092 -0.0072 59  ASN   B N   
4904 C CA  . ASN   B 59  ? 0.1669 0.2090 0.1955 -0.0083 -0.0214 -0.0005 59  ASN   B CA  
4905 C C   . ASN   B 59  ? 0.1602 0.1996 0.1838 -0.0142 -0.0214 -0.0103 59  ASN   B C   
4906 O O   . ASN   B 59  ? 0.1608 0.1972 0.1892 -0.0148 -0.0151 -0.0030 59  ASN   B O   
4907 C CB  . ASN   B 59  ? 0.1723 0.2241 0.2122 -0.0028 -0.0252 0.0011  59  ASN   B CB  
4908 C CG  . ASN   B 59  ? 0.1855 0.2409 0.2277 0.0041  -0.0344 -0.0019 59  ASN   B CG  
4909 O OD1 . ASN   B 59  ? 0.1851 0.2484 0.2296 0.0039  -0.0280 0.0144  59  ASN   B OD1 
4910 N ND2 . ASN   B 59  ? 0.1859 0.2488 0.2407 -0.0025 -0.0365 -0.0059 59  ASN   B ND2 
4917 N N   . ALA   B 60  ? 0.1562 0.1877 0.1904 -0.0117 0.0003  -0.0031 60  ALA   B N   
4918 C CA  . ALA   B 60  ? 0.1649 0.1762 0.1957 -0.0180 -0.0054 0.0038  60  ALA   B CA  
4919 C C   . ALA   B 60  ? 0.1663 0.1629 0.1734 -0.0131 -0.0136 0.0057  60  ALA   B C   
4920 O O   . ALA   B 60  ? 0.1710 0.1680 0.2033 -0.0132 -0.0047 -0.0150 60  ALA   B O   
4921 C CB  . ALA   B 60  ? 0.1791 0.1745 0.2280 -0.0212 0.0038  -0.0020 60  ALA   B CB  
4927 N N   . MET   B 61  ? 0.1603 0.1572 0.1735 -0.0110 -0.0005 0.0022  61  MET   B N   
4928 C CA  . MET   B 61  ? 0.1534 0.1584 0.1653 -0.0056 -0.0160 0.0017  61  MET   B CA  
4929 C C   . MET   B 61  ? 0.1567 0.1567 0.1681 -0.0102 -0.0181 -0.0018 61  MET   B C   
4930 O O   . MET   B 61  ? 0.1579 0.1612 0.1627 0.0013  -0.0150 -0.0178 61  MET   B O   
4931 C CB  . MET   B 61  ? 0.1501 0.1608 0.1622 0.0008  -0.0186 -0.0035 61  MET   B CB  
4932 C CG  . MET   B 61  ? 0.1505 0.1600 0.1471 0.0028  -0.0076 -0.0024 61  MET   B CG  
4933 S SD  . MET   B 61  ? 0.1523 0.1584 0.1821 -0.0029 -0.0098 -0.0122 61  MET   B SD  
4934 C CE  . MET   B 61  ? 0.1557 0.1788 0.1950 0.0051  -0.0114 -0.0252 61  MET   B CE  
4944 N N   . GLN   B 62  ? 0.1540 0.1580 0.1476 -0.0012 -0.0167 -0.0016 62  GLN   B N   
4945 C CA  . GLN   B 62  ? 0.1599 0.1663 0.1592 0.0048  -0.0258 -0.0036 62  GLN   B CA  
4946 C C   . GLN   B 62  ? 0.1553 0.1715 0.1635 -0.0045 -0.0266 -0.0061 62  GLN   B C   
4947 O O   . GLN   B 62  ? 0.1674 0.1713 0.1795 -0.0080 -0.0322 -0.0134 62  GLN   B O   
4948 C CB  . GLN   B 62  ? 0.1641 0.1742 0.1635 0.0018  -0.0191 0.0027  62  GLN   B CB  
4949 C CG  . GLN   B 62  ? 0.1713 0.1758 0.1667 0.0048  -0.0265 -0.0109 62  GLN   B CG  
4950 C CD  . GLN   B 62  ? 0.1670 0.1718 0.1644 0.0091  -0.0274 0.0008  62  GLN   B CD  
4951 O OE1 . GLN   B 62  ? 0.1685 0.1623 0.1849 0.0055  -0.0326 -0.0086 62  GLN   B OE1 
4952 N NE2 . GLN   B 62  ? 0.1650 0.1742 0.1632 0.0093  -0.0197 -0.0133 62  GLN   B NE2 
4961 N N   . VAL   B 63  ? 0.1618 0.1720 0.1862 -0.0083 -0.0282 -0.0148 63  VAL   B N   
4962 C CA  . VAL   B 63  ? 0.1739 0.1788 0.1989 -0.0109 -0.0313 -0.0151 63  VAL   B CA  
4963 C C   . VAL   B 63  ? 0.1738 0.1680 0.1842 -0.0138 -0.0346 -0.0236 63  VAL   B C   
4964 O O   . VAL   B 63  ? 0.1840 0.1718 0.1996 -0.0079 -0.0435 -0.0194 63  VAL   B O   
4965 C CB  . VAL   B 63  ? 0.1731 0.1912 0.2369 -0.0149 -0.0346 -0.0230 63  VAL   B CB  
4966 C CG1 . VAL   B 63  ? 0.1833 0.1943 0.2497 -0.0216 -0.0204 -0.0253 63  VAL   B CG1 
4967 C CG2 . VAL   B 63  ? 0.1668 0.2108 0.2532 -0.0053 -0.0401 -0.0205 63  VAL   B CG2 
4977 N N   . GLU   B 64  ? 0.1714 0.1527 0.1864 -0.0045 -0.0331 -0.0150 64  GLU   B N   
4978 C CA  . GLU   B 64  ? 0.1695 0.1499 0.1821 -0.0074 -0.0382 -0.0050 64  GLU   B CA  
4979 C C   . GLU   B 64  ? 0.1632 0.1518 0.1761 -0.0066 -0.0323 -0.0186 64  GLU   B C   
4980 O O   . GLU   B 64  ? 0.1754 0.1572 0.1756 -0.0064 -0.0298 -0.0229 64  GLU   B O   
4981 C CB  . GLU   B 64  ? 0.1688 0.1667 0.1886 -0.0123 -0.0304 -0.0073 64  GLU   B CB  
4982 C CG  . GLU   B 64  ? 0.1780 0.1693 0.1765 -0.0227 -0.0339 -0.0252 64  GLU   B CG  
4983 C CD  . GLU   B 64  ? 0.1853 0.1801 0.1954 -0.0314 -0.0311 -0.0145 64  GLU   B CD  
4984 O OE1 . GLU   B 64  ? 0.1866 0.1933 0.2088 -0.0310 -0.0213 -0.0337 64  GLU   B OE1 
4985 O OE2 . GLU   B 64  ? 0.2005 0.1839 0.1932 -0.0365 -0.0387 -0.0112 64  GLU   B OE2 
4992 N N   . SER   B 65  ? 0.1712 0.1502 0.1650 -0.0084 -0.0275 -0.0192 65  SER   B N   
4993 C CA  . SER   B 65  ? 0.1671 0.1483 0.1705 0.0041  -0.0330 -0.0180 65  SER   B CA  
4994 C C   . SER   B 65  ? 0.1719 0.1524 0.1732 0.0128  -0.0373 -0.0207 65  SER   B C   
4995 O O   . SER   B 65  ? 0.1675 0.1569 0.1615 0.0074  -0.0250 -0.0212 65  SER   B O   
4996 C CB  . SER   B 65  ? 0.1644 0.1493 0.1834 -0.0045 -0.0262 -0.0141 65  SER   B CB  
4997 O OG  . SER   B 65  ? 0.1678 0.1508 0.1821 -0.0062 -0.0290 -0.0261 65  SER   B OG  
5003 N N   . ASP   B 66  ? 0.1787 0.1608 0.1676 0.0020  -0.0367 -0.0248 66  ASP   B N   
5004 C CA  . ASP   B 66  ? 0.1808 0.1638 0.1622 0.0031  -0.0441 -0.0134 66  ASP   B CA  
5005 C C   . ASP   B 66  ? 0.1864 0.1671 0.1612 -0.0090 -0.0333 -0.0264 66  ASP   B C   
5006 O O   . ASP   B 66  ? 0.1907 0.1765 0.1716 0.0002  -0.0315 -0.0236 66  ASP   B O   
5007 C CB  . ASP   B 66  ? 0.1924 0.1736 0.1939 0.0132  -0.0488 -0.0197 66  ASP   B CB  
5008 C CG  . ASP   B 66  ? 0.2154 0.1960 0.2177 0.0199  -0.0591 -0.0068 66  ASP   B CG  
5009 O OD1 . ASP   B 66  ? 0.2393 0.1938 0.2208 0.0106  -0.0567 0.0089  66  ASP   B OD1 
5010 O OD2 . ASP   B 66  ? 0.2330 0.2233 0.2814 0.0359  -0.0464 -0.0076 66  ASP   B OD2 
5015 N N   . ASP   B 67  ? 0.1845 0.1681 0.1520 -0.0072 -0.0255 -0.0235 67  ASP   B N   
5016 C CA  . ASP   B 67  ? 0.2006 0.1619 0.1693 -0.0075 -0.0289 -0.0076 67  ASP   B CA  
5017 C C   . ASP   B 67  ? 0.1928 0.1599 0.1813 0.0064  -0.0316 -0.0176 67  ASP   B C   
5018 O O   . ASP   B 67  ? 0.1898 0.1614 0.1965 0.0056  -0.0239 -0.0329 67  ASP   B O   
5019 C CB  . ASP   B 67  ? 0.2210 0.1667 0.1818 -0.0201 -0.0453 -0.0193 67  ASP   B CB  
5020 C CG  . ASP   B 67  ? 0.2570 0.1764 0.2061 -0.0152 -0.0721 -0.0227 67  ASP   B CG  
5021 O OD1 . ASP   B 67  ? 0.2805 0.1833 0.2272 -0.0172 -0.0623 -0.0196 67  ASP   B OD1 
5022 O OD2 . ASP   B 67  ? 0.2741 0.1806 0.2224 0.0031  -0.0769 -0.0080 67  ASP   B OD2 
5027 N N   . TYR   B 68  ? 0.1922 0.1558 0.1774 0.0116  -0.0408 -0.0313 68  TYR   B N   
5028 C CA  . TYR   B 68  ? 0.1886 0.1707 0.1893 0.0145  -0.0527 -0.0353 68  TYR   B CA  
5029 C C   . TYR   B 68  ? 0.1816 0.1627 0.1824 0.0064  -0.0409 -0.0337 68  TYR   B C   
5030 O O   . TYR   B 68  ? 0.1859 0.1748 0.1960 0.0151  -0.0380 -0.0500 68  TYR   B O   
5031 C CB  . TYR   B 68  ? 0.1934 0.1928 0.1973 0.0194  -0.0520 -0.0523 68  TYR   B CB  
5032 C CG  . TYR   B 68  ? 0.2048 0.2085 0.1990 0.0254  -0.0451 -0.0580 68  TYR   B CG  
5033 C CD1 . TYR   B 68  ? 0.2041 0.2100 0.2177 0.0046  -0.0410 -0.0585 68  TYR   B CD1 
5034 C CD2 . TYR   B 68  ? 0.2090 0.2266 0.2098 0.0309  -0.0635 -0.0503 68  TYR   B CD2 
5035 C CE1 . TYR   B 68  ? 0.2064 0.2239 0.2316 0.0040  -0.0401 -0.0567 68  TYR   B CE1 
5036 C CE2 . TYR   B 68  ? 0.2025 0.2286 0.2194 0.0191  -0.0577 -0.0549 68  TYR   B CE2 
5037 C CZ  . TYR   B 68  ? 0.1984 0.2318 0.2375 0.0106  -0.0466 -0.0530 68  TYR   B CZ  
5038 O OH  . TYR   B 68  ? 0.1914 0.2494 0.2664 0.0031  -0.0367 -0.0350 68  TYR   B OH  
5048 N N   . ILE   B 69  ? 0.1765 0.1628 0.1732 0.0059  -0.0486 -0.0333 69  ILE   B N   
5049 C CA  . ILE   B 69  ? 0.1831 0.1716 0.1789 -0.0013 -0.0401 -0.0285 69  ILE   B CA  
5050 C C   . ILE   B 69  ? 0.1758 0.1637 0.1731 0.0042  -0.0409 -0.0223 69  ILE   B C   
5051 O O   . ILE   B 69  ? 0.1820 0.1686 0.1712 0.0090  -0.0341 -0.0262 69  ILE   B O   
5052 C CB  . ILE   B 69  ? 0.1808 0.1698 0.1993 -0.0079 -0.0217 -0.0236 69  ILE   B CB  
5053 C CG1 . ILE   B 69  ? 0.1814 0.1707 0.2094 -0.0072 -0.0164 -0.0250 69  ILE   B CG1 
5054 C CG2 . ILE   B 69  ? 0.1976 0.1777 0.2009 -0.0067 -0.0250 -0.0204 69  ILE   B CG2 
5055 C CD1 . ILE   B 69  ? 0.1694 0.1763 0.2123 -0.0193 -0.0116 -0.0367 69  ILE   B CD1 
5067 N N   . ALA   B 70  ? 0.1734 0.1637 0.1756 0.0055  -0.0337 -0.0208 70  ALA   B N   
5068 C CA  . ALA   B 70  ? 0.1780 0.1694 0.1577 -0.0001 -0.0434 -0.0271 70  ALA   B CA  
5069 C C   . ALA   B 70  ? 0.1815 0.1662 0.1830 -0.0108 -0.0418 -0.0269 70  ALA   B C   
5070 O O   . ALA   B 70  ? 0.1871 0.1622 0.1857 -0.0018 -0.0362 -0.0259 70  ALA   B O   
5071 C CB  . ALA   B 70  ? 0.1865 0.1856 0.1744 0.0009  -0.0379 -0.0324 70  ALA   B CB  
5077 N N   . THR   B 71  ? 0.1999 0.1669 0.1869 0.0005  -0.0533 -0.0221 71  THR   B N   
5078 C CA  . THR   B 71  ? 0.2154 0.1726 0.2066 0.0144  -0.0712 -0.0238 71  THR   B CA  
5079 C C   . THR   B 71  ? 0.2006 0.1733 0.2295 0.0347  -0.0715 -0.0469 71  THR   B C   
5080 O O   . THR   B 71  ? 0.2132 0.1822 0.2683 0.0353  -0.0673 -0.0585 71  THR   B O   
5081 C CB  . THR   B 71  ? 0.2480 0.1920 0.2324 0.0118  -0.0681 -0.0141 71  THR   B CB  
5082 O OG1 . THR   B 71  ? 0.2698 0.2177 0.2855 -0.0130 -0.0633 0.0142  71  THR   B OG1 
5083 C CG2 . THR   B 71  ? 0.2679 0.1910 0.2568 0.0197  -0.0547 0.0006  71  THR   B CG2 
5091 N N   . ASN   B 72  ? 0.1967 0.1820 0.2246 0.0268  -0.0723 -0.0682 72  ASN   B N   
5092 C CA  . ASN   B 72  ? 0.1906 0.1940 0.2442 0.0315  -0.0626 -0.0789 72  ASN   B CA  
5093 C C   . ASN   B 72  ? 0.1900 0.2087 0.2495 0.0112  -0.0419 -0.0726 72  ASN   B C   
5094 O O   . ASN   B 72  ? 0.1920 0.2231 0.2895 0.0102  -0.0273 -0.0798 72  ASN   B O   
5095 C CB  . ASN   B 72  ? 0.2054 0.2187 0.2460 0.0269  -0.0809 -0.0649 72  ASN   B CB  
5096 C CG  . ASN   B 72  ? 0.2273 0.2305 0.2482 0.0452  -0.0824 -0.0423 72  ASN   B CG  
5097 O OD1 . ASN   B 72  ? 0.2560 0.2587 0.2497 0.0310  -0.0611 -0.0451 72  ASN   B OD1 
5098 N ND2 . ASN   B 72  ? 0.2409 0.2328 0.2955 0.0571  -0.0766 -0.0071 72  ASN   B ND2 
5105 N N   . GLY   B 73  ? 0.1873 0.2058 0.2183 0.0051  -0.0453 -0.0710 73  GLY   B N   
5106 C CA  . GLY   B 73  ? 0.1781 0.2119 0.1958 0.0031  -0.0298 -0.0561 73  GLY   B CA  
5107 C C   . GLY   B 73  ? 0.1756 0.2080 0.1528 0.0070  -0.0316 -0.0520 73  GLY   B C   
5108 O O   . GLY   B 73  ? 0.1751 0.1934 0.1774 0.0144  -0.0232 -0.0440 73  GLY   B O   
5112 N N   . PRO   B 74  ? 0.1781 0.2196 0.1470 0.0048  -0.0260 -0.0358 74  PRO   B N   
5113 C CA  . PRO   B 74  ? 0.1671 0.2132 0.1360 0.0139  -0.0141 -0.0213 74  PRO   B CA  
5114 C C   . PRO   B 74  ? 0.1550 0.1944 0.1424 0.0106  -0.0208 -0.0171 74  PRO   B C   
5115 O O   . PRO   B 74  ? 0.1619 0.1973 0.1971 0.0149  -0.0101 -0.0362 74  PRO   B O   
5116 C CB  . PRO   B 74  ? 0.1841 0.2376 0.1410 0.0130  -0.0172 -0.0090 74  PRO   B CB  
5117 C CG  . PRO   B 74  ? 0.2052 0.2485 0.1543 0.0090  -0.0194 -0.0068 74  PRO   B CG  
5118 C CD  . PRO   B 74  ? 0.2031 0.2390 0.1560 0.0125  -0.0128 -0.0223 74  PRO   B CD  
5126 N N   . LEU   B 75  ? 0.1622 0.1856 0.1280 0.0121  -0.0226 -0.0238 75  LEU   B N   
5127 C CA  . LEU   B 75  ? 0.1744 0.1860 0.1252 0.0037  -0.0230 -0.0080 75  LEU   B CA  
5128 C C   . LEU   B 75  ? 0.1800 0.1982 0.1292 0.0074  -0.0077 0.0026  75  LEU   B C   
5129 O O   . LEU   B 75  ? 0.1882 0.2154 0.1507 0.0015  -0.0030 0.0055  75  LEU   B O   
5130 C CB  . LEU   B 75  ? 0.1787 0.1908 0.1210 -0.0040 -0.0207 0.0081  75  LEU   B CB  
5131 C CG  . LEU   B 75  ? 0.2140 0.2074 0.1537 -0.0217 -0.0139 0.0008  75  LEU   B CG  
5132 C CD1 . LEU   B 75  ? 0.2489 0.2244 0.1571 -0.0360 0.0074  -0.0073 75  LEU   B CD1 
5133 C CD2 . LEU   B 75  ? 0.2480 0.2283 0.2270 -0.0121 -0.0005 0.0057  75  LEU   B CD2 
5145 N N   . LYS   B 76  ? 0.1863 0.2256 0.1707 0.0049  -0.0022 0.0020  76  LYS   B N   
5146 C CA  . LYS   B 76  ? 0.1939 0.2307 0.2009 -0.0042 0.0180  0.0001  76  LYS   B CA  
5147 C C   . LYS   B 76  ? 0.1790 0.2141 0.1650 -0.0009 0.0142  0.0204  76  LYS   B C   
5148 O O   . LYS   B 76  ? 0.1787 0.1930 0.1742 -0.0003 0.0094  0.0117  76  LYS   B O   
5149 C CB  . LYS   B 76  ? 0.2110 0.2358 0.2591 -0.0077 0.0310  -0.0426 76  LYS   B CB  
5150 C CG  . LYS   B 76  ? 0.2143 0.2552 0.3108 -0.0028 0.0209  -0.0478 76  LYS   B CG  
5151 C CD  . LYS   B 76  ? 0.2098 0.2619 0.3452 0.0034  0.0140  -0.0611 76  LYS   B CD  
5152 C CE  . LYS   B 76  ? 0.2202 0.2796 0.4025 0.0055  -0.0005 -0.0634 76  LYS   B CE  
5153 N NZ  . LYS   B 76  ? 0.2217 0.2841 0.4215 0.0017  -0.0251 -0.0789 76  LYS   B NZ  
5167 N N   . VAL   B 77  ? 0.1908 0.2268 0.1756 0.0047  0.0108  0.0238  77  VAL   B N   
5168 C CA  . VAL   B 77  ? 0.1956 0.2158 0.1830 0.0111  0.0169  0.0461  77  VAL   B CA  
5169 C C   . VAL   B 77  ? 0.1849 0.1953 0.1654 0.0130  0.0221  0.0344  77  VAL   B C   
5170 O O   . VAL   B 77  ? 0.1827 0.1940 0.1752 0.0210  0.0292  0.0261  77  VAL   B O   
5171 C CB  . VAL   B 77  ? 0.2143 0.2292 0.2277 0.0089  0.0225  0.0613  77  VAL   B CB  
5172 C CG1 . VAL   B 77  ? 0.2163 0.2169 0.2455 0.0058  0.0196  0.0807  77  VAL   B CG1 
5173 C CG2 . VAL   B 77  ? 0.2378 0.2460 0.2403 0.0053  0.0109  0.0715  77  VAL   B CG2 
5183 N N   . GLY   B 78  ? 0.1808 0.1796 0.1573 0.0118  0.0159  0.0226  78  GLY   B N   
5184 C CA  . GLY   B 78  ? 0.1743 0.1702 0.1409 0.0139  0.0177  0.0194  78  GLY   B CA  
5185 C C   . GLY   B 78  ? 0.1693 0.1611 0.1473 0.0142  0.0148  0.0265  78  GLY   B C   
5186 O O   . GLY   B 78  ? 0.1655 0.1598 0.1794 0.0172  0.0176  0.0273  78  GLY   B O   
5190 N N   . GLY   B 79  ? 0.1609 0.1687 0.1643 0.0093  0.0074  0.0107  79  GLY   B N   
5191 C CA  . GLY   B 79  ? 0.1615 0.1615 0.1587 0.0142  0.0084  0.0058  79  GLY   B CA  
5192 C C   . GLY   B 79  ? 0.1488 0.1550 0.1515 0.0158  0.0050  0.0057  79  GLY   B C   
5193 O O   . GLY   B 79  ? 0.1593 0.1542 0.1685 0.0151  0.0159  0.0184  79  GLY   B O   
5197 N N   . SER   B 80  ? 0.1520 0.1452 0.1640 0.0077  0.0122  0.0090  80  SER   B N   
5198 C CA  . SER   B 80  ? 0.1433 0.1489 0.1691 -0.0001 0.0035  0.0050  80  SER   B CA  
5199 C C   . SER   B 80  ? 0.1454 0.1481 0.1671 0.0104  -0.0015 -0.0053 80  SER   B C   
5200 O O   . SER   B 80  ? 0.1575 0.1496 0.1970 0.0127  -0.0010 -0.0086 80  SER   B O   
5201 C CB  . SER   B 80  ? 0.1484 0.1536 0.1706 -0.0080 -0.0072 0.0085  80  SER   B CB  
5202 O OG  . SER   B 80  ? 0.1516 0.1678 0.1906 -0.0022 -0.0151 0.0104  80  SER   B OG  
5208 N N   . CYS   B 81  ? 0.1464 0.1352 0.1702 0.0010  -0.0072 -0.0069 81  CYS   B N   
5209 C CA  . CYS   B 81  ? 0.1484 0.1358 0.1702 0.0023  -0.0154 -0.0079 81  CYS   B CA  
5210 C C   . CYS   B 81  ? 0.1479 0.1334 0.1460 0.0010  -0.0127 -0.0104 81  CYS   B C   
5211 O O   . CYS   B 81  ? 0.1632 0.1336 0.1616 0.0054  -0.0012 -0.0075 81  CYS   B O   
5212 C CB  . CYS   B 81  ? 0.1689 0.1425 0.1806 -0.0014 -0.0234 0.0009  81  CYS   B CB  
5213 S SG  . CYS   B 81  ? 0.1708 0.1662 0.1628 -0.0026 -0.0284 -0.0113 81  CYS   B SG  
5219 N N   . VAL   B 82  ? 0.1532 0.1340 0.1510 -0.0028 -0.0131 -0.0071 82  VAL   B N   
5220 C CA  . VAL   B 82  ? 0.1558 0.1351 0.1506 -0.0068 -0.0161 -0.0024 82  VAL   B CA  
5221 C C   . VAL   B 82  ? 0.1645 0.1321 0.1675 -0.0084 -0.0134 -0.0013 82  VAL   B C   
5222 O O   . VAL   B 82  ? 0.1713 0.1286 0.1963 -0.0047 -0.0133 -0.0152 82  VAL   B O   
5223 C CB  . VAL   B 82  ? 0.1646 0.1500 0.1694 -0.0059 -0.0137 0.0021  82  VAL   B CB  
