data_7HEG
# 
_entry.id   7HEG 
# 
_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   7HEG         pdb_00007heg 10.2210/pdb7heg/pdb 
WWPDB D_1001407370 ?            ?                   
# 
_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                        7HEG 
_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 '(2R)-3-(2-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 282.340   1   ? ? ? ? 
4 water       nat water                                                                           18.015    432 ? ? ? ? 
# 
_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 '(2R)-3-(2-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9S 
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 
A1A9S non-polymer         . '(2R)-3-(2-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C16 H18 N4 O'   
282.340 
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 A1A9S 1   202 201  A1A9S LA1 A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 196  HOH   HOH A . 
E 4 HOH   3   303 247  HOH   HOH A . 
E 4 HOH   4   304 209  HOH   HOH A . 
E 4 HOH   5   305 409  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 6    HOH   HOH A . 
E 4 HOH   9   309 7    HOH   HOH A . 
E 4 HOH   10  310 229  HOH   HOH A . 
E 4 HOH   11  311 26   HOH   HOH A . 
E 4 HOH   12  312 1283 HOH   HOH A . 
E 4 HOH   13  313 96   HOH   HOH A . 
E 4 HOH   14  314 151  HOH   HOH A . 
E 4 HOH   15  315 192  HOH   HOH A . 
E 4 HOH   16  316 1295 HOH   HOH A . 
E 4 HOH   17  317 76   HOH   HOH A . 
E 4 HOH   18  318 155  HOH   HOH A . 
E 4 HOH   19  319 136  HOH   HOH A . 
E 4 HOH   20  320 236  HOH   HOH A . 
E 4 HOH   21  321 281  HOH   HOH A . 
E 4 HOH   22  322 964  HOH   HOH A . 
E 4 HOH   23  323 1290 HOH   HOH A . 
E 4 HOH   24  324 241  HOH   HOH A . 
E 4 HOH   25  325 39   HOH   HOH A . 
E 4 HOH   26  326 124  HOH   HOH A . 
E 4 HOH   27  327 15   HOH   HOH A . 
E 4 HOH   28  328 21   HOH   HOH A . 
E 4 HOH   29  329 18   HOH   HOH A . 
E 4 HOH   30  330 36   HOH   HOH A . 
E 4 HOH   31  331 140  HOH   HOH A . 
E 4 HOH   32  332 469  HOH   HOH A . 
E 4 HOH   33  333 33   HOH   HOH A . 
E 4 HOH   34  334 153  HOH   HOH A . 
E 4 HOH   35  335 337  HOH   HOH A . 
E 4 HOH   36  336 661  HOH   HOH A . 
E 4 HOH   37  337 42   HOH   HOH A . 
E 4 HOH   38  338 92   HOH   HOH A . 
E 4 HOH   39  339 320  HOH   HOH A . 
E 4 HOH   40  340 165  HOH   HOH A . 
E 4 HOH   41  341 2    HOH   HOH A . 
E 4 HOH   42  342 225  HOH   HOH A . 
E 4 HOH   43  343 662  HOH   HOH A . 
E 4 HOH   44  344 396  HOH   HOH A . 
E 4 HOH   45  345 169  HOH   HOH A . 
E 4 HOH   46  346 164  HOH   HOH A . 
E 4 HOH   47  347 105  HOH   HOH A . 
E 4 HOH   48  348 57   HOH   HOH A . 
E 4 HOH   49  349 354  HOH   HOH A . 
E 4 HOH   50  350 381  HOH   HOH A . 
E 4 HOH   51  351 93   HOH   HOH A . 
E 4 HOH   52  352 1300 HOH   HOH A . 
E 4 HOH   53  353 102  HOH   HOH A . 
E 4 HOH   54  354 162  HOH   HOH A . 
E 4 HOH   55  355 20   HOH   HOH A . 
E 4 HOH   56  356 939  HOH   HOH A . 
E 4 HOH   57  357 159  HOH   HOH A . 
E 4 HOH   58  358 66   HOH   HOH A . 
E 4 HOH   59  359 17   HOH   HOH A . 
E 4 HOH   60  360 630  HOH   HOH A . 
E 4 HOH   61  361 1238 HOH   HOH A . 
E 4 HOH   62  362 186  HOH   HOH A . 
E 4 HOH   63  363 81   HOH   HOH A . 
E 4 HOH   64  364 56   HOH   HOH A . 
E 4 HOH   65  365 366  HOH   HOH A . 
E 4 HOH   66  366 19   HOH   HOH A . 
E 4 HOH   67  367 148  HOH   HOH A . 
E 4 HOH   68  368 493  HOH   HOH A . 
E 4 HOH   69  369 115  HOH   HOH A . 
E 4 HOH   70  370 5    HOH   HOH A . 
E 4 HOH   71  371 333  HOH   HOH A . 
E 4 HOH   72  372 139  HOH   HOH A . 
E 4 HOH   73  373 138  HOH   HOH A . 
E 4 HOH   74  374 17   HOH   HOH A . 
E 4 HOH   75  375 45   HOH   HOH A . 
E 4 HOH   76  376 46   HOH   HOH A . 
E 4 HOH   77  377 49   HOH   HOH A . 
E 4 HOH   78  378 1296 HOH   HOH A . 
E 4 HOH   79  379 35   HOH   HOH A . 
E 4 HOH   80  380 393  HOH   HOH A . 
E 4 HOH   81  381 27   HOH   HOH A . 
E 4 HOH   82  382 86   HOH   HOH A . 
E 4 HOH   83  383 62   HOH   HOH A . 
E 4 HOH   84  384 140  HOH   HOH A . 
E 4 HOH   85  385 1    HOH   HOH A . 
E 4 HOH   86  386 218  HOH   HOH A . 
E 4 HOH   87  387 85   HOH   HOH A . 
E 4 HOH   88  388 134  HOH   HOH A . 
E 4 HOH   89  389 19   HOH   HOH A . 
E 4 HOH   90  390 351  HOH   HOH A . 
E 4 HOH   91  391 21   HOH   HOH A . 
E 4 HOH   92  392 78   HOH   HOH A . 
E 4 HOH   93  393 405  HOH   HOH A . 
E 4 HOH   94  394 1279 HOH   HOH A . 
E 4 HOH   95  395 116  HOH   HOH A . 
E 4 HOH   96  396 296  HOH   HOH A . 
E 4 HOH   97  397 154  HOH   HOH A . 
E 4 HOH   98  398 461  HOH   HOH A . 
E 4 HOH   99  399 6    HOH   HOH A . 
E 4 HOH   100 400 303  HOH   HOH A . 
E 4 HOH   101 401 1315 HOH   HOH A . 
E 4 HOH   102 402 1308 HOH   HOH A . 
E 4 HOH   103 403 68   HOH   HOH A . 
E 4 HOH   104 404 58   HOH   HOH A . 
E 4 HOH   105 405 12   HOH   HOH A . 
E 4 HOH   106 406 121  HOH   HOH A . 
E 4 HOH   107 407 74   HOH   HOH A . 
E 4 HOH   108 408 195  HOH   HOH A . 
E 4 HOH   109 409 22   HOH   HOH A . 
E 4 HOH   110 410 278  HOH   HOH A . 
E 4 HOH   111 411 10   HOH   HOH A . 
E 4 HOH   112 412 1289 HOH   HOH A . 
E 4 HOH   113 413 24   HOH   HOH A . 
E 4 HOH   114 414 199  HOH   HOH A . 
E 4 HOH   115 415 1310 HOH   HOH A . 
E 4 HOH   116 416 34   HOH   HOH A . 
E 4 HOH   117 417 23   HOH   HOH A . 
E 4 HOH   118 418 1301 HOH   HOH A . 
E 4 HOH   119 419 83   HOH   HOH A . 
E 4 HOH   120 420 67   HOH   HOH A . 
E 4 HOH   121 421 25   HOH   HOH A . 
E 4 HOH   122 422 1313 HOH   HOH A . 
E 4 HOH   123 423 3    HOH   HOH A . 
E 4 HOH   124 424 1275 HOH   HOH A . 
E 4 HOH   125 425 14   HOH   HOH A . 
E 4 HOH   126 426 125  HOH   HOH A . 
E 4 HOH   127 427 123  HOH   HOH A . 
E 4 HOH   128 428 8    HOH   HOH A . 
E 4 HOH   129 429 8    HOH   HOH A . 
E 4 HOH   130 430 952  HOH   HOH A . 
E 4 HOH   131 431 53   HOH   HOH A . 
E 4 HOH   132 432 1309 HOH   HOH A . 
E 4 HOH   133 433 1068 HOH   HOH A . 
E 4 HOH   134 434 156  HOH   HOH A . 
E 4 HOH   135 435 397  HOH   HOH A . 
E 4 HOH   136 436 95   HOH   HOH A . 
E 4 HOH   137 437 7    HOH   HOH A . 
E 4 HOH   138 438 1222 HOH   HOH A . 
E 4 HOH   139 439 132  HOH   HOH A . 
E 4 HOH   140 440 11   HOH   HOH A . 
E 4 HOH   141 441 70   HOH   HOH A . 
E 4 HOH   142 442 51   HOH   HOH A . 
E 4 HOH   143 443 122  HOH   HOH A . 
E 4 HOH   144 444 4    HOH   HOH A . 
E 4 HOH   145 445 212  HOH   HOH A . 
E 4 HOH   146 446 576  HOH   HOH A . 
E 4 HOH   147 447 582  HOH   HOH A . 
E 4 HOH   148 448 13   HOH   HOH A . 
E 4 HOH   149 449 71   HOH   HOH A . 
E 4 HOH   150 450 80   HOH   HOH A . 
E 4 HOH   151 451 104  HOH   HOH A . 
E 4 HOH   152 452 188  HOH   HOH A . 
E 4 HOH   153 453 944  HOH   HOH A . 
E 4 HOH   154 454 79   HOH   HOH A . 
E 4 HOH   155 455 15   HOH   HOH A . 
E 4 HOH   156 456 94   HOH   HOH A . 
E 4 HOH   157 457 16   HOH   HOH A . 
E 4 HOH   158 458 1189 HOH   HOH A . 
E 4 HOH   159 459 97   HOH   HOH A . 
E 4 HOH   160 460 40   HOH   HOH A . 
E 4 HOH   161 461 1286 HOH   HOH A . 
E 4 HOH   162 462 330  HOH   HOH A . 
E 4 HOH   163 463 73   HOH   HOH A . 
E 4 HOH   164 464 1094 HOH   HOH A . 
E 4 HOH   165 465 1134 HOH   HOH A . 
E 4 HOH   166 466 2    HOH   HOH A . 
E 4 HOH   167 467 107  HOH   HOH A . 
E 4 HOH   168 468 509  HOH   HOH A . 
E 4 HOH   169 469 9    HOH   HOH A . 
E 4 HOH   170 470 163  HOH   HOH A . 
E 4 HOH   171 471 726  HOH   HOH A . 
E 4 HOH   172 472 1119 HOH   HOH A . 
E 4 HOH   173 473 756  HOH   HOH A . 
E 4 HOH   174 474 408  HOH   HOH A . 
E 4 HOH   175 475 801  HOH   HOH A . 
E 4 HOH   176 476 361  HOH   HOH A . 
E 4 HOH   177 477 126  HOH   HOH A . 
E 4 HOH   178 478 342  HOH   HOH A . 
E 4 HOH   179 479 319  HOH   HOH A . 
E 4 HOH   180 480 1276 HOH   HOH A . 
E 4 HOH   181 481 556  HOH   HOH A . 
E 4 HOH   182 482 370  HOH   HOH A . 
E 4 HOH   183 483 1307 HOH   HOH A . 
E 4 HOH   184 484 224  HOH   HOH A . 
E 4 HOH   185 485 63   HOH   HOH A . 
E 4 HOH   186 486 250  HOH   HOH A . 
E 4 HOH   187 487 280  HOH   HOH A . 
E 4 HOH   188 488 12   HOH   HOH A . 
E 4 HOH   189 489 267  HOH   HOH A . 
E 4 HOH   190 490 1287 HOH   HOH A . 
E 4 HOH   191 491 135  HOH   HOH A . 
E 4 HOH   192 492 695  HOH   HOH A . 
E 4 HOH   193 493 5    HOH   HOH A . 
E 4 HOH   194 494 1306 HOH   HOH A . 
E 4 HOH   195 495 674  HOH   HOH A . 
E 4 HOH   196 496 711  HOH   HOH A . 
E 4 HOH   197 497 919  HOH   HOH A . 
E 4 HOH   198 498 202  HOH   HOH A . 
E 4 HOH   199 499 1299 HOH   HOH A . 
E 4 HOH   200 500 521  HOH   HOH A . 
E 4 HOH   201 501 331  HOH   HOH A . 
E 4 HOH   202 502 1314 HOH   HOH A . 
E 4 HOH   203 503 309  HOH   HOH A . 
E 4 HOH   204 504 318  HOH   HOH A . 
E 4 HOH   205 505 315  HOH   HOH A . 
E 4 HOH   206 506 805  HOH   HOH A . 
E 4 HOH   207 507 4    HOH   HOH A . 
E 4 HOH   208 508 263  HOH   HOH A . 
E 4 HOH   209 509 941  HOH   HOH A . 
E 4 HOH   210 510 152  HOH   HOH A . 
E 4 HOH   211 511 356  HOH   HOH A . 
E 4 HOH   212 512 208  HOH   HOH A . 
E 4 HOH   213 513 180  HOH   HOH A . 
E 4 HOH   214 514 1071 HOH   HOH A . 
E 4 HOH   215 515 350  HOH   HOH A . 
E 4 HOH   216 516 363  HOH   HOH A . 
E 4 HOH   217 517 18   HOH   HOH A . 
E 4 HOH   218 518 313  HOH   HOH A . 
E 4 HOH   219 519 371  HOH   HOH A . 
E 4 HOH   220 520 1284 HOH   HOH A . 
E 4 HOH   221 521 326  HOH   HOH A . 
E 4 HOH   222 522 3    HOH   HOH A . 
E 4 HOH   223 523 185  HOH   HOH A . 
E 4 HOH   224 524 429  HOH   HOH A . 
E 4 HOH   225 525 16   HOH   HOH A . 
E 4 HOH   226 526 376  HOH   HOH A . 
E 4 HOH   227 527 772  HOH   HOH A . 
E 4 HOH   228 528 70   HOH   HOH A . 
E 4 HOH   229 529 1074 HOH   HOH A . 
E 4 HOH   230 530 1292 HOH   HOH A . 
E 4 HOH   231 531 346  HOH   HOH A . 
E 4 HOH   232 532 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 358  HOH   HOH B . 
F 4 HOH   3   203 531  HOH   HOH B . 
F 4 HOH   4   204 758  HOH   HOH B . 
F 4 HOH   5   205 549  HOH   HOH B . 
F 4 HOH   6   206 900  HOH   HOH B . 
F 4 HOH   7   207 1249 HOH   HOH B . 
F 4 HOH   8   208 353  HOH   HOH B . 
F 4 HOH   9   209 398  HOH   HOH B . 
F 4 HOH   10  210 364  HOH   HOH B . 
F 4 HOH   11  211 654  HOH   HOH B . 
F 4 HOH   12  212 452  HOH   HOH B . 
F 4 HOH   13  213 120  HOH   HOH B . 
F 4 HOH   14  214 743  HOH   HOH B . 
F 4 HOH   15  215 264  HOH   HOH B . 
F 4 HOH   16  216 343  HOH   HOH B . 
F 4 HOH   17  217 50   HOH   HOH B . 
F 4 HOH   18  218 1278 HOH   HOH B . 
F 4 HOH   19  219 282  HOH   HOH B . 
F 4 HOH   20  220 1140 HOH   HOH B . 
F 4 HOH   21  221 240  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 54   HOH   HOH B . 
F 4 HOH   25  225 75   HOH   HOH B . 
F 4 HOH   26  226 205  HOH   HOH B . 
F 4 HOH   27  227 82   HOH   HOH B . 
F 4 HOH   28  228 232  HOH   HOH B . 
F 4 HOH   29  229 272  HOH   HOH B . 
F 4 HOH   30  230 252  HOH   HOH B . 
F 4 HOH   31  231 69   HOH   HOH B . 
F 4 HOH   32  232 332  HOH   HOH B . 
F 4 HOH   33  233 110  HOH   HOH B . 
F 4 HOH   34  234 60   HOH   HOH B . 
F 4 HOH   35  235 1    HOH   HOH B . 
F 4 HOH   36  236 723  HOH   HOH B . 
F 4 HOH   37  237 276  HOH   HOH B . 
F 4 HOH   38  238 271  HOH   HOH B . 
F 4 HOH   39  239 300  HOH   HOH B . 
F 4 HOH   40  240 181  HOH   HOH B . 
F 4 HOH   41  241 166  HOH   HOH B . 
F 4 HOH   42  242 128  HOH   HOH B . 
F 4 HOH   43  243 127  HOH   HOH B . 
F 4 HOH   44  244 14   HOH   HOH B . 
F 4 HOH   45  245 9    HOH   HOH B . 
F 4 HOH   46  246 391  HOH   HOH B . 
F 4 HOH   47  247 231  HOH   HOH B . 
F 4 HOH   48  248 1312 HOH   HOH B . 
F 4 HOH   49  249 325  HOH   HOH B . 
F 4 HOH   50  250 143  HOH   HOH B . 
F 4 HOH   51  251 133  HOH   HOH B . 
F 4 HOH   52  252 172  HOH   HOH B . 
F 4 HOH   53  253 52   HOH   HOH B . 
F 4 HOH   54  254 72   HOH   HOH B . 
F 4 HOH   55  255 129  HOH   HOH B . 
F 4 HOH   56  256 144  HOH   HOH B . 
F 4 HOH   57  257 30   HOH   HOH B . 
F 4 HOH   58  258 47   HOH   HOH B . 
F 4 HOH   59  259 150  HOH   HOH B . 
F 4 HOH   60  260 103  HOH   HOH B . 
F 4 HOH   61  261 31   HOH   HOH B . 
F 4 HOH   62  262 41   HOH   HOH B . 
F 4 HOH   63  263 10   HOH   HOH B . 
F 4 HOH   64  264 242  HOH   HOH B . 
F 4 HOH   65  265 347  HOH   HOH B . 
F 4 HOH   66  266 59   HOH   HOH B . 
F 4 HOH   67  267 61   HOH   HOH B . 
F 4 HOH   68  268 243  HOH   HOH B . 
F 4 HOH   69  269 11   HOH   HOH B . 
F 4 HOH   70  270 1277 HOH   HOH B . 
F 4 HOH   71  271 20   HOH   HOH B . 
F 4 HOH   72  272 416  HOH   HOH B . 
F 4 HOH   73  273 221  HOH   HOH B . 
F 4 HOH   74  274 77   HOH   HOH B . 
F 4 HOH   75  275 43   HOH   HOH B . 
F 4 HOH   76  276 220  HOH   HOH B . 
F 4 HOH   77  277 117  HOH   HOH B . 
F 4 HOH   78  278 84   HOH   HOH B . 
F 4 HOH   79  279 114  HOH   HOH B . 
F 4 HOH   80  280 387  HOH   HOH B . 
F 4 HOH   81  281 302  HOH   HOH B . 
F 4 HOH   82  282 235  HOH   HOH B . 
F 4 HOH   83  283 141  HOH   HOH B . 
F 4 HOH   84  284 175  HOH   HOH B . 
F 4 HOH   85  285 147  HOH   HOH B . 
F 4 HOH   86  286 22   HOH   HOH B . 
F 4 HOH   87  287 88   HOH   HOH B . 
F 4 HOH   88  288 1066 HOH   HOH B . 
F 4 HOH   89  289 99   HOH   HOH B . 
F 4 HOH   90  290 216  HOH   HOH B . 
F 4 HOH   91  291 341  HOH   HOH B . 
F 4 HOH   92  292 106  HOH   HOH B . 
F 4 HOH   93  293 1106 HOH   HOH B . 
F 4 HOH   94  294 1305 HOH   HOH B . 
F 4 HOH   95  295 635  HOH   HOH B . 
F 4 HOH   96  296 13   HOH   HOH B . 
F 4 HOH   97  297 142  HOH   HOH B . 
F 4 HOH   98  298 89   HOH   HOH B . 
F 4 HOH   99  299 137  HOH   HOH B . 
F 4 HOH   100 300 287  HOH   HOH B . 
F 4 HOH   101 301 32   HOH   HOH B . 
F 4 HOH   102 302 101  HOH   HOH B . 
F 4 HOH   103 303 215  HOH   HOH B . 
F 4 HOH   104 304 112  HOH   HOH B . 
F 4 HOH   105 305 160  HOH   HOH B . 
F 4 HOH   106 306 161  HOH   HOH B . 
F 4 HOH   107 307 1274 HOH   HOH B . 
F 4 HOH   108 308 170  HOH   HOH B . 
F 4 HOH   109 309 316  HOH   HOH B . 
F 4 HOH   110 310 91   HOH   HOH B . 
F 4 HOH   111 311 311  HOH   HOH B . 
F 4 HOH   112 312 38   HOH   HOH B . 
F 4 HOH   113 313 118  HOH   HOH B . 
F 4 HOH   114 314 100  HOH   HOH B . 
F 4 HOH   115 315 297  HOH   HOH B . 
F 4 HOH   116 316 299  HOH   HOH B . 
F 4 HOH   117 317 1291 HOH   HOH B . 
F 4 HOH   118 318 28   HOH   HOH B . 
F 4 HOH   119 319 48   HOH   HOH B . 
F 4 HOH   120 320 23   HOH   HOH B . 
F 4 HOH   121 321 37   HOH   HOH B . 
F 4 HOH   122 322 1294 HOH   HOH B . 
F 4 HOH   123 323 44   HOH   HOH B . 
F 4 HOH   124 324 334  HOH   HOH B . 
F 4 HOH   125 325 1126 HOH   HOH B . 
F 4 HOH   126 326 1285 HOH   HOH B . 
F 4 HOH   127 327 182  HOH   HOH B . 
F 4 HOH   128 328 177  HOH   HOH B . 
F 4 HOH   129 329 197  HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 98   HOH   HOH B . 
F 4 HOH   132 332 704  HOH   HOH B . 
F 4 HOH   133 333 55   HOH   HOH B . 
F 4 HOH   134 334 207  HOH   HOH B . 
F 4 HOH   135 335 717  HOH   HOH B . 
F 4 HOH   136 336 65   HOH   HOH B . 
F 4 HOH   137 337 234  HOH   HOH B . 
F 4 HOH   138 338 1293 HOH   HOH B . 
F 4 HOH   139 339 339  HOH   HOH B . 
F 4 HOH   140 340 619  HOH   HOH B . 
F 4 HOH   141 341 445  HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 90   HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 1304 HOH   HOH B . 
F 4 HOH   146 346 463  HOH   HOH B . 
F 4 HOH   147 347 960  HOH   HOH B . 
F 4 HOH   148 348 335  HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 623  HOH   HOH B . 
F 4 HOH   151 351 1046 HOH   HOH B . 
F 4 HOH   152 352 304  HOH   HOH B . 
F 4 HOH   153 353 1280 HOH   HOH B . 
F 4 HOH   154 354 479  HOH   HOH B . 
F 4 HOH   155 355 541  HOH   HOH B . 
F 4 HOH   156 356 87   HOH   HOH B . 
F 4 HOH   157 357 290  HOH   HOH B . 
F 4 HOH   158 358 203  HOH   HOH B . 
F 4 HOH   159 359 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 1316 HOH   HOH B . 
F 4 HOH   165 365 340  HOH   HOH B . 
F 4 HOH   166 366 615  HOH   HOH B . 
F 4 HOH   167 367 373  HOH   HOH B . 
F 4 HOH   168 368 898  HOH   HOH B . 
F 4 HOH   169 369 1303 HOH   HOH B . 
F 4 HOH   170 370 291  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 190  HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 149  HOH   HOH B . 
F 4 HOH   176 376 183  HOH   HOH B . 
F 4 HOH   177 377 1163 HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 1000 HOH   HOH B . 
F 4 HOH   180 380 1311 HOH   HOH B . 
F 4 HOH   181 381 418  HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 981  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 248  HOH   HOH B . 
F 4 HOH   187 387 1298 HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 470  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   194 394 566  HOH   HOH B . 
F 4 HOH   195 395 274  HOH   HOH B . 
F 4 HOH   196 396 792  HOH   HOH B . 
F 4 HOH   197 397 157  HOH   HOH B . 
F 4 HOH   198 398 314  HOH   HOH B . 
F 4 HOH   199 399 321  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           7HEG 
_cell.length_a           88.777 
_cell.length_b           88.777 
_cell.length_c           39.600 
_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                         7HEG 
_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          7HEG 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.79 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HEG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156364 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.300 
_reflns.B_iso_Wilson_estimate        11.470 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.049 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1001638 
_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 1.020 1.040  ? 41268 7392 ? 1.203 ? ? ? 5.600 ? 1.000  ? ? ? ? ? ? 95.700 1.328 0.550 0.608 
1 2 5.590 44.390 ? 7127  1037 ? 0.024 ? ? ? 6.900 ? 57.300 ? ? ? ? ? ? 99.700 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HEG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3900 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6600 
_refine.ls_number_reflns_obs                     156303 
_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                          0.1442 
_refine.ls_R_factor_R_work                       0.1435 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1583 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7542 
_refine.ls_number_reflns_R_work                  148761 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.3787 
_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                            0.1300 
_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                                60.650 
_refine.B_iso_min                                7.710 
_refine.pdbx_overall_phase_error                 15.8900 
_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                       1.0200 
_refine_hist.d_res_low                        44.3900 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.number_atoms_solvent             432 
_refine_hist.number_atoms_total               3020 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.02 
_refine_hist.pdbx_B_iso_mean_solvent          28.75 
_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 
1.0200 1.0300  30 93.0000  4641 . 0.4370 0.4447 . 187 0.0000 4828 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4953 . 0.3576 0.3525 . 281 0.0000 5234 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4876 . 0.3011 0.3021 . 278 0.0000 5154 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4951 . 0.2661 0.2712 . 277 0.0000 5228 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4913 . 0.2243 0.2448 . 241 0.0000 5154 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4978 . 0.1981 0.2322 . 240 0.0000 5218 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4925 . 0.1780 0.1998 . 255 0.0000 5180 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5011 . 0.1652 0.1883 . 224 0.0000 5235 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4921 . 0.1515 0.1852 . 249 0.0000 5170 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4997 . 0.1383 0.1587 . 255 0.0000 5252 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4932 . 0.1331 0.1552 . 239 0.0000 5171 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4889 . 0.1242 0.1627 . 283 0.0000 5172 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5010 . 0.1222 0.1499 . 218 0.0000 5228 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4943 . 0.1261 0.1366 . 254 0.0000 5197 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4957 . 0.1297 0.1429 . 246 0.0000 5203 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4966 . 0.1324 0.1461 . 265 0.0000 5231 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4956 . 0.1405 0.1547 . 257 0.0000 5213 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4956 . 0.1271 0.1566 . 253 0.0000 5209 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4983 . 0.1220 0.1468 . 241 0.0000 5224 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4965 . 0.1174 0.1361 . 250 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4985 . 0.1150 0.1267 . 237 0.0000 5222 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 4983 . 0.1163 0.1300 . 265 0.0000 5248 . 'X-RAY DIFFRACTION' 
1.5900 1.6600  30 100.0000 4954 . 0.1168 0.1325 . 262 0.0000 5216 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5034 . 0.1243 0.1418 . 202 0.0000 5236 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4953 . 0.1271 0.1384 . 296 0.0000 5249 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4977 . 0.1346 0.1352 . 247 0.0000 5224 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4960 . 0.1367 0.1466 . 286 0.0000 5246 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5022 . 0.1388 0.1406 . 251 0.0000 5273 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5017 . 0.1503 0.1615 . 250 0.0000 5267 . 'X-RAY DIFFRACTION' 
3.1700 44.3900 30 99.0000  5153 . 0.1497 0.1764 . 253 0.0000 5406 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEG 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003674' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEG 
_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 7HEG A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEG 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 7HEG SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEG MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEG SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEG 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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEG 
_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_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.59 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86 ? ? 55.75 -133.61 
2 1 HIS B 86 ? ? 56.63 -128.54 
# 
_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 531 ? 6.06 . 
2 1 O ? A HOH 532 ? 7.70 . 
3 1 O ? B HOH 400 ? 6.15 . 
# 
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 
A1A9S N2   N Y N 1   
A1A9S C3   C Y N 2   
A1A9S C6   C Y N 3   
A1A9S C9   C N R 4   
A1A9S C12  C Y N 5   
A1A9S C14  C Y N 6   
A1A9S C1   C N N 7   
A1A9S C10  C N N 8   
A1A9S C11  C Y N 9   
A1A9S C13  C Y N 10  
A1A9S C15  C Y N 11  
A1A9S C16  C Y N 12  
A1A9S C2   C Y N 13  
A1A9S C4   C Y N 14  
A1A9S C5   C Y N 15  
A1A9S C7   C Y N 16  
A1A9S C8   C N N 17  
A1A9S N1   N N N 18  
A1A9S N3   N Y N 19  
A1A9S N4   N Y N 20  
A1A9S O1   O N N 21  
A1A9S H5   H N N 22  
A1A9S H8   H N N 23  
A1A9S H1   H N N 24  
A1A9S H15  H N N 25  
A1A9S H4   H N N 26  
A1A9S H2   H N N 27  
A1A9S H3   H N N 28  
A1A9S H12  H N N 29  
A1A9S H11  H N N 30  
A1A9S H16  H N N 31  
A1A9S H17  H N N 32  
A1A9S H6   H N N 33  
A1A9S H7   H N N 34  
A1A9S H9   H N N 35  
A1A9S H10  H N N 36  
A1A9S H14  H N N 37  
A1A9S H18  H N N 38  
A1A9S H13  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
GLN   N    N N N 127 
GLN   CA   C N S 128 
GLN   C    C N N 129 
GLN   O    O N N 130 
GLN   CB   C N N 131 
GLN   CG   C N N 132 
GLN   CD   C N N 133 
GLN   OE1  O N N 134 
GLN   NE2  N N N 135 
GLN   OXT  O N N 136 
GLN   H    H N N 137 
GLN   H2   H N N 138 
GLN   HA   H N N 139 
GLN   HB2  H N N 140 
GLN   HB3  H N N 141 
GLN   HG2  H N N 142 
GLN   HG3  H N N 143 
GLN   HE21 H N N 144 
GLN   HE22 H N N 145 
GLN   HXT  H N N 146 
GLU   N    N N N 147 
GLU   CA   C N S 148 
GLU   C    C N N 149 
GLU   O    O N N 150 
GLU   CB   C N N 151 
GLU   CG   C N N 152 
GLU   CD   C N N 153 
GLU   OE1  O N N 154 
GLU   OE2  O N N 155 
GLU   OXT  O N N 156 
GLU   H    H N N 157 
GLU   H2   H N N 158 
GLU   HA   H N N 159 
GLU   HB2  H N N 160 
GLU   HB3  H N N 161 
GLU   HG2  H N N 162 
GLU   HG3  H N N 163 
GLU   HE2  H N N 164 
GLU   HXT  H N N 165 
GLY   N    N N N 166 
GLY   CA   C N N 167 
GLY   C    C N N 168 
GLY   O    O N N 169 
GLY   OXT  O N N 170 
GLY   H    H N N 171 
GLY   H2   H N N 172 
GLY   HA2  H N N 173 
GLY   HA3  H N N 174 
GLY   HXT  H N N 175 
HIS   N    N N N 176 
HIS   CA   C N S 177 
HIS   C    C N N 178 
HIS   O    O N N 179 
HIS   CB   C N N 180 
HIS   CG   C Y N 181 
HIS   ND1  N Y N 182 
HIS   CD2  C Y N 183 
HIS   CE1  C Y N 184 
HIS   NE2  N Y N 185 
HIS   OXT  O N N 186 
HIS   H    H N N 187 
HIS   H2   H N N 188 
HIS   HA   H N N 189 
HIS   HB2  H N N 190 
HIS   HB3  H N N 191 
HIS   HD1  H N N 192 
HIS   HD2  H N N 193 
HIS   HE1  H N N 194 
HIS   HE2  H N N 195 
HIS   HXT  H N N 196 
HOH   O    O N N 197 
HOH   H1   H N N 198 
HOH   H2   H N N 199 
ILE   N    N N N 200 
ILE   CA   C N S 201 
ILE   C    C N N 202 
ILE   O    O N N 203 
ILE   CB   C N S 204 
ILE   CG1  C N N 205 
ILE   CG2  C N N 206 
ILE   CD1  C N N 207 
ILE   OXT  O N N 208 
ILE   H    H N N 209 
ILE   H2   H N N 210 
ILE   HA   H N N 211 
ILE   HB   H N N 212 
ILE   HG12 H N N 213 
ILE   HG13 H N N 214 
ILE   HG21 H N N 215 
ILE   HG22 H N N 216 
ILE   HG23 H N N 217 
ILE   HD11 H N N 218 
ILE   HD12 H N N 219 
ILE   HD13 H N N 220 
ILE   HXT  H N N 221 
LEU   N    N N N 222 
LEU   CA   C N S 223 
LEU   C    C N N 224 
LEU   O    O N N 225 
LEU   CB   C N N 226 
LEU   CG   C N N 227 
LEU   CD1  C N N 228 
LEU   CD2  C N N 229 
LEU   OXT  O N N 230 
LEU   H    H N N 231 
LEU   H2   H N N 232 
LEU   HA   H N N 233 
LEU   HB2  H N N 234 
LEU   HB3  H N N 235 
LEU   HG   H N N 236 
LEU   HD11 H N N 237 
LEU   HD12 H N N 238 
LEU   HD13 H N N 239 
LEU   HD21 H N N 240 
LEU   HD22 H N N 241 
LEU   HD23 H N N 242 
LEU   HXT  H N N 243 
LYS   N    N N N 244 
LYS   CA   C N S 245 
LYS   C    C N N 246 
LYS   O    O N N 247 
LYS   CB   C N N 248 
LYS   CG   C N N 249 
LYS   CD   C N N 250 
LYS   CE   C N N 251 
LYS   NZ   N N N 252 
LYS   OXT  O N N 253 
LYS   H    H N N 254 
LYS   H2   H N N 255 
LYS   HA   H N N 256 
LYS   HB2  H N N 257 
LYS   HB3  H N N 258 
LYS   HG2  H N N 259 
LYS   HG3  H N N 260 
LYS   HD2  H N N 261 
LYS   HD3  H N N 262 
LYS   HE2  H N N 263 
LYS   HE3  H N N 264 
LYS   HZ1  H N N 265 
LYS   HZ2  H N N 266 
LYS   HZ3  H N N 267 
LYS   HXT  H N N 268 
MET   N    N N N 269 
MET   CA   C N S 270 
MET   C    C N N 271 
MET   O    O N N 272 
MET   CB   C N N 273 
MET   CG   C N N 274 
MET   SD   S N N 275 
MET   CE   C N N 276 
MET   OXT  O N N 277 
MET   H    H N N 278 
MET   H2   H N N 279 
MET   HA   H N N 280 
MET   HB2  H N N 281 
MET   HB3  H N N 282 
MET   HG2  H N N 283 
MET   HG3  H N N 284 
MET   HE1  H N N 285 
MET   HE2  H N N 286 
MET   HE3  H N N 287 
MET   HXT  H N N 288 
PHE   N    N N N 289 
PHE   CA   C N S 290 
PHE   C    C N N 291 
PHE   O    O N N 292 
PHE   CB   C N N 293 
PHE   CG   C Y N 294 
PHE   CD1  C Y N 295 
PHE   CD2  C Y N 296 
PHE   CE1  C Y N 297 
PHE   CE2  C Y N 298 
PHE   CZ   C Y N 299 
PHE   OXT  O N N 300 
PHE   H    H N N 301 
PHE   H2   H N N 302 
PHE   HA   H N N 303 
PHE   HB2  H N N 304 
PHE   HB3  H N N 305 
PHE   HD1  H N N 306 
PHE   HD2  H N N 307 
PHE   HE1  H N N 308 
PHE   HE2  H N N 309 
PHE   HZ   H N N 310 
PHE   HXT  H N N 311 
PRO   N    N N N 312 
PRO   CA   C N S 313 
PRO   C    C N N 314 
PRO   O    O N N 315 
PRO   CB   C N N 316 
PRO   CG   C N N 317 
PRO   CD   C N N 318 
PRO   OXT  O N N 319 
PRO   H    H N N 320 
PRO   HA   H N N 321 
PRO   HB2  H N N 322 
PRO   HB3  H N N 323 
PRO   HG2  H N N 324 
PRO   HG3  H N N 325 
PRO   HD2  H N N 326 
PRO   HD3  H N N 327 
PRO   HXT  H N N 328 
SER   N    N N N 329 
SER   CA   C N S 330 
SER   C    C N N 331 
SER   O    O N N 332 
SER   CB   C N N 333 
SER   OG   O N N 334 
SER   OXT  O N N 335 
SER   H    H N N 336 
SER   H2   H N N 337 
SER   HA   H N N 338 
SER   HB2  H N N 339 
SER   HB3  H N N 340 
SER   HG   H N N 341 
SER   HXT  H N N 342 
TFA   C1   C N N 343 
TFA   C2   C N N 344 
TFA   O    O N N 345 
TFA   F1   F N N 346 
TFA   F2   F N N 347 
TFA   F3   F N N 348 
TFA   OXT  O N N 349 
TFA   HXT  H N N 350 
THR   N    N N N 351 
THR   CA   C N S 352 
THR   C    C N N 353 
THR   O    O N N 354 
THR   CB   C N R 355 
THR   OG1  O N N 356 
THR   CG2  C N N 357 
THR   OXT  O N N 358 
THR   H    H N N 359 
THR   H2   H N N 360 
THR   HA   H N N 361 
THR   HB   H N N 362 
THR   HG1  H N N 363 
THR   HG21 H N N 364 
THR   HG22 H N N 365 
THR   HG23 H N N 366 
THR   HXT  H N N 367 
TYR   N    N N N 368 
TYR   CA   C N S 369 
TYR   C    C N N 370 
TYR   O    O N N 371 
TYR   CB   C N N 372 
TYR   CG   C Y N 373 
TYR   CD1  C Y N 374 
TYR   CD2  C Y N 375 
TYR   CE1  C Y N 376 
TYR   CE2  C Y N 377 
TYR   CZ   C Y N 378 
TYR   OH   O N N 379 
TYR   OXT  O N N 380 
TYR   H    H N N 381 
TYR   H2   H N N 382 
TYR   HA   H N N 383 
TYR   HB2  H N N 384 
TYR   HB3  H N N 385 
TYR   HD1  H N N 386 
TYR   HD2  H N N 387 
TYR   HE1  H N N 388 
TYR   HE2  H N N 389 
TYR   HH   H N N 390 
TYR   HXT  H N N 391 
VAL   N    N N N 392 
VAL   CA   C N S 393 
VAL   C    C N N 394 
VAL   O    O N N 395 
VAL   CB   C N N 396 
VAL   CG1  C N N 397 
VAL   CG2  C N N 398 
VAL   OXT  O N N 399 
VAL   H    H N N 400 
VAL   H2   H N N 401 
VAL   HA   H N N 402 
VAL   HB   H N N 403 
VAL   HG11 H N N 404 
VAL   HG12 H N N 405 
VAL   HG13 H N N 406 
VAL   HG21 H N N 407 
VAL   HG22 H N N 408 
VAL   HG23 H N N 409 
VAL   HXT  H N N 410 
# 
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 
A1A9S C4  C5   doub Y N 1   
A1A9S C4  C3   sing Y N 2   
A1A9S C5  C6   sing Y N 3   
A1A9S C3  C2   doub Y N 4   
A1A9S C6  C7   doub Y N 5   
A1A9S C2  C7   sing Y N 6   
A1A9S C2  C1   sing N N 7   
A1A9S C7  C8   sing N N 8   
A1A9S C8  C9   sing N N 9   
A1A9S C9  C10  sing N N 10  
A1A9S C9  N1   sing N N 11  
A1A9S C10 O1   sing N N 12  
A1A9S N1  C11  sing N N 13  
A1A9S C11 C14  doub Y N 14  
A1A9S C11 N2   sing Y N 15  
A1A9S C15 C14  sing Y N 16  
A1A9S C15 C16  doub Y N 17  
A1A9S C14 C13  sing Y N 18  
A1A9S N2  C12  doub Y N 19  
A1A9S C16 N4   sing Y N 20  
A1A9S C13 N4   sing Y N 21  
A1A9S C13 N3   doub Y N 22  
A1A9S C12 N3   sing Y N 23  
A1A9S C3  H5   sing N N 24  
A1A9S C6  H8   sing N N 25  
A1A9S C9  H1   sing N N 26  
A1A9S C12 H15  sing N N 27  
A1A9S C1  H4   sing N N 28  
A1A9S C1  H2   sing N N 29  
A1A9S C1  H3   sing N N 30  
A1A9S C10 H12  sing N N 31  
A1A9S C10 H11  sing N N 32  
A1A9S C15 H16  sing N N 33  
A1A9S C16 H17  sing N N 34  
A1A9S C4  H6   sing N N 35  
A1A9S C5  H7   sing N N 36  
A1A9S C8  H9   sing N N 37  
A1A9S C8  H10  sing N N 38  
A1A9S N1  H14  sing N N 39  
A1A9S N4  H18  sing N N 40  
A1A9S O1  H13  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
TFA   C1  C2   sing N N 331 
TFA   C1  O    doub N N 332 
TFA   C1  OXT  sing N N 333 
TFA   C2  F1   sing N N 334 
TFA   C2  F2   sing N N 335 
TFA   C2  F3   sing N N 336 
TFA   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TYR   N   CA   sing N N 354 
TYR   N   H    sing N N 355 
TYR   N   H2   sing N N 356 
TYR   CA  C    sing N N 357 
TYR   CA  CB   sing N N 358 
TYR   CA  HA   sing N N 359 
TYR   C   O    doub N N 360 
TYR   C   OXT  sing N N 361 
TYR   CB  CG   sing N N 362 
TYR   CB  HB2  sing N N 363 
TYR   CB  HB3  sing N N 364 
TYR   CG  CD1  doub Y N 365 
TYR   CG  CD2  sing Y N 366 
TYR   CD1 CE1  sing Y N 367 
TYR   CD1 HD1  sing N N 368 
TYR   CD2 CE2  doub Y N 369 
TYR   CD2 HD2  sing N N 370 
TYR   CE1 CZ   doub Y N 371 
TYR   CE1 HE1  sing N N 372 
TYR   CE2 CZ   sing Y N 373 
TYR   CE2 HE2  sing N N 374 
TYR   CZ  OH   sing N N 375 
TYR   OH  HH   sing N N 376 
TYR   OXT HXT  sing N N 377 
VAL   N   CA   sing N N 378 
VAL   N   H    sing N N 379 
VAL   N   H2   sing N N 380 
VAL   CA  C    sing N N 381 
VAL   CA  CB   sing N N 382 
VAL   CA  HA   sing N N 383 
VAL   C   O    doub N N 384 
VAL   C   OXT  sing N N 385 
VAL   CB  CG1  sing N N 386 
VAL   CB  CG2  sing N N 387 
VAL   CB  HB   sing N N 388 
VAL   CG1 HG11 sing N N 389 
VAL   CG1 HG12 sing N N 390 
VAL   CG1 HG13 sing N N 391 
VAL   CG2 HG21 sing N N 392 
VAL   CG2 HG22 sing N N 393 
VAL   CG2 HG23 sing N N 394 
VAL   OXT HXT  sing N N 395 
# 
_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                    7HEG 
_atom_sites.fract_transf_matrix[1][1]   0.011264 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011264 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025253 
_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 -16.206 22.225  0.62 45.88 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.544 -16.000 22.301  0.38 44.49 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.661 -15.130 22.406  0.62 45.38 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.572 -14.930 22.492  0.38 44.06 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.315 -13.780 22.124  0.62 43.68 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.216 -13.576 22.202  0.38 42.45 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.439 -13.523 22.557  0.62 44.12 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.324 -13.293 22.660  0.38 42.87 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.029 -15.176 23.817  0.62 46.24 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.963 -14.972 23.910  0.38 44.92 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.003 -14.063 23.984  0.62 46.44 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.921 -13.874 24.079  0.38 45.14 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.392 -16.536 24.072  0.62 46.44 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.352 -16.340 24.189  0.38 45.15 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.945 -15.243 21.768  0.62 54.48 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.844 -15.050 21.863  0.38 52.89 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.722 -15.045 24.481  0.62 55.50 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.664 -14.821 24.562  0.38 53.92 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.498 -14.219 24.799  0.62 55.74 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.439 -14.022 24.908  0.38 54.18 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.464 -13.212 24.042  0.62 55.74 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.368 -13.014 24.107  0.38 54.18 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.404 -14.067 23.221  0.62 55.74 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.306 -13.905 23.329  0.38 54.18 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.941 -16.518 24.931  0.62 55.75 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.905 -16.317 25.050  0.38 54.19 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.753 -16.722 23.366  0.62 55.75 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.713 -16.548 23.490  0.38 54.19 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.086 -17.214 24.077  0.62 55.75 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.058 -17.005 24.201  0.38 54.19 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.612 -12.927 21.378  0.62 41.21 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.513 -12.747 21.430  0.38 40.15 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.055 -11.567 21.097  0.62 38.44 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.951 -11.385 21.147  0.38 37.60 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.894 -10.602 21.327  0.62 36.05 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.822 -10.409 21.452  0.38 35.39 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.776 -11.006 21.662  0.62 35.96 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.767 -10.810 21.956  0.38 35.42 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.637 -11.438 19.681  0.62 37.72 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.444 -11.241 19.701  0.38 37.10 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.665 -11.870 18.604  0.62 36.87 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.387 -11.605 18.678  0.38 36.56 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.529 -11.400 18.552  0.62 36.51 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.258 -11.117 18.730  0.38 36.35 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.110 -12.773 17.735  0.62 36.63 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.752 -12.470 17.736  0.38 36.50 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.859 -13.124 21.013  0.62 49.47 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.765 -12.950 21.068  0.38 48.19 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.757 -11.336 21.720  0.62 46.14 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.695 -11.169 21.723  0.38 45.14 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.870 -10.510 19.518  0.62 45.28 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.710 -10.318 19.543  0.38 44.53 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.428 -11.994 19.614  0.62 45.28 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.204 -11.827 19.565  0.38 44.53 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.600 -13.051 17.102  0.62 43.98 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.193 -12.708 17.128  0.38 43.82 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.913 -13.077 17.805  0.62 43.98 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.551 -12.791 17.734  0.38 43.82 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.168 -9.311  21.138  0.62 33.55 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.028 -9.131  21.145  0.38 33.06 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.238 -8.247  21.493  0.62 31.13 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.115 -8.070  21.550  0.38 30.83 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.396 -7.757  20.316  0.62 27.83 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.246 -7.550  20.407  0.38 28.05 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.727 -6.727  20.437  0.62 27.99 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.558 -6.540  20.582  0.38 28.27 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 17.993 -7.076  22.129  0.62 32.19 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.888 -6.915  22.192  0.38 31.52 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.004 -6.590  21.264  0.62 32.65 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.572 -6.149  21.216  0.38 31.78 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.904 -9.025  20.795  0.62 40.27 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.702 -8.861  20.692  0.38 39.69 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.629 -8.588  22.164  0.62 37.37 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.522 -8.424  22.229  0.38 37.02 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.367 -6.358  22.315  0.62 38.64 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.261 -6.343  22.663  0.38 37.84 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.403 -7.376  22.957  0.62 38.64 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.536 -7.277  22.819  0.38 37.84 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.411 -5.949  21.628  0.62 39.19 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 18.986 -5.517  21.587  0.38 38.15 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.409 -8.463  19.189  0.62 23.92 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.259 -8.204  19.248  0.38 25.01 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.532 -8.109  18.079  0.62 20.72 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.338 -7.826  18.184  0.38 22.26 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.093 -8.480  18.423  0.62 20.55 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.914 -8.194  18.588  0.38 21.77 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.824 -9.599  18.866  0.62 21.73 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.675 -9.251  19.176  0.38 22.44 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.970 -8.848  16.817  0.62 18.47 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.712 -8.536  16.883  0.38 20.46 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.249 -8.323  16.214  0.62 17.25 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.013 -8.070  16.284  0.38 19.33 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.259 -7.131  15.509  0.62 16.80 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.059 -6.937  15.485  0.38 18.98 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.435 -9.027  16.344  0.62 17.84 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.186 -8.770  16.510  0.38 19.37 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.425 -6.648  14.950  0.62 17.12 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.251 -6.509  14.929  0.38 19.00 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.606 -8.548  15.784  0.62 18.16 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.381 -8.347  15.955  0.38 19.43 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.600 -7.356  15.087  0.62 17.45 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.413 -7.215  15.164  0.38 19.10 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.908 -9.149  19.047  0.62 28.72 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.780 -8.862  19.057  0.38 30.02 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.576 -7.159  17.921  0.62 24.88 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.381 -6.871  18.043  0.38 26.73 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.102 -9.788  17.038  0.62 22.18 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.791 -9.487  17.056  0.38 24.57 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.268 -8.768  16.153  0.62 22.18 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.012 -8.378  16.230  0.38 24.57 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.467 -6.655  15.416  0.62 20.18 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.278 -6.458  15.323  0.38 22.79 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.443 -9.835  16.817  0.62 21.42 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.171 -9.533  17.042  0.38 23.27 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.418 -5.848  14.481  0.62 20.56 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.269 -5.747  14.396  0.38 22.82 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.398 -9.028  15.881  0.62 21.81 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.164 -8.824  16.116  0.38 23.33 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.386 -7.033  14.713  0.62 20.96 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.215 -6.928  14.792  0.38 22.93 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.161 -7.550  18.202  0.62 19.93 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 12.963 -7.313  18.278  0.38 20.92 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.789 -7.689  18.681  0.62 20.86 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.592 -7.465  18.750  0.38 20.59 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.789 -7.409  17.565  0.62 18.97 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.596 -7.232  17.621  0.38 18.45 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.000 -6.515  16.740  0.62 19.26 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.791 -6.352  16.777  0.38 18.54 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.536 -6.718  19.843  0.62 23.60 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.305 -6.488  19.897  0.38 22.48 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.194 -6.784  20.286  0.62 25.27 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 9.957  -6.580  20.319  0.38 23.82 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.305 -6.827  17.762  0.62 23.93 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.092 -6.613  17.793  0.38 25.12 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.645 -8.592  19.000  0.62 25.04 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.467 -8.367  19.081  0.38 24.72 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.121 -6.950  20.581  0.62 28.34 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 11.892 -6.699  20.642  0.38 26.99 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.725 -5.814  19.545  0.62 28.34 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.473 -5.585  19.590  0.38 26.99 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.071 -6.245  20.921  0.62 30.34 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 9.819  -6.051  20.955  0.38 28.60 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.696  -8.177  17.549  0.62 17.59 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.521  -8.022  17.621  0.38 16.75 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.604  -7.910  16.635  0.62 16.76 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.442  -7.845  16.672  0.38 15.94 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.811  -8.377  15.213  0.62 14.97 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.691  -8.399  15.289  0.38 14.50 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.110  -7.903  14.312  0.62 15.36 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 7.899  -8.119  14.380  0.38 14.83 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.573  -8.858  18.061  0.62 21.13 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.399  -8.669  18.175  0.38 20.12 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.801  -8.334  16.980  0.62 20.12 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.650  -8.279  17.017  0.38 19.14 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.446  -6.953  16.612  0.62 20.12 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.256  -6.898  16.587  0.38 19.14 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.757  -9.282  14.976  0.62 13.75 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.750  -9.182  15.098  0.38 13.79 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.002 -9.818  13.647  0.62 12.43 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.076 -9.699  13.777  0.38 12.84 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.111  -11.025 13.374  0.62 11.66 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.286  -10.964 13.466  0.38 12.42 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.789  -11.812 14.271  0.62 13.07 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 9.146  -11.857 14.309  0.38 12.96 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.470 -10.236 13.490  0.62 12.42 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.574 -9.991  13.671  0.38 12.36 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.422 -9.071  13.358  0.62 12.89 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.419 -8.755  13.455  0.38 12.05 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.835 -8.359  14.476  0.62 12.94 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.635 -7.851  14.484  0.38 12.10 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.901 -8.679  12.116  0.62 13.33 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.000 -8.494  12.221  0.38 11.55 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.689 -7.281  14.361  0.62 13.59 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.396 -6.717  14.290  0.38 11.76 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.755 -7.605  11.989  0.62 13.61 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.762 -7.361  12.017  0.38 11.36 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.151 -6.910  13.114  0.62 14.07 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 13.960 -6.478  13.054  0.38 11.45 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 15.003 -5.841  12.985  0.62 14.98 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.717 -5.352  12.852  0.38 12.04 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.275 -9.603  15.579  0.62 16.52 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.293 -9.431  15.721  0.38 16.57 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.815  -9.130  12.980  0.62 14.94 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.852  -9.030  13.115  0.38 15.43 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.739 -10.755 14.263  0.62 14.92 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.871 -10.421 14.488  0.38 14.85 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.548 -10.771 12.686  0.62 14.92 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.715 -10.584 12.916  0.38 14.85 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.522 -8.609  15.316  0.62 15.54 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.250 -8.009  15.318  0.38 14.53 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.634 -9.145  11.354  0.62 16.01 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.864 -9.087  11.518  0.38 13.88 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.960 -6.818  15.118  0.62 16.33 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.531 -6.120  14.988  0.38 14.13 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.072 -7.356  11.148  0.62 16.35 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.146 -7.198  11.184  0.38 13.65 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.160 -5.515  13.743  0.62 17.99 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.779 -4.914  13.569  0.38 14.47 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.713  -11.155 12.115  0.62 11.55 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.786  -11.038 12.234  0.38 12.02 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.146  -12.389 11.606  0.62 11.44 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.135  -12.238 11.727  0.38 11.25 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.286  -13.319 11.198  0.62 11.62 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.213  -13.214 11.260  0.38 10.77 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.283 -12.882 10.615  0.62 11.25 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.051 -12.868 10.419  0.38 10.61 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.286  -12.061 10.390  0.62 12.78 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.200  -11.865 10.575  0.38 11.62 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.532  -13.226 9.759   0.62 14.51 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.789  -13.001 9.627   0.38 12.68 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.466  -13.745 10.705  0.62 15.88 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.921  -14.043 10.327  0.38 13.25 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 5.932  -12.817 8.423   0.62 15.84 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.094  -12.445 8.395   0.38 13.02 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.764  -10.528 11.520  0.62 13.87 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.828  -10.396 11.659  0.38 14.43 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.600  -12.815 12.290  0.62 13.74 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.611  -12.654 12.431  0.38 13.52 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.625  -11.402 10.654  0.62 15.36 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.380  -11.496 10.953  0.38 13.96 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.860  -11.686 9.707   0.62 15.36 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.633  -11.181 10.039  0.38 13.96 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.158  -13.948 9.595   0.62 17.43 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.589  -13.450 9.314   0.38 15.23 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 4.962  -14.444 10.259  0.62 19.07 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.699  -14.743 9.693   0.38 15.91 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.891  -14.101 11.501  0.62 19.07 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.417  -14.419 11.073  0.38 15.91 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.874  -13.014 10.946  0.62 19.07 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.112  -13.617 10.649  0.38 15.91 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.462  -13.575 8.046   0.62 19.03 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.851  -13.185 7.817   0.38 15.64 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.320  -12.080 8.566   0.62 19.03 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.301  -11.964 8.672   0.38 15.64 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.650  -12.542 7.829   0.62 19.03 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.703  -11.849 7.932   0.38 15.64 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.136  -14.607 11.503  0.62 11.80 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.197  -14.425 11.811  0.38 10.25 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.149 -15.611 11.200  0.62 12.25 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.127 -15.462 11.384  0.38 10.47 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.822  -16.212 9.838   0.62 12.77 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.731  -15.968 10.000  0.38 9.81  ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.804  -16.892 9.686   0.62 13.91 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.571  -16.320 9.767   0.38 9.53  ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.158 -16.671 12.301  0.62 12.59 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.121 -16.606 12.402  0.38 11.12 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.193 -17.773 12.151  0.62 12.77 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.163 -17.701 12.160  0.38 11.50 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.233 -18.624 13.418  0.62 13.26 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.248 -18.641 13.366  0.38 12.22 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.211 -19.783 13.315  0.62 13.44 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.216 -19.802 13.149  0.38 12.61 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.600 -19.315 13.063  0.62 13.71 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.627 -19.360 12.952  0.38 12.88 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.428  -14.934 11.873  0.62 14.17 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.654  -14.660 12.434  0.38 12.31 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.022 -15.191 11.158  0.62 14.71 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.016 -15.088 11.332  0.38 12.58 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.331 -16.225 13.148  0.62 15.13 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.290 -16.227 13.282  0.38 13.36 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.287  -17.089 12.330  0.62 15.13 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.246  -17.020 12.393  0.38 13.36 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 10.953 -18.343 11.405  0.62 15.34 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.908 -18.223 11.383  0.38 13.81 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.069 -17.381 12.017  0.62 15.34 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.034 -17.298 12.027  0.38 13.81 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.501 -18.068 14.166  0.62 15.93 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.550 -18.140 14.139  0.38 14.68 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.346 -18.990 13.581  0.62 15.93 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.368 -19.015 13.539  0.38 14.68 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.205 -20.283 14.149  0.62 16.15 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.192 -20.385 13.927  0.38 15.14 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 11.946 -20.362 12.581  0.62 16.15 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.946 -20.298 12.360  0.38 15.14 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.135 -20.012 12.924  0.62 16.47 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.152 -20.068 12.818  0.38 15.47 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.617 -18.789 12.345  0.62 16.47 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.682 -18.823 12.247  0.38 15.47 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 13.898 -18.857 13.764  0.62 16.47 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.913 -18.924 13.673  0.38 15.47 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.671 -15.957 8.838   0.62 11.86 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.689 -15.988 9.072   0.38 10.06 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.446 -16.565 7.529   0.62 12.15 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.450 -16.490 7.721   0.38 10.74 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.017 -17.971 7.461   0.62 12.35 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.022 -17.887 7.478   0.38 11.35 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.367 -18.882 6.930   0.62 13.28 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.377 -18.701 6.808   0.38 11.24 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.051 -15.713 6.414   0.62 12.40 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.006 -15.516 6.673   0.38 10.97 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.376 -14.367 6.166   0.62 12.98 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.413 -14.102 6.612   0.38 10.31 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.096 -13.627 5.058   0.62 12.87 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.154 -13.294 5.559   0.38 10.37 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 8.908  -14.559 5.822   0.62 13.39 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.921  -14.121 6.315   0.38 9.90  ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.361 -15.443 8.886   0.62 14.24 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.486 -15.686 9.201   0.38 12.08 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.492  -16.635 7.378   0.62 14.59 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.493  -16.540 7.584   0.38 12.90 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 11.979 -15.540 6.632   0.62 14.89 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 11.957 -15.416 6.831   0.38 13.18 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.003 -16.220 5.586   0.62 14.89 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.870 -15.913 5.799   0.38 13.18 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.432 -13.834 6.973   0.62 15.59 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.547 -13.662 7.467   0.38 12.39 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.663 -12.775 4.915   0.62 15.46 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.779 -12.400 5.524   0.38 12.46 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.022 -13.492 5.319   0.62 15.46 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.094 -13.248 5.798   0.38 12.46 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.059 -14.161 4.247   0.62 15.46 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 11.053 -13.730 4.699   0.38 12.46 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.560  -13.739 5.446   0.62 16.09 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.606  -13.207 6.220   0.38 11.89 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.828  -15.280 5.175   0.62 16.09 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.770  -14.609 5.492   0.38 11.89 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.420  -14.790 6.628   0.62 16.09 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.461  -14.554 7.049   0.38 11.89 ?  12  LEU   A HD23 1 
ATOM   319  N N    . THR   A 1 13  ? 12.230 -18.158 7.974   1.00 11.93 ?  13  THR   A N    1 
ATOM   320  C CA   . THR   A 1 13  ? 12.907 -19.447 7.880   1.00 12.11 ?  13  THR   A CA   1 
ATOM   321  C C    . THR   A 1 13  ? 13.665 -19.681 9.182   1.00 12.36 ?  13  THR   A C    1 
ATOM   322  O O    . THR   A 1 13  ? 13.567 -18.908 10.139  1.00 12.38 ?  13  THR   A O    1 
ATOM   323  C CB   . THR   A 1 13  ? 13.889 -19.496 6.699   1.00 13.14 ?  13  THR   A CB   1 
ATOM   324  O OG1  . THR   A 1 13  ? 14.958 -18.588 6.952   1.00 13.14 ?  13  THR   A OG1  1 
ATOM   325  C CG2  . THR   A 1 13  ? 13.220 -19.134 5.377   1.00 14.24 ?  13  THR   A CG2  1 
ATOM   326  H H    A THR   A 1 13  ? 12.682 -17.552 8.384   0.62 14.33 ?  13  THR   A H    1 
ATOM   327  H H    B THR   A 1 13  ? 12.714 -17.564 8.364   0.38 14.33 ?  13  THR   A H    1 
ATOM   328  H HA   . THR   A 1 13  ? 12.253 -20.152 7.767   1.00 14.55 ?  13  THR   A HA   1 
ATOM   329  H HB   . THR   A 1 13  ? 14.250 -20.391 6.617   1.00 15.78 ?  13  THR   A HB   1 
ATOM   330  H HG1  . THR   A 1 13  ? 15.506 -18.598 6.301   1.00 15.78 ?  13  THR   A HG1  1 
ATOM   331  H HG21 . THR   A 1 13  ? 13.795 -19.394 4.635   1.00 17.10 ?  13  THR   A HG21 1 
ATOM   332  H HG22 . THR   A 1 13  ? 12.377 -19.608 5.293   1.00 17.10 ?  13  THR   A HG22 1 
ATOM   333  H HG23 . THR   A 1 13  ? 13.056 -18.183 5.331   1.00 17.10 ?  13  THR   A HG23 1 
ATOM   334  N N    . ASP   A 1 14  ? 14.461 -20.748 9.199   1.00 13.10 ?  14  ASP   A N    1 
ATOM   335  C CA   . ASP   A 1 14  ? 15.308 -21.033 10.347  1.00 13.43 ?  14  ASP   A CA   1 
ATOM   336  C C    . ASP   A 1 14  ? 16.142 -19.822 10.746  1.00 12.88 ?  14  ASP   A C    1 
ATOM   337  O O    . ASP   A 1 14  ? 16.368 -19.587 11.937  1.00 14.04 ?  14  ASP   A O    1 
ATOM   338  C CB   . ASP   A 1 14  ? 16.231 -22.197 10.014  1.00 16.80 ?  14  ASP   A CB   1 
ATOM   339  C CG   . ASP   A 1 14  ? 17.157 -22.539 11.154  1.00 21.15 ?  14  ASP   A CG   1 
ATOM   340  O OD1  . ASP   A 1 14  ? 16.659 -22.934 12.232  1.00 22.24 ?  14  ASP   A OD1  1 
ATOM   341  O OD2  . ASP   A 1 14  ? 18.379 -22.404 10.966  1.00 23.95 -1 14  ASP   A OD2  1 
ATOM   342  H H    . ASP   A 1 14  ? 14.531 -21.306 8.555   1.00 15.73 ?  14  ASP   A H    1 
ATOM   343  H HA   . ASP   A 1 14  ? 14.750 -21.286 11.102  1.00 16.13 ?  14  ASP   A HA   1 
ATOM   344  H HB2  . ASP   A 1 14  ? 15.687 -22.981 9.809   1.00 20.18 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  . ASP   A 1 14  ? 16.768 -21.963 9.241   1.00 20.18 ?  14  ASP   A HB3  1 
ATOM   346  N N    . ASN   A 1 15  ? 16.614 -19.037 9.764   1.00 12.21 ?  15  ASN   A N    1 
ATOM   347  C CA   . ASN   A 1 15  ? 17.612 -18.007 10.032  1.00 12.36 ?  15  ASN   A CA   1 
ATOM   348  C C    . ASN   A 1 15  ? 17.258 -16.607 9.539   1.00 12.53 ?  15  ASN   A C    1 
ATOM   349  O O    . ASN   A 1 15  ? 18.034 -15.684 9.793   1.00 14.25 ?  15  ASN   A O    1 
ATOM   350  C CB   . ASN   A 1 15  ? 18.984 -18.417 9.459   1.00 12.02 ?  15  ASN   A CB   1 
ATOM   351  C CG   . ASN   A 1 15  ? 18.978 -18.514 7.947   1.00 12.41 ?  15  ASN   A CG   1 
ATOM   352  O OD1  . ASN   A 1 15  ? 18.251 -19.323 7.370   1.00 13.86 ?  15  ASN   A OD1  1 
ATOM   353  N ND2  . ASN   A 1 15  ? 19.781 -17.680 7.294   1.00 12.69 ?  15  ASN   A ND2  1 
ATOM   354  H H    . ASN   A 1 15  ? 16.358 -19.083 8.947   1.00 14.67 ?  15  ASN   A H    1 
ATOM   355  H HA   . ASN   A 1 15  ? 17.722 -17.940 10.989  1.00 14.85 ?  15  ASN   A HA   1 
ATOM   356  H HB2  . ASN   A 1 15  ? 19.646 -17.750 9.716   1.00 14.44 ?  15  ASN   A HB2  1 
ATOM   357  H HB3  . ASN   A 1 15  ? 19.234 -19.282 9.815   1.00 14.44 ?  15  ASN   A HB3  1 
ATOM   358  H HD21 . ASN   A 1 15  ? 19.818 -17.702 6.435   1.00 15.25 ?  15  ASN   A HD21 1 
ATOM   359  H HD22 . ASN   A 1 15  ? 20.280 -17.125 7.728   1.00 15.25 ?  15  ASN   A HD22 1 
ATOM   360  N N    A VAL   A 1 16  ? 16.122 -16.415 8.867   0.62 12.08 ?  16  VAL   A N    1 
ATOM   361  N N    B VAL   A 1 16  ? 16.131 -16.418 8.855   0.38 12.14 ?  16  VAL   A N    1 
ATOM   362  C CA   A VAL   A 1 16  ? 15.744 -15.129 8.288   0.62 12.19 ?  16  VAL   A CA   1 
ATOM   363  C CA   B VAL   A 1 16  ? 15.754 -15.121 8.303   0.38 12.09 ?  16  VAL   A CA   1 
ATOM   364  C C    A VAL   A 1 16  ? 14.458 -14.629 8.938   0.62 11.43 ?  16  VAL   A C    1 
ATOM   365  C C    B VAL   A 1 16  ? 14.475 -14.634 8.972   0.38 11.62 ?  16  VAL   A C    1 
ATOM   366  O O    A VAL   A 1 16  ? 13.455 -15.356 8.993   0.62 11.58 ?  16  VAL   A O    1 
ATOM   367  O O    B VAL   A 1 16  ? 13.497 -15.384 9.090   0.38 11.83 ?  16  VAL   A O    1 
ATOM   368  C CB   A VAL   A 1 16  ? 15.585 -15.211 6.759   0.62 12.94 ?  16  VAL   A CB   1 
ATOM   369  C CB   B VAL   A 1 16  ? 15.597 -15.163 6.771   0.38 12.41 ?  16  VAL   A CB   1 
ATOM   370  C CG1  A VAL   A 1 16  ? 15.146 -13.857 6.194   0.62 13.81 ?  16  VAL   A CG1  1 
ATOM   371  C CG1  B VAL   A 1 16  ? 15.279 -13.766 6.235   0.38 12.76 ?  16  VAL   A CG1  1 
ATOM   372  C CG2  A VAL   A 1 16  ? 16.881 -15.672 6.104   0.62 13.85 ?  16  VAL   A CG2  1 
ATOM   373  C CG2  B VAL   A 1 16  ? 16.859 -15.715 6.117   0.38 13.14 ?  16  VAL   A CG2  1 
ATOM   374  H H    A VAL   A 1 16  ? 15.538 -17.036 8.729   0.62 14.52 ?  16  VAL   A H    1 
ATOM   375  H H    B VAL   A 1 16  ? 15.558 -17.041 8.694   0.38 14.58 ?  16  VAL   A H    1 
ATOM   376  H HA   A VAL   A 1 16  ? 16.447 -14.487 8.475   0.62 14.65 ?  16  VAL   A HA   1 
ATOM   377  H HA   B VAL   A 1 16  ? 16.455 -14.484 8.504   0.38 14.52 ?  16  VAL   A HA   1 
ATOM   378  H HB   A VAL   A 1 16  ? 14.896 -15.862 6.549   0.62 15.54 ?  16  VAL   A HB   1 
ATOM   379  H HB   B VAL   A 1 16  ? 14.859 -15.749 6.543   0.38 14.91 ?  16  VAL   A HB   1 
ATOM   380  H HG11 A VAL   A 1 16  ? 15.255 -13.870 5.231   0.62 16.59 ?  16  VAL   A HG11 1 
ATOM   381  H HG11 B VAL   A 1 16  ? 15.352 -13.778 5.268   0.38 15.32 ?  16  VAL   A HG11 1 
ATOM   382  H HG12 A VAL   A 1 16  ? 14.215 -13.706 6.419   0.62 16.59 ?  16  VAL   A HG12 1 
ATOM   383  H HG12 B VAL   A 1 16  ? 14.376 -13.525 6.495   0.38 15.32 ?  16  VAL   A HG12 1 
ATOM   384  H HG13 A VAL   A 1 16  ? 15.700 -13.161 6.581   0.62 16.59 ?  16  VAL   A HG13 1 
ATOM   385  H HG13 B VAL   A 1 16  ? 15.913 -13.134 6.606   0.38 15.32 ?  16  VAL   A HG13 1 
ATOM   386  H HG21 A VAL   A 1 16  ? 16.783 -15.629 5.141   0.62 16.63 ?  16  VAL   A HG21 1 
ATOM   387  H HG21 B VAL   A 1 16  ? 16.776 -15.639 5.154   0.38 15.78 ?  16  VAL   A HG21 1 
ATOM   388  H HG22 A VAL   A 1 16  ? 17.604 -15.093 6.390   0.62 16.63 ?  16  VAL   A HG22 1 
ATOM   389  H HG22 B VAL   A 1 16  ? 17.625 -15.205 6.424   0.38 15.78 ?  16  VAL   A HG22 1 
ATOM   390  H HG23 A VAL   A 1 16  ? 17.066 -16.586 6.377   0.62 16.63 ?  16  VAL   A HG23 1 
ATOM   391  H HG23 B VAL   A 1 16  ? 16.963 -16.648 6.367   0.38 15.78 ?  16  VAL   A HG23 1 
ATOM   392  N N    . TYR   A 1 17  ? 14.495 -13.367 9.389   1.00 11.48 ?  17  TYR   A N    1 
ATOM   393  C CA   . TYR   A 1 17  ? 13.404 -12.686 10.076  1.00 11.37 ?  17  TYR   A CA   1 
ATOM   394  C C    . TYR   A 1 17  ? 13.145 -11.356 9.370   1.00 11.08 ?  17  TYR   A C    1 
ATOM   395  O O    . TYR   A 1 17  ? 14.056 -10.806 8.752   1.00 11.81 ?  17  TYR   A O    1 
ATOM   396  C CB   . TYR   A 1 17  ? 13.821 -12.425 11.533  1.00 11.99 ?  17  TYR   A CB   1 
ATOM   397  C CG   . TYR   A 1 17  ? 14.017 -13.692 12.337  1.00 12.74 ?  17  TYR   A CG   1 
ATOM   398  C CD1  . TYR   A 1 17  ? 15.189 -14.445 12.248  1.00 14.10 ?  17  TYR   A CD1  1 
ATOM   399  C CD2  . TYR   A 1 17  ? 13.012 -14.149 13.173  1.00 13.61 ?  17  TYR   A CD2  1 
ATOM   400  C CE1  . TYR   A 1 17  ? 15.347 -15.624 12.981  1.00 14.71 ?  17  TYR   A CE1  1 
ATOM   401  C CE2  . TYR   A 1 17  ? 13.156 -15.329 13.903  1.00 14.44 ?  17  TYR   A CE2  1 
ATOM   402  C CZ   . TYR   A 1 17  ? 14.327 -16.056 13.809  1.00 14.63 ?  17  TYR   A CZ   1 
ATOM   403  O OH   . TYR   A 1 17  ? 14.469 -17.221 14.535  1.00 15.66 ?  17  TYR   A OH   1 
ATOM   404  H H    A TYR   A 1 17  ? 15.192 -12.861 9.295   0.62 13.79 ?  17  TYR   A H    1 
ATOM   405  H H    B TYR   A 1 17  ? 15.184 -12.854 9.276   0.38 13.79 ?  17  TYR   A H    1 
ATOM   406  H HA   . TYR   A 1 17  ? 12.604 -13.230 10.055  1.00 13.66 ?  17  TYR   A HA   1 
ATOM   407  H HB2  . TYR   A 1 17  ? 14.657 -11.935 11.534  1.00 14.40 ?  17  TYR   A HB2  1 
ATOM   408  H HB3  . TYR   A 1 17  ? 13.132 -11.903 11.960  1.00 14.40 ?  17  TYR   A HB3  1 
ATOM   409  H HD1  . TYR   A 1 17  ? 15.879 -14.162 11.690  1.00 16.94 ?  17  TYR   A HD1  1 
ATOM   410  H HD2  . TYR   A 1 17  ? 12.217 -13.670 13.238  1.00 16.34 ?  17  TYR   A HD2  1 
ATOM   411  H HE1  . TYR   A 1 17  ? 16.136 -16.117 12.916  1.00 17.67 ?  17  TYR   A HE1  1 
ATOM   412  H HE2  . TYR   A 1 17  ? 12.469 -15.617 14.461  1.00 17.35 ?  17  TYR   A HE2  1 
ATOM   413  H HH   . TYR   A 1 17  ? 13.745 -17.403 14.920  1.00 18.81 ?  17  TYR   A HH   1 
ATOM   414  N N    A ILE   A 1 18  ? 11.900 -10.866 9.410   0.62 10.95 ?  18  ILE   A N    1 
ATOM   415  N N    B ILE   A 1 18  ? 11.944 -10.781 9.551   0.38 10.53 ?  18  ILE   A N    1 
ATOM   416  C CA   A ILE   A 1 18  ? 11.522 -9.690  8.628   0.62 10.60 ?  18  ILE   A CA   1 
ATOM   417  C CA   B ILE   A 1 18  ? 11.578 -9.543  8.855   0.38 9.78  ?  18  ILE   A CA   1 
ATOM   418  C C    A ILE   A 1 18  ? 10.512 -8.845  9.398   0.62 11.39 ?  18  ILE   A C    1 
ATOM   419  C C    B ILE   A 1 18  ? 10.667 -8.667  9.715   0.38 9.33  ?  18  ILE   A C    1 
ATOM   420  O O    A ILE   A 1 18  ? 9.679  -9.365  10.145  0.62 11.42 ?  18  ILE   A O    1 
ATOM   421  O O    B ILE   A 1 18  ? 9.853  -9.163  10.498  0.38 9.60  ?  18  ILE   A O    1 
ATOM   422  C CB   A ILE   A 1 18  ? 11.009 -10.107 7.225   0.62 10.68 ?  18  ILE   A CB   1 
ATOM   423  C CB   B ILE   A 1 18  ? 10.929 -9.859  7.488   0.38 10.05 ?  18  ILE   A CB   1 
ATOM   424  C CG1  A ILE   A 1 18  ? 10.991 -8.909  6.276   0.62 10.85 ?  18  ILE   A CG1  1 
ATOM   425  C CG1  B ILE   A 1 18  ? 10.904 -8.614  6.599   0.38 11.00 ?  18  ILE   A CG1  1 
ATOM   426  C CG2  A ILE   A 1 18  ? 9.649  -10.797 7.308   0.62 10.46 ?  18  ILE   A CG2  1 
ATOM   427  C CG2  B ILE   A 1 18  ? 9.533  -10.458 7.669   0.38 10.43 ?  18  ILE   A CG2  1 
ATOM   428  C CD1  A ILE   A 1 18  ? 10.789 -9.288  4.835   0.62 11.68 ?  18  ILE   A CD1  1 
ATOM   429  C CD1  B ILE   A 1 18  ? 10.552 -8.918  5.163   0.38 12.39 ?  18  ILE   A CD1  1 
ATOM   430  H H    A ILE   A 1 18  ? 11.261 -11.205 9.879   0.62 13.15 ?  18  ILE   A H    1 
ATOM   431  H H    B ILE   A 1 18  ? 11.334 -11.093 10.075  0.38 12.66 ?  18  ILE   A H    1 
ATOM   432  H HA   A ILE   A 1 18  ? 12.324 -9.153  8.494   0.62 12.74 ?  18  ILE   A HA   1 
ATOM   433  H HA   B ILE   A 1 18  ? 12.393 -9.042  8.691   0.38 11.75 ?  18  ILE   A HA   1 
ATOM   434  H HB   A ILE   A 1 18  ? 11.641 -10.752 6.862   0.62 12.83 ?  18  ILE   A HB   1 
ATOM   435  H HB   B ILE   A 1 18  ? 11.482 -10.519 7.057   0.38 12.08 ?  18  ILE   A HB   1 
ATOM   436  H HG12 A ILE   A 1 18  ? 10.274 -8.315  6.532   0.62 13.04 ?  18  ILE   A HG12 1 
ATOM   437  H HG12 B ILE   A 1 18  ? 10.248 -7.989  6.940   0.38 13.22 ?  18  ILE   A HG12 1 
ATOM   438  H HG13 A ILE   A 1 18  ? 11.844 -8.444  6.339   0.62 13.04 ?  18  ILE   A HG13 1 
ATOM   439  H HG13 B ILE   A 1 18  ? 11.786 -8.202  6.606   0.38 13.22 ?  18  ILE   A HG13 1 
ATOM   440  H HG21 A ILE   A 1 18  ? 9.444  -11.187 6.440   0.62 12.56 ?  18  ILE   A HG21 1 
ATOM   441  H HG21 B ILE   A 1 18  ? 9.233  -10.806 6.814   0.38 12.53 ?  18  ILE   A HG21 1 
ATOM   442  H HG22 A ILE   A 1 18  ? 9.691  -11.492 7.980   0.62 12.56 ?  18  ILE   A HG22 1 
ATOM   443  H HG22 B ILE   A 1 18  ? 9.579  -11.175 8.319   0.38 12.53 ?  18  ILE   A HG22 1 
ATOM   444  H HG23 A ILE   A 1 18  ? 8.978  -10.142 7.542   0.62 12.56 ?  18  ILE   A HG23 1 
ATOM   445  H HG23 B ILE   A 1 18  ? 8.924  -9.769  7.977   0.38 12.53 ?  18  ILE   A HG23 1 
ATOM   446  H HD11 A ILE   A 1 18  ? 10.846 -8.484  4.287   0.62 14.03 ?  18  ILE   A HD11 1 
ATOM   447  H HD11 B ILE   A 1 18  ? 10.611 -8.101  4.642   0.38 14.88 ?  18  ILE   A HD11 1 
ATOM   448  H HD12 A ILE   A 1 18  ? 11.474 -9.916  4.569   0.62 14.03 ?  18  ILE   A HD12 1 
ATOM   449  H HD12 B ILE   A 1 18  ? 11.178 -9.575  4.815   0.38 14.88 ?  18  ILE   A HD12 1 
ATOM   450  H HD13 A ILE   A 1 18  ? 9.911  -9.688  4.735   0.62 14.03 ?  18  ILE   A HD13 1 
ATOM   451  H HD13 B ILE   A 1 18  ? 9.650  -9.270  5.126   0.38 14.88 ?  18  ILE   A HD13 1 
ATOM   452  N N    A LYS   A 1 19  ? 10.590 -7.527  9.203   0.62 11.80 ?  19  LYS   A N    1 
ATOM   453  N N    B LYS   A 1 19  ? 10.794 -7.345  9.533   0.38 9.05  ?  19  LYS   A N    1 
ATOM   454  C CA   A LYS   A 1 19  ? 9.789  -6.576  9.967   0.62 12.92 ?  19  LYS   A CA   1 
ATOM   455  C CA   B LYS   A 1 19  ? 9.988  -6.359  10.248  0.38 9.93  ?  19  LYS   A CA   1 
ATOM   456  C C    A LYS   A 1 19  ? 9.632  -5.304  9.145   0.62 12.77 ?  19  LYS   A C    1 
ATOM   457  C C    B LYS   A 1 19  ? 9.780  -5.128  9.370   0.38 10.36 ?  19  LYS   A C    1 
ATOM   458  O O    A LYS   A 1 19  ? 10.546 -4.923  8.411   0.62 13.16 ?  19  LYS   A O    1 
ATOM   459  O O    B LYS   A 1 19  ? 10.666 -4.748  8.601   0.38 10.54 ?  19  LYS   A O    1 
ATOM   460  C CB   A LYS   A 1 19  ? 10.507 -6.251  11.286  0.62 14.61 ?  19  LYS   A CB   1 
ATOM   461  C CB   B LYS   A 1 19  ? 10.672 -5.928  11.554  0.38 10.30 ?  19  LYS   A CB   1 
ATOM   462  C CG   A LYS   A 1 19  ? 9.826  -5.260  12.237  0.62 15.92 ?  19  LYS   A CG   1 
ATOM   463  C CG   B LYS   A 1 19  ? 9.808  -5.089  12.468  0.38 11.82 ?  19  LYS   A CG   1 
ATOM   464  C CD   A LYS   A 1 19  ? 10.721 -5.025  13.464  0.62 17.01 ?  19  LYS   A CD   1 
ATOM   465  C CD   B LYS   A 1 19  ? 10.592 -4.643  13.680  0.38 13.57 ?  19  LYS   A CD   1 
ATOM   466  C CE   A LYS   A 1 19  ? 10.114 -4.080  14.498  0.62 17.48 ?  19  LYS   A CE   1 
ATOM   467  C CE   B LYS   A 1 19  ? 9.751  -3.779  14.595  0.38 14.73 ?  19  LYS   A CE   1 
ATOM   468  N NZ   A LYS   A 1 19  ? 11.034 -3.874  15.665  0.62 17.05 ?  19  LYS   A NZ   1 
ATOM   469  N NZ   B LYS   A 1 19  ? 10.543 -3.336  15.767  0.38 14.95 ?  19  LYS   A NZ   1 
ATOM   470  H H    A LYS   A 1 19  ? 11.116 -7.160  8.624   0.62 14.17 ?  19  LYS   A H    1 
ATOM   471  H H    B LYS   A 1 19  ? 11.365 -6.982  8.990   0.38 10.87 ?  19  LYS   A H    1 
ATOM   472  H HA   A LYS   A 1 19  ? 8.918  -6.959  10.152  0.62 15.52 ?  19  LYS   A HA   1 
ATOM   473  H HA   B LYS   A 1 19  ? 9.125  -6.731  10.465  0.38 11.93 ?  19  LYS   A HA   1 
ATOM   474  H HB2  A LYS   A 1 19  ? 10.618 -7.081  11.775  0.62 17.55 ?  19  LYS   A HB2  1 
ATOM   475  H HB2  B LYS   A 1 19  ? 10.926 -6.723  12.052  0.38 12.38 ?  19  LYS   A HB2  1 
ATOM   476  H HB3  A LYS   A 1 19  ? 11.377 -5.888  11.070  0.62 17.55 ?  19  LYS   A HB3  1 
ATOM   477  H HB3  B LYS   A 1 19  ? 11.464 -5.409  11.346  0.38 12.38 ?  19  LYS   A HB3  1 
ATOM   478  H HG2  A LYS   A 1 19  ? 9.690  -4.412  11.785  0.62 19.12 ?  19  LYS   A HG2  1 
ATOM   479  H HG2  B LYS   A 1 19  ? 9.505  -4.301  11.995  0.38 14.20 ?  19  LYS   A HG2  1 
ATOM   480  H HG3  A LYS   A 1 19  ? 8.977  -5.623  12.539  0.62 19.12 ?  19  LYS   A HG3  1 
ATOM   481  H HG3  B LYS   A 1 19  ? 9.051  -5.616  12.771  0.38 14.20 ?  19  LYS   A HG3  1 
ATOM   482  H HD2  A LYS   A 1 19  ? 10.883 -5.874  13.901  0.62 20.43 ?  19  LYS   A HD2  1 
ATOM   483  H HD2  B LYS   A 1 19  ? 10.880 -5.425  14.179  0.38 16.29 ?  19  LYS   A HD2  1 
ATOM   484  H HD3  A LYS   A 1 19  ? 11.560 -4.639  13.169  0.62 20.43 ?  19  LYS   A HD3  1 
ATOM   485  H HD3  B LYS   A 1 19  ? 11.360 -4.127  13.391  0.38 16.29 ?  19  LYS   A HD3  1 
ATOM   486  H HE2  A LYS   A 1 19  ? 9.950  -3.214  14.089  0.62 20.99 ?  19  LYS   A HE2  1 
ATOM   487  H HE2  B LYS   A 1 19  ? 9.451  -2.995  14.109  0.38 17.69 ?  19  LYS   A HE2  1 
ATOM   488  H HE3  A LYS   A 1 19  ? 9.284  -4.454  14.832  0.62 20.99 ?  19  LYS   A HE3  1 
ATOM   489  H HE3  B LYS   A 1 19  ? 8.990  -4.291  14.912  0.38 17.69 ?  19  LYS   A HE3  1 
ATOM   490  H HZ1  A LYS   A 1 19  ? 10.696 -3.266  16.219  0.62 20.48 ?  19  LYS   A HZ1  1 
ATOM   491  H HZ1  B LYS   A 1 19  ? 10.040 -2.828  16.297  0.38 17.95 ?  19  LYS   A HZ1  1 
ATOM   492  H HZ2  A LYS   A 1 19  ? 11.140 -4.641  16.106  0.62 20.48 ?  19  LYS   A HZ2  1 
ATOM   493  H HZ2  B LYS   A 1 19  ? 10.827 -4.042  16.226  0.38 17.95 ?  19  LYS   A HZ2  1 
ATOM   494  H HZ3  A LYS   A 1 19  ? 11.829 -3.595  15.380  0.62 20.48 ?  19  LYS   A HZ3  1 
ATOM   495  H HZ3  B LYS   A 1 19  ? 11.246 -2.862  15.496  0.38 17.95 ?  19  LYS   A HZ3  1 
ATOM   496  N N    A ASN   A 1 20  ? 8.472  -4.650  9.270   0.62 13.14 ?  20  ASN   A N    1 
ATOM   497  N N    B ASN   A 1 20  ? 8.603  -4.499  9.500   0.38 10.72 ?  20  ASN   A N    1 
ATOM   498  C CA   A ASN   A 1 20  ? 8.289  -3.309  8.712   0.62 14.09 ?  20  ASN   A CA   1 
ATOM   499  C CA   B ASN   A 1 20  ? 8.298  -3.224  8.837   0.38 11.08 ?  20  ASN   A CA   1 
ATOM   500  C C    A ASN   A 1 20  ? 8.918  -2.312  9.680   0.62 14.47 ?  20  ASN   A C    1 
ATOM   501  C C    B ASN   A 1 20  ? 8.831  -2.098  9.723   0.38 11.66 ?  20  ASN   A C    1 
ATOM   502  O O    A ASN   A 1 20  ? 8.400  -2.095  10.782  0.62 14.70 ?  20  ASN   A O    1 
ATOM   503  O O    B ASN   A 1 20  ? 8.153  -1.626  10.638  0.38 11.97 ?  20  ASN   A O    1 
ATOM   504  C CB   A ASN   A 1 20  ? 6.804  -3.027  8.487   0.62 14.69 ?  20  ASN   A CB   1 
ATOM   505  C CB   B ASN   A 1 20  ? 6.790  -3.104  8.604   0.38 11.03 ?  20  ASN   A CB   1 
ATOM   506  C CG   A ASN   A 1 20  ? 6.513  -1.574  8.110   0.62 15.72 ?  20  ASN   A CG   1 
ATOM   507  C CG   B ASN   A 1 20  ? 6.376  -1.833  7.834   0.38 11.01 ?  20  ASN   A CG   1 
ATOM   508  O OD1  A ASN   A 1 20  ? 5.513  -1.012  8.547   0.62 18.24 ?  20  ASN   A OD1  1 
ATOM   509  O OD1  B ASN   A 1 20  ? 5.211  -1.405  7.908   0.38 10.37 ?  20  ASN   A OD1  1 
ATOM   510  N ND2  A ASN   A 1 20  ? 7.370  -0.973  7.294   0.62 15.08 ?  20  ASN   A ND2  1 
ATOM   511  N ND2  B ASN   A 1 20  ? 7.306  -1.245  7.086   0.38 11.96 ?  20  ASN   A ND2  1 
ATOM   512  H H    A ASN   A 1 20  ? 7.779  -4.966  9.669   0.62 15.78 ?  20  ASN   A H    1 
ATOM   513  H H    B ASN   A 1 20  ? 7.953  -4.806  9.966   0.38 12.88 ?  20  ASN   A H    1 
ATOM   514  H HA   A ASN   A 1 20  ? 8.751  -3.252  7.861   0.62 16.92 ?  20  ASN   A HA   1 
ATOM   515  H HA   B ASN   A 1 20  ? 8.756  -3.196  7.982   0.38 13.32 ?  20  ASN   A HA   1 
ATOM   516  H HB2  A ASN   A 1 20  ? 6.484  -3.591  7.768   0.62 17.64 ?  20  ASN   A HB2  1 
ATOM   517  H HB2  B ASN   A 1 20  ? 6.490  -3.873  8.099   0.38 13.25 ?  20  ASN   A HB2  1 
ATOM   518  H HB3  A ASN   A 1 20  ? 6.323  -3.230  9.303   0.62 17.64 ?  20  ASN   A HB3  1 
ATOM   519  H HB3  B ASN   A 1 20  ? 6.346  -3.086  9.464   0.38 13.25 ?  20  ASN   A HB3  1 
ATOM   520  H HD21 A ASN   A 1 20  ? 7.239  -0.162  7.059   0.62 18.11 ?  20  ASN   A HD21 1 
ATOM   521  H HD21 B ASN   A 1 20  ? 7.112  -0.539  6.644   0.38 14.36 ?  20  ASN   A HD21 1 
ATOM   522  H HD22 A ASN   A 1 20  ? 8.062  -1.402  7.004   0.62 18.11 ?  20  ASN   A HD22 1 
ATOM   523  H HD22 B ASN   A 1 20  ? 8.102  -1.572  7.041   0.38 14.36 ?  20  ASN   A HD22 1 
ATOM   524  N N    A ALA   A 1 21  ? 10.050 -1.728  9.289   0.62 14.76 ?  21  ALA   A N    1 
ATOM   525  N N    B ALA   A 1 21  ? 10.065 -1.664  9.452   0.38 12.30 ?  21  ALA   A N    1 
ATOM   526  C CA   A ALA   A 1 21  ? 10.771 -0.847  10.194  0.62 14.69 ?  21  ALA   A CA   1 
ATOM   527  C CA   B ALA   A 1 21  ? 10.720 -0.663  10.287  0.38 12.89 ?  21  ALA   A CA   1 
ATOM   528  C C    A ALA   A 1 21  ? 11.726 0.035   9.409   0.62 14.19 ?  21  ALA   A C    1 
ATOM   529  C C    B ALA   A 1 21  ? 11.868 -0.016  9.524   0.38 11.97 ?  21  ALA   A C    1 
ATOM   530  O O    A ALA   A 1 21  ? 12.199 -0.336  8.330   0.62 14.32 ?  21  ALA   A O    1 
ATOM   531  O O    B ALA   A 1 21  ? 12.379 -0.565  8.544   0.38 12.14 ?  21  ALA   A O    1 
ATOM   532  C CB   A ALA   A 1 21  ? 11.554 -1.640  11.242  0.62 14.74 ?  21  ALA   A CB   1 
ATOM   533  C CB   B ALA   A 1 21  ? 11.231 -1.274  11.598  0.38 13.84 ?  21  ALA   A CB   1 
ATOM   534  H H    A ALA   A 1 21  ? 10.413 -1.829  8.516   0.62 17.73 ?  21  ALA   A H    1 
ATOM   535  H H    B ALA   A 1 21  ? 10.540 -1.935  8.790   0.38 14.77 ?  21  ALA   A H    1 
ATOM   536  H HA   A ALA   A 1 21  ? 10.129 -0.279  10.655  0.62 17.65 ?  21  ALA   A HA   1 
ATOM   537  H HA   B ALA   A 1 21  ? 10.081 0.030   10.511  0.38 15.48 ?  21  ALA   A HA   1 
ATOM   538  H HB1  A ALA   A 1 21  ? 11.992 -1.015  11.838  0.62 17.71 ?  21  ALA   A HB1  1 
ATOM   539  H HB1  B ALA   A 1 21  ? 11.659 -0.579  12.124  0.38 16.63 ?  21  ALA   A HB1  1 
ATOM   540  H HB2  A ALA   A 1 21  ? 10.936 -2.197  11.743  0.62 17.71 ?  21  ALA   A HB2  1 
ATOM   541  H HB2  B ALA   A 1 21  ? 10.480 -1.644  12.089  0.38 16.63 ?  21  ALA   A HB2  1 
ATOM   542  H HB3  A ALA   A 1 21  ? 12.209 -2.192  10.793  0.62 17.71 ?  21  ALA   A HB3  1 
ATOM   543  H HB3  B ALA   A 1 21  ? 11.870 -1.974  11.393  0.38 16.63 ?  21  ALA   A HB3  1 
ATOM   544  N N    A ASP   A 1 22  ? 11.983 1.214   9.973   0.62 14.39 ?  22  ASP   A N    1 
ATOM   545  N N    B ASP   A 1 22  ? 12.254 1.173   9.996   0.38 12.02 ?  22  ASP   A N    1 
ATOM   546  C CA   A ASP   A 1 22  ? 13.040 2.104   9.514   0.62 14.17 ?  22  ASP   A CA   1 
ATOM   547  C CA   B ASP   A 1 22  ? 13.427 1.887   9.504   0.38 11.97 ?  22  ASP   A CA   1 
ATOM   548  C C    A ASP   A 1 22  ? 14.360 1.607   10.095  0.62 12.92 ?  22  ASP   A C    1 
ATOM   549  C C    B ASP   A 1 22  ? 14.673 1.236   10.094  0.38 10.70 ?  22  ASP   A C    1 
ATOM   550  O O    A ASP   A 1 22  ? 14.537 1.593   11.318  0.62 13.21 ?  22  ASP   A O    1 
ATOM   551  O O    B ASP   A 1 22  ? 14.782 1.085   11.315  0.38 10.80 ?  22  ASP   A O    1 
ATOM   552  C CB   A ASP   A 1 22  ? 12.717 3.517   9.999   0.62 16.18 ?  22  ASP   A CB   1 
ATOM   553  C CB   B ASP   A 1 22  ? 13.346 3.348   9.964   0.38 13.08 ?  22  ASP   A CB   1 
ATOM   554  C CG   A ASP   A 1 22  ? 13.761 4.547   9.585   0.62 18.29 ?  22  ASP   A CG   1 
ATOM   555  C CG   B ASP   A 1 22  ? 14.361 4.255   9.282   0.38 13.78 ?  22  ASP   A CG   1 
ATOM   556  O OD1  A ASP   A 1 22  ? 14.889 4.179   9.205   0.62 18.69 ?  22  ASP   A OD1  1 
ATOM   557  O OD1  B ASP   A 1 22  ? 15.343 3.738   8.710   0.38 12.85 ?  22  ASP   A OD1  1 
ATOM   558  O OD2  A ASP   A 1 22  ? 13.449 5.753   9.654   0.62 19.95 -1 22  ASP   A OD2  1 
ATOM   559  O OD2  B ASP   A 1 22  ? 14.182 5.493   9.340   0.38 15.09 -1 22  ASP   A OD2  1 
ATOM   560  H H    A ASP   A 1 22  ? 11.540 1.526   10.644  0.62 17.29 ?  22  ASP   A H    1 
ATOM   561  H H    B ASP   A 1 22  ? 11.839 1.594   10.621  0.38 14.44 ?  22  ASP   A H    1 
ATOM   562  H HA   A ASP   A 1 22  ? 13.091 2.098   8.547   0.62 17.02 ?  22  ASP   A HA   1 
ATOM   563  H HA   B ASP   A 1 22  ? 13.467 1.847   8.534   0.38 14.38 ?  22  ASP   A HA   1 
ATOM   564  H HB2  A ASP   A 1 22  ? 11.860 3.789   9.623   0.62 19.43 ?  22  ASP   A HB2  1 
ATOM   565  H HB2  B ASP   A 1 22  ? 12.464 3.689   9.771   0.38 15.71 ?  22  ASP   A HB2  1 
ATOM   566  H HB3  A ASP   A 1 22  ? 12.655 3.511   10.969  0.62 19.43 ?  22  ASP   A HB3  1 
ATOM   567  H HB3  B ASP   A 1 22  ? 13.524 3.386   10.914  0.38 15.71 ?  22  ASP   A HB3  1 
ATOM   568  N N    A ILE   A 1 23  ? 15.278 1.188   9.220   0.62 12.80 ?  23  ILE   A N    1 
ATOM   569  N N    B ILE   A 1 23  ? 15.607 0.833   9.228   0.38 9.81  ?  23  ILE   A N    1 
ATOM   570  C CA   A ILE   A 1 23  ? 16.526 0.577   9.677   0.62 12.19 ?  23  ILE   A CA   1 
ATOM   571  C CA   B ILE   A 1 23  ? 16.838 0.205   9.704   0.38 9.67  ?  23  ILE   A CA   1 
ATOM   572  C C    A ILE   A 1 23  ? 17.318 1.524   10.570  0.62 12.21 ?  23  ILE   A C    1 
ATOM   573  C C    B ILE   A 1 23  ? 17.592 1.132   10.652  0.38 9.73  ?  23  ILE   A C    1 
ATOM   574  O O    A ILE   A 1 23  ? 18.021 1.079   11.483  0.62 12.83 ?  23  ILE   A O    1 
ATOM   575  O O    B ILE   A 1 23  ? 18.259 0.669   11.586  0.38 9.76  ?  23  ILE   A O    1 
ATOM   576  C CB   A ILE   A 1 23  ? 17.349 0.062   8.475   0.62 11.81 ?  23  ILE   A CB   1 
ATOM   577  C CB   B ILE   A 1 23  ? 17.709 -0.288  8.523   0.38 9.69  ?  23  ILE   A CB   1 
ATOM   578  C CG1  A ILE   A 1 23  ? 18.463 -0.881  8.946   0.62 12.04 ?  23  ILE   A CG1  1 
ATOM   579  C CG1  B ILE   A 1 23  ? 18.803 -1.243  9.026   0.38 9.82  ?  23  ILE   A CG1  1 
ATOM   580  C CG2  A ILE   A 1 23  ? 17.894 1.225   7.643   0.62 12.07 ?  23  ILE   A CG2  1 
ATOM   581  C CG2  B ILE   A 1 23  ? 18.318 0.883   7.749   0.38 10.07 ?  23  ILE   A CG2  1 
ATOM   582  C CD1  A ILE   A 1 23  ? 19.198 -1.568  7.814   0.62 12.07 ?  23  ILE   A CD1  1 
ATOM   583  C CD1  B ILE   A 1 23  ? 19.610 -1.920  7.923   0.38 10.22 ?  23  ILE   A CD1  1 
ATOM   584  H H    A ILE   A 1 23  ? 15.203 1.247   8.369   0.62 15.38 ?  23  ILE   A H    1 
ATOM   585  H H    B ILE   A 1 23  ? 15.551 0.907   8.379   0.38 11.79 ?  23  ILE   A H    1 
ATOM   586  H HA   A ILE   A 1 23  ? 16.306 -0.195  10.218  0.62 14.64 ?  23  ILE   A HA   1 
ATOM   587  H HA   B ILE   A 1 23  ? 16.588 -0.580  10.209  0.38 11.63 ?  23  ILE   A HA   1 
ATOM   588  H HB   A ILE   A 1 23  ? 16.754 -0.448  7.909   0.62 14.19 ?  23  ILE   A HB   1 
ATOM   589  H HB   B ILE   A 1 23  ? 17.142 -0.785  7.914   0.38 11.64 ?  23  ILE   A HB   1 
ATOM   590  H HG12 A ILE   A 1 23  ? 19.115 -0.374  9.455   0.62 14.46 ?  23  ILE   A HG12 1 
ATOM   591  H HG12 B ILE   A 1 23  ? 19.422 -0.746  9.580   0.38 11.80 ?  23  ILE   A HG12 1 
ATOM   592  H HG13 A ILE   A 1 23  ? 18.074 -1.572  9.505   0.62 14.46 ?  23  ILE   A HG13 1 
ATOM   593  H HG13 B ILE   A 1 23  ? 18.383 -1.944  9.553   0.38 11.80 ?  23  ILE   A HG13 1 
ATOM   594  H HG21 A ILE   A 1 23  ? 18.252 0.878   6.809   0.62 14.50 ?  23  ILE   A HG21 1 
ATOM   595  H HG21 B ILE   A 1 23  ? 18.706 0.548   6.920   0.38 12.10 ?  23  ILE   A HG21 1 
ATOM   596  H HG22 A ILE   A 1 23  ? 17.168 1.844   7.454   0.62 14.50 ?  23  ILE   A HG22 1 
ATOM   597  H HG22 B ILE   A 1 23  ? 17.622 1.525   7.547   0.38 12.10 ?  23  ILE   A HG22 1 
ATOM   598  H HG23 A ILE   A 1 23  ? 18.592 1.677   8.139   0.62 14.50 ?  23  ILE   A HG23 1 
ATOM   599  H HG23 B ILE   A 1 23  ? 19.009 1.298   8.288   0.38 12.10 ?  23  ILE   A HG23 1 
ATOM   600  H HD11 A ILE   A 1 23  ? 19.832 -2.200  8.185   0.62 14.50 ?  23  ILE   A HD11 1 
ATOM   601  H HD11 B ILE   A 1 23  ? 20.229 -2.551  8.327   0.38 12.28 ?  23  ILE   A HD11 1 
ATOM   602  H HD12 A ILE   A 1 23  ? 18.554 -2.034  7.257   0.62 14.50 ?  23  ILE   A HD12 1 
ATOM   603  H HD12 B ILE   A 1 23  ? 19.004 -2.389  7.329   0.38 12.28 ?  23  ILE   A HD12 1 
ATOM   604  H HD13 A ILE   A 1 23  ? 19.666 -0.900  7.289   0.62 14.50 ?  23  ILE   A HD13 1 
ATOM   605  H HD13 B ILE   A 1 23  ? 20.102 -1.246  7.431   0.38 12.28 ?  23  ILE   A HD13 1 
ATOM   606  N N    A VAL   A 1 24  ? 17.207 2.835   10.341  0.62 12.43 ?  24  VAL   A N    1 
ATOM   607  N N    B VAL   A 1 24  ? 17.489 2.448   10.442  0.38 10.94 ?  24  VAL   A N    1 
ATOM   608  C CA   A VAL   A 1 24  ? 17.883 3.800   11.208  0.62 13.89 ?  24  VAL   A CA   1 
ATOM   609  C CA   B VAL   A 1 24  ? 18.141 3.405   11.335  0.38 12.15 ?  24  VAL   A CA   1 
ATOM   610  C C    A VAL   A 1 24  ? 17.340 3.710   12.625  0.62 14.94 ?  24  VAL   A C    1 
ATOM   611  C C    B VAL   A 1 24  ? 17.558 3.309   12.741  0.38 12.58 ?  24  VAL   A C    1 
ATOM   612  O O    A VAL   A 1 24  ? 18.097 3.647   13.601  0.62 15.44 ?  24  VAL   A O    1 
ATOM   613  O O    B VAL   A 1 24  ? 18.292 3.308   13.738  0.38 13.18 ?  24  VAL   A O    1 
ATOM   614  C CB   A VAL   A 1 24  ? 17.744 5.225   10.642  0.62 14.73 ?  24  VAL   A CB   1 
ATOM   615  C CB   B VAL   A 1 24  ? 18.030 4.830   10.758  0.38 13.78 ?  24  VAL   A CB   1 
ATOM   616  C CG1  A VAL   A 1 24  ? 18.281 6.261   11.639  0.62 15.50 ?  24  VAL   A CG1  1 
ATOM   617  C CG1  B VAL   A 1 24  ? 18.569 5.855   11.742  0.38 14.98 ?  24  VAL   A CG1  1 
ATOM   618  C CG2  A VAL   A 1 24  ? 18.452 5.334   9.307   0.62 15.49 ?  24  VAL   A CG2  1 
ATOM   619  C CG2  B VAL   A 1 24  ? 18.768 4.921   9.426   0.38 14.50 ?  24  VAL   A CG2  1 
ATOM   620  H H    A VAL   A 1 24  ? 16.753 3.186   9.701   0.62 14.93 ?  24  VAL   A H    1 
ATOM   621  H H    B VAL   A 1 24  ? 17.056 2.806   9.796   0.38 13.15 ?  24  VAL   A H    1 
ATOM   622  H HA   A VAL   A 1 24  ? 18.827 3.589   11.241  0.62 16.68 ?  24  VAL   A HA   1 
ATOM   623  H HA   B VAL   A 1 24  ? 19.084 3.186   11.393  0.38 14.59 ?  24  VAL   A HA   1 
ATOM   624  H HB   A VAL   A 1 24  ? 16.804 5.418   10.496  0.62 17.70 ?  24  VAL   A HB   1 
ATOM   625  H HB   B VAL   A 1 24  ? 17.096 5.034   10.593  0.38 16.55 ?  24  VAL   A HB   1 
ATOM   626  H HG11 A VAL   A 1 24  ? 18.421 7.101   11.175  0.62 18.61 ?  24  VAL   A HG11 1 
ATOM   627  H HG11 B VAL   A 1 24  ? 18.743 6.685   11.269  0.38 17.99 ?  24  VAL   A HG11 1 
ATOM   628  H HG12 A VAL   A 1 24  ? 17.638 6.380   12.353  0.62 18.61 ?  24  VAL   A HG12 1 
ATOM   629  H HG12 B VAL   A 1 24  ? 17.904 6.002   12.430  0.38 17.99 ?  24  VAL   A HG12 1 
ATOM   630  H HG13 A VAL   A 1 24  ? 19.125 5.941   12.000  0.62 18.61 ?  24  VAL   A HG13 1 
ATOM   631  H HG13 B VAL   A 1 24  ? 19.390 5.519   12.132  0.38 17.99 ?  24  VAL   A HG13 1 
ATOM   632  H HG21 A VAL   A 1 24  ? 18.299 6.218   8.939   0.62 18.61 ?  24  VAL   A HG21 1 
ATOM   633  H HG21 B VAL   A 1 24  ? 18.679 5.820   9.074   0.38 17.42 ?  24  VAL   A HG21 1 
ATOM   634  H HG22 A VAL   A 1 24  ? 19.403 5.194   9.442   0.62 18.61 ?  24  VAL   A HG22 1 
ATOM   635  H HG22 B VAL   A 1 24  ? 19.705 4.714   9.569   0.38 17.42 ?  24  VAL   A HG22 1 
ATOM   636  H HG23 A VAL   A 1 24  ? 18.100 4.660   8.704   0.62 18.61 ?  24  VAL   A HG23 1 
ATOM   637  H HG23 B VAL   A 1 24  ? 18.381 4.283   8.804   0.38 17.42 ?  24  VAL   A HG23 1 
ATOM   638  N N    A GLU   A 1 25  ? 16.013 3.729   12.761  0.62 15.45 ?  25  GLU   A N    1 
ATOM   639  N N    B GLU   A 1 25  ? 16.228 3.221   12.840  0.38 12.96 ?  25  GLU   A N    1 
ATOM   640  C CA   A GLU   A 1 25  ? 15.411 3.680   14.089  0.62 16.40 ?  25  GLU   A CA   1 
ATOM   641  C CA   B GLU   A 1 25  ? 15.575 3.117   14.141  0.38 14.55 ?  25  GLU   A CA   1 
ATOM   642  C C    A GLU   A 1 25  ? 15.641 2.326   14.751  0.62 15.44 ?  25  GLU   A C    1 
ATOM   643  C C    B GLU   A 1 25  ? 15.859 1.771   14.799  0.38 13.47 ?  25  GLU   A C    1 
ATOM   644  O O    A GLU   A 1 25  ? 15.839 2.250   15.969  0.62 16.46 ?  25  GLU   A O    1 
ATOM   645  O O    B GLU   A 1 25  ? 16.095 1.705   16.011  0.38 13.43 ?  25  GLU   A O    1 
ATOM   646  C CB   A GLU   A 1 25  ? 13.924 4.024   14.001  0.62 18.92 ?  25  GLU   A CB   1 
ATOM   647  C CB   B GLU   A 1 25  ? 14.071 3.350   13.983  0.38 16.39 ?  25  GLU   A CB   1 
ATOM   648  C CG   A GLU   A 1 25  ? 13.668 5.495   13.684  0.62 22.06 ?  25  GLU   A CG   1 
ATOM   649  C CG   B GLU   A 1 25  ? 13.727 4.734   13.466  0.38 19.03 ?  25  GLU   A CG   1 
ATOM   650  C CD   A GLU   A 1 25  ? 14.492 6.442   14.546  0.62 24.55 ?  25  GLU   A CD   1 
ATOM   651  C CD   B GLU   A 1 25  ? 14.159 5.823   14.424  0.38 21.44 ?  25  GLU   A CD   1 
ATOM   652  O OE1  A GLU   A 1 25  ? 14.599 6.201   15.767  0.62 25.07 ?  25  GLU   A OE1  1 
ATOM   653  O OE1  B GLU   A 1 25  ? 14.076 5.605   15.653  0.38 22.05 ?  25  GLU   A OE1  1 
ATOM   654  O OE2  A GLU   A 1 25  ? 15.055 7.414   13.995  0.62 25.75 -1 25  GLU   A OE2  1 
ATOM   655  O OE2  B GLU   A 1 25  ? 14.590 6.893   13.950  0.38 22.74 -1 25  GLU   A OE2  1 
ATOM   656  H H    A GLU   A 1 25  ? 15.449 3.793   12.108  0.62 18.56 ?  25  GLU   A H    1 
ATOM   657  H H    B GLU   A 1 25  ? 15.690 3.215   12.173  0.38 15.57 ?  25  GLU   A H    1 
ATOM   658  H HA   A GLU   A 1 25  ? 15.843 4.346   14.644  0.62 19.69 ?  25  GLU   A HA   1 
ATOM   659  H HA   B GLU   A 1 25  ? 15.925 3.803   14.725  0.38 17.48 ?  25  GLU   A HA   1 
ATOM   660  H HB2  A GLU   A 1 25  ? 13.511 3.499   13.294  0.62 22.72 ?  25  GLU   A HB2  1 
ATOM   661  H HB2  B GLU   A 1 25  ? 13.714 2.703   13.356  0.38 19.69 ?  25  GLU   A HB2  1 
ATOM   662  H HB3  A GLU   A 1 25  ? 13.497 3.828   14.849  0.62 22.72 ?  25  GLU   A HB3  1 
ATOM   663  H HB3  B GLU   A 1 25  ? 13.643 3.244   14.847  0.38 19.69 ?  25  GLU   A HB3  1 
ATOM   664  H HG2  A GLU   A 1 25  ? 13.906 5.667   12.762  0.62 26.49 ?  25  GLU   A HG2  1 
ATOM   665  H HG2  B GLU   A 1 25  ? 14.178 4.880   12.618  0.38 22.85 ?  25  GLU   A HG2  1 
ATOM   666  H HG3  A GLU   A 1 25  ? 12.728 5.693   13.831  0.62 26.49 ?  25  GLU   A HG3  1 
ATOM   667  H HG3  B GLU   A 1 25  ? 12.766 4.800   13.343  0.38 22.85 ?  25  GLU   A HG3  1 
ATOM   668  N N    A GLU   A 1 26  ? 15.634 1.248   13.964  0.62 15.48 ?  26  GLU   A N    1 
ATOM   669  N N    B GLU   A 1 26  ? 15.844 0.686   14.018  0.38 13.53 ?  26  GLU   A N    1 
ATOM   670  C CA   A GLU   A 1 26  ? 15.934 -0.070  14.514  0.62 15.40 ?  26  GLU   A CA   1 
ATOM   671  C CA   B GLU   A 1 26  ? 16.223 -0.614  14.565  0.38 13.27 ?  26  GLU   A CA   1 
ATOM   672  C C    A GLU   A 1 26  ? 17.361 -0.130  15.041  0.62 15.02 ?  26  GLU   A C    1 
ATOM   673  C C    B GLU   A 1 26  ? 17.646 -0.584  15.105  0.38 12.48 ?  26  GLU   A C    1 
ATOM   674  O O    A GLU   A 1 26  ? 17.609 -0.641  16.139  0.62 15.47 ?  26  GLU   A O    1 
ATOM   675  O O    B GLU   A 1 26  ? 17.920 -1.124  16.182  0.38 12.75 ?  26  GLU   A O    1 
ATOM   676  C CB   A GLU   A 1 26  ? 15.737 -1.139  13.441  0.62 16.37 ?  26  GLU   A CB   1 
ATOM   677  C CB   B GLU   A 1 26  ? 16.073 -1.706  13.500  0.38 14.62 ?  26  GLU   A CB   1 
ATOM   678  C CG   A GLU   A 1 26  ? 14.324 -1.641  13.290  0.62 19.11 ?  26  GLU   A CG   1 
ATOM   679  C CG   B GLU   A 1 26  ? 14.636 -2.044  13.146  0.38 15.97 ?  26  GLU   A CG   1 
ATOM   680  C CD   A GLU   A 1 26  ? 13.889 -2.505  14.458  0.62 20.83 ?  26  GLU   A CD   1 
ATOM   681  C CD   B GLU   A 1 26  ? 13.852 -2.582  14.322  0.38 16.39 ?  26  GLU   A CD   1 
ATOM   682  O OE1  A GLU   A 1 26  ? 14.375 -3.652  14.585  0.62 21.17 ?  26  GLU   A OE1  1 
ATOM   683  O OE1  B GLU   A 1 26  ? 14.297 -3.576  14.940  0.38 16.76 ?  26  GLU   A OE1  1 
ATOM   684  O OE2  A GLU   A 1 26  ? 13.069 -2.021  15.256  0.62 21.76 -1 26  GLU   A OE2  1 
ATOM   685  O OE2  B GLU   A 1 26  ? 12.793 -1.996  14.625  0.38 15.17 -1 26  GLU   A OE2  1 
ATOM   686  H H    A GLU   A 1 26  ? 15.450 1.264   13.123  0.62 18.60 ?  26  GLU   A H    1 
ATOM   687  H H    B GLU   A 1 26  ? 15.622 0.673   13.188  0.38 16.25 ?  26  GLU   A H    1 
ATOM   688  H HA   A GLU   A 1 26  ? 15.325 -0.245  15.246  0.62 18.49 ?  26  GLU   A HA   1 
ATOM   689  H HA   B GLU   A 1 26  ? 15.636 -0.838  15.300  0.38 15.94 ?  26  GLU   A HA   1 
ATOM   690  H HB2  A GLU   A 1 26  ? 16.013 -0.771  12.588  0.62 19.66 ?  26  GLU   A HB2  1 
ATOM   691  H HB2  B GLU   A 1 26  ? 16.510 -1.415  12.683  0.38 17.55 ?  26  GLU   A HB2  1 
ATOM   692  H HB3  A GLU   A 1 26  ? 16.297 -1.894  13.668  0.62 19.66 ?  26  GLU   A HB3  1 
ATOM   693  H HB3  B GLU   A 1 26  ? 16.495 -2.522  13.818  0.38 17.55 ?  26  GLU   A HB3  1 
ATOM   694  H HG2  A GLU   A 1 26  ? 13.726 -0.878  13.222  0.62 22.94 ?  26  GLU   A HG2  1 
ATOM   695  H HG2  B GLU   A 1 26  ? 14.189 -1.244  12.834  0.38 19.17 ?  26  GLU   A HG2  1 
ATOM   696  H HG3  A GLU   A 1 26  ? 14.265 -2.178  12.485  0.62 22.94 ?  26  GLU   A HG3  1 
ATOM   697  H HG3  B GLU   A 1 26  ? 14.624 -2.725  12.457  0.38 19.17 ?  26  GLU   A HG3  1 
ATOM   698  N N    A ALA   A 1 27  ? 18.318 0.379   14.261  0.62 14.17 ?  27  ALA   A N    1 
ATOM   699  N N    B ALA   A 1 27  ? 18.566 0.053   14.377  0.38 12.65 ?  27  ALA   A N    1 
ATOM   700  C CA   A ALA   A 1 27  ? 19.714 0.313   14.675  0.62 14.78 ?  27  ALA   A CA   1 
ATOM   701  C CA   B ALA   A 1 27  ? 19.936 0.151   14.866  0.38 13.86 ?  27  ALA   A CA   1 
ATOM   702  C C    A ALA   A 1 27  ? 19.934 1.060   15.983  0.62 16.01 ?  27  ALA   A C    1 
ATOM   703  C C    B ALA   A 1 27  ? 20.014 1.038   16.104  0.38 15.42 ?  27  ALA   A C    1 
ATOM   704  O O    A ALA   A 1 27  ? 20.614 0.560   16.887  0.62 16.05 ?  27  ALA   A O    1 
ATOM   705  O O    B ALA   A 1 27  ? 20.689 0.691   17.080  0.38 15.25 ?  27  ALA   A O    1 
ATOM   706  C CB   A ALA   A 1 27  ? 20.611 0.882   13.575  0.62 14.17 ?  27  ALA   A CB   1 
ATOM   707  C CB   B ALA   A 1 27  ? 20.859 0.660   13.755  0.38 13.65 ?  27  ALA   A CB   1 
ATOM   708  H H    A ALA   A 1 27  ? 18.181 0.765   13.502  0.62 17.02 ?  27  ALA   A H    1 
ATOM   709  H H    B ALA   A 1 27  ? 18.426 0.418   13.611  0.38 15.19 ?  27  ALA   A H    1 
ATOM   710  H HA   A ALA   A 1 27  ? 19.952 -0.611  14.814  0.62 17.76 ?  27  ALA   A HA   1 
ATOM   711  H HA   B ALA   A 1 27  ? 20.244 -0.734  15.114  0.38 16.64 ?  27  ALA   A HA   1 
ATOM   712  H HB1  A ALA   A 1 27  ? 21.534 0.829   13.865  0.62 17.02 ?  27  ALA   A HB1  1 
ATOM   713  H HB1  B ALA   A 1 27  ? 21.768 0.715   14.096  0.38 16.40 ?  27  ALA   A HB1  1 
ATOM   714  H HB2  A ALA   A 1 27  ? 20.486 0.359   12.767  0.62 17.02 ?  27  ALA   A HB2  1 
ATOM   715  H HB2  B ALA   A 1 27  ? 20.830 0.038   13.007  0.38 16.40 ?  27  ALA   A HB2  1 
ATOM   716  H HB3  A ALA   A 1 27  ? 20.367 1.807   13.412  0.62 17.02 ?  27  ALA   A HB3  1 
ATOM   717  H HB3  B ALA   A 1 27  ? 20.562 1.535   13.466  0.38 16.40 ?  27  ALA   A HB3  1 
ATOM   718  N N    A LYS   A 1 28  ? 19.358 2.257   16.110  0.62 17.58 ?  28  LYS   A N    1 
ATOM   719  N N    B LYS   A 1 28  ? 19.316 2.178   16.094  0.38 17.19 ?  28  LYS   A N    1 
ATOM   720  C CA   A LYS   A 1 28  ? 19.542 3.032   17.331  0.62 19.87 ?  28  LYS   A CA   1 
ATOM   721  C CA   B LYS   A 1 28  ? 19.322 3.055   17.263  0.38 19.46 ?  28  LYS   A CA   1 
ATOM   722  C C    A LYS   A 1 28  ? 18.985 2.304   18.548  0.62 20.42 ?  28  LYS   A C    1 
ATOM   723  C C    B LYS   A 1 28  ? 18.794 2.347   18.503  0.38 20.88 ?  28  LYS   A C    1 
ATOM   724  O O    A LYS   A 1 28  ? 19.516 2.455   19.653  0.62 21.99 ?  28  LYS   A O    1 
ATOM   725  O O    B LYS   A 1 28  ? 19.246 2.632   19.617  0.38 21.75 ?  28  LYS   A O    1 
ATOM   726  C CB   A LYS   A 1 28  ? 18.919 4.421   17.176  0.62 22.04 ?  28  LYS   A CB   1 
ATOM   727  C CB   B LYS   A 1 28  ? 18.507 4.322   16.996  0.38 20.52 ?  28  LYS   A CB   1 
ATOM   728  C CG   A LYS   A 1 28  ? 19.683 5.309   16.202  0.62 24.15 ?  28  LYS   A CG   1 
ATOM   729  C CG   B LYS   A 1 28  ? 19.246 5.367   16.175  0.38 21.91 ?  28  LYS   A CG   1 
ATOM   730  C CD   A LYS   A 1 28  ? 19.223 6.756   16.249  0.62 26.82 ?  28  LYS   A CD   1 
ATOM   731  C CD   B LYS   A 1 28  ? 18.651 6.759   16.345  0.38 24.05 ?  28  LYS   A CD   1 
ATOM   732  C CE   A LYS   A 1 28  ? 17.894 6.940   15.547  0.62 28.70 ?  28  LYS   A CE   1 
ATOM   733  C CE   B LYS   A 1 28  ? 17.832 7.171   15.136  0.38 25.85 ?  28  LYS   A CE   1 
ATOM   734  N NZ   A LYS   A 1 28  ? 17.514 8.377   15.468  0.62 29.96 ?  28  LYS   A NZ   1 
ATOM   735  N NZ   B LYS   A 1 28  ? 17.580 8.639   15.111  0.38 26.83 ?  28  LYS   A NZ   1 
ATOM   736  H H    A LYS   A 1 28  ? 18.870 2.636   15.514  0.62 21.11 ?  28  LYS   A H    1 
ATOM   737  H H    B LYS   A 1 28  ? 18.844 2.461   15.434  0.38 20.64 ?  28  LYS   A H    1 
ATOM   738  H HA   A LYS   A 1 28  ? 20.490 3.156   17.483  0.62 23.86 ?  28  LYS   A HA   1 
ATOM   739  H HA   B LYS   A 1 28  ? 20.234 3.324   17.447  0.38 23.37 ?  28  LYS   A HA   1 
ATOM   740  H HB2  A LYS   A 1 28  ? 18.013 4.330   16.845  0.62 26.46 ?  28  LYS   A HB2  1 
ATOM   741  H HB2  B LYS   A 1 28  ? 17.701 4.084   16.513  0.38 24.63 ?  28  LYS   A HB2  1 
ATOM   742  H HB3  A LYS   A 1 28  ? 18.913 4.867   18.038  0.62 26.46 ?  28  LYS   A HB3  1 
ATOM   743  H HB3  B LYS   A 1 28  ? 18.272 4.725   17.848  0.38 24.63 ?  28  LYS   A HB3  1 
ATOM   744  H HG2  A LYS   A 1 28  ? 20.627 5.286   16.424  0.62 28.99 ?  28  LYS   A HG2  1 
ATOM   745  H HG2  B LYS   A 1 28  ? 20.172 5.400   16.459  0.38 26.30 ?  28  LYS   A HG2  1 
ATOM   746  H HG3  A LYS   A 1 28  ? 19.546 4.979   15.299  0.62 28.99 ?  28  LYS   A HG3  1 
ATOM   747  H HG3  B LYS   A 1 28  ? 19.193 5.127   15.236  0.38 26.30 ?  28  LYS   A HG3  1 
ATOM   748  H HD2  A LYS   A 1 28  ? 19.118 7.028   17.174  0.62 32.20 ?  28  LYS   A HD2  1 
ATOM   749  H HD2  B LYS   A 1 28  ? 18.070 6.772   17.123  0.38 28.88 ?  28  LYS   A HD2  1 
ATOM   750  H HD3  A LYS   A 1 28  ? 19.881 7.316   15.807  0.62 32.20 ?  28  LYS   A HD3  1 
ATOM   751  H HD3  B LYS   A 1 28  ? 19.370 7.401   16.457  0.38 28.88 ?  28  LYS   A HD3  1 
ATOM   752  H HE2  A LYS   A 1 28  ? 17.959 6.593   14.643  0.62 34.46 ?  28  LYS   A HE2  1 
ATOM   753  H HE2  B LYS   A 1 28  ? 18.319 6.939   14.332  0.38 31.04 ?  28  LYS   A HE2  1 
ATOM   754  H HE3  A LYS   A 1 28  ? 17.203 6.470   16.038  0.62 34.46 ?  28  LYS   A HE3  1 
ATOM   755  H HE3  B LYS   A 1 28  ? 16.976 6.714   15.157  0.38 31.04 ?  28  LYS   A HE3  1 
ATOM   756  H HZ1  A LYS   A 1 28  ? 16.733 8.464   15.052  0.62 35.96 ?  28  LYS   A HZ1  1 
ATOM   757  H HZ1  B LYS   A 1 28  ? 17.100 8.853   14.393  0.38 32.21 ?  28  LYS   A HZ1  1 
ATOM   758  H HZ2  A LYS   A 1 28  ? 17.446 8.719   16.287  0.62 35.96 ?  28  LYS   A HZ2  1 
ATOM   759  H HZ2  B LYS   A 1 28  ? 17.135 8.884   15.841  0.38 32.21 ?  28  LYS   A HZ2  1 
ATOM   760  H HZ3  A LYS   A 1 28  ? 18.134 8.831   15.017  0.62 35.96 ?  28  LYS   A HZ3  1 
ATOM   761  H HZ3  B LYS   A 1 28  ? 18.354 9.079   15.083  0.38 32.21 ?  28  LYS   A HZ3  1 
ATOM   762  N N    A LYS   A 1 29  ? 17.942 1.492   18.364  0.62 20.76 ?  29  LYS   A N    1 
ATOM   763  N N    B LYS   A 1 29  ? 17.843 1.429   18.336  0.38 21.97 ?  29  LYS   A N    1 
ATOM   764  C CA   A LYS   A 1 29  ? 17.339 0.772   19.483  0.62 22.65 ?  29  LYS   A CA   1 
ATOM   765  C CA   B LYS   A 1 29  ? 17.257 0.724   19.470  0.38 23.63 ?  29  LYS   A CA   1 
ATOM   766  C C    A LYS   A 1 29  ? 18.159 -0.456  19.869  0.62 22.39 ?  29  LYS   A C    1 
ATOM   767  C C    B LYS   A 1 29  ? 18.065 -0.506  19.866  0.38 22.93 ?  29  LYS   A C    1 
ATOM   768  O O    A LYS   A 1 29  ? 18.468 -0.661  21.049  0.62 23.05 ?  29  LYS   A O    1 
ATOM   769  O O    B LYS   A 1 29  ? 18.272 -0.754  21.060  0.38 23.36 ?  29  LYS   A O    1 
ATOM   770  C CB   A LYS   A 1 29  ? 15.908 0.365   19.120  0.62 25.49 ?  29  LYS   A CB   1 
ATOM   771  C CB   B LYS   A 1 29  ? 15.827 0.298   19.129  0.38 26.10 ?  29  LYS   A CB   1 
ATOM   772  C CG   A LYS   A 1 29  ? 15.136 -0.301  20.248  0.62 28.48 ?  29  LYS   A CG   1 
ATOM   773  C CG   B LYS   A 1 29  ? 15.040 -0.274  20.297  0.38 28.50 ?  29  LYS   A CG   1 
ATOM   774  C CD   A LYS   A 1 29  ? 14.789 0.694   21.342  0.62 31.32 ?  29  LYS   A CD   1 
ATOM   775  C CD   B LYS   A 1 29  ? 14.688 0.804   21.306  0.38 30.60 ?  29  LYS   A CD   1 
ATOM   776  C CE   A LYS   A 1 29  ? 13.916 0.061   22.414  0.62 33.24 ?  29  LYS   A CE   1 
ATOM   777  C CE   B LYS   A 1 29  ? 13.773 0.268   22.393  0.38 32.02 ?  29  LYS   A CE   1 
ATOM   778  N NZ   A LYS   A 1 29  ? 13.490 1.055   23.439  0.62 34.25 ?  29  LYS   A NZ   1 
ATOM   779  N NZ   B LYS   A 1 29  ? 13.400 1.323   23.374  0.38 32.83 ?  29  LYS   A NZ   1 
ATOM   780  H H    A LYS   A 1 29  ? 17.572 1.339   17.602  0.62 24.93 ?  29  LYS   A H    1 
ATOM   781  H H    B LYS   A 1 29  ? 17.517 1.196   17.572  0.38 26.38 ?  29  LYS   A H    1 
ATOM   782  H HA   A LYS   A 1 29  ? 17.301 1.358   20.250  0.62 27.20 ?  29  LYS   A HA   1 
ATOM   783  H HA   B LYS   A 1 29  ? 17.224 1.324   20.231  0.38 28.38 ?  29  LYS   A HA   1 
ATOM   784  H HB2  A LYS   A 1 29  ? 15.418 1.161   18.859  0.62 30.60 ?  29  LYS   A HB2  1 
ATOM   785  H HB2  B LYS   A 1 29  ? 15.345 1.073   18.803  0.38 31.34 ?  29  LYS   A HB2  1 
ATOM   786  H HB3  A LYS   A 1 29  ? 15.939 -0.257  18.377  0.62 30.60 ?  29  LYS   A HB3  1 
ATOM   787  H HB3  B LYS   A 1 29  ? 15.863 -0.381  18.439  0.38 31.34 ?  29  LYS   A HB3  1 
ATOM   788  H HG2  A LYS   A 1 29  ? 14.308 -0.664  19.896  0.62 34.19 ?  29  LYS   A HG2  1 
ATOM   789  H HG2  B LYS   A 1 29  ? 14.215 -0.662  19.966  0.38 34.21 ?  29  LYS   A HG2  1 
ATOM   790  H HG3  A LYS   A 1 29  ? 15.672 -1.009  20.638  0.62 34.19 ?  29  LYS   A HG3  1 
ATOM   791  H HG3  B LYS   A 1 29  ? 15.571 -0.951  20.746  0.38 34.21 ?  29  LYS   A HG3  1 
ATOM   792  H HD2  A LYS   A 1 29  ? 15.607 1.007   21.761  0.62 37.60 ?  29  LYS   A HD2  1 
ATOM   793  H HD2  B LYS   A 1 29  ? 15.500 1.129   21.724  0.38 36.74 ?  29  LYS   A HD2  1 
ATOM   794  H HD3  A LYS   A 1 29  ? 14.304 1.440   20.954  0.62 37.60 ?  29  LYS   A HD3  1 
ATOM   795  H HD3  B LYS   A 1 29  ? 14.230 1.529   20.852  0.38 36.74 ?  29  LYS   A HD3  1 
ATOM   796  H HE2  A LYS   A 1 29  ? 13.120 -0.308  21.999  0.62 39.90 ?  29  LYS   A HE2  1 
ATOM   797  H HE2  B LYS   A 1 29  ? 12.959 -0.071  21.987  0.38 38.44 ?  29  LYS   A HE2  1 
ATOM   798  H HE3  A LYS   A 1 29  ? 14.416 -0.640  22.860  0.62 39.90 ?  29  LYS   A HE3  1 
ATOM   799  H HE3  B LYS   A 1 29  ? 14.229 -0.443  22.871  0.38 38.44 ?  29  LYS   A HE3  1 
ATOM   800  H HZ1  A LYS   A 1 29  ? 12.981 0.660   24.052  0.62 41.12 ?  29  LYS   A HZ1  1 
ATOM   801  H HZ1  B LYS   A 1 29  ? 12.865 0.982   23.999  0.38 39.41 ?  29  LYS   A HZ1  1 
ATOM   802  H HZ2  A LYS   A 1 29  ? 14.204 1.406   23.837  0.62 41.12 ?  29  LYS   A HZ2  1 
ATOM   803  H HZ2  B LYS   A 1 29  ? 14.131 1.647   23.764  0.38 39.41 ?  29  LYS   A HZ2  1 
ATOM   804  H HZ3  A LYS   A 1 29  ? 13.024 1.708   23.053  0.62 41.12 ?  29  LYS   A HZ3  1 
ATOM   805  H HZ3  B LYS   A 1 29  ? 12.975 1.986   22.960  0.38 39.41 ?  29  LYS   A HZ3  1 
ATOM   806  N N    . VAL   A 1 30  ? 18.515 -1.287  18.888  1.00 21.90 ?  30  VAL   A N    1 
ATOM   807  C CA   . VAL   A 1 30  ? 19.177 -2.554  19.181  1.00 21.25 ?  30  VAL   A CA   1 
ATOM   808  C C    . VAL   A 1 30  ? 20.681 -2.398  19.402  1.00 20.41 ?  30  VAL   A C    1 
ATOM   809  O O    . VAL   A 1 30  ? 21.268 -3.136  20.201  1.00 20.98 ?  30  VAL   A O    1 
ATOM   810  C CB   . VAL   A 1 30  ? 18.870 -3.554  18.050  1.00 22.59 ?  30  VAL   A CB   1 
ATOM   811  C CG1  . VAL   A 1 30  ? 19.646 -4.852  18.236  1.00 23.56 ?  30  VAL   A CG1  1 
ATOM   812  C CG2  . VAL   A 1 30  ? 17.375 -3.829  17.980  1.00 23.19 ?  30  VAL   A CG2  1 
ATOM   813  H H    A VAL   A 1 30  ? 18.393 -1.139  18.048  0.62 26.30 ?  30  VAL   A H    1 
ATOM   814  H H    B VAL   A 1 30  ? 18.437 -1.116  18.046  0.38 26.30 ?  30  VAL   A H    1 
ATOM   815  H HA   . VAL   A 1 30  ? 18.799 -2.918  19.994  1.00 25.51 ?  30  VAL   A HA   1 
ATOM   816  H HB   . VAL   A 1 30  ? 19.138 -3.172  17.202  1.00 27.12 ?  30  VAL   A HB   1 
ATOM   817  H HG11 . VAL   A 1 30  ? 19.265 -5.534  17.656  1.00 28.28 ?  30  VAL   A HG11 1 
ATOM   818  H HG12 . VAL   A 1 30  ? 20.574 -4.704  18.002  1.00 28.28 ?  30  VAL   A HG12 1 
ATOM   819  H HG13 . VAL   A 1 30  ? 19.574 -5.134  19.161  1.00 28.28 ?  30  VAL   A HG13 1 
ATOM   820  H HG21 . VAL   A 1 30  ? 17.205 -4.499  17.297  1.00 27.84 ?  30  VAL   A HG21 1 
ATOM   821  H HG22 . VAL   A 1 30  ? 17.073 -4.157  18.843  1.00 27.84 ?  30  VAL   A HG22 1 
ATOM   822  H HG23 . VAL   A 1 30  ? 16.913 -3.007  17.758  1.00 27.84 ?  30  VAL   A HG23 1 
ATOM   823  N N    . LYS   A 1 31  ? 21.320 -1.448  18.725  1.00 18.94 ?  31  LYS   A N    1 
ATOM   824  C CA   . LYS   A 1 31  ? 22.773 -1.342  18.685  1.00 19.57 ?  31  LYS   A CA   1 
ATOM   825  C C    . LYS   A 1 31  ? 23.374 -2.699  18.308  1.00 17.43 ?  31  LYS   A C    1 
ATOM   826  O O    . LYS   A 1 31  ? 24.160 -3.273  19.069  1.00 18.60 ?  31  LYS   A O    1 
ATOM   827  C CB   . LYS   A 1 31  ? 23.349 -0.830  19.998  1.00 24.61 ?  31  LYS   A CB   1 
ATOM   828  C CG   . LYS   A 1 31  ? 22.640 0.413   20.524  1.00 31.32 ?  31  LYS   A CG   1 
ATOM   829  C CD   . LYS   A 1 31  ? 23.620 1.493   20.961  1.00 36.45 ?  31  LYS   A CD   1 
ATOM   830  C CE   . LYS   A 1 31  ? 22.932 2.557   21.809  1.00 39.76 ?  31  LYS   A CE   1 
ATOM   831  N NZ   . LYS   A 1 31  ? 21.808 3.234   21.102  1.00 41.61 ?  31  LYS   A NZ   1 
ATOM   832  H H    . LYS   A 1 31  ? 20.929 -0.836  18.268  1.00 22.74 ?  31  LYS   A H    1 
ATOM   833  H HA   . LYS   A 1 31  ? 23.013 -0.707  17.993  1.00 23.50 ?  31  LYS   A HA   1 
ATOM   834  H HB2  . LYS   A 1 31  ? 23.275 -1.527  20.668  1.00 29.54 ?  31  LYS   A HB2  1 
ATOM   835  H HB3  . LYS   A 1 31  ? 24.287 -0.604  19.864  1.00 29.54 ?  31  LYS   A HB3  1 
ATOM   836  H HG2  . LYS   A 1 31  ? 22.082 0.781   19.821  1.00 37.60 ?  31  LYS   A HG2  1 
ATOM   837  H HG3  . LYS   A 1 31  ? 22.095 0.171   21.289  1.00 37.60 ?  31  LYS   A HG3  1 
ATOM   838  H HD2  . LYS   A 1 31  ? 24.327 1.091   21.490  1.00 43.75 ?  31  LYS   A HD2  1 
ATOM   839  H HD3  . LYS   A 1 31  ? 23.995 1.924   20.175  1.00 43.75 ?  31  LYS   A HD3  1 
ATOM   840  H HE2  . LYS   A 1 31  ? 22.572 2.138   22.607  1.00 47.73 ?  31  LYS   A HE2  1 
ATOM   841  H HE3  . LYS   A 1 31  ? 23.581 3.234   22.055  1.00 47.73 ?  31  LYS   A HE3  1 
ATOM   842  H HZ1  . LYS   A 1 31  ? 21.439 3.847   21.634  1.00 49.95 ?  31  LYS   A HZ1  1 
ATOM   843  H HZ2  . LYS   A 1 31  ? 22.107 3.634   20.366  1.00 49.95 ?  31  LYS   A HZ2  1 
ATOM   844  H HZ3  . LYS   A 1 31  ? 21.186 2.639   20.876  1.00 49.95 ?  31  LYS   A HZ3  1 
ATOM   845  N N    . PRO   A 1 32  ? 23.009 -3.235  17.149  1.00 15.35 ?  32  PRO   A N    1 
ATOM   846  C CA   . PRO   A 1 32  ? 23.477 -4.567  16.772  1.00 15.70 ?  32  PRO   A CA   1 
ATOM   847  C C    . PRO   A 1 32  ? 24.977 -4.573  16.567  1.00 15.47 ?  32  PRO   A C    1 
ATOM   848  O O    . PRO   A 1 32  ? 25.611 -3.538  16.346  1.00 15.90 ?  32  PRO   A O    1 
ATOM   849  C CB   . PRO   A 1 32  ? 22.748 -4.828  15.450  1.00 15.77 ?  32  PRO   A CB   1 
ATOM   850  C CG   . PRO   A 1 32  ? 22.570 -3.448  14.867  1.00 14.31 ?  32  PRO   A CG   1 
ATOM   851  C CD   . PRO   A 1 32  ? 22.285 -2.574  16.052  1.00 14.20 ?  32  PRO   A CD   1 
ATOM   852  H HA   . PRO   A 1 32  ? 23.227 -5.234  17.428  1.00 18.85 ?  32  PRO   A HA   1 
ATOM   853  H HB2  . PRO   A 1 32  ? 23.294 -5.384  14.867  1.00 18.94 ?  32  PRO   A HB2  1 
ATOM   854  H HB3  . PRO   A 1 32  ? 21.888 -5.251  15.621  1.00 18.94 ?  32  PRO   A HB3  1 
ATOM   855  H HG2  . PRO   A 1 32  ? 23.382 -3.177  14.421  1.00 17.19 ?  32  PRO   A HG2  1 
ATOM   856  H HG3  . PRO   A 1 32  ? 21.818 -3.451  14.253  1.00 17.19 ?  32  PRO   A HG3  1 
ATOM   857  H HD2  . PRO   A 1 32  ? 22.640 -1.685  15.895  1.00 17.05 ?  32  PRO   A HD2  1 
ATOM   858  H HD3  . PRO   A 1 32  ? 21.336 -2.555  16.234  1.00 17.05 ?  32  PRO   A HD3  1 
ATOM   859  N N    . THR   A 1 33  ? 25.541 -5.777  16.610  1.00 15.64 ?  33  THR   A N    1 
ATOM   860  C CA   . THR   A 1 33  ? 26.948 -5.932  16.272  1.00 15.95 ?  33  THR   A CA   1 
ATOM   861  C C    . THR   A 1 33  ? 27.227 -5.462  14.851  1.00 14.19 ?  33  THR   A C    1 
ATOM   862  O O    . THR   A 1 33  ? 28.253 -4.820  14.597  1.00 14.45 ?  33  THR   A O    1 
ATOM   863  C CB   . THR   A 1 33  ? 27.362 -7.389  16.460  1.00 17.58 ?  33  THR   A CB   1 
ATOM   864  O OG1  . THR   A 1 33  ? 27.078 -7.783  17.805  1.00 19.50 ?  33  THR   A OG1  1 
ATOM   865  C CG2  . THR   A 1 33  ? 28.846 -7.570  16.181  1.00 18.92 ?  33  THR   A CG2  1 
ATOM   866  H H    . THR   A 1 33  ? 25.141 -6.510  16.827  1.00 18.78 ?  33  THR   A H    1 
ATOM   867  H HA   . THR   A 1 33  ? 27.481 -5.396  16.877  1.00 19.15 ?  33  THR   A HA   1 
ATOM   868  H HB   . THR   A 1 33  ? 26.865 -7.958  15.845  1.00 21.11 ?  33  THR   A HB   1 
ATOM   869  H HG1  . THR   A 1 33  ? 27.517 -7.306  18.342  1.00 23.41 ?  33  THR   A HG1  1 
ATOM   870  H HG21 . THR   A 1 33  ? 29.131 -8.456  16.459  1.00 22.72 ?  33  THR   A HG21 1 
ATOM   871  H HG22 . THR   A 1 33  ? 29.024 -7.467  15.233  1.00 22.72 ?  33  THR   A HG22 1 
ATOM   872  H HG23 . THR   A 1 33  ? 29.355 -6.908  16.673  1.00 22.72 ?  33  THR   A HG23 1 
ATOM   873  N N    . VAL   A 1 34  ? 26.328 -5.772  13.916  1.00 12.64 ?  34  VAL   A N    1 
ATOM   874  C CA   . VAL   A 1 34  ? 26.510 -5.436  12.507  1.00 11.60 ?  34  VAL   A CA   1 
ATOM   875  C C    . VAL   A 1 34  ? 25.208 -4.871  11.944  1.00 11.24 ?  34  VAL   A C    1 
ATOM   876  O O    . VAL   A 1 34  ? 24.166 -5.536  11.994  1.00 11.93 ?  34  VAL   A O    1 
ATOM   877  C CB   . VAL   A 1 34  ? 26.943 -6.646  11.659  1.00 12.26 ?  34  VAL   A CB   1 
ATOM   878  C CG1  . VAL   A 1 34  ? 27.111 -6.240  10.203  1.00 12.64 ?  34  VAL   A CG1  1 
ATOM   879  C CG2  . VAL   A 1 34  ? 28.219 -7.273  12.211  1.00 13.89 ?  34  VAL   A CG2  1 
ATOM   880  H H    . VAL   A 1 34  ? 25.589 -6.184  14.078  1.00 15.18 ?  34  VAL   A H    1 
ATOM   881  H HA   . VAL   A 1 34  ? 27.189 -4.748  12.422  1.00 13.93 ?  34  VAL   A HA   1 
ATOM   882  H HB   . VAL   A 1 34  ? 26.242 -7.316  11.701  1.00 14.73 ?  34  VAL   A HB   1 
ATOM   883  H HG11 . VAL   A 1 34  ? 27.609 -6.931  9.742   1.00 15.18 ?  34  VAL   A HG11 1 
ATOM   884  H HG12 . VAL   A 1 34  ? 26.237 -6.136  9.797   1.00 15.18 ?  34  VAL   A HG12 1 
ATOM   885  H HG13 . VAL   A 1 34  ? 27.598 -5.401  10.165  1.00 15.18 ?  34  VAL   A HG13 1 
ATOM   886  H HG21 . VAL   A 1 34  ? 28.482 -8.007  11.634  1.00 16.68 ?  34  VAL   A HG21 1 
ATOM   887  H HG22 . VAL   A 1 34  ? 28.916 -6.601  12.235  1.00 16.68 ?  34  VAL   A HG22 1 
ATOM   888  H HG23 . VAL   A 1 34  ? 28.046 -7.604  13.108  1.00 16.68 ?  34  VAL   A HG23 1 
ATOM   889  N N    . VAL   A 1 35  ? 25.271 -3.661  11.389  1.00 10.47 ?  35  VAL   A N    1 
ATOM   890  C CA   . VAL   A 1 35  ? 24.231 -3.135  10.509  1.00 9.78  ?  35  VAL   A CA   1 
ATOM   891  C C    . VAL   A 1 35  ? 24.779 -3.133  9.089   1.00 9.49  ?  35  VAL   A C    1 
ATOM   892  O O    . VAL   A 1 35  ? 25.925 -2.732  8.859   1.00 9.97  ?  35  VAL   A O    1 
ATOM   893  C CB   . VAL   A 1 35  ? 23.716 -1.743  10.938  1.00 10.73 ?  35  VAL   A CB   1 
ATOM   894  C CG1  . VAL   A 1 35  ? 24.786 -0.649  10.818  1.00 11.48 ?  35  VAL   A CG1  1 
ATOM   895  C CG2  . VAL   A 1 35  ? 22.476 -1.371  10.125  1.00 11.14 ?  35  VAL   A CG2  1 
ATOM   896  H H    . VAL   A 1 35  ? 25.914 -3.106  11.515  1.00 12.57 ?  35  VAL   A H    1 
ATOM   897  H HA   . VAL   A 1 35  ? 23.468 -3.738  10.531  1.00 11.76 ?  35  VAL   A HA   1 
ATOM   898  H HB   . VAL   A 1 35  ? 23.440 -1.781  11.866  1.00 12.89 ?  35  VAL   A HB   1 
ATOM   899  H HG11 . VAL   A 1 35  ? 24.436 0.184   11.186  1.00 13.80 ?  35  VAL   A HG11 1 
ATOM   900  H HG12 . VAL   A 1 35  ? 25.572 -0.919  11.312  1.00 13.80 ?  35  VAL   A HG12 1 
ATOM   901  H HG13 . VAL   A 1 35  ? 25.009 -0.517  9.882   1.00 13.80 ?  35  VAL   A HG13 1 
ATOM   902  H HG21 . VAL   A 1 35  ? 22.124 -0.524  10.441  1.00 13.38 ?  35  VAL   A HG21 1 
ATOM   903  H HG22 . VAL   A 1 35  ? 22.723 -1.291  9.185   1.00 13.38 ?  35  VAL   A HG22 1 
ATOM   904  H HG23 . VAL   A 1 35  ? 21.807 -2.066  10.226  1.00 13.38 ?  35  VAL   A HG23 1 
ATOM   905  N N    . VAL   A 1 36  ? 23.967 -3.598  8.143   1.00 8.82  ?  36  VAL   A N    1 
ATOM   906  C CA   . VAL   A 1 36  ? 24.342 -3.612  6.735   1.00 8.69  ?  36  VAL   A CA   1 
ATOM   907  C C    . VAL   A 1 36  ? 23.881 -2.319  6.076   1.00 8.65  ?  36  VAL   A C    1 
ATOM   908  O O    . VAL   A 1 36  ? 22.717 -1.914  6.217   1.00 9.42  ?  36  VAL   A O    1 
ATOM   909  C CB   . VAL   A 1 36  ? 23.727 -4.828  6.020   1.00 8.81  ?  36  VAL   A CB   1 
ATOM   910  C CG1  . VAL   A 1 36  ? 23.989 -4.745  4.523   1.00 9.18  ?  36  VAL   A CG1  1 
ATOM   911  C CG2  . VAL   A 1 36  ? 24.276 -6.121  6.613   1.00 9.67  ?  36  VAL   A CG2  1 
ATOM   912  H H    . VAL   A 1 36  ? 23.182 -3.930  8.296   1.00 10.60 ?  36  VAL   A H    1 
ATOM   913  H HA   . VAL   A 1 36  ? 25.309 -3.676  6.661   1.00 10.45 ?  36  VAL   A HA   1 
ATOM   914  H HB   . VAL   A 1 36  ? 22.766 -4.817  6.154   1.00 10.59 ?  36  VAL   A HB   1 
ATOM   915  H HG11 . VAL   A 1 36  ? 23.845 -5.618  4.131   1.00 11.03 ?  36  VAL   A HG11 1 
ATOM   916  H HG12 . VAL   A 1 36  ? 23.382 -4.100  4.127   1.00 11.03 ?  36  VAL   A HG12 1 
ATOM   917  H HG13 . VAL   A 1 36  ? 24.909 -4.466  4.382   1.00 11.03 ?  36  VAL   A HG13 1 
ATOM   918  H HG21 . VAL   A 1 36  ? 23.904 -6.877  6.134   1.00 11.62 ?  36  VAL   A HG21 1 
ATOM   919  H HG22 . VAL   A 1 36  ? 25.246 -6.123  6.526   1.00 11.62 ?  36  VAL   A HG22 1 
ATOM   920  H HG23 . VAL   A 1 36  ? 24.034 -6.173  7.552   1.00 11.62 ?  36  VAL   A HG23 1 
ATOM   921  N N    . ASN   A 1 37  ? 24.792 -1.688  5.335   1.00 8.38  ?  37  ASN   A N    1 
ATOM   922  C CA   . ASN   A 1 37  ? 24.458 -0.571  4.471   1.00 8.43  ?  37  ASN   A CA   1 
ATOM   923  C C    . ASN   A 1 37  ? 24.306 -1.042  3.036   1.00 8.46  ?  37  ASN   A C    1 
ATOM   924  O O    . ASN   A 1 37  ? 25.090 -1.863  2.548   1.00 9.01  ?  37  ASN   A O    1 
ATOM   925  C CB   . ASN   A 1 37  ? 25.534 0.510   4.538   1.00 8.58  ?  37  ASN   A CB   1 
ATOM   926  C CG   . ASN   A 1 37  ? 25.200 1.705   3.679   1.00 8.78  ?  37  ASN   A CG   1 
ATOM   927  O OD1  . ASN   A 1 37  ? 24.025 2.046   3.494   1.00 9.14  ?  37  ASN   A OD1  1 
ATOM   928  N ND2  . ASN   A 1 37  ? 26.226 2.358   3.163   1.00 9.20  ?  37  ASN   A ND2  1 
ATOM   929  H H    . ASN   A 1 37  ? 25.632 -1.890  5.330   1.00 10.07 ?  37  ASN   A H    1 
ATOM   930  H HA   . ASN   A 1 37  ? 23.625 -0.178  4.764   1.00 10.13 ?  37  ASN   A HA   1 
ATOM   931  H HB2  . ASN   A 1 37  ? 25.626 0.822   5.456   1.00 10.31 ?  37  ASN   A HB2  1 
ATOM   932  H HB3  . ASN   A 1 37  ? 26.383 0.143   4.233   1.00 10.31 ?  37  ASN   A HB3  1 
ATOM   933  H HD21 . ASN   A 1 37  ? 26.089 3.046   2.662   1.00 11.05 ?  37  ASN   A HD21 1 
ATOM   934  H HD22 . ASN   A 1 37  ? 27.029 2.101   3.311   1.00 11.05 ?  37  ASN   A HD22 1 
ATOM   935  N N    A ALA   A 1 38  ? 23.289 -0.495  2.365   0.62 8.50  ?  38  ALA   A N    1 
ATOM   936  N N    B ALA   A 1 38  ? 23.276 -0.533  2.359   0.38 8.80  ?  38  ALA   A N    1 
ATOM   937  C CA   A ALA   A 1 38  ? 23.080 -0.640  0.925   0.62 8.60  ?  38  ALA   A CA   1 
ATOM   938  C CA   B ALA   A 1 38  ? 23.084 -0.788  0.931   0.38 9.37  ?  38  ALA   A CA   1 
ATOM   939  C C    A ALA   A 1 38  ? 23.978 0.369   0.206   0.62 8.38  ?  38  ALA   A C    1 
ATOM   940  C C    B ALA   A 1 38  ? 23.907 0.239   0.155   0.38 9.63  ?  38  ALA   A C    1 
ATOM   941  O O    A ALA   A 1 38  ? 23.568 1.468   -0.176  0.62 8.31  ?  38  ALA   A O    1 
ATOM   942  O O    B ALA   A 1 38  ? 23.411 1.267   -0.314  0.38 9.80  ?  38  ALA   A O    1 
ATOM   943  C CB   A ALA   A 1 38  ? 21.607 -0.430  0.590   0.62 9.14  ?  38  ALA   A CB   1 
ATOM   944  C CB   B ALA   A 1 38  ? 21.606 -0.724  0.574   0.38 9.98  ?  38  ALA   A CB   1 
ATOM   945  H H    A ALA   A 1 38  ? 22.690 -0.009  2.748   0.62 10.22 ?  38  ALA   A H    1 
ATOM   946  H H    B ALA   A 1 38  ? 22.671 -0.034  2.716   0.38 10.57 ?  38  ALA   A H    1 
ATOM   947  H HA   A ALA   A 1 38  ? 23.335 -1.532  0.651   0.62 10.34 ?  38  ALA   A HA   1 
ATOM   948  H HA   B ALA   A 1 38  ? 23.418 -1.676  0.718   0.38 11.26 ?  38  ALA   A HA   1 
ATOM   949  H HB1  A ALA   A 1 38  ? 21.478 -0.539  -0.363  0.62 10.98 ?  38  ALA   A HB1  1 
ATOM   950  H HB1  B ALA   A 1 38  ? 21.510 -0.876  -0.378  0.38 11.99 ?  38  ALA   A HB1  1 
ATOM   951  H HB2  A ALA   A 1 38  ? 21.076 -1.091  1.072   0.62 10.98 ?  38  ALA   A HB2  1 
ATOM   952  H HB2  B ALA   A 1 38  ? 21.129 -1.407  1.071   0.38 11.99 ?  38  ALA   A HB2  1 
ATOM   953  H HB3  A ALA   A 1 38  ? 21.341 0.462   0.863   0.62 10.98 ?  38  ALA   A HB3  1 
ATOM   954  H HB3  B ALA   A 1 38  ? 21.267 0.154   0.806   0.38 11.99 ?  38  ALA   A HB3  1 
ATOM   955  N N    A ALA   A 1 39  ? 25.244 -0.011  0.051   0.62 8.14  ?  39  ALA   A N    1 
ATOM   956  N N    B ALA   A 1 39  ? 25.196 -0.056  0.020   0.38 10.22 ?  39  ALA   A N    1 
ATOM   957  C CA   A ALA   A 1 39  ? 26.296 0.858   -0.450  0.62 8.34  ?  39  ALA   A CA   1 
ATOM   958  C CA   B ALA   A 1 39  ? 26.167 0.916   -0.455  0.38 10.42 ?  39  ALA   A CA   1 
ATOM   959  C C    A ALA   A 1 39  ? 26.414 0.805   -1.973  0.62 8.52  ?  39  ALA   A C    1 
ATOM   960  C C    B ALA   A 1 39  ? 26.350 0.838   -1.970  0.38 10.15 ?  39  ALA   A C    1 
ATOM   961  O O    A ALA   A 1 39  ? 25.915 -0.110  -2.631  0.62 8.94  ?  39  ALA   A O    1 
ATOM   962  O O    B ALA   A 1 39  ? 25.803 -0.032  -2.651  0.38 10.34 ?  39  ALA   A O    1 
ATOM   963  C CB   A ALA   A 1 39  ? 27.630 0.430   0.172   0.62 8.62  ?  39  ALA   A CB   1 
ATOM   964  C CB   B ALA   A 1 39  ? 27.507 0.691   0.245   0.38 11.45 ?  39  ALA   A CB   1 
ATOM   965  H H    A ALA   A 1 39  ? 25.521 -0.807  0.241   0.62 9.79  ?  39  ALA   A H    1 
ATOM   966  H H    B ALA   A 1 39  ? 25.531 -0.833  0.194   0.38 12.28 ?  39  ALA   A H    1 
ATOM   967  H HA   A ALA   A 1 39  ? 26.110 1.769   -0.188  0.62 10.03 ?  39  ALA   A HA   1 
ATOM   968  H HA   B ALA   A 1 39  ? 25.856 1.802   -0.229  0.38 12.53 ?  39  ALA   A HA   1 
ATOM   969  H HB1  A ALA   A 1 39  ? 28.330 1.012   -0.159  0.62 10.36 ?  39  ALA   A HB1  1 
ATOM   970  H HB1  B ALA   A 1 39  ? 28.143 1.348   -0.077  0.38 13.75 ?  39  ALA   A HB1  1 
ATOM   971  H HB2  A ALA   A 1 39  ? 27.566 0.512   1.141   0.62 10.36 ?  39  ALA   A HB2  1 
ATOM   972  H HB2  B ALA   A 1 39  ? 27.384 0.793   1.204   0.38 13.75 ?  39  ALA   A HB2  1 
ATOM   973  H HB3  A ALA   A 1 39  ? 27.815 -0.488  -0.069  0.62 10.36 ?  39  ALA   A HB3  1 
ATOM   974  H HB3  B ALA   A 1 39  ? 27.824 -0.204  0.047   0.38 13.75 ?  39  ALA   A HB3  1 
ATOM   975  N N    A ASN   A 1 40  ? 27.097 1.811   -2.526  0.62 8.76  ?  40  ASN   A N    1 
ATOM   976  N N    B ASN   A 1 40  ? 27.128 1.784   -2.495  0.38 10.29 ?  40  ASN   A N    1 
ATOM   977  C CA   A ASN   A 1 40  ? 27.631 1.768   -3.882  0.62 8.99  ?  40  ASN   A CA   1 
ATOM   978  C CA   B ASN   A 1 40  ? 27.640 1.731   -3.857  0.38 10.24 ?  40  ASN   A CA   1 
ATOM   979  C C    A ASN   A 1 40  ? 29.155 1.637   -3.825  0.62 8.68  ?  40  ASN   A C    1 
ATOM   980  C C    B ASN   A 1 40  ? 29.163 1.622   -3.817  0.38 9.54  ?  40  ASN   A C    1 
ATOM   981  O O    A ASN   A 1 40  ? 29.769 1.729   -2.760  0.62 8.89  ?  40  ASN   A O    1 
ATOM   982  O O    B ASN   A 1 40  ? 29.787 1.729   -2.758  0.38 9.60  ?  40  ASN   A O    1 
ATOM   983  C CB   A ASN   A 1 40  ? 27.175 2.970   -4.726  0.62 10.07 ?  40  ASN   A CB   1 
ATOM   984  C CB   B ASN   A 1 40  ? 27.164 2.923   -4.703  0.38 11.10 ?  40  ASN   A CB   1 
ATOM   985  C CG   A ASN   A 1 40  ? 27.596 4.308   -4.143  0.62 10.47 ?  40  ASN   A CG   1 
ATOM   986  C CG   B ASN   A 1 40  ? 27.413 4.265   -4.038  0.38 11.78 ?  40  ASN   A CG   1 
ATOM   987  O OD1  A ASN   A 1 40  ? 28.785 4.555   -3.916  0.62 10.44 ?  40  ASN   A OD1  1 
ATOM   988  O OD1  B ASN   A 1 40  ? 28.499 4.523   -3.523  0.38 12.89 ?  40  ASN   A OD1  1 
ATOM   989  N ND2  A ASN   A 1 40  ? 26.615 5.189   -3.920  0.62 11.23 ?  40  ASN   A ND2  1 
ATOM   990  N ND2  B ASN   A 1 40  ? 26.398 5.123   -4.044  0.38 11.50 ?  40  ASN   A ND2  1 
ATOM   991  H H    A ASN   A 1 40  ? 27.272 2.541   -2.115  0.62 10.53 ?  40  ASN   A H    1 
ATOM   992  H H    B ASN   A 1 40  ? 27.382 2.482   -2.061  0.38 12.36 ?  40  ASN   A H    1 
ATOM   993  H HA   A ASN   A 1 40  ? 27.296 0.967   -4.317  0.62 10.80 ?  40  ASN   A HA   1 
ATOM   994  H HA   B ASN   A 1 40  ? 27.304 0.927   -4.277  0.38 12.30 ?  40  ASN   A HA   1 
ATOM   995  H HB2  A ASN   A 1 40  ? 27.561 2.897   -5.612  0.62 12.10 ?  40  ASN   A HB2  1 
ATOM   996  H HB2  B ASN   A 1 40  ? 27.637 2.910   -5.555  0.38 13.34 ?  40  ASN   A HB2  1 
ATOM   997  H HB3  A ASN   A 1 40  ? 26.206 2.958   -4.788  0.62 12.10 ?  40  ASN   A HB3  1 
ATOM   998  H HB3  B ASN   A 1 40  ? 26.212 2.839   -4.858  0.38 13.34 ?  40  ASN   A HB3  1 
ATOM   999  H HD21 A ASN   A 1 40  ? 26.796 5.966   -3.596  0.62 13.49 ?  40  ASN   A HD21 1 
ATOM   1000 H HD21 B ASN   A 1 40  ? 26.490 5.901   -3.690  0.38 13.81 ?  40  ASN   A HD21 1 
ATOM   1001 H HD22 A ASN   A 1 40  ? 25.798 4.982   -4.101  0.62 13.49 ?  40  ASN   A HD22 1 
ATOM   1002 H HD22 B ASN   A 1 40  ? 25.650 4.900   -4.405  0.38 13.81 ?  40  ASN   A HD22 1 
ATOM   1003 N N    . VAL   A 1 41  ? 29.768 1.383   -4.982  1.00 9.61  ?  41  VAL   A N    1 
ATOM   1004 C CA   . VAL   A 1 41  ? 31.201 1.076   -5.013  1.00 10.12 ?  41  VAL   A CA   1 
ATOM   1005 C C    . VAL   A 1 41  ? 32.070 2.227   -4.542  1.00 10.22 ?  41  VAL   A C    1 
ATOM   1006 O O    . VAL   A 1 41  ? 33.212 1.997   -4.128  1.00 10.76 ?  41  VAL   A O    1 
ATOM   1007 C CB   . VAL   A 1 41  ? 31.687 0.592   -6.397  1.00 11.25 ?  41  VAL   A CB   1 
ATOM   1008 C CG1  . VAL   A 1 41  ? 30.991 -0.704  -6.791  1.00 11.83 ?  41  VAL   A CG1  1 
ATOM   1009 C CG2  . VAL   A 1 41  ? 31.527 1.662   -7.471  1.00 12.10 ?  41  VAL   A CG2  1 
ATOM   1010 H H    A VAL   A 1 41  ? 29.381 1.374   -5.748  0.62 11.54 ?  41  VAL   A H    1 
ATOM   1011 H H    B VAL   A 1 41  ? 29.380 1.395   -5.747  0.38 11.54 ?  41  VAL   A H    1 
ATOM   1012 H HA   . VAL   A 1 41  ? 31.355 0.341   -4.395  1.00 12.15 ?  41  VAL   A HA   1 
ATOM   1013 H HB   . VAL   A 1 41  ? 32.635 0.384   -6.329  1.00 13.52 ?  41  VAL   A HB   1 
ATOM   1014 H HG11 . VAL   A 1 41  ? 31.329 -1.001  -7.650  1.00 14.21 ?  41  VAL   A HG11 1 
ATOM   1015 H HG12 . VAL   A 1 41  ? 31.168 -1.382  -6.116  1.00 14.21 ?  41  VAL   A HG12 1 
ATOM   1016 H HG13 . VAL   A 1 41  ? 30.035 -0.544  -6.849  1.00 14.21 ?  41  VAL   A HG13 1 
ATOM   1017 H HG21 . VAL   A 1 41  ? 31.752 1.275   -8.335  1.00 14.54 ?  41  VAL   A HG21 1 
ATOM   1018 H HG22 . VAL   A 1 41  ? 30.613 1.970   -7.473  1.00 14.54 ?  41  VAL   A HG22 1 
ATOM   1019 H HG23 . VAL   A 1 41  ? 32.130 2.394   -7.273  1.00 14.54 ?  41  VAL   A HG23 1 
ATOM   1020 N N    A TYR   A 1 42  ? 31.562 3.464   -4.609  0.62 9.95  ?  42  TYR   A N    1 
ATOM   1021 N N    B TYR   A 1 42  ? 31.575 3.466   -4.618  0.38 9.92  ?  42  TYR   A N    1 
ATOM   1022 C CA   A TYR   A 1 42  ? 32.300 4.654   -4.207  0.62 10.00 ?  42  TYR   A CA   1 
ATOM   1023 C CA   B TYR   A 1 42  ? 32.336 4.636   -4.194  0.38 9.80  ?  42  TYR   A CA   1 
ATOM   1024 C C    A TYR   A 1 42  ? 32.074 5.009   -2.747  0.62 9.85  ?  42  TYR   A C    1 
ATOM   1025 C C    B TYR   A 1 42  ? 32.034 5.040   -2.761  0.38 9.69  ?  42  TYR   A C    1 
ATOM   1026 O O    A TYR   A 1 42  ? 32.675 5.968   -2.247  0.62 10.56 ?  42  TYR   A O    1 
ATOM   1027 O O    B TYR   A 1 42  ? 32.550 6.061   -2.293  0.38 9.91  ?  42  TYR   A O    1 
ATOM   1028 C CB   A TYR   A 1 42  ? 31.917 5.842   -5.111  0.62 11.01 ?  42  TYR   A CB   1 
ATOM   1029 C CB   B TYR   A 1 42  ? 32.079 5.820   -5.140  0.38 10.06 ?  42  TYR   A CB   1 
ATOM   1030 C CG   A TYR   A 1 42  ? 32.079 5.547   -6.590  0.62 11.77 ?  42  TYR   A CG   1 
ATOM   1031 C CG   B TYR   A 1 42  ? 32.330 5.479   -6.590  0.38 10.53 ?  42  TYR   A CG   1 
ATOM   1032 C CD1  A TYR   A 1 42  ? 33.332 5.326   -7.140  0.62 11.99 ?  42  TYR   A CD1  1 
ATOM   1033 C CD1  B TYR   A 1 42  ? 33.619 5.280   -7.060  0.38 11.06 ?  42  TYR   A CD1  1 
ATOM   1034 C CD2  A TYR   A 1 42  ? 30.975 5.472   -7.432  0.62 13.20 ?  42  TYR   A CD2  1 
ATOM   1035 C CD2  B TYR   A 1 42  ? 31.275 5.325   -7.481  0.38 11.08 ?  42  TYR   A CD2  1 
ATOM   1036 C CE1  A TYR   A 1 42  ? 33.484 5.041   -8.488  0.62 12.29 ?  42  TYR   A CE1  1 
ATOM   1037 C CE1  B TYR   A 1 42  ? 33.852 4.945   -8.382  0.38 11.57 ?  42  TYR   A CE1  1 
ATOM   1038 C CE2  A TYR   A 1 42  ? 31.118 5.198   -8.783  0.62 13.65 ?  42  TYR   A CE2  1 
ATOM   1039 C CE2  B TYR   A 1 42  ? 31.501 5.000   -8.806  0.38 11.35 ?  42  TYR   A CE2  1 
ATOM   1040 C CZ   A TYR   A 1 42  ? 32.376 4.981   -9.304  0.62 13.29 ?  42  TYR   A CZ   1 
ATOM   1041 C CZ   B TYR   A 1 42  ? 32.791 4.811   -9.251  0.38 11.44 ?  42  TYR   A CZ   1 
ATOM   1042 O OH   A TYR   A 1 42  ? 32.537 4.704   -10.643 0.62 14.37 ?  42  TYR   A OH   1 
ATOM   1043 O OH   B TYR   A 1 42  ? 33.014 4.479   -10.566 0.38 12.56 ?  42  TYR   A OH   1 
ATOM   1044 H H    A TYR   A 1 42  ? 30.766 3.636   -4.894  0.62 11.95 ?  42  TYR   A H    1 
ATOM   1045 H H    B TYR   A 1 42  ? 30.788 3.653   -4.918  0.38 11.92 ?  42  TYR   A H    1 
ATOM   1046 H HA   A TYR   A 1 42  ? 33.245 4.491   -4.333  0.62 12.02 ?  42  TYR   A HA   1 
ATOM   1047 H HA   B TYR   A 1 42  ? 33.279 4.427   -4.244  0.38 11.77 ?  42  TYR   A HA   1 
ATOM   1048 H HB2  A TYR   A 1 42  ? 30.986 6.073   -4.956  0.62 13.22 ?  42  TYR   A HB2  1 
ATOM   1049 H HB2  B TYR   A 1 42  ? 31.153 6.099   -5.054  0.38 12.09 ?  42  TYR   A HB2  1 
ATOM   1050 H HB3  A TYR   A 1 42  ? 32.483 6.600   -4.898  0.62 13.22 ?  42  TYR   A HB3  1 
ATOM   1051 H HB3  B TYR   A 1 42  ? 32.669 6.550   -4.898  0.38 12.09 ?  42  TYR   A HB3  1 
ATOM   1052 H HD1  A TYR   A 1 42  ? 34.085 5.360   -6.595  0.62 14.40 ?  42  TYR   A HD1  1 
ATOM   1053 H HD1  B TYR   A 1 42  ? 34.339 5.368   -6.475  0.38 13.28 ?  42  TYR   A HD1  1 
ATOM   1054 H HD2  A TYR   A 1 42  ? 30.125 5.620   -7.089  0.62 15.86 ?  42  TYR   A HD2  1 
ATOM   1055 H HD2  B TYR   A 1 42  ? 30.403 5.455   -7.184  0.38 13.31 ?  42  TYR   A HD2  1 
ATOM   1056 H HE1  A TYR   A 1 42  ? 34.335 4.893   -8.843  0.62 14.77 ?  42  TYR   A HE1  1 
ATOM   1057 H HE1  B TYR   A 1 42  ? 34.724 4.822   -8.685  0.38 13.90 ?  42  TYR   A HE1  1 
ATOM   1058 H HE2  A TYR   A 1 42  ? 30.371 5.154   -9.339  0.62 16.40 ?  42  TYR   A HE2  1 
ATOM   1059 H HE2  B TYR   A 1 42  ? 30.784 4.910   -9.394  0.38 13.63 ?  42  TYR   A HE2  1 
ATOM   1060 H HH   A TYR   A 1 42  ? 31.796 4.695   -11.035 0.62 17.26 ?  42  TYR   A HH   1 
ATOM   1061 H HH   B TYR   A 1 42  ? 33.818 4.266   -10.673 0.38 15.08 ?  42  TYR   A HH   1 
ATOM   1062 N N    . LEU   A 1 43  ? 31.206 4.265   -2.063  1.00 9.66  ?  43  LEU   A N    1 
ATOM   1063 C CA   . LEU   A 1 43  ? 30.768 4.600   -0.712  1.00 9.19  ?  43  LEU   A CA   1 
ATOM   1064 C C    . LEU   A 1 43  ? 30.295 6.049   -0.613  1.00 9.43  ?  43  LEU   A C    1 
ATOM   1065 O O    . LEU   A 1 43  ? 30.563 6.744   0.367   1.00 10.65 ?  43  LEU   A O    1 
ATOM   1066 C CB   . LEU   A 1 43  ? 31.820 4.284   0.354   1.00 9.86  ?  43  LEU   A CB   1 
ATOM   1067 C CG   . LEU   A 1 43  ? 32.308 2.828   0.437   1.00 9.99  ?  43  LEU   A CG   1 
ATOM   1068 C CD1  . LEU   A 1 43  ? 33.355 2.714   1.534   1.00 11.18 ?  43  LEU   A CD1  1 
ATOM   1069 C CD2  . LEU   A 1 43  ? 31.170 1.850   0.688   1.00 10.66 ?  43  LEU   A CD2  1 
ATOM   1070 H H    A LEU   A 1 43  ? 30.846 3.541   -2.365  0.62 11.61 ?  43  LEU   A H    1 
ATOM   1071 H H    B LEU   A 1 43  ? 30.882 3.518   -2.351  0.38 11.61 ?  43  LEU   A H    1 
ATOM   1072 H HA   . LEU   A 1 43  ? 29.996 4.045   -0.509  1.00 11.05 ?  43  LEU   A HA   1 
ATOM   1073 H HB2  . LEU   A 1 43  ? 32.594 4.843   0.194   1.00 11.85 ?  43  LEU   A HB2  1 
ATOM   1074 H HB3  . LEU   A 1 43  ? 31.442 4.507   1.225   1.00 11.85 ?  43  LEU   A HB3  1 
ATOM   1075 H HG   . LEU   A 1 43  ? 32.731 2.594   -0.401  1.00 12.01 ?  43  LEU   A HG   1 
ATOM   1076 H HD11 . LEU   A 1 43  ? 33.665 1.795   1.585   1.00 13.43 ?  43  LEU   A HD11 1 
ATOM   1077 H HD12 . LEU   A 1 43  ? 34.101 3.302   1.330   1.00 13.43 ?  43  LEU   A HD12 1 
ATOM   1078 H HD13 . LEU   A 1 43  ? 32.959 2.973   2.384   1.00 13.43 ?  43  LEU   A HD13 1 
ATOM   1079 H HD21 . LEU   A 1 43  ? 31.547 0.965   0.811   1.00 12.80 ?  43  LEU   A HD21 1 
ATOM   1080 H HD22 . LEU   A 1 43  ? 30.695 2.124   1.486   1.00 12.80 ?  43  LEU   A HD22 1 
ATOM   1081 H HD23 . LEU   A 1 43  ? 30.580 1.860   -0.077  1.00 12.80 ?  43  LEU   A HD23 1 
ATOM   1082 N N    . LYS   A 1 44  ? 29.565 6.494   -1.636  1.00 9.86  ?  44  LYS   A N    1 
ATOM   1083 C CA   . LYS   A 1 44  ? 28.923 7.806   -1.624  1.00 9.88  ?  44  LYS   A CA   1 
ATOM   1084 C C    . LYS   A 1 44  ? 27.501 7.618   -1.115  1.00 9.30  ?  44  LYS   A C    1 
ATOM   1085 O O    . LYS   A 1 44  ? 26.632 7.106   -1.824  1.00 10.24 ?  44  LYS   A O    1 
ATOM   1086 C CB   . LYS   A 1 44  ? 28.959 8.431   -3.011  1.00 11.92 ?  44  LYS   A CB   1 
ATOM   1087 C CG   . LYS   A 1 44  ? 30.338 8.897   -3.448  1.00 15.35 ?  44  LYS   A CG   1 
ATOM   1088 C CD   . LYS   A 1 44  ? 31.013 9.775   -2.399  1.00 21.16 ?  44  LYS   A CD   1 
ATOM   1089 C CE   . LYS   A 1 44  ? 32.350 10.291  -2.889  1.00 23.84 ?  44  LYS   A CE   1 
ATOM   1090 N NZ   . LYS   A 1 44  ? 33.228 10.731  -1.770  1.00 25.33 ?  44  LYS   A NZ   1 
ATOM   1091 H H    . LYS   A 1 44  ? 29.429 6.050   -2.360  1.00 11.84 ?  44  LYS   A H    1 
ATOM   1092 H HA   . LYS   A 1 44  ? 29.378 8.382   -0.991  1.00 11.88 ?  44  LYS   A HA   1 
ATOM   1093 H HB2  . LYS   A 1 44  ? 28.646 7.780   -3.656  1.00 14.32 ?  44  LYS   A HB2  1 
ATOM   1094 H HB3  . LYS   A 1 44  ? 28.369 9.205   -3.017  1.00 14.32 ?  44  LYS   A HB3  1 
ATOM   1095 H HG2  . LYS   A 1 44  ? 30.898 8.124   -3.606  1.00 18.44 ?  44  LYS   A HG2  1 
ATOM   1096 H HG3  . LYS   A 1 44  ? 30.251 9.420   -4.264  1.00 18.44 ?  44  LYS   A HG3  1 
ATOM   1097 H HD2  . LYS   A 1 44  ? 30.436 10.526  -2.193  1.00 25.41 ?  44  LYS   A HD2  1 
ATOM   1098 H HD3  . LYS   A 1 44  ? 31.177 9.246   -1.600  1.00 25.41 ?  44  LYS   A HD3  1 
ATOM   1099 H HE2  . LYS   A 1 44  ? 32.807 9.582   -3.368  1.00 28.63 ?  44  LYS   A HE2  1 
ATOM   1100 H HE3  . LYS   A 1 44  ? 32.201 11.048  -3.472  1.00 28.63 ?  44  LYS   A HE3  1 
ATOM   1101 H HZ1  . LYS   A 1 44  ? 34.003 11.029  -2.091  1.00 30.42 ?  44  LYS   A HZ1  1 
ATOM   1102 H HZ2  . LYS   A 1 44  ? 32.833 11.387  -1.313  1.00 30.42 ?  44  LYS   A HZ2  1 
ATOM   1103 H HZ3  . LYS   A 1 44  ? 33.386 10.051  -1.218  1.00 30.42 ?  44  LYS   A HZ3  1 
ATOM   1104 N N    . HIS   A 1 45  ? 27.266 8.016   0.130   1.00 9.04  ?  45  HIS   A N    1 
ATOM   1105 C CA   . HIS   A 1 45  ? 26.028 7.675   0.829   1.00 9.48  ?  45  HIS   A CA   1 
ATOM   1106 C C    . HIS   A 1 45  ? 25.009 8.801   0.660   1.00 10.16 ?  45  HIS   A C    1 
ATOM   1107 O O    . HIS   A 1 45  ? 24.707 9.556   1.582   1.00 12.15 ?  45  HIS   A O    1 
ATOM   1108 C CB   . HIS   A 1 45  ? 26.324 7.410   2.294   1.00 9.44  ?  45  HIS   A CB   1 
ATOM   1109 C CG   . HIS   A 1 45  ? 27.434 6.438   2.514   1.00 8.94  ?  45  HIS   A CG   1 
ATOM   1110 N ND1  . HIS   A 1 45  ? 27.424 5.153   2.005   1.00 9.25  ?  45  HIS   A ND1  1 
ATOM   1111 C CD2  . HIS   A 1 45  ? 28.599 6.581   3.192   1.00 9.38  ?  45  HIS   A CD2  1 
ATOM   1112 C CE1  . HIS   A 1 45  ? 28.547 4.554   2.365   1.00 8.86  ?  45  HIS   A CE1  1 
ATOM   1113 N NE2  . HIS   A 1 45  ? 29.273 5.393   3.090   1.00 9.35  ?  45  HIS   A NE2  1 
ATOM   1114 H H    . HIS   A 1 45  ? 27.804 8.496   0.599   1.00 10.87 ?  45  HIS   A H    1 
ATOM   1115 H HA   . HIS   A 1 45  ? 25.652 6.867   0.443   1.00 11.39 ?  45  HIS   A HA   1 
ATOM   1116 H HB2  . HIS   A 1 45  ? 26.562 8.247   2.721   1.00 11.34 ?  45  HIS   A HB2  1 
ATOM   1117 H HB3  . HIS   A 1 45  ? 25.520 7.050   2.714   1.00 11.34 ?  45  HIS   A HB3  1 
ATOM   1118 H HD2  . HIS   A 1 45  ? 28.890 7.344   3.641   1.00 11.27 ?  45  HIS   A HD2  1 
ATOM   1119 H HE1  . HIS   A 1 45  ? 28.779 3.678   2.164   1.00 10.65 ?  45  HIS   A HE1  1 
ATOM   1120 H HE2  . HIS   A 1 45  ? 30.043 5.219   3.435   1.00 11.24 ?  45  HIS   A HE2  1 
ATOM   1121 N N    A GLY   A 1 46  ? 24.415 8.852   -0.530  0.62 11.38 ?  46  GLY   A N    1 
ATOM   1122 N N    B GLY   A 1 46  ? 24.525 8.940   -0.571  0.38 10.82 ?  46  GLY   A N    1 
ATOM   1123 C CA   A GLY   A 1 46  ? 23.549 9.961   -0.885  0.62 12.24 ?  46  GLY   A CA   1 
ATOM   1124 C CA   B GLY   A 1 46  ? 23.754 10.114  -0.942  0.38 11.38 ?  46  GLY   A CA   1 
ATOM   1125 C C    A GLY   A 1 46  ? 22.073 9.786   -0.585  0.62 11.93 ?  46  GLY   A C    1 
ATOM   1126 C C    B GLY   A 1 46  ? 22.276 10.040  -0.622  0.38 10.88 ?  46  GLY   A C    1 
ATOM   1127 O O    A GLY   A 1 46  ? 21.409 10.736  -0.152  0.62 12.87 ?  46  GLY   A O    1 
ATOM   1128 O O    B GLY   A 1 46  ? 21.638 11.063  -0.351  0.38 11.38 ?  46  GLY   A O    1 
ATOM   1129 H H    A GLY   A 1 46  ? 24.486 8.255   -1.146  0.62 13.67 ?  46  GLY   A H    1 
ATOM   1130 H H    B GLY   A 1 46  ? 24.621 8.369   -1.206  0.38 13.00 ?  46  GLY   A H    1 
ATOM   1131 H HA2  A GLY   A 1 46  ? 23.841 10.753  -0.407  0.62 14.71 ?  46  GLY   A HA2  1 
ATOM   1132 H HA2  B GLY   A 1 46  ? 24.121 10.889  -0.486  0.38 13.67 ?  46  GLY   A HA2  1 
ATOM   1133 H HA3  A GLY   A 1 46  ? 23.636 10.138  -1.833  0.62 14.71 ?  46  GLY   A HA3  1 
ATOM   1134 H HA3  B GLY   A 1 46  ? 23.838 10.260  -1.896  0.38 13.67 ?  46  GLY   A HA3  1 
ATOM   1135 N N    A GLY   A 1 47  ? 21.541 8.591   -0.825  0.62 11.69 ?  47  GLY   A N    1 
ATOM   1136 N N    B GLY   A 1 47  ? 21.712 8.840   -0.671  0.38 10.20 ?  47  GLY   A N    1 
ATOM   1137 C CA   A GLY   A 1 47  ? 20.110 8.385   -0.762  0.62 11.34 ?  47  GLY   A CA   1 
ATOM   1138 C CA   B GLY   A 1 47  ? 20.285 8.669   -0.480  0.38 10.98 ?  47  GLY   A CA   1 
ATOM   1139 C C    A GLY   A 1 47  ? 19.769 6.983   -0.309  0.62 10.68 ?  47  GLY   A C    1 
ATOM   1140 C C    B GLY   A 1 47  ? 19.972 7.232   -0.118  0.38 10.94 ?  47  GLY   A C    1 
ATOM   1141 O O    A GLY   A 1 47  ? 20.648 6.164   -0.039  0.62 10.57 ?  47  GLY   A O    1 
ATOM   1142 O O    B GLY   A 1 47  ? 20.865 6.401   0.061   0.38 11.13 ?  47  GLY   A O    1 
ATOM   1143 H H    A GLY   A 1 47  ? 21.991 7.880   -1.015  0.62 14.04 ?  47  GLY   A H    1 
ATOM   1144 H H    B GLY   A 1 47  ? 22.137 8.113   -0.812  0.38 12.26 ?  47  GLY   A H    1 
ATOM   1145 H HA2  A GLY   A 1 47  ? 19.712 9.010   -0.138  0.62 13.62 ?  47  GLY   A HA2  1 
ATOM   1146 H HA2  B GLY   A 1 47  ? 19.969 9.252   0.231   0.38 13.19 ?  47  GLY   A HA2  1 
ATOM   1147 H HA3  A GLY   A 1 47  ? 19.718 8.526   -1.638  0.62 13.62 ?  47  GLY   A HA3  1 
ATOM   1148 H HA3  B GLY   A 1 47  ? 19.812 8.894   -1.299  0.38 13.19 ?  47  GLY   A HA3  1 
ATOM   1149 N N    A GLY   A 1 48  ? 18.471 6.707   -0.237  0.62 10.87 ?  48  GLY   A N    1 
ATOM   1150 N N    B GLY   A 1 48  ? 18.680 6.948   -0.010  0.38 11.19 ?  48  GLY   A N    1 
ATOM   1151 C CA   A GLY   A 1 48  ? 18.041 5.395   0.187   0.62 11.24 ?  48  GLY   A CA   1 
ATOM   1152 C CA   B GLY   A 1 48  ? 18.226 5.624   0.357   0.38 11.07 ?  48  GLY   A CA   1 
ATOM   1153 C C    A GLY   A 1 48  ? 18.514 5.091   1.592   0.62 10.56 ?  48  GLY   A C    1 
ATOM   1154 C C    B GLY   A 1 48  ? 18.699 5.226   1.743   0.38 10.49 ?  48  GLY   A C    1 
ATOM   1155 O O    A GLY   A 1 48  ? 18.628 5.975   2.450   0.62 11.25 ?  48  GLY   A O    1 
ATOM   1156 O O    B GLY   A 1 48  ? 18.885 6.059   2.640   0.38 10.99 ?  48  GLY   A O    1 
ATOM   1157 H H    A GLY   A 1 48  ? 17.833 7.256   -0.414  0.62 13.05 ?  48  GLY   A H    1 
ATOM   1158 H H    B GLY   A 1 48  ? 18.052 7.507   -0.149  0.38 13.44 ?  48  GLY   A H    1 
ATOM   1159 H HA2  A GLY   A 1 48  ? 17.075 5.340   0.177   0.62 13.51 ?  48  GLY   A HA2  1 
ATOM   1160 H HA2  B GLY   A 1 48  ? 17.256 5.596   0.318   0.38 13.30 ?  48  GLY   A HA2  1 
ATOM   1161 H HA3  A GLY   A 1 48  ? 18.401 4.722   -0.413  0.62 13.51 ?  48  GLY   A HA3  1 
ATOM   1162 H HA3  B GLY   A 1 48  ? 18.576 4.973   -0.272  0.38 13.30 ?  48  GLY   A HA3  1 
ATOM   1163 N N    A VAL   A 1 49  ? 18.801 3.812   1.832   0.62 10.18 ?  49  VAL   A N    1 
ATOM   1164 N N    B VAL   A 1 49  ? 18.901 3.917   1.917   0.38 9.42  ?  49  VAL   A N    1 
ATOM   1165 C CA   A VAL   A 1 49  ? 19.304 3.386   3.134   0.62 10.38 ?  49  VAL   A CA   1 
ATOM   1166 C CA   B VAL   A 1 49  ? 19.427 3.393   3.175   0.38 9.11  ?  49  VAL   A CA   1 
ATOM   1167 C C    A VAL   A 1 49  ? 20.607 4.104   3.468   0.62 9.51  ?  49  VAL   A C    1 
ATOM   1168 C C    B VAL   A 1 49  ? 20.751 4.062   3.520   0.38 8.22  ?  49  VAL   A C    1 
ATOM   1169 O O    A VAL   A 1 49  ? 20.804 4.560   4.598   0.62 9.74  ?  49  VAL   A O    1 
ATOM   1170 O O    B VAL   A 1 49  ? 20.997 4.418   4.678   0.38 8.22  ?  49  VAL   A O    1 
ATOM   1171 C CB   A VAL   A 1 49  ? 19.478 1.856   3.158   0.62 11.18 ?  49  VAL   A CB   1 
ATOM   1172 C CB   B VAL   A 1 49  ? 19.576 1.860   3.087   0.38 9.40  ?  49  VAL   A CB   1 
ATOM   1173 C CG1  A VAL   A 1 49  ? 20.261 1.423   4.388   0.62 11.69 ?  49  VAL   A CG1  1 
ATOM   1174 C CG1  B VAL   A 1 49  ? 20.435 1.331   4.233   0.38 8.99  ?  49  VAL   A CG1  1 
ATOM   1175 C CG2  A VAL   A 1 49  ? 18.119 1.168   3.105   0.62 12.95 ?  49  VAL   A CG2  1 
ATOM   1176 C CG2  B VAL   A 1 49  ? 18.212 1.179   3.073   0.38 10.91 ?  49  VAL   A CG2  1 
ATOM   1177 H H    A VAL   A 1 49  ? 18.707 3.169   1.267   0.62 12.23 ?  49  VAL   A H    1 
ATOM   1178 H H    B VAL   A 1 49  ? 18.753 3.315   1.320   0.38 11.31 ?  49  VAL   A H    1 
ATOM   1179 H HA   A VAL   A 1 49  ? 18.660 3.620   3.817   0.62 12.47 ?  49  VAL   A HA   1 
ATOM   1180 H HA   B VAL   A 1 49  ? 18.800 3.586   3.889   0.38 10.95 ?  49  VAL   A HA   1 
ATOM   1181 H HB   A VAL   A 1 49  ? 19.984 1.582   2.377   0.62 13.43 ?  49  VAL   A HB   1 
ATOM   1182 H HB   B VAL   A 1 49  ? 20.025 1.634   2.258   0.38 11.30 ?  49  VAL   A HB   1 
ATOM   1183 H HG11 A VAL   A 1 49  ? 20.113 0.478   4.536   0.62 14.04 ?  49  VAL   A HG11 1 
ATOM   1184 H HG11 B VAL   A 1 49  ? 20.281 0.378   4.328   0.38 10.81 ?  49  VAL   A HG11 1 
ATOM   1185 H HG12 A VAL   A 1 49  ? 21.204 1.592   4.240   0.62 14.04 ?  49  VAL   A HG12 1 
ATOM   1186 H HG12 B VAL   A 1 49  ? 21.369 1.496   4.034   0.38 10.81 ?  49  VAL   A HG12 1 
ATOM   1187 H HG13 A VAL   A 1 49  ? 19.946 1.931   5.153   0.62 14.04 ?  49  VAL   A HG13 1 
ATOM   1188 H HG13 B VAL   A 1 49  ? 20.182 1.786   5.052   0.38 10.81 ?  49  VAL   A HG13 1 
ATOM   1189 H HG21 A VAL   A 1 49  ? 18.250 0.206   3.121   0.62 15.56 ?  49  VAL   A HG21 1 
ATOM   1190 H HG21 B VAL   A 1 49  ? 18.337 0.217   3.009   0.38 13.11 ?  49  VAL   A HG21 1 
ATOM   1191 H HG22 A VAL   A 1 49  ? 17.595 1.443   3.874   0.62 15.56 ?  49  VAL   A HG22 1 
ATOM   1192 H HG22 B VAL   A 1 49  ? 17.741 1.395   3.894   0.38 13.11 ?  49  VAL   A HG22 1 
ATOM   1193 H HG23 A VAL   A 1 49  ? 17.668 1.426   2.286   0.62 15.56 ?  49  VAL   A HG23 1 
ATOM   1194 H HG23 B VAL   A 1 49  ? 17.708 1.497   2.309   0.38 13.11 ?  49  VAL   A HG23 1 
ATOM   1195 N N    A ALA   A 1 50  ? 21.525 4.178   2.501   0.62 9.08  ?  50  ALA   A N    1 
ATOM   1196 N N    B ALA   A 1 50  ? 21.636 4.208   2.530   0.38 8.19  ?  50  ALA   A N    1 
ATOM   1197 C CA   A ALA   A 1 50  ? 22.852 4.728   2.768   0.62 8.99  ?  50  ALA   A CA   1 
ATOM   1198 C CA   B ALA   A 1 50  ? 22.951 4.785   2.793   0.38 8.40  ?  50  ALA   A CA   1 
ATOM   1199 C C    A ALA   A 1 50  ? 22.768 6.184   3.201   0.62 8.73  ?  50  ALA   A C    1 
ATOM   1200 C C    B ALA   A 1 50  ? 22.832 6.238   3.228   0.38 8.26  ?  50  ALA   A C    1 
ATOM   1201 O O    A ALA   A 1 50  ? 23.417 6.595   4.169   0.62 9.48  ?  50  ALA   A O    1 
ATOM   1202 O O    B ALA   A 1 50  ? 23.458 6.660   4.209   0.38 8.62  ?  50  ALA   A O    1 
ATOM   1203 C CB   A ALA   A 1 50  ? 23.720 4.592   1.520   0.62 8.83  ?  50  ALA   A CB   1 
ATOM   1204 C CB   B ALA   A 1 50  ? 23.830 4.665   1.548   0.38 8.59  ?  50  ALA   A CB   1 
ATOM   1205 H H    A ALA   A 1 50  ? 21.412 3.913   1.693   0.62 10.92 ?  50  ALA   A H    1 
ATOM   1206 H H    B ALA   A 1 50  ? 21.496 3.975   1.710   0.38 9.84  ?  50  ALA   A H    1 
ATOM   1207 H HA   A ALA   A 1 50  ? 23.272 4.235   3.488   0.62 10.80 ?  50  ALA   A HA   1 
ATOM   1208 H HA   B ALA   A 1 50  ? 23.372 4.293   3.510   0.38 10.09 ?  50  ALA   A HA   1 
ATOM   1209 H HB1  A ALA   A 1 50  ? 24.597 4.965   1.702   0.62 10.62 ?  50  ALA   A HB1  1 
ATOM   1210 H HB1  B ALA   A 1 50  ? 24.698 5.054   1.740   0.38 10.32 ?  50  ALA   A HB1  1 
ATOM   1211 H HB2  A ALA   A 1 50  ? 23.798 3.654   1.294   0.62 10.62 ?  50  ALA   A HB2  1 
ATOM   1212 H HB2  B ALA   A 1 50  ? 23.930 3.727   1.320   0.38 10.32 ?  50  ALA   A HB2  1 
ATOM   1213 H HB3  A ALA   A 1 50  ? 23.301 5.076   0.790   0.62 10.62 ?  50  ALA   A HB3  1 
ATOM   1214 H HB3  B ALA   A 1 50  ? 23.409 5.141   0.815   0.38 10.32 ?  50  ALA   A HB3  1 
ATOM   1215 N N    A GLY   A 1 51  ? 21.986 6.986   2.480   0.62 9.19  ?  51  GLY   A N    1 
ATOM   1216 N N    B GLY   A 1 51  ? 22.035 7.022   2.503   0.38 9.03  ?  51  GLY   A N    1 
ATOM   1217 C CA   A GLY   A 1 51  ? 21.832 8.379   2.864   0.62 9.86  ?  51  GLY   A CA   1 
ATOM   1218 C CA   B GLY   A 1 51  ? 21.844 8.409   2.888   0.38 9.68  ?  51  GLY   A CA   1 
ATOM   1219 C C    A GLY   A 1 51  ? 21.243 8.526   4.252   0.62 9.94  ?  51  GLY   A C    1 
ATOM   1220 C C    B GLY   A 1 51  ? 21.232 8.542   4.267   0.38 9.95  ?  51  GLY   A C    1 
ATOM   1221 O O    A GLY   A 1 51  ? 21.647 9.409   5.015   0.62 10.47 ?  51  GLY   A O    1 
ATOM   1222 O O    B GLY   A 1 51  ? 21.610 9.426   5.040   0.38 10.45 ?  51  GLY   A O    1 
ATOM   1223 H H    A GLY   A 1 51  ? 21.549 6.753   1.776   0.62 11.04 ?  51  GLY   A H    1 
ATOM   1224 H H    B GLY   A 1 51  ? 21.607 6.777   1.796   0.38 10.85 ?  51  GLY   A H    1 
ATOM   1225 H HA2  A GLY   A 1 51  ? 22.694 8.819   2.850   0.62 11.85 ?  51  GLY   A HA2  1 
ATOM   1226 H HA2  B GLY   A 1 51  ? 22.698 8.864   2.887   0.38 11.63 ?  51  GLY   A HA2  1 
ATOM   1227 H HA3  A GLY   A 1 51  ? 21.246 8.828   2.232   0.62 11.85 ?  51  GLY   A HA3  1 
ATOM   1228 H HA3  B GLY   A 1 51  ? 21.260 8.844   2.248   0.38 11.63 ?  51  GLY   A HA3  1 
ATOM   1229 N N    . ALA   A 1 52  ? 20.278 7.666   4.595   1.00 9.84  ?  52  ALA   A N    1 
ATOM   1230 C CA   . ALA   A 1 52  ? 19.641 7.721   5.908   1.00 10.52 ?  52  ALA   A CA   1 
ATOM   1231 C C    . ALA   A 1 52  ? 20.605 7.309   7.022   1.00 10.01 ?  52  ALA   A C    1 
ATOM   1232 O O    . ALA   A 1 52  ? 20.679 7.968   8.065   1.00 10.53 ?  52  ALA   A O    1 
ATOM   1233 C CB   . ALA   A 1 52  ? 18.380 6.849   5.910   1.00 12.32 ?  52  ALA   A CB   1 
ATOM   1234 H H    A ALA   A 1 52  ? 19.983 7.037   4.081   0.62 11.82 ?  52  ALA   A H    1 
ATOM   1235 H H    B ALA   A 1 52  ? 19.992 7.035   4.079   0.38 11.82 ?  52  ALA   A H    1 
ATOM   1236 H HA   . ALA   A 1 52  ? 19.363 8.628   6.080   1.00 12.64 ?  52  ALA   A HA   1 
ATOM   1237 H HB1  . ALA   A 1 52  ? 17.954 6.906   6.782   1.00 14.80 ?  52  ALA   A HB1  1 
ATOM   1238 H HB2  . ALA   A 1 52  ? 17.769 7.169   5.227   1.00 14.80 ?  52  ALA   A HB2  1 
ATOM   1239 H HB3  . ALA   A 1 52  ? 18.625 5.927   5.725   1.00 14.80 ?  52  ALA   A HB3  1 
ATOM   1240 N N    A LEU   A 1 53  ? 21.331 6.208   6.837   0.62 9.50  ?  53  LEU   A N    1 
ATOM   1241 N N    B LEU   A 1 53  ? 21.337 6.206   6.829   0.38 9.59  ?  53  LEU   A N    1 
ATOM   1242 C CA   A LEU   A 1 53  ? 22.305 5.810   7.852   0.62 9.73  ?  53  LEU   A CA   1 
ATOM   1243 C CA   B LEU   A 1 53  ? 22.312 5.783   7.835   0.38 9.63  ?  53  LEU   A CA   1 
ATOM   1244 C C    A LEU   A 1 53  ? 23.347 6.902   8.041   0.62 9.18  ?  53  LEU   A C    1 
ATOM   1245 C C    B LEU   A 1 53  ? 23.384 6.846   8.034   0.38 9.41  ?  53  LEU   A C    1 
ATOM   1246 O O    A LEU   A 1 53  ? 23.652 7.300   9.171   0.62 10.03 ?  53  LEU   A O    1 
ATOM   1247 O O    B LEU   A 1 53  ? 23.772 7.146   9.169   0.38 10.22 ?  53  LEU   A O    1 
ATOM   1248 C CB   A LEU   A 1 53  ? 22.975 4.479   7.481   0.62 9.99  ?  53  LEU   A CB   1 
ATOM   1249 C CB   B LEU   A 1 53  ? 22.975 4.457   7.434   0.38 9.41  ?  53  LEU   A CB   1 
ATOM   1250 C CG   A LEU   A 1 53  ? 22.071 3.237   7.516   0.62 11.00 ?  53  LEU   A CG   1 
ATOM   1251 C CG   B LEU   A 1 53  ? 22.220 3.129   7.583   0.38 9.58  ?  53  LEU   A CG   1 
ATOM   1252 C CD1  A LEU   A 1 53  ? 22.798 2.031   6.947   0.62 11.57 ?  53  LEU   A CD1  1 
ATOM   1253 C CD1  B LEU   A 1 53  ? 22.964 2.038   6.826   0.38 10.10 ?  53  LEU   A CD1  1 
ATOM   1254 C CD2  A LEU   A 1 53  ? 21.581 2.944   8.927   0.62 11.35 ?  53  LEU   A CD2  1 
ATOM   1255 C CD2  B LEU   A 1 53  ? 22.044 2.723   9.040   0.38 9.41  ?  53  LEU   A CD2  1 
ATOM   1256 H H    A LEU   A 1 53  ? 21.278 5.681   6.157   0.62 11.41 ?  53  LEU   A H    1 
ATOM   1257 H H    B LEU   A 1 53  ? 21.286 5.691   6.140   0.38 11.53 ?  53  LEU   A H    1 
ATOM   1258 H HA   A LEU   A 1 53  ? 21.846 5.684   8.698   0.62 11.69 ?  53  LEU   A HA   1 
ATOM   1259 H HA   B LEU   A 1 53  ? 21.858 5.644   8.684   0.38 11.58 ?  53  LEU   A HA   1 
ATOM   1260 H HB2  A LEU   A 1 53  ? 23.330 4.553   6.581   0.62 12.00 ?  53  LEU   A HB2  1 
ATOM   1261 H HB2  B LEU   A 1 53  ? 23.218 4.525   6.499   0.38 11.31 ?  53  LEU   A HB2  1 
ATOM   1262 H HB3  A LEU   A 1 53  ? 23.706 4.319   8.101   0.62 12.00 ?  53  LEU   A HB3  1 
ATOM   1263 H HB3  B LEU   A 1 53  ? 23.784 4.364   7.960   0.38 11.31 ?  53  LEU   A HB3  1 
ATOM   1264 H HG   A LEU   A 1 53  ? 21.293 3.402   6.960   0.62 13.22 ?  53  LEU   A HG   1 
ATOM   1265 H HG   B LEU   A 1 53  ? 21.339 3.216   7.186   0.38 11.51 ?  53  LEU   A HG   1 
ATOM   1266 H HD11 A LEU   A 1 53  ? 22.206 1.263   6.978   0.62 13.90 ?  53  LEU   A HD11 1 
ATOM   1267 H HD11 B LEU   A 1 53  ? 22.490 1.197   6.936   0.38 12.14 ?  53  LEU   A HD11 1 
ATOM   1268 H HD12 A LEU   A 1 53  ? 23.047 2.220   6.028   0.62 13.90 ?  53  LEU   A HD12 1 
ATOM   1269 H HD12 B LEU   A 1 53  ? 23.000 2.275   5.885   0.38 12.14 ?  53  LEU   A HD12 1 
ATOM   1270 H HD13 A LEU   A 1 53  ? 23.591 1.862   7.477   0.62 13.90 ?  53  LEU   A HD13 1 
ATOM   1271 H HD13 B LEU   A 1 53  ? 23.861 1.961   7.183   0.38 12.14 ?  53  LEU   A HD13 1 
ATOM   1272 H HD21 A LEU   A 1 53  ? 21.060 2.125   8.919   0.62 13.63 ?  53  LEU   A HD21 1 
ATOM   1273 H HD21 B LEU   A 1 53  ? 21.512 1.911   9.082   0.38 11.31 ?  53  LEU   A HD21 1 
ATOM   1274 H HD22 A LEU   A 1 53  ? 22.347 2.841   9.513   0.62 13.63 ?  53  LEU   A HD22 1 
ATOM   1275 H HD22 B LEU   A 1 53  ? 22.918 2.564   9.432   0.38 11.31 ?  53  LEU   A HD22 1 
ATOM   1276 H HD23 A LEU   A 1 53  ? 21.029 3.681   9.233   0.62 13.63 ?  53  LEU   A HD23 1 
ATOM   1277 H HD23 B LEU   A 1 53  ? 21.593 3.437   9.515   0.38 11.31 ?  53  LEU   A HD23 1 
ATOM   1278 N N    . ASN   A 1 54  ? 23.887 7.417   6.939   1.00 9.12  ?  54  ASN   A N    1 
ATOM   1279 C CA   . ASN   A 1 54  ? 24.938 8.416   7.057   1.00 9.30  ?  54  ASN   A CA   1 
ATOM   1280 C C    . ASN   A 1 54  ? 24.435 9.662   7.782   1.00 9.51  ?  54  ASN   A C    1 
ATOM   1281 O O    . ASN   A 1 54  ? 25.126 10.210  8.648   1.00 9.98  ?  54  ASN   A O    1 
ATOM   1282 C CB   . ASN   A 1 54  ? 25.496 8.774   5.689   1.00 9.33  ?  54  ASN   A CB   1 
ATOM   1283 C CG   . ASN   A 1 54  ? 26.510 9.873   5.791   1.00 9.42  ?  54  ASN   A CG   1 
ATOM   1284 O OD1  . ASN   A 1 54  ? 27.518 9.730   6.497   1.00 9.60  ?  54  ASN   A OD1  1 
ATOM   1285 N ND2  . ASN   A 1 54  ? 26.250 10.991  5.130   1.00 10.48 ?  54  ASN   A ND2  1 
ATOM   1286 H H    A ASN   A 1 54  ? 23.667 7.205   6.135   0.62 10.95 ?  54  ASN   A H    1 
ATOM   1287 H H    B ASN   A 1 54  ? 23.638 7.239   6.135   0.38 10.95 ?  54  ASN   A H    1 
ATOM   1288 H HA   . ASN   A 1 54  ? 25.660 8.045   7.583   1.00 11.18 ?  54  ASN   A HA   1 
ATOM   1289 H HB2  . ASN   A 1 54  ? 25.926 7.988   5.310   1.00 11.21 ?  54  ASN   A HB2  1 
ATOM   1290 H HB3  . ASN   A 1 54  ? 24.771 9.067   5.115   1.00 11.21 ?  54  ASN   A HB3  1 
ATOM   1291 H HD21 . ASN   A 1 54  ? 26.803 11.647  5.165   1.00 12.59 ?  54  ASN   A HD21 1 
ATOM   1292 H HD22 . ASN   A 1 54  ? 25.533 11.054  4.659   1.00 12.59 ?  54  ASN   A HD22 1 
ATOM   1293 N N    . LYS   A 1 55  ? 23.227 10.122  7.446   1.00 9.92  ?  55  LYS   A N    1 
ATOM   1294 C CA   . LYS   A 1 55  ? 22.648 11.281  8.117   1.00 10.48 ?  55  LYS   A CA   1 
ATOM   1295 C C    . LYS   A 1 55  ? 22.556 11.043  9.617   1.00 10.53 ?  55  LYS   A C    1 
ATOM   1296 O O    . LYS   A 1 55  ? 22.837 11.943  10.419  1.00 11.36 ?  55  LYS   A O    1 
ATOM   1297 C CB   . LYS   A 1 55  ? 21.274 11.580  7.501   1.00 11.80 ?  55  LYS   A CB   1 
ATOM   1298 C CG   . LYS   A 1 55  ? 20.494 12.727  8.127   1.00 13.98 ?  55  LYS   A CG   1 
ATOM   1299 C CD   . LYS   A 1 55  ? 19.175 12.960  7.368   1.00 15.36 ?  55  LYS   A CD   1 
ATOM   1300 C CE   . LYS   A 1 55  ? 18.305 14.030  8.011   1.00 17.47 ?  55  LYS   A CE   1 
ATOM   1301 N NZ   . LYS   A 1 55  ? 16.965 14.139  7.351   1.00 18.36 ?  55  LYS   A NZ   1 
ATOM   1302 H H    . LYS   A 1 55  ? 22.717 9.768   6.848   1.00 11.93 ?  55  LYS   A H    1 
ATOM   1303 H HA   . LYS   A 1 55  ? 23.218 12.048  7.968   1.00 12.59 ?  55  LYS   A HA   1 
ATOM   1304 H HB2  . LYS   A 1 55  ? 21.401 11.798  6.566   1.00 14.18 ?  55  LYS   A HB2  1 
ATOM   1305 H HB3  . LYS   A 1 55  ? 20.726 10.783  7.576   1.00 14.18 ?  55  LYS   A HB3  1 
ATOM   1306 H HG2  . LYS   A 1 55  ? 20.274 12.508  9.049   1.00 16.80 ?  55  LYS   A HG2  1 
ATOM   1307 H HG3  . LYS   A 1 55  ? 21.014 13.540  8.086   1.00 16.80 ?  55  LYS   A HG3  1 
ATOM   1308 H HD2  . LYS   A 1 55  ? 19.376 13.240  6.462   1.00 18.45 ?  55  LYS   A HD2  1 
ATOM   1309 H HD3  . LYS   A 1 55  ? 18.666 12.131  7.351   1.00 18.45 ?  55  LYS   A HD3  1 
ATOM   1310 H HE2  . LYS   A 1 55  ? 18.159 13.809  8.944   1.00 20.98 ?  55  LYS   A HE2  1 
ATOM   1311 H HE3  . LYS   A 1 55  ? 18.746 14.890  7.935   1.00 20.98 ?  55  LYS   A HE3  1 
ATOM   1312 H HZ1  . LYS   A 1 55  ? 16.374 14.506  7.908   1.00 22.05 ?  55  LYS   A HZ1  1 
ATOM   1313 H HZ2  . LYS   A 1 55  ? 17.020 14.650  6.621   1.00 22.05 ?  55  LYS   A HZ2  1 
ATOM   1314 H HZ3  . LYS   A 1 55  ? 16.669 13.332  7.114   1.00 22.05 ?  55  LYS   A HZ3  1 
ATOM   1315 N N    . ALA   A 1 56  ? 22.156 9.835   10.017  1.00 10.99 ?  56  ALA   A N    1 
ATOM   1316 C CA   . ALA   A 1 56  ? 22.041 9.501   11.431  1.00 11.73 ?  56  ALA   A CA   1 
ATOM   1317 C C    . ALA   A 1 56  ? 23.386 9.524   12.152  1.00 11.80 ?  56  ALA   A C    1 
ATOM   1318 O O    . ALA   A 1 56  ? 23.410 9.707   13.372  1.00 13.04 ?  56  ALA   A O    1 
ATOM   1319 C CB   . ALA   A 1 56  ? 21.357 8.141   11.608  1.00 12.43 ?  56  ALA   A CB   1 
ATOM   1320 H H    . ALA   A 1 56  ? 21.943 9.198   9.486   1.00 13.20 ?  56  ALA   A H    1 
ATOM   1321 H HA   . ALA   A 1 56  ? 21.475 10.157  11.860  1.00 14.09 ?  56  ALA   A HA   1 
ATOM   1322 H HB1  . ALA   A 1 56  ? 21.287 7.937   12.556  1.00 14.94 ?  56  ALA   A HB1  1 
ATOM   1323 H HB2  . ALA   A 1 56  ? 20.469 8.177   11.216  1.00 14.94 ?  56  ALA   A HB2  1 
ATOM   1324 H HB3  . ALA   A 1 56  ? 21.883 7.456   11.164  1.00 14.94 ?  56  ALA   A HB3  1 
ATOM   1325 N N    . THR   A 1 57  ? 24.499 9.338   11.437  1.00 10.80 ?  57  THR   A N    1 
ATOM   1326 C CA   . THR   A 1 57  ? 25.841 9.455   12.013  1.00 10.72 ?  57  THR   A CA   1 
ATOM   1327 C C    . THR   A 1 57  ? 26.401 10.869  11.934  1.00 11.16 ?  57  THR   A C    1 
ATOM   1328 O O    . THR   A 1 57  ? 27.587 11.074  12.223  1.00 11.65 ?  57  THR   A O    1 
ATOM   1329 C CB   . THR   A 1 57  ? 26.846 8.500   11.343  1.00 10.55 ?  57  THR   A CB   1 
ATOM   1330 O OG1  . THR   A 1 57  ? 27.228 8.991   10.043  1.00 10.41 ?  57  THR   A OG1  1 
ATOM   1331 C CG2  . THR   A 1 57  ? 26.302 7.096   11.241  1.00 10.93 ?  57  THR   A CG2  1 
ATOM   1332 H H    . THR   A 1 57  ? 24.501 9.123   10.602  1.00 12.97 ?  57  THR   A H    1 
ATOM   1333 H HA   . THR   A 1 57  ? 25.789 9.202   12.954  1.00 12.88 ?  57  THR   A HA   1 
ATOM   1334 H HB   . THR   A 1 57  ? 27.644 8.458   11.904  1.00 12.67 ?  57  THR   A HB   1 
ATOM   1335 H HG1  . THR   A 1 57  ? 26.547 9.054   9.556   1.00 12.51 ?  57  THR   A HG1  1 
ATOM   1336 H HG21 . THR   A 1 57  ? 27.027 6.458   11.155  1.00 13.13 ?  57  THR   A HG21 1 
ATOM   1337 H HG22 . THR   A 1 57  ? 25.783 6.877   12.032  1.00 13.13 ?  57  THR   A HG22 1 
ATOM   1338 H HG23 . THR   A 1 57  ? 25.727 7.021   10.462  1.00 13.13 ?  57  THR   A HG23 1 
ATOM   1339 N N    . ASN   A 1 58  ? 25.593 11.844  11.532  1.00 11.61 ?  58  ASN   A N    1 
ATOM   1340 C CA   . ASN   A 1 58  ? 26.064 13.221  11.444  1.00 12.36 ?  58  ASN   A CA   1 
ATOM   1341 C C    . ASN   A 1 58  ? 27.201 13.350  10.426  1.00 11.33 ?  58  ASN   A C    1 
ATOM   1342 O O    . ASN   A 1 58  ? 28.096 14.186  10.576  1.00 12.10 ?  58  ASN   A O    1 
ATOM   1343 C CB   . ASN   A 1 58  ? 26.461 13.739  12.841  1.00 15.20 ?  58  ASN   A CB   1 
ATOM   1344 C CG   . ASN   A 1 58  ? 26.881 15.194  12.851  1.00 18.81 ?  58  ASN   A CG   1 
ATOM   1345 O OD1  . ASN   A 1 58  ? 26.256 16.029  12.207  1.00 20.56 ?  58  ASN   A OD1  1 
ATOM   1346 N ND2  . ASN   A 1 58  ? 27.940 15.508  13.608  1.00 19.82 ?  58  ASN   A ND2  1 
ATOM   1347 H H    . ASN   A 1 58  ? 24.771 11.728  11.296  1.00 13.95 ?  58  ASN   A H    1 
ATOM   1348 H HA   . ASN   A 1 58  ? 25.329 13.767  11.134  1.00 14.85 ?  58  ASN   A HA   1 
ATOM   1349 H HB2  . ASN   A 1 58  ? 25.697 13.641  13.444  1.00 18.26 ?  58  ASN   A HB2  1 
ATOM   1350 H HB3  . ASN   A 1 58  ? 27.204 13.220  13.181  1.00 18.26 ?  58  ASN   A HB3  1 
ATOM   1351 H HD21 . ASN   A 1 58  ? 28.210 16.326  13.654  1.00 23.80 ?  58  ASN   A HD21 1 
ATOM   1352 H HD22 . ASN   A 1 58  ? 28.351 14.896  14.047  1.00 23.80 ?  58  ASN   A HD22 1 
ATOM   1353 N N    . ASN   A 1 59  ? 27.163 12.535  9.366   1.00 10.54 ?  59  ASN   A N    1 
ATOM   1354 C CA   . ASN   A 1 59  ? 28.143 12.512  8.268   1.00 10.22 ?  59  ASN   A CA   1 
ATOM   1355 C C    . ASN   A 1 59  ? 29.464 11.830  8.650   1.00 9.99  ?  59  ASN   A C    1 
ATOM   1356 O O    . ASN   A 1 59  ? 30.374 11.779  7.815   1.00 10.38 ?  59  ASN   A O    1 
ATOM   1357 C CB   . ASN   A 1 59  ? 28.431 13.902  7.662   1.00 10.53 ?  59  ASN   A CB   1 
ATOM   1358 C CG   . ASN   A 1 59  ? 28.787 13.835  6.190   1.00 10.64 ?  59  ASN   A CG   1 
ATOM   1359 O OD1  . ASN   A 1 59  ? 28.077 13.212  5.393   1.00 10.89 ?  59  ASN   A OD1  1 
ATOM   1360 N ND2  . ASN   A 1 59  ? 29.877 14.488  5.815   1.00 11.67 ?  59  ASN   A ND2  1 
ATOM   1361 H H    . ASN   A 1 59  ? 26.534 11.955  9.248   1.00 12.67 ?  59  ASN   A H    1 
ATOM   1362 H HA   . ASN   A 1 59  ? 27.757 11.982  7.556   1.00 12.28 ?  59  ASN   A HA   1 
ATOM   1363 H HB2  . ASN   A 1 59  ? 27.643 14.458  7.750   1.00 12.65 ?  59  ASN   A HB2  1 
ATOM   1364 H HB3  . ASN   A 1 59  ? 29.178 14.303  8.129   1.00 12.65 ?  59  ASN   A HB3  1 
ATOM   1365 H HD21 . ASN   A 1 59  ? 30.125 14.477  4.997   1.00 14.02 ?  59  ASN   A HD21 1 
ATOM   1366 H HD22 . ASN   A 1 59  ? 30.354 14.905  6.405   1.00 14.02 ?  59  ASN   A HD22 1 
ATOM   1367 N N    . ALA   A 1 60  ? 29.593 11.276  9.856   1.00 10.08 ?  60  ALA   A N    1 
ATOM   1368 C CA   . ALA   A 1 60  ? 30.830 10.586  10.206  1.00 10.33 ?  60  ALA   A CA   1 
ATOM   1369 C C    . ALA   A 1 60  ? 31.049 9.351   9.338   1.00 10.17 ?  60  ALA   A C    1 
ATOM   1370 O O    . ALA   A 1 60  ? 32.192 9.022   9.003   1.00 10.60 ?  60  ALA   A O    1 
ATOM   1371 C CB   . ALA   A 1 60  ? 30.837 10.229  11.689  1.00 11.05 ?  60  ALA   A CB   1 
ATOM   1372 H H    . ALA   A 1 60  ? 28.994 11.274  10.473  1.00 12.11 ?  60  ALA   A H    1 
ATOM   1373 H HA   . ALA   A 1 60  ? 31.574 11.188  10.044  1.00 12.42 ?  60  ALA   A HA   1 
ATOM   1374 H HB1  . ALA   A 1 60  ? 31.669 9.776   11.903  1.00 13.27 ?  60  ALA   A HB1  1 
ATOM   1375 H HB2  . ALA   A 1 60  ? 30.766 11.046  12.210  1.00 13.27 ?  60  ALA   A HB2  1 
ATOM   1376 H HB3  . ALA   A 1 60  ? 30.086 9.649   11.880  1.00 13.27 ?  60  ALA   A HB3  1 
ATOM   1377 N N    . MET   A 1 61  ? 29.976 8.658   8.959   1.00 9.66  ?  61  MET   A N    1 
ATOM   1378 C CA   . MET   A 1 61  ? 30.107 7.522   8.054   1.00 9.63  ?  61  MET   A CA   1 
ATOM   1379 C C    . MET   A 1 61  ? 30.733 7.950   6.730   1.00 9.49  ?  61  MET   A C    1 
ATOM   1380 O O    . MET   A 1 61  ? 31.614 7.261   6.202   1.00 9.82  ?  61  MET   A O    1 
ATOM   1381 C CB   . MET   A 1 61  ? 28.741 6.857   7.844   1.00 9.58  ?  61  MET   A CB   1 
ATOM   1382 C CG   . MET   A 1 61  ? 28.745 5.692   6.864   1.00 10.13 ?  61  MET   A CG   1 
ATOM   1383 S SD   . MET   A 1 61  ? 27.110 4.951   6.671   1.00 10.96 ?  61  MET   A SD   1 
ATOM   1384 C CE   . MET   A 1 61  ? 26.995 4.065   8.236   1.00 12.02 ?  61  MET   A CE   1 
ATOM   1385 H H    . MET   A 1 61  ? 29.170 8.821   9.212   1.00 11.61 ?  61  MET   A H    1 
ATOM   1386 H HA   . MET   A 1 61  ? 30.685 6.865   8.467   1.00 11.57 ?  61  MET   A HA   1 
ATOM   1387 H HB2  . MET   A 1 61  ? 28.426 6.520   8.696   1.00 11.51 ?  61  MET   A HB2  1 
ATOM   1388 H HB3  . MET   A 1 61  ? 28.120 7.521   7.506   1.00 11.51 ?  61  MET   A HB3  1 
ATOM   1389 H HG2  . MET   A 1 61  ? 29.024 6.008   5.990   1.00 12.17 ?  61  MET   A HG2  1 
ATOM   1390 H HG3  . MET   A 1 61  ? 29.350 5.008   7.183   1.00 12.17 ?  61  MET   A HG3  1 
ATOM   1391 H HE1  . MET   A 1 61  ? 26.161 3.576   8.262   1.00 14.44 ?  61  MET   A HE1  1 
ATOM   1392 H HE2  . MET   A 1 61  ? 27.744 3.448   8.303   1.00 14.44 ?  61  MET   A HE2  1 
ATOM   1393 H HE3  . MET   A 1 61  ? 27.030 4.701   8.970   1.00 14.44 ?  61  MET   A HE3  1 
ATOM   1394 N N    . GLN   A 1 62  ? 30.290 9.078   6.173   1.00 9.37  ?  62  GLN   A N    1 
ATOM   1395 C CA   . GLN   A 1 62  ? 30.848 9.552   4.913   1.00 9.62  ?  62  GLN   A CA   1 
ATOM   1396 C C    . GLN   A 1 62  ? 32.320 9.929   5.053   1.00 9.58  ?  62  GLN   A C    1 
ATOM   1397 O O    . GLN   A 1 62  ? 33.126 9.613   4.171   1.00 9.87  ?  62  GLN   A O    1 
ATOM   1398 C CB   . GLN   A 1 62  ? 30.041 10.732  4.380   1.00 9.79  ?  62  GLN   A CB   1 
ATOM   1399 C CG   . GLN   A 1 62  ? 30.431 11.112  2.954   1.00 9.97  ?  62  GLN   A CG   1 
ATOM   1400 C CD   . GLN   A 1 62  ? 30.098 9.985   1.994   1.00 9.96  ?  62  GLN   A CD   1 
ATOM   1401 O OE1  . GLN   A 1 62  ? 28.915 9.668   1.799   1.00 10.41 ?  62  GLN   A OE1  1 
ATOM   1402 N NE2  . GLN   A 1 62  ? 31.117 9.319   1.457   1.00 10.44 ?  62  GLN   A NE2  1 
ATOM   1403 H H    . GLN   A 1 62  ? 29.668 9.571   6.501   1.00 11.27 ?  62  GLN   A H    1 
ATOM   1404 H HA   . GLN   A 1 62  ? 30.792 8.834   4.263   1.00 11.56 ?  62  GLN   A HA   1 
ATOM   1405 H HB2  . GLN   A 1 62  ? 29.097 10.505  4.383   1.00 11.77 ?  62  GLN   A HB2  1 
ATOM   1406 H HB3  . GLN   A 1 62  ? 30.194 11.508  4.948   1.00 11.77 ?  62  GLN   A HB3  1 
ATOM   1407 H HG2  . GLN   A 1 62  ? 29.930 11.897  2.681   1.00 11.98 ?  62  GLN   A HG2  1 
ATOM   1408 H HG3  . GLN   A 1 62  ? 31.382 11.284  2.911   1.00 11.98 ?  62  GLN   A HG3  1 
ATOM   1409 H HE21 . GLN   A 1 62  ? 31.925 9.560   1.627   1.00 12.55 ?  62  GLN   A HE21 1 
ATOM   1410 H HE22 . GLN   A 1 62  ? 30.967 8.668   0.917   1.00 12.55 ?  62  GLN   A HE22 1 
ATOM   1411 N N    . VAL   A 1 63  ? 32.696 10.607  6.145   1.00 10.21 ?  63  VAL   A N    1 
ATOM   1412 C CA   . VAL   A 1 63  ? 34.094 11.002  6.341   1.00 11.06 ?  63  VAL   A CA   1 
ATOM   1413 C C    . VAL   A 1 63  ? 34.988 9.767   6.396   1.00 10.28 ?  63  VAL   A C    1 
ATOM   1414 O O    . VAL   A 1 63  ? 36.037 9.700   5.740   1.00 10.75 ?  63  VAL   A O    1 
ATOM   1415 C CB   . VAL   A 1 63  ? 34.217 11.880  7.601   1.00 12.62 ?  63  VAL   A CB   1 
ATOM   1416 C CG1  . VAL   A 1 63  ? 35.666 12.141  7.935   1.00 14.56 ?  63  VAL   A CG1  1 
ATOM   1417 C CG2  . VAL   A 1 63  ? 33.468 13.206  7.405   1.00 13.17 ?  63  VAL   A CG2  1 
ATOM   1418 H H    . VAL   A 1 63  ? 32.156 10.850  6.776   1.00 12.27 ?  63  VAL   A H    1 
ATOM   1419 H HA   . VAL   A 1 63  ? 34.366 11.535  5.583   1.00 13.29 ?  63  VAL   A HA   1 
ATOM   1420 H HB   . VAL   A 1 63  ? 33.818 11.415  8.354   1.00 15.17 ?  63  VAL   A HB   1 
ATOM   1421 H HG11 . VAL   A 1 63  ? 35.716 12.876  8.569   1.00 17.49 ?  63  VAL   A HG11 1 
ATOM   1422 H HG12 . VAL   A 1 63  ? 36.056 11.344  8.324   1.00 17.49 ?  63  VAL   A HG12 1 
ATOM   1423 H HG13 . VAL   A 1 63  ? 36.139 12.380  7.121   1.00 17.49 ?  63  VAL   A HG13 1 
ATOM   1424 H HG21 . VAL   A 1 63  ? 33.571 13.747  8.205   1.00 15.82 ?  63  VAL   A HG21 1 
ATOM   1425 H HG22 . VAL   A 1 63  ? 33.845 13.670  6.642   1.00 15.82 ?  63  VAL   A HG22 1 
ATOM   1426 H HG23 . VAL   A 1 63  ? 32.530 13.018  7.251   1.00 15.82 ?  63  VAL   A HG23 1 
ATOM   1427 N N    . GLU   A 1 64  ? 34.574 8.762   7.175   1.00 10.48 ?  64  GLU   A N    1 
ATOM   1428 C CA   . GLU   A 1 64  ? 35.325 7.515   7.268   1.00 10.44 ?  64  GLU   A CA   1 
ATOM   1429 C C    . GLU   A 1 64  ? 35.409 6.827   5.911   1.00 9.94  ?  64  GLU   A C    1 
ATOM   1430 O O    . GLU   A 1 64  ? 36.457 6.271   5.537   1.00 10.56 ?  64  GLU   A O    1 
ATOM   1431 C CB   . GLU   A 1 64  ? 34.637 6.616   8.297   1.00 10.76 ?  64  GLU   A CB   1 
ATOM   1432 C CG   . GLU   A 1 64  ? 35.270 5.258   8.445   1.00 11.79 ?  64  GLU   A CG   1 
ATOM   1433 C CD   . GLU   A 1 64  ? 34.393 4.268   9.175   1.00 11.92 ?  64  GLU   A CD   1 
ATOM   1434 O OE1  . GLU   A 1 64  ? 33.153 4.357   9.042   1.00 12.71 ?  64  GLU   A OE1  1 
ATOM   1435 O OE2  . GLU   A 1 64  ? 34.941 3.374   9.861   1.00 12.29 -1 64  GLU   A OE2  1 
ATOM   1436 H H    . GLU   A 1 64  ? 33.863 8.781   7.664   1.00 12.60 ?  64  GLU   A H    1 
ATOM   1437 H HA   . GLU   A 1 64  ? 36.228 7.709   7.578   1.00 12.55 ?  64  GLU   A HA   1 
ATOM   1438 H HB2  . GLU   A 1 64  ? 34.675 7.057   9.167   1.00 12.93 ?  64  GLU   A HB2  1 
ATOM   1439 H HB3  . GLU   A 1 64  ? 33.716 6.496   8.033   1.00 12.93 ?  64  GLU   A HB3  1 
ATOM   1440 H HG2  . GLU   A 1 64  ? 35.462 4.890   7.566   1.00 14.17 ?  64  GLU   A HG2  1 
ATOM   1441 H HG3  . GLU   A 1 64  ? 36.099 5.350   8.944   1.00 14.17 ?  64  GLU   A HG3  1 
ATOM   1442 N N    . SER   A 1 65  ? 34.287 6.815   5.181   1.00 9.39  ?  65  SER   A N    1 
ATOM   1443 C CA   . SER   A 1 65  ? 34.227 6.161   3.879   1.00 9.66  ?  65  SER   A CA   1 
ATOM   1444 C C    . SER   A 1 65  ? 35.152 6.832   2.872   1.00 9.58  ?  65  SER   A C    1 
ATOM   1445 O O    . SER   A 1 65  ? 35.789 6.156   2.058   1.00 10.77 ?  65  SER   A O    1 
ATOM   1446 C CB   . SER   A 1 65  ? 32.789 6.179   3.353   1.00 9.40  ?  65  SER   A CB   1 
ATOM   1447 O OG   . SER   A 1 65  ? 31.938 5.357   4.141   1.00 10.32 ?  65  SER   A OG   1 
ATOM   1448 H H    . SER   A 1 65  ? 33.549 7.186   5.425   1.00 11.29 ?  65  SER   A H    1 
ATOM   1449 H HA   . SER   A 1 65  ? 34.505 5.239   3.975   1.00 11.61 ?  65  SER   A HA   1 
ATOM   1450 H HB2  . SER   A 1 65  ? 32.454 7.087   3.373   1.00 11.29 ?  65  SER   A HB2  1 
ATOM   1451 H HB3  . SER   A 1 65  ? 32.786 5.846   2.441   1.00 11.29 ?  65  SER   A HB3  1 
ATOM   1452 H HG   . SER   A 1 65  ? 31.930 5.633   4.939   1.00 12.41 ?  65  SER   A HG   1 
ATOM   1453 N N    . ASP   A 1 66  ? 35.233 8.165   2.900   1.00 9.73  ?  66  ASP   A N    1 
ATOM   1454 C CA   . ASP   A 1 66  ? 36.092 8.866   1.952   1.00 10.54 ?  66  ASP   A CA   1 
ATOM   1455 C C    . ASP   A 1 66  ? 37.553 8.498   2.176   1.00 10.41 ?  66  ASP   A C    1 
ATOM   1456 O O    . ASP   A 1 66  ? 38.316 8.323   1.218   1.00 11.72 ?  66  ASP   A O    1 
ATOM   1457 C CB   . ASP   A 1 66  ? 35.886 10.375  2.067   1.00 12.11 ?  66  ASP   A CB   1 
ATOM   1458 C CG   . ASP   A 1 66  ? 34.548 10.849  1.485   1.00 13.96 ?  66  ASP   A CG   1 
ATOM   1459 O OD1  . ASP   A 1 66  ? 33.818 10.066  0.840   1.00 14.12 ?  66  ASP   A OD1  1 
ATOM   1460 O OD2  . ASP   A 1 66  ? 34.259 12.050  1.644   1.00 16.86 -1 66  ASP   A OD2  1 
ATOM   1461 H H    . ASP   A 1 66  ? 34.796 8.676   3.443   1.00 11.69 ?  66  ASP   A H    1 
ATOM   1462 H HA   . ASP   A 1 66  ? 35.847 8.600   1.053   1.00 12.66 ?  66  ASP   A HA   1 
ATOM   1463 H HB2  . ASP   A 1 66  ? 35.909 10.628  3.003   1.00 14.54 ?  66  ASP   A HB2  1 
ATOM   1464 H HB3  . ASP   A 1 66  ? 36.599 10.826  1.586   1.00 14.54 ?  66  ASP   A HB3  1 
ATOM   1465 N N    . ASP   A 1 67  ? 37.956 8.355   3.436   1.00 10.76 ?  67  ASP   A N    1 
ATOM   1466 C CA   . ASP   A 1 67  ? 39.309 7.904   3.727   1.00 11.70 ?  67  ASP   A CA   1 
ATOM   1467 C C    . ASP   A 1 67  ? 39.519 6.466   3.259   1.00 11.40 ?  67  ASP   A C    1 
ATOM   1468 O O    . ASP   A 1 67  ? 40.578 6.137   2.709   1.00 11.92 ?  67  ASP   A O    1 
ATOM   1469 C CB   . ASP   A 1 67  ? 39.584 8.040   5.223   1.00 12.71 ?  67  ASP   A CB   1 
ATOM   1470 C CG   . ASP   A 1 67  ? 40.881 7.370   5.635   1.00 14.22 ?  67  ASP   A CG   1 
ATOM   1471 O OD1  . ASP   A 1 67  ? 41.960 7.984   5.469   1.00 16.93 ?  67  ASP   A OD1  1 
ATOM   1472 O OD2  . ASP   A 1 67  ? 40.825 6.216   6.115   1.00 13.99 -1 67  ASP   A OD2  1 
ATOM   1473 H H    . ASP   A 1 67  ? 37.472 8.507   4.125   1.00 12.92 ?  67  ASP   A H    1 
ATOM   1474 H HA   . ASP   A 1 67  ? 39.940 8.467   3.251   1.00 14.05 ?  67  ASP   A HA   1 
ATOM   1475 H HB2  . ASP   A 1 67  ? 39.648 8.975   5.446   1.00 15.26 ?  67  ASP   A HB2  1 
ATOM   1476 H HB3  . ASP   A 1 67  ? 38.855 7.623   5.712   1.00 15.26 ?  67  ASP   A HB3  1 
ATOM   1477 N N    . TYR   A 1 68  ? 38.520 5.596   3.454   1.00 11.26 ?  68  TYR   A N    1 
ATOM   1478 C CA   . TYR   A 1 68  ? 38.632 4.215   2.983   1.00 11.26 ?  68  TYR   A CA   1 
ATOM   1479 C C    . TYR   A 1 68  ? 38.877 4.169   1.476   1.00 10.91 ?  68  TYR   A C    1 
ATOM   1480 O O    . TYR   A 1 68  ? 39.752 3.433   0.998   1.00 11.47 ?  68  TYR   A O    1 
ATOM   1481 C CB   . TYR   A 1 68  ? 37.373 3.401   3.355   1.00 11.13 ?  68  TYR   A CB   1 
ATOM   1482 C CG   . TYR   A 1 68  ? 37.391 2.009   2.728   1.00 12.53 ?  68  TYR   A CG   1 
ATOM   1483 C CD1  . TYR   A 1 68  ? 36.942 1.821   1.423   1.00 13.75 ?  68  TYR   A CD1  1 
ATOM   1484 C CD2  . TYR   A 1 68  ? 37.932 0.920   3.392   1.00 14.16 ?  68  TYR   A CD2  1 
ATOM   1485 C CE1  . TYR   A 1 68  ? 37.007 0.604   0.802   1.00 15.00 ?  68  TYR   A CE1  1 
ATOM   1486 C CE2  . TYR   A 1 68  ? 37.996 -0.341  2.769   1.00 14.19 ?  68  TYR   A CE2  1 
ATOM   1487 C CZ   . TYR   A 1 68  ? 37.540 -0.470  1.471   1.00 14.89 ?  68  TYR   A CZ   1 
ATOM   1488 O OH   . TYR   A 1 68  ? 37.616 -1.680  0.834   1.00 15.83 ?  68  TYR   A OH   1 
ATOM   1489 H H    . TYR   A 1 68  ? 37.775 5.778   3.851   1.00 13.52 ?  68  TYR   A H    1 
ATOM   1490 H HA   . TYR   A 1 68  ? 39.388 3.798   3.421   1.00 13.53 ?  68  TYR   A HA   1 
ATOM   1491 H HB2  . TYR   A 1 68  ? 37.334 3.292   4.319   1.00 13.37 ?  68  TYR   A HB2  1 
ATOM   1492 H HB3  . TYR   A 1 68  ? 36.583 3.864   3.038   1.00 13.37 ?  68  TYR   A HB3  1 
ATOM   1493 H HD1  . TYR   A 1 68  ? 36.599 2.552   0.956   1.00 16.52 ?  68  TYR   A HD1  1 
ATOM   1494 H HD2  . TYR   A 1 68  ? 38.260 1.021   4.254   1.00 17.00 ?  68  TYR   A HD2  1 
ATOM   1495 H HE1  . TYR   A 1 68  ? 36.695 0.505   -0.069  1.00 18.02 ?  68  TYR   A HE1  1 
ATOM   1496 H HE2  . TYR   A 1 68  ? 38.357 -1.070  3.209   1.00 17.04 ?  68  TYR   A HE2  1 
ATOM   1497 H HH   . TYR   A 1 68  ? 37.941 -2.254  1.353   1.00 19.01 ?  68  TYR   A HH   1 
ATOM   1498 N N    . ILE   A 1 69  ? 38.093 4.932   0.708   1.00 10.76 ?  69  ILE   A N    1 
ATOM   1499 C CA   . ILE   A 1 69  ? 38.228 4.925   -0.747  1.00 10.85 ?  69  ILE   A CA   1 
ATOM   1500 C C    . ILE   A 1 69  ? 39.565 5.524   -1.176  1.00 10.88 ?  69  ILE   A C    1 
ATOM   1501 O O    . ILE   A 1 69  ? 40.207 5.032   -2.111  1.00 11.11 ?  69  ILE   A O    1 
ATOM   1502 C CB   . ILE   A 1 69  ? 37.033 5.642   -1.411  1.00 11.52 ?  69  ILE   A CB   1 
ATOM   1503 C CG1  . ILE   A 1 69  ? 35.715 4.910   -1.142  1.00 12.07 ?  69  ILE   A CG1  1 
ATOM   1504 C CG2  . ILE   A 1 69  ? 37.279 5.841   -2.911  1.00 13.01 ?  69  ILE   A CG2  1 
ATOM   1505 C CD1  . ILE   A 1 69  ? 35.552 3.618   -1.908  1.00 12.53 ?  69  ILE   A CD1  1 
ATOM   1506 H H    . ILE   A 1 69  ? 37.488 5.466   1.012   1.00 12.93 ?  69  ILE   A H    1 
ATOM   1507 H HA   . ILE   A 1 69  ? 38.217 4.006   -1.041  1.00 13.03 ?  69  ILE   A HA   1 
ATOM   1508 H HB   . ILE   A 1 69  ? 36.958 6.519   -1.009  1.00 13.84 ?  69  ILE   A HB   1 
ATOM   1509 H HG12 . ILE   A 1 69  ? 35.663 4.694   -0.197  1.00 14.49 ?  69  ILE   A HG12 1 
ATOM   1510 H HG13 . ILE   A 1 69  ? 34.979 5.490   -1.385  1.00 14.49 ?  69  ILE   A HG13 1 
ATOM   1511 H HG21 . ILE   A 1 69  ? 36.433 6.056   -3.340  1.00 15.63 ?  69  ILE   A HG21 1 
ATOM   1512 H HG22 . ILE   A 1 69  ? 37.901 6.579   -3.033  1.00 15.63 ?  69  ILE   A HG22 1 
ATOM   1513 H HG23 . ILE   A 1 69  ? 37.644 5.030   -3.285  1.00 15.63 ?  69  ILE   A HG23 1 
ATOM   1514 H HD11 . ILE   A 1 69  ? 34.742 3.175   -1.608  1.00 15.05 ?  69  ILE   A HD11 1 
ATOM   1515 H HD12 . ILE   A 1 69  ? 35.481 3.820   -2.856  1.00 15.05 ?  69  ILE   A HD12 1 
ATOM   1516 H HD13 . ILE   A 1 69  ? 36.319 3.051   -1.746  1.00 15.05 ?  69  ILE   A HD13 1 
ATOM   1517 N N    . ALA   A 1 70  ? 39.992 6.606   -0.525  1.00 11.29 ?  70  ALA   A N    1 