5224 C CG1 . VAL   B 82  ? 0.1841 0.1753 0.1785 0.0007  -0.0188 0.0154  82  VAL   B CG1 
5225 C CG2 . VAL   B 82  ? 0.1699 0.1594 0.1877 -0.0030 -0.0214 0.0081  82  VAL   B CG2 
5235 N N   . LEU   B 83  ? 0.1498 0.1308 0.1539 -0.0188 -0.0249 -0.0056 83  LEU   B N   
5236 C CA  . LEU   B 83  ? 0.1550 0.1336 0.1431 -0.0153 -0.0248 -0.0050 83  LEU   B CA  
5237 C C   . LEU   B 83  ? 0.1573 0.1330 0.1381 -0.0205 -0.0251 0.0022  83  LEU   B C   
5238 O O   . LEU   B 83  ? 0.1610 0.1459 0.1366 -0.0220 -0.0192 0.0063  83  LEU   B O   
5239 C CB  . LEU   B 83  ? 0.1597 0.1454 0.1488 -0.0136 -0.0344 -0.0137 83  LEU   B CB  
5240 C CG  . LEU   B 83  ? 0.1817 0.1636 0.1580 -0.0148 -0.0256 -0.0116 83  LEU   B CG  
5241 C CD1 . LEU   B 83  ? 0.1920 0.1662 0.1698 -0.0149 -0.0295 -0.0036 83  LEU   B CD1 
5242 C CD2 . LEU   B 83  ? 0.1987 0.1664 0.1840 -0.0040 -0.0276 -0.0203 83  LEU   B CD2 
5254 N N   . SER   B 84  ? 0.1682 0.1458 0.1569 -0.0254 -0.0313 0.0023  84  SER   B N   
5255 C CA  . SER   B 84  ? 0.1660 0.1615 0.1451 -0.0341 -0.0219 0.0175  84  SER   B CA  
5256 C C   . SER   B 84  ? 0.1537 0.1749 0.0986 -0.0219 -0.0233 0.0219  84  SER   B C   
5257 O O   . SER   B 84  ? 0.1684 0.1644 0.1165 -0.0187 -0.0155 0.0071  84  SER   B O   
5258 C CB  . SER   B 84  ? 0.1867 0.1638 0.1950 -0.0326 0.0068  0.0112  84  SER   B CB  
5259 O OG  . SER   B 84  ? 0.1822 0.1813 0.2467 -0.0410 -0.0041 0.0187  84  SER   B OG  
5265 N N   . GLY   B 85  ? 0.1602 0.1984 0.1264 -0.0305 -0.0190 0.0233  85  GLY   B N   
5266 C CA  . GLY   B 85  ? 0.1716 0.2040 0.1480 -0.0413 -0.0024 -0.0072 85  GLY   B CA  
5267 C C   . GLY   B 85  ? 0.1637 0.1857 0.1345 -0.0428 -0.0005 0.0010  85  GLY   B C   
5268 O O   . GLY   B 85  ? 0.1705 0.1878 0.1474 -0.0587 0.0130  -0.0137 85  GLY   B O   
5272 N N   . HIS   B 86  ? 0.1571 0.1713 0.1483 -0.0279 -0.0124 0.0096  86  HIS   B N   
5273 C CA  . HIS   B 86  ? 0.1545 0.1748 0.1467 -0.0265 -0.0239 0.0126  86  HIS   B CA  
5274 C C   . HIS   B 86  ? 0.1589 0.1837 0.1498 -0.0415 -0.0063 0.0270  86  HIS   B C   
5275 O O   . HIS   B 86  ? 0.1733 0.1981 0.1596 -0.0424 0.0019  0.0203  86  HIS   B O   
5276 C CB  . HIS   B 86  ? 0.1657 0.1756 0.1483 -0.0198 -0.0308 -0.0067 86  HIS   B CB  
5277 C CG  . HIS   B 86  ? 0.1679 0.1798 0.1639 -0.0166 -0.0306 0.0090  86  HIS   B CG  
5278 N ND1 . HIS   B 86  ? 0.1791 0.2018 0.1917 -0.0280 -0.0303 -0.0104 86  HIS   B ND1 
5279 C CD2 . HIS   B 86  ? 0.1687 0.1764 0.1858 -0.0087 -0.0254 -0.0008 86  HIS   B CD2 
5280 C CE1 . HIS   B 86  ? 0.1848 0.1955 0.1870 -0.0130 -0.0082 -0.0290 86  HIS   B CE1 
5281 N NE2 . HIS   B 86  ? 0.1814 0.1897 0.1777 0.0033  -0.0108 -0.0041 86  HIS   B NE2 
5289 N N   . ASN   B 87  ? 0.1571 0.1825 0.1683 -0.0336 -0.0009 0.0170  87  ASN   B N   
5290 C CA  . ASN   B 87  ? 0.1710 0.1982 0.1684 -0.0315 0.0230  0.0115  87  ASN   B CA  
5291 C C   . ASN   B 87  ? 0.1845 0.1814 0.1557 -0.0322 0.0303  0.0131  87  ASN   B C   
5292 O O   . ASN   B 87  ? 0.2135 0.1913 0.1987 -0.0252 0.0518  0.0058  87  ASN   B O   
5293 C CB  . ASN   B 87  ? 0.1714 0.2320 0.2035 -0.0238 0.0221  0.0104  87  ASN   B CB  
5294 C CG  . ASN   B 87  ? 0.1778 0.2501 0.2054 0.0044  0.0300  0.0311  87  ASN   B CG  
5295 O OD1 . ASN   B 87  ? 0.1754 0.2338 0.2000 0.0062  0.0433  0.0416  87  ASN   B OD1 
5296 N ND2 . ASN   B 87  ? 0.2165 0.2634 0.2497 0.0117  0.0394  0.0257  87  ASN   B ND2 
5303 N N   . LEU   B 88  ? 0.1698 0.1765 0.1416 -0.0382 0.0159  0.0114  88  LEU   B N   
5304 C CA  . LEU   B 88  ? 0.1853 0.1702 0.1491 -0.0414 -0.0025 0.0057  88  LEU   B CA  
5305 C C   . LEU   B 88  ? 0.1927 0.1565 0.1424 -0.0384 -0.0165 0.0069  88  LEU   B C   
5306 O O   . LEU   B 88  ? 0.2145 0.1644 0.1790 -0.0214 -0.0373 -0.0104 88  LEU   B O   
5307 C CB  . LEU   B 88  ? 0.2028 0.1728 0.1784 -0.0520 -0.0073 0.0188  88  LEU   B CB  
5308 C CG  . LEU   B 88  ? 0.2467 0.2012 0.1938 -0.0404 -0.0258 0.0346  88  LEU   B CG  
5309 C CD1 . LEU   B 88  ? 0.2578 0.2376 0.2115 -0.0519 -0.0180 0.0443  88  LEU   B CD1 
5310 C CD2 . LEU   B 88  ? 0.2862 0.2336 0.2525 -0.0063 -0.0400 0.0194  88  LEU   B CD2 
5322 N N   . ALA   B 89  ? 0.1756 0.1555 0.1386 -0.0359 0.0122  0.0030  89  ALA   B N   
5323 C CA  . ALA   B 89  ? 0.1712 0.1485 0.1341 -0.0373 0.0052  0.0103  89  ALA   B CA  
5324 C C   . ALA   B 89  ? 0.1761 0.1557 0.1262 -0.0439 0.0063  0.0039  89  ALA   B C   
5325 O O   . ALA   B 89  ? 0.1605 0.1627 0.1777 -0.0440 0.0073  -0.0219 89  ALA   B O   
5326 C CB  . ALA   B 89  ? 0.1649 0.1473 0.1518 -0.0368 0.0141  0.0131  89  ALA   B CB  
5332 N N   . LYS   B 90  ? 0.2088 0.1413 0.1467 -0.0493 -0.0134 0.0094  90  LYS   B N   
5333 C CA  . LYS   B 90  ? 0.2217 0.1429 0.1388 -0.0485 -0.0159 0.0049  90  LYS   B CA  
5334 C C   . LYS   B 90  ? 0.2076 0.1361 0.1330 -0.0430 -0.0166 -0.0043 90  LYS   B C   
5335 O O   . LYS   B 90  ? 0.2094 0.1550 0.1578 -0.0528 -0.0007 -0.0052 90  LYS   B O   
5336 C CB  . LYS   B 90  ? 0.2302 0.1540 0.1771 -0.0368 -0.0059 0.0156  90  LYS   B CB  
5337 C CG  . LYS   B 90  ? 0.2221 0.1611 0.1725 -0.0266 0.0215  0.0100  90  LYS   B CG  
5338 C CD  . LYS   B 90  ? 0.2468 0.1787 0.2173 -0.0110 0.0328  -0.0047 90  LYS   B CD  
5339 C CE  . LYS   B 90  ? 0.2595 0.1905 0.2699 -0.0127 0.0376  -0.0149 90  LYS   B CE  
5340 N NZ  . LYS   B 90  ? 0.2676 0.1818 0.2601 -0.0254 0.0598  -0.0184 90  LYS   B NZ  
5354 N N   . HIS   B 91  ? 0.1807 0.1290 0.1264 -0.0356 -0.0160 0.0064  91  HIS   B N   
5355 C CA  . HIS   B 91  ? 0.1640 0.1318 0.1376 -0.0286 -0.0205 -0.0016 91  HIS   B CA  
5356 C C   . HIS   B 91  ? 0.1566 0.1383 0.1221 -0.0328 -0.0100 -0.0057 91  HIS   B C   
5357 O O   . HIS   B 91  ? 0.1702 0.1406 0.1239 -0.0267 -0.0212 0.0004  91  HIS   B O   
5358 C CB  . HIS   B 91  ? 0.1791 0.1336 0.1802 -0.0135 -0.0096 0.0100  91  HIS   B CB  
5359 C CG  . HIS   B 91  ? 0.2173 0.1566 0.2602 -0.0032 0.0183  0.0174  91  HIS   B CG  
5360 N ND1 . HIS   B 91  ? 0.2438 0.1671 0.3210 -0.0041 0.0240  0.0178  91  HIS   B ND1 
5361 C CD2 . HIS   B 91  ? 0.2232 0.1907 0.3159 0.0089  0.0014  0.0520  91  HIS   B CD2 
5362 C CE1 . HIS   B 91  ? 0.2446 0.1832 0.3446 0.0109  0.0262  0.0222  91  HIS   B CE1 
5363 N NE2 . HIS   B 91  ? 0.2362 0.1952 0.3496 0.0225  0.0182  0.0599  91  HIS   B NE2 
5371 N N   . CYS   B 92  ? 0.1532 0.1337 0.1256 -0.0334 -0.0158 -0.0045 92  CYS   B N   
5372 C CA  . CYS   B 92  ? 0.1489 0.1318 0.1224 -0.0246 -0.0102 -0.0061 92  CYS   B CA  
5373 C C   . CYS   B 92  ? 0.1454 0.1251 0.1192 -0.0199 -0.0089 -0.0047 92  CYS   B C   
5374 O O   . CYS   B 92  ? 0.1499 0.1373 0.1342 -0.0200 -0.0083 -0.0068 92  CYS   B O   
5375 C CB  . CYS   B 92  ? 0.1521 0.1437 0.1401 -0.0189 -0.0110 0.0036  92  CYS   B CB  
5376 S SG  . CYS   B 92  ? 0.1482 0.1420 0.1461 -0.0120 -0.0147 0.0055  92  CYS   B SG  
5382 N N   . LEU   B 93  ? 0.1396 0.1329 0.1181 -0.0109 -0.0092 -0.0016 93  LEU   B N   
5383 C CA  . LEU   B 93  ? 0.1408 0.1301 0.1211 -0.0048 -0.0133 -0.0025 93  LEU   B CA  
5384 C C   . LEU   B 93  ? 0.1313 0.1263 0.1168 -0.0084 -0.0131 0.0027  93  LEU   B C   
5385 O O   . LEU   B 93  ? 0.1369 0.1297 0.1460 -0.0132 -0.0106 -0.0003 93  LEU   B O   
5386 C CB  . LEU   B 93  ? 0.1434 0.1291 0.1450 -0.0058 -0.0170 0.0041  93  LEU   B CB  
5387 C CG  . LEU   B 93  ? 0.1416 0.1442 0.1661 -0.0088 -0.0066 0.0050  93  LEU   B CG  
5388 C CD1 . LEU   B 93  ? 0.1462 0.1533 0.1738 0.0017  -0.0018 -0.0137 93  LEU   B CD1 
5389 C CD2 . LEU   B 93  ? 0.1360 0.1406 0.1843 -0.0084 -0.0167 -0.0008 93  LEU   B CD2 
5401 N N   . HIS   B 94  ? 0.1380 0.1181 0.1298 -0.0068 -0.0223 0.0021  94  HIS   B N   
5402 C CA  . HIS   B 94  ? 0.1432 0.1236 0.1289 -0.0013 -0.0110 0.0028  94  HIS   B CA  
5403 C C   . HIS   B 94  ? 0.1334 0.1285 0.1485 -0.0045 -0.0070 0.0080  94  HIS   B C   
5404 O O   . HIS   B 94  ? 0.1389 0.1373 0.1866 -0.0071 0.0122  -0.0124 94  HIS   B O   
5405 C CB  . HIS   B 94  ? 0.1357 0.1335 0.1381 0.0012  -0.0097 0.0003  94  HIS   B CB  
5406 C CG  . HIS   B 94  ? 0.1384 0.1283 0.1420 -0.0101 -0.0249 -0.0016 94  HIS   B CG  
5407 N ND1 . HIS   B 94  ? 0.1456 0.1385 0.1293 -0.0027 -0.0232 0.0036  94  HIS   B ND1 
5408 C CD2 . HIS   B 94  ? 0.1468 0.1356 0.1364 0.0032  -0.0186 0.0030  94  HIS   B CD2 
5409 C CE1 . HIS   B 94  ? 0.1543 0.1377 0.1371 -0.0049 -0.0200 0.0078  94  HIS   B CE1 
5410 N NE2 . HIS   B 94  ? 0.1386 0.1418 0.1499 -0.0136 -0.0208 0.0078  94  HIS   B NE2 
5418 N N   . VAL   B 95  ? 0.1273 0.1256 0.1481 -0.0030 -0.0052 0.0100  95  VAL   B N   
5419 C CA  . VAL   B 95  ? 0.1349 0.1408 0.1360 0.0011  -0.0021 0.0147  95  VAL   B CA  
5420 C C   . VAL   B 95  ? 0.1404 0.1370 0.1413 -0.0027 0.0031  0.0045  95  VAL   B C   
5421 O O   . VAL   B 95  ? 0.1493 0.1382 0.1520 0.0078  0.0054  0.0164  95  VAL   B O   
5422 C CB  . VAL   B 95  ? 0.1434 0.1357 0.1398 -0.0076 -0.0148 0.0100  95  VAL   B CB  
5423 C CG1 . VAL   B 95  ? 0.1519 0.1483 0.1668 -0.0136 -0.0035 0.0150  95  VAL   B CG1 
5424 C CG2 . VAL   B 95  ? 0.1531 0.1345 0.1385 0.0032  -0.0087 -0.0019 95  VAL   B CG2 
5434 N N   . VAL   B 96  ? 0.1532 0.1374 0.1426 0.0101  0.0030  0.0114  96  VAL   B N   
5435 C CA  . VAL   B 96  ? 0.1623 0.1472 0.1376 0.0091  0.0032  0.0194  96  VAL   B CA  
5436 C C   . VAL   B 96  ? 0.1663 0.1480 0.1577 0.0043  0.0136  0.0141  96  VAL   B C   
5437 O O   . VAL   B 96  ? 0.1691 0.1525 0.1670 -0.0013 0.0155  0.0033  96  VAL   B O   
5438 C CB  . VAL   B 96  ? 0.1680 0.1718 0.1347 0.0067  0.0006  0.0075  96  VAL   B CB  
5439 C CG1 . VAL   B 96  ? 0.1658 0.1888 0.1523 0.0145  -0.0010 0.0018  96  VAL   B CG1 
5440 C CG2 . VAL   B 96  ? 0.1759 0.1697 0.1519 0.0021  0.0137  0.0074  96  VAL   B CG2 
5450 N N   . GLY   B 97  ? 0.1713 0.1493 0.1509 0.0022  0.0038  0.0216  97  GLY   B N   
5451 C CA  . GLY   B 97  ? 0.1920 0.1562 0.1516 0.0073  0.0084  0.0205  97  GLY   B CA  
5452 C C   . GLY   B 97  ? 0.2130 0.1625 0.1670 0.0074  0.0066  0.0135  97  GLY   B C   
5453 O O   . GLY   B 97  ? 0.2314 0.1700 0.1715 0.0045  -0.0046 0.0103  97  GLY   B O   
5457 N N   . PRO   B 98  ? 0.2262 0.1666 0.1796 0.0066  0.0325  0.0326  98  PRO   B N   
5458 C CA  . PRO   B 98  ? 0.2369 0.1901 0.1921 0.0150  0.0314  0.0271  98  PRO   B CA  
5459 C C   . PRO   B 98  ? 0.2473 0.1895 0.1695 0.0333  0.0415  0.0504  98  PRO   B C   
5460 O O   . PRO   B 98  ? 0.2363 0.1901 0.1887 0.0245  0.0482  0.0473  98  PRO   B O   
5461 C CB  . PRO   B 98  ? 0.2285 0.1966 0.2038 0.0145  0.0473  0.0328  98  PRO   B CB  
5462 C CG  . PRO   B 98  ? 0.2258 0.1852 0.2035 0.0119  0.0410  0.0483  98  PRO   B CG  
5463 C CD  . PRO   B 98  ? 0.2145 0.1723 0.1956 0.0083  0.0438  0.0423  98  PRO   B CD  
5471 N N   . ASN   B 99  ? 0.2512 0.2085 0.1891 0.0580  0.0478  0.0253  99  ASN   B N   
5472 C CA  . ASN   B 99  ? 0.2780 0.2210 0.1870 0.0592  0.0377  0.0529  99  ASN   B CA  
5473 C C   . ASN   B 99  ? 0.3081 0.2569 0.2029 0.0501  0.0580  0.0894  99  ASN   B C   
5474 O O   . ASN   B 99  ? 0.3163 0.2706 0.2036 0.0526  0.0453  0.0829  99  ASN   B O   
5475 C CB  . ASN   B 99  ? 0.2844 0.2163 0.1964 0.0572  0.0234  0.0372  99  ASN   B CB  
5476 C CG  . ASN   B 99  ? 0.2900 0.2269 0.2214 0.0484  0.0136  0.0368  99  ASN   B CG  
5477 O OD1 . ASN   B 99  ? 0.2952 0.2261 0.2472 0.0543  0.0198  0.0509  99  ASN   B OD1 
5478 N ND2 . ASN   B 99  ? 0.2838 0.2267 0.2260 0.0477  -0.0089 0.0350  99  ASN   B ND2 
5485 N N   A VAL   B 100 ? 0.3280 0.2706 0.2597 0.0361  0.0607  0.1045  100 VAL   B N   
5486 N N   B VAL   B 100 ? 0.3288 0.2699 0.2556 0.0375  0.0555  0.1024  100 VAL   B N   
5487 C CA  A VAL   B 100 ? 0.3548 0.2887 0.3163 0.0225  0.0593  0.1196  100 VAL   B CA  
5488 C CA  B VAL   B 100 ? 0.3543 0.2859 0.3067 0.0252  0.0503  0.1151  100 VAL   B CA  
5489 C C   A VAL   B 100 ? 0.3755 0.2963 0.3103 0.0265  0.0561  0.1339  100 VAL   B C   
5490 C C   B VAL   B 100 ? 0.3742 0.2936 0.3053 0.0281  0.0478  0.1302  100 VAL   B C   
5491 O O   A VAL   B 100 ? 0.3836 0.3051 0.3191 0.0238  0.0625  0.1238  100 VAL   B O   
5492 O O   B VAL   B 100 ? 0.3797 0.2981 0.3082 0.0246  0.0510  0.1223  100 VAL   B O   
5493 C CB  A VAL   B 100 ? 0.3619 0.3004 0.3804 0.0034  0.0585  0.1269  100 VAL   B CB  
5494 C CB  B VAL   B 100 ? 0.3605 0.2952 0.3595 0.0093  0.0466  0.1180  100 VAL   B CB  
5495 C CG1 A VAL   B 100 ? 0.3669 0.3058 0.4088 -0.0004 0.0581  0.1257  100 VAL   B CG1 
5496 C CG1 B VAL   B 100 ? 0.3647 0.2994 0.3825 0.0059  0.0456  0.1172  100 VAL   B CG1 
5497 C CG2 A VAL   B 100 ? 0.3623 0.3058 0.3959 -0.0053 0.0613  0.1333  100 VAL   B CG2 
5498 C CG2 B VAL   B 100 ? 0.3611 0.2997 0.3747 0.0023  0.0469  0.1198  100 VAL   B CG2 
5517 N N   . ASN   B 101 ? 0.3886 0.2987 0.3035 0.0377  0.0367  0.1417  101 ASN   B N   
5518 C CA  . ASN   B 101 ? 0.4222 0.3128 0.3090 0.0495  0.0145  0.1510  101 ASN   B CA  
5519 C C   . ASN   B 101 ? 0.4640 0.3484 0.3125 0.0560  -0.0023 0.1603  101 ASN   B C   
5520 O O   . ASN   B 101 ? 0.4714 0.3652 0.3459 0.0642  0.0069  0.1201  101 ASN   B O   
5521 C CB  . ASN   B 101 ? 0.4187 0.3049 0.3300 0.0402  0.0224  0.1252  101 ASN   B CB  
5522 C CG  . ASN   B 101 ? 0.4135 0.2937 0.3260 0.0343  0.0312  0.1223  101 ASN   B CG  
5523 O OD1 . ASN   B 101 ? 0.4150 0.2924 0.3525 0.0256  0.0551  0.1110  101 ASN   B OD1 
5524 N ND2 . ASN   B 101 ? 0.4090 0.2893 0.3084 0.0342  0.0211  0.1157  101 ASN   B ND2 
5532 N N   . LYS   B 102 ? 0.4956 0.3815 0.3307 0.0435  -0.0032 0.1563  102 LYS   B N   
5533 C CA  . LYS   B 102 ? 0.5260 0.4227 0.3529 0.0250  0.0060  0.1295  102 LYS   B CA  
5534 C C   . LYS   B 102 ? 0.5269 0.4280 0.3472 0.0190  0.0174  0.1325  102 LYS   B C   
5535 O O   . LYS   B 102 ? 0.5358 0.4316 0.3605 0.0172  0.0020  0.1243  102 LYS   B O   
5536 C CB  . LYS   B 102 ? 0.5515 0.4569 0.3949 0.0137  0.0154  0.0841  102 LYS   B CB  
5537 C CG  . LYS   B 102 ? 0.5734 0.4870 0.4453 0.0063  0.0248  0.0395  102 LYS   B CG  
5538 C CD  . LYS   B 102 ? 0.5924 0.5119 0.4999 0.0013  0.0344  0.0059  102 LYS   B CD  
5539 C CE  . LYS   B 102 ? 0.6059 0.5294 0.5437 -0.0034 0.0403  -0.0172 102 LYS   B CE  
5540 N NZ  . LYS   B 102 ? 0.6139 0.5408 0.5720 -0.0047 0.0418  -0.0302 102 LYS   B NZ  
5554 N N   . GLY   B 103 ? 0.5150 0.4251 0.3494 0.0142  0.0423  0.1315  103 GLY   B N   
5555 C CA  . GLY   B 103 ? 0.5005 0.4214 0.3650 0.0122  0.0626  0.1129  103 GLY   B CA  
5556 C C   . GLY   B 103 ? 0.4818 0.4133 0.3606 0.0097  0.0803  0.0943  103 GLY   B C   
5557 O O   . GLY   B 103 ? 0.4871 0.4217 0.3636 0.0084  0.0841  0.0964  103 GLY   B O   
5561 N N   A GLU   B 104 ? 0.4689 0.4037 0.3466 0.0080  0.0937  0.0827  104 GLU   B N   
5562 N N   B GLU   B 104 ? 0.4671 0.4027 0.3545 0.0066  0.0777  0.0799  104 GLU   B N   
5563 C CA  A GLU   B 104 ? 0.4558 0.3926 0.3298 0.0100  0.1020  0.0693  104 GLU   B CA  
5564 C CA  B GLU   B 104 ? 0.4519 0.3906 0.3435 0.0059  0.0727  0.0638  104 GLU   B CA  
5565 C C   A GLU   B 104 ? 0.4545 0.3965 0.3319 0.0017  0.1408  0.0742  104 GLU   B C   
5566 C C   B GLU   B 104 ? 0.4474 0.3923 0.3495 0.0010  0.0951  0.0612  104 GLU   B C   
5567 O O   A GLU   B 104 ? 0.4541 0.4004 0.3387 -0.0022 0.1456  0.0775  104 GLU   B O   
5568 O O   B GLU   B 104 ? 0.4476 0.3943 0.3571 -0.0011 0.0965  0.0615  104 GLU   B O   
5569 C CB  A GLU   B 104 ? 0.4468 0.3758 0.3202 0.0213  0.0674  0.0424  104 GLU   B CB  
5570 C CB  B GLU   B 104 ? 0.4431 0.3752 0.3310 0.0100  0.0444  0.0452  104 GLU   B CB  
5571 C CG  A GLU   B 104 ? 0.4391 0.3611 0.3055 0.0328  0.0299  0.0106  104 GLU   B CG  
5572 C CG  B GLU   B 104 ? 0.4356 0.3615 0.3158 0.0145  0.0151  0.0238  104 GLU   B CG  
5573 C CD  A GLU   B 104 ? 0.4311 0.3465 0.2828 0.0426  -0.0013 -0.0109 104 GLU   B CD  
5574 C CD  B GLU   B 104 ? 0.4288 0.3485 0.2964 0.0173  -0.0081 0.0098  104 GLU   B CD  
5575 O OE1 A GLU   B 104 ? 0.4224 0.3337 0.2537 0.0497  0.0025  -0.0174 104 GLU   B OE1 
5576 O OE1 B GLU   B 104 ? 0.4234 0.3394 0.2801 0.0184  -0.0068 0.0079  104 GLU   B OE1 
5577 O OE2 A GLU   B 104 ? 0.4310 0.3466 0.2729 0.0428  -0.0311 -0.0258 104 GLU   B OE2 
5578 O OE2 B GLU   B 104 ? 0.4279 0.3472 0.2859 0.0175  -0.0283 -0.0003 104 GLU   B OE2 
5591 N N   A ASP   B 105 ? 0.4491 0.3962 0.3256 -0.0020 0.1720  0.0730  105 ASP   B N   
5592 N N   B ASP   B 105 ? 0.4405 0.3920 0.3438 -0.0017 0.1144  0.0565  105 ASP   B N   
5593 C CA  A ASP   B 105 ? 0.4478 0.3978 0.3479 -0.0068 0.1915  0.0565  105 ASP   B CA  
5594 C CA  B ASP   B 105 ? 0.4367 0.3919 0.3551 -0.0054 0.1275  0.0421  105 ASP   B CA  
5595 C C   A ASP   B 105 ? 0.4321 0.3752 0.3193 -0.0195 0.1951  0.0472  105 ASP   B C   
5596 C C   B ASP   B 105 ? 0.4254 0.3786 0.3300 -0.0130 0.1303  0.0313  105 ASP   B C   
5597 O O   A ASP   B 105 ? 0.4222 0.3712 0.3030 -0.0165 0.1994  0.0481  105 ASP   B O   
5598 O O   B ASP   B 105 ? 0.4228 0.3765 0.3123 -0.0118 0.1380  0.0324  105 ASP   B O   
5599 C CB  A ASP   B 105 ? 0.4623 0.4191 0.4143 0.0041  0.1941  0.0386  105 ASP   B CB  
5600 C CB  B ASP   B 105 ? 0.4418 0.4037 0.3963 0.0002  0.1331  0.0339  105 ASP   B CB  
5601 C CG  A ASP   B 105 ? 0.4734 0.4350 0.4828 0.0097  0.1970  0.0278  105 ASP   B CG  
5602 C CG  B ASP   B 105 ? 0.4459 0.4113 0.4391 0.0016  0.1388  0.0310  105 ASP   B CG  
5603 O OD1 A ASP   B 105 ? 0.4733 0.4393 0.4947 0.0061  0.2087  0.0342  105 ASP   B OD1 
5604 O OD1 B ASP   B 105 ? 0.4463 0.4147 0.4498 -0.0014 0.1425  0.0346  105 ASP   B OD1 
5605 O OD2 A ASP   B 105 ? 0.4796 0.4421 0.5220 0.0170  0.1859  0.0165  105 ASP   B OD2 
5606 O OD2 B ASP   B 105 ? 0.4450 0.4137 0.4527 0.0025  0.1442  0.0301  105 ASP   B OD2 
5615 N N   A ILE   B 106 ? 0.4199 0.3566 0.3279 -0.0299 0.1839  0.0387  106 ILE   B N   
5616 N N   B ILE   B 106 ? 0.4151 0.3664 0.3295 -0.0189 0.1205  0.0222  106 ILE   B N   
5617 C CA  A ILE   B 106 ? 0.3985 0.3351 0.3379 -0.0454 0.1887  0.0313  106 ILE   B CA  
5618 C CA  B ILE   B 106 ? 0.3990 0.3540 0.3364 -0.0261 0.1198  0.0126  106 ILE   B CA  
5619 C C   A ILE   B 106 ? 0.3668 0.3288 0.3248 -0.0450 0.1870  0.0193  106 ILE   B C   
5620 C C   B ILE   B 106 ? 0.3746 0.3490 0.3295 -0.0258 0.1161  -0.0002 106 ILE   B C   
5621 O O   A ILE   B 106 ? 0.3603 0.3139 0.3237 -0.0524 0.1857  0.0214  106 ILE   B O   
5622 O O   B ILE   B 106 ? 0.3701 0.3413 0.3225 -0.0315 0.1137  -0.0027 106 ILE   B O   
5623 C CB  A ILE   B 106 ? 0.4126 0.3246 0.3602 -0.0544 0.1843  0.0356  106 ILE   B CB  
5624 C CB  B ILE   B 106 ? 0.4083 0.3500 0.3495 -0.0306 0.1203  0.0162  106 ILE   B CB  
5625 C CG1 A ILE   B 106 ? 0.4172 0.3206 0.3681 -0.0475 0.1763  0.0279  106 ILE   B CG1 
5626 C CG1 B ILE   B 106 ? 0.4124 0.3478 0.3558 -0.0253 0.1152  0.0132  106 ILE   B CG1 
5627 C CG2 A ILE   B 106 ? 0.4175 0.3266 0.3741 -0.0592 0.1881  0.0402  106 ILE   B CG2 
5628 C CG2 B ILE   B 106 ? 0.4111 0.3527 0.3586 -0.0339 0.1241  0.0185  106 ILE   B CG2 
5629 C CD1 A ILE   B 106 ? 0.4183 0.3183 0.3571 -0.0431 0.1791  0.0318  106 ILE   B CD1 
5630 C CD1 B ILE   B 106 ? 0.4140 0.3464 0.3534 -0.0214 0.1149  0.0146  106 ILE   B CD1 
5653 N N   A GLN   B 107 ? 0.3463 0.3401 0.3429 -0.0407 0.1759  0.0152  107 GLN   B N   
5654 N N   B GLN   B 107 ? 0.3573 0.3541 0.3462 -0.0222 0.1114  -0.0051 107 GLN   B N   
5655 C CA  A GLN   B 107 ? 0.3280 0.3504 0.3680 -0.0314 0.1463  0.0108  107 GLN   B CA  
5656 C CA  B GLN   B 107 ? 0.3404 0.3574 0.3657 -0.0164 0.1004  -0.0041 107 GLN   B CA  
5657 C C   A GLN   B 107 ? 0.2984 0.3314 0.3363 -0.0154 0.1173  -0.0039 107 GLN   B C   
5658 C C   B GLN   B 107 ? 0.3069 0.3362 0.3327 -0.0079 0.0972  -0.0102 107 GLN   B C   
5659 O O   A GLN   B 107 ? 0.2891 0.3351 0.3584 -0.0058 0.0976  -0.0204 107 GLN   B O   
5660 O O   B GLN   B 107 ? 0.3020 0.3414 0.3456 -0.0023 0.0855  -0.0227 107 GLN   B O   
5661 C CB  A GLN   B 107 ? 0.3541 0.3834 0.4498 -0.0279 0.1165  0.0120  107 GLN   B CB  
5662 C CB  B GLN   B 107 ? 0.3633 0.3828 0.4339 -0.0142 0.0804  -0.0010 107 GLN   B CB  
5663 C CG  A GLN   B 107 ? 0.3806 0.4140 0.5253 -0.0224 0.0825  0.0136  107 GLN   B CG  
5664 C CG  B GLN   B 107 ? 0.3851 0.4065 0.4980 -0.0110 0.0579  0.0025  107 GLN   B CG  
5665 C CD  A GLN   B 107 ? 0.4000 0.4368 0.5849 -0.0215 0.0584  0.0178  107 GLN   B CD  
5666 C CD  B GLN   B 107 ? 0.4015 0.4242 0.5496 -0.0106 0.0410  0.0068  107 GLN   B CD  
5667 O OE1 A GLN   B 107 ? 0.4063 0.4453 0.6066 -0.0200 0.0546  0.0168  107 GLN   B OE1 
5668 O OE1 B GLN   B 107 ? 0.4074 0.4309 0.5675 -0.0102 0.0390  0.0071  107 GLN   B OE1 
5669 N NE2 A GLN   B 107 ? 0.4077 0.4439 0.6046 -0.0192 0.0479  0.0226  107 GLN   B NE2 
5670 N NE2 B GLN   B 107 ? 0.4079 0.4297 0.5665 -0.0088 0.0339  0.0103  107 GLN   B NE2 
5687 N N   . LEU   B 108 ? 0.2755 0.3094 0.3002 0.0002  0.1008  -0.0039 108 LEU   B N   
5688 C CA  . LEU   B 108 ? 0.2486 0.2711 0.2397 0.0203  0.0797  0.0142  108 LEU   B CA  
5689 C C   . LEU   B 108 ? 0.2055 0.2226 0.2331 0.0250  0.0523  0.0185  108 LEU   B C   
5690 O O   . LEU   B 108 ? 0.1994 0.2051 0.2149 0.0295  0.0347  0.0221  108 LEU   B O   
5691 C CB  . LEU   B 108 ? 0.2625 0.2845 0.2254 0.0184  0.0777  0.0273  108 LEU   B CB  
5692 C CG  . LEU   B 108 ? 0.2746 0.3111 0.2400 0.0212  0.0687  0.0055  108 LEU   B CG  
5693 C CD1 . LEU   B 108 ? 0.2818 0.3239 0.2290 0.0165  0.0681  0.0048  108 LEU   B CD1 
5694 C CD2 . LEU   B 108 ? 0.2881 0.3226 0.2585 0.0324  0.0516  -0.0117 108 LEU   B CD2 
5707 N N   . LEU   B 109 ? 0.1850 0.1928 0.2245 0.0196  0.0385  0.0173  109 LEU   B N   
5708 C CA  . LEU   B 109 ? 0.1703 0.1635 0.2314 0.0023  0.0338  0.0316  109 LEU   B CA  
5709 C C   . LEU   B 109 ? 0.1589 0.1416 0.2343 0.0051  0.0375  0.0194  109 LEU   B C   
5710 O O   . LEU   B 109 ? 0.1601 0.1425 0.2212 0.0037  0.0306  0.0287  109 LEU   B O   
5711 C CB  . LEU   B 109 ? 0.1770 0.1483 0.2440 -0.0001 0.0239  0.0343  109 LEU   B CB  
5712 C CG  . LEU   B 109 ? 0.1715 0.1438 0.2498 -0.0036 0.0306  0.0184  109 LEU   B CG  
5713 C CD1 . LEU   B 109 ? 0.1706 0.1558 0.2361 0.0138  0.0240  0.0278  109 LEU   B CD1 
5714 C CD2 . LEU   B 109 ? 0.1857 0.1474 0.2551 -0.0023 0.0182  0.0231  109 LEU   B CD2 
5726 N N   . LYS   B 110 ? 0.1564 0.1428 0.2337 -0.0016 0.0361  0.0148  110 LYS   B N   
5727 C CA  . LYS   B 110 ? 0.1513 0.1399 0.2267 0.0015  0.0265  0.0113  110 LYS   B CA  
5728 C C   . LYS   B 110 ? 0.1516 0.1413 0.2169 -0.0026 0.0231  0.0116  110 LYS   B C   
5729 O O   . LYS   B 110 ? 0.1433 0.1487 0.2198 -0.0072 0.0221  0.0078  110 LYS   B O   
5730 C CB  . LYS   B 110 ? 0.1520 0.1419 0.2598 -0.0046 0.0375  0.0176  110 LYS   B CB  
5731 C CG  . LYS   B 110 ? 0.1507 0.1440 0.2803 -0.0074 0.0110  0.0182  110 LYS   B CG  
5732 C CD  . LYS   B 110 ? 0.1584 0.1469 0.2791 -0.0151 0.0131  0.0192  110 LYS   B CD  
5733 C CE  . LYS   B 110 ? 0.1560 0.1614 0.2968 -0.0058 0.0154  0.0115  110 LYS   B CE  
5734 N NZ  . LYS   B 110 ? 0.1615 0.1786 0.2848 0.0021  0.0112  0.0061  110 LYS   B NZ  
5748 N N   . SER   B 111 ? 0.1499 0.1465 0.2250 -0.0077 0.0322  0.0084  111 SER   B N   
5749 C CA  . SER   B 111 ? 0.1579 0.1431 0.2108 -0.0034 0.0230  0.0109  111 SER   B CA  
5750 C C   . SER   B 111 ? 0.1467 0.1413 0.2159 -0.0066 0.0221  0.0031  111 SER   B C   
5751 O O   . SER   B 111 ? 0.1470 0.1458 0.2236 -0.0101 0.0126  0.0018  111 SER   B O   
5752 C CB  . SER   B 111 ? 0.1741 0.1679 0.2276 0.0067  0.0436  0.0251  111 SER   B CB  
5753 O OG  . SER   B 111 ? 0.1898 0.1994 0.2429 0.0131  0.0534  0.0286  111 SER   B OG  
5759 N N   . ALA   B 112 ? 0.1424 0.1431 0.2193 0.0035  0.0282  0.0117  112 ALA   B N   
5760 C CA  . ALA   B 112 ? 0.1453 0.1484 0.1957 0.0004  0.0164  0.0002  112 ALA   B CA  
5761 C C   . ALA   B 112 ? 0.1421 0.1392 0.1950 -0.0007 0.0119  -0.0006 112 ALA   B C   
5762 O O   . ALA   B 112 ? 0.1376 0.1391 0.1991 -0.0059 0.0137  0.0002  112 ALA   B O   
5763 C CB  . ALA   B 112 ? 0.1449 0.1536 0.2126 0.0037  0.0134  0.0191  112 ALA   B CB  
5769 N N   . TYR   B 113 ? 0.1364 0.1230 0.2040 -0.0015 0.0128  0.0054  113 TYR   B N   
5770 C CA  . TYR   B 113 ? 0.1377 0.1265 0.1896 -0.0071 0.0124  -0.0003 113 TYR   B CA  
5771 C C   . TYR   B 113 ? 0.1295 0.1194 0.1846 -0.0118 0.0044  0.0040  113 TYR   B C   
5772 O O   . TYR   B 113 ? 0.1419 0.1273 0.1827 -0.0094 0.0038  -0.0001 113 TYR   B O   
5773 C CB  . TYR   B 113 ? 0.1377 0.1234 0.1987 -0.0057 0.0218  0.0129  113 TYR   B CB  
5774 C CG  . TYR   B 113 ? 0.1361 0.1264 0.2077 -0.0077 0.0133  0.0060  113 TYR   B CG  
5775 C CD1 . TYR   B 113 ? 0.1393 0.1311 0.2225 -0.0064 0.0171  0.0108  113 TYR   B CD1 
5776 C CD2 . TYR   B 113 ? 0.1485 0.1313 0.2148 -0.0069 0.0076  0.0094  113 TYR   B CD2 
5777 C CE1 . TYR   B 113 ? 0.1404 0.1357 0.2186 -0.0101 0.0197  -0.0014 113 TYR   B CE1 
5778 C CE2 . TYR   B 113 ? 0.1509 0.1253 0.2199 0.0001  0.0078  0.0118  113 TYR   B CE2 
5779 C CZ  . TYR   B 113 ? 0.1413 0.1305 0.2247 0.0033  0.0071  0.0060  113 TYR   B CZ  
5780 O OH  . TYR   B 113 ? 0.1480 0.1239 0.2626 0.0075  0.0218  0.0045  113 TYR   B OH  
5790 N N   . GLU   B 114 ? 0.1273 0.1181 0.2024 -0.0045 0.0149  0.0022  114 GLU   B N   
5791 C CA  . GLU   B 114 ? 0.1305 0.1220 0.2031 0.0055  0.0014  -0.0034 114 GLU   B CA  
5792 C C   . GLU   B 114 ? 0.1334 0.1228 0.2001 0.0002  -0.0016 -0.0013 114 GLU   B C   
5793 O O   . GLU   B 114 ? 0.1299 0.1261 0.2128 0.0018  -0.0037 0.0089  114 GLU   B O   
5794 C CB  . GLU   B 114 ? 0.1329 0.1293 0.2216 0.0038  0.0174  0.0056  114 GLU   B CB  
5795 C CG  . GLU   B 114 ? 0.1407 0.1259 0.2140 -0.0030 0.0101  0.0038  114 GLU   B CG  
5796 C CD  . GLU   B 114 ? 0.1338 0.1326 0.2202 -0.0061 0.0039  0.0033  114 GLU   B CD  
5797 O OE1 . GLU   B 114 ? 0.1334 0.1426 0.2218 -0.0093 0.0148  0.0077  114 GLU   B OE1 
5798 O OE2 . GLU   B 114 ? 0.1358 0.1475 0.2371 -0.0176 0.0120  0.0063  114 GLU   B OE2 
5805 N N   . ASN   B 115 ? 0.1386 0.1138 0.1909 0.0017  0.0007  0.0001  115 ASN   B N   
5806 C CA  . ASN   B 115 ? 0.1388 0.1223 0.1711 -0.0091 -0.0043 0.0022  115 ASN   B CA  
5807 C C   . ASN   B 115 ? 0.1332 0.1239 0.1852 -0.0140 -0.0055 -0.0039 115 ASN   B C   
5808 O O   . ASN   B 115 ? 0.1458 0.1227 0.1946 -0.0152 -0.0057 -0.0003 115 ASN   B O   
5809 C CB  . ASN   B 115 ? 0.1543 0.1345 0.1848 -0.0068 -0.0102 -0.0039 115 ASN   B CB  
5810 C CG  . ASN   B 115 ? 0.1567 0.1482 0.1790 -0.0017 -0.0066 -0.0041 115 ASN   B CG  
5811 O OD1 . ASN   B 115 ? 0.2028 0.1599 0.2031 -0.0002 0.0159  -0.0065 115 ASN   B OD1 
5812 N ND2 . ASN   B 115 ? 0.1510 0.1666 0.1832 -0.0091 0.0018  0.0102  115 ASN   B ND2 
5819 N N   . PHE   B 116 ? 0.1337 0.1264 0.1754 -0.0038 -0.0037 0.0011  116 PHE   B N   
5820 C CA  . PHE   B 116 ? 0.1342 0.1309 0.1700 -0.0145 -0.0015 0.0025  116 PHE   B CA  
5821 C C   . PHE   B 116 ? 0.1359 0.1113 0.1729 -0.0162 -0.0067 0.0071  116 PHE   B C   
5822 O O   . PHE   B 116 ? 0.1457 0.1259 0.1926 -0.0052 -0.0103 0.0012  116 PHE   B O   
5823 C CB  . PHE   B 116 ? 0.1336 0.1295 0.1629 -0.0107 -0.0140 0.0021  116 PHE   B CB  
5824 C CG  . PHE   B 116 ? 0.1261 0.1248 0.1596 -0.0080 -0.0041 0.0075  116 PHE   B CG  
5825 C CD1 . PHE   B 116 ? 0.1406 0.1291 0.1720 0.0011  -0.0030 0.0017  116 PHE   B CD1 
5826 C CD2 . PHE   B 116 ? 0.1309 0.1371 0.1683 -0.0040 -0.0003 -0.0019 116 PHE   B CD2 
5827 C CE1 . PHE   B 116 ? 0.1438 0.1339 0.1758 -0.0044 -0.0174 -0.0011 116 PHE   B CE1 
5828 C CE2 . PHE   B 116 ? 0.1362 0.1317 0.1728 -0.0051 -0.0000 0.0055  116 PHE   B CE2 
5829 C CZ  . PHE   B 116 ? 0.1323 0.1383 0.1760 -0.0052 -0.0096 0.0023  116 PHE   B CZ  
5839 N N   . ASN   B 117 ? 0.1341 0.1255 0.1854 -0.0140 -0.0171 0.0090  117 ASN   B N   
5840 C CA  . ASN   B 117 ? 0.1426 0.1296 0.1945 -0.0053 -0.0115 0.0021  117 ASN   B CA  
5841 C C   . ASN   B 117 ? 0.1444 0.1300 0.1965 -0.0051 -0.0168 0.0056  117 ASN   B C   
5842 O O   . ASN   B 117 ? 0.1555 0.1285 0.2260 -0.0073 -0.0357 0.0101  117 ASN   B O   
5843 C CB  . ASN   B 117 ? 0.1454 0.1302 0.2011 -0.0013 -0.0037 -0.0005 117 ASN   B CB  
5844 C CG  . ASN   B 117 ? 0.1409 0.1258 0.2084 -0.0002 -0.0085 -0.0044 117 ASN   B CG  
5845 O OD1 . ASN   B 117 ? 0.1566 0.1267 0.2332 -0.0164 -0.0105 -0.0034 117 ASN   B OD1 
5846 N ND2 . ASN   B 117 ? 0.1451 0.1298 0.2050 -0.0050 -0.0086 -0.0063 117 ASN   B ND2 
5853 N N   . GLN   B 118 ? 0.1444 0.1289 0.1837 -0.0134 -0.0171 0.0024  118 GLN   B N   
5854 C CA  . GLN   B 118 ? 0.1537 0.1288 0.1979 -0.0040 -0.0089 -0.0043 118 GLN   B CA  
5855 C C   . GLN   B 118 ? 0.1515 0.1250 0.2103 -0.0055 -0.0116 -0.0057 118 GLN   B C   
5856 O O   . GLN   B 118 ? 0.1709 0.1274 0.2434 -0.0112 -0.0037 0.0098  118 GLN   B O   
5857 C CB  . GLN   B 118 ? 0.1554 0.1379 0.2106 -0.0019 -0.0123 0.0029  118 GLN   B CB  
5858 C CG  . GLN   B 118 ? 0.1656 0.1368 0.2084 0.0102  -0.0104 -0.0048 118 GLN   B CG  
5859 C CD  . GLN   B 118 ? 0.1708 0.1300 0.2111 -0.0022 -0.0122 -0.0146 118 GLN   B CD  
5860 O OE1 . GLN   B 118 ? 0.1718 0.1293 0.2314 -0.0049 -0.0035 -0.0062 118 GLN   B OE1 
5861 N NE2 . GLN   B 118 ? 0.1798 0.1342 0.2149 0.0009  -0.0159 -0.0049 118 GLN   B NE2 
5870 N N   . HIS   B 119 ? 0.1518 0.1281 0.1784 -0.0083 -0.0173 0.0040  119 HIS   B N   
5871 C CA  . HIS   B 119 ? 0.1627 0.1388 0.1749 -0.0065 -0.0232 0.0043  119 HIS   B CA  
5872 C C   . HIS   B 119 ? 0.1684 0.1406 0.1658 -0.0073 -0.0375 0.0115  119 HIS   B C   
5873 O O   . HIS   B 119 ? 0.1760 0.1370 0.1918 -0.0311 -0.0295 0.0055  119 HIS   B O   
5874 C CB  . HIS   B 119 ? 0.1630 0.1444 0.1837 -0.0073 -0.0269 -0.0005 119 HIS   B CB  
5875 C CG  . HIS   B 119 ? 0.1666 0.1751 0.2047 0.0015  -0.0503 -0.0146 119 HIS   B CG  
5876 N ND1 . HIS   B 119 ? 0.1752 0.1894 0.2410 -0.0016 -0.0492 -0.0335 119 HIS   B ND1 
5877 C CD2 . HIS   B 119 ? 0.1818 0.1929 0.2089 0.0336  -0.0550 -0.0191 119 HIS   B CD2 
5878 C CE1 . HIS   B 119 ? 0.1951 0.2044 0.2552 0.0115  -0.0517 -0.0418 119 HIS   B CE1 
5879 N NE2 . HIS   B 119 ? 0.1987 0.2159 0.2249 0.0271  -0.0568 -0.0331 119 HIS   B NE2 
5887 N N   . GLU   B 120 ? 0.1891 0.1352 0.1659 -0.0122 -0.0407 0.0092  120 GLU   B N   