ATOM   1518 C CA   . ALA   A 1 70  ? 41.273 7.208   -0.881  1.00 12.10 ?  70  ALA   A CA   1 
ATOM   1519 C C    . ALA   A 1 70  ? 42.421 6.223   -0.710  1.00 12.50 ?  70  ALA   A C    1 
ATOM   1520 O O    . ALA   A 1 70  ? 43.388 6.256   -1.475  1.00 14.14 ?  70  ALA   A O    1 
ATOM   1521 C CB   . ALA   A 1 70  ? 41.516 8.462   -0.037  1.00 12.93 ?  70  ALA   A CB   1 
ATOM   1522 H H    . ALA   A 1 70  ? 39.571 6.997   0.117   1.00 13.56 ?  70  ALA   A H    1 
ATOM   1523 H HA   . ALA   A 1 70  ? 41.239 7.484   -1.811  1.00 14.53 ?  70  ALA   A HA   1 
ATOM   1524 H HB1  . ALA   A 1 70  ? 42.375 8.849   -0.292  1.00 15.53 ?  70  ALA   A HB1  1 
ATOM   1525 H HB2  . ALA   A 1 70  ? 40.810 9.101   -0.195  1.00 15.53 ?  70  ALA   A HB2  1 
ATOM   1526 H HB3  . ALA   A 1 70  ? 41.541 8.212   0.901   1.00 15.53 ?  70  ALA   A HB3  1 
ATOM   1527 N N    . THR   A 1 71  ? 42.320 5.325   0.269   1.00 11.87 ?  71  THR   A N    1 
ATOM   1528 C CA   . THR   A 1 71  ? 43.369 4.341   0.515   1.00 13.14 ?  71  THR   A CA   1 
ATOM   1529 C C    . THR   A 1 71  ? 43.237 3.117   -0.382  1.00 13.52 ?  71  THR   A C    1 
ATOM   1530 O O    . THR   A 1 71  ? 44.242 2.609   -0.897  1.00 15.32 ?  71  THR   A O    1 
ATOM   1531 C CB   . THR   A 1 71  ? 43.302 3.901   1.973   1.00 15.05 ?  71  THR   A CB   1 
ATOM   1532 O OG1  . THR   A 1 71  ? 43.546 5.033   2.816   1.00 16.08 ?  71  THR   A OG1  1 
ATOM   1533 C CG2  . THR   A 1 71  ? 44.321 2.810   2.260   1.00 16.66 ?  71  THR   A CG2  1 
ATOM   1534 H H    . THR   A 1 71  ? 41.646 5.267   0.799   1.00 14.26 ?  71  THR   A H    1 
ATOM   1535 H HA   . THR   A 1 71  ? 44.231 4.748   0.351   1.00 15.79 ?  71  THR   A HA   1 
ATOM   1536 H HB   . THR   A 1 71  ? 42.415 3.542   2.155   1.00 18.08 ?  71  THR   A HB   1 
ATOM   1537 H HG1  . THR   A 1 71  ? 43.504 4.792   3.622   1.00 19.31 ?  71  THR   A HG1  1 
ATOM   1538 H HG21 . THR   A 1 71  ? 44.453 2.729   3.217   1.00 20.01 ?  71  THR   A HG21 1 
ATOM   1539 H HG22 . THR   A 1 71  ? 44.014 1.960   1.911   1.00 20.01 ?  71  THR   A HG22 1 
ATOM   1540 H HG23 . THR   A 1 71  ? 45.170 3.035   1.844   1.00 20.01 ?  71  THR   A HG23 1 
ATOM   1541 N N    . ASN   A 1 72  ? 42.013 2.610   -0.556  1.00 12.51 ?  72  ASN   A N    1 
ATOM   1542 C CA   . ASN   A 1 72  ? 41.793 1.287   -1.125  1.00 12.55 ?  72  ASN   A CA   1 
ATOM   1543 C C    . ASN   A 1 72  ? 41.162 1.280   -2.505  1.00 12.65 ?  72  ASN   A C    1 
ATOM   1544 O O    . ASN   A 1 72  ? 41.174 0.228   -3.157  1.00 14.08 ?  72  ASN   A O    1 
ATOM   1545 C CB   . ASN   A 1 72  ? 40.917 0.454   -0.182  1.00 13.39 ?  72  ASN   A CB   1 
ATOM   1546 C CG   . ASN   A 1 72  ? 41.534 0.314   1.178   1.00 14.40 ?  72  ASN   A CG   1 
ATOM   1547 O OD1  . ASN   A 1 72  ? 41.073 0.905   2.152   1.00 16.03 ?  72  ASN   A OD1  1 
ATOM   1548 N ND2  . ASN   A 1 72  ? 42.603 -0.452  1.251   1.00 14.86 ?  72  ASN   A ND2  1 
ATOM   1549 H H    . ASN   A 1 72  ? 41.283 3.019   -0.349  1.00 15.02 ?  72  ASN   A H    1 
ATOM   1550 H HA   . ASN   A 1 72  ? 42.651 0.841   -1.204  1.00 15.08 ?  72  ASN   A HA   1 
ATOM   1551 H HB2  . ASN   A 1 72  ? 40.059 0.882   -0.084  1.00 16.08 ?  72  ASN   A HB2  1 
ATOM   1552 H HB3  . ASN   A 1 72  ? 40.813 -0.437  -0.557  1.00 16.08 ?  72  ASN   A HB3  1 
ATOM   1553 H HD21 . ASN   A 1 72  ? 43.008 -0.559  2.005   1.00 17.85 ?  72  ASN   A HD21 1 
ATOM   1554 H HD22 . ASN   A 1 72  ? 42.909 -0.845  0.546   1.00 17.85 ?  72  ASN   A HD22 1 
ATOM   1555 N N    . GLY   A 1 73  ? 40.606 2.393   -2.963  1.00 12.12 ?  73  GLY   A N    1 
ATOM   1556 C CA   . GLY   A 1 73  ? 39.877 2.402   -4.205  1.00 12.27 ?  73  GLY   A CA   1 
ATOM   1557 C C    . GLY   A 1 73  ? 38.481 1.834   -4.032  1.00 11.71 ?  73  GLY   A C    1 
ATOM   1558 O O    . GLY   A 1 73  ? 38.098 1.375   -2.951  1.00 12.15 ?  73  GLY   A O    1 
ATOM   1559 H H    . GLY   A 1 73  ? 40.642 3.164   -2.571  1.00 14.56 ?  73  GLY   A H    1 
ATOM   1560 H HA2  . GLY   A 1 73  ? 39.810 3.317   -4.532  1.00 14.74 ?  73  GLY   A HA2  1 
ATOM   1561 H HA3  . GLY   A 1 73  ? 40.355 1.875   -4.867  1.00 14.74 ?  73  GLY   A HA3  1 
ATOM   1562 N N    . PRO   A 1 74  ? 37.702 1.852   -5.111  1.00 11.90 ?  74  PRO   A N    1 
ATOM   1563 C CA   . PRO   A 1 74  ? 36.300 1.432   -5.030  1.00 12.31 ?  74  PRO   A CA   1 
ATOM   1564 C C    . PRO   A 1 74  ? 36.144 -0.051  -4.721  1.00 11.20 ?  74  PRO   A C    1 
ATOM   1565 O O    . PRO   A 1 74  ? 37.008 -0.884  -5.009  1.00 12.05 ?  74  PRO   A O    1 
ATOM   1566 C CB   . PRO   A 1 74  ? 35.759 1.744   -6.429  1.00 13.95 ?  74  PRO   A CB   1 
ATOM   1567 C CG   . PRO   A 1 74  ? 36.719 2.711   -7.031  1.00 16.70 ?  74  PRO   A CG   1 
ATOM   1568 C CD   . PRO   A 1 74  ? 38.053 2.384   -6.439  1.00 13.78 ?  74  PRO   A CD   1 
ATOM   1569 H HA   . PRO   A 1 74  ? 35.824 1.962   -4.365  1.00 14.79 ?  74  PRO   A HA   1 
ATOM   1570 H HB2  . PRO   A 1 74  ? 35.721 0.924   -6.943  1.00 16.76 ?  74  PRO   A HB2  1 
ATOM   1571 H HB3  . PRO   A 1 74  ? 34.875 2.139   -6.348  1.00 16.76 ?  74  PRO   A HB3  1 
ATOM   1572 H HG2  . PRO   A 1 74  ? 36.740 2.595   -7.991  1.00 20.05 ?  74  PRO   A HG2  1 
ATOM   1573 H HG3  . PRO   A 1 74  ? 36.462 3.616   -6.798  1.00 20.05 ?  74  PRO   A HG3  1 
ATOM   1574 H HD2  . PRO   A 1 74  ? 38.507 1.706   -6.967  1.00 16.55 ?  74  PRO   A HD2  1 
ATOM   1575 H HD3  . PRO   A 1 74  ? 38.592 3.190   -6.363  1.00 16.55 ?  74  PRO   A HD3  1 
ATOM   1576 N N    . LEU   A 1 75  ? 34.992 -0.368  -4.136  1.00 10.63 ?  75  LEU   A N    1 
ATOM   1577 C CA   . LEU   A 1 75  ? 34.585 -1.754  -3.991  1.00 10.53 ?  75  LEU   A CA   1 
ATOM   1578 C C    . LEU   A 1 75  ? 34.195 -2.330  -5.352  1.00 11.02 ?  75  LEU   A C    1 
ATOM   1579 O O    . LEU   A 1 75  ? 34.083 -1.616  -6.352  1.00 12.41 ?  75  LEU   A O    1 
ATOM   1580 C CB   . LEU   A 1 75  ? 33.398 -1.869  -3.035  1.00 10.61 ?  75  LEU   A CB   1 
ATOM   1581 C CG   . LEU   A 1 75  ? 33.613 -1.447  -1.583  1.00 11.85 ?  75  LEU   A CG   1 
ATOM   1582 C CD1  . LEU   A 1 75  ? 32.333 -1.625  -0.770  1.00 13.54 ?  75  LEU   A CD1  1 
ATOM   1583 C CD2  . LEU   A 1 75  ? 34.755 -2.187  -0.944  1.00 14.97 ?  75  LEU   A CD2  1 
ATOM   1584 H H    . LEU   A 1 75  ? 34.425 0.202   -3.825  1.00 12.77 ?  75  LEU   A H    1 
ATOM   1585 H HA   . LEU   A 1 75  ? 35.321 -2.272  -3.639  1.00 12.65 ?  75  LEU   A HA   1 
ATOM   1586 H HB2  . LEU   A 1 75  ? 32.676 -1.325  -3.383  1.00 12.75 ?  75  LEU   A HB2  1 
ATOM   1587 H HB3  . LEU   A 1 75  ? 33.116 -2.799  -3.020  1.00 12.75 ?  75  LEU   A HB3  1 
ATOM   1588 H HG   . LEU   A 1 75  ? 33.842 -0.504  -1.571  1.00 14.24 ?  75  LEU   A HG   1 
ATOM   1589 H HD11 . LEU   A 1 75  ? 32.502 -1.344  0.144   1.00 16.26 ?  75  LEU   A HD11 1 
ATOM   1590 H HD12 . LEU   A 1 75  ? 31.639 -1.072  -1.162  1.00 16.26 ?  75  LEU   A HD12 1 
ATOM   1591 H HD13 . LEU   A 1 75  ? 32.073 -2.555  -0.792  1.00 16.26 ?  75  LEU   A HD13 1 
ATOM   1592 H HD21 . LEU   A 1 75  ? 34.804 -1.945  -0.006  1.00 17.98 ?  75  LEU   A HD21 1 
ATOM   1593 H HD22 . LEU   A 1 75  ? 34.606 -3.141  -1.033  1.00 17.98 ?  75  LEU   A HD22 1 
ATOM   1594 H HD23 . LEU   A 1 75  ? 35.585 -1.941  -1.389  1.00 17.98 ?  75  LEU   A HD23 1 
ATOM   1595 N N    . LYS   A 1 76  ? 33.987 -3.648  -5.375  1.00 11.53 ?  76  LYS   A N    1 
ATOM   1596 C CA   . LYS   A 1 76  ? 33.382 -4.344  -6.504  1.00 12.09 ?  76  LYS   A CA   1 
ATOM   1597 C C    . LYS   A 1 76  ? 31.868 -4.426  -6.308  1.00 10.71 ?  76  LYS   A C    1 
ATOM   1598 O O    . LYS   A 1 76  ? 31.388 -4.556  -5.183  1.00 10.59 ?  76  LYS   A O    1 
ATOM   1599 C CB   . LYS   A 1 76  ? 33.917 -5.787  -6.582  1.00 14.28 ?  76  LYS   A CB   1 
ATOM   1600 C CG   . LYS   A 1 76  ? 35.432 -5.916  -6.718  1.00 15.70 ?  76  LYS   A CG   1 
ATOM   1601 C CD   . LYS   A 1 76  ? 35.931 -7.334  -6.527  1.00 17.56 ?  76  LYS   A CD   1 
ATOM   1602 C CE   . LYS   A 1 76  ? 37.429 -7.398  -6.729  1.00 20.19 ?  76  LYS   A CE   1 
ATOM   1603 N NZ   . LYS   A 1 76  ? 37.971 -8.752  -6.512  1.00 21.11 ?  76  LYS   A NZ   1 
ATOM   1604 H H    . LYS   A 1 76  ? 34.196 -4.174  -4.725  1.00 13.85 ?  76  LYS   A H    1 
ATOM   1605 H HA   . LYS   A 1 76  ? 33.580 -3.877  -7.333  1.00 14.53 ?  76  LYS   A HA   1 
ATOM   1606 H HB2  . LYS   A 1 76  ? 33.653 -6.252  -5.775  1.00 17.15 ?  76  LYS   A HB2  1 
ATOM   1607 H HB3  . LYS   A 1 76  ? 33.516 -6.216  -7.354  1.00 17.15 ?  76  LYS   A HB3  1 
ATOM   1608 H HG2  . LYS   A 1 76  ? 35.689 -5.618  -7.604  1.00 18.86 ?  76  LYS   A HG2  1 
ATOM   1609 H HG3  . LYS   A 1 76  ? 35.851 -5.352  -6.046  1.00 18.86 ?  76  LYS   A HG3  1 
ATOM   1610 H HD2  . LYS   A 1 76  ? 35.720 -7.625  -5.623  1.00 21.09 ?  76  LYS   A HD2  1 
ATOM   1611 H HD3  . LYS   A 1 76  ? 35.499 -7.912  -7.176  1.00 21.09 ?  76  LYS   A HD3  1 
ATOM   1612 H HE2  . LYS   A 1 76  ? 37.630 -7.127  -7.636  1.00 24.25 ?  76  LYS   A HE2  1 
ATOM   1613 H HE3  . LYS   A 1 76  ? 37.851 -6.795  -6.097  1.00 24.25 ?  76  LYS   A HE3  1 
ATOM   1614 H HZ1  . LYS   A 1 76  ? 38.848 -8.752  -6.639  1.00 25.35 ?  76  LYS   A HZ1  1 
ATOM   1615 H HZ2  . LYS   A 1 76  ? 37.796 -9.022  -5.681  1.00 25.35 ?  76  LYS   A HZ2  1 
ATOM   1616 H HZ3  . LYS   A 1 76  ? 37.594 -9.325  -7.083  1.00 25.35 ?  76  LYS   A HZ3  1 
ATOM   1617 N N    . VAL   A 1 77  ? 31.109 -4.400  -7.412  1.00 11.09 ?  77  VAL   A N    1 
ATOM   1618 C CA   . VAL   A 1 77  ? 29.700 -4.780  -7.318  1.00 11.15 ?  77  VAL   A CA   1 
ATOM   1619 C C    . VAL   A 1 77  ? 29.639 -6.233  -6.876  1.00 10.62 ?  77  VAL   A C    1 
ATOM   1620 O O    . VAL   A 1 77  ? 30.299 -7.100  -7.458  1.00 10.99 ?  77  VAL   A O    1 
ATOM   1621 C CB   . VAL   A 1 77  ? 28.966 -4.549  -8.649  1.00 12.18 ?  77  VAL   A CB   1 
ATOM   1622 C CG1  . VAL   A 1 77  ? 27.505 -4.983  -8.529  1.00 13.32 ?  77  VAL   A CG1  1 
ATOM   1623 C CG2  . VAL   A 1 77  ? 29.044 -3.091  -9.062  1.00 13.90 ?  77  VAL   A CG2  1 
ATOM   1624 H H    . VAL   A 1 77  ? 31.384 -4.170  -8.194  1.00 13.33 ?  77  VAL   A H    1 
ATOM   1625 H HA   . VAL   A 1 77  ? 29.274 -4.237  -6.636  1.00 13.39 ?  77  VAL   A HA   1 
ATOM   1626 H HB   . VAL   A 1 77  ? 29.389 -5.083  -9.340  1.00 14.64 ?  77  VAL   A HB   1 
ATOM   1627 H HG11 . VAL   A 1 77  ? 27.030 -4.703  -9.324  1.00 16.00 ?  77  VAL   A HG11 1 
ATOM   1628 H HG12 . VAL   A 1 77  ? 27.464 -5.946  -8.436  1.00 16.00 ?  77  VAL   A HG12 1 
ATOM   1629 H HG13 . VAL   A 1 77  ? 27.116 -4.558  -7.745  1.00 16.00 ?  77  VAL   A HG13 1 
ATOM   1630 H HG21 . VAL   A 1 77  ? 28.538 -2.969  -9.879  1.00 16.70 ?  77  VAL   A HG21 1 
ATOM   1631 H HG22 . VAL   A 1 77  ? 28.670 -2.543  -8.354  1.00 16.70 ?  77  VAL   A HG22 1 
ATOM   1632 H HG23 . VAL   A 1 77  ? 29.973 -2.851  -9.209  1.00 16.70 ?  77  VAL   A HG23 1 
ATOM   1633 N N    . GLY   A 1 78  ? 28.859 -6.507  -5.832  1.00 10.56 ?  78  GLY   A N    1 
ATOM   1634 C CA   . GLY   A 1 78  ? 28.844 -7.798  -5.181  1.00 10.50 ?  78  GLY   A CA   1 
ATOM   1635 C C    . GLY   A 1 78  ? 29.758 -7.888  -3.980  1.00 10.14 ?  78  GLY   A C    1 
ATOM   1636 O O    . GLY   A 1 78  ? 29.703 -8.894  -3.252  1.00 10.77 ?  78  GLY   A O    1 
ATOM   1637 H H    . GLY   A 1 78  ? 28.309 -5.940  -5.491  1.00 12.69 ?  78  GLY   A H    1 
ATOM   1638 H HA2  . GLY   A 1 78  ? 27.939 -7.992  -4.892  1.00 12.62 ?  78  GLY   A HA2  1 
ATOM   1639 H HA3  . GLY   A 1 78  ? 29.110 -8.477  -5.819  1.00 12.62 ?  78  GLY   A HA3  1 
ATOM   1640 N N    . GLY   A 1 79  ? 30.605 -6.879  -3.754  1.00 10.21 ?  79  GLY   A N    1 
ATOM   1641 C CA   . GLY   A 1 79  ? 31.579 -6.905  -2.687  1.00 10.43 ?  79  GLY   A CA   1 
ATOM   1642 C C    . GLY   A 1 79  ? 31.146 -6.114  -1.467  1.00 9.66  ?  79  GLY   A C    1 
ATOM   1643 O O    . GLY   A 1 79  ? 30.026 -5.608  -1.375  1.00 10.36 ?  79  GLY   A O    1 
ATOM   1644 H H    . GLY   A 1 79  ? 30.627 -6.150  -4.220  1.00 12.26 ?  79  GLY   A H    1 
ATOM   1645 H HA2  . GLY   A 1 79  ? 31.734 -7.828  -2.422  1.00 12.53 ?  79  GLY   A HA2  1 
ATOM   1646 H HA3  . GLY   A 1 79  ? 32.417 -6.538  -3.009  1.00 12.53 ?  79  GLY   A HA3  1 
ATOM   1647 N N    . SER   A 1 80  ? 32.063 -6.016  -0.506  1.00 10.29 ?  80  SER   A N    1 
ATOM   1648 C CA   . SER   A 1 80  ? 31.749 -5.387  0.767   1.00 9.84  ?  80  SER   A CA   1 
ATOM   1649 C C    . SER   A 1 80  ? 33.024 -4.940  1.469   1.00 10.06 ?  80  SER   A C    1 
ATOM   1650 O O    . SER   A 1 80  ? 34.136 -5.379  1.136   1.00 11.46 ?  80  SER   A O    1 
ATOM   1651 C CB   . SER   A 1 80  ? 30.985 -6.357  1.683   1.00 11.11 ?  80  SER   A CB   1 
ATOM   1652 O OG   . SER   A 1 80  ? 31.818 -7.402  2.163   1.00 12.77 ?  80  SER   A OG   1 
ATOM   1653 H H    . SER   A 1 80  ? 32.871 -6.315  -0.564  1.00 12.37 ?  80  SER   A H    1 
ATOM   1654 H HA   . SER   A 1 80  ? 31.194 -4.612  0.595   1.00 11.83 ?  80  SER   A HA   1 
ATOM   1655 H HB2  . SER   A 1 80  ? 30.633 -5.860  2.439   1.00 13.35 ?  80  SER   A HB2  1 
ATOM   1656 H HB3  . SER   A 1 80  ? 30.249 -6.746  1.178   1.00 13.35 ?  80  SER   A HB3  1 
ATOM   1657 H HG   . SER   A 1 80  ? 32.129 -7.833  1.510   1.00 15.34 ?  80  SER   A HG   1 
ATOM   1658 N N    . CYS   A 1 81  ? 32.841 -4.083  2.474   1.00 9.89  ?  81  CYS   A N    1 
ATOM   1659 C CA   . CYS   A 1 81  ? 33.894 -3.817  3.443   1.00 9.81  ?  81  CYS   A CA   1 
ATOM   1660 C C    . CYS   A 1 81  ? 33.261 -3.581  4.808   1.00 9.82  ?  81  CYS   A C    1 
ATOM   1661 O O    . CYS   A 1 81  ? 32.096 -3.186  4.901   1.00 10.82 ?  81  CYS   A O    1 
ATOM   1662 C CB   . CYS   A 1 81  ? 34.775 -2.635  3.027   1.00 10.69 ?  81  CYS   A CB   1 
ATOM   1663 S SG   . CYS   A 1 81  ? 33.894 -1.051  3.055   1.00 10.55 ?  81  CYS   A SG   1 
ATOM   1664 H H    . CYS   A 1 81  ? 32.112 -3.632  2.617   1.00 11.88 ?  81  CYS   A H    1 
ATOM   1665 H HA   . CYS   A 1 81  ? 34.458 -4.599  3.508   1.00 11.79 ?  81  CYS   A HA   1 
ATOM   1666 H HB2  . CYS   A 1 81  ? 35.530 -2.577  3.639   1.00 12.84 ?  81  CYS   A HB2  1 
ATOM   1667 H HB3  . CYS   A 1 81  ? 35.100 -2.790  2.124   1.00 12.84 ?  81  CYS   A HB3  1 
ATOM   1668 H HG   . CYS   A 1 81  ? 34.643 -0.176  2.721   1.00 12.67 ?  81  CYS   A HG   1 
ATOM   1669 N N    . VAL   A 1 82  ? 34.032 -3.839  5.862   1.00 10.04 ?  82  VAL   A N    1 
ATOM   1670 C CA   . VAL   A 1 82  ? 33.615 -3.591  7.235   1.00 10.38 ?  82  VAL   A CA   1 
ATOM   1671 C C    . VAL   A 1 82  ? 34.220 -2.278  7.702   1.00 10.55 ?  82  VAL   A C    1 
ATOM   1672 O O    . VAL   A 1 82  ? 35.443 -2.111  7.680   1.00 11.34 ?  82  VAL   A O    1 
ATOM   1673 C CB   . VAL   A 1 82  ? 34.044 -4.731  8.171   1.00 11.70 ?  82  VAL   A CB   1 
ATOM   1674 C CG1  . VAL   A 1 82  ? 33.606 -4.427  9.596   1.00 13.39 ?  82  VAL   A CG1  1 
ATOM   1675 C CG2  . VAL   A 1 82  ? 33.483 -6.061  7.698   1.00 12.85 ?  82  VAL   A CG2  1 
ATOM   1676 H H    . VAL   A 1 82  ? 34.823 -4.182  5.803   1.00 12.06 ?  82  VAL   A H    1 
ATOM   1677 H HA   . VAL   A 1 82  ? 32.646 -3.511  7.267   1.00 12.47 ?  82  VAL   A HA   1 
ATOM   1678 H HB   . VAL   A 1 82  ? 35.008 -4.791  8.167   1.00 14.05 ?  82  VAL   A HB   1 
ATOM   1679 H HG11 . VAL   A 1 82  ? 33.678 -5.234  10.127  1.00 16.08 ?  82  VAL   A HG11 1 
ATOM   1680 H HG12 . VAL   A 1 82  ? 34.174 -3.734  9.967   1.00 16.08 ?  82  VAL   A HG12 1 
ATOM   1681 H HG13 . VAL   A 1 82  ? 32.680 -4.124  9.586   1.00 16.08 ?  82  VAL   A HG13 1 
ATOM   1682 H HG21 . VAL   A 1 82  ? 33.727 -6.748  8.336   1.00 15.43 ?  82  VAL   A HG21 1 
ATOM   1683 H HG22 . VAL   A 1 82  ? 32.516 -5.992  7.638   1.00 15.43 ?  82  VAL   A HG22 1 
ATOM   1684 H HG23 . VAL   A 1 82  ? 33.855 -6.266  6.828   1.00 15.43 ?  82  VAL   A HG23 1 
ATOM   1685 N N    . LEU   A 1 83  ? 33.372 -1.357  8.141   1.00 10.22 ?  83  LEU   A N    1 
ATOM   1686 C CA   . LEU   A 1 83  ? 33.796 -0.093  8.718   1.00 10.39 ?  83  LEU   A CA   1 
ATOM   1687 C C    . LEU   A 1 83  ? 33.081 0.081   10.056  1.00 10.37 ?  83  LEU   A C    1 
ATOM   1688 O O    . LEU   A 1 83  ? 32.363 -0.816  10.521  1.00 10.98 ?  83  LEU   A O    1 
ATOM   1689 C CB   . LEU   A 1 83  ? 33.543 1.063   7.739   1.00 10.49 ?  83  LEU   A CB   1 
ATOM   1690 C CG   . LEU   A 1 83  ? 34.425 1.072   6.485   1.00 11.14 ?  83  LEU   A CG   1 
ATOM   1691 C CD1  . LEU   A 1 83  ? 33.980 2.131   5.497   1.00 11.75 ?  83  LEU   A CD1  1 
ATOM   1692 C CD2  . LEU   A 1 83  ? 35.898 1.279   6.859   1.00 12.20 ?  83  LEU   A CD2  1 
ATOM   1693 H H    . LEU   A 1 83  ? 32.522 -1.448  8.113   1.00 12.28 ?  83  LEU   A H    1 
ATOM   1694 H HA   . LEU   A 1 83  ? 34.751 -0.126  8.896   1.00 12.48 ?  83  LEU   A HA   1 
ATOM   1695 H HB2  . LEU   A 1 83  ? 32.622 1.019   7.441   1.00 12.60 ?  83  LEU   A HB2  1 
ATOM   1696 H HB3  . LEU   A 1 83  ? 33.692 1.902   8.203   1.00 12.60 ?  83  LEU   A HB3  1 
ATOM   1697 H HG   . LEU   A 1 83  ? 34.358 0.209   6.048   1.00 13.39 ?  83  LEU   A HG   1 
ATOM   1698 H HD11 . LEU   A 1 83  ? 34.562 2.099   4.720   1.00 14.12 ?  83  LEU   A HD11 1 
ATOM   1699 H HD12 . LEU   A 1 83  ? 33.067 1.945   5.235   1.00 14.12 ?  83  LEU   A HD12 1 
ATOM   1700 H HD13 . LEU   A 1 83  ? 34.039 2.999   5.920   1.00 14.12 ?  83  LEU   A HD13 1 
ATOM   1701 H HD21 . LEU   A 1 83  ? 36.415 1.429   6.047   1.00 14.66 ?  83  LEU   A HD21 1 
ATOM   1702 H HD22 . LEU   A 1 83  ? 35.974 2.052   7.440   1.00 14.66 ?  83  LEU   A HD22 1 
ATOM   1703 H HD23 . LEU   A 1 83  ? 36.230 0.489   7.313   1.00 14.66 ?  83  LEU   A HD23 1 
ATOM   1704 N N    . SER   A 1 84  ? 33.295 1.232   10.688  1.00 11.01 ?  84  SER   A N    1 
ATOM   1705 C CA   . SER   A 1 84  ? 32.651 1.486   11.966  1.00 11.03 ?  84  SER   A CA   1 
ATOM   1706 C C    . SER   A 1 84  ? 31.133 1.578   11.819  1.00 10.63 ?  84  SER   A C    1 
ATOM   1707 O O    . SER   A 1 84  ? 30.610 2.050   10.810  1.00 11.00 ?  84  SER   A O    1 
ATOM   1708 C CB   . SER   A 1 84  ? 33.162 2.796   12.557  1.00 11.72 ?  84  SER   A CB   1 
ATOM   1709 O OG   . SER   A 1 84  ? 32.527 3.073   13.790  1.00 12.57 ?  84  SER   A OG   1 
ATOM   1710 H H    . SER   A 1 84  ? 33.799 1.872   10.392  1.00 13.23 ?  84  SER   A H    1 
ATOM   1711 H HA   . SER   A 1 84  ? 32.868 0.766   12.574  1.00 13.25 ?  84  SER   A HA   1 
ATOM   1712 H HB2  . SER   A 1 84  ? 34.121 2.727   12.703  1.00 14.08 ?  84  SER   A HB2  1 
ATOM   1713 H HB3  . SER   A 1 84  ? 32.979 3.518   11.932  1.00 14.08 ?  84  SER   A HB3  1 
ATOM   1714 H HG   . SER   A 1 84  ? 32.812 3.800   14.108  1.00 15.10 ?  84  SER   A HG   1 
ATOM   1715 N N    . GLY   A 1 85  ? 30.428 1.174   12.870  1.00 11.63 ?  85  GLY   A N    1 
ATOM   1716 C CA   . GLY   A 1 85  ? 29.010 1.432   12.959  1.00 12.36 ?  85  GLY   A CA   1 
ATOM   1717 C C    . GLY   A 1 85  ? 28.659 2.735   13.627  1.00 11.77 ?  85  GLY   A C    1 
ATOM   1718 O O    . GLY   A 1 85  ? 27.473 3.054   13.758  1.00 12.57 ?  85  GLY   A O    1 
ATOM   1719 H H    . GLY   A 1 85  ? 30.760 0.749   13.542  1.00 13.98 ?  85  GLY   A H    1 
ATOM   1720 H HA2  . GLY   A 1 85  ? 28.635 1.439   12.064  1.00 14.85 ?  85  GLY   A HA2  1 
ATOM   1721 H HA3  . GLY   A 1 85  ? 28.592 0.718   13.457  1.00 14.85 ?  85  GLY   A HA3  1 
ATOM   1722 N N    . HIS   A 1 86  ? 29.658 3.492   14.065  1.00 11.63 ?  86  HIS   A N    1 
ATOM   1723 C CA   . HIS   A 1 86  ? 29.446 4.822   14.642  1.00 12.34 ?  86  HIS   A CA   1 
ATOM   1724 C C    . HIS   A 1 86  ? 28.469 4.698   15.804  1.00 13.04 ?  86  HIS   A C    1 
ATOM   1725 O O    . HIS   A 1 86  ? 28.646 3.812   16.656  1.00 13.99 ?  86  HIS   A O    1 
ATOM   1726 C CB   . HIS   A 1 86  ? 29.062 5.810   13.548  1.00 12.00 ?  86  HIS   A CB   1 
ATOM   1727 C CG   . HIS   A 1 86  ? 30.109 5.917   12.500  1.00 12.06 ?  86  HIS   A CG   1 
ATOM   1728 N ND1  . HIS   A 1 86  ? 31.209 6.739   12.630  1.00 13.56 ?  86  HIS   A ND1  1 
ATOM   1729 C CD2  . HIS   A 1 86  ? 30.271 5.241   11.341  1.00 11.57 ?  86  HIS   A CD2  1 
ATOM   1730 C CE1  . HIS   A 1 86  ? 31.990 6.577   11.576  1.00 13.10 ?  86  HIS   A CE1  1 
ATOM   1731 N NE2  . HIS   A 1 86  ? 31.448 5.670   10.785  1.00 11.99 ?  86  HIS   A NE2  1 
ATOM   1732 H H    . HIS   A 1 86  ? 30.485 3.256   14.053  1.00 13.97 ?  86  HIS   A H    1 
ATOM   1733 H HA   . HIS   A 1 86  ? 30.288 5.131   15.012  1.00 14.83 ?  86  HIS   A HA   1 
ATOM   1734 H HB2  . HIS   A 1 86  ? 28.238 5.524   13.126  1.00 14.41 ?  86  HIS   A HB2  1 
ATOM   1735 H HB3  . HIS   A 1 86  ? 28.942 6.695   13.939  1.00 14.41 ?  86  HIS   A HB3  1 
ATOM   1736 H HD2  . HIS   A 1 86  ? 29.696 4.593   10.992  1.00 13.90 ?  86  HIS   A HD2  1 
ATOM   1737 H HE1  . HIS   A 1 86  ? 32.784 7.030   11.403  1.00 15.74 ?  86  HIS   A HE1  1 
ATOM   1738 H HE2  . HIS   A 1 86  ? 31.769 5.398   10.027  1.00 14.40 ?  86  HIS   A HE2  1 
ATOM   1739 N N    . ASN   A 1 87  ? 27.470 5.559   15.891  1.00 13.99 ?  87  ASN   A N    1 
ATOM   1740 C CA   . ASN   A 1 87  ? 26.503 5.554   16.970  1.00 14.96 ?  87  ASN   A CA   1 
ATOM   1741 C C    . ASN   A 1 87  ? 25.372 4.563   16.748  1.00 15.99 ?  87  ASN   A C    1 
ATOM   1742 O O    . ASN   A 1 87  ? 24.476 4.484   17.590  1.00 18.30 ?  87  ASN   A O    1 
ATOM   1743 C CB   . ASN   A 1 87  ? 25.914 6.961   17.121  1.00 15.77 ?  87  ASN   A CB   1 
ATOM   1744 C CG   . ASN   A 1 87  ? 25.395 7.526   15.804  1.00 16.59 ?  87  ASN   A CG   1 
ATOM   1745 O OD1  . ASN   A 1 87  ? 26.049 7.437   14.767  1.00 17.20 ?  87  ASN   A OD1  1 
ATOM   1746 N ND2  . ASN   A 1 87  ? 24.213 8.110   15.845  1.00 17.61 ?  87  ASN   A ND2  1 
ATOM   1747 H H    . ASN   A 1 87  ? 27.327 6.175   15.316  1.00 16.81 ?  87  ASN   A H    1 
ATOM   1748 H HA   . ASN   A 1 87  ? 26.944 5.318   17.804  1.00 17.96 ?  87  ASN   A HA   1 
ATOM   1749 H HB2  . ASN   A 1 87  ? 25.170 6.927   17.753  1.00 18.95 ?  87  ASN   A HB2  1 
ATOM   1750 H HB3  . ASN   A 1 87  ? 26.600 7.556   17.458  1.00 18.95 ?  87  ASN   A HB3  1 
ATOM   1751 H HD21 . ASN   A 1 87  ? 23.875 8.437   15.128  1.00 21.15 ?  87  ASN   A HD21 1 
ATOM   1752 H HD22 . ASN   A 1 87  ? 23.779 8.154   16.587  1.00 21.15 ?  87  ASN   A HD22 1 
ATOM   1753 N N    A LEU   A 1 88  ? 25.404 3.799   15.659  0.62 15.05 ?  88  LEU   A N    1 
ATOM   1754 N N    B LEU   A 1 88  ? 25.392 3.800   15.655  0.38 15.42 ?  88  LEU   A N    1 
ATOM   1755 C CA   A LEU   A 1 88  ? 24.287 2.943   15.275  0.62 14.82 ?  88  LEU   A CA   1 
ATOM   1756 C CA   B LEU   A 1 88  ? 24.268 2.943   15.288  0.38 15.24 ?  88  LEU   A CA   1 
ATOM   1757 C C    A LEU   A 1 88  ? 24.502 1.470   15.589  0.62 14.50 ?  88  LEU   A C    1 
ATOM   1758 C C    B LEU   A 1 88  ? 24.499 1.461   15.555  0.38 14.67 ?  88  LEU   A C    1 
ATOM   1759 O O    A LEU   A 1 88  ? 23.525 0.750   15.822  0.62 15.97 ?  88  LEU   A O    1 
ATOM   1760 O O    B LEU   A 1 88  ? 23.526 0.719   15.724  0.38 15.55 ?  88  LEU   A O    1 
ATOM   1761 C CB   A LEU   A 1 88  ? 24.032 3.077   13.772  0.62 15.37 ?  88  LEU   A CB   1 
ATOM   1762 C CB   B LEU   A 1 88  ? 23.938 3.125   13.802  0.38 15.76 ?  88  LEU   A CB   1 
ATOM   1763 C CG   A LEU   A 1 88  ? 23.717 4.476   13.243  0.62 17.03 ?  88  LEU   A CG   1 
ATOM   1764 C CG   B LEU   A 1 88  ? 23.640 4.562   13.373  0.38 16.55 ?  88  LEU   A CG   1 
ATOM   1765 C CD1  A LEU   A 1 88  ? 23.547 4.426   11.736  0.62 17.55 ?  88  LEU   A CD1  1 
ATOM   1766 C CD1  B LEU   A 1 88  ? 23.415 4.642   11.869  0.38 16.58 ?  88  LEU   A CD1  1 
ATOM   1767 C CD2  A LEU   A 1 88  ? 22.473 5.042   13.908  0.62 18.64 ?  88  LEU   A CD2  1 
ATOM   1768 C CD2  B LEU   A 1 88  ? 22.437 5.107   14.130  0.38 17.54 ?  88  LEU   A CD2  1 
ATOM   1769 H H    A LEU   A 1 88  ? 26.074 3.757   15.123  0.62 18.08 ?  88  LEU   A H    1 
ATOM   1770 H H    B LEU   A 1 88  ? 26.049 3.771   15.104  0.38 18.52 ?  88  LEU   A H    1 
ATOM   1771 H HA   A LEU   A 1 88  ? 23.491 3.235   15.743  0.62 17.80 ?  88  LEU   A HA   1 
ATOM   1772 H HA   B LEU   A 1 88  ? 23.490 3.217   15.796  0.38 18.30 ?  88  LEU   A HA   1 
ATOM   1773 H HB2  A LEU   A 1 88  ? 24.819 2.769   13.302  0.62 18.46 ?  88  LEU   A HB2  1 
ATOM   1774 H HB2  B LEU   A 1 88  ? 24.690 2.814   13.276  0.38 18.93 ?  88  LEU   A HB2  1 
ATOM   1775 H HB3  A LEU   A 1 88  ? 23.277 2.514   13.544  0.62 18.46 ?  88  LEU   A HB3  1 
ATOM   1776 H HB3  B LEU   A 1 88  ? 23.153 2.593   13.593  0.38 18.93 ?  88  LEU   A HB3  1 
ATOM   1777 H HG   A LEU   A 1 88  ? 24.459 5.068   13.439  0.62 20.45 ?  88  LEU   A HG   1 
ATOM   1778 H HG   B LEU   A 1 88  ? 24.406 5.116   13.587  0.38 19.88 ?  88  LEU   A HG   1 
ATOM   1779 H HD11 A LEU   A 1 88  ? 23.372 5.320   11.405  0.62 21.08 ?  88  LEU   A HD11 1 
ATOM   1780 H HD11 B LEU   A 1 88  ? 23.236 5.564   11.625  0.38 19.91 ?  88  LEU   A HD11 1 
ATOM   1781 H HD12 A LEU   A 1 88  ? 24.360 4.078   11.338  0.62 21.08 ?  88  LEU   A HD12 1 
ATOM   1782 H HD12 B LEU   A 1 88  ? 24.212 4.329   11.411  0.38 19.91 ?  88  LEU   A HD12 1 
ATOM   1783 H HD13 A LEU   A 1 88  ? 22.800 3.843   11.523  0.62 21.08 ?  88  LEU   A HD13 1 
ATOM   1784 H HD13 B LEU   A 1 88  ? 22.657 4.084   11.631  0.38 19.91 ?  88  LEU   A HD13 1 
ATOM   1785 H HD21 A LEU   A 1 88  ? 22.245 5.885   13.484  0.62 22.38 ?  88  LEU   A HD21 1 
ATOM   1786 H HD21 B LEU   A 1 88  ? 22.183 5.959   13.744  0.38 21.06 ?  88  LEU   A HD21 1 
ATOM   1787 H HD22 A LEU   A 1 88  ? 21.745 4.411   13.803  0.62 22.38 ?  88  LEU   A HD22 1 
ATOM   1788 H HD22 B LEU   A 1 88  ? 21.705 4.476   14.052  0.38 21.06 ?  88  LEU   A HD22 1 
ATOM   1789 H HD23 A LEU   A 1 88  ? 22.658 5.184   14.849  0.62 22.38 ?  88  LEU   A HD23 1 
ATOM   1790 H HD23 B LEU   A 1 88  ? 22.677 5.223   15.062  0.38 21.06 ?  88  LEU   A HD23 1 
ATOM   1791 N N    . ALA   A 1 89  ? 25.749 1.013   15.583  1.00 13.55 ?  89  ALA   A N    1 
ATOM   1792 C CA   . ALA   A 1 89  ? 26.076 -0.403  15.685  1.00 12.93 ?  89  ALA   A CA   1 
ATOM   1793 C C    . ALA   A 1 89  ? 27.566 -0.478  15.973  1.00 13.63 ?  89  ALA   A C    1 
ATOM   1794 O O    . ALA   A 1 89  ? 28.281 0.516   15.844  1.00 14.26 ?  89  ALA   A O    1 
ATOM   1795 C CB   . ALA   A 1 89  ? 25.773 -1.108  14.365  1.00 12.60 ?  89  ALA   A CB   1 
ATOM   1796 H H    A ALA   A 1 89  ? 26.441 1.522   15.515  0.62 16.28 ?  89  ALA   A H    1 
ATOM   1797 H H    B ALA   A 1 89  ? 26.441 1.525   15.535  0.38 16.28 ?  89  ALA   A H    1 
ATOM   1798 H HA   . ALA   A 1 89  ? 25.574 -0.814  16.410  1.00 15.53 ?  89  ALA   A HA   1 
ATOM   1799 H HB1  . ALA   A 1 89  ? 26.014 -2.045  14.451  1.00 15.13 ?  89  ALA   A HB1  1 
ATOM   1800 H HB2  . ALA   A 1 89  ? 24.824 -1.030  14.174  1.00 15.13 ?  89  ALA   A HB2  1 
ATOM   1801 H HB3  . ALA   A 1 89  ? 26.290 -0.695  13.661  1.00 15.13 ?  89  ALA   A HB3  1 
ATOM   1802 N N    . LYS   A 1 90  ? 28.044 -1.661  16.356  1.00 13.86 ?  90  LYS   A N    1 
ATOM   1803 C CA   . LYS   A 1 90  ? 29.489 -1.820  16.490  1.00 14.64 ?  90  LYS   A CA   1 
ATOM   1804 C C    . LYS   A 1 90  ? 30.177 -1.626  15.139  1.00 13.84 ?  90  LYS   A C    1 
ATOM   1805 O O    . LYS   A 1 90  ? 31.105 -0.812  15.003  1.00 15.04 ?  90  LYS   A O    1 
ATOM   1806 C CB   . LYS   A 1 90  ? 29.826 -3.185  17.094  1.00 17.03 ?  90  LYS   A CB   1 
ATOM   1807 C CG   . LYS   A 1 90  ? 31.295 -3.323  17.458  1.00 21.02 ?  90  LYS   A CG   1 
ATOM   1808 C CD   . LYS   A 1 90  ? 31.534 -4.550  18.322  1.00 25.39 ?  90  LYS   A CD   1 
ATOM   1809 C CE   . LYS   A 1 90  ? 32.961 -4.612  18.841  1.00 28.77 ?  90  LYS   A CE   1 
ATOM   1810 N NZ   . LYS   A 1 90  ? 33.931 -4.987  17.777  1.00 30.50 ?  90  LYS   A NZ   1 
ATOM   1811 H H    . LYS   A 1 90  ? 27.571 -2.350  16.540  1.00 16.64 ?  90  LYS   A H    1 
ATOM   1812 H HA   . LYS   A 1 90  ? 29.825 -1.138  17.091  1.00 17.58 ?  90  LYS   A HA   1 
ATOM   1813 H HB2  . LYS   A 1 90  ? 29.300 -3.310  17.901  1.00 20.45 ?  90  LYS   A HB2  1 
ATOM   1814 H HB3  . LYS   A 1 90  ? 29.608 -3.877  16.448  1.00 20.45 ?  90  LYS   A HB3  1 
ATOM   1815 H HG2  . LYS   A 1 90  ? 31.821 -3.414  16.649  1.00 25.23 ?  90  LYS   A HG2  1 
ATOM   1816 H HG3  . LYS   A 1 90  ? 31.578 -2.540  17.957  1.00 25.23 ?  90  LYS   A HG3  1 
ATOM   1817 H HD2  . LYS   A 1 90  ? 30.936 -4.526  19.087  1.00 30.49 ?  90  LYS   A HD2  1 
ATOM   1818 H HD3  . LYS   A 1 90  ? 31.369 -5.350  17.797  1.00 30.49 ?  90  LYS   A HD3  1 
ATOM   1819 H HE2  . LYS   A 1 90  ? 33.213 -3.740  19.184  1.00 34.54 ?  90  LYS   A HE2  1 
ATOM   1820 H HE3  . LYS   A 1 90  ? 33.016 -5.275  19.548  1.00 34.54 ?  90  LYS   A HE3  1 
ATOM   1821 H HZ1  . LYS   A 1 90  ? 34.754 -5.029  18.117  1.00 36.61 ?  90  LYS   A HZ1  1 
ATOM   1822 H HZ2  . LYS   A 1 90  ? 33.718 -5.783  17.439  1.00 36.61 ?  90  LYS   A HZ2  1 
ATOM   1823 H HZ3  . LYS   A 1 90  ? 33.918 -4.382  17.126  1.00 36.61 ?  90  LYS   A HZ3  1 
ATOM   1824 N N    . HIS   A 1 91  ? 29.701 -2.343  14.121  1.00 12.28 ?  91  HIS   A N    1 
ATOM   1825 C CA   . HIS   A 1 91  ? 30.268 -2.328  12.786  1.00 11.62 ?  91  HIS   A CA   1 
ATOM   1826 C C    . HIS   A 1 91  ? 29.176 -2.043  11.772  1.00 10.51 ?  91  HIS   A C    1 
ATOM   1827 O O    . HIS   A 1 91  ? 28.010 -2.391  11.980  1.00 11.16 ?  91  HIS   A O    1 
ATOM   1828 C CB   . HIS   A 1 91  ? 30.844 -3.704  12.418  1.00 13.63 ?  91  HIS   A CB   1 
ATOM   1829 C CG   . HIS   A 1 91  ? 31.846 -4.232  13.394  1.00 18.49 ?  91  HIS   A CG   1 
ATOM   1830 N ND1  . HIS   A 1 91  ? 33.120 -3.719  13.504  1.00 20.77 ?  91  HIS   A ND1  1 
ATOM   1831 C CD2  . HIS   A 1 91  ? 31.768 -5.240  14.296  1.00 20.65 ?  91  HIS   A CD2  1 
ATOM   1832 C CE1  . HIS   A 1 91  ? 33.781 -4.383  14.436  1.00 21.85 ?  91  HIS   A CE1  1 
ATOM   1833 N NE2  . HIS   A 1 91  ? 32.984 -5.313  14.931  1.00 22.15 ?  91  HIS   A NE2  1 
ATOM   1834 H H    . HIS   A 1 91  ? 29.021 -2.880  14.192  1.00 14.76 ?  91  HIS   A H    1 
ATOM   1835 H HA   . HIS   A 1 91  ? 30.962 -1.659  12.718  1.00 13.96 ?  91  HIS   A HA   1 
ATOM   1836 H HB2  . HIS   A 1 91  ? 30.114 -4.346  12.371  1.00 16.37 ?  91  HIS   A HB2  1 
ATOM   1837 H HB3  . HIS   A 1 91  ? 31.277 -3.641  11.553  1.00 16.37 ?  91  HIS   A HB3  1 
ATOM   1838 H HD1  . HIS   A 1 91  ? 33.435 -3.066  13.036  1.00 24.94 ?  91  HIS   A HD1  1 
ATOM   1839 H HD2  . HIS   A 1 91  ? 31.029 -5.778  14.457  1.00 24.79 ?  91  HIS   A HD2  1 
ATOM   1840 H HE1  . HIS   A 1 91  ? 34.660 -4.220  14.695  1.00 26.23 ?  91  HIS   A HE1  1 
ATOM   1841 N N    . CYS   A 1 92  ? 29.577 -1.460  10.646  1.00 10.46 ?  92  CYS   A N    1 
ATOM   1842 C CA   . CYS   A 1 92  ? 28.731 -1.381  9.463   1.00 10.01 ?  92  CYS   A CA   1 
ATOM   1843 C C    . CYS   A 1 92  ? 29.373 -2.200  8.354   1.00 9.63  ?  92  CYS   A C    1 
ATOM   1844 O O    . CYS   A 1 92  ? 30.530 -1.953  7.988   1.00 10.28 ?  92  CYS   A O    1 
ATOM   1845 C CB   . CYS   A 1 92  ? 28.528 0.063   9.002   1.00 10.59 ?  92  CYS   A CB   1 
ATOM   1846 S SG   . CYS   A 1 92  ? 27.505 0.181   7.498   1.00 9.91  ?  92  CYS   A SG   1 
ATOM   1847 H H    . CYS   A 1 92  ? 30.348 -1.096  10.539  1.00 12.57 ?  92  CYS   A H    1 
ATOM   1848 H HA   . CYS   A 1 92  ? 27.863 -1.761  9.658   1.00 12.03 ?  92  CYS   A HA   1 
ATOM   1849 H HB2  . CYS   A 1 92  ? 28.084 0.563   9.705   1.00 12.73 ?  92  CYS   A HB2  1 
ATOM   1850 H HB3  . CYS   A 1 92  ? 29.391 0.461   8.807   1.00 12.73 ?  92  CYS   A HB3  1 
ATOM   1851 H HG   . CYS   A 1 92  ? 27.381 1.339   7.209   1.00 11.91 ?  92  CYS   A HG   1 
ATOM   1852 N N    . LEU   A 1 93  ? 28.635 -3.177  7.842   1.00 9.38  ?  93  LEU   A N    1 
ATOM   1853 C CA   . LEU   A 1 93  ? 29.041 -3.934  6.667   1.00 8.73  ?  93  LEU   A CA   1 
ATOM   1854 C C    . LEU   A 1 93  ? 28.444 -3.240  5.452   1.00 8.53  ?  93  LEU   A C    1 
ATOM   1855 O O    . LEU   A 1 93  ? 27.227 -3.295  5.235   1.00 8.88  ?  93  LEU   A O    1 
ATOM   1856 C CB   . LEU   A 1 93  ? 28.558 -5.378  6.775   1.00 9.48  ?  93  LEU   A CB   1 
ATOM   1857 C CG   . LEU   A 1 93  ? 28.935 -6.282  5.603   1.00 9.85  ?  93  LEU   A CG   1 
ATOM   1858 C CD1  . LEU   A 1 93  ? 30.448 -6.543  5.579   1.00 10.81 ?  93  LEU   A CD1  1 
ATOM   1859 C CD2  . LEU   A 1 93  ? 28.166 -7.607  5.616   1.00 10.65 ?  93  LEU   A CD2  1 
ATOM   1860 H H    . LEU   A 1 93  ? 27.878 -3.417  8.165   1.00 11.27 ?  93  LEU   A H    1 
ATOM   1861 H HA   . LEU   A 1 93  ? 30.004 -3.925  6.587   1.00 10.49 ?  93  LEU   A HA   1 
ATOM   1862 H HB2  . LEU   A 1 93  ? 28.942 -5.765  7.580   1.00 11.39 ?  93  LEU   A HB2  1 
ATOM   1863 H HB3  . LEU   A 1 93  ? 27.594 -5.379  6.842   1.00 11.39 ?  93  LEU   A HB3  1 
ATOM   1864 H HG   . LEU   A 1 93  ? 28.718 -5.832  4.781   1.00 11.83 ?  93  LEU   A HG   1 
ATOM   1865 H HD11 . LEU   A 1 93  ? 30.661 -7.156  4.859   1.00 12.99 ?  93  LEU   A HD11 1 
ATOM   1866 H HD12 . LEU   A 1 93  ? 30.919 -5.703  5.448   1.00 12.99 ?  93  LEU   A HD12 1 
ATOM   1867 H HD13 . LEU   A 1 93  ? 30.723 -6.936  6.431   1.00 12.99 ?  93  LEU   A HD13 1 
ATOM   1868 H HD21 . LEU   A 1 93  ? 28.449 -8.143  4.854   1.00 12.80 ?  93  LEU   A HD21 1 
ATOM   1869 H HD22 . LEU   A 1 93  ? 28.359 -8.082  6.439   1.00 12.80 ?  93  LEU   A HD22 1 
ATOM   1870 H HD23 . LEU   A 1 93  ? 27.219 -7.419  5.553   1.00 12.80 ?  93  LEU   A HD23 1 
ATOM   1871 N N    . HIS   A 1 94  ? 29.290 -2.552  4.688   1.00 8.38  ?  94  HIS   A N    1 
ATOM   1872 C CA   . HIS   A 1 94  ? 28.861 -1.877  3.469   1.00 8.56  ?  94  HIS   A CA   1 
ATOM   1873 C C    . HIS   A 1 94  ? 28.858 -2.907  2.355   1.00 8.76  ?  94  HIS   A C    1 
ATOM   1874 O O    . HIS   A 1 94  ? 29.921 -3.430  2.006   1.00 10.23 ?  94  HIS   A O    1 
ATOM   1875 C CB   . HIS   A 1 94  ? 29.824 -0.735  3.132   1.00 8.88  ?  94  HIS   A CB   1 
ATOM   1876 C CG   . HIS   A 1 94  ? 29.814 0.360   4.144   1.00 8.69  ?  94  HIS   A CG   1 
ATOM   1877 N ND1  . HIS   A 1 94  ? 28.941 1.431   4.090   1.00 8.79  ?  94  HIS   A ND1  1 
ATOM   1878 C CD2  . HIS   A 1 94  ? 30.554 0.524   5.265   1.00 9.35  ?  94  HIS   A CD2  1 
ATOM   1879 C CE1  . HIS   A 1 94  ? 29.164 2.208   5.134   1.00 8.89  ?  94  HIS   A CE1  1 
ATOM   1880 N NE2  . HIS   A 1 94  ? 30.133 1.680   5.862   1.00 9.40  ?  94  HIS   A NE2  1 
ATOM   1881 H H    . HIS   A 1 94  ? 30.131 -2.458  4.850   1.00 10.08 ?  94  HIS   A H    1 
ATOM   1882 H HA   . HIS   A 1 94  ? 27.962 -1.519  3.576   1.00 10.29 ?  94  HIS   A HA   1 
ATOM   1883 H HB2  . HIS   A 1 94  ? 30.719 -1.090  3.079   1.00 10.68 ?  94  HIS   A HB2  1 
ATOM   1884 H HB3  . HIS   A 1 94  ? 29.565 -0.353  2.275   1.00 10.68 ?  94  HIS   A HB3  1 
ATOM   1885 H HD2  . HIS   A 1 94  ? 31.222 -0.042  5.569   1.00 11.24 ?  94  HIS   A HD2  1 
ATOM   1886 H HE1  . HIS   A 1 94  ? 28.702 2.993   5.322   1.00 10.68 ?  94  HIS   A HE1  1 
ATOM   1887 H HE2  . HIS   A 1 94  ? 30.446 2.015   6.584   1.00 11.30 ?  94  HIS   A HE2  1 
ATOM   1888 N N    . VAL   A 1 95  ? 27.680 -3.229  1.818   1.00 8.13  ?  95  VAL   A N    1 
ATOM   1889 C CA   . VAL   A 1 95  ? 27.530 -4.261  0.792   1.00 8.70  ?  95  VAL   A CA   1 
ATOM   1890 C C    . VAL   A 1 95  ? 26.984 -3.624  -0.475  1.00 7.93  ?  95  VAL   A C    1 
ATOM   1891 O O    . VAL   A 1 95  ? 25.985 -2.897  -0.418  1.00 9.01  ?  95  VAL   A O    1 
ATOM   1892 C CB   . VAL   A 1 95  ? 26.601 -5.401  1.248   1.00 9.18  ?  95  VAL   A CB   1 
ATOM   1893 C CG1  . VAL   A 1 95  ? 26.474 -6.452  0.145   1.00 9.97  ?  95  VAL   A CG1  1 
ATOM   1894 C CG2  . VAL   A 1 95  ? 27.106 -6.014  2.534   1.00 9.29  ?  95  VAL   A CG2  1 
ATOM   1895 H H    . VAL   A 1 95  ? 26.929 -2.864  2.043   1.00 9.77  ?  95  VAL   A H    1 
ATOM   1896 H HA   . VAL   A 1 95  ? 28.398 -4.639  0.590   1.00 10.45 ?  95  VAL   A HA   1 
ATOM   1897 H HB   . VAL   A 1 95  ? 25.720 -5.042  1.416   1.00 11.03 ?  95  VAL   A HB   1 
ATOM   1898 H HG11 . VAL   A 1 95  ? 26.078 -7.256  0.520   1.00 11.98 ?  95  VAL   A HG11 1 
ATOM   1899 H HG12 . VAL   A 1 95  ? 25.913 -6.108  -0.564  1.00 11.98 ?  95  VAL   A HG12 1 
ATOM   1900 H HG13 . VAL   A 1 95  ? 27.360 -6.657  -0.201  1.00 11.98 ?  95  VAL   A HG13 1 
ATOM   1901 H HG21 . VAL   A 1 95  ? 26.550 -6.772  2.761   1.00 11.17 ?  95  VAL   A HG21 1 
ATOM   1902 H HG22 . VAL   A 1 95  ? 28.025 -6.295  2.410   1.00 11.17 ?  95  VAL   A HG22 1 
ATOM   1903 H HG23 . VAL   A 1 95  ? 27.058 -5.344  3.237   1.00 11.17 ?  95  VAL   A HG23 1 
ATOM   1904 N N    . VAL   A 1 96  ? 27.605 -3.919  -1.615  1.00 8.24  ?  96  VAL   A N    1 
ATOM   1905 C CA   . VAL   A 1 96  ? 27.192 -3.364  -2.899  1.00 9.06  ?  96  VAL   A CA   1 
ATOM   1906 C C    . VAL   A 1 96  ? 26.380 -4.410  -3.661  1.00 9.33  ?  96  VAL   A C    1 
ATOM   1907 O O    . VAL   A 1 96  ? 26.934 -5.346  -4.244  1.00 10.16 ?  96  VAL   A O    1 
ATOM   1908 C CB   . VAL   A 1 96  ? 28.381 -2.882  -3.732  1.00 9.29  ?  96  VAL   A CB   1 
ATOM   1909 C CG1  . VAL   A 1 96  ? 27.873 -2.249  -5.006  1.00 9.47  ?  96  VAL   A CG1  1 
ATOM   1910 C CG2  . VAL   A 1 96  ? 29.252 -1.921  -2.941  1.00 9.97  ?  96  VAL   A CG2  1 
ATOM   1911 H H    . VAL   A 1 96  ? 28.294 -4.445  -1.674  1.00 9.90  ?  96  VAL   A H    1 
ATOM   1912 H HA   . VAL   A 1 96  ? 26.619 -2.601  -2.739  1.00 10.89 ?  96  VAL   A HA   1 
ATOM   1913 H HB   . VAL   A 1 96  ? 28.928 -3.640  -3.977  1.00 11.17 ?  96  VAL   A HB   1 
ATOM   1914 H HG11 . VAL   A 1 96  ? 28.605 -1.764  -5.426  1.00 11.38 ?  96  VAL   A HG11 1 
ATOM   1915 H HG12 . VAL   A 1 96  ? 27.556 -2.943  -5.600  1.00 11.38 ?  96  VAL   A HG12 1 
ATOM   1916 H HG13 . VAL   A 1 96  ? 27.156 -1.635  -4.790  1.00 11.38 ?  96  VAL   A HG13 1 
ATOM   1917 H HG21 . VAL   A 1 96  ? 29.956 -1.575  -3.516  1.00 11.98 ?  96  VAL   A HG21 1 
ATOM   1918 H HG22 . VAL   A 1 96  ? 28.706 -1.184  -2.616  1.00 11.98 ?  96  VAL   A HG22 1 
ATOM   1919 H HG23 . VAL   A 1 96  ? 29.646 -2.391  -2.188  1.00 11.98 ?  96  VAL   A HG23 1 
ATOM   1920 N N    A GLY   A 1 97  ? 25.059 -4.262  -3.672  0.62 9.20  ?  97  GLY   A N    1 
ATOM   1921 N N    B GLY   A 1 97  ? 25.060 -4.241  -3.674  0.38 9.93  ?  97  GLY   A N    1 
ATOM   1922 C CA   A GLY   A 1 97  ? 24.245 -5.011  -4.594  0.62 9.69  ?  97  GLY   A CA   1 
ATOM   1923 C CA   B GLY   A 1 97  ? 24.213 -4.991  -4.566  0.38 10.82 ?  97  GLY   A CA   1 
ATOM   1924 C C    A GLY   A 1 97  ? 24.288 -4.358  -5.960  0.62 9.25  ?  97  GLY   A C    1 
ATOM   1925 C C    B GLY   A 1 97  ? 24.103 -4.293  -5.907  0.38 11.25 ?  97  GLY   A C    1 
ATOM   1926 O O    A GLY   A 1 97  ? 24.598 -3.169  -6.085  0.62 10.05 ?  97  GLY   A O    1 
ATOM   1927 O O    B GLY   A 1 97  ? 24.313 -3.081  -6.016  0.38 11.33 ?  97  GLY   A O    1 
ATOM   1928 H H    A GLY   A 1 97  ? 24.621 -3.729  -3.152  0.62 11.06 ?  97  GLY   A H    1 
ATOM   1929 H H    B GLY   A 1 97  ? 24.635 -3.688  -3.166  0.38 11.93 ?  97  GLY   A H    1 
ATOM   1930 H HA2  A GLY   A 1 97  ? 24.583 -5.919  -4.656  0.62 11.65 ?  97  GLY   A HA2  1 
ATOM   1931 H HA2  B GLY   A 1 97  ? 24.590 -5.876  -4.695  0.38 13.00 ?  97  GLY   A HA2  1 
ATOM   1932 H HA3  A GLY   A 1 97  ? 23.329 -5.039  -4.274  0.62 11.65 ?  97  GLY   A HA3  1 
ATOM   1933 H HA3  B GLY   A 1 97  ? 23.327 -5.082  -4.182  0.38 13.00 ?  97  GLY   A HA3  1 
ATOM   1934 N N    A PRO   A 1 98  ? 23.966 -5.105  -7.012  0.62 9.24  ?  98  PRO   A N    1 
ATOM   1935 N N    B PRO   A 1 98  ? 23.764 -5.040  -6.954  0.38 11.11 ?  98  PRO   A N    1 
ATOM   1936 C CA   A PRO   A 1 98  ? 23.863 -4.485  -8.336  0.62 10.75 ?  98  PRO   A CA   1 
ATOM   1937 C CA   B PRO   A 1 98  ? 23.641 -4.426  -8.283  0.38 11.61 ?  98  PRO   A CA   1 
ATOM   1938 C C    A PRO   A 1 98  ? 22.737 -3.463  -8.384  0.62 11.35 ?  98  PRO   A C    1 
ATOM   1939 C C    B PRO   A 1 98  ? 22.520 -3.395  -8.332  0.38 11.53 ?  98  PRO   A C    1 
ATOM   1940 O O    A PRO   A 1 98  ? 21.659 -3.664  -7.818  0.62 11.61 ?  98  PRO   A O    1 
ATOM   1941 O O    B PRO   A 1 98  ? 21.448 -3.584  -7.752  0.38 10.87 ?  98  PRO   A O    1 
ATOM   1942 C CB   A PRO   A 1 98  ? 23.578 -5.672  -9.262  0.62 11.24 ?  98  PRO   A CB   1 
ATOM   1943 C CB   B PRO   A 1 98  ? 23.355 -5.624  -9.198  0.38 12.18 ?  98  PRO   A CB   1 
ATOM   1944 C CG   A PRO   A 1 98  ? 22.948 -6.705  -8.370  0.62 11.15 ?  98  PRO   A CG   1 
ATOM   1945 C CG   B PRO   A 1 98  ? 22.779 -6.674  -8.291  0.38 11.83 ?  98  PRO   A CG   1 
ATOM   1946 C CD   A PRO   A 1 98  ? 23.660 -6.548  -7.050  0.62 9.80  ?  98  PRO   A CD   1 
ATOM   1947 C CD   B PRO   A 1 98  ? 23.484 -6.487  -6.980  0.38 11.14 ?  98  PRO   A CD   1 
ATOM   1948 H HA   A PRO   A 1 98  ? 24.701 -4.065  -8.580  0.62 12.92 ?  98  PRO   A HA   1 
ATOM   1949 H HA   B PRO   A 1 98  ? 24.477 -4.010  -8.540  0.38 13.94 ?  98  PRO   A HA   1 
ATOM   1950 H HB2  A PRO   A 1 98  ? 22.959 -5.394  -9.958  0.62 13.51 ?  98  PRO   A HB2  1 
ATOM   1951 H HB2  B PRO   A 1 98  ? 22.715 -5.370  -9.881  0.38 14.63 ?  98  PRO   A HB2  1 
ATOM   1952 H HB3  A PRO   A 1 98  ? 24.404 -5.996  -9.640  0.62 13.51 ?  98  PRO   A HB3  1 
ATOM   1953 H HB3  B PRO   A 1 98  ? 24.183 -5.933  -9.600  0.38 14.63 ?  98  PRO   A HB3  1 
ATOM   1954 H HG2  A PRO   A 1 98  ? 21.999 -6.523  -8.274  0.62 13.40 ?  98  PRO   A HG2  1 
ATOM   1955 H HG2  B PRO   A 1 98  ? 21.826 -6.532  -8.192  0.38 14.21 ?  98  PRO   A HG2  1 
ATOM   1956 H HG3  A PRO   A 1 98  ? 23.094 -7.587  -8.742  0.62 13.40 ?  98  PRO   A HG3  1 
ATOM   1957 H HG3  B PRO   A 1 98  ? 22.961 -7.555  -8.654  0.38 14.21 ?  98  PRO   A HG3  1 
ATOM   1958 H HD2  A PRO   A 1 98  ? 23.075 -6.797  -6.318  0.62 11.77 ?  98  PRO   A HD2  1 
ATOM   1959 H HD2  B PRO   A 1 98  ? 22.903 -6.738  -6.244  0.38 13.38 ?  98  PRO   A HD2  1 
ATOM   1960 H HD3  A PRO   A 1 98  ? 24.481 -7.068  -7.044  0.62 11.77 ?  98  PRO   A HD3  1 
ATOM   1961 H HD3  B PRO   A 1 98  ? 24.315 -6.985  -6.964  0.38 13.38 ?  98  PRO   A HD3  1 
ATOM   1962 N N    A ASN   A 1 99  ? 23.004 -2.348  -9.062  0.62 12.18 ?  99  ASN   A N    1 
ATOM   1963 N N    B ASN   A 1 99  ? 22.789 -2.284  -9.026  0.38 12.31 ?  99  ASN   A N    1 
ATOM   1964 C CA   A ASN   A 1 99  ? 22.010 -1.308  -9.303  0.62 12.85 ?  99  ASN   A CA   1 
ATOM   1965 C CA   B ASN   A 1 99  ? 21.819 -1.207  -9.219  0.38 12.51 ?  99  ASN   A CA   1 
ATOM   1966 C C    A ASN   A 1 99  ? 21.470 -1.514  -10.716 0.62 13.53 ?  99  ASN   A C    1 
ATOM   1967 C C    B ASN   A 1 99  ? 21.283 -1.274  -10.646 0.38 13.26 ?  99  ASN   A C    1 
ATOM   1968 O O    A ASN   A 1 99  ? 22.179 -1.291  -11.705 0.62 14.43 ?  99  ASN   A O    1 
ATOM   1969 O O    B ASN   A 1 99  ? 21.971 -0.883  -11.598 0.38 14.13 ?  99  ASN   A O    1 
ATOM   1970 C CB   A ASN   A 1 99  ? 22.638 0.076   -9.133  0.62 13.89 ?  99  ASN   A CB   1 
ATOM   1971 C CB   B ASN   A 1 99  ? 22.461 0.152   -8.944  0.38 12.12 ?  99  ASN   A CB   1 
ATOM   1972 C CG   A ASN   A 1 99  ? 21.608 1.200   -9.122  0.62 15.00 ?  99  ASN   A CG   1 
ATOM   1973 C CG   B ASN   A 1 99  ? 21.449 1.294   -8.941  0.38 12.13 ?  99  ASN   A CG   1 
ATOM   1974 O OD1  A ASN   A 1 99  ? 20.615 1.152   -9.853  0.62 15.77 ?  99  ASN   A OD1  1 
ATOM   1975 O OD1  B ASN   A 1 99  ? 20.499 1.305   -9.731  0.38 12.38 ?  99  ASN   A OD1  1 
ATOM   1976 N ND2  A ASN   A 1 99  ? 21.846 2.222   -8.294  0.62 15.41 ?  99  ASN   A ND2  1 
ATOM   1977 N ND2  B ASN   A 1 99  ? 21.650 2.260   -8.049  0.38 12.39 ?  99  ASN   A ND2  1 
ATOM   1978 H H    A ASN   A 1 99  ? 23.776 -2.161  -9.386  0.62 14.64 ?  99  ASN   A H    1 
ATOM   1979 H H    B ASN   A 1 99  ? 23.553 -2.124  -9.384  0.38 14.79 ?  99  ASN   A H    1 
ATOM   1980 H HA   A ASN   A 1 99  ? 21.279 -1.394  -8.656  0.62 15.44 ?  99  ASN   A HA   1 
ATOM   1981 H HA   B ASN   A 1 99  ? 21.077 -1.328  -8.604  0.38 15.03 ?  99  ASN   A HA   1 
ATOM   1982 H HB2  A ASN   A 1 99  ? 23.127 0.110   -8.293  0.62 16.68 ?  99  ASN   A HB2  1 
ATOM   1983 H HB2  B ASN   A 1 99  ? 22.894 0.131   -8.077  0.38 14.57 ?  99  ASN   A HB2  1 
ATOM   1984 H HB3  A ASN   A 1 99  ? 23.240 0.240   -9.873  0.62 16.68 ?  99  ASN   A HB3  1 
ATOM   1985 H HB3  B ASN   A 1 99  ? 23.114 0.336   -9.638  0.38 14.57 ?  99  ASN   A HB3  1 
ATOM   1986 H HD21 A ASN   A 1 99  ? 21.295 2.883   -8.243  0.62 18.51 ?  99  ASN   A HD21 1 
ATOM   1987 H HD21 B ASN   A 1 99  ? 21.106 2.925   -8.002  0.38 14.89 ?  99  ASN   A HD21 1 
ATOM   1988 H HD22 A ASN   A 1 99  ? 22.557 2.224   -7.803  0.62 18.51 ?  99  ASN   A HD22 1 
ATOM   1989 H HD22 B ASN   A 1 99  ? 22.324 2.218   -7.516  0.38 14.89 ?  99  ASN   A HD22 1 
ATOM   1990 N N    A VAL   A 1 100 ? 20.218 -1.973  -10.799 0.62 14.45 ?  100 VAL   A N    1 
ATOM   1991 N N    B VAL   A 1 100 ? 20.038 -1.739  -10.782 0.38 12.96 ?  100 VAL   A N    1 
ATOM   1992 C CA   A VAL   A 1 100 ? 19.594 -2.223  -12.092 0.62 16.58 ?  100 VAL   A CA   1 
ATOM   1993 C CA   B VAL   A 1 100 ? 19.422 -1.896  -12.095 0.38 13.47 ?  100 VAL   A CA   1 
ATOM   1994 C C    A VAL   A 1 100 ? 19.498 -0.941  -12.903 0.62 17.16 ?  100 VAL   A C    1 
ATOM   1995 C C    B VAL   A 1 100 ? 19.295 -0.557  -12.802 0.38 12.16 ?  100 VAL   A C    1 
ATOM   1996 O O    A VAL   A 1 100 ? 19.598 -0.967  -14.137 0.62 18.41 ?  100 VAL   A O    1 
ATOM   1997 O O    B VAL   A 1 100 ? 19.339 -0.492  -14.037 0.38 12.66 ?  100 VAL   A O    1 
ATOM   1998 C CB   A VAL   A 1 100 ? 18.222 -2.896  -11.886 0.62 18.23 ?  100 VAL   A CB   1 
ATOM   1999 C CB   B VAL   A 1 100 ? 18.064 -2.617  -11.952 0.38 15.16 ?  100 VAL   A CB   1 
ATOM   2000 C CG1  A VAL   A 1 100 ? 17.479 -3.033  -13.208 0.62 18.96 ?  100 VAL   A CG1  1 
ATOM   2001 C CG1  B VAL   A 1 100 ? 17.371 -2.756  -13.304 0.38 15.72 ?  100 VAL   A CG1  1 
ATOM   2002 C CG2  A VAL   A 1 100 ? 18.407 -4.252  -11.228 0.62 19.21 ?  100 VAL   A CG2  1 
ATOM   2003 C CG2  B VAL   A 1 100 ? 18.265 -3.980  -11.313 0.38 16.21 ?  100 VAL   A CG2  1 
ATOM   2004 H H    A VAL   A 1 100 ? 19.711 -2.147  -10.115 0.62 17.35 ?  100 VAL   A H    1 
ATOM   2005 H H    B VAL   A 1 100 ? 19.526 -1.951  -10.123 0.38 15.57 ?  100 VAL   A H    1 
ATOM   2006 H HA   A VAL   A 1 100 ? 20.155 -2.838  -12.582 0.62 19.91 ?  100 VAL   A HA   1 
ATOM   2007 H HA   B VAL   A 1 100 ? 19.991 -2.447  -12.641 0.38 16.18 ?  100 VAL   A HA   1 
ATOM   2008 H HB   A VAL   A 1 100 ? 17.685 -2.343  -11.297 0.62 21.89 ?  100 VAL   A HB   1 
ATOM   2009 H HB   B VAL   A 1 100 ? 17.484 -2.096  -11.374 0.38 18.21 ?  100 VAL   A HB   1 
ATOM   2010 H HG11 A VAL   A 1 100 ? 16.725 -3.628  -13.083 0.62 22.76 ?  100 VAL   A HG11 1 
ATOM   2011 H HG11 B VAL   A 1 100 ? 16.613 -3.357  -13.208 0.38 18.88 ?  100 VAL   A HG11 1 
ATOM   2012 H HG12 A VAL   A 1 100 ? 17.166 -2.159  -13.492 0.62 22.76 ?  100 VAL   A HG12 1 
ATOM   2013 H HG12 B VAL   A 1 100 ? 17.065 -1.886  -13.599 0.38 18.88 ?  100 VAL   A HG12 1 
ATOM   2014 H HG13 A VAL   A 1 100 ? 18.083 -3.400  -13.873 0.62 22.76 ?  100 VAL   A HG13 1 
ATOM   2015 H HG13 B VAL   A 1 100 ? 18.000 -3.124  -13.946 0.38 18.88 ?  100 VAL   A HG13 1 
ATOM   2016 H HG21 A VAL   A 1 100 ? 17.542 -4.683  -11.153 0.62 23.07 ?  100 VAL   A HG21 1 
ATOM   2017 H HG21 B VAL   A 1 100 ? 17.422 -4.456  -11.313 0.38 19.47 ?  100 VAL   A HG21 1 
ATOM   2018 H HG22 A VAL   A 1 100 ? 19.000 -4.788  -11.776 0.62 23.07 ?  100 VAL   A HG22 1 
ATOM   2019 H HG22 B VAL   A 1 100 ? 18.925 -4.473  -11.825 0.38 19.47 ?  100 VAL   A HG22 1 
ATOM   2020 H HG23 A VAL   A 1 100 ? 18.793 -4.125  -10.348 0.62 23.07 ?  100 VAL   A HG23 1 
ATOM   2021 H HG23 B VAL   A 1 100 ? 18.577 -3.858  -10.402 0.38 19.47 ?  100 VAL   A HG23 1 
ATOM   2022 N N    A ASN   A 1 101 ? 19.303 0.198   -12.237 0.62 17.99 ?  101 ASN   A N    1 
ATOM   2023 N N    B ASN   A 1 101 ? 19.128 0.529   -12.046 0.38 11.50 ?  101 ASN   A N    1 
ATOM   2024 C CA   A ASN   A 1 101 ? 19.251 1.483   -12.926 0.62 19.36 ?  101 ASN   A CA   1 
ATOM   2025 C CA   B ASN   A 1 101 ? 19.011 1.846   -12.662 0.38 11.78 ?  101 ASN   A CA   1 
ATOM   2026 C C    A ASN   A 1 101 ? 20.612 1.927   -13.461 0.62 21.21 ?  101 ASN   A C    1 
ATOM   2027 C C    B ASN   A 1 101 ? 20.339 2.364   -13.201 0.38 12.89 ?  101 ASN   A C    1 
ATOM   2028 O O    A ASN   A 1 101 ? 20.685 2.952   -14.152 0.62 22.66 ?  101 ASN   A O    1 
ATOM   2029 O O    B ASN   A 1 101 ? 20.341 3.358   -13.938 0.38 14.72 ?  101 ASN   A O    1 
ATOM   2030 C CB   A ASN   A 1 101 ? 18.622 2.530   -12.002 0.62 18.80 ?  101 ASN   A CB   1 
ATOM   2031 C CB   B ASN   A 1 101 ? 18.353 2.824   -11.684 0.38 12.26 ?  101 ASN   A CB   1 
ATOM   2032 C CG   A ASN   A 1 101 ? 17.254 2.098   -11.494 0.62 18.36 ?  101 ASN   A CG   1 
ATOM   2033 C CG   B ASN   A 1 101 ? 16.934 2.410   -11.340 0.38 13.13 ?  101 ASN   A CG   1 
ATOM   2034 O OD1  A ASN   A 1 101 ? 16.437 1.575   -12.255 0.62 18.53 ?  101 ASN   A OD1  1 
ATOM   2035 O OD1  B ASN   A 1 101 ? 16.193 1.955   -12.213 0.38 14.17 ?  101 ASN   A OD1  1 
ATOM   2036 N ND2  A ASN   A 1 101 ? 17.008 2.293   -10.203 0.62 18.02 ?  101 ASN   A ND2  1 
ATOM   2037 N ND2  B ASN   A 1 101 ? 16.553 2.544   -10.071 0.38 12.84 ?  101 ASN   A ND2  1 
ATOM   2038 H H    A ASN   A 1 101 ? 19.189 0.251   -11.384 0.62 21.60 ?  101 ASN   A H    1 
ATOM   2039 H H    B ASN   A 1 101 ? 19.071 0.535   -11.181 0.38 13.82 ?  101 ASN   A H    1 
ATOM   2040 H HA   A ASN   A 1 101 ? 18.670 1.396   -13.690 0.62 23.24 ?  101 ASN   A HA   1 
ATOM   2041 H HA   B ASN   A 1 101 ? 18.411 1.774   -13.413 0.38 14.16 ?  101 ASN   A HA   1 
ATOM   2042 H HB2  A ASN   A 1 101 ? 19.193 2.676   -11.233 0.62 22.57 ?  101 ASN   A HB2  1 
ATOM   2043 H HB2  B ASN   A 1 101 ? 18.859 2.864   -10.858 0.38 14.72 ?  101 ASN   A HB2  1 
ATOM   2044 H HB3  A ASN   A 1 101 ? 18.510 3.365   -12.493 0.62 22.57 ?  101 ASN   A HB3  1 
ATOM   2045 H HB3  B ASN   A 1 101 ? 18.317 3.715   -12.087 0.38 14.72 ?  101 ASN   A HB3  1 
ATOM   2046 H HD21 A ASN   A 1 101 ? 16.247 2.066   -9.868  0.62 21.64 ?  101 ASN   A HD21 1 
ATOM   2047 H HD21 B ASN   A 1 101 ? 15.752 2.326   -9.828  0.38 15.43 ?  101 ASN   A HD21 1 
ATOM   2048 H HD22 A ASN   A 1 101 ? 17.606 2.651   -9.699  0.62 21.64 ?  101 ASN   A HD22 1 
ATOM   2049 H HD22 B ASN   A 1 101 ? 17.100 2.862   -9.486  0.38 15.43 ?  101 ASN   A HD22 1 
ATOM   2050 N N    A LYS   A 1 102 ? 21.677 1.172   -13.182 0.62 22.73 ?  102 LYS   A N    1 
ATOM   2051 N N    B LYS   A 1 102 ? 21.454 1.711   -12.856 0.38 13.17 ?  102 LYS   A N    1 
ATOM   2052 C CA   A LYS   A 1 102 ? 22.975 1.361   -13.816 0.62 23.80 ?  102 LYS   A CA   1 
ATOM   2053 C CA   B LYS   A 1 102 ? 22.753 1.939   -13.476 0.38 14.75 ?  102 LYS   A CA   1 
ATOM   2054 C C    A LYS   A 1 102 ? 23.301 0.240   -14.795 0.62 23.87 ?  102 LYS   A C    1 
ATOM   2055 C C    B LYS   A 1 102 ? 23.077 0.912   -14.553 0.38 15.54 ?  102 LYS   A C    1 
ATOM   2056 O O    A LYS   A 1 102 ? 24.423 0.191   -15.308 0.62 24.23 ?  102 LYS   A O    1 
ATOM   2057 O O    B LYS   A 1 102 ? 24.099 1.057   -15.235 0.38 15.99 ?  102 LYS   A O    1 
ATOM   2058 C CB   A LYS   A 1 102 ? 24.086 1.426   -12.760 0.62 25.04 ?  102 LYS   A CB   1 
ATOM   2059 C CB   B LYS   A 1 102 ? 23.862 1.903   -12.412 0.38 15.58 ?  102 LYS   A CB   1 
ATOM   2060 C CG   A LYS   A 1 102 ? 23.959 2.559   -11.758 0.62 25.80 ?  102 LYS   A CG   1 
ATOM   2061 C CG   B LYS   A 1 102 ? 23.770 2.995   -11.361 0.38 16.23 ?  102 LYS   A CG   1 
ATOM   2062 C CD   A LYS   A 1 102 ? 25.119 2.531   -10.771 0.62 26.80 ?  102 LYS   A CD   1 
ATOM   2063 C CD   B LYS   A 1 102 ? 24.855 2.840   -10.300 0.38 17.14 ?  102 LYS   A CD   1 
ATOM   2064 C CE   A LYS   A 1 102 ? 25.025 3.650   -9.746  0.62 27.64 ?  102 LYS   A CE   1 
ATOM   2065 C CE   B LYS   A 1 102 ? 24.769 3.940   -9.252  0.38 17.76 ?  102 LYS   A CE   1 
ATOM   2066 N NZ   A LYS   A 1 102 ? 26.131 3.561   -8.746  0.62 28.03 ?  102 LYS   A NZ   1 
ATOM   2067 N NZ   B LYS   A 1 102 ? 25.754 3.747   -8.149  0.38 17.97 ?  102 LYS   A NZ   1 
ATOM   2068 H H    A LYS   A 1 102 ? 21.666 0.517   -12.625 0.62 27.29 ?  102 LYS   A H    1 
ATOM   2069 H H    B LYS   A 1 102 ? 21.475 1.110   -12.241 0.38 15.81 ?  102 LYS   A H    1 
ATOM   2070 H HA   A LYS   A 1 102 ? 22.971 2.210   -14.290 0.62 28.57 ?  102 LYS   A HA   1 
ATOM   2071 H HA   B LYS   A 1 102 ? 22.765 2.806   -13.891 0.38 17.72 ?  102 LYS   A HA   1 
ATOM   2072 H HB2  A LYS   A 1 102 ? 24.087 0.594   -12.263 0.62 30.06 ?  102 LYS   A HB2  1 
ATOM   2073 H HB2  B LYS   A 1 102 ? 23.824 1.052   -11.950 0.38 18.71 ?  102 LYS   A HB2  1 
ATOM   2074 H HB3  A LYS   A 1 102 ? 24.937 1.532   -13.216 0.62 30.06 ?  102 LYS   A HB3  1 
ATOM   2075 H HB3  B LYS   A 1 102 ? 24.717 1.998   -12.856 0.38 18.71 ?  102 LYS   A HB3  1 
ATOM   2076 H HG2  A LYS   A 1 102 ? 23.975 3.408   -12.227 0.62 30.97 ?  102 LYS   A HG2  1 
ATOM   2077 H HG2  B LYS   A 1 102 ? 23.885 3.859   -11.788 0.38 19.49 ?  102 LYS   A HG2  1 
ATOM   2078 H HG3  A LYS   A 1 102 ? 23.131 2.460   -11.263 0.62 30.97 ?  102 LYS   A HG3  1 
ATOM   2079 H HG3  B LYS   A 1 102 ? 22.906 2.948   -10.924 0.38 19.49 ?  102 LYS   A HG3  1 
ATOM   2080 H HD2  A LYS   A 1 102 ? 25.112 1.685   -10.296 0.62 32.18 ?  102 LYS   A HD2  1 
ATOM   2081 H HD2  B LYS   A 1 102 ? 24.746 1.984   -9.854  0.38 20.58 ?  102 LYS   A HD2  1 
ATOM   2082 H HD3  A LYS   A 1 102 ? 25.953 2.635   -11.256 0.62 32.18 ?  102 LYS   A HD3  1 
ATOM   2083 H HD3  B LYS   A 1 102 ? 25.727 2.888   -10.723 0.38 20.58 ?  102 LYS   A HD3  1 
ATOM   2084 H HE2  A LYS   A 1 102 ? 25.091 4.507   -10.199 0.62 33.18 ?  102 LYS   A HE2  1 
ATOM   2085 H HE2  B LYS   A 1 102 ? 24.951 4.794   -9.673  0.38 21.33 ?  102 LYS   A HE2  1 
ATOM   2086 H HE3  A LYS   A 1 102 ? 24.179 3.584   -9.275  0.62 33.18 ?  102 LYS   A HE3  1 
ATOM   2087 H HE3  B LYS   A 1 102 ? 23.878 3.942   -8.866  0.38 21.33 ?  102 LYS   A HE3  1 
ATOM   2088 H HZ1  A LYS   A 1 102 ? 26.061 4.221   -8.155  0.62 33.66 ?  102 LYS   A HZ1  1 
ATOM   2089 H HZ1  B LYS   A 1 102 ? 25.677 4.404   -7.554  0.38 21.58 ?  102 LYS   A HZ1  1 
ATOM   2090 H HZ2  A LYS   A 1 102 ? 26.089 2.782   -8.316  0.62 33.66 ?  102 LYS   A HZ2  1 
ATOM   2091 H HZ2  B LYS   A 1 102 ? 25.603 2.969   -7.740  0.38 21.58 ?  102 LYS   A HZ2  1 
ATOM   2092 H HZ3  A LYS   A 1 102 ? 26.918 3.621   -9.157  0.62 33.66 ?  102 LYS   A HZ3  1 
ATOM   2093 H HZ3  B LYS   A 1 102 ? 26.581 3.746   -8.476  0.38 21.58 ?  102 LYS   A HZ3  1 
ATOM   2094 N N    A GLY   A 1 103 ? 22.371 -0.682  -15.031 0.62 24.35 ?  103 GLY   A N    1 
ATOM   2095 N N    B GLY   A 1 103 ? 22.245 -0.116  -14.712 0.38 16.77 ?  103 GLY   A N    1 
ATOM   2096 C CA   A GLY   A 1 103 ? 22.588 -1.764  -15.973 0.62 23.99 ?  103 GLY   A CA   1 
ATOM   2097 C CA   B GLY   A 1 103 ? 22.517 -1.165  -15.673 0.38 17.99 ?  103 GLY   A CA   1 
ATOM   2098 C C    A GLY   A 1 103 ? 23.384 -2.937  -15.444 0.62 23.63 ?  103 GLY   A C    1 
ATOM   2099 C C    B GLY   A 1 103 ? 23.449 -2.241  -15.173 0.38 19.09 ?  103 GLY   A C    1 
ATOM   2100 O O    A GLY   A 1 103 ? 23.860 -3.755  -16.236 0.62 24.36 ?  103 GLY   A O    1 
ATOM   2101 O O    B GLY   A 1 103 ? 24.175 -2.839  -15.976 0.38 19.83 ?  103 GLY   A O    1 
ATOM   2102 H H    A GLY   A 1 103 ? 21.605 -0.702  -14.646 0.62 29.24 ?  103 GLY   A H    1 
ATOM   2103 H H    B GLY   A 1 103 ? 21.517 -0.239  -14.260 0.38 20.13 ?  103 GLY   A H    1 
ATOM   2104 H HA2  A GLY   A 1 103 ? 21.728 -2.102  -16.264 0.62 28.80 ?  103 GLY   A HA2  1 
ATOM   2105 H HA2  B GLY   A 1 103 ? 21.676 -1.573  -15.948 0.38 21.60 ?  103 GLY   A HA2  1 
ATOM   2106 H HA3  A GLY   A 1 103 ? 23.047 -1.409  -16.753 0.62 28.80 ?  103 GLY   A HA3  1 
ATOM   2107 H HA3  B GLY   A 1 103 ? 22.938 -0.785  -16.449 0.38 21.60 ?  103 GLY   A HA3  1 
ATOM   2108 N N    A GLU   A 1 104 ? 23.525 -3.063  -14.129 0.62 22.16 ?  104 GLU   A N    1 
ATOM   2109 N N    B GLU   A 1 104 ? 23.458 -2.506  -13.868 0.38 19.40 ?  104 GLU   A N    1 
ATOM   2110 C CA   A GLU   A 1 104 ? 24.419 -4.058  -13.553 0.62 20.84 ?  104 GLU   A CA   1 
ATOM   2111 C CA   B GLU   A 1 104 ? 24.338 -3.510  -13.289 0.38 19.99 ?  104 GLU   A CA   1 
ATOM   2112 C C    A GLU   A 1 104 ? 23.733 -5.419  -13.434 0.62 20.97 ?  104 GLU   A C    1 
ATOM   2113 C C    B GLU   A 1 104 ? 23.652 -4.871  -13.238 0.38 21.57 ?  104 GLU   A C    1 
ATOM   2114 O O    A GLU   A 1 104 ? 22.508 -5.521  -13.328 0.62 21.79 ?  104 GLU   A O    1 
ATOM   2115 O O    B GLU   A 1 104 ? 22.446 -4.969  -12.988 0.38 22.03 ?  104 GLU   A O    1 
ATOM   2116 C CB   A GLU   A 1 104 ? 24.945 -3.563  -12.203 0.62 19.51 ?  104 GLU   A CB   1 
ATOM   2117 C CB   B GLU   A 1 104 ? 24.816 -3.063  -11.904 0.38 18.97 ?  104 GLU   A CB   1 
ATOM   2118 C CG   A GLU   A 1 104 ? 25.708 -2.242  -12.347 0.62 18.97 ?  104 GLU   A CG   1 
ATOM   2119 C CG   B GLU   A 1 104 ? 25.882 -1.971  -11.989 0.38 18.38 ?  104 GLU   A CG   1 
ATOM   2120 C CD   A GLU   A 1 104 ? 26.149 -1.600  -11.041 0.62 17.71 ?  104 GLU   A CD   1 
ATOM   2121 C CD   B GLU   A 1 104 ? 26.060 -1.197  -10.701 0.38 17.49 ?  104 GLU   A CD   1 
ATOM   2122 O OE1  A GLU   A 1 104 ? 25.581 -1.913  -9.972  0.62 16.92 ?  104 GLU   A OE1  1 
ATOM   2123 O OE1  B GLU   A 1 104 ? 25.480 -1.600  -9.671  0.38 15.81 ?  104 GLU   A OE1  1 
ATOM   2124 O OE2  A GLU   A 1 104 ? 27.070 -0.750  -11.107 0.62 17.74 -1 104 GLU   A OE2  1 
ATOM   2125 O OE2  B GLU   A 1 104 ? 26.779 -0.175  -10.725 0.38 18.46 -1 104 GLU   A OE2  1 
ATOM   2126 H H    A GLU   A 1 104 ? 23.107 -2.583  -13.552 0.62 26.60 ?  104 GLU   A H    1 
ATOM   2127 H H    B GLU   A 1 104 ? 22.957 -2.115  -13.284 0.38 23.30 ?  104 GLU   A H    1 
ATOM   2128 H HA   A GLU   A 1 104 ? 25.179 -4.162  -14.147 0.62 25.02 ?  104 GLU   A HA   1 
ATOM   2129 H HA   B GLU   A 1 104 ? 25.115 -3.606  -13.849 0.38 24.01 ?  104 GLU   A HA   1 
ATOM   2130 H HB2  A GLU   A 1 104 ? 24.197 -3.422  -11.606 0.62 23.43 ?  104 GLU   A HB2  1 
ATOM   2131 H HB2  B GLU   A 1 104 ? 24.063 -2.709  -11.402 0.38 22.78 ?  104 GLU   A HB2  1 
ATOM   2132 H HB3  A GLU   A 1 104 ? 25.549 -4.228  -11.842 0.62 23.43 ?  104 GLU   A HB3  1 
ATOM   2133 H HB3  B GLU   A 1 104 ? 25.200 -3.820  -11.431 0.38 22.78 ?  104 GLU   A HB3  1 
ATOM   2134 H HG2  A GLU   A 1 104 ? 26.504 -2.406  -12.874 0.62 22.78 ?  104 GLU   A HG2  1 
ATOM   2135 H HG2  B GLU   A 1 104 ? 26.736 -2.379  -12.206 0.38 22.08 ?  104 GLU   A HG2  1 
ATOM   2136 H HG3  A GLU   A 1 104 ? 25.136 -1.606  -12.805 0.62 22.78 ?  104 GLU   A HG3  1 
ATOM   2137 H HG3  B GLU   A 1 104 ? 25.634 -1.343  -12.687 0.38 22.08 ?  104 GLU   A HG3  1 
ATOM   2138 N N    A ASP   A 1 105 ? 24.550 -6.470  -13.451 0.62 21.64 ?  105 ASP   A N    1 
ATOM   2139 N N    B ASP   A 1 105 ? 24.437 -5.920  -13.494 0.38 22.49 ?  105 ASP   A N    1 
ATOM   2140 C CA   A ASP   A 1 105 ? 24.056 -7.838  -13.577 0.62 23.03 ?  105 ASP   A CA   1 
ATOM   2141 C CA   B ASP   A 1 105 ? 23.909 -7.269  -13.660 0.38 23.54 ?  105 ASP   A CA   1 
ATOM   2142 C C    A ASP   A 1 105 ? 23.360 -8.277  -12.293 0.62 20.83 ?  105 ASP   A C    1 
ATOM   2143 C C    B ASP   A 1 105 ? 23.266 -7.768  -12.372 0.38 22.63 ?  105 ASP   A C    1 
ATOM   2144 O O    A ASP   A 1 105 ? 23.993 -8.369  -11.238 0.62 18.68 ?  105 ASP   A O    1 
ATOM   2145 O O    B ASP   A 1 105 ? 23.909 -7.807  -11.320 0.38 22.02 ?  105 ASP   A O    1 
ATOM   2146 C CB   A ASP   A 1 105 ? 25.233 -8.760  -13.888 0.62 26.31 ?  105 ASP   A CB   1 
ATOM   2147 C CB   B ASP   A 1 105 ? 25.044 -8.201  -14.088 0.38 25.33 ?  105 ASP   A CB   1 
ATOM   2148 C CG   A ASP   A 1 105 ? 24.804 -10.174 -14.217 0.62 29.20 ?  105 ASP   A CG   1 
ATOM   2149 C CG   B ASP   A 1 105 ? 24.715 -9.658  -13.861 0.38 26.75 ?  105 ASP   A CG   1 
ATOM   2150 O OD1  A ASP   A 1 105 ? 23.585 -10.422 -14.299 0.62 30.18 ?  105 ASP   A OD1  1 
ATOM   2151 O OD1  B ASP   A 1 105 ? 23.604 -10.079 -14.242 0.38 27.08 ?  105 ASP   A OD1  1 
ATOM   2152 O OD2  A ASP   A 1 105 ? 25.692 -11.036 -14.399 0.62 30.48 -1 105 ASP   A OD2  1 
ATOM   2153 O OD2  B ASP   A 1 105 ? 25.568 -10.385 -13.311 0.38 27.53 -1 105 ASP   A OD2  1 
ATOM   2154 H H    A ASP   A 1 105 ? 25.407 -6.410  -13.388 0.62 25.98 ?  105 ASP   A H    1 
ATOM   2155 H H    B ASP   A 1 105 ? 25.292 -5.880  -13.578 0.38 27.00 ?  105 ASP   A H    1 
ATOM   2156 H HA   A ASP   A 1 105 ? 23.420 -7.885  -14.304 0.62 27.65 ?  105 ASP   A HA   1 
ATOM   2157 H HA   B ASP   A 1 105 ? 23.239 -7.282  -14.354 0.38 28.26 ?  105 ASP   A HA   1 
ATOM   2158 H HB2  A ASP   A 1 105 ? 25.713 -8.409  -14.654 0.62 31.58 ?  105 ASP   A HB2  1 
ATOM   2159 H HB2  B ASP   A 1 105 ? 25.210 -8.094  -15.040 0.38 30.41 ?  105 ASP   A HB2  1 
ATOM   2160 H HB3  A ASP   A 1 105 ? 25.819 -8.793  -13.116 0.62 31.58 ?  105 ASP   A HB3  1 
ATOM   2161 H HB3  B ASP   A 1 105 ? 25.852 -7.983  -13.591 0.38 30.41 ?  105 ASP   A HB3  1 
ATOM   2162 N N    A ILE   A 1 106 ? 22.061 -8.571  -12.387 0.62 21.26 ?  106 ILE   A N    1 
ATOM   2163 N N    B ILE   A 1 106 ? 21.999 -8.180  -12.469 0.38 22.69 ?  106 ILE   A N    1 
ATOM   2164 C CA   A ILE   A 1 106 ? 21.299 -9.007  -11.223 0.62 20.87 ?  106 ILE   A CA   1 
ATOM   2165 C CA   B ILE   A 1 106 ? 21.254 -8.607  -11.291 0.38 22.14 ?  106 ILE   A CA   1 
ATOM   2166 C C    A ILE   A 1 106 ? 21.845 -10.304 -10.649 0.62 20.35 ?  106 ILE   A C    1 
ATOM   2167 C C    B ILE   A 1 106 ? 21.759 -9.930  -10.729 0.38 21.11 ?  106 ILE   A C    1 
ATOM   2168 O O    A ILE   A 1 106 ? 21.657 -10.574 -9.460  0.62 19.78 ?  106 ILE   A O    1 
ATOM   2169 O O    B ILE   A 1 106 ? 21.503 -10.234 -9.559  0.38 20.02 ?  106 ILE   A O    1 
ATOM   2170 C CB   A ILE   A 1 106 ? 19.792 -9.100  -11.558 0.62 22.34 ?  106 ILE   A CB   1 
ATOM   2171 C CB   B ILE   A 1 106 ? 19.739 -8.656  -11.588 0.38 22.98 ?  106 ILE   A CB   1 
ATOM   2172 C CG1  A ILE   A 1 106 ? 18.956 -9.200  -10.280 0.62 22.96 ?  106 ILE   A CG1  1 
ATOM   2173 C CG1  B ILE   A 1 106 ? 18.931 -8.742  -10.290 0.38 23.42 ?  106 ILE   A CG1  1 
ATOM   2174 C CG2  A ILE   A 1 106 ? 19.510 -10.295 -12.446 0.62 23.20 ?  106 ILE   A CG2  1 
ATOM   2175 C CG2  B ILE   A 1 106 ? 19.407 -9.848  -12.474 0.38 23.49 ?  106 ILE   A CG2  1 
ATOM   2176 C CD1  A ILE   A 1 106 ? 19.008 -7.962  -9.415  0.62 23.20 ?  106 ILE   A CD1  1 
ATOM   2177 C CD1  B ILE   A 1 106 ? 19.351 -7.737  -9.240  0.38 23.70 ?  106 ILE   A CD1  1 
ATOM   2178 H H    A ILE   A 1 106 ? 21.606 -8.514  -13.108 0.62 25.52 ?  106 ILE   A H    1 
ATOM   2179 H H    B ILE   A 1 106 ? 21.551 -8.215  -13.200 0.38 27.24 ?  106 ILE   A H    1 
ATOM   2180 H HA   A ILE   A 1 106 ? 21.403 -8.342  -10.531 0.62 25.06 ?  106 ILE   A HA   1 
ATOM   2181 H HA   B ILE   A 1 106 ? 21.406 -7.943  -10.612 0.38 26.58 ?  106 ILE   A HA   1 
ATOM   2182 H HB   A ILE   A 1 106 ? 19.535 -8.293  -12.031 0.62 26.83 ?  106 ILE   A HB   1 
ATOM   2183 H HB   B ILE   A 1 106 ? 19.488 -7.846  -12.057 0.38 27.59 ?  106 ILE   A HB   1 
ATOM   2184 H HG12 A ILE   A 1 106 ? 18.029 -9.346  -10.523 0.62 27.57 ?  106 ILE   A HG12 1 
ATOM   2185 H HG12 B ILE   A 1 106 ? 17.994 -8.581  -10.494 0.38 28.13 ?  106 ILE   A HG12 1 
ATOM   2186 H HG13 A ILE   A 1 106 ? 19.277 -9.944  -9.748  0.62 27.57 ?  106 ILE   A HG13 1 
ATOM   2187 H HG13 B ILE   A 1 106 ? 19.035 -9.629  -9.912  0.38 28.13 ?  106 ILE   A HG13 1 
ATOM   2188 H HG21 A ILE   A 1 106 ? 18.624 -10.196 -12.827 0.62 27.85 ?  106 ILE   A HG21 1 
ATOM   2189 H HG21 B ILE   A 1 106 ? 18.510 -9.740  -12.827 0.38 28.20 ?  106 ILE   A HG21 1 
ATOM   2190 H HG22 A ILE   A 1 106 ? 20.175 -10.322 -13.148 0.62 27.85 ?  106 ILE   A HG22 1 
ATOM   2191 H HG22 B ILE   A 1 106 ? 20.047 -9.886  -13.202 0.38 28.20 ?  106 ILE   A HG22 1 
ATOM   2192 H HG23 A ILE   A 1 106 ? 19.555 -11.101 -11.911 0.62 27.85 ?  106 ILE   A HG23 1 
ATOM   2193 H HG23 B ILE   A 1 106 ? 19.458 -10.662 -11.947 0.38 28.20 ?  106 ILE   A HG23 1 
ATOM   2194 H HD11 A ILE   A 1 106 ? 18.298 -8.006  -8.758  0.62 27.86 ?  106 ILE   A HD11 1 
ATOM   2195 H HD11 B ILE   A 1 106 ? 18.630 -7.624  -8.608  0.38 28.46 ?  106 ILE   A HD11 1 
ATOM   2196 H HD12 A ILE   A 1 106 ? 19.869 -7.922  -8.967  0.62 27.86 ?  106 ILE   A HD12 1 
ATOM   2197 H HD12 B ILE   A 1 106 ? 20.142 -8.071  -8.786  0.38 28.46 ?  106 ILE   A HD12 1 
ATOM   2198 H HD13 A ILE   A 1 106 ? 18.892 -7.179  -9.977  0.62 27.86 ?  106 ILE   A HD13 1 
ATOM   2199 H HD13 B ILE   A 1 106 ? 19.550 -6.893  -9.676  0.38 28.46 ?  106 ILE   A HD13 1 
ATOM   2200 N N    A GLN   A 1 107 ? 22.532 -11.114 -11.465 0.62 20.88 ?  107 GLN   A N    1 
ATOM   2201 N N    B GLN   A 1 107 ? 22.476 -10.729 -11.525 0.38 21.72 ?  107 GLN   A N    1 
ATOM   2202 C CA   A GLN   A 1 107 ? 23.181 -12.315 -10.953 0.62 22.88 ?  107 GLN   A CA   1 
ATOM   2203 C CA   B GLN   A 1 107 ? 22.978 -12.007 -11.028 0.38 22.46 ?  107 GLN   A CA   1 
ATOM   2204 C C    A GLN   A 1 107 ? 24.171 -11.990 -9.845  0.62 20.87 ?  107 GLN   A C    1 
ATOM   2205 C C    B GLN   A 1 107 ? 23.996 -11.831 -9.912  0.38 20.52 ?  107 GLN   A C    1 
ATOM   2206 O O    A GLN   A 1 107 ? 24.474 -12.857 -9.019  0.62 23.03 ?  107 GLN   A O    1 
ATOM   2207 O O    B GLN   A 1 107 ? 24.196 -12.760 -9.123  0.38 21.78 ?  107 GLN   A O    1 
ATOM   2208 C CB   A GLN   A 1 107 ? 23.887 -13.055 -12.097 0.62 26.81 ?  107 GLN   A CB   1 
ATOM   2209 C CB   B GLN   A 1 107 ? 23.590 -12.832 -12.165 0.38 25.48 ?  107 GLN   A CB   1 
ATOM   2210 C CG   A GLN   A 1 107 ? 22.993 -13.330 -13.302 0.62 30.95 ?  107 GLN   A CG   1 
ATOM   2211 C CG   B GLN   A 1 107 ? 22.637 -13.111 -13.316 0.38 28.50 ?  107 GLN   A CG   1 
ATOM   2212 C CD   A GLN   A 1 107 ? 21.766 -14.142 -12.944 0.62 34.38 ?  107 GLN   A CD   1 
ATOM   2213 C CD   B GLN   A 1 107 ? 21.325 -13.718 -12.861 0.38 30.90 ?  107 GLN   A CD   1 
ATOM   2214 O OE1  A GLN   A 1 107 ? 21.868 -15.201 -12.323 0.62 35.53 ?  107 GLN   A OE1  1 
ATOM   2215 O OE1  B GLN   A 1 107 ? 21.295 -14.565 -11.967 0.38 31.94 ?  107 GLN   A OE1  1 
ATOM   2216 N NE2  A GLN   A 1 107 ? 20.593 -13.646 -13.328 0.62 35.48 ?  107 GLN   A NE2  1 
ATOM   2217 N NE2  B GLN   A 1 107 ? 20.230 -13.282 -13.471 0.38 31.59 ?  107 GLN   A NE2  1 
ATOM   2218 H H    A GLN   A 1 107 ? 22.633 -10.990 -12.309 0.62 25.07 ?  107 GLN   A H    1 
ATOM   2219 H H    B GLN   A 1 107 ? 22.680 -10.560 -12.338 0.38 26.08 ?  107 GLN   A H    1 
ATOM   2220 H HA   A GLN   A 1 107 ? 22.513 -12.916 -10.589 0.62 27.48 ?  107 GLN   A HA   1 
ATOM   2221 H HA   B GLN   A 1 107 ? 22.242 -12.515 -10.659 0.38 26.97 ?  107 GLN   A HA   1 
ATOM   2222 H HB2  A GLN   A 1 107 ? 24.636 -12.523 -12.405 0.62 32.19 ?  107 GLN   A HB2  1 
ATOM   2223 H HB2  B GLN   A 1 107 ? 24.353 -12.355 -12.525 0.38 30.59 ?  107 GLN   A HB2  1 
ATOM   2224 H HB3  A GLN   A 1 107 ? 24.207 -13.914 -11.773 0.62 32.19 ?  107 GLN   A HB3  1 
ATOM   2225 H HB3  B GLN   A 1 107 ? 23.880 -13.690 -11.810 0.38 30.59 ?  107 GLN   A HB3  1 
ATOM   2226 H HG2  A GLN   A 1 107 ? 22.695 -12.487 -13.679 0.62 37.16 ?  107 GLN   A HG2  1 
ATOM   2227 H HG2  B GLN   A 1 107 ? 22.440 -12.280 -13.770 0.38 34.21 ?  107 GLN   A HG2  1 
ATOM   2228 H HG3  A GLN   A 1 107 ? 23.497 -13.827 -13.964 0.62 37.16 ?  107 GLN   A HG3  1 
ATOM   2229 H HG3  B GLN   A 1 107 ? 23.058 -13.734 -13.930 0.38 34.21 ?  107 GLN   A HG3  1 
ATOM   2230 H HE21 A GLN   A 1 107 ? 20.560 -12.902 -13.759 0.62 42.59 ?  107 GLN   A HE21 1 
ATOM   2231 H HE21 B GLN   A 1 107 ? 20.292 -12.689 -14.090 0.38 37.93 ?  107 GLN   A HE21 1 
ATOM   2232 H HE22 A GLN   A 1 107 ? 19.867 -14.069 -13.146 0.62 42.59 ?  107 GLN   A HE22 1 
ATOM   2233 H HE22 B GLN   A 1 107 ? 19.460 -13.595 -13.250 0.38 37.93 ?  107 GLN   A HE22 1 
ATOM   2234 N N    A LEU   A 1 108 ? 24.667 -10.751 -9.796  0.62 16.94 ?  108 LEU   A N    1 
ATOM   2235 N N    B LEU   A 1 108 ? 24.633 -10.663 -9.814  0.38 17.30 ?  108 LEU   A N    1 
ATOM   2236 C CA   A LEU   A 1 108 ? 25.580 -10.335 -8.743  0.62 14.67 ?  108 LEU   A CA   1 
ATOM   2237 C CA   B LEU   A 1 108 ? 25.577 -10.417 -8.731  0.38 14.89 ?  108 LEU   A CA   1 
ATOM   2238 C C    A LEU   A 1 108 ? 24.892 -10.209 -7.391  0.62 12.79 ?  108 LEU   A C    1 
ATOM   2239 C C    B LEU   A 1 108 ? 24.892 -10.227 -7.389  0.38 13.11 ?  108 LEU   A C    1 
ATOM   2240 O O    A LEU   A 1 108 ? 25.579 -10.079 -6.376  0.62 12.85 ?  108 LEU   A O    1 
ATOM   2241 O O    B LEU   A 1 108 ? 25.582 -10.046 -6.383  0.38 13.16 ?  108 LEU   A O    1 
ATOM   2242 C CB   A LEU   A 1 108 ? 26.255 -9.016  -9.134  0.62 14.36 ?  108 LEU   A CB   1 
ATOM   2243 C CB   B LEU   A 1 108 ? 26.454 -9.205  -9.051  0.38 14.37 ?  108 LEU   A CB   1 
ATOM   2244 C CG   A LEU   A 1 108 ? 27.218 -9.136  -10.318 0.62 15.55 ?  108 LEU   A CG   1 
ATOM   2245 C CG   B LEU   A 1 108 ? 27.480 -9.449  -10.159 0.38 14.68 ?  108 LEU   A CG   1 
ATOM   2246 C CD1  A LEU   A 1 108 ? 27.585 -7.765  -10.871 0.62 15.41 ?  108 LEU   A CD1  1 
ATOM   2247 C CD1  B LEU   A 1 108 ? 28.152 -8.145  -10.569 0.38 14.40 ?  108 LEU   A CD1  1 
ATOM   2248 C CD2  A LEU   A 1 108 ? 28.473 -9.894  -9.905  0.62 16.76 ?  108 LEU   A CD2  1 
ATOM   2249 C CD2  B LEU   A 1 108 ? 28.518 -10.470 -9.716  0.38 15.52 ?  108 LEU   A CD2  1 
ATOM   2250 H H    A LEU   A 1 108 ? 24.489 -10.143 -10.369 0.62 20.34 ?  108 LEU   A H    1 
ATOM   2251 H H    B LEU   A 1 108 ? 24.539 -10.008 -10.359 0.38 20.78 ?  108 LEU   A H    1 
ATOM   2252 H HA   A LEU   A 1 108 ? 26.275 -11.003 -8.650  0.62 17.62 ?  108 LEU   A HA   1 
ATOM   2253 H HA   B LEU   A 1 108 ? 26.159 -11.187 -8.647  0.38 17.88 ?  108 LEU   A HA   1 
ATOM   2254 H HB2  A LEU   A 1 108 ? 25.570 -8.372  -9.378  0.62 17.25 ?  108 LEU   A HB2  1 
ATOM   2255 H HB2  B LEU   A 1 108 ? 25.886 -8.473  -9.333  0.38 17.26 ?  108 LEU   A HB2  1 
ATOM   2256 H HB3  A LEU   A 1 108 ? 26.760 -8.686  -8.377  0.62 17.25 ?  108 LEU   A HB3  1 
ATOM   2257 H HB3  B LEU   A 1 108 ? 26.941 -8.952  -8.250  0.38 17.26 ?  108 LEU   A HB3  1 
ATOM   2258 H HG   A LEU   A 1 108 ? 26.789 -9.639  -11.029 0.62 18.68 ?  108 LEU   A HG   1 
ATOM   2259 H HG   B LEU   A 1 108 ? 27.024 -9.808  -10.936 0.38 17.63 ?  108 LEU   A HG   1 
ATOM   2260 H HD11 A LEU   A 1 108 ? 28.137 -7.879  -11.663 0.62 18.51 ?  108 LEU   A HD11 1 
ATOM   2261 H HD11 B LEU   A 1 108 ? 28.792 -8.329  -11.275 0.38 17.29 ?  108 LEU   A HD11 1 
ATOM   2262 H HD12 A LEU   A 1 108 ? 26.772 -7.290  -11.103 0.62 18.51 ?  108 LEU   A HD12 1 
ATOM   2263 H HD12 B LEU   A 1 108 ? 27.474 -7.529  -10.887 0.38 17.29 ?  108 LEU   A HD12 1 
ATOM   2264 H HD13 A LEU   A 1 108 ? 28.076 -7.272  -10.196 0.62 18.51 ?  108 LEU   A HD13 1 
ATOM   2265 H HD13 B LEU   A 1 108 ? 28.607 -7.770  -9.799  0.38 17.29 ?  108 LEU   A HD13 1 
ATOM   2266 H HD21 A LEU   A 1 108 ? 29.121 -9.852  -10.626 0.62 20.12 ?  108 LEU   A HD21 1 
ATOM   2267 H HD21 B LEU   A 1 108 ? 29.263 -10.453 -10.335 0.38 18.64 ?  108 LEU   A HD21 1 
ATOM   2268 H HD22 A LEU   A 1 108 ? 28.841 -9.484  -9.107  0.62 20.12 ?  108 LEU   A HD22 1 
ATOM   2269 H HD22 B LEU   A 1 108 ? 28.823 -10.242 -8.823  0.38 18.64 ?  108 LEU   A HD22 1 
ATOM   2270 H HD23 A LEU   A 1 108 ? 28.241 -10.819 -9.724  0.62 20.12 ?  108 LEU   A HD23 1 
ATOM   2271 H HD23 B LEU   A 1 108 ? 28.112 -11.352 -9.710  0.38 18.64 ?  108 LEU   A HD23 1 
ATOM   2272 N N    . LEU   A 1 109 ? 23.559 -10.268 -7.344  1.00 12.20 ?  109 LEU   A N    1 
ATOM   2273 C CA   . LEU   A 1 109 ? 22.866 -10.146 -6.067  1.00 11.11 ?  109 LEU   A CA   1 
ATOM   2274 C C    . LEU   A 1 109 ? 23.217 -11.295 -5.126  1.00 10.56 ?  109 LEU   A C    1 
ATOM   2275 O O    . LEU   A 1 109 ? 23.355 -11.090 -3.914  1.00 11.12 ?  109 LEU   A O    1 
ATOM   2276 C CB   . LEU   A 1 109 ? 21.357 -10.062 -6.304  1.00 11.70 ?  109 LEU   A CB   1 
ATOM   2277 C CG   . LEU   A 1 109 ? 20.473 -9.786  -5.087  1.00 11.68 ?  109 LEU   A CG   1 
ATOM   2278 C CD1  . LEU   A 1 109 ? 20.932 -8.525  -4.355  1.00 11.92 ?  109 LEU   A CD1  1 
ATOM   2279 C CD2  . LEU   A 1 109 ? 19.012 -9.663  -5.509  1.00 12.52 ?  109 LEU   A CD2  1 
ATOM   2280 H H    A LEU   A 1 109 ? 23.043 -10.385 -8.022  0.62 14.65 ?  109 LEU   A H    1 
ATOM   2281 H H    B LEU   A 1 109 ? 23.042 -10.366 -8.024  0.38 14.65 ?  109 LEU   A H    1 
ATOM   2282 H HA   . LEU   A 1 109 ? 23.147 -9.321  -5.643  1.00 13.34 ?  109 LEU   A HA   1 
ATOM   2283 H HB2  . LEU   A 1 109 ? 21.195 -9.345  -6.941  1.00 14.05 ?  109 LEU   A HB2  1 
ATOM   2284 H HB3  . LEU   A 1 109 ? 21.064 -10.900 -6.686  1.00 14.05 ?  109 LEU   A HB3  1 
ATOM   2285 H HG   . LEU   A 1 109 ? 20.549 -10.529 -4.472  1.00 14.03 ?  109 LEU   A HG   1 
ATOM   2286 H HD11 . LEU   A 1 109 ? 20.263 -8.280  -3.698  1.00 14.32 ?  109 LEU   A HD11 1 
ATOM   2287 H HD12 . LEU   A 1 109 ? 21.779 -8.700  -3.916  1.00 14.32 ?  109 LEU   A HD12 1 
ATOM   2288 H HD13 . LEU   A 1 109 ? 21.037 -7.804  -5.000  1.00 14.32 ?  109 LEU   A HD13 1 
ATOM   2289 H HD21 . LEU   A 1 109 ? 18.491 -9.342  -4.755  1.00 15.03 ?  109 LEU   A HD21 1 
ATOM   2290 H HD22 . LEU   A 1 109 ? 18.943 -9.042  -6.248  1.00 15.03 ?  109 LEU   A HD22 1 
ATOM   2291 H HD23 . LEU   A 1 109 ? 18.688 -10.539 -5.782  1.00 15.03 ?  109 LEU   A HD23 1 
ATOM   2292 N N    . LYS   A 1 110 ? 23.360 -12.514 -5.654  1.00 10.43 ?  110 LYS   A N    1 
ATOM   2293 C CA   . LYS   A 1 110 ? 23.732 -13.626 -4.788  1.00 10.62 ?  110 LYS   A CA   1 
ATOM   2294 C C    . LYS   A 1 110 ? 25.112 -13.402 -4.179  1.00 9.94  ?  110 LYS   A C    1 
ATOM   2295 O O    . LYS   A 1 110 ? 25.305 -13.597 -2.977  1.00 10.13 ?  110 LYS   A O    1 
ATOM   2296 C CB   . LYS   A 1 110 ? 23.652 -14.953 -5.547  1.00 11.59 ?  110 LYS   A CB   1 
ATOM   2297 C CG   . LYS   A 1 110 ? 23.847 -16.169 -4.632  1.00 11.79 ?  110 LYS   A CG   1 
ATOM   2298 C CD   . LYS   A 1 110 ? 23.605 -17.496 -5.332  1.00 12.11 ?  110 LYS   A CD   1 
ATOM   2299 C CE   . LYS   A 1 110 ? 23.732 -18.664 -4.368  1.00 13.02 ?  110 LYS   A CE   1 
ATOM   2300 N NZ   . LYS   A 1 110 ? 22.543 -18.802 -3.488  1.00 13.27 ?  110 LYS   A NZ   1 
ATOM   2301 H H    . LYS   A 1 110 ? 23.240 -12.715 -6.477  1.00 12.53 ?  110 LYS   A H    1 
ATOM   2302 H HA   . LYS   A 1 110 ? 23.095 -13.680 -4.057  1.00 12.76 ?  110 LYS   A HA   1 
ATOM   2303 H HB2  . LYS   A 1 110 ? 22.780 -15.032 -5.966  1.00 13.93 ?  110 LYS   A HB2  1 
ATOM   2304 H HB3  . LYS   A 1 110 ? 24.348 -14.977 -6.223  1.00 13.93 ?  110 LYS   A HB3  1 
ATOM   2305 H HG2  . LYS   A 1 110 ? 24.755 -16.167 -4.296  1.00 14.16 ?  110 LYS   A HG2  1 
ATOM   2306 H HG3  . LYS   A 1 110 ? 23.221 -16.104 -3.892  1.00 14.16 ?  110 LYS   A HG3  1 
ATOM   2307 H HD2  . LYS   A 1 110 ? 22.712 -17.506 -5.702  1.00 14.54 ?  110 LYS   A HD2  1 
ATOM   2308 H HD3  . LYS   A 1 110 ? 24.265 -17.611 -6.032  1.00 14.54 ?  110 LYS   A HD3  1 
ATOM   2309 H HE2  . LYS   A 1 110 ? 23.831 -19.487 -4.870  1.00 15.64 ?  110 LYS   A HE2  1 
ATOM   2310 H HE3  . LYS   A 1 110 ? 24.508 -18.529 -3.797  1.00 15.64 ?  110 LYS   A HE3  1 
ATOM   2311 H HZ1  . LYS   A 1 110 ? 22.642 -19.492 -2.937  1.00 15.94 ?  110 LYS   A HZ1  1 
ATOM   2312 H HZ2  . LYS   A 1 110 ? 22.428 -18.060 -3.008  1.00 15.94 ?  110 LYS   A HZ2  1 
ATOM   2313 H HZ3  . LYS   A 1 110 ? 21.811 -18.934 -3.985  1.00 15.94 ?  110 LYS   A HZ3  1 
ATOM   2314 N N    . SER   A 1 111 ? 26.073 -12.961 -4.992  1.00 10.56 ?  111 SER   A N    1 
ATOM   2315 C CA   . SER   A 1 111 ? 27.402 -12.653 -4.473  1.00 10.56 ?  111 SER   A CA   1 
ATOM   2316 C C    . SER   A 1 111 ? 27.337 -11.604 -3.371  1.00 10.13 ?  111 SER   A C    1 
ATOM   2317 O O    . SER   A 1 111 ? 28.031 -11.709 -2.355  1.00 10.66 ?  111 SER   A O    1 
ATOM   2318 C CB   . SER   A 1 111 ? 28.299 -12.163 -5.609  1.00 11.43 ?  111 SER   A CB   1 
ATOM   2319 O OG   . SER   A 1 111 ? 28.424 -13.169 -6.600  1.00 13.78 ?  111 SER   A OG   1 
ATOM   2320 H H    . SER   A 1 111 ? 25.979 -12.835 -5.838  1.00 12.68 ?  111 SER   A H    1 
ATOM   2321 H HA   . SER   A 1 111 ? 27.796 -13.459 -4.104  1.00 12.69 ?  111 SER   A HA   1 
ATOM   2322 H HB2  . SER   A 1 111 ? 27.905 -11.378 -6.013  1.00 13.73 ?  111 SER   A HB2  1 
ATOM   2323 H HB3  . SER   A 1 111 ? 29.178 -11.954 -5.255  1.00 13.73 ?  111 SER   A HB3  1 
ATOM   2324 H HG   . SER   A 1 111 ? 28.929 -12.900 -7.224  1.00 16.55 ?  111 SER   A HG   1 
ATOM   2325 N N    . ALA   A 1 112 ? 26.500 -10.585 -3.553  1.00 10.23 ?  112 ALA   A N    1 
ATOM   2326 C CA   . ALA   A 1 112 ? 26.350 -9.552  -2.532  1.00 10.17 ?  112 ALA   A CA   1 
ATOM   2327 C C    . ALA   A 1 112 ? 25.866 -10.148 -1.210  1.00 9.76  ?  112 ALA   A C    1 
ATOM   2328 O O    . ALA   A 1 112 ? 26.418 -9.858  -0.143  1.00 10.07 ?  112 ALA   A O    1 
ATOM   2329 C CB   . ALA   A 1 112 ? 25.392 -8.468  -3.032  1.00 10.92 ?  112 ALA   A CB   1 
ATOM   2330 H H    . ALA   A 1 112 ? 26.013 -10.465 -4.248  1.00 12.30 ?  112 ALA   A H    1 
ATOM   2331 H HA   . ALA   A 1 112 ? 27.208 -9.130  -2.370  1.00 12.22 ?  112 ALA   A HA   1 
ATOM   2332 H HB1  . ALA   A 1 112 ? 25.303 -7.776  -2.347  1.00 13.12 ?  112 ALA   A HB1  1 
ATOM   2333 H HB2  . ALA   A 1 112 ? 25.749 -8.071  -3.843  1.00 13.12 ?  112 ALA   A HB2  1 
ATOM   2334 H HB3  . ALA   A 1 112 ? 24.524 -8.860  -3.209  1.00 13.12 ?  112 ALA   A HB3  1 
ATOM   2335 N N    . TYR   A 1 113 ? 24.832 -10.990 -1.261  1.00 9.89  ?  113 TYR   A N    1 
ATOM   2336 C CA   . TYR   A 1 113 ? 24.323 -11.597 -0.032  1.00 9.85  ?  113 TYR   A CA   1 
ATOM   2337 C C    . TYR   A 1 113 ? 25.330 -12.542 0.620   1.00 9.59  ?  113 TYR   A C    1 
ATOM   2338 O O    . TYR   A 1 113 ? 25.286 -12.728 1.839   1.00 10.17 ?  113 TYR   A O    1 
ATOM   2339 C CB   . TYR   A 1 113 ? 23.004 -12.324 -0.295  1.00 10.16 ?  113 TYR   A CB   1 
ATOM   2340 C CG   . TYR   A 1 113 ? 21.781 -11.424 -0.223  1.00 9.67  ?  113 TYR   A CG   1 
ATOM   2341 C CD1  . TYR   A 1 113 ? 21.409 -10.816 0.972   1.00 10.04 ?  113 TYR   A CD1  1 
ATOM   2342 C CD2  . TYR   A 1 113 ? 20.984 -11.208 -1.339  1.00 9.95  ?  113 TYR   A CD2  1 
ATOM   2343 C CE1  . TYR   A 1 113 ? 20.286 -10.028 1.053   1.00 10.01 ?  113 TYR   A CE1  1 
ATOM   2344 C CE2  . TYR   A 1 113 ? 19.836 -10.404 -1.265  1.00 10.05 ?  113 TYR   A CE2  1 
ATOM   2345 C CZ   . TYR   A 1 113 ? 19.501 -9.823  -0.064  1.00 9.93  ?  113 TYR   A CZ   1 
ATOM   2346 O OH   . TYR   A 1 113 ? 18.372 -9.032  0.068   1.00 10.67 ?  113 TYR   A OH   1 
ATOM   2347 H H    . TYR   A 1 113 ? 24.418 -11.218 -1.980  1.00 11.88 ?  113 TYR   A H    1 
ATOM   2348 H HA   . TYR   A 1 113 ? 24.144 -10.888 0.602   1.00 11.84 ?  113 TYR   A HA   1 
ATOM   2349 H HB2  . TYR   A 1 113 ? 23.033 -12.711 -1.186  1.00 12.20 ?  113 TYR   A HB2  1 
ATOM   2350 H HB3  . TYR   A 1 113 ? 22.901 -13.027 0.364   1.00 12.20 ?  113 TYR   A HB3  1 
ATOM   2351 H HD1  . TYR   A 1 113 ? 21.928 -10.958 1.734   1.00 12.06 ?  113 TYR   A HD1  1 
ATOM   2352 H HD2  . TYR   A 1 113 ? 21.208 -11.612 -2.145  1.00 11.96 ?  113 TYR   A HD2  1 
ATOM   2353 H HE1  . TYR   A 1 113 ? 20.058 -9.634  1.864   1.00 12.03 ?  113 TYR   A HE1  1 
ATOM   2354 H HE2  . TYR   A 1 113 ? 19.303 -10.264 -2.015  1.00 12.08 ?  113 TYR   A HE2  1 
ATOM   2355 H HH   . TYR   A 1 113 ? 17.975 -8.980  -0.679  1.00 12.82 ?  113 TYR   A HH   1 
ATOM   2356 N N    . GLU   A 1 114 ? 26.228 -13.161 -0.162  1.00 9.92  ?  114 GLU   A N    1 
ATOM   2357 C CA   . GLU   A 1 114 ? 27.216 -14.064 0.434   1.00 10.02 ?  114 GLU   A CA   1 
ATOM   2358 C C    . GLU   A 1 114 ? 28.072 -13.359 1.478   1.00 9.67  ?  114 GLU   A C    1 
ATOM   2359 O O    . GLU   A 1 114 ? 28.552 -13.992 2.430   1.00 10.06 ?  114 GLU   A O    1 
ATOM   2360 C CB   . GLU   A 1 114 ? 28.087 -14.717 -0.650  1.00 10.12 ?  114 GLU   A CB   1 
ATOM   2361 C CG   . GLU   A 1 114 ? 27.320 -15.761 -1.437  1.00 10.43 ?  114 GLU   A CG   1 
ATOM   2362 C CD   . GLU   A 1 114 ? 28.030 -16.305 -2.674  1.00 10.93 ?  114 GLU   A CD   1 
ATOM   2363 O OE1  . GLU   A 1 114 ? 28.990 -15.686 -3.170  1.00 11.09 ?  114 GLU   A OE1  1 
ATOM   2364 O OE2  . GLU   A 1 114 ? 27.582 -17.372 -3.163  1.00 12.10 -1 114 GLU   A OE2  1 
ATOM   2365 H H    . GLU   A 1 114 ? 26.288 -13.068 -1.025  1.00 11.92 ?  114 GLU   A H    1 
ATOM   2366 H HA   . GLU   A 1 114 ? 26.742 -14.770 0.879   1.00 12.04 ?  114 GLU   A HA   1 
ATOM   2367 H HB2  . GLU   A 1 114 ? 28.396 -14.040 -1.277  1.00 12.16 ?  114 GLU   A HB2  1 
ATOM   2368 H HB3  . GLU   A 1 114 ? 28.846 -15.155 -0.235  1.00 12.16 ?  114 GLU   A HB3  1 
ATOM   2369 H HG2  . GLU   A 1 114 ? 27.136 -16.514 -0.853  1.00 12.53 ?  114 GLU   A HG2  1 
ATOM   2370 H HG3  . GLU   A 1 114 ? 26.478 -15.371 -1.730  1.00 12.53 ?  114 GLU   A HG3  1 
ATOM   2371 N N    . ASN   A 1 115 ? 28.264 -12.042 1.339   1.00 9.57  ?  115 ASN   A N    1 
ATOM   2372 C CA   . ASN   A 1 115 ? 29.031 -11.310 2.342   1.00 9.97  ?  115 ASN   A CA   1 
ATOM   2373 C C    . ASN   A 1 115 ? 28.416 -11.443 3.731   1.00 9.56  ?  115 ASN   A C    1 
ATOM   2374 O O    . ASN   A 1 115 ? 29.130 -11.376 4.739   1.00 10.36 ?  115 ASN   A O    1 
ATOM   2375 C CB   . ASN   A 1 115 ? 29.136 -9.836  1.959   1.00 9.94  ?  115 ASN   A CB   1 
ATOM   2376 C CG   . ASN   A 1 115 ? 29.926 -9.631  0.692   1.00 11.06 ?  115 ASN   A CG   1 
ATOM   2377 O OD1  . ASN   A 1 115 ? 31.146 -9.773  0.694   1.00 14.39 ?  115 ASN   A OD1  1 
ATOM   2378 N ND2  . ASN   A 1 115 ? 29.252 -9.310  -0.395  1.00 10.59 ?  115 ASN   A ND2  1 
ATOM   2379 H H    . ASN   A 1 115 ? 27.962 -11.553 0.693   1.00 11.50 ?  115 ASN   A H    1 
ATOM   2380 H HA   . ASN   A 1 115 ? 29.926 -11.672 2.381   1.00 11.98 ?  115 ASN   A HA   1 
ATOM   2381 H HB2  . ASN   A 1 115 ? 28.240 -9.480  1.832   1.00 11.94 ?  115 ASN   A HB2  1 
ATOM   2382 H HB3  . ASN   A 1 115 ? 29.578 -9.355  2.682   1.00 11.94 ?  115 ASN   A HB3  1 
ATOM   2383 H HD21 . ASN   A 1 115 ? 29.668 -9.179  -1.132  1.00 12.73 ?  115 ASN   A HD21 1 
ATOM   2384 H HD22 . ASN   A 1 115 ? 28.393 -9.246  -0.366  1.00 12.73 ?  115 ASN   A HD22 1 
ATOM   2385 N N    . PHE   A 1 116 ? 27.090 -11.610 3.813   1.00 10.03 ?  116 PHE   A N    1 
ATOM   2386 C CA   . PHE   A 1 116 ? 26.447 -11.708 5.120   1.00 9.83  ?  116 PHE   A CA   1 
ATOM   2387 C C    . PHE   A 1 116 ? 26.923 -12.939 5.890   1.00 10.04 ?  116 PHE   A C    1 
ATOM   2388 O O    . PHE   A 1 116 ? 26.852 -12.958 7.121   1.00 10.79 ?  116 PHE   A O    1 
ATOM   2389 C CB   . PHE   A 1 116 ? 24.912 -11.824 4.996   1.00 9.97  ?  116 PHE   A CB   1 
ATOM   2390 C CG   . PHE   A 1 116 ? 24.158 -10.575 4.530   1.00 9.53  ?  116 PHE   A CG   1 
ATOM   2391 C CD1  . PHE   A 1 116 ? 24.735 -9.554  3.785   1.00 9.77  ?  116 PHE   A CD1  1 
ATOM   2392 C CD2  . PHE   A 1 116 ? 22.797 -10.470 4.837   1.00 10.29 ?  116 PHE   A CD2  1 
ATOM   2393 C CE1  . PHE   A 1 116 ? 23.975 -8.467  3.361   1.00 9.79  ?  116 PHE   A CE1  1 
ATOM   2394 C CE2  . PHE   A 1 116 ? 22.033 -9.398  4.416   1.00 10.38 ?  116 PHE   A CE2  1 
ATOM   2395 C CZ   . PHE   A 1 116 ? 22.617 -8.395  3.679   1.00 9.79  ?  116 PHE   A CZ   1 
ATOM   2396 H H    . PHE   A 1 116 ? 26.555 -11.659 3.139   1.00 12.05 ?  116 PHE   A H    1 
ATOM   2397 H HA   . PHE   A 1 116 ? 26.649 -10.918 5.643   1.00 11.81 ?  116 PHE   A HA   1 
ATOM   2398 H HB2  . PHE   A 1 116 ? 24.711 -12.534 4.364   1.00 11.98 ?  116 PHE   A HB2  1 
ATOM   2399 H HB3  . PHE   A 1 116 ? 24.555 -12.066 5.866   1.00 11.98 ?  116 PHE   A HB3  1 
ATOM   2400 H HD1  . PHE   A 1 116 ? 25.633 -9.608  3.559   1.00 11.74 ?  116 PHE   A HD1  1 
ATOM   2401 H HD2  . PHE   A 1 116 ? 22.391 -11.159 5.323   1.00 12.36 ?  116 PHE   A HD2  1 
ATOM   2402 H HE1  . PHE   A 1 116 ? 24.374 -7.789  2.869   1.00 11.77 ?  116 PHE   A HE1  1 
ATOM   2403 H HE2  . PHE   A 1 116 ? 21.129 -9.357  4.642   1.00 12.47 ?  116 PHE   A HE2  1 
ATOM   2404 H HZ   . PHE   A 1 116 ? 22.115 -7.664  3.413   1.00 11.77 ?  116 PHE   A HZ   1 
ATOM   2405 N N    . ASN   A 1 117 ? 27.360 -13.991 5.187   1.00 10.43 ?  117 ASN   A N    1 
ATOM   2406 C CA   . ASN   A 1 117 ? 27.728 -15.237 5.856   1.00 10.68 ?  117 ASN   A CA   1 
ATOM   2407 C C    . ASN   A 1 117 ? 28.993 -15.120 6.686   1.00 10.95 ?  117 ASN   A C    1 
ATOM   2408 O O    . ASN   A 1 117 ? 29.287 -16.034 7.463   1.00 11.85 ?  117 ASN   A O    1 
ATOM   2409 C CB   . ASN   A 1 117 ? 27.837 -16.357 4.829   1.00 10.74 ?  117 ASN   A CB   1 
ATOM   2410 C CG   . ASN   A 1 117 ? 26.478 -16.746 4.306   1.00 10.77 ?  117 ASN   A CG   1 
ATOM   2411 O OD1  . ASN   A 1 117 ? 25.501 -16.763 5.064   1.00 11.44 ?  117 ASN   A OD1  1 
ATOM   2412 N ND2  . ASN   A 1 117 ? 26.382 -17.016 3.019   1.00 10.76 ?  117 ASN   A ND2  1 
ATOM   2413 H H    . ASN   A 1 117 ? 27.432 -14.010 4.326   1.00 12.54 ?  117 ASN   A H    1 
ATOM   2414 H HA   . ASN   A 1 117 ? 27.006 -15.474 6.460   1.00 12.83 ?  117 ASN   A HA   1 
ATOM   2415 H HB2  . ASN   A 1 117 ? 28.376 -16.058 4.078   1.00 12.91 ?  117 ASN   A HB2  1 
ATOM   2416 H HB3  . ASN   A 1 117 ? 28.236 -17.135 5.242   1.00 12.91 ?  117 ASN   A HB3  1 
ATOM   2417 H HD21 . ASN   A 1 117 ? 25.624 -17.235 2.685   1.00 12.93 ?  117 ASN   A HD21 1 
ATOM   2418 H HD22 . ASN   A 1 117 ? 27.083 -16.984 2.521   1.00 12.93 ?  117 ASN   A HD22 1 
ATOM   2419 N N    . GLN   A 1 118 ? 29.716 -14.011 6.570   1.00 10.98 ?  118 GLN   A N    1 
ATOM   2420 C CA   . GLN   A 1 118 ? 30.896 -13.773 7.386   1.00 11.41 ?  118 GLN   A CA   1 
ATOM   2421 C C    . GLN   A 1 118 ? 30.556 -13.209 8.760   1.00 11.18 ?  118 GLN   A C    1 
ATOM   2422 O O    . GLN   A 1 118 ? 31.471 -12.910 9.536   1.00 12.98 ?  118 GLN   A O    1 
ATOM   2423 C CB   . GLN   A 1 118 ? 31.884 -12.874 6.641   1.00 11.51 ?  118 GLN   A CB   1 
ATOM   2424 C CG   . GLN   A 1 118 ? 32.360 -13.465 5.322   1.00 11.67 ?  118 GLN   A CG   1 
ATOM   2425 C CD   . GLN   A 1 118 ? 33.189 -14.725 5.497   1.00 12.34 ?  118 GLN   A CD   1 
ATOM   2426 O OE1  . GLN   A 1 118 ? 34.046 -14.799 6.389   1.00 13.11 ?  118 GLN   A OE1  1 
ATOM   2427 N NE2  . GLN   A 1 118 ? 32.943 -15.724 4.644   1.00 12.38 ?  118 GLN   A NE2  1 
ATOM   2428 H H    . GLN   A 1 118 ? 29.531 -13.362 6.025   1.00 13.19 ?  118 GLN   A H    1 
ATOM   2429 H HA   . GLN   A 1 118 ? 31.328 -14.629 7.529   1.00 13.71 ?  118 GLN   A HA   1 
ATOM   2430 H HB2  . GLN   A 1 118 ? 31.458 -12.027 6.455   1.00 13.83 ?  118 GLN   A HB2  1 
ATOM   2431 H HB3  . GLN   A 1 118 ? 32.663 -12.740 7.205   1.00 13.83 ?  118 GLN   A HB3  1 
ATOM   2432 H HG2  . GLN   A 1 118 ? 31.588 -13.682 4.774   1.00 14.02 ?  118 GLN   A HG2  1 
ATOM   2433 H HG3  . GLN   A 1 118 ? 32.911 -12.809 4.865   1.00 14.02 ?  118 GLN   A HG3  1 
ATOM   2434 H HE21 . GLN   A 1 118 ? 32.338 -15.629 4.028   1.00 14.87 ?  118 GLN   A HE21 1 
ATOM   2435 H HE22 . GLN   A 1 118 ? 33.382 -16.460 4.691   1.00 14.87 ?  118 GLN   A HE22 1 
ATOM   2436 N N    . HIS   A 1 119 ? 29.271 -13.058 9.082   1.00 11.07 ?  119 HIS   A N    1 
ATOM   2437 C CA   . HIS   A 1 119 ? 28.830 -12.444 10.329  1.00 11.43 ?  119 HIS   A CA   1 
ATOM   2438 C C    . HIS   A 1 119 ? 27.690 -13.263 10.906  1.00 11.91 ?  119 HIS   A C    1 
ATOM   2439 O O    . HIS   A 1 119 ? 26.746 -13.602 10.191  1.00 12.23 ?  119 HIS   A O    1 
ATOM   2440 C CB   . HIS   A 1 119 ? 28.377 -11.010 10.057  1.00 11.99 ?  119 HIS   A CB   1 
ATOM   2441 C CG   . HIS   A 1 119 ? 29.459 -10.198 9.440   1.00 13.53 ?  119 HIS   A CG   1 
ATOM   2442 N ND1  . HIS   A 1 119 ? 30.438 -9.595  10.193  1.00 15.86 ?  119 HIS   A ND1  1 
ATOM   2443 C CD2  . HIS   A 1 119 ? 29.796 -9.998  8.146   1.00 14.37 ?  119 HIS   A CD2  1 
ATOM   2444 C CE1  . HIS   A 1 119 ? 31.306 -9.009  9.388   1.00 16.07 ?  119 HIS   A CE1  1 
ATOM   2445 N NE2  . HIS   A 1 119 ? 30.951 -9.255  8.141   1.00 16.06 ?  119 HIS   A NE2  1 
ATOM   2446 H H    . HIS   A 1 119 ? 28.618 -13.326 8.585   1.00 13.30 ?  119 HIS   A H    1 
ATOM   2447 H HA   . HIS   A 1 119 ? 29.562 -12.437 10.967  1.00 13.73 ?  119 HIS   A HA   1 
ATOM   2448 H HB2  . HIS   A 1 119 ? 27.624 -11.031 9.446   1.00 14.40 ?  119 HIS   A HB2  1 
ATOM   2449 H HB3  . HIS   A 1 119 ? 28.125 -10.598 10.893  1.00 14.40 ?  119 HIS   A HB3  1 
ATOM   2450 H HD1  . HIS   A 1 119 ? 30.472 -9.587  11.049  1.00 19.05 ?  119 HIS   A HD1  1 
ATOM   2451 H HD2  . HIS   A 1 119 ? 29.333 -10.307 7.398   1.00 17.26 ?  119 HIS   A HD2  1 
ATOM   2452 H HE1  . HIS   A 1 119 ? 32.045 -8.511  9.651   1.00 19.30 ?  119 HIS   A HE1  1 
ATOM   2453 N N    . GLU   A 1 120 ? 27.779 -13.580 12.198  1.00 12.77 ?  120 GLU   A N    1 
ATOM   2454 C CA   . GLU   A 1 120 ? 26.821 -14.510 12.788  1.00 14.86 ?  120 GLU   A CA   1 
ATOM   2455 C C    . GLU   A 1 120 ? 25.407 -13.938 12.863  1.00 13.29 ?  120 GLU   A C    1 
ATOM   2456 O O    . GLU   A 1 120 ? 24.431 -14.697 12.751  1.00 13.57 ?  120 GLU   A O    1 
ATOM   2457 C CB   . GLU   A 1 120 ? 27.297 -14.939 14.175  1.00 20.42 ?  120 GLU   A CB   1 
ATOM   2458 C CG   . GLU   A 1 120 ? 28.481 -15.891 14.151  1.00 27.99 ?  120 GLU   A CG   1 
ATOM   2459 C CD   . GLU   A 1 120 ? 28.682 -16.595 15.478  1.00 35.56 ?  120 GLU   A CD   1 
ATOM   2460 O OE1  . GLU   A 1 120 ? 28.204 -16.074 16.508  1.00 37.67 ?  120 GLU   A OE1  1 
ATOM   2461 O OE2  . GLU   A 1 120 ? 29.315 -17.673 15.490  1.00 39.27 -1 120 GLU   A OE2  1 
ATOM   2462 H H    . GLU   A 1 120 ? 28.381 -13.284 12.741  1.00 15.34 ?  120 GLU   A H    1 
ATOM   2463 H HA   . GLU   A 1 120 ? 26.783 -15.303 12.242  1.00 17.84 ?  120 GLU   A HA   1 
ATOM   2464 H HB2  . GLU   A 1 120 ? 27.565 -14.159 14.683  1.00 24.52 ?  120 GLU   A HB2  1 
ATOM   2465 H HB3  . GLU   A 1 120 ? 26.571 -15.395 14.635  1.00 24.52 ?  120 GLU   A HB3  1 
ATOM   2466 H HG2  . GLU   A 1 120 ? 28.338 -16.564 13.465  1.00 33.60 ?  120 GLU   A HG2  1 
ATOM   2467 H HG3  . GLU   A 1 120 ? 29.290 -15.393 13.965  1.00 33.60 ?  120 GLU   A HG3  1 
ATOM   2468 N N    . VAL   A 1 121 ? 25.276 -12.630 13.087  1.00 12.47 ?  121 VAL   A N    1 
ATOM   2469 C CA   . VAL   A 1 121 ? 23.987 -11.955 13.210  1.00 12.63 ?  121 VAL   A CA   1 
ATOM   2470 C C    . VAL   A 1 121 ? 24.108 -10.577 12.571  1.00 11.42 ?  121 VAL   A C    1 
ATOM   2471 O O    . VAL   A 1 121 ? 25.078 -9.854  12.821  1.00 12.31 ?  121 VAL   A O    1 
ATOM   2472 C CB   . VAL   A 1 121 ? 23.561 -11.797 14.689  1.00 15.74 ?  121 VAL   A CB   1 
ATOM   2473 C CG1  . VAL   A 1 121 ? 22.187 -11.138 14.782  1.00 16.41 ?  121 VAL   A CG1  1 
ATOM   2474 C CG2  . VAL   A 1 121 ? 23.564 -13.125 15.422  1.00 17.63 ?  121 VAL   A CG2  1 
ATOM   2475 H H    . VAL   A 1 121 ? 25.945 -12.093 13.183  1.00 14.99 ?  121 VAL   A H    1 
ATOM   2476 H HA   . VAL   A 1 121 ? 23.308 -12.466 12.747  1.00 15.17 ?  121 VAL   A HA   1 
ATOM   2477 H HB   . VAL   A 1 121 ? 24.195 -11.218 15.139  1.00 18.91 ?  121 VAL   A HB   1 
ATOM   2478 H HG11 . VAL   A 1 121 ? 21.866 -11.199 15.697  1.00 19.71 ?  121 VAL   A HG11 1 
ATOM   2479 H HG12 . VAL   A 1 121 ? 22.262 -10.206 14.524  1.00 19.71 ?  121 VAL   A HG12 1 
ATOM   2480 H HG13 . VAL   A 1 121 ? 21.573 -11.598 14.188  1.00 19.71 ?  121 VAL   A HG13 1 
ATOM   2481 H HG21 . VAL   A 1 121 ? 23.223 -12.989 16.326  1.00 21.17 ?  121 VAL   A HG21 1 
ATOM   2482 H HG22 . VAL   A 1 121 ? 22.988 -13.749 14.950  1.00 21.17 ?  121 VAL   A HG22 1 
ATOM   2483 H HG23 . VAL   A 1 121 ? 24.466 -13.468 15.460  1.00 21.17 ?  121 VAL   A HG23 1 
ATOM   2484 N N    . LEU   A 1 122 ? 23.094 -10.185 11.792  1.00 10.93 ?  122 LEU   A N    1 
ATOM   2485 C CA   . LEU   A 1 122 ? 23.087 -8.883  11.129  1.00 10.68 ?  122 LEU   A CA   1 
ATOM   2486 C C    . LEU   A 1 122 ? 21.688 -8.286  11.092  1.00 10.58 ?  122 LEU   A C    1 
ATOM   2487 O O    . LEU   A 1 122 ? 20.699 -9.007  10.954  1.00 11.94 ?  122 LEU   A O    1 
ATOM   2488 C CB   . LEU   A 1 122 ? 23.518 -8.970  9.658   1.00 12.02 ?  122 LEU   A CB   1 
ATOM   2489 C CG   . LEU   A 1 122 ? 24.720 -9.825  9.288   1.00 12.00 ?  122 LEU   A CG   1 
ATOM   2490 C CD1  . LEU   A 1 122 ? 24.312 -11.274 9.055   1.00 13.29 ?  122 LEU   A CD1  1 
ATOM   2491 C CD2  . LEU   A 1 122 ? 25.411 -9.257  8.055   1.00 11.89 ?  122 LEU   A CD2  1 
ATOM   2492 H H    . LEU   A 1 122 ? 22.389 -10.655 11.634  1.00 13.14 ?  122 LEU   A H    1 
ATOM   2493 H HA   . LEU   A 1 122 ? 23.683 -8.269  11.598  1.00 12.83 ?  122 LEU   A HA   1 
ATOM   2494 H HB2  . LEU   A 1 122 ? 22.773 -9.314  9.151   1.00 14.44 ?  122 LEU   A HB2  1 
ATOM   2495 H HB3  . LEU   A 1 122 ? 23.721 -8.070  9.354   1.00 14.44 ?  122 LEU   A HB3  1 
ATOM   2496 H HG   . LEU   A 1 122 ? 25.370 -9.812  10.013  1.00 14.42 ?  122 LEU   A HG   1 
ATOM   2497 H HD11 . LEU   A 1 122 ? 25.084 -11.788 8.773   1.00 15.96 ?  122 LEU   A HD11 1 
ATOM   2498 H HD12 . LEU   A 1 122 ? 23.960 -11.639 9.884   1.00 15.96 ?  122 LEU   A HD12 1 
ATOM   2499 H HD13 . LEU   A 1 122 ? 23.627 -11.302 8.368   1.00 15.96 ?  122 LEU   A HD13 1 
ATOM   2500 H HD21 . LEU   A 1 122 ? 26.155 -9.829  7.803   1.00 14.28 ?  122 LEU   A HD21 1 
ATOM   2501 H HD22 . LEU   A 1 122 ? 24.772 -9.210  7.325   1.00 14.28 ?  122 LEU   A HD22 1 
ATOM   2502 H HD23 . LEU   A 1 122 ? 25.742 -8.363  8.256   1.00 14.28 ?  122 LEU   A HD23 1 
ATOM   2503 N N    A LEU   A 1 123 ? 21.626 -6.953  11.183  0.62 10.32 ?  123 LEU   A N    1 
ATOM   2504 N N    B LEU   A 1 123 ? 21.635 -6.956  11.216  0.38 10.35 ?  123 LEU   A N    1 
ATOM   2505 C CA   A LEU   A 1 123 ? 20.457 -6.160  10.802  0.62 9.91  ?  123 LEU   A CA   1 
ATOM   2506 C CA   B LEU   A 1 123 ? 20.466 -6.146  10.889  0.38 10.20 ?  123 LEU   A CA   1 
ATOM   2507 C C    A LEU   A 1 123 ? 20.703 -5.634  9.392   0.62 9.36  ?  123 LEU   A C    1 
ATOM   2508 C C    B LEU   A 1 123 ? 20.709 -5.584  9.492   0.38 9.83  ?  123 LEU   A C    1 
ATOM   2509 O O    A LEU   A 1 123 ? 21.806 -5.149  9.106   0.62 9.00  ?  123 LEU   A O    1 
ATOM   2510 O O    B LEU   A 1 123 ? 21.637 -4.790  9.295   0.38 10.02 ?  123 LEU   A O    1 
ATOM   2511 C CB   A LEU   A 1 123 ? 20.312 -4.974  11.758  0.62 10.63 ?  123 LEU   A CB   1 
ATOM   2512 C CB   B LEU   A 1 123 ? 20.342 -5.012  11.904  0.38 10.84 ?  123 LEU   A CB   1 
ATOM   2513 C CG   A LEU   A 1 123 ? 19.248 -3.931  11.414  0.62 11.68 ?  123 LEU   A CG   1 
ATOM   2514 C CG   B LEU   A 1 123 ? 19.375 -3.878  11.561  0.38 10.94 ?  123 LEU   A CG   1 
ATOM   2515 C CD1  A LEU   A 1 123 ? 17.859 -4.553  11.392  0.62 12.30 ?  123 LEU   A CD1  1 
ATOM   2516 C CD1  B LEU   A 1 123 ? 17.931 -4.367  11.528  0.38 11.33 ?  123 LEU   A CD1  1 
ATOM   2517 C CD2  A LEU   A 1 123 ? 19.309 -2.766  12.397  0.62 12.11 ?  123 LEU   A CD2  1 
ATOM   2518 C CD2  B LEU   A 1 123 ? 19.539 -2.725  12.533  0.38 11.04 ?  123 LEU   A CD2  1 
ATOM   2519 H H    A LEU   A 1 123 ? 22.280 -6.473  11.470  0.62 12.39 ?  123 LEU   A H    1 
ATOM   2520 H H    B LEU   A 1 123 ? 22.294 -6.480  11.497  0.38 12.43 ?  123 LEU   A H    1 
ATOM   2521 H HA   A LEU   A 1 123 ? 19.654 -6.702  10.818  0.62 11.91 ?  123 LEU   A HA   1 
ATOM   2522 H HA   B LEU   A 1 123 ? 19.656 -6.682  10.892  0.38 12.26 ?  123 LEU   A HA   1 
ATOM   2523 H HB2  A LEU   A 1 123 ? 20.088 -5.322  12.638  0.62 12.77 ?  123 LEU   A HB2  1 
ATOM   2524 H HB2  B LEU   A 1 123 ? 20.048 -5.394  12.747  0.38 13.02 ?  123 LEU   A HB2  1 
ATOM   2525 H HB3  A LEU   A 1 123 ? 21.159 -4.512  11.802  0.62 12.77 ?  123 LEU   A HB3  1 
ATOM   2526 H HB3  B LEU   A 1 123 ? 21.217 -4.614  12.021  0.38 13.02 ?  123 LEU   A HB3  1 
ATOM   2527 H HG   A LEU   A 1 123 ? 19.427 -3.574  10.530  0.62 14.03 ?  123 LEU   A HG   1 
ATOM   2528 H HG   B LEU   A 1 123 ? 19.588 -3.540  10.682  0.38 13.14 ?  123 LEU   A HG   1 
ATOM   2529 H HD11 A LEU   A 1 123 ? 17.201 -3.858  11.233  0.62 14.77 ?  123 LEU   A HD11 1 
ATOM   2530 H HD11 B LEU   A 1 123 ? 17.349 -3.620  11.318  0.38 13.61 ?  123 LEU   A HD11 1 
ATOM   2531 H HD12 A LEU   A 1 123 ? 17.818 -5.214  10.684  0.62 14.77 ?  123 LEU   A HD12 1 
ATOM   2532 H HD12 B LEU   A 1 123 ? 17.844 -5.055  10.847  0.38 13.61 ?  123 LEU   A HD12 1 
ATOM   2533 H HD13 A LEU   A 1 123 ? 17.688 -4.977  12.250  0.62 14.77 ?  123 LEU   A HD13 1 
ATOM   2534 H HD13 B LEU   A 1 123 ? 17.698 -4.734  12.396  0.38 13.61 ?  123 LEU   A HD13 1 
ATOM   2535 H HD21 A LEU   A 1 123 ? 18.629 -2.115  12.163  0.62 14.55 ?  123 LEU   A HD21 1 
ATOM   2536 H HD21 B LEU   A 1 123 ? 18.913 -2.024  12.295  0.38 13.26 ?  123 LEU   A HD21 1 
ATOM   2537 H HD22 A LEU   A 1 123 ? 19.148 -3.101  13.295  0.62 14.55 ?  123 LEU   A HD22 1 
ATOM   2538 H HD22 B LEU   A 1 123 ? 19.356 -3.041  13.432  0.38 13.26 ?  123 LEU   A HD22 1 
ATOM   2539 H HD23 A LEU   A 1 123 ? 20.188 -2.358  12.352  0.62 14.55 ?  123 LEU   A HD23 1 
ATOM   2540 H HD23 B LEU   A 1 123 ? 20.447 -2.393  12.477  0.38 13.26 ?  123 LEU   A HD23 1 
ATOM   2541 N N    A ALA   A 1 124 ? 19.701 -5.719  8.508   0.62 8.63  ?  124 ALA   A N    1 
ATOM   2542 N N    B ALA   A 1 124 ? 19.893 -5.993  8.525   0.38 9.09  ?  124 ALA   A N    1 
ATOM   2543 C CA   A ALA   A 1 124 ? 20.001 -5.457  7.105   0.62 8.42  ?  124 ALA   A CA   1 
ATOM   2544 C CA   B ALA   A 1 124 ? 20.150 -5.712  7.121   0.38 9.84  ?  124 ALA   A CA   1 
ATOM   2545 C C    A ALA   A 1 124 ? 18.745 -5.018  6.353   0.62 8.60  ?  124 ALA   A C    1 
ATOM   2546 C C    B ALA   A 1 124 ? 18.940 -5.123  6.411   0.38 10.11 ?  124 ALA   A C    1 
ATOM   2547 O O    A ALA   A 1 124 ? 17.621 -5.408  6.711   0.62 9.26  ?  124 ALA   A O    1 
ATOM   2548 O O    B ALA   A 1 124 ? 17.795 -5.344  6.821   0.38 11.21 ?  124 ALA   A O    1 
ATOM   2549 C CB   A ALA   A 1 124 ? 20.596 -6.697  6.434   0.62 8.63  ?  124 ALA   A CB   1 
ATOM   2550 C CB   B ALA   A 1 124 ? 20.580 -6.989  6.383   0.38 10.53 ?  124 ALA   A CB   1 
ATOM   2551 H H    A ALA   A 1 124 ? 18.875 -5.904  8.688   0.62 10.37 ?  124 ALA   A H    1 
ATOM   2552 H H    B ALA   A 1 124 ? 19.179 -6.453  8.664   0.38 10.92 ?  124 ALA   A H    1 
ATOM   2553 H HA   A ALA   A 1 124 ? 20.654 -4.738  7.066   0.62 10.12 ?  124 ALA   A HA   1 
ATOM   2554 H HA   B ALA   A 1 124 ? 20.881 -5.082  7.072   0.38 11.83 ?  124 ALA   A HA   1 
ATOM   2555 H HB1  A ALA   A 1 124 ? 20.790 -6.490  5.509   0.62 10.37 ?  124 ALA   A HB1  1 
ATOM   2556 H HB1  B ALA   A 1 124 ? 20.745 -6.774  5.450   0.38 12.65 ?  124 ALA   A HB1  1 
ATOM   2557 H HB2  A ALA   A 1 124 ? 21.415 -6.941  6.898   0.62 10.37 ?  124 ALA   A HB2  1 
ATOM   2558 H HB2  B ALA   A 1 124 ? 21.394 -7.335  6.788   0.38 12.65 ?  124 ALA   A HB2  1 
ATOM   2559 H HB3  A ALA   A 1 124 ? 19.957 -7.421  6.490   0.62 10.37 ?  124 ALA   A HB3  1 
ATOM   2560 H HB3  B ALA   A 1 124 ? 19.874 -7.649  6.451   0.38 12.65 ?  124 ALA   A HB3  1 
ATOM   2561 N N    A PRO   A 1 125 ? 18.923 -4.286  5.251   0.62 9.04  ?  125 PRO   A N    1 
ATOM   2562 N N    B PRO   A 1 125 ? 19.164 -4.396  5.316   0.38 8.85  ?  125 PRO   A N    1 
ATOM   2563 C CA   A PRO   A 1 125 ? 17.863 -4.075  4.265   0.62 9.50  ?  125 PRO   A CA   1 
ATOM   2564 C CA   B PRO   A 1 125 ? 18.070 -3.961  4.447   0.38 8.97  ?  125 PRO   A CA   1 
ATOM   2565 C C    A PRO   A 1 125 ? 17.933 -5.141  3.177   0.62 9.42  ?  125 PRO   A C    1 
ATOM   2566 C C    B PRO   A 1 125 ? 17.917 -4.970  3.313   0.38 9.56  ?  125 PRO   A C    1 
ATOM   2567 O O    A PRO   A 1 125 ? 18.901 -5.896  3.070   0.62 9.68  ?  125 PRO   A O    1 
ATOM   2568 O O    B PRO   A 1 125 ? 18.724 -5.889  3.161   0.38 10.07 ?  125 PRO   A O    1 
ATOM   2569 C CB   A PRO   A 1 125 ? 18.268 -2.724  3.663   0.62 10.07 ?  125 PRO   A CB   1 
ATOM   2570 C CB   B PRO   A 1 125 ? 18.611 -2.636  3.900   0.38 8.59  ?  125 PRO   A CB   1 
ATOM   2571 C CG   A PRO   A 1 125 ? 19.770 -2.837  3.599   0.62 9.81  ?  125 PRO   A CG   1 
ATOM   2572 C CG   B PRO   A 1 125 ? 20.073 -2.941  3.693   0.38 8.30  ?  125 PRO   A CG   1 
ATOM   2573 C CD   A PRO   A 1 125 ? 20.164 -3.584  4.865   0.62 9.38  ?  125 PRO   A CD   1 
ATOM   2574 C CD   B PRO   A 1 125 ? 20.462 -3.906  4.813   0.38 8.19  ?  125 PRO   A CD   1 
ATOM   2575 H HA   A PRO   A 1 125 ? 16.981 -4.038  4.666   0.62 11.42 ?  125 PRO   A HA   1 
ATOM   2576 H HA   B PRO   A 1 125 ? 17.247 -3.826  4.945   0.38 10.78 ?  125 PRO   A HA   1 
ATOM   2577 H HB2  A PRO   A 1 125 ? 17.883 -2.623  2.776   0.62 12.10 ?  125 PRO   A HB2  1 
ATOM   2578 H HB2  B PRO   A 1 125 ? 18.169 -2.417  3.063   0.38 10.33 ?  125 PRO   A HB2  1 
ATOM   2579 H HB3  A PRO   A 1 125 ? 17.992 -2.004  4.250   0.62 12.10 ?  125 PRO   A HB3  1 
ATOM   2580 H HB3  B PRO   A 1 125 ? 18.486 -1.926  4.555   0.38 10.33 ?  125 PRO   A HB3  1 
ATOM   2581 H HG2  A PRO   A 1 125 ? 20.028 -3.343  2.812   0.62 11.78 ?  125 PRO   A HG2  1 
ATOM   2582 H HG2  B PRO   A 1 125 ? 20.196 -3.358  2.824   0.38 9.98  ?  125 PRO   A HG2  1 
ATOM   2583 H HG3  A PRO   A 1 125 ? 20.164 -1.953  3.584   0.62 11.78 ?  125 PRO   A HG3  1 
ATOM   2584 H HG3  B PRO   A 1 125 ? 20.589 -2.123  3.753   0.38 9.98  ?  125 PRO   A HG3  1 
ATOM   2585 H HD2  A PRO   A 1 125 ? 20.872 -4.215  4.679   0.62 11.27 ?  125 PRO   A HD2  1 
ATOM   2586 H HD2  B PRO   A 1 125 ? 20.997 -4.636  4.455   0.38 9.84  ?  125 PRO   A HD2  1 
ATOM   2587 H HD3  A PRO   A 1 125 ? 20.422 -2.951  5.558   0.62 11.27 ?  125 PRO   A HD3  1 
ATOM   2588 H HD3  B PRO   A 1 125 ? 20.936 -3.432  5.512   0.38 9.84  ?  125 PRO   A HD3  1 
ATOM   2589 N N    A LEU   A 1 126 ? 16.888 -5.167  2.348   0.62 9.58  ?  126 LEU   A N    1 
ATOM   2590 N N    B LEU   A 1 126 ? 16.877 -4.776  2.498   0.38 9.96  ?  126 LEU   A N    1 
ATOM   2591 C CA   A LEU   A 1 126 ? 16.900 -5.982  1.140   0.62 9.51  ?  126 LEU   A CA   1 
ATOM   2592 C CA   B LEU   A 1 126 ? 16.652 -5.660  1.353   0.38 9.75  ?  126 LEU   A CA   1 
ATOM   2593 C C    A LEU   A 1 126 ? 17.822 -5.360  0.097   0.62 9.27  ?  126 LEU   A C    1 
ATOM   2594 C C    B LEU   A 1 126 ? 17.522 -5.185  0.193   0.38 9.55  ?  126 LEU   A C    1 
ATOM   2595 O O    A LEU   A 1 126 ? 17.599 -4.235  -0.365  0.62 10.04 ?  126 LEU   A O    1 
ATOM   2596 O O    B LEU   A 1 126 ? 17.199 -4.203  -0.481  0.38 10.65 ?  126 LEU   A O    1 
ATOM   2597 C CB   A LEU   A 1 126 ? 15.489 -6.127  0.578   0.62 10.40 ?  126 LEU   A CB   1 
ATOM   2598 C CB   B LEU   A 1 126 ? 15.175 -5.670  0.978   0.38 11.21 ?  126 LEU   A CB   1 
ATOM   2599 C CG   A LEU   A 1 126 ? 14.564 -7.056  1.358   0.62 11.24 ?  126 LEU   A CG   1 
ATOM   2600 C CG   B LEU   A 1 126 ? 14.699 -6.745  0.000   0.38 12.14 ?  126 LEU   A CG   1 
ATOM   2601 C CD1  A LEU   A 1 126 ? 13.139 -6.930  0.841   0.62 12.73 ?  126 LEU   A CD1  1 
ATOM   2602 C CD1  B LEU   A 1 126 ? 14.894 -8.139  0.566   0.38 12.65 ?  126 LEU   A CD1  1 
ATOM   2603 C CD2  A LEU   A 1 126 ? 15.047 -8.497  1.250   0.62 10.90 ?  126 LEU   A CD2  1 
ATOM   2604 C CD2  B LEU   A 1 126 ? 13.233 -6.529  -0.345  0.38 11.96 ?  126 LEU   A CD2  1 
ATOM   2605 H H    A LEU   A 1 126 ? 16.170 -4.714  2.456   0.62 11.51 ?  126 LEU   A H    1 
ATOM   2606 H H    B LEU   A 1 126 ? 16.274 -4.148  2.567   0.38 11.97 ?  126 LEU   A H    1 
ATOM   2607 H HA   A LEU   A 1 126 ? 17.239 -6.865  1.350   0.62 11.42 ?  126 LEU   A HA   1 
ATOM   2608 H HA   B LEU   A 1 126 ? 16.916 -6.563  1.586   0.38 11.72 ?  126 LEU   A HA   1 
ATOM   2609 H HB2  A LEU   A 1 126 ? 15.073 -5.252  0.563   0.62 12.49 ?  126 LEU   A HB2  1 
ATOM   2610 H HB2  B LEU   A 1 126 ? 14.661 -5.786  1.787   0.38 13.46 ?  126 LEU   A HB2  1 
ATOM   2611 H HB3  A LEU   A 1 126 ? 15.548 -6.474  -0.325  0.62 12.49 ?  126 LEU   A HB3  1 
ATOM   2612 H HB3  B LEU   A 1 126 ? 14.959 -4.814  0.578   0.38 13.46 ?  126 LEU   A HB3  1 
ATOM   2613 H HG   A LEU   A 1 126 ? 14.564 -6.803  2.295   0.62 13.51 ?  126 LEU   A HG   1 
ATOM   2614 H HG   B LEU   A 1 126 ? 15.209 -6.673  -0.823  0.38 14.59 ?  126 LEU   A HG   1 
ATOM   2615 H HD11 A LEU   A 1 126 ? 12.564 -7.528  1.346   0.62 15.29 ?  126 LEU   A HD11 1 
ATOM   2616 H HD11 B LEU   A 1 126 ? 14.476 -8.780  -0.029  0.38 15.19 ?  126 LEU   A HD11 1 
ATOM   2617 H HD12 A LEU   A 1 126 ? 12.841 -6.015  0.949   0.62 15.29 ?  126 LEU   A HD12 1 
ATOM   2618 H HD12 B LEU   A 1 126 ? 15.843 -8.319  0.634   0.38 15.19 ?  126 LEU   A HD12 1 
ATOM   2619 H HD13 A LEU   A 1 126 ? 13.123 -7.175  -0.099  0.62 15.29 ?  126 LEU   A HD13 1 
ATOM   2620 H HD13 B LEU   A 1 126 ? 14.481 -8.182  1.442   0.38 15.19 ?  126 LEU   A HD13 1 
ATOM   2621 H HD21 A LEU   A 1 126 ? 14.368 -9.087  1.609   0.62 13.09 ?  126 LEU   A HD21 1 
ATOM   2622 H HD21 B LEU   A 1 126 ? 12.948 -7.218  -0.969  0.38 14.37 ?  126 LEU   A HD21 1 
ATOM   2623 H HD22 A LEU   A 1 126 ? 15.206 -8.705  0.315   0.62 13.09 ?  126 LEU   A HD22 1 
ATOM   2624 H HD22 B LEU   A 1 126 ? 12.704 -6.584  0.468   0.38 14.37 ?  126 LEU   A HD22 1 
ATOM   2625 H HD23 A LEU   A 1 126 ? 15.870 -8.591  1.754   0.62 13.09 ?  126 LEU   A HD23 1 
ATOM   2626 H HD23 B LEU   A 1 126 ? 13.123 -5.654  -0.750  0.38 14.37 ?  126 LEU   A HD23 1 
ATOM   2627 N N    A LEU   A 1 127 ? 18.854 -6.106  -0.279  0.62 9.09  ?  127 LEU   A N    1 
ATOM   2628 N N    B LEU   A 1 127 ? 18.626 -5.891  -0.056  0.38 9.31  ?  127 LEU   A N    1 
ATOM   2629 C CA   A LEU   A 1 127 ? 19.844 -5.609  -1.220  0.62 9.37  ?  127 LEU   A CA   1 
ATOM   2630 C CA   B LEU   A 1 127 ? 19.599 -5.422  -1.036  0.38 9.64  ?  127 LEU   A CA   1 
ATOM   2631 C C    A LEU   A 1 127 ? 19.241 -5.432  -2.604  0.62 9.19  ?  127 LEU   A C    1 
ATOM   2632 C C    B LEU   A 1 127 ? 18.989 -5.346  -2.430  0.38 9.32  ?  127 LEU   A C    1 
ATOM   2633 O O    A LEU   A 1 127 ? 18.423 -6.236  -3.064  0.62 9.41  ?  127 LEU   A O    1 
ATOM   2634 O O    B LEU   A 1 127 ? 18.153 -6.170  -2.815  0.38 10.11 ?  127 LEU   A O    1 
ATOM   2635 C CB   A LEU   A 1 127 ? 21.023 -6.574  -1.304  0.62 10.05 ?  127 LEU   A CB   1 
ATOM   2636 C CB   B LEU   A 1 127 ? 20.837 -6.325  -1.065  0.38 10.15 ?  127 LEU   A CB   1 
ATOM   2637 C CG   A LEU   A 1 127 ? 21.774 -6.844  -0.005  0.62 10.42 ?  127 LEU   A CG   1 
ATOM   2638 C CG   B LEU   A 1 127 ? 21.743 -6.331  0.175   0.38 10.63 ?  127 LEU   A CG   1 
ATOM   2639 C CD1  A LEU   A 1 127 ? 22.876 -7.836  -0.273  0.62 10.52 ?  127 LEU   A CD1  1 
ATOM   2640 C CD1  B LEU   A 1 127 ? 22.944 -7.271  0.001   0.38 11.25 ?  127 LEU   A CD1  1 
ATOM   2641 C CD2  A LEU   A 1 127 ? 22.350 -5.560  0.557   0.62 10.86 ?  127 LEU   A CD2  1 
ATOM   2642 C CD2  B LEU   A 1 127 ? 22.207 -4.922  0.544   0.38 10.78 ?  127 LEU   A CD2  1 
ATOM   2643 H H    A LEU   A 1 127 ? 19.015 -6.900  0.010   0.62 10.92 ?  127 LEU   A H    1 
ATOM   2644 H H    B LEU   A 1 127 ? 18.836 -6.630  0.331   0.38 11.19 ?  127 LEU   A H    1 
ATOM   2645 H HA   A LEU   A 1 127 ? 20.180 -4.748  -0.915  0.62 11.26 ?  127 LEU   A HA   1 
ATOM   2646 H HA   B LEU   A 1 127 ? 19.881 -4.531  -0.789  0.38 11.58 ?  127 LEU   A HA   1 
ATOM   2647 H HB2  A LEU   A 1 127 ? 20.696 -7.427  -1.628  0.62 12.07 ?  127 LEU   A HB2  1 
ATOM   2648 H HB2  B LEU   A 1 127 ? 20.540 -7.235  -1.206  0.38 12.19 ?  127 LEU   A HB2  1 
ATOM   2649 H HB3  A LEU   A 1 127 ? 21.669 -6.217  -1.935  0.62 12.07 ?  127 LEU   A HB3  1 
ATOM   2650 H HB3  B LEU   A 1 127 ? 21.385 -6.049  -1.818  0.38 12.19 ?  127 LEU   A HB3  1 
ATOM   2651 H HG   A LEU   A 1 127 ? 21.162 -7.225  0.652   0.62 12.52 ?  127 LEU   A HG   1 
ATOM   2652 H HG   B LEU   A 1 127 ? 21.228 -6.667  0.920   0.38 12.77 ?  127 LEU   A HG   1 
ATOM   2653 H HD11 A LEU   A 1 127 ? 23.339 -8.026  0.558   0.62 12.64 ?  127 LEU   A HD11 1 
ATOM   2654 H HD11 B LEU   A 1 127 ? 23.489 -7.235  0.805   0.38 13.51 ?  127 LEU   A HD11 1 
ATOM   2655 H HD12 A LEU   A 1 127 ? 22.486 -8.653  -0.627  0.62 12.64 ?  127 LEU   A HD12 1 
ATOM   2656 H HD12 B LEU   A 1 127 ? 22.621 -8.174  -0.137  0.38 13.51 ?  127 LEU   A HD12 1 
ATOM   2657 H HD13 A LEU   A 1 127 ? 23.490 -7.456  -0.917  0.62 12.64 ?  127 LEU   A HD13 1 
ATOM   2658 H HD13 B LEU   A 1 127 ? 23.465 -6.983  -0.763  0.38 13.51 ?  127 LEU   A HD13 1 
ATOM   2659 H HD21 A LEU   A 1 127 ? 22.922 -5.776  1.309   0.62 13.05 ?  127 LEU   A HD21 1 
ATOM   2660 H HD21 B LEU   A 1 127 ? 22.874 -4.985  1.246   0.38 12.95 ?  127 LEU   A HD21 1 
ATOM   2661 H HD22 A LEU   A 1 127 ? 22.864 -5.121  -0.138  0.62 13.05 ?  127 LEU   A HD22 1 
ATOM   2662 H HD22 B LEU   A 1 127 ? 22.588 -4.498  -0.239  0.38 12.95 ?  127 LEU   A HD22 1 
ATOM   2663 H HD23 A LEU   A 1 127 ? 21.624 -4.987  0.846   0.62 13.05 ?  127 LEU   A HD23 1 
ATOM   2664 H HD23 B LEU   A 1 127 ? 21.443 -4.414  0.859   0.38 12.95 ?  127 LEU   A HD23 1 
ATOM   2665 N N    A SER   A 1 128 ? 19.675 -4.368  -3.273  0.62 9.69  ?  128 SER   A N    1 
ATOM   2666 N N    B SER   A 1 128 ? 19.423 -4.338  -3.187  0.38 9.07  ?  128 SER   A N    1 
ATOM   2667 C CA   A SER   A 1 128 ? 19.288 -3.986  -4.623  0.62 9.96  ?  128 SER   A CA   1 
ATOM   2668 C CA   B SER   A 1 128 ? 19.025 -4.078  -4.568  0.38 9.16  ?  128 SER   A CA   1 
ATOM   2669 C C    A SER   A 1 128 ? 17.831 -3.540  -4.735  0.62 9.58  ?  128 SER   A C    1 
ATOM   2670 C C    B SER   A 1 128 ? 17.557 -3.696  -4.736  0.38 9.25  ?  128 SER   A C    1 
ATOM   2671 O O    A SER   A 1 128 ? 17.390 -3.210  -5.838  0.62 9.99  ?  128 SER   A O    1 
ATOM   2672 O O    B SER   A 1 128 ? 17.095 -3.554  -5.874  0.38 10.68 ?  128 SER   A O    1 
ATOM   2673 C CB   A SER   A 1 128 ? 19.634 -5.047  -5.678  0.62 9.93  ?  128 SER   A CB   1 
ATOM   2674 C CB   B SER   A 1 128 ? 19.417 -5.207  -5.529  0.38 9.42  ?  128 SER   A CB   1 
ATOM   2675 O OG   A SER   A 1 128 ? 21.040 -5.283  -5.707  0.62 10.91 ?  128 SER   A OG   1 
ATOM   2676 O OG   B SER   A 1 128 ? 20.830 -5.277  -5.659  0.38 10.21 ?  128 SER   A OG   1 
ATOM   2677 H H    A SER   A 1 128 ? 20.247 -3.816  -2.938  0.62 11.64 ?  128 SER   A H    1 
ATOM   2678 H H    B SER   A 1 128 ? 20.001 -3.759  -2.905  0.38 10.90 ?  128 SER   A H    1 
ATOM   2679 H HA   A SER   A 1 128 ? 19.820 -3.212  -4.850  0.62 11.97 ?  128 SER   A HA   1 
ATOM   2680 H HA   B SER   A 1 128 ? 19.531 -3.308  -4.859  0.38 11.01 ?  128 SER   A HA   1 
ATOM   2681 H HB2  A SER   A 1 128 ? 19.177 -5.872  -5.463  0.62 11.94 ?  128 SER   A HB2  1 
ATOM   2682 H HB2  B SER   A 1 128 ? 19.087 -6.050  -5.187  0.38 11.32 ?  128 SER   A HB2  1 
ATOM   2683 H HB3  A SER   A 1 128 ? 19.346 -4.725  -6.551  0.62 11.94 ?  128 SER   A HB3  1 
ATOM   2684 H HB3  B SER   A 1 128 ? 19.027 -5.028  -6.404  0.38 11.32 ?  128 SER   A HB3  1 
ATOM   2685 H HG   A SER   A 1 128 ? 21.441 -4.567  -5.895  0.62 13.11 ?  128 SER   A HG   1 
ATOM   2686 H HG   B SER   A 1 128 ? 21.122 -4.542  -5.955  0.38 12.27 ?  128 SER   A HG   1 
ATOM   2687 N N    A ALA   A 1 129 ? 17.084 -3.493  -3.632  0.62 10.40 ?  129 ALA   A N    1 
ATOM   2688 N N    B ALA   A 1 129 ? 16.815 -3.509  -3.649  0.38 9.39  ?  129 ALA   A N    1 
ATOM   2689 C CA   A ALA   A 1 129 ? 15.709 -3.009  -3.633  0.62 10.78 ?  129 ALA   A CA   1 
ATOM   2690 C CA   B ALA   A 1 129 ? 15.434 -3.060  -3.743  0.38 9.56  ?  129 ALA   A CA   1 
ATOM   2691 C C    A ALA   A 1 129 ? 15.693 -1.482  -3.602  0.62 11.01 ?  129 ALA   A C    1 
ATOM   2692 C C    B ALA   A 1 129 ? 15.390 -1.530  -3.733  0.38 9.53  ?  129 ALA   A C    1 
ATOM   2693 O O    A ALA   A 1 129 ? 16.731 -0.819  -3.686  0.62 11.86 ?  129 ALA   A O    1 
ATOM   2694 O O    B ALA   A 1 129 ? 16.423 -0.857  -3.794  0.38 9.78  ?  129 ALA   A O    1 
ATOM   2695 C CB   A ALA   A 1 129 ? 14.936 -3.606  -2.457  0.62 12.02 ?  129 ALA   A CB   1 
ATOM   2696 C CB   B ALA   A 1 129 ? 14.594 -3.706  -2.641  0.38 9.84  ?  129 ALA   A CB   1 
ATOM   2697 H H    A ALA   A 1 129 ? 17.357 -3.742  -2.857  0.62 12.49 ?  129 ALA   A H    1 
ATOM   2698 H H    B ALA   A 1 129 ? 17.088 -3.634  -2.842  0.38 11.28 ?  129 ALA   A H    1 
ATOM   2699 H HA   A ALA   A 1 129 ? 15.274 -3.290  -4.448  0.62 12.95 ?  129 ALA   A HA   1 
ATOM   2700 H HA   B ALA   A 1 129 ? 15.071 -3.358  -4.589  0.38 11.48 ?  129 ALA   A HA   1 
ATOM   2701 H HB1  A ALA   A 1 129 ? 14.021 -3.283  -2.480  0.62 14.44 ?  129 ALA   A HB1  1 
ATOM   2702 H HB1  B ALA   A 1 129 ? 13.677 -3.400  -2.722  0.38 11.82 ?  129 ALA   A HB1  1 
ATOM   2703 H HB2  A ALA   A 1 129 ? 14.947 -4.572  -2.524  0.62 14.44 ?  129 ALA   A HB2  1 
ATOM   2704 H HB2  B ALA   A 1 129 ? 14.632 -4.670  -2.742  0.38 11.82 ?  129 ALA   A HB2  1 
ATOM   2705 H HB3  A ALA   A 1 129 ? 15.358 -3.330  -1.624  0.62 14.44 ?  129 ALA   A HB3  1 
ATOM   2706 H HB3  B ALA   A 1 129 ? 14.953 -3.449  -1.777  0.38 11.82 ?  129 ALA   A HB3  1 
ATOM   2707 N N    A GLY   A 1 130 ? 14.500 -0.907  -3.483  0.62 11.66 ?  130 GLY   A N    1 
ATOM   2708 N N    B GLY   A 1 130 ? 14.187 -0.963  -3.679  0.38 9.61  ?  130 GLY   A N    1 
ATOM   2709 C CA   A GLY   A 1 130 ? 14.398 0.543   -3.425  0.62 12.39 ?  130 GLY   A CA   1 
ATOM   2710 C CA   B GLY   A 1 130 ? 14.063 0.487   -3.651  0.38 9.15  ?  130 GLY   A CA   1 
ATOM   2711 C C    A GLY   A 1 130 ? 15.001 1.177   -4.662  0.62 11.88 ?  130 GLY   A C    1 
ATOM   2712 C C    B GLY   A 1 130 ? 14.665 1.120   -4.892  0.38 9.05  ?  130 GLY   A C    1 
ATOM   2713 O O    A GLY   A 1 130 ? 14.768 0.736   -5.792  0.62 12.20 ?  130 GLY   A O    1 
ATOM   2714 O O    B GLY   A 1 130 ? 14.442 0.668   -6.020  0.38 9.35  ?  130 GLY   A O    1 
ATOM   2715 H H    A GLY   A 1 130 ? 13.744 -1.329  -3.438  0.62 14.01 ?  130 GLY   A H    1 
ATOM   2716 H H    B GLY   A 1 130 ? 13.436 -1.388  -3.662  0.38 11.55 ?  130 GLY   A H    1 
ATOM   2717 H HA2  A GLY   A 1 130 ? 13.466 0.803   -3.352  0.62 14.89 ?  130 GLY   A HA2  1 
ATOM   2718 H HA2  B GLY   A 1 130 ? 13.128 0.737   -3.573  0.38 11.00 ?  130 GLY   A HA2  1 
ATOM   2719 H HA3  A GLY   A 1 130 ? 14.875 0.871   -2.649  0.62 14.89 ?  130 GLY   A HA3  1 
ATOM   2720 H HA3  B GLY   A 1 130 ? 14.535 0.836   -2.881  0.38 11.00 ?  130 GLY   A HA3  1 
ATOM   2721 N N    A ILE   A 1 131 ? 15.797 2.229   -4.453  0.62 11.98 ?  131 ILE   A N    1 
ATOM   2722 N N    B ILE   A 1 131 ? 15.442 2.187   -4.686  0.38 9.23  ?  131 ILE   A N    1 
ATOM   2723 C CA   A ILE   A 1 131 ? 16.355 2.987   -5.569  0.62 11.04 ?  131 ILE   A CA   1 
ATOM   2724 C CA   B ILE   A 1 131 ? 16.000 2.964   -5.792  0.38 9.57  ?  131 ILE   A CA   1 
ATOM   2725 C C    A ILE   A 1 131 ? 17.396 2.215   -6.372  0.62 10.58 ?  131 ILE   A C    1 
ATOM   2726 C C    B ILE   A 1 131 ? 17.129 2.218   -6.499  0.38 10.01 ?  131 ILE   A C    1 
ATOM   2727 O O    A ILE   A 1 131 ? 17.832 2.707   -7.422  0.62 12.09 ?  131 ILE   A O    1 
ATOM   2728 O O    B ILE   A 1 131 ? 17.687 2.717   -7.484  0.38 10.39 ?  131 ILE   A O    1 
ATOM   2729 C CB   A ILE   A 1 131 ? 16.904 4.358   -5.117  0.62 12.51 ?  131 ILE   A CB   1 
ATOM   2730 C CB   B ILE   A 1 131 ? 16.425 4.386   -5.365  0.38 9.65  ?  131 ILE   A CB   1 
ATOM   2731 C CG1  A ILE   A 1 131 ? 18.124 4.192   -4.201  0.62 13.96 ?  131 ILE   A CG1  1 
ATOM   2732 C CG1  B ILE   A 1 131 ? 17.614 4.366   -4.396  0.38 10.57 ?  131 ILE   A CG1  1 
ATOM   2733 C CG2  A ILE   A 1 131 ? 15.812 5.166   -4.433  0.62 13.16 ?  131 ILE   A CG2  1 
ATOM   2734 C CG2  B ILE   A 1 131 ? 15.238 5.126   -4.762  0.38 9.38  ?  131 ILE   A CG2  1 
ATOM   2735 C CD1  A ILE   A 1 131 ? 18.764 5.510   -3.777  0.62 15.24 ?  131 ILE   A CD1  1 
ATOM   2736 C CD1  B ILE   A 1 131 ? 18.137 5.760   -4.040  0.38 10.86 ?  131 ILE   A CD1  1 
ATOM   2737 H H    A ILE   A 1 131 ? 16.008 2.524   -3.680  0.62 14.40 ?  131 ILE   A H    1 
ATOM   2738 H H    B ILE   A 1 131 ? 15.656 2.480   -3.907  0.38 11.09 ?  131 ILE   A H    1 
ATOM   2739 H HA   A ILE   A 1 131 ? 15.629 3.176   -6.184  0.62 13.26 ?  131 ILE   A HA   1 
ATOM   2740 H HA   B ILE   A 1 131 ? 15.292 3.079   -6.445  0.38 11.49 ?  131 ILE   A HA   1 
ATOM   2741 H HB   A ILE   A 1 131 ? 17.182 4.844   -5.911  0.62 15.02 ?  131 ILE   A HB   1 
ATOM   2742 H HB   B ILE   A 1 131 ? 16.702 4.861   -6.162  0.38 11.59 ?  131 ILE   A HB   1 
ATOM   2743 H HG12 A ILE   A 1 131 ? 17.846 3.724   -3.402  0.62 16.77 ?  131 ILE   A HG12 1 
ATOM   2744 H HG12 B ILE   A 1 131 ? 17.340 3.930   -3.574  0.38 12.70 ?  131 ILE   A HG12 1 
ATOM   2745 H HG13 A ILE   A 1 131 ? 18.798 3.677   -4.670  0.62 16.77 ?  131 ILE   A HG13 1 
ATOM   2746 H HG13 B ILE   A 1 131 ? 18.345 3.870   -4.800  0.38 12.70 ?  131 ILE   A HG13 1 
ATOM   2747 H HG21 A ILE   A 1 131 ? 16.125 6.075   -4.306  0.62 15.81 ?  131 ILE   A HG21 1 
ATOM   2748 H HG21 B ILE   A 1 131 ? 15.475 6.058   -4.639  0.38 11.27 ?  131 ILE   A HG21 1 
ATOM   2749 H HG22 A ILE   A 1 131 ? 15.021 5.165   -4.995  0.62 15.81 ?  131 ILE   A HG22 1 
ATOM   2750 H HG22 B ILE   A 1 131 ? 14.483 5.055   -5.367  0.38 11.27 ?  131 ILE   A HG22 1 
ATOM   2751 H HG23 A ILE   A 1 131 ? 15.611 4.759   -3.578  0.62 15.81 ?  131 ILE   A HG23 1 
ATOM   2752 H HG23 B ILE   A 1 131 ? 15.015 4.725   -3.908  0.38 11.27 ?  131 ILE   A HG23 1 
ATOM   2753 H HD11 A ILE   A 1 131 ? 19.587 5.321   -3.297  0.62 18.30 ?  131 ILE   A HD11 1 
ATOM   2754 H HD11 B ILE   A 1 131 ? 18.956 5.668   -3.529  0.38 13.04 ?  131 ILE   A HD11 1 
ATOM   2755 H HD12 A ILE   A 1 131 ? 18.960 6.041   -4.567  0.62 18.30 ?  131 ILE   A HD12 1 
ATOM   2756 H HD12 B ILE   A 1 131 ? 18.311 6.248   -4.860  0.38 13.04 ?  131 ILE   A HD12 1 
ATOM   2757 H HD13 A ILE   A 1 131 ? 18.151 5.994   -3.200  0.62 18.30 ?  131 ILE   A HD13 1 
ATOM   2758 H HD13 B ILE   A 1 131 ? 17.468 6.224   -3.514  0.38 13.04 ?  131 ILE   A HD13 1 
ATOM   2759 N N    A PHE   A 1 132 ? 17.818 1.026   -5.918  0.62 9.90  ?  132 PHE   A N    1 
ATOM   2760 N N    B PHE   A 1 132 ? 17.475 1.018   -6.014  0.38 10.72 ?  132 PHE   A N    1 
ATOM   2761 C CA   A PHE   A 1 132 ? 18.681 0.190   -6.746  0.62 10.33 ?  132 PHE   A CA   1 
ATOM   2762 C CA   B PHE   A 1 132 ? 18.407 0.166   -6.745  0.38 11.07 ?  132 PHE   A CA   1 
ATOM   2763 C C    A PHE   A 1 132 ? 17.903 -0.572  -7.821  0.62 11.00 ?  132 PHE   A C    1 
ATOM   2764 C C    B PHE   A 1 132 ? 17.746 -0.565  -7.910  0.38 11.64 ?  132 PHE   A C    1 
ATOM   2765 O O    A PHE   A 1 132 ? 18.520 -1.240  -8.657  0.62 12.11 ?  132 PHE   A O    1 
ATOM   2766 O O    B PHE   A 1 132 ? 18.452 -1.065  -8.791  0.38 12.10 ?  132 PHE   A O    1 
ATOM   2767 C CB   A PHE   A 1 132 ? 19.491 -0.790  -5.888  0.62 9.37  ?  132 PHE   A CB   1 
ATOM   2768 C CB   B PHE   A 1 132 ? 19.087 -0.836  -5.808  0.38 10.90 ?  132 PHE   A CB   1 
ATOM   2769 C CG   A PHE   A 1 132 ? 20.719 -0.191  -5.217  0.62 9.56  ?  132 PHE   A CG   1 
ATOM   2770 C CG   B PHE   A 1 132 ? 20.280 -0.283  -5.074  0.38 10.77 ?  132 PHE   A CG   1 
ATOM   2771 C CD1  A PHE   A 1 132 ? 20.616 0.868   -4.326  0.62 10.79 ?  132 PHE   A CD1  1 
ATOM   2772 C CD1  B PHE   A 1 132 ? 20.116 0.640   -4.058  0.38 11.06 ?  132 PHE   A CD1  1 
ATOM   2773 C CD2  A PHE   A 1 132 ? 21.981 -0.733  -5.446  0.62 10.17 ?  132 PHE   A CD2  1 
ATOM   2774 C CD2  B PHE   A 1 132 ? 21.566 -0.707  -5.384  0.38 11.12 ?  132 PHE   A CD2  1 
ATOM   2775 C CE1  A PHE   A 1 132 ? 21.746 1.384   -3.694  0.62 11.34 ?  132 PHE   A CE1  1 
ATOM   2776 C CE1  B PHE   A 1 132 ? 21.207 1.143   -3.375  0.38 11.47 ?  132 PHE   A CE1  1 
ATOM   2777 C CE2  A PHE   A 1 132 ? 23.117 -0.217  -4.817  0.62 10.74 ?  132 PHE   A CE2  1 
ATOM   2778 C CE2  B PHE   A 1 132 ? 22.662 -0.210  -4.698  0.38 11.55 ?  132 PHE   A CE2  1 
ATOM   2779 C CZ   A PHE   A 1 132 ? 22.993 0.846   -3.944  0.62 11.03 ?  132 PHE   A CZ   1 
ATOM   2780 C CZ   B PHE   A 1 132 ? 22.481 0.721   -3.694  0.38 11.38 ?  132 PHE   A CZ   1 
ATOM   2781 H H    A PHE   A 1 132 ? 17.623 0.692   -5.146  0.62 11.89 ?  132 PHE   A H    1 
ATOM   2782 H H    B PHE   A 1 132 ? 17.192 0.692   -5.269  0.38 12.88 ?  132 PHE   A H    1 
ATOM   2783 H HA   A PHE   A 1 132 ? 19.318 0.773   -7.192  0.62 12.41 ?  132 PHE   A HA   1 
ATOM   2784 H HA   B PHE   A 1 132 ? 19.101 0.728   -7.119  0.38 13.29 ?  132 PHE   A HA   1 
ATOM   2785 H HB2  A PHE   A 1 132 ? 18.922 -1.128  -5.184  0.62 11.26 ?  132 PHE   A HB2  1 
ATOM   2786 H HB2  B PHE   A 1 132 ? 18.449 -1.129  -5.140  0.38 13.10 ?  132 PHE   A HB2  1 
ATOM   2787 H HB3  A PHE   A 1 132 ? 19.793 -1.519  -6.451  0.62 11.26 ?  132 PHE   A HB3  1 
ATOM   2788 H HB3  B PHE   A 1 132 ? 19.392 -1.592  -6.329  0.38 13.10 ?  132 PHE   A HB3  1 
ATOM   2789 H HD1  A PHE   A 1 132 ? 19.787 1.239   -4.148  0.62 12.96 ?  132 PHE   A HD1  1 
ATOM   2790 H HD1  B PHE   A 1 132 ? 19.261 0.930   -3.838  0.38 13.29 ?  132 PHE   A HD1  1 
ATOM   2791 H HD2  A PHE   A 1 132 ? 22.074 -1.451  -6.034  0.62 12.22 ?  132 PHE   A HD2  1 
ATOM   2792 H HD2  B PHE   A 1 132 ? 21.694 -1.335  -6.060  0.38 13.36 ?  132 PHE   A HD2  1 
ATOM   2793 H HE1  A PHE   A 1 132 ? 21.665 2.102   -3.106  0.62 13.62 ?  132 PHE   A HE1  1 
ATOM   2794 H HE1  B PHE   A 1 132 ? 21.081 1.766   -2.699  0.38 13.78 ?  132 PHE   A HE1  1 
ATOM   2795 H HE2  A PHE   A 1 132 ? 23.954 -0.589  -4.993  0.62 12.90 ?  132 PHE   A HE2  1 
ATOM   2796 H HE2  B PHE   A 1 132 ? 23.521 -0.499  -4.919  0.38 13.87 ?  132 PHE   A HE2  1 
ATOM   2797 H HZ   A PHE   A 1 132 ? 23.750 1.195   -3.525  0.62 13.25 ?  132 PHE   A HZ   1 
ATOM   2798 H HZ   B PHE   A 1 132 ? 23.213 1.059   -3.232  0.38 13.67 ?  132 PHE   A HZ   1 
ATOM   2799 N N    A GLY   A 1 133 ? 16.573 -0.512  -7.811  0.62 11.13 ?  133 GLY   A N    1 
ATOM   2800 N N    B GLY   A 1 133 ? 16.419 -0.645  -7.939  0.38 11.99 ?  133 GLY   A N    1 
ATOM   2801 C CA   A GLY   A 1 133 ? 15.783 -0.855  -8.977  0.62 11.44 ?  133 GLY   A CA   1 
ATOM   2802 C CA   B GLY   A 1 133 ? 15.715 -1.025  -9.146  0.38 12.34 ?  133 GLY   A CA   1 
ATOM   2803 C C    A GLY   A 1 133 ? 15.381 -2.308  -9.148  0.62 11.59 ?  133 GLY   A C    1 
ATOM   2804 C C    B GLY   A 1 133 ? 15.472 -2.504  -9.377  0.38 12.79 ?  133 GLY   A C    1 
ATOM   2805 O O    A GLY   A 1 133 ? 14.656 -2.607  -10.105 0.62 12.73 ?  133 GLY   A O    1 
ATOM   2806 O O    B GLY   A 1 133 ? 14.932 -2.854  -10.435 0.38 13.53 ?  133 GLY   A O    1 
ATOM   2807 H H    A GLY   A 1 133 ? 16.105 -0.270  -7.131  0.62 13.37 ?  133 GLY   A H    1 
ATOM   2808 H H    B GLY   A 1 133 ? 15.906 -0.463  -7.272  0.38 14.41 ?  133 GLY   A H    1 
ATOM   2809 H HA2  A GLY   A 1 133 ? 14.965 -0.338  -8.953  0.62 13.75 ?  133 GLY   A HA2  1 
ATOM   2810 H HA2  B GLY   A 1 133 ? 14.859 -0.577  -9.149  0.38 14.82 ?  133 GLY   A HA2  1 
ATOM   2811 H HA3  A GLY   A 1 133 ? 16.274 -0.589  -9.773  0.62 13.75 ?  133 GLY   A HA3  1 
ATOM   2812 H HA3  B GLY   A 1 133 ? 16.224 -0.698  -9.905  0.38 14.82 ?  133 GLY   A HA3  1 
ATOM   2813 N N    A ALA   A 1 134 ? 15.811 -3.217  -8.276  0.62 11.47 ?  134 ALA   A N    1 
ATOM   2814 N N    B ALA   A 1 134 ? 15.845 -3.385  -8.452  0.38 12.80 ?  134 ALA   A N    1 
ATOM   2815 C CA   A ALA   A 1 134 ? 15.447 -4.619  -8.432  0.62 12.06 ?  134 ALA   A CA   1 
ATOM   2816 C CA   B ALA   A 1 134 ? 15.590 -4.805  -8.656  0.38 12.73 ?  134 ALA   A CA   1 
ATOM   2817 C C    A ALA   A 1 134 ? 14.095 -4.904  -7.784  0.62 12.15 ?  134 ALA   A C    1 
ATOM   2818 C C    B ALA   A 1 134 ? 14.232 -5.209  -8.077  0.38 12.42 ?  134 ALA   A C    1 
ATOM   2819 O O    A ALA   A 1 134 ? 13.586 -4.120  -6.980  0.62 13.14 ?  134 ALA   A O    1 
ATOM   2820 O O    B ALA   A 1 134 ? 13.604 -4.471  -7.315  0.38 13.10 ?  134 ALA   A O    1 
ATOM   2821 C CB   A ALA   A 1 134 ? 16.509 -5.539  -7.828  0.62 12.71 ?  134 ALA   A CB   1 
ATOM   2822 C CB   B ALA   A 1 134 ? 16.704 -5.657  -8.047  0.38 13.30 ?  134 ALA   A CB   1 
ATOM   2823 H H    A ALA   A 1 134 ? 16.310 -3.046  -7.596  0.62 13.78 ?  134 ALA   A H    1 
ATOM   2824 H H    B ALA   A 1 134 ? 16.253 -3.189  -7.716  0.38 15.37 ?  134 ALA   A H    1 
ATOM   2825 H HA   A ALA   A 1 134 ? 15.375 -4.822  -9.378  0.62 14.49 ?  134 ALA   A HA   1 
ATOM   2826 H HA   B ALA   A 1 134 ? 15.576 -4.980  -9.609  0.38 15.29 ?  134 ALA   A HA   1 
ATOM   2827 H HB1  A ALA   A 1 134 ? 16.239 -6.458  -7.962  0.62 15.27 ?  134 ALA   A HB1  1 
ATOM   2828 H HB1  B ALA   A 1 134 ? 16.539 -6.586  -8.269  0.38 15.98 ?  134 ALA   A HB1  1 
ATOM   2829 H HB2  A ALA   A 1 134 ? 17.355 -5.370  -8.274  0.62 15.27 ?  134 ALA   A HB2  1 
ATOM   2830 H HB2  B ALA   A 1 134 ? 17.555 -5.374  -8.418  0.38 15.98 ?  134 ALA   A HB2  1 
ATOM   2831 H HB3  A ALA   A 1 134 ? 16.588 -5.345  -6.882  0.62 15.27 ?  134 ALA   A HB3  1 
ATOM   2832 H HB3  B ALA   A 1 134 ? 16.704 -5.539  -7.087  0.38 15.98 ?  134 ALA   A HB3  1 
ATOM   2833 N N    A ASP   A 1 135 ? 13.518 -6.048  -8.154  0.62 12.53 ?  135 ASP   A N    1 
ATOM   2834 N N    B ASP   A 1 135 ? 13.785 -6.406  -8.455  0.38 12.40 ?  135 ASP   A N    1 
ATOM   2835 C CA   A ASP   A 1 135 ? 12.266 -6.516  -7.568  0.62 13.61 ?  135 ASP   A CA   1 
ATOM   2836 C CA   B ASP   A 1 135 ? 12.531 -6.963  -7.955  0.38 12.45 ?  135 ASP   A CA   1 
ATOM   2837 C C    A ASP   A 1 135 ? 12.524 -6.973  -6.137  0.62 13.12 ?  135 ASP   A C    1 
ATOM   2838 C C    B ASP   A 1 135 ? 12.700 -7.319  -6.484  0.38 11.84 ?  135 ASP   A C    1 
ATOM   2839 O O    A ASP   A 1 135 ? 13.290 -7.924  -5.932  0.62 12.77 ?  135 ASP   A O    1 
ATOM   2840 O O    B ASP   A 1 135 ? 13.554 -8.153  -6.155  0.38 12.09 ?  135 ASP   A O    1 
ATOM   2841 C CB   A ASP   A 1 135 ? 11.747 -7.680  -8.407  0.62 16.30 ?  135 ASP   A CB   1 
ATOM   2842 C CB   B ASP   A 1 135 ? 12.188 -8.215  -8.763  0.38 14.10 ?  135 ASP   A CB   1 
ATOM   2843 C CG   A ASP   A 1 135 ? 10.416 -8.222  -7.908  0.62 19.13 ?  135 ASP   A CG   1 
ATOM   2844 C CG   B ASP   A 1 135 ? 10.936 -8.925  -8.264  0.38 15.70 ?  135 ASP   A CG   1 
ATOM   2845 O OD1  A ASP   A 1 135 ? 9.934  -7.766  -6.846  0.62 19.29 ?  135 ASP   A OD1  1 
ATOM   2846 O OD1  B ASP   A 1 135 ? 10.319 -8.475  -7.275  0.38 15.78 ?  135 ASP   A OD1  1 
ATOM   2847 O OD2  A ASP   A 1 135 ? 9.843  -9.100  -8.591  0.62 21.48 -1 135 ASP   A OD2  1 
ATOM   2848 O OD2  B ASP   A 1 135 ? 10.579 -9.958  -8.866  0.38 17.43 -1 135 ASP   A OD2  1 
ATOM   2849 H H    A ASP   A 1 135 ? 13.830 -6.571  -8.758  0.62 15.05 ?  135 ASP   A H    1 
ATOM   2850 H H    B ASP   A 1 135 ? 14.201 -6.921  -9.006  0.38 14.90 ?  135 ASP   A H    1 
ATOM   2851 H HA   A ASP   A 1 135 ? 11.602 -5.803  -7.585  0.62 16.35 ?  135 ASP   A HA   1 
ATOM   2852 H HA   B ASP   A 1 135 ? 11.820 -6.315  -8.066  0.38 14.96 ?  135 ASP   A HA   1 
ATOM   2853 H HB2  A ASP   A 1 135 ? 11.620 -7.378  -9.321  0.62 19.57 ?  135 ASP   A HB2  1 
ATOM   2854 H HB2  B ASP   A 1 135 ? 12.065 -7.964  -9.694  0.38 16.94 ?  135 ASP   A HB2  1 
ATOM   2855 H HB3  A ASP   A 1 135 ? 12.409 -8.393  -8.389  0.62 19.57 ?  135 ASP   A HB3  1 
ATOM   2856 H HB3  B ASP   A 1 135 ? 12.915 -8.849  -8.685  0.38 16.94 ?  135 ASP   A HB3  1 
ATOM   2857 N N    A PRO   A 1 136 ? 11.927 -6.335  -5.125  0.62 12.64 ?  136 PRO   A N    1 
ATOM   2858 N N    B PRO   A 1 136 ? 11.927 -6.724  -5.572  0.38 11.65 ?  136 PRO   A N    1 
ATOM   2859 C CA   A PRO   A 1 136 ? 12.205 -6.747  -3.737  0.62 12.56 ?  136 PRO   A CA   1 
ATOM   2860 C CA   B PRO   A 1 136 ? 12.122 -7.035  -4.146  0.38 11.42 ?  136 PRO   A CA   1 
ATOM   2861 C C    A PRO   A 1 136 ? 11.773 -8.169  -3.414  0.62 11.52 ?  136 PRO   A C    1 
ATOM   2862 C C    B PRO   A 1 136 ? 11.743 -8.458  -3.768  0.38 11.09 ?  136 PRO   A C    1 
ATOM   2863 O O    A PRO   A 1 136 ? 12.367 -8.798  -2.530  0.62 11.09 ?  136 PRO   A O    1 
ATOM   2864 O O    B PRO   A 1 136 ? 12.370 -9.026  -2.867  0.38 11.23 ?  136 PRO   A O    1 
ATOM   2865 C CB   A PRO   A 1 136 ? 11.449 -5.703  -2.901  0.62 13.44 ?  136 PRO   A CB   1 
ATOM   2866 C CB   B PRO   A 1 136 ? 11.252 -5.990  -3.435  0.38 11.89 ?  136 PRO   A CB   1 
ATOM   2867 C CG   A PRO   A 1 136 ? 10.405 -5.163  -3.822  0.62 14.58 ?  136 PRO   A CG   1 
ATOM   2868 C CG   B PRO   A 1 136 ? 10.220 -5.603  -4.451  0.38 12.02 ?  136 PRO   A CG   1 
ATOM   2869 C CD   A PRO   A 1 136 ? 10.986 -5.203  -5.195  0.62 13.84 ?  136 PRO   A CD   1 
ATOM   2870 C CD   B PRO   A 1 136 ? 10.906 -5.682  -5.782  0.38 12.17 ?  136 PRO   A CD   1 
ATOM   2871 H HA   A PRO   A 1 136 ? 13.153 -6.660  -3.551  0.62 15.09 ?  136 PRO   A HA   1 
ATOM   2872 H HA   B PRO   A 1 136 ? 13.051 -6.890  -3.901  0.38 13.72 ?  136 PRO   A HA   1 
ATOM   2873 H HB2  A PRO   A 1 136 ? 11.039 -6.129  -2.133  0.62 16.15 ?  136 PRO   A HB2  1 
ATOM   2874 H HB2  B PRO   A 1 136 ? 10.838 -6.389  -2.655  0.38 14.29 ?  136 PRO   A HB2  1 
ATOM   2875 H HB3  A PRO   A 1 136 ? 12.057 -4.999  -2.622  0.62 16.15 ?  136 PRO   A HB3  1 
ATOM   2876 H HB3  B PRO   A 1 136 ? 11.799 -5.228  -3.185  0.38 14.29 ?  136 PRO   A HB3  1 
ATOM   2877 H HG2  A PRO   A 1 136 ? 9.615  -5.722  -3.779  0.62 17.51 ?  136 PRO   A HG2  1 
ATOM   2878 H HG2  B PRO   A 1 136 ? 9.480  -6.225  -4.416  0.38 14.44 ?  136 PRO   A HG2  1 
ATOM   2879 H HG3  A PRO   A 1 136 ? 10.192 -4.251  -3.575  0.62 17.51 ?  136 PRO   A HG3  1 
ATOM   2880 H HG3  B PRO   A 1 136 ? 9.921  -4.698  -4.280  0.38 14.44 ?  136 PRO   A HG3  1 
ATOM   2881 H HD2  A PRO   A 1 136 ? 10.290 -5.384  -5.852  0.62 16.62 ?  136 PRO   A HD2  1 
ATOM   2882 H HD2  B PRO   A 1 136 ? 10.284 -5.960  -6.474  0.38 14.62 ?  136 PRO   A HD2  1 
ATOM   2883 H HD3  A PRO   A 1 136 ? 11.454 -4.377  -5.396  0.62 16.62 ?  136 PRO   A HD3  1 
ATOM   2884 H HD3  B PRO   A 1 136 ? 11.329 -4.835  -6.006  0.38 14.62 ?  136 PRO   A HD3  1 
ATOM   2885 N N    A ILE   A 1 137 ? 10.743 -8.690  -4.084  0.62 11.93 ?  137 ILE   A N    1 
ATOM   2886 N N    B ILE   A 1 137 ? 10.734 -9.049  -4.413  0.38 10.74 ?  137 ILE   A N    1 
ATOM   2887 C CA   A ILE   A 1 137 ? 10.356 -10.084 -3.884  0.62 11.90 ?  137 ILE   A CA   1 
ATOM   2888 C CA   B ILE   A 1 137 ? 10.402 -10.448 -4.151  0.38 11.04 ?  137 ILE   A CA   1 
ATOM   2889 C C    A ILE   A 1 137 ? 11.503 -11.002 -4.284  0.62 11.44 ?  137 ILE   A C    1 
ATOM   2890 C C    B ILE   A 1 137 ? 11.591 -11.337 -4.484  0.38 11.13 ?  137 ILE   A C    1 
ATOM   2891 O O    A ILE   A 1 137 ? 11.810 -11.980 -3.593  0.62 11.64 ?  137 ILE   A O    1 
ATOM   2892 O O    B ILE   A 1 137 ? 11.928 -12.263 -3.734  0.38 11.72 ?  137 ILE   A O    1 
ATOM   2893 C CB   A ILE   A 1 137 ? 9.055  -10.392 -4.656  0.62 12.68 ?  137 ILE   A CB   1 
ATOM   2894 C CB   B ILE   A 1 137 ? 9.140  -10.857 -4.936  0.38 11.93 ?  137 ILE   A CB   1 
ATOM   2895 C CG1  A ILE   A 1 137 ? 7.904  -9.519  -4.141  0.62 14.49 ?  137 ILE   A CG1  1 
ATOM   2896 C CG1  B ILE   A 1 137 ? 7.899  -10.130 -4.405  0.38 12.38 ?  137 ILE   A CG1  1 
ATOM   2897 C CG2  A ILE   A 1 137 ? 8.690  -11.873 -4.547  0.62 13.01 ?  137 ILE   A CG2  1 
ATOM   2898 C CG2  B ILE   A 1 137 ? 8.944  -12.367 -4.875  0.38 12.28 ?  137 ILE   A CG2  1 
ATOM   2899 C CD1  A ILE   A 1 137 ? 6.614  -9.701  -4.904  0.62 16.12 ?  137 ILE   A CD1  1 
ATOM   2900 C CD1  B ILE   A 1 137 ? 6.669  -10.299 -5.278  0.38 13.06 ?  137 ILE   A CD1  1 
ATOM   2901 H H    A ILE   A 1 137 ? 10.258 -8.260  -4.652  0.62 14.34 ?  137 ILE   A H    1 
ATOM   2902 H H    B ILE   A 1 137 ? 10.233 -8.667  -4.999  0.38 12.90 ?  137 ILE   A H    1 
ATOM   2903 H HA   A ILE   A 1 137 ? 10.180 -10.225 -2.944  0.62 14.30 ?  137 ILE   A HA   1 
ATOM   2904 H HA   B ILE   A 1 137 ? 10.212 -10.555 -3.209  0.38 13.27 ?  137 ILE   A HA   1 
ATOM   2905 H HB   A ILE   A 1 137 ? 9.195  -10.181 -5.591  0.62 15.24 ?  137 ILE   A HB   1 
ATOM   2906 H HB   B ILE   A 1 137 ? 9.260  -10.608 -5.864  0.38 14.34 ?  137 ILE   A HB   1 
ATOM   2907 H HG12 A ILE   A 1 137 ? 7.736  -9.731  -3.211  0.62 17.41 ?  137 ILE   A HG12 1 
ATOM   2908 H HG12 B ILE   A 1 137 ? 7.683  -10.476 -3.525  0.38 14.87 ?  137 ILE   A HG12 1 
ATOM   2909 H HG13 A ILE   A 1 137 ? 8.161  -8.581  -4.220  0.62 17.41 ?  137 ILE   A HG13 1 
ATOM   2910 H HG13 B ILE   A 1 137 ? 8.092  -9.183  -4.349  0.38 14.87 ?  137 ILE   A HG13 1 
ATOM   2911 H HG21 A ILE   A 1 137 ? 7.860  -12.042 -5.022  0.62 15.62 ?  137 ILE   A HG21 1 
ATOM   2912 H HG21 B ILE   A 1 137 ? 8.046  -12.590 -5.170  0.38 14.75 ?  137 ILE   A HG21 1 
ATOM   2913 H HG22 A ILE   A 1 137 ? 9.396  -12.401 -4.941  0.62 15.62 ?  137 ILE   A HG22 1 
ATOM   2914 H HG22 B ILE   A 1 137 ? 9.589  -12.795 -5.459  0.38 14.75 ?  137 ILE   A HG22 1 
ATOM   2915 H HG23 A ILE   A 1 137 ? 8.583  -12.099 -3.612  0.62 15.62 ?  137 ILE   A HG23 1 
ATOM   2916 H HG23 B ILE   A 1 137 ? 9.071  -12.666 -3.962  0.38 14.75 ?  137 ILE   A HG23 1 
ATOM   2917 H HD11 A ILE   A 1 137 ? 5.920  -9.990  -4.290  0.62 19.36 ?  137 ILE   A HD11 1 
ATOM   2918 H HD11 B ILE   A 1 137 ? 5.985  -9.686  -4.977  0.38 15.69 ?  137 ILE   A HD11 1 
ATOM   2919 H HD12 A ILE   A 1 137 ? 6.377  -8.852  -5.302  0.62 19.36 ?  137 ILE   A HD12 1 
ATOM   2920 H HD12 B ILE   A 1 137 ? 6.909  -10.103 -6.199  0.38 15.69 ?  137 ILE   A HD12 1 
ATOM   2921 H HD13 A ILE   A 1 137 ? 6.738  -10.360 -5.603  0.62 19.36 ?  137 ILE   A HD13 1 
ATOM   2922 H HD13 B ILE   A 1 137 ? 6.350  -11.212 -5.209  0.38 15.69 ?  137 ILE   A HD13 1 
ATOM   2923 N N    A HIS   A 1 138 ? 12.161 -10.686 -5.401  0.62 11.72 ?  138 HIS   A N    1 
ATOM   2924 N N    B HIS   A 1 138 ? 12.250 -11.065 -5.612  0.38 11.18 ?  138 HIS   A N    1 
ATOM   2925 C CA   A HIS   A 1 138 ? 13.337 -11.440 -5.824  0.62 11.45 ?  138 HIS   A CA   1 
ATOM   2926 C CA   B HIS   A 1 138 ? 13.417 -11.848 -5.997  0.38 11.79 ?  138 HIS   A CA   1 
ATOM   2927 C C    A HIS   A 1 138 ? 14.478 -11.296 -4.821  0.62 10.70 ?  138 HIS   A C    1 
ATOM   2928 C C    B HIS   A 1 138 ? 14.548 -11.680 -4.993  0.38 11.42 ?  138 HIS   A C    1 
ATOM   2929 O O    A HIS   A 1 138 ? 15.140 -12.280 -4.473  0.62 10.63 ?  138 HIS   A O    1 
ATOM   2930 O O    B HIS   A 1 138 ? 15.212 -12.657 -4.627  0.38 12.07 ?  138 HIS   A O    1 
ATOM   2931 C CB   A HIS   A 1 138 ? 13.759 -10.973 -7.218  0.62 11.98 ?  138 HIS   A CB   1 
ATOM   2932 C CB   B HIS   A 1 138 ? 13.871 -11.445 -7.399  0.38 12.45 ?  138 HIS   A CB   1 
ATOM   2933 C CG   A HIS   A 1 138 ? 15.026 -11.598 -7.706  0.62 12.81 ?  138 HIS   A CG   1 
ATOM   2934 C CG   B HIS   A 1 138 ? 15.174 -12.057 -7.804  0.38 12.94 ?  138 HIS   A CG   1 
ATOM   2935 N ND1  A HIS   A 1 138 ? 15.147 -12.949 -7.944  0.62 14.14 ?  138 HIS   A ND1  1 
ATOM   2936 N ND1  B HIS   A 1 138 ? 15.317 -13.405 -8.051  0.38 13.70 ?  138 HIS   A ND1  1 
ATOM   2937 C CD2  A HIS   A 1 138 ? 16.231 -11.054 -7.996  0.62 13.16 ?  138 HIS   A CD2  1 
ATOM   2938 C CD2  B HIS   A 1 138 ? 16.397 -11.507 -7.990  0.38 13.24 ?  138 HIS   A CD2  1 
ATOM   2939 C CE1  A HIS   A 1 138 ? 16.374 -13.211 -8.363  0.62 14.38 ?  138 HIS   A CE1  1 
ATOM   2940 C CE1  B HIS   A 1 138 ? 16.571 -13.658 -8.382  0.38 14.22 ?  138 HIS   A CE1  1 
ATOM   2941 N NE2  A HIS   A 1 138 ? 17.051 -12.077 -8.403  0.62 13.73 ?  138 HIS   A NE2  1 
ATOM   2942 N NE2  B HIS   A 1 138 ? 17.247 -12.524 -8.351  0.38 13.83 ?  138 HIS   A NE2  1 
ATOM   2943 H H    A HIS   A 1 138 ? 11.946 -10.038 -5.932  0.62 14.08 ?  138 HIS   A H    1 
ATOM   2944 H H    B HIS   A 1 138 ? 12.048 -10.430 -6.161  0.38 13.44 ?  138 HIS   A H    1 
ATOM   2945 H HA   A HIS   A 1 138 ? 13.102 -12.378 -5.887  0.62 13.76 ?  138 HIS   A HA   1 
ATOM   2946 H HA   B HIS   A 1 138 ? 13.173 -12.784 -6.023  0.38 14.17 ?  138 HIS   A HA   1 
ATOM   2947 H HB2  A HIS   A 1 138 ? 13.057 -11.194 -7.853  0.62 14.39 ?  138 HIS   A HB2  1 
ATOM   2948 H HB2  B HIS   A 1 138 ? 13.199 -11.727 -8.041  0.38 14.95 ?  138 HIS   A HB2  1 
ATOM   2949 H HB3  A HIS   A 1 138 ? 13.892 -10.011 -7.203  0.62 14.39 ?  138 HIS   A HB3  1 
ATOM   2950 H HB3  B HIS   A 1 138 ? 13.974 -10.481 -7.433  0.38 14.95 ?  138 HIS   A HB3  1 
ATOM   2951 H HD1  A HIS   A 1 138 ? 14.521 -13.531 -7.837  0.62 16.99 ?  138 HIS   A HD1  1 
ATOM   2952 H HD1  B HIS   A 1 138 ? 14.687 -13.989 -8.004  0.38 16.46 ?  138 HIS   A HD1  1 
ATOM   2953 H HD2  A HIS   A 1 138 ? 16.460 -10.156 -7.936  0.62 15.81 ?  138 HIS   A HD2  1 
ATOM   2954 H HD2  B HIS   A 1 138 ? 16.616 -10.608 -7.895  0.38 15.91 ?  138 HIS   A HD2  1 
ATOM   2955 H HE1  A HIS   A 1 138 ? 16.702 -14.053 -8.588  0.62 17.27 ?  138 HIS   A HE1  1 
ATOM   2956 H HE1  B HIS   A 1 138 ? 16.915 -14.490 -8.597  0.38 17.09 ?  138 HIS   A HE1  1 
ATOM   2957 N N    A SER   A 1 139 ? 14.723 -10.074 -4.341  0.62 9.92  ?  139 SER   A N    1 
ATOM   2958 N N    B SER   A 1 139 ? 14.786 -10.450 -4.534  0.38 10.52 ?  139 SER   A N    1 
ATOM   2959 C CA   A SER   A 1 139 ? 15.787 -9.871  -3.364  0.62 10.15 ?  139 SER   A CA   1 
ATOM   2960 C CA   B SER   A 1 139 ? 15.869 -10.231 -3.582  0.38 9.99  ?  139 SER   A CA   1 
ATOM   2961 C C    A SER   A 1 139 ? 15.568 -10.713 -2.112  0.62 10.15 ?  139 SER   A C    1 
ATOM   2962 C C    B SER   A 1 139 ? 15.639 -11.007 -2.289  0.38 9.97  ?  139 SER   A C    1 
ATOM   2963 O O    A SER   A 1 139 ? 16.523 -11.291 -1.572  0.62 10.59 ?  139 SER   A O    1 
ATOM   2964 O O    B SER   A 1 139 ? 16.581 -11.585 -1.730  0.38 9.48  ?  139 SER   A O    1 
ATOM   2965 C CB   A SER   A 1 139 ? 15.905 -8.391  -3.005  0.62 10.16 ?  139 SER   A CB   1 
ATOM   2966 C CB   B SER   A 1 139 ? 16.038 -8.741  -3.294  0.38 9.07  ?  139 SER   A CB   1 
ATOM   2967 O OG   A SER   A 1 139 ? 16.952 -8.187  -2.063  0.62 10.60 ?  139 SER   A OG   1 
ATOM   2968 O OG   B SER   A 1 139 ? 17.106 -8.554  -2.379  0.38 8.55  ?  139 SER   A OG   1 
ATOM   2969 H H    A SER   A 1 139 ? 14.297 -9.364  -4.564  0.62 11.92 ?  139 SER   A H    1 
ATOM   2970 H H    B SER   A 1 139 ? 14.347 -9.743  -4.756  0.38 12.64 ?  139 SER   A H    1 
ATOM   2971 H HA   A SER   A 1 139 ? 16.629 -10.149 -3.756  0.62 12.19 ?  139 SER   A HA   1 
ATOM   2972 H HA   B SER   A 1 139 ? 16.697 -10.546 -3.977  0.38 12.00 ?  139 SER   A HA   1 
ATOM   2973 H HB2  A SER   A 1 139 ? 16.101 -7.885  -3.811  0.62 12.21 ?  139 SER   A HB2  1 
ATOM   2974 H HB2  B SER   A 1 139 ? 16.234 -8.271  -4.126  0.38 10.90 ?  139 SER   A HB2  1 
ATOM   2975 H HB3  A SER   A 1 139 ? 15.068 -8.089  -2.620  0.62 12.21 ?  139 SER   A HB3  1 
ATOM   2976 H HB3  B SER   A 1 139 ? 15.222 -8.392  -2.903  0.38 10.90 ?  139 SER   A HB3  1 
ATOM   2977 H HG   A SER   A 1 139 ? 17.011 -7.367  -1.872  0.62 12.73 ?  139 SER   A HG   1 
ATOM   2978 H HG   B SER   A 1 139 ? 17.211 -7.734  -2.228  0.38 10.28 ?  139 SER   A HG   1 
ATOM   2979 N N    A LEU   A 1 140 ? 14.324 -10.787 -1.628  0.62 9.90  ?  140 LEU   A N    1 
ATOM   2980 N N    B LEU   A 1 140 ? 14.398 -11.017 -1.790  0.38 10.27 ?  140 LEU   A N    1 
ATOM   2981 C CA   A LEU   A 1 140 ? 14.055 -11.591 -0.441  0.62 9.82  ?  140 LEU   A CA   1 
ATOM   2982 C CA   B LEU   A 1 140 ? 14.096 -11.780 -0.582  0.38 10.59 ?  140 LEU   A CA   1 
ATOM   2983 C C    A LEU   A 1 140 ? 14.344 -13.068 -0.706  0.62 10.21 ?  140 LEU   A C    1 
ATOM   2984 C C    B LEU   A 1 140 ? 14.325 -13.269 -0.812  0.38 10.45 ?  140 LEU   A C    1 
ATOM   2985 O O    A LEU   A 1 140 ? 14.904 -13.769 0.150   0.62 11.18 ?  140 LEU   A O    1 
ATOM   2986 O O    B LEU   A 1 140 ? 14.862 -13.967 0.058   0.38 10.74 ?  140 LEU   A O    1 
ATOM   2987 C CB   A LEU   A 1 140 ? 12.613 -11.376 0.023   0.62 10.36 ?  140 LEU   A CB   1 
ATOM   2988 C CB   B LEU   A 1 140 ? 12.658 -11.500 -0.131  0.38 10.91 ?  140 LEU   A CB   1 
ATOM   2989 C CG   A LEU   A 1 140 ? 12.184 -12.294 1.170   0.62 11.16 ?  140 LEU   A CG   1 
ATOM   2990 C CG   B LEU   A 1 140 ? 12.161 -12.079 1.205   0.38 10.23 ?  140 LEU   A CG   1 
ATOM   2991 C CD1  A LEU   A 1 140 ? 13.090 -12.139 2.387   0.62 11.22 ?  140 LEU   A CD1  1 
ATOM   2992 C CD1  B LEU   A 1 140 ? 13.079 -11.735 2.371   0.38 10.13 ?  140 LEU   A CD1  1 
ATOM   2993 C CD2  A LEU   A 1 140 ? 10.727 -12.040 1.524   0.62 11.77 ?  140 LEU   A CD2  1 
ATOM   2994 C CD2  B LEU   A 1 140 ? 10.726 -11.622 1.500   0.38 10.25 ?  140 LEU   A CD2  1 
ATOM   2995 H H    A LEU   A 1 140 ? 13.635 -10.389 -1.961  0.62 11.89 ?  140 LEU   A H    1 
ATOM   2996 H H    B LEU   A 1 140 ? 13.730 -10.598 -2.127  0.38 12.34 ?  140 LEU   A H    1 
ATOM   2997 H HA   A LEU   A 1 140 ? 14.638 -11.297 0.273   0.62 11.80 ?  140 LEU   A HA   1 
ATOM   2998 H HA   B LEU   A 1 140 ? 14.694 -11.496 0.124   0.38 12.73 ?  140 LEU   A HA   1 
ATOM   2999 H HB2  A LEU   A 1 140 ? 12.511 -10.460 0.323   0.62 12.45 ?  140 LEU   A HB2  1 
ATOM   3000 H HB2  B LEU   A 1 140 ? 12.551 -10.543 -0.074  0.38 13.11 ?  140 LEU   A HB2  1 
ATOM   3001 H HB3  A LEU   A 1 140 ? 12.014 -11.543 -0.725  0.62 12.45 ?  140 LEU   A HB3  1 
ATOM   3002 H HB3  B LEU   A 1 140 ? 12.065 -11.846 -0.816  0.38 13.11 ?  140 LEU   A HB3  1 
ATOM   3003 H HG   A LEU   A 1 140 ? 12.248 -13.215 0.874   0.62 13.41 ?  140 LEU   A HG   1 
ATOM   3004 H HG   B LEU   A 1 140 ? 12.140 -13.045 1.132   0.38 12.29 ?  140 LEU   A HG   1 
ATOM   3005 H HD11 A LEU   A 1 140 ? 12.734 -12.669 3.115   0.62 13.48 ?  140 LEU   A HD11 1 
ATOM   3006 H HD11 B LEU   A 1 140 ? 12.687 -12.076 3.191   0.38 12.17 ?  140 LEU   A HD11 1 
ATOM   3007 H HD12 A LEU   A 1 140 ? 13.983 -12.450 2.161   0.62 13.48 ?  140 LEU   A HD12 1 
ATOM   3008 H HD12 B LEU   A 1 140 ? 13.943 -12.147 2.221   0.38 12.17 ?  140 LEU   A HD12 1 
ATOM   3009 H HD13 A LEU   A 1 140 ? 13.123 -11.204 2.642   0.62 13.48 ?  140 LEU   A HD13 1 
ATOM   3010 H HD13 B LEU   A 1 140 ? 13.173 -10.772 2.425   0.38 12.17 ?  140 LEU   A HD13 1 
ATOM   3011 H HD21 A LEU   A 1 140 ? 10.472 -12.628 2.250   0.62 14.14 ?  140 LEU   A HD21 1 
ATOM   3012 H HD21 B LEU   A 1 140 ? 10.439 -12.003 2.348   0.38 12.31 ?  140 LEU   A HD21 1 
ATOM   3013 H HD22 A LEU   A 1 140 ? 10.624 -11.114 1.792   0.62 14.14 ?  140 LEU   A HD22 1 
ATOM   3014 H HD22 B LEU   A 1 140 ? 10.702 -10.654 1.550   0.38 12.31 ?  140 LEU   A HD22 1 
ATOM   3015 H HD23 A LEU   A 1 140 ? 10.178 -12.221 0.743   0.62 14.14 ?  140 LEU   A HD23 1 
ATOM   3016 H HD23 B LEU   A 1 140 ? 10.141 -11.932 0.789   0.38 12.31 ?  140 LEU   A HD23 1 
ATOM   3017 N N    A ARG   A 1 141 ? 13.968 -13.555 -1.891  0.62 10.85 ?  141 ARG   A N    1 
ATOM   3018 N N    B ARG   A 1 141 ? 13.927 -13.774 -1.984  0.38 10.70 ?  141 ARG   A N    1 
ATOM   3019 C CA   A ARG   A 1 141 ? 14.189 -14.956 -2.242  0.62 11.99 ?  141 ARG   A CA   1 
ATOM   3020 C CA   B ARG   A 1 141 ? 14.221 -15.162 -2.318  0.38 11.46 ?  141 ARG   A CA   1 
ATOM   3021 C C    A ARG   A 1 141 ? 15.681 -15.292 -2.245  0.62 11.60 ?  141 ARG   A C    1 
ATOM   3022 C C    B ARG   A 1 141 ? 15.722 -15.403 -2.346  0.38 11.16 ?  141 ARG   A C    1 
ATOM   3023 O O    A ARG   A 1 141 ? 16.116 -16.270 -1.625  0.62 11.92 ?  141 ARG   A O    1 
ATOM   3024 O O    B ARG   A 1 141 ? 16.205 -16.421 -1.837  0.38 10.87 ?  141 ARG   A O    1 
ATOM   3025 C CB   A ARG   A 1 141 ? 13.561 -15.205 -3.618  0.62 13.37 ?  141 ARG   A CB   1 
ATOM   3026 C CB   B ARG   A 1 141 ? 13.616 -15.512 -3.675  0.38 12.68 ?  141 ARG   A CB   1 
ATOM   3027 C CG   A ARG   A 1 141 ? 13.531 -16.640 -4.094  0.62 15.46 ?  141 ARG   A CG   1 
ATOM   3028 C CG   B ARG   A 1 141 ? 13.653 -16.994 -4.006  0.38 14.52 ?  141 ARG   A CG   1 
ATOM   3029 C CD   A ARG   A 1 141 ? 12.507 -17.421 -3.334  0.62 17.49 ?  141 ARG   A CD   1 
ATOM   3030 C CD   B ARG   A 1 141 ? 12.580 -17.730 -3.243  0.38 17.11 ?  141 ARG   A CD   1 
ATOM   3031 N NE   A ARG   A 1 141 ? 13.132 -18.224 -2.298  0.62 17.84 ?  141 ARG   A NE   1 
ATOM   3032 N NE   B ARG   A 1 141 ? 13.097 -18.405 -2.062  0.38 19.35 ?  141 ARG   A NE   1 
ATOM   3033 C CZ   A ARG   A 1 141 ? 12.465 -18.808 -1.312  0.62 18.39 ?  141 ARG   A CZ   1 
ATOM   3034 C CZ   B ARG   A 1 141 ? 12.340 -18.829 -1.059  0.38 20.42 ?  141 ARG   A CZ   1 
ATOM   3035 N NH1  A ARG   A 1 141 ? 11.178 -18.576 -1.117  0.62 17.68 ?  141 ARG   A NH1  1 
ATOM   3036 N NH1  B ARG   A 1 141 ? 11.044 -18.569 -1.013  0.38 20.64 ?  141 ARG   A NH1  1 
ATOM   3037 N NH2  A ARG   A 1 141 ? 13.107 -19.640 -0.497  0.62 19.39 ?  141 ARG   A NH2  1 
ATOM   3038 N NH2  B ARG   A 1 141 ? 12.900 -19.523 -0.072  0.38 21.14 ?  141 ARG   A NH2  1 
ATOM   3039 H H    A ARG   A 1 141 ? 13.586 -13.093 -2.510  0.62 13.03 ?  141 ARG   A H    1 
ATOM   3040 H H    B ARG   A 1 141 ? 13.502 -13.342 -2.593  0.38 12.85 ?  141 ARG   A H    1 
ATOM   3041 H HA   A ARG   A 1 141 ? 13.748 -15.526 -1.594  0.62 14.40 ?  141 ARG   A HA   1 
ATOM   3042 H HA   B ARG   A 1 141 ? 13.834 -15.747 -1.649  0.38 13.77 ?  141 ARG   A HA   1 
ATOM   3043 H HB2  A ARG   A 1 141 ? 12.644 -14.884 -3.600  0.62 16.06 ?  141 ARG   A HB2  1 
ATOM   3044 H HB2  B ARG   A 1 141 ? 12.692 -15.223 -3.692  0.38 15.23 ?  141 ARG   A HB2  1 
ATOM   3045 H HB3  A ARG   A 1 141 ? 14.061 -14.698 -4.276  0.62 16.06 ?  141 ARG   A HB3  1 
ATOM   3046 H HB3  B ARG   A 1 141 ? 14.115 -15.048 -4.366  0.38 15.23 ?  141 ARG   A HB3  1 
ATOM   3047 H HG2  A ARG   A 1 141 ? 13.297 -16.664 -5.037  0.62 18.56 ?  141 ARG   A HG2  1 
ATOM   3048 H HG2  B ARG   A 1 141 ? 13.498 -17.118 -4.956  0.38 17.43 ?  141 ARG   A HG2  1 
ATOM   3049 H HG3  A ARG   A 1 141 ? 14.399 -17.049 -3.953  0.62 18.56 ?  141 ARG   A HG3  1 
ATOM   3050 H HG3  B ARG   A 1 141 ? 14.518 -17.363 -3.757  0.38 17.43 ?  141 ARG   A HG3  1 
ATOM   3051 H HD2  A ARG   A 1 141 ? 11.885 -16.811 -2.906  0.62 21.00 ?  141 ARG   A HD2  1 
ATOM   3052 H HD2  B ARG   A 1 141 ? 11.907 -17.093 -2.951  0.38 20.55 ?  141 ARG   A HD2  1 
ATOM   3053 H HD3  A ARG   A 1 141 ? 12.034 -18.010 -3.942  0.62 21.00 ?  141 ARG   A HD3  1 
ATOM   3054 H HD3  B ARG   A 1 141 ? 12.178 -18.391 -3.825  0.38 20.55 ?  141 ARG   A HD3  1 
ATOM   3055 H HE   A ARG   A 1 141 ? 13.962 -18.429 -2.394  0.62 21.43 ?  141 ARG   A HE   1 
ATOM   3056 H HE   B ARG   A 1 141 ? 13.932 -18.612 -2.051  0.38 23.23 ?  141 ARG   A HE   1 
ATOM   3057 H HH11 A ARG   A 1 141 ? 10.746 -18.052 -1.644  0.62 21.24 ?  141 ARG   A HH11 1 
ATOM   3058 H HH11 B ARG   A 1 141 ? 10.668 -18.126 -1.648  0.38 24.78 ?  141 ARG   A HH11 1 
ATOM   3059 H HH12 A ARG   A 1 141 ? 10.764 -18.966 -0.470  0.62 21.24 ?  141 ARG   A HH12 1 
ATOM   3060 H HH12 B ARG   A 1 141 ? 10.574 -18.851 -0.351  0.38 24.78 ?  141 ARG   A HH12 1 
ATOM   3061 H HH21 A ARG   A 1 141 ? 13.947 -19.793 -0.613  0.62 23.28 ?  141 ARG   A HH21 1 
ATOM   3062 H HH21 B ARG   A 1 141 ? 13.742 -19.698 -0.093  0.38 25.38 ?  141 ARG   A HH21 1 
ATOM   3063 H HH22 A ARG   A 1 141 ? 12.689 -20.016 0.154   0.62 23.28 ?  141 ARG   A HH22 1 
ATOM   3064 H HH22 B ARG   A 1 141 ? 12.421 -19.797 0.587   0.38 25.38 ?  141 ARG   A HH22 1 
ATOM   3065 N N    . VAL   A 1 142 ? 16.484 -14.479 -2.938  1.00 11.16 ?  142 VAL   A N    1 
ATOM   3066 C CA   . VAL   A 1 142 ? 17.932 -14.679 -2.971  1.00 11.26 ?  142 VAL   A CA   1 
ATOM   3067 C C    . VAL   A 1 142 ? 18.506 -14.640 -1.560  1.00 10.89 ?  142 VAL   A C    1 
ATOM   3068 O O    . VAL   A 1 142 ? 19.363 -15.456 -1.202  1.00 11.42 ?  142 VAL   A O    1 
ATOM   3069 C CB   . VAL   A 1 142 ? 18.624 -13.668 -3.905  1.00 11.59 ?  142 VAL   A CB   1 
ATOM   3070 C CG1  . VAL   A 1 142 ? 20.138 -13.880 -3.878  1.00 11.70 ?  142 VAL   A CG1  1 
ATOM   3071 C CG2  . VAL   A 1 142 ? 18.115 -13.811 -5.328  1.00 12.79 ?  142 VAL   A CG2  1 
ATOM   3072 H H    A VAL   A 1 142 ? 16.215 -13.798 -3.394  0.62 13.41 ?  142 VAL   A H    1 
ATOM   3073 H H    B VAL   A 1 142 ? 16.203 -13.753 -3.310  0.38 13.41 ?  142 VAL   A H    1 
ATOM   3074 H HA   . VAL   A 1 142 ? 18.112 -15.558 -3.328  1.00 13.53 ?  142 VAL   A HA   1 
ATOM   3075 H HB   . VAL   A 1 142 ? 18.442 -12.761 -3.604  1.00 13.93 ?  142 VAL   A HB   1 
ATOM   3076 H HG11 . VAL   A 1 142 ? 20.537 -13.399 -4.621  1.00 14.05 ?  142 VAL   A HG11 1 
ATOM   3077 H HG12 . VAL   A 1 142 ? 20.492 -13.541 -3.040  1.00 14.05 ?  142 VAL   A HG12 1 
ATOM   3078 H HG13 . VAL   A 1 142 ? 20.323 -14.827 -3.960  1.00 14.05 ?  142 VAL   A HG13 1 
ATOM   3079 H HG21 . VAL   A 1 142 ? 18.432 -13.059 -5.853  1.00 15.36 ?  142 VAL   A HG21 1 
ATOM   3080 H HG22 . VAL   A 1 142 ? 18.455 -14.640 -5.698  1.00 15.36 ?  142 VAL   A HG22 1 
ATOM   3081 H HG23 . VAL   A 1 142 ? 17.149 -13.823 -5.318  1.00 15.36 ?  142 VAL   A HG23 1 
ATOM   3082 N N    . CYS   A 1 143 ? 18.031 -13.712 -0.730  1.00 10.55 ?  143 CYS   A N    1 
ATOM   3083 C CA   . CYS   A 1 143 ? 18.493 -13.650 0.653   1.00 10.72 ?  143 CYS   A CA   1 
ATOM   3084 C C    . CYS   A 1 143 ? 18.273 -14.983 1.361   1.00 10.83 ?  143 CYS   A C    1 
ATOM   3085 O O    . CYS   A 1 143 ? 19.202 -15.564 1.928   1.00 10.95 ?  143 CYS   A O    1 
ATOM   3086 C CB   . CYS   A 1 143 ? 17.757 -12.534 1.392   1.00 11.14 ?  143 CYS   A CB   1 
ATOM   3087 S SG   . CYS   A 1 143 ? 18.244 -12.342 3.113   1.00 11.50 ?  143 CYS   A SG   1 
ATOM   3088 H H    . CYS   A 1 143 ? 17.454 -13.110 -0.941  1.00 12.68 ?  143 CYS   A H    1 
ATOM   3089 H HA   . CYS   A 1 143 ? 19.443 -13.452 0.666   1.00 12.88 ?  143 CYS   A HA   1 
ATOM   3090 H HB2  . CYS   A 1 143 ? 17.921 -11.694 0.939   1.00 13.38 ?  143 CYS   A HB2  1 
ATOM   3091 H HB3  . CYS   A 1 143 ? 16.807 -12.730 1.377   1.00 13.38 ?  143 CYS   A HB3  1 
ATOM   3092 H HG   . CYS   A 1 143 ? 17.707 -11.373 3.562   1.00 13.81 ?  143 CYS   A HG   1 
ATOM   3093 N N    . VAL   A 1 144 ? 17.040 -15.482 1.338   1.00 11.38 ?  144 VAL   A N    1 
ATOM   3094 C CA   . VAL   A 1 144 ? 16.716 -16.714 2.053   1.00 12.85 ?  144 VAL   A CA   1 
ATOM   3095 C C    . VAL   A 1 144 ? 17.511 -17.893 1.516   1.00 12.45 ?  144 VAL   A C    1 
ATOM   3096 O O    . VAL   A 1 144 ? 17.884 -18.800 2.276   1.00 13.44 ?  144 VAL   A O    1 
ATOM   3097 C CB   . VAL   A 1 144 ? 15.192 -16.944 1.979   1.00 16.46 ?  144 VAL   A CB   1 
ATOM   3098 C CG1  . VAL   A 1 144 ? 14.835 -18.365 2.346   1.00 19.50 ?  144 VAL   A CG1  1 
ATOM   3099 C CG2  . VAL   A 1 144 ? 14.472 -15.925 2.862   1.00 16.28 ?  144 VAL   A CG2  1 
ATOM   3100 H H    . VAL   A 1 144 ? 16.380 -15.124 0.907   1.00 13.67 ?  144 VAL   A H    1 
ATOM   3101 H HA   . VAL   A 1 144 ? 16.945 -16.590 2.979   1.00 15.44 ?  144 VAL   A HA   1 
ATOM   3102 H HB   . VAL   A 1 144 ? 14.896 -16.790 1.064   1.00 19.76 ?  144 VAL   A HB   1 
ATOM   3103 H HG11 . VAL   A 1 144 ? 13.887 -18.409 2.546   1.00 23.41 ?  144 VAL   A HG11 1 
ATOM   3104 H HG12 . VAL   A 1 144 ? 15.041 -18.947 1.599   1.00 23.41 ?  144 VAL   A HG12 1 
ATOM   3105 H HG13 . VAL   A 1 144 ? 15.349 -18.626 3.125   1.00 23.41 ?  144 VAL   A HG13 1 
ATOM   3106 H HG21 . VAL   A 1 144 ? 13.517 -16.098 2.837   1.00 19.56 ?  144 VAL   A HG21 1 
ATOM   3107 H HG22 . VAL   A 1 144 ? 14.798 -16.006 3.772   1.00 19.56 ?  144 VAL   A HG22 1 
ATOM   3108 H HG23 . VAL   A 1 144 ? 14.650 -15.027 2.529   1.00 19.56 ?  144 VAL   A HG23 1 
ATOM   3109 N N    . ASP   A 1 145 ? 17.770 -17.916 0.211   1.00 12.98 ?  145 ASP   A N    1 
ATOM   3110 C CA   . ASP   A 1 145 ? 18.478 -19.023 -0.420  1.00 13.83 ?  145 ASP   A CA   1 
ATOM   3111 C C    . ASP   A 1 145 ? 19.999 -18.878 -0.386  1.00 13.26 ?  145 ASP   A C    1 
ATOM   3112 O O    . ASP   A 1 145 ? 20.698 -19.775 -0.868  1.00 15.19 ?  145 ASP   A O    1 
ATOM   3113 C CB   . ASP   A 1 145 ? 18.027 -19.173 -1.876  1.00 15.68 ?  145 ASP   A CB   1 
ATOM   3114 C CG   . ASP   A 1 145 ? 16.577 -19.609 -2.000  1.00 18.12 ?  145 ASP   A CG   1 
ATOM   3115 O OD1  . ASP   A 1 145 ? 16.016 -20.153 -1.024  1.00 18.75 ?  145 ASP   A OD1  1 
ATOM   3116 O OD2  . ASP   A 1 145 ? 15.994 -19.412 -3.085  1.00 19.57 -1 145 ASP   A OD2  1 
ATOM   3117 H H    . ASP   A 1 145 ? 17.535 -17.295 -0.343  1.00 15.59 ?  145 ASP   A H    1 
ATOM   3118 H HA   . ASP   A 1 145 ? 18.247 -19.839 0.044   1.00 16.61 ?  145 ASP   A HA   1 
ATOM   3119 H HB2  . ASP   A 1 145 ? 18.125 -18.320 -2.330  1.00 18.83 ?  145 ASP   A HB2  1 
ATOM   3120 H HB3  . ASP   A 1 145 ? 18.571 -19.846 -2.310  1.00 18.83 ?  145 ASP   A HB3  1 
ATOM   3121 N N    . THR   A 1 146 ? 20.531 -17.788 0.154   1.00 11.54 ?  146 THR   A N    1 
ATOM   3122 C CA   . THR   A 1 146 ? 21.972 -17.549 0.172   1.00 11.38 ?  146 THR   A CA   1 
ATOM   3123 C C    . THR   A 1 146 ? 22.532 -17.357 1.569   1.00 11.19 ?  146 THR   A C    1 
ATOM   3124 O O    . THR   A 1 146 ? 23.606 -17.890 1.877   1.00 12.24 ?  146 THR   A O    1 
ATOM   3125 C CB   . THR   A 1 146 ? 22.296 -16.301 -0.674  1.00 11.08 ?  146 THR   A CB   1 
ATOM   3126 O OG1  . THR   A 1 146 ? 21.777 -16.472 -1.991  1.00 11.53 ?  146 THR   A OG1  1 
ATOM   3127 C CG2  . THR   A 1 146 ? 23.806 -16.063 -0.772  1.00 11.69 ?  146 THR   A CG2  1 
ATOM   3128 H H    . THR   A 1 146 ? 20.074 -17.155 0.518   1.00 13.86 ?  146 THR   A H    1 
ATOM   3129 H HA   . THR   A 1 146 ? 22.427 -18.305 -0.226  1.00 13.67 ?  146 THR   A HA   1 
ATOM   3130 H HB   . THR   A 1 146 ? 21.899 -15.515 -0.272  1.00 13.31 ?  146 THR   A HB   1 
ATOM   3131 H HG1  . THR   A 1 146 ? 20.941 -16.548 -1.966  1.00 13.85 ?  146 THR   A HG1  1 
ATOM   3132 H HG21 . THR   A 1 146 ? 23.993 -15.387 -1.442  1.00 14.04 ?  146 THR   A HG21 1 
ATOM   3133 H HG22 . THR   A 1 146 ? 24.151 -15.764 0.082   1.00 14.04 ?  146 THR   A HG22 1 
ATOM   3134 H HG23 . THR   A 1 146 ? 24.253 -16.887 -1.025  1.00 14.04 ?  146 THR   A HG23 1 
ATOM   3135 N N    . VAL   A 1 147 ? 21.859 -16.576 2.406   1.00 10.73 ?  147 VAL   A N    1 
ATOM   3136 C CA   . VAL   A 1 147 ? 22.354 -16.280 3.742   1.00 11.17 ?  147 VAL   A CA   1 
ATOM   3137 C C    . VAL   A 1 147 ? 22.028 -17.447 4.661   1.00 11.16 ?  147 VAL   A C    1 
ATOM   3138 O O    . VAL   A 1 147 ? 20.886 -17.918 4.710   1.00 12.12 ?  147 VAL   A O    1 
ATOM   3139 C CB   . VAL   A 1 147 ? 21.745 -14.970 4.266   1.00 11.05 ?  147 VAL   A CB   1 
ATOM   3140 C CG1  . VAL   A 1 147 ? 22.303 -14.652 5.629   1.00 11.98 ?  147 VAL   A CG1  1 
ATOM   3141 C CG2  . VAL   A 1 147 ? 21.994 -13.821 3.290   1.00 11.23 ?  147 VAL   A CG2  1 
ATOM   3142 H H    . VAL   A 1 147 ? 21.103 -16.204 2.222   1.00 12.89 ?  147 VAL   A H    1 
ATOM   3143 H HA   . VAL   A 1 147 ? 23.317 -16.175 3.706   1.00 13.42 ?  147 VAL   A HA   1 
ATOM   3144 H HB   . VAL   A 1 147 ? 20.791 -15.081 4.361   1.00 13.28 ?  147 VAL   A HB   1 
ATOM   3145 H HG11 . VAL   A 1 147 ? 22.058 -13.748 5.867   1.00 14.39 ?  147 VAL   A HG11 1 
ATOM   3146 H HG12 . VAL   A 1 147 ? 21.934 -15.277 6.275   1.00 14.39 ?  147 VAL   A HG12 1 
ATOM   3147 H HG13 . VAL   A 1 147 ? 23.270 -14.738 5.603   1.00 14.39 ?  147 VAL   A HG13 1 
ATOM   3148 H HG21 . VAL   A 1 147 ? 21.672 -12.996 3.687   1.00 13.49 ?  147 VAL   A HG21 1 
ATOM   3149 H HG22 . VAL   A 1 147 ? 22.943 -13.756 3.112   1.00 13.49 ?  147 VAL   A HG22 1 
ATOM   3150 H HG23 . VAL   A 1 147 ? 21.512 -14.002 2.468   1.00 13.49 ?  147 VAL   A HG23 1 
ATOM   3151 N N    . ARG   A 1 148 ? 23.051 -17.928 5.371   1.00 11.52 ?  148 ARG   A N    1 
ATOM   3152 C CA   . ARG   A 1 148 ? 22.915 -19.000 6.338   1.00 11.86 ?  148 ARG   A CA   1 
ATOM   3153 C C    . ARG   A 1 148 ? 23.040 -18.523 7.774   1.00 12.00 ?  148 ARG   A C    1 
ATOM   3154 O O    . ARG   A 1 148 ? 22.632 -19.248 8.691   1.00 13.72 ?  148 ARG   A O    1 
ATOM   3155 C CB   . ARG   A 1 148 ? 23.962 -20.089 6.058   1.00 12.44 ?  148 ARG   A CB   1 
ATOM   3156 C CG   . ARG   A 1 148 ? 23.789 -20.751 4.698   1.00 13.92 ?  148 ARG   A CG   1 
ATOM   3157 C CD   . ARG   A 1 148 ? 24.881 -21.782 4.399   1.00 14.74 ?  148 ARG   A CD   1 
ATOM   3158 N NE   . ARG   A 1 148 ? 26.216 -21.193 4.423   1.00 14.45 ?  148 ARG   A NE   1 
ATOM   3159 C CZ   . ARG   A 1 148 ? 26.730 -20.459 3.444   1.00 13.92 ?  148 ARG   A CZ   1 
ATOM   3160 N NH1  . ARG   A 1 148 ? 26.055 -20.223 2.329   1.00 14.18 ?  148 ARG   A NH1  1 
ATOM   3161 N NH2  . ARG   A 1 148 ? 27.949 -19.934 3.593   1.00 14.23 ?  148 ARG   A NH2  1 
ATOM   3162 H H    . ARG   A 1 148 ? 23.858 -17.631 5.294   1.00 13.84 ?  148 ARG   A H    1 
ATOM   3163 H HA   . ARG   A 1 148 ? 22.043 -19.402 6.233   1.00 14.24 ?  148 ARG   A HA   1 
ATOM   3164 H HB2  . ARG   A 1 148 ? 24.848 -19.708 6.087   1.00 14.95 ?  148 ARG   A HB2  1 
ATOM   3165 H HB3  . ARG   A 1 148 ? 23.880 -20.791 6.729   1.00 14.95 ?  148 ARG   A HB3  1 
ATOM   3166 H HG2  . ARG   A 1 148 ? 22.932 -21.205 4.670   1.00 16.72 ?  148 ARG   A HG2  1 
ATOM   3167 H HG3  . ARG   A 1 148 ? 23.827 -20.068 4.010   1.00 16.72 ?  148 ARG   A HG3  1 
ATOM   3168 H HD2  . ARG   A 1 148 ? 24.850 -22.484 5.068   1.00 17.70 ?  148 ARG   A HD2  1 
ATOM   3169 H HD3  . ARG   A 1 148 ? 24.730 -22.162 3.515   1.00 17.70 ?  148 ARG   A HD3  1 
ATOM   3170 H HE   . ARG   A 1 148 ? 26.704 -21.337 5.110   1.00 17.36 ?  148 ARG   A HE   1 
ATOM   3171 H HH11 . ARG   A 1 148 ? 25.265 -20.547 2.220   1.00 17.03 ?  148 ARG   A HH11 1 
ATOM   3172 H HH12 . ARG   A 1 148 ? 26.402 -19.733 1.709   1.00 17.03 ?  148 ARG   A HH12 1 
ATOM   3173 H HH21 . ARG   A 1 148 ? 28.389 -20.076 4.315   1.00 17.10 ?  148 ARG   A HH21 1 
ATOM   3174 H HH22 . ARG   A 1 148 ? 28.288 -19.447 2.970   1.00 17.10 ?  148 ARG   A HH22 1 
ATOM   3175 N N    . THR   A 1 149 ? 23.589 -17.330 7.987   1.00 12.05 ?  149 THR   A N    1 
ATOM   3176 C CA   . THR   A 1 149 ? 23.684 -16.731 9.306   1.00 12.31 ?  149 THR   A CA   1 
ATOM   3177 C C    . THR   A 1 149 ? 22.364 -16.026 9.622   1.00 11.80 ?  149 THR   A C    1 
ATOM   3178 O O    . THR   A 1 149 ? 21.426 -16.019 8.816   1.00 12.40 ?  149 THR   A O    1 
ATOM   3179 C CB   . THR   A 1 149 ? 24.891 -15.798 9.356   1.00 12.68 ?  149 THR   A CB   1 
ATOM   3180 O OG1  . THR   A 1 149 ? 24.767 -14.867 8.281   1.00 12.35 ?  149 THR   A OG1  1 
ATOM   3181 C CG2  . THR   A 1 149 ? 26.200 -16.592 9.229   1.00 12.97 ?  149 THR   A CG2  1 
ATOM   3182 H H    . THR   A 1 149 ? 23.926 -16.836 7.361   1.00 14.48 ?  149 THR   A H    1 
ATOM   3183 H HA   . THR   A 1 149 ? 23.812 -17.430 9.958   1.00 14.79 ?  149 THR   A HA   1 
ATOM   3184 H HB   . THR   A 1 149 ? 24.888 -15.318 10.197  1.00 15.23 ?  149 THR   A HB   1 
ATOM   3185 H HG1  . THR   A 1 149 ? 25.423 -14.343 8.273   1.00 14.84 ?  149 THR   A HG1  1 
ATOM   3186 H HG21 . THR   A 1 149 ? 26.956 -15.986 9.275   1.00 15.58 ?  149 THR   A HG21 1 
ATOM   3187 H HG22 . THR   A 1 149 ? 26.268 -17.236 9.950   1.00 15.58 ?  149 THR   A HG22 1 
ATOM   3188 H HG23 . THR   A 1 149 ? 26.223 -17.062 8.381   1.00 15.58 ?  149 THR   A HG23 1 
ATOM   3189 N N    . ASN   A 1 150 ? 22.246 -15.484 10.829  1.00 12.12 ?  150 ASN   A N    1 
ATOM   3190 C CA   . ASN   A 1 150 ? 20.964 -14.964 11.311  1.00 12.53 ?  150 ASN   A CA   1 
ATOM   3191 C C    . ASN   A 1 150 ? 20.790 -13.521 10.860  1.00 11.80 ?  150 ASN   A C    1 
ATOM   3192 O O    . ASN   A 1 150 ? 21.538 -12.630 11.287  1.00 13.17 ?  150 ASN   A O    1 
ATOM   3193 C CB   . ASN   A 1 150 ? 20.900 -15.077 12.827  1.00 15.25 ?  150 ASN   A CB   1 
ATOM   3194 C CG   . ASN   A 1 150 ? 20.787 -16.508 13.287  1.00 19.80 ?  150 ASN   A CG   1 
ATOM   3195 O OD1  . ASN   A 1 150 ? 20.196 -17.340 12.598  1.00 21.29 ?  150 ASN   A OD1  1 
ATOM   3196 N ND2  . ASN   A 1 150 ? 21.358 -16.812 14.448  1.00 22.24 ?  150 ASN   A ND2  1 
ATOM   3197 H H    . ASN   A 1 150 ? 22.887 -15.406 11.389  1.00 14.56 ?  150 ASN   A H    1 
ATOM   3198 H HA   . ASN   A 1 150 ? 20.236 -15.501 10.938  1.00 15.05 ?  150 ASN   A HA   1 
ATOM   3199 H HB2  . ASN   A 1 150 ? 21.708 -14.701 13.208  1.00 18.32 ?  150 ASN   A HB2  1 
ATOM   3200 H HB3  . ASN   A 1 150 ? 20.121 -14.600 13.153  1.00 18.32 ?  150 ASN   A HB3  1 
ATOM   3201 H HD21 . ASN   A 1 150 ? 21.325 -17.620 14.754  1.00 26.70 ?  150 ASN   A HD21 1 
ATOM   3202 H HD22 . ASN   A 1 150 ? 21.760 -16.204 14.908  1.00 26.70 ?  150 ASN   A HD22 1 
ATOM   3203 N N    . VAL   A 1 151 ? 19.800 -13.284 10.007  1.00 11.47 ?  151 VAL   A N    1 
ATOM   3204 C CA   . VAL   A 1 151 ? 19.591 -11.973 9.414   1.00 11.27 ?  151 VAL   A CA   1 
ATOM   3205 C C    . VAL   A 1 151 ? 18.202 -11.465 9.784   1.00 10.98 ?  151 VAL   A C    1 
ATOM   3206 O O    . VAL   A 1 151 ? 17.196 -12.174 9.627   1.00 12.81 ?  151 VAL   A O    1 
ATOM   3207 C CB   . VAL   A 1 151 ? 19.871 -11.968 7.897   1.00 13.13 ?  151 VAL   A CB   1 
ATOM   3208 C CG1  . VAL   A 1 151 ? 19.052 -13.002 7.155   1.00 14.61 ?  151 VAL   A CG1  1 
ATOM   3209 C CG2  . VAL   A 1 151 ? 19.668 -10.563 7.313   1.00 13.60 ?  151 VAL   A CG2  1 
ATOM   3210 H H    . VAL   A 1 151 ? 19.235 -13.882 9.744   1.00 13.78 ?  151 VAL   A H    1 
ATOM   3211 H HA   . VAL   A 1 151 ? 20.233 -11.364 9.808   1.00 13.55 ?  151 VAL   A HA   1 
ATOM   3212 H HB   . VAL   A 1 151 ? 20.807 -12.194 7.754   1.00 15.77 ?  151 VAL   A HB   1 
ATOM   3213 H HG11 . VAL   A 1 151 ? 19.235 -12.937 6.203   1.00 17.55 ?  151 VAL   A HG11 1 
ATOM   3214 H HG12 . VAL   A 1 151 ? 19.295 -13.887 7.475   1.00 17.55 ?  151 VAL   A HG12 1 
ATOM   3215 H HG13 . VAL   A 1 151 ? 18.110 -12.840 7.321   1.00 17.55 ?  151 VAL   A HG13 1 
ATOM   3216 H HG21 . VAL   A 1 151 ? 19.980 -10.553 6.391   1.00 16.34 ?  151 VAL   A HG21 1 
ATOM   3217 H HG22 . VAL   A 1 151 ? 18.724 -10.341 7.338   1.00 16.34 ?  151 VAL   A HG22 1 
ATOM   3218 H HG23 . VAL   A 1 151 ? 20.175 -9.925  7.836   1.00 16.34 ?  151 VAL   A HG23 1 
ATOM   3219 N N    . TYR   A 1 152 ? 18.178 -10.218 10.269  1.00 11.12 ?  152 TYR   A N    1 
ATOM   3220 C CA   . TYR   A 1 152 ? 16.982 -9.477  10.641  1.00 10.86 ?  152 TYR   A CA   1 
ATOM   3221 C C    . TYR   A 1 152 ? 16.809 -8.380  9.603   1.00 10.36 ?  152 TYR   A C    1 
ATOM   3222 O O    . TYR   A 1 152 ? 17.587 -7.420  9.562   1.00 10.73 ?  152 TYR   A O    1 
ATOM   3223 C CB   . TYR   A 1 152 ? 17.146 -8.926  12.055  1.00 11.46 ?  152 TYR   A CB   1 
ATOM   3224 C CG   . TYR   A 1 152 ? 17.108 -10.050 13.051  1.00 12.45 ?  152 TYR   A CG   1 
ATOM   3225 C CD1  . TYR   A 1 152 ? 18.242 -10.801 13.336  1.00 13.93 ?  152 TYR   A CD1  1 
ATOM   3226 C CD2  . TYR   A 1 152 ? 15.919 -10.406 13.670  1.00 12.93 ?  152 TYR   A CD2  1 
ATOM   3227 C CE1  . TYR   A 1 152 ? 18.197 -11.859 14.222  1.00 15.67 ?  152 TYR   A CE1  1 
ATOM   3228 C CE2  . TYR   A 1 152 ? 15.858 -11.473 14.563  1.00 14.70 ?  152 TYR   A CE2  1 
ATOM   3229 C CZ   . TYR   A 1 152 ? 17.003 -12.193 14.835  1.00 15.35 ?  152 TYR   A CZ   1 
ATOM   3230 O OH   . TYR   A 1 152 ? 16.963 -13.260 15.713  1.00 17.64 ?  152 TYR   A OH   1 
ATOM   3231 H H    . TYR   A 1 152 ? 18.898 -9.752  10.386  1.00 13.35 ?  152 TYR   A H    1 
ATOM   3232 H HA   . TYR   A 1 152 ? 16.212 -10.065 10.616  1.00 13.05 ?  152 TYR   A HA   1 
ATOM   3233 H HB2  . TYR   A 1 152 ? 18.002 -8.477  12.130  1.00 13.77 ?  152 TYR   A HB2  1 
ATOM   3234 H HB3  . TYR   A 1 152 ? 16.422 -8.314  12.250  1.00 13.77 ?  152 TYR   A HB3  1 
ATOM   3235 H HD1  . TYR   A 1 152 ? 19.047 -10.582 12.920  1.00 16.73 ?  152 TYR   A HD1  1 
ATOM   3236 H HD2  . TYR   A 1 152 ? 15.143 -9.922  13.482  1.00 15.53 ?  152 TYR   A HD2  1 
ATOM   3237 H HE1  . TYR   A 1 152 ? 18.965 -12.344 14.407  1.00 18.82 ?  152 TYR   A HE1  1 
ATOM   3238 H HE2  . TYR   A 1 152 ? 15.054 -11.694 14.979  1.00 17.66 ?  152 TYR   A HE2  1 
ATOM   3239 H HH   . TYR   A 1 152 ? 16.187 -13.344 16.021  1.00 21.18 ?  152 TYR   A HH   1 
ATOM   3240 N N    A LEU   A 1 153 ? 15.818 -8.562  8.736   0.62 10.09 ?  153 LEU   A N    1 
ATOM   3241 N N    B LEU   A 1 153 ? 15.784 -8.509  8.771   0.38 10.34 ?  153 LEU   A N    1 
ATOM   3242 C CA   A LEU   A 1 153 ? 15.552 -7.671  7.616   0.62 10.28 ?  153 LEU   A CA   1 
ATOM   3243 C CA   B LEU   A 1 153 ? 15.547 -7.570  7.682   0.38 10.42 ?  153 LEU   A CA   1 
ATOM   3244 C C    A LEU   A 1 153 ? 14.554 -6.595  8.017   0.62 10.31 ?  153 LEU   A C    1 
ATOM   3245 C C    B LEU   A 1 153 ? 14.564 -6.494  8.122   0.38 10.12 ?  153 LEU   A C    1 
ATOM   3246 O O    A LEU   A 1 153 ? 13.479 -6.897  8.553   0.62 11.57 ?  153 LEU   A O    1 
ATOM   3247 O O    B LEU   A 1 153 ? 13.414 -6.793  8.467   0.38 10.98 ?  153 LEU   A O    1 
ATOM   3248 C CB   A LEU   A 1 153 ? 14.983 -8.459  6.436   0.62 10.15 ?  153 LEU   A CB   1 
ATOM   3249 C CB   B LEU   A 1 153 ? 15.003 -8.302  6.459   0.38 10.71 ?  153 LEU   A CB   1 
ATOM   3250 C CG   A LEU   A 1 153 ? 15.913 -9.439  5.726   0.62 10.32 ?  153 LEU   A CG   1 
ATOM   3251 C CG   B LEU   A 1 153 ? 15.919 -9.365  5.854   0.38 11.22 ?  153 LEU   A CG   1 
ATOM   3252 C CD1  A LEU   A 1 153 ? 15.110 -10.323 4.792   0.62 10.84 ?  153 LEU   A CD1  1 
ATOM   3253 C CD1  B LEU   A 1 153 ? 15.171 -10.136 4.785   0.38 11.66 ?  153 LEU   A CD1  1 
ATOM   3254 C CD2  A LEU   A 1 153 ? 16.966 -8.687  4.948   0.62 10.18 ?  153 LEU   A CD2  1 
ATOM   3255 C CD2  B LEU   A 1 153 ? 17.185 -8.744  5.279   0.38 11.74 ?  153 LEU   A CD2  1 
ATOM   3256 H H    A LEU   A 1 153 ? 15.261 -9.222  8.785   0.62 12.13 ?  153 LEU   A H    1 
ATOM   3257 H H    B LEU   A 1 153 ? 15.197 -9.138  8.822   0.38 12.43 ?  153 LEU   A H    1 
ATOM   3258 H HA   A LEU   A 1 153 ? 16.375 -7.251  7.341   0.62 12.35 ?  153 LEU   A HA   1 
ATOM   3259 H HA   B LEU   A 1 153 ? 16.378 -7.139  7.444   0.38 12.52 ?  153 LEU   A HA   1 
ATOM   3260 H HB2  A LEU   A 1 153 ? 14.223 -8.970  6.753   0.62 12.20 ?  153 LEU   A HB2  1 
ATOM   3261 H HB2  B LEU   A 1 153 ? 14.176 -8.739  6.710   0.38 12.86 ?  153 LEU   A HB2  1 
ATOM   3262 H HB3  A LEU   A 1 153 ? 14.683 -7.823  5.768   0.62 12.20 ?  153 LEU   A HB3  1 
ATOM   3263 H HB3  B LEU   A 1 153 ? 14.825 -7.644  5.770   0.38 12.86 ?  153 LEU   A HB3  1 
ATOM   3264 H HG   A LEU   A 1 153 ? 16.358 -10.003 6.383   0.62 12.40 ?  153 LEU   A HG   1 
ATOM   3265 H HG   B LEU   A 1 153 ? 16.182 -9.988  6.550   0.38 13.48 ?  153 LEU   A HG   1 
ATOM   3266 H HD11 A LEU   A 1 153 ? 15.692 -10.997 4.414   0.62 13.02 ?  153 LEU   A HD11 1 
ATOM   3267 H HD11 B LEU   A 1 153 ? 15.722 -10.870 4.480   0.38 14.01 ?  153 LEU   A HD11 1 
ATOM   3268 H HD12 A LEU   A 1 153 ? 14.395 -10.742 5.294   0.62 13.02 ?  153 LEU   A HD12 1 
ATOM   3269 H HD12 B LEU   A 1 153 ? 14.344 -10.475 5.163   0.38 14.01 ?  153 LEU   A HD12 1 
ATOM   3270 H HD13 A LEU   A 1 153 ? 14.737 -9.770  4.085   0.62 13.02 ?  153 LEU   A HD13 1 
ATOM   3271 H HD13 B LEU   A 1 153 ? 14.974 -9.538  4.046   0.38 14.01 ?  153 LEU   A HD13 1 
ATOM   3272 H HD21 A LEU   A 1 153 ? 17.535 -9.325  4.498   0.62 12.23 ?  153 LEU   A HD21 1 
ATOM   3273 H HD21 B LEU   A 1 153 ? 17.713 -9.441  4.860   0.38 14.11 ?  153 LEU   A HD21 1 
ATOM   3274 H HD22 A LEU   A 1 153 ? 16.522 -8.117  4.303   0.62 12.23 ?  153 LEU   A HD22 1 
ATOM   3275 H HD22 B LEU   A 1 153 ? 16.937 -8.075  4.623   0.38 14.11 ?  153 LEU   A HD22 1 
ATOM   3276 H HD23 A LEU   A 1 153 ? 17.485 -8.151  5.566   0.62 12.23 ?  153 LEU   A HD23 1 
ATOM   3277 H HD23 B LEU   A 1 153 ? 17.691 -8.332  5.998   0.38 14.11 ?  153 LEU   A HD23 1 
ATOM   3278 N N    A ALA   A 1 154 ? 14.909 -5.343  7.737   0.62 10.33 ?  154 ALA   A N    1 
ATOM   3279 N N    B ALA   A 1 154 ? 15.016 -5.242  8.094   0.38 9.32  ?  154 ALA   A N    1 
ATOM   3280 C CA   A ALA   A 1 154 ? 14.037 -4.195  7.953   0.62 10.39 ?  154 ALA   A CA   1 
ATOM   3281 C CA   B ALA   A 1 154 ? 14.168 -4.088  8.357   0.38 9.56  ?  154 ALA   A CA   1 
ATOM   3282 C C    A ALA   A 1 154 ? 13.546 -3.695  6.601   0.62 9.81  ?  154 ALA   A C    1 
ATOM   3283 C C    B ALA   A 1 154 ? 13.736 -3.506  7.018   0.38 9.03  ?  154 ALA   A C    1 
ATOM   3284 O O    A ALA   A 1 154 ? 14.353 -3.330  5.743   0.62 10.61 ?  154 ALA   A O    1 
ATOM   3285 O O    B ALA   A 1 154 ? 14.580 -3.080  6.223   0.38 9.12  ?  154 ALA   A O    1 
ATOM   3286 C CB   A ALA   A 1 154 ? 14.788 -3.078  8.679   0.62 11.05 ?  154 ALA   A CB   1 
ATOM   3287 C CB   B ALA   A 1 154 ? 14.930 -3.043  9.173   0.38 10.14 ?  154 ALA   A CB   1 
ATOM   3288 H H    A ALA   A 1 154 ? 15.677 -5.133  7.407   0.62 12.41 ?  154 ALA   A H    1 
ATOM   3289 H H    B ALA   A 1 154 ? 15.832 -5.031  7.912   0.38 11.20 ?  154 ALA   A H    1 
ATOM   3290 H HA   A ALA   A 1 154 ? 13.276 -4.458  8.488   0.62 12.49 ?  154 ALA   A HA   1 
ATOM   3291 H HA   B ALA   A 1 154 ? 13.383 -4.356  8.850   0.38 11.49 ?  154 ALA   A HA   1 
ATOM   3292 H HB1  A ALA   A 1 154 ? 14.187 -2.328  8.809   0.62 13.28 ?  154 ALA   A HB1  1 
ATOM   3293 H HB1  B ALA   A 1 154 ? 14.350 -2.282  9.336   0.38 12.18 ?  154 ALA   A HB1  1 
ATOM   3294 H HB2  A ALA   A 1 154 ? 15.098 -3.408  9.537   0.62 13.28 ?  154 ALA   A HB2  1 
ATOM   3295 H HB2  B ALA   A 1 154 ? 15.203 -3.438  10.016  0.38 12.18 ?  154 ALA   A HB2  1 
ATOM   3296 H HB3  A ALA   A 1 154 ? 15.547 -2.803  8.139   0.62 13.28 ?  154 ALA   A HB3  1 
ATOM   3297 H HB3  B ALA   A 1 154 ? 15.714 -2.758  8.674   0.38 12.18 ?  154 ALA   A HB3  1 
ATOM   3298 N N    A VAL   A 1 155 ? 12.230 -3.700  6.411   0.32 7.75  ?  155 VAL   A N    1 
ATOM   3299 N N    B VAL   A 1 155 ? 12.428 -3.503  6.762   0.38 8.93  ?  155 VAL   A N    1 
ATOM   3300 C CA   A VAL   A 1 155 ? 11.585 -3.196  5.202   0.32 10.03 ?  155 VAL   A CA   1 
ATOM   3301 C CA   B VAL   A 1 155 ? 11.860 -2.981  5.524   0.38 10.40 ?  155 VAL   A CA   1 
ATOM   3302 C CA   T VAL   A 1 155 ? 11.615 -3.245  5.246   0.30 12.47 ?  155 VAL   A CA   1 
ATOM   3303 C C    A VAL   A 1 155 ? 10.881 -1.894  5.566   0.32 11.33 ?  155 VAL   A C    1 
ATOM   3304 C C    B VAL   A 1 155 ? 11.035 -1.750  5.880   0.38 11.16 ?  155 VAL   A C    1 
ATOM   3305 C C    T VAL   A 1 155 ? 10.990 -1.876  5.533   0.30 12.27 ?  155 VAL   A C    1 
ATOM   3306 O O    A VAL   A 1 155 ? 9.917  -1.902  6.340   0.32 11.92 ?  155 VAL   A O    1 
ATOM   3307 O O    B VAL   A 1 155 ? 10.013 -1.856  6.569   0.38 11.99 ?  155 VAL   A O    1 
ATOM   3308 O O    T VAL   A 1 155 ? 10.120 -1.749  6.392   0.30 12.31 ?  155 VAL   A O    1 
ATOM   3309 C CB   A VAL   A 1 155 ? 10.588 -4.215  4.633   0.32 10.56 ?  155 VAL   A CB   1 
ATOM   3310 C CB   B VAL   A 1 155 ? 11.020 -4.037  4.794   0.38 10.93 ?  155 VAL   A CB   1 
ATOM   3311 C CB   T VAL   A 1 155 ? 10.579 -4.258  4.720   0.30 12.47 ?  155 VAL   A CB   1 
ATOM   3312 C CG1  A VAL   A 1 155 ? 9.940  -3.678  3.366   0.32 10.98 ?  155 VAL   A CG1  1 
ATOM   3313 C CG1  B VAL   A 1 155 ? 10.323 -3.420  3.597   0.38 11.55 ?  155 VAL   A CG1  1 
ATOM   3314 C CG1  T VAL   A 1 155 ? 9.887  -3.717  3.480   0.30 12.67 ?  155 VAL   A CG1  1 
ATOM   3315 C CG2  A VAL   A 1 155 ? 11.276 -5.549  4.372   0.32 11.37 ?  155 VAL   A CG2  1 
ATOM   3316 C CG2  B VAL   A 1 155 ? 11.908 -5.201  4.358   0.38 10.89 ?  155 VAL   A CG2  1 
ATOM   3317 C CG2  T VAL   A 1 155 ? 11.243 -5.600  4.422   0.30 12.87 ?  155 VAL   A CG2  1 
ATOM   3318 H H    A VAL   A 1 155 ? 11.675 -4.023  6.984   0.32 9.31  ?  155 VAL   A H    1 
ATOM   3319 H H    B VAL   A 1 155 ? 11.837 -3.796  7.314   0.38 10.74 ?  155 VAL   A H    1 
ATOM   3320 H HA   A VAL   A 1 155 ? 12.258 -3.006  4.531   0.32 12.05 ?  155 VAL   A HA   1 
ATOM   3321 H HA   B VAL   A 1 155 ? 12.577 -2.703  4.935   0.38 12.50 ?  155 VAL   A HA   1 
ATOM   3322 H HB   A VAL   A 1 155 ? 9.886  -4.362  5.288   0.32 12.69 ?  155 VAL   A HB   1 
ATOM   3323 H HB   B VAL   A 1 155 ? 10.343 -4.380  5.400   0.38 13.13 ?  155 VAL   A HB   1 
ATOM   3324 H HB   T VAL   A 1 155 ? 9.907  -4.401  5.404   0.30 14.98 ?  155 VAL   A HB   1 
ATOM   3325 H HG11 A VAL   A 1 155 ? 9.420  -4.386  2.957   0.32 13.19 ?  155 VAL   A HG11 1 
ATOM   3326 H HG11 B VAL   A 1 155 ? 10.001 -4.131  3.023   0.38 13.87 ?  155 VAL   A HG11 1 
ATOM   3327 H HG11 T VAL   A 1 155 ? 9.373  -4.429  3.071   0.30 15.21 ?  155 VAL   A HG11 1 
ATOM   3328 H HG12 A VAL   A 1 155 ? 9.361  -2.933  3.595   0.32 13.19 ?  155 VAL   A HG12 1 
ATOM   3329 H HG12 B VAL   A 1 155 ? 9.575  -2.883  3.906   0.38 13.87 ?  155 VAL   A HG12 1 
ATOM   3330 H HG12 T VAL   A 1 155 ? 9.299  -2.989  3.736   0.30 15.21 ?  155 VAL   A HG12 1 
ATOM   3331 H HG13 A VAL   A 1 155 ? 10.635 -3.383  2.758   0.32 13.19 ?  155 VAL   A HG13 1 
ATOM   3332 H HG13 B VAL   A 1 155 ? 10.955 -2.865  3.116   0.38 13.87 ?  155 VAL   A HG13 1 
ATOM   3333 H HG13 T VAL   A 1 155 ? 10.560 -3.396  2.858   0.30 15.21 ?  155 VAL   A HG13 1 
ATOM   3334 H HG21 A VAL   A 1 155 ? 10.647 -6.145  3.939   0.32 13.66 ?  155 VAL   A HG21 1 
ATOM   3335 H HG21 B VAL   A 1 155 ? 11.362 -5.855  3.892   0.38 13.09 ?  155 VAL   A HG21 1 
ATOM   3336 H HG21 T VAL   A 1 155 ? 10.571 -6.219  4.097   0.30 15.46 ?  155 VAL   A HG21 1 
ATOM   3337 H HG22 A VAL   A 1 155 ? 12.042 -5.398  3.796   0.32 13.66 ?  155 VAL   A HG22 1 
ATOM   3338 H HG22 B VAL   A 1 155 ? 12.599 -4.866  3.767   0.38 13.09 ?  155 VAL   A HG22 1 
ATOM   3339 H HG22 T VAL   A 1 155 ? 11.928 -5.470  3.745   0.30 15.46 ?  155 VAL   A HG22 1 
ATOM   3340 H HG23 A VAL   A 1 155 ? 11.566 -5.927  5.216   0.32 13.66 ?  155 VAL   A HG23 1 
ATOM   3341 H HG23 B VAL   A 1 155 ? 12.309 -5.606  5.143   0.38 13.09 ?  155 VAL   A HG23 1 
ATOM   3342 H HG23 T VAL   A 1 155 ? 11.644 -5.943  5.235   0.30 15.46 ?  155 VAL   A HG23 1 
ATOM   3343 N N    A PHE   A 1 156 ? 11.343 -0.775  4.993   0.32 12.57 ?  156 PHE   A N    1 
ATOM   3344 N N    B PHE   A 1 156 ? 11.486 -0.577  5.417   0.38 11.08 ?  156 PHE   A N    1 
ATOM   3345 N N    T PHE   A 1 156 ? 11.446 -0.856  4.801   0.30 12.47 ?  156 PHE   A N    1 
ATOM   3346 C CA   A PHE   A 1 156 ? 10.816 0.536   5.378   0.32 14.12 ?  156 PHE   A CA   1 
ATOM   3347 C CA   B PHE   A 1 156 ? 10.869 0.683   5.831   0.38 12.32 ?  156 PHE   A CA   1 
ATOM   3348 C CA   T PHE   A 1 156 ? 11.023 0.519   5.066   0.30 12.54 ?  156 PHE   A CA   1 
ATOM   3349 C C    A PHE   A 1 156 ? 9.364  0.717   4.947   0.32 14.24 ?  156 PHE   A C    1 
ATOM   3350 C C    B PHE   A 1 156 ? 9.476  0.863   5.230   0.38 12.10 ?  156 PHE   A C    1 
ATOM   3351 C C    T PHE   A 1 156 ? 9.562  0.740   4.685   0.30 12.92 ?  156 PHE   A C    1 
ATOM   3352 O O    A PHE   A 1 156 ? 8.548  1.250   5.709   0.32 14.53 ?  156 PHE   A O    1 
ATOM   3353 O O    B PHE   A 1 156 ? 8.541  1.268   5.931   0.38 12.82 ?  156 PHE   A O    1 
ATOM   3354 O O    T PHE   A 1 156 ? 8.796  1.351   5.440   0.30 13.45 ?  156 PHE   A O    1 
ATOM   3355 C CB   A PHE   A 1 156 ? 11.692 1.651   4.794   0.32 15.87 ?  156 PHE   A CB   1 