5888 C CA  . GLU   B 120 ? 0.2127 0.1509 0.1700 -0.0034 -0.0521 0.0228  120 GLU   B CA  
5889 C C   . GLU   B 120 ? 0.1878 0.1343 0.1697 -0.0176 -0.0376 0.0254  120 GLU   B C   
5890 O O   . GLU   B 120 ? 0.1866 0.1524 0.1752 -0.0171 -0.0372 0.0136  120 GLU   B O   
5891 C CB  . GLU   B 120 ? 0.2840 0.1854 0.2345 0.0207  -0.0803 0.0411  120 GLU   B CB  
5892 C CG  . GLU   B 120 ? 0.3449 0.2674 0.3413 0.0278  -0.0969 0.0614  120 GLU   B CG  
5893 C CD  . GLU   B 120 ? 0.3907 0.3413 0.4443 0.0301  -0.0993 0.0784  120 GLU   B CD  
5894 O OE1 . GLU   B 120 ? 0.4140 0.3655 0.4789 0.0212  -0.0923 0.0955  120 GLU   B OE1 
5895 O OE2 . GLU   B 120 ? 0.4137 0.3703 0.4973 0.0306  -0.0972 0.0714  120 GLU   B OE2 
5902 N N   . VAL   B 121 ? 0.1741 0.1388 0.1677 -0.0202 -0.0263 0.0151  121 VAL   B N   
5903 C CA  . VAL   B 121 ? 0.1721 0.1524 0.1547 -0.0182 -0.0325 0.0197  121 VAL   B CA  
5904 C C   . VAL   B 121 ? 0.1695 0.1412 0.1486 -0.0212 -0.0264 0.0148  121 VAL   B C   
5905 O O   . VAL   B 121 ? 0.1765 0.1411 0.1697 -0.0319 -0.0293 0.0085  121 VAL   B O   
5906 C CB  . VAL   B 121 ? 0.1921 0.1901 0.1615 -0.0138 -0.0394 0.0234  121 VAL   B CB  
5907 C CG1 . VAL   B 121 ? 0.1961 0.1981 0.2110 -0.0258 -0.0194 0.0293  121 VAL   B CG1 
5908 C CG2 . VAL   B 121 ? 0.2193 0.2110 0.1756 -0.0042 -0.0216 0.0042  121 VAL   B CG2 
5918 N N   . LEU   B 122 ? 0.1597 0.1365 0.1495 -0.0171 -0.0300 0.0104  122 LEU   B N   
5919 C CA  . LEU   B 122 ? 0.1464 0.1491 0.1369 -0.0197 -0.0287 0.0159  122 LEU   B CA  
5920 C C   . LEU   B 122 ? 0.1509 0.1318 0.1491 -0.0232 -0.0287 0.0085  122 LEU   B C   
5921 O O   . LEU   B 122 ? 0.1610 0.1331 0.1801 -0.0310 -0.0348 0.0014  122 LEU   B O   
5922 C CB  . LEU   B 122 ? 0.1657 0.1634 0.1846 -0.0077 -0.0272 0.0206  122 LEU   B CB  
5923 C CG  . LEU   B 122 ? 0.1585 0.1758 0.1955 -0.0211 -0.0130 0.0155  122 LEU   B CG  
5924 C CD1 . LEU   B 122 ? 0.1585 0.2019 0.1978 -0.0270 -0.0290 0.0133  122 LEU   B CD1 
5925 C CD2 . LEU   B 122 ? 0.1607 0.1669 0.1628 -0.0114 -0.0167 -0.0023 122 LEU   B CD2 
5937 N N   . LEU   B 123 ? 0.1500 0.1195 0.1414 -0.0203 -0.0257 0.0097  123 LEU   B N   
5938 C CA  . LEU   B 123 ? 0.1531 0.1251 0.1558 -0.0275 -0.0249 0.0041  123 LEU   B CA  
5939 C C   . LEU   B 123 ? 0.1483 0.1250 0.1456 -0.0254 -0.0238 0.0029  123 LEU   B C   
5940 O O   . LEU   B 123 ? 0.1591 0.1292 0.1428 -0.0314 -0.0167 0.0007  123 LEU   B O   
5941 C CB  . LEU   B 123 ? 0.1524 0.1310 0.1576 -0.0280 -0.0168 0.0048  123 LEU   B CB  
5942 C CG  . LEU   B 123 ? 0.1497 0.1350 0.1635 -0.0183 -0.0134 0.0106  123 LEU   B CG  
5943 C CD1 . LEU   B 123 ? 0.1646 0.1392 0.1721 -0.0142 -0.0021 -0.0104 123 LEU   B CD1 
5944 C CD2 . LEU   B 123 ? 0.1647 0.1441 0.1758 -0.0178 -0.0063 0.0139  123 LEU   B CD2 
5956 N N   . ALA   B 124 ? 0.1405 0.1249 0.1425 -0.0238 -0.0124 -0.0026 124 ALA   B N   
5957 C CA  . ALA   B 124 ? 0.1410 0.1286 0.1462 -0.0178 -0.0111 -0.0035 124 ALA   B CA  
5958 C C   . ALA   B 124 ? 0.1404 0.1253 0.1321 -0.0206 -0.0153 -0.0078 124 ALA   B C   
5959 O O   . ALA   B 124 ? 0.1452 0.1335 0.1445 -0.0167 -0.0146 0.0007  124 ALA   B O   
5960 C CB  . ALA   B 124 ? 0.1481 0.1212 0.1545 -0.0057 -0.0076 -0.0030 124 ALA   B CB  
5966 N N   . PRO   B 125 ? 0.1491 0.1269 0.1371 -0.0193 -0.0219 0.0103  125 PRO   B N   
5967 C CA  . PRO   B 125 ? 0.1518 0.1321 0.1465 -0.0199 -0.0192 0.0270  125 PRO   B CA  
5968 C C   . PRO   B 125 ? 0.1412 0.1311 0.1644 -0.0179 -0.0089 0.0128  125 PRO   B C   
5969 O O   . PRO   B 125 ? 0.1393 0.1369 0.1851 -0.0135 0.0013  0.0186  125 PRO   B O   
5970 C CB  . PRO   B 125 ? 0.1625 0.1567 0.1761 -0.0226 -0.0256 0.0369  125 PRO   B CB  
5971 C CG  . PRO   B 125 ? 0.1605 0.1604 0.1651 -0.0303 -0.0298 0.0224  125 PRO   B CG  
5972 C CD  . PRO   B 125 ? 0.1545 0.1398 0.1485 -0.0319 -0.0211 0.0099  125 PRO   B CD  
5980 N N   . LEU   B 126 ? 0.1499 0.1278 0.1969 -0.0222 0.0074  0.0215  126 LEU   B N   
5981 C CA  . LEU   B 126 ? 0.1629 0.1356 0.1980 -0.0142 0.0158  0.0180  126 LEU   B CA  
5982 C C   . LEU   B 126 ? 0.1556 0.1430 0.2004 0.0025  0.0209  0.0263  126 LEU   B C   
5983 O O   . LEU   B 126 ? 0.1754 0.1748 0.2266 0.0267  -0.0058 0.0022  126 LEU   B O   
5984 C CB  . LEU   B 126 ? 0.1816 0.1401 0.2321 -0.0211 0.0279  0.0153  126 LEU   B CB  
5985 C CG  . LEU   B 126 ? 0.1954 0.1494 0.2508 -0.0266 0.0203  -0.0141 126 LEU   B CG  
5986 C CD1 . LEU   B 126 ? 0.2063 0.1604 0.3027 -0.0286 0.0160  -0.0220 126 LEU   B CD1 
5987 C CD2 . LEU   B 126 ? 0.2004 0.1535 0.2470 -0.0283 0.0177  -0.0053 126 LEU   B CD2 
5999 N N   . LEU   B 127 ? 0.1513 0.1306 0.2068 0.0016  0.0251  0.0152  127 LEU   B N   
6000 C CA  . LEU   B 127 ? 0.1533 0.1379 0.2067 0.0012  0.0290  0.0175  127 LEU   B CA  
6001 C C   . LEU   B 127 ? 0.1520 0.1346 0.2118 -0.0046 0.0129  0.0197  127 LEU   B C   
6002 O O   . LEU   B 127 ? 0.1484 0.1390 0.2318 -0.0147 0.0064  0.0235  127 LEU   B O   
6003 C CB  . LEU   B 127 ? 0.1653 0.1457 0.2261 -0.0088 0.0227  0.0214  127 LEU   B CB  
6004 C CG  . LEU   B 127 ? 0.1728 0.1398 0.2308 0.0001  0.0269  0.0148  127 LEU   B CG  
6005 C CD1 . LEU   B 127 ? 0.1856 0.1422 0.2416 -0.0042 0.0156  0.0074  127 LEU   B CD1 
6006 C CD2 . LEU   B 127 ? 0.1846 0.1499 0.2428 -0.0112 0.0198  0.0244  127 LEU   B CD2 
6018 N N   . SER   B 128 ? 0.1508 0.1356 0.2169 0.0042  0.0052  0.0123  128 SER   B N   
6019 C CA  . SER   B 128 ? 0.1726 0.1491 0.2142 0.0058  -0.0006 0.0247  128 SER   B CA  
6020 C C   . SER   B 128 ? 0.1849 0.1497 0.2456 0.0055  -0.0204 0.0237  128 SER   B C   
6021 O O   . SER   B 128 ? 0.2074 0.1476 0.2904 0.0040  -0.0155 0.0299  128 SER   B O   
6022 C CB  . SER   B 128 ? 0.1848 0.1528 0.2092 0.0044  0.0062  0.0335  128 SER   B CB  
6023 O OG  . SER   B 128 ? 0.1873 0.1609 0.2212 0.0111  0.0141  0.0338  128 SER   B OG  
6029 N N   . ALA   B 129 ? 0.2011 0.1565 0.2640 0.0231  -0.0100 0.0078  129 ALA   B N   
6030 C CA  . ALA   B 129 ? 0.2116 0.1643 0.2728 0.0298  -0.0105 0.0034  129 ALA   B CA  
6031 C C   . ALA   B 129 ? 0.2003 0.1544 0.2652 0.0209  0.0032  -0.0022 129 ALA   B C   
6032 O O   . ALA   B 129 ? 0.1846 0.1594 0.2514 0.0205  -0.0030 0.0055  129 ALA   B O   
6033 C CB  . ALA   B 129 ? 0.2334 0.1904 0.3053 0.0299  -0.0033 -0.0057 129 ALA   B CB  
6039 N N   . GLY   B 130 ? 0.1904 0.1534 0.2740 0.0316  0.0028  0.0024  130 GLY   B N   
6040 C CA  . GLY   B 130 ? 0.2001 0.1662 0.2830 0.0200  0.0280  0.0116  130 GLY   B CA  
6041 C C   . GLY   B 130 ? 0.2055 0.1690 0.2624 0.0145  0.0188  0.0187  130 GLY   B C   
6042 O O   . GLY   B 130 ? 0.2165 0.1840 0.2793 0.0213  0.0137  0.0280  130 GLY   B O   
6046 N N   . ILE   B 131 ? 0.2001 0.1895 0.2682 0.0308  0.0121  0.0135  131 ILE   B N   
6047 C CA  . ILE   B 131 ? 0.2229 0.2015 0.2771 0.0271  -0.0036 0.0209  131 ILE   B CA  
6048 C C   . ILE   B 131 ? 0.2339 0.1927 0.2383 0.0182  -0.0054 0.0197  131 ILE   B C   
6049 O O   . ILE   B 131 ? 0.2627 0.2134 0.2551 0.0167  -0.0211 0.0249  131 ILE   B O   
6050 C CB  . ILE   B 131 ? 0.2230 0.2280 0.3230 0.0265  -0.0093 0.0252  131 ILE   B CB  
6051 C CG1 . ILE   B 131 ? 0.2294 0.2488 0.3478 -0.0012 -0.0016 0.0326  131 ILE   B CG1 
6052 C CG2 . ILE   B 131 ? 0.2301 0.2412 0.3459 0.0386  -0.0096 0.0137  131 ILE   B CG2 
6053 C CD1 . ILE   B 131 ? 0.2356 0.2684 0.3686 -0.0169 -0.0009 0.0367  131 ILE   B CD1 
6065 N N   . PHE   B 132 ? 0.2211 0.1709 0.2221 0.0181  0.0158  0.0191  132 PHE   B N   
6066 C CA  . PHE   B 132 ? 0.2304 0.1736 0.2274 0.0101  0.0353  0.0155  132 PHE   B CA  
6067 C C   . PHE   B 132 ? 0.2456 0.1908 0.2473 0.0090  0.0444  0.0156  132 PHE   B C   
6068 O O   . PHE   B 132 ? 0.2565 0.2129 0.2720 0.0047  0.0542  0.0191  132 PHE   B O   
6069 C CB  . PHE   B 132 ? 0.2151 0.1680 0.2163 0.0083  0.0412  0.0197  132 PHE   B CB  
6070 C CG  . PHE   B 132 ? 0.2072 0.1720 0.2092 0.0161  0.0281  0.0245  132 PHE   B CG  
6071 C CD1 . PHE   B 132 ? 0.2148 0.1723 0.2460 0.0085  0.0255  0.0288  132 PHE   B CD1 
6072 C CD2 . PHE   B 132 ? 0.2019 0.1778 0.1853 0.0204  0.0166  0.0293  132 PHE   B CD2 
6073 C CE1 . PHE   B 132 ? 0.2160 0.1793 0.2605 0.0003  0.0238  0.0278  132 PHE   B CE1 
6074 C CE2 . PHE   B 132 ? 0.2130 0.1850 0.2081 0.0139  0.0150  0.0243  132 PHE   B CE2 
6075 C CZ  . PHE   B 132 ? 0.2195 0.1828 0.2426 0.0035  0.0075  0.0402  132 PHE   B CZ  
6085 N N   . GLY   B 133 ? 0.2399 0.1820 0.2468 0.0009  0.0281  0.0399  133 GLY   B N   
6086 C CA  . GLY   B 133 ? 0.2455 0.1909 0.2709 -0.0183 0.0251  0.0478  133 GLY   B CA  
6087 C C   . GLY   B 133 ? 0.2500 0.1991 0.2807 -0.0310 0.0326  0.0574  133 GLY   B C   
6088 O O   . GLY   B 133 ? 0.2664 0.2117 0.3223 -0.0514 0.0331  0.0659  133 GLY   B O   
6092 N N   . ALA   B 134 ? 0.2403 0.2022 0.2572 -0.0272 0.0311  0.0378  134 ALA   B N   
6093 C CA  . ALA   B 134 ? 0.2380 0.1998 0.2721 -0.0199 0.0382  0.0221  134 ALA   B CA  
6094 C C   . ALA   B 134 ? 0.2417 0.1839 0.2679 -0.0203 0.0393  0.0436  134 ALA   B C   
6095 O O   . ALA   B 134 ? 0.2504 0.2008 0.2807 -0.0021 0.0362  0.0350  134 ALA   B O   
6096 C CB  . ALA   B 134 ? 0.2377 0.2022 0.2828 -0.0143 0.0377  0.0206  134 ALA   B CB  
6102 N N   . ASP   B 135 ? 0.2544 0.1765 0.2656 -0.0237 0.0163  0.0498  135 ASP   B N   
6103 C CA  . ASP   B 135 ? 0.2669 0.1735 0.2784 -0.0182 0.0027  0.0458  135 ASP   B CA  
6104 C C   . ASP   B 135 ? 0.2420 0.1593 0.2696 -0.0058 0.0003  0.0395  135 ASP   B C   
6105 O O   . ASP   B 135 ? 0.2328 0.1552 0.2848 -0.0052 0.0080  0.0380  135 ASP   B O   
6106 C CB  . ASP   B 135 ? 0.2995 0.1842 0.3047 -0.0393 0.0006  0.0416  135 ASP   B CB  
6107 C CG  . ASP   B 135 ? 0.3283 0.1854 0.3531 -0.0609 0.0079  0.0404  135 ASP   B CG  
6108 O OD1 . ASP   B 135 ? 0.3421 0.1708 0.3533 -0.0377 -0.0023 0.0398  135 ASP   B OD1 
6109 O OD2 . ASP   B 135 ? 0.3486 0.2171 0.4090 -0.0783 0.0151  0.0253  135 ASP   B OD2 
6114 N N   . PRO   B 136 ? 0.2282 0.1610 0.2858 0.0180  -0.0181 0.0312  136 PRO   B N   
6115 C CA  . PRO   B 136 ? 0.2030 0.1529 0.2827 0.0144  -0.0141 0.0165  136 PRO   B CA  
6116 C C   . PRO   B 136 ? 0.1792 0.1395 0.2885 0.0146  -0.0116 0.0144  136 PRO   B C   
6117 O O   . PRO   B 136 ? 0.1658 0.1409 0.2834 0.0099  -0.0015 0.0135  136 PRO   B O   
6118 C CB  . PRO   B 136 ? 0.2121 0.1739 0.2971 0.0259  -0.0272 0.0037  136 PRO   B CB  
6119 C CG  . PRO   B 136 ? 0.2396 0.1863 0.3225 0.0305  -0.0156 0.0063  136 PRO   B CG  
6120 C CD  . PRO   B 136 ? 0.2395 0.1799 0.3059 0.0340  -0.0114 0.0130  136 PRO   B CD  
6128 N N   . ILE   B 137 ? 0.1943 0.1364 0.2992 0.0115  -0.0131 0.0044  137 ILE   B N   
6129 C CA  . ILE   B 137 ? 0.2028 0.1314 0.2999 -0.0005 0.0001  0.0054  137 ILE   B CA  
6130 C C   . ILE   B 137 ? 0.1926 0.1413 0.2943 -0.0078 0.0115  0.0135  137 ILE   B C   
6131 O O   . ILE   B 137 ? 0.1862 0.1411 0.2917 -0.0067 0.0079  0.0088  137 ILE   B O   
6132 C CB  . ILE   B 137 ? 0.2332 0.1413 0.3437 -0.0088 -0.0023 0.0076  137 ILE   B CB  
6133 C CG1 . ILE   B 137 ? 0.2586 0.1610 0.3807 -0.0018 -0.0008 -0.0012 137 ILE   B CG1 
6134 C CG2 . ILE   B 137 ? 0.2374 0.1440 0.3541 -0.0342 0.0006  0.0102  137 ILE   B CG2 
6135 C CD1 . ILE   B 137 ? 0.2825 0.1902 0.4188 0.0082  -0.0078 0.0049  137 ILE   B CD1 
6147 N N   . HIS   B 138 ? 0.2034 0.1439 0.2913 -0.0142 0.0300  0.0137  138 HIS   B N   
6148 C CA  . HIS   B 138 ? 0.2151 0.1503 0.2889 -0.0098 0.0346  0.0173  138 HIS   B CA  
6149 C C   . HIS   B 138 ? 0.1965 0.1481 0.2760 -0.0088 0.0306  0.0265  138 HIS   B C   
6150 O O   . HIS   B 138 ? 0.1879 0.1520 0.2966 -0.0045 0.0369  0.0311  138 HIS   B O   
6151 C CB  . HIS   B 138 ? 0.2414 0.1678 0.3066 -0.0135 0.0470  0.0151  138 HIS   B CB  
6152 C CG  . HIS   B 138 ? 0.2577 0.1816 0.3101 -0.0111 0.0698  0.0313  138 HIS   B CG  
6153 N ND1 . HIS   B 138 ? 0.2671 0.1990 0.3378 -0.0043 0.0875  0.0255  138 HIS   B ND1 
6154 C CD2 . HIS   B 138 ? 0.2725 0.1901 0.3126 -0.0151 0.0699  0.0331  138 HIS   B CD2 
6155 C CE1 . HIS   B 138 ? 0.2725 0.1977 0.3336 -0.0040 0.0904  0.0278  138 HIS   B CE1 
6156 N NE2 . HIS   B 138 ? 0.2777 0.1872 0.3137 -0.0045 0.0841  0.0238  138 HIS   B NE2 
6164 N N   . SER   B 139 ? 0.1912 0.1323 0.2705 0.0023  0.0242  0.0214  139 SER   B N   
6165 C CA  . SER   B 139 ? 0.1841 0.1317 0.2481 -0.0028 0.0217  0.0116  139 SER   B CA  
6166 C C   . SER   B 139 ? 0.1587 0.1253 0.2415 -0.0015 0.0146  0.0123  139 SER   B C   
6167 O O   . SER   B 139 ? 0.1633 0.1264 0.2550 -0.0008 0.0054  0.0181  139 SER   B O   
6168 C CB  . SER   B 139 ? 0.1903 0.1388 0.2587 -0.0029 -0.0007 0.0080  139 SER   B CB  
6169 O OG  . SER   B 139 ? 0.1939 0.1324 0.2532 -0.0056 -0.0089 0.0222  139 SER   B OG  
6175 N N   . LEU   B 140 ? 0.1608 0.1231 0.2307 -0.0091 0.0185  -0.0036 140 LEU   B N   
6176 C CA  . LEU   B 140 ? 0.1614 0.1260 0.2444 -0.0078 0.0155  0.0019  140 LEU   B CA  
6177 C C   . LEU   B 140 ? 0.1522 0.1255 0.2481 -0.0106 0.0013  0.0011  140 LEU   B C   
6178 O O   . LEU   B 140 ? 0.1520 0.1331 0.2530 -0.0073 -0.0000 0.0079  140 LEU   B O   
6179 C CB  . LEU   B 140 ? 0.1580 0.1250 0.2590 -0.0154 0.0212  -0.0146 140 LEU   B CB  
6180 C CG  . LEU   B 140 ? 0.1684 0.1278 0.2544 -0.0171 0.0052  0.0015  140 LEU   B CG  
6181 C CD1 . LEU   B 140 ? 0.1777 0.1385 0.2678 -0.0159 0.0014  0.0071  140 LEU   B CD1 
6182 C CD2 . LEU   B 140 ? 0.1825 0.1480 0.2637 -0.0160 -0.0021 -0.0077 140 LEU   B CD2 
6194 N N   . ARG   B 141 ? 0.1486 0.1250 0.2679 -0.0055 0.0137  0.0030  141 ARG   B N   
6195 C CA  . ARG   B 141 ? 0.1563 0.1213 0.3109 -0.0139 0.0232  -0.0013 141 ARG   B CA  
6196 C C   . ARG   B 141 ? 0.1473 0.1252 0.3017 -0.0173 0.0080  -0.0062 141 ARG   B C   
6197 O O   . ARG   B 141 ? 0.1454 0.1307 0.3031 -0.0158 -0.0079 -0.0135 141 ARG   B O   
6198 C CB  . ARG   B 141 ? 0.1708 0.1386 0.3411 -0.0195 0.0420  -0.0028 141 ARG   B CB  
6199 C CG  . ARG   B 141 ? 0.2061 0.1685 0.3621 -0.0189 0.0434  -0.0021 141 ARG   B CG  
6200 C CD  . ARG   B 141 ? 0.2514 0.1890 0.3642 -0.0153 0.0212  -0.0178 141 ARG   B CD  
6201 N NE  . ARG   B 141 ? 0.2755 0.1905 0.3557 -0.0346 0.0278  -0.0235 141 ARG   B NE  
6202 C CZ  . ARG   B 141 ? 0.2883 0.1790 0.3291 -0.0353 0.0353  -0.0321 141 ARG   B CZ  
6203 N NH1 . ARG   B 141 ? 0.3021 0.1682 0.3075 -0.0335 0.0296  -0.0264 141 ARG   B NH1 
6204 N NH2 . ARG   B 141 ? 0.2937 0.1925 0.3457 -0.0231 0.0237  -0.0209 141 ARG   B NH2 
6218 N N   . VAL   B 142 ? 0.1496 0.1303 0.2802 -0.0122 0.0190  -0.0018 142 VAL   B N   
6219 C CA  . VAL   B 142 ? 0.1488 0.1213 0.2772 -0.0073 0.0259  -0.0105 142 VAL   B CA  
6220 C C   . VAL   B 142 ? 0.1407 0.1220 0.2697 -0.0026 0.0100  -0.0088 142 VAL   B C   
6221 O O   . VAL   B 142 ? 0.1510 0.1248 0.2908 0.0022  0.0162  -0.0013 142 VAL   B O   
6222 C CB  . VAL   B 142 ? 0.1592 0.1391 0.2741 -0.0002 0.0287  0.0146  142 VAL   B CB  
6223 C CG1 . VAL   B 142 ? 0.1610 0.1449 0.2761 0.0043  0.0246  0.0048  142 VAL   B CG1 
6224 C CG2 . VAL   B 142 ? 0.1789 0.1447 0.2779 0.0085  0.0197  0.0147  142 VAL   B CG2 