ATOM   3356 C CB   B PHE   A 1 156 ? 11.787 1.845   5.433   0.38 14.00 ?  156 PHE   A CB   1 
ATOM   3357 C CB   T PHE   A 1 156 ? 11.926 1.484   4.292   0.30 11.96 ?  156 PHE   A CB   1 
ATOM   3358 C CG   A PHE   A 1 156 ? 11.198 3.044   5.112   0.32 16.87 ?  156 PHE   A CG   1 
ATOM   3359 C CG   B PHE   A 1 156 ? 11.393 3.179   6.018   0.38 16.15 ?  156 PHE   A CG   1 
ATOM   3360 C CG   T PHE   A 1 156 ? 11.588 2.939   4.498   0.30 12.29 ?  156 PHE   A CG   1 
ATOM   3361 C CD1  A PHE   A 1 156 ? 11.143 3.488   6.423   0.32 17.24 ?  156 PHE   A CD1  1 
ATOM   3362 C CD1  B PHE   A 1 156 ? 10.654 3.265   7.188   0.38 17.14 ?  156 PHE   A CD1  1 
ATOM   3363 C CD1  T PHE   A 1 156 ? 11.966 3.587   5.666   0.30 13.37 ?  156 PHE   A CD1  1 
ATOM   3364 C CD2  A PHE   A 1 156 ? 10.801 3.910   4.101   0.32 17.46 ?  156 PHE   A CD2  1 
ATOM   3365 C CD2  B PHE   A 1 156 ? 11.779 4.354   5.392   0.38 17.27 ?  156 PHE   A CD2  1 
ATOM   3366 C CD2  T PHE   A 1 156 ? 10.907 3.660   3.527   0.30 13.13 ?  156 PHE   A CD2  1 
ATOM   3367 C CE1  A PHE   A 1 156 ? 10.693 4.763   6.724   0.32 17.55 ?  156 PHE   A CE1  1 
ATOM   3368 C CE1  B PHE   A 1 156 ? 10.304 4.496   7.716   0.38 17.86 ?  156 PHE   A CE1  1 
ATOM   3369 C CE1  T PHE   A 1 156 ? 11.665 4.920   5.868   0.30 14.06 ?  156 PHE   A CE1  1 
ATOM   3370 C CE2  A PHE   A 1 156 ? 10.349 5.188   4.396   0.32 17.90 ?  156 PHE   A CE2  1 
ATOM   3371 C CE2  B PHE   A 1 156 ? 11.430 5.585   5.914   0.38 17.77 ?  156 PHE   A CE2  1 
ATOM   3372 C CE2  T PHE   A 1 156 ? 10.606 4.999   3.724   0.30 13.90 ?  156 PHE   A CE2  1 
ATOM   3373 C CZ   A PHE   A 1 156 ? 10.300 5.615   5.708   0.32 17.88 ?  156 PHE   A CZ   1 
ATOM   3374 C CZ   B PHE   A 1 156 ? 10.695 5.656   7.079   0.38 18.04 ?  156 PHE   A CZ   1 
ATOM   3375 C CZ   T PHE   A 1 156 ? 10.985 5.626   4.896   0.30 13.94 ?  156 PHE   A CZ   1 
ATOM   3376 H H    A PHE   A 1 156 ? 11.956 -0.753  4.389   0.32 15.10 ?  156 PHE   A H    1 
ATOM   3377 H H    B PHE   A 1 156 ? 12.162 -0.482  4.884   0.38 13.31 ?  156 PHE   A H    1 
ATOM   3378 H H    T PHE   A 1 156 ? 12.006 -0.941  4.157   0.30 14.98 ?  156 PHE   A H    1 
ATOM   3379 H HA   A PHE   A 1 156 ? 10.855 0.616   6.343   0.32 16.95 ?  156 PHE   A HA   1 
ATOM   3380 H HA   B PHE   A 1 156 ? 10.798 0.682   6.798   0.38 14.80 ?  156 PHE   A HA   1 
ATOM   3381 H HA   T PHE   A 1 156 ? 11.127 0.703   6.016   0.30 15.06 ?  156 PHE   A HA   1 
ATOM   3382 H HB2  A PHE   A 1 156 ? 12.591 1.569   5.153   0.32 19.06 ?  156 PHE   A HB2  1 
ATOM   3383 H HB2  B PHE   A 1 156 ? 12.690 1.656   5.738   0.38 16.82 ?  156 PHE   A HB2  1 
ATOM   3384 H HB2  T PHE   A 1 156 ? 12.845 1.348   4.577   0.30 14.36 ?  156 PHE   A HB2  1 
ATOM   3385 H HB3  A PHE   A 1 156 ? 11.716 1.560   3.829   0.32 19.06 ?  156 PHE   A HB3  1 
ATOM   3386 H HB3  B PHE   A 1 156 ? 11.786 1.940   4.466   0.38 16.82 ?  156 PHE   A HB3  1 
ATOM   3387 H HB3  T PHE   A 1 156 ? 11.845 1.291   3.346   0.30 14.36 ?  156 PHE   A HB3  1 
ATOM   3388 H HD1  A PHE   A 1 156 ? 11.407 2.920   7.111   0.32 20.71 ?  156 PHE   A HD1  1 
ATOM   3389 H HD1  B PHE   A 1 156 ? 10.393 2.486   7.621   0.38 20.58 ?  156 PHE   A HD1  1 
ATOM   3390 H HD1  T PHE   A 1 156 ? 12.423 3.110   6.326   0.30 16.06 ?  156 PHE   A HD1  1 
ATOM   3391 H HD2  A PHE   A 1 156 ? 10.835 3.628   3.215   0.32 20.97 ?  156 PHE   A HD2  1 
ATOM   3392 H HD2  B PHE   A 1 156 ? 12.280 4.319   4.607   0.38 20.74 ?  156 PHE   A HD2  1 
ATOM   3393 H HD2  T PHE   A 1 156 ? 10.648 3.235   2.742   0.30 15.77 ?  156 PHE   A HD2  1 
ATOM   3394 H HE1  A PHE   A 1 156 ? 10.659 5.046   7.610   0.32 21.07 ?  156 PHE   A HE1  1 
ATOM   3395 H HE1  B PHE   A 1 156 ? 9.806  4.537   8.500   0.38 21.45 ?  156 PHE   A HE1  1 
ATOM   3396 H HE1  T PHE   A 1 156 ? 11.921 5.336   6.659   0.30 16.89 ?  156 PHE   A HE1  1 
ATOM   3397 H HE2  A PHE   A 1 156 ? 10.085 5.759   3.711   0.32 21.50 ?  156 PHE   A HE2  1 
ATOM   3398 H HE2  B PHE   A 1 156 ? 11.695 6.366   5.483   0.38 21.34 ?  156 PHE   A HE2  1 
ATOM   3399 H HE2  T PHE   A 1 156 ? 10.142 5.469   3.074   0.30 16.70 ?  156 PHE   A HE2  1 
ATOM   3400 H HZ   A PHE   A 1 156 ? 9.995  6.471   5.911   0.32 21.47 ?  156 PHE   A HZ   1 
ATOM   3401 H HZ   B PHE   A 1 156 ? 10.457 6.482   7.431   0.38 21.67 ?  156 PHE   A HZ   1 
ATOM   3402 H HZ   T PHE   A 1 156 ? 10.779 6.520   5.034   0.30 16.74 ?  156 PHE   A HZ   1 
ATOM   3403 N N    A ASP   A 1 157 ? 9.023  0.293   3.734   0.32 14.60 ?  157 ASP   A N    1 
ATOM   3404 N N    B ASP   A 1 157 ? 9.321  0.579   3.938   0.38 11.45 ?  157 ASP   A N    1 
ATOM   3405 N N    T ASP   A 1 157 ? 9.168  0.269   3.505   0.30 13.12 ?  157 ASP   A N    1 
ATOM   3406 C CA   A ASP   A 1 157 ? 7.698  0.548   3.181   0.32 15.75 ?  157 ASP   A CA   1 
ATOM   3407 C CA   B ASP   A 1 157 ? 8.080  0.874   3.228   0.38 11.36 ?  157 ASP   A CA   1 
ATOM   3408 C CA   T ASP   A 1 157 ? 7.853  0.557   2.946   0.30 13.62 ?  157 ASP   A CA   1 
ATOM   3409 C C    A ASP   A 1 157 ? 6.713  -0.495  3.699   0.32 16.56 ?  157 ASP   A C    1 
ATOM   3410 C C    B ASP   A 1 157 ? 6.990  -0.112  3.639   0.38 11.32 ?  157 ASP   A C    1 
ATOM   3411 C C    T ASP   A 1 157 ? 6.829  -0.413  3.522   0.30 14.16 ?  157 ASP   A C    1 
ATOM   3412 O O    A ASP   A 1 157 ? 6.857  -1.690  3.414   0.32 16.55 ?  157 ASP   A O    1 
ATOM   3413 O O    B ASP   A 1 157 ? 7.144  -1.328  3.474   0.38 11.83 ?  157 ASP   A O    1 
ATOM   3414 O O    T ASP   A 1 157 ? 6.917  -1.625  3.295   0.30 14.19 ?  157 ASP   A O    1 
ATOM   3415 C CB   A ASP   A 1 157 ? 7.764  0.511   1.657   0.32 16.65 ?  157 ASP   A CB   1 
ATOM   3416 C CB   B ASP   A 1 157 ? 8.335  0.799   1.724   0.38 11.02 ?  157 ASP   A CB   1 
ATOM   3417 C CB   T ASP   A 1 157 ? 7.917  0.415   1.428   0.30 14.25 ?  157 ASP   A CB   1 
ATOM   3418 C CG   A ASP   A 1 157 ? 6.509  1.041   1.003   0.32 17.53 ?  157 ASP   A CG   1 
ATOM   3419 C CG   B ASP   A 1 157 ? 7.136  1.235   0.908   0.38 11.74 ?  157 ASP   A CG   1 
ATOM   3420 C CG   T ASP   A 1 157 ? 6.711  1.009   0.733   0.30 14.61 ?  157 ASP   A CG   1 
ATOM   3421 O OD1  A ASP   A 1 157 ? 6.241  2.253   1.133   0.32 18.60 ?  157 ASP   A OD1  1 
ATOM   3422 O OD1  B ASP   A 1 157 ? 6.152  0.462   0.827   0.38 12.43 ?  157 ASP   A OD1  1 
ATOM   3423 O OD1  T ASP   A 1 157 ? 5.602  0.454   0.890   0.30 15.06 ?  157 ASP   A OD1  1 
ATOM   3424 O OD2  A ASP   A 1 157 ? 5.794  0.247   0.354   0.32 17.38 -1 157 ASP   A OD2  1 
ATOM   3425 O OD2  B ASP   A 1 157 ? 7.176  2.362   0.366   0.38 12.42 -1 157 ASP   A OD2  1 
ATOM   3426 O OD2  T ASP   A 1 157 ? 6.867  2.033   0.037   0.30 14.83 -1 157 ASP   A OD2  1 
ATOM   3427 H H    A ASP   A 1 157 ? 9.548  -0.149  3.211   0.32 17.54 ?  157 ASP   A H    1 
ATOM   3428 H H    B ASP   A 1 157 ? 9.938  0.222   3.453   0.38 13.76 ?  157 ASP   A H    1 
ATOM   3429 H H    T ASP   A 1 157 ? 9.659  -0.225  3.004   0.30 15.76 ?  157 ASP   A H    1 
ATOM   3430 H HA   A ASP   A 1 157 ? 7.400  1.428   3.461   0.32 18.91 ?  157 ASP   A HA   1 
ATOM   3431 H HA   B ASP   A 1 157 ? 7.798  1.781   3.450   0.38 13.64 ?  157 ASP   A HA   1 
ATOM   3432 H HA   T ASP   A 1 157 ? 7.597  1.469   3.168   0.30 16.36 ?  157 ASP   A HA   1 
ATOM   3433 H HB2  A ASP   A 1 157 ? 8.514  1.045   1.362   0.32 20.00 ?  157 ASP   A HB2  1 
ATOM   3434 H HB2  B ASP   A 1 157 ? 9.099  1.366   1.504   0.38 13.24 ?  157 ASP   A HB2  1 
ATOM   3435 H HB2  T ASP   A 1 157 ? 8.720  0.844   1.102   0.30 17.11 ?  157 ASP   A HB2  1 
ATOM   3436 H HB3  A ASP   A 1 157 ? 7.877  -0.404  1.371   0.32 20.00 ?  157 ASP   A HB3  1 
ATOM   3437 H HB3  B ASP   A 1 157 ? 8.541  -0.120  1.491   0.38 13.24 ?  157 ASP   A HB3  1 
ATOM   3438 H HB3  T ASP   A 1 157 ? 7.939  -0.529  1.207   0.30 17.11 ?  157 ASP   A HB3  1 
ATOM   3439 N N    A LYS   A 1 158 ? 5.707  -0.042  4.454   0.32 17.53 ?  158 LYS   A N    1 
ATOM   3440 N N    B LYS   A 1 158 ? 5.879  0.416   4.161   0.38 11.06 ?  158 LYS   A N    1 
ATOM   3441 N N    T LYS   A 1 158 ? 5.851  0.120   4.261   0.30 15.30 ?  158 LYS   A N    1 
ATOM   3442 C CA   A LYS   A 1 158 ? 4.731  -0.973  5.017   0.32 18.55 ?  158 LYS   A CA   1 
ATOM   3443 C CA   B LYS   A 1 158 ? 4.827  -0.447  4.694   0.38 11.10 ?  158 LYS   A CA   1 
ATOM   3444 C CA   T LYS   A 1 158 ? 4.855  -0.745  4.888   0.30 16.86 ?  158 LYS   A CA   1 
ATOM   3445 C C    A LYS   A 1 158 ? 3.965  -1.699  3.919   0.32 18.11 ?  158 LYS   A C    1 
ATOM   3446 C C    B LYS   A 1 158 ? 4.175  -1.274  3.592   0.38 10.74 ?  158 LYS   A C    1 
ATOM   3447 C C    T LYS   A 1 158 ? 4.066  -1.530  3.847   0.30 16.75 ?  158 LYS   A C    1 
ATOM   3448 O O    A LYS   A 1 158 ? 3.730  -2.910  4.012   0.32 18.22 ?  158 LYS   A O    1 
ATOM   3449 O O    B LYS   A 1 158 ? 3.946  -2.480  3.755   0.38 11.56 ?  158 LYS   A O    1 
ATOM   3450 O O    T LYS   A 1 158 ? 3.803  -2.725  4.027   0.30 16.97 ?  158 LYS   A O    1 
ATOM   3451 C CB   A LYS   A 1 158 ? 3.771  -0.237  5.955   0.32 20.09 ?  158 LYS   A CB   1 
ATOM   3452 C CB   B LYS   A 1 158 ? 3.767  0.379   5.428   0.38 12.55 ?  158 LYS   A CB   1 
ATOM   3453 C CB   T LYS   A 1 158 ? 3.914  0.071   5.778   0.30 18.86 ?  158 LYS   A CB   1 
ATOM   3454 C CG   A LYS   A 1 158 ? 2.526  -1.037  6.358   0.32 21.70 ?  158 LYS   A CG   1 
ATOM   3455 C CG   B LYS   A 1 158 ? 2.553  -0.459  5.825   0.38 14.48 ?  158 LYS   A CG   1 
ATOM   3456 C CG   T LYS   A 1 158 ? 2.681  -0.701  6.255   0.30 20.74 ?  158 LYS   A CG   1 
ATOM   3457 C CD   A LYS   A 1 158 ? 2.863  -2.317  7.125   0.32 23.21 ?  158 LYS   A CD   1 
ATOM   3458 C CD   B LYS   A 1 158 ? 1.484  0.344   6.529   0.38 16.09 ?  158 LYS   A CD   1 
ATOM   3459 C CD   T LYS   A 1 158 ? 3.049  -1.934  7.077   0.30 22.43 ?  158 LYS   A CD   1 
ATOM   3460 C CE   A LYS   A 1 158 ? 1.598  -2.995  7.649   0.32 23.98 ?  158 LYS   A CE   1 
ATOM   3461 C CE   B LYS   A 1 158 ? 0.329  -0.549  6.966   0.38 16.86 ?  158 LYS   A CE   1 
ATOM   3462 C CE   T LYS   A 1 158 ? 1.807  -2.735  7.465   0.30 23.47 ?  158 LYS   A CE   1 
ATOM   3463 N NZ   A LYS   A 1 158 ? 1.865  -4.324  8.270   0.32 24.30 ?  158 LYS   A NZ   1 
ATOM   3464 N NZ   B LYS   A 1 158 ? -0.339 -1.239  5.826   0.38 17.44 ?  158 LYS   A NZ   1 
ATOM   3465 N NZ   T LYS   A 1 158 ? 2.131  -3.951  8.269   0.30 23.82 ?  158 LYS   A NZ   1 
ATOM   3466 H H    A LYS   A 1 158 ? 5.572  0.786   4.649   0.32 21.05 ?  158 LYS   A H    1 
ATOM   3467 H H    B LYS   A 1 158 ? 5.717  1.265   4.212   0.38 13.29 ?  158 LYS   A H    1 
ATOM   3468 H H    T LYS   A 1 158 ? 5.749  0.964   4.411   0.30 18.38 ?  158 LYS   A H    1 
ATOM   3469 H HA   A LYS   A 1 158 ? 5.203  -1.637  5.540   0.32 22.27 ?  158 LYS   A HA   1 
ATOM   3470 H HA   B LYS   A 1 158 ? 5.224  -1.053  5.337   0.38 13.34 ?  158 LYS   A HA   1 
ATOM   3471 H HA   T LYS   A 1 158 ? 5.316  -1.380  5.455   0.30 20.24 ?  158 LYS   A HA   1 
ATOM   3472 H HB2  A LYS   A 1 158 ? 4.247  -0.007  6.771   0.32 24.12 ?  158 LYS   A HB2  1 
ATOM   3473 H HB2  B LYS   A 1 158 ? 4.156  0.751   6.241   0.38 15.08 ?  158 LYS   A HB2  1 
ATOM   3474 H HB2  T LYS   A 1 158 ? 4.403  0.361   6.567   0.30 22.65 ?  158 LYS   A HB2  1 
ATOM   3475 H HB3  A LYS   A 1 158 ? 3.470  0.575   5.519   0.32 24.12 ?  158 LYS   A HB3  1 
ATOM   3476 H HB3  B LYS   A 1 158 ? 3.465  1.099   4.851   0.38 15.08 ?  158 LYS   A HB3  1 
ATOM   3477 H HB3  T LYS   A 1 158 ? 3.606  0.846   5.283   0.30 22.65 ?  158 LYS   A HB3  1 
ATOM   3478 H HG2  A LYS   A 1 158 ? 1.977  -0.485  6.934   0.32 26.06 ?  158 LYS   A HG2  1 
ATOM   3479 H HG2  B LYS   A 1 158 ? 2.151  -0.837  5.030   0.38 17.39 ?  158 LYS   A HG2  1 
ATOM   3480 H HG2  T LYS   A 1 158 ? 2.147  -0.120  6.816   0.30 24.91 ?  158 LYS   A HG2  1 
ATOM   3481 H HG3  A LYS   A 1 158 ? 2.021  -1.280  5.565   0.32 26.06 ?  158 LYS   A HG3  1 
ATOM   3482 H HG3  B LYS   A 1 158 ? 2.846  -1.167  6.420   0.38 17.39 ?  158 LYS   A HG3  1 
ATOM   3483 H HG3  T LYS   A 1 158 ? 2.156  -0.988  5.490   0.30 24.91 ?  158 LYS   A HG3  1 
ATOM   3484 H HD2  A LYS   A 1 158 ? 3.320  -2.935  6.535   0.32 27.87 ?  158 LYS   A HD2  1 
ATOM   3485 H HD2  B LYS   A 1 158 ? 1.864  0.764   7.315   0.38 19.32 ?  158 LYS   A HD2  1 
ATOM   3486 H HD2  T LYS   A 1 158 ? 3.629  -2.512  6.558   0.30 26.93 ?  158 LYS   A HD2  1 
ATOM   3487 H HD3  A LYS   A 1 158 ? 3.426  -2.096  7.883   0.32 27.87 ?  158 LYS   A HD3  1 
ATOM   3488 H HD3  B LYS   A 1 158 ? 1.139  1.018   5.920   0.38 19.32 ?  158 LYS   A HD3  1 
ATOM   3489 H HD3  T LYS   A 1 158 ? 3.495  -1.656  7.893   0.30 26.93 ?  158 LYS   A HD3  1 
ATOM   3490 H HE2  A LYS   A 1 158 ? 1.190  -2.427  8.322   0.32 28.79 ?  158 LYS   A HE2  1 
ATOM   3491 H HE2  B LYS   A 1 158 ? 0.668  -1.229  7.566   0.38 20.25 ?  158 LYS   A HE2  1 
ATOM   3492 H HE2  T LYS   A 1 158 ? 1.217  -2.176  7.995   0.30 28.18 ?  158 LYS   A HE2  1 
ATOM   3493 H HE3  A LYS   A 1 158 ? 0.981  -3.126  6.912   0.32 28.79 ?  158 LYS   A HE3  1 
ATOM   3494 H HE3  B LYS   A 1 158 ? -0.334 -0.005  7.417   0.38 20.25 ?  158 LYS   A HE3  1 
ATOM   3495 H HE3  T LYS   A 1 158 ? 1.349  -3.025  6.659   0.30 28.18 ?  158 LYS   A HE3  1 
ATOM   3496 H HZ1  A LYS   A 1 158 ? 1.104  -4.684  8.560   0.32 29.18 ?  158 LYS   A HZ1  1 
ATOM   3497 H HZ1  B LYS   A 1 158 ? -1.020 -1.727  6.122   0.38 20.94 ?  158 LYS   A HZ1  1 
ATOM   3498 H HZ1  T LYS   A 1 158 ? 1.383  -4.391  8.475   0.30 28.61 ?  158 LYS   A HZ1  1 
ATOM   3499 H HZ2  A LYS   A 1 158 ? 2.232  -4.871  7.671   0.32 29.18 ?  158 LYS   A HZ2  1 
ATOM   3500 H HZ2  B LYS   A 1 158 ? -0.645 -0.638  5.243   0.38 20.94 ?  158 LYS   A HZ2  1 
ATOM   3501 H HZ2  T LYS   A 1 158 ? 2.663  -4.492  7.804   0.30 28.61 ?  158 LYS   A HZ2  1 
ATOM   3502 H HZ3  A LYS   A 1 158 ? 2.422  -4.233  8.958   0.32 29.18 ?  158 LYS   A HZ3  1 
ATOM   3503 H HZ3  B LYS   A 1 158 ? 0.241  -1.772  5.410   0.38 20.94 ?  158 LYS   A HZ3  1 
ATOM   3504 H HZ3  T LYS   A 1 158 ? 2.543  -3.718  9.022   0.30 28.61 ?  158 LYS   A HZ3  1 
ATOM   3505 N N    A ASN   A 1 159 ? 3.553  -0.977  2.876   0.32 17.70 ?  159 ASN   A N    1 
ATOM   3506 N N    B ASN   A 1 159 ? 3.827  -0.636  2.474   0.38 10.69 ?  159 ASN   A N    1 
ATOM   3507 N N    T ASN   A 1 159 ? 3.663  -0.877  2.763   0.30 16.92 ?  159 ASN   A N    1 
ATOM   3508 C CA   A ASN   A 1 159 ? 2.866  -1.635  1.771   0.32 17.11 ?  159 ASN   A CA   1 
ATOM   3509 C CA   B ASN   A 1 159 ? 3.173  -1.371  1.398   0.38 12.07 ?  159 ASN   A CA   1 
ATOM   3510 C CA   T ASN   A 1 159 ? 2.907  -1.563  1.722   0.30 17.04 ?  159 ASN   A CA   1 
ATOM   3511 C C    A ASN   A 1 159 ? 3.753  -2.692  1.123   0.32 16.31 ?  159 ASN   A C    1 
ATOM   3512 C C    B ASN   A 1 159 ? 4.067  -2.491  0.875   0.38 12.46 ?  159 ASN   A C    1 
ATOM   3513 C C    T ASN   A 1 159 ? 3.720  -2.678  1.064   0.30 17.10 ?  159 ASN   A C    1 
ATOM   3514 O O    A ASN   A 1 159 ? 3.293  -3.801  0.824   0.32 16.01 ?  159 ASN   A O    1 
ATOM   3515 O O    B ASN   A 1 159 ? 3.589  -3.597  0.587   0.38 12.41 ?  159 ASN   A O    1 
ATOM   3516 O O    T ASN   A 1 159 ? 3.175  -3.730  0.723   0.30 17.11 ?  159 ASN   A O    1 
ATOM   3517 C CB   A ASN   A 1 159 ? 2.379  -0.601  0.755   0.32 17.44 ?  159 ASN   A CB   1 
ATOM   3518 C CB   B ASN   A 1 159 ? 2.765  -0.409  0.281   0.38 13.83 ?  159 ASN   A CB   1 
ATOM   3519 C CB   T ASN   A 1 159 ? 2.389  -0.567  0.680   0.30 17.33 ?  159 ASN   A CB   1 
ATOM   3520 C CG   A ASN   A 1 159 ? 1.135  0.133   1.225   0.32 18.18 ?  159 ASN   A CG   1 
ATOM   3521 C CG   B ASN   A 1 159 ? 1.538  0.414   0.642   0.38 15.14 ?  159 ASN   A CG   1 
ATOM   3522 C CG   T ASN   A 1 159 ? 1.165  0.190   1.162   0.30 17.92 ?  159 ASN   A CG   1 
ATOM   3523 O OD1  A ASN   A 1 159 ? 0.316  -0.426  1.957   0.32 18.83 ?  159 ASN   A OD1  1 
ATOM   3524 O OD1  B ASN   A 1 159 ? 0.706  -0.008  1.443   0.38 16.12 ?  159 ASN   A OD1  1 
ATOM   3525 O OD1  T ASN   A 1 159 ? 0.385  -0.322  1.966   0.30 18.53 ?  159 ASN   A OD1  1 
ATOM   3526 N ND2  A ASN   A 1 159 ? 0.984  1.384   0.805   0.32 18.24 ?  159 ASN   A ND2  1 
ATOM   3527 N ND2  B ASN   A 1 159 ? 1.425  1.601   0.055   0.38 15.50 ?  159 ASN   A ND2  1 
ATOM   3528 N ND2  T ASN   A 1 159 ? 0.987  1.410   0.670   0.30 17.97 ?  159 ASN   A ND2  1 
ATOM   3529 H H    A ASN   A 1 159 ? 3.650  -0.126  2.792   0.32 21.26 ?  159 ASN   A H    1 
ATOM   3530 H H    B ASN   A 1 159 ? 3.967  0.201   2.316   0.38 12.85 ?  159 ASN   A H    1 
ATOM   3531 H H    T ASN   A 1 159 ? 3.799  -0.040  2.616   0.30 20.32 ?  159 ASN   A H    1 
ATOM   3532 H HA   A ASN   A 1 159 ? 2.088  -2.091  2.121   0.32 20.55 ?  159 ASN   A HA   1 
ATOM   3533 H HA   B ASN   A 1 159 ? 2.368  -1.776  1.747   0.38 14.50 ?  159 ASN   A HA   1 
ATOM   3534 H HA   T ASN   A 1 159 ? 2.138  -1.980  2.131   0.30 20.46 ?  159 ASN   A HA   1 
ATOM   3535 H HB2  A ASN   A 1 159 ? 3.077  0.056   0.608   0.32 20.94 ?  159 ASN   A HB2  1 
ATOM   3536 H HB2  B ASN   A 1 159 ? 3.495  0.208   0.107   0.38 16.61 ?  159 ASN   A HB2  1 
ATOM   3537 H HB2  T ASN   A 1 159 ? 3.083  0.081   0.484   0.30 20.81 ?  159 ASN   A HB2  1 
ATOM   3538 H HB3  A ASN   A 1 159 ? 2.165  -1.052  -0.077  0.32 20.94 ?  159 ASN   A HB3  1 
ATOM   3539 H HB3  B ASN   A 1 159 ? 2.560  -0.917  -0.517  0.38 16.61 ?  159 ASN   A HB3  1 
ATOM   3540 H HB3  T ASN   A 1 159 ? 2.147  -1.051  -0.126  0.30 20.81 ?  159 ASN   A HB3  1 
ATOM   3541 H HD21 A ASN   A 1 159 ? 0.295  1.841   1.046   0.32 21.91 ?  159 ASN   A HD21 1 
ATOM   3542 H HD21 B ASN   A 1 159 ? 0.742  2.100   0.226   0.38 18.61 ?  159 ASN   A HD21 1 
ATOM   3543 H HD21 T ASN   A 1 159 ? 0.306  1.877   0.913   0.30 21.58 ?  159 ASN   A HD21 1 
ATOM   3544 H HD22 A ASN   A 1 159 ? 1.577  1.741   0.295   0.32 21.91 ?  159 ASN   A HD22 1 
ATOM   3545 H HD22 B ASN   A 1 159 ? 2.021  1.865   -0.501  0.38 18.61 ?  159 ASN   A HD22 1 
ATOM   3546 H HD22 T ASN   A 1 159 ? 1.553  1.735   0.111   0.30 21.58 ?  159 ASN   A HD22 1 
ATOM   3547 N N    A LEU   A 1 160 ? 5.038  -2.383  0.927   0.32 15.57 ?  160 LEU   A N    1 
ATOM   3548 N N    B LEU   A 1 160 ? 5.371  -2.226  0.767   0.38 12.41 ?  160 LEU   A N    1 
ATOM   3549 N N    T LEU   A 1 160 ? 5.022  -2.464  0.907   0.30 17.09 ?  160 LEU   A N    1 
ATOM   3550 C CA   A LEU   A 1 160 ? 5.948  -3.396  0.403   0.32 15.06 ?  160 LEU   A CA   1 
ATOM   3551 C CA   B LEU   A 1 160 ? 6.311  -3.257  0.337   0.38 13.19 ?  160 LEU   A CA   1 
ATOM   3552 C CA   T LEU   A 1 160 ? 5.883  -3.494  0.335   0.30 17.12 ?  160 LEU   A CA   1 
ATOM   3553 C C    A LEU   A 1 160 ? 6.117  -4.544  1.392   0.32 14.08 ?  160 LEU   A C    1 
ATOM   3554 C C    B LEU   A 1 160 ? 6.329  -4.424  1.318   0.38 12.48 ?  160 LEU   A C    1 
ATOM   3555 O O    A LEU   A 1 160 ? 6.097  -5.718  1.001   0.32 13.47 ?  160 LEU   A O    1 
ATOM   3556 O O    B LEU   A 1 160 ? 6.283  -5.593  0.917   0.38 12.07 ?  160 LEU   A O    1 
ATOM   3557 C CB   A LEU   A 1 160 ? 7.300  -2.774  0.047   0.32 15.38 ?  160 LEU   A CB   1 
ATOM   3558 C CB   B LEU   A 1 160 ? 7.710  -2.653  0.196   0.38 14.41 ?  160 LEU   A CB   1 
ATOM   3559 C CB   T LEU   A 1 160 ? 7.269  -2.933  0.021   0.30 17.08 ?  160 LEU   A CB   1 
ATOM   3560 C CG   A LEU   A 1 160 ? 8.350  -3.800  -0.378  0.32 16.11 ?  160 LEU   A CG   1 
ATOM   3561 C CG   B LEU   A 1 160 ? 8.831  -3.645  -0.118  0.38 15.82 ?  160 LEU   A CG   1 
ATOM   3562 C CG   T LEU   A 1 160 ? 8.306  -3.969  -0.412  0.30 17.32 ?  160 LEU   A CG   1 
ATOM   3563 C CD1  A LEU   A 1 160 ? 7.846  -4.618  -1.553  0.32 16.41 ?  160 LEU   A CD1  1 
ATOM   3564 C CD1  B LEU   A 1 160 ? 8.527  -4.391  -1.408  0.38 15.98 ?  160 LEU   A CD1  1 
ATOM   3565 C CD1  T LEU   A 1 160 ? 7.844  -4.704  -1.654  0.30 17.58 ?  160 LEU   A CD1  1 
ATOM   3566 C CD2  A LEU   A 1 160 ? 9.666  -3.128  -0.715  0.32 16.30 ?  160 LEU   A CD2  1 
ATOM   3567 C CD2  B LEU   A 1 160 ? 10.179 -2.940  -0.196  0.38 16.48 ?  160 LEU   A CD2  1 
ATOM   3568 C CD2  T LEU   A 1 160 ? 9.644  -3.300  -0.654  0.30 17.26 ?  160 LEU   A CD2  1 
ATOM   3569 H H    A LEU   A 1 160 ? 5.402  -1.617  1.093   0.32 18.70 ?  160 LEU   A H    1 
ATOM   3570 H H    B LEU   A 1 160 ? 5.731  -1.459  0.939   0.38 14.90 ?  160 LEU   A H    1 
ATOM   3571 H H    T LEU   A 1 160 ? 5.434  -1.736  1.129   0.30 20.53 ?  160 LEU   A H    1 
ATOM   3572 H HA   A LEU   A 1 160 ? 5.572  -3.756  -0.408  0.32 18.09 ?  160 LEU   A HA   1 
ATOM   3573 H HA   B LEU   A 1 160 ? 6.033  -3.587  -0.530  0.38 15.85 ?  160 LEU   A HA   1 
ATOM   3574 H HB2  A LEU   A 1 160 ? 7.186  -2.132  -0.681  0.32 18.47 ?  160 LEU   A HB2  1 
ATOM   3575 H HB2  B LEU   A 1 160 ? 7.691  -1.996  -0.519  0.38 17.31 ?  160 LEU   A HB2  1 
ATOM   3576 H HB2  T LEU   A 1 160 ? 7.185  -2.275  -0.689  0.30 20.51 ?  160 LEU   A HB2  1 
ATOM   3577 H HB3  A LEU   A 1 160 ? 7.649  -2.324  0.829   0.32 18.47 ?  160 LEU   A HB3  1 
ATOM   3578 H HB3  B LEU   A 1 160 ? 7.936  -2.213  1.031   0.38 17.31 ?  160 LEU   A HB3  1 
ATOM   3579 H HB3  T LEU   A 1 160 ? 7.617  -2.511  0.820   0.30 20.51 ?  160 LEU   A HB3  1 
ATOM   3580 H HG   A LEU   A 1 160 ? 8.520  -4.405  0.361   0.32 19.35 ?  160 LEU   A HG   1 
ATOM   3581 H HG   B LEU   A 1 160 ? 8.882  -4.296  0.599   0.38 19.00 ?  160 LEU   A HG   1 
ATOM   3582 H HG   T LEU   A 1 160 ? 8.421  -4.617  0.301   0.30 20.80 ?  160 LEU   A HG   1 
ATOM   3583 H HD11 A LEU   A 1 160 ? 8.561  -5.192  -1.861  0.32 19.70 ?  160 LEU   A HD11 1 
ATOM   3584 H HD11 B LEU   A 1 160 ? 9.298  -4.925  -1.649  0.38 19.19 ?  160 LEU   A HD11 1 
ATOM   3585 H HD11 T LEU   A 1 160 ? 8.556  -5.288  -1.956  0.30 21.11 ?  160 LEU   A HD11 1 
ATOM   3586 H HD12 A LEU   A 1 160 ? 7.093  -5.158  -1.266  0.32 19.70 ?  160 LEU   A HD12 1 
ATOM   3587 H HD12 B LEU   A 1 160 ? 7.757  -4.964  -1.268  0.38 19.19 ?  160 LEU   A HD12 1 
ATOM   3588 H HD12 T LEU   A 1 160 ? 7.057  -5.226  -1.436  0.30 21.11 ?  160 LEU   A HD12 1 
ATOM   3589 H HD13 A LEU   A 1 160 ? 7.572  -4.016  -2.263  0.32 19.70 ?  160 LEU   A HD13 1 
ATOM   3590 H HD13 B LEU   A 1 160 ? 8.338  -3.746  -2.107  0.38 19.19 ?  160 LEU   A HD13 1 
ATOM   3591 H HD13 T LEU   A 1 160 ? 7.632  -4.055  -2.343  0.30 21.11 ?  160 LEU   A HD13 1 
ATOM   3592 H HD21 A LEU   A 1 160 ? 10.310 -3.807  -0.974  0.32 19.58 ?  160 LEU   A HD21 1 
ATOM   3593 H HD21 B LEU   A 1 160 ? 10.868 -3.597  -0.380  0.38 19.79 ?  160 LEU   A HD21 1 
ATOM   3594 H HD21 T LEU   A 1 160 ? 10.289 -3.972  -0.925  0.30 20.72 ?  160 LEU   A HD21 1 
ATOM   3595 H HD22 A LEU   A 1 160 ? 9.527  -2.508  -1.446  0.32 19.58 ?  160 LEU   A HD22 1 
ATOM   3596 H HD22 B LEU   A 1 160 ? 10.150 -2.281  -0.907  0.38 19.79 ?  160 LEU   A HD22 1 
ATOM   3597 H HD22 T LEU   A 1 160 ? 9.543  -2.636  -1.354  0.30 20.72 ?  160 LEU   A HD22 1 
ATOM   3598 H HD23 A LEU   A 1 160 ? 9.989  -2.651  0.067   0.32 19.58 ?  160 LEU   A HD23 1 
ATOM   3599 H HD23 B LEU   A 1 160 ? 10.356 -2.503  0.653   0.38 19.79 ?  160 LEU   A HD23 1 
ATOM   3600 H HD23 T LEU   A 1 160 ? 9.938  -2.872  0.167   0.30 20.72 ?  160 LEU   A HD23 1 
ATOM   3601 N N    A TYR   A 1 161 ? 6.290  -4.227  2.677   0.62 14.77 ?  161 TYR   A N    1 
ATOM   3602 N N    B TYR   A 1 161 ? 6.429  -4.122  2.613   0.38 13.11 ?  161 TYR   A N    1 
ATOM   3603 C CA   A TYR   A 1 161 ? 6.407  -5.273  3.689   0.62 14.76 ?  161 TYR   A CA   1 
ATOM   3604 C CA   B TYR   A 1 161 ? 6.455  -5.177  3.620   0.38 13.32 ?  161 TYR   A CA   1 
ATOM   3605 C C    A TYR   A 1 161 ? 5.240  -6.248  3.603   0.62 15.17 ?  161 TYR   A C    1 
ATOM   3606 C C    B TYR   A 1 161 ? 5.236  -6.083  3.496   0.38 13.82 ?  161 TYR   A C    1 
ATOM   3607 O O    A TYR   A 1 161 ? 5.431  -7.470  3.589   0.62 14.47 ?  161 TYR   A O    1 
ATOM   3608 O O    B TYR   A 1 161 ? 5.356  -7.315  3.511   0.38 13.52 ?  161 TYR   A O    1 
ATOM   3609 C CB   A TYR   A 1 161 ? 6.480  -4.653  5.086   0.62 14.78 ?  161 TYR   A CB   1 
ATOM   3610 C CB   B TYR   A 1 161 ? 6.528  -4.561  5.017   0.38 13.25 ?  161 TYR   A CB   1 
ATOM   3611 C CG   A TYR   A 1 161 ? 6.394  -5.697  6.169   0.62 14.14 ?  161 TYR   A CG   1 
ATOM   3612 C CG   B TYR   A 1 161 ? 6.424  -5.600  6.099   0.38 12.78 ?  161 TYR   A CG   1 
ATOM   3613 C CD1  A TYR   A 1 161 ? 7.517  -6.407  6.563   0.62 14.31 ?  161 TYR   A CD1  1 
ATOM   3614 C CD1  B TYR   A 1 161 ? 7.537  -6.323  6.498   0.38 12.92 ?  161 TYR   A CD1  1 
ATOM   3615 C CD2  A TYR   A 1 161 ? 5.184  -5.992  6.784   0.62 13.75 ?  161 TYR   A CD2  1 
ATOM   3616 C CD2  B TYR   A 1 161 ? 5.209  -5.876  6.708   0.38 12.76 ?  161 TYR   A CD2  1 
ATOM   3617 C CE1  A TYR   A 1 161 ? 7.436  -7.379  7.541   0.62 14.13 ?  161 TYR   A CE1  1 
ATOM   3618 C CE1  B TYR   A 1 161 ? 7.443  -7.290  7.479   0.38 13.01 ?  161 TYR   A CE1  1 
ATOM   3619 C CE2  A TYR   A 1 161 ? 5.093  -6.961  7.762   0.62 13.55 ?  161 TYR   A CE2  1 
ATOM   3620 C CE2  B TYR   A 1 161 ? 5.103  -6.841  7.690   0.38 12.75 ?  161 TYR   A CE2  1 
ATOM   3621 C CZ   A TYR   A 1 161 ? 6.221  -7.655  8.137   0.62 13.92 ?  161 TYR   A CZ   1 
ATOM   3622 C CZ   B TYR   A 1 161 ? 6.222  -7.547  8.071   0.38 13.10 ?  161 TYR   A CZ   1 
ATOM   3623 O OH   A TYR   A 1 161 ? 6.156  -8.625  9.111   0.62 15.04 ?  161 TYR   A OH   1 
ATOM   3624 O OH   B TYR   A 1 161 ? 6.134  -8.509  9.049   0.38 13.84 ?  161 TYR   A OH   1 
ATOM   3625 H H    A TYR   A 1 161 ? 6.345  -3.422  2.982   0.62 17.74 ?  161 TYR   A H    1 
ATOM   3626 H H    B TYR   A 1 161 ? 6.488  -3.324  2.926   0.38 15.75 ?  161 TYR   A H    1 
ATOM   3627 H HA   A TYR   A 1 161 ? 7.225  -5.769  3.537   0.62 17.73 ?  161 TYR   A HA   1 
ATOM   3628 H HA   B TYR   A 1 161 ? 7.247  -5.717  3.487   0.38 16.00 ?  161 TYR   A HA   1 
ATOM   3629 H HB2  A TYR   A 1 161 ? 7.327  -4.185  5.182   0.62 17.75 ?  161 TYR   A HB2  1 
ATOM   3630 H HB2  B TYR   A 1 161 ? 7.379  -4.103  5.117   0.38 15.91 ?  161 TYR   A HB2  1 
ATOM   3631 H HB3  A TYR   A 1 161 ? 5.743  -4.034  5.200   0.62 17.75 ?  161 TYR   A HB3  1 
ATOM   3632 H HB3  B TYR   A 1 161 ? 5.797  -3.933  5.127   0.38 15.91 ?  161 TYR   A HB3  1 
ATOM   3633 H HD1  A TYR   A 1 161 ? 8.337  -6.230  6.160   0.62 17.19 ?  161 TYR   A HD1  1 
ATOM   3634 H HD1  B TYR   A 1 161 ? 8.361  -6.157  6.098   0.38 15.52 ?  161 TYR   A HD1  1 
ATOM   3635 H HD2  A TYR   A 1 161 ? 4.416  -5.530  6.531   0.62 16.52 ?  161 TYR   A HD2  1 
ATOM   3636 H HD2  B TYR   A 1 161 ? 4.449  -5.404  6.451   0.38 15.33 ?  161 TYR   A HD2  1 
ATOM   3637 H HE1  A TYR   A 1 161 ? 8.198  -7.847  7.796   0.62 16.97 ?  161 TYR   A HE1  1 
ATOM   3638 H HE1  B TYR   A 1 161 ? 8.198  -7.768  7.739   0.38 15.62 ?  161 TYR   A HE1  1 
ATOM   3639 H HE2  A TYR   A 1 161 ? 4.273  -7.142  8.164   0.62 16.28 ?  161 TYR   A HE2  1 
ATOM   3640 H HE2  B TYR   A 1 161 ? 4.281  -7.011  8.090   0.38 15.32 ?  161 TYR   A HE2  1 
ATOM   3641 H HH   A TYR   A 1 161 ? 5.363  -8.688  9.392   0.62 18.07 ?  161 TYR   A HH   1 
ATOM   3642 H HH   B TYR   A 1 161 ? 5.339  -8.564  9.328   0.38 16.63 ?  161 TYR   A HH   1 
ATOM   3643 N N    A ASP   A 1 162 ? 4.016  -5.718  3.544   0.62 15.98 ?  162 ASP   A N    1 
ATOM   3644 N N    B ASP   A 1 162 ? 4.047  -5.486  3.380   0.38 14.42 ?  162 ASP   A N    1 
ATOM   3645 C CA   A ASP   A 1 162 ? 2.842  -6.587  3.484   0.62 16.79 ?  162 ASP   A CA   1 
ATOM   3646 C CA   B ASP   A 1 162 ? 2.832  -6.281  3.224   0.38 14.79 ?  162 ASP   A CA   1 
ATOM   3647 C C    A ASP   A 1 162 ? 2.871  -7.472  2.245   0.62 16.31 ?  162 ASP   A C    1 
ATOM   3648 C C    B ASP   A 1 162 ? 2.904  -7.151  1.972   0.38 14.96 ?  162 ASP   A C    1 
ATOM   3649 O O    A ASP   A 1 162 ? 2.509  -8.654  2.308   0.62 15.91 ?  162 ASP   A O    1 
ATOM   3650 O O    B ASP   A 1 162 ? 2.522  -8.328  1.998   0.38 14.97 ?  162 ASP   A O    1 
ATOM   3651 C CB   A ASP   A 1 162 ? 1.556  -5.758  3.516   0.62 18.34 ?  162 ASP   A CB   1 
ATOM   3652 C CB   B ASP   A 1 162 ? 1.605  -5.364  3.177   0.38 15.17 ?  162 ASP   A CB   1 
ATOM   3653 C CG   A ASP   A 1 162 ? 1.233  -5.226  4.895   0.62 20.21 ?  162 ASP   A CG   1 
ATOM   3654 C CG   B ASP   A 1 162 ? 1.353  -4.639  4.498   0.38 15.02 ?  162 ASP   A CG   1 
ATOM   3655 O OD1  A ASP   A 1 162 ? 1.795  -5.739  5.883   0.62 20.50 ?  162 ASP   A OD1  1 
ATOM   3656 O OD1  B ASP   A 1 162 ? 1.884  -5.074  5.543   0.38 15.12 ?  162 ASP   A OD1  1 
ATOM   3657 O OD2  A ASP   A 1 162 ? 0.395  -4.303  4.986   0.62 21.34 -1 162 ASP   A OD2  1 
ATOM   3658 O OD2  B ASP   A 1 162 ? 0.601  -3.639  4.495   0.38 15.26 -1 162 ASP   A OD2  1 
ATOM   3659 H H    A ASP   A 1 162 ? 3.840  -4.871  3.531   0.62 19.19 ?  162 ASP   A H    1 
ATOM   3660 H H    B ASP   A 1 162 ? 3.921  -4.635  3.384   0.38 17.32 ?  162 ASP   A H    1 
ATOM   3661 H HA   A ASP   A 1 162 ? 2.844  -7.164  4.257   0.62 20.16 ?  162 ASP   A HA   1 
ATOM   3662 H HA   B ASP   A 1 162 ? 2.736  -6.867  3.987   0.38 17.76 ?  162 ASP   A HA   1 
ATOM   3663 H HB2  A ASP   A 1 162 ? 1.649  -4.997  2.921   0.62 22.03 ?  162 ASP   A HB2  1 
ATOM   3664 H HB2  B ASP   A 1 162 ? 1.732  -4.698  2.482   0.38 18.22 ?  162 ASP   A HB2  1 
ATOM   3665 H HB3  A ASP   A 1 162 ? 0.813  -6.312  3.236   0.62 22.03 ?  162 ASP   A HB3  1 
ATOM   3666 H HB3  B ASP   A 1 162 ? 0.818  -5.897  2.984   0.38 18.22 ?  162 ASP   A HB3  1 
ATOM   3667 N N    A LYS   A 1 163 ? 3.306  -6.923  1.109   0.62 16.64 ?  163 LYS   A N    1 
ATOM   3668 N N    B LYS   A 1 163 ? 3.397  -6.588  0.866   0.38 15.31 ?  163 LYS   A N    1 
ATOM   3669 C CA   A LYS   A 1 163 ? 3.375  -7.727  -0.107  0.62 17.29 ?  163 LYS   A CA   1 
ATOM   3670 C CA   B LYS   A 1 163 ? 3.538  -7.359  -0.366  0.38 16.01 ?  163 LYS   A CA   1 
ATOM   3671 C C    A LYS   A 1 163 ? 4.459  -8.800  -0.009  0.62 16.22 ?  163 LYS   A C    1 
ATOM   3672 C C    B LYS   A 1 163 ? 4.524  -8.507  -0.190  0.38 15.22 ?  163 LYS   A C    1 
ATOM   3673 O O    A LYS   A 1 163 ? 4.284  -9.916  -0.510  0.62 16.47 ?  163 LYS   A O    1 
ATOM   3674 O O    B LYS   A 1 163 ? 4.280  -9.625  -0.659  0.38 14.80 ?  163 LYS   A O    1 
ATOM   3675 C CB   A LYS   A 1 163 ? 3.616  -6.828  -1.320  0.62 19.73 ?  163 LYS   A CB   1 
ATOM   3676 C CB   B LYS   A 1 163 ? 3.995  -6.436  -1.499  0.38 17.70 ?  163 LYS   A CB   1 
ATOM   3677 C CG   A LYS   A 1 163 ? 3.649  -7.582  -2.637  0.62 22.54 ?  163 LYS   A CG   1 
ATOM   3678 C CG   B LYS   A 1 163 ? 4.141  -7.111  -2.861  0.38 19.98 ?  163 LYS   A CG   1 
ATOM   3679 C CD   A LYS   A 1 163 ? 4.026  -6.666  -3.783  0.62 25.10 ?  163 LYS   A CD   1 
ATOM   3680 C CD   B LYS   A 1 163 ? 4.661  -6.117  -3.898  0.38 22.19 ?  163 LYS   A CD   1 
ATOM   3681 C CE   A LYS   A 1 163 ? 3.948  -7.392  -5.114  0.62 26.86 ?  163 LYS   A CE   1 
ATOM   3682 C CE   B LYS   A 1 163 ? 4.116  -6.392  -5.298  0.38 23.78 ?  163 LYS   A CE   1 
ATOM   3683 N NZ   A LYS   A 1 163 ? 4.579  -6.609  -6.211  0.62 27.83 ?  163 LYS   A NZ   1 
ATOM   3684 N NZ   B LYS   A 1 163 ? 4.878  -7.438  -6.032  0.38 24.72 ?  163 LYS   A NZ   1 
ATOM   3685 H H    A LYS   A 1 163 ? 3.554  -6.100  1.016   0.62 19.98 ?  163 LYS   A H    1 
ATOM   3686 H H    B LYS   A 1 163 ? 3.647  -5.766  0.804   0.38 18.39 ?  163 LYS   A H    1 
ATOM   3687 H HA   A LYS   A 1 163 ? 2.521  -8.170  -0.234  0.62 20.77 ?  163 LYS   A HA   1 
ATOM   3688 H HA   B LYS   A 1 163 ? 2.676  -7.729  -0.613  0.38 19.23 ?  163 LYS   A HA   1 
ATOM   3689 H HB2  A LYS   A 1 163 ? 2.900  -6.171  -1.374  0.62 23.69 ?  163 LYS   A HB2  1 
ATOM   3690 H HB2  B LYS   A 1 163 ? 3.346  -5.719  -1.600  0.38 21.26 ?  163 LYS   A HB2  1 
ATOM   3691 H HB3  A LYS   A 1 163 ? 4.466  -6.377  -1.214  0.62 23.69 ?  163 LYS   A HB3  1 
ATOM   3692 H HB3  B LYS   A 1 163 ? 4.857  -6.060  -1.266  0.38 21.26 ?  163 LYS   A HB3  1 
ATOM   3693 H HG2  A LYS   A 1 163 ? 4.308  -8.292  -2.589  0.62 27.06 ?  163 LYS   A HG2  1 
ATOM   3694 H HG2  B LYS   A 1 163 ? 4.777  -7.842  -2.798  0.38 23.99 ?  163 LYS   A HG2  1 
ATOM   3695 H HG3  A LYS   A 1 163 ? 2.770  -7.952  -2.818  0.62 27.06 ?  163 LYS   A HG3  1 
ATOM   3696 H HG3  B LYS   A 1 163 ? 3.277  -7.441  -3.155  0.38 23.99 ?  163 LYS   A HG3  1 
ATOM   3697 H HD2  A LYS   A 1 163 ? 3.412  -5.916  -3.809  0.62 30.14 ?  163 LYS   A HD2  1 
ATOM   3698 H HD2  B LYS   A 1 163 ? 4.392  -5.222  -3.642  0.38 26.64 ?  163 LYS   A HD2  1 
ATOM   3699 H HD3  A LYS   A 1 163 ? 4.935  -6.353  -3.656  0.62 30.14 ?  163 LYS   A HD3  1 
ATOM   3700 H HD3  B LYS   A 1 163 ? 5.630  -6.175  -3.936  0.38 26.64 ?  163 LYS   A HD3  1 
ATOM   3701 H HE2  A LYS   A 1 163 ? 4.395  -8.248  -5.041  0.62 32.24 ?  163 LYS   A HE2  1 
ATOM   3702 H HE2  B LYS   A 1 163 ? 3.196  -6.688  -5.229  0.38 28.56 ?  163 LYS   A HE2  1 
ATOM   3703 H HE3  A LYS   A 1 163 ? 3.018  -7.527  -5.342  0.62 32.24 ?  163 LYS   A HE3  1 
ATOM   3704 H HE3  B LYS   A 1 163 ? 4.161  -5.575  -5.817  0.38 28.56 ?  163 LYS   A HE3  1 
ATOM   3705 H HZ1  A LYS   A 1 163 ? 4.521  -7.057  -6.977  0.62 33.42 ?  163 LYS   A HZ1  1 
ATOM   3706 H HZ1  B LYS   A 1 163 ? 4.639  -7.442  -6.891  0.38 29.68 ?  163 LYS   A HZ1  1 
ATOM   3707 H HZ2  A LYS   A 1 163 ? 4.164  -5.826  -6.301  0.62 33.42 ?  163 LYS   A HZ2  1 
ATOM   3708 H HZ2  B LYS   A 1 163 ? 5.752  -7.274  -5.978  0.38 29.68 ?  163 LYS   A HZ2  1 
ATOM   3709 H HZ3  A LYS   A 1 163 ? 5.437  -6.460  -6.027  0.62 33.42 ?  163 LYS   A HZ3  1 
ATOM   3710 H HZ3  B LYS   A 1 163 ? 4.712  -8.238  -5.683  0.38 29.68 ?  163 LYS   A HZ3  1 
ATOM   3711 N N    A LEU   A 1 164 ? 5.592  -8.478  0.620   0.62 14.42 ?  164 LEU   A N    1 
ATOM   3712 N N    B LEU   A 1 164 ? 5.651  -8.252  0.479   0.38 14.72 ?  164 LEU   A N    1 
ATOM   3713 C CA   A LEU   A 1 164 ? 6.668  -9.458  0.761   0.62 13.77 ?  164 LEU   A CA   1 
ATOM   3714 C CA   B LEU   A 1 164 ? 6.658  -9.294  0.656   0.38 14.53 ?  164 LEU   A CA   1 
ATOM   3715 C C    A LEU   A 1 164 ? 6.228  -10.638 1.620   0.62 13.59 ?  164 LEU   A C    1 
ATOM   3716 C C    B LEU   A 1 164 ? 6.129  -10.434 1.516   0.38 14.04 ?  164 LEU   A C    1 
ATOM   3717 O O    A LEU   A 1 164 ? 6.510  -11.800 1.296   0.62 13.34 ?  164 LEU   A O    1 
ATOM   3718 O O    B LEU   A 1 164 ? 6.364  -11.610 1.215   0.38 14.31 ?  164 LEU   A O    1 
ATOM   3719 C CB   A LEU   A 1 164 ? 7.884  -8.779  1.383   0.62 13.39 ?  164 LEU   A CB   1 
ATOM   3720 C CB   B LEU   A 1 164 ? 7.913  -8.697  1.286   0.38 14.73 ?  164 LEU   A CB   1 
ATOM   3721 C CG   A LEU   A 1 164 ? 8.680  -7.837  0.479   0.62 13.70 ?  164 LEU   A CG   1 
ATOM   3722 C CG   B LEU   A 1 164 ? 8.769  -7.800  0.393   0.38 14.95 ?  164 LEU   A CG   1 
ATOM   3723 C CD1  A LEU   A 1 164 ? 9.579  -6.949  1.323   0.62 13.68 ?  164 LEU   A CD1  1 
ATOM   3724 C CD1  B LEU   A 1 164 ? 9.822  -7.098  1.228   0.38 15.01 ?  164 LEU   A CD1  1 
ATOM   3725 C CD2  A LEU   A 1 164 ? 9.504  -8.633  -0.516  0.62 13.72 ?  164 LEU   A CD2  1 
ATOM   3726 C CD2  B LEU   A 1 164 ? 9.419  -8.608  -0.721  0.38 15.00 ?  164 LEU   A CD2  1 
ATOM   3727 H H    A LEU   A 1 164 ? 5.759  -7.703  0.965   0.62 17.32 ?  164 LEU   A H    1 
ATOM   3728 H H    B LEU   A 1 164 ? 5.849  -7.491  0.835   0.38 17.68 ?  164 LEU   A H    1 
ATOM   3729 H HA   A LEU   A 1 164 ? 6.916  -9.783  -0.117  0.62 16.53 ?  164 LEU   A HA   1 
ATOM   3730 H HA   B LEU   A 1 164 ? 6.892  -9.653  -0.210  0.38 17.45 ?  164 LEU   A HA   1 
ATOM   3731 H HB2  A LEU   A 1 164 ? 7.586  -8.254  2.142   0.62 16.09 ?  164 LEU   A HB2  1 
ATOM   3732 H HB2  B LEU   A 1 164 ? 7.645  -8.165  2.051   0.38 17.69 ?  164 LEU   A HB2  1 
ATOM   3733 H HB3  A LEU   A 1 164 ? 8.494  -9.465  1.681   0.62 16.09 ?  164 LEU   A HB3  1 
ATOM   3734 H HB3  B LEU   A 1 164 ? 8.476  -9.427  1.582   0.38 17.69 ?  164 LEU   A HB3  1 
ATOM   3735 H HG   A LEU   A 1 164 ? 8.071  -7.265  -0.017  0.62 16.46 ?  164 LEU   A HG   1 
ATOM   3736 H HG   B LEU   A 1 164 ? 8.205  -7.124  -0.014  0.38 17.95 ?  164 LEU   A HG   1 
ATOM   3737 H HD11 A LEU   A 1 164 ? 10.080 -6.358  0.741   0.62 16.43 ?  164 LEU   A HD11 1 
ATOM   3738 H HD11 B LEU   A 1 164 ? 10.355 -6.530  0.652   0.38 18.03 ?  164 LEU   A HD11 1 
ATOM   3739 H HD12 A LEU   A 1 164 ? 9.027  -6.427  1.928   0.62 16.43 ?  164 LEU   A HD12 1 
ATOM   3740 H HD12 B LEU   A 1 164 ? 9.381  -6.563  1.907   0.38 18.03 ?  164 LEU   A HD12 1 
ATOM   3741 H HD13 A LEU   A 1 164 ? 10.186 -7.508  1.831   0.62 16.43 ?  164 LEU   A HD13 1 
ATOM   3742 H HD13 B LEU   A 1 164 ? 10.387 -7.766  1.649   0.38 18.03 ?  164 LEU   A HD13 1 
ATOM   3743 H HD21 A LEU   A 1 164 ? 10.025 -8.021  -1.060  0.62 16.47 ?  164 LEU   A HD21 1 
ATOM   3744 H HD21 B LEU   A 1 164 ? 10.040 -8.039  -1.202  0.38 18.02 ?  164 LEU   A HD21 1 
ATOM   3745 H HD22 A LEU   A 1 164 ? 10.099 -9.227  -0.029  0.62 16.47 ?  164 LEU   A HD22 1 
ATOM   3746 H HD22 B LEU   A 1 164 ? 9.895  -9.359  -0.330  0.38 18.02 ?  164 LEU   A HD22 1 
ATOM   3747 H HD23 A LEU   A 1 164 ? 8.908  -9.150  -1.078  0.62 16.47 ?  164 LEU   A HD23 1 
ATOM   3748 H HD23 B LEU   A 1 164 ? 8.731  -8.932  -1.323  0.38 18.02 ?  164 LEU   A HD23 1 
ATOM   3749 N N    A VAL   A 1 165 ? 5.560  -10.354 2.736   0.62 13.51 ?  165 VAL   A N    1 
ATOM   3750 N N    B VAL   A 1 165 ? 5.422  -10.104 2.597   0.38 13.11 ?  165 VAL   A N    1 
ATOM   3751 C CA   A VAL   A 1 165 ? 5.069  -11.421 3.604   0.62 13.86 ?  165 VAL   A CA   1 
ATOM   3752 C CA   B VAL   A 1 165 ? 4.882  -11.141 3.472   0.38 12.66 ?  165 VAL   A CA   1 
ATOM   3753 C C    A VAL   A 1 165 ? 4.029  -12.264 2.877   0.62 14.11 ?  165 VAL   A C    1 
ATOM   3754 C C    B VAL   A 1 165 ? 3.875  -12.000 2.718   0.38 12.33 ?  165 VAL   A C    1 
ATOM   3755 O O    A VAL   A 1 165 ? 4.117  -13.498 2.835   0.62 14.34 ?  165 VAL   A O    1 
ATOM   3756 O O    B VAL   A 1 165 ? 3.945  -13.234 2.737   0.38 12.20 ?  165 VAL   A O    1 
ATOM   3757 C CB   A VAL   A 1 165 ? 4.516  -10.827 4.911   0.62 14.25 ?  165 VAL   A CB   1 
ATOM   3758 C CB   B VAL   A 1 165 ? 4.270  -10.510 4.736   0.38 13.61 ?  165 VAL   A CB   1 
ATOM   3759 C CG1  A VAL   A 1 165 ? 3.756  -11.886 5.707   0.62 14.06 ?  165 VAL   A CG1  1 
ATOM   3760 C CG1  B VAL   A 1 165 ? 3.445  -11.534 5.506   0.38 13.60 ?  165 VAL   A CG1  1 
ATOM   3761 C CG2  A VAL   A 1 165 ? 5.642  -10.216 5.740   0.62 14.82 ?  165 VAL   A CG2  1 
ATOM   3762 C CG2  B VAL   A 1 165 ? 5.369  -9.936  5.617   0.38 14.09 ?  165 VAL   A CG2  1 
ATOM   3763 H H    A VAL   A 1 165 ? 5.379  -9.558  3.005   0.62 16.22 ?  165 VAL   A H    1 
ATOM   3764 H H    B VAL   A 1 165 ? 5.239  -9.297  2.837   0.38 15.75 ?  165 VAL   A H    1 
ATOM   3765 H HA   A VAL   A 1 165 ? 5.815  -11.996 3.836   0.62 16.65 ?  165 VAL   A HA   1 
ATOM   3766 H HA   B VAL   A 1 165 ? 5.605  -11.716 3.754   0.38 15.21 ?  165 VAL   A HA   1 
ATOM   3767 H HB   A VAL   A 1 165 ? 3.895  -10.111 4.690   0.62 17.12 ?  165 VAL   A HB   1 
ATOM   3768 H HB   B VAL   A 1 165 ? 3.682  -9.780  4.480   0.38 16.35 ?  165 VAL   A HB   1 
ATOM   3769 H HG11 A VAL   A 1 165 ? 3.659  -11.579 6.621   0.62 16.88 ?  165 VAL   A HG11 1 
ATOM   3770 H HG11 B VAL   A 1 165 ? 3.312  -11.213 6.412   0.38 16.34 ?  165 VAL   A HG11 1 
ATOM   3771 H HG12 A VAL   A 1 165 ? 2.881  -12.013 5.307   0.62 16.88 ?  165 VAL   A HG12 1 
ATOM   3772 H HG12 B VAL   A 1 165 ? 2.588  -11.647 5.067   0.38 16.34 ?  165 VAL   A HG12 1 
ATOM   3773 H HG13 A VAL   A 1 165 ? 4.258  -12.713 5.685   0.62 16.88 ?  165 VAL   A HG13 1 
ATOM   3774 H HG13 B VAL   A 1 165 ? 3.927  -12.375 5.523   0.38 16.34 ?  165 VAL   A HG13 1 
ATOM   3775 H HG21 A VAL   A 1 165 ? 5.270  -9.855  6.560   0.62 17.80 ?  165 VAL   A HG21 1 
ATOM   3776 H HG21 B VAL   A 1 165 ? 4.969  -9.540  6.407   0.38 16.92 ?  165 VAL   A HG21 1 
ATOM   3777 H HG22 A VAL   A 1 165 ? 6.292  -10.904 5.944   0.62 17.80 ?  165 VAL   A HG22 1 
ATOM   3778 H HG22 B VAL   A 1 165 ? 5.972  -10.652 5.874   0.38 16.92 ?  165 VAL   A HG22 1 
ATOM   3779 H HG23 A VAL   A 1 165 ? 6.062  -9.504  5.228   0.62 17.80 ?  165 VAL   A HG23 1 
ATOM   3780 H HG23 B VAL   A 1 165 ? 5.854  -9.260  5.117   0.38 16.92 ?  165 VAL   A HG23 1 
ATOM   3781 N N    A SER   A 1 166 ? 3.031  -11.607 2.282   0.62 14.39 ?  166 SER   A N    1 
ATOM   3782 N N    B SER   A 1 166 ? 2.937  -11.359 2.021   0.38 12.62 ?  166 SER   A N    1 
ATOM   3783 C CA   A SER   A 1 166 ? 1.915  -12.344 1.698   0.62 15.51 ?  166 SER   A CA   1 
ATOM   3784 C CA   B SER   A 1 166 ? 1.835  -12.099 1.421   0.38 13.50 ?  166 SER   A CA   1 
ATOM   3785 C C    A SER   A 1 166 ? 2.358  -13.209 0.528   0.62 15.96 ?  166 SER   A C    1 
ATOM   3786 C C    B SER   A 1 166 ? 2.273  -12.952 0.239   0.38 13.42 ?  166 SER   A C    1 
ATOM   3787 O O    A SER   A 1 166 ? 1.717  -14.228 0.239   0.62 16.92 ?  166 SER   A O    1 
ATOM   3788 O O    B SER   A 1 166 ? 1.526  -13.852 -0.158  0.38 13.14 ?  166 SER   A O    1 
ATOM   3789 C CB   A SER   A 1 166 ? 0.816  -11.381 1.241   0.62 16.76 ?  166 SER   A CB   1 
ATOM   3790 C CB   B SER   A 1 166 ? 0.731  -11.141 0.977   0.38 14.99 ?  166 SER   A CB   1 
ATOM   3791 O OG   A SER   A 1 166 ? 0.156  -10.772 2.338   0.62 18.11 ?  166 SER   A OG   1 
ATOM   3792 O OG   B SER   A 1 166 ? 1.107  -10.456 -0.201  0.38 16.50 ?  166 SER   A OG   1 
ATOM   3793 H H    A SER   A 1 166 ? 2.974  -10.754 2.211   0.62 17.29 ?  166 SER   A H    1 
ATOM   3794 H H    B SER   A 1 166 ? 2.915  -10.509 1.881   0.38 15.16 ?  166 SER   A H    1 
ATOM   3795 H HA   A SER   A 1 166 ? 1.534  -12.933 2.368   0.62 18.63 ?  166 SER   A HA   1 
ATOM   3796 H HA   B SER   A 1 166 ? 1.456  -12.694 2.083   0.38 16.22 ?  166 SER   A HA   1 
ATOM   3797 H HB2  A SER   A 1 166 ? 1.213  -10.691 0.687   0.62 20.13 ?  166 SER   A HB2  1 
ATOM   3798 H HB2  B SER   A 1 166 ? -0.084 -11.645 0.810   0.38 18.00 ?  166 SER   A HB2  1 
ATOM   3799 H HB3  A SER   A 1 166 ? 0.157  -11.875 0.727   0.62 20.13 ?  166 SER   A HB3  1 
ATOM   3800 H HB3  B SER   A 1 166 ? 0.574  -10.487 1.679   0.38 18.00 ?  166 SER   A HB3  1 
ATOM   3801 H HG   A SER   A 1 166 ? -0.433 -10.240 2.061   0.62 21.75 ?  166 SER   A HG   1 
ATOM   3802 H HG   B SER   A 1 166 ? 0.491  -9.938  -0.444  0.38 19.81 ?  166 SER   A HG   1 
ATOM   3803 N N    A SER   A 1 167 ? 3.428  -12.820 -0.165  0.62 15.69 ?  167 SER   A N    1 
ATOM   3804 N N    B SER   A 1 167 ? 3.447  -12.695 -0.339  0.38 13.46 ?  167 SER   A N    1 
ATOM   3805 C CA   A SER   A 1 167 ? 3.883  -13.544 -1.345  0.62 16.42 ?  167 SER   A CA   1 
ATOM   3806 C CA   B SER   A 1 167 ? 3.918  -13.450 -1.494  0.38 14.08 ?  167 SER   A CA   1 
ATOM   3807 C C    A SER   A 1 167 ? 5.020  -14.516 -1.050  0.62 16.24 ?  167 SER   A C    1 
ATOM   3808 C C    B SER   A 1 167 ? 5.063  -14.400 -1.169  0.38 14.60 ?  167 SER   A C    1 
ATOM   3809 O O    A SER   A 1 167 ? 5.511  -15.174 -1.974  0.62 17.55 ?  167 SER   A O    1 
ATOM   3810 O O    B SER   A 1 167 ? 5.539  -15.106 -2.066  0.38 15.69 ?  167 SER   A O    1 
ATOM   3811 C CB   A SER   A 1 167 ? 4.306  -12.563 -2.447  0.62 17.09 ?  167 SER   A CB   1 
ATOM   3812 C CB   B SER   A 1 167 ? 4.347  -12.501 -2.622  0.38 14.20 ?  167 SER   A CB   1 
ATOM   3813 O OG   A SER   A 1 167 ? 5.408  -11.774 -2.029  0.62 17.71 ?  167 SER   A OG   1 
ATOM   3814 O OG   B SER   A 1 167 ? 5.436  -11.686 -2.224  0.38 14.52 ?  167 SER   A OG   1 
ATOM   3815 H H    A SER   A 1 167 ? 3.907  -12.126 0.033   0.62 18.84 ?  167 SER   A H    1 
ATOM   3816 H H    B SER   A 1 167 ? 3.990  -12.078 -0.077  0.38 16.16 ?  167 SER   A H    1 
ATOM   3817 H HA   A SER   A 1 167 ? 3.137  -14.051 -1.690  0.62 19.72 ?  167 SER   A HA   1 
ATOM   3818 H HA   B SER   A 1 167 ? 3.178  -13.977 -1.833  0.38 16.91 ?  167 SER   A HA   1 
ATOM   3819 H HB2  A SER   A 1 167 ? 4.560  -13.067 -3.236  0.62 20.52 ?  167 SER   A HB2  1 
ATOM   3820 H HB2  B SER   A 1 167 ? 4.614  -13.031 -3.390  0.38 17.06 ?  167 SER   A HB2  1 
ATOM   3821 H HB3  A SER   A 1 167 ? 3.552  -11.981 -2.664  0.62 20.52 ?  167 SER   A HB3  1 
ATOM   3822 H HB3  B SER   A 1 167 ? 3.597  -11.932 -2.860  0.38 17.06 ?  167 SER   A HB3  1 
ATOM   3823 H HG   A SER   A 1 167 ? 5.188  -11.307 -1.365  0.62 21.27 ?  167 SER   A HG   1 
ATOM   3824 H HG   B SER   A 1 167 ? 5.215  -11.221 -1.561  0.38 17.44 ?  167 SER   A HG   1 
ATOM   3825 N N    A PHE   A 1 168 ? 5.437  -14.642 0.207   0.62 15.54 ?  168 PHE   A N    1 
ATOM   3826 N N    B PHE   A 1 168 ? 5.518  -14.445 0.080   0.38 14.34 ?  168 PHE   A N    1 
ATOM   3827 C CA   A PHE   A 1 168 ? 6.614  -15.446 0.510   0.62 15.22 ?  168 PHE   A CA   1 
ATOM   3828 C CA   B PHE   A 1 168 ? 6.678  -15.258 0.418   0.38 14.77 ?  168 PHE   A CA   1 
ATOM   3829 C C    A PHE   A 1 168 ? 6.296  -16.928 0.407   0.62 16.64 ?  168 PHE   A C    1 
ATOM   3830 C C    B PHE   A 1 168 ? 6.317  -16.736 0.420   0.38 15.21 ?  168 PHE   A C    1 
ATOM   3831 O O    A PHE   A 1 168 ? 5.296  -17.400 0.957   0.62 18.39 ?  168 PHE   A O    1 
ATOM   3832 O O    B PHE   A 1 168 ? 5.363  -17.154 1.085   0.38 15.76 ?  168 PHE   A O    1 
ATOM   3833 C CB   A PHE   A 1 168 ? 7.138  -15.153 1.911   0.62 14.50 ?  168 PHE   A CB   1 
ATOM   3834 C CB   B PHE   A 1 168 ? 7.216  -14.871 1.790   0.38 15.15 ?  168 PHE   A CB   1 
ATOM   3835 C CG   A PHE   A 1 168 ? 8.395  -15.912 2.233   0.62 13.99 ?  168 PHE   A CG   1 
ATOM   3836 C CG   B PHE   A 1 168 ? 8.454  -15.626 2.178   0.38 15.31 ?  168 PHE   A CG   1 
ATOM   3837 C CD1  A PHE   A 1 168 ? 9.590  -15.562 1.630   0.62 13.91 ?  168 PHE   A CD1  1 
ATOM   3838 C CD1  B PHE   A 1 168 ? 9.687  -15.247 1.681   0.38 15.68 ?  168 PHE   A CD1  1 
ATOM   3839 C CD2  A PHE   A 1 168 ? 8.385  -16.994 3.099   0.62 14.29 ?  168 PHE   A CD2  1 
ATOM   3840 C CD2  B PHE   A 1 168 ? 8.387  -16.722 3.021   0.38 15.41 ?  168 PHE   A CD2  1 
ATOM   3841 C CE1  A PHE   A 1 168 ? 10.753 -16.265 1.897   0.62 13.66 ?  168 PHE   A CE1  1 
ATOM   3842 C CE1  B PHE   A 1 168 ? 10.831 -15.939 2.025   0.38 15.98 ?  168 PHE   A CE1  1 
ATOM   3843 C CE2  A PHE   A 1 168 ? 9.549  -17.695 3.375   0.62 14.63 ?  168 PHE   A CE2  1 
ATOM   3844 C CE2  B PHE   A 1 168 ? 9.531  -17.421 3.370   0.38 15.73 ?  168 PHE   A CE2  1 
ATOM   3845 C CZ   A PHE   A 1 168 ? 10.734 -17.327 2.773   0.62 14.14 ?  168 PHE   A CZ   1 
ATOM   3846 C CZ   B PHE   A 1 168 ? 10.754 -17.027 2.869   0.38 15.88 ?  168 PHE   A CZ   1 
ATOM   3847 H H    A PHE   A 1 168 ? 5.061  -14.277 0.890   0.62 18.67 ?  168 PHE   A H    1 
ATOM   3848 H H    B PHE   A 1 168 ? 5.178  -14.009 0.741   0.38 17.23 ?  168 PHE   A H    1 
ATOM   3849 H HA   A PHE   A 1 168 ? 7.309  -15.236 -0.130  0.62 18.28 ?  168 PHE   A HA   1 
ATOM   3850 H HA   B PHE   A 1 168 ? 7.372  -15.110 -0.244  0.38 17.74 ?  168 PHE   A HA   1 
ATOM   3851 H HB2  A PHE   A 1 168 ? 7.333  -14.205 1.981   0.62 17.42 ?  168 PHE   A HB2  1 
ATOM   3852 H HB2  B PHE   A 1 168 ? 7.431  -13.925 1.786   0.38 18.19 ?  168 PHE   A HB2  1 
ATOM   3853 H HB3  A PHE   A 1 168 ? 6.462  -15.402 2.558   0.62 17.42 ?  168 PHE   A HB3  1 
ATOM   3854 H HB3  B PHE   A 1 168 ? 6.534  -15.053 2.455   0.38 18.19 ?  168 PHE   A HB3  1 
ATOM   3855 H HD1  A PHE   A 1 168 ? 9.616  -14.844 1.037   0.62 16.71 ?  168 PHE   A HD1  1 
ATOM   3856 H HD1  B PHE   A 1 168 ? 9.747  -14.514 1.109   0.38 18.83 ?  168 PHE   A HD1  1 
ATOM   3857 H HD2  A PHE   A 1 168 ? 7.589  -17.247 3.506   0.62 17.16 ?  168 PHE   A HD2  1 
ATOM   3858 H HD2  B PHE   A 1 168 ? 7.563  -16.992 3.359   0.38 18.50 ?  168 PHE   A HD2  1 
ATOM   3859 H HE1  A PHE   A 1 168 ? 11.555 -16.012 1.491   0.62 16.41 ?  168 PHE   A HE1  1 
ATOM   3860 H HE1  B PHE   A 1 168 ? 11.656 -15.671 1.685   0.38 19.19 ?  168 PHE   A HE1  1 
ATOM   3861 H HE2  A PHE   A 1 168 ? 9.528  -18.417 3.962   0.62 17.57 ?  168 PHE   A HE2  1 
ATOM   3862 H HE2  B PHE   A 1 168 ? 9.474  -18.154 3.939   0.38 18.90 ?  168 PHE   A HE2  1 
ATOM   3863 H HZ   A PHE   A 1 168 ? 11.518 -17.799 2.953   0.62 16.99 ?  168 PHE   A HZ   1 
ATOM   3864 H HZ   B PHE   A 1 168 ? 11.526 -17.491 3.099   0.38 19.07 ?  168 PHE   A HZ   1 
ATOM   3865 N N    A LEU   A 1 169 ? 7.171  -17.668 -0.265  0.62 17.97 ?  169 LEU   A N    1 
ATOM   3866 N N    B LEU   A 1 169 ? 7.101  -17.531 -0.303  0.38 15.99 ?  169 LEU   A N    1 
ATOM   3867 C CA   A LEU   A 1 169 ? 6.968  -19.096 -0.420  0.62 20.51 ?  169 LEU   A CA   1 
ATOM   3868 C CA   B LEU   A 1 169 ? 6.863  -18.966 -0.385  0.38 17.09 ?  169 LEU   A CA   1 
ATOM   3869 C C    A LEU   A 1 169 ? 7.814  -19.866 0.592   0.62 20.70 ?  169 LEU   A C    1 
ATOM   3870 C C    B LEU   A 1 169 ? 7.644  -19.710 0.700   0.38 16.37 ?  169 LEU   A C    1 
ATOM   3871 O O    A LEU   A 1 169 ? 7.288  -20.358 1.594   0.62 21.50 ?  169 LEU   A O    1 
ATOM   3872 O O    B LEU   A 1 169 ? 7.061  -20.421 1.526   0.38 16.90 ?  169 LEU   A O    1 
ATOM   3873 C CB   A LEU   A 1 169 ? 7.313  -19.530 -1.847  0.62 22.43 ?  169 LEU   A CB   1 
ATOM   3874 C CB   B LEU   A 1 169 ? 7.262  -19.488 -1.768  0.38 18.93 ?  169 LEU   A CB   1 
ATOM   3875 C CG   A LEU   A 1 169 ? 6.990  -20.986 -2.192  0.62 24.26 ?  169 LEU   A CG   1 
ATOM   3876 C CG   B LEU   A 1 169 ? 7.085  -20.992 -1.993  0.38 20.63 ?  169 LEU   A CG   1 
ATOM   3877 C CD1  A LEU   A 1 169 ? 5.557  -21.333 -1.816  0.62 25.00 ?  169 LEU   A CD1  1 
ATOM   3878 C CD1  B LEU   A 1 169 ? 5.658  -21.415 -1.694  0.38 21.37 ?  169 LEU   A CD1  1 
ATOM   3879 C CD2  A LEU   A 1 169 ? 7.230  -21.247 -3.671  0.62 24.90 ?  169 LEU   A CD2  1 
ATOM   3880 C CD2  B LEU   A 1 169 ? 7.469  -21.376 -3.416  0.38 21.16 ?  169 LEU   A CD2  1 
ATOM   3881 O OXT  A LEU   A 1 169 ? 9.032  -20.006 0.437   0.62 20.50 -1 169 LEU   A OXT  1 
ATOM   3882 O OXT  B LEU   A 1 169 ? 8.873  -19.611 0.776   0.38 16.07 -1 169 LEU   A OXT  1 
ATOM   3883 H H    A LEU   A 1 169 ? 7.884  -17.363 -0.635  0.62 21.59 ?  169 LEU   A H    1 
ATOM   3884 H H    B LEU   A 1 169 ? 7.780  -17.258 -0.759  0.38 19.21 ?  169 LEU   A H    1 
ATOM   3885 H HA   A LEU   A 1 169 ? 6.033  -19.298 -0.257  0.62 24.62 ?  169 LEU   A HA   1 
ATOM   3886 H HA   B LEU   A 1 169 ? 5.913  -19.133 -0.262  0.38 20.52 ?  169 LEU   A HA   1 
ATOM   3887 H HB2  A LEU   A 1 169 ? 6.820  -18.972 -2.469  0.62 26.94 ?  169 LEU   A HB2  1 
ATOM   3888 H HB2  B LEU   A 1 169 ? 6.727  -19.034 -2.438  0.38 22.73 ?  169 LEU   A HB2  1 
ATOM   3889 H HB3  A LEU   A 1 169 ? 8.264  -19.406 -1.985  0.62 26.94 ?  169 LEU   A HB3  1 
ATOM   3890 H HB3  B LEU   A 1 169 ? 8.198  -19.287 -1.912  0.38 22.73 ?  169 LEU   A HB3  1 
ATOM   3891 H HG   A LEU   A 1 169 ? 7.580  -21.568 -1.688  0.62 29.13 ?  169 LEU   A HG   1 
ATOM   3892 H HG   B LEU   A 1 169 ? 7.670  -21.475 -1.390  0.38 24.77 ?  169 LEU   A HG   1 
ATOM   3893 H HD11 A LEU   A 1 169 ? 5.316  -22.173 -2.235  0.62 30.02 ?  169 LEU   A HD11 1 
ATOM   3894 H HD11 B LEU   A 1 169 ? 5.534  -22.331 -1.986  0.38 25.66 ?  169 LEU   A HD11 1 
ATOM   3895 H HD12 A LEU   A 1 169 ? 5.494  -21.417 -0.851  0.62 30.02 ?  169 LEU   A HD12 1 
ATOM   3896 H HD12 B LEU   A 1 169 ? 5.502  -21.348 -0.739  0.38 25.66 ?  169 LEU   A HD12 1 
ATOM   3897 H HD13 A LEU   A 1 169 ? 4.969  -20.627 -2.127  0.62 30.02 ?  169 LEU   A HD13 1 
ATOM   3898 H HD13 B LEU   A 1 169 ? 5.049  -20.831 -2.172  0.38 25.66 ?  169 LEU   A HD13 1 
ATOM   3899 H HD21 A LEU   A 1 169 ? 7.027  -22.176 -3.866  0.62 29.89 ?  169 LEU   A HD21 1 
ATOM   3900 H HD21 B LEU   A 1 169 ? 7.349  -22.332 -3.530  0.38 25.40 ?  169 LEU   A HD21 1 
ATOM   3901 H HD22 A LEU   A 1 169 ? 6.653  -20.666 -4.192  0.62 29.89 ?  169 LEU   A HD22 1 
ATOM   3902 H HD22 B LEU   A 1 169 ? 6.898  -20.896 -4.037  0.38 25.40 ?  169 LEU   A HD22 1 
ATOM   3903 H HD23 A LEU   A 1 169 ? 8.159  -21.061 -3.878  0.62 29.89 ?  169 LEU   A HD23 1 
ATOM   3904 H HD23 B LEU   A 1 169 ? 8.396  -21.138 -3.568  0.38 25.40 ?  169 LEU   A HD23 1 
ATOM   3905 N N    A SER   B 1 1   ? 50.779 -9.219  -23.726 0.62 28.51 ?  1   SER   B N    1 
ATOM   3906 N N    B SER   B 1 1   ? 50.698 -9.201  -23.750 0.38 26.26 ?  1   SER   B N    1 
ATOM   3907 C CA   A SER   B 1 1   ? 51.272 -10.285 -22.831 0.62 28.52 ?  1   SER   B CA   1 
ATOM   3908 C CA   B SER   B 1 1   ? 51.167 -10.217 -22.788 0.38 26.11 ?  1   SER   B CA   1 
ATOM   3909 C C    A SER   B 1 1   ? 50.192 -11.322 -22.567 0.62 27.40 ?  1   SER   B C    1 
ATOM   3910 C C    B SER   B 1 1   ? 50.080 -11.248 -22.522 0.38 24.80 ?  1   SER   B C    1 
ATOM   3911 O O    A SER   B 1 1   ? 48.998 -11.096 -22.806 0.62 27.22 ?  1   SER   B O    1 
ATOM   3912 O O    B SER   B 1 1   ? 48.920 -11.084 -22.921 0.38 24.27 ?  1   SER   B O    1 
ATOM   3913 C CB   A SER   B 1 1   ? 51.752 -9.701  -21.505 0.62 29.07 ?  1   SER   B CB   1 
ATOM   3914 C CB   B SER   B 1 1   ? 51.585 -9.565  -21.474 0.38 26.77 ?  1   SER   B CB   1 
ATOM   3915 O OG   A SER   B 1 1   ? 50.656 -9.423  -20.655 0.62 30.80 ?  1   SER   B OG   1 
ATOM   3916 O OG   B SER   B 1 1   ? 50.461 -9.380  -20.633 0.38 28.17 ?  1   SER   B OG   1 
ATOM   3917 H H1   A SER   B 1 1   ? 50.545 -9.579  -24.503 0.62 34.23 ?  1   SER   B H1   1 
ATOM   3918 H H1   B SER   B 1 1   ? 51.395 -8.725  -24.027 0.38 31.53 ?  1   SER   B H1   1 
ATOM   3919 H H2   A SER   B 1 1   ? 50.081 -8.825  -23.350 0.62 34.23 ?  1   SER   B H2   1 
ATOM   3920 H H2   B SER   B 1 1   ? 50.318 -9.609  -24.440 0.38 31.53 ?  1   SER   B H2   1 
ATOM   3921 H H3   A SER   B 1 1   ? 51.430 -8.627  -23.852 0.62 34.23 ?  1   SER   B H3   1 
ATOM   3922 H H3   B SER   B 1 1   ? 50.111 -8.673  -23.348 0.38 31.53 ?  1   SER   B H3   1 
ATOM   3923 H HA   A SER   B 1 1   ? 52.021 -10.718 -23.263 0.62 34.24 ?  1   SER   B HA   1 
ATOM   3924 H HA   B SER   B 1 1   ? 51.936 -10.665 -23.168 0.38 31.35 ?  1   SER   B HA   1 
ATOM   3925 H HB2  A SER   B 1 1   ? 52.330 -10.349 -21.075 0.62 34.90 ?  1   SER   B HB2  1 
ATOM   3926 H HB2  B SER   B 1 1   ? 52.230 -10.141 -21.035 0.38 32.14 ?  1   SER   B HB2  1 
ATOM   3927 H HB3  A SER   B 1 1   ? 52.237 -8.880  -21.676 0.62 34.90 ?  1   SER   B HB3  1 
ATOM   3928 H HB3  B SER   B 1 1   ? 51.983 -8.701  -21.661 0.38 32.14 ?  1   SER   B HB3  1 
ATOM   3929 H HG   A SER   B 1 1   ? 50.881 -8.852  -20.081 0.62 36.97 ?  1   SER   B HG   1 
ATOM   3930 H HG   B SER   B 1 1   ? 50.596 -8.730  -20.119 0.38 33.82 ?  1   SER   B HG   1 
ATOM   3931 N N    A MET   B 1 2   ? 50.633 -12.457 -22.046 0.62 26.27 ?  2   MET   B N    1 
ATOM   3932 N N    B MET   B 1 2   ? 50.470 -12.305 -21.820 0.38 23.94 ?  2   MET   B N    1 
ATOM   3933 C CA   A MET   B 1 2   ? 49.804 -13.643 -21.882 0.62 25.89 ?  2   MET   B CA   1 
ATOM   3934 C CA   B MET   B 1 2   ? 49.657 -13.503 -21.655 0.38 23.59 ?  2   MET   B CA   1 
ATOM   3935 C C    A MET   B 1 2   ? 49.565 -13.854 -20.395 0.62 23.04 ?  2   MET   B C    1 
ATOM   3936 C C    B MET   B 1 2   ? 49.390 -13.694 -20.168 0.38 21.50 ?  2   MET   B C    1 
ATOM   3937 O O    A MET   B 1 2   ? 50.506 -14.121 -19.641 0.62 23.30 ?  2   MET   B O    1 
ATOM   3938 O O    B MET   B 1 2   ? 50.292 -14.080 -19.417 0.38 21.87 ?  2   MET   B O    1 
ATOM   3939 C CB   A MET   B 1 2   ? 50.517 -14.841 -22.495 0.62 29.54 ?  2   MET   B CB   1 
ATOM   3940 C CB   B MET   B 1 2   ? 50.411 -14.694 -22.238 0.38 26.12 ?  2   MET   B CB   1 
ATOM   3941 C CG   A MET   B 1 2   ? 49.661 -16.087 -22.633 0.62 32.81 ?  2   MET   B CG   1 
ATOM   3942 C CG   B MET   B 1 2   ? 49.546 -15.838 -22.741 0.38 28.26 ?  2   MET   B CG   1 
ATOM   3943 S SD   A MET   B 1 2   ? 50.485 -17.340 -23.634 0.62 35.94 ?  2   MET   B SD   1 
ATOM   3944 S SD   B MET   B 1 2   ? 50.486 -16.958 -23.793 0.38 30.39 ?  2   MET   B SD   1 
ATOM   3945 C CE   A MET   B 1 2   ? 51.028 -16.317 -25.001 0.62 36.20 ?  2   MET   B CE   1 
ATOM   3946 C CE   B MET   B 1 2   ? 51.439 -15.790 -24.745 0.38 30.44 ?  2   MET   B CE   1 
ATOM   3947 H H    A MET   B 1 2   ? 51.440 -12.571 -21.768 0.62 31.54 ?  2   MET   B H    1 
ATOM   3948 H H    B MET   B 1 2   ? 51.232 -12.360 -21.420 0.38 28.74 ?  2   MET   B H    1 
ATOM   3949 H HA   A MET   B 1 2   ? 48.961 -13.525 -22.342 0.62 31.09 ?  2   MET   B HA   1 
ATOM   3950 H HA   B MET   B 1 2   ? 48.824 -13.414 -22.142 0.38 28.33 ?  2   MET   B HA   1 
ATOM   3951 H HB2  A MET   B 1 2   ? 50.820 -14.563 -23.370 0.62 35.47 ?  2   MET   B HB2  1 
ATOM   3952 H HB2  B MET   B 1 2   ? 50.935 -14.339 -22.969 0.38 31.37 ?  2   MET   B HB2  1 
ATOM   3953 H HB3  A MET   B 1 2   ? 51.280 -15.080 -21.948 0.62 35.47 ?  2   MET   B HB3  1 
ATOM   3954 H HB3  B MET   B 1 2   ? 51.003 -15.070 -21.574 0.38 31.37 ?  2   MET   B HB3  1 
ATOM   3955 H HG2  A MET   B 1 2   ? 49.494 -16.456 -21.749 0.62 39.39 ?  2   MET   B HG2  1 
ATOM   3956 H HG2  B MET   B 1 2   ? 49.208 -16.344 -21.982 0.38 33.92 ?  2   MET   B HG2  1 
ATOM   3957 H HG3  A MET   B 1 2   ? 48.824 -15.858 -23.067 0.62 39.39 ?  2   MET   B HG3  1 
ATOM   3958 H HG3  B MET   B 1 2   ? 48.810 -15.496 -23.263 0.38 33.92 ?  2   MET   B HG3  1 
ATOM   3959 H HE1  A MET   B 1 2   ? 51.183 -16.880 -25.762 0.62 43.46 ?  2   MET   B HE1  1 
ATOM   3960 H HE1  B MET   B 1 2   ? 51.740 -16.225 -25.540 0.38 36.54 ?  2   MET   B HE1  1 
ATOM   3961 H HE2  A MET   B 1 2   ? 50.329 -15.668 -25.198 0.62 43.46 ?  2   MET   B HE2  1 
ATOM   3962 H HE2  B MET   B 1 2   ? 50.872 -15.033 -24.971 0.38 36.54 ?  2   MET   B HE2  1 
ATOM   3963 H HE3  A MET   B 1 2   ? 51.847 -15.848 -24.756 0.62 43.46 ?  2   MET   B HE3  1 
ATOM   3964 H HE3  B MET   B 1 2   ? 52.200 -15.492 -24.214 0.38 36.54 ?  2   MET   B HE3  1 
ATOM   3965 N N    A VAL   B 1 3   ? 48.310 -13.714 -19.974 0.62 20.43 ?  3   VAL   B N    1 
ATOM   3966 N N    B VAL   B 1 3   ? 48.163 -13.406 -19.741 0.38 19.31 ?  3   VAL   B N    1 
ATOM   3967 C CA   A VAL   B 1 3   ? 47.906 -13.964 -18.598 0.62 19.10 ?  3   VAL   B CA   1 
ATOM   3968 C CA   B VAL   B 1 3   ? 47.726 -13.671 -18.375 0.38 17.88 ?  3   VAL   B CA   1 
ATOM   3969 C C    A VAL   B 1 3   ? 46.665 -14.846 -18.616 0.62 17.14 ?  3   VAL   B C    1 
ATOM   3970 C C    B VAL   B 1 3   ? 46.475 -14.535 -18.417 0.38 16.32 ?  3   VAL   B C    1 
ATOM   3971 O O    A VAL   B 1 3   ? 45.965 -14.955 -19.627 0.62 17.08 ?  3   VAL   B O    1 
ATOM   3972 O O    B VAL   B 1 3   ? 45.624 -14.378 -19.299 0.38 15.70 ?  3   VAL   B O    1 
ATOM   3973 C CB   A VAL   B 1 3   ? 47.616 -12.658 -17.828 0.62 20.59 ?  3   VAL   B CB   1 
ATOM   3974 C CB   B VAL   B 1 3   ? 47.496 -12.388 -17.543 0.38 18.24 ?  3   VAL   B CB   1 
ATOM   3975 C CG1  A VAL   B 1 3   ? 48.872 -11.804 -17.719 0.62 21.16 ?  3   VAL   B CG1  1 
ATOM   3976 C CG1  B VAL   B 1 3   ? 48.791 -11.593 -17.419 0.38 18.53 ?  3   VAL   B CG1  1 
ATOM   3977 C CG2  A VAL   B 1 3   ? 46.493 -11.886 -18.506 0.62 21.11 ?  3   VAL   B CG2  1 
ATOM   3978 C CG2  B VAL   B 1 3   ? 46.385 -11.537 -18.138 0.38 18.27 ?  3   VAL   B CG2  1 
ATOM   3979 H H    A VAL   B 1 3   ? 47.665 -13.466 -20.485 0.62 24.53 ?  3   VAL   B H    1 
ATOM   3980 H H    B VAL   B 1 3   ? 47.555 -13.056 -20.242 0.38 23.19 ?  3   VAL   B H    1 
ATOM   3981 H HA   A VAL   B 1 3   ? 48.626 -14.436 -18.140 0.62 22.94 ?  3   VAL   B HA   1 
ATOM   3982 H HA   B VAL   B 1 3   ? 48.407 -14.184 -17.930 0.38 21.47 ?  3   VAL   B HA   1 
ATOM   3983 H HB   A VAL   B 1 3   ? 47.326 -12.888 -16.931 0.62 24.73 ?  3   VAL   B HB   1 
ATOM   3984 H HB   B VAL   B 1 3   ? 47.221 -12.644 -16.648 0.38 21.90 ?  3   VAL   B HB   1 
ATOM   3985 H HG11 A VAL   B 1 3   ? 48.658 -11.000 -17.221 0.62 25.40 ?  3   VAL   B HG11 1 
ATOM   3986 H HG11 B VAL   B 1 3   ? 48.627 -10.802 -16.882 0.38 22.25 ?  3   VAL   B HG11 1 
ATOM   3987 H HG12 A VAL   B 1 3   ? 49.557 -12.309 -17.256 0.62 25.40 ?  3   VAL   B HG12 1 
ATOM   3988 H HG12 B VAL   B 1 3   ? 49.462 -12.149 -16.993 0.38 22.25 ?  3   VAL   B HG12 1 
ATOM   3989 H HG13 A VAL   B 1 3   ? 49.173 -11.573 -18.611 0.62 25.40 ?  3   VAL   B HG13 1 
ATOM   3990 H HG13 B VAL   B 1 3   ? 49.088 -11.335 -18.306 0.38 22.25 ?  3   VAL   B HG13 1 
ATOM   3991 H HG21 A VAL   B 1 3   ? 46.404 -11.023 -18.078 0.62 25.35 ?  3   VAL   B HG21 1 
ATOM   3992 H HG21 B VAL   B 1 3   ? 46.355 -10.686 -17.672 0.38 21.94 ?  3   VAL   B HG21 1 
ATOM   3993 H HG22 A VAL   B 1 3   ? 46.709 -11.771 -19.445 0.62 25.35 ?  3   VAL   B HG22 1 
ATOM   3994 H HG22 B VAL   B 1 3   ? 46.569 -11.392 -19.078 0.38 21.94 ?  3   VAL   B HG22 1 
ATOM   3995 H HG23 A VAL   B 1 3   ? 45.664 -12.386 -18.418 0.62 25.35 ?  3   VAL   B HG23 1 
ATOM   3996 H HG23 B VAL   B 1 3   ? 45.539 -12.001 -18.032 0.38 21.94 ?  3   VAL   B HG23 1 
ATOM   3997 N N    . ASN   B 1 4   ? 46.382 -15.462 -17.467 1.00 15.66 ?  4   ASN   B N    1 
ATOM   3998 C CA   . ASN   B 1 4   ? 45.248 -16.382 -17.350 1.00 15.01 ?  4   ASN   B CA   1 
ATOM   3999 C C    . ASN   B 1 4   ? 45.198 -17.350 -18.533 1.00 15.48 ?  4   ASN   B C    1 
ATOM   4000 O O    . ASN   B 1 4   ? 44.137 -17.621 -19.092 1.00 16.42 ?  4   ASN   B O    1 
ATOM   4001 C CB   . ASN   B 1 4   ? 43.919 -15.637 -17.179 1.00 14.57 ?  4   ASN   B CB   1 
ATOM   4002 C CG   . ASN   B 1 4   ? 43.881 -14.813 -15.907 1.00 13.65 ?  4   ASN   B CG   1 
ATOM   4003 O OD1  . ASN   B 1 4   ? 44.165 -15.323 -14.822 1.00 13.45 ?  4   ASN   B OD1  1 
ATOM   4004 N ND2  . ASN   B 1 4   ? 43.562 -13.531 -16.037 1.00 14.55 ?  4   ASN   B ND2  1 
ATOM   4005 H H    A ASN   B 1 4   ? 46.822 -15.350 -16.739 0.62 18.81 ?  4   ASN   B H    1 
ATOM   4006 H H    B ASN   B 1 4   ? 46.989 -15.587 -16.872 0.38 18.81 ?  4   ASN   B H    1 
ATOM   4007 H HA   . ASN   B 1 4   ? 45.384 -16.916 -16.549 1.00 18.03 ?  4   ASN   B HA   1 
ATOM   4008 H HB2  . ASN   B 1 4   ? 43.781 -15.041 -17.925 1.00 17.50 ?  4   ASN   B HB2  1 
ATOM   4009 H HB3  . ASN   B 1 4   ? 43.197 -16.288 -17.134 1.00 17.50 ?  4   ASN   B HB3  1 
ATOM   4010 H HD21 . ASN   B 1 4   ? 43.531 -13.021 -15.342 1.00 17.47 ?  4   ASN   B HD21 1 
ATOM   4011 H HD22 . ASN   B 1 4   ? 43.381 -13.207 -16.813 1.00 17.47 ?  4   ASN   B HD22 1 
ATOM   4012 N N    . SER   B 1 5   ? 46.361 -17.876 -18.912 1.00 16.40 ?  5   SER   B N    1 
ATOM   4013 C CA   . SER   B 1 5   ? 46.465 -18.789 -20.048 1.00 18.89 ?  5   SER   B CA   1 
ATOM   4014 C C    . SER   B 1 5   ? 46.464 -20.225 -19.532 1.00 20.21 ?  5   SER   B C    1 
ATOM   4015 O O    . SER   B 1 5   ? 47.485 -20.908 -19.488 1.00 22.44 ?  5   SER   B O    1 
ATOM   4016 C CB   . SER   B 1 5   ? 47.715 -18.478 -20.868 1.00 20.67 ?  5   SER   B CB   1 
ATOM   4017 O OG   . SER   B 1 5   ? 48.887 -18.603 -20.080 1.00 23.38 ?  5   SER   B OG   1 
ATOM   4018 H H    . SER   B 1 5   ? 47.109 -17.733 -18.513 1.00 19.70 ?  5   SER   B H    1 
ATOM   4019 H HA   . SER   B 1 5   ? 45.692 -18.678 -20.620 1.00 22.69 ?  5   SER   B HA   1 
ATOM   4020 H HB2  . SER   B 1 5   ? 47.760 -19.090 -21.620 1.00 24.82 ?  5   SER   B HB2  1 
ATOM   4021 H HB3  . SER   B 1 5   ? 47.644 -17.568 -21.191 1.00 24.82 ?  5   SER   B HB3  1 
ATOM   4022 H HG   . SER   B 1 5   ? 48.975 -19.396 -19.820 1.00 28.07 ?  5   SER   B HG   1 
ATOM   4023 N N    . PHE   B 1 6   ? 45.279 -20.662 -19.116 1.00 20.03 ?  6   PHE   B N    1 
ATOM   4024 C CA   . PHE   B 1 6   ? 45.095 -22.008 -18.594 1.00 19.39 ?  6   PHE   B CA   1 
ATOM   4025 C C    . PHE   B 1 6   ? 45.018 -22.996 -19.747 1.00 22.30 ?  6   PHE   B C    1 
ATOM   4026 O O    . PHE   B 1 6   ? 44.342 -22.743 -20.746 1.00 24.45 ?  6   PHE   B O    1 
ATOM   4027 C CB   . PHE   B 1 6   ? 43.802 -22.074 -17.781 1.00 17.51 ?  6   PHE   B CB   1 
ATOM   4028 C CG   . PHE   B 1 6   ? 43.812 -21.211 -16.553 1.00 15.86 ?  6   PHE   B CG   1 
ATOM   4029 C CD1  . PHE   B 1 6   ? 44.316 -21.693 -15.362 1.00 14.73 ?  6   PHE   B CD1  1 
ATOM   4030 C CD2  . PHE   B 1 6   ? 43.324 -19.914 -16.594 1.00 15.43 ?  6   PHE   B CD2  1 
ATOM   4031 C CE1  . PHE   B 1 6   ? 44.322 -20.902 -14.223 1.00 14.50 ?  6   PHE   B CE1  1 
ATOM   4032 C CE2  . PHE   B 1 6   ? 43.341 -19.111 -15.462 1.00 16.08 ?  6   PHE   B CE2  1 
ATOM   4033 C CZ   . PHE   B 1 6   ? 43.842 -19.602 -14.278 1.00 15.17 ?  6   PHE   B CZ   1 
ATOM   4034 H H    . PHE   B 1 6   ? 44.557 -20.198 -19.134 1.00 24.05 ?  6   PHE   B H    1 
ATOM   4035 H HA   . PHE   B 1 6   ? 45.836 -22.249 -18.020 1.00 23.29 ?  6   PHE   B HA   1 
ATOM   4036 H HB2  . PHE   B 1 6   ? 43.063 -21.783 -18.340 1.00 21.03 ?  6   PHE   B HB2  1 
ATOM   4037 H HB3  . PHE   B 1 6   ? 43.653 -22.990 -17.496 1.00 21.03 ?  6   PHE   B HB3  1 
ATOM   4038 H HD1  . PHE   B 1 6   ? 44.648 -22.559 -15.317 1.00 17.69 ?  6   PHE   B HD1  1 
ATOM   4039 H HD2  . PHE   B 1 6   ? 42.982 -19.580 -17.390 1.00 18.54 ?  6   PHE   B HD2  1 
ATOM   4040 H HE1  . PHE   B 1 6   ? 44.673 -21.233 -13.425 1.00 17.42 ?  6   PHE   B HE1  1 
ATOM   4041 H HE2  . PHE   B 1 6   ? 43.003 -18.244 -15.501 1.00 19.31 ?  6   PHE   B HE2  1 
ATOM   4042 H HZ   . PHE   B 1 6   ? 43.851 -19.074 -13.512 1.00 18.22 ?  6   PHE   B HZ   1 
ATOM   4043 N N    . SER   B 1 7   ? 45.720 -24.122 -19.608 1.00 22.92 ?  7   SER   B N    1 
ATOM   4044 C CA   . SER   B 1 7   ? 45.790 -25.122 -20.664 1.00 24.98 ?  7   SER   B CA   1 
ATOM   4045 C C    . SER   B 1 7   ? 45.779 -26.524 -20.068 1.00 24.40 ?  7   SER   B C    1 
ATOM   4046 O O    . SER   B 1 7   ? 46.388 -26.772 -19.023 1.00 25.52 ?  7   SER   B O    1 
ATOM   4047 C CB   . SER   B 1 7   ? 47.058 -24.935 -21.510 1.00 27.50 ?  7   SER   B CB   1 
ATOM   4048 O OG   . SER   B 1 7   ? 47.043 -25.775 -22.649 1.00 29.56 ?  7   SER   B OG   1 
ATOM   4049 H H    . SER   B 1 7   ? 46.175 -24.329 -18.904 1.00 27.51 ?  7   SER   B H    1 
ATOM   4050 H HA   . SER   B 1 7   ? 45.021 -25.034 -21.245 1.00 29.99 ?  7   SER   B HA   1 
ATOM   4051 H HB2  . SER   B 1 7   ? 47.104 -24.014 -21.809 1.00 33.01 ?  7   SER   B HB2  1 
ATOM   4052 H HB3  . SER   B 1 7   ? 47.834 -25.146 -20.966 1.00 33.01 ?  7   SER   B HB3  1 
ATOM   4053 H HG   . SER   B 1 7   ? 47.747 -25.672 -23.096 1.00 35.49 ?  7   SER   B HG   1 
ATOM   4054 N N    A GLY   B 1 8   ? 45.084 -27.437 -20.743 0.62 24.22 ?  8   GLY   B N    1 
ATOM   4055 N N    B GLY   B 1 8   ? 45.090 -27.438 -20.746 0.38 24.08 ?  8   GLY   B N    1 
ATOM   4056 C CA   A GLY   B 1 8   ? 45.071 -28.826 -20.334 0.62 23.75 ?  8   GLY   B CA   1 
ATOM   4057 C CA   B GLY   B 1 8   ? 45.072 -28.824 -20.330 0.38 23.59 ?  8   GLY   B CA   1 
ATOM   4058 C C    A GLY   B 1 8   ? 44.100 -29.163 -19.230 0.62 22.58 ?  8   GLY   B C    1 
ATOM   4059 C C    B GLY   B 1 8   ? 44.124 -29.143 -19.201 0.38 22.58 ?  8   GLY   B C    1 
ATOM   4060 O O    A GLY   B 1 8   ? 44.222 -30.232 -18.621 0.62 23.54 ?  8   GLY   B O    1 
ATOM   4061 O O    B GLY   B 1 8   ? 44.293 -30.173 -18.540 0.38 23.28 ?  8   GLY   B O    1 
ATOM   4062 H H    A GLY   B 1 8   ? 44.615 -27.271 -21.443 0.62 29.08 ?  8   GLY   B H    1 
ATOM   4063 H H    B GLY   B 1 8   ? 44.627 -27.275 -21.451 0.38 28.91 ?  8   GLY   B H    1 
ATOM   4064 H HA2  A GLY   B 1 8   ? 44.848 -29.376 -21.100 0.62 28.52 ?  8   GLY   B HA2  1 
ATOM   4065 H HA2  B GLY   B 1 8   ? 44.828 -29.377 -21.088 0.38 28.33 ?  8   GLY   B HA2  1 
ATOM   4066 H HA3  A GLY   B 1 8   ? 45.956 -29.074 -20.032 0.62 28.52 ?  8   GLY   B HA3  1 
ATOM   4067 H HA3  B GLY   B 1 8   ? 45.962 -29.080 -20.046 0.38 28.33 ?  8   GLY   B HA3  1 
ATOM   4068 N N    . TYR   B 1 9   ? 43.125 -28.299 -18.958 1.00 21.41 ?  9   TYR   B N    1 
ATOM   4069 C CA   . TYR   B 1 9   ? 42.151 -28.554 -17.910 1.00 19.29 ?  9   TYR   B CA   1 
ATOM   4070 C C    . TYR   B 1 9   ? 40.969 -29.344 -18.445 1.00 18.59 ?  9   TYR   B C    1 
ATOM   4071 O O    . TYR   B 1 9   ? 40.562 -29.200 -19.603 1.00 20.36 ?  9   TYR   B O    1 
ATOM   4072 C CB   . TYR   B 1 9   ? 41.642 -27.256 -17.288 1.00 18.63 ?  9   TYR   B CB   1 
ATOM   4073 C CG   . TYR   B 1 9   ? 42.652 -26.631 -16.365 1.00 18.19 ?  9   TYR   B CG   1 
ATOM   4074 C CD1  . TYR   B 1 9   ? 43.756 -25.960 -16.875 1.00 19.02 ?  9   TYR   B CD1  1 
ATOM   4075 C CD2  . TYR   B 1 9   ? 42.526 -26.733 -14.990 1.00 17.36 ?  9   TYR   B CD2  1 
ATOM   4076 C CE1  . TYR   B 1 9   ? 44.702 -25.400 -16.042 1.00 18.93 ?  9   TYR   B CE1  1 
ATOM   4077 C CE2  . TYR   B 1 9   ? 43.468 -26.173 -14.146 1.00 17.70 ?  9   TYR   B CE2  1 
ATOM   4078 C CZ   . TYR   B 1 9   ? 44.554 -25.507 -14.682 1.00 18.69 ?  9   TYR   B CZ   1 
ATOM   4079 O OH   . TYR   B 1 9   ? 45.501 -24.957 -13.857 1.00 19.34 ?  9   TYR   B OH   1 
ATOM   4080 H H    A TYR   B 1 9   ? 42.998 -27.562 -19.380 0.62 25.71 ?  9   TYR   B H    1 
ATOM   4081 H H    B TYR   B 1 9   ? 42.983 -27.576 -19.398 0.38 25.71 ?  9   TYR   B H    1 
ATOM   4082 H HA   . TYR   B 1 9   ? 42.564 -29.078 -17.209 1.00 23.16 ?  9   TYR   B HA   1 
ATOM   4083 H HB2  . TYR   B 1 9   ? 41.434 -26.619 -17.989 1.00 22.37 ?  9   TYR   B HB2  1 
ATOM   4084 H HB3  . TYR   B 1 9   ? 40.850 -27.457 -16.771 1.00 22.37 ?  9   TYR   B HB3  1 
ATOM   4085 H HD1  . TYR   B 1 9   ? 43.858 -25.891 -17.796 1.00 22.84 ?  9   TYR   B HD1  1 
ATOM   4086 H HD2  . TYR   B 1 9   ? 41.792 -27.184 -14.628 1.00 20.85 ?  9   TYR   B HD2  1 
ATOM   4087 H HE1  . TYR   B 1 9   ? 45.431 -24.955 -16.397 1.00 22.74 ?  9   TYR   B HE1  1 
ATOM   4088 H HE2  . TYR   B 1 9   ? 43.361 -26.250 -13.221 1.00 21.25 ?  9   TYR   B HE2  1 
ATOM   4089 H HH   . TYR   B 1 9   ? 46.098 -24.586 -14.312 1.00 23.22 ?  9   TYR   B HH   1 
ATOM   4090 N N    . LEU   B 1 10  ? 40.425 -30.189 -17.576 1.00 16.62 ?  10  LEU   B N    1 
ATOM   4091 C CA   . LEU   B 1 10  ? 39.217 -30.944 -17.853 1.00 16.50 ?  10  LEU   B CA   1 
ATOM   4092 C C    . LEU   B 1 10  ? 38.026 -30.182 -17.288 1.00 15.73 ?  10  LEU   B C    1 
ATOM   4093 O O    . LEU   B 1 10  ? 38.034 -29.770 -16.123 1.00 15.64 ?  10  LEU   B O    1 
ATOM   4094 C CB   . LEU   B 1 10  ? 39.322 -32.316 -17.189 1.00 17.34 ?  10  LEU   B CB   1 
ATOM   4095 C CG   . LEU   B 1 10  ? 38.168 -33.266 -17.490 1.00 19.23 ?  10  LEU   B CG   1 
ATOM   4096 C CD1  . LEU   B 1 10  ? 38.230 -33.755 -18.931 1.00 20.95 ?  10  LEU   B CD1  1 
ATOM   4097 C CD2  . LEU   B 1 10  ? 38.168 -34.433 -16.518 1.00 20.55 ?  10  LEU   B CD2  1 
ATOM   4098 H H    . LEU   B 1 10  ? 40.750 -30.341 -16.789 1.00 19.96 ?  10  LEU   B H    1 
ATOM   4099 H HA   . LEU   B 1 10  ? 39.104 -31.060 -18.807 1.00 19.81 ?  10  LEU   B HA   1 
ATOM   4100 H HB2  . LEU   B 1 10  ? 40.140 -32.746 -17.488 1.00 20.82 ?  10  LEU   B HB2  1 
ATOM   4101 H HB3  . LEU   B 1 10  ? 39.355 -32.195 -16.225 1.00 20.82 ?  10  LEU   B HB3  1 
ATOM   4102 H HG   . LEU   B 1 10  ? 37.332 -32.791 -17.377 1.00 23.10 ?  10  LEU   B HG   1 
ATOM   4103 H HD11 . LEU   B 1 10  ? 37.517 -34.398 -19.074 1.00 25.15 ?  10  LEU   B HD11 1 
ATOM   4104 H HD12 . LEU   B 1 10  ? 38.113 -32.997 -19.525 1.00 25.15 ?  10  LEU   B HD12 1 
ATOM   4105 H HD13 . LEU   B 1 10  ? 39.089 -34.172 -19.087 1.00 25.15 ?  10  LEU   B HD13 1 
ATOM   4106 H HD21 . LEU   B 1 10  ? 37.429 -35.021 -16.736 1.00 24.67 ?  10  LEU   B HD21 1 
ATOM   4107 H HD22 . LEU   B 1 10  ? 39.008 -34.907 -16.596 1.00 24.67 ?  10  LEU   B HD22 1 
ATOM   4108 H HD23 . LEU   B 1 10  ? 38.063 -34.087 -15.618 1.00 24.67 ?  10  LEU   B HD23 1 
ATOM   4109 N N    . LYS   B 1 11  ? 37.006 -29.991 -18.114 1.00 17.07 ?  11  LYS   B N    1 
ATOM   4110 C CA   . LYS   B 1 11  ? 35.812 -29.273 -17.696 1.00 18.80 ?  11  LYS   B CA   1 
ATOM   4111 C C    . LYS   B 1 11  ? 34.928 -30.200 -16.866 1.00 18.08 ?  11  LYS   B C    1 
ATOM   4112 O O    . LYS   B 1 11  ? 34.560 -31.287 -17.325 1.00 19.89 ?  11  LYS   B O    1 
ATOM   4113 C CB   . LYS   B 1 11  ? 35.072 -28.788 -18.940 1.00 22.90 ?  11  LYS   B CB   1 
ATOM   4114 C CG   . LYS   B 1 11  ? 33.892 -27.872 -18.679 1.00 26.52 ?  11  LYS   B CG   1 
ATOM   4115 C CD   . LYS   B 1 11  ? 33.150 -27.584 -19.979 1.00 29.74 ?  11  LYS   B CD   1 
ATOM   4116 C CE   . LYS   B 1 11  ? 32.134 -26.468 -19.816 1.00 32.07 ?  11  LYS   B CE   1 
ATOM   4117 N NZ   . LYS   B 1 11  ? 32.794 -25.147 -19.641 1.00 33.26 ?  11  LYS   B NZ   1 
ATOM   4118 H H    . LYS   B 1 11  ? 36.980 -30.276 -18.926 1.00 20.50 ?  11  LYS   B H    1 
ATOM   4119 H HA   . LYS   B 1 11  ? 36.062 -28.507 -17.156 1.00 22.58 ?  11  LYS   B HA   1 
ATOM   4120 H HB2  . LYS   B 1 11  ? 35.699 -28.301 -19.500 1.00 27.49 ?  11  LYS   B HB2  1 
ATOM   4121 H HB3  . LYS   B 1 11  ? 34.741 -29.561 -19.423 1.00 27.49 ?  11  LYS   B HB3  1 
ATOM   4122 H HG2  . LYS   B 1 11  ? 33.277 -28.302 -18.065 1.00 31.84 ?  11  LYS   B HG2  1 
ATOM   4123 H HG3  . LYS   B 1 11  ? 34.207 -27.032 -18.313 1.00 31.84 ?  11  LYS   B HG3  1 
ATOM   4124 H HD2  . LYS   B 1 11  ? 33.790 -27.315 -20.658 1.00 35.70 ?  11  LYS   B HD2  1 
ATOM   4125 H HD3  . LYS   B 1 11  ? 32.681 -28.385 -20.263 1.00 35.70 ?  11  LYS   B HD3  1 
ATOM   4126 H HE2  . LYS   B 1 11  ? 31.576 -26.428 -20.609 1.00 38.49 ?  11  LYS   B HE2  1 
ATOM   4127 H HE3  . LYS   B 1 11  ? 31.592 -26.648 -19.033 1.00 38.49 ?  11  LYS   B HE3  1 
ATOM   4128 H HZ1  . LYS   B 1 11  ? 32.179 -24.510 -19.561 1.00 39.93 ?  11  LYS   B HZ1  1 
ATOM   4129 H HZ2  . LYS   B 1 11  ? 33.301 -25.155 -18.910 1.00 39.93 ?  11  LYS   B HZ2  1 
ATOM   4130 H HZ3  . LYS   B 1 11  ? 33.306 -24.968 -20.347 1.00 39.93 ?  11  LYS   B HZ3  1 
ATOM   4131 N N    . LEU   B 1 12  ? 34.591 -29.777 -15.647 1.00 17.06 ?  12  LEU   B N    1 
ATOM   4132 C CA   . LEU   B 1 12  ? 33.631 -30.489 -14.808 1.00 16.56 ?  12  LEU   B CA   1 
ATOM   4133 C C    . LEU   B 1 12  ? 32.238 -29.888 -14.900 1.00 16.41 ?  12  LEU   B C    1 
ATOM   4134 O O    . LEU   B 1 12  ? 31.255 -30.614 -15.075 1.00 17.04 ?  12  LEU   B O    1 
ATOM   4135 C CB   . LEU   B 1 12  ? 34.087 -30.497 -13.345 1.00 15.92 ?  12  LEU   B CB   1 
ATOM   4136 C CG   . LEU   B 1 12  ? 35.420 -31.186 -13.065 1.00 15.84 ?  12  LEU   B CG   1 
ATOM   4137 C CD1  . LEU   B 1 12  ? 35.737 -31.147 -11.582 1.00 16.12 ?  12  LEU   B CD1  1 
ATOM   4138 C CD2  . LEU   B 1 12  ? 35.410 -32.619 -13.578 1.00 16.51 ?  12  LEU   B CD2  1 
ATOM   4139 H H    . LEU   B 1 12  ? 34.908 -29.064 -15.283 1.00 20.49 ?  12  LEU   B H    1 
ATOM   4140 H HA   . LEU   B 1 12  ? 33.565 -31.400 -15.111 1.00 19.89 ?  12  LEU   B HA   1 
ATOM   4141 H HB2  . LEU   B 1 12  ? 34.167 -29.577 -13.045 1.00 19.12 ?  12  LEU   B HB2  1 
ATOM   4142 H HB3  . LEU   B 1 12  ? 33.408 -30.948 -12.820 1.00 19.12 ?  12  LEU   B HB3  1 
ATOM   4143 H HG   . LEU   B 1 12  ? 36.123 -30.710 -13.533 1.00 19.03 ?  12  LEU   B HG   1 
ATOM   4144 H HD11 . LEU   B 1 12  ? 36.588 -31.590 -11.430 1.00 19.36 ?  12  LEU   B HD11 1 
ATOM   4145 H HD12 . LEU   B 1 12  ? 35.789 -30.224 -11.293 1.00 19.36 ?  12  LEU   B HD12 1 
ATOM   4146 H HD13 . LEU   B 1 12  ? 35.035 -31.609 -11.096 1.00 19.36 ?  12  LEU   B HD13 1 
ATOM   4147 H HD21 . LEU   B 1 12  ? 36.196 -33.077 -13.249 1.00 19.82 ?  12  LEU   B HD21 1 
ATOM   4148 H HD22 . LEU   B 1 12  ? 34.608 -33.062 -13.257 1.00 19.82 ?  12  LEU   B HD22 1 
ATOM   4149 H HD23 . LEU   B 1 12  ? 35.413 -32.607 -14.549 1.00 19.82 ?  12  LEU   B HD23 1 
ATOM   4150 N N    . THR   B 1 13  ? 32.142 -28.569 -14.768 1.00 16.15 ?  13  THR   B N    1 
ATOM   4151 C CA   . THR   B 1 13  ? 30.915 -27.820 -14.977 1.00 16.08 ?  13  THR   B CA   1 
ATOM   4152 C C    . THR   B 1 13  ? 31.244 -26.621 -15.859 1.00 17.92 ?  13  THR   B C    1 
ATOM   4153 O O    . THR   B 1 13  ? 32.391 -26.424 -16.281 1.00 18.98 ?  13  THR   B O    1 
ATOM   4154 C CB   . THR   B 1 13  ? 30.309 -27.350 -13.650 1.00 15.69 ?  13  THR   B CB   1 
ATOM   4155 O OG1  . THR   B 1 13  ? 31.138 -26.320 -13.105 1.00 15.45 ?  13  THR   B OG1  1 
ATOM   4156 C CG2  . THR   B 1 13  ? 30.200 -28.498 -12.652 1.00 16.39 ?  13  THR   B CG2  1 
ATOM   4157 H H    . THR   B 1 13  ? 32.804 -28.059 -14.548 1.00 19.40 ?  13  THR   B H    1 
ATOM   4158 H HA   . THR   B 1 13  ? 30.265 -28.372 -15.429 1.00 19.31 ?  13  THR   B HA   1 
ATOM   4159 H HB   . THR   B 1 13  ? 29.417 -26.990 -13.806 1.00 18.84 ?  13  THR   B HB   1 
ATOM   4160 H HG1  . THR   B 1 13  ? 30.816 -25.557 -13.286 1.00 18.56 ?  13  THR   B HG1  1 
ATOM   4161 H HG21 . THR   B 1 13  ? 29.686 -28.218 -11.878 1.00 19.68 ?  13  THR   B HG21 1 
ATOM   4162 H HG22 . THR   B 1 13  ? 29.756 -29.251 -13.069 1.00 19.68 ?  13  THR   B HG22 1 
ATOM   4163 H HG23 . THR   B 1 13  ? 31.084 -28.770 -12.364 1.00 19.68 ?  13  THR   B HG23 1 
ATOM   4164 N N    A ASP   B 1 14  ? 30.228 -25.799 -16.125 0.62 18.73 ?  14  ASP   B N    1 
ATOM   4165 N N    B ASP   B 1 14  ? 30.233 -25.787 -16.116 0.38 18.82 ?  14  ASP   B N    1 
ATOM   4166 C CA   A ASP   B 1 14  ? 30.436 -24.633 -16.976 0.62 20.39 ?  14  ASP   B CA   1 
ATOM   4167 C CA   B ASP   B 1 14  ? 30.423 -24.626 -16.979 0.38 19.93 ?  14  ASP   B CA   1 
ATOM   4168 C C    A ASP   B 1 14  ? 31.545 -23.732 -16.444 0.62 18.45 ?  14  ASP   B C    1 
ATOM   4169 C C    B ASP   B 1 14  ? 31.390 -23.603 -16.404 0.38 18.09 ?  14  ASP   B C    1 
ATOM   4170 O O    A ASP   B 1 14  ? 32.228 -23.066 -17.231 0.62 18.79 ?  14  ASP   B O    1 
ATOM   4171 O O    B ASP   B 1 14  ? 31.774 -22.677 -17.125 0.38 18.16 ?  14  ASP   B O    1 
ATOM   4172 C CB   A ASP   B 1 14  ? 29.129 -23.853 -17.128 0.62 23.80 ?  14  ASP   B CB   1 
ATOM   4173 C CB   B ASP   B 1 14  ? 29.092 -23.925 -17.244 0.38 22.70 ?  14  ASP   B CB   1 
ATOM   4174 C CG   A ASP   B 1 14  ? 28.145 -24.529 -18.061 0.62 27.48 ?  14  ASP   B CG   1 
ATOM   4175 C CG   B ASP   B 1 14  ? 28.241 -24.660 -18.261 0.38 25.44 ?  14  ASP   B CG   1 
ATOM   4176 O OD1  A ASP   B 1 14  ? 28.513 -25.513 -18.742 0.62 28.67 ?  14  ASP   B OD1  1 
ATOM   4177 O OD1  B ASP   B 1 14  ? 28.817 -25.272 -19.186 0.38 26.34 ?  14  ASP   B OD1  1 
ATOM   4178 O OD2  A ASP   B 1 14  ? 26.986 -24.070 -18.104 0.62 28.83 -1 14  ASP   B OD2  1 
ATOM   4179 O OD2  B ASP   B 1 14  ? 27.000 -24.629 -18.139 0.38 26.33 -1 14  ASP   B OD2  1 
ATOM   4180 H H    A ASP   B 1 14  ? 29.430 -25.883 -15.817 0.62 22.49 ?  14  ASP   B H    1 
ATOM   4181 H H    B ASP   B 1 14  ? 29.438 -25.864 -15.796 0.38 22.59 ?  14  ASP   B H    1 
ATOM   4182 H HA   A ASP   B 1 14  ? 30.706 -24.927 -17.854 0.62 24.48 ?  14  ASP   B HA   1 
ATOM   4183 H HA   B ASP   B 1 14  ? 30.771 -24.929 -17.833 0.38 23.93 ?  14  ASP   B HA   1 
ATOM   4184 H HB2  A ASP   B 1 14  ? 28.687 -23.785 -16.269 0.62 28.57 ?  14  ASP   B HB2  1 
ATOM   4185 H HB2  B ASP   B 1 14  ? 28.596 -23.869 -16.411 0.38 27.26 ?  14  ASP   B HB2  1 
ATOM   4186 H HB3  A ASP   B 1 14  ? 29.315 -22.970 -17.481 0.62 28.57 ?  14  ASP   B HB3  1 
ATOM   4187 H HB3  B ASP   B 1 14  ? 29.271 -23.027 -17.578 0.38 27.26 ?  14  ASP   B HB3  1 
ATOM   4188 N N    . ASN   B 1 15  ? 31.761 -23.718 -15.126 1.00 16.18 ?  15  ASN   B N    1 
ATOM   4189 C CA   . ASN   B 1 15  ? 32.713 -22.790 -14.520 1.00 14.10 ?  15  ASN   B CA   1 
ATOM   4190 C C    . ASN   B 1 15  ? 33.809 -23.442 -13.685 1.00 12.79 ?  15  ASN   B C    1 
ATOM   4191 O O    . ASN   B 1 15  ? 34.646 -22.716 -13.139 1.00 13.36 ?  15  ASN   B O    1 
ATOM   4192 C CB   . ASN   B 1 15  ? 31.992 -21.740 -13.659 1.00 14.48 ?  15  ASN   B CB   1 
ATOM   4193 C CG   . ASN   B 1 15  ? 31.370 -22.340 -12.421 1.00 14.17 ?  15  ASN   B CG   1 
ATOM   4194 O OD1  . ASN   B 1 15  ? 30.430 -23.131 -12.509 1.00 15.83 ?  15  ASN   B OD1  1 
ATOM   4195 N ND2  . ASN   B 1 15  ? 31.894 -21.988 -11.261 1.00 13.27 ?  15  ASN   B ND2  1 
ATOM   4196 H H    A ASN   B 1 15  ? 31.379 -24.251 -14.565 0.62 19.43 ?  15  ASN   B H    1 
ATOM   4197 H H    B ASN   B 1 15  ? 31.445 -24.307 -14.582 0.38 19.43 ?  15  ASN   B H    1 
ATOM   4198 H HA   . ASN   B 1 15  ? 33.161 -22.309 -15.225 1.00 16.94 ?  15  ASN   B HA   1 
ATOM   4199 H HB2  . ASN   B 1 15  ? 32.636 -21.064 -13.378 1.00 17.39 ?  15  ASN   B HB2  1 
ATOM   4200 H HB3  . ASN   B 1 15  ? 31.288 -21.322 -14.180 1.00 17.39 ?  15  ASN   B HB3  1 
ATOM   4201 H HD21 . ASN   B 1 15  ? 31.575 -22.302 -10.525 1.00 15.94 ?  15  ASN   B HD21 1 
ATOM   4202 H HD22 . ASN   B 1 15  ? 32.563 -21.439 -11.230 1.00 15.94 ?  15  ASN   B HD22 1 
ATOM   4203 N N    . VAL   B 1 16  ? 33.835 -24.767 -13.555 1.00 12.96 ?  16  VAL   B N    1 
ATOM   4204 C CA   . VAL   B 1 16  ? 34.829 -25.459 -12.738 1.00 12.51 ?  16  VAL   B CA   1 
ATOM   4205 C C    . VAL   B 1 16  ? 35.625 -26.399 -13.627 1.00 12.42 ?  16  VAL   B C    1 
ATOM   4206 O O    . VAL   B 1 16  ? 35.051 -27.281 -14.284 1.00 13.88 ?  16  VAL   B O    1 
ATOM   4207 C CB   . VAL   B 1 16  ? 34.188 -26.223 -11.565 1.00 13.05 ?  16  VAL   B CB   1 
ATOM   4208 C CG1  . VAL   B 1 16  ? 35.261 -26.970 -10.773 1.00 12.96 ?  16  VAL   B CG1  1 
ATOM   4209 C CG2  . VAL   B 1 16  ? 33.401 -25.269 -10.670 1.00 13.70 ?  16  VAL   B CG2  1 
ATOM   4210 H H    . VAL   B 1 16  ? 33.274 -25.301 -13.938 1.00 15.57 ?  16  VAL   B H    1 
ATOM   4211 H HA   . VAL   B 1 16  ? 35.441 -24.807 -12.364 1.00 15.02 ?  16  VAL   B HA   1 
ATOM   4212 H HB   . VAL   B 1 16  ? 33.569 -26.882 -11.919 1.00 15.67 ?  16  VAL   B HB   1 
ATOM   4213 H HG11 . VAL   B 1 16  ? 34.879 -27.267 -9.930  1.00 15.56 ?  16  VAL   B HG11 1 
ATOM   4214 H HG12 . VAL   B 1 16  ? 35.562 -27.737 -11.284 1.00 15.56 ?  16  VAL   B HG12 1 
ATOM   4215 H HG13 . VAL   B 1 16  ? 36.004 -26.370 -10.602 1.00 15.56 ?  16  VAL   B HG13 1 
ATOM   4216 H HG21 . VAL   B 1 16  ? 33.047 -25.762 -9.914  1.00 16.46 ?  16  VAL   B HG21 1 
ATOM   4217 H HG22 . VAL   B 1 16  ? 33.990 -24.565 -10.361 1.00 16.46 ?  16  VAL   B HG22 1 
ATOM   4218 H HG23 . VAL   B 1 16  ? 32.671 -24.885 -11.184 1.00 16.46 ?  16  VAL   B HG23 1 
ATOM   4219 N N    . TYR   B 1 17  ? 36.951 -26.234 -13.595 1.00 12.91 ?  17  TYR   B N    1 
ATOM   4220 C CA   . TYR   B 1 17  ? 37.903 -26.981 -14.405 1.00 13.30 ?  17  TYR   B CA   1 
ATOM   4221 C C    . TYR   B 1 17  ? 38.954 -27.591 -13.489 1.00 12.71 ?  17  TYR   B C    1 
ATOM   4222 O O    . TYR   B 1 17  ? 39.220 -27.065 -12.405 1.00 12.78 ?  17  TYR   B O    1 
ATOM   4223 C CB   . TYR   B 1 17  ? 38.613 -26.042 -15.393 1.00 15.77 ?  17  TYR   B CB   1 
ATOM   4224 C CG   . TYR   B 1 17  ? 37.681 -25.276 -16.299 1.00 18.72 ?  17  TYR   B CG   1 
ATOM   4225 C CD1  . TYR   B 1 17  ? 37.065 -24.106 -15.872 1.00 19.84 ?  17  TYR   B CD1  1 
ATOM   4226 C CD2  . TYR   B 1 17  ? 37.422 -25.722 -17.587 1.00 20.71 ?  17  TYR   B CD2  1 
ATOM   4227 C CE1  . TYR   B 1 17  ? 36.210 -23.403 -16.705 1.00 21.08 ?  17  TYR   B CE1  1 
ATOM   4228 C CE2  . TYR   B 1 17  ? 36.571 -25.029 -18.427 1.00 22.05 ?  17  TYR   B CE2  1 
ATOM   4229 C CZ   . TYR   B 1 17  ? 35.967 -23.871 -17.981 1.00 22.56 ?  17  TYR   B CZ   1 
ATOM   4230 O OH   . TYR   B 1 17  ? 35.123 -23.176 -18.816 1.00 24.48 ?  17  TYR   B OH   1 
ATOM   4231 H H    . TYR   B 1 17  ? 37.347 -25.661 -13.079 1.00 15.50 ?  17  TYR   B H    1 
ATOM   4232 H HA   . TYR   B 1 17  ? 37.450 -27.687 -14.896 1.00 15.97 ?  17  TYR   B HA   1 
ATOM   4233 H HB2  . TYR   B 1 17  ? 39.141 -25.399 -14.894 1.00 18.94 ?  17  TYR   B HB2  1 
ATOM   4234 H HB3  . TYR   B 1 17  ? 39.192 -26.571 -15.959 1.00 18.94 ?  17  TYR   B HB3  1 
ATOM   4235 H HD1  . TYR   B 1 17  ? 37.229 -23.790 -15.013 1.00 23.82 ?  17  TYR   B HD1  1 
ATOM   4236 H HD2  . TYR   B 1 17  ? 37.825 -26.501 -17.893 1.00 24.86 ?  17  TYR   B HD2  1 
ATOM   4237 H HE1  . TYR   B 1 17  ? 35.801 -22.620 -16.408 1.00 25.32 ?  17  TYR   B HE1  1 
ATOM   4238 H HE2  . TYR   B 1 17  ? 36.403 -25.340 -19.288 1.00 26.48 ?  17  TYR   B HE2  1 
ATOM   4239 H HH   . TYR   B 1 17  ? 35.057 -23.564 -19.557 1.00 29.39 ?  17  TYR   B HH   1 
ATOM   4240 N N    . ILE   B 1 18  ? 39.573 -28.693 -13.921 1.00 12.94 ?  18  ILE   B N    1 
ATOM   4241 C CA   . ILE   B 1 18  ? 40.500 -29.418 -13.058 1.00 12.50 ?  18  ILE   B CA   1 
ATOM   4242 C C    . ILE   B 1 18  ? 41.663 -29.969 -13.874 1.00 13.09 ?  18  ILE   B C    1 
ATOM   4243 O O    . ILE   B 1 18  ? 41.504 -30.367 -15.031 1.00 14.34 ?  18  ILE   B O    1 
ATOM   4244 C CB   . ILE   B 1 18  ? 39.748 -30.519 -12.265 1.00 13.25 ?  18  ILE   B CB   1 
ATOM   4245 C CG1  . ILE   B 1 18  ? 40.607 -31.078 -11.129 1.00 13.86 ?  18  ILE   B CG1  1 
ATOM   4246 C CG2  . ILE   B 1 18  ? 39.251 -31.637 -13.195 1.00 13.29 ?  18  ILE   B CG2  1 
ATOM   4247 C CD1  . ILE   B 1 18  ? 39.796 -31.879 -10.106 1.00 15.41 ?  18  ILE   B CD1  1 
ATOM   4248 H H    . ILE   B 1 18  ? 39.474 -29.036 -14.703 1.00 15.54 ?  18  ILE   B H    1 
ATOM   4249 H HA   . ILE   B 1 18  ? 40.863 -28.800 -12.407 1.00 15.01 ?  18  ILE   B HA   1 
ATOM   4250 H HB   . ILE   B 1 18  ? 38.966 -30.115 -11.860 1.00 15.91 ?  18  ILE   B HB   1 
ATOM   4251 H HG12 . ILE   B 1 18  ? 41.281 -31.666 -11.500 1.00 16.64 ?  18  ILE   B HG12 1 
ATOM   4252 H HG13 . ILE   B 1 18  ? 41.028 -30.339 -10.663 1.00 16.64 ?  18  ILE   B HG13 1 
ATOM   4253 H HG21 . ILE   B 1 18  ? 38.662 -32.227 -12.695 1.00 15.96 ?  18  ILE   B HG21 1 
ATOM   4254 H HG22 . ILE   B 1 18  ? 38.762 -31.234 -13.931 1.00 15.96 ?  18  ILE   B HG22 1 
ATOM   4255 H HG23 . ILE   B 1 18  ? 40.010 -32.133 -13.532 1.00 15.96 ?  18  ILE   B HG23 1 
ATOM   4256 H HD11 . ILE   B 1 18  ? 40.385 -32.166 -9.391  1.00 18.51 ?  18  ILE   B HD11 1 
ATOM   4257 H HD12 . ILE   B 1 18  ? 39.093 -31.312 -9.747  1.00 18.51 ?  18  ILE   B HD12 1 
ATOM   4258 H HD13 . ILE   B 1 18  ? 39.406 -32.650 -10.544 1.00 18.51 ?  18  ILE   B HD13 1 
ATOM   4259 N N    . LYS   B 1 19  ? 42.844 -29.997 -13.253 1.00 13.72 ?  19  LYS   B N    1 
ATOM   4260 C CA   . LYS   B 1 19  ? 44.057 -30.477 -13.900 1.00 14.44 ?  19  LYS   B CA   1 
ATOM   4261 C C    . LYS   B 1 19  ? 44.949 -31.164 -12.878 1.00 14.13 ?  19  LYS   B C    1 
ATOM   4262 O O    . LYS   B 1 19  ? 45.034 -30.731 -11.727 1.00 13.65 ?  19  LYS   B O    1 
ATOM   4263 C CB   . LYS   B 1 19  ? 44.839 -29.315 -14.529 1.00 15.99 ?  19  LYS   B CB   1 
ATOM   4264 C CG   . LYS   B 1 19  ? 46.066 -29.724 -15.329 1.00 17.68 ?  19  LYS   B CG   1 
ATOM   4265 C CD   . LYS   B 1 19  ? 46.786 -28.493 -15.863 1.00 19.57 ?  19  LYS   B CD   1 
ATOM   4266 C CE   . LYS   B 1 19  ? 47.926 -28.861 -16.793 1.00 21.81 ?  19  LYS   B CE   1 
ATOM   4267 N NZ   . LYS   B 1 19  ? 48.666 -27.660 -17.265 1.00 22.79 ?  19  LYS   B NZ   1 
ATOM   4268 H H    . LYS   B 1 19  ? 42.961 -29.730 -12.440 1.00 16.48 ?  19  LYS   B H    1 
ATOM   4269 H HA   . LYS   B 1 19  ? 43.825 -31.112 -14.591 1.00 17.35 ?  19  LYS   B HA   1 
ATOM   4270 H HB2  . LYS   B 1 19  ? 44.248 -28.835 -15.126 1.00 19.21 ?  19  LYS   B HB2  1 
ATOM   4271 H HB3  . LYS   B 1 19  ? 45.135 -28.721 -13.817 1.00 19.21 ?  19  LYS   B HB3  1 
ATOM   4272 H HG2  . LYS   B 1 19  ? 46.676 -30.216 -14.758 1.00 21.23 ?  19  LYS   B HG2  1 
ATOM   4273 H HG3  . LYS   B 1 19  ? 45.789 -30.272 -16.080 1.00 21.23 ?  19  LYS   B HG3  1 
ATOM   4274 H HD2  . LYS   B 1 19  ? 46.155 -27.943 -16.354 1.00 23.49 ?  19  LYS   B HD2  1 
ATOM   4275 H HD3  . LYS   B 1 19  ? 47.152 -27.991 -15.115 1.00 23.49 ?  19  LYS   B HD3  1 
ATOM   4276 H HE2  . LYS   B 1 19  ? 48.548 -29.436 -16.321 1.00 26.19 ?  19  LYS   B HE2  1 
ATOM   4277 H HE3  . LYS   B 1 19  ? 47.566 -29.322 -17.567 1.00 26.19 ?  19  LYS   B HE3  1 
ATOM   4278 H HZ1  . LYS   B 1 19  ? 49.301 -27.902 -17.840 1.00 27.36 ?  19  LYS   B HZ1  1 
ATOM   4279 H HZ2  . LYS   B 1 19  ? 48.107 -27.099 -17.672 1.00 27.36 ?  19  LYS   B HZ2  1 
ATOM   4280 H HZ3  . LYS   B 1 19  ? 49.043 -27.244 -16.576 1.00 27.36 ?  19  LYS   B HZ3  1 
ATOM   4281 N N    . ASN   B 1 20  ? 45.641 -32.209 -13.316 1.00 15.44 ?  20  ASN   B N    1 
ATOM   4282 C CA   . ASN   B 1 20  ? 46.670 -32.840 -12.496 1.00 16.36 ?  20  ASN   B CA   1 
ATOM   4283 C C    . ASN   B 1 20  ? 47.938 -32.015 -12.686 1.00 16.53 ?  20  ASN   B C    1 
ATOM   4284 O O    . ASN   B 1 20  ? 48.583 -32.087 -13.738 1.00 18.50 ?  20  ASN   B O    1 
ATOM   4285 C CB   . ASN   B 1 20  ? 46.850 -34.293 -12.928 1.00 17.61 ?  20  ASN   B CB   1 
ATOM   4286 C CG   . ASN   B 1 20  ? 48.014 -34.980 -12.242 1.00 18.85 ?  20  ASN   B CG   1 
ATOM   4287 O OD1  . ASN   B 1 20  ? 48.712 -35.793 -12.857 1.00 21.27 ?  20  ASN   B OD1  1 
ATOM   4288 N ND2  . ASN   B 1 20  ? 48.225 -34.677 -10.971 1.00 18.65 ?  20  ASN   B ND2  1 
ATOM   4289 H H    . ASN   B 1 20  ? 45.536 -32.561 -14.091 1.00 18.54 ?  20  ASN   B H    1 
ATOM   4290 H HA   . ASN   B 1 20  ? 46.396 -32.813 -11.563 1.00 19.64 ?  20  ASN   B HA   1 
ATOM   4291 H HB2  . ASN   B 1 20  ? 46.042 -34.783 -12.710 1.00 21.15 ?  20  ASN   B HB2  1 
ATOM   4292 H HB3  . ASN   B 1 20  ? 47.002 -34.310 -13.884 1.00 21.15 ?  20  ASN   B HB3  1 
ATOM   4293 H HD21 . ASN   B 1 20  ? 48.878 -35.032 -10.546 1.00 22.40 ?  20  ASN   B HD21 1 
ATOM   4294 H HD22 . ASN   B 1 20  ? 47.711 -34.109 -10.568 1.00 22.40 ?  20  ASN   B HD22 1 
ATOM   4295 N N    . ALA   B 1 21  ? 48.291 -31.208 -11.680 1.00 16.04 ?  21  ALA   B N    1 
ATOM   4296 C CA   . ALA   B 1 21  ? 49.405 -30.283 -11.824 1.00 17.00 ?  21  ALA   B CA   1 
ATOM   4297 C C    . ALA   B 1 21  ? 49.860 -29.787 -10.459 1.00 15.89 ?  21  ALA   B C    1 
ATOM   4298 O O    . ALA   B 1 21  ? 49.115 -29.824 -9.476  1.00 16.00 ?  21  ALA   B O    1 
ATOM   4299 C CB   . ALA   B 1 21  ? 49.025 -29.104 -12.720 1.00 18.29 ?  21  ALA   B CB   1 
ATOM   4300 H H    . ALA   B 1 21  ? 47.901 -31.181 -10.907 1.00 19.27 ?  21  ALA   B H    1 
ATOM   4301 H HA   . ALA   B 1 21  ? 50.145 -30.752 -12.235 1.00 20.42 ?  21  ALA   B HA   1 
ATOM   4302 H HB1  . ALA   B 1 21  ? 49.811 -28.560 -12.861 1.00 21.97 ?  21  ALA   B HB1  1 
ATOM   4303 H HB2  . ALA   B 1 21  ? 48.702 -29.450 -13.566 1.00 21.97 ?  21  ALA   B HB2  1 
ATOM   4304 H HB3  . ALA   B 1 21  ? 48.328 -28.590 -12.285 1.00 21.97 ?  21  ALA   B HB3  1 
ATOM   4305 N N    . ASP   B 1 22  ? 51.116 -29.341 -10.431 1.00 15.38 ?  22  ASP   B N    1 
ATOM   4306 C CA   . ASP   B 1 22  ? 51.721 -28.640 -9.305  1.00 14.62 ?  22  ASP   B CA   1 
ATOM   4307 C C    . ASP   B 1 22  ? 51.309 -27.173 -9.395  1.00 13.18 ?  22  ASP   B C    1 
ATOM   4308 O O    . ASP   B 1 22  ? 51.624 -26.501 -10.382 1.00 13.75 ?  22  ASP   B O    1 
ATOM   4309 C CB   . ASP   B 1 22  ? 53.239 -28.802 -9.461  1.00 16.21 ?  22  ASP   B CB   1 
ATOM   4310 C CG   . ASP   B 1 22  ? 54.063 -28.042 -8.426  1.00 17.80 ?  22  ASP   B CG   1 
ATOM   4311 O OD1  . ASP   B 1 22  ? 53.691 -26.931 -8.019  1.00 18.01 ?  22  ASP   B OD1  1 
ATOM   4312 O OD2  . ASP   B 1 22  ? 55.138 -28.555 -8.044  1.00 20.13 -1 22  ASP   B OD2  1 
ATOM   4313 H H    . ASP   B 1 22  ? 51.660 -29.441 -11.089 1.00 18.48 ?  22  ASP   B H    1 
ATOM   4314 H HA   . ASP   B 1 22  ? 51.433 -29.024 -8.459  1.00 17.56 ?  22  ASP   B HA   1 
ATOM   4315 H HB2  . ASP   B 1 22  ? 53.468 -29.738 -9.381  1.00 19.47 ?  22  ASP   B HB2  1 
ATOM   4316 H HB3  . ASP   B 1 22  ? 53.497 -28.473 -10.338 1.00 19.47 ?  22  ASP   B HB3  1 
ATOM   4317 N N    . ILE   B 1 23  ? 50.596 -26.680 -8.376  1.00 12.58 ?  23  ILE   B N    1 
ATOM   4318 C CA   . ILE   B 1 23  ? 50.007 -25.339 -8.441  1.00 12.09 ?  23  ILE   B CA   1 
ATOM   4319 C C    . ILE   B 1 23  ? 51.059 -24.246 -8.579  1.00 11.75 ?  23  ILE   B C    1 
ATOM   4320 O O    . ILE   B 1 23  ? 50.792 -23.203 -9.188  1.00 11.45 ?  23  ILE   B O    1 
ATOM   4321 C CB   . ILE   B 1 23  ? 49.063 -25.101 -7.245  1.00 12.62 ?  23  ILE   B CB   1 
ATOM   4322 C CG1  . ILE   B 1 23  ? 48.228 -23.838 -7.452  1.00 13.23 ?  23  ILE   B CG1  1 
ATOM   4323 C CG2  . ILE   B 1 23  ? 49.830 -25.040 -5.943  1.00 13.66 ?  23  ILE   B CG2  1 
ATOM   4324 C CD1  . ILE   B 1 23  ? 47.104 -23.675 -6.437  1.00 13.68 ?  23  ILE   B CD1  1 
ATOM   4325 H H    . ILE   B 1 23  ? 50.448 -27.102 -7.640  1.00 15.11 ?  23  ILE   B H    1 
ATOM   4326 H HA   . ILE   B 1 23  ? 49.462 -25.303 -9.241  1.00 14.53 ?  23  ILE   B HA   1 
ATOM   4327 H HB   . ILE   B 1 23  ? 48.454 -25.856 -7.198  1.00 15.16 ?  23  ILE   B HB   1 
ATOM   4328 H HG12 . ILE   B 1 23  ? 48.812 -23.065 -7.380  1.00 15.89 ?  23  ILE   B HG12 1 
ATOM   4329 H HG13 . ILE   B 1 23  ? 47.833 -23.866 -8.340  1.00 15.89 ?  23  ILE   B HG13 1 
ATOM   4330 H HG21 . ILE   B 1 23  ? 49.203 -25.060 -5.207  1.00 16.40 ?  23  ILE   B HG21 1 
ATOM   4331 H HG22 . ILE   B 1 23  ? 50.426 -25.806 -5.891  1.00 16.40 ?  23  ILE   B HG22 1 
ATOM   4332 H HG23 . ILE   B 1 23  ? 50.348 -24.220 -5.920  1.00 16.40 ?  23  ILE   B HG23 1 
ATOM   4333 H HD11 . ILE   B 1 23  ? 46.574 -22.902 -6.677  1.00 16.43 ?  23  ILE   B HD11 1 
ATOM   4334 H HD12 . ILE   B 1 23  ? 46.552 -24.475 -6.454  1.00 16.43 ?  23  ILE   B HD12 1 
ATOM   4335 H HD13 . ILE   B 1 23  ? 47.489 -23.558 -5.557  1.00 16.43 ?  23  ILE   B HD13 1 
ATOM   4336 N N    . VAL   B 1 24  ? 52.257 -24.450 -8.022  1.00 12.12 ?  24  VAL   B N    1 
ATOM   4337 C CA   . VAL   B 1 24  ? 53.329 -23.470 -8.194  1.00 12.84 ?  24  VAL   B CA   1 
ATOM   4338 C C    . VAL   B 1 24  ? 53.775 -23.423 -9.649  1.00 13.18 ?  24  VAL   B C    1 
ATOM   4339 O O    . VAL   B 1 24  ? 53.921 -22.344 -10.240 1.00 13.57 ?  24  VAL   B O    1 
ATOM   4340 C CB   . VAL   B 1 24  ? 54.508 -23.789 -7.253  1.00 13.83 ?  24  VAL   B CB   1 
ATOM   4341 C CG1  . VAL   B 1 24  ? 55.721 -22.908 -7.589  1.00 14.92 ?  24  VAL   B CG1  1 
ATOM   4342 C CG2  . VAL   B 1 24  ? 54.103 -23.599 -5.804  1.00 14.87 ?  24  VAL   B CG2  1 
ATOM   4343 H H    . VAL   B 1 24  ? 52.472 -25.136 -7.545  1.00 14.56 ?  24  VAL   B H    1 
ATOM   4344 H HA   . VAL   B 1 24  ? 52.997 -22.596 -7.953  1.00 15.42 ?  24  VAL   B HA   1 
ATOM   4345 H HB   . VAL   B 1 24  ? 54.772 -24.720 -7.367  1.00 16.61 ?  24  VAL   B HB   1 
ATOM   4346 H HG11 . VAL   B 1 24  ? 56.316 -22.885 -6.823  1.00 17.93 ?  24  VAL   B HG11 1 
ATOM   4347 H HG12 . VAL   B 1 24  ? 56.183 -23.288 -8.352  1.00 17.93 ?  24  VAL   B HG12 1 
ATOM   4348 H HG13 . VAL   B 1 24  ? 55.411 -22.014 -7.794  1.00 17.93 ?  24  VAL   B HG13 1 
ATOM   4349 H HG21 . VAL   B 1 24  ? 54.838 -23.864 -5.229  1.00 17.86 ?  24  VAL   B HG21 1 
ATOM   4350 H HG22 . VAL   B 1 24  ? 53.889 -22.665 -5.659  1.00 17.86 ?  24  VAL   B HG22 1 
ATOM   4351 H HG23 . VAL   B 1 24  ? 53.325 -24.150 -5.618  1.00 17.86 ?  24  VAL   B HG23 1 
ATOM   4352 N N    . GLU   B 1 25  ? 54.041 -24.592 -10.239 1.00 13.70 ?  25  GLU   B N    1 
ATOM   4353 C CA   . GLU   B 1 25  ? 54.435 -24.624 -11.642 1.00 15.18 ?  25  GLU   B CA   1 
ATOM   4354 C C    . GLU   B 1 25  ? 53.328 -24.079 -12.531 1.00 14.16 ?  25  GLU   B C    1 
ATOM   4355 O O    . GLU   B 1 25  ? 53.597 -23.361 -13.503 1.00 15.11 ?  25  GLU   B O    1 
ATOM   4356 C CB   . GLU   B 1 25  ? 54.821 -26.045 -12.041 1.00 19.01 ?  25  GLU   B CB   1 
ATOM   4357 C CG   . GLU   B 1 25  ? 56.108 -26.503 -11.376 1.00 24.28 ?  25  GLU   B CG   1 
ATOM   4358 C CD   . GLU   B 1 25  ? 57.231 -25.478 -11.474 1.00 29.29 ?  25  GLU   B CD   1 
ATOM   4359 O OE1  . GLU   B 1 25  ? 57.626 -25.123 -12.606 1.00 31.60 ?  25  GLU   B OE1  1 
ATOM   4360 O OE2  . GLU   B 1 25  ? 57.707 -25.005 -10.415 1.00 31.44 -1 25  GLU   B OE2  1 
ATOM   4361 H H    . GLU   B 1 25  ? 53.998 -25.362 -9.855  1.00 16.46 ?  25  GLU   B H    1 
ATOM   4362 H HA   . GLU   B 1 25  ? 55.196 -24.042 -11.765 1.00 18.23 ?  25  GLU   B HA   1 
ATOM   4363 H HB2  . GLU   B 1 25  ? 54.113 -26.655 -11.774 1.00 22.83 ?  25  GLU   B HB2  1 
ATOM   4364 H HB3  . GLU   B 1 25  ? 54.945 -26.083 -13.002 1.00 22.83 ?  25  GLU   B HB3  1 
ATOM   4365 H HG2  . GLU   B 1 25  ? 55.945 -26.642 -10.436 1.00 29.15 ?  25  GLU   B HG2  1 
ATOM   4366 H HG3  . GLU   B 1 25  ? 56.401 -27.326 -11.797 1.00 29.15 ?  25  GLU   B HG3  1 
ATOM   4367 N N    . GLU   B 1 26  ? 52.075 -24.397 -12.200 1.00 13.54 ?  26  GLU   B N    1 
ATOM   4368 C CA   . GLU   B 1 26  ? 50.944 -23.859 -12.949 1.00 13.86 ?  26  GLU   B CA   1 
ATOM   4369 C C    . GLU   B 1 26  ? 50.907 -22.341 -12.870 1.00 13.03 ?  26  GLU   B C    1 
ATOM   4370 O O    . GLU   B 1 26  ? 50.704 -21.662 -13.881 1.00 14.33 ?  26  GLU   B O    1 
ATOM   4371 C CB   . GLU   B 1 26  ? 49.632 -24.435 -12.415 1.00 15.83 ?  26  GLU   B CB   1 
ATOM   4372 C CG   . GLU   B 1 26  ? 49.190 -25.731 -13.056 1.00 19.58 ?  26  GLU   B CG   1 
ATOM   4373 C CD   . GLU   B 1 26  ? 48.978 -25.622 -14.560 1.00 21.22 ?  26  GLU   B CD   1 
ATOM   4374 O OE1  . GLU   B 1 26  ? 48.037 -24.933 -15.015 1.00 21.55 ?  26  GLU   B OE1  1 
ATOM   4375 O OE2  . GLU   B 1 26  ? 49.760 -26.253 -15.285 1.00 22.84 -1 26  GLU   B OE2  1 
ATOM   4376 H H    . GLU   B 1 26  ? 51.852 -24.933 -11.555 1.00 16.26 ?  26  GLU   B H    1 
ATOM   4377 H HA   . GLU   B 1 26  ? 51.031 -24.114 -13.878 1.00 16.65 ?  26  GLU   B HA   1 
ATOM   4378 H HB2  . GLU   B 1 26  ? 49.725 -24.602 -11.462 1.00 19.01 ?  26  GLU   B HB2  1 
ATOM   4379 H HB3  . GLU   B 1 26  ? 48.925 -23.784 -12.559 1.00 19.01 ?  26  GLU   B HB3  1 
ATOM   4380 H HG2  . GLU   B 1 26  ? 49.874 -26.394 -12.904 1.00 23.51 ?  26  GLU   B HG2  1 
ATOM   4381 H HG3  . GLU   B 1 26  ? 48.352 -26.011 -12.657 1.00 23.51 ?  26  GLU   B HG3  1 
ATOM   4382 N N    . ALA   B 1 27  ? 51.062 -21.790 -11.665 1.00 12.54 ?  27  ALA   B N    1 
ATOM   4383 C CA   . ALA   B 1 27  ? 51.020 -20.339 -11.521 1.00 12.69 ?  27  ALA   B CA   1 
ATOM   4384 C C    . ALA   B 1 27  ? 52.095 -19.676 -12.370 1.00 13.57 ?  27  ALA   B C    1 
ATOM   4385 O O    . ALA   B 1 27  ? 51.838 -18.668 -13.045 1.00 14.49 ?  27  ALA   B O    1 
ATOM   4386 C CB   . ALA   B 1 27  ? 51.156 -19.953 -10.049 1.00 12.75 ?  27  ALA   B CB   1 
ATOM   4387 H H    . ALA   B 1 27  ? 51.181 -22.227 -10.930 1.00 15.06 ?  27  ALA   B H    1 
ATOM   4388 H HA   . ALA   B 1 27  ? 50.160 -20.021 -11.830 1.00 15.24 ?  27  ALA   B HA   1 
ATOM   4389 H HB1  . ALA   B 1 27  ? 51.116 -18.986 -9.973  1.00 15.32 ?  27  ALA   B HB1  1 
ATOM   4390 H HB2  . ALA   B 1 27  ? 50.421 -20.350 -9.550  1.00 15.32 ?  27  ALA   B HB2  1 
ATOM   4391 H HB3  . ALA   B 1 27  ? 52.000 -20.280 -9.710  1.00 15.32 ?  27  ALA   B HB3  1 
ATOM   4392 N N    . LYS   B 1 28  ? 53.306 -20.229 -12.360 1.00 14.75 ?  28  LYS   B N    1 
ATOM   4393 C CA   . LYS   B 1 28  ? 54.384 -19.622 -13.132 1.00 16.92 ?  28  LYS   B CA   1 
ATOM   4394 C C    . LYS   B 1 28  ? 54.124 -19.701 -14.632 1.00 17.86 ?  28  LYS   B C    1 
ATOM   4395 O O    . LYS   B 1 28  ? 54.540 -18.806 -15.376 1.00 19.13 ?  28  LYS   B O    1 
ATOM   4396 C CB   . LYS   B 1 28  ? 55.736 -20.236 -12.746 1.00 19.75 ?  28  LYS   B CB   1 
ATOM   4397 C CG   . LYS   B 1 28  ? 56.136 -19.921 -11.307 1.00 22.73 ?  28  LYS   B CG   1 
ATOM   4398 C CD   . LYS   B 1 28  ? 57.557 -20.351 -10.968 1.00 27.43 ?  28  LYS   B CD   1 
ATOM   4399 C CE   . LYS   B 1 28  ? 57.649 -21.836 -10.710 1.00 31.06 ?  28  LYS   B CE   1 
ATOM   4400 N NZ   . LYS   B 1 28  ? 59.008 -22.214 -10.227 1.00 32.28 ?  28  LYS   B NZ   1 
ATOM   4401 H H    . LYS   B 1 28  ? 53.529 -20.932 -11.918 1.00 17.72 ?  28  LYS   B H    1 
ATOM   4402 H HA   . LYS   B 1 28  ? 54.428 -18.682 -12.905 1.00 20.32 ?  28  LYS   B HA   1 
ATOM   4403 H HB2  . LYS   B 1 28  ? 55.688 -21.199 -12.837 1.00 23.72 ?  28  LYS   B HB2  1 
ATOM   4404 H HB3  . LYS   B 1 28  ? 56.425 -19.880 -13.329 1.00 23.72 ?  28  LYS   B HB3  1 
ATOM   4405 H HG2  . LYS   B 1 28  ? 56.068 -18.963 -11.169 1.00 27.30 ?  28  LYS   B HG2  1 
ATOM   4406 H HG3  . LYS   B 1 28  ? 55.529 -20.385 -10.709 1.00 27.30 ?  28  LYS   B HG3  1 
ATOM   4407 H HD2  . LYS   B 1 28  ? 58.140 -20.133 -11.711 1.00 32.93 ?  28  LYS   B HD2  1 
ATOM   4408 H HD3  . LYS   B 1 28  ? 57.843 -19.883 -10.168 1.00 32.93 ?  28  LYS   B HD3  1 
ATOM   4409 H HE2  . LYS   B 1 28  ? 57.003 -22.085 -10.030 1.00 37.29 ?  28  LYS   B HE2  1 
ATOM   4410 H HE3  . LYS   B 1 28  ? 57.474 -22.318 -11.533 1.00 37.29 ?  28  LYS   B HE3  1 
ATOM   4411 H HZ1  . LYS   B 1 28  ? 59.046 -23.091 -10.079 1.00 38.76 ?  28  LYS   B HZ1  1 
ATOM   4412 H HZ2  . LYS   B 1 28  ? 59.619 -21.996 -10.836 1.00 38.76 ?  28  LYS   B HZ2  1 
ATOM   4413 H HZ3  . LYS   B 1 28  ? 59.191 -21.785 -9.468  1.00 38.76 ?  28  LYS   B HZ3  1 
ATOM   4414 N N    . LYS   B 1 29  ? 53.415 -20.735 -15.093 1.00 19.06 ?  29  LYS   B N    1 
ATOM   4415 C CA   . LYS   B 1 29  ? 53.129 -20.867 -16.519 1.00 21.84 ?  29  LYS   B CA   1 
ATOM   4416 C C    . LYS   B 1 29  ? 51.897 -20.069 -16.939 1.00 20.68 ?  29  LYS   B C    1 
ATOM   4417 O O    . LYS   B 1 29  ? 51.913 -19.409 -17.985 1.00 22.00 ?  29  LYS   B O    1 
ATOM   4418 C CB   . LYS   B 1 29  ? 52.947 -22.340 -16.879 1.00 26.26 ?  29  LYS   B CB   1 
ATOM   4419 C CG   . LYS   B 1 29  ? 52.896 -22.609 -18.376 1.00 30.37 ?  29  LYS   B CG   1 
ATOM   4420 C CD   . LYS   B 1 29  ? 53.125 -24.082 -18.689 1.00 33.71 ?  29  LYS   B CD   1 
ATOM   4421 C CE   . LYS   B 1 29  ? 51.989 -24.951 -18.175 1.00 35.97 ?  29  LYS   B CE   1 
ATOM   4422 N NZ   . LYS   B 1 29  ? 52.225 -26.396 -18.461 1.00 37.08 ?  29  LYS   B NZ   1 
ATOM   4423 H H    . LYS   B 1 29  ? 53.093 -21.364 -14.602 1.00 22.89 ?  29  LYS   B H    1 
ATOM   4424 H HA   . LYS   B 1 29  ? 53.881 -20.526 -17.019 1.00 26.23 ?  29  LYS   B HA   1 
ATOM   4425 H HB2  . LYS   B 1 29  ? 53.691 -22.842 -16.512 1.00 31.53 ?  29  LYS   B HB2  1 
ATOM   4426 H HB3  . LYS   B 1 29  ? 52.115 -22.656 -16.492 1.00 31.53 ?  29  LYS   B HB3  1 
ATOM   4427 H HG2  . LYS   B 1 29  ? 52.023 -22.358 -18.717 1.00 36.46 ?  29  LYS   B HG2  1 
ATOM   4428 H HG3  . LYS   B 1 29  ? 53.589 -22.092 -18.818 1.00 36.46 ?  29  LYS   B HG3  1 
ATOM   4429 H HD2  . LYS   B 1 29  ? 53.187 -24.199 -19.650 1.00 40.46 ?  29  LYS   B HD2  1 
ATOM   4430 H HD3  . LYS   B 1 29  ? 53.947 -24.375 -18.263 1.00 40.46 ?  29  LYS   B HD3  1 
ATOM   4431 H HE2  . LYS   B 1 29  ? 51.909 -24.843 -17.214 1.00 43.18 ?  29  LYS   B HE2  1 
ATOM   4432 H HE3  . LYS   B 1 29  ? 51.163 -24.687 -18.611 1.00 43.18 ?  29  LYS   B HE3  1 
ATOM   4433 H HZ1  . LYS   B 1 29  ? 51.547 -26.883 -18.151 1.00 44.52 ?  29  LYS   B HZ1  1 
ATOM   4434 H HZ2  . LYS   B 1 29  ? 52.296 -26.526 -19.339 1.00 44.52 ?  29  LYS   B HZ2  1 
ATOM   4435 H HZ3  . LYS   B 1 29  ? 52.977 -26.665 -18.068 1.00 44.52 ?  29  LYS   B HZ3  1 
ATOM   4436 N N    . VAL   B 1 30  ? 50.823 -20.132 -16.141 1.00 19.00 ?  30  VAL   B N    1 
ATOM   4437 C CA   . VAL   B 1 30  ? 49.532 -19.535 -16.500 1.00 19.07 ?  30  VAL   B CA   1 
ATOM   4438 C C    . VAL   B 1 30  ? 49.540 -18.021 -16.334 1.00 18.34 ?  30  VAL   B C    1 
ATOM   4439 O O    . VAL   B 1 30  ? 48.808 -17.305 -17.032 1.00 19.53 ?  30  VAL   B O    1 
ATOM   4440 C CB   . VAL   B 1 30  ? 48.430 -20.158 -15.621 1.00 19.55 ?  30  VAL   B CB   1 
ATOM   4441 C CG1  . VAL   B 1 30  ? 47.140 -19.349 -15.690 1.00 19.53 ?  30  VAL   B CG1  1 
ATOM   4442 C CG2  . VAL   B 1 30  ? 48.182 -21.604 -16.017 1.00 20.78 ?  30  VAL   B CG2  1 
ATOM   4443 H H    . VAL   B 1 30  ? 50.811 -20.541 -15.373 1.00 22.82 ?  30  VAL   B H    1 
ATOM   4444 H HA   . VAL   B 1 30  ? 49.329 -19.758 -17.424 1.00 22.90 ?  30  VAL   B HA   1 
ATOM   4445 H HB   . VAL   B 1 30  ? 48.723 -20.159 -14.696 1.00 23.47 ?  30  VAL   B HB   1 
ATOM   4446 H HG11 . VAL   B 1 30  ? 46.397 -19.929 -15.448 1.00 23.45 ?  30  VAL   B HG11 1 
ATOM   4447 H HG12 . VAL   B 1 30  ? 47.190 -18.610 -15.067 1.00 23.45 ?  30  VAL   B HG12 1 
ATOM   4448 H HG13 . VAL   B 1 30  ? 47.012 -19.028 -16.592 1.00 23.45 ?  30  VAL   B HG13 1 
ATOM   4449 H HG21 . VAL   B 1 30  ? 47.495 -21.979 -15.441 1.00 24.95 ?  30  VAL   B HG21 1 
ATOM   4450 H HG22 . VAL   B 1 30  ? 47.885 -21.630 -16.941 1.00 24.95 ?  30  VAL   B HG22 1 
ATOM   4451 H HG23 . VAL   B 1 30  ? 49.005 -22.103 -15.918 1.00 24.95 ?  30  VAL   B HG23 1 
ATOM   4452 N N    . LYS   B 1 31  ? 50.313 -17.528 -15.386 1.00 18.32 ?  31  LYS   B N    1 
ATOM   4453 C CA   . LYS   B 1 31  ? 50.335 -16.119 -15.019 1.00 18.98 ?  31  LYS   B CA   1 
ATOM   4454 C C    . LYS   B 1 31  ? 48.932 -15.649 -14.644 1.00 16.35 ?  31  LYS   B C    1 
ATOM   4455 O O    . LYS   B 1 31  ? 48.393 -14.722 -15.265 1.00 17.60 ?  31  LYS   B O    1 
ATOM   4456 C CB   . LYS   B 1 31  ? 50.981 -15.297 -16.139 1.00 22.42 ?  31  LYS   B CB   1 
ATOM   4457 C CG   . LYS   B 1 31  ? 52.392 -15.785 -16.489 1.00 25.77 ?  31  LYS   B CG   1 
ATOM   4458 C CD   . LYS   B 1 31  ? 52.970 -15.045 -17.684 1.00 29.57 ?  31  LYS   B CD   1 
ATOM   4459 C CE   . LYS   B 1 31  ? 54.451 -15.331 -17.847 1.00 32.20 ?  31  LYS   B CE   1 
ATOM   4460 N NZ   . LYS   B 1 31  ? 55.188 -14.978 -16.606 1.00 33.22 ?  31  LYS   B NZ   1 
ATOM   4461 H H    . LYS   B 1 31  ? 50.851 -18.021 -14.933 1.00 22.00 ?  31  LYS   B H    1 
ATOM   4462 H HA   . LYS   B 1 31  ? 50.881 -16.041 -14.236 1.00 22.79 ?  31  LYS   B HA   1 
ATOM   4463 H HB2  . LYS   B 1 31  ? 50.437 -15.357 -16.940 1.00 26.92 ?  31  LYS   B HB2  1 
ATOM   4464 H HB3  . LYS   B 1 31  ? 51.046 -14.378 -15.845 1.00 26.92 ?  31  LYS   B HB3  1 
ATOM   4465 H HG2  . LYS   B 1 31  ? 52.965 -15.644 -15.720 1.00 30.94 ?  31  LYS   B HG2  1 
ATOM   4466 H HG3  . LYS   B 1 31  ? 52.355 -16.733 -16.704 1.00 30.94 ?  31  LYS   B HG3  1 
ATOM   4467 H HD2  . LYS   B 1 31  ? 52.509 -15.337 -18.486 1.00 35.50 ?  31  LYS   B HD2  1 
ATOM   4468 H HD3  . LYS   B 1 31  ? 52.851 -14.094 -17.551 1.00 35.50 ?  31  LYS   B HD3  1 
ATOM   4469 H HE2  . LYS   B 1 31  ? 54.585 -16.276 -18.025 1.00 38.66 ?  31  LYS   B HE2  1 
ATOM   4470 H HE3  . LYS   B 1 31  ? 54.805 -14.797 -18.577 1.00 38.66 ?  31  LYS   B HE3  1 
ATOM   4471 H HZ1  . LYS   B 1 31  ? 56.063 -14.965 -16.764 1.00 39.88 ?  31  LYS   B HZ1  1 
ATOM   4472 H HZ2  . LYS   B 1 31  ? 54.933 -14.174 -16.322 1.00 39.88 ?  31  LYS   B HZ2  1 
ATOM   4473 H HZ3  . LYS   B 1 31  ? 55.017 -15.576 -15.970 1.00 39.88 ?  31  LYS   B HZ3  1 
ATOM   4474 N N    . PRO   B 1 32  ? 48.318 -16.255 -13.620 1.00 13.68 ?  32  PRO   B N    1 
ATOM   4475 C CA   . PRO   B 1 32  ? 46.936 -15.905 -13.272 1.00 12.71 ?  32  PRO   B CA   1 
ATOM   4476 C C    . PRO   B 1 32  ? 46.840 -14.555 -12.574 1.00 12.73 ?  32  PRO   B C    1 
ATOM   4477 O O    . PRO   B 1 32  ? 47.750 -14.130 -11.859 1.00 13.75 ?  32  PRO   B O    1 
ATOM   4478 C CB   . PRO   B 1 32  ? 46.533 -17.034 -12.315 1.00 13.04 ?  32  PRO   B CB   1 
ATOM   4479 C CG   . PRO   B 1 32  ? 47.837 -17.381 -11.635 1.00 13.58 ?  32  PRO   B CG   1 
ATOM   4480 C CD   . PRO   B 1 32  ? 48.886 -17.250 -12.688 1.00 13.61 ?  32  PRO   B CD   1 
ATOM   4481 H HA   . PRO   B 1 32  ? 46.365 -15.917 -14.056 1.00 15.27 ?  32  PRO   B HA   1 
ATOM   4482 H HB2  . PRO   B 1 32  ? 45.877 -16.711 -11.674 1.00 15.66 ?  32  PRO   B HB2  1 
ATOM   4483 H HB3  . PRO   B 1 32  ? 46.185 -17.790 -12.817 1.00 15.66 ?  32  PRO   B HB3  1 
ATOM   4484 H HG2  . PRO   B 1 32  ? 48.008 -16.755 -10.911 1.00 16.32 ?  32  PRO   B HG2  1 
ATOM   4485 H HG3  . PRO   B 1 32  ? 47.807 -18.289 -11.301 1.00 16.32 ?  32  PRO   B HG3  1 
ATOM   4486 H HD2  . PRO   B 1 32  ? 49.710 -16.916 -12.300 1.00 16.34 ?  32  PRO   B HD2  1 
ATOM   4487 H HD3  . PRO   B 1 32  ? 49.017 -18.097 -13.135 1.00 16.34 ?  32  PRO   B HD3  1 
ATOM   4488 N N    . THR   B 1 33  ? 45.693 -13.899 -12.756 1.00 12.05 ?  33  THR   B N    1 
ATOM   4489 C CA   . THR   B 1 33  ? 45.388 -12.727 -11.945 1.00 12.34 ?  33  THR   B CA   1 
ATOM   4490 C C    . THR   B 1 33  ? 45.341 -13.083 -10.466 1.00 12.17 ?  33  THR   B C    1 
ATOM   4491 O O    . THR   B 1 33  ? 45.812 -12.309 -9.619  1.00 13.02 ?  33  THR   B O    1 
ATOM   4492 C CB   . THR   B 1 33  ? 44.064 -12.110 -12.400 1.00 13.16 ?  33  THR   B CB   1 
ATOM   4493 O OG1  . THR   B 1 33  ? 44.135 -11.827 -13.799 1.00 13.31 ?  33  THR   B OG1  1 
ATOM   4494 C CG2  . THR   B 1 33  ? 43.756 -10.826 -11.634 1.00 14.19 ?  33  THR   B CG2  1 
ATOM   4495 H H    . THR   B 1 33  ? 45.084 -14.109 -13.329 1.00 14.48 ?  33  THR   B H    1 
ATOM   4496 H HA   . THR   B 1 33  ? 46.079 -12.063 -12.070 1.00 14.82 ?  33  THR   B HA   1 
ATOM   4497 H HB   . THR   B 1 33  ? 43.339 -12.743 -12.241 1.00 15.80 ?  33  THR   B HB   1 
ATOM   4498 H HG1  . THR   B 1 33  ? 43.415 -11.477 -14.065 1.00 15.99 ?  33  THR   B HG1  1 
ATOM   4499 H HG21 . THR   B 1 33  ? 42.994 -10.378 -12.032 1.00 17.04 ?  33  THR   B HG21 1 
ATOM   4500 H HG22 . THR   B 1 33  ? 43.553 -11.032 -10.709 1.00 17.04 ?  33  THR   B HG22 1 
ATOM   4501 H HG23 . THR   B 1 33  ? 44.522 -10.234 -11.667 1.00 17.04 ?  33  THR   B HG23 1 
ATOM   4502 N N    . VAL   B 1 34  ? 44.795 -14.258 -10.133 1.00 11.43 ?  34  VAL   B N    1 
ATOM   4503 C CA   . VAL   B 1 34  ? 44.602 -14.655 -8.741  1.00 10.75 ?  34  VAL   B CA   1 
ATOM   4504 C C    . VAL   B 1 34  ? 45.029 -16.106 -8.572  1.00 10.24 ?  34  VAL   B C    1 
ATOM   4505 O O    . VAL   B 1 34  ? 44.505 -16.997 -9.255  1.00 10.90 ?  34  VAL   B O    1 
ATOM   4506 C CB   . VAL   B 1 34  ? 43.135 -14.512 -8.290  1.00 11.84 ?  34  VAL   B CB   1 
ATOM   4507 C CG1  . VAL   B 1 34  ? 42.973 -14.992 -6.854  1.00 12.63 ?  34  VAL   B CG1  1 
ATOM   4508 C CG2  . VAL   B 1 34  ? 42.633 -13.094 -8.464  1.00 12.94 ?  34  VAL   B CG2  1 
ATOM   4509 H H    . VAL   B 1 34  ? 44.530 -14.849 -10.705 1.00 13.74 ?  34  VAL   B H    1 
ATOM   4510 H HA   . VAL   B 1 34  ? 45.161 -14.107 -8.171  1.00 12.92 ?  34  VAL   B HA   1 
ATOM   4511 H HB   . VAL   B 1 34  ? 42.588 -15.084 -8.848  1.00 14.23 ?  34  VAL   B HB   1 
ATOM   4512 H HG11 . VAL   B 1 34  ? 42.127 -14.667 -6.507  1.00 15.17 ?  34  VAL   B HG11 1 
ATOM   4513 H HG12 . VAL   B 1 34  ? 42.979 -15.965 -6.839  1.00 15.17 ?  34  VAL   B HG12 1 
ATOM   4514 H HG13 . VAL   B 1 34  ? 43.703 -14.648 -6.318  1.00 15.17 ?  34  VAL   B HG13 1 
ATOM   4515 H HG21 . VAL   B 1 34  ? 41.718 -13.041 -8.149  1.00 15.54 ?  34  VAL   B HG21 1 
ATOM   4516 H HG22 . VAL   B 1 34  ? 43.195 -12.493 -7.951  1.00 15.54 ?  34  VAL   B HG22 1 
ATOM   4517 H HG23 . VAL   B 1 34  ? 42.672 -12.859 -9.406  1.00 15.54 ?  34  VAL   B HG23 1 
ATOM   4518 N N    . VAL   B 1 35  ? 45.945 -16.351 -7.637  1.00 9.73  ?  35  VAL   B N    1 
ATOM   4519 C CA   . VAL   B 1 35  ? 46.186 -17.693 -7.114  1.00 9.21  ?  35  VAL   B CA   1 
ATOM   4520 C C    . VAL   B 1 35  ? 45.647 -17.750 -5.692  1.00 9.10  ?  35  VAL   B C    1 
ATOM   4521 O O    . VAL   B 1 35  ? 45.864 -16.825 -4.902  1.00 9.69  ?  35  VAL   B O    1 
ATOM   4522 C CB   . VAL   B 1 35  ? 47.669 -18.119 -7.199  1.00 9.79  ?  35  VAL   B CB   1 
ATOM   4523 C CG1  . VAL   B 1 35  ? 48.580 -17.270 -6.292  1.00 10.94 ?  35  VAL   B CG1  1 
ATOM   4524 C CG2  . VAL   B 1 35  ? 47.799 -19.615 -6.874  1.00 10.37 ?  35  VAL   B CG2  1 
ATOM   4525 H H    . VAL   B 1 35  ? 46.448 -15.747 -7.282  1.00 11.69 ?  35  VAL   B H    1 
ATOM   4526 H HA   . VAL   B 1 35  ? 45.672 -18.323 -7.644  1.00 11.07 ?  35  VAL   B HA   1 
ATOM   4527 H HB   . VAL   B 1 35  ? 47.972 -18.005 -8.117  1.00 11.76 ?  35  VAL   B HB   1 
ATOM   4528 H HG11 . VAL   B 1 35  ? 49.502 -17.514 -6.460  1.00 13.14 ?  35  VAL   B HG11 1 
ATOM   4529 H HG12 . VAL   B 1 35  ? 48.434 -16.338 -6.495  1.00 13.14 ?  35  VAL   B HG12 1 
ATOM   4530 H HG13 . VAL   B 1 35  ? 48.353 -17.453 -5.366  1.00 13.14 ?  35  VAL   B HG13 1 
ATOM   4531 H HG21 . VAL   B 1 35  ? 48.719 -19.892 -6.990  1.00 12.46 ?  35  VAL   B HG21 1 
ATOM   4532 H HG22 . VAL   B 1 35  ? 47.520 -19.768 -5.955  1.00 12.46 ?  35  VAL   B HG22 1 
ATOM   4533 H HG23 . VAL   B 1 35  ? 47.225 -20.127 -7.475  1.00 12.46 ?  35  VAL   B HG23 1 
ATOM   4534 N N    . VAL   B 1 36  ? 44.926 -18.830 -5.375  1.00 9.03  ?  36  VAL   B N    1 
ATOM   4535 C CA   . VAL   B 1 36  ? 44.381 -19.037 -4.044  1.00 8.66  ?  36  VAL   B CA   1 
ATOM   4536 C C    . VAL   B 1 36  ? 45.387 -19.798 -3.192  1.00 8.65  ?  36  VAL   B C    1 
ATOM   4537 O O    . VAL   B 1 36  ? 45.928 -20.826 -3.615  1.00 9.60  ?  36  VAL   B O    1 
ATOM   4538 C CB   . VAL   B 1 36  ? 43.047 -19.800 -4.119  1.00 9.24  ?  36  VAL   B CB   1 
ATOM   4539 C CG1  . VAL   B 1 36  ? 42.555 -20.164 -2.729  1.00 9.94  ?  36  VAL   B CG1  1 
ATOM   4540 C CG2  . VAL   B 1 36  ? 42.012 -18.969 -4.864  1.00 10.08 ?  36  VAL   B CG2  1 
ATOM   4541 H H    . VAL   B 1 36  ? 44.747 -19.469 -5.927  1.00 10.86 ?  36  VAL   B H    1 
ATOM   4542 H HA   . VAL   B 1 36  ? 44.214 -18.176 -3.629  1.00 10.40 ?  36  VAL   B HA   1 
ATOM   4543 H HB   . VAL   B 1 36  ? 43.181 -20.622 -4.613  1.00 11.10 ?  36  VAL   B HB   1 
ATOM   4544 H HG11 . VAL   B 1 36  ? 41.612 -20.386 -2.778  1.00 11.94 ?  36  VAL   B HG11 1 
ATOM   4545 H HG12 . VAL   B 1 36  ? 43.058 -20.921 -2.401  1.00 11.94 ?  36  VAL   B HG12 1 
ATOM   4546 H HG13 . VAL   B 1 36  ? 42.680 -19.398 -2.142  1.00 11.94 ?  36  VAL   B HG13 1 
ATOM   4547 H HG21 . VAL   B 1 36  ? 41.173 -19.455 -4.884  1.00 12.11 ?  36  VAL   B HG21 1 
ATOM   4548 H HG22 . VAL   B 1 36  ? 41.897 -18.123 -4.407  1.00 12.11 ?  36  VAL   B HG22 1 
ATOM   4549 H HG23 . VAL   B 1 36  ? 42.326 -18.816 -5.771  1.00 12.11 ?  36  VAL   B HG23 1 
ATOM   4550 N N    . ASN   B 1 37  ? 45.610 -19.302 -1.977  1.00 9.13  ?  37  ASN   B N    1 
ATOM   4551 C CA   . ASN   B 1 37  ? 46.365 -20.022 -0.966  1.00 9.26  ?  37  ASN   B CA   1 
ATOM   4552 C C    . ASN   B 1 37  ? 45.423 -20.698 0.020   1.00 9.27  ?  37  ASN   B C    1 
ATOM   4553 O O    . ASN   B 1 37  ? 44.406 -20.121 0.426   1.00 9.88  ?  37  ASN   B O    1 
ATOM   4554 C CB   . ASN   B 1 37  ? 47.294 -19.079 -0.203  1.00 9.36  ?  37  ASN   B CB   1 
ATOM   4555 C CG   . ASN   B 1 37  ? 48.147 -19.800 0.808   1.00 9.86  ?  37  ASN   B CG   1 
ATOM   4556 O OD1  . ASN   B 1 37  ? 48.491 -20.975 0.626   1.00 10.67 ?  37  ASN   B OD1  1 
ATOM   4557 N ND2  . ASN   B 1 37  ? 48.500 -19.102 1.883   1.00 9.84  ?  37  ASN   B ND2  1 
ATOM   4558 H H    . ASN   B 1 37  ? 45.320 -18.537 -1.704  1.00 10.97 ?  37  ASN   B H    1 
ATOM   4559 H HA   . ASN   B 1 37  ? 46.901 -20.713 -1.387  1.00 11.12 ?  37  ASN   B HA   1 
ATOM   4560 H HB2  . ASN   B 1 37  ? 47.884 -18.647 -0.834  1.00 11.25 ?  37  ASN   B HB2  1 
ATOM   4561 H HB3  . ASN   B 1 37  ? 46.760 -18.422 0.268   1.00 11.25 ?  37  ASN   B HB3  1 
ATOM   4562 H HD21 . ASN   B 1 37  ? 48.992 -19.461 2.490   1.00 11.83 ?  37  ASN   B HD21 1 
ATOM   4563 H HD22 . ASN   B 1 37  ? 48.244 -18.287 1.976   1.00 11.83 ?  37  ASN   B HD22 1 
ATOM   4564 N N    . ALA   B 1 38  ? 45.779 -21.930 0.399   1.00 9.47  ?  38  ALA   B N    1 
ATOM   4565 C CA   . ALA   B 1 38  ? 45.125 -22.676 1.475   1.00 9.85  ?  38  ALA   B CA   1 
ATOM   4566 C C    . ALA   B 1 38  ? 45.708 -22.191 2.801   1.00 9.93  ?  38  ALA   B C    1 
ATOM   4567 O O    . ALA   B 1 38  ? 46.604 -22.801 3.393   1.00 10.68 ?  38  ALA   B O    1 
ATOM   4568 C CB   . ALA   B 1 38  ? 45.356 -24.168 1.280   1.00 10.84 ?  38  ALA   B CB   1 
ATOM   4569 H H    . ALA   B 1 38  ? 46.429 -22.361 0.043   1.00 11.38 ?  38  ALA   B H    1 
ATOM   4570 H HA   . ALA   B 1 38  ? 44.172 -22.501 1.470   1.00 11.83 ?  38  ALA   B HA   1 
ATOM   4571 H HB1  . ALA   B 1 38  ? 44.912 -24.656 1.998   1.00 13.02 ?  38  ALA   B HB1  1 
ATOM   4572 H HB2  . ALA   B 1 38  ? 44.979 -24.438 0.426   1.00 13.02 ?  38  ALA   B HB2  1 
ATOM   4573 H HB3  . ALA   B 1 38  ? 46.305 -24.353 1.297   1.00 13.02 ?  38  ALA   B HB3  1 
ATOM   4574 N N    . ALA   B 1 39  ? 45.186 -21.057 3.262   1.00 9.87  ?  39  ALA   B N    1 
ATOM   4575 C CA   . ALA   B 1 39  ? 45.731 -20.321 4.393   1.00 10.01 ?  39  ALA   B CA   1 
ATOM   4576 C C    . ALA   B 1 39  ? 45.106 -20.760 5.715   1.00 10.02 ?  39  ALA   B C    1 
ATOM   4577 O O    . ALA   B 1 39  ? 44.075 -21.435 5.764   1.00 11.27 ?  39  ALA   B O    1 
ATOM   4578 C CB   . ALA   B 1 39  ? 45.493 -18.823 4.191   1.00 10.84 ?  39  ALA   B CB   1 
ATOM   4579 H H    . ALA   B 1 39  ? 44.493 -20.683 2.920   1.00 11.86 ?  39  ALA   B H    1 
ATOM   4580 H HA   . ALA   B 1 39  ? 46.685 -20.475 4.447   1.00 12.02 ?  39  ALA   B HA   1 
ATOM   4581 H HB1  . ALA   B 1 39  ? 45.860 -18.340 4.948   1.00 13.02 ?  39  ALA   B HB1  1 
ATOM   4582 H HB2  . ALA   B 1 39  ? 45.939 -18.542 3.374   1.00 13.02 ?  39  ALA   B HB2  1 
ATOM   4583 H HB3  . ALA   B 1 39  ? 44.541 -18.658 4.121   1.00 13.02 ?  39  ALA   B HB3  1 
ATOM   4584 N N    . ASN   B 1 40  ? 45.751 -20.345 6.803   1.00 10.85 ?  40  ASN   B N    1 
ATOM   4585 C CA   . ASN   B 1 40  ? 45.188 -20.392 8.145   1.00 11.45 ?  40  ASN   B CA   1 
ATOM   4586 C C    . ASN   B 1 40  ? 45.009 -18.963 8.668   1.00 11.41 ?  40  ASN   B C    1 
ATOM   4587 O O    . ASN   B 1 40  ? 45.424 -17.984 8.041   1.00 11.30 ?  40  ASN   B O    1 
ATOM   4588 C CB   . ASN   B 1 40  ? 46.036 -21.266 9.087   1.00 12.15 ?  40  ASN   B CB   1 
ATOM   4589 C CG   . ASN   B 1 40  ? 47.498 -20.862 9.118   1.00 13.00 ?  40  ASN   B CG   1 
ATOM   4590 O OD1  . ASN   B 1 40  ? 47.821 -19.682 9.189   1.00 14.95 ?  40  ASN   B OD1  1 
ATOM   4591 N ND2  . ASN   B 1 40  ? 48.385 -21.841 9.079   1.00 13.44 ?  40  ASN   B ND2  1 
ATOM   4592 H H    . ASN   B 1 40  ? 46.550 -20.036 6.787   1.00 13.03 ?  40  ASN   B H    1 
ATOM   4593 H HA   . ASN   B 1 40  ? 44.304 -20.787 8.099   1.00 13.76 ?  40  ASN   B HA   1 
ATOM   4594 H HB2  . ASN   B 1 40  ? 45.680 -21.191 9.991   1.00 14.59 ?  40  ASN   B HB2  1 
ATOM   4595 H HB3  . ASN   B 1 40  ? 45.982 -22.187 8.791   1.00 14.59 ?  40  ASN   B HB3  1 
ATOM   4596 H HD21 . ASN   B 1 40  ? 49.224 -21.659 9.101   1.00 16.14 ?  40  ASN   B HD21 1 
ATOM   4597 H HD22 . ASN   B 1 40  ? 48.122 -22.659 9.037   1.00 16.14 ?  40  ASN   B HD22 1 
ATOM   4598 N N    . VAL   B 1 41  ? 44.360 -18.836 9.829   1.00 11.91 ?  41  VAL   B N    1 
ATOM   4599 C CA   . VAL   B 1 41  ? 43.902 -17.515 10.277  1.00 12.50 ?  41  VAL   B CA   1 
ATOM   4600 C C    . VAL   B 1 41  ? 45.055 -16.563 10.582  1.00 12.21 ?  41  VAL   B C    1 
ATOM   4601 O O    . VAL   B 1 41  ? 44.880 -15.341 10.506  1.00 12.50 ?  41  VAL   B O    1 
ATOM   4602 C CB   . VAL   B 1 41  ? 42.916 -17.597 11.462  1.00 13.81 ?  41  VAL   B CB   1 
ATOM   4603 C CG1  . VAL   B 1 41  ? 41.618 -18.282 11.044  1.00 14.35 ?  41  VAL   B CG1  1 
ATOM   4604 C CG2  . VAL   B 1 41  ? 43.548 -18.288 12.658  1.00 14.61 ?  41  VAL   B CG2  1 
ATOM   4605 H H    . VAL   B 1 41  ? 44.173 -19.478 10.361  1.00 14.30 ?  41  VAL   B H    1 
ATOM   4606 H HA   . VAL   B 1 41  ? 43.410 -17.112 9.547   1.00 15.01 ?  41  VAL   B HA   1 
ATOM   4607 H HB   . VAL   B 1 41  ? 42.687 -16.693 11.738  1.00 16.59 ?  41  VAL   B HB   1 
ATOM   4608 H HG11 . VAL   B 1 41  ? 41.008 -18.292 11.799  1.00 17.24 ?  41  VAL   B HG11 1 
ATOM   4609 H HG12 . VAL   B 1 41  ? 41.224 -17.791 10.307  1.00 17.24 ?  41  VAL   B HG12 1 
ATOM   4610 H HG13 . VAL   B 1 41  ? 41.818 -19.190 10.769  1.00 17.24 ?  41  VAL   B HG13 1 
ATOM   4611 H HG21 . VAL   B 1 41  ? 42.907 -18.317 13.383  1.00 17.55 ?  41  VAL   B HG21 1 
ATOM   4612 H HG22 . VAL   B 1 41  ? 43.799 -19.191 12.402  1.00 17.55 ?  41  VAL   B HG22 1 
ATOM   4613 H HG23 . VAL   B 1 41  ? 44.335 -17.792 12.930  1.00 17.55 ?  41  VAL   B HG23 1 
ATOM   4614 N N    . TYR   B 1 42  ? 46.221 -17.081 10.959  1.00 12.34 ?  42  TYR   B N    1 
ATOM   4615 C CA   . TYR   B 1 42  ? 47.379 -16.237 11.228  1.00 13.02 ?  42  TYR   B CA   1 
ATOM   4616 C C    . TYR   B 1 42  ? 48.343 -16.164 10.045  1.00 12.07 ?  42  TYR   B C    1 
ATOM   4617 O O    . TYR   B 1 42  ? 49.434 -15.597 10.177  1.00 13.56 ?  42  TYR   B O    1 
ATOM   4618 C CB   . TYR   B 1 42  ? 48.076 -16.640 12.537  1.00 15.01 ?  42  TYR   B CB   1 
ATOM   4619 C CG   . TYR   B 1 42  ? 47.460 -15.966 13.762  1.00 15.58 ?  42  TYR   B CG   1 
ATOM   4620 C CD1  . TYR   B 1 42  ? 47.666 -14.612 14.007  1.00 14.61 ?  42  TYR   B CD1  1 
ATOM   4621 C CD2  . TYR   B 1 42  ? 46.677 -16.674 14.658  1.00 17.49 ?  42  TYR   B CD2  1 
ATOM   4622 C CE1  . TYR   B 1 42  ? 47.112 -13.986 15.103  1.00 15.84 ?  42  TYR   B CE1  1 
ATOM   4623 C CE2  . TYR   B 1 42  ? 46.119 -16.056 15.765  1.00 17.64 ?  42  TYR   B CE2  1 
ATOM   4624 C CZ   . TYR   B 1 42  ? 46.335 -14.708 15.981  1.00 18.01 ?  42  TYR   B CZ   1 
ATOM   4625 O OH   . TYR   B 1 42  ? 45.792 -14.073 17.080  1.00 20.79 ?  42  TYR   B OH   1 
ATOM   4626 H H    . TYR   B 1 42  ? 46.366 -17.928 11.062  1.00 14.82 ?  42  TYR   B H    1 
ATOM   4627 H HA   . TYR   B 1 42  ? 47.051 -15.340 11.366  1.00 15.65 ?  42  TYR   B HA   1 
ATOM   4628 H HB2  . TYR   B 1 42  ? 48.008 -17.598 12.655  1.00 18.03 ?  42  TYR   B HB2  1 
ATOM   4629 H HB3  . TYR   B 1 42  ? 49.011 -16.377 12.488  1.00 18.03 ?  42  TYR   B HB3  1 
ATOM   4630 H HD1  . TYR   B 1 42  ? 48.190 -14.118 13.411  1.00 17.55 ?  42  TYR   B HD1  1 
ATOM   4631 H HD2  . TYR   B 1 42  ? 46.527 -17.581 14.509  1.00 21.01 ?  42  TYR   B HD2  1 
ATOM   4632 H HE1  . TYR   B 1 42  ? 47.262 -13.079 15.246  1.00 19.02 ?  42  TYR   B HE1  1 
ATOM   4633 H HE2  . TYR   B 1 42  ? 45.592 -16.546 16.354  1.00 21.19 ?  42  TYR   B HE2  1 
ATOM   4634 H HH   . TYR   B 1 42  ? 46.010 -13.263 17.076  1.00 24.96 ?  42  TYR   B HH   1 
ATOM   4635 N N    . LEU   B 1 43  ? 47.944 -16.678 8.886   1.00 11.17 ?  43  LEU   B N    1 
ATOM   4636 C CA   . LEU   B 1 43  ? 48.757 -16.602 7.677   1.00 11.18 ?  43  LEU   B CA   1 
ATOM   4637 C C    . LEU   B 1 43  ? 50.170 -17.114 7.930   1.00 11.30 ?  43  LEU   B C    1 
ATOM   4638 O O    . LEU   B 1 43  ? 51.153 -16.529 7.473   1.00 12.17 ?  43  LEU   B O    1 
ATOM   4639 C CB   . LEU   B 1 43  ? 48.773 -15.198 7.072   1.00 11.49 ?  43  LEU   B CB   1 
ATOM   4640 C CG   . LEU   B 1 43  ? 47.417 -14.592 6.706   1.00 11.18 ?  43  LEU   B CG   1 
ATOM   4641 C CD1  . LEU   B 1 43  ? 47.645 -13.189 6.139   1.00 12.74 ?  43  LEU   B CD1  1 
ATOM   4642 C CD2  . LEU   B 1 43  ? 46.637 -15.471 5.725   1.00 11.45 ?  43  LEU   B CD2  1 
ATOM   4643 H H    . LEU   B 1 43  ? 47.199 -17.091 8.771   1.00 13.42 ?  43  LEU   B H    1 
ATOM   4644 H HA   . LEU   B 1 43  ? 48.359 -17.188 7.013   1.00 13.43 ?  43  LEU   B HA   1 
ATOM   4645 H HB2  . LEU   B 1 43  ? 49.194 -14.599 7.707   1.00 13.80 ?  43  LEU   B HB2  1 
ATOM   4646 H HB3  . LEU   B 1 43  ? 49.301 -15.227 6.258   1.00 13.80 ?  43  LEU   B HB3  1 
ATOM   4647 H HG   . LEU   B 1 43  ? 46.885 -14.502 7.511   1.00 13.44 ?  43  LEU   B HG   1 
ATOM   4648 H HD11 . LEU   B 1 43  ? 46.787 -12.799 5.906   1.00 15.30 ?  43  LEU   B HD11 1 
ATOM   4649 H HD12 . LEU   B 1 43  ? 48.082 -12.644 6.814   1.00 15.30 ?  43  LEU   B HD12 1 
ATOM   4650 H HD13 . LEU   B 1 43  ? 48.205 -13.253 5.351   1.00 15.30 ?  43  LEU   B HD13 1 
ATOM   4651 H HD21 . LEU   B 1 43  ? 45.828 -15.007 5.457   1.00 13.76 ?  43  LEU   B HD21 1 
ATOM   4652 H HD22 . LEU   B 1 43  ? 47.190 -15.647 4.948   1.00 13.76 ?  43  LEU   B HD22 1 
ATOM   4653 H HD23 . LEU   B 1 43  ? 46.408 -16.306 6.164   1.00 13.76 ?  43  LEU   B HD23 1 
ATOM   4654 N N    . LYS   B 1 44  ? 50.270 -18.238 8.648   1.00 11.33 ?  44  LYS   B N    1 
ATOM   4655 C CA   . LYS   B 1 44  ? 51.537 -18.918 8.883   1.00 12.04 ?  44  LYS   B CA   1 
ATOM   4656 C C    . LYS   B 1 44  ? 51.656 -20.034 7.854   1.00 11.75 ?  44  LYS   B C    1 
ATOM   4657 O O    . LYS   B 1 44  ? 50.959 -21.051 7.939   1.00 12.79 ?  44  LYS   B O    1 
ATOM   4658 C CB   . LYS   B 1 44  ? 51.609 -19.436 10.320  1.00 13.97 ?  44  LYS   B CB   1 
ATOM   4659 C CG   . LYS   B 1 44  ? 51.791 -18.324 11.348  1.00 16.98 ?  44  LYS   B CG   1 
ATOM   4660 C CD   . LYS   B 1 44  ? 53.026 -17.488 10.996  1.00 19.99 ?  44  LYS   B CD   1 
ATOM   4661 C CE   . LYS   B 1 44  ? 53.390 -16.480 12.056  1.00 22.68 ?  44  LYS   B CE   1 
ATOM   4662 N NZ   . LYS   B 1 44  ? 54.639 -15.743 11.727  1.00 23.90 ?  44  LYS   B NZ   1 
ATOM   4663 H H    . LYS   B 1 44  ? 49.600 -18.626 9.018   1.00 13.62 ?  44  LYS   B H    1 
ATOM   4664 H HA   . LYS   B 1 44  ? 52.269 -18.305 8.721   1.00 14.47 ?  44  LYS   B HA   1 
ATOM   4665 H HB2  . LYS   B 1 44  ? 50.781 -19.899 10.532  1.00 16.78 ?  44  LYS   B HB2  1 
ATOM   4666 H HB3  . LYS   B 1 44  ? 52.358 -20.043 10.403  1.00 16.78 ?  44  LYS   B HB3  1 
ATOM   4667 H HG2  . LYS   B 1 44  ? 51.015 -17.747 11.350  1.00 20.39 ?  44  LYS   B HG2  1 
ATOM   4668 H HG3  . LYS   B 1 44  ? 51.927 -18.717 12.230  1.00 20.39 ?  44  LYS   B HG3  1 
ATOM   4669 H HD2  . LYS   B 1 44  ? 53.782 -18.089 10.858  1.00 24.00 ?  44  LYS   B HD2  1 
ATOM   4670 H HD3  . LYS   B 1 44  ? 52.849 -16.993 10.182  1.00 24.00 ?  44  LYS   B HD3  1 
ATOM   4671 H HE2  . LYS   B 1 44  ? 52.674 -15.834 12.127  1.00 27.23 ?  44  LYS   B HE2  1 
ATOM   4672 H HE3  . LYS   B 1 44  ? 53.523 -16.939 12.896  1.00 27.23 ?  44  LYS   B HE3  1 
ATOM   4673 H HZ1  . LYS   B 1 44  ? 54.823 -15.154 12.368  1.00 28.69 ?  44  LYS   B HZ1  1 
ATOM   4674 H HZ2  . LYS   B 1 44  ? 55.321 -16.310 11.652  1.00 28.69 ?  44  LYS   B HZ2  1 
ATOM   4675 H HZ3  . LYS   B 1 44  ? 54.544 -15.306 10.955  1.00 28.69 ?  44  LYS   B HZ3  1 
ATOM   4676 N N    . HIS   B 1 45  ? 52.512 -19.813 6.857   1.00 11.52 ?  45  HIS   B N    1 
ATOM   4677 C CA   . HIS   B 1 45  ? 52.544 -20.647 5.657   1.00 11.45 ?  45  HIS   B CA   1 
ATOM   4678 C C    . HIS   B 1 45  ? 53.568 -21.767 5.820   1.00 13.40 ?  45  HIS   B C    1 
ATOM   4679 O O    . HIS   B 1 45  ? 54.630 -21.785 5.204   1.00 15.83 ?  45  HIS   B O    1 
ATOM   4680 C CB   . HIS   B 1 45  ? 52.851 -19.791 4.441   1.00 11.45 ?  45  HIS   B CB   1 
ATOM   4681 C CG   . HIS   B 1 45  ? 51.974 -18.587 4.329   1.00 11.20 ?  45  HIS   B CG   1 
ATOM   4682 N ND1  . HIS   B 1 45  ? 50.595 -18.662 4.281   1.00 11.43 ?  45  HIS   B ND1  1 
ATOM   4683 C CD2  . HIS   B 1 45  ? 52.292 -17.272 4.269   1.00 11.76 ?  45  HIS   B CD2  1 
ATOM   4684 C CE1  . HIS   B 1 45  ? 50.108 -17.437 4.183   1.00 11.14 ?  45  HIS   B CE1  1 
ATOM   4685 N NE2  . HIS   B 1 45  ? 51.114 -16.578 4.166   1.00 11.64 ?  45  HIS   B NE2  1 
ATOM   4686 H H    . HIS   B 1 45  ? 53.079 -19.166 6.846   1.00 13.84 ?  45  HIS   B H    1 
ATOM   4687 H HA   . HIS   B 1 45  ? 51.665 -21.047 5.528   1.00 13.76 ?  45  HIS   B HA   1 
ATOM   4688 H HB2  . HIS   B 1 45  ? 53.769 -19.487 4.493   1.00 13.75 ?  45  HIS   B HB2  1 
ATOM   4689 H HB3  . HIS   B 1 45  ? 52.726 -20.328 3.640   1.00 13.75 ?  45  HIS   B HB3  1 
ATOM   4690 H HD2  . HIS   B 1 45  ? 53.148 -16.907 4.290   1.00 14.13 ?  45  HIS   B HD2  1 
ATOM   4691 H HE1  . HIS   B 1 45  ? 49.207 -17.220 4.121   1.00 13.39 ?  45  HIS   B HE1  1 
ATOM   4692 H HE2  . HIS   B 1 45  ? 51.037 -15.723 4.123   1.00 13.98 ?  45  HIS   B HE2  1 
ATOM   4693 N N    A GLY   B 1 46  ? 53.204 -22.738 6.653   0.62 14.68 ?  46  GLY   B N    1 
ATOM   4694 N N    B GLY   B 1 46  ? 53.216 -22.723 6.671   0.38 14.58 ?  46  GLY   B N    1 
ATOM   4695 C CA   A GLY   B 1 46  ? 54.125 -23.795 7.035   0.62 16.34 ?  46  GLY   B CA   1 
ATOM   4696 C CA   B GLY   B 1 46  ? 54.136 -23.791 7.002   0.38 15.88 ?  46  GLY   B CA   1 
ATOM   4697 C C    A GLY   B 1 46  ? 54.183 -25.016 6.138   0.62 17.96 ?  46  GLY   B C    1 
ATOM   4698 C C    B GLY   B 1 46  ? 54.163 -24.925 5.997   0.38 17.12 ?  46  GLY   B C    1 
ATOM   4699 O O    A GLY   B 1 46  ? 55.269 -25.461 5.750   0.62 20.68 ?  46  GLY   B O    1 
ATOM   4700 O O    B GLY   B 1 46  ? 55.189 -25.183 5.360   0.38 18.05 ?  46  GLY   B O    1 
ATOM   4701 H H    A GLY   B 1 46  ? 52.427 -22.788 7.028   0.62 17.63 ?  46  GLY   B H    1 
ATOM   4702 H H    B GLY   B 1 46  ? 52.452 -22.765 7.073   0.38 17.51 ?  46  GLY   B H    1 
ATOM   4703 H HA2  A GLY   B 1 46  ? 55.016 -23.419 7.087   0.62 19.63 ?  46  GLY   B HA2  1 
ATOM   4704 H HA2  B GLY   B 1 46  ? 55.031 -23.423 7.066   0.38 19.07 ?  46  GLY   B HA2  1 
ATOM   4705 H HA3  A GLY   B 1 46  ? 53.881 -24.109 7.918   0.62 19.63 ?  46  GLY   B HA3  1 
ATOM   4706 H HA3  B GLY   B 1 46  ? 53.897 -24.151 7.870   0.38 19.07 ?  46  GLY   B HA3  1 
ATOM   4707 N N    . GLY   B 1 47  ? 53.027 -25.599 5.825   1.00 17.26 ?  47  GLY   B N    1 
ATOM   4708 C CA   . GLY   B 1 47  ? 52.974 -26.861 5.118   1.00 15.27 ?  47  GLY   B CA   1 
ATOM   4709 C C    . GLY   B 1 47  ? 52.042 -26.845 3.922   1.00 13.22 ?  47  GLY   B C    1 
ATOM   4710 O O    . GLY   B 1 47  ? 51.383 -25.847 3.632   1.00 13.10 ?  47  GLY   B O    1 
ATOM   4711 H H    A GLY   B 1 47  ? 52.252 -25.292 6.046   0.62 20.73 ?  47  GLY   B H    1 
ATOM   4712 H H    B GLY   B 1 47  ? 52.259 -25.334 6.117   0.38 20.73 ?  47  GLY   B H    1 
ATOM   4713 H HA2  . GLY   B 1 47  ? 53.861 -27.098 4.805   1.00 18.34 ?  47  GLY   B HA2  1 
ATOM   4714 H HA3  . GLY   B 1 47  ? 52.676 -27.555 5.728   1.00 18.34 ?  47  GLY   B HA3  1 
ATOM   4715 N N    . GLY   B 1 48  ? 52.000 -27.985 3.233   1.00 12.38 ?  48  GLY   B N    1 
ATOM   4716 C CA   . GLY   B 1 48  ? 51.079 -28.144 2.123   1.00 12.08 ?  48  GLY   B CA   1 
ATOM   4717 C C    . GLY   B 1 48  ? 51.209 -27.034 1.105   1.00 11.15 ?  48  GLY   B C    1 
ATOM   4718 O O    . GLY   B 1 48  ? 52.307 -26.561 0.798   1.00 11.71 ?  48  GLY   B O    1 
ATOM   4719 H H    . GLY   B 1 48  ? 52.496 -28.665 3.388   1.00 14.87 ?  48  GLY   B H    1 
ATOM   4720 H HA2  . GLY   B 1 48  ? 51.253 -28.991 1.682   1.00 14.51 ?  48  GLY   B HA2  1 
ATOM   4721 H HA3  . GLY   B 1 48  ? 50.169 -28.151 2.455   1.00 14.51 ?  48  GLY   B HA3  1 
ATOM   4722 N N    . VAL   B 1 49  ? 50.061 -26.604 0.576   1.00 11.11 ?  49  VAL   B N    1 
ATOM   4723 C CA   . VAL   B 1 49  ? 50.031 -25.574 -0.459  1.00 11.19 ?  49  VAL   B CA   1 
ATOM   4724 C C    . VAL   B 1 49  ? 50.694 -24.288 0.025   1.00 10.21 ?  49  VAL   B C    1 
ATOM   4725 O O    . VAL   B 1 49  ? 51.485 -23.670 -0.699  1.00 11.17 ?  49  VAL   B O    1 
ATOM   4726 C CB   . VAL   B 1 49  ? 48.580 -25.319 -0.911  1.00 12.39 ?  49  VAL   B CB   1 
ATOM   4727 C CG1  . VAL   B 1 49  ? 48.497 -24.079 -1.795  1.00 12.38 ?  49  VAL   B CG1  1 
ATOM   4728 C CG2  . VAL   B 1 49  ? 48.012 -26.537 -1.641  1.00 13.65 ?  49  VAL   B CG2  1 
ATOM   4729 H H    . VAL   B 1 49  ? 49.281 -26.892 0.805   1.00 13.34 ?  49  VAL   B H    1 
ATOM   4730 H HA   . VAL   B 1 49  ? 50.525 -25.892 -1.230  1.00 13.45 ?  49  VAL   B HA   1 
ATOM   4731 H HB   . VAL   B 1 49  ? 48.029 -25.159 -0.129  1.00 14.88 ?  49  VAL   B HB   1 
ATOM   4732 H HG11 . VAL   B 1 49  ? 47.658 -24.093 -2.282  1.00 14.88 ?  49  VAL   B HG11 1 
ATOM   4733 H HG12 . VAL   B 1 49  ? 48.535 -23.284 -1.235  1.00 14.88 ?  49  VAL   B HG12 1 
ATOM   4734 H HG13 . VAL   B 1 49  ? 49.239 -24.082 -2.417  1.00 14.88 ?  49  VAL   B HG13 1 
ATOM   4735 H HG21 . VAL   B 1 49  ? 47.098 -26.347 -1.912  1.00 16.40 ?  49  VAL   B HG21 1 
ATOM   4736 H HG22 . VAL   B 1 49  ? 48.555 -26.716 -2.426  1.00 16.40 ?  49  VAL   B HG22 1 
ATOM   4737 H HG23 . VAL   B 1 49  ? 48.029 -27.299 -1.045  1.00 16.40 ?  49  VAL   B HG23 1 
ATOM   4738 N N    . ALA   B 1 50  ? 50.353 -23.840 1.233   1.00 10.22 ?  50  ALA   B N    1 
ATOM   4739 C CA   . ALA   B 1 50  ? 50.871 -22.559 1.701   1.00 10.27 ?  50  ALA   B CA   1 
ATOM   4740 C C    . ALA   B 1 50  ? 52.391 -22.587 1.809   1.00 10.41 ?  50  ALA   B C    1 
ATOM   4741 O O    . ALA   B 1 50  ? 53.071 -21.620 1.440   1.00 10.47 ?  50  ALA   B O    1 
ATOM   4742 C CB   . ALA   B 1 50  ? 50.236 -22.193 3.038   1.00 10.80 ?  50  ALA   B CB   1 
ATOM   4743 H H    . ALA   B 1 50  ? 49.836 -24.246 1.787   1.00 12.28 ?  50  ALA   B H    1 
ATOM   4744 H HA   . ALA   B 1 50  ? 50.637 -21.871 1.062   1.00 12.34 ?  50  ALA   B HA   1 
ATOM   4745 H HB1  . ALA   B 1 50  ? 50.591 -21.336 3.333   1.00 12.97 ?  50  ALA   B HB1  1 
ATOM   4746 H HB2  . ALA   B 1 50  ? 49.274 -22.124 2.923   1.00 12.97 ?  50  ALA   B HB2  1 
ATOM   4747 H HB3  . ALA   B 1 50  ? 50.444 -22.878 3.689   1.00 12.97 ?  50  ALA   B HB3  1 
ATOM   4748 N N    . GLY   B 1 51  ? 52.943 -23.677 2.332   1.00 10.87 ?  51  GLY   B N    1 
ATOM   4749 C CA   . GLY   B 1 51  ? 54.389 -23.780 2.406   1.00 11.38 ?  51  GLY   B CA   1 
ATOM   4750 C C    . GLY   B 1 51  ? 55.038 -23.728 1.040   1.00 11.38 ?  51  GLY   B C    1 
ATOM   4751 O O    . GLY   B 1 51  ? 56.076 -23.083 0.860   1.00 12.34 ?  51  GLY   B O    1 
ATOM   4752 H H    . GLY   B 1 51  ? 52.517 -24.353 2.641   1.00 13.06 ?  51  GLY   B H    1 
ATOM   4753 H HA2  . GLY   B 1 51  ? 54.745 -23.046 2.935   1.00 13.67 ?  51  GLY   B HA2  1 
ATOM   4754 H HA3  . GLY   B 1 51  ? 54.639 -24.614 2.832   1.00 13.67 ?  51  GLY   B HA3  1 
ATOM   4755 N N    . ALA   B 1 52  ? 54.438 -24.399 0.057   1.00 10.84 ?  52  ALA   B N    1 
ATOM   4756 C CA   . ALA   B 1 52  ? 54.995 -24.406 -1.291  1.00 11.37 ?  52  ALA   B CA   1 
ATOM   4757 C C    . ALA   B 1 52  ? 54.910 -23.026 -1.941  1.00 10.56 ?  52  ALA   B C    1 
ATOM   4758 O O    . ALA   B 1 52  ? 55.876 -22.569 -2.572  1.00 11.70 ?  52  ALA   B O    1 
ATOM   4759 C CB   . ALA   B 1 52  ? 54.284 -25.459 -2.141  1.00 12.45 ?  52  ALA   B CB   1 
ATOM   4760 H H    . ALA   B 1 52  ? 53.711 -24.857 0.143   1.00 13.02 ?  52  ALA   B H    1 
ATOM   4761 H HA   . ALA   B 1 52  ? 55.931 -24.653 -1.239  1.00 13.66 ?  52  ALA   B HA   1 
ATOM   4762 H HB1  . ALA   B 1 52  ? 54.669 -25.455 -3.033  1.00 14.96 ?  52  ALA   B HB1  1 
ATOM   4763 H HB2  . ALA   B 1 52  ? 54.415 -26.333 -1.733  1.00 14.96 ?  52  ALA   B HB2  1 
ATOM   4764 H HB3  . ALA   B 1 52  ? 53.342 -25.251 -2.183  1.00 14.96 ?  52  ALA   B HB3  1 
ATOM   4765 N N    . LEU   B 1 53  ? 53.763 -22.351 -1.821  1.00 10.51 ?  53  LEU   B N    1 
ATOM   4766 C CA   . LEU   B 1 53  ? 53.651 -21.012 -2.390  1.00 10.57 ?  53  LEU   B CA   1 
ATOM   4767 C C    . LEU   B 1 53  ? 54.654 -20.069 -1.741  1.00 10.72 ?  53  LEU   B C    1 
ATOM   4768 O O    . LEU   B 1 53  ? 55.357 -19.321 -2.430  1.00 11.20 ?  53  LEU   B O    1 
ATOM   4769 C CB   . LEU   B 1 53  ? 52.224 -20.475 -2.221  1.00 11.09 ?  53  LEU   B CB   1 
ATOM   4770 C CG   . LEU   B 1 53  ? 51.097 -21.196 -2.974  1.00 11.74 ?  53  LEU   B CG   1 
ATOM   4771 C CD1  . LEU   B 1 53  ? 49.744 -20.608 -2.609  1.00 12.99 ?  53  LEU   B CD1  1 
ATOM   4772 C CD2  . LEU   B 1 53  ? 51.304 -21.165 -4.487  1.00 13.40 ?  53  LEU   B CD2  1 
ATOM   4773 H H    . LEU   B 1 53  ? 53.056 -22.640 -1.422  1.00 12.63 ?  53  LEU   B H    1 
ATOM   4774 H HA   . LEU   B 1 53  ? 53.848 -21.054 -3.340  1.00 12.70 ?  53  LEU   B HA   1 
ATOM   4775 H HB2  . LEU   B 1 53  ? 52.000 -20.507 -1.280  1.00 13.33 ?  53  LEU   B HB2  1 
ATOM   4776 H HB3  . LEU   B 1 53  ? 52.214 -19.551 -2.520  1.00 13.33 ?  53  LEU   B HB3  1 
ATOM   4777 H HG   . LEU   B 1 53  ? 51.089 -22.124 -2.699  1.00 14.10 ?  53  LEU   B HG   1 
ATOM   4778 H HD11 . LEU   B 1 53  ? 49.049 -21.085 -3.094  1.00 15.61 ?  53  LEU   B HD11 1 
ATOM   4779 H HD12 . LEU   B 1 53  ? 49.601 -20.711 -1.652  1.00 15.61 ?  53  LEU   B HD12 1 
ATOM   4780 H HD13 . LEU   B 1 53  ? 49.727 -19.670 -2.846  1.00 15.61 ?  53  LEU   B HD13 1 
ATOM   4781 H HD21 . LEU   B 1 53  ? 50.623 -21.709 -4.910  1.00 16.09 ?  53  LEU   B HD21 1 
ATOM   4782 H HD22 . LEU   B 1 53  ? 51.234 -20.250 -4.798  1.00 16.09 ?  53  LEU   B HD22 1 
ATOM   4783 H HD23 . LEU   B 1 53  ? 52.184 -21.520 -4.695  1.00 16.09 ?  53  LEU   B HD23 1 
ATOM   4784 N N    . ASN   B 1 54  ? 54.744 -20.095 -0.412  1.00 10.45 ?  54  ASN   B N    1 
ATOM   4785 C CA   . ASN   B 1 54  ? 55.660 -19.185 0.259   1.00 11.23 ?  54  ASN   B CA   1 
ATOM   4786 C C    . ASN   B 1 54  ? 57.104 -19.464 -0.142  1.00 11.52 ?  54  ASN   B C    1 
ATOM   4787 O O    . ASN   B 1 54  ? 57.881 -18.527 -0.374  1.00 12.12 ?  54  ASN   B O    1 
ATOM   4788 C CB   . ASN   B 1 54  ? 55.506 -19.263 1.770   1.00 11.66 ?  54  ASN   B CB   1 
ATOM   4789 C CG   . ASN   B 1 54  ? 56.482 -18.352 2.477   1.00 11.98 ?  54  ASN   B CG   1 
ATOM   4790 O OD1  . ASN   B 1 54  ? 56.501 -17.141 2.230   1.00 12.25 ?  54  ASN   B OD1  1 
ATOM   4791 N ND2  . ASN   B 1 54  ? 57.321 -18.922 3.332   1.00 13.35 ?  54  ASN   B ND2  1 
ATOM   4792 H H    . ASN   B 1 54  ? 54.304 -20.622 0.104   1.00 12.56 ?  54  ASN   B H    1 
ATOM   4793 H HA   . ASN   B 1 54  ? 55.449 -18.280 -0.018  1.00 13.49 ?  54  ASN   B HA   1 
ATOM   4794 H HB2  . ASN   B 1 54  ? 54.608 -18.991 2.012   1.00 14.01 ?  54  ASN   B HB2  1 
ATOM   4795 H HB3  . ASN   B 1 54  ? 55.676 -20.170 2.061   1.00 14.01 ?  54  ASN   B HB3  1 
ATOM   4796 H HD21 . ASN   B 1 54  ? 57.900 -18.442 3.755   1.00 16.03 ?  54  ASN   B HD21 1 
ATOM   4797 H HD22 . ASN   B 1 54  ? 57.288 -19.769 3.466   1.00 16.03 ?  54  ASN   B HD22 1 
ATOM   4798 N N    . LYS   B 1 55  ? 57.487 -20.741 -0.216  1.00 11.96 ?  55  LYS   B N    1 
ATOM   4799 C CA   . LYS   B 1 55  ? 58.845 -21.078 -0.633  1.00 13.37 ?  55  LYS   B CA   1 
ATOM   4800 C C    . LYS   B 1 55  ? 59.147 -20.540 -2.027  1.00 12.65 ?  55  LYS   B C    1 
ATOM   4801 O O    . LYS   B 1 55  ? 60.250 -20.039 -2.281  1.00 13.27 ?  55  LYS   B O    1 
ATOM   4802 C CB   . LYS   B 1 55  ? 59.048 -22.591 -0.580  1.00 14.82 ?  55  LYS   B CB   1 
ATOM   4803 C CG   . LYS   B 1 55  ? 60.423 -23.054 -1.031  1.00 18.88 ?  55  LYS   B CG   1 
ATOM   4804 C CD   . LYS   B 1 55  ? 60.596 -24.554 -0.845  1.00 22.41 ?  55  LYS   B CD   1 
ATOM   4805 C CE   . LYS   B 1 55  ? 60.661 -24.939 0.631   1.00 25.67 ?  55  LYS   B CE   1 
ATOM   4806 N NZ   . LYS   B 1 55  ? 61.069 -26.351 0.819   1.00 27.34 ?  55  LYS   B NZ   1 
ATOM   4807 H H    . LYS   B 1 55  ? 56.985 -21.417 -0.035  1.00 14.37 ?  55  LYS   B H    1 
ATOM   4808 H HA   . LYS   B 1 55  ? 59.470 -20.672 -0.016  1.00 16.05 ?  55  LYS   B HA   1 
ATOM   4809 H HB2  . LYS   B 1 55  ? 58.920 -22.883 0.335   1.00 17.80 ?  55  LYS   B HB2  1 
ATOM   4810 H HB3  . LYS   B 1 55  ? 58.393 -23.013 -1.154  1.00 17.80 ?  55  LYS   B HB3  1 
ATOM   4811 H HG2  . LYS   B 1 55  ? 60.540 -22.856 -1.973  1.00 22.68 ?  55  LYS   B HG2  1 
ATOM   4812 H HG3  . LYS   B 1 55  ? 61.104 -22.606 -0.506  1.00 22.68 ?  55  LYS   B HG3  1 
ATOM   4813 H HD2  . LYS   B 1 55  ? 59.843 -25.020 -1.243  1.00 26.90 ?  55  LYS   B HD2  1 
ATOM   4814 H HD3  . LYS   B 1 55  ? 61.424 -24.841 -1.265  1.00 26.90 ?  55  LYS   B HD3  1 
ATOM   4815 H HE2  . LYS   B 1 55  ? 61.308 -24.367 1.077   1.00 30.82 ?  55  LYS   B HE2  1 
ATOM   4816 H HE3  . LYS   B 1 55  ? 59.782 -24.817 1.028   1.00 30.82 ?  55  LYS   B HE3  1 
ATOM   4817 H HZ1  . LYS   B 1 55  ? 61.051 -26.558 1.684   1.00 32.82 ?  55  LYS   B HZ1  1 
ATOM   4818 H HZ2  . LYS   B 1 55  ? 60.509 -26.886 0.381   1.00 32.82 ?  55  LYS   B HZ2  1 
ATOM   4819 H HZ3  . LYS   B 1 55  ? 61.891 -26.472 0.506   1.00 32.82 ?  55  LYS   B HZ3  1 
ATOM   4820 N N    . ALA   B 1 56  ? 58.180 -20.632 -2.945  1.00 12.29 ?  56  ALA   B N    1 
ATOM   4821 C CA   . ALA   B 1 56  ? 58.388 -20.119 -4.294  1.00 12.99 ?  56  ALA   B CA   1 
ATOM   4822 C C    . ALA   B 1 56  ? 58.667 -18.623 -4.287  1.00 12.59 ?  56  ALA   B C    1 
ATOM   4823 O O    . ALA   B 1 56  ? 59.390 -18.123 -5.161  1.00 13.93 ?  56  ALA   B O    1 
ATOM   4824 C CB   . ALA   B 1 56  ? 57.183 -20.444 -5.178  1.00 13.39 ?  56  ALA   B CB   1 
ATOM   4825 H H    . ALA   B 1 56  ? 57.401 -20.975 -2.811  1.00 14.76 ?  56  ALA   B H    1 
ATOM   4826 H HA   . ALA   B 1 56  ? 59.160 -20.552 -4.677  1.00 15.60 ?  56  ALA   B HA   1 
ATOM   4827 H HB1  . ALA   B 1 56  ? 57.345 -20.101 -6.073  1.00 16.08 ?  56  ALA   B HB1  1 
ATOM   4828 H HB2  . ALA   B 1 56  ? 57.072 -21.408 -5.212  1.00 16.08 ?  56  ALA   B HB2  1 
ATOM   4829 H HB3  . ALA   B 1 56  ? 56.390 -20.032 -4.805  1.00 16.08 ?  56  ALA   B HB3  1 
ATOM   4830 N N    . THR   B 1 57  ? 58.107 -17.892 -3.319  1.00 12.34 ?  57  THR   B N    1 
ATOM   4831 C CA   . THR   B 1 57  ? 58.343 -16.459 -3.193  1.00 12.52 ?  57  THR   B CA   1 
ATOM   4832 C C    . THR   B 1 57  ? 59.598 -16.129 -2.392  1.00 13.31 ?  57  THR   B C    1 
ATOM   4833 O O    . THR   B 1 57  ? 59.839 -14.951 -2.098  1.00 14.19 ?  57  THR   B O    1 
ATOM   4834 C CB   . THR   B 1 57  ? 57.138 -15.738 -2.554  1.00 12.01 ?  57  THR   B CB   1 
ATOM   4835 O OG1  . THR   B 1 57  ? 57.112 -15.948 -1.133  1.00 12.21 ?  57  THR   B OG1  1 
ATOM   4836 C CG2  . THR   B 1 57  ? 55.821 -16.160 -3.195  1.00 11.99 ?  57  THR   B CG2  1 
ATOM   4837 H H    . THR   B 1 57  ? 57.572 -18.208 -2.720  1.00 14.82 ?  57  THR   B H    1 
ATOM   4838 H HA   . THR   B 1 57  ? 58.457 -16.091 -4.084  1.00 15.04 ?  57  THR   B HA   1 
ATOM   4839 H HB   . THR   B 1 57  ? 57.237 -14.786 -2.717  1.00 14.43 ?  57  THR   B HB   1 
ATOM   4840 H HG1  . THR   B 1 57  ? 57.046 -16.773 -0.972  1.00 14.67 ?  57  THR   B HG1  1 
ATOM   4841 H HG21 . THR   B 1 57  ? 55.094 -15.628 -2.841  1.00 14.40 ?  57  THR   B HG21 1 
ATOM   4842 H HG22 . THR   B 1 57  ? 55.864 -16.042 -4.155  1.00 14.40 ?  57  THR   B HG22 1 
ATOM   4843 H HG23 . THR   B 1 57  ? 55.645 -17.096 -3.003  1.00 14.40 ?  57  THR   B HG23 1 
ATOM   4844 N N    . ASN   B 1 58  ? 60.393 -17.130 -2.030  1.00 13.84 ?  58  ASN   B N    1 
ATOM   4845 C CA   . ASN   B 1 58  ? 61.589 -16.906 -1.227  1.00 16.53 ?  58  ASN   B CA   1 
ATOM   4846 C C    . ASN   B 1 58  ? 61.248 -16.198 0.085   1.00 14.70 ?  58  ASN   B C    1 
ATOM   4847 O O    . ASN   B 1 58  ? 61.987 -15.327 0.553   1.00 15.85 ?  58  ASN   B O    1 
ATOM   4848 C CB   . ASN   B 1 58  ? 62.665 -16.147 -2.011  1.00 24.08 ?  58  ASN   B CB   1 
ATOM   4849 C CG   . ASN   B 1 58  ? 64.035 -16.255 -1.369  1.00 32.39 ?  58  ASN   B CG   1 
ATOM   4850 O OD1  . ASN   B 1 58  ? 64.352 -17.255 -0.725  1.00 34.67 ?  58  ASN   B OD1  1 
ATOM   4851 N ND2  . ASN   B 1 58  ? 64.855 -15.222 -1.540  1.00 36.63 ?  58  ASN   B ND2  1 
ATOM   4852 H H    . ASN   B 1 58  ? 60.261 -17.958 -2.236  1.00 16.62 ?  58  ASN   B H    1 
ATOM   4853 H HA   . ASN   B 1 58  ? 61.964 -17.771 -1.005  1.00 19.85 ?  58  ASN   B HA   1 
ATOM   4854 H HB2  . ASN   B 1 58  ? 62.727 -16.513 -2.911  1.00 28.91 ?  58  ASN   B HB2  1 
ATOM   4855 H HB3  . ASN   B 1 58  ? 62.432 -15.208 -2.053  1.00 28.91 ?  58  ASN   B HB3  1 
ATOM   4856 H HD21 . ASN   B 1 58  ? 65.644 -15.236 -1.196  1.00 43.98 ?  58  ASN   B HD21 1 
ATOM   4857 H HD22 . ASN   B 1 58  ? 64.597 -14.539 -1.994  1.00 43.98 ?  58  ASN   B HD22 1 
ATOM   4858 N N    . ASN   B 1 59  ? 60.120 -16.581 0.688   1.00 13.91 ?  59  ASN   B N    1 
ATOM   4859 C CA   . ASN   B 1 59  ? 59.646 -16.110 1.992   1.00 13.90 ?  59  ASN   B CA   1 
ATOM   4860 C C    . ASN   B 1 59  ? 59.053 -14.703 1.942   1.00 13.28 ?  59  ASN   B C    1 
ATOM   4861 O O    . ASN   B 1 59  ? 58.615 -14.200 2.987   1.00 13.47 ?  59  ASN   B O    1 
ATOM   4862 C CB   . ASN   B 1 59  ? 60.718 -16.174 3.096   1.00 14.99 ?  59  ASN   B CB   1 
ATOM   4863 C CG   . ASN   B 1 59  ? 60.126 -16.340 4.479   1.00 16.17 ?  59  ASN   B CG   1 
ATOM   4864 O OD1  . ASN   B 1 59  ? 59.301 -17.229 4.711   1.00 16.29 ?  59  ASN   B OD1  1 
ATOM   4865 N ND2  . ASN   B 1 59  ? 60.551 -15.491 5.413   1.00 17.03 ?  59  ASN   B ND2  1 
ATOM   4866 H H    . ASN   B 1 59  ? 59.578 -17.155 0.338   1.00 16.70 ?  59  ASN   B H    1 
ATOM   4867 H HA   . ASN   B 1 59  ? 58.938 -16.706 2.273   1.00 16.70 ?  59  ASN   B HA   1 
ATOM   4868 H HB2  . ASN   B 1 59  ? 61.306 -16.931 2.936   1.00 18.01 ?  59  ASN   B HB2  1 
ATOM   4869 H HB3  . ASN   B 1 59  ? 61.233 -15.352 3.095   1.00 18.01 ?  59  ASN   B HB3  1 
ATOM   4870 H HD21 . ASN   B 1 59  ? 60.245 -15.541 6.217   1.00 20.45 ?  59  ASN   B HD21 1 
ATOM   4871 H HD22 . ASN   B 1 59  ? 61.127 -14.884 5.213   1.00 20.45 ?  59  ASN   B HD22 1 
ATOM   4872 N N    . ALA   B 1 60  ? 58.987 -14.059 0.773   1.00 13.04 ?  60  ALA   B N    1 
ATOM   4873 C CA   . ALA   B 1 60  ? 58.387 -12.729 0.711   1.00 12.61 ?  60  ALA   B CA   1 
ATOM   4874 C C    . ALA   B 1 60  ? 56.916 -12.758 1.099   1.00 12.12 ?  60  ALA   B C    1 
ATOM   4875 O O    . ALA   B 1 60  ? 56.412 -11.805 1.710   1.00 12.67 ?  60  ALA   B O    1 
ATOM   4876 C CB   . ALA   B 1 60  ? 58.554 -12.138 -0.686  1.00 13.97 ?  60  ALA   B CB   1 
ATOM   4877 H H    . ALA   B 1 60  ? 59.269 -14.373 0.022   1.00 15.67 ?  60  ALA   B H    1 
ATOM   4878 H HA   . ALA   B 1 60  ? 58.853 -12.155 1.337   1.00 15.15 ?  60  ALA   B HA   1 
ATOM   4879 H HB1  . ALA   B 1 60  ? 58.155 -11.257 -0.701  1.00 16.78 ?  60  ALA   B HB1  1 
ATOM   4880 H HB2  . ALA   B 1 60  ? 59.503 -12.078 -0.891  1.00 16.78 ?  60  ALA   B HB2  1 
ATOM   4881 H HB3  . ALA   B 1 60  ? 58.115 -12.717 -1.328  1.00 16.78 ?  60  ALA   B HB3  1 
ATOM   4882 N N    . MET   B 1 61  ? 56.214 -13.840 0.763   1.00 11.87 ?  61  MET   B N    1 
ATOM   4883 C CA   . MET   B 1 61  ? 54.820 -13.965 1.157   1.00 11.37 ?  61  MET   B CA   1 
ATOM   4884 C C    . MET   B 1 61  ? 54.682 -13.973 2.678   1.00 11.64 ?  61  MET   B C    1 
ATOM   4885 O O    . MET   B 1 61  ? 53.780 -13.324 3.226   1.00 11.50 ?  61  MET   B O    1 
ATOM   4886 C CB   . MET   B 1 61  ? 54.239 -15.235 0.529   1.00 11.69 ?  61  MET   B CB   1 
ATOM   4887 C CG   . MET   B 1 61  ? 52.785 -15.522 0.913   1.00 10.93 ?  61  MET   B CG   1 
ATOM   4888 S SD   . MET   B 1 61  ? 52.152 -17.031 0.160   1.00 11.59 ?  61  MET   B SD   1 
ATOM   4889 C CE   . MET   B 1 61  ? 51.885 -16.449 -1.514  1.00 12.90 ?  61  MET   B CE   1 
ATOM   4890 H H    . MET   B 1 61  ? 56.522 -14.509 0.314   1.00 14.26 ?  61  MET   B H    1 
ATOM   4891 H HA   . MET   B 1 61  ? 54.326 -13.212 0.802   1.00 13.66 ?  61  MET   B HA   1 
ATOM   4892 H HB2  . MET   B 1 61  ? 54.274 -15.152 -0.437  1.00 14.04 ?  61  MET   B HB2  1 
ATOM   4893 H HB3  . MET   B 1 61  ? 54.770 -15.996 0.811   1.00 14.04 ?  61  MET   B HB3  1 
ATOM   4894 H HG2  . MET   B 1 61  ? 52.722 -15.625 1.876   1.00 13.13 ?  61  MET   B HG2  1 
ATOM   4895 H HG3  . MET   B 1 61  ? 52.228 -14.782 0.623   1.00 13.13 ?  61  MET   B HG3  1 
ATOM   4896 H HE1  . MET   B 1 61  ? 51.516 -17.173 -2.047  1.00 15.50 ?  61  MET   B HE1  1 
ATOM   4897 H HE2  . MET   B 1 61  ? 51.258 -15.703 -1.502  1.00 15.50 ?  61  MET   B HE2  1 
ATOM   4898 H HE3  . MET   B 1 61  ? 52.730 -16.160 -1.890  1.00 15.50 ?  61  MET   B HE3  1 
ATOM   4899 N N    . GLN   B 1 62  ? 55.562 -14.696 3.382   1.00 11.33 ?  62  GLN   B N    1 
ATOM   4900 C CA   . GLN   B 1 62  ? 55.460 -14.755 4.837   1.00 11.81 ?  62  GLN   B CA   1 
ATOM   4901 C C    . GLN   B 1 62  ? 55.738 -13.398 5.470   1.00 11.98 ?  62  GLN   B C    1 
ATOM   4902 O O    . GLN   B 1 62  ? 55.048 -12.996 6.413   1.00 12.56 ?  62  GLN   B O    1 
ATOM   4903 C CB   . GLN   B 1 62  ? 56.418 -15.809 5.398   1.00 11.83 ?  62  GLN   B CB   1 
ATOM   4904 C CG   . GLN   B 1 62  ? 56.199 -16.086 6.872   1.00 12.25 ?  62  GLN   B CG   1 
ATOM   4905 C CD   . GLN   B 1 62  ? 54.820 -16.668 7.115   1.00 12.14 ?  62  GLN   B CD   1 
ATOM   4906 O OE1  . GLN   B 1 62  ? 54.559 -17.818 6.762   1.00 12.42 ?  62  GLN   B OE1  1 
ATOM   4907 N NE2  . GLN   B 1 62  ? 53.914 -15.866 7.678   1.00 12.28 ?  62  GLN   B NE2  1 
ATOM   4908 H H    . GLN   B 1 62  ? 56.209 -15.153 3.044   1.00 13.61 ?  62  GLN   B H    1 
ATOM   4909 H HA   . GLN   B 1 62  ? 54.556 -15.013 5.074   1.00 14.18 ?  62  GLN   B HA   1 
ATOM   4910 H HB2  . GLN   B 1 62  ? 56.294 -16.638 4.916   1.00 14.21 ?  62  GLN   B HB2  1 
ATOM   4911 H HB3  . GLN   B 1 62  ? 57.331 -15.492 5.286   1.00 14.21 ?  62  GLN   B HB3  1 
ATOM   4912 H HG2  . GLN   B 1 62  ? 56.859 -16.726 7.179   1.00 14.72 ?  62  GLN   B HG2  1 
ATOM   4913 H HG3  . GLN   B 1 62  ? 56.279 -15.257 7.374   1.00 14.72 ?  62  GLN   B HG3  1 
ATOM   4914 H HE21 . GLN   B 1 62  ? 54.133 -15.060 7.900   1.00 14.75 ?  62  GLN   B HE21 1 
ATOM   4915 H HE22 . GLN   B 1 62  ? 53.121 -16.151 7.828   1.00 14.75 ?  62  GLN   B HE22 1 
ATOM   4916 N N    . VAL   B 1 63  ? 56.748 -12.679 4.979   1.00 12.67 ?  63  VAL   B N    1 
ATOM   4917 C CA   . VAL   B 1 63  ? 57.055 -11.364 5.538   1.00 13.41 ?  63  VAL   B CA   1 
ATOM   4918 C C    . VAL   B 1 63  ? 55.865 -10.429 5.357   1.00 12.89 ?  63  VAL   B C    1 
ATOM   4919 O O    . VAL   B 1 63  ? 55.450 -9.723  6.289   1.00 13.36 ?  63  VAL   B O    1 
ATOM   4920 C CB   . VAL   B 1 63  ? 58.343 -10.808 4.907   1.00 15.05 ?  63  VAL   B CB   1 
ATOM   4921 C CG1  . VAL   B 1 63  ? 58.566 -9.365  5.335   1.00 15.78 ?  63  VAL   B CG1  1 
ATOM   4922 C CG2  . VAL   B 1 63  ? 59.536 -11.670 5.307   1.00 15.86 ?  63  VAL   B CG2  1 
ATOM   4923 H H    . VAL   B 1 63  ? 57.251 -12.920 4.324   1.00 15.22 ?  63  VAL   B H    1 
ATOM   4924 H HA   . VAL   B 1 63  ? 57.212 -11.463 6.488   1.00 16.10 ?  63  VAL   B HA   1 
ATOM   4925 H HB   . VAL   B 1 63  ? 58.271 -10.833 3.942   1.00 18.07 ?  63  VAL   B HB   1 
ATOM   4926 H HG11 . VAL   B 1 63  ? 59.485 -9.119  5.151   1.00 18.95 ?  63  VAL   B HG11 1 
ATOM   4927 H HG12 . VAL   B 1 63  ? 57.964 -8.792  4.837   1.00 18.95 ?  63  VAL   B HG12 1 
ATOM   4928 H HG13 . VAL   B 1 63  ? 58.389 -9.288  6.287   1.00 18.95 ?  63  VAL   B HG13 1 
ATOM   4929 H HG21 . VAL   B 1 63  ? 60.343 -11.299 4.914   1.00 19.05 ?  63  VAL   B HG21 1 
ATOM   4930 H HG22 . VAL   B 1 63  ? 59.616 -11.671 6.277   1.00 19.05 ?  63  VAL   B HG22 1 
ATOM   4931 H HG23 . VAL   B 1 63  ? 59.398 -12.574 4.988   1.00 19.05 ?  63  VAL   B HG23 1 
ATOM   4932 N N    . GLU   B 1 64  ? 55.294 -10.418 4.151   1.00 12.37 ?  64  GLU   B N    1 
ATOM   4933 C CA   . GLU   B 1 64  ? 54.127 -9.584  3.876   1.00 12.10 ?  64  GLU   B CA   1 
ATOM   4934 C C    . GLU   B 1 64  ? 52.945 -9.985  4.752   1.00 11.68 ?  64  GLU   B C    1 
ATOM   4935 O O    . GLU   B 1 64  ? 52.207 -9.124  5.258   1.00 12.34 ?  64  GLU   B O    1 
ATOM   4936 C CB   . GLU   B 1 64  ? 53.763 -9.730  2.398   1.00 12.26 ?  64  GLU   B CB   1 
ATOM   4937 C CG   . GLU   B 1 64  ? 52.503 -8.991  1.966   1.00 12.55 ?  64  GLU   B CG   1 
ATOM   4938 C CD   . GLU   B 1 64  ? 51.965 -9.486  0.628   1.00 13.37 ?  64  GLU   B CD   1 
ATOM   4939 O OE1  . GLU   B 1 64  ? 52.145 -10.689 0.305   1.00 13.97 ?  64  GLU   B OE1  1 
ATOM   4940 O OE2  . GLU   B 1 64  ? 51.349 -8.671  -0.101  1.00 14.09 -1 64  GLU   B OE2  1 
ATOM   4941 H H    . GLU   B 1 64  ? 55.568 -10.885 3.476   1.00 14.86 ?  64  GLU   B H    1 
ATOM   4942 H HA   . GLU   B 1 64  ? 54.344 -8.657  4.049   1.00 14.54 ?  64  GLU   B HA   1 
ATOM   4943 H HB2  . GLU   B 1 64  ? 54.494 -9.389  1.860   1.00 14.73 ?  64  GLU   B HB2  1 
ATOM   4944 H HB3  . GLU   B 1 64  ? 53.628 -10.670 2.205   1.00 14.73 ?  64  GLU   B HB3  1 
ATOM   4945 H HG2  . GLU   B 1 64  ? 51.805 -9.114  2.633   1.00 15.08 ?  64  GLU   B HG2  1 
ATOM   4946 H HG3  . GLU   B 1 64  ? 52.707 -8.045  1.881   1.00 15.08 ?  64  GLU   B HG3  1 
ATOM   4947 N N    . SER   B 1 65  ? 52.751 -11.294 4.929   1.00 11.49 ?  65  SER   B N    1 
ATOM   4948 C CA   . SER   B 1 65  ? 51.648 -11.806 5.733   1.00 11.56 ?  65  SER   B CA   1 
ATOM   4949 C C    . SER   B 1 65  ? 51.788 -11.403 7.196   1.00 12.04 ?  65  SER   B C    1 
ATOM   4950 O O    . SER   B 1 65  ? 50.795 -11.025 7.839   1.00 12.27 ?  65  SER   B O    1 
ATOM   4951 C CB   . SER   B 1 65  ? 51.594 -13.327 5.609   1.00 11.15 ?  65  SER   B CB   1 
ATOM   4952 O OG   . SER   B 1 65  ? 51.229 -13.720 4.296   1.00 11.97 ?  65  SER   B OG   1 
ATOM   4953 H H    . SER   B 1 65  ? 53.242 -11.915 4.586   1.00 13.81 ?  65  SER   B H    1 
ATOM   4954 H HA   . SER   B 1 65  ? 50.809 -11.445 5.400   1.00 13.89 ?  65  SER   B HA   1 
ATOM   4955 H HB2  . SER   B 1 65  ? 52.461 -13.696 5.814   1.00 13.40 ?  65  SER   B HB2  1 
ATOM   4956 H HB3  . SER   B 1 65  ? 50.929 -13.672 6.233   1.00 13.40 ?  65  SER   B HB3  1 
ATOM   4957 H HG   . SER   B 1 65  ? 51.785 -13.420 3.737   1.00 14.37 ?  65  SER   B HG   1 
ATOM   4958 N N    . ASP   B 1 66  ? 53.004 -11.493 7.750   1.00 12.05 ?  66  ASP   B N    1 
ATOM   4959 C CA   . ASP   B 1 66  ? 53.197 -11.115 9.149   1.00 12.20 ?  66  ASP   B CA   1 
ATOM   4960 C C    . ASP   B 1 66  ? 52.885 -9.638  9.362   1.00 12.54 ?  66  ASP   B C    1 
ATOM   4961 O O    . ASP   B 1 66  ? 52.318 -9.254  10.393  1.00 13.12 ?  66  ASP   B O    1 
ATOM   4962 C CB   . ASP   B 1 66  ? 54.625 -11.428 9.602   1.00 13.50 ?  66  ASP   B CB   1 
ATOM   4963 C CG   . ASP   B 1 66  ? 54.890 -12.923 9.754   1.00 15.80 ?  66  ASP   B CG   1 
ATOM   4964 O OD1  . ASP   B 1 66  ? 53.935 -13.733 9.699   1.00 16.44 ?  66  ASP   B OD1  1 
ATOM   4965 O OD2  . ASP   B 1 66  ? 56.072 -13.289 9.944   1.00 18.62 -1 66  ASP   B OD2  1 
ATOM   4966 H H    . ASP   B 1 66  ? 53.708 -11.776 7.350   1.00 14.48 ?  66  ASP   B H    1 
ATOM   4967 H HA   . ASP   B 1 66  ? 52.592 -11.621 9.706   1.00 14.66 ?  66  ASP   B HA   1 
ATOM   4968 H HB2  . ASP   B 1 66  ? 55.251 -11.085 8.947   1.00 16.21 ?  66  ASP   B HB2  1 
ATOM   4969 H HB3  . ASP   B 1 66  ? 54.784 -11.004 10.463  1.00 16.21 ?  66  ASP   B HB3  1 
ATOM   4970 N N    . ASP   B 1 67  ? 53.258 -8.790  8.402   1.00 11.97 ?  67  ASP   B N    1 
ATOM   4971 C CA   . ASP   B 1 67  ? 52.910 -7.378  8.494   1.00 12.83 ?  67  ASP   B CA   1 
ATOM   4972 C C    . ASP   B 1 67  ? 51.399 -7.174  8.420   1.00 13.10 ?  67  ASP   B C    1 
ATOM   4973 O O    . ASP   B 1 67  ? 50.840 -6.374  9.176   1.00 13.54 ?  67  ASP   B O    1 
ATOM   4974 C CB   . ASP   B 1 67  ? 53.618 -6.605  7.389   1.00 14.20 ?  67  ASP   B CB   1 
ATOM   4975 C CG   . ASP   B 1 67  ? 53.197 -5.159  7.352   1.00 15.45 ?  67  ASP   B CG   1 
ATOM   4976 O OD1  . ASP   B 1 67  ? 53.678 -4.363  8.188   1.00 16.31 ?  67  ASP   B OD1  1 
ATOM   4977 O OD2  . ASP   B 1 67  ? 52.353 -4.838  6.504   1.00 16.48 -1 67  ASP   B OD2  1 
ATOM   4978 H H    . ASP   B 1 67  ? 53.719 -9.003  7.701   1.00 14.38 ?  67  ASP   B H    1 
ATOM   4979 H HA   . ASP   B 1 67  ? 53.223 -7.031  9.342   1.00 15.41 ?  67  ASP   B HA   1 
ATOM   4980 H HB2  . ASP   B 1 67  ? 54.576 -6.633  7.538   1.00 17.06 ?  67  ASP   B HB2  1 
ATOM   4981 H HB3  . ASP   B 1 67  ? 53.407 -7.012  6.529   1.00 17.06 ?  67  ASP   B HB3  1 
ATOM   4982 N N    . TYR   B 1 68  ? 50.720 -7.898  7.525   1.00 12.42 ?  68  TYR   B N    1 
ATOM   4983 C CA   . TYR   B 1 68  ? 49.261 -7.823  7.455   1.00 13.20 ?  68  TYR   B CA   1 
ATOM   4984 C C    . TYR   B 1 68  ? 48.627 -8.167  8.799   1.00 12.93 ?  68  TYR   B C    1 
ATOM   4985 O O    . TYR   B 1 68  ? 47.698 -7.485  9.251   1.00 13.48 ?  68  TYR   B O    1 
ATOM   4986 C CB   . TYR   B 1 68  ? 48.726 -8.743  6.347   1.00 13.93 ?  68  TYR   B CB   1 
ATOM   4987 C CG   . TYR   B 1 68  ? 47.217 -8.899  6.400   1.00 15.22 ?  68  TYR   B CG   1 
ATOM   4988 C CD1  . TYR   B 1 68  ? 46.629 -9.850  7.228   1.00 16.05 ?  68  TYR   B CD1  1 
ATOM   4989 C CD2  . TYR   B 1 68  ? 46.387 -8.066  5.671   1.00 16.05 ?  68  TYR   B CD2  1 
ATOM   4990 C CE1  . TYR   B 1 68  ? 45.262 -9.972  7.319   1.00 17.08 ?  68  TYR   B CE1  1 
ATOM   4991 C CE2  . TYR   B 1 68  ? 45.005 -8.194  5.747   1.00 16.51 ?  68  TYR   B CE2  1 
ATOM   4992 C CZ   . TYR   B 1 68  ? 44.462 -9.144  6.576   1.00 17.00 ?  68  TYR   B CZ   1 
ATOM   4993 O OH   . TYR   B 1 68  ? 43.096 -9.260  6.669   1.00 18.36 ?  68  TYR   B OH   1 
ATOM   4994 H H    . TYR   B 1 68  ? 51.078 -8.436  6.953   1.00 14.92 ?  68  TYR   B H    1 
ATOM   4995 H HA   . TYR   B 1 68  ? 49.011 -6.917  7.240   1.00 15.85 ?  68  TYR   B HA   1 
ATOM   4996 H HB2  . TYR   B 1 68  ? 48.954 -8.363  5.488   1.00 16.73 ?  68  TYR   B HB2  1 
ATOM   4997 H HB3  . TYR   B 1 68  ? 49.122 -9.622  6.444   1.00 16.73 ?  68  TYR   B HB3  1 
ATOM   4998 H HD1  . TYR   B 1 68  ? 47.171 -10.415 7.740   1.00 19.28 ?  68  TYR   B HD1  1 
ATOM   4999 H HD2  . TYR   B 1 68  ? 46.758 -7.414  5.129   1.00 19.27 ?  68  TYR   B HD2  1 
ATOM   5000 H HE1  . TYR   B 1 68  ? 44.882 -10.626 7.869   1.00 20.52 ?  68  TYR   B HE1  1 
ATOM   5001 H HE2  . TYR   B 1 68  ? 44.453 -7.630  5.261   1.00 19.83 ?  68  TYR   B HE2  1 
ATOM   5002 H HH   . TYR   B 1 68  ? 42.713 -8.707  6.161   1.00 22.05 ?  68  TYR   B HH   1 
ATOM   5003 N N    . ILE   B 1 69  ? 49.103 -9.241  9.443   1.00 12.69 ?  69  ILE   B N    1 
ATOM   5004 C CA   . ILE   B 1 69  ? 48.544 -9.671  10.725  1.00 13.61 ?  69  ILE   B CA   1 
ATOM   5005 C C    . ILE   B 1 69  ? 48.798 -8.625  11.803  1.00 13.27 ?  69  ILE   B C    1 
ATOM   5006 O O    . ILE   B 1 69  ? 47.931 -8.350  12.639  1.00 13.72 ?  69  ILE   B O    1 
ATOM   5007 C CB   . ILE   B 1 69  ? 49.119 -11.049 11.118  1.00 14.62 ?  69  ILE   B CB   1 
ATOM   5008 C CG1  . ILE   B 1 69  ? 48.595 -12.152 10.194  1.00 14.80 ?  69  ILE   B CG1  1 
ATOM   5009 C CG2  . ILE   B 1 69  ? 48.818 -11.376 12.581  1.00 15.77 ?  69  ILE   B CG2  1 
ATOM   5010 C CD1  . ILE   B 1 69  ? 47.110 -12.466 10.348  1.00 15.00 ?  69  ILE   B CD1  1 
ATOM   5011 H H    . ILE   B 1 69  ? 49.748 -9.741  9.162   1.00 15.24 ?  69  ILE   B H    1 
ATOM   5012 H HA   . ILE   B 1 69  ? 47.586 -9.772  10.630  1.00 16.35 ?  69  ILE   B HA   1 
ATOM   5013 H HB   . ILE   B 1 69  ? 50.085 -11.011 11.020  1.00 17.56 ?  69  ILE   B HB   1 
ATOM   5014 H HG12 . ILE   B 1 69  ? 48.749 -11.884 9.275   1.00 17.78 ?  69  ILE   B HG12 1 
ATOM   5015 H HG13 . ILE   B 1 69  ? 49.090 -12.971 10.377  1.00 17.78 ?  69  ILE   B HG13 1 
ATOM   5016 H HG21 . ILE   B 1 69  ? 48.966 -12.323 12.727  1.00 18.94 ?  69  ILE   B HG21 1 
ATOM   5017 H HG22 . ILE   B 1 69  ? 49.408 -10.859 13.152  1.00 18.94 ?  69  ILE   B HG22 1 
ATOM   5018 H HG23 . ILE   B 1 69  ? 47.893 -11.154 12.769  1.00 18.94 ?  69  ILE   B HG23 1 
ATOM   5019 H HD11 . ILE   B 1 69  ? 46.877 -13.172 9.728   1.00 18.02 ?  69  ILE   B HD11 1 
ATOM   5020 H HD12 . ILE   B 1 69  ? 46.940 -12.755 11.257  1.00 18.02 ?  69  ILE   B HD12 1 
ATOM   5021 H HD13 . ILE   B 1 69  ? 46.599 -11.668 10.150  1.00 18.02 ?  69  ILE   B HD13 1 
ATOM   5022 N N    . ALA   B 1 70  ? 49.995 -8.040  11.822  1.00 12.94 ?  70  ALA   B N    1 
ATOM   5023 C CA   . ALA   B 1 70  ? 50.284 -7.011  12.815  1.00 12.79 ?  70  ALA   B CA   1 
ATOM   5024 C C    . ALA   B 1 70  ? 49.298 -5.858  12.704  1.00 13.04 ?  70  ALA   B C    1 
ATOM   5025 O O    . ALA   B 1 70  ? 48.857 -5.308  13.718  1.00 13.58 ?  70  ALA   B O    1 
ATOM   5026 C CB   . ALA   B 1 70  ? 51.719 -6.515  12.653  1.00 13.44 ?  70  ALA   B CB   1 
ATOM   5027 H H    . ALA   B 1 70  ? 50.634 -8.217  11.283  1.00 15.55 ?  70  ALA   B H    1 
ATOM   5028 H HA   . ALA   B 1 70  ? 50.196 -7.391  13.702  1.00 15.36 ?  70  ALA   B HA   1 
ATOM   5029 H HB1  . ALA   B 1 70  ? 51.901 -5.846  13.333  1.00 16.15 ?  70  ALA   B HB1  1 
ATOM   5030 H HB2  . ALA   B 1 70  ? 52.325 -7.265  12.759  1.00 16.15 ?  70  ALA   B HB2  1 
ATOM   5031 H HB3  . ALA   B 1 70  ? 51.823 -6.126  11.771  1.00 16.15 ?  70  ALA   B HB3  1 
ATOM   5032 N N    . THR   B 1 71  ? 48.927 -5.491  11.479  1.00 13.83 ?  71  THR   B N    1 
ATOM   5033 C CA   . THR   B 1 71  ? 48.037 -4.354  11.270  1.00 14.63 ?  71  THR   B CA   1 
ATOM   5034 C C    . THR   B 1 71  ? 46.570 -4.716  11.476  1.00 15.05 ?  71  THR   B C    1 
ATOM   5035 O O    . THR   B 1 71  ? 45.790 -3.899  11.986  1.00 16.66 ?  71  THR   B O    1 
ATOM   5036 C CB   . THR   B 1 71  ? 48.257 -3.786  9.867   1.00 16.55 ?  71  THR   B CB   1 
ATOM   5037 O OG1  . THR   B 1 71  ? 49.590 -3.266  9.769   1.00 18.49 ?  71  THR   B OG1  1 
ATOM   5038 C CG2  . THR   B 1 71  ? 47.240 -2.686  9.544   1.00 17.72 ?  71  THR   B CG2  1 
ATOM   5039 H H    . THR   B 1 71  ? 49.178 -5.878  10.756  1.00 16.61 ?  71  THR   B H    1 
ATOM   5040 H HA   . THR   B 1 71  ? 48.258 -3.657  11.903  1.00 17.58 ?  71  THR   B HA   1 
ATOM   5041 H HB   . THR   B 1 71  ? 48.153 -4.490  9.208   1.00 19.88 ?  71  THR   B HB   1 
ATOM   5042 H HG1  . THR   B 1 71  ? 49.713 -2.926  9.005   1.00 22.20 ?  71  THR   B HG1  1 
ATOM   5043 H HG21 . THR   B 1 71  ? 47.540 -2.166  8.780   1.00 21.29 ?  71  THR   B HG21 1 
ATOM   5044 H HG22 . THR   B 1 71  ? 46.377 -3.075  9.336   1.00 21.29 ?  71  THR   B HG22 1 
ATOM   5045 H HG23 . THR   B 1 71  ? 47.143 -2.090  10.305  1.00 21.29 ?  71  THR   B HG23 1 
ATOM   5046 N N    . ASN   B 1 72  ? 46.175 -5.931  11.090  1.00 14.93 ?  72  ASN   B N    1 
ATOM   5047 C CA   . ASN   B 1 72  ? 44.769 -6.288  10.954  1.00 15.50 ?  72  ASN   B CA   1 
ATOM   5048 C C    . ASN   B 1 72  ? 44.292 -7.390  11.891  1.00 15.92 ?  72  ASN   B C    1 
ATOM   5049 O O    . ASN   B 1 72  ? 43.073 -7.558  12.045  1.00 17.12 ?  72  ASN   B O    1 
ATOM   5050 C CB   . ASN   B 1 72  ? 44.461 -6.706  9.507   1.00 16.46 ?  72  ASN   B CB   1 
ATOM   5051 C CG   . ASN   B 1 72  ? 44.739 -5.598  8.520   1.00 17.32 ?  72  ASN   B CG   1 
ATOM   5052 O OD1  . ASN   B 1 72  ? 45.744 -5.608  7.802   1.00 18.43 ?  72  ASN   B OD1  1 
ATOM   5053 N ND2  . ASN   B 1 72  ? 43.866 -4.611  8.506   1.00 18.95 ?  72  ASN   B ND2  1 
ATOM   5054 H H    . ASN   B 1 72  ? 46.716 -6.579  10.896  1.00 17.93 ?  72  ASN   B H    1 
ATOM   5055 H HA   . ASN   B 1 72  ? 44.240 -5.501  11.147  1.00 18.61 ?  72  ASN   B HA   1 
ATOM   5056 H HB2  . ASN   B 1 72  ? 45.017 -7.466  9.273   1.00 19.77 ?  72  ASN   B HB2  1 
ATOM   5057 H HB3  . ASN   B 1 72  ? 43.524 -6.945  9.443   1.00 19.77 ?  72  ASN   B HB3  1 
ATOM   5058 H HD21 . ASN   B 1 72  ? 43.970 -3.948  7.969   1.00 22.75 ?  72  ASN   B HD21 1 
ATOM   5059 H HD22 . ASN   B 1 72  ? 43.176 -4.631  9.028   1.00 22.75 ?  72  ASN   B HD22 1 
ATOM   5060 N N    . GLY   B 1 73  ? 45.197 -8.137  12.521  1.00 15.24 ?  73  GLY   B N    1 
ATOM   5061 C CA   . GLY   B 1 73  ? 44.804 -9.279  13.308  1.00 14.95 ?  73  GLY   B CA   1 
ATOM   5062 C C    . GLY   B 1 73  ? 44.429 -10.457 12.432  1.00 13.48 ?  73  GLY   B C    1 
ATOM   5063 O O    . GLY   B 1 73  ? 44.415 -10.365 11.200  1.00 13.64 ?  73  GLY   B O    1 
ATOM   5064 H H    . GLY   B 1 73  ? 46.050 -8.002  12.499  1.00 18.30 ?  73  GLY   B H    1 
ATOM   5065 H HA2  . GLY   B 1 73  ? 45.535 -9.545  13.886  1.00 17.96 ?  73  GLY   B HA2  1 
ATOM   5066 H HA3  . GLY   B 1 73  ? 44.040 -9.049  13.858  1.00 17.96 ?  73  GLY   B HA3  1 
ATOM   5067 N N    . PRO   B 1 74  ? 44.116 -11.587 13.062  1.00 14.02 ?  74  PRO   B N    1 
ATOM   5068 C CA   . PRO   B 1 74  ? 43.863 -12.814 12.307  1.00 13.70 ?  74  PRO   B CA   1 
ATOM   5069 C C    . PRO   B 1 74  ? 42.560 -12.757 11.519  1.00 12.81 ?  74  PRO   B C    1 
ATOM   5070 O O    . PRO   B 1 74  ? 41.617 -12.022 11.841  1.00 13.61 ?  74  PRO   B O    1 
ATOM   5071 C CB   . PRO   B 1 74  ? 43.790 -13.887 13.402  1.00 14.31 ?  74  PRO   B CB   1 
ATOM   5072 C CG   . PRO   B 1 74  ? 43.368 -13.154 14.623  1.00 15.72 ?  74  PRO   B CG   1 
ATOM   5073 C CD   . PRO   B 1 74  ? 44.028 -11.810 14.514  1.00 15.05 ?  74  PRO   B CD   1 
ATOM   5074 H HA   . PRO   B 1 74  ? 44.603 -13.005 11.705  1.00 16.45 ?  74  PRO   B HA   1 
ATOM   5075 H HB2  . PRO   B 1 74  ? 43.135 -14.561 13.155  1.00 17.19 ?  74  PRO   B HB2  1 
ATOM   5076 H HB3  . PRO   B 1 74  ? 44.666 -14.289 13.523  1.00 17.19 ?  74  PRO   B HB3  1 
ATOM   5077 H HG2  . PRO   B 1 74  ? 42.401 -13.066 14.630  1.00 18.88 ?  74  PRO   B HG2  1 
ATOM   5078 H HG3  . PRO   B 1 74  ? 43.676 -13.629 15.410  1.00 18.88 ?  74  PRO   B HG3  1 
ATOM   5079 H HD2  . PRO   B 1 74  ? 43.477 -11.129 14.935  1.00 18.08 ?  74  PRO   B HD2  1 
ATOM   5080 H HD3  . PRO   B 1 74  ? 44.917 -11.837 14.900  1.00 18.08 ?  74  PRO   B HD3  1 
ATOM   5081 N N    . LEU   B 1 75  ? 42.522 -13.575 10.467  1.00 12.19 ?  75  LEU   B N    1 
ATOM   5082 C CA   . LEU   B 1 75  ? 41.309 -13.793 9.699   1.00 12.09 ?  75  LEU   B CA   1 
ATOM   5083 C C    . LEU   B 1 75  ? 40.342 -14.658 10.502  1.00 12.27 ?  75  LEU   B C    1 
ATOM   5084 O O    . LEU   B 1 75  ? 40.682 -15.201 11.552  1.00 13.45 ?  75  LEU   B O    1 
ATOM   5085 C CB   . LEU   B 1 75  ? 41.633 -14.501 8.381   1.00 12.23 ?  75  LEU   B CB   1 
ATOM   5086 C CG   . LEU   B 1 75  ? 42.505 -13.759 7.361   1.00 13.83 ?  75  LEU   B CG   1 
ATOM   5087 C CD1  . LEU   B 1 75  ? 42.720 -14.597 6.100   1.00 14.91 ?  75  LEU   B CD1  1 
ATOM   5088 C CD2  . LEU   B 1 75  ? 41.934 -12.416 7.004   1.00 17.33 ?  75  LEU   B CD2  1 
ATOM   5089 H H    . LEU   B 1 75  ? 43.196 -14.031 10.180  1.00 14.65 ?  75  LEU   B H    1 
ATOM   5090 H HA   . LEU   B 1 75  ? 40.885 -12.947 9.505   1.00 14.52 ?  75  LEU   B HA   1 
ATOM   5091 H HB2  . LEU   B 1 75  ? 42.092 -15.331 8.590   1.00 14.69 ?  75  LEU   B HB2  1 
ATOM   5092 H HB3  . LEU   B 1 75  ? 40.798 -14.707 7.935   1.00 14.69 ?  75  LEU   B HB3  1 
ATOM   5093 H HG   . LEU   B 1 75  ? 43.380 -13.612 7.754   1.00 16.61 ?  75  LEU   B HG   1 
ATOM   5094 H HD11 . LEU   B 1 75  ? 43.280 -14.097 5.478   1.00 17.91 ?  75  LEU   B HD11 1 
ATOM   5095 H HD12 . LEU   B 1 75  ? 43.158 -15.429 6.337   1.00 17.91 ?  75  LEU   B HD12 1 
ATOM   5096 H HD13 . LEU   B 1 75  ? 41.861 -14.781 5.689   1.00 17.91 ?  75  LEU   B HD13 1 
ATOM   5097 H HD21 . LEU   B 1 75  ? 42.480 -12.016 6.310   1.00 20.81 ?  75  LEU   B HD21 1 
ATOM   5098 H HD22 . LEU   B 1 75  ? 41.027 -12.535 6.688   1.00 20.81 ?  75  LEU   B HD22 1 
ATOM   5099 H HD23 . LEU   B 1 75  ? 41.941 -11.854 7.795   1.00 20.81 ?  75  LEU   B HD23 1 
ATOM   5100 N N    . LYS   B 1 76  ? 39.115 -14.771 9.992   1.00 13.44 ?  76  LYS   B N    1 
ATOM   5101 C CA   . LYS   B 1 76  ? 38.129 -15.730 10.473  1.00 15.21 ?  76  LYS   B CA   1 
ATOM   5102 C C    . LYS   B 1 76  ? 38.212 -17.001 9.631   1.00 13.29 ?  76  LYS   B C    1 
ATOM   5103 O O    . LYS   B 1 76  ? 38.482 -16.944 8.432   1.00 12.78 ?  76  LYS   B O    1 
ATOM   5104 C CB   . LYS   B 1 76  ? 36.707 -15.159 10.306  1.00 17.76 ?  76  LYS   B CB   1 
ATOM   5105 C CG   . LYS   B 1 76  ? 36.420 -13.784 10.937  1.00 19.55 ?  76  LYS   B CG   1 
ATOM   5106 C CD   . LYS   B 1 76  ? 35.025 -13.242 10.558  1.00 20.76 ?  76  LYS   B CD   1 
ATOM   5107 C CE   . LYS   B 1 76  ? 34.766 -11.871 11.166  1.00 23.20 ?  76  LYS   B CE   1 
ATOM   5108 N NZ   . LYS   B 1 76  ? 33.471 -11.282 10.725  1.00 24.37 ?  76  LYS   B NZ   1 
ATOM   5109 H H    . LYS   B 1 76  ? 38.822 -14.285 9.347   1.00 16.15 ?  76  LYS   B H    1 
ATOM   5110 H HA   . LYS   B 1 76  ? 38.284 -15.950 11.407  1.00 18.27 ?  76  LYS   B HA   1 
ATOM   5111 H HB2  . LYS   B 1 76  ? 36.526 -15.082 9.355   1.00 21.32 ?  76  LYS   B HB2  1 
ATOM   5112 H HB3  . LYS   B 1 76  ? 36.081 -15.789 10.698  1.00 21.32 ?  76  LYS   B HB3  1 
ATOM   5113 H HG2  . LYS   B 1 76  ? 36.464 -13.865 11.901  1.00 23.48 ?  76  LYS   B HG2  1 
ATOM   5114 H HG3  . LYS   B 1 76  ? 37.088 -13.151 10.624  1.00 23.48 ?  76  LYS   B HG3  1 
ATOM   5115 H HD2  . LYS   B 1 76  ? 34.971 -13.164 9.591   1.00 24.93 ?  76  LYS   B HD2  1 
ATOM   5116 H HD3  . LYS   B 1 76  ? 34.351 -13.856 10.883  1.00 24.93 ?  76  LYS   B HD3  1 
ATOM   5117 H HE2  . LYS   B 1 76  ? 34.749 -11.956 12.132  1.00 27.85 ?  76  LYS   B HE2  1 
ATOM   5118 H HE3  . LYS   B 1 76  ? 35.481 -11.269 10.900  1.00 27.85 ?  76  LYS   B HE3  1 
ATOM   5119 H HZ1  . LYS   B 1 76  ? 33.358 -10.482 11.102  1.00 29.26 ?  76  LYS   B HZ1  1 
ATOM   5120 H HZ2  . LYS   B 1 76  ? 33.465 -11.185 9.840   1.00 29.26 ?  76  LYS   B HZ2  1 
ATOM   5121 H HZ3  . LYS   B 1 76  ? 32.798 -11.811 10.964  1.00 29.26 ?  76  LYS   B HZ3  1 
ATOM   5122 N N    . VAL   B 1 77  ? 37.955 -18.158 10.252  1.00 13.88 ?  77  VAL   B N    1 
ATOM   5123 C CA   . VAL   B 1 77  ? 37.748 -19.366 9.457   1.00 13.97 ?  77  VAL   B CA   1 
ATOM   5124 C C    . VAL   B 1 77  ? 36.556 -19.127 8.541   1.00 12.86 ?  77  VAL   B C    1 
ATOM   5125 O O    . VAL   B 1 77  ? 35.494 -18.669 8.984   1.00 12.83 ?  77  VAL   B O    1 
ATOM   5126 C CB   . VAL   B 1 77  ? 37.547 -20.598 10.352  1.00 15.42 ?  77  VAL   B CB   1 
ATOM   5127 C CG1  . VAL   B 1 77  ? 37.273 -21.829 9.490   1.00 16.30 ?  77  VAL   B CG1  1 
ATOM   5128 C CG2  . VAL   B 1 77  ? 38.770 -20.830 11.235  1.00 16.88 ?  77  VAL   B CG2  1 
ATOM   5129 H H    . VAL   B 1 77  ? 37.903 -18.265 11.098  1.00 16.67 ?  77  VAL   B H    1 
ATOM   5130 H HA   . VAL   B 1 77  ? 38.525 -19.520 8.900   1.00 16.78 ?  77  VAL   B HA   1 
ATOM   5131 H HB   . VAL   B 1 77  ? 36.777 -20.452 10.926  1.00 18.52 ?  77  VAL   B HB   1 
ATOM   5132 H HG11 . VAL   B 1 77  ? 37.335 -22.620 10.046  1.00 19.57 ?  77  VAL   B HG11 1 
ATOM   5133 H HG12 . VAL   B 1 77  ? 36.377 -21.762 9.115   1.00 19.57 ?  77  VAL   B HG12 1 
ATOM   5134 H HG13 . VAL   B 1 77  ? 37.927 -21.869 8.779   1.00 19.57 ?  77  VAL   B HG13 1 
ATOM   5135 H HG21 . VAL   B 1 77  ? 38.629 -21.632 11.759  1.00 20.27 ?  77  VAL   B HG21 1 
ATOM   5136 H HG22 . VAL   B 1 77  ? 39.549 -20.932 10.669  1.00 20.27 ?  77  VAL   B HG22 1 
ATOM   5137 H HG23 . VAL   B 1 77  ? 38.882 -20.065 11.821  1.00 20.27 ?  77  VAL   B HG23 1 
ATOM   5138 N N    . GLY   B 1 78  ? 36.737 -19.409 7.251   1.00 12.49 ?  78  GLY   B N    1 
ATOM   5139 C CA   . GLY   B 1 78  ? 35.764 -19.081 6.236   1.00 11.94 ?  78  GLY   B CA   1 
ATOM   5140 C C    . GLY   B 1 78  ? 36.008 -17.765 5.536   1.00 11.34 ?  78  GLY   B C    1 
ATOM   5141 O O    . GLY   B 1 78  ? 35.323 -17.475 4.550   1.00 11.58 ?  78  GLY   B O    1 
ATOM   5142 H H    . GLY   B 1 78  ? 37.440 -19.797 6.936   1.00 15.00 ?  78  GLY   B H    1 
ATOM   5143 H HA2  . GLY   B 1 78  ? 35.757 -19.776 5.565   1.00 14.34 ?  78  GLY   B HA2  1 
ATOM   5144 H HA3  . GLY   B 1 78  ? 34.884 -19.042 6.643   1.00 14.34 ?  78  GLY   B HA3  1 
ATOM   5145 N N    . GLY   B 1 79  ? 36.953 -16.960 6.025   1.00 11.55 ?  79  GLY   B N    1 
ATOM   5146 C CA   . GLY   B 1 79  ? 37.252 -15.666 5.450   1.00 11.41 ?  79  GLY   B CA   1 
ATOM   5147 C C    . GLY   B 1 79  ? 38.497 -15.683 4.570   1.00 10.75 ?  79  GLY   B C    1 
ATOM   5148 O O    . GLY   B 1 79  ? 39.113 -16.714 4.318   1.00 11.39 ?  79  GLY   B O    1 
ATOM   5149 H H    . GLY   B 1 79  ? 37.446 -17.153 6.696   1.00 13.87 ?  79  GLY   B H    1 
ATOM   5150 H HA2  . GLY   B 1 79  ? 36.499 -15.364 4.913   1.00 13.71 ?  79  GLY   B HA2  1 
ATOM   5151 H HA3  . GLY   B 1 79  ? 37.396 -15.022 6.159   1.00 13.71 ?  79  GLY   B HA3  1 
ATOM   5152 N N    . SER   B 1 80  ? 38.863 -14.489 4.098   1.00 11.00 ?  80  SER   B N    1 
ATOM   5153 C CA   . SER   B 1 80  ? 39.967 -14.343 3.158   1.00 10.88 ?  80  SER   B CA   1 
ATOM   5154 C C    . SER   B 1 80  ? 40.544 -12.935 3.224   1.00 10.80 ?  80  SER   B C    1 
ATOM   5155 O O    . SER   B 1 80  ? 39.924 -12.005 3.742   1.00 11.90 ?  80  SER   B O    1 
ATOM   5156 C CB   . SER   B 1 80  ? 39.518 -14.631 1.722   1.00 11.00 ?  80  SER   B CB   1 
ATOM   5157 O OG   . SER   B 1 80  ? 38.675 -13.603 1.221   1.00 11.87 ?  80  SER   B OG   1 
ATOM   5158 H H    . SER   B 1 80  ? 38.485 -13.744 4.306   1.00 13.22 ?  80  SER   B H    1 
ATOM   5159 H HA   . SER   B 1 80  ? 40.660 -14.975 3.400   1.00 13.08 ?  80  SER   B HA   1 
ATOM   5160 H HB2  . SER   B 1 80  ? 40.301 -14.689 1.152   1.00 13.22 ?  80  SER   B HB2  1 
ATOM   5161 H HB3  . SER   B 1 80  ? 39.035 -15.473 1.703   1.00 13.22 ?  80  SER   B HB3  1 
ATOM   5162 H HG   . SER   B 1 80  ? 37.981 -13.544 1.706   1.00 14.26 ?  80  SER   B HG   1 
ATOM   5163 N N    . CYS   B 1 81  ? 41.729 -12.787 2.640   1.00 10.54 ?  81  CYS   B N    1 
ATOM   5164 C CA   . CYS   B 1 81  ? 42.281 -11.477 2.329   1.00 10.50 ?  81  CYS   B CA   1 
ATOM   5165 C C    . CYS   B 1 81  ? 43.057 -11.560 1.022   1.00 10.01 ?  81  CYS   B C    1 
ATOM   5166 O O    . CYS   B 1 81  ? 43.567 -12.618 0.645   1.00 11.08 ?  81  CYS   B O    1 
ATOM   5167 C CB   . CYS   B 1 81  ? 43.169 -10.932 3.452   1.00 11.34 ?  81  CYS   B CB   1 
ATOM   5168 S SG   . CYS   B 1 81  ? 44.691 -11.861 3.706   1.00 11.90 ?  81  CYS   B SG   1 
ATOM   5169 H H    . CYS   B 1 81  ? 42.237 -13.443 2.404   1.00 12.66 ?  81  CYS   B H    1 
ATOM   5170 H HA   . CYS   B 1 81  ? 41.548 -10.854 2.201   1.00 12.62 ?  81  CYS   B HA   1 
ATOM   5171 H HB2  . CYS   B 1 81  ? 43.414 -10.014 3.242   1.00 13.62 ?  81  CYS   B HB2  1 
ATOM   5172 H HB3  . CYS   B 1 81  ? 42.667 -10.947 4.286   1.00 13.62 ?  81  CYS   B HB3  1 
ATOM   5173 H HG   . CYS   B 1 81  ? 45.315 -11.363 4.601   1.00 14.29 ?  81  CYS   B HG   1 
ATOM   5174 N N    . VAL   B 1 82  ? 43.154 -10.419 0.345   1.00 10.44 ?  82  VAL   B N    1 
ATOM   5175 C CA   . VAL   B 1 82  ? 43.917 -10.288 -0.893  1.00 10.62 ?  82  VAL   B CA   1 
ATOM   5176 C C    . VAL   B 1 82  ? 45.258 -9.650  -0.571  1.00 10.90 ?  82  VAL   B C    1 
ATOM   5177 O O    . VAL   B 1 82  ? 45.305 -8.535  -0.034  1.00 11.89 ?  82  VAL   B O    1 
ATOM   5178 C CB   . VAL   B 1 82  ? 43.169 -9.444  -1.935  1.00 11.81 ?  82  VAL   B CB   1 
ATOM   5179 C CG1  . VAL   B 1 82  ? 44.018 -9.268  -3.192  1.00 13.32 ?  82  VAL   B CG1  1 
ATOM   5180 C CG2  . VAL   B 1 82  ? 41.822 -10.055 -2.265  1.00 12.37 ?  82  VAL   B CG2  1 
ATOM   5181 H H    . VAL   B 1 82  ? 42.770 -9.685  0.586   1.00 12.55 ?  82  VAL   B H    1 
ATOM   5182 H HA   . VAL   B 1 82  ? 44.076 -11.169 -1.268  1.00 12.76 ?  82  VAL   B HA   1 
ATOM   5183 H HB   . VAL   B 1 82  ? 43.006 -8.567  -1.564  1.00 14.19 ?  82  VAL   B HB   1 
ATOM   5184 H HG11 . VAL   B 1 82  ? 43.454 -8.951  -3.913  1.00 16.00 ?  82  VAL   B HG11 1 
ATOM   5185 H HG12 . VAL   B 1 82  ? 44.719 -8.620  -3.013  1.00 16.00 ?  82  VAL   B HG12 1 
ATOM   5186 H HG13 . VAL   B 1 82  ? 44.411 -10.122 -3.432  1.00 16.00 ?  82  VAL   B HG13 1 
ATOM   5187 H HG21 . VAL   B 1 82  ? 41.387 -9.521  -2.948  1.00 14.86 ?  82  VAL   B HG21 1 
ATOM   5188 H HG22 . VAL   B 1 82  ? 41.953 -10.962 -2.593  1.00 14.86 ?  82  VAL   B HG22 1 
ATOM   5189 H HG23 . VAL   B 1 82  ? 41.273 -10.075 -1.464  1.00 14.86 ?  82  VAL   B HG23 1 
ATOM   5190 N N    . LEU   B 1 83  ? 46.342 -10.330 -0.942  1.00 10.32 ?  83  LEU   B N    1 
ATOM   5191 C CA   . LEU   B 1 83  ? 47.701 -9.821  -0.809  1.00 10.15 ?  83  LEU   B CA   1 
ATOM   5192 C C    . LEU   B 1 83  ? 48.407 -9.957  -2.159  1.00 10.08 ?  83  LEU   B C    1 
ATOM   5193 O O    . LEU   B 1 83  ? 47.806 -10.366 -3.159  1.00 10.48 ?  83  LEU   B O    1 
ATOM   5194 C CB   . LEU   B 1 83  ? 48.440 -10.501 0.352   1.00 10.80 ?  83  LEU   B CB   1 