6234 N N   . CYS   B 143 ? 0.1399 0.1278 0.2511 -0.0042 0.0037  0.0062  143 CYS   B N   
6235 C CA  . CYS   B 143 ? 0.1408 0.1303 0.2570 -0.0073 0.0085  -0.0007 143 CYS   B CA  
6236 C C   . CYS   B 143 ? 0.1335 0.1293 0.2629 -0.0069 0.0008  -0.0104 143 CYS   B C   
6237 O O   . CYS   B 143 ? 0.1358 0.1344 0.2614 -0.0052 -0.0067 -0.0097 143 CYS   B O   
6238 C CB  . CYS   B 143 ? 0.1497 0.1408 0.2528 -0.0113 0.0030  0.0019  143 CYS   B CB  
6239 S SG  . CYS   B 143 ? 0.1516 0.1495 0.2334 -0.0071 0.0028  0.0046  143 CYS   B SG  
6245 N N   . VAL   B 144 ? 0.1405 0.1280 0.2832 -0.0144 -0.0015 -0.0177 144 VAL   B N   
6246 C CA  . VAL   B 144 ? 0.1483 0.1374 0.3035 -0.0230 -0.0188 -0.0214 144 VAL   B CA  
6247 C C   . VAL   B 144 ? 0.1414 0.1448 0.3065 -0.0144 -0.0208 0.0015  144 VAL   B C   
6248 O O   . VAL   B 144 ? 0.1546 0.1655 0.3259 -0.0027 -0.0154 0.0170  144 VAL   B O   
6249 C CB  . VAL   B 144 ? 0.1765 0.1603 0.3532 -0.0183 -0.0193 -0.0376 144 VAL   B CB  
6250 C CG1 . VAL   B 144 ? 0.2003 0.1945 0.3991 -0.0079 -0.0212 -0.0320 144 VAL   B CG1 
6251 C CG2 . VAL   B 144 ? 0.1895 0.1628 0.3321 -0.0031 -0.0364 -0.0414 144 VAL   B CG2 
6261 N N   . ASP   B 145 ? 0.1475 0.1354 0.3105 -0.0111 -0.0064 -0.0070 145 ASP   B N   
6262 C CA  . ASP   B 145 ? 0.1513 0.1380 0.3370 -0.0059 0.0079  -0.0066 145 ASP   B CA  
6263 C C   . ASP   B 145 ? 0.1467 0.1429 0.3188 -0.0101 0.0016  -0.0179 145 ASP   B C   
6264 O O   . ASP   B 145 ? 0.1530 0.1526 0.3717 -0.0075 0.0052  -0.0263 145 ASP   B O   
6265 C CB  . ASP   B 145 ? 0.1615 0.1426 0.3784 -0.0118 0.0190  -0.0113 145 ASP   B CB  
6266 C CG  . ASP   B 145 ? 0.1722 0.1501 0.4157 -0.0175 0.0265  -0.0098 145 ASP   B CG  
6267 O OD1 . ASP   B 145 ? 0.1753 0.1550 0.4166 -0.0220 -0.0098 -0.0250 145 ASP   B OD1 
6268 O OD2 . ASP   B 145 ? 0.2060 0.1583 0.4542 -0.0283 0.0467  0.0025  145 ASP   B OD2 
6273 N N   . THR   B 146 ? 0.1375 0.1300 0.2687 -0.0144 -0.0040 -0.0037 146 THR   B N   
6274 C CA  . THR   B 146 ? 0.1404 0.1335 0.2418 -0.0125 0.0119  -0.0024 146 THR   B CA  
6275 C C   . THR   B 146 ? 0.1454 0.1313 0.2378 -0.0083 0.0042  0.0009  146 THR   B C   
6276 O O   . THR   B 146 ? 0.1458 0.1274 0.2492 -0.0077 -0.0013 -0.0013 146 THR   B O   
6277 C CB  . THR   B 146 ? 0.1514 0.1346 0.2516 -0.0085 0.0136  0.0043  146 THR   B CB  
6278 O OG1 . THR   B 146 ? 0.1499 0.1349 0.2577 -0.0065 0.0219  0.0071  146 THR   B OG1 
6279 C CG2 . THR   B 146 ? 0.1634 0.1363 0.2444 -0.0064 0.0152  -0.0023 146 THR   B CG2 
6287 N N   . VAL   B 147 ? 0.1483 0.1349 0.2226 -0.0053 0.0094  0.0022  147 VAL   B N   
6288 C CA  . VAL   B 147 ? 0.1503 0.1311 0.2248 -0.0092 0.0000  0.0038  147 VAL   B CA  
6289 C C   . VAL   B 147 ? 0.1463 0.1270 0.2405 -0.0192 -0.0110 -0.0038 147 VAL   B C   
6290 O O   . VAL   B 147 ? 0.1549 0.1405 0.2480 -0.0220 -0.0387 -0.0067 147 VAL   B O   
6291 C CB  . VAL   B 147 ? 0.1582 0.1427 0.2120 -0.0074 -0.0125 0.0040  147 VAL   B CB  
6292 C CG1 . VAL   B 147 ? 0.1562 0.1567 0.1938 -0.0090 -0.0176 0.0006  147 VAL   B CG1 
6293 C CG2 . VAL   B 147 ? 0.1583 0.1377 0.2108 -0.0122 0.0050  0.0017  147 VAL   B CG2 
6303 N N   . ARG   B 148 ? 0.1487 0.1255 0.2346 -0.0075 -0.0195 -0.0064 148 ARG   B N   
6304 C CA  . ARG   B 148 ? 0.1513 0.1347 0.2238 -0.0090 -0.0340 -0.0148 148 ARG   B CA  
6305 C C   . ARG   B 148 ? 0.1545 0.1443 0.2088 -0.0115 -0.0381 -0.0064 148 ARG   B C   
6306 O O   . ARG   B 148 ? 0.1792 0.1786 0.2170 -0.0278 -0.0510 0.0005  148 ARG   B O   
6307 C CB  . ARG   B 148 ? 0.1558 0.1520 0.2200 -0.0031 -0.0368 -0.0161 148 ARG   B CB  
6308 C CG  . ARG   B 148 ? 0.1553 0.1687 0.2338 -0.0066 -0.0371 -0.0306 148 ARG   B CG  
6309 C CD  . ARG   B 148 ? 0.1623 0.1842 0.2490 0.0097  -0.0243 -0.0338 148 ARG   B CD  
6310 N NE  . ARG   B 148 ? 0.1643 0.1809 0.2516 0.0232  -0.0397 -0.0373 148 ARG   B NE  
6311 C CZ  . ARG   B 148 ? 0.1587 0.1760 0.2355 0.0111  -0.0287 -0.0265 148 ARG   B CZ  
6312 N NH1 . ARG   B 148 ? 0.1469 0.1828 0.2384 0.0018  0.0007  -0.0227 148 ARG   B NH1 
6313 N NH2 . ARG   B 148 ? 0.1778 0.1590 0.2251 0.0121  -0.0272 -0.0225 148 ARG   B NH2 
6327 N N   . THR   B 149 ? 0.1555 0.1363 0.2114 -0.0163 -0.0276 0.0068  149 THR   B N   
6328 C CA  . THR   B 149 ? 0.1610 0.1411 0.2001 -0.0174 -0.0316 0.0146  149 THR   B CA  
6329 C C   . THR   B 149 ? 0.1640 0.1432 0.1864 -0.0177 -0.0339 0.0069  149 THR   B C   
6330 O O   . THR   B 149 ? 0.1609 0.1397 0.2049 -0.0236 -0.0204 0.0077  149 THR   B O   
6331 C CB  . THR   B 149 ? 0.1619 0.1405 0.2114 -0.0204 -0.0314 0.0039  149 THR   B CB  
6332 O OG1 . THR   B 149 ? 0.1679 0.1462 0.2035 -0.0269 -0.0427 0.0007  149 THR   B OG1 
6333 C CG2 . THR   B 149 ? 0.1679 0.1485 0.2280 -0.0087 -0.0138 0.0052  149 THR   B CG2 
6341 N N   . ASN   B 150 ? 0.1726 0.1389 0.1856 -0.0171 -0.0425 0.0083  150 ASN   B N   
6342 C CA  . ASN   B 150 ? 0.1796 0.1558 0.1790 -0.0175 -0.0423 0.0017  150 ASN   B CA  
6343 C C   . ASN   B 150 ? 0.1677 0.1490 0.1803 -0.0172 -0.0381 0.0007  150 ASN   B C   
6344 O O   . ASN   B 150 ? 0.1760 0.1446 0.2050 -0.0314 -0.0466 -0.0029 150 ASN   B O   
6345 C CB  . ASN   B 150 ? 0.2018 0.1842 0.1928 -0.0256 -0.0578 0.0150  150 ASN   B CB  
6346 C CG  . ASN   B 150 ? 0.2245 0.2218 0.2421 -0.0242 -0.0457 0.0375  150 ASN   B CG  
6347 O OD1 . ASN   B 150 ? 0.2288 0.2401 0.2398 -0.0343 -0.0607 0.0344  150 ASN   B OD1 
6348 N ND2 . ASN   B 150 ? 0.2409 0.2431 0.2789 -0.0134 -0.0553 0.0811  150 ASN   B ND2 
6355 N N   . VAL   B 151 ? 0.1583 0.1424 0.1850 -0.0217 -0.0443 0.0064  151 VAL   B N   
6356 C CA  . VAL   B 151 ? 0.1591 0.1443 0.1772 -0.0240 -0.0311 0.0054  151 VAL   B CA  
6357 C C   . VAL   B 151 ? 0.1605 0.1391 0.1682 -0.0340 -0.0335 0.0008  151 VAL   B C   
6358 O O   . VAL   B 151 ? 0.1748 0.1495 0.2119 -0.0290 -0.0338 -0.0082 151 VAL   B O   
6359 C CB  . VAL   B 151 ? 0.1783 0.1583 0.1974 -0.0180 -0.0305 0.0012  151 VAL   B CB  
6360 C CG1 . VAL   B 151 ? 0.1949 0.1689 0.2279 -0.0187 -0.0169 -0.0034 151 VAL   B CG1 
6361 C CG2 . VAL   B 151 ? 0.1897 0.1814 0.1812 0.0034  -0.0314 0.0224  151 VAL   B CG2 
6371 N N   . TYR   B 152 ? 0.1552 0.1316 0.1753 -0.0258 -0.0287 -0.0033 152 TYR   B N   
6372 C CA  . TYR   B 152 ? 0.1620 0.1478 0.1440 -0.0282 -0.0212 -0.0045 152 TYR   B CA  
6373 C C   . TYR   B 152 ? 0.1635 0.1304 0.1424 -0.0247 -0.0188 -0.0097 152 TYR   B C   
6374 O O   . TYR   B 152 ? 0.1707 0.1344 0.1624 -0.0262 -0.0152 -0.0044 152 TYR   B O   
6375 C CB  . TYR   B 152 ? 0.1819 0.1588 0.1521 -0.0283 -0.0162 0.0146  152 TYR   B CB  
6376 C CG  . TYR   B 152 ? 0.1995 0.1695 0.1480 -0.0466 -0.0203 0.0051  152 TYR   B CG  
6377 C CD1 . TYR   B 152 ? 0.2072 0.1846 0.1363 -0.0403 -0.0293 0.0209  152 TYR   B CD1 
6378 C CD2 . TYR   B 152 ? 0.2150 0.1851 0.1570 -0.0576 -0.0148 -0.0040 152 TYR   B CD2 
6379 C CE1 . TYR   B 152 ? 0.2237 0.2051 0.1686 -0.0386 -0.0383 0.0274  152 TYR   B CE1 
6380 C CE2 . TYR   B 152 ? 0.2243 0.2094 0.1560 -0.0586 -0.0264 0.0026  152 TYR   B CE2 
6381 C CZ  . TYR   B 152 ? 0.2282 0.2277 0.1554 -0.0491 -0.0538 0.0243  152 TYR   B CZ  
6382 O OH  . TYR   B 152 ? 0.2483 0.2644 0.2102 -0.0367 -0.0565 0.0288  152 TYR   B OH  
6392 N N   . LEU   B 153 ? 0.1666 0.1274 0.1599 -0.0292 -0.0225 0.0005  153 LEU   B N   
6393 C CA  . LEU   B 153 ? 0.1698 0.1234 0.1557 -0.0241 -0.0064 -0.0122 153 LEU   B CA  
6394 C C   . LEU   B 153 ? 0.1696 0.1234 0.1625 -0.0253 -0.0082 -0.0194 153 LEU   B C   
6395 O O   . LEU   B 153 ? 0.1745 0.1497 0.1685 -0.0133 -0.0141 -0.0307 153 LEU   B O   
6396 C CB  . LEU   B 153 ? 0.1660 0.1192 0.1670 -0.0284 -0.0044 -0.0030 153 LEU   B CB  
6397 C CG  . LEU   B 153 ? 0.1606 0.1330 0.2064 -0.0274 -0.0041 -0.0033 153 LEU   B CG  
6398 C CD1 . LEU   B 153 ? 0.1724 0.1521 0.2163 -0.0257 0.0005  0.0101  153 LEU   B CD1 
6399 C CD2 . LEU   B 153 ? 0.1623 0.1484 0.2194 -0.0295 0.0076  0.0040  153 LEU   B CD2 
6411 N N   . ALA   B 154 ? 0.1597 0.1303 0.1698 -0.0133 -0.0129 -0.0164 154 ALA   B N   
6412 C CA  . ALA   B 154 ? 0.1678 0.1414 0.1883 -0.0048 -0.0146 -0.0142 154 ALA   B CA  
6413 C C   . ALA   B 154 ? 0.1834 0.1440 0.1910 0.0034  -0.0218 -0.0242 154 ALA   B C   
6414 O O   . ALA   B 154 ? 0.2129 0.1467 0.2151 0.0089  -0.0182 -0.0078 154 ALA   B O   
6415 C CB  . ALA   B 154 ? 0.1653 0.1545 0.2077 -0.0034 -0.0119 -0.0220 154 ALA   B CB  
6421 N N   . VAL   B 155 ? 0.1529 0.1362 0.2154 -0.0037 0.0013  -0.0127 155 VAL   B N   
6422 C CA  . VAL   B 155 ? 0.1495 0.1342 0.2388 -0.0004 -0.0072 -0.0074 155 VAL   B CA  
6423 C C   . VAL   B 155 ? 0.1489 0.1314 0.2193 -0.0002 -0.0096 -0.0209 155 VAL   B C   
6424 O O   . VAL   B 155 ? 0.1641 0.1525 0.2578 -0.0012 -0.0097 -0.0394 155 VAL   B O   
6425 C CB  . VAL   B 155 ? 0.1523 0.1501 0.2710 -0.0032 -0.0149 0.0141  155 VAL   B CB  
6426 C CG1 . VAL   B 155 ? 0.1591 0.1498 0.2815 -0.0130 -0.0159 0.0153  155 VAL   B CG1 
6427 C CG2 . VAL   B 155 ? 0.1550 0.1602 0.2937 -0.0067 -0.0139 0.0407  155 VAL   B CG2 
6437 N N   . PHE   B 156 ? 0.1363 0.1437 0.2358 0.0046  -0.0060 -0.0177 156 PHE   B N   
6438 C CA  . PHE   B 156 ? 0.1394 0.1527 0.2776 0.0069  -0.0048 -0.0145 156 PHE   B CA  
6439 C C   . PHE   B 156 ? 0.1390 0.1615 0.3207 0.0100  -0.0090 -0.0332 156 PHE   B C   
6440 O O   . PHE   B 156 ? 0.1609 0.1904 0.3425 0.0175  -0.0007 -0.0423 156 PHE   B O   
6441 C CB  . PHE   B 156 ? 0.1497 0.1533 0.2629 -0.0040 -0.0085 -0.0092 156 PHE   B CB  
6442 C CG  . PHE   B 156 ? 0.1477 0.1625 0.2772 -0.0019 -0.0084 0.0061  156 PHE   B CG  
6443 C CD1 . PHE   B 156 ? 0.1536 0.1833 0.3151 0.0101  -0.0035 0.0403  156 PHE   B CD1 
6444 C CD2 . PHE   B 156 ? 0.1617 0.1750 0.2758 0.0080  -0.0238 0.0099  156 PHE   B CD2 
6445 C CE1 . PHE   B 156 ? 0.1594 0.2016 0.3392 0.0121  -0.0019 0.0329  156 PHE   B CE1 
6446 C CE2 . PHE   B 156 ? 0.1676 0.1968 0.2956 0.0178  -0.0273 0.0125  156 PHE   B CE2 
6447 C CZ  . PHE   B 156 ? 0.1578 0.2086 0.3342 0.0137  -0.0213 0.0203  156 PHE   B CZ  
6457 N N   . ASP   B 157 ? 0.1447 0.1534 0.3516 0.0136  -0.0255 -0.0172 157 ASP   B N   
6458 C CA  . ASP   B 157 ? 0.1597 0.1589 0.3838 0.0088  -0.0272 -0.0313 157 ASP   B CA  
6459 C C   . ASP   B 157 ? 0.1571 0.1531 0.4001 0.0097  -0.0291 -0.0526 157 ASP   B C   
6460 O O   . ASP   B 157 ? 0.1385 0.1568 0.3934 0.0052  -0.0293 -0.0359 157 ASP   B O   
6461 C CB  . ASP   B 157 ? 0.1831 0.1770 0.3925 0.0045  -0.0397 -0.0111 157 ASP   B CB  
6462 C CG  . ASP   B 157 ? 0.2317 0.1940 0.4153 -0.0024 -0.0259 -0.0068 157 ASP   B CG  
6463 O OD1 . ASP   B 157 ? 0.2428 0.1870 0.4350 0.0060  -0.0217 -0.0028 157 ASP   B OD1 
6464 O OD2 . ASP   B 157 ? 0.2620 0.2153 0.4293 -0.0037 -0.0156 -0.0006 157 ASP   B OD2 
6469 N N   . LYS   B 158 ? 0.1663 0.1791 0.4143 0.0108  -0.0083 -0.0735 158 LYS   B N   
6470 C CA  . LYS   B 158 ? 0.1852 0.2017 0.4157 0.0081  0.0043  -0.0961 158 LYS   B CA  
6471 C C   . LYS   B 158 ? 0.1848 0.1938 0.4180 0.0111  -0.0043 -0.0938 158 LYS   B C   
6472 O O   . LYS   B 158 ? 0.1841 0.1903 0.4169 -0.0008 -0.0036 -0.1026 158 LYS   B O   
6473 C CB  . LYS   B 158 ? 0.2097 0.2512 0.4124 0.0076  0.0153  -0.1178 158 LYS   B CB  
6474 C CG  . LYS   B 158 ? 0.2445 0.2979 0.4122 0.0179  0.0164  -0.1290 158 LYS   B CG  
6475 C CD  . LYS   B 158 ? 0.2695 0.3474 0.4194 0.0127  0.0147  -0.1243 158 LYS   B CD  
6476 C CE  . LYS   B 158 ? 0.2934 0.3837 0.4297 0.0125  0.0156  -0.1210 158 LYS   B CE  
6477 N NZ  . LYS   B 158 ? 0.2955 0.4045 0.4277 0.0109  0.0189  -0.1192 158 LYS   B NZ  
6491 N N   . ASN   B 159 ? 0.1803 0.1854 0.4407 0.0054  -0.0225 -0.0730 159 ASN   B N   
6492 C CA  . ASN   B 159 ? 0.1936 0.1777 0.4507 0.0166  -0.0411 -0.0497 159 ASN   B CA  
6493 C C   . ASN   B 159 ? 0.1736 0.1564 0.4330 0.0090  -0.0572 -0.0427 159 ASN   B C   
6494 O O   . ASN   B 159 ? 0.1788 0.1531 0.4514 -0.0017 -0.0617 -0.0271 159 ASN   B O   
6495 C CB  . ASN   B 159 ? 0.2119 0.1952 0.4753 0.0316  -0.0474 -0.0367 159 ASN   B CB  
6496 C CG  . ASN   B 159 ? 0.2387 0.2188 0.4959 0.0322  -0.0556 -0.0452 159 ASN   B CG  
6497 O OD1 . ASN   B 159 ? 0.2567 0.2243 0.4965 0.0408  -0.0539 -0.0564 159 ASN   B OD1 
6498 N ND2 . ASN   B 159 ? 0.2403 0.2344 0.5088 0.0302  -0.0640 -0.0424 159 ASN   B ND2 
6505 N N   . LEU   B 160 ? 0.1580 0.1612 0.4073 0.0021  -0.0455 -0.0406 160 LEU   B N   
6506 C CA  . LEU   B 160 ? 0.1597 0.1599 0.3620 0.0067  -0.0377 -0.0180 160 LEU   B CA  
6507 C C   . LEU   B 160 ? 0.1551 0.1429 0.3393 0.0024  -0.0264 -0.0270 160 LEU   B C   
6508 O O   . LEU   B 160 ? 0.1457 0.1534 0.3319 -0.0009 -0.0281 -0.0148 160 LEU   B O   
6509 C CB  . LEU   B 160 ? 0.1578 0.1638 0.3466 0.0031  -0.0368 -0.0053 160 LEU   B CB  
6510 C CG  . LEU   B 160 ? 0.1597 0.1758 0.3266 0.0080  -0.0247 0.0063  160 LEU   B CG  
6511 C CD1 . LEU   B 160 ? 0.1760 0.1941 0.3411 -0.0048 -0.0030 0.0011  160 LEU   B CD1 
6512 C CD2 . LEU   B 160 ? 0.1635 0.1820 0.3128 0.0216  -0.0215 -0.0007 160 LEU   B CD2 
6524 N N   . TYR   B 161 ? 0.1579 0.1504 0.3426 -0.0107 -0.0066 -0.0372 161 TYR   B N   
6525 C CA  . TYR   B 161 ? 0.1713 0.1514 0.3266 -0.0201 0.0197  -0.0430 161 TYR   B CA  
6526 C C   . TYR   B 161 ? 0.1708 0.1498 0.3196 -0.0107 0.0252  -0.0338 161 TYR   B C   
6527 O O   . TYR   B 161 ? 0.1737 0.1574 0.3061 -0.0158 0.0097  -0.0299 161 TYR   B O   
6528 C CB  . TYR   B 161 ? 0.1830 0.1584 0.3320 -0.0281 0.0385  -0.0499 161 TYR   B CB  
6529 C CG  . TYR   B 161 ? 0.2070 0.1614 0.3279 -0.0351 0.0421  -0.0561 161 TYR   B CG  
6530 C CD1 . TYR   B 161 ? 0.2160 0.1610 0.3333 -0.0384 0.0448  -0.0548 161 TYR   B CD1 
6531 C CD2 . TYR   B 161 ? 0.2314 0.1739 0.3168 -0.0306 0.0271  -0.0589 161 TYR   B CD2 
6532 C CE1 . TYR   B 161 ? 0.2309 0.1791 0.3274 -0.0428 0.0375  -0.0582 161 TYR   B CE1 
6533 C CE2 . TYR   B 161 ? 0.2523 0.1887 0.3229 -0.0393 0.0304  -0.0563 161 TYR   B CE2 
6534 C CZ  . TYR   B 161 ? 0.2501 0.1938 0.3292 -0.0538 0.0239  -0.0478 161 TYR   B CZ  
6535 O OH  . TYR   B 161 ? 0.2805 0.2245 0.3524 -0.0568 0.0217  -0.0448 161 TYR   B OH  
6545 N N   . ASP   B 162 ? 0.1797 0.1467 0.3423 -0.0096 0.0088  -0.0470 162 ASP   B N   
6546 C CA  . ASP   B 162 ? 0.1903 0.1548 0.3421 -0.0074 -0.0006 -0.0499 162 ASP   B CA  
6547 C C   . ASP   B 162 ? 0.1807 0.1457 0.3267 -0.0150 -0.0140 -0.0363 162 ASP   B C   
6548 O O   . ASP   B 162 ? 0.1905 0.1521 0.3213 -0.0283 -0.0270 -0.0331 162 ASP   B O   
6549 C CB  . ASP   B 162 ? 0.2077 0.1763 0.3627 0.0045  -0.0084 -0.0742 162 ASP   B CB  
6550 C CG  . ASP   B 162 ? 0.2141 0.1996 0.3917 0.0112  -0.0055 -0.0910 162 ASP   B CG  
6551 O OD1 . ASP   B 162 ? 0.2170 0.2209 0.3900 0.0013  0.0123  -0.0806 162 ASP   B OD1 
6552 O OD2 . ASP   B 162 ? 0.2243 0.2257 0.4300 0.0260  -0.0048 -0.0814 162 ASP   B OD2 
6557 N N   A LYS   B 163 ? 0.1735 0.1330 0.3253 -0.0151 -0.0351 -0.0240 163 LYS   B N   
6558 N N   B LYS   B 163 ? 0.1797 0.1471 0.3266 -0.0170 -0.0276 -0.0218 163 LYS   B N   
6559 C CA  A LYS   B 163 ? 0.1864 0.1456 0.3290 -0.0251 -0.0249 -0.0071 163 LYS   B CA  