ATOM   5195 C CG   . LEU   B 1 83  ? 47.932 -10.134 1.750   1.00 11.94 ?  83  LEU   B CG   1 
ATOM   5196 C CD1  . LEU   B 1 83  ? 48.561 -11.012 2.817   1.00 12.67 ?  83  LEU   B CD1  1 
ATOM   5197 C CD2  . LEU   B 1 83  ? 48.158 -8.654  2.067   1.00 12.96 ?  83  LEU   B CD2  1 
ATOM   5198 H H    . LEU   B 1 83  ? 46.307 -11.122 -1.284  1.00 12.41 ?  83  LEU   B H    1 
ATOM   5199 H HA   . LEU   B 1 83  ? 47.654 -8.879  -0.607  1.00 12.20 ?  83  LEU   B HA   1 
ATOM   5200 H HB2  . LEU   B 1 83  ? 48.362 -11.462 0.256   1.00 12.98 ?  83  LEU   B HB2  1 
ATOM   5201 H HB3  . LEU   B 1 83  ? 49.380 -10.250 0.310   1.00 12.98 ?  83  LEU   B HB3  1 
ATOM   5202 H HG   . LEU   B 1 83  ? 46.978 -10.291 1.775   1.00 14.34 ?  83  LEU   B HG   1 
ATOM   5203 H HD11 . LEU   B 1 83  ? 48.210 -10.758 3.685   1.00 15.21 ?  83  LEU   B HD11 1 
ATOM   5204 H HD12 . LEU   B 1 83  ? 48.334 -11.941 2.633   1.00 15.21 ?  83  LEU   B HD12 1 
ATOM   5205 H HD13 . LEU   B 1 83  ? 49.522 -10.899 2.800   1.00 15.21 ?  83  LEU   B HD13 1 
ATOM   5206 H HD21 . LEU   B 1 83  ? 47.956 -8.498  3.004   1.00 15.57 ?  83  LEU   B HD21 1 
ATOM   5207 H HD22 . LEU   B 1 83  ? 49.083 -8.429  1.886   1.00 15.57 ?  83  LEU   B HD22 1 
ATOM   5208 H HD23 . LEU   B 1 83  ? 47.571 -8.119  1.510   1.00 15.57 ?  83  LEU   B HD23 1 
ATOM   5209 N N    . SER   B 1 84  ? 49.679 -9.581  -2.211  1.00 11.21 ?  84  SER   B N    1 
ATOM   5210 C CA   . SER   B 1 84  ? 50.411 -9.686  -3.463  1.00 11.76 ?  84  SER   B CA   1 
ATOM   5211 C C    . SER   B 1 84  ? 50.568 -11.144 -3.888  1.00 10.95 ?  84  SER   B C    1 
ATOM   5212 O O    . SER   B 1 84  ? 50.681 -12.052 -3.064  1.00 10.76 ?  84  SER   B O    1 
ATOM   5213 C CB   . SER   B 1 84  ? 51.807 -9.082  -3.313  1.00 13.93 ?  84  SER   B CB   1 
ATOM   5214 O OG   . SER   B 1 84  ? 52.560 -9.289  -4.494  1.00 15.46 ?  84  SER   B OG   1 
ATOM   5215 H H    . SER   B 1 84  ? 50.132 -9.257  -1.551  1.00 13.46 ?  84  SER   B H    1 
ATOM   5216 H HA   . SER   B 1 84  ? 49.939 -9.207  -4.161  1.00 14.13 ?  84  SER   B HA   1 
ATOM   5217 H HB2  . SER   B 1 84  ? 51.724 -8.125  -3.146  1.00 16.73 ?  84  SER   B HB2  1 
ATOM   5218 H HB3  . SER   B 1 84  ? 52.265 -9.507  -2.574  1.00 16.73 ?  84  SER   B HB3  1 
ATOM   5219 H HG   . SER   B 1 84  ? 53.322 -8.942  -4.418  1.00 18.57 ?  84  SER   B HG   1 
ATOM   5220 N N    . GLY   B 1 85  ? 50.625 -11.352 -5.199  1.00 11.82 ?  85  GLY   B N    1 
ATOM   5221 C CA   . GLY   B 1 85  ? 50.973 -12.637 -5.755  1.00 12.26 ?  85  GLY   B CA   1 
ATOM   5222 C C    . GLY   B 1 85  ? 52.443 -12.839 -6.049  1.00 11.86 ?  85  GLY   B C    1 
ATOM   5223 O O    . GLY   B 1 85  ? 52.824 -13.920 -6.502  1.00 11.95 ?  85  GLY   B O    1 
ATOM   5224 H H    . GLY   B 1 85  ? 50.476 -10.752 -5.790  1.00 14.20 ?  85  GLY   B H    1 
ATOM   5225 H HA2  . GLY   B 1 85  ? 50.697 -13.335 -5.138  1.00 14.73 ?  85  GLY   B HA2  1 
ATOM   5226 H HA3  . GLY   B 1 85  ? 50.491 -12.765 -6.582  1.00 14.73 ?  85  GLY   B HA3  1 
ATOM   5227 N N    . HIS   B 1 86  ? 53.299 -11.850 -5.807  1.00 11.59 ?  86  HIS   B N    1 
ATOM   5228 C CA   . HIS   B 1 86  ? 54.761 -12.025 -5.894  1.00 11.51 ?  86  HIS   B CA   1 
ATOM   5229 C C    . HIS   B 1 86  ? 55.128 -12.533 -7.287  1.00 11.81 ?  86  HIS   B C    1 
ATOM   5230 O O    . HIS   B 1 86  ? 54.743 -11.911 -8.290  1.00 12.62 ?  86  HIS   B O    1 
ATOM   5231 C CB   . HIS   B 1 86  ? 55.260 -12.865 -4.720  1.00 11.98 ?  86  HIS   B CB   1 
ATOM   5232 C CG   . HIS   B 1 86  ? 54.940 -12.263 -3.396  1.00 12.45 ?  86  HIS   B CG   1 
ATOM   5233 N ND1  . HIS   B 1 86  ? 55.771 -11.360 -2.769  1.00 13.65 ?  86  HIS   B ND1  1 
ATOM   5234 C CD2  . HIS   B 1 86  ? 53.862 -12.414 -2.590  1.00 12.42 ?  86  HIS   B CD2  1 
ATOM   5235 C CE1  . HIS   B 1 86  ? 55.212 -10.973 -1.638  1.00 13.68 ?  86  HIS   B CE1  1 
ATOM   5236 N NE2  . HIS   B 1 86  ? 54.054 -11.596 -1.505  1.00 12.88 ?  86  HIS   B NE2  1 
ATOM   5237 H H    . HIS   B 1 86  ? 53.064 -11.055 -5.593  1.00 13.93 ?  86  HIS   B H    1 
ATOM   5238 H HA   . HIS   B 1 86  ? 55.172 -11.151 -5.802  1.00 13.83 ?  86  HIS   B HA   1 
ATOM   5239 H HB2  . HIS   B 1 86  ? 54.853 -13.741 -4.761  1.00 14.39 ?  86  HIS   B HB2  1 
ATOM   5240 H HB3  . HIS   B 1 86  ? 56.229 -12.948 -4.780  1.00 14.39 ?  86  HIS   B HB3  1 
ATOM   5241 H HD2  . HIS   B 1 86  ? 53.117 -12.953 -2.754  1.00 14.92 ?  86  HIS   B HD2  1 
ATOM   5242 H HE1  . HIS   B 1 86  ? 55.578 -10.381 -1.023  1.00 16.43 ?  86  HIS   B HE1  1 
ATOM   5243 H HE2  . HIS   B 1 86  ? 53.511 -11.516 -0.840  1.00 15.47 ?  86  HIS   B HE2  1 
ATOM   5244 N N    . ASN   B 1 87  ? 55.897 -13.611 -7.402  1.00 12.30 ?  87  ASN   B N    1 
ATOM   5245 C CA   . ASN   B 1 87  ? 56.291 -14.180 -8.681  1.00 12.89 ?  87  ASN   B CA   1 
ATOM   5246 C C    . ASN   B 1 87  ? 55.311 -15.227 -9.187  1.00 12.64 ?  87  ASN   B C    1 
ATOM   5247 O O    . ASN   B 1 87  ? 55.627 -15.940 -10.144 1.00 14.48 ?  87  ASN   B O    1 
ATOM   5248 C CB   . ASN   B 1 87  ? 57.686 -14.802 -8.564  1.00 14.87 ?  87  ASN   B CB   1 
ATOM   5249 C CG   . ASN   B 1 87  ? 57.741 -15.932 -7.539  1.00 15.89 ?  87  ASN   B CG   1 
ATOM   5250 O OD1  . ASN   B 1 87  ? 57.108 -15.862 -6.482  1.00 15.11 ?  87  ASN   B OD1  1 
ATOM   5251 N ND2  . ASN   B 1 87  ? 58.469 -17.000 -7.869  1.00 18.24 ?  87  ASN   B ND2  1 
ATOM   5252 H H    . ASN   B 1 87  ? 56.216 -14.047 -6.730  1.00 14.78 ?  87  ASN   B H    1 
ATOM   5253 H HA   . ASN   B 1 87  ? 56.337 -13.467 -9.340  1.00 15.49 ?  87  ASN   B HA   1 
ATOM   5254 H HB2  . ASN   B 1 87  ? 57.944 -15.164 -9.430  1.00 17.85 ?  87  ASN   B HB2  1 
ATOM   5255 H HB3  . ASN   B 1 87  ? 58.318 -14.117 -8.294  1.00 17.85 ?  87  ASN   B HB3  1 
ATOM   5256 H HD21 . ASN   B 1 87  ? 58.528 -17.660 -7.328  1.00 21.90 ?  87  ASN   B HD21 1 
ATOM   5257 H HD22 . ASN   B 1 87  ? 58.888 -17.018 -8.623  1.00 21.90 ?  87  ASN   B HD22 1 
ATOM   5258 N N    . LEU   B 1 88  ? 54.131 -15.330 -8.573  1.00 11.82 ?  88  LEU   B N    1 
ATOM   5259 C CA   . LEU   B 1 88  ? 53.153 -16.365 -8.898  1.00 11.96 ?  88  LEU   B CA   1 
ATOM   5260 C C    . LEU   B 1 88  ? 51.917 -15.853 -9.616  1.00 11.52 ?  88  LEU   B C    1 
ATOM   5261 O O    . LEU   B 1 88  ? 51.312 -16.605 -10.387 1.00 13.25 ?  88  LEU   B O    1 
ATOM   5262 C CB   . LEU   B 1 88  ? 52.686 -17.057 -7.613  1.00 12.81 ?  88  LEU   B CB   1 
ATOM   5263 C CG   . LEU   B 1 88  ? 53.802 -17.697 -6.796  1.00 15.17 ?  88  LEU   B CG   1 
ATOM   5264 C CD1  . LEU   B 1 88  ? 53.274 -18.125 -5.439  1.00 16.84 ?  88  LEU   B CD1  1 
ATOM   5265 C CD2  . LEU   B 1 88  ? 54.383 -18.867 -7.556  1.00 18.36 ?  88  LEU   B CD2  1 
ATOM   5266 H H    . LEU   B 1 88  ? 53.873 -14.800 -7.941  1.00 14.20 ?  88  LEU   B H    1 
ATOM   5267 H HA   . LEU   B 1 88  ? 53.573 -17.026 -9.461  1.00 14.37 ?  88  LEU   B HA   1 
ATOM   5268 H HB2  . LEU   B 1 88  ? 52.244 -16.405 -7.047  1.00 15.39 ?  88  LEU   B HB2  1 
ATOM   5269 H HB3  . LEU   B 1 88  ? 52.060 -17.759 -7.851  1.00 15.39 ?  88  LEU   B HB3  1 
ATOM   5270 H HG   . LEU   B 1 88  ? 54.505 -17.042 -6.652  1.00 18.22 ?  88  LEU   B HG   1 
ATOM   5271 H HD11 . LEU   B 1 88  ? 53.930 -18.692 -5.007  1.00 20.23 ?  88  LEU   B HD11 1 
ATOM   5272 H HD12 . LEU   B 1 88  ? 53.108 -17.337 -4.897  1.00 20.23 ?  88  LEU   B HD12 1 
ATOM   5273 H HD13 . LEU   B 1 88  ? 52.445 -18.615 -5.567  1.00 20.23 ?  88  LEU   B HD13 1 
ATOM   5274 H HD21 . LEU   B 1 88  ? 55.010 -19.331 -6.981  1.00 22.05 ?  88  LEU   B HD21 1 
ATOM   5275 H HD22 . LEU   B 1 88  ? 53.664 -19.461 -7.814  1.00 22.05 ?  88  LEU   B HD22 1 
ATOM   5276 H HD23 . LEU   B 1 88  ? 54.840 -18.534 -8.344  1.00 22.05 ?  88  LEU   B HD23 1 
ATOM   5277 N N    . ALA   B 1 89  ? 51.513 -14.614 -9.360  1.00 10.70 ?  89  ALA   B N    1 
ATOM   5278 C CA   . ALA   B 1 89  ? 50.215 -14.124 -9.797  1.00 10.25 ?  89  ALA   B CA   1 
ATOM   5279 C C    . ALA   B 1 89  ? 50.190 -12.630 -9.524  1.00 10.94 ?  89  ALA   B C    1 
ATOM   5280 O O    . ALA   B 1 89  ? 51.033 -12.109 -8.794  1.00 11.72 ?  89  ALA   B O    1 
ATOM   5281 C CB   . ALA   B 1 89  ? 49.082 -14.795 -9.024  1.00 10.68 ?  89  ALA   B CB   1 
ATOM   5282 H H    . ALA   B 1 89  ? 51.974 -14.025 -8.924  1.00 12.86 ?  89  ALA   B H    1 
ATOM   5283 H HA   . ALA   B 1 89  ? 50.093 -14.277 -10.745 1.00 12.32 ?  89  ALA   B HA   1 
ATOM   5284 H HB1  . ALA   B 1 89  ? 48.231 -14.461 -9.354  1.00 12.84 ?  89  ALA   B HB1  1 
ATOM   5285 H HB2  . ALA   B 1 89  ? 49.133 -15.755 -9.166  1.00 12.84 ?  89  ALA   B HB2  1 
ATOM   5286 H HB3  . ALA   B 1 89  ? 49.176 -14.594 -8.083  1.00 12.84 ?  89  ALA   B HB3  1 
ATOM   5287 N N    . LYS   B 1 90  ? 49.189 -11.945 -10.077 1.00 11.79 ?  90  LYS   B N    1 
ATOM   5288 C CA   . LYS   B 1 90  ? 48.998 -10.554 -9.681  1.00 11.91 ?  90  LYS   B CA   1 
ATOM   5289 C C    . LYS   B 1 90  ? 48.686 -10.472 -8.193  1.00 11.68 ?  90  LYS   B C    1 
ATOM   5290 O O    . LYS   B 1 90  ? 49.340 -9.730  -7.446  1.00 13.05 ?  90  LYS   B O    1 
ATOM   5291 C CB   . LYS   B 1 90  ? 47.920 -9.887  -10.535 1.00 13.55 ?  90  LYS   B CB   1 
ATOM   5292 C CG   . LYS   B 1 90  ? 47.649 -8.435  -10.168 1.00 14.56 ?  90  LYS   B CG   1 
ATOM   5293 C CD   . LYS   B 1 90  ? 48.870 -7.557  -10.275 1.00 18.12 ?  90  LYS   B CD   1 
ATOM   5294 C CE   . LYS   B 1 90  ? 48.463 -6.114  -10.073 1.00 20.46 ?  90  LYS   B CE   1 
ATOM   5295 N NZ   . LYS   B 1 90  ? 49.636 -5.215  -9.945  1.00 20.45 ?  90  LYS   B NZ   1 
ATOM   5296 H H    . LYS   B 1 90  ? 48.628 -12.249 -10.659 1.00 14.16 ?  90  LYS   B H    1 
ATOM   5297 H HA   . LYS   B 1 90  ? 49.822 -10.078 -9.830  1.00 14.31 ?  90  LYS   B HA   1 
ATOM   5298 H HB2  . LYS   B 1 90  ? 48.203 -9.905  -11.467 1.00 16.28 ?  90  LYS   B HB2  1 
ATOM   5299 H HB3  . LYS   B 1 90  ? 47.088 -10.378 -10.442 1.00 16.28 ?  90  LYS   B HB3  1 
ATOM   5300 H HG2  . LYS   B 1 90  ? 46.971 -8.080  -10.767 1.00 17.49 ?  90  LYS   B HG2  1 
ATOM   5301 H HG3  . LYS   B 1 90  ? 47.325 -8.396  -9.252  1.00 17.49 ?  90  LYS   B HG3  1 
ATOM   5302 H HD2  . LYS   B 1 90  ? 49.509 -7.800  -9.584  1.00 21.76 ?  90  LYS   B HD2  1 
ATOM   5303 H HD3  . LYS   B 1 90  ? 49.266 -7.652  -11.155 1.00 21.76 ?  90  LYS   B HD3  1 
ATOM   5304 H HE2  . LYS   B 1 90  ? 47.944 -5.815  -10.838 1.00 24.56 ?  90  LYS   B HE2  1 
ATOM   5305 H HE3  . LYS   B 1 90  ? 47.940 -6.034  -9.262  1.00 24.56 ?  90  LYS   B HE3  1 
ATOM   5306 H HZ1  . LYS   B 1 90  ? 49.372 -4.370  -9.830  1.00 24.56 ?  90  LYS   B HZ1  1 
ATOM   5307 H HZ2  . LYS   B 1 90  ? 50.136 -5.454  -9.247  1.00 24.56 ?  90  LYS   B HZ2  1 
ATOM   5308 H HZ3  . LYS   B 1 90  ? 50.140 -5.255  -10.682 1.00 24.56 ?  90  LYS   B HZ3  1 
ATOM   5309 N N    . HIS   B 1 91  ? 47.731 -11.287 -7.739  1.00 10.40 ?  91  HIS   B N    1 
ATOM   5310 C CA   . HIS   B 1 91  ? 47.277 -11.310 -6.361  1.00 10.60 ?  91  HIS   B CA   1 
ATOM   5311 C C    . HIS   B 1 91  ? 47.278 -12.741 -5.843  1.00 10.08 ?  91  HIS   B C    1 
ATOM   5312 O O    . HIS   B 1 91  ? 47.037 -13.694 -6.594  1.00 10.51 ?  91  HIS   B O    1 
ATOM   5313 C CB   . HIS   B 1 91  ? 45.823 -10.841 -6.250  1.00 11.95 ?  91  HIS   B CB   1 
ATOM   5314 C CG   . HIS   B 1 91  ? 45.601 -9.438  -6.698  1.00 15.75 ?  91  HIS   B CG   1 
ATOM   5315 N ND1  . HIS   B 1 91  ? 46.178 -8.351  -6.075  1.00 18.40 ?  91  HIS   B ND1  1 
ATOM   5316 C CD2  . HIS   B 1 91  ? 44.834 -8.940  -7.691  1.00 18.25 ?  91  HIS   B CD2  1 
ATOM   5317 C CE1  . HIS   B 1 91  ? 45.789 -7.243  -6.680  1.00 19.41 ?  91  HIS   B CE1  1 
ATOM   5318 N NE2  . HIS   B 1 91  ? 44.971 -7.574  -7.664  1.00 19.57 ?  91  HIS   B NE2  1 
ATOM   5319 H H    . HIS   B 1 91  ? 47.316 -11.861 -8.233  1.00 12.49 ?  91  HIS   B H    1 
ATOM   5320 H HA   . HIS   B 1 91  ? 47.843 -10.753 -5.801  1.00 12.74 ?  91  HIS   B HA   1 
ATOM   5321 H HB2  . HIS   B 1 91  ? 45.265 -11.418 -6.797  1.00 14.36 ?  91  HIS   B HB2  1 
ATOM   5322 H HB3  . HIS   B 1 91  ? 45.542 -10.904 -5.321  1.00 14.36 ?  91  HIS   B HB3  1 
ATOM   5323 H HD1  . HIS   B 1 91  ? 46.711 -8.389  -5.401  1.00 22.09 ?  91  HIS   B HD1  1 
ATOM   5324 H HD2  . HIS   B 1 91  ? 44.319 -9.423  -8.292  1.00 21.91 ?  91  HIS   B HD2  1 
ATOM   5325 H HE1  . HIS   B 1 91  ? 46.048 -6.378  -6.448  1.00 23.31 ?  91  HIS   B HE1  1 
ATOM   5326 N N    . CYS   B 1 92  ? 47.474 -12.880 -4.535  1.00 10.02 ?  92  CYS   B N    1 
ATOM   5327 C CA   . CYS   B 1 92  ? 47.171 -14.117 -3.825  1.00 9.54  ?  92  CYS   B CA   1 
ATOM   5328 C C    . CYS   B 1 92  ? 45.949 -13.884 -2.941  1.00 9.24  ?  92  CYS   B C    1 
ATOM   5329 O O    . CYS   B 1 92  ? 45.948 -12.990 -2.085  1.00 10.30 ?  92  CYS   B O    1 
ATOM   5330 C CB   . CYS   B 1 92  ? 48.354 -14.578 -2.976  1.00 10.09 ?  92  CYS   B CB   1 
ATOM   5331 S SG   . CYS   B 1 92  ? 47.995 -16.119 -2.078  1.00 10.29 ?  92  CYS   B SG   1 
ATOM   5332 H H    . CYS   B 1 92  ? 47.794 -12.260 -4.026  1.00 12.04 ?  92  CYS   B H    1 
ATOM   5333 H HA   . CYS   B 1 92  ? 46.970 -14.814 -4.472  1.00 11.46 ?  92  CYS   B HA   1 
ATOM   5334 H HB2  . CYS   B 1 92  ? 49.119 -14.731 -3.547  1.00 12.12 ?  92  CYS   B HB2  1 
ATOM   5335 H HB3  . CYS   B 1 92  ? 48.555 -13.892 -2.319  1.00 12.12 ?  92  CYS   B HB3  1 
ATOM   5336 H HG   . CYS   B 1 92  ? 48.964 -16.434 -1.450  1.00 12.36 ?  92  CYS   B HG   1 
ATOM   5337 N N    . LEU   B 1 93  ? 44.913 -14.689 -3.155  1.00 9.49  ?  93  LEU   B N    1 
ATOM   5338 C CA   . LEU   B 1 93  ? 43.737 -14.712 -2.296  1.00 9.79  ?  93  LEU   B CA   1 
ATOM   5339 C C    . LEU   B 1 93  ? 43.963 -15.772 -1.226  1.00 9.04  ?  93  LEU   B C    1 
ATOM   5340 O O    . LEU   B 1 93  ? 43.913 -16.975 -1.513  1.00 9.48  ?  93  LEU   B O    1 
ATOM   5341 C CB   . LEU   B 1 93  ? 42.479 -15.011 -3.106  1.00 10.01 ?  93  LEU   B CB   1 
ATOM   5342 C CG   . LEU   B 1 93  ? 41.180 -15.017 -2.297  1.00 10.46 ?  93  LEU   B CG   1 
ATOM   5343 C CD1  . LEU   B 1 93  ? 40.830 -13.628 -1.795  1.00 10.97 ?  93  LEU   B CD1  1 
ATOM   5344 C CD2  . LEU   B 1 93  ? 40.043 -15.599 -3.119  1.00 10.45 ?  93  LEU   B CD2  1 
ATOM   5345 H H    . LEU   B 1 93  ? 44.870 -15.258 -3.812  1.00 11.41 ?  93  LEU   B H    1 
ATOM   5346 H HA   . LEU   B 1 93  ? 43.637 -13.849 -1.869  1.00 11.76 ?  93  LEU   B HA   1 
ATOM   5347 H HB2  . LEU   B 1 93  ? 42.387 -14.331 -3.796  1.00 12.03 ?  93  LEU   B HB2  1 
ATOM   5348 H HB3  . LEU   B 1 93  ? 42.571 -15.880 -3.517  1.00 12.03 ?  93  LEU   B HB3  1 
ATOM   5349 H HG   . LEU   B 1 93  ? 41.299 -15.585 -1.524  1.00 12.56 ?  93  LEU   B HG   1 
ATOM   5350 H HD11 . LEU   B 1 93  ? 39.973 -13.663 -1.348  1.00 13.18 ?  93  LEU   B HD11 1 
ATOM   5351 H HD12 . LEU   B 1 93  ? 41.518 -13.337 -1.174  1.00 13.18 ?  93  LEU   B HD12 1 
ATOM   5352 H HD13 . LEU   B 1 93  ? 40.789 -13.021 -2.551  1.00 13.18 ?  93  LEU   B HD13 1 
ATOM   5353 H HD21 . LEU   B 1 93  ? 39.232 -15.588 -2.587  1.00 12.55 ?  93  LEU   B HD21 1 
ATOM   5354 H HD22 . LEU   B 1 93  ? 39.921 -15.061 -3.918  1.00 12.55 ?  93  LEU   B HD22 1 
ATOM   5355 H HD23 . LEU   B 1 93  ? 40.265 -16.511 -3.365  1.00 12.55 ?  93  LEU   B HD23 1 
ATOM   5356 N N    . HIS   B 1 94  ? 44.239 -15.334 -0.005  1.00 8.80  ?  94  HIS   B N    1 
ATOM   5357 C CA   . HIS   B 1 94  ? 44.456 -16.243 1.111   1.00 9.14  ?  94  HIS   B CA   1 
ATOM   5358 C C    . HIS   B 1 94  ? 43.096 -16.602 1.688   1.00 9.32  ?  94  HIS   B C    1 
ATOM   5359 O O    . HIS   B 1 94  ? 42.428 -15.734 2.249   1.00 10.81 ?  94  HIS   B O    1 
ATOM   5360 C CB   . HIS   B 1 94  ? 45.326 -15.566 2.167   1.00 9.59  ?  94  HIS   B CB   1 
ATOM   5361 C CG   . HIS   B 1 94  ? 46.713 -15.263 1.697   1.00 9.52  ?  94  HIS   B CG   1 
ATOM   5362 N ND1  . HIS   B 1 94  ? 47.744 -16.173 1.788   1.00 9.75  ?  94  HIS   B ND1  1 
ATOM   5363 C CD2  . HIS   B 1 94  ? 47.226 -14.151 1.114   1.00 9.95  ?  94  HIS   B CD2  1 
ATOM   5364 C CE1  . HIS   B 1 94  ? 48.831 -15.625 1.275   1.00 9.84  ?  94  HIS   B CE1  1 
ATOM   5365 N NE2  . HIS   B 1 94  ? 48.547 -14.400 0.862   1.00 10.08 ?  94  HIS   B NE2  1 
ATOM   5366 H H    . HIS   B 1 94  ? 44.309 -14.496 0.203   1.00 10.57 ?  94  HIS   B H    1 
ATOM   5367 H HA   . HIS   B 1 94  ? 44.894 -17.049 0.798   1.00 10.99 ?  94  HIS   B HA   1 
ATOM   5368 H HB2  . HIS   B 1 94  ? 44.909 -14.735 2.428   1.00 11.53 ?  94  HIS   B HB2  1 
ATOM   5369 H HB3  . HIS   B 1 94  ? 45.393 -16.160 2.933   1.00 11.53 ?  94  HIS   B HB3  1 
ATOM   5370 H HD2  . HIS   B 1 94  ? 46.765 -13.369 0.921   1.00 11.95 ?  94  HIS   B HD2  1 
ATOM   5371 H HE1  . HIS   B 1 94  ? 49.666 -16.038 1.226   1.00 11.83 ?  94  HIS   B HE1  1 
ATOM   5372 H HE2  . HIS   B 1 94  ? 49.105 -13.855 0.507   1.00 12.12 ?  94  HIS   B HE2  1 
ATOM   5373 N N    . VAL   B 1 95  ? 42.666 -17.858 1.541   1.00 9.32  ?  95  VAL   B N    1 
ATOM   5374 C CA   . VAL   B 1 95  ? 41.339 -18.304 1.974   1.00 9.45  ?  95  VAL   B CA   1 
ATOM   5375 C C    . VAL   B 1 95  ? 41.505 -19.341 3.071   1.00 9.82  ?  95  VAL   B C    1 
ATOM   5376 O O    . VAL   B 1 95  ? 42.272 -20.295 2.910   1.00 10.37 ?  95  VAL   B O    1 
ATOM   5377 C CB   . VAL   B 1 95  ? 40.528 -18.905 0.810   1.00 9.86  ?  95  VAL   B CB   1 
ATOM   5378 C CG1  . VAL   B 1 95  ? 39.153 -19.359 1.295   1.00 11.15 ?  95  VAL   B CG1  1 
ATOM   5379 C CG2  . VAL   B 1 95  ? 40.388 -17.914 -0.337  1.00 9.97  ?  95  VAL   B CG2  1 
ATOM   5380 H H    . VAL   B 1 95  ? 43.128 -18.488 1.180   1.00 11.20 ?  95  VAL   B H    1 
ATOM   5381 H HA   . VAL   B 1 95  ? 40.839 -17.554 2.332   1.00 11.36 ?  95  VAL   B HA   1 
ATOM   5382 H HB   . VAL   B 1 95  ? 40.990 -19.684 0.468   1.00 11.85 ?  95  VAL   B HB   1 
ATOM   5383 H HG11 . VAL   B 1 95  ? 38.588 -19.545 0.521   1.00 13.39 ?  95  VAL   B HG11 1 
ATOM   5384 H HG12 . VAL   B 1 95  ? 39.249 -20.165 1.824   1.00 13.39 ?  95  VAL   B HG12 1 
ATOM   5385 H HG13 . VAL   B 1 95  ? 38.752 -18.655 1.825   1.00 13.39 ?  95  VAL   B HG13 1 
ATOM   5386 H HG21 . VAL   B 1 95  ? 39.817 -18.301 -1.024  1.00 11.98 ?  95  VAL   B HG21 1 
ATOM   5387 H HG22 . VAL   B 1 95  ? 39.983 -17.097 -0.001  1.00 11.98 ?  95  VAL   B HG22 1 
ATOM   5388 H HG23 . VAL   B 1 95  ? 41.263 -17.727 -0.701  1.00 11.98 ?  95  VAL   B HG23 1 
ATOM   5389 N N    . VAL   B 1 96  ? 40.767 -19.173 4.165   1.00 10.19 ?  96  VAL   B N    1 
ATOM   5390 C CA   . VAL   B 1 96  ? 40.847 -20.087 5.303   1.00 10.55 ?  96  VAL   B CA   1 
ATOM   5391 C C    . VAL   B 1 96  ? 39.659 -21.045 5.255   1.00 10.94 ?  96  VAL   B C    1 
ATOM   5392 O O    . VAL   B 1 96  ? 38.538 -20.689 5.629   1.00 11.73 ?  96  VAL   B O    1 
ATOM   5393 C CB   . VAL   B 1 96  ? 40.906 -19.343 6.639   1.00 11.20 ?  96  VAL   B CB   1 
ATOM   5394 C CG1  . VAL   B 1 96  ? 41.098 -20.341 7.775   1.00 11.88 ?  96  VAL   B CG1  1 
ATOM   5395 C CG2  . VAL   B 1 96  ? 42.018 -18.308 6.638   1.00 11.75 ?  96  VAL   B CG2  1 
ATOM   5396 H H    . VAL   B 1 96  ? 40.209 -18.531 4.277   1.00 12.24 ?  96  VAL   B H    1 
ATOM   5397 H HA   . VAL   B 1 96  ? 41.655 -20.618 5.225   1.00 12.68 ?  96  VAL   B HA   1 
ATOM   5398 H HB   . VAL   B 1 96  ? 40.066 -18.884 6.787   1.00 13.46 ?  96  VAL   B HB   1 
ATOM   5399 H HG11 . VAL   B 1 96  ? 41.288 -19.853 8.596   1.00 14.28 ?  96  VAL   B HG11 1 
ATOM   5400 H HG12 . VAL   B 1 96  ? 40.293 -20.865 7.885   1.00 14.28 ?  96  VAL   B HG12 1 
ATOM   5401 H HG13 . VAL   B 1 96  ? 41.849 -20.922 7.565   1.00 14.28 ?  96  VAL   B HG13 1 
ATOM   5402 H HG21 . VAL   B 1 96  ? 42.079 -17.906 7.521   1.00 14.11 ?  96  VAL   B HG21 1 
ATOM   5403 H HG22 . VAL   B 1 96  ? 42.855 -18.740 6.414   1.00 14.11 ?  96  VAL   B HG22 1 
ATOM   5404 H HG23 . VAL   B 1 96  ? 41.812 -17.623 5.981   1.00 14.11 ?  96  VAL   B HG23 1 
ATOM   5405 N N    . GLY   B 1 97  ? 39.899 -22.281 4.829   1.00 10.91 ?  97  GLY   B N    1 
ATOM   5406 C CA   . GLY   B 1 97  ? 38.924 -23.336 4.984   1.00 11.68 ?  97  GLY   B CA   1 
ATOM   5407 C C    . GLY   B 1 97  ? 39.039 -23.946 6.364   1.00 12.12 ?  97  GLY   B C    1 
ATOM   5408 O O    . GLY   B 1 97  ? 40.078 -23.818 7.026   1.00 12.60 ?  97  GLY   B O    1 
ATOM   5409 H H    . GLY   B 1 97  ? 40.632 -22.527 4.445   1.00 13.10 ?  97  GLY   B H    1 
ATOM   5410 H HA2  . GLY   B 1 97  ? 38.033 -22.974 4.860   1.00 14.04 ?  97  GLY   B HA2  1 
ATOM   5411 H HA3  . GLY   B 1 97  ? 39.077 -24.026 4.315   1.00 14.04 ?  97  GLY   B HA3  1 
ATOM   5412 N N    . PRO   B 1 98  ? 37.989 -24.631 6.827   1.00 12.93 ?  98  PRO   B N    1 
ATOM   5413 C CA   . PRO   B 1 98  ? 38.081 -25.332 8.111   1.00 13.66 ?  98  PRO   B CA   1 
ATOM   5414 C C    . PRO   B 1 98  ? 39.109 -26.453 8.062   1.00 13.25 ?  98  PRO   B C    1 
ATOM   5415 O O    . PRO   B 1 98  ? 39.213 -27.188 7.081   1.00 13.70 ?  98  PRO   B O    1 
ATOM   5416 C CB   . PRO   B 1 98  ? 36.662 -25.877 8.311   1.00 13.99 ?  98  PRO   B CB   1 
ATOM   5417 C CG   . PRO   B 1 98  ? 36.116 -26.011 6.933   1.00 13.69 ?  98  PRO   B CG   1 
ATOM   5418 C CD   . PRO   B 1 98  ? 36.678 -24.833 6.185   1.00 12.98 ?  98  PRO   B CD   1 
ATOM   5419 H HA   . PRO   B 1 98  ? 38.307 -24.711 8.818   1.00 16.41 ?  98  PRO   B HA   1 
ATOM   5420 H HB2  . PRO   B 1 98  ? 36.708 -26.739 8.753   1.00 16.80 ?  98  PRO   B HB2  1 
ATOM   5421 H HB3  . PRO   B 1 98  ? 36.145 -25.246 8.828   1.00 16.80 ?  98  PRO   B HB3  1 
ATOM   5422 H HG2  . PRO   B 1 98  ? 36.422 -26.847 6.539   1.00 16.45 ?  98  PRO   B HG2  1 
ATOM   5423 H HG3  . PRO   B 1 98  ? 35.150 -25.977 6.959   1.00 16.45 ?  98  PRO   B HG3  1 
ATOM   5424 H HD2  . PRO   B 1 98  ? 36.783 -25.045 5.241   1.00 15.59 ?  98  PRO   B HD2  1 
ATOM   5425 H HD3  . PRO   B 1 98  ? 36.120 -24.049 6.311   1.00 15.59 ?  98  PRO   B HD3  1 
ATOM   5426 N N    . ASN   B 1 99  ? 39.872 -26.579 9.142   1.00 14.17 ?  99  ASN   B N    1 
ATOM   5427 C CA   . ASN   B 1 99  ? 40.852 -27.651 9.299   1.00 14.87 ?  99  ASN   B CA   1 
ATOM   5428 C C    . ASN   B 1 99  ? 40.218 -28.734 10.173  1.00 17.16 ?  99  ASN   B C    1 
ATOM   5429 O O    . ASN   B 1 99  ? 40.131 -28.590 11.395  1.00 17.94 ?  99  ASN   B O    1 
ATOM   5430 C CB   . ASN   B 1 99  ? 42.125 -27.094 9.921   1.00 15.01 ?  99  ASN   B CB   1 
ATOM   5431 C CG   . ASN   B 1 99  ? 43.247 -28.106 9.951   1.00 16.27 ?  99  ASN   B CG   1 
ATOM   5432 O OD1  . ASN   B 1 99  ? 43.010 -29.296 10.122  1.00 17.19 ?  99  ASN   B OD1  1 
ATOM   5433 N ND2  . ASN   B 1 99  ? 44.476 -27.639 9.784   1.00 16.71 ?  99  ASN   B ND2  1 
ATOM   5434 H H    . ASN   B 1 99  ? 39.842 -26.042 9.813   1.00 17.02 ?  99  ASN   B H    1 
ATOM   5435 H HA   . ASN   B 1 99  ? 41.066 -28.034 8.434   1.00 17.86 ?  99  ASN   B HA   1 
ATOM   5436 H HB2  . ASN   B 1 99  ? 42.421 -26.333 9.411   1.00 18.02 ?  99  ASN   B HB2  1 
ATOM   5437 H HB3  . ASN   B 1 99  ? 41.934 -26.832 10.838  1.00 18.02 ?  99  ASN   B HB3  1 
ATOM   5438 H HD21 . ASN   B 1 99  ? 45.147 -28.179 9.793   1.00 20.07 ?  99  ASN   B HD21 1 
ATOM   5439 H HD22 . ASN   B 1 99  ? 44.600 -26.799 9.671   1.00 20.07 ?  99  ASN   B HD22 1 
ATOM   5440 N N    A VAL   B 1 100 ? 39.755 -29.815 9.536   0.62 18.82 ?  100 VAL   B N    1 
ATOM   5441 N N    B VAL   B 1 100 ? 39.763 -29.815 9.532   0.38 19.07 ?  100 VAL   B N    1 
ATOM   5442 C CA   A VAL   B 1 100 ? 39.127 -30.909 10.276  0.62 21.53 ?  100 VAL   B CA   1 
ATOM   5443 C CA   B VAL   B 1 100 ? 39.135 -30.918 10.256  0.38 21.52 ?  100 VAL   B CA   1 
ATOM   5444 C C    A VAL   B 1 100 ? 40.126 -31.581 11.212  0.62 22.10 ?  100 VAL   B C    1 
ATOM   5445 C C    B VAL   B 1 100 ? 40.125 -31.583 11.203  0.38 22.21 ?  100 VAL   B C    1 
ATOM   5446 O O    A VAL   B 1 100 ? 39.746 -32.089 12.275  0.62 22.79 ?  100 VAL   B O    1 
ATOM   5447 O O    B VAL   B 1 100 ? 39.739 -32.083 12.267  0.38 22.70 ?  100 VAL   B O    1 
ATOM   5448 C CB   A VAL   B 1 100 ? 38.480 -31.913 9.299   0.62 23.92 ?  100 VAL   B CB   1 
ATOM   5449 C CB   B VAL   B 1 100 ? 38.520 -31.921 9.257   0.38 23.31 ?  100 VAL   B CB   1 
ATOM   5450 C CG1  A VAL   B 1 100 ? 38.004 -33.156 10.038  0.62 24.97 ?  100 VAL   B CG1  1 
ATOM   5451 C CG1  B VAL   B 1 100 ? 38.008 -33.160 9.979   0.38 24.07 ?  100 VAL   B CG1  1 
ATOM   5452 C CG2  A VAL   B 1 100 ? 37.321 -31.262 8.562   0.62 24.64 ?  100 VAL   B CG2  1 
ATOM   5453 C CG2  B VAL   B 1 100 ? 37.399 -31.263 8.471   0.38 23.90 ?  100 VAL   B CG2  1 
ATOM   5454 H H    A VAL   B 1 100 ? 39.782 -29.927 8.682   0.62 22.59 ?  100 VAL   B H    1 
ATOM   5455 H H    B VAL   B 1 100 ? 39.802 -29.924 8.680   0.38 22.90 ?  100 VAL   B H    1 
ATOM   5456 H HA   A VAL   B 1 100 ? 38.414 -30.541 10.821  0.62 25.86 ?  100 VAL   B HA   1 
ATOM   5457 H HA   B VAL   B 1 100 ? 38.410 -30.563 10.792  0.38 25.84 ?  100 VAL   B HA   1 
ATOM   5458 H HB   A VAL   B 1 100 ? 39.137 -32.190 8.644   0.62 28.72 ?  100 VAL   B HB   1 
ATOM   5459 H HB   B VAL   B 1 100 ? 39.202 -32.204 8.629   0.38 27.99 ?  100 VAL   B HB   1 
ATOM   5460 H HG11 A VAL   B 1 100 ? 37.409 -33.659 9.458   0.62 29.98 ?  100 VAL   B HG11 1 
ATOM   5461 H HG11 B VAL   B 1 100 ? 37.439 -33.664 9.374   0.38 28.90 ?  100 VAL   B HG11 1 
ATOM   5462 H HG12 A VAL   B 1 100 ? 38.771 -33.702 10.273  0.62 29.98 ?  100 VAL   B HG12 1 
ATOM   5463 H HG12 B VAL   B 1 100 ? 38.763 -33.707 10.249  0.38 28.90 ?  100 VAL   B HG12 1 
ATOM   5464 H HG13 A VAL   B 1 100 ? 37.529 -32.887 10.840  0.62 29.98 ?  100 VAL   B HG13 1 
ATOM   5465 H HG13 B VAL   B 1 100 ? 37.499 -32.887 10.757  0.38 28.90 ?  100 VAL   B HG13 1 
ATOM   5466 H HG21 A VAL   B 1 100 ? 36.932 -31.910 7.952   0.62 29.58 ?  100 VAL   B HG21 1 
ATOM   5467 H HG21 B VAL   B 1 100 ? 37.013 -31.914 7.865   0.38 28.70 ?  100 VAL   B HG21 1 
ATOM   5468 H HG22 A VAL   B 1 100 ? 36.655 -30.978 9.209   0.62 29.58 ?  100 VAL   B HG22 1 
ATOM   5469 H HG22 B VAL   B 1 100 ? 36.723 -30.947 9.092   0.38 28.70 ?  100 VAL   B HG22 1 
ATOM   5470 H HG23 A VAL   B 1 100 ? 37.652 -30.498 8.068   0.62 29.58 ?  100 VAL   B HG23 1 
ATOM   5471 H HG23 B VAL   B 1 100 ? 37.763 -30.517 7.970   0.38 28.70 ?  100 VAL   B HG23 1 
ATOM   5472 N N    . ASN   B 1 101 ? 41.408 -31.612 10.834  1.00 22.65 ?  101 ASN   B N    1 
ATOM   5473 C CA   . ASN   B 1 101 ? 42.433 -32.153 11.726  1.00 24.84 ?  101 ASN   B CA   1 
ATOM   5474 C C    . ASN   B 1 101 ? 42.603 -31.314 12.988  1.00 27.37 ?  101 ASN   B C    1 
ATOM   5475 O O    . ASN   B 1 101 ? 43.201 -31.793 13.960  1.00 28.67 ?  101 ASN   B O    1 
ATOM   5476 C CB   . ASN   B 1 101 ? 43.768 -32.289 10.989  1.00 25.12 ?  101 ASN   B CB   1 
ATOM   5477 C CG   . ASN   B 1 101 ? 43.764 -33.424 9.980   1.00 24.68 ?  101 ASN   B CG   1 
ATOM   5478 O OD1  . ASN   B 1 101 ? 43.087 -34.429 10.170  1.00 25.95 ?  101 ASN   B OD1  1 
ATOM   5479 N ND2  . ASN   B 1 101 ? 44.513 -33.260 8.897   1.00 24.28 ?  101 ASN   B ND2  1 
ATOM   5480 H H    A ASN   B 1 101 ? 41.699 -31.343 10.069  0.62 27.19 ?  101 ASN   B H    1 
ATOM   5481 H H    B ASN   B 1 101 ? 41.703 -31.333 10.074  0.38 27.19 ?  101 ASN   B H    1 
ATOM   5482 H HA   . ASN   B 1 101 ? 42.160 -33.037 12.000  1.00 29.83 ?  101 ASN   B HA   1 
ATOM   5483 H HB2  . ASN   B 1 101 ? 43.961 -31.468 10.511  1.00 30.16 ?  101 ASN   B HB2  1 
ATOM   5484 H HB3  . ASN   B 1 101 ? 44.469 -32.467 11.637  1.00 30.16 ?  101 ASN   B HB3  1 
ATOM   5485 H HD21 . ASN   B 1 101 ? 44.542 -33.878 8.298   1.00 29.15 ?  101 ASN   B HD21 1 
ATOM   5486 H HD22 . ASN   B 1 101 ? 44.967 -32.539 8.795   1.00 29.15 ?  101 ASN   B HD22 1 
ATOM   5487 N N    A LYS   B 1 102 ? 42.102 -30.077 12.989  0.62 28.60 ?  102 LYS   B N    1 
ATOM   5488 N N    B LYS   B 1 102 ? 42.100 -30.078 12.990  0.38 28.78 ?  102 LYS   B N    1 
ATOM   5489 C CA   A LYS   B 1 102 ? 42.070 -29.230 14.174  0.62 30.19 ?  102 LYS   B CA   1 
ATOM   5490 C CA   B LYS   B 1 102 ? 42.071 -29.231 14.175  0.38 30.29 ?  102 LYS   B CA   1 
ATOM   5491 C C    A LYS   B 1 102 ? 40.691 -29.190 14.821  0.62 29.56 ?  102 LYS   B C    1 
ATOM   5492 C C    B LYS   B 1 102 ? 40.704 -29.218 14.847  0.38 29.78 ?  102 LYS   B C    1 
ATOM   5493 O O    A LYS   B 1 102 ? 40.464 -28.378 15.723  0.62 30.12 ?  102 LYS   B O    1 
ATOM   5494 O O    B LYS   B 1 102 ? 40.501 -28.462 15.802  0.38 30.35 ?  102 LYS   B O    1 
ATOM   5495 C CB   A LYS   B 1 102 ? 42.494 -27.801 13.824  0.62 32.59 ?  102 LYS   B CB   1 
ATOM   5496 C CB   B LYS   B 1 102 ? 42.467 -27.795 13.817  0.38 32.29 ?  102 LYS   B CB   1 
ATOM   5497 C CG   A LYS   B 1 102 ? 43.962 -27.622 13.483  0.62 34.93 ?  102 LYS   B CG   1 
ATOM   5498 C CG   B LYS   B 1 102 ? 43.919 -27.601 13.419  0.38 34.11 ?  102 LYS   B CG   1 
ATOM   5499 C CD   A LYS   B 1 102 ? 44.238 -26.171 13.110  0.62 37.16 ?  102 LYS   B CD   1 
ATOM   5500 C CD   B LYS   B 1 102 ? 44.156 -26.159 12.992  0.38 35.74 ?  102 LYS   B CD   1 
ATOM   5501 C CE   A LYS   B 1 102 ? 45.710 -25.919 12.833  0.62 38.79 ?  102 LYS   B CE   1 
ATOM   5502 C CE   B LYS   B 1 102 ? 45.618 -25.883 12.695  0.38 36.90 ?  102 LYS   B CE   1 
ATOM   5503 N NZ   A LYS   B 1 102 ? 45.959 -24.498 12.453  0.62 39.83 ?  102 LYS   B NZ   1 
ATOM   5504 N NZ   B LYS   B 1 102 ? 45.826 -24.474 12.256  0.38 37.60 ?  102 LYS   B NZ   1 
ATOM   5505 H H    A LYS   B 1 102 ? 41.761 -29.698 12.295  0.62 34.33 ?  102 LYS   B H    1 
ATOM   5506 H H    B LYS   B 1 102 ? 41.759 -29.699 12.296  0.38 34.56 ?  102 LYS   B H    1 
ATOM   5507 H HA   A LYS   B 1 102 ? 42.703 -29.574 14.823  0.62 36.25 ?  102 LYS   B HA   1 
ATOM   5508 H HA   B LYS   B 1 102 ? 42.719 -29.564 14.814  0.38 36.36 ?  102 LYS   B HA   1 
ATOM   5509 H HB2  A LYS   B 1 102 ? 41.978 -27.507 13.058  0.62 39.12 ?  102 LYS   B HB2  1 
ATOM   5510 H HB2  B LYS   B 1 102 ? 41.920 -27.499 13.074  0.38 38.76 ?  102 LYS   B HB2  1 
ATOM   5511 H HB3  A LYS   B 1 102 ? 42.301 -27.228 14.584  0.62 39.12 ?  102 LYS   B HB3  1 
ATOM   5512 H HB3  B LYS   B 1 102 ? 42.300 -27.229 14.588  0.38 38.76 ?  102 LYS   B HB3  1 
ATOM   5513 H HG2  A LYS   B 1 102 ? 44.506 -27.851 14.253  0.62 41.94 ?  102 LYS   B HG2  1 
ATOM   5514 H HG2  B LYS   B 1 102 ? 44.494 -27.795 14.176  0.38 40.94 ?  102 LYS   B HG2  1 
ATOM   5515 H HG3  A LYS   B 1 102 ? 44.191 -28.184 12.726  0.62 41.94 ?  102 LYS   B HG3  1 
ATOM   5516 H HG3  B LYS   B 1 102 ? 44.132 -28.182 12.672  0.38 40.94 ?  102 LYS   B HG3  1 
ATOM   5517 H HD2  A LYS   B 1 102 ? 43.737 -25.949 12.309  0.62 44.61 ?  102 LYS   B HD2  1 
ATOM   5518 H HD2  B LYS   B 1 102 ? 43.644 -25.977 12.188  0.38 42.90 ?  102 LYS   B HD2  1 
ATOM   5519 H HD3  A LYS   B 1 102 ? 43.965 -25.597 13.843  0.62 44.61 ?  102 LYS   B HD3  1 
ATOM   5520 H HD3  B LYS   B 1 102 ? 43.875 -25.565 13.707  0.38 42.90 ?  102 LYS   B HD3  1 
ATOM   5521 H HE2  A LYS   B 1 102 ? 46.224 -26.115 13.632  0.62 46.56 ?  102 LYS   B HE2  1 
ATOM   5522 H HE2  B LYS   B 1 102 ? 46.142 -26.032 13.498  0.38 44.29 ?  102 LYS   B HE2  1 
ATOM   5523 H HE3  A LYS   B 1 102 ? 45.999 -26.485 12.100  0.62 46.56 ?  102 LYS   B HE3  1 
ATOM   5524 H HE3  B LYS   B 1 102 ? 45.917 -26.471 11.984  0.38 44.29 ?  102 LYS   B HE3  1 
ATOM   5525 H HZ1  A LYS   B 1 102 ? 46.826 -24.372 12.296  0.62 47.82 ?  102 LYS   B HZ1  1 
ATOM   5526 H HZ1  B LYS   B 1 102 ? 46.688 -24.332 12.087  0.38 45.14 ?  102 LYS   B HZ1  1 
ATOM   5527 H HZ2  A LYS   B 1 102 ? 45.499 -24.294 11.719  0.62 47.82 ?  102 LYS   B HZ2  1 
ATOM   5528 H HZ2  B LYS   B 1 102 ? 45.356 -24.313 11.517  0.38 45.14 ?  102 LYS   B HZ2  1 
ATOM   5529 H HZ3  A LYS   B 1 102 ? 45.704 -23.957 13.113  0.62 47.82 ?  102 LYS   B HZ3  1 
ATOM   5530 H HZ3  B LYS   B 1 102 ? 45.561 -23.914 12.895  0.38 45.14 ?  102 LYS   B HZ3  1 
ATOM   5531 N N    . GLY   B 1 103 ? 39.760 -30.024 14.365  1.00 28.81 ?  103 GLY   B N    1 
ATOM   5532 C CA   . GLY   B 1 103 ? 38.430 -30.066 14.940  1.00 28.08 ?  103 GLY   B CA   1 
ATOM   5533 C C    . GLY   B 1 103 ? 37.489 -28.978 14.477  1.00 26.77 ?  103 GLY   B C    1 
ATOM   5534 O O    . GLY   B 1 103 ? 36.401 -28.839 15.049  1.00 27.64 ?  103 GLY   B O    1 
ATOM   5535 H H    A GLY   B 1 103 ? 39.878 -30.576 13.718  0.62 34.58 ?  103 GLY   B H    1 
ATOM   5536 H H    B GLY   B 1 103 ? 39.871 -30.559 13.703  0.38 34.58 ?  103 GLY   B H    1 
ATOM   5537 H HA2  . GLY   B 1 103 ? 38.022 -30.919 14.723  1.00 33.71 ?  103 GLY   B HA2  1 
ATOM   5538 H HA3  . GLY   B 1 103 ? 38.502 -30.008 15.907  1.00 33.71 ?  103 GLY   B HA3  1 
ATOM   5539 N N    A GLU   B 1 104 ? 37.870 -28.198 13.469  0.62 25.17 ?  104 GLU   B N    1 
ATOM   5540 N N    B GLU   B 1 104 ? 37.857 -28.211 13.456  0.38 25.95 ?  104 GLU   B N    1 
ATOM   5541 C CA   A GLU   B 1 104 ? 37.041 -27.096 13.010  0.62 23.71 ?  104 GLU   B CA   1 
ATOM   5542 C CA   B GLU   B 1 104 ? 37.003 -27.130 12.987  0.38 25.03 ?  104 GLU   B CA   1 
ATOM   5543 C C    A GLU   B 1 104 ? 35.858 -27.617 12.194  0.62 24.38 ?  104 GLU   B C    1 
ATOM   5544 C C    B GLU   B 1 104 ? 35.848 -27.676 12.152  0.38 25.05 ?  104 GLU   B C    1 
ATOM   5545 O O    A GLU   B 1 104 ? 35.891 -28.710 11.621  0.62 25.53 ?  104 GLU   B O    1 
ATOM   5546 O O    B GLU   B 1 104 ? 35.936 -28.751 11.553  0.38 25.59 ?  104 GLU   B O    1 
ATOM   5547 C CB   A GLU   B 1 104 ? 37.885 -26.098 12.215  0.62 22.34 ?  104 GLU   B CB   1 
ATOM   5548 C CB   B GLU   B 1 104 ? 37.826 -26.112 12.199  0.38 24.31 ?  104 GLU   B CB   1 
ATOM   5549 C CG   A GLU   B 1 104 ? 38.981 -25.472 13.068  0.62 21.24 ?  104 GLU   B CG   1 
ATOM   5550 C CG   B GLU   B 1 104 ? 38.890 -25.451 13.063  0.38 23.81 ?  104 GLU   B CG   1 
ATOM   5551 C CD   A GLU   B 1 104 ? 39.931 -24.582 12.294  0.62 20.01 ?  104 GLU   B CD   1 
ATOM   5552 C CD   B GLU   B 1 104 ? 39.862 -24.594 12.280  0.38 23.35 ?  104 GLU   B CD   1 
ATOM   5553 O OE1  A GLU   B 1 104 ? 39.947 -24.625 11.043  0.62 18.05 ?  104 GLU   B OE1  1 
ATOM   5554 O OE1  B GLU   B 1 104 ? 39.803 -24.586 11.032  0.38 22.79 ?  104 GLU   B OE1  1 
ATOM   5555 O OE2  A GLU   B 1 104 ? 40.676 -23.834 12.959  0.62 20.83 -1 104 GLU   B OE2  1 
ATOM   5556 O OE2  B GLU   B 1 104 ? 40.696 -23.926 12.926  0.38 23.59 -1 104 GLU   B OE2  1 
ATOM   5557 H H    A GLU   B 1 104 ? 38.612 -28.283 13.041  0.62 30.22 ?  104 GLU   B H    1 
ATOM   5558 H H    B GLU   B 1 104 ? 38.597 -28.291 13.025  0.38 31.15 ?  104 GLU   B H    1 
ATOM   5559 H HA   A GLU   B 1 104 ? 36.689 -26.629 13.785  0.62 28.47 ?  104 GLU   B HA   1 
ATOM   5560 H HA   B GLU   B 1 104 ? 36.628 -26.674 13.755  0.38 30.05 ?  104 GLU   B HA   1 
ATOM   5561 H HB2  A GLU   B 1 104 ? 38.307 -26.554 11.471  0.62 26.82 ?  104 GLU   B HB2  1 
ATOM   5562 H HB2  B GLU   B 1 104 ? 38.269 -26.561 11.463  0.38 29.19 ?  104 GLU   B HB2  1 
ATOM   5563 H HB3  A GLU   B 1 104 ? 37.314 -25.384 11.889  0.62 26.82 ?  104 GLU   B HB3  1 
ATOM   5564 H HB3  B GLU   B 1 104 ? 37.235 -25.419 11.862  0.38 29.19 ?  104 GLU   B HB3  1 
ATOM   5565 H HG2  A GLU   B 1 104 ? 38.571 -24.937 13.768  0.62 25.50 ?  104 GLU   B HG2  1 
ATOM   5566 H HG2  B GLU   B 1 104 ? 38.452 -24.890 13.724  0.38 28.59 ?  104 GLU   B HG2  1 
ATOM   5567 H HG3  A GLU   B 1 104 ? 39.515 -26.176 13.468  0.62 25.50 ?  104 GLU   B HG3  1 
ATOM   5568 H HG3  B GLU   B 1 104 ? 39.404 -26.141 13.512  0.38 28.59 ?  104 GLU   B HG3  1 
ATOM   5569 N N    A ASP   B 1 105 ? 34.796 -26.814 12.158  0.62 24.36 ?  105 ASP   B N    1 
ATOM   5570 N N    B ASP   B 1 105 ? 34.755 -26.916 12.124  0.38 24.54 ?  105 ASP   B N    1 
ATOM   5571 C CA   A ASP   B 1 105 ? 33.513 -27.256 11.625  0.62 25.27 ?  105 ASP   B CA   1 
ATOM   5572 C CA   B ASP   B 1 105 ? 33.493 -27.392 11.572  0.38 24.58 ?  105 ASP   B CA   1 
ATOM   5573 C C    A ASP   B 1 105 ? 33.563 -27.311 10.101  0.62 23.69 ?  105 ASP   B C    1 
ATOM   5574 C C    B ASP   B 1 105 ? 33.556 -27.402 10.049  0.38 23.81 ?  105 ASP   B C    1 
ATOM   5575 O O    A ASP   B 1 105 ? 33.711 -26.278 9.440   0.62 22.79 ?  105 ASP   B O    1 
ATOM   5576 O O    B ASP   B 1 105 ? 33.748 -26.355 9.420   0.38 23.22 ?  105 ASP   B O    1 
ATOM   5577 C CB   A ASP   B 1 105 ? 32.409 -26.308 12.091  0.62 28.40 ?  105 ASP   B CB   1 
ATOM   5578 C CB   B ASP   B 1 105 ? 32.348 -26.504 12.058  0.38 25.47 ?  105 ASP   B CB   1 
ATOM   5579 C CG   A ASP   B 1 105 ? 31.032 -26.744 11.637  0.62 30.99 ?  105 ASP   B CG   1 
ATOM   5580 C CG   B ASP   B 1 105 ? 30.984 -27.095 11.754  0.38 26.17 ?  105 ASP   B CG   1 
ATOM   5581 O OD1  A ASP   B 1 105 ? 30.900 -27.868 11.109  0.62 31.39 ?  105 ASP   B OD1  1 
ATOM   5582 O OD1  B ASP   B 1 105 ? 30.914 -28.062 10.966  0.38 26.21 ?  105 ASP   B OD1  1 
ATOM   5583 O OD2  A ASP   B 1 105 ? 30.077 -25.953 11.800  0.62 32.59 -1 105 ASP   B OD2  1 
ATOM   5584 O OD2  B ASP   B 1 105 ? 29.980 -26.602 12.314  0.38 26.11 -1 105 ASP   B OD2  1 
ATOM   5585 H H    A ASP   B 1 105 ? 34.799 -25.999 12.436  0.62 29.25 ?  105 ASP   B H    1 
ATOM   5586 H H    B ASP   B 1 105 ? 34.724 -26.110 12.419  0.38 29.46 ?  105 ASP   B H    1 
ATOM   5587 H HA   A ASP   B 1 105 ? 33.317 -28.145 11.959  0.62 30.34 ?  105 ASP   B HA   1 
ATOM   5588 H HA   B ASP   B 1 105 ? 33.323 -28.297 11.877  0.38 29.51 ?  105 ASP   B HA   1 
ATOM   5589 H HB2  A ASP   B 1 105 ? 32.429 -26.255 13.062  0.62 34.10 ?  105 ASP   B HB2  1 
ATOM   5590 H HB2  B ASP   B 1 105 ? 32.417 -26.395 13.020  0.38 30.59 ?  105 ASP   B HB2  1 
ATOM   5591 H HB3  A ASP   B 1 105 ? 32.560 -25.433 11.709  0.62 34.10 ?  105 ASP   B HB3  1 
ATOM   5592 H HB3  B ASP   B 1 105 ? 32.414 -25.636 11.623  0.38 30.59 ?  105 ASP   B HB3  1 
ATOM   5593 N N    A ILE   B 1 106 ? 33.415 -28.518 9.546   0.62 23.36 ?  106 ILE   B N    1 
ATOM   5594 N N    B ILE   B 1 106 ? 33.377 -28.587 9.458   0.38 23.46 ?  106 ILE   B N    1 
ATOM   5595 C CA   A ILE   B 1 106 ? 33.411 -28.704 8.099   0.62 22.46 ?  106 ILE   B CA   1 
ATOM   5596 C CA   B ILE   B 1 106 ? 33.381 -28.731 8.007   0.38 22.99 ?  106 ILE   B CA   1 
ATOM   5597 C C    A ILE   B 1 106 ? 32.314 -27.887 7.420   0.62 21.57 ?  106 ILE   B C    1 
ATOM   5598 C C    B ILE   B 1 106 ? 32.284 -27.901 7.351   0.38 22.46 ?  106 ILE   B C    1 
ATOM   5599 O O    A ILE   B 1 106 ? 32.426 -27.566 6.232   0.62 20.73 ?  106 ILE   B O    1 
ATOM   5600 O O    B ILE   B 1 106 ? 32.369 -27.596 6.156   0.38 21.93 ?  106 ILE   B O    1 
ATOM   5601 C CB   A ILE   B 1 106 ? 33.316 -30.212 7.769   0.62 23.48 ?  106 ILE   B CB   1 
ATOM   5602 C CB   B ILE   B 1 106 ? 33.279 -30.229 7.633   0.38 23.54 ?  106 ILE   B CB   1 
ATOM   5603 C CG1  A ILE   B 1 106 ? 33.570 -30.465 6.284   0.62 24.09 ?  106 ILE   B CG1  1 
ATOM   5604 C CG1  B ILE   B 1 106 ? 33.578 -30.446 6.148   0.38 23.86 ?  106 ILE   B CG1  1 
ATOM   5605 C CG2  A ILE   B 1 106 ? 31.958 -30.770 8.182   0.62 24.49 ?  106 ILE   B CG2  1 
ATOM   5606 C CG2  B ILE   B 1 106 ? 31.901 -30.777 7.981   0.38 24.14 ?  106 ILE   B CG2  1 
ATOM   5607 C CD1  A ILE   B 1 106 ? 34.933 -30.012 5.821   0.62 24.12 ?  106 ILE   B CD1  1 
ATOM   5608 C CD1  B ILE   B 1 106 ? 34.955 -29.986 5.735   0.38 23.90 ?  106 ILE   B CD1  1 
ATOM   5609 H H    A ILE   B 1 106 ? 33.319 -29.244 9.995   0.62 28.04 ?  106 ILE   B H    1 
ATOM   5610 H H    B ILE   B 1 106 ? 33.258 -29.324 9.882   0.38 28.16 ?  106 ILE   B H    1 
ATOM   5611 H HA   A ILE   B 1 106 ? 34.258 -28.386 7.761   0.62 26.97 ?  106 ILE   B HA   1 
ATOM   5612 H HA   B ILE   B 1 106 ? 34.227 -28.401 7.675   0.38 27.60 ?  106 ILE   B HA   1 
ATOM   5613 H HB   A ILE   B 1 106 ? 33.999 -30.679 8.278   0.62 28.19 ?  106 ILE   B HB   1 
ATOM   5614 H HB   B ILE   B 1 106 ? 33.938 -30.718 8.150   0.38 28.26 ?  106 ILE   B HB   1 
ATOM   5615 H HG12 A ILE   B 1 106 ? 33.506 -31.419 6.113   0.62 28.92 ?  106 ILE   B HG12 1 
ATOM   5616 H HG12 B ILE   B 1 106 ? 33.514 -31.396 5.952   0.38 28.65 ?  106 ILE   B HG12 1 
ATOM   5617 H HG13 A ILE   B 1 106 ? 32.907 -29.992 5.762   0.62 28.92 ?  106 ILE   B HG13 1 
ATOM   5618 H HG13 B ILE   B 1 106 ? 32.930 -29.958 5.620   0.38 28.65 ?  106 ILE   B HG13 1 
ATOM   5619 H HG21 A ILE   B 1 106 ? 31.970 -31.736 8.088   0.62 29.40 ?  106 ILE   B HG21 1 
ATOM   5620 H HG21 B ILE   B 1 106 ? 31.918 -31.744 7.906   0.38 28.99 ?  106 ILE   B HG21 1 
ATOM   5621 H HG22 A ILE   B 1 106 ? 31.786 -30.532 9.107   0.62 29.40 ?  106 ILE   B HG22 1 
ATOM   5622 H HG22 B ILE   B 1 106 ? 31.681 -30.521 8.891   0.38 28.99 ?  106 ILE   B HG22 1 
ATOM   5623 H HG23 A ILE   B 1 106 ? 31.271 -30.392 7.611   0.62 29.40 ?  106 ILE   B HG23 1 
ATOM   5624 H HG23 B ILE   B 1 106 ? 31.247 -30.409 7.367   0.38 28.99 ?  106 ILE   B HG23 1 
ATOM   5625 H HD11 A ILE   B 1 106 ? 35.129 -30.420 4.965   0.62 28.95 ?  106 ILE   B HD11 1 
ATOM   5626 H HD11 B ILE   B 1 106 ? 35.178 -30.387 4.882   0.38 28.70 ?  106 ILE   B HD11 1 
ATOM   5627 H HD12 A ILE   B 1 106 ? 34.934 -29.045 5.734   0.62 28.95 ?  106 ILE   B HD12 1 
ATOM   5628 H HD12 B ILE   B 1 106 ? 34.955 -29.019 5.658   0.38 28.70 ?  106 ILE   B HD12 1 
ATOM   5629 H HD13 A ILE   B 1 106 ? 35.597 -30.285 6.476   0.62 28.95 ?  106 ILE   B HD13 1 
ATOM   5630 H HD13 B ILE   B 1 106 ? 35.596 -30.266 6.409   0.38 28.70 ?  106 ILE   B HD13 1 
ATOM   5631 N N    A GLN   B 1 107 ? 31.257 -27.527 8.151   0.62 22.21 ?  107 GLN   B N    1 
ATOM   5632 N N    B GLN   B 1 107 ? 31.252 -27.520 8.107   0.38 22.86 ?  107 GLN   B N    1 
ATOM   5633 C CA   A GLN   B 1 107 ? 30.185 -26.723 7.569   0.62 22.84 ?  107 GLN   B CA   1 
ATOM   5634 C CA   B GLN   B 1 107 ? 30.172 -26.713 7.548   0.38 23.19 ?  107 GLN   B CA   1 
ATOM   5635 C C    A GLN   B 1 107 ? 30.678 -25.375 7.054   0.62 20.98 ?  107 GLN   B C    1 
ATOM   5636 C C    B GLN   B 1 107 ? 30.654 -25.345 7.078   0.38 21.17 ?  107 GLN   B C    1 
ATOM   5637 O O    A GLN   B 1 107 ? 30.048 -24.799 6.163   0.62 21.71 ?  107 GLN   B O    1 
ATOM   5638 O O    B GLN   B 1 107 ? 29.987 -24.721 6.247   0.38 21.73 ?  107 GLN   B O    1 
ATOM   5639 C CB   A GLN   B 1 107 ? 29.070 -26.522 8.600   0.62 26.30 ?  107 GLN   B CB   1 
ATOM   5640 C CB   B GLN   B 1 107 ? 29.053 -26.557 8.582   0.38 25.92 ?  107 GLN   B CB   1 
ATOM   5641 C CG   A GLN   B 1 107 ? 27.751 -26.000 8.028   0.62 29.95 ?  107 GLN   B CG   1 
ATOM   5642 C CG   B GLN   B 1 107 ? 27.742 -26.006 8.029   0.38 28.64 ?  107 GLN   B CG   1 
ATOM   5643 C CD   A GLN   B 1 107 ? 27.701 -24.483 7.931   0.62 32.73 ?  107 GLN   B CD   1 
ATOM   5644 C CD   B GLN   B 1 107 ? 27.662 -24.491 8.094   0.38 30.71 ?  107 GLN   B CD   1 
ATOM   5645 O OE1  A GLN   B 1 107 ? 28.533 -23.783 8.512   0.62 33.68 ?  107 GLN   B OE1  1 
ATOM   5646 O OE1  B GLN   B 1 107 ? 28.510 -23.836 8.703   0.38 31.37 ?  107 GLN   B OE1  1 
ATOM   5647 N NE2  A GLN   B 1 107 ? 26.719 -23.969 7.194   0.62 33.66 ?  107 GLN   B NE2  1 
ATOM   5648 N NE2  B GLN   B 1 107 ? 26.635 -23.927 7.467   0.38 31.49 ?  107 GLN   B NE2  1 
ATOM   5649 H H    A GLN   B 1 107 ? 31.142 -27.729 8.974   0.62 26.66 ?  107 GLN   B H    1 
ATOM   5650 H H    B GLN   B 1 107 ? 31.153 -27.716 8.936   0.38 27.45 ?  107 GLN   B H    1 
ATOM   5651 H HA   A GLN   B 1 107 ? 29.810 -27.207 6.818   0.62 27.42 ?  107 GLN   B HA   1 
ATOM   5652 H HA   B GLN   B 1 107 ? 29.801 -27.179 6.781   0.38 27.84 ?  107 GLN   B HA   1 
ATOM   5653 H HB2  A GLN   B 1 107 ? 28.889 -27.373 9.021   0.62 31.58 ?  107 GLN   B HB2  1 
ATOM   5654 H HB2  B GLN   B 1 107 ? 28.863 -27.426 8.963   0.38 31.12 ?  107 GLN   B HB2  1 
ATOM   5655 H HB3  A GLN   B 1 107 ? 29.377 -25.887 9.265   0.62 31.58 ?  107 GLN   B HB3  1 
ATOM   5656 H HB3  B GLN   B 1 107 ? 29.356 -25.955 9.280   0.38 31.12 ?  107 GLN   B HB3  1 
ATOM   5657 H HG2  A GLN   B 1 107 ? 27.626 -26.358 7.136   0.62 35.95 ?  107 GLN   B HG2  1 
ATOM   5658 H HG2  B GLN   B 1 107 ? 27.653 -26.269 7.100   0.38 34.38 ?  107 GLN   B HG2  1 
ATOM   5659 H HG3  A GLN   B 1 107 ? 27.023 -26.289 8.604   0.62 35.95 ?  107 GLN   B HG3  1 
ATOM   5660 H HG3  B GLN   B 1 107 ? 27.003 -26.370 8.547   0.38 34.38 ?  107 GLN   B HG3  1 
ATOM   5661 H HE21 A GLN   B 1 107 ? 26.156 -24.489 6.800   0.62 40.41 ?  107 GLN   B HE21 1 
ATOM   5662 H HE21 B GLN   B 1 107 ? 26.062 -24.416 7.050   0.38 37.80 ?  107 GLN   B HE21 1 
ATOM   5663 H HE22 A GLN   B 1 107 ? 26.643 -23.115 7.110   0.62 40.41 ?  107 GLN   B HE22 1 
ATOM   5664 H HE22 B GLN   B 1 107 ? 26.542 -23.072 7.476   0.38 37.80 ?  107 GLN   B HE22 1 
ATOM   5665 N N    . LEU   B 1 108 ? 31.794 -24.865 7.579   1.00 18.80 ?  108 LEU   B N    1 
ATOM   5666 C CA   . LEU   B 1 108 ? 32.331 -23.567 7.165   1.00 16.40 ?  108 LEU   B CA   1 
ATOM   5667 C C    . LEU   B 1 108 ? 32.983 -23.589 5.792   1.00 14.58 ?  108 LEU   B C    1 
ATOM   5668 O O    . LEU   B 1 108 ? 33.411 -22.530 5.306   1.00 14.46 ?  108 LEU   B O    1 
ATOM   5669 C CB   . LEU   B 1 108 ? 33.330 -23.058 8.198   1.00 16.95 ?  108 LEU   B CB   1 
ATOM   5670 C CG   . LEU   B 1 108 ? 32.693 -22.637 9.520   1.00 18.61 ?  108 LEU   B CG   1 
ATOM   5671 C CD1  . LEU   B 1 108 ? 33.722 -22.557 10.628  1.00 18.49 ?  108 LEU   B CD1  1 
ATOM   5672 C CD2  . LEU   B 1 108 ? 31.996 -21.298 9.352   1.00 20.03 ?  108 LEU   B CD2  1 
ATOM   5673 H H    A LEU   B 1 108 ? 32.255 -25.252 8.188   0.62 22.58 ?  108 LEU   B H    1 
ATOM   5674 H H    B LEU   B 1 108 ? 32.267 -25.268 8.167   0.38 22.58 ?  108 LEU   B H    1 
ATOM   5675 H HA   . LEU   B 1 108 ? 31.599 -22.936 7.125   1.00 19.70 ?  108 LEU   B HA   1 
ATOM   5676 H HB2  . LEU   B 1 108 ? 33.965 -23.762 8.392   1.00 20.35 ?  108 LEU   B HB2  1 
ATOM   5677 H HB3  . LEU   B 1 108 ? 33.787 -22.287 7.834   1.00 20.35 ?  108 LEU   B HB3  1 
ATOM   5678 H HG   . LEU   B 1 108 ? 32.022 -23.292 9.778   1.00 22.35 ?  108 LEU   B HG   1 
ATOM   5679 H HD11 . LEU   B 1 108 ? 33.282 -22.293 11.454  1.00 22.20 ?  108 LEU   B HD11 1 
ATOM   5680 H HD12 . LEU   B 1 108 ? 34.134 -23.428 10.741  1.00 22.20 ?  108 LEU   B HD12 1 
ATOM   5681 H HD13 . LEU   B 1 108 ? 34.394 -21.900 10.389  1.00 22.20 ?  108 LEU   B HD13 1 
ATOM   5682 H HD21 . LEU   B 1 108 ? 31.662 -21.003 10.215  1.00 24.05 ?  108 LEU   B HD21 1 
ATOM   5683 H HD22 . LEU   B 1 108 ? 32.631 -20.654 9.005   1.00 24.05 ?  108 LEU   B HD22 1 
ATOM   5684 H HD23 . LEU   B 1 108 ? 31.256 -21.401 8.732   1.00 24.05 ?  108 LEU   B HD23 1 
ATOM   5685 N N    . LEU   B 1 109 ? 33.055 -24.757 5.160   1.00 13.67 ?  109 LEU   B N    1 
ATOM   5686 C CA   . LEU   B 1 109 ? 33.687 -24.863 3.855   1.00 12.94 ?  109 LEU   B CA   1 
ATOM   5687 C C    . LEU   B 1 109 ? 32.922 -24.076 2.797   1.00 11.99 ?  109 LEU   B C    1 
ATOM   5688 O O    . LEU   B 1 109 ? 33.536 -23.481 1.901   1.00 12.17 ?  109 LEU   B O    1 
ATOM   5689 C CB   . LEU   B 1 109 ? 33.804 -26.341 3.480   1.00 13.03 ?  109 LEU   B CB   1 
ATOM   5690 C CG   . LEU   B 1 109 ? 34.578 -26.676 2.210   1.00 12.96 ?  109 LEU   B CG   1 
ATOM   5691 C CD1  . LEU   B 1 109 ? 35.959 -26.018 2.208   1.00 12.78 ?  109 LEU   B CD1  1 
ATOM   5692 C CD2  . LEU   B 1 109 ? 34.710 -28.183 2.072   1.00 13.60 ?  109 LEU   B CD2  1 
ATOM   5693 H H    . LEU   B 1 109 ? 32.749 -25.500 5.459   1.00 16.42 ?  109 LEU   B H    1 
ATOM   5694 H HA   . LEU   B 1 109 ? 34.580 -24.497 3.904   1.00 15.55 ?  109 LEU   B HA   1 
ATOM   5695 H HB2  . LEU   B 1 109 ? 34.250 -26.805 4.208   1.00 15.65 ?  109 LEU   B HB2  1 
ATOM   5696 H HB3  . LEU   B 1 109 ? 32.913 -26.706 3.370   1.00 15.65 ?  109 LEU   B HB3  1 
ATOM   5697 H HG   . LEU   B 1 109 ? 34.088 -26.354 1.436   1.00 15.57 ?  109 LEU   B HG   1 
ATOM   5698 H HD11 . LEU   B 1 109 ? 36.482 -26.378 1.472   1.00 15.35 ?  109 LEU   B HD11 1 
ATOM   5699 H HD12 . LEU   B 1 109 ? 35.851 -25.062 2.099   1.00 15.35 ?  109 LEU   B HD12 1 
ATOM   5700 H HD13 . LEU   B 1 109 ? 36.401 -26.212 3.050   1.00 15.35 ?  109 LEU   B HD13 1 
ATOM   5701 H HD21 . LEU   B 1 109 ? 35.271 -28.385 1.305   1.00 16.33 ?  109 LEU   B HD21 1 
ATOM   5702 H HD22 . LEU   B 1 109 ? 35.116 -28.539 2.878   1.00 16.33 ?  109 LEU   B HD22 1 
ATOM   5703 H HD23 . LEU   B 1 109 ? 33.829 -28.569 1.947   1.00 16.33 ?  109 LEU   B HD23 1 
ATOM   5704 N N    . LYS   B 1 110 ? 31.590 -24.044 2.881   1.00 12.05 ?  110 LYS   B N    1 
ATOM   5705 C CA   . LYS   B 1 110 ? 30.831 -23.284 1.895   1.00 11.67 ?  110 LYS   B CA   1 
ATOM   5706 C C    . LYS   B 1 110 ? 31.167 -21.795 1.977   1.00 11.24 ?  110 LYS   B C    1 
ATOM   5707 O O    . LYS   B 1 110 ? 31.427 -21.155 0.956   1.00 11.33 ?  110 LYS   B O    1 
ATOM   5708 C CB   . LYS   B 1 110 ? 29.327 -23.537 2.039   1.00 12.56 ?  110 LYS   B CB   1 
ATOM   5709 C CG   . LYS   B 1 110 ? 28.516 -22.905 0.906   1.00 12.83 ?  110 LYS   B CG   1 
ATOM   5710 C CD   . LYS   B 1 110 ? 27.055 -23.332 0.915   1.00 13.32 ?  110 LYS   B CD   1 
ATOM   5711 C CE   . LYS   B 1 110 ? 26.304 -22.801 -0.306  1.00 14.17 ?  110 LYS   B CE   1 
ATOM   5712 N NZ   . LYS   B 1 110 ? 26.636 -23.526 -1.562  1.00 14.64 ?  110 LYS   B NZ   1 
ATOM   5713 H H    . LYS   B 1 110 ? 31.119 -24.451 3.472   1.00 14.48 ?  110 LYS   B H    1 
ATOM   5714 H HA   . LYS   B 1 110 ? 31.086 -23.591 1.007   1.00 14.02 ?  110 LYS   B HA   1 
ATOM   5715 H HB2  . LYS   B 1 110 ? 29.162 -24.496 2.024   1.00 15.08 ?  110 LYS   B HB2  1 
ATOM   5716 H HB3  . LYS   B 1 110 ? 29.020 -23.161 2.875   1.00 15.08 ?  110 LYS   B HB3  1 
ATOM   5717 H HG2  . LYS   B 1 110 ? 28.538 -21.941 1.000   1.00 15.42 ?  110 LYS   B HG2  1 
ATOM   5718 H HG3  . LYS   B 1 110 ? 28.896 -23.167 0.055   1.00 15.42 ?  110 LYS   B HG3  1 
ATOM   5719 H HD2  . LYS   B 1 110 ? 27.002 -24.308 0.900   1.00 16.00 ?  110 LYS   B HD2  1 
ATOM   5720 H HD3  . LYS   B 1 110 ? 26.618 -22.993 1.713   1.00 16.00 ?  110 LYS   B HD3  1 
ATOM   5721 H HE2  . LYS   B 1 110 ? 25.350 -22.886 -0.157  1.00 17.01 ?  110 LYS   B HE2  1 
ATOM   5722 H HE3  . LYS   B 1 110 ? 26.538 -21.868 -0.433  1.00 17.01 ?  110 LYS   B HE3  1 
ATOM   5723 H HZ1  . LYS   B 1 110 ? 26.184 -23.185 -2.246  1.00 17.58 ?  110 LYS   B HZ1  1 
ATOM   5724 H HZ2  . LYS   B 1 110 ? 27.510 -23.463 -1.732  1.00 17.58 ?  110 LYS   B HZ2  1 
ATOM   5725 H HZ3  . LYS   B 1 110 ? 26.427 -24.391 -1.480  1.00 17.58 ?  110 LYS   B HZ3  1 
ATOM   5726 N N    . SER   B 1 111 ? 31.192 -21.236 3.191   1.00 11.98 ?  111 SER   B N    1 
ATOM   5727 C CA   . SER   B 1 111 ? 31.582 -19.836 3.358   1.00 11.98 ?  111 SER   B CA   1 
ATOM   5728 C C    . SER   B 1 111 ? 32.965 -19.580 2.776   1.00 11.53 ?  111 SER   B C    1 
ATOM   5729 O O    . SER   B 1 111 ? 33.193 -18.547 2.130   1.00 11.63 ?  111 SER   B O    1 
ATOM   5730 C CB   . SER   B 1 111 ? 31.569 -19.452 4.838   1.00 13.00 ?  111 SER   B CB   1 
ATOM   5731 O OG   . SER   B 1 111 ? 30.262 -19.475 5.368   1.00 15.01 ?  111 SER   B OG   1 
ATOM   5732 H H    . SER   B 1 111 ? 30.998 -21.647 3.918   1.00 14.39 ?  111 SER   B H    1 
ATOM   5733 H HA   . SER   B 1 111 ? 30.950 -19.272 2.891   1.00 14.39 ?  111 SER   B HA   1 
ATOM   5734 H HB2  . SER   B 1 111 ? 32.116 -20.082 5.331   1.00 15.62 ?  111 SER   B HB2  1 
ATOM   5735 H HB3  . SER   B 1 111 ? 31.921 -18.558 4.934   1.00 15.62 ?  111 SER   B HB3  1 
ATOM   5736 H HG   . SER   B 1 111 ? 30.273 -19.269 6.185   1.00 18.03 ?  111 SER   B HG   1 
ATOM   5737 N N    . ALA   B 1 112 ? 33.902 -20.504 3.000   1.00 11.49 ?  112 ALA   B N    1 
ATOM   5738 C CA   . ALA   B 1 112 ? 35.250 -20.342 2.464   1.00 11.38 ?  112 ALA   B CA   1 
ATOM   5739 C C    . ALA   B 1 112 ? 35.222 -20.244 0.943   1.00 10.59 ?  112 ALA   B C    1 
ATOM   5740 O O    . ALA   B 1 112 ? 35.852 -19.355 0.356   1.00 10.85 ?  112 ALA   B O    1 
ATOM   5741 C CB   . ALA   B 1 112 ? 36.142 -21.493 2.937   1.00 12.12 ?  112 ALA   B CB   1 
ATOM   5742 H H    . ALA   B 1 112 ? 33.781 -21.226 3.456   1.00 13.80 ?  112 ALA   B H    1 
ATOM   5743 H HA   . ALA   B 1 112 ? 35.624 -19.518 2.807   1.00 13.68 ?  112 ALA   B HA   1 
ATOM   5744 H HB1  . ALA   B 1 112 ? 37.035 -21.367 2.578   1.00 14.56 ?  112 ALA   B HB1  1 
ATOM   5745 H HB2  . ALA   B 1 112 ? 36.176 -21.489 3.908   1.00 14.56 ?  112 ALA   B HB2  1 
ATOM   5746 H HB3  . ALA   B 1 112 ? 35.774 -22.332 2.624   1.00 14.56 ?  112 ALA   B HB3  1 
ATOM   5747 N N    . TYR   B 1 113 ? 34.479 -21.138 0.284   1.00 10.76 ?  113 TYR   B N    1 
ATOM   5748 C CA   . TYR   B 1 113 ? 34.404 -21.087 -1.169  1.00 10.34 ?  113 TYR   B CA   1 
ATOM   5749 C C    . TYR   B 1 113 ? 33.695 -19.840 -1.682  1.00 10.09 ?  113 TYR   B C    1 
ATOM   5750 O O    . TYR   B 1 113 ? 33.969 -19.412 -2.804  1.00 10.09 ?  113 TYR   B O    1 
ATOM   5751 C CB   . TYR   B 1 113 ? 33.739 -22.354 -1.718  1.00 10.74 ?  113 TYR   B CB   1 
ATOM   5752 C CG   . TYR   B 1 113 ? 34.703 -23.505 -1.979  1.00 11.10 ?  113 TYR   B CG   1 
ATOM   5753 C CD1  . TYR   B 1 113 ? 35.698 -23.394 -2.946  1.00 11.28 ?  113 TYR   B CD1  1 
ATOM   5754 C CD2  . TYR   B 1 113 ? 34.607 -24.694 -1.275  1.00 11.50 ?  113 TYR   B CD2  1 
ATOM   5755 C CE1  . TYR   B 1 113 ? 36.571 -24.421 -3.202  1.00 11.30 ?  113 TYR   B CE1  1 
ATOM   5756 C CE2  . TYR   B 1 113 ? 35.471 -25.748 -1.523  1.00 11.77 ?  113 TYR   B CE2  1 
ATOM   5757 C CZ   . TYR   B 1 113 ? 36.452 -25.609 -2.494  1.00 11.55 ?  113 TYR   B CZ   1 
ATOM   5758 O OH   . TYR   B 1 113 ? 37.338 -26.623 -2.771  1.00 12.02 ?  113 TYR   B OH   1 
ATOM   5759 H H    . TYR   B 1 113 ? 34.012 -21.767 0.656   1.00 12.93 ?  113 TYR   B H    1 
ATOM   5760 H HA   . TYR   B 1 113 ? 35.304 -21.068 -1.507  1.00 12.42 ?  113 TYR   B HA   1 
ATOM   5761 H HB2  . TYR   B 1 113 ? 33.078 -22.674 -1.080  1.00 12.90 ?  113 TYR   B HB2  1 
ATOM   5762 H HB3  . TYR   B 1 113 ? 33.301 -22.142 -2.557  1.00 12.90 ?  113 TYR   B HB3  1 
ATOM   5763 H HD1  . TYR   B 1 113 ? 35.776 -22.602 -3.436  1.00 13.56 ?  113 TYR   B HD1  1 
ATOM   5764 H HD2  . TYR   B 1 113 ? 33.943 -24.793 -0.634  1.00 13.82 ?  113 TYR   B HD2  1 
ATOM   5765 H HE1  . TYR   B 1 113 ? 37.229 -24.334 -3.860  1.00 13.57 ?  113 TYR   B HE1  1 
ATOM   5766 H HE2  . TYR   B 1 113 ? 35.392 -26.545 -1.046  1.00 14.14 ?  113 TYR   B HE2  1 
ATOM   5767 H HH   . TYR   B 1 113 ? 37.167 -27.294 -2.292  1.00 14.45 ?  113 TYR   B HH   1 
ATOM   5768 N N    . GLU   B 1 114 ? 32.774 -19.259 -0.904  1.00 10.19 ?  114 GLU   B N    1 
ATOM   5769 C CA   . GLU   B 1 114 ? 32.099 -18.053 -1.366  1.00 10.50 ?  114 GLU   B CA   1 
ATOM   5770 C C    . GLU   B 1 114 ? 33.080 -16.926 -1.661  1.00 10.08 ?  114 GLU   B C    1 
ATOM   5771 O O    . GLU   B 1 114 ? 32.798 -16.069 -2.501  1.00 10.39 ?  114 GLU   B O    1 
ATOM   5772 C CB   . GLU   B 1 114 ? 31.033 -17.625 -0.357  1.00 10.98 ?  114 GLU   B CB   1 
ATOM   5773 C CG   . GLU   B 1 114 ? 29.817 -18.554 -0.416  1.00 10.94 ?  114 GLU   B CG   1 
ATOM   5774 C CD   . GLU   B 1 114 ? 28.787 -18.356 0.695   1.00 11.05 ?  114 GLU   B CD   1 
ATOM   5775 O OE1  . GLU   B 1 114 ? 29.092 -17.739 1.739   1.00 11.43 ?  114 GLU   B OE1  1 
ATOM   5776 O OE2  . GLU   B 1 114 ? 27.656 -18.878 0.535   1.00 11.95 -1 114 GLU   B OE2  1 
ATOM   5777 H H    . GLU   B 1 114 ? 32.519 -19.550 -0.128  1.00 12.24 ?  114 GLU   B H    1 
ATOM   5778 H HA   . GLU   B 1 114 ? 31.645 -18.256 -2.191  1.00 12.62 ?  114 GLU   B HA   1 
ATOM   5779 H HB2  . GLU   B 1 114 ? 31.396 -17.658 0.541   1.00 13.20 ?  114 GLU   B HB2  1 
ATOM   5780 H HB3  . GLU   B 1 114 ? 30.733 -16.726 -0.566  1.00 13.20 ?  114 GLU   B HB3  1 
ATOM   5781 H HG2  . GLU   B 1 114 ? 29.367 -18.415 -1.261  1.00 13.14 ?  114 GLU   B HG2  1 
ATOM   5782 H HG3  . GLU   B 1 114 ? 30.135 -19.471 -0.363  1.00 13.14 ?  114 GLU   B HG3  1 
ATOM   5783 N N    . ASN   B 1 115 ? 34.246 -16.920 -1.009  1.00 9.91  ?  115 ASN   B N    1 
ATOM   5784 C CA   . ASN   B 1 115 ? 35.235 -15.888 -1.307  1.00 10.04 ?  115 ASN   B CA   1 
ATOM   5785 C C    . ASN   B 1 115 ? 35.644 -15.908 -2.774  1.00 9.71  ?  115 ASN   B C    1 
ATOM   5786 O O    . ASN   B 1 115 ? 36.028 -14.867 -3.329  1.00 10.43 ?  115 ASN   B O    1 
ATOM   5787 C CB   . ASN   B 1 115 ? 36.473 -16.074 -0.423  1.00 10.54 ?  115 ASN   B CB   1 
ATOM   5788 C CG   . ASN   B 1 115 ? 36.209 -15.801 1.039   1.00 11.27 ?  115 ASN   B CG   1 
ATOM   5789 O OD1  . ASN   B 1 115 ? 36.214 -14.650 1.478   1.00 13.03 ?  115 ASN   B OD1  1 
ATOM   5790 N ND2  . ASN   B 1 115 ? 36.044 -16.863 1.821   1.00 11.41 ?  115 ASN   B ND2  1 
ATOM   5791 H H    . ASN   B 1 115 ? 34.485 -17.487 -0.396  1.00 11.91 ?  115 ASN   B H    1 
ATOM   5792 H HA   . ASN   B 1 115 ? 34.857 -15.018 -1.109  1.00 12.07 ?  115 ASN   B HA   1 
ATOM   5793 H HB2  . ASN   B 1 115 ? 36.788 -16.988 -0.507  1.00 12.67 ?  115 ASN   B HB2  1 
ATOM   5794 H HB3  . ASN   B 1 115 ? 37.165 -15.460 -0.719  1.00 12.67 ?  115 ASN   B HB3  1 
ATOM   5795 H HD21 . ASN   B 1 115 ? 35.904 -16.760 2.663   1.00 13.71 ?  115 ASN   B HD21 1 
ATOM   5796 H HD22 . ASN   B 1 115 ? 36.066 -17.654 1.483   1.00 13.71 ?  115 ASN   B HD22 1 
ATOM   5797 N N    . PHE   B 1 116 ? 35.623 -17.089 -3.405  1.00 9.60  ?  116 PHE   B N    1 
ATOM   5798 C CA   . PHE   B 1 116 ? 36.051 -17.192 -4.796  1.00 10.13 ?  116 PHE   B CA   1 
ATOM   5799 C C    . PHE   B 1 116 ? 35.149 -16.370 -5.713  1.00 9.87  ?  116 PHE   B C    1 
ATOM   5800 O O    . PHE   B 1 116 ? 35.585 -15.936 -6.783  1.00 10.16 ?  116 PHE   B O    1 
ATOM   5801 C CB   . PHE   B 1 116 ? 36.022 -18.644 -5.307  1.00 9.78  ?  116 PHE   B CB   1 
ATOM   5802 C CG   . PHE   B 1 116 ? 37.096 -19.588 -4.763  1.00 9.58  ?  116 PHE   B CG   1 
ATOM   5803 C CD1  . PHE   B 1 116 ? 37.753 -19.401 -3.556  1.00 10.42 ?  116 PHE   B CD1  1 
ATOM   5804 C CD2  . PHE   B 1 116 ? 37.397 -20.727 -5.494  1.00 9.98  ?  116 PHE   B CD2  1 
ATOM   5805 C CE1  . PHE   B 1 116 ? 38.691 -20.329 -3.104  1.00 10.40 ?  116 PHE   B CE1  1 
ATOM   5806 C CE2  . PHE   B 1 116 ? 38.327 -21.649 -5.050  1.00 10.42 ?  116 PHE   B CE2  1 
ATOM   5807 C CZ   . PHE   B 1 116 ? 38.969 -21.456 -3.858  1.00 10.18 ?  116 PHE   B CZ   1 
ATOM   5808 H H    . PHE   B 1 116 ? 35.367 -17.837 -3.053  1.00 11.54 ?  116 PHE   B H    1 
ATOM   5809 H HA   . PHE   B 1 116 ? 36.959 -16.863 -4.878  1.00 12.17 ?  116 PHE   B HA   1 
ATOM   5810 H HB2  . PHE   B 1 116 ? 35.154 -19.027 -5.077  1.00 11.75 ?  116 PHE   B HB2  1 
ATOM   5811 H HB3  . PHE   B 1 116 ? 36.109 -18.627 -6.273  1.00 11.75 ?  116 PHE   B HB3  1 
ATOM   5812 H HD1  . PHE   B 1 116 ? 37.561 -18.652 -3.038  1.00 12.53 ?  116 PHE   B HD1  1 
ATOM   5813 H HD2  . PHE   B 1 116 ? 36.957 -20.881 -6.298  1.00 11.99 ?  116 PHE   B HD2  1 
ATOM   5814 H HE1  . PHE   B 1 116 ? 39.136 -20.193 -2.298  1.00 12.49 ?  116 PHE   B HE1  1 
ATOM   5815 H HE2  . PHE   B 1 116 ? 38.520 -22.405 -5.559  1.00 12.52 ?  116 PHE   B HE2  1 
ATOM   5816 H HZ   . PHE   B 1 116 ? 39.607 -22.066 -3.567  1.00 12.23 ?  116 PHE   B HZ   1 
ATOM   5817 N N    . ASN   B 1 117 ? 33.878 -16.164 -5.329  1.00 10.14 ?  117 ASN   B N    1 
ATOM   5818 C CA   . ASN   B 1 117 ? 32.935 -15.462 -6.197  1.00 10.26 ?  117 ASN   B CA   1 
ATOM   5819 C C    . ASN   B 1 117 ? 33.246 -13.981 -6.339  1.00 10.61 ?  117 ASN   B C    1 
ATOM   5820 O O    . ASN   B 1 117 ? 32.657 -13.328 -7.199  1.00 11.49 ?  117 ASN   B O    1 
ATOM   5821 C CB   . ASN   B 1 117 ? 31.509 -15.683 -5.710  1.00 10.44 ?  117 ASN   B CB   1 
ATOM   5822 C CG   . ASN   B 1 117 ? 31.059 -17.094 -5.957  1.00 10.36 ?  117 ASN   B CG   1 
ATOM   5823 O OD1  . ASN   B 1 117 ? 31.405 -17.683 -6.981  1.00 11.38 ?  117 ASN   B OD1  1 
ATOM   5824 N ND2  . ASN   B 1 117 ? 30.323 -17.667 -5.011  1.00 10.62 ?  117 ASN   B ND2  1 
ATOM   5825 H H    . ASN   B 1 117 ? 33.552 -16.421 -4.572  1.00 12.19 ?  117 ASN   B H    1 
ATOM   5826 H HA   . ASN   B 1 117 ? 33.001 -15.857 -7.076  1.00 12.33 ?  117 ASN   B HA   1 
ATOM   5827 H HB2  . ASN   B 1 117 ? 31.466 -15.513 -4.751  1.00 12.55 ?  117 ASN   B HB2  1 
ATOM   5828 H HB3  . ASN   B 1 117 ? 30.915 -15.078 -6.179  1.00 12.55 ?  117 ASN   B HB3  1 
ATOM   5829 H HD21 . ASN   B 1 117 ? 30.036 -18.472 -5.113  1.00 12.76 ?  117 ASN   B HD21 1 
ATOM   5830 H HD22 . ASN   B 1 117 ? 30.103 -17.224 -4.303  1.00 12.76 ?  117 ASN   B HD22 1 
ATOM   5831 N N    . GLN   B 1 118 ? 34.178 -13.453 -5.561  1.00 10.42 ?  118 GLN   B N    1 
ATOM   5832 C CA   . GLN   B 1 118 ? 34.607 -12.067 -5.705  1.00 11.10 ?  118 GLN   B CA   1 
ATOM   5833 C C    . GLN   B 1 118 ? 35.677 -11.879 -6.776  1.00 11.56 ?  118 GLN   B C    1 
ATOM   5834 O O    . GLN   B 1 118 ? 36.153 -10.751 -6.957  1.00 12.64 ?  118 GLN   B O    1 
ATOM   5835 C CB   . GLN   B 1 118 ? 35.087 -11.532 -4.354  1.00 11.88 ?  118 GLN   B CB   1 
ATOM   5836 C CG   . GLN   B 1 118 ? 34.004 -11.578 -3.286  1.00 11.70 ?  118 GLN   B CG   1 
ATOM   5837 C CD   . GLN   B 1 118 ? 32.824 -10.672 -3.620  1.00 11.59 ?  118 GLN   B CD   1 
ATOM   5838 O OE1  . GLN   B 1 118 ? 33.011 -9.529  -4.052  1.00 12.29 ?  118 GLN   B OE1  1 
ATOM   5839 N NE2  . GLN   B 1 118 ? 31.607 -11.160 -3.411  1.00 11.80 ?  118 GLN   B NE2  1 
ATOM   5840 H H    . GLN   B 1 118 ? 34.594 -13.879 -4.940  1.00 12.52 ?  118 GLN   B H    1 
ATOM   5841 H HA   . GLN   B 1 118 ? 33.845 -11.537 -5.975  1.00 13.34 ?  118 GLN   B HA   1 
ATOM   5842 H HB2  . GLN   B 1 118 ? 35.834 -12.059 -4.046  1.00 14.27 ?  118 GLN   B HB2  1 
ATOM   5843 H HB3  . GLN   B 1 118 ? 35.358 -10.601 -4.461  1.00 14.27 ?  118 GLN   B HB3  1 
ATOM   5844 H HG2  . GLN   B 1 118 ? 33.677 -12.484 -3.206  1.00 14.05 ?  118 GLN   B HG2  1 
ATOM   5845 H HG3  . GLN   B 1 118 ? 34.383 -11.282 -2.442  1.00 14.05 ?  118 GLN   B HG3  1 
ATOM   5846 H HE21 . GLN   B 1 118 ? 31.515 -11.961 -3.109  1.00 14.17 ?  118 GLN   B HE21 1 
ATOM   5847 H HE22 . GLN   B 1 118 ? 30.920 -10.683 -3.589  1.00 14.17 ?  118 GLN   B HE22 1 
ATOM   5848 N N    . HIS   B 1 119 ? 36.040 -12.935 -7.507  1.00 10.49 ?  119 HIS   B N    1 
ATOM   5849 C CA   . HIS   B 1 119 ? 37.078 -12.885 -8.527  1.00 10.84 ?  119 HIS   B CA   1 
ATOM   5850 C C    . HIS   B 1 119 ? 36.596 -13.622 -9.761  1.00 10.83 ?  119 HIS   B C    1 
ATOM   5851 O O    . HIS   B 1 119 ? 36.091 -14.738 -9.653  1.00 11.39 ?  119 HIS   B O    1 
ATOM   5852 C CB   . HIS   B 1 119 ? 38.364 -13.513 -7.978  1.00 11.47 ?  119 HIS   B CB   1 
ATOM   5853 C CG   . HIS   B 1 119 ? 38.846 -12.812 -6.754  1.00 12.67 ?  119 HIS   B CG   1 
ATOM   5854 N ND1  . HIS   B 1 119 ? 39.631 -11.679 -6.810  1.00 14.11 ?  119 HIS   B ND1  1 
ATOM   5855 C CD2  . HIS   B 1 119 ? 38.556 -13.009 -5.448  1.00 13.78 ?  119 HIS   B CD2  1 
ATOM   5856 C CE1  . HIS   B 1 119 ? 39.834 -11.235 -5.584  1.00 15.40 ?  119 HIS   B CE1  1 
ATOM   5857 N NE2  . HIS   B 1 119 ? 39.189 -12.019 -4.740  1.00 15.47 ?  119 HIS   B NE2  1 
ATOM   5858 H H    . HIS   B 1 119 ? 35.686 -13.717 -7.432  1.00 12.60 ?  119 HIS   B H    1 
ATOM   5859 H HA   . HIS   B 1 119 ? 37.262 -11.962 -8.767  1.00 13.03 ?  119 HIS   B HA   1 
ATOM   5860 H HB2  . HIS   B 1 119 ? 38.198 -14.438 -7.757  1.00 13.78 ?  119 HIS   B HB2  1 
ATOM   5861 H HB3  . HIS   B 1 119 ? 39.062 -13.450 -8.655  1.00 13.78 ?  119 HIS   B HB3  1 
ATOM   5862 H HD2  . HIS   B 1 119 ? 38.026 -13.694 -5.099  1.00 16.56 ?  119 HIS   B HD2  1 
ATOM   5863 H HE1  . HIS   B 1 119 ? 40.359 -10.507 -5.346  1.00 18.50 ?  119 HIS   B HE1  1 
ATOM   5864 H HE2  . HIS   B 1 119 ? 39.192 -11.948 -3.881  1.00 18.58 ?  119 HIS   B HE2  1 
ATOM   5865 N N    . GLU   B 1 120 ? 36.753 -13.013 -10.933 1.00 11.55 ?  120 GLU   B N    1 
ATOM   5866 C CA   . GLU   B 1 120 ? 36.158 -13.597 -12.128 1.00 12.97 ?  120 GLU   B CA   1 
ATOM   5867 C C    . GLU   B 1 120 ? 36.843 -14.891 -12.547 1.00 11.74 ?  120 GLU   B C    1 
ATOM   5868 O O    . GLU   B 1 120 ? 36.184 -15.760 -13.127 1.00 11.82 ?  120 GLU   B O    1 
ATOM   5869 C CB   . GLU   B 1 120 ? 36.139 -12.588 -13.273 1.00 17.86 ?  120 GLU   B CB   1 
ATOM   5870 C CG   . GLU   B 1 120 ? 35.182 -11.430 -13.031 1.00 24.17 ?  120 GLU   B CG   1 
ATOM   5871 C CD   . GLU   B 1 120 ? 35.034 -10.521 -14.235 1.00 30.61 ?  120 GLU   B CD   1 
ATOM   5872 O OE1  . GLU   B 1 120 ? 36.042 -10.280 -14.932 1.00 32.76 ?  120 GLU   B OE1  1 
ATOM   5873 O OE2  . GLU   B 1 120 ? 33.904 -10.050 -14.484 1.00 33.65 -1 120 GLU   B OE2  1 
ATOM   5874 H H    . GLU   B 1 120 ? 37.183 -12.276 -11.063 1.00 13.88 ?  120 GLU   B H    1 
ATOM   5875 H HA   . GLU   B 1 120 ? 35.239 -13.821 -11.928 1.00 15.58 ?  120 GLU   B HA   1 
ATOM   5876 H HB2  . GLU   B 1 120 ? 37.026 -12.220 -13.386 1.00 21.45 ?  120 GLU   B HB2  1 
ATOM   5877 H HB3  . GLU   B 1 120 ? 35.857 -13.038 -14.085 1.00 21.45 ?  120 GLU   B HB3  1 
ATOM   5878 H HG2  . GLU   B 1 120 ? 34.301 -11.783 -12.823 1.00 29.02 ?  120 GLU   B HG2  1 
ATOM   5879 H HG3  . GLU   B 1 120 ? 35.508 -10.899 -12.288 1.00 29.02 ?  120 GLU   B HG3  1 
ATOM   5880 N N    . VAL   B 1 121 ? 38.143 -15.030 -12.282 1.00 11.10 ?  121 VAL   B N    1 
ATOM   5881 C CA   . VAL   B 1 121 ? 38.890 -16.237 -12.631 1.00 11.37 ?  121 VAL   B CA   1 
ATOM   5882 C C    . VAL   B 1 121 ? 40.006 -16.441 -11.610 1.00 10.78 ?  121 VAL   B C    1 
ATOM   5883 O O    . VAL   B 1 121 ? 40.679 -15.480 -11.212 1.00 11.32 ?  121 VAL   B O    1 
ATOM   5884 C CB   . VAL   B 1 121 ? 39.409 -16.190 -14.087 1.00 12.91 ?  121 VAL   B CB   1 
ATOM   5885 C CG1  . VAL   B 1 121 ? 40.280 -14.964 -14.336 1.00 14.50 ?  121 VAL   B CG1  1 
ATOM   5886 C CG2  . VAL   B 1 121 ? 40.155 -17.467 -14.432 1.00 14.18 ?  121 VAL   B CG2  1 
ATOM   5887 H H    . VAL   B 1 121 ? 38.626 -14.428 -11.900 1.00 13.34 ?  121 VAL   B H    1 
ATOM   5888 H HA   . VAL   B 1 121 ? 38.282 -16.992 -12.568 1.00 13.66 ?  121 VAL   B HA   1 
ATOM   5889 H HB   . VAL   B 1 121 ? 38.646 -16.131 -14.687 1.00 15.50 ?  121 VAL   B HB   1 
ATOM   5890 H HG11 . VAL   B 1 121 ? 40.587 -14.973 -15.256 1.00 17.42 ?  121 VAL   B HG11 1 
ATOM   5891 H HG12 . VAL   B 1 121 ? 39.754 -14.163 -14.173 1.00 17.42 ?  121 VAL   B HG12 1 
ATOM   5892 H HG13 . VAL   B 1 121 ? 41.040 -14.988 -13.734 1.00 17.42 ?  121 VAL   B HG13 1 
ATOM   5893 H HG21 . VAL   B 1 121 ? 40.347 -17.473 -15.385 1.00 17.03 ?  121 VAL   B HG21 1 
ATOM   5894 H HG22 . VAL   B 1 121 ? 40.986 -17.494 -13.932 1.00 17.03 ?  121 VAL   B HG22 1 
ATOM   5895 H HG23 . VAL   B 1 121 ? 39.604 -18.229 -14.203 1.00 17.03 ?  121 VAL   B HG23 1 
ATOM   5896 N N    . LEU   B 1 122 ? 40.192 -17.700 -11.179 1.00 10.56 ?  122 LEU   B N    1 
ATOM   5897 C CA   . LEU   B 1 122 ? 41.180 -18.042 -10.157 1.00 10.20 ?  122 LEU   B CA   1 
ATOM   5898 C C    . LEU   B 1 122 ? 41.830 -19.376 -10.474 1.00 9.92  ?  122 LEU   B C    1 
ATOM   5899 O O    . LEU   B 1 122 ? 41.173 -20.294 -10.972 1.00 11.14 ?  122 LEU   B O    1 
ATOM   5900 C CB   . LEU   B 1 122 ? 40.535 -18.257 -8.775  1.00 12.03 ?  122 LEU   B CB   1 
ATOM   5901 C CG   . LEU   B 1 122 ? 39.488 -17.252 -8.286  1.00 11.79 ?  122 LEU   B CG   1 
ATOM   5902 C CD1  . LEU   B 1 122 ? 38.083 -17.602 -8.760  1.00 12.62 ?  122 LEU   B CD1  1 
ATOM   5903 C CD2  . LEU   B 1 122 ? 39.528 -17.145 -6.775  1.00 11.33 ?  122 LEU   B CD2  1 
ATOM   5904 H H    . LEU   B 1 122 ? 39.750 -18.382 -11.473 1.00 12.69 ?  122 LEU   B H    1 
ATOM   5905 H HA   . LEU   B 1 122 ? 41.858 -17.351 -10.099 1.00 12.25 ?  122 LEU   B HA   1 
ATOM   5906 H HB2  . LEU   B 1 122 ? 40.106 -19.123 -8.779  1.00 14.45 ?  122 LEU   B HB2  1 
ATOM   5907 H HB3  . LEU   B 1 122 ? 41.242 -18.253 -8.115  1.00 14.45 ?  122 LEU   B HB3  1 
ATOM   5908 H HG   . LEU   B 1 122 ? 39.698 -16.378 -8.644  1.00 14.16 ?  122 LEU   B HG   1 
ATOM   5909 H HD11 . LEU   B 1 122 ? 37.450 -16.963 -8.387  1.00 15.16 ?  122 LEU   B HD11 1 
ATOM   5910 H HD12 . LEU   B 1 122 ? 38.053 -17.553 -9.732  1.00 15.16 ?  122 LEU   B HD12 1 
ATOM   5911 H HD13 . LEU   B 1 122 ? 37.857 -18.496 -8.469  1.00 15.16 ?  122 LEU   B HD13 1 
ATOM   5912 H HD21 . LEU   B 1 122 ? 38.832 -16.536 -6.480  1.00 13.61 ?  122 LEU   B HD21 1 
ATOM   5913 H HD22 . LEU   B 1 122 ? 39.382 -18.024 -6.392  1.00 13.61 ?  122 LEU   B HD22 1 
ATOM   5914 H HD23 . LEU   B 1 122 ? 40.397 -16.808 -6.510  1.00 13.61 ?  122 LEU   B HD23 1 
ATOM   5915 N N    . LEU   B 1 123 ? 43.117 -19.485 -10.126 1.00 9.68  ?  123 LEU   B N    1 
ATOM   5916 C CA   . LEU   B 1 123 ? 43.831 -20.751 -9.998  1.00 9.91  ?  123 LEU   B CA   1 
ATOM   5917 C C    . LEU   B 1 123 ? 43.797 -21.140 -8.525  1.00 9.71  ?  123 LEU   B C    1 
ATOM   5918 O O    . LEU   B 1 123 ? 44.159 -20.321 -7.670  1.00 10.33 ?  123 LEU   B O    1 
ATOM   5919 C CB   . LEU   B 1 123 ? 45.283 -20.569 -10.452 1.00 10.25 ?  123 LEU   B CB   1 
ATOM   5920 C CG   . LEU   B 1 123 ? 46.238 -21.743 -10.217 1.00 10.87 ?  123 LEU   B CG   1 
ATOM   5921 C CD1  . LEU   B 1 123 ? 45.807 -22.995 -10.997 1.00 11.21 ?  123 LEU   B CD1  1 
ATOM   5922 C CD2  . LEU   B 1 123 ? 47.650 -21.339 -10.599 1.00 11.48 ?  123 LEU   B CD2  1 
ATOM   5923 H H    . LEU   B 1 123 ? 43.616 -18.803 -9.942  1.00 11.63 ?  123 LEU   B H    1 
ATOM   5924 H HA   . LEU   B 1 123 ? 43.401 -21.442 -10.531 1.00 11.91 ?  123 LEU   B HA   1 
ATOM   5925 H HB2  . LEU   B 1 123 ? 45.277 -20.393 -11.407 1.00 12.32 ?  123 LEU   B HB2  1 
ATOM   5926 H HB3  . LEU   B 1 123 ? 45.649 -19.804 -9.988  1.00 12.32 ?  123 LEU   B HB3  1 
ATOM   5927 H HG   . LEU   B 1 123 ? 46.239 -21.965 -9.275  1.00 13.06 ?  123 LEU   B HG   1 
ATOM   5928 H HD11 . LEU   B 1 123 ? 46.447 -23.701 -10.831 1.00 13.47 ?  123 LEU   B HD11 1 
ATOM   5929 H HD12 . LEU   B 1 123 ? 44.926 -23.265 -10.692 1.00 13.47 ?  123 LEU   B HD12 1 
ATOM   5930 H HD13 . LEU   B 1 123 ? 45.780 -22.782 -11.942 1.00 13.47 ?  123 LEU   B HD13 1 
ATOM   5931 H HD21 . LEU   B 1 123 ? 48.246 -22.084 -10.449 1.00 13.80 ?  123 LEU   B HD21 1 
ATOM   5932 H HD22 . LEU   B 1 123 ? 47.664 -21.084 -11.538 1.00 13.80 ?  123 LEU   B HD22 1 
ATOM   5933 H HD23 . LEU   B 1 123 ? 47.919 -20.580 -10.053 1.00 13.80 ?  123 LEU   B HD23 1 
ATOM   5934 N N    . ALA   B 1 124 ? 43.369 -22.373 -8.221  1.00 9.63  ?  124 ALA   B N    1 
ATOM   5935 C CA   . ALA   B 1 124 ? 43.116 -22.694 -6.824  1.00 9.55  ?  124 ALA   B CA   1 
ATOM   5936 C C    . ALA   B 1 124 ? 43.381 -24.153 -6.490  1.00 9.37  ?  124 ALA   B C    1 
ATOM   5937 O O    . ALA   B 1 124 ? 43.265 -25.026 -7.361  1.00 10.06 ?  124 ALA   B O    1 
ATOM   5938 C CB   . ALA   B 1 124 ? 41.660 -22.368 -6.457  1.00 10.03 ?  124 ALA   B CB   1 
ATOM   5939 H H    . ALA   B 1 124 ? 43.217 -23.016 -8.782  1.00 11.58 ?  124 ALA   B H    1 
ATOM   5940 H HA   . ALA   B 1 124 ? 43.692 -22.142 -6.278  1.00 11.47 ?  124 ALA   B HA   1 
ATOM   5941 H HB1  . ALA   B 1 124 ? 41.510 -22.580 -5.523  1.00 12.05 ?  124 ALA   B HB1  1 
ATOM   5942 H HB2  . ALA   B 1 124 ? 41.504 -21.417 -6.606  1.00 12.05 ?  124 ALA   B HB2  1 
ATOM   5943 H HB3  . ALA   B 1 124 ? 41.065 -22.887 -7.017  1.00 12.05 ?  124 ALA   B HB3  1 
ATOM   5944 N N    . PRO   B 1 125 ? 43.676 -24.443 -5.223  1.00 9.82  ?  125 PRO   B N    1 
ATOM   5945 C CA   . PRO   B 1 125 ? 43.622 -25.807 -4.700  1.00 10.50 ?  125 PRO   B CA   1 
ATOM   5946 C C    . PRO   B 1 125 ? 42.221 -26.082 -4.158  1.00 10.49 ?  125 PRO   B C    1 
ATOM   5947 O O    . PRO   B 1 125 ? 41.423 -25.172 -3.941  1.00 11.03 ?  125 PRO   B O    1 
ATOM   5948 C CB   . PRO   B 1 125 ? 44.604 -25.719 -3.524  1.00 11.56 ?  125 PRO   B CB   1 
ATOM   5949 C CG   . PRO   B 1 125 ? 44.345 -24.341 -2.961  1.00 11.46 ?  125 PRO   B CG   1 
ATOM   5950 C CD   . PRO   B 1 125 ? 44.015 -23.473 -4.160  1.00 10.39 ?  125 PRO   B CD   1 
ATOM   5951 H HA   . PRO   B 1 125 ? 43.902 -26.475 -5.348  1.00 12.61 ?  125 PRO   B HA   1 
ATOM   5952 H HB2  . PRO   B 1 125 ? 44.401 -26.406 -2.866  1.00 13.89 ?  125 PRO   B HB2  1 
ATOM   5953 H HB3  . PRO   B 1 125 ? 45.515 -25.799 -3.841  1.00 13.89 ?  125 PRO   B HB3  1 
ATOM   5954 H HG2  . PRO   B 1 125 ? 43.592 -24.370 -2.345  1.00 13.77 ?  125 PRO   B HG2  1 
ATOM   5955 H HG3  . PRO   B 1 125 ? 45.140 -24.014 -2.506  1.00 13.77 ?  125 PRO   B HG3  1 
ATOM   5956 H HD2  . PRO   B 1 125 ? 43.259 -22.896 -3.970  1.00 12.49 ?  125 PRO   B HD2  1 
ATOM   5957 H HD3  . PRO   B 1 125 ? 44.797 -22.949 -4.422  1.00 12.49 ?  125 PRO   B HD3  1 
ATOM   5958 N N    . LEU   B 1 126 ? 41.953 -27.365 -3.884  1.00 10.86 ?  126 LEU   B N    1 
ATOM   5959 C CA   . LEU   B 1 126 ? 40.729 -27.738 -3.176  1.00 11.47 ?  126 LEU   B CA   1 
ATOM   5960 C C    . LEU   B 1 126 ? 40.831 -27.335 -1.711  1.00 11.62 ?  126 LEU   B C    1 
ATOM   5961 O O    . LEU   B 1 126 ? 41.709 -27.801 -0.980  1.00 13.37 ?  126 LEU   B O    1 
ATOM   5962 C CB   . LEU   B 1 126 ? 40.471 -29.235 -3.289  1.00 12.71 ?  126 LEU   B CB   1 
ATOM   5963 C CG   . LEU   B 1 126 ? 39.953 -29.724 -4.641  1.00 13.80 ?  126 LEU   B CG   1 
ATOM   5964 C CD1  . LEU   B 1 126 ? 39.991 -31.234 -4.704  1.00 15.71 ?  126 LEU   B CD1  1 
ATOM   5965 C CD2  . LEU   B 1 126 ? 38.538 -29.228 -4.893  1.00 14.11 ?  126 LEU   B CD2  1 
ATOM   5966 H H    . LEU   B 1 126 ? 42.462 -28.033 -4.090  1.00 13.05 ?  126 LEU   B H    1 
ATOM   5967 H HA   . LEU   B 1 126 ? 39.982 -27.267 -3.571  1.00 13.78 ?  126 LEU   B HA   1 
ATOM   5968 H HB2  . LEU   B 1 126 ? 41.300 -29.704 -3.106  1.00 15.26 ?  126 LEU   B HB2  1 
ATOM   5969 H HB3  . LEU   B 1 126 ? 39.809 -29.480 -2.620  1.00 15.26 ?  126 LEU   B HB3  1 
ATOM   5970 H HG   . LEU   B 1 126 ? 40.528 -29.379 -5.344  1.00 16.57 ?  126 LEU   B HG   1 
ATOM   5971 H HD11 . LEU   B 1 126 ? 39.658 -31.524 -5.568  1.00 18.86 ?  126 LEU   B HD11 1 
ATOM   5972 H HD12 . LEU   B 1 126 ? 40.903 -31.536 -4.582  1.00 18.86 ?  126 LEU   B HD12 1 
ATOM   5973 H HD13 . LEU   B 1 126 ? 39.427 -31.593 -3.998  1.00 18.86 ?  126 LEU   B HD13 1 
ATOM   5974 H HD21 . LEU   B 1 126 ? 38.193 -29.644 -5.697  1.00 16.95 ?  126 LEU   B HD21 1 
ATOM   5975 H HD22 . LEU   B 1 126 ? 37.981 -29.459 -4.134  1.00 16.95 ?  126 LEU   B HD22 1 
ATOM   5976 H HD23 . LEU   B 1 126 ? 38.555 -28.261 -5.004  1.00 16.95 ?  126 LEU   B HD23 1 
ATOM   5977 N N    . LEU   B 1 127 ? 39.906 -26.496 -1.265  1.00 11.55 ?  127 LEU   B N    1 
ATOM   5978 C CA   . LEU   B 1 127 ? 39.956 -26.000 0.099   1.00 12.03 ?  127 LEU   B CA   1 
ATOM   5979 C C    . LEU   B 1 127 ? 39.685 -27.123 1.096   1.00 11.73 ?  127 LEU   B C    1 
ATOM   5980 O O    . LEU   B 1 127 ? 38.865 -28.025 0.869   1.00 12.13 ?  127 LEU   B O    1 
ATOM   5981 C CB   . LEU   B 1 127 ? 38.937 -24.882 0.304   1.00 12.16 ?  127 LEU   B CB   1 
ATOM   5982 C CG   . LEU   B 1 127 ? 39.120 -23.613 -0.532  1.00 12.82 ?  127 LEU   B CG   1 
ATOM   5983 C CD1  . LEU   B 1 127 ? 38.000 -22.651 -0.198  1.00 13.03 ?  127 LEU   B CD1  1 
ATOM   5984 C CD2  . LEU   B 1 127 ? 40.482 -22.968 -0.291  1.00 13.75 ?  127 LEU   B CD2  1 
ATOM   5985 H H    . LEU   B 1 127 ? 39.244 -26.190 -1.729  1.00 13.88 ?  127 LEU   B H    1 
ATOM   5986 H HA   . LEU   B 1 127 ? 40.841 -25.635 0.276   1.00 14.45 ?  127 LEU   B HA   1 
ATOM   5987 H HB2  . LEU   B 1 127 ? 38.055 -25.231 0.101   1.00 14.61 ?  127 LEU   B HB2  1 
ATOM   5988 H HB3  . LEU   B 1 127 ? 38.962 -24.610 1.237   1.00 14.61 ?  127 LEU   B HB3  1 
ATOM   5989 H HG   . LEU   B 1 127 ? 39.040 -23.831 -1.471  1.00 15.41 ?  127 LEU   B HG   1 
ATOM   5990 H HD11 . LEU   B 1 127 ? 38.109 -21.837 -0.722  1.00 15.65 ?  127 LEU   B HD11 1 
ATOM   5991 H HD12 . LEU   B 1 127 ? 37.146 -23.060 -0.408  1.00 15.65 ?  127 LEU   B HD12 1 
ATOM   5992 H HD13 . LEU   B 1 127 ? 38.035 -22.432 0.749   1.00 15.65 ?  127 LEU   B HD13 1 
ATOM   5993 H HD21 . LEU   B 1 127 ? 40.517 -22.114 -0.754  1.00 16.51 ?  127 LEU   B HD21 1 
ATOM   5994 H HD22 . LEU   B 1 127 ? 40.603 -22.829 0.663   1.00 16.51 ?  127 LEU   B HD22 1 
ATOM   5995 H HD23 . LEU   B 1 127 ? 41.170 -23.557 -0.631  1.00 16.51 ?  127 LEU   B HD23 1 
ATOM   5996 N N    . SER   B 1 128 ? 40.385 -27.041 2.220   1.00 11.80 ?  128 SER   B N    1 
ATOM   5997 C CA   . SER   B 1 128 ? 40.276 -27.953 3.344   1.00 12.16 ?  128 SER   B CA   1 
ATOM   5998 C C    . SER   B 1 128 ? 40.773 -29.359 3.028   1.00 12.88 ?  128 SER   B C    1 
ATOM   5999 O O    . SER   B 1 128 ? 40.677 -30.229 3.885   1.00 14.57 ?  128 SER   B O    1 
ATOM   6000 C CB   . SER   B 1 128 ? 38.874 -27.964 3.975   1.00 12.79 ?  128 SER   B CB   1 
ATOM   6001 O OG   . SER   B 1 128 ? 38.543 -26.694 4.524   1.00 13.14 ?  128 SER   B OG   1 
ATOM   6002 H H    . SER   B 1 128 ? 40.969 -26.423 2.359   1.00 14.17 ?  128 SER   B H    1 
ATOM   6003 H HA   . SER   B 1 128 ? 40.862 -27.614 4.029   1.00 14.61 ?  128 SER   B HA   1 
ATOM   6004 H HB2  . SER   B 1 128 ? 38.217 -28.200 3.300   1.00 15.36 ?  128 SER   B HB2  1 
ATOM   6005 H HB3  . SER   B 1 128 ? 38.855 -28.630 4.690   1.00 15.36 ?  128 SER   B HB3  1 
ATOM   6006 H HG   . SER   B 1 128 ? 39.101 -26.484 5.114   1.00 15.78 ?  128 SER   B HG   1 
ATOM   6007 N N    . ALA   B 1 129 ? 41.352 -29.585 1.846   1.00 13.90 ?  129 ALA   B N    1 
ATOM   6008 C CA   . ALA   B 1 129 ? 41.893 -30.888 1.494   1.00 14.69 ?  129 ALA   B CA   1 
ATOM   6009 C C    . ALA   B 1 129 ? 43.286 -31.064 2.089   1.00 13.99 ?  129 ALA   B C    1 
ATOM   6010 O O    . ALA   B 1 129 ? 43.841 -30.166 2.735   1.00 14.00 ?  129 ALA   B O    1 
ATOM   6011 C CB   . ALA   B 1 129 ? 41.939 -31.051 -0.022  1.00 16.45 ?  129 ALA   B CB   1 
ATOM   6012 H H    . ALA   B 1 129 ? 41.434 -28.991 1.224   1.00 16.69 ?  129 ALA   B H    1 
ATOM   6013 H HA   . ALA   B 1 129 ? 41.315 -31.577 1.855   1.00 17.65 ?  129 ALA   B HA   1 
ATOM   6014 H HB1  . ALA   B 1 129 ? 42.292 -31.930 -0.233  1.00 19.76 ?  129 ALA   B HB1  1 
ATOM   6015 H HB2  . ALA   B 1 129 ? 41.041 -30.963 -0.377  1.00 19.76 ?  129 ALA   B HB2  1 
ATOM   6016 H HB3  . ALA   B 1 129 ? 42.513 -30.365 -0.397  1.00 19.76 ?  129 ALA   B HB3  1 
ATOM   6017 N N    . GLY   B 1 130 ? 43.853 -32.245 1.860   1.00 14.05 ?  130 GLY   B N    1 
ATOM   6018 C CA   . GLY   B 1 130 ? 45.239 -32.476 2.221   1.00 14.85 ?  130 GLY   B CA   1 
ATOM   6019 C C    . GLY   B 1 130 ? 45.448 -32.380 3.712   1.00 14.74 ?  130 GLY   B C    1 
ATOM   6020 O O    . GLY   B 1 130 ? 44.742 -33.019 4.508   1.00 15.56 ?  130 GLY   B O    1 
ATOM   6021 H H    . GLY   B 1 130 ? 43.459 -32.918 1.495   1.00 16.87 ?  130 GLY   B H    1 
ATOM   6022 H HA2  . GLY   B 1 130 ? 45.508 -33.360 1.927   1.00 17.84 ?  130 GLY   B HA2  1 
ATOM   6023 H HA3  . GLY   B 1 130 ? 45.802 -31.819 1.784   1.00 17.84 ?  130 GLY   B HA3  1 
ATOM   6024 N N    . ILE   B 1 131 ? 46.425 -31.555 4.104   1.00 14.99 ?  131 ILE   B N    1 
ATOM   6025 C CA   . ILE   B 1 131 ? 46.775 -31.415 5.508   1.00 15.91 ?  131 ILE   B CA   1 
ATOM   6026 C C    . ILE   B 1 131 ? 45.646 -30.830 6.341   1.00 15.32 ?  131 ILE   B C    1 
ATOM   6027 O O    . ILE   B 1 131 ? 45.704 -30.908 7.570   1.00 16.78 ?  131 ILE   B O    1 
ATOM   6028 C CB   . ILE   B 1 131 ? 48.092 -30.623 5.710   1.00 18.20 ?  131 ILE   B CB   1 
ATOM   6029 C CG1  . ILE   B 1 131 ? 47.909 -29.134 5.370   1.00 18.84 ?  131 ILE   B CG1  1 
ATOM   6030 C CG2  . ILE   B 1 131 ? 49.226 -31.248 4.893   1.00 19.34 ?  131 ILE   B CG2  1 
ATOM   6031 C CD1  . ILE   B 1 131 ? 49.117 -28.271 5.704   1.00 19.83 ?  131 ILE   B CD1  1 
ATOM   6032 H H    . ILE   B 1 131 ? 46.903 -31.076 3.571   1.00 18.00 ?  131 ILE   B H    1 
ATOM   6033 H HA   . ILE   B 1 131 ? 46.937 -32.304 5.855   1.00 19.11 ?  131 ILE   B HA   1 
ATOM   6034 H HB   . ILE   B 1 131 ? 48.330 -30.685 6.647   1.00 21.86 ?  131 ILE   B HB   1 
ATOM   6035 H HG12 . ILE   B 1 131 ? 47.736 -29.050 4.421   1.00 22.62 ?  131 ILE   B HG12 1 
ATOM   6036 H HG13 . ILE   B 1 131 ? 47.156 -28.781 5.872   1.00 22.62 ?  131 ILE   B HG13 1 
ATOM   6037 H HG21 . ILE   B 1 131 ? 50.060 -30.827 5.146   1.00 23.22 ?  131 ILE   B HG21 1 
ATOM   6038 H HG22 . ILE   B 1 131 ? 49.258 -32.195 5.080   1.00 23.22 ?  131 ILE   B HG22 1 
ATOM   6039 H HG23 . ILE   B 1 131 ? 49.049 -31.098 3.951   1.00 23.22 ?  131 ILE   B HG23 1 
ATOM   6040 H HD11 . ILE   B 1 131 ? 48.891 -27.341 5.549   1.00 23.81 ?  131 ILE   B HD11 1 
ATOM   6041 H HD12 . ILE   B 1 131 ? 49.350 -28.404 6.637   1.00 23.81 ?  131 ILE   B HD12 1 
ATOM   6042 H HD13 . ILE   B 1 131 ? 49.858 -28.533 5.137   1.00 23.81 ?  131 ILE   B HD13 1 
ATOM   6043 N N    . PHE   B 1 132 ? 44.621 -30.247 5.707   1.00 13.98 ?  132 PHE   B N    1 
ATOM   6044 C CA   . PHE   B 1 132 ? 43.459 -29.741 6.434   1.00 14.17 ?  132 PHE   B CA   1 
ATOM   6045 C C    . PHE   B 1 132 ? 42.434 -30.833 6.762   1.00 15.51 ?  132 PHE   B C    1 
ATOM   6046 O O    . PHE   B 1 132 ? 41.528 -30.585 7.567   1.00 17.39 ?  132 PHE   B O    1 
ATOM   6047 C CB   . PHE   B 1 132 ? 42.782 -28.603 5.657   1.00 13.29 ?  132 PHE   B CB   1 
ATOM   6048 C CG   . PHE   B 1 132 ? 43.476 -27.259 5.775   1.00 13.34 ?  132 PHE   B CG   1 
ATOM   6049 C CD1  . PHE   B 1 132 ? 44.765 -27.068 5.288   1.00 14.43 ?  132 PHE   B CD1  1 
ATOM   6050 C CD2  . PHE   B 1 132 ? 42.808 -26.169 6.316   1.00 12.54 ?  132 PHE   B CD2  1 
ATOM   6051 C CE1  . PHE   B 1 132 ? 45.382 -25.827 5.379   1.00 15.26 ?  132 PHE   B CE1  1 
ATOM   6052 C CE2  . PHE   B 1 132 ? 43.417 -24.927 6.401   1.00 13.44 ?  132 PHE   B CE2  1 
ATOM   6053 C CZ   . PHE   B 1 132 ? 44.704 -24.759 5.937   1.00 15.00 ?  132 PHE   B CZ   1 
ATOM   6054 H H    . PHE   B 1 132 ? 44.577 -30.136 4.852   1.00 16.79 ?  132 PHE   B H    1 
ATOM   6055 H HA   . PHE   B 1 132 ? 43.767 -29.373 7.272   1.00 17.02 ?  132 PHE   B HA   1 
ATOM   6056 H HB2  . PHE   B 1 132 ? 42.767 -28.837 4.717   1.00 15.97 ?  132 PHE   B HB2  1 
ATOM   6057 H HB3  . PHE   B 1 132 ? 41.878 -28.496 5.986   1.00 15.97 ?  132 PHE   B HB3  1 
ATOM   6058 H HD1  . PHE   B 1 132 ? 45.225 -27.788 4.916   1.00 17.34 ?  132 PHE   B HD1  1 
ATOM   6059 H HD2  . PHE   B 1 132 ? 41.943 -26.279 6.635   1.00 15.07 ?  132 PHE   B HD2  1 
ATOM   6060 H HE1  . PHE   B 1 132 ? 46.250 -25.717 5.064   1.00 18.32 ?  132 PHE   B HE1  1 
ATOM   6061 H HE2  . PHE   B 1 132 ? 42.964 -24.209 6.783   1.00 16.14 ?  132 PHE   B HE2  1 
ATOM   6062 H HZ   . PHE   B 1 132 ? 45.115 -23.923 6.002   1.00 18.02 ?  132 PHE   B HZ   1 
ATOM   6063 N N    . GLY   B 1 133 ? 42.539 -32.027 6.160   1.00 15.16 ?  133 GLY   B N    1 
ATOM   6064 C CA   . GLY   B 1 133 ? 41.830 -33.198 6.647   1.00 16.33 ?  133 GLY   B CA   1 
ATOM   6065 C C    . GLY   B 1 133 ? 40.436 -33.465 6.110   1.00 16.54 ?  133 GLY   B C    1 
ATOM   6066 O O    . GLY   B 1 133 ? 39.851 -34.489 6.476   1.00 18.41 ?  133 GLY   B O    1 
ATOM   6067 H H    . GLY   B 1 133 ? 43.031 -32.179 5.467   1.00 18.21 ?  133 GLY   B H    1 
ATOM   6068 H HA2  . GLY   B 1 133 ? 42.369 -33.980 6.455   1.00 19.61 ?  133 GLY   B HA2  1 
ATOM   6069 H HA3  . GLY   B 1 133 ? 41.756 -33.125 7.610   1.00 19.61 ?  133 GLY   B HA3  1 
ATOM   6070 N N    . ALA   B 1 134 ? 39.870 -32.599 5.279   1.00 15.58 ?  134 ALA   B N    1 
ATOM   6071 C CA   . ALA   B 1 134 ? 38.546 -32.880 4.746   1.00 15.85 ?  134 ALA   B CA   1 
ATOM   6072 C C    . ALA   B 1 134 ? 38.628 -33.873 3.590   1.00 15.85 ?  134 ALA   B C    1 
ATOM   6073 O O    . ALA   B 1 134 ? 39.679 -34.063 2.973   1.00 16.75 ?  134 ALA   B O    1 
ATOM   6074 C CB   . ALA   B 1 134 ? 37.869 -31.595 4.274   1.00 15.91 ?  134 ALA   B CB   1 
ATOM   6075 H H    . ALA   B 1 134 ? 40.218 -31.857 5.019   1.00 18.71 ?  134 ALA   B H    1 
ATOM   6076 H HA   . ALA   B 1 134 ? 37.996 -33.271 5.448   1.00 19.03 ?  134 ALA   B HA   1 
ATOM   6077 H HB1  . ALA   B 1 134 ? 36.985 -31.813 3.938   1.00 19.11 ?  134 ALA   B HB1  1 
ATOM   6078 H HB2  . ALA   B 1 134 ? 37.798 -30.984 5.022   1.00 19.11 ?  134 ALA   B HB2  1 
ATOM   6079 H HB3  . ALA   B 1 134 ? 38.405 -31.201 3.570   1.00 19.11 ?  134 ALA   B HB3  1 
ATOM   6080 N N    . ASP   B 1 135 ? 37.496 -34.502 3.300   1.00 16.02 ?  135 ASP   B N    1 
ATOM   6081 C CA   . ASP   B 1 135 ? 37.395 -35.395 2.154   1.00 16.81 ?  135 ASP   B CA   1 
ATOM   6082 C C    . ASP   B 1 135 ? 37.497 -34.561 0.883   1.00 15.50 ?  135 ASP   B C    1 
ATOM   6083 O O    . ASP   B 1 135 ? 36.644 -33.688 0.656   1.00 15.47 ?  135 ASP   B O    1 
ATOM   6084 C CB   . ASP   B 1 135 ? 36.052 -36.126 2.218   1.00 18.96 ?  135 ASP   B CB   1 
ATOM   6085 C CG   . ASP   B 1 135 ? 35.849 -37.109 1.079   1.00 20.87 ?  135 ASP   B CG   1 
ATOM   6086 O OD1  . ASP   B 1 135 ? 36.714 -37.187 0.182   1.00 20.54 ?  135 ASP   B OD1  1 
ATOM   6087 O OD2  . ASP   B 1 135 ? 34.818 -37.824 1.100   1.00 23.71 -1 135 ASP   B OD2  1 
ATOM   6088 H H    . ASP   B 1 135 ? 36.774 -34.432 3.754   1.00 19.24 ?  135 ASP   B H    1 
ATOM   6089 H HA   . ASP   B 1 135 ? 38.114 -36.051 2.184   1.00 20.19 ?  135 ASP   B HA   1 
ATOM   6090 H HB2  . ASP   B 1 135 ? 36.007 -36.618 3.047   1.00 22.76 ?  135 ASP   B HB2  1 
ATOM   6091 H HB3  . ASP   B 1 135 ? 35.344 -35.469 2.173   1.00 22.76 ?  135 ASP   B HB3  1 
ATOM   6092 N N    . PRO   B 1 136 ? 38.511 -34.769 0.040   1.00 15.56 ?  136 PRO   B N    1 
ATOM   6093 C CA   . PRO   B 1 136 ? 38.614 -33.942 -1.173  1.00 14.80 ?  136 PRO   B CA   1 
ATOM   6094 C C    . PRO   B 1 136 ? 37.425 -34.095 -2.102  1.00 14.12 ?  136 PRO   B C    1 
ATOM   6095 O O    . PRO   B 1 136 ? 37.102 -33.148 -2.828  1.00 13.45 ?  136 PRO   B O    1 
ATOM   6096 C CB   . PRO   B 1 136 ? 39.926 -34.419 -1.817  1.00 16.16 ?  136 PRO   B CB   1 
ATOM   6097 C CG   . PRO   B 1 136 ? 40.131 -35.811 -1.275  1.00 17.32 ?  136 PRO   B CG   1 
ATOM   6098 C CD   . PRO   B 1 136 ? 39.595 -35.763 0.127   1.00 16.70 ?  136 PRO   B CD   1 
ATOM   6099 H HA   . PRO   B 1 136 ? 38.703 -33.005 -0.938  1.00 17.78 ?  136 PRO   B HA   1 
ATOM   6100 H HB2  . PRO   B 1 136 ? 39.831 -34.435 -2.785  1.00 19.41 ?  136 PRO   B HB2  1 
ATOM   6101 H HB3  . PRO   B 1 136 ? 40.651 -33.832 -1.554  1.00 19.41 ?  136 PRO   B HB3  1 
ATOM   6102 H HG2  . PRO   B 1 136 ? 39.633 -36.452 -1.807  1.00 20.80 ?  136 PRO   B HG2  1 
ATOM   6103 H HG3  . PRO   B 1 136 ? 41.077 -36.028 -1.271  1.00 20.80 ?  136 PRO   B HG3  1 
ATOM   6104 H HD2  . PRO   B 1 136 ? 39.239 -36.624 0.387   1.00 20.05 ?  136 PRO   B HD2  1 
ATOM   6105 H HD3  . PRO   B 1 136 ? 40.280 -35.457 0.747   1.00 20.05 ?  136 PRO   B HD3  1 
ATOM   6106 N N    . ILE   B 1 137 ? 36.764 -35.260 -2.102  1.00 14.74 ?  137 ILE   B N    1 
ATOM   6107 C CA   . ILE   B 1 137 ? 35.544 -35.429 -2.891  1.00 14.98 ?  137 ILE   B CA   1 
ATOM   6108 C C    . ILE   B 1 137 ? 34.465 -34.455 -2.421  1.00 14.46 ?  137 ILE   B C    1 
ATOM   6109 O O    . ILE   B 1 137 ? 33.752 -33.843 -3.229  1.00 14.18 ?  137 ILE   B O    1 
ATOM   6110 C CB   . ILE   B 1 137 ? 35.069 -36.896 -2.827  1.00 17.20 ?  137 ILE   B CB   1 
ATOM   6111 C CG1  . ILE   B 1 137 ? 36.081 -37.807 -3.523  1.00 19.53 ?  137 ILE   B CG1  1 
ATOM   6112 C CG2  . ILE   B 1 137 ? 33.675 -37.045 -3.443  1.00 17.80 ?  137 ILE   B CG2  1 
ATOM   6113 C CD1  . ILE   B 1 137 ? 35.723 -39.277 -3.469  1.00 22.06 ?  137 ILE   B CD1  1 