6560 C CA  B LYS   B 163 ? 0.1909 0.1634 0.3303 -0.0237 -0.0199 -0.0052 163 LYS   B CA  
6561 C C   A LYS   B 163 ? 0.1596 0.1450 0.3148 -0.0266 -0.0219 -0.0019 163 LYS   B C   
6562 C C   B LYS   B 163 ? 0.1633 0.1526 0.3148 -0.0240 -0.0188 0.0019  163 LYS   B C   
6563 O O   A LYS   B 163 ? 0.1564 0.1517 0.3257 -0.0289 -0.0297 0.0049  163 LYS   B O   
6564 O O   B LYS   B 163 ? 0.1605 0.1565 0.3241 -0.0250 -0.0239 0.0127  163 LYS   B O   
6565 C CB  A LYS   B 163 ? 0.2325 0.1800 0.3635 -0.0183 -0.0225 -0.0010 163 LYS   B CB  
6566 C CB  B LYS   B 163 ? 0.2331 0.2019 0.3624 -0.0217 -0.0179 -0.0005 163 LYS   B CB  
6567 C CG  A LYS   B 163 ? 0.2980 0.2494 0.4084 -0.0185 -0.0094 0.0027  163 LYS   B CG  
6568 C CG  B LYS   B 163 ? 0.2878 0.2596 0.4016 -0.0222 -0.0099 0.0030  163 LYS   B CG  
6569 C CD  A LYS   B 163 ? 0.3516 0.3009 0.4523 -0.0251 -0.0007 -0.0040 163 LYS   B CD  
6570 C CD  B LYS   B 163 ? 0.3325 0.3066 0.4418 -0.0271 -0.0050 -0.0002 163 LYS   B CD  
6571 C CE  A LYS   B 163 ? 0.3910 0.3371 0.4809 -0.0290 0.0106  -0.0062 163 LYS   B CE  
6572 C CE  B LYS   B 163 ? 0.3656 0.3379 0.4703 -0.0307 0.0027  -0.0013 163 LYS   B CE  
6573 N NZ  A LYS   B 163 ? 0.4156 0.3550 0.5003 -0.0308 0.0169  -0.0097 163 LYS   B NZ  
6574 N NZ  B LYS   B 163 ? 0.3848 0.3504 0.4878 -0.0322 0.0067  -0.0036 163 LYS   B NZ  
6601 N N   . LEU   B 164 ? 0.1426 0.1370 0.2954 -0.0169 -0.0179 -0.0015 164 LEU   B N   
6602 C CA  . LEU   B 164 ? 0.1493 0.1378 0.2780 -0.0139 -0.0256 -0.0021 164 LEU   B CA  
6603 C C   . LEU   B 164 ? 0.1569 0.1434 0.2744 -0.0189 -0.0339 0.0034  164 LEU   B C   
6604 O O   . LEU   B 164 ? 0.1630 0.1592 0.3135 -0.0171 -0.0311 0.0115  164 LEU   B O   
6605 C CB  . LEU   B 164 ? 0.1417 0.1364 0.2577 -0.0152 -0.0161 -0.0069 164 LEU   B CB  
6606 C CG  . LEU   B 164 ? 0.1538 0.1551 0.2544 -0.0139 -0.0114 0.0021  164 LEU   B CG  
6607 C CD1 . LEU   B 164 ? 0.1557 0.1562 0.2493 -0.0207 -0.0211 -0.0122 164 LEU   B CD1 
6608 C CD2 . LEU   B 164 ? 0.1796 0.1874 0.2766 -0.0033 0.0060  -0.0039 164 LEU   B CD2 
6621 N N   . VAL   B 165 ? 0.1939 0.1508 0.2921 -0.0235 -0.0340 -0.0023 165 VAL   B N   
6622 C CA  . VAL   B 165 ? 0.2317 0.1600 0.3032 -0.0346 -0.0589 0.0018  165 VAL   B CA  
6623 C C   . VAL   B 165 ? 0.2592 0.1731 0.3338 -0.0417 -0.0880 0.0078  165 VAL   B C   
6624 O O   . VAL   B 165 ? 0.2784 0.1849 0.3430 -0.0468 -0.0892 0.0159  165 VAL   B O   
6625 C CB  . VAL   B 165 ? 0.2564 0.1700 0.3088 -0.0124 -0.0331 -0.0212 165 VAL   B CB  
6626 C CG1 . VAL   B 165 ? 0.2747 0.1793 0.3364 -0.0108 -0.0215 -0.0201 165 VAL   B CG1 
6627 C CG2 . VAL   B 165 ? 0.2537 0.1734 0.3071 -0.0066 -0.0210 -0.0164 165 VAL   B CG2 
6637 N N   . SER   B 166 ? 0.2669 0.1602 0.3716 -0.0450 -0.1029 -0.0151 166 SER   B N   
6638 C CA  . SER   B 166 ? 0.2612 0.1597 0.4217 -0.0396 -0.0948 -0.0217 166 SER   B CA  
6639 C C   . SER   B 166 ? 0.2428 0.1721 0.4406 -0.0416 -0.0892 0.0015  166 SER   B C   
6640 O O   . SER   B 166 ? 0.2455 0.1951 0.4652 -0.0564 -0.0984 -0.0222 166 SER   B O   
6641 C CB  . SER   B 166 ? 0.2635 0.1711 0.4568 -0.0330 -0.0862 -0.0250 166 SER   B CB  
6642 O OG  . SER   B 166 ? 0.2530 0.1743 0.4769 -0.0223 -0.0859 -0.0105 166 SER   B OG  
6648 N N   . SER   B 167 ? 0.2196 0.1689 0.4199 -0.0480 -0.0930 0.0366  167 SER   B N   
6649 C CA  . SER   B 167 ? 0.2170 0.1806 0.4014 -0.0381 -0.0597 0.0427  167 SER   B CA  
6650 C C   . SER   B 167 ? 0.2090 0.1843 0.3769 -0.0557 -0.0541 0.0475  167 SER   B C   
6651 O O   . SER   B 167 ? 0.2091 0.1937 0.3724 -0.0552 -0.0477 0.0459  167 SER   B O   
6652 C CB  . SER   B 167 ? 0.2119 0.1869 0.4057 -0.0368 -0.0324 0.0481  167 SER   B CB  
6653 O OG  . SER   B 167 ? 0.2043 0.1954 0.4023 -0.0269 -0.0211 0.0432  167 SER   B OG  
6659 N N   . PHE   B 168 ? 0.2091 0.1813 0.3656 -0.0481 -0.0473 0.0585  168 PHE   B N   
6660 C CA  . PHE   B 168 ? 0.2088 0.1793 0.3294 -0.0530 -0.0500 0.0367  168 PHE   B CA  
6661 C C   . PHE   B 168 ? 0.1891 0.1661 0.2754 -0.0324 -0.0232 0.0189  168 PHE   B C   
6662 O O   . PHE   B 168 ? 0.2137 0.1601 0.2781 -0.0037 -0.0183 -0.0020 168 PHE   B O   
6663 C CB  . PHE   B 168 ? 0.2292 0.1879 0.3384 -0.0609 -0.0644 0.0511  168 PHE   B CB  
6664 C CG  . PHE   B 168 ? 0.2617 0.1718 0.3177 -0.0578 -0.0628 0.0323  168 PHE   B CG  
6665 C CD1 . PHE   B 168 ? 0.2982 0.1759 0.3292 -0.0537 -0.0663 0.0268  168 PHE   B CD1 
6666 C CD2 . PHE   B 168 ? 0.2546 0.1603 0.3212 -0.0483 -0.0636 0.0319  168 PHE   B CD2 
6667 C CE1 . PHE   B 168 ? 0.3118 0.1821 0.3274 -0.0449 -0.0553 0.0327  168 PHE   B CE1 
6668 C CE2 . PHE   B 168 ? 0.2851 0.1652 0.3213 -0.0363 -0.0642 0.0236  168 PHE   B CE2 
6669 C CZ  . PHE   B 168 ? 0.3008 0.1668 0.3209 -0.0316 -0.0668 0.0397  168 PHE   B CZ  
6679 N N   . LEU   B 169 ? 0.1974 0.1772 0.2671 -0.0126 -0.0064 0.0028  169 LEU   B N   
6680 C CA  . LEU   B 169 ? 0.2195 0.2068 0.2924 -0.0106 -0.0073 -0.0394 169 LEU   B CA  
6681 C C   . LEU   B 169 ? 0.2539 0.2340 0.3403 0.0046  -0.0098 -0.0575 169 LEU   B C   
6682 O O   . LEU   B 169 ? 0.2722 0.2539 0.3998 0.0001  -0.0143 -0.0706 169 LEU   B O   
6683 C CB  . LEU   B 169 ? 0.2360 0.2548 0.3065 -0.0171 -0.0096 -0.0127 169 LEU   B CB  
6684 C CG  . LEU   B 169 ? 0.2739 0.2944 0.3523 -0.0043 -0.0097 -0.0043 169 LEU   B CG  
6685 C CD1 . LEU   B 169 ? 0.2873 0.3127 0.3604 -0.0061 -0.0135 0.0168  169 LEU   B CD1 
6686 C CD2 . LEU   B 169 ? 0.2674 0.3018 0.3492 0.0117  0.0088  -0.0177 169 LEU   B CD2 
6687 O OXT . LEU   B 169 ? 0.2747 0.2514 0.3310 0.0331  0.0078  -0.0553 169 LEU   B OXT 
6699 C C1  T TFA   C .   ? 0.1264 0.1493 0.1279 -0.0095 0.0229  0.0117  201 TFA   A C1  
6700 C C2  T TFA   C .   ? 0.1499 0.1724 0.1724 -0.0248 0.0139  -0.0102 201 TFA   A C2  
6701 O O   T TFA   C .   ? 0.1036 0.1277 0.1179 -0.0121 0.0283  0.0212  201 TFA   A O   
6702 F F1  T TFA   C .   ? 0.1636 0.1788 0.2112 -0.0254 -0.0026 -0.0252 201 TFA   A F1  
6703 F F2  T TFA   C .   ? 0.1600 0.1787 0.1585 -0.0270 0.0196  0.0041  201 TFA   A F2  
6704 F F3  T TFA   C .   ? 0.1654 0.1902 0.2057 -0.0390 0.0336  -0.0209 201 TFA   A F3  
6705 O OXT T TFA   C .   ? 0.1220 0.1494 0.1403 0.0270  0.0202  0.0200  201 TFA   A OXT 
6706 N N2  B A1A61 D .   ? 0.2047 0.2006 0.2480 -0.0081 -0.0120 -0.0137 202 A1A61 A N2  
6707 C C3  B A1A61 D .   ? 0.2563 0.2638 0.3060 0.0208  0.0002  -0.0004 202 A1A61 A C3  
6708 C C6  B A1A61 D .   ? 0.2763 0.3087 0.3422 0.0214  0.0216  0.0093  202 A1A61 A C6  
6709 C C9  B A1A61 D .   ? 0.2388 0.2636 0.2890 0.0128  0.0072  -0.0135 202 A1A61 A C9  
6710 C C12 B A1A61 D .   ? 0.1824 0.1702 0.2103 -0.0020 -0.0092 0.0181  202 A1A61 A C12 
6711 C C14 B A1A61 D .   ? 0.1733 0.1813 0.2149 -0.0053 -0.0132 -0.0019 202 A1A61 A C14 
6712 C C1  B A1A61 D .   ? 0.2431 0.2388 0.2946 0.0152  -0.0355 0.0085  202 A1A61 A C1  
6713 C C10 B A1A61 D .   ? 0.2058 0.2120 0.2446 -0.0028 -0.0147 -0.0061 202 A1A61 A C10 
6714 C C11 B A1A61 D .   ? 0.2021 0.1953 0.2396 -0.0067 -0.0032 0.0061  202 A1A61 A C11 
6715 C C13 B A1A61 D .   ? 0.1855 0.1868 0.2230 -0.0029 -0.0145 0.0044  202 A1A61 A C13 
6716 C C15 B A1A61 D .   ? 0.1640 0.1633 0.2068 -0.0026 -0.0235 0.0123  202 A1A61 A C15 
6717 C C2  B A1A61 D .   ? 0.2450 0.2468 0.2976 0.0140  -0.0171 -0.0008 202 A1A61 A C2  
6718 C C4  B A1A61 D .   ? 0.2580 0.2810 0.3111 0.0208  0.0095  -0.0032 202 A1A61 A C4  
6719 C C5  B A1A61 D .   ? 0.2690 0.2979 0.3297 0.0204  0.0180  0.0090  202 A1A61 A C5  
6720 C C7  B A1A61 D .   ? 0.2736 0.2983 0.3269 0.0251  0.0306  0.0050  202 A1A61 A C7  
6721 C C8  B A1A61 D .   ? 0.2666 0.2923 0.3238 0.0223  0.0231  -0.0076 202 A1A61 A C8  
6722 N N1  B A1A61 D .   ? 0.2290 0.2418 0.2786 0.0038  -0.0120 -0.0106 202 A1A61 A N1  
6723 N N3  B A1A61 D .   ? 0.2006 0.1832 0.2227 -0.0060 0.0034  0.0187  202 A1A61 A N3  
6724 N N4  B A1A61 D .   ? 0.1680 0.1535 0.1994 0.0022  -0.0177 0.0225  202 A1A61 A N4  
6725 O O1  B A1A61 D .   ? 0.2389 0.2277 0.2925 0.0148  -0.0480 0.0093  202 A1A61 A O1  
6726 O O2  B A1A61 D .   ? 0.2807 0.3130 0.3505 0.0212  0.0257  0.0132  202 A1A61 A O2  
6747 O O   . HOH   E .   ? 0.3492 0.2683 0.4136 -0.0846 -0.0505 0.0419  301 HOH   A O   
6748 O O   A HOH   E .   ? 0.3263 0.6151 0.4324 -0.0893 0.0208  0.1244  302 HOH   A O   
6749 O O   . HOH   E .   ? 0.4400 0.3500 0.4269 0.0123  0.1142  0.0071  303 HOH   A O   
6750 O O   . HOH   E .   ? 0.3476 0.5598 0.2626 -0.0476 -0.0692 -0.0297 304 HOH   A O   
6751 O O   . HOH   E .   ? 0.2643 0.5126 0.4850 -0.0155 0.0681  0.2569  305 HOH   A O   
6752 O O   . HOH   E .   ? 0.6441 0.4873 0.3492 0.2027  -0.1530 0.0321  306 HOH   A O   
6753 O O   . HOH   E .   ? 0.2843 0.3600 0.2288 -0.0198 0.0566  0.0763  307 HOH   A O   
6754 O O   . HOH   E .   ? 0.6466 0.7979 0.5882 -0.0901 -0.1396 -0.0646 308 HOH   A O   
6755 O O   . HOH   E .   ? 0.3327 0.5091 0.4336 0.0313  -0.0728 0.0418  309 HOH   A O   
6756 O O   . HOH   E .   ? 0.5967 0.4162 0.6015 -0.0602 0.1601  0.1582  310 HOH   A O   
6757 O O   . HOH   E .   ? 0.2288 0.2586 0.2728 -0.0388 0.0232  0.0707  311 HOH   A O   
6758 O O   . HOH   E .   ? 0.3705 0.3734 0.3354 -0.1337 0.0014  0.1201  312 HOH   A O   
6759 O O   . HOH   E .   ? 0.2078 0.1748 0.3774 -0.0298 -0.0002 0.0011  313 HOH   A O   
6760 O O   . HOH   E .   ? 0.4526 0.5153 0.5741 -0.0646 0.1194  0.2321  314 HOH   A O   
6761 O O   . HOH   E .   ? 0.6846 0.6151 0.3828 -0.0861 -0.0724 0.1278  315 HOH   A O   
6762 O O   . HOH   E .   ? 0.4849 0.3032 0.2850 -0.1003 0.0438  0.0417  316 HOH   A O   
6763 O O   . HOH   E .   ? 0.5927 0.6827 0.5056 0.1740  -0.0566 -0.1252 317 HOH   A O   
6764 O O   A HOH   E .   ? 0.3947 0.3182 0.2536 -0.0496 -0.0090 0.0193  318 HOH   A O   
6765 O O   . HOH   E .   ? 0.5321 0.5251 0.5039 0.0384  0.2010  -0.1143 319 HOH   A O   
6766 O O   . HOH   E .   ? 0.1950 0.3103 0.3623 0.0323  -0.0178 -0.0131 320 HOH   A O   
6767 O O   . HOH   E .   ? 0.3872 0.4877 0.4821 0.1810  0.1132  0.0964  321 HOH   A O   
6768 O O   . HOH   E .   ? 0.4394 0.5378 0.5210 0.1816  0.0895  -0.1120 322 HOH   A O   
6769 O O   . HOH   E .   ? 0.6362 0.4596 0.5640 0.1053  -0.0257 -0.0205 323 HOH   A O   
6770 O O   . HOH   E .   ? 0.5543 0.3461 0.5010 0.1517  -0.0593 -0.0181 324 HOH   A O   
6771 O O   . HOH   E .   ? 0.6371 0.4960 0.7688 -0.0942 -0.0743 0.0980  325 HOH   A O   
6772 O O   . HOH   E .   ? 0.3638 0.3328 0.4074 -0.0719 -0.0163 -0.0390 326 HOH   A O   
6773 O O   . HOH   E .   ? 0.1682 0.1630 0.2504 -0.0256 -0.0003 0.0025  327 HOH   A O   
6774 O O   . HOH   E .   ? 0.1848 0.1869 0.2303 0.0137  -0.0287 0.0231  328 HOH   A O   
6775 O O   . HOH   E .   ? 0.2482 0.2276 0.3019 0.0430  0.0213  0.0405  329 HOH   A O   
6776 O O   A HOH   E .   ? 0.3296 0.4482 0.2151 -0.1176 0.0199  0.0817  330 HOH   A O   
6777 O O   . HOH   E .   ? 0.2471 0.4245 0.4103 -0.0254 -0.0621 0.1572  331 HOH   A O   
6778 O O   A HOH   E .   ? 0.1332 0.2403 0.1943 0.0479  0.0486  0.0730  332 HOH   A O   
6779 O O   . HOH   E .   ? 0.2449 0.3992 0.4048 0.0976  -0.0748 -0.0340 333 HOH   A O   
6780 O O   . HOH   E .   ? 0.2245 0.3857 0.4706 -0.0553 0.0544  -0.1343 334 HOH   A O   
6781 O O   . HOH   E .   ? 0.5861 0.2418 0.4504 -0.0212 -0.1501 0.1174  335 HOH   A O   
6782 O O   . HOH   E .   ? 0.3701 0.4153 0.4969 -0.0233 0.2205  0.0578  336 HOH   A O   
6783 O O   . HOH   E .   ? 0.3274 0.2739 0.5258 -0.0254 -0.1496 0.1169  337 HOH   A O   
6784 O O   . HOH   E .   ? 0.7589 0.4328 0.5821 -0.1055 -0.1302 0.0732  338 HOH   A O   
6785 O O   . HOH   E .   ? 0.5459 0.3030 0.3375 0.0398  -0.1019 -0.0315 339 HOH   A O   
6786 O O   . HOH   E .   ? 0.3818 0.4406 0.2479 -0.0252 0.0754  0.0187  340 HOH   A O   
6787 O O   A HOH   E .   ? 0.1784 0.2119 0.2424 0.0169  0.0460  0.0056  341 HOH   A O   
6788 O O   . HOH   E .   ? 0.6056 0.2066 0.6219 0.0893  -0.0102 -0.0227 342 HOH   A O   
6789 O O   . HOH   E .   ? 0.2646 0.2202 0.2997 -0.0372 -0.0621 0.0210  343 HOH   A O   
6790 O O   A HOH   E .   ? 0.1400 0.3210 0.2441 0.0207  0.0280  0.0929  344 HOH   A O   
6791 O O   . HOH   E .   ? 0.3611 0.4046 0.4984 -0.0946 -0.1041 -0.0942 345 HOH   A O   
6792 O O   . HOH   E .   ? 0.2588 0.3301 0.3460 -0.0373 0.0858  -0.0432 346 HOH   A O   
6793 O O   . HOH   E .   ? 0.2082 0.1762 0.1858 -0.0070 0.0155  0.0251  347 HOH   A O   
6794 O O   . HOH   E .   ? 0.6892 0.3926 0.3437 0.0501  -0.0382 0.1147  348 HOH   A O   
6795 O O   A HOH   E .   ? 0.2366 0.4113 0.4562 0.0409  0.0290  0.0488  349 HOH   A O   
6796 O O   . HOH   E .   ? 0.1728 0.1896 0.3042 0.0111  -0.0466 -0.0541 350 HOH   A O   
6797 O O   . HOH   E .   ? 0.3298 0.3695 0.4504 -0.1068 -0.1031 -0.0118 351 HOH   A O   
6798 O O   . HOH   E .   ? 0.1943 0.2705 0.2533 -0.0359 -0.0029 0.0887  352 HOH   A O   
6799 O O   . HOH   E .   ? 0.2071 0.1989 0.3871 0.0147  0.0929  -0.0042 353 HOH   A O   
6800 O O   . HOH   E .   ? 0.1532 0.1964 0.2606 0.0009  -0.0059 0.0459  354 HOH   A O   
6801 O O   . HOH   E .   ? 0.1971 0.2463 0.4060 0.0098  0.0826  -0.0759 355 HOH   A O   
6802 O O   . HOH   E .   ? 0.1400 0.1439 0.1669 -0.0069 0.0090  0.0127  356 HOH   A O   
6803 O O   . HOH   E .   ? 0.2391 0.1789 0.2641 0.0382  -0.0385 -0.0062 357 HOH   A O   
6804 O O   A HOH   E .   ? 0.1786 0.1751 0.2595 -0.0008 -0.0367 0.0307  358 HOH   A O   
6805 O O   . HOH   E .   ? 0.3382 0.4030 0.2488 -0.1252 0.0026  -0.0754 359 HOH   A O   
6806 O O   . HOH   E .   ? 0.1684 0.1448 0.2280 -0.0191 0.0160  -0.0104 360 HOH   A O   
6807 O O   . HOH   E .   ? 0.5327 0.4003 0.4788 -0.1925 -0.1218 0.1980  361 HOH   A O   
6808 O O   . HOH   E .   ? 0.3453 0.7768 0.6376 -0.0814 -0.0835 0.1513  362 HOH   A O   
6809 O O   . HOH   E .   ? 0.1568 0.2070 0.2561 0.0036  -0.0025 0.0009  363 HOH   A O   
6810 O O   . HOH   E .   ? 0.2224 0.2125 0.2239 0.0060  0.0168  0.0129  364 HOH   A O   
6811 O O   . HOH   E .   ? 0.4012 0.2086 0.2595 0.1037  0.0630  0.0295  365 HOH   A O   
6812 O O   . HOH   E .   ? 0.4411 0.2462 0.4569 -0.1362 0.0900  0.0005  366 HOH   A O   
6813 O O   . HOH   E .   ? 0.1496 0.1604 0.1764 -0.0074 -0.0187 -0.0112 367 HOH   A O   
6814 O O   . HOH   E .   ? 0.4891 0.2413 0.3778 -0.1385 0.1653  -0.0429 368 HOH   A O   
6815 O O   . HOH   E .   ? 0.3388 0.2928 0.3832 -0.0106 -0.0065 0.1209  369 HOH   A O   
6816 O O   . HOH   E .   ? 0.3090 0.4126 0.3641 -0.1495 0.0897  -0.0322 370 HOH   A O   
6817 O O   . HOH   E .   ? 0.2221 0.2475 0.2552 -0.0433 -0.0457 0.0637  371 HOH   A O   
6818 O O   . HOH   E .   ? 0.1600 0.1971 0.2023 0.0197  -0.0406 -0.0487 372 HOH   A O   
6819 O O   . HOH   E .   ? 0.2954 0.6881 0.3561 0.1111  0.0638  -0.0943 373 HOH   A O   
6820 O O   . HOH   E .   ? 0.2865 0.2431 0.3194 -0.0212 0.0181  -0.0352 374 HOH   A O   
6821 O O   . HOH   E .   ? 0.3689 0.2764 0.5120 -0.0876 0.0002  -0.0357 375 HOH   A O   
6822 O O   . HOH   E .   ? 0.1866 0.2919 0.2778 0.0297  0.0433  0.0855  376 HOH   A O   
6823 O O   . HOH   E .   ? 0.3872 0.6765 0.4806 0.0963  -0.0409 0.1430  377 HOH   A O   
6824 O O   . HOH   E .   ? 0.1859 0.2125 0.2517 -0.0297 0.0041  0.0333  378 HOH   A O   
6825 O O   . HOH   E .   ? 0.4426 0.6868 0.5655 0.1962  0.1543  0.0187  379 HOH   A O   
6826 O O   A HOH   E .   ? 0.2873 0.1676 0.1919 -0.0113 0.0085  0.0057  380 HOH   A O   
6827 O O   . HOH   E .   ? 0.1810 0.1782 0.2838 -0.0204 0.0145  0.0338  381 HOH   A O   
6828 O O   . HOH   E .   ? 0.3303 0.2881 0.2335 0.0147  0.0559  -0.0112 382 HOH   A O   
6829 O O   . HOH   E .   ? 0.1447 0.1565 0.2031 -0.0028 -0.0219 0.0080  383 HOH   A O   
6830 O O   . HOH   E .   ? 0.2561 0.3844 0.4252 -0.0293 0.0808  -0.0825 384 HOH   A O   
6831 O O   . HOH   E .   ? 0.2618 0.4657 0.4904 -0.0755 0.0533  -0.0162 385 HOH   A O   
6832 O O   . HOH   E .   ? 0.4246 0.7433 0.6019 -0.0533 -0.1354 -0.0435 386 HOH   A O   
6833 O O   . HOH   E .   ? 0.2684 0.2065 0.2083 -0.0682 0.0091  0.0269  387 HOH   A O   
6834 O O   . HOH   E .   ? 0.6359 0.5678 0.3956 -0.1258 -0.0817 0.1998  388 HOH   A O   
6835 O O   . HOH   E .   ? 0.6183 0.6601 0.4676 -0.0788 0.0997  0.0717  389 HOH   A O   
6836 O O   T HOH   E .   ? 0.1033 0.0932 0.3016 -0.0178 0.0049  0.0256  390 HOH   A O   
6837 O O   . HOH   E .   ? 0.1928 0.1959 0.2473 0.0046  -0.0290 0.0051  391 HOH   A O   
6838 O O   . HOH   E .   ? 0.3106 0.2796 0.2666 -0.0637 -0.1037 0.0245  392 HOH   A O   
6839 O O   . HOH   E .   ? 0.3122 0.5660 0.3010 0.0808  0.0883  0.2016  393 HOH   A O   
6840 O O   . HOH   E .   ? 0.4151 0.4664 0.3888 0.1919  0.0452  -0.0267 394 HOH   A O   
6841 O O   . HOH   E .   ? 0.1884 0.1959 0.3914 0.0292  0.0932  0.0893  395 HOH   A O   
6842 O O   . HOH   E .   ? 0.1921 0.2512 0.2990 -0.0205 0.0713  0.0649  396 HOH   A O   
6843 O O   . HOH   E .   ? 0.2480 0.1863 0.3522 0.0056  -0.0414 0.0068  397 HOH   A O   
6844 O O   . HOH   E .   ? 0.4056 0.7737 0.4297 -0.1146 -0.0507 0.1376  398 HOH   A O   
6845 O O   . HOH   E .   ? 0.4886 0.5160 0.2051 -0.1108 0.0830  0.0416  399 HOH   A O   
6846 O O   . HOH   E .   ? 0.3109 0.4182 0.4106 -0.0743 0.1262  -0.0099 400 HOH   A O   
6847 O O   . HOH   E .   ? 0.2016 0.2644 0.4152 -0.0064 -0.0229 0.0503  401 HOH   A O   
6848 O O   . HOH   E .   ? 0.2152 0.2327 0.2838 -0.0299 -0.0350 0.0795  402 HOH   A O   
6849 O O   . HOH   E .   ? 0.5288 0.6082 0.6852 0.1328  -0.0920 0.2154  403 HOH   A O   
6850 O O   . HOH   E .   ? 0.2546 0.2122 0.2824 -0.0609 -0.0106 0.0548  404 HOH   A O   
6851 O O   A HOH   E .   ? 0.1539 0.1715 0.2466 -0.0143 0.0054  0.0094  405 HOH   A O   
6852 O O   . HOH   E .   ? 0.6973 0.7022 0.6454 0.0880  0.0411  0.1077  406 HOH   A O   
6853 O O   A HOH   E .   ? 0.1704 0.1935 0.3368 -0.0121 0.0430  0.0024  407 HOH   A O   
6854 O O   . HOH   E .   ? 0.1664 0.1785 0.3575 0.0018  -0.0124 0.0186  408 HOH   A O   
6855 O O   . HOH   E .   ? 0.2791 0.1932 0.2704 -0.0112 0.0210  0.0258  409 HOH   A O   
6856 O O   A HOH   E .   ? 0.5017 0.3195 0.4054 0.0325  0.1021  0.0680  410 HOH   A O   
6857 O O   . HOH   E .   ? 0.2154 0.2509 0.4626 0.0132  -0.0378 -0.0542 411 HOH   A O   
6858 O O   . HOH   E .   ? 0.1803 0.1398 0.1806 -0.0196 0.0121  0.0006  412 HOH   A O   
6859 O O   . HOH   E .   ? 0.3518 0.1374 0.2333 -0.0115 -0.0540 0.0123  413 HOH   A O   
6860 O O   . HOH   E .   ? 0.5283 0.7060 0.4302 0.2167  -0.0017 0.0031  414 HOH   A O   
6861 O O   A HOH   E .   ? 0.2012 0.1842 0.2250 0.0028  -0.0310 0.0349  415 HOH   A O   
6862 O O   . HOH   E .   ? 0.2912 0.3857 0.7871 -0.0222 0.1003  -0.0168 416 HOH   A O   
6863 O O   . HOH   E .   ? 0.5799 0.4774 0.6090 0.0334  0.1593  -0.1699 417 HOH   A O   
6864 O O   . HOH   E .   ? 0.2218 0.2920 0.2931 -0.0101 -0.0565 0.0624  418 HOH   A O   
6865 O O   . HOH   E .   ? 0.4205 0.7217 0.3539 -0.1043 -0.0056 0.1488  419 HOH   A O   
6866 O O   . HOH   E .   ? 0.4629 0.5467 0.4732 0.1806  -0.0624 -0.1734 420 HOH   A O   
6867 O O   . HOH   E .   ? 0.2843 0.6648 0.2126 -0.0434 0.0539  0.0494  421 HOH   A O   
6868 O O   . HOH   E .   ? 0.2182 0.2017 0.3104 0.0222  -0.0697 0.0187  422 HOH   A O   
6869 O O   . HOH   E .   ? 0.6770 0.7058 0.6652 -0.0145 -0.0823 -0.0827 423 HOH   A O   
6870 O O   . HOH   E .   ? 0.4672 0.2422 0.5461 -0.1028 -0.2479 0.1099  424 HOH   A O   
6871 O O   . HOH   E .   ? 0.2504 0.4279 0.2950 0.1696  0.0160  0.0379  425 HOH   A O   
6872 O O   . HOH   E .   ? 0.8506 0.5367 0.4987 0.0933  0.1664  0.1506  426 HOH   A O   
6873 O O   . HOH   E .   ? 0.6920 0.3898 0.4592 0.1846  -0.0953 0.1153  427 HOH   A O   
6874 O O   . HOH   E .   ? 0.5701 0.5229 0.4026 -0.0319 -0.1605 -0.0018 428 HOH   A O   
6875 O O   A HOH   E .   ? 0.5608 0.4588 0.3354 -0.1326 -0.0177 0.1559  429 HOH   A O   
6876 O O   . HOH   E .   ? 0.2356 0.2067 0.2266 -0.0154 0.0020  -0.0085 430 HOH   A O   
6877 O O   A HOH   E .   ? 0.4107 0.6261 0.3357 0.0847  -0.0550 0.1383  431 HOH   A O   
6878 O O   . HOH   E .   ? 0.3653 0.3659 0.2857 -0.0680 -0.0494 0.0402  432 HOH   A O   
6879 O O   . HOH   E .   ? 0.6858 0.7995 0.4493 0.0385  0.3128  -0.0268 433 HOH   A O   
6880 O O   . HOH   E .   ? 0.2703 0.1802 0.3224 0.0033  0.0035  0.0058  434 HOH   A O   
6881 O O   . HOH   E .   ? 0.2065 0.1792 0.1957 0.0130  -0.0158 0.0027  435 HOH   A O   
6882 O O   . HOH   E .   ? 0.3549 0.3909 0.6729 -0.0262 0.1241  -0.2068 436 HOH   A O   
6883 O O   . HOH   E .   ? 0.1985 0.2239 0.5186 -0.0302 -0.0937 0.0590  437 HOH   A O   
6884 O O   . HOH   E .   ? 0.3889 0.2966 0.2136 -0.0895 0.0248  0.0566  438 HOH   A O   
6885 O O   . HOH   E .   ? 0.4570 0.3904 0.3477 0.2482  -0.0522 -0.0464 439 HOH   A O   
6886 O O   . HOH   E .   ? 0.6721 0.5962 0.7919 0.0320  -0.0919 0.1604  440 HOH   A O   
6887 O O   . HOH   E .   ? 0.4854 0.4692 0.5151 -0.1366 -0.0709 -0.1176 441 HOH   A O   
6888 O O   A HOH   E .   ? 0.3837 0.3931 0.4510 -0.0679 0.0031  0.0218  442 HOH   A O   
6889 O O   . HOH   E .   ? 0.6222 0.6985 0.6886 -0.1255 -0.0039 -0.1296 443 HOH   A O   
6890 O O   . HOH   E .   ? 0.2269 0.2082 0.2994 -0.0019 0.0076  0.0350  444 HOH   A O   
6891 O O   . HOH   E .   ? 0.2391 0.2950 0.2664 0.0031  -0.0063 -0.0521 445 HOH   A O   
6892 O O   . HOH   E .   ? 0.8099 0.7213 0.8006 0.0632  -0.0673 -0.0036 446 HOH   A O   
6893 O O   A HOH   E .   ? 0.6706 0.3117 0.4176 -0.1139 0.2292  -0.0873 447 HOH   A O   
6894 O O   A HOH   E .   ? 0.5000 0.2992 0.2648 0.0280  0.0820  -0.0173 448 HOH   A O   
6895 O O   . HOH   E .   ? 1.1715 1.0607 0.8931 -0.0112 -0.0835 -0.0234 449 HOH   A O   
6896 O O   . HOH   E .   ? 0.4653 0.3801 0.4624 0.0367  0.1546  0.0423  450 HOH   A O   
6897 O O   B HOH   E .   ? 0.5135 0.5012 0.2815 0.1131  -0.1211 0.0356  451 HOH   A O   
6898 O O   . HOH   E .   ? 0.4380 0.3223 0.4494 -0.0197 0.0074  0.0291  452 HOH   A O   
6899 O O   . HOH   E .   ? 0.5177 0.4809 0.5202 0.2666  -0.0652 0.0934  453 HOH   A O   
6900 O O   . HOH   E .   ? 0.8199 0.8206 0.5204 0.0606  -0.1112 -0.0291 454 HOH   A O   
6901 O O   . HOH   E .   ? 0.3825 0.2670 0.4725 -0.0278 -0.0453 -0.1073 455 HOH   A O   
6902 O O   . HOH   E .   ? 0.3831 0.5924 0.5467 0.0705  0.0259  0.0649  456 HOH   A O   
6903 O O   . HOH   E .   ? 0.3836 0.5335 0.5124 -0.1634 0.0708  -0.1240 457 HOH   A O   
6904 O O   . HOH   E .   ? 0.3441 0.5149 0.5095 0.0589  -0.0618 0.0945  458 HOH   A O   
6905 O O   . HOH   E .   ? 0.6252 0.5345 0.6225 -0.1230 -0.0864 -0.0649 459 HOH   A O   
6906 O O   . HOH   E .   ? 0.3211 0.3047 0.3732 -0.1173 0.0848  -0.0551 460 HOH   A O   
6907 O O   . HOH   E .   ? 0.2597 0.4571 0.5421 0.0575  -0.0177 -0.1793 461 HOH   A O   
6908 O O   . HOH   E .   ? 0.7153 0.4544 0.4549 0.0155  0.1716  0.0164  462 HOH   A O   
6909 O O   . HOH   E .   ? 0.6476 0.4660 0.5163 -0.0265 0.1024  0.0162  463 HOH   A O   
6910 O O   A HOH   E .   ? 0.2973 0.2612 0.4768 0.0877  -0.1867 -0.0840 464 HOH   A O   
6911 O O   . HOH   E .   ? 0.3807 0.4895 0.4904 -0.0880 0.0103  -0.0104 465 HOH   A O   
6912 O O   . HOH   E .   ? 0.4376 0.6216 0.3901 -0.0568 -0.0927 0.1805  466 HOH   A O   
6913 O O   . HOH   E .   ? 0.7243 0.3876 0.7173 0.1351  0.0312  0.2249  467 HOH   A O   
6914 O O   . HOH   E .   ? 0.7218 0.6006 0.6728 0.0946  0.1726  0.2434  468 HOH   A O   
6915 O O   A HOH   E .   ? 0.3565 0.4212 0.3156 0.0208  -0.0123 0.0456  469 HOH   A O   
6916 O O   . HOH   E .   ? 0.2729 0.1900 0.2799 0.0237  -0.0900 -0.0424 470 HOH   A O   
6917 O O   . HOH   E .   ? 0.5102 0.6923 0.5664 0.1171  0.0180  -0.0221 471 HOH   A O   
6918 O O   . HOH   E .   ? 0.4256 0.5745 0.3174 0.0132  -0.0376 0.0107  472 HOH   A O   
6919 O O   . HOH   E .   ? 0.3822 0.2975 0.4468 0.0579  0.1146  0.0433  473 HOH   A O   
6920 O O   . HOH   E .   ? 0.5423 0.5696 0.3094 -0.0331 0.0035  -0.0164 474 HOH   A O   
6921 O O   . HOH   E .   ? 0.4690 0.4492 0.6855 -0.1777 -0.0441 -0.0262 475 HOH   A O   
6922 O O   . HOH   E .   ? 0.3720 0.6987 0.4472 0.2322  0.1449  0.2421  476 HOH   A O   
6923 O O   . HOH   E .   ? 0.6739 0.6429 0.7311 -0.1476 0.0895  -0.0964 477 HOH   A O   
6924 O O   . HOH   E .   ? 0.2559 0.2664 0.2901 0.0332  0.0008  -0.0120 478 HOH   A O   
6925 O O   B HOH   E .   ? 0.4338 0.5223 0.3647 -0.0532 -0.0950 0.0680  479 HOH   A O   
6926 O O   . HOH   E .   ? 0.6406 0.7015 0.6880 -0.1321 -0.1334 -0.0659 480 HOH   A O   
6927 O O   . HOH   E .   ? 0.5944 0.4699 0.5097 -0.1546 0.1979  0.1449  481 HOH   A O   
6928 O O   . HOH   E .   ? 0.5411 0.5136 0.5022 -0.0537 -0.0060 -0.1273 482 HOH   A O   
6929 O O   . HOH   E .   ? 0.5559 0.6782 0.6993 0.0154  0.1972  -0.1244 483 HOH   A O   
6930 O O   . HOH   E .   ? 0.8009 0.3963 0.3625 0.0154  -0.1280 0.0325  484 HOH   A O   
6931 O O   . HOH   E .   ? 0.6093 0.2991 0.3541 -0.0577 -0.1341 0.0432  485 HOH   A O   
6932 O O   . HOH   E .   ? 0.3580 0.4633 0.3256 -0.0014 -0.0519 -0.0600 486 HOH   A O   
6933 O O   . HOH   E .   ? 0.7295 0.6577 0.4756 -0.0642 0.1641  0.1458  487 HOH   A O   
6934 O O   . HOH   E .   ? 0.2810 0.2408 0.7792 -0.0080 -0.1458 0.0224  488 HOH   A O   
6935 O O   . HOH   E .   ? 0.5192 0.3899 0.2838 -0.1294 0.1607  -0.0846 489 HOH   A O   
6936 O O   . HOH   E .   ? 0.6645 0.6616 0.5970 0.1485  -0.1508 -0.0590 490 HOH   A O   
6937 O O   . HOH   E .   ? 0.4415 0.4386 0.4896 -0.0415 0.0230  0.1243  491 HOH   A O   
6938 O O   . HOH   E .   ? 0.5711 0.5275 0.5383 0.0646  -0.0410 0.0197  492 HOH   A O   
6939 O O   . HOH   E .   ? 0.4584 0.3087 0.5869 -0.0020 0.2602  0.0535  493 HOH   A O   
6940 O O   . HOH   E .   ? 0.6987 0.2417 0.4462 -0.1029 0.0316  0.0537  494 HOH   A O   
6941 O O   . HOH   E .   ? 0.3341 0.2290 0.6697 0.0136  0.0630  0.0779  495 HOH   A O   
6942 O O   . HOH   E .   ? 0.2728 0.3054 0.5599 -0.0253 0.0606  -0.0299 496 HOH   A O   
6943 O O   . HOH   E .   ? 0.4062 0.8652 0.6360 -0.0909 -0.0669 0.2453  497 HOH   A O   
6944 O O   . HOH   E .   ? 0.5107 0.2588 0.4612 -0.1375 0.0308  0.0178  498 HOH   A O   
6945 O O   . HOH   E .   ? 0.2900 0.4286 0.3776 0.1107  -0.0020 0.1258  499 HOH   A O   
6946 O O   . HOH   E .   ? 0.2698 0.4018 0.5671 -0.0008 -0.1064 0.0267  500 HOH   A O   
6947 O O   . HOH   E .   ? 0.4720 0.2651 0.3150 0.1159  -0.1403 -0.0540 501 HOH   A O   
6948 O O   . HOH   E .   ? 0.5475 0.7759 0.5461 0.1291  0.0102  0.0466  502 HOH   A O   
6949 O O   . HOH   E .   ? 0.3151 0.7522 0.4958 0.0872  0.0953  0.0016  503 HOH   A O   
6950 O O   . HOH   E .   ? 0.3057 0.2539 0.5025 0.0274  0.0622  0.0714  504 HOH   A O   
6951 O O   . HOH   E .   ? 0.5821 0.7551 0.5309 0.3361  -0.0399 0.1435  505 HOH   A O   
6952 O O   A HOH   E .   ? 0.4571 0.4885 0.3309 -0.0464 -0.0779 -0.1069 506 HOH   A O   
6953 O O   T HOH   E .   ? 0.1126 0.1570 0.2335 -0.0416 -0.0366 0.0681  507 HOH   A O   
6954 O O   . HOH   E .   ? 0.3533 0.7646 0.4679 0.0736  0.0306  -0.1206 508 HOH   A O   
6955 O O   . HOH   E .   ? 0.5322 0.6953 0.5742 -0.0605 -0.0805 0.1046  509 HOH   A O   
6956 O O   . HOH   E .   ? 0.5876 0.5025 0.4938 0.0004  0.0975  0.1174  510 HOH   A O   
6957 O O   . HOH   E .   ? 0.3075 0.4974 0.6097 -0.0394 -0.0681 0.3054  511 HOH   A O   
6958 O O   . HOH   F .   ? 0.2396 0.2615 0.3266 0.0029  0.0863  0.0202  201 HOH   B O   
6959 O O   . HOH   F .   ? 0.3505 0.3114 0.6026 -0.0286 -0.0317 0.0209  202 HOH   B O   
6960 O O   . HOH   F .   ? 0.5068 0.3373 0.3769 -0.0552 0.0311  -0.1376 203 HOH   B O   
6961 O O   . HOH   F .   ? 0.7619 0.3668 0.4526 0.0780  0.1036  0.0090  204 HOH   B O   
6962 O O   . HOH   F .   ? 0.3457 0.2184 0.5959 0.0127  0.2252  0.0725  205 HOH   B O   
6963 O O   . HOH   F .   ? 0.5087 0.3847 0.6832 0.0416  -0.1234 0.2467  206 HOH   B O   
6964 O O   . HOH   F .   ? 0.2794 0.5299 0.5566 -0.0360 0.1454  -0.2268 207 HOH   B O   
6965 O O   . HOH   F .   ? 0.3738 0.6235 0.3331 0.0300  0.0188  0.1961  208 HOH   B O   
6966 O O   . HOH   F .   ? 0.3916 0.4107 0.3495 0.0099  -0.0867 0.0535  209 HOH   B O   
6967 O O   . HOH   F .   ? 0.1604 0.2034 0.3080 -0.0168 0.0011  0.0018  210 HOH   B O   
6968 O O   . HOH   F .   ? 0.6201 0.5722 0.6759 0.1928  0.1135  -0.0581 211 HOH   B O   
6969 O O   . HOH   F .   ? 0.4031 0.5121 0.5145 0.2421  0.0864  0.0248  212 HOH   B O   
6970 O O   . HOH   F .   ? 0.3518 0.2341 0.5610 -0.0146 0.2137  -0.0073 213 HOH   B O   
6971 O O   . HOH   F .   ? 0.1941 0.2219 0.3501 -0.0119 0.0162  -0.0180 214 HOH   B O   
6972 O O   . HOH   F .   ? 0.3118 0.2683 0.7251 0.0686  -0.1045 0.0733  215 HOH   B O   
6973 O O   . HOH   F .   ? 0.4462 0.5455 0.3872 0.2336  -0.0665 0.0008  216 HOH   B O   
6974 O O   . HOH   F .   ? 0.3441 0.3457 0.4416 0.0147  -0.1093 0.0483  217 HOH   B O   
6975 O O   . HOH   F .   ? 0.4934 0.6038 0.4134 0.2973  -0.0957 0.0045  218 HOH   B O   
6976 O O   . HOH   F .   ? 0.4480 0.3804 0.4487 -0.1769 0.0121  0.0373  219 HOH   B O   
6977 O O   . HOH   F .   ? 0.3986 0.5616 0.6979 -0.0518 -0.0809 -0.0957 220 HOH   B O   
6978 O O   . HOH   F .   ? 0.2509 0.2299 0.4180 -0.0450 -0.0075 -0.0508 221 HOH   B O   
6979 O O   . HOH   F .   ? 0.5397 0.2090 0.3204 0.0063  -0.0944 0.0118  222 HOH   B O   
6980 O O   . HOH   F .   ? 0.4748 0.4422 0.3854 0.0320  0.0634  -0.1639 223 HOH   B O   
6981 O O   . HOH   F .   ? 0.4436 0.6040 0.3887 0.1754  0.0405  0.0560  224 HOH   B O   
6982 O O   . HOH   F .   ? 0.1880 0.2011 0.3294 -0.0139 0.0133  -0.0066 225 HOH   B O   
6983 O O   . HOH   F .   ? 0.2341 0.1820 0.2694 -0.0280 0.0703  0.0016  226 HOH   B O   
6984 O O   . HOH   F .   ? 0.3754 0.2857 0.4746 0.0896  -0.1898 -0.1488 227 HOH   B O   
6985 O O   . HOH   F .   ? 0.2327 0.2487 0.3288 -0.0688 0.0100  -0.0147 228 HOH   B O   
6986 O O   . HOH   F .   ? 0.2897 0.4167 0.6873 -0.0169 0.1082  0.0192  229 HOH   B O   
6987 O O   . HOH   F .   ? 0.5456 0.2794 0.3284 -0.1007 0.0450  -0.0618 230 HOH   B O   
6988 O O   . HOH   F .   ? 0.2155 0.1465 0.3575 0.0042  -0.0595 -0.0237 231 HOH   B O   
6989 O O   . HOH   F .   ? 0.3753 0.1817 0.2108 0.0158  -0.0777 -0.0171 232 HOH   B O   
6990 O O   . HOH   F .   ? 0.1630 0.1501 0.1646 -0.0099 -0.0031 -0.0089 233 HOH   B O   
6991 O O   . HOH   F .   ? 0.5285 0.5550 0.6354 0.0785  -0.1591 -0.1082 234 HOH   B O   
6992 O O   . HOH   F .   ? 0.3974 0.2945 0.4194 0.1020  -0.0492 -0.0530 235 HOH   B O   
6993 O O   . HOH   F .   ? 0.5676 0.3422 0.2807 -0.0198 0.0777  -0.0213 236 HOH   B O   
6994 O O   . HOH   F .   ? 0.2306 0.4022 0.2584 -0.0598 -0.0367 0.0541  237 HOH   B O   
6995 O O   . HOH   F .   ? 0.2720 0.2637 0.3295 0.0352  0.0128  -0.0938 238 HOH   B O   
6996 O O   . HOH   F .   ? 0.3170 0.3031 0.2135 0.0210  0.0164  0.0387  239 HOH   B O   
6997 O O   . HOH   F .   ? 0.5855 0.3309 0.3910 -0.2418 -0.0294 0.0207  240 HOH   B O   
6998 O O   . HOH   F .   ? 0.2443 0.3846 0.3717 -0.0434 -0.1085 -0.0654 241 HOH   B O   
6999 O O   . HOH   F .   ? 0.1755 0.1567 0.2607 -0.0072 0.0022  -0.0147 242 HOH   B O   
7000 O O   . HOH   F .   ? 0.6513 0.6354 0.3579 0.0504  0.0497  0.0315  243 HOH   B O   
7001 O O   . HOH   F .   ? 0.2434 0.2083 0.2880 0.0756  -0.0816 -0.0661 244 HOH   B O   
7002 O O   . HOH   F .   ? 0.2949 0.3543 0.3074 -0.0768 0.0370  -0.0548 245 HOH   B O   
7003 O O   . HOH   F .   ? 0.3357 0.3766 0.2465 0.0205  0.0695  0.0165  246 HOH   B O   
7004 O O   . HOH   F .   ? 0.2598 0.4389 0.5515 0.1272  -0.0573 -0.1289 247 HOH   B O   
7005 O O   . HOH   F .   ? 0.1586 0.1414 0.1755 0.0002  -0.0111 0.0042  248 HOH   B O   
7006 O O   . HOH   F .   ? 0.4357 0.2834 0.3447 -0.1225 -0.0574 0.0266  249 HOH   B O   
7007 O O   . HOH   F .   ? 0.2886 0.2374 0.3049 0.0744  0.0730  -0.0026 250 HOH   B O   
7008 O O   . HOH   F .   ? 0.3271 0.1785 0.6594 -0.0082 -0.1103 -0.0311 251 HOH   B O   
7009 O O   . HOH   F .   ? 0.6774 0.3840 0.2797 -0.0809 -0.0803 -0.1187 252 HOH   B O   
7010 O O   . HOH   F .   ? 0.2155 0.1512 0.2220 -0.0248 -0.0410 0.0195  253 HOH   B O   
7011 O O   . HOH   F .   ? 0.2211 0.2084 0.2258 -0.0405 -0.0524 0.0054  254 HOH   B O   
7012 O O   . HOH   F .   ? 0.2339 0.1974 0.4072 0.0092  -0.0425 -0.0393 255 HOH   B O   
7013 O O   . HOH   F .   ? 0.2474 0.3252 0.2284 -0.0535 0.0258  0.0351  256 HOH   B O   
7014 O O   . HOH   F .   ? 0.1708 0.1822 0.3392 -0.0274 -0.0263 0.0132  257 HOH   B O   
7015 O O   . HOH   F .   ? 0.3510 0.4610 0.3104 -0.0194 -0.1026 0.0684  258 HOH   B O   
7016 O O   . HOH   F .   ? 0.2516 0.2226 0.2403 0.0364  -0.0061 -0.0055 259 HOH   B O   
7017 O O   . HOH   F .   ? 0.3295 0.2763 0.2991 -0.0428 0.0203  -0.0518 260 HOH   B O   
7018 O O   . HOH   F .   ? 0.7695 0.4552 0.5430 0.1111  -0.0583 -0.1321 261 HOH   B O   
7019 O O   . HOH   F .   ? 0.2793 0.2276 0.2107 0.0106  -0.0199 -0.0000 262 HOH   B O   
7020 O O   . HOH   F .   ? 0.1523 0.1754 0.2277 -0.0138 0.0093  0.0107  263 HOH   B O   
7021 O O   . HOH   F .   ? 0.2657 0.2006 0.3171 -0.0620 0.0011  -0.0130 264 HOH   B O   
7022 O O   . HOH   F .   ? 0.2120 0.1600 0.2298 -0.0243 -0.0125 0.0238  265 HOH   B O   
7023 O O   . HOH   F .   ? 0.4317 0.3131 0.4135 -0.0269 -0.1268 -0.0126 266 HOH   B O   
7024 O O   . HOH   F .   ? 0.2202 0.4701 0.4665 -0.0308 -0.0159 -0.1085 267 HOH   B O   
7025 O O   . HOH   F .   ? 0.2664 0.3790 0.3930 0.0341  0.1269  0.0668  268 HOH   B O   
7026 O O   . HOH   F .   ? 0.2476 0.3196 0.3323 -0.0346 0.0341  -0.1027 269 HOH   B O   
7027 O O   . HOH   F .   ? 0.1990 0.1770 0.1825 -0.0478 -0.0537 0.0130  270 HOH   B O   
7028 O O   . HOH   F .   ? 0.5015 0.3702 0.3024 0.0313  -0.0250 -0.0852 271 HOH   B O   
7029 O O   . HOH   F .   ? 0.2729 0.2846 0.2508 -0.0511 -0.0967 0.0242  272 HOH   B O   
7030 O O   . HOH   F .   ? 0.2310 0.2230 0.5442 -0.0549 0.0133  0.1177  273 HOH   B O   
7031 O O   . HOH   F .   ? 0.2411 0.2513 0.2706 -0.0267 -0.0804 -0.0564 274 HOH   B O   
7032 O O   . HOH   F .   ? 0.2641 0.4654 0.2764 -0.0678 -0.0468 -0.0581 275 HOH   B O   
7033 O O   . HOH   F .   ? 0.2481 0.3716 0.2241 0.1159  -0.0413 -0.0370 276 HOH   B O   
7034 O O   . HOH   F .   ? 0.2992 0.2140 0.5613 0.0152  0.0766  0.0493  277 HOH   B O   
7035 O O   . HOH   F .   ? 0.2354 0.4434 0.6663 -0.0170 0.0809  -0.0733 278 HOH   B O   
7036 O O   . HOH   F .   ? 0.1757 0.1637 0.3766 -0.0138 0.0068  0.0015  279 HOH   B O   
7037 O O   . HOH   F .   ? 0.2228 0.6358 0.4737 -0.1109 -0.0242 -0.0428 280 HOH   B O   
7038 O O   . HOH   F .   ? 0.3101 0.2816 0.5390 -0.0409 -0.0538 0.1306  281 HOH   B O   
7039 O O   . HOH   F .   ? 0.1891 0.1565 0.3856 -0.0068 -0.0395 -0.0111 282 HOH   B O   
7040 O O   . HOH   F .   ? 0.5859 0.4074 0.3312 0.2679  0.1582  0.1150  283 HOH   B O   
7041 O O   . HOH   F .   ? 0.1765 0.1610 0.1983 0.0051  0.0101  0.0019  284 HOH   B O   
7042 O O   . HOH   F .   ? 0.2966 0.2761 0.4474 -0.0310 -0.0149 -0.0580 285 HOH   B O   
7043 O O   . HOH   F .   ? 0.3472 0.2173 0.4292 -0.0861 -0.1863 0.0827  286 HOH   B O   
7044 O O   . HOH   F .   ? 0.3526 0.3577 0.4852 0.1085  -0.0733 -0.1046 287 HOH   B O   
7045 O O   . HOH   F .   ? 0.2571 0.2778 0.3036 0.0130  -0.0765 0.0292  288 HOH   B O   
7046 O O   . HOH   F .   ? 0.1822 0.2250 0.2875 0.0199  -0.0026 0.0112  289 HOH   B O   
7047 O O   . HOH   F .   ? 0.4476 0.5149 0.4996 0.0119  -0.1435 0.0329  290 HOH   B O   
7048 O O   . HOH   F .   ? 0.3493 0.2816 0.2872 -0.0396 0.0256  -0.1230 291 HOH   B O   
7049 O O   . HOH   F .   ? 0.1675 0.2140 0.1688 -0.0074 -0.0268 0.0103  292 HOH   B O   
7050 O O   . HOH   F .   ? 0.2751 0.5125 0.4787 -0.0981 -0.1252 0.0620  293 HOH   B O   
7051 O O   . HOH   F .   ? 0.1989 0.3005 0.6394 0.0494  -0.0305 -0.1325 294 HOH   B O   
7052 O O   . HOH   F .   ? 0.3969 0.6263 0.2082 -0.0539 -0.0819 0.0836  295 HOH   B O   
7053 O O   . HOH   F .   ? 0.4414 0.2551 0.2546 0.0379  -0.1227 -0.0179 296 HOH   B O   
7054 O O   . HOH   F .   ? 0.2530 0.7294 0.2508 0.0529  -0.0232 -0.0646 297 HOH   B O   
7055 O O   . HOH   F .   ? 0.1799 0.3594 0.5382 0.0436  -0.0084 -0.1434 298 HOH   B O   
7056 O O   . HOH   F .   ? 0.3461 0.2768 0.2310 -0.1295 -0.0056 0.0094  299 HOH   B O   
7057 O O   . HOH   F .   ? 0.3393 0.2729 0.2381 0.0447  -0.0412 0.0383  300 HOH   B O   
7058 O O   . HOH   F .   ? 0.3302 0.3953 0.4485 -0.1449 0.1411  -0.0829 301 HOH   B O   
7059 O O   . HOH   F .   ? 0.2178 0.1754 0.2836 -0.0388 -0.0381 -0.0085 302 HOH   B O   
7060 O O   . HOH   F .   ? 0.4029 0.5407 0.2248 0.0226  0.0611  0.0809  303 HOH   B O   
7061 O O   . HOH   F .   ? 0.2009 0.1745 0.2485 0.0089  0.0071  0.0141  304 HOH   B O   
7062 O O   . HOH   F .   ? 0.3365 0.8181 0.6619 0.2226  -0.0400 -0.1607 305 HOH   B O   
7063 O O   . HOH   F .   ? 0.3868 0.1933 0.3460 0.0688  0.1428  0.0400  306 HOH   B O   
7064 O O   . HOH   F .   ? 0.2369 0.3479 0.5135 -0.0481 -0.0312 -0.0204 307 HOH   B O   
7065 O O   . HOH   F .   ? 0.6395 0.6118 0.4292 0.3027  -0.0018 0.0141  308 HOH   B O   
7066 O O   . HOH   F .   ? 0.4610 0.3710 0.4614 -0.0277 0.0762  0.1281  309 HOH   B O   
7067 O O   . HOH   F .   ? 0.2463 0.1525 0.3065 -0.0167 -0.0258 0.0248  310 HOH   B O   
7068 O O   . HOH   F .   ? 0.2191 0.1643 0.3645 0.0370  -0.1094 -0.0074 311 HOH   B O   
7069 O O   . HOH   F .   ? 0.2868 0.2932 0.3852 -0.0373 0.1121  -0.0985 312 HOH   B O   
7070 O O   . HOH   F .   ? 0.5082 0.4804 0.2869 0.0589  -0.0524 -0.0834 313 HOH   B O   
7071 O O   . HOH   F .   ? 0.2318 0.2024 0.2190 0.0029  0.0218  0.0202  314 HOH   B O   
7072 O O   . HOH   F .   ? 0.1724 0.1589 0.3500 0.0054  -0.0061 -0.0057 315 HOH   B O   
7073 O O   . HOH   F .   ? 0.3705 0.6664 0.4057 0.1291  0.0087  0.1109  316 HOH   B O   
7074 O O   . HOH   F .   ? 0.5284 0.3035 0.5663 0.1323  0.2801  0.1619  317 HOH   B O   
7075 O O   . HOH   F .   ? 0.4500 0.2291 0.2972 0.1568  0.1043  0.0403  318 HOH   B O   
7076 O O   . HOH   F .   ? 0.4960 0.2735 0.3431 -0.0004 -0.0020 0.0996  319 HOH   B O   
7077 O O   . HOH   F .   ? 0.6253 0.6150 0.5569 -0.1235 -0.0622 0.1868  320 HOH   B O   
7078 O O   . HOH   F .   ? 0.1595 0.1851 0.3217 -0.0175 -0.0105 0.0141  321 HOH   B O   
7079 O O   . HOH   F .   ? 0.1798 0.2977 0.2510 -0.0137 -0.0274 0.0690  322 HOH   B O   
7080 O O   . HOH   F .   ? 0.1727 0.1748 0.3156 -0.0195 -0.0185 -0.0112 323 HOH   B O   
7081 O O   . HOH   F .   ? 0.3404 0.2573 0.2746 0.0420  -0.0043 0.0442  324 HOH   B O   
7082 O O   . HOH   F .   ? 0.4671 0.4363 0.5680 0.0593  0.0060  0.0226  325 HOH   B O   
7083 O O   . HOH   F .   ? 0.6520 0.4334 0.6067 0.1444  0.2116  0.0149  326 HOH   B O   
7084 O O   . HOH   F .   ? 0.6388 0.4634 0.7326 0.1465  -0.0919 0.1711  327 HOH   B O   
7085 O O   . HOH   F .   ? 0.8014 0.2113 0.3655 0.0160  -0.0995 0.0154  328 HOH   B O   
7086 O O   . HOH   F .   ? 0.3716 0.4184 0.7276 -0.0021 -0.0842 0.1928  329 HOH   B O   
7087 O O   . HOH   F .   ? 0.2044 0.2013 0.2991 0.0347  0.0540  0.0172  330 HOH   B O   
7088 O O   . HOH   F .   ? 0.2794 0.3869 0.5825 -0.0733 -0.1731 0.1649  331 HOH   B O   
7089 O O   . HOH   F .   ? 0.5651 0.4006 0.4300 0.0563  0.1270  0.1797  332 HOH   B O   
7090 O O   . HOH   F .   ? 0.2833 0.2099 0.5843 -0.0171 -0.0038 0.0754  333 HOH   B O   
7091 O O   . HOH   F .   ? 0.1868 0.2911 0.3182 0.0252  -0.0154 -0.0562 334 HOH   B O   
7092 O O   . HOH   F .   ? 0.4887 0.3371 0.2242 0.1555  -0.1207 -0.0360 335 HOH   B O   
7093 O O   . HOH   F .   ? 0.4078 0.7500 0.4263 -0.0642 -0.0623 0.1739  336 HOH   B O   
7094 O O   . HOH   F .   ? 0.5396 0.3630 0.4490 0.0279  0.0680  -0.1198 337 HOH   B O   
7095 O O   . HOH   F .   ? 0.6093 0.4710 0.6544 -0.0665 -0.0893 -0.1139 338 HOH   B O   
7096 O O   . HOH   F .   ? 0.5096 0.4867 0.3402 -0.0473 -0.1157 -0.0283 339 HOH   B O   
7097 O O   . HOH   F .   ? 0.1882 0.1593 0.2482 0.0030  -0.0256 0.0084  340 HOH   B O   
7098 O O   . HOH   F .   ? 0.2699 0.5445 0.7595 -0.0523 -0.0222 0.0291  341 HOH   B O   
7099 O O   . HOH   F .   ? 0.3893 0.6280 0.4135 -0.1036 -0.1265 -0.0478 342 HOH   B O   
7100 O O   . HOH   F .   ? 0.4171 0.3063 0.3314 0.0709  -0.1087 -0.0854 343 HOH   B O   
7101 O O   . HOH   F .   ? 0.5229 0.5999 0.5491 -0.1233 0.0760  0.1102  344 HOH   B O   
7102 O O   . HOH   F .   ? 0.2234 0.2168 0.3257 -0.0140 0.0794  -0.0073 345 HOH   B O   
7103 O O   . HOH   F .   ? 0.7444 0.4972 0.3212 0.0404  -0.0227 0.1126  346 HOH   B O   
7104 O O   . HOH   F .   ? 0.3165 0.2014 0.4240 0.0378  -0.1224 -0.0560 347 HOH   B O   
7105 O O   . HOH   F .   ? 0.2882 0.2353 0.4968 -0.0231 -0.0600 -0.0682 348 HOH   B O   
7106 O O   . HOH   F .   ? 0.3942 0.5518 0.6157 0.0210  -0.0754 0.1114  349 HOH   B O   
7107 O O   . HOH   F .   ? 0.2324 0.6056 0.3684 0.1460  -0.0653 -0.1228 350 HOH   B O   
7108 O O   . HOH   F .   ? 0.3544 0.4588 0.4808 -0.1424 0.0338  -0.0794 351 HOH   B O   
7109 O O   . HOH   F .   ? 0.5003 0.3239 0.5470 -0.0927 0.1050  0.0842  352 HOH   B O   
7110 O O   . HOH   F .   ? 0.4951 0.6958 0.7516 0.0519  0.0842  -0.0690 353 HOH   B O   
7111 O O   . HOH   F .   ? 0.2527 0.4273 0.4872 -0.0123 0.0249  0.0050  354 HOH   B O   
7112 O O   . HOH   F .   ? 0.3832 0.2373 0.3417 -0.0777 0.0300  -0.0912 355 HOH   B O   
7113 O O   . HOH   F .   ? 0.5775 0.3910 0.3880 0.0348  0.1325  -0.0706 356 HOH   B O   
7114 O O   . HOH   F .   ? 0.4472 0.2601 0.4172 -0.0934 -0.0168 -0.0450 357 HOH   B O   
7115 O O   . HOH   F .   ? 0.3477 0.3145 0.4103 -0.0378 -0.0917 0.0056  358 HOH   B O   
7116 O O   . HOH   F .   ? 0.4920 0.5431 0.5375 0.2023  -0.1286 0.1198  359 HOH   B O   
7117 O O   . HOH   F .   ? 0.5493 0.3636 0.5175 0.0075  -0.1677 -0.0569 360 HOH   B O   
7118 O O   . HOH   F .   ? 0.5313 0.4023 0.6507 0.0473  0.1515  0.1855  361 HOH   B O   
7119 O O   . HOH   F .   ? 0.4755 0.7375 0.2736 0.2347  0.0021  0.0249  362 HOH   B O   
7120 O O   . HOH   F .   ? 0.2375 0.4182 0.6864 -0.0974 -0.0527 -0.0925 363 HOH   B O   
7121 O O   . HOH   F .   ? 0.6255 0.2298 0.3186 -0.0207 -0.0286 0.0456  364 HOH   B O   
7122 O O   . HOH   F .   ? 0.5153 0.3142 0.5185 -0.1306 -0.0425 0.0203  365 HOH   B O   
7123 O O   . HOH   F .   ? 0.5762 0.5987 0.5193 -0.0686 -0.0620 -0.1211 366 HOH   B O   
7124 O O   . HOH   F .   ? 0.6792 0.4557 0.4650 0.1639  0.0685  0.0831  367 HOH   B O   
7125 O O   . HOH   F .   ? 0.4157 0.4791 0.6597 0.1810  -0.1441 0.0224  368 HOH   B O   
7126 O O   . HOH   F .   ? 0.4762 0.6168 0.4289 0.2986  0.1333  0.1831  369 HOH   B O   
7127 O O   . HOH   F .   ? 0.5185 0.6423 0.3300 0.2343  -0.1009 0.0636  370 HOH   B O   
7128 O O   . HOH   F .   ? 0.6220 0.3701 0.2989 -0.1331 -0.1010 -0.0179 371 HOH   B O   
7129 O O   . HOH   F .   ? 0.4483 0.5496 0.5033 -0.0804 -0.0473 -0.0011 372 HOH   B O   
7130 O O   . HOH   F .   ? 0.9067 0.7738 0.5360 0.2156  -0.1422 0.0104  373 HOH   B O   
7131 O O   . HOH   F .   ? 0.4848 0.6858 0.6249 0.1435  -0.0044 0.2536  374 HOH   B O   
7132 O O   . HOH   F .   ? 0.3245 0.3797 0.3000 0.0603  -0.0618 -0.0409 375 HOH   B O   
7133 O O   . HOH   F .   ? 0.3134 0.5366 0.2374 -0.0099 0.0229  0.0022  376 HOH   B O   
7134 O O   . HOH   F .   ? 0.2349 0.4320 0.4263 0.0280  -0.0614 -0.0242 377 HOH   B O   
7135 O O   . HOH   F .   ? 0.4160 0.5261 0.6396 0.1410  -0.0623 0.0265  378 HOH   B O   
7136 O O   . HOH   F .   ? 0.4921 0.6672 0.3590 -0.1693 -0.0349 -0.1909 379 HOH   B O   
7137 O O   . HOH   F .   ? 0.7447 0.3883 0.5490 -0.0902 -0.1095 0.0768  380 HOH   B O   
7138 O O   . HOH   F .   ? 0.3190 0.2533 0.3252 0.0190  0.0200  0.0223  381 HOH   B O   
7139 O O   . HOH   F .   ? 0.5687 0.4305 0.4207 0.0484  -0.0127 -0.0727 382 HOH   B O   
7140 O O   . HOH   F .   ? 0.3462 0.7540 0.5469 0.0622  0.1178  0.1069  383 HOH   B O   
7141 O O   . HOH   F .   ? 0.3661 0.6973 0.5714 0.0047  0.1361  0.1226  384 HOH   B O   
7142 O O   . HOH   F .   ? 0.5785 0.5170 0.5040 0.0096  -0.0947 -0.0595 385 HOH   B O   
7143 O O   . HOH   F .   ? 0.6322 0.5426 0.4934 -0.0838 0.0193  0.0831  386 HOH   B O   
7144 O O   . HOH   F .   ? 0.6359 0.4745 0.4121 0.1745  -0.0365 -0.0368 387 HOH   B O   
7145 O O   . HOH   F .   ? 0.2457 0.4327 0.4576 -0.0580 -0.0831 -0.0103 388 HOH   B O   
7146 O O   . HOH   F .   ? 0.4664 0.3954 0.3172 0.0035  0.0901  -0.0382 389 HOH   B O   
7147 O O   . HOH   F .   ? 0.4057 0.2561 0.3443 0.0883  -0.0037 0.0104  390 HOH   B O   
7148 O O   . HOH   F .   ? 0.5602 0.4159 0.4815 0.0001  0.0812  0.0442  391 HOH   B O   
7149 O O   . HOH   F .   ? 0.2648 0.3899 0.6655 -0.1077 -0.0801 0.0170  392 HOH   B O   
7150 O O   . HOH   F .   ? 0.4364 0.2581 0.5362 -0.0283 0.0993  0.0696  393 HOH   B O   
7151 O O   . HOH   F .   ? 0.4337 0.6099 0.4507 0.0644  0.0035  -0.1010 394 HOH   B O   
7152 O O   . HOH   F .   ? 0.4845 0.4384 0.4968 0.0075  0.1464  0.1091  395 HOH   B O   
7153 O O   . HOH   F .   ? 0.3611 0.4012 0.4000 0.0087  0.0245  -0.0798 396 HOH   B O   
7154 O O   . HOH   F .   ? 0.2062 0.2886 0.6297 -0.0512 -0.0717 -0.0116 397 HOH   B O   
7155 O O   . HOH   F .   ? 0.6013 0.4106 0.3166 -0.2436 -0.0391 0.0865  398 HOH   B O   
7156 O O   . HOH   F .   ? 0.5444 0.6243 0.6491 0.0817  -0.1246 0.2167  399 HOH   B O   
7157 O O   . HOH   F .   ? 0.4782 0.5421 0.3182 0.1811  -0.0254 -0.0370 400 HOH   B O   
# 