ATOM   6114 H H    . ILE   B 1 137 ? 36.997 -35.958 -1.659  1.00 17.70 ?  137 ILE   B H    1 
ATOM   6115 H HA   . ILE   B 1 137 ? 35.739 -35.227 -3.821  1.00 18.00 ?  137 ILE   B HA   1 
ATOM   6116 H HB   . ILE   B 1 137 ? 35.011 -37.156 -1.900  1.00 20.65 ?  137 ILE   B HB   1 
ATOM   6117 H HG12 . ILE   B 1 137 ? 36.146 -37.555 -4.457  1.00 23.45 ?  137 ILE   B HG12 1 
ATOM   6118 H HG13 . ILE   B 1 137 ? 36.943 -37.701 -3.092  1.00 23.45 ?  137 ILE   B HG13 1 
ATOM   6119 H HG21 . ILE   B 1 137 ? 33.391 -37.970 -3.384  1.00 21.38 ?  137 ILE   B HG21 1 
ATOM   6120 H HG22 . ILE   B 1 137 ? 33.043 -36.494 -2.959  1.00 21.38 ?  137 ILE   B HG22 1 
ATOM   6121 H HG23 . ILE   B 1 137 ? 33.709 -36.770 -4.373  1.00 21.38 ?  137 ILE   B HG23 1 
ATOM   6122 H HD11 . ILE   B 1 137 ? 36.358 -39.758 -4.016  1.00 26.49 ?  137 ILE   B HD11 1 
ATOM   6123 H HD12 . ILE   B 1 137 ? 35.769 -39.584 -2.550  1.00 26.49 ?  137 ILE   B HD12 1 
ATOM   6124 H HD13 . ILE   B 1 137 ? 34.832 -39.415 -3.823  1.00 26.49 ?  137 ILE   B HD13 1 
ATOM   6125 N N    . HIS   B 1 138 ? 34.328 -34.296 -1.106  1.00 14.49 ?  138 HIS   B N    1 
ATOM   6126 C CA   . HIS   B 1 138 ? 33.374 -33.331 -0.576  1.00 14.79 ?  138 HIS   B CA   1 
ATOM   6127 C C    . HIS   B 1 138 ? 33.799 -31.903 -0.887  1.00 13.97 ?  138 HIS   B C    1 
ATOM   6128 O O    . HIS   B 1 138 ? 32.956 -31.058 -1.198  1.00 14.69 ?  138 HIS   B O    1 
ATOM   6129 C CB   . HIS   B 1 138 ? 33.243 -33.519 0.927   1.00 16.47 ?  138 HIS   B CB   1 
ATOM   6130 C CG   . HIS   B 1 138 ? 32.314 -32.539 1.564   1.00 17.54 ?  138 HIS   B CG   1 
ATOM   6131 N ND1  . HIS   B 1 138 ? 30.972 -32.478 1.254   1.00 19.15 ?  138 HIS   B ND1  1 
ATOM   6132 C CD2  . HIS   B 1 138 ? 32.538 -31.559 2.470   1.00 17.91 ?  138 HIS   B CD2  1 
ATOM   6133 C CE1  . HIS   B 1 138 ? 30.406 -31.513 1.956   1.00 18.91 ?  138 HIS   B CE1  1 
ATOM   6134 N NE2  . HIS   B 1 138 ? 31.333 -30.944 2.706   1.00 18.20 ?  138 HIS   B NE2  1 
ATOM   6135 H H    . HIS   B 1 138 ? 34.771 -34.733 -0.517  1.00 17.40 ?  138 HIS   B H    1 
ATOM   6136 H HA   . HIS   B 1 138 ? 32.506 -33.490 -0.983  1.00 17.76 ?  138 HIS   B HA   1 
ATOM   6137 H HB2  . HIS   B 1 138 ? 32.901 -34.408 1.103   1.00 19.78 ?  138 HIS   B HB2  1 
ATOM   6138 H HB3  . HIS   B 1 138 ? 34.114 -33.409 1.332   1.00 19.78 ?  138 HIS   B HB3  1 
ATOM   6139 H HD1  . HIS   B 1 138 ? 30.564 -32.995 0.695   1.00 23.00 ?  138 HIS   B HD1  1 
ATOM   6140 H HD2  . HIS   B 1 138 ? 33.344 -31.350 2.873   1.00 21.51 ?  138 HIS   B HD2  1 
ATOM   6141 H HE1  . HIS   B 1 138 ? 29.500 -31.285 1.933   1.00 22.71 ?  138 HIS   B HE1  1 
ATOM   6142 N N    . SER   B 1 139 ? 35.095 -31.612 -0.817  1.00 13.72 ?  139 SER   B N    1 
ATOM   6143 C CA   . SER   B 1 139 ? 35.534 -30.263 -1.139  1.00 12.84 ?  139 SER   B CA   1 
ATOM   6144 C C    . SER   B 1 139 ? 35.194 -29.911 -2.579  1.00 12.50 ?  139 SER   B C    1 
ATOM   6145 O O    . SER   B 1 139 ? 34.740 -28.795 -2.857  1.00 12.45 ?  139 SER   B O    1 
ATOM   6146 C CB   . SER   B 1 139 ? 37.031 -30.128 -0.882  1.00 13.36 ?  139 SER   B CB   1 
ATOM   6147 O OG   . SER   B 1 139 ? 37.430 -28.792 -1.138  1.00 13.53 ?  139 SER   B OG   1 
ATOM   6148 H H    . SER   B 1 139 ? 35.715 -32.162 -0.603  1.00 16.48 ?  139 SER   B H    1 
ATOM   6149 H HA   . SER   B 1 139 ? 35.072 -29.639 -0.567  1.00 15.42 ?  139 SER   B HA   1 
ATOM   6150 H HB2  . SER   B 1 139 ? 37.217 -30.351 0.045   1.00 16.05 ?  139 SER   B HB2  1 
ATOM   6151 H HB3  . SER   B 1 139 ? 37.517 -30.728 -1.472  1.00 16.05 ?  139 SER   B HB3  1 
ATOM   6152 H HG   . SER   B 1 139 ? 38.261 -28.709 -0.990  1.00 16.25 ?  139 SER   B HG   1 
ATOM   6153 N N    . LEU   B 1 140 ? 35.398 -30.853 -3.508  1.00 11.71 ?  140 LEU   B N    1 
ATOM   6154 C CA   . LEU   B 1 140 ? 35.027 -30.612 -4.897  1.00 11.78 ?  140 LEU   B CA   1 
ATOM   6155 C C    . LEU   B 1 140 ? 33.527 -30.381 -5.028  1.00 12.01 ?  140 LEU   B C    1 
ATOM   6156 O O    . LEU   B 1 140 ? 33.092 -29.489 -5.763  1.00 12.40 ?  140 LEU   B O    1 
ATOM   6157 C CB   . LEU   B 1 140 ? 35.486 -31.783 -5.770  1.00 12.11 ?  140 LEU   B CB   1 
ATOM   6158 C CG   . LEU   B 1 140 ? 35.142 -31.674 -7.253  1.00 12.39 ?  140 LEU   B CG   1 
ATOM   6159 C CD1  . LEU   B 1 140 ? 35.718 -30.399 -7.853  1.00 13.22 ?  140 LEU   B CD1  1 
ATOM   6160 C CD2  . LEU   B 1 140 ? 35.631 -32.899 -7.995  1.00 13.62 ?  140 LEU   B CD2  1 
ATOM   6161 H H    . LEU   B 1 140 ? 35.745 -31.626 -3.362  1.00 14.07 ?  140 LEU   B H    1 
ATOM   6162 H HA   . LEU   B 1 140 ? 35.488 -29.813 -5.209  1.00 14.15 ?  140 LEU   B HA   1 
ATOM   6163 H HB2  . LEU   B 1 140 ? 36.450 -31.861 -5.702  1.00 14.54 ?  140 LEU   B HB2  1 
ATOM   6164 H HB3  . LEU   B 1 140 ? 35.070 -32.592 -5.437  1.00 14.54 ?  140 LEU   B HB3  1 
ATOM   6165 H HG   . LEU   B 1 140 ? 34.178 -31.630 -7.346  1.00 14.88 ?  140 LEU   B HG   1 
ATOM   6166 H HD11 . LEU   B 1 140 ? 35.600 -30.426 -8.815  1.00 15.88 ?  140 LEU   B HD11 1 
ATOM   6167 H HD12 . LEU   B 1 140 ? 35.247 -29.632 -7.485  1.00 15.88 ?  140 LEU   B HD12 1 
ATOM   6168 H HD13 . LEU   B 1 140 ? 36.660 -30.345 -7.635  1.00 15.88 ?  140 LEU   B HD13 1 
ATOM   6169 H HD21 . LEU   B 1 140 ? 35.400 -32.806 -8.933  1.00 16.36 ?  140 LEU   B HD21 1 
ATOM   6170 H HD22 . LEU   B 1 140 ? 36.591 -32.964 -7.894  1.00 16.36 ?  140 LEU   B HD22 1 
ATOM   6171 H HD23 . LEU   B 1 140 ? 35.199 -33.681 -7.622  1.00 16.36 ?  140 LEU   B HD23 1 
ATOM   6172 N N    . ARG   B 1 141 ? 32.725 -31.174 -4.317  1.00 12.35 ?  141 ARG   B N    1 
ATOM   6173 C CA   . ARG   B 1 141 ? 31.272 -31.000 -4.300  1.00 13.56 ?  141 ARG   B CA   1 
ATOM   6174 C C    . ARG   B 1 141 ? 30.888 -29.588 -3.871  1.00 12.74 ?  141 ARG   B C    1 
ATOM   6175 O O    . ARG   B 1 141 ? 30.082 -28.909 -4.529  1.00 13.26 ?  141 ARG   B O    1 
ATOM   6176 C CB   . ARG   B 1 141 ? 30.693 -32.032 -3.324  1.00 15.19 ?  141 ARG   B CB   1 
ATOM   6177 C CG   . ARG   B 1 141 ? 29.232 -31.903 -2.971  1.00 17.36 ?  141 ARG   B CG   1 
ATOM   6178 C CD   . ARG   B 1 141 ? 28.420 -32.543 -4.021  1.00 19.01 ?  141 ARG   B CD   1 
ATOM   6179 N NE   . ARG   B 1 141 ? 28.175 -31.641 -5.135  1.00 19.68 ?  141 ARG   B NE   1 
ATOM   6180 C CZ   . ARG   B 1 141 ? 28.161 -32.008 -6.409  1.00 18.97 ?  141 ARG   B CZ   1 
ATOM   6181 N NH1  . ARG   B 1 141 ? 28.592 -33.202 -6.792  1.00 18.72 ?  141 ARG   B NH1  1 
ATOM   6182 N NH2  . ARG   B 1 141 ? 27.698 -31.157 -7.321  1.00 19.78 ?  141 ARG   B NH2  1 
ATOM   6183 H H    . ARG   B 1 141 ? 33.005 -31.822 -3.831  1.00 14.83 ?  141 ARG   B H    1 
ATOM   6184 H HA   . ARG   B 1 141 ? 30.911 -31.168 -5.183  1.00 16.29 ?  141 ARG   B HA   1 
ATOM   6185 H HB2  . ARG   B 1 141 ? 30.831 -32.917 -3.702  1.00 18.25 ?  141 ARG   B HB2  1 
ATOM   6186 H HB3  . ARG   B 1 141 ? 31.190 -31.971 -2.494  1.00 18.25 ?  141 ARG   B HB3  1 
ATOM   6187 H HG2  . ARG   B 1 141 ? 29.066 -32.350 -2.128  1.00 20.85 ?  141 ARG   B HG2  1 
ATOM   6188 H HG3  . ARG   B 1 141 ? 28.980 -30.964 -2.907  1.00 20.85 ?  141 ARG   B HG3  1 
ATOM   6189 H HD2  . ARG   B 1 141 ? 28.884 -33.333 -4.347  1.00 22.83 ?  141 ARG   B HD2  1 
ATOM   6190 H HD3  . ARG   B 1 141 ? 27.570 -32.802 -3.642  1.00 22.83 ?  141 ARG   B HD3  1 
ATOM   6191 H HE   . ARG   B 1 141 ? 27.994 -30.820 -4.952  1.00 23.63 ?  141 ARG   B HE   1 
ATOM   6192 H HH11 . ARG   B 1 141 ? 28.880 -33.768 -6.213  1.00 22.48 ?  141 ARG   B HH11 1 
ATOM   6193 H HH12 . ARG   B 1 141 ? 28.583 -33.412 -7.623  1.00 22.48 ?  141 ARG   B HH12 1 
ATOM   6194 H HH21 . ARG   B 1 141 ? 27.422 -30.376 -7.084  1.00 23.75 ?  141 ARG   B HH21 1 
ATOM   6195 H HH22 . ARG   B 1 141 ? 27.705 -31.372 -8.155  1.00 23.75 ?  141 ARG   B HH22 1 
ATOM   6196 N N    . VAL   B 1 142 ? 31.443 -29.134 -2.750  1.00 12.68 ?  142 VAL   B N    1 
ATOM   6197 C CA   . VAL   B 1 142 ? 31.093 -27.803 -2.264  1.00 12.48 ?  142 VAL   B CA   1 
ATOM   6198 C C    . VAL   B 1 142 ? 31.567 -26.741 -3.247  1.00 12.37 ?  142 VAL   B C    1 
ATOM   6199 O O    . VAL   B 1 142 ? 30.864 -25.754 -3.504  1.00 12.79 ?  142 VAL   B O    1 
ATOM   6200 C CB   . VAL   B 1 142 ? 31.636 -27.578 -0.841  1.00 13.27 ?  142 VAL   B CB   1 
ATOM   6201 C CG1  . VAL   B 1 142 ? 31.344 -26.148 -0.377  1.00 13.66 ?  142 VAL   B CG1  1 
ATOM   6202 C CG2  . VAL   B 1 142 ? 31.045 -28.598 0.129   1.00 13.92 ?  142 VAL   B CG2  1 
ATOM   6203 H H    . VAL   B 1 142 ? 32.007 -29.565 -2.261  1.00 15.23 ?  142 VAL   B H    1 
ATOM   6204 H HA   . VAL   B 1 142 ? 30.131 -27.739 -2.215  1.00 15.00 ?  142 VAL   B HA   1 
ATOM   6205 H HB   . VAL   B 1 142 ? 32.600 -27.699 -0.849  1.00 15.94 ?  142 VAL   B HB   1 
ATOM   6206 H HG11 . VAL   B 1 142 ? 31.518 -26.082 0.573   1.00 16.40 ?  142 VAL   B HG11 1 
ATOM   6207 H HG12 . VAL   B 1 142 ? 31.919 -25.531 -0.861  1.00 16.40 ?  142 VAL   B HG12 1 
ATOM   6208 H HG13 . VAL   B 1 142 ? 30.413 -25.941 -0.558  1.00 16.40 ?  142 VAL   B HG13 1 
ATOM   6209 H HG21 . VAL   B 1 142 ? 31.375 -28.411 1.020   1.00 16.72 ?  142 VAL   B HG21 1 
ATOM   6210 H HG22 . VAL   B 1 142 ? 30.078 -28.523 0.110   1.00 16.72 ?  142 VAL   B HG22 1 
ATOM   6211 H HG23 . VAL   B 1 142 ? 31.314 -29.488 -0.147  1.00 16.72 ?  142 VAL   B HG23 1 
ATOM   6212 N N    . CYS   B 1 143 ? 32.748 -26.945 -3.835  1.00 12.12 ?  143 CYS   B N    1 
ATOM   6213 C CA   . CYS   B 1 143 ? 33.251 -26.003 -4.831  1.00 12.09 ?  143 CYS   B CA   1 
ATOM   6214 C C    . CYS   B 1 143 ? 32.253 -25.847 -5.974  1.00 11.99 ?  143 CYS   B C    1 
ATOM   6215 O O    . CYS   B 1 143 ? 31.841 -24.734 -6.325  1.00 12.21 ?  143 CYS   B O    1 
ATOM   6216 C CB   . CYS   B 1 143 ? 34.609 -26.488 -5.354  1.00 12.23 ?  143 CYS   B CB   1 
ATOM   6217 S SG   . CYS   B 1 143 ? 35.361 -25.387 -6.579  1.00 12.49 ?  143 CYS   B SG   1 
ATOM   6218 H H    . CYS   B 1 143 ? 33.278 -27.598 -3.668  1.00 14.56 ?  143 CYS   B H    1 
ATOM   6219 H HA   . CYS   B 1 143 ? 33.385 -25.133 -4.427  1.00 14.52 ?  143 CYS   B HA   1 
ATOM   6220 H HB2  . CYS   B 1 143 ? 35.231 -26.572 -4.609  1.00 14.69 ?  143 CYS   B HB2  1 
ATOM   6221 H HB3  . CYS   B 1 143 ? 34.497 -27.355 -5.772  1.00 14.69 ?  143 CYS   B HB3  1 
ATOM   6222 H HG   . CYS   B 1 143 ? 36.435 -25.827 -6.896  1.00 15.00 ?  143 CYS   B HG   1 
ATOM   6223 N N    . VAL   B 1 144 ? 31.840 -26.971 -6.557  1.00 12.59 ?  144 VAL   B N    1 
ATOM   6224 C CA   . VAL   B 1 144 ? 30.937 -26.930 -7.701  1.00 13.26 ?  144 VAL   B CA   1 
ATOM   6225 C C    . VAL   B 1 144 ? 29.596 -26.308 -7.325  1.00 13.43 ?  144 VAL   B C    1 
ATOM   6226 O O    . VAL   B 1 144 ? 28.974 -25.605 -8.132  1.00 14.91 ?  144 VAL   B O    1 
ATOM   6227 C CB   . VAL   B 1 144 ? 30.776 -28.345 -8.275  1.00 15.71 ?  144 VAL   B CB   1 
ATOM   6228 C CG1  . VAL   B 1 144 ? 29.518 -28.461 -9.127  1.00 18.26 ?  144 VAL   B CG1  1 
ATOM   6229 C CG2  . VAL   B 1 144 ? 32.026 -28.753 -9.056  1.00 15.69 ?  144 VAL   B CG2  1 
ATOM   6230 H H    . VAL   B 1 144 ? 32.072 -27.765 -6.314  1.00 15.12 ?  144 VAL   B H    1 
ATOM   6231 H HA   . VAL   B 1 144 ? 31.330 -26.383 -8.393  1.00 15.93 ?  144 VAL   B HA   1 
ATOM   6232 H HB   . VAL   B 1 144 ? 30.680 -28.974 -7.541  1.00 18.87 ?  144 VAL   B HB   1 
ATOM   6233 H HG11 . VAL   B 1 144 ? 29.594 -29.245 -9.698  1.00 21.92 ?  144 VAL   B HG11 1 
ATOM   6234 H HG12 . VAL   B 1 144 ? 28.749 -28.557 -8.545  1.00 21.92 ?  144 VAL   B HG12 1 
ATOM   6235 H HG13 . VAL   B 1 144 ? 29.431 -27.667 -9.673  1.00 21.92 ?  144 VAL   B HG13 1 
ATOM   6236 H HG21 . VAL   B 1 144 ? 31.903 -29.653 -9.406  1.00 18.84 ?  144 VAL   B HG21 1 
ATOM   6237 H HG22 . VAL   B 1 144 ? 32.154 -28.131 -9.791  1.00 18.84 ?  144 VAL   B HG22 1 
ATOM   6238 H HG23 . VAL   B 1 144 ? 32.789 -28.731 -8.463  1.00 18.84 ?  144 VAL   B HG23 1 
ATOM   6239 N N    . ASP   B 1 145 ? 29.122 -26.561 -6.107  1.00 13.67 ?  145 ASP   B N    1 
ATOM   6240 C CA   . ASP   B 1 145 ? 27.812 -26.085 -5.685  1.00 14.15 ?  145 ASP   B CA   1 
ATOM   6241 C C    . ASP   B 1 145 ? 27.843 -24.662 -5.141  1.00 13.68 ?  145 ASP   B C    1 
ATOM   6242 O O    . ASP   B 1 145 ? 26.783 -24.122 -4.807  1.00 15.40 ?  145 ASP   B O    1 
ATOM   6243 C CB   . ASP   B 1 145 ? 27.222 -27.004 -4.610  1.00 15.55 ?  145 ASP   B CB   1 
ATOM   6244 C CG   . ASP   B 1 145 ? 26.858 -28.381 -5.130  1.00 17.22 ?  145 ASP   B CG   1 
ATOM   6245 O OD1  . ASP   B 1 145 ? 26.765 -28.577 -6.358  1.00 17.34 ?  145 ASP   B OD1  1 
ATOM   6246 O OD2  . ASP   B 1 145 ? 26.661 -29.272 -4.284  1.00 19.62 -1 145 ASP   B OD2  1 
ATOM   6247 H H    . ASP   B 1 145 ? 29.549 -27.001 -5.504  1.00 16.43 ?  145 ASP   B H    1 
ATOM   6248 H HA   . ASP   B 1 145 ? 27.220 -26.087 -6.449  1.00 17.00 ?  145 ASP   B HA   1 
ATOM   6249 H HB2  . ASP   B 1 145 ? 27.865 -27.128 -3.905  1.00 18.67 ?  145 ASP   B HB2  1 
ATOM   6250 H HB3  . ASP   B 1 145 ? 26.410 -26.598 -4.262  1.00 18.67 ?  145 ASP   B HB3  1 
ATOM   6251 N N    . THR   B 1 146 ? 29.019 -24.051 -5.020  1.00 12.09 ?  146 THR   B N    1 
ATOM   6252 C CA   . THR   B 1 146 ? 29.147 -22.725 -4.417  1.00 11.78 ?  146 THR   B CA   1 
ATOM   6253 C C    . THR   B 1 146 ? 29.781 -21.693 -5.334  1.00 11.81 ?  146 THR   B C    1 
ATOM   6254 O O    . THR   B 1 146 ? 29.325 -20.531 -5.380  1.00 12.02 ?  146 THR   B O    1 
ATOM   6255 C CB   . THR   B 1 146 ? 29.975 -22.827 -3.124  1.00 12.21 ?  146 THR   B CB   1 
ATOM   6256 O OG1  . THR   B 1 146 ? 29.406 -23.820 -2.264  1.00 12.60 ?  146 THR   B OG1  1 
ATOM   6257 C CG2  . THR   B 1 146 ? 30.048 -21.477 -2.406  1.00 12.11 ?  146 THR   B CG2  1 
ATOM   6258 H H    . THR   B 1 146 ? 29.770 -24.384 -5.282  1.00 14.53 ?  146 THR   B H    1 
ATOM   6259 H HA   . THR   B 1 146 ? 28.268 -22.398 -4.188  1.00 14.16 ?  146 THR   B HA   1 
ATOM   6260 H HB   . THR   B 1 146 ? 30.878 -23.085 -3.349  1.00 14.67 ?  146 THR   B HB   1 
ATOM   6261 H HG1  . THR   B 1 146 ? 29.437 -24.577 -2.644  1.00 15.14 ?  146 THR   B HG1  1 
ATOM   6262 H HG21 . THR   B 1 146 ? 30.409 -21.594 -1.515  1.00 14.55 ?  146 THR   B HG21 1 
ATOM   6263 H HG22 . THR   B 1 146 ? 30.627 -20.867 -2.899  1.00 14.55 ?  146 THR   B HG22 1 
ATOM   6264 H HG23 . THR   B 1 146 ? 29.165 -21.082 -2.340  1.00 14.55 ?  146 THR   B HG23 1 
ATOM   6265 N N    . VAL   B 1 147 ? 30.849 -22.070 -6.031  1.00 11.54 ?  147 VAL   B N    1 
ATOM   6266 C CA   . VAL   B 1 147 ? 31.574 -21.125 -6.869  1.00 11.12 ?  147 VAL   B CA   1 
ATOM   6267 C C    . VAL   B 1 147 ? 30.846 -20.992 -8.194  1.00 11.42 ?  147 VAL   B C    1 
ATOM   6268 O O    . VAL   B 1 147 ? 30.474 -21.996 -8.819  1.00 12.44 ?  147 VAL   B O    1 
ATOM   6269 C CB   . VAL   B 1 147 ? 33.029 -21.576 -7.074  1.00 11.36 ?  147 VAL   B CB   1 
ATOM   6270 C CG1  . VAL   B 1 147 ? 33.786 -20.547 -7.890  1.00 11.52 ?  147 VAL   B CG1  1 
ATOM   6271 C CG2  . VAL   B 1 147 ? 33.714 -21.789 -5.735  1.00 11.69 ?  147 VAL   B CG2  1 
ATOM   6272 H H    . VAL   B 1 147 ? 31.178 -22.868 -6.046  1.00 13.86 ?  147 VAL   B H    1 
ATOM   6273 H HA   . VAL   B 1 147 ? 31.591 -20.256 -6.438  1.00 13.36 ?  147 VAL   B HA   1 
ATOM   6274 H HB   . VAL   B 1 147 ? 33.045 -22.418 -7.562  1.00 13.64 ?  147 VAL   B HB   1 
ATOM   6275 H HG11 . VAL   B 1 147 ? 34.733 -20.760 -7.871  1.00 13.84 ?  147 VAL   B HG11 1 
ATOM   6276 H HG12 . VAL   B 1 147 ? 33.463 -20.562 -8.803  1.00 13.84 ?  147 VAL   B HG12 1 
ATOM   6277 H HG13 . VAL   B 1 147 ? 33.640 -19.670 -7.499  1.00 13.84 ?  147 VAL   B HG13 1 
ATOM   6278 H HG21 . VAL   B 1 147 ? 34.653 -21.989 -5.886  1.00 14.04 ?  147 VAL   B HG21 1 
ATOM   6279 H HG22 . VAL   B 1 147 ? 33.631 -20.979 -5.209  1.00 14.04 ?  147 VAL   B HG22 1 
ATOM   6280 H HG23 . VAL   B 1 147 ? 33.289 -22.529 -5.277  1.00 14.04 ?  147 VAL   B HG23 1 
ATOM   6281 N N    . ARG   B 1 148 ? 30.633 -19.741 -8.614  1.00 11.24 ?  148 ARG   B N    1 
ATOM   6282 C CA   . ARG   B 1 148 ? 30.012 -19.421 -9.888  1.00 11.46 ?  148 ARG   B CA   1 
ATOM   6283 C C    . ARG   B 1 148 ? 30.971 -18.752 -10.860 1.00 11.38 ?  148 ARG   B C    1 
ATOM   6284 O O    . ARG   B 1 148 ? 30.684 -18.725 -12.060 1.00 13.27 ?  148 ARG   B O    1 
ATOM   6285 C CB   . ARG   B 1 148 ? 28.783 -18.521 -9.670  1.00 12.09 ?  148 ARG   B CB   1 
ATOM   6286 C CG   . ARG   B 1 148 ? 27.694 -19.214 -8.867  1.00 12.85 ?  148 ARG   B CG   1 
ATOM   6287 C CD   . ARG   B 1 148 ? 26.496 -18.319 -8.566  1.00 13.62 ?  148 ARG   B CD   1 
ATOM   6288 N NE   . ARG   B 1 148 ? 26.888 -17.133 -7.816  1.00 13.63 ?  148 ARG   B NE   1 
ATOM   6289 C CZ   . ARG   B 1 148 ? 27.183 -17.114 -6.522  1.00 12.75 ?  148 ARG   B CZ   1 
ATOM   6290 N NH1  . ARG   B 1 148 ? 27.102 -18.206 -5.774  1.00 12.97 ?  148 ARG   B NH1  1 
ATOM   6291 N NH2  . ARG   B 1 148 ? 27.583 -15.972 -5.966  1.00 12.57 ?  148 ARG   B NH2  1 
ATOM   6292 H H    . ARG   B 1 148 ? 30.853 -19.038 -8.158  1.00 13.50 ?  148 ARG   B H    1 
ATOM   6293 H HA   . ARG   B 1 148 ? 29.706 -20.239 -10.297 1.00 13.77 ?  148 ARG   B HA   1 
ATOM   6294 H HB2  . ARG   B 1 148 ? 29.053 -17.723 -9.186  1.00 14.53 ?  148 ARG   B HB2  1 
ATOM   6295 H HB3  . ARG   B 1 148 ? 28.413 -18.275 -10.533 1.00 14.53 ?  148 ARG   B HB3  1 
ATOM   6296 H HG2  . ARG   B 1 148 ? 27.370 -19.979 -9.371  1.00 15.43 ?  148 ARG   B HG2  1 
ATOM   6297 H HG3  . ARG   B 1 148 ? 28.063 -19.510 -8.021  1.00 15.43 ?  148 ARG   B HG3  1 
ATOM   6298 H HD2  . ARG   B 1 148 ? 26.097 -18.028 -9.400  1.00 16.36 ?  148 ARG   B HD2  1 
ATOM   6299 H HD3  . ARG   B 1 148 ? 25.850 -18.813 -8.038  1.00 16.36 ?  148 ARG   B HD3  1 
ATOM   6300 H HE   . ARG   B 1 148 ? 26.939 -16.390 -8.241  1.00 16.37 ?  148 ARG   B HE   1 
ATOM   6301 H HH11 . ARG   B 1 148 ? 26.836 -18.950 -6.118  1.00 15.58 ?  148 ARG   B HH11 1 
ATOM   6302 H HH12 . ARG   B 1 148 ? 27.290 -18.170 -4.933  1.00 15.58 ?  148 ARG   B HH12 1 
ATOM   6303 H HH21 . ARG   B 1 148 ? 27.649 -15.262 -6.442  1.00 15.10 ?  148 ARG   B HH21 1 
ATOM   6304 H HH22 . ARG   B 1 148 ? 27.780 -15.946 -5.127  1.00 15.10 ?  148 ARG   B HH22 1 
ATOM   6305 N N    . THR   B 1 149 ? 32.077 -18.196 -10.373 1.00 11.34 ?  149 THR   B N    1 
ATOM   6306 C CA   . THR   B 1 149 ? 33.116 -17.644 -11.224 1.00 11.59 ?  149 THR   B CA   1 
ATOM   6307 C C    . THR   B 1 149 ? 34.010 -18.780 -11.727 1.00 11.19 ?  149 THR   B C    1 
ATOM   6308 O O    . THR   B 1 149 ? 33.821 -19.951 -11.383 1.00 11.84 ?  149 THR   B O    1 
ATOM   6309 C CB   . THR   B 1 149 ? 33.890 -16.589 -10.443 1.00 11.56 ?  149 THR   B CB   1 
ATOM   6310 O OG1  . THR   B 1 149 ? 34.344 -17.183 -9.225  1.00 11.67 ?  149 THR   B OG1  1 
ATOM   6311 C CG2  . THR   B 1 149 ? 33.001 -15.381 -10.143 1.00 12.38 ?  149 THR   B CG2  1 
ATOM   6312 H H    . THR   B 1 149 ? 32.246 -18.126 -9.536  1.00 13.62 ?  149 THR   B H    1 
ATOM   6313 H HA   . THR   B 1 149 ? 32.710 -17.213 -11.993 1.00 13.92 ?  149 THR   B HA   1 
ATOM   6314 H HB   . THR   B 1 149 ? 34.654 -16.297 -10.962 1.00 13.89 ?  149 THR   B HB   1 
ATOM   6315 H HG1  . THR   B 1 149 ? 34.773 -16.610 -8.771  1.00 14.02 ?  149 THR   B HG1  1 
ATOM   6316 H HG21 . THR   B 1 149 ? 33.508 -14.709 -9.660  1.00 14.87 ?  149 THR   B HG21 1 
ATOM   6317 H HG22 . THR   B 1 149 ? 32.680 -14.994 -10.973 1.00 14.87 ?  149 THR   B HG22 1 
ATOM   6318 H HG23 . THR   B 1 149 ? 32.241 -15.650 -9.606  1.00 14.87 ?  149 THR   B HG23 1 
ATOM   6319 N N    . ASN   B 1 150 ? 34.974 -18.454 -12.580 1.00 11.52 ?  150 ASN   B N    1 
ATOM   6320 C CA   . ASN   B 1 150 ? 35.745 -19.483 -13.272 1.00 11.88 ?  150 ASN   B CA   1 
ATOM   6321 C C    . ASN   B 1 150 ? 36.913 -19.931 -12.400 1.00 11.44 ?  150 ASN   B C    1 
ATOM   6322 O O    . ASN   B 1 150 ? 37.836 -19.154 -12.136 1.00 12.13 ?  150 ASN   B O    1 
ATOM   6323 C CB   . ASN   B 1 150 ? 36.218 -18.963 -14.620 1.00 13.58 ?  150 ASN   B CB   1 
ATOM   6324 C CG   . ASN   B 1 150 ? 35.074 -18.736 -15.561 1.00 16.48 ?  150 ASN   B CG   1 
ATOM   6325 O OD1  . ASN   B 1 150 ? 34.174 -19.564 -15.656 1.00 17.71 ?  150 ASN   B OD1  1 
ATOM   6326 N ND2  . ASN   B 1 150 ? 35.067 -17.592 -16.227 1.00 18.32 ?  150 ASN   B ND2  1 
ATOM   6327 H H    . ASN   B 1 150 ? 35.203 -17.646 -12.778 1.00 13.84 ?  150 ASN   B H    1 
ATOM   6328 H HA   . ASN   B 1 150 ? 35.170 -20.251 -13.434 1.00 14.27 ?  150 ASN   B HA   1 
ATOM   6329 H HB2  . ASN   B 1 150 ? 36.675 -18.117 -14.493 1.00 16.32 ?  150 ASN   B HB2  1 
ATOM   6330 H HB3  . ASN   B 1 150 ? 36.814 -19.611 -15.023 1.00 16.32 ?  150 ASN   B HB3  1 
ATOM   6331 H HD21 . ASN   B 1 150 ? 34.429 -17.412 -16.777 1.00 22.00 ?  150 ASN   B HD21 1 
ATOM   6332 H HD22 . ASN   B 1 150 ? 35.711 -17.027 -16.123 1.00 22.00 ?  150 ASN   B HD22 1 
ATOM   6333 N N    . VAL   B 1 151 ? 36.876 -21.183 -11.957 1.00 11.29 ?  151 VAL   B N    1 
ATOM   6334 C CA   . VAL   B 1 151 ? 37.893 -21.714 -11.063 1.00 11.47 ?  151 VAL   B CA   1 
ATOM   6335 C C    . VAL   B 1 151 ? 38.603 -22.881 -11.736 1.00 11.22 ?  151 VAL   B C    1 
ATOM   6336 O O    . VAL   B 1 151 ? 37.966 -23.819 -12.239 1.00 12.17 ?  151 VAL   B O    1 
ATOM   6337 C CB   . VAL   B 1 151 ? 37.326 -22.056 -9.671  1.00 12.83 ?  151 VAL   B CB   1 
ATOM   6338 C CG1  . VAL   B 1 151 ? 36.174 -23.057 -9.753  1.00 13.71 ?  151 VAL   B CG1  1 
ATOM   6339 C CG2  . VAL   B 1 151 ? 38.436 -22.551 -8.755  1.00 13.22 ?  151 VAL   B CG2  1 
ATOM   6340 H H    . VAL   B 1 151 ? 36.257 -21.750 -12.164 1.00 13.56 ?  151 VAL   B H    1 
ATOM   6341 H HA   . VAL   B 1 151 ? 38.559 -21.025 -10.930 1.00 13.78 ?  151 VAL   B HA   1 
ATOM   6342 H HB   . VAL   B 1 151 ? 36.975 -21.242 -9.281  1.00 15.42 ?  151 VAL   B HB   1 
ATOM   6343 H HG11 . VAL   B 1 151 ? 35.853 -23.245 -8.856  1.00 16.47 ?  151 VAL   B HG11 1 
ATOM   6344 H HG12 . VAL   B 1 151 ? 35.458 -22.675 -10.285 1.00 16.47 ?  151 VAL   B HG12 1 
ATOM   6345 H HG13 . VAL   B 1 151 ? 36.491 -23.876 -10.167 1.00 16.47 ?  151 VAL   B HG13 1 
ATOM   6346 H HG21 . VAL   B 1 151 ? 38.089 -22.625 -7.852  1.00 15.88 ?  151 VAL   B HG21 1 
ATOM   6347 H HG22 . VAL   B 1 151 ? 38.745 -23.416 -9.063  1.00 15.88 ?  151 VAL   B HG22 1 
ATOM   6348 H HG23 . VAL   B 1 151 ? 39.169 -21.912 -8.772  1.00 15.88 ?  151 VAL   B HG23 1 
ATOM   6349 N N    . TYR   B 1 152 ? 39.931 -22.796 -11.748 1.00 10.62 ?  152 TYR   B N    1 
ATOM   6350 C CA   . TYR   B 1 152 ? 40.838 -23.773 -12.331 1.00 10.74 ?  152 TYR   B CA   1 
ATOM   6351 C C    . TYR   B 1 152 ? 41.560 -24.451 -11.174 1.00 10.25 ?  152 TYR   B C    1 
ATOM   6352 O O    . TYR   B 1 152 ? 42.401 -23.830 -10.517 1.00 10.87 ?  152 TYR   B O    1 
ATOM   6353 C CB   . TYR   B 1 152 ? 41.804 -23.066 -13.283 1.00 11.57 ?  152 TYR   B CB   1 
ATOM   6354 C CG   . TYR   B 1 152 ? 41.124 -22.600 -14.546 1.00 12.37 ?  152 TYR   B CG   1 
ATOM   6355 C CD1  . TYR   B 1 152 ? 40.454 -21.383 -14.604 1.00 12.58 ?  152 TYR   B CD1  1 
ATOM   6356 C CD2  . TYR   B 1 152 ? 41.120 -23.405 -15.676 1.00 13.58 ?  152 TYR   B CD2  1 
ATOM   6357 C CE1  . TYR   B 1 152 ? 39.810 -20.977 -15.761 1.00 14.00 ?  152 TYR   B CE1  1 
ATOM   6358 C CE2  . TYR   B 1 152 ? 40.482 -23.010 -16.834 1.00 14.72 ?  152 TYR   B CE2  1 
ATOM   6359 C CZ   . TYR   B 1 152 ? 39.827 -21.799 -16.875 1.00 14.48 ?  152 TYR   B CZ   1 
ATOM   6360 O OH   . TYR   B 1 152 ? 39.198 -21.430 -18.039 1.00 16.80 ?  152 TYR   B OH   1 
ATOM   6361 H H    . TYR   B 1 152 ? 40.359 -22.138 -11.391 1.00 12.76 ?  152 TYR   B H    1 
ATOM   6362 H HA   . TYR   B 1 152 ? 40.333 -24.442 -12.828 1.00 12.91 ?  152 TYR   B HA   1 
ATOM   6363 H HB2  . TYR   B 1 152 ? 42.170 -22.289 -12.831 1.00 13.90 ?  152 TYR   B HB2  1 
ATOM   6364 H HB3  . TYR   B 1 152 ? 42.515 -23.676 -13.525 1.00 13.90 ?  152 TYR   B HB3  1 
ATOM   6365 H HD1  . TYR   B 1 152 ? 40.436 -20.835 -13.851 1.00 15.11 ?  152 TYR   B HD1  1 
ATOM   6366 H HD2  . TYR   B 1 152 ? 41.556 -24.228 -15.650 1.00 16.31 ?  152 TYR   B HD2  1 
ATOM   6367 H HE1  . TYR   B 1 152 ? 39.369 -20.160 -15.789 1.00 16.81 ?  152 TYR   B HE1  1 
ATOM   6368 H HE2  . TYR   B 1 152 ? 40.495 -23.560 -17.581 1.00 17.67 ?  152 TYR   B HE2  1 
ATOM   6369 H HH   . TYR   B 1 152 ? 38.845 -20.673 -17.940 1.00 20.17 ?  152 TYR   B HH   1 
ATOM   6370 N N    . LEU   B 1 153 ? 41.192 -25.707 -10.901 1.00 10.68 ?  153 LEU   B N    1 
ATOM   6371 C CA   . LEU   B 1 153 ? 41.702 -26.454 -9.762  1.00 10.43 ?  153 LEU   B CA   1 
ATOM   6372 C C    . LEU   B 1 153 ? 42.932 -27.262 -10.151 1.00 10.85 ?  153 LEU   B C    1 
ATOM   6373 O O    . LEU   B 1 153 ? 42.915 -27.988 -11.147 1.00 11.90 ?  153 LEU   B O    1 
ATOM   6374 C CB   . LEU   B 1 153 ? 40.623 -27.404 -9.244  1.00 10.77 ?  153 LEU   B CB   1 
ATOM   6375 C CG   . LEU   B 1 153 ? 39.360 -26.752 -8.680  1.00 11.70 ?  153 LEU   B CG   1 
ATOM   6376 C CD1  . LEU   B 1 153 ? 38.270 -27.800 -8.529  1.00 12.54 ?  153 LEU   B CD1  1 
ATOM   6377 C CD2  . LEU   B 1 153 ? 39.654 -26.089 -7.344  1.00 12.64 ?  153 LEU   B CD2  1 
ATOM   6378 H H    . LEU   B 1 153 ? 40.620 -26.154 -11.375 1.00 12.83 ?  153 LEU   B H    1 
ATOM   6379 H HA   . LEU   B 1 153 ? 41.928 -25.834 -9.050  1.00 12.53 ?  153 LEU   B HA   1 
ATOM   6380 H HB2  . LEU   B 1 153 ? 40.345 -27.984 -9.971  1.00 12.94 ?  153 LEU   B HB2  1 
ATOM   6381 H HB3  . LEU   B 1 153 ? 41.005 -27.945 -8.532  1.00 12.94 ?  153 LEU   B HB3  1 
ATOM   6382 H HG   . LEU   B 1 153 ? 39.038 -26.070 -9.293  1.00 14.05 ?  153 LEU   B HG   1 
ATOM   6383 H HD11 . LEU   B 1 153 ? 37.460 -27.372 -8.197  1.00 15.07 ?  153 LEU   B HD11 1 
ATOM   6384 H HD12 . LEU   B 1 153 ? 38.096 -28.202 -9.392  1.00 15.07 ?  153 LEU   B HD12 1 
ATOM   6385 H HD13 . LEU   B 1 153 ? 38.565 -28.474 -7.899  1.00 15.07 ?  153 LEU   B HD13 1 
ATOM   6386 H HD21 . LEU   B 1 153 ? 38.838 -25.718 -6.980  1.00 15.18 ?  153 LEU   B HD21 1 
ATOM   6387 H HD22 . LEU   B 1 153 ? 40.016 -26.755 -6.736  1.00 15.18 ?  153 LEU   B HD22 1 
ATOM   6388 H HD23 . LEU   B 1 153 ? 40.307 -25.383 -7.482  1.00 15.18 ?  153 LEU   B HD23 1 
ATOM   6389 N N    . ALA   B 1 154 ? 43.985 -27.147 -9.347  1.00 11.11 ?  154 ALA   B N    1 
ATOM   6390 C CA   . ALA   B 1 154 ? 45.218 -27.905 -9.530  1.00 12.16 ?  154 ALA   B CA   1 
ATOM   6391 C C    . ALA   B 1 154 ? 45.289 -28.983 -8.452  1.00 12.47 ?  154 ALA   B C    1 
ATOM   6392 O O    . ALA   B 1 154 ? 45.221 -28.677 -7.254  1.00 13.88 ?  154 ALA   B O    1 
ATOM   6393 C CB   . ALA   B 1 154 ? 46.437 -26.987 -9.462  1.00 13.26 ?  154 ALA   B CB   1 
ATOM   6394 H H    . ALA   B 1 154 ? 44.009 -26.611 -8.670  1.00 13.35 ?  154 ALA   B H    1 
ATOM   6395 H HA   . ALA   B 1 154 ? 45.206 -28.333 -10.396 1.00 14.61 ?  154 ALA   B HA   1 
ATOM   6396 H HB1  . ALA   B 1 154 ? 47.241 -27.516 -9.584  1.00 15.92 ?  154 ALA   B HB1  1 
ATOM   6397 H HB2  . ALA   B 1 154 ? 46.374 -26.317 -10.163 1.00 15.92 ?  154 ALA   B HB2  1 
ATOM   6398 H HB3  . ALA   B 1 154 ? 46.462 -26.549 -8.594  1.00 15.92 ?  154 ALA   B HB3  1 
ATOM   6399 N N    . VAL   B 1 155 ? 45.400 -30.238 -8.878  1.00 11.86 ?  155 VAL   B N    1 
ATOM   6400 C CA   . VAL   B 1 155 ? 45.508 -31.383 -7.980  1.00 12.09 ?  155 VAL   B CA   1 
ATOM   6401 C C    . VAL   B 1 155 ? 46.855 -32.051 -8.256  1.00 11.80 ?  155 VAL   B C    1 
ATOM   6402 O O    . VAL   B 1 155 ? 47.094 -32.540 -9.367  1.00 13.49 ?  155 VAL   B O    1 
ATOM   6403 C CB   . VAL   B 1 155 ? 44.351 -32.372 -8.180  1.00 13.49 ?  155 VAL   B CB   1 
ATOM   6404 C CG1  . VAL   B 1 155 ? 44.531 -33.573 -7.275  1.00 13.43 ?  155 VAL   B CG1  1 
ATOM   6405 C CG2  . VAL   B 1 155 ? 43.018 -31.676 -7.914  1.00 14.61 ?  155 VAL   B CG2  1 
ATOM   6406 H H    . VAL   B 1 155 ? 45.430 -30.455 -9.712  1.00 14.25 ?  155 VAL   B H    1 
ATOM   6407 H HA   . VAL   B 1 155 ? 45.499 -31.074 -7.060  1.00 14.52 ?  155 VAL   B HA   1 
ATOM   6408 H HB   . VAL   B 1 155 ? 44.353 -32.676 -9.102  1.00 16.21 ?  155 VAL   B HB   1 
ATOM   6409 H HG11 . VAL   B 1 155 ? 43.703 -34.079 -7.252  1.00 16.13 ?  155 VAL   B HG11 1 
ATOM   6410 H HG12 . VAL   B 1 155 ? 45.245 -34.135 -7.625  1.00 16.13 ?  155 VAL   B HG12 1 
ATOM   6411 H HG13 . VAL   B 1 155 ? 44.758 -33.271 -6.382  1.00 16.13 ?  155 VAL   B HG13 1 
ATOM   6412 H HG21 . VAL   B 1 155 ? 42.307 -32.329 -8.002  1.00 17.55 ?  155 VAL   B HG21 1 
ATOM   6413 H HG22 . VAL   B 1 155 ? 43.029 -31.316 -7.014  1.00 17.55 ?  155 VAL   B HG22 1 
ATOM   6414 H HG23 . VAL   B 1 155 ? 42.899 -30.964 -8.558  1.00 17.55 ?  155 VAL   B HG23 1 
ATOM   6415 N N    . PHE   B 1 156 ? 47.726 -32.082 -7.243  1.00 12.52 ?  156 PHE   B N    1 
ATOM   6416 C CA   . PHE   B 1 156 ? 49.105 -32.538 -7.446  1.00 13.69 ?  156 PHE   B CA   1 
ATOM   6417 C C    . PHE   B 1 156 ? 49.200 -34.039 -7.729  1.00 14.46 ?  156 PHE   B C    1 
ATOM   6418 O O    . PHE   B 1 156 ? 49.919 -34.468 -8.641  1.00 16.50 ?  156 PHE   B O    1 
ATOM   6419 C CB   . PHE   B 1 156 ? 49.940 -32.167 -6.222  1.00 13.89 ?  156 PHE   B CB   1 
ATOM   6420 C CG   . PHE   B 1 156 ? 51.365 -32.626 -6.295  1.00 14.33 ?  156 PHE   B CG   1 
ATOM   6421 C CD1  . PHE   B 1 156 ? 52.232 -32.097 -7.235  1.00 16.09 ?  156 PHE   B CD1  1 
ATOM   6422 C CD2  . PHE   B 1 156 ? 51.840 -33.562 -5.408  1.00 14.67 ?  156 PHE   B CD2  1 
ATOM   6423 C CE1  . PHE   B 1 156 ? 53.554 -32.504 -7.294  1.00 17.17 ?  156 PHE   B CE1  1 
ATOM   6424 C CE2  . PHE   B 1 156 ? 53.163 -33.978 -5.464  1.00 16.09 ?  156 PHE   B CE2  1 
ATOM   6425 C CZ   . PHE   B 1 156 ? 54.010 -33.451 -6.413  1.00 16.95 ?  156 PHE   B CZ   1 
ATOM   6426 H H    . PHE   B 1 156 ? 47.542 -31.854 -6.433  1.00 15.04 ?  156 PHE   B H    1 
ATOM   6427 H HA   . PHE   B 1 156 ? 49.474 -32.065 -8.207  1.00 16.44 ?  156 PHE   B HA   1 
ATOM   6428 H HB2  . PHE   B 1 156 ? 49.945 -31.201 -6.127  1.00 16.68 ?  156 PHE   B HB2  1 
ATOM   6429 H HB3  . PHE   B 1 156 ? 49.541 -32.570 -5.435  1.00 16.68 ?  156 PHE   B HB3  1 
ATOM   6430 H HD1  . PHE   B 1 156 ? 51.923 -31.453 -7.837  1.00 19.32 ?  156 PHE   B HD1  1 
ATOM   6431 H HD2  . PHE   B 1 156 ? 51.270 -33.926 -4.771  1.00 17.62 ?  156 PHE   B HD2  1 
ATOM   6432 H HE1  . PHE   B 1 156 ? 54.124 -32.144 -7.939  1.00 20.62 ?  156 PHE   B HE1  1 
ATOM   6433 H HE2  . PHE   B 1 156 ? 53.473 -34.621 -4.868  1.00 19.33 ?  156 PHE   B HE2  1 
ATOM   6434 H HZ   . PHE   B 1 156 ? 54.897 -33.731 -6.451  1.00 20.36 ?  156 PHE   B HZ   1 
ATOM   6435 N N    . ASP   B 1 157 ? 48.533 -34.856 -6.931  1.00 15.03 ?  157 ASP   B N    1 
ATOM   6436 C CA   . ASP   B 1 157 ? 48.683 -36.301 -7.024  1.00 16.12 ?  157 ASP   B CA   1 
ATOM   6437 C C    . ASP   B 1 157 ? 47.771 -36.855 -8.114  1.00 16.23 ?  157 ASP   B C    1 
ATOM   6438 O O    . ASP   B 1 157 ? 46.545 -36.747 -8.012  1.00 15.71 ?  157 ASP   B O    1 
ATOM   6439 C CB   . ASP   B 1 157 ? 48.313 -36.907 -5.677  1.00 17.91 ?  157 ASP   B CB   1 
ATOM   6440 C CG   . ASP   B 1 157 ? 48.469 -38.415 -5.646  1.00 20.02 ?  157 ASP   B CG   1 
ATOM   6441 O OD1  . ASP   B 1 157 ? 48.807 -39.023 -6.687  1.00 20.41 ?  157 ASP   B OD1  1 
ATOM   6442 O OD2  . ASP   B 1 157 ? 48.273 -38.992 -4.560  1.00 22.00 -1 157 ASP   B OD2  1 
ATOM   6443 H H    . ASP   B 1 157 ? 47.986 -34.599 -6.328  1.00 18.05 ?  157 ASP   B H    1 
ATOM   6444 H HA   . ASP   B 1 157 ? 49.604 -36.531 -7.238  1.00 19.36 ?  157 ASP   B HA   1 
ATOM   6445 H HB2  . ASP   B 1 157 ? 48.888 -36.519 -5.000  1.00 21.50 ?  157 ASP   B HB2  1 
ATOM   6446 H HB3  . ASP   B 1 157 ? 47.387 -36.691 -5.487  1.00 21.50 ?  157 ASP   B HB3  1 
ATOM   6447 N N    . LYS   B 1 158 ? 48.367 -37.478 -9.139  1.00 17.47 ?  158 LYS   B N    1 
ATOM   6448 C CA   . LYS   B 1 158 ? 47.586 -38.081 -10.222 1.00 18.64 ?  158 LYS   B CA   1 
ATOM   6449 C C    . LYS   B 1 158 ? 46.526 -39.050 -9.694  1.00 18.22 ?  158 LYS   B C    1 
ATOM   6450 O O    . LYS   B 1 158 ? 45.421 -39.140 -10.244 1.00 18.03 ?  158 LYS   B O    1 
ATOM   6451 C CB   . LYS   B 1 158 ? 48.528 -38.786 -11.209 1.00 20.55 ?  158 LYS   B CB   1 
ATOM   6452 C CG   . LYS   B 1 158 ? 47.846 -39.691 -12.226 1.00 22.66 ?  158 LYS   B CG   1 
ATOM   6453 C CD   . LYS   B 1 158 ? 46.990 -38.921 -13.209 1.00 24.96 ?  158 LYS   B CD   1 
ATOM   6454 C CE   . LYS   B 1 158 ? 46.417 -39.853 -14.266 1.00 26.56 ?  158 LYS   B CE   1 
ATOM   6455 N NZ   . LYS   B 1 158 ? 45.314 -39.220 -15.043 1.00 26.55 ?  158 LYS   B NZ   1 
ATOM   6456 H H    . LYS   B 1 158 ? 49.221 -37.564 -9.234  1.00 20.98 ?  158 LYS   B H    1 
ATOM   6457 H HA   . LYS   B 1 158 ? 47.132 -37.376 -10.713 1.00 22.38 ?  158 LYS   B HA   1 
ATOM   6458 H HB2  . LYS   B 1 158 ? 49.019 -38.110 -11.711 1.00 24.67 ?  158 LYS   B HB2  1 
ATOM   6459 H HB3  . LYS   B 1 158 ? 49.155 -39.329 -10.708 1.00 24.67 ?  158 LYS   B HB3  1 
ATOM   6460 H HG2  . LYS   B 1 158 ? 48.529 -40.157 -12.735 1.00 27.21 ?  158 LYS   B HG2  1 
ATOM   6461 H HG3  . LYS   B 1 158 ? 47.285 -40.340 -11.773 1.00 27.21 ?  158 LYS   B HG3  1 
ATOM   6462 H HD2  . LYS   B 1 158 ? 46.254 -38.500 -12.738 1.00 29.96 ?  158 LYS   B HD2  1 
ATOM   6463 H HD3  . LYS   B 1 158 ? 47.533 -38.251 -13.655 1.00 29.96 ?  158 LYS   B HD3  1 
ATOM   6464 H HE2  . LYS   B 1 158 ? 47.119 -40.101 -14.886 1.00 31.89 ?  158 LYS   B HE2  1 
ATOM   6465 H HE3  . LYS   B 1 158 ? 46.063 -40.646 -13.831 1.00 31.89 ?  158 LYS   B HE3  1 
ATOM   6466 H HZ1  . LYS   B 1 158 ? 45.003 -39.792 -15.649 1.00 31.88 ?  158 LYS   B HZ1  1 
ATOM   6467 H HZ2  . LYS   B 1 158 ? 44.652 -38.987 -14.497 1.00 31.88 ?  158 LYS   B HZ2  1 
ATOM   6468 H HZ3  . LYS   B 1 158 ? 45.616 -38.493 -15.459 1.00 31.88 ?  158 LYS   B HZ3  1 
ATOM   6469 N N    . ASN   B 1 159 ? 46.849 -39.810 -8.646  1.00 18.57 ?  159 ASN   B N    1 
ATOM   6470 C CA   . ASN   B 1 159 ? 45.897 -40.794 -8.137  1.00 19.33 ?  159 ASN   B CA   1 
ATOM   6471 C C    . ASN   B 1 159 ? 44.696 -40.123 -7.464  1.00 17.97 ?  159 ASN   B C    1 
ATOM   6472 O O    . ASN   B 1 159 ? 43.565 -40.613 -7.570  1.00 18.03 ?  159 ASN   B O    1 
ATOM   6473 C CB   . ASN   B 1 159 ? 46.609 -41.757 -7.194  1.00 21.53 ?  159 ASN   B CB   1 
ATOM   6474 C CG   . ASN   B 1 159 ? 47.641 -42.604 -7.907  1.00 23.66 ?  159 ASN   B CG   1 
ATOM   6475 O OD1  . ASN   B 1 159 ? 47.392 -43.117 -9.007  1.00 24.35 ?  159 ASN   B OD1  1 
ATOM   6476 N ND2  . ASN   B 1 159 ? 48.804 -42.774 -7.282  1.00 24.30 ?  159 ASN   B ND2  1 
ATOM   6477 H H    . ASN   B 1 159 ? 47.602 -39.771 -8.235  1.00 22.30 ?  159 ASN   B H    1 
ATOM   6478 H HA   . ASN   B 1 159 ? 45.567 -41.307 -8.893  1.00 23.21 ?  159 ASN   B HA   1 
ATOM   6479 H HB2  . ASN   B 1 159 ? 47.062 -41.251 -6.505  1.00 25.85 ?  159 ASN   B HB2  1 
ATOM   6480 H HB3  . ASN   B 1 159 ? 45.956 -42.353 -6.807  1.00 25.85 ?  159 ASN   B HB3  1 
ATOM   6481 H HD21 . ASN   B 1 159 ? 49.427 -43.245 -7.646  1.00 29.17 ?  159 ASN   B HD21 1 
ATOM   6482 H HD22 . ASN   B 1 159 ? 48.935 -42.416 -6.510  1.00 29.17 ?  159 ASN   B HD22 1 
ATOM   6483 N N    . LEU   B 1 160 ? 44.907 -38.991 -6.784  1.00 16.83 ?  160 LEU   B N    1 
ATOM   6484 C CA   . LEU   B 1 160 ? 43.771 -38.252 -6.243  1.00 15.97 ?  160 LEU   B CA   1 
ATOM   6485 C C    . LEU   B 1 160 ? 42.984 -37.587 -7.361  1.00 15.21 ?  160 LEU   B C    1 
ATOM   6486 O O    . LEU   B 1 160 ? 41.745 -37.588 -7.346  1.00 14.60 ?  160 LEU   B O    1 
ATOM   6487 C CB   . LEU   B 1 160 ? 44.242 -37.216 -5.222  1.00 15.53 ?  160 LEU   B CB   1 
ATOM   6488 C CG   . LEU   B 1 160 ? 43.116 -36.323 -4.681  1.00 15.52 ?  160 LEU   B CG   1 
ATOM   6489 C CD1  . LEU   B 1 160 ? 41.989 -37.150 -4.075  1.00 16.63 ?  160 LEU   B CD1  1 
ATOM   6490 C CD2  . LEU   B 1 160 ? 43.651 -35.331 -3.661  1.00 15.17 ?  160 LEU   B CD2  1 
ATOM   6491 H H    . LEU   B 1 160 ? 45.684 -38.635 -6.638  1.00 20.21 ?  160 LEU   B H    1 
ATOM   6492 H HA   . LEU   B 1 160 ? 43.186 -38.876 -5.799  1.00 19.18 ?  160 LEU   B HA   1 
ATOM   6493 H HB2  . LEU   B 1 160 ? 44.646 -37.683 -4.472  1.00 18.65 ?  160 LEU   B HB2  1 
ATOM   6494 H HB3  . LEU   B 1 160 ? 44.906 -36.642 -5.641  1.00 18.65 ?  160 LEU   B HB3  1 
ATOM   6495 H HG   . LEU   B 1 160 ? 42.745 -35.813 -5.414  1.00 18.64 ?  160 LEU   B HG   1 
ATOM   6496 H HD11 . LEU   B 1 160 ? 41.364 -36.554 -3.637  1.00 19.98 ?  160 LEU   B HD11 1 
ATOM   6497 H HD12 . LEU   B 1 160 ? 41.538 -37.641 -4.781  1.00 19.98 ?  160 LEU   B HD12 1 
ATOM   6498 H HD13 . LEU   B 1 160 ? 42.362 -37.771 -3.428  1.00 19.98 ?  160 LEU   B HD13 1 
ATOM   6499 H HD21 . LEU   B 1 160 ? 42.922 -34.768 -3.357  1.00 18.22 ?  160 LEU   B HD21 1 
ATOM   6500 H HD22 . LEU   B 1 160 ? 44.028 -35.817 -2.910  1.00 18.22 ?  160 LEU   B HD22 1 
ATOM   6501 H HD23 . LEU   B 1 160 ? 44.337 -34.785 -4.078  1.00 18.22 ?  160 LEU   B HD23 1 
ATOM   6502 N N    . TYR   B 1 161 ? 43.685 -37.019 -8.344  1.00 15.40 ?  161 TYR   B N    1 
ATOM   6503 C CA   . TYR   B 1 161 ? 43.015 -36.444 -9.504  1.00 15.15 ?  161 TYR   B CA   1 
ATOM   6504 C C    . TYR   B 1 161 ? 42.073 -37.468 -10.132 1.00 15.35 ?  161 TYR   B C    1 
ATOM   6505 O O    . TYR   B 1 161 ? 40.899 -37.179 -10.387 1.00 15.05 ?  161 TYR   B O    1 
ATOM   6506 C CB   . TYR   B 1 161 ? 44.057 -35.957 -10.520 1.00 15.84 ?  161 TYR   B CB   1 
ATOM   6507 C CG   . TYR   B 1 161 ? 43.478 -35.497 -11.837 1.00 16.39 ?  161 TYR   B CG   1 
ATOM   6508 C CD1  . TYR   B 1 161 ? 43.069 -34.178 -12.010 1.00 16.33 ?  161 TYR   B CD1  1 
ATOM   6509 C CD2  . TYR   B 1 161 ? 43.329 -36.373 -12.907 1.00 17.14 ?  161 TYR   B CD2  1 
ATOM   6510 C CE1  . TYR   B 1 161 ? 42.537 -33.748 -13.203 1.00 17.69 ?  161 TYR   B CE1  1 
ATOM   6511 C CE2  . TYR   B 1 161 ? 42.787 -35.950 -14.104 1.00 18.29 ?  161 TYR   B CE2  1 
ATOM   6512 C CZ   . TYR   B 1 161 ? 42.396 -34.635 -14.248 1.00 18.23 ?  161 TYR   B CZ   1 
ATOM   6513 O OH   . TYR   B 1 161 ? 41.852 -34.198 -15.432 1.00 20.18 ?  161 TYR   B OH   1 
ATOM   6514 H H    . TYR   B 1 161 ? 44.543 -36.957 -8.366  1.00 18.50 ?  161 TYR   B H    1 
ATOM   6515 H HA   . TYR   B 1 161 ? 42.488 -35.680 -9.226  1.00 18.19 ?  161 TYR   B HA   1 
ATOM   6516 H HB2  . TYR   B 1 161 ? 44.537 -35.202 -10.139 1.00 19.02 ?  161 TYR   B HB2  1 
ATOM   6517 H HB3  . TYR   B 1 161 ? 44.674 -36.674 -10.713 1.00 19.02 ?  161 TYR   B HB3  1 
ATOM   6518 H HD1  . TYR   B 1 161 ? 43.160 -33.566 -11.313 1.00 19.61 ?  161 TYR   B HD1  1 
ATOM   6519 H HD2  . TYR   B 1 161 ? 43.588 -37.260 -12.815 1.00 20.59 ?  161 TYR   B HD2  1 
ATOM   6520 H HE1  . TYR   B 1 161 ? 42.267 -32.858 -13.302 1.00 21.24 ?  161 TYR   B HE1  1 
ATOM   6521 H HE2  . TYR   B 1 161 ? 42.690 -36.549 -14.813 1.00 21.97 ?  161 TYR   B HE2  1 
ATOM   6522 H HH   . TYR   B 1 161 ? 41.819 -34.831 -15.986 1.00 24.23 ?  161 TYR   B HH   1 
ATOM   6523 N N    . ASP   B 1 162 ? 42.572 -38.685 -10.363 1.00 15.64 ?  162 ASP   B N    1 
ATOM   6524 C CA   . ASP   B 1 162 ? 41.748 -39.725 -10.975 1.00 16.33 ?  162 ASP   B CA   1 
ATOM   6525 C C    . ASP   B 1 162 ? 40.539 -40.066 -10.109 1.00 15.63 ?  162 ASP   B C    1 
ATOM   6526 O O    . ASP   B 1 162 ? 39.437 -40.282 -10.627 1.00 15.86 ?  162 ASP   B O    1 
ATOM   6527 C CB   . ASP   B 1 162 ? 42.582 -40.986 -11.222 1.00 17.88 ?  162 ASP   B CB   1 
ATOM   6528 C CG   . ASP   B 1 162 ? 43.587 -40.826 -12.351 1.00 19.67 ?  162 ASP   B CG   1 
ATOM   6529 O OD1  . ASP   B 1 162 ? 43.461 -39.875 -13.147 1.00 19.63 ?  162 ASP   B OD1  1 
ATOM   6530 O OD2  . ASP   B 1 162 ? 44.497 -41.678 -12.449 1.00 21.33 -1 162 ASP   B OD2  1 
ATOM   6531 H H    . ASP   B 1 162 ? 43.375 -38.922 -10.186 1.00 18.78 ?  162 ASP   B H    1 
ATOM   6532 H HA   . ASP   B 1 162 ? 41.423 -39.409 -11.832 1.00 19.61 ?  162 ASP   B HA   1 
ATOM   6533 H HB2  . ASP   B 1 162 ? 43.081 -41.199 -10.420 1.00 21.47 ?  162 ASP   B HB2  1 
ATOM   6534 H HB3  . ASP   B 1 162 ? 41.993 -41.715 -11.457 1.00 21.47 ?  162 ASP   B HB3  1 
ATOM   6535 N N    A LYS   B 1 163 ? 40.727 -40.143 -8.790  0.62 15.22 ?  163 LYS   B N    1 
ATOM   6536 N N    B LYS   B 1 163 ? 40.724 -40.127 -8.788  0.38 15.60 ?  163 LYS   B N    1 
ATOM   6537 C CA   A LYS   B 1 163 ? 39.600 -40.422 -7.907  0.62 15.45 ?  163 LYS   B CA   1 
ATOM   6538 C CA   B LYS   B 1 163 ? 39.603 -40.422 -7.901  0.38 15.98 ?  163 LYS   B CA   1 
ATOM   6539 C C    A LYS   B 1 163 ? 38.555 -39.316 -7.980  0.62 14.02 ?  163 LYS   B C    1 
ATOM   6540 C C    B LYS   B 1 163 ? 38.558 -39.313 -7.941  0.38 14.49 ?  163 LYS   B C    1 
ATOM   6541 O O    A LYS   B 1 163 ? 37.347 -39.590 -8.011  0.62 14.79 ?  163 LYS   B O    1 
ATOM   6542 O O    B LYS   B 1 163 ? 37.351 -39.586 -7.902  0.38 15.08 ?  163 LYS   B O    1 
ATOM   6543 C CB   A LYS   B 1 163 ? 40.079 -40.604 -6.469  0.62 17.82 ?  163 LYS   B CB   1 
ATOM   6544 C CB   B LYS   B 1 163 ? 40.102 -40.624 -6.472  0.38 18.24 ?  163 LYS   B CB   1 
ATOM   6545 C CG   A LYS   B 1 163 ? 38.998 -41.144 -5.554  0.62 21.61 ?  163 LYS   B CG   1 
ATOM   6546 C CG   B LYS   B 1 163 ? 39.023 -41.109 -5.522  0.38 20.96 ?  163 LYS   B CG   1 
ATOM   6547 C CD   A LYS   B 1 163 ? 39.408 -41.147 -4.095  0.62 25.10 ?  163 LYS   B CD   1 
ATOM   6548 C CD   B LYS   B 1 163 ? 39.528 -41.237 -4.097  0.38 23.70 ?  163 LYS   B CD   1 
ATOM   6549 C CE   A LYS   B 1 163 ? 38.331 -41.801 -3.242  0.62 27.23 ?  163 LYS   B CE   1 
ATOM   6550 C CE   B LYS   B 1 163 ? 38.470 -41.869 -3.207  0.38 25.88 ?  163 LYS   B CE   1 
ATOM   6551 N NZ   A LYS   B 1 163 ? 38.500 -41.519 -1.791  0.62 28.40 ?  163 LYS   B NZ   1 
ATOM   6552 N NZ   B LYS   B 1 163 ? 38.796 -41.747 -1.760  0.38 26.37 ?  163 LYS   B NZ   1 
ATOM   6553 H H    A LYS   B 1 163 ? 41.487 -40.039 -8.393  0.62 18.28 ?  163 LYS   B H    1 
ATOM   6554 H H    B LYS   B 1 163 ? 41.480 -40.005 -8.391  0.38 18.73 ?  163 LYS   B H    1 
ATOM   6555 H HA   A LYS   B 1 163 ? 39.184 -41.250 -8.192  0.62 18.55 ?  163 LYS   B HA   1 
ATOM   6556 H HA   B LYS   B 1 163 ? 39.183 -41.245 -8.194  0.38 19.19 ?  163 LYS   B HA   1 
ATOM   6557 H HB2  A LYS   B 1 163 ? 40.821 -41.231 -6.459  0.62 21.40 ?  163 LYS   B HB2  1 
ATOM   6558 H HB2  B LYS   B 1 163 ? 40.814 -41.285 -6.477  0.38 21.91 ?  163 LYS   B HB2  1 
ATOM   6559 H HB3  A LYS   B 1 163 ? 40.366 -39.746 -6.121  0.62 21.40 ?  163 LYS   B HB3  1 
ATOM   6560 H HB3  B LYS   B 1 163 ? 40.439 -39.780 -6.134  0.38 21.91 ?  163 LYS   B HB3  1 
ATOM   6561 H HG2  A LYS   B 1 163 ? 38.204 -40.594 -5.640  0.62 25.94 ?  163 LYS   B HG2  1 
ATOM   6562 H HG2  B LYS   B 1 163 ? 38.287 -40.478 -5.525  0.38 25.16 ?  163 LYS   B HG2  1 
ATOM   6563 H HG3  A LYS   B 1 163 ? 38.795 -42.059 -5.810  0.62 25.94 ?  163 LYS   B HG3  1 
ATOM   6564 H HG3  B LYS   B 1 163 ? 38.714 -41.983 -5.812  0.38 25.16 ?  163 LYS   B HG3  1 
ATOM   6565 H HD2  A LYS   B 1 163 ? 40.230 -41.652 -3.992  0.62 30.13 ?  163 LYS   B HD2  1 
ATOM   6566 H HD2  B LYS   B 1 163 ? 40.317 -41.801 -4.083  0.38 28.46 ?  163 LYS   B HD2  1 
ATOM   6567 H HD3  A LYS   B 1 163 ? 39.529 -40.234 -3.792  0.62 30.13 ?  163 LYS   B HD3  1 
ATOM   6568 H HD3  B LYS   B 1 163 ? 39.735 -40.356 -3.748  0.38 28.46 ?  163 LYS   B HD3  1 
ATOM   6569 H HE2  A LYS   B 1 163 ? 37.460 -41.476 -3.517  0.62 32.69 ?  163 LYS   B HE2  1 
ATOM   6570 H HE2  B LYS   B 1 163 ? 37.619 -41.431 -3.363  0.38 31.07 ?  163 LYS   B HE2  1 
ATOM   6571 H HE3  A LYS   B 1 163 ? 38.374 -42.761 -3.367  0.62 32.69 ?  163 LYS   B HE3  1 
ATOM   6572 H HE3  B LYS   B 1 163 ? 38.400 -42.813 -3.421  0.38 31.07 ?  163 LYS   B HE3  1 
ATOM   6573 H HZ1  A LYS   B 1 163 ? 37.853 -41.916 -1.327  0.62 34.09 ?  163 LYS   B HZ1  1 
ATOM   6574 H HZ1  B LYS   B 1 163 ? 38.156 -42.126 -1.272  0.38 31.66 ?  163 LYS   B HZ1  1 
ATOM   6575 H HZ2  A LYS   B 1 163 ? 39.287 -41.827 -1.513  0.62 34.09 ?  163 LYS   B HZ2  1 
ATOM   6576 H HZ2  B LYS   B 1 163 ? 39.569 -42.150 -1.588  0.38 31.66 ?  163 LYS   B HZ2  1 
ATOM   6577 H HZ3  A LYS   B 1 163 ? 38.465 -40.642 -1.646  0.62 34.09 ?  163 LYS   B HZ3  1 
ATOM   6578 H HZ3  B LYS   B 1 163 ? 38.860 -40.887 -1.536  0.38 31.66 ?  163 LYS   B HZ3  1 
ATOM   6579 N N    . LEU   B 1 164 ? 39.007 -38.058 -8.011  1.00 13.33 ?  164 LEU   B N    1 
ATOM   6580 C CA   . LEU   B 1 164 ? 38.090 -36.927 -8.059  1.00 13.10 ?  164 LEU   B CA   1 
ATOM   6581 C C    . LEU   B 1 164 ? 37.315 -36.911 -9.369  1.00 13.39 ?  164 LEU   B C    1 
ATOM   6582 O O    . LEU   B 1 164 ? 36.093 -36.707 -9.374  1.00 14.63 ?  164 LEU   B O    1 
ATOM   6583 C CB   . LEU   B 1 164 ? 38.882 -35.627 -7.886  1.00 12.72 ?  164 LEU   B CB   1 
ATOM   6584 C CG   . LEU   B 1 164 ? 39.410 -35.352 -6.482  1.00 13.79 ?  164 LEU   B CG   1 
ATOM   6585 C CD1  . LEU   B 1 164 ? 40.492 -34.278 -6.532  1.00 13.70 ?  164 LEU   B CD1  1 
ATOM   6586 C CD2  . LEU   B 1 164 ? 38.284 -34.927 -5.547  1.00 15.54 ?  164 LEU   B CD2  1 
ATOM   6587 H H    A LEU   B 1 164 ? 39.844 -37.837 -8.010  0.62 16.01 ?  164 LEU   B H    1 
ATOM   6588 H H    B LEU   B 1 164 ? 39.844 -37.838 -8.039  0.38 16.01 ?  164 LEU   B H    1 
ATOM   6589 H HA   . LEU   B 1 164 ? 37.459 -37.000 -7.335  1.00 15.74 ?  164 LEU   B HA   1 
ATOM   6590 H HB2  . LEU   B 1 164 ? 39.648 -35.652 -8.483  1.00 15.29 ?  164 LEU   B HB2  1 
ATOM   6591 H HB3  . LEU   B 1 164 ? 38.310 -34.886 -8.129  1.00 15.29 ?  164 LEU   B HB3  1 
ATOM   6592 H HG   . LEU   B 1 164 ? 39.815 -36.157 -6.128  1.00 16.56 ?  164 LEU   B HG   1 
ATOM   6593 H HD11 . LEU   B 1 164 ? 40.814 -34.105 -5.631  1.00 16.46 ?  164 LEU   B HD11 1 
ATOM   6594 H HD12 . LEU   B 1 164 ? 41.228 -34.589 -7.086  1.00 16.46 ?  164 LEU   B HD12 1 
ATOM   6595 H HD13 . LEU   B 1 164 ? 40.120 -33.465 -6.909  1.00 16.46 ?  164 LEU   B HD13 1 
ATOM   6596 H HD21 . LEU   B 1 164 ? 38.656 -34.713 -4.677  1.00 18.66 ?  164 LEU   B HD21 1 
ATOM   6597 H HD22 . LEU   B 1 164 ? 37.840 -34.150 -5.917  1.00 18.66 ?  164 LEU   B HD22 1 
ATOM   6598 H HD23 . LEU   B 1 164 ? 37.654 -35.661 -5.465  1.00 18.66 ?  164 LEU   B HD23 1 
ATOM   6599 N N    . VAL   B 1 165 ? 38.011 -37.088 -10.494 1.00 14.85 ?  165 VAL   B N    1 
ATOM   6600 C CA   . VAL   B 1 165 ? 37.358 -37.030 -11.798 1.00 16.35 ?  165 VAL   B CA   1 
ATOM   6601 C C    . VAL   B 1 165 ? 36.434 -38.225 -11.980 1.00 17.96 ?  165 VAL   B C    1 
ATOM   6602 O O    . VAL   B 1 165 ? 35.276 -38.085 -12.391 1.00 19.07 ?  165 VAL   B O    1 
ATOM   6603 C CB   . VAL   B 1 165 ? 38.408 -36.946 -12.922 1.00 17.51 ?  165 VAL   B CB   1 
ATOM   6604 C CG1  . VAL   B 1 165 ? 37.756 -37.050 -14.285 1.00 19.14 ?  165 VAL   B CG1  1 
ATOM   6605 C CG2  . VAL   B 1 165 ? 39.205 -35.651 -12.816 1.00 17.48 ?  165 VAL   B CG2  1 
ATOM   6606 H H    . VAL   B 1 165 ? 38.862 -37.239 -10.529 1.00 17.83 ?  165 VAL   B H    1 
ATOM   6607 H HA   . VAL   B 1 165 ? 36.820 -36.227 -11.844 1.00 19.64 ?  165 VAL   B HA   1 
ATOM   6608 H HB   . VAL   B 1 165 ? 39.036 -37.680 -12.829 1.00 21.02 ?  165 VAL   B HB   1 
ATOM   6609 H HG11 . VAL   B 1 165 ? 38.391 -36.773 -14.963 1.00 22.99 ?  165 VAL   B HG11 1 
ATOM   6610 H HG12 . VAL   B 1 165 ? 37.501 -37.976 -14.439 1.00 22.99 ?  165 VAL   B HG12 1 
ATOM   6611 H HG13 . VAL   B 1 165 ? 36.975 -36.483 -14.307 1.00 22.99 ?  165 VAL   B HG13 1 
ATOM   6612 H HG21 . VAL   B 1 165 ? 39.842 -35.604 -13.550 1.00 20.99 ?  165 VAL   B HG21 1 
ATOM   6613 H HG22 . VAL   B 1 165 ? 38.596 -34.896 -12.865 1.00 20.99 ?  165 VAL   B HG22 1 
ATOM   6614 H HG23 . VAL   B 1 165 ? 39.682 -35.633 -11.970 1.00 20.99 ?  165 VAL   B HG23 1 
ATOM   6615 N N    . SER   B 1 166 ? 36.936 -39.422 -11.671 1.00 18.86 ?  166 SER   B N    1 
ATOM   6616 C CA   . SER   B 1 166 ? 36.180 -40.630 -11.959 1.00 19.75 ?  166 SER   B CA   1 
ATOM   6617 C C    . SER   B 1 166 ? 34.924 -40.721 -11.109 1.00 19.94 ?  166 SER   B C    1 
ATOM   6618 O O    . SER   B 1 166 ? 33.965 -41.368 -11.522 1.00 21.72 ?  166 SER   B O    1 
ATOM   6619 C CB   . SER   B 1 166 ? 37.053 -41.875 -11.786 1.00 20.68 ?  166 SER   B CB   1 
ATOM   6620 O OG   . SER   B 1 166 ? 37.410 -42.084 -10.432 1.00 20.42 ?  166 SER   B OG   1 
ATOM   6621 H H    . SER   B 1 166 ? 37.711 -39.554 -11.307 1.00 22.65 ?  166 SER   B H    1 
ATOM   6622 H HA   . SER   B 1 166 ? 35.910 -40.598 -12.890 1.00 23.71 ?  166 SER   B HA   1 
ATOM   6623 H HB2  . SER   B 1 166 ? 36.558 -42.647 -12.102 1.00 24.84 ?  166 SER   B HB2  1 
ATOM   6624 H HB3  . SER   B 1 166 ? 37.862 -41.770 -12.317 1.00 24.84 ?  166 SER   B HB3  1 
ATOM   6625 H HG   . SER   B 1 166 ? 37.854 -41.428 -10.152 1.00 24.52 ?  166 SER   B HG   1 
ATOM   6626 N N    . SER   B 1 167 ? 34.896 -40.091 -9.937  1.00 18.78 ?  167 SER   B N    1 
ATOM   6627 C CA   . SER   B 1 167 ? 33.741 -40.153 -9.048  1.00 17.91 ?  167 SER   B CA   1 
ATOM   6628 C C    . SER   B 1 167 ? 32.824 -38.932 -9.137  1.00 17.64 ?  167 SER   B C    1 
ATOM   6629 O O    . SER   B 1 167 ? 31.748 -38.940 -8.527  1.00 18.02 ?  167 SER   B O    1 
ATOM   6630 C CB   . SER   B 1 167 ? 34.192 -40.349 -7.595  1.00 17.69 ?  167 SER   B CB   1 
ATOM   6631 O OG   . SER   B 1 167 ? 34.863 -39.191 -7.112  1.00 17.30 ?  167 SER   B OG   1 
ATOM   6632 H H    . SER   B 1 167 ? 35.540 -39.622 -9.635  1.00 22.55 ?  167 SER   B H    1 
ATOM   6633 H HA   . SER   B 1 167 ? 33.213 -40.931 -9.291  1.00 21.51 ?  167 SER   B HA   1 
ATOM   6634 H HB2  . SER   B 1 167 ? 33.408 -40.522 -7.048  1.00 21.24 ?  167 SER   B HB2  1 
ATOM   6635 H HB3  . SER   B 1 167 ? 34.792 -41.116 -7.558  1.00 21.24 ?  167 SER   B HB3  1 
ATOM   6636 H HG   . SER   B 1 167 ? 35.543 -39.045 -7.585  1.00 20.77 ?  167 SER   B HG   1 
ATOM   6637 N N    . PHE   B 1 168 ? 33.197 -37.901 -9.896  1.00 17.56 ?  168 PHE   B N    1 
ATOM   6638 C CA   . PHE   B 1 168 ? 32.361 -36.703 -9.970  1.00 16.81 ?  168 PHE   B CA   1 
ATOM   6639 C C    . PHE   B 1 168 ? 31.045 -36.973 -10.702 1.00 14.43 ?  168 PHE   B C    1 
ATOM   6640 O O    . PHE   B 1 168 ? 29.997 -36.382 -10.367 1.00 15.11 ?  168 PHE   B O    1 
ATOM   6641 C CB   . PHE   B 1 168 ? 33.131 -35.575 -10.656 1.00 17.73 ?  168 PHE   B CB   1 
ATOM   6642 C CG   . PHE   B 1 168 ? 32.340 -34.319 -10.785 1.00 17.30 ?  168 PHE   B CG   1 
ATOM   6643 C CD1  . PHE   B 1 168 ? 32.001 -33.596 -9.654  1.00 18.69 ?  168 PHE   B CD1  1 
ATOM   6644 C CD2  . PHE   B 1 168 ? 31.909 -33.874 -12.018 1.00 17.13 ?  168 PHE   B CD2  1 
ATOM   6645 C CE1  . PHE   B 1 168 ? 31.249 -32.448 -9.746  1.00 19.20 ?  168 PHE   B CE1  1 
ATOM   6646 C CE2  . PHE   B 1 168 ? 31.165 -32.711 -12.124 1.00 18.01 ?  168 PHE   B CE2  1 
ATOM   6647 C CZ   . PHE   B 1 168 ? 30.835 -31.994 -10.983 1.00 18.49 ?  168 PHE   B CZ   1 
ATOM   6648 H H    . PHE   B 1 168 ? 33.917 -37.869 -10.366 1.00 21.09 ?  168 PHE   B H    1 
ATOM   6649 H HA   . PHE   B 1 168 ? 32.145 -36.416 -9.071  1.00 20.19 ?  168 PHE   B HA   1 
ATOM   6650 H HB2  . PHE   B 1 168 ? 33.923 -35.374 -10.136 1.00 21.29 ?  168 PHE   B HB2  1 
ATOM   6651 H HB3  . PHE   B 1 168 ? 33.382 -35.860 -11.548 1.00 21.29 ?  168 PHE   B HB3  1 
ATOM   6652 H HD1  . PHE   B 1 168 ? 32.278 -33.901 -8.819  1.00 22.44 ?  168 PHE   B HD1  1 
ATOM   6653 H HD2  . PHE   B 1 168 ? 32.133 -34.348 -12.785 1.00 20.57 ?  168 PHE   B HD2  1 
ATOM   6654 H HE1  . PHE   B 1 168 ? 31.034 -31.970 -8.978  1.00 23.05 ?  168 PHE   B HE1  1 
ATOM   6655 H HE2  . PHE   B 1 168 ? 30.885 -32.407 -12.959 1.00 21.62 ?  168 PHE   B HE2  1 
ATOM   6656 H HZ   . PHE   B 1 168 ? 30.332 -31.214 -11.053 1.00 22.21 ?  168 PHE   B HZ   1 
ATOM   6657 N N    . LEU   B 1 169 ? 31.086 -37.846 -11.706 1.00 15.00 ?  169 LEU   B N    1 
ATOM   6658 C CA   . LEU   B 1 169 ? 29.916 -38.158 -12.521 1.00 17.49 ?  169 LEU   B CA   1 
ATOM   6659 C C    . LEU   B 1 169 ? 29.930 -39.595 -13.028 1.00 20.24 ?  169 LEU   B C    1 
ATOM   6660 O O    . LEU   B 1 169 ? 29.047 -40.007 -13.785 1.00 22.90 ?  169 LEU   B O    1 
ATOM   6661 C CB   . LEU   B 1 169 ? 29.839 -37.209 -13.716 1.00 19.71 ?  169 LEU   B CB   1 
ATOM   6662 C CG   . LEU   B 1 169 ? 28.596 -36.318 -13.775 1.00 23.15 ?  169 LEU   B CG   1 
ATOM   6663 C CD1  . LEU   B 1 169 ? 28.580 -35.511 -15.063 1.00 24.33 ?  169 LEU   B CD1  1 
ATOM   6664 C CD2  . LEU   B 1 169 ? 27.322 -37.136 -13.638 1.00 23.39 ?  169 LEU   B CD2  1 
ATOM   6665 O OXT  . LEU   B 1 169 ? 30.830 -40.367 -12.704 1.00 21.12 -1 169 LEU   B OXT  1 
ATOM   6666 H H    . LEU   B 1 169 ? 31.796 -38.270 -11.950 1.00 18.01 ?  169 LEU   B H    1 
ATOM   6667 H HA   . LEU   B 1 169 ? 29.123 -38.025 -11.982 1.00 21.01 ?  169 LEU   B HA   1 
ATOM   6668 H HB2  . LEU   B 1 169 ? 30.613 -36.623 -13.699 1.00 23.66 ?  169 LEU   B HB2  1 
ATOM   6669 H HB3  . LEU   B 1 169 ? 29.853 -37.735 -14.532 1.00 23.66 ?  169 LEU   B HB3  1 
ATOM   6670 H HG   . LEU   B 1 169 ? 28.628 -35.691 -13.037 1.00 27.80 ?  169 LEU   B HG   1 
ATOM   6671 H HD11 . LEU   B 1 169 ? 27.796 -34.941 -15.065 1.00 29.21 ?  169 LEU   B HD11 1 
ATOM   6672 H HD12 . LEU   B 1 169 ? 29.384 -34.973 -15.107 1.00 29.21 ?  169 LEU   B HD12 1 
ATOM   6673 H HD13 . LEU   B 1 169 ? 28.547 -36.123 -15.815 1.00 29.21 ?  169 LEU   B HD13 1 
ATOM   6674 H HD21 . LEU   B 1 169 ? 26.583 -36.638 -14.018 1.00 28.09 ?  169 LEU   B HD21 1 
ATOM   6675 H HD22 . LEU   B 1 169 ? 27.435 -37.976 -14.112 1.00 28.09 ?  169 LEU   B HD22 1 
ATOM   6676 H HD23 . LEU   B 1 169 ? 27.158 -37.308 -12.698 1.00 28.09 ?  169 LEU   B HD23 1 
HETATM 6677 C C1   T TFA   C 2 .   ? 12.147 -1.243  1.471   0.30 11.39 ?  201 TFA   A C1   1 
HETATM 6678 C C2   T TFA   C 2 .   ? 12.766 -1.711  0.128   0.30 13.59 ?  201 TFA   A C2   1 
HETATM 6679 O O    T TFA   C 2 .   ? 12.834 -1.530  2.456   0.30 9.88  ?  201 TFA   A O    1 
HETATM 6680 F F1   T TFA   C 2 .   ? 12.786 -3.055  0.092   0.30 14.96 ?  201 TFA   A F1   1 
HETATM 6681 F F2   T TFA   C 2 .   ? 12.070 -1.308  -0.948  0.30 13.83 ?  201 TFA   A F2   1 
HETATM 6682 F F3   T TFA   C 2 .   ? 14.017 -1.280  -0.067  0.30 14.58 ?  201 TFA   A F3   1 
HETATM 6683 O OXT  T TFA   C 2 .   ? 11.071 -0.656  1.383   0.30 11.52 ?  201 TFA   A OXT  1 
HETATM 6684 N N2   B A1A9S D 3 .   ? 14.724 -0.032  4.271   0.38 10.04 ?  202 A1A9S A N2   1 
HETATM 6685 C C3   B A1A9S D 3 .   ? 17.891 1.111   -0.912  0.38 13.55 ?  202 A1A9S A C3   1 
HETATM 6686 C C6   B A1A9S D 3 .   ? 15.383 2.276   -0.791  0.38 13.33 ?  202 A1A9S A C6   1 
HETATM 6687 C C9   B A1A9S D 3 .   ? 14.123 -0.192  1.441   0.38 11.20 ?  202 A1A9S A C9   1 
HETATM 6688 C C12  B A1A9S D 3 .   ? 15.026 0.047   5.598   0.38 10.07 ?  202 A1A9S A C12  1 
HETATM 6689 C C14  B A1A9S D 3 .   ? 14.984 2.383   4.161   0.38 10.31 ?  202 A1A9S A C14  1 
HETATM 6690 C C1   B A1A9S D 3 .   ? 17.001 -1.144  -0.251  0.38 13.95 ?  202 A1A9S A C1   1 
HETATM 6691 C C10  B A1A9S D 3 .   ? 12.739 -0.879  1.819   0.38 11.64 ?  202 A1A9S A C10  1 
HETATM 6692 C C11  B A1A9S D 3 .   ? 14.687 1.136   3.530   0.38 9.80  ?  202 A1A9S A C11  1 
HETATM 6693 C C13  B A1A9S D 3 .   ? 15.271 2.255   5.527   0.38 10.16 ?  202 A1A9S A C13  1 
HETATM 6694 C C15  B A1A9S D 3 .   ? 15.074 3.796   3.881   0.38 11.24 ?  202 A1A9S A C15  1 
HETATM 6695 C C16  B A1A9S D 3 .   ? 15.431 4.450   5.040   0.38 10.74 ?  202 A1A9S A C16  1 
HETATM 6696 C C2   B A1A9S D 3 .   ? 16.789 0.314   -0.556  0.38 13.65 ?  202 A1A9S A C2   1 
HETATM 6697 C C4   B A1A9S D 3 .   ? 17.750 2.467   -1.209  0.38 13.54 ?  202 A1A9S A C4   1 
HETATM 6698 C C5   B A1A9S D 3 .   ? 16.487 3.050   -1.149  0.38 14.47 ?  202 A1A9S A C5   1 
HETATM 6699 C C7   B A1A9S D 3 .   ? 15.494 0.895   -0.494  0.38 12.93 ?  202 A1A9S A C7   1 
HETATM 6700 C C8   B A1A9S D 3 .   ? 14.247 0.072   -0.108  0.38 11.79 ?  202 A1A9S A C8   1 
HETATM 6701 N N1   B A1A9S D 3 .   ? 14.367 1.041   2.204   0.38 10.35 ?  202 A1A9S A N1   1 
HETATM 6702 N N3   B A1A9S D 3 .   ? 15.314 1.138   6.319   0.38 10.32 ?  202 A1A9S A N3   1 
HETATM 6703 N N4   B A1A9S D 3 .   ? 15.546 3.502   6.094   0.38 9.95  ?  202 A1A9S A N4   1 
HETATM 6704 O O1   B A1A9S D 3 .   ? 11.722 0.077   1.915   0.38 12.50 ?  202 A1A9S A O1   1 
HETATM 6705 H H5   B A1A9S D 3 .   ? 18.918 0.683   -0.971  0.38 16.28 ?  202 A1A9S A H5   1 
HETATM 6706 H H8   B A1A9S D 3 .   ? 14.402 2.777   -0.765  0.38 16.01 ?  202 A1A9S A H8   1 
HETATM 6707 H H1   B A1A9S D 3 .   ? 14.940 -0.902  1.695   0.38 13.45 ?  202 A1A9S A H1   1 
HETATM 6708 H H15  B A1A9S D 3 .   ? 15.039 -0.886  6.213   0.38 12.10 ?  202 A1A9S A H15  1 
HETATM 6709 H H4   B A1A9S D 3 .   ? 17.786 -1.355  0.493   0.38 16.76 ?  202 A1A9S A H4   1 
HETATM 6710 H H2   B A1A9S D 3 .   ? 17.312 -1.740  -1.129  0.38 16.76 ?  202 A1A9S A H2   1 
HETATM 6711 H H3   B A1A9S D 3 .   ? 16.144 -1.722  0.127   0.38 16.76 ?  202 A1A9S A H3   1 
HETATM 6712 H H12  B A1A9S D 3 .   ? 12.863 -1.441  2.781   0.38 13.98 ?  202 A1A9S A H12  1 
HETATM 6713 H H11  B A1A9S D 3 .   ? 12.459 -1.663  1.076   0.38 13.98 ?  202 A1A9S A H11  1 
HETATM 6714 H H16  B A1A9S D 3 .   ? 14.938 4.354   2.970   0.38 13.50 ?  202 A1A9S A H16  1 
HETATM 6715 H H17  B A1A9S D 3 .   ? 15.621 5.461   5.393   0.38 12.90 ?  202 A1A9S A H17  1 
HETATM 6716 H H6   B A1A9S D 3 .   ? 18.634 3.094   -1.488  0.38 16.27 ?  202 A1A9S A H6   1 
HETATM 6717 H H7   B A1A9S D 3 .   ? 16.370 4.130   -1.382  0.38 17.38 ?  202 A1A9S A H7   1 
HETATM 6718 H H9   B A1A9S D 3 .   ? 14.217 -0.897  -0.668  0.38 14.16 ?  202 A1A9S A H9   1 
HETATM 6719 H H10  B A1A9S D 3 .   ? 13.317 0.568   -0.463  0.38 14.16 ?  202 A1A9S A H10  1 
HETATM 6720 H H14  B A1A9S D 3 .   ? 14.277 1.897   1.671   0.38 12.44 ?  202 A1A9S A H14  1 
HETATM 6721 H H18  B A1A9S D 3 .   ? 15.776 3.708   7.012   0.38 11.95 ?  202 A1A9S A H18  1 
HETATM 6722 H H13  B A1A9S D 3 .   ? 10.865 -0.369  1.927   0.38 15.01 ?  202 A1A9S A H13  1 
HETATM 6723 O O    . HOH   E 4 .   ? 14.698 -4.500  20.536  1.00 43.92 ?  301 HOH   A O    1 
HETATM 6724 O O    A HOH   E 4 .   ? 4.665  3.960   0.619   0.62 18.21 ?  302 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 0.904  -4.001  -0.098  1.00 27.39 ?  303 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 15.047 -12.146 18.659  1.00 36.52 ?  304 HOH   A O    1 
HETATM 6727 O O    A HOH   E 4 .   ? -0.511 -3.045  3.100   0.62 30.09 ?  305 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 34.381 -1.851  12.460  1.00 36.54 ?  306 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 28.906 0.554   -9.657  1.00 19.26 ?  307 HOH   A O    1 
HETATM 6730 O O    B HOH   E 4 .   ? 9.062  3.498   -0.808  0.38 22.90 ?  308 HOH   A O    1 
HETATM 6731 O O    B HOH   E 4 .   ? 4.927  3.471   0.296   0.38 11.72 ?  309 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 11.940 0.418   14.794  1.00 30.06 ?  310 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 25.570 -0.706  -7.251  1.00 13.86 ?  311 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 14.982 3.918   17.752  1.00 37.47 ?  312 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 15.167 -8.081  -9.871  1.00 22.94 ?  313 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 19.846 -12.391 -9.079  1.00 22.06 ?  314 HOH   A O    1 
HETATM 6737 O O    A HOH   E 4 .   ? 14.036 -4.546  -11.734 0.62 23.92 ?  315 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 28.073 -6.259  19.687  1.00 36.88 ?  316 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 42.475 10.548  5.220   1.00 20.16 ?  317 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 13.553 -15.273 -7.491  1.00 23.12 ?  318 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 14.615 -13.918 16.708  1.00 22.31 ?  319 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 36.137 -5.079  -0.550  1.00 31.16 ?  320 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 31.070 6.124   -12.315 1.00 28.03 ?  321 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 28.180 -0.013  -13.394 1.00 33.41 ?  322 HOH   A O    1 
HETATM 6745 O O    . HOH   E 4 .   ? -0.706 -8.269  2.178   1.00 44.72 ?  323 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 27.321 13.816  2.922   1.00 26.08 ?  324 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 13.077 -1.518  -6.797  1.00 16.58 ?  325 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 30.182 -13.338 -8.591  1.00 18.61 ?  326 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 26.411 -19.336 -1.797  1.00 13.32 ?  327 HOH   A O    1 
HETATM 6750 O O    A HOH   E 4 .   ? 14.601 -3.620  3.097   0.62 14.77 ?  328 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 22.711 12.505  1.639   1.00 14.48 ?  329 HOH   A O    1 
HETATM 6752 O O    A HOH   E 4 .   ? 17.463 -1.681  0.442   0.62 24.61 ?  330 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 30.946 -18.114 7.807   1.00 19.39 ?  331 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 38.281 10.103  7.175   1.00 25.70 ?  332 HOH   A O    1 
HETATM 6755 O O    A HOH   E 4 .   ? 14.245 0.606   6.801   0.62 17.70 ?  333 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 17.019 -17.959 15.024  1.00 26.76 ?  334 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 18.811 -21.943 7.024   1.00 32.96 ?  335 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 9.113  -10.110 19.345  1.00 37.91 ?  336 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 38.570 4.969   6.943   1.00 14.49 ?  337 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? 39.707 -1.043  -5.225  1.00 18.60 ?  338 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 20.565 -19.781 -5.069  1.00 29.40 ?  339 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 44.362 7.111   6.395   1.00 25.64 ?  340 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 23.977 -2.078  -2.062  1.00 9.47  ?  341 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 33.925 -1.074  -9.015  1.00 26.02 ?  342 HOH   A O    1 
HETATM 6765 O O    A HOH   E 4 .   ? 8.141  -21.358 3.983   0.62 32.43 ?  343 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 22.233 -19.226 11.389  1.00 33.42 ?  344 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 14.250 -21.160 -4.247  1.00 30.25 ?  345 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 37.584 2.774   10.194  1.00 29.78 ?  346 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 7.904  -12.390 -0.978  1.00 16.85 ?  347 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 9.818  -21.205 5.598   1.00 20.40 ?  348 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 42.552 4.258   5.302   1.00 26.89 ?  349 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 5.473  3.095   4.531   1.00 30.25 ?  350 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 26.828 11.432  1.672   1.00 16.52 ?  351 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 22.248 5.365   18.912  1.00 37.68 ?  352 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 31.717 8.219   14.876  1.00 23.83 ?  353 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 37.398 11.949  4.968   1.00 30.69 ?  354 HOH   A O    1 
HETATM 6777 O O    B HOH   E 4 .   ? 11.921 6.576   10.446  0.38 25.38 ?  355 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 37.174 -2.798  9.702   1.00 39.64 ?  356 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 43.943 8.414   -3.085  1.00 25.30 ?  357 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 35.723 -12.667 6.836   1.00 14.91 ?  358 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 21.213 -2.271  -2.356  1.00 12.61 ?  359 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 18.613 -19.405 13.533  1.00 37.98 ?  360 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 18.454 4.962   -15.161 1.00 35.58 ?  361 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 16.432 -22.024 0.966   1.00 27.94 ?  362 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 31.748 -9.319  -6.671  1.00 20.53 ?  363 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 18.600 9.485   9.083   1.00 21.39 ?  364 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 21.281 10.238  15.059  1.00 32.49 ?  365 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 31.009 -13.919 -2.484  1.00 12.24 ?  366 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 13.875 -4.851  17.388  1.00 26.05 ?  367 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 7.558  -6.341  -6.744  1.00 43.79 ?  368 HOH   A O    1 
HETATM 6791 O O    A HOH   E 4 .   ? 11.035 -0.343  1.935   0.32 20.37 ?  369 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 30.791 3.106   8.252   1.00 10.83 ?  370 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 21.768 -13.733 -8.193  1.00 31.55 ?  371 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 17.066 -17.749 -5.033  1.00 26.09 ?  372 HOH   A O    1 
HETATM 6795 O O    . HOH   E 4 .   ? 21.816 -21.892 8.458   1.00 26.04 ?  373 HOH   A O    1 
HETATM 6796 O O    B HOH   E 4 .   ? 25.156 6.180   -6.948  0.38 16.17 ?  374 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 33.627 -7.143  4.256   1.00 15.71 ?  375 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 27.457 -10.603 14.051  1.00 16.02 ?  376 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 16.933 -19.201 4.924   1.00 14.41 ?  377 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 19.587 -11.086 24.184  1.00 60.65 ?  378 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 24.223 -7.749  14.428  1.00 16.19 ?  379 HOH   A O    1 
HETATM 6802 O O    A HOH   E 4 .   ? 3.562  -9.424  9.728   0.62 19.13 ?  380 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 24.297 3.628   -1.775  1.00 12.32 ?  381 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 6.852  -7.987  11.803  1.00 16.66 ?  382 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 33.463 -16.953 8.059   1.00 17.84 ?  383 HOH   A O    1 
HETATM 6806 O O    T HOH   E 4 .   ? 15.376 -0.388  2.387   0.30 12.67 ?  384 HOH   A O    1 
HETATM 6807 O O    B HOH   E 4 .   ? 15.080 -2.823  3.490   0.38 10.98 ?  385 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 43.396 7.819   2.690   1.00 22.27 ?  386 HOH   A O    1 
HETATM 6809 O O    A HOH   E 4 .   ? 24.552 2.071   -6.986  0.62 14.12 ?  387 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 31.656 -7.280  -9.897  1.00 19.73 ?  388 HOH   A O    1 
HETATM 6811 O O    B HOH   E 4 .   ? 14.989 7.250   7.316   0.38 18.53 ?  389 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 6.587  -3.046  12.696  1.00 24.82 ?  390 HOH   A O    1 
HETATM 6813 O O    B HOH   E 4 .   ? 10.822 2.089   12.225  0.38 17.39 ?  391 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 19.982 4.513   -7.529  1.00 15.12 ?  392 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 8.986  -12.127 17.114  1.00 40.03 ?  393 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 44.779 -0.710  3.033   1.00 35.89 ?  394 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 37.476 -2.013  5.721   1.00 24.67 ?  395 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 15.490 11.809  7.982   1.00 40.27 ?  396 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 24.654 -17.517 12.721  1.00 23.65 ?  397 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 22.653 -11.949 21.760  1.00 42.94 ?  398 HOH   A O    1 
HETATM 6821 O O    A HOH   E 4 .   ? 21.319 3.186   -0.347  0.62 11.92 ?  399 HOH   A O    1 
HETATM 6822 O O    A HOH   E 4 .   ? 15.768 -0.913  5.271   0.62 18.28 ?  400 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 27.390 2.336   18.740  1.00 25.77 ?  401 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 27.294 -5.902  -13.961 1.00 37.60 ?  402 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 38.140 -1.385  -1.951  1.00 17.61 ?  403 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 32.737 -9.230  5.915   1.00 19.31 ?  404 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 23.483 11.399  4.103   1.00 11.89 ?  405 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 30.022 -10.109 12.974  1.00 20.87 ?  406 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 15.102 -21.452 14.225  1.00 17.34 ?  407 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 14.468 -0.504  -12.228 1.00 19.35 ?  408 HOH   A O    1 
HETATM 6831 O O    B HOH   E 4 .   ? 7.473  2.449   8.312   0.38 28.50 ?  409 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 16.175 16.601  8.585   1.00 33.15 ?  410 HOH   A O    1 
HETATM 6833 O O    B HOH   E 4 .   ? 20.989 2.858   0.078   0.38 7.71  ?  411 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 18.620 -2.417  -16.417 1.00 42.77 ?  412 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 6.334  -5.360  11.055  1.00 16.21 ?  413 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 23.845 -15.659 -9.194  1.00 33.14 ?  414 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 28.506 -10.629 -13.952 1.00 48.35 ?  415 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 13.955 -22.962 7.430   1.00 17.06 ?  416 HOH   A O    1 
HETATM 6839 O O    B HOH   E 4 .   ? 2.976  -3.180  8.285   0.38 19.26 ?  417 HOH   A O    1 
HETATM 6840 O O    A HOH   E 4 .   ? 11.692 -10.740 -10.068 0.62 36.17 ?  418 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 30.749 1.843   16.695  1.00 18.10 ?  419 HOH   A O    1 
HETATM 6842 O O    . HOH   E 4 .   ? 20.484 -20.003 2.760   1.00 17.10 ?  420 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 23.832 -20.258 -1.356  1.00 15.26 ?  421 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 15.853 2.120   24.720  1.00 44.22 ?  422 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 26.878 4.203   -0.674  1.00 11.36 ?  423 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 14.421 -24.674 11.594  1.00 34.92 ?  424 HOH   A O    1 
HETATM 6847 O O    B HOH   E 4 .   ? 24.193 1.889   -6.538  0.38 17.26 ?  425 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 32.592 -4.317  -9.928  1.00 27.34 ?  426 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 30.295 -12.893 13.518  1.00 18.76 ?  427 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 27.868 0.834   -7.136  1.00 12.80 ?  428 HOH   A O    1 
HETATM 6851 O O    B HOH   E 4 .   ? 5.602  -0.007  -2.007  0.38 23.88 ?  429 HOH   A O    1 
HETATM 6852 O O    . HOH   E 4 .   ? 9.446  -16.280 -1.898  1.00 26.04 ?  430 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 34.953 -5.225  -3.100  1.00 16.77 ?  431 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 10.322 -22.120 -1.137  1.00 39.72 ?  432 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 40.857 -8.219  -6.700  1.00 36.94 ?  433 HOH   A O    1 
HETATM 6856 O O    . HOH   E 4 .   ? 32.503 -10.631 3.165   1.00 30.90 ?  434 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 41.575 1.569   4.985   1.00 34.64 ?  435 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 36.704 -5.011  5.360   1.00 22.50 ?  436 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 15.871 6.885   3.038   1.00 16.53 ?  437 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 22.733 8.028   18.411  1.00 41.72 ?  438 HOH   A O    1 
HETATM 6861 O O    A HOH   E 4 .   ? 11.006 1.584   12.753  0.62 19.06 ?  439 HOH   A O    1 
HETATM 6862 O O    B HOH   E 4 .   ? 20.751 4.462   -2.188  0.38 10.44 ?  440 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 11.604 -10.567 16.966  1.00 23.28 ?  441 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 10.288 -13.665 -1.670  1.00 14.84 ?  442 HOH   A O    1 
HETATM 6865 O O    A HOH   E 4 .   ? 24.063 3.989   -4.914  0.62 18.51 ?  443 HOH   A O    1 
HETATM 6866 O O    A HOH   E 4 .   ? 18.927 -0.636  -1.625  0.62 13.48 ?  444 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 27.175 -3.230  19.264  1.00 34.80 ?  445 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 21.398 -14.735 17.952  1.00 52.83 ?  446 HOH   A O    1 
HETATM 6869 O O    . HOH   E 4 .   ? 16.083 -14.141 20.231  1.00 48.03 ?  447 HOH   A O    1 
HETATM 6870 O O    B HOH   E 4 .   ? 23.776 3.627   -4.429  0.38 14.83 ?  448 HOH   A O    1 
HETATM 6871 O O    . HOH   E 4 .   ? 23.559 -8.045  17.104  1.00 20.77 ?  449 HOH   A O    1 
HETATM 6872 O O    . HOH   E 4 .   ? 23.253 -20.926 1.322   1.00 16.83 ?  450 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 31.249 -12.780 0.014   1.00 18.30 ?  451 HOH   A O    1 
HETATM 6874 O O    A HOH   E 4 .   ? 23.174 7.543   -3.232  0.62 28.50 ?  452 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 18.349 -15.949 16.374  1.00 38.65 ?  453 HOH   A O    1 
HETATM 6876 O O    A HOH   E 4 .   ? 13.996 -0.304  3.462   0.32 24.68 ?  454 HOH   A O    1 
HETATM 6877 O O    B HOH   E 4 .   ? 23.196 6.417   -1.996  0.38 11.92 ?  455 HOH   A O    1 
HETATM 6878 O O    . HOH   E 4 .   ? 34.395 -8.081  -0.557  1.00 29.51 ?  456 HOH   A O    1 
HETATM 6879 O O    A HOH   E 4 .   ? 18.833 2.066   -0.750  0.62 12.46 ?  457 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 20.552 -17.791 24.755  1.00 48.42 ?  458 HOH   A O    1 
HETATM 6881 O O    . HOH   E 4 .   ? 30.609 14.774  2.784   1.00 18.39 ?  459 HOH   A O    1 
HETATM 6882 O O    A HOH   E 4 .   ? 16.229 2.983   -1.439  0.62 13.45 ?  460 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 21.298 -9.131  21.391  1.00 51.30 ?  461 HOH   A O    1 
HETATM 6884 O O    . HOH   E 4 .   ? 29.698 -16.030 10.621  1.00 34.15 ?  462 HOH   A O    1 
HETATM 6885 O O    . HOH   E 4 .   ? 37.606 -8.758  -3.269  1.00 23.58 ?  463 HOH   A O    1 
HETATM 6886 O O    A HOH   E 4 .   ? -1.464 -4.899  7.645   0.62 43.43 ?  464 HOH   A O    1 
HETATM 6887 O O    . HOH   E 4 .   ? 29.748 -1.878  -12.729 1.00 42.89 ?  465 HOH   A O    1 
HETATM 6888 O O    B HOH   E 4 .   ? 11.026 0.296   -1.365  0.38 25.79 ?  466 HOH   A O    1 
HETATM 6889 O O    . HOH   E 4 .   ? 25.419 8.223   -4.949  1.00 42.30 ?  467 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 32.392 -15.903 10.889  1.00 34.08 ?  468 HOH   A O    1 
HETATM 6891 O O    B HOH   E 4 .   ? 5.255  -2.684  -2.629  0.38 25.32 ?  469 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 19.820 -17.379 -5.013  1.00 23.63 ?  470 HOH   A O    1 
HETATM 6893 O O    . HOH   E 4 .   ? 24.900 5.629   20.822  1.00 48.80 ?  471 HOH   A O    1 
HETATM 6894 O O    . HOH   E 4 .   ? 27.885 7.145   -6.539  1.00 36.97 ?  472 HOH   A O    1 
HETATM 6895 O O    . HOH   E 4 .   ? 24.614 14.697  7.868   1.00 36.41 ?  473 HOH   A O    1 
HETATM 6896 O O    . HOH   E 4 .   ? 23.115 -22.429 -3.312  1.00 34.30 ?  474 HOH   A O    1 
HETATM 6897 O O    . HOH   E 4 .   ? 27.438 -11.303 16.655  1.00 34.94 ?  475 HOH   A O    1 
HETATM 6898 O O    . HOH   E 4 .   ? 26.888 11.699  -1.474  1.00 33.90 ?  476 HOH   A O    1 
HETATM 6899 O O    . HOH   E 4 .   ? 15.665 -21.477 3.697   1.00 28.03 ?  477 HOH   A O    1 
HETATM 6900 O O    . HOH   E 4 .   ? 11.059 -14.947 -6.240  1.00 32.18 ?  478 HOH   A O    1 
HETATM 6901 O O    . HOH   E 4 .   ? 18.792 10.993  11.314  1.00 30.93 ?  479 HOH   A O    1 
HETATM 6902 O O    . HOH   E 4 .   ? 11.915 -13.355 16.416  1.00 51.78 ?  480 HOH   A O    1 
HETATM 6903 O O    . HOH   E 4 .   ? 39.552 -6.981  -3.473  1.00 41.87 ?  481 HOH   A O    1 
HETATM 6904 O O    . HOH   E 4 .   ? 17.976 -16.307 -8.829  1.00 41.15 ?  482 HOH   A O    1 
HETATM 6905 O O    . HOH   E 4 .   ? 12.247 1.677   17.369  1.00 38.98 ?  483 HOH   A O    1 
HETATM 6906 O O    . HOH   E 4 .   ? 15.650 -17.150 -6.992  1.00 28.60 ?  484 HOH   A O    1 
HETATM 6907 O O    . HOH   E 4 .   ? 23.504 13.758  5.519   1.00 18.26 ?  485 HOH   A O    1 
HETATM 6908 O O    . HOH   E 4 .   ? 25.743 10.797  -3.809  1.00 33.36 ?  486 HOH   A O    1 
HETATM 6909 O O    A HOH   E 4 .   ? 21.937 5.299   -5.833  0.62 27.60 ?  487 HOH   A O    1 
HETATM 6910 O O    B HOH   E 4 .   ? 21.248 4.744   -4.962  0.38 11.15 ?  488 HOH   A O    1 
HETATM 6911 O O    . HOH   E 4 .   ? 13.973 -10.359 -10.977 1.00 33.00 ?  489 HOH   A O    1 
HETATM 6912 O O    . HOH   E 4 .   ? 29.011 8.918   17.482  1.00 38.36 ?  490 HOH   A O    1 
HETATM 6913 O O    . HOH   E 4 .   ? 23.062 11.761  -4.069  1.00 18.23 ?  491 HOH   A O    1 
HETATM 6914 O O    . HOH   E 4 .   ? 17.432 -18.678 19.874  1.00 48.57 ?  492 HOH   A O    1 
HETATM 6915 O O    B HOH   E 4 .   ? 8.317  1.986   -3.549  0.38 19.11 ?  493 HOH   A O    1 
HETATM 6916 O O    . HOH   E 4 .   ? 35.292 7.372   12.282  1.00 41.80 ?  494 HOH   A O    1 
HETATM 6917 O O    . HOH   E 4 .   ? 40.874 -3.995  -0.429  1.00 39.51 ?  495 HOH   A O    1 
HETATM 6918 O O    . HOH   E 4 .   ? 16.010 -6.731  -12.044 1.00 40.22 ?  496 HOH   A O    1 
HETATM 6919 O O    . HOH   E 4 .   ? 30.893 0.727   19.205  1.00 39.57 ?  497 HOH   A O    1 
HETATM 6920 O O    . HOH   E 4 .   ? 16.751 -20.508 16.100  1.00 28.53 ?  498 HOH   A O    1 
HETATM 6921 O O    . HOH   E 4 .   ? 23.271 -12.828 19.372  1.00 41.54 ?  499 HOH   A O    1 
HETATM 6922 O O    . HOH   E 4 .   ? 28.504 -4.657  -12.336 1.00 32.37 ?  500 HOH   A O    1 
HETATM 6923 O O    . HOH   E 4 .   ? 39.177 2.418   7.460   1.00 33.01 ?  501 HOH   A O    1 
HETATM 6924 O O    . HOH   E 4 .   ? 28.552 -7.853  -15.285 1.00 48.50 ?  502 HOH   A O    1 
HETATM 6925 O O    . HOH   E 4 .   ? 41.721 9.300   -4.138  1.00 29.28 ?  503 HOH   A O    1 
HETATM 6926 O O    . HOH   E 4 .   ? 44.537 10.480  -1.544  1.00 30.49 ?  504 HOH   A O    1 
HETATM 6927 O O    . HOH   E 4 .   ? 31.424 -0.544  -10.549 1.00 27.45 ?  505 HOH   A O    1 
HETATM 6928 O O    . HOH   E 4 .   ? 18.407 -23.157 1.864   1.00 41.96 ?  506 HOH   A O    1 
HETATM 6929 O O    B HOH   E 4 .   ? 10.419 -1.804  -5.825  0.38 21.83 ?  507 HOH   A O    1 
HETATM 6930 O O    . HOH   E 4 .   ? 40.545 -0.229  -7.774  1.00 34.28 ?  508 HOH   A O    1 
HETATM 6931 O O    . HOH   E 4 .   ? 13.838 -25.156 8.869   1.00 29.94 ?  509 HOH   A O    1 
HETATM 6932 O O    . HOH   E 4 .   ? 19.971 -22.347 4.159   1.00 25.32 ?  510 HOH   A O    1 
HETATM 6933 O O    . HOH   E 4 .   ? 30.766 5.747   -14.738 1.00 32.43 ?  511 HOH   A O    1 
HETATM 6934 O O    . HOH   E 4 .   ? 16.124 -23.387 5.780   1.00 30.56 ?  512 HOH   A O    1 
HETATM 6935 O O    . HOH   E 4 .   ? 37.341 -6.624  7.538   1.00 22.90 ?  513 HOH   A O    1 
HETATM 6936 O O    . HOH   E 4 .   ? 30.715 -5.764  -11.882 1.00 46.49 ?  514 HOH   A O    1 
HETATM 6937 O O    . HOH   E 4 .   ? 23.098 -23.760 1.684   1.00 29.88 ?  515 HOH   A O    1 
HETATM 6938 O O    . HOH   E 4 .   ? 39.528 0.022   6.528   1.00 28.22 ?  516 HOH   A O    1 
HETATM 6939 O O    B HOH   E 4 .   ? 14.378 7.892   4.695   0.38 20.07 ?  517 HOH   A O    1 
HETATM 6940 O O    . HOH   E 4 .   ? 38.040 13.900  6.784   1.00 46.34 ?  518 HOH   A O    1 
HETATM 6941 O O    . HOH   E 4 .   ? 29.006 14.387  0.860   1.00 46.76 ?  519 HOH   A O    1 
HETATM 6942 O O    . HOH   E 4 .   ? 8.026  -3.156  -5.914  1.00 47.47 ?  520 HOH   A O    1 
HETATM 6943 O O    . HOH   E 4 .   ? 20.434 -16.178 -7.382  1.00 25.97 ?  521 HOH   A O    1 
HETATM 6944 O O    B HOH   E 4 .   ? 9.369  0.808   -5.600  0.38 25.75 ?  522 HOH   A O    1 
HETATM 6945 O O    . HOH   E 4 .   ? 21.955 -24.018 4.403   1.00 26.76 ?  523 HOH   A O    1 
HETATM 6946 O O    . HOH   E 4 .   ? 36.406 -6.537  10.133  1.00 44.11 ?  524 HOH   A O    1 
HETATM 6947 O O    B HOH   E 4 .   ? 21.493 7.418   -5.729  0.38 17.85 ?  525 HOH   A O    1 
HETATM 6948 O O    A HOH   E 4 .   ? 14.826 8.684   4.894   0.62 39.66 ?  526 HOH   A O    1 
HETATM 6949 O O    . HOH   E 4 .   ? 17.307 -6.516  -14.197 1.00 38.04 ?  527 HOH   A O    1 
HETATM 6950 O O    T HOH   E 4 .   ? 11.888 -2.109  -3.654  0.30 11.12 ?  528 HOH   A O    1 
HETATM 6951 O O    . HOH   E 4 .   ? 24.024 9.008   -7.209  1.00 43.31 ?  529 HOH   A O    1 
HETATM 6952 O O    . HOH   E 4 .   ? 15.860 -12.347 27.459  1.00 44.28 ?  530 HOH   A O    1 
HETATM 6953 O O    . HOH   E 4 .   ? 16.350 -21.060 18.824  1.00 36.75 ?  531 HOH   A O    1 
HETATM 6954 O O    . HOH   E 4 .   ? 14.718 -22.799 19.842  1.00 36.89 ?  532 HOH   A O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 29.763 -22.418 5.450   1.00 19.83 ?  201 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 48.120 -6.839  15.547  1.00 33.05 ?  202 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 52.860 -13.419 -20.279 1.00 31.64 ?  203 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 41.297 -7.854  5.485   1.00 37.71 ?  204 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 41.791 -36.050 -17.223 1.00 29.82 ?  205 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 49.371 -22.682 -19.720 1.00 45.00 ?  206 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 37.906 -39.468 -0.196  1.00 37.37 ?  207 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 50.232 -3.320  7.246   1.00 35.68 ?  208 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 27.871 -41.927 -15.099 1.00 33.16 ?  209 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 59.131 -18.815 6.774   1.00 33.50 ?  210 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 47.277 -7.391  -3.900  1.00 39.30 ?  211 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 57.695 -24.460 5.066   1.00 32.71 ?  212 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 54.453 -9.348  -8.817  1.00 17.31 ?  213 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 56.322 -19.699 7.313   1.00 32.26 ?  214 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 58.206 -12.888 8.429   1.00 33.03 ?  215 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 55.414 -16.528 -14.347 1.00 35.54 ?  216 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 30.194 -41.046 -8.098  1.00 15.58 ?  217 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 37.127 -19.765 -18.086 1.00 33.80 ?  218 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 35.942 -43.247 -8.545  1.00 28.51 ?  219 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 57.185 -26.890 -7.686  1.00 42.09 ?  220 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 27.660 -29.206 -1.805  1.00 37.70 ?  221 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 50.694 -6.087  0.177   1.00 25.45 ?  222 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 44.408 -7.119  2.083   1.00 34.95 ?  223 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 57.406 -16.259 -12.151 1.00 17.99 ?  224 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 34.503 -36.378 -7.202  1.00 16.78 ?  225 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 30.778 -28.755 4.289   1.00 23.72 ?  226 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 41.486 -39.178 -14.872 1.00 21.25 ?  227 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 29.789 -26.303 3.917   1.00 27.31 ?  228 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 39.288 -10.910 6.151   1.00 25.51 ?  229 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 48.037 -24.514 -17.705 1.00 28.36 ?  230 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 32.809 -43.827 -11.326 1.00 19.02 ?  231 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 56.694 -30.776 -7.754  1.00 33.20 ?  232 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 35.010 -7.997  -2.996  1.00 18.27 ?  233 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 51.630 -6.472  4.438   1.00 19.21 ?  234 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 50.673 -12.947 -0.479  1.00 11.43 ?  235 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 45.119 -34.983 6.860   1.00 37.44 ?  236 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 29.820 -34.275 -0.464  1.00 33.84 ?  237 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 31.700 -17.893 -14.469 1.00 29.58 ?  238 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 25.411 -25.973 -1.340  1.00 30.52 ?  239 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 28.348 -19.700 -13.138 1.00 23.73 ?  240 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 44.961 -43.542 -10.479 1.00 27.31 ?  241 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 40.648 -16.019 14.179  1.00 24.56 ?  242 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 41.305 -9.602  13.113  1.00 22.58 ?  243 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 42.530 -25.360 2.636   1.00 14.19 ?  244 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 42.587 -22.874 3.840   1.00 10.80 ?  245 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 50.961 -39.935 -8.153  1.00 31.23 ?  246 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 51.544 -13.853 11.076  1.00 24.59 ?  247 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 48.581 -36.466 -15.534 1.00 42.13 ?  248 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 46.385 -1.524  13.272  1.00 28.12 ?  249 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 43.194 -32.390 -17.038 1.00 22.35 ?  250 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 44.463 -27.737 -0.703  1.00 21.44 ?  251 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 34.836 -24.626 13.863  1.00 29.16 ?  252 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 57.577 -24.373 -3.821  1.00 21.10 ?  253 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 41.813 -23.511 9.312   1.00 15.98 ?  254 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 43.055 -43.267 -8.220  1.00 27.91 ?  255 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 34.178 -18.480 11.429  1.00 22.75 ?  256 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 39.420 -11.068 0.340   1.00 15.86 ?  257 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 29.677 -25.226 -10.833 1.00 15.51 ?  258 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 58.114 -10.587 -4.070  1.00 20.92 ?  259 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 27.122 -31.839 -9.964  1.00 19.47 ?  260 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 40.263 -12.735 -11.503 1.00 13.95 ?  261 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 38.385 -11.044 -2.243  1.00 17.61 ?  262 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 30.799 -15.715 2.650   1.00 12.73 ?  263 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 56.128 -23.503 -14.706 1.00 24.70 ?  264 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 38.872 -11.974 12.422  1.00 33.71 ?  265 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 47.961 -22.771 5.852   1.00 16.65 ?  266 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 57.458 -9.211  1.452   1.00 19.29 ?  267 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 28.475 -30.839 -14.740 1.00 27.52 ?  268 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 43.305 -15.773 -12.174 1.00 13.11 ?  269 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 34.910 -33.389 -19.160 1.00 28.83 ?  270 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 49.297 -28.677 -6.876  1.00 14.29 ?  271 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 42.890 -20.330 -20.834 1.00 32.72 ?  272 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 30.557 -42.239 -10.616 1.00 27.98 ?  273 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 28.252 -34.379 -9.415  1.00 18.32 ?  274 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 27.912 -22.904 -8.024  1.00 16.51 ?  275 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 49.866 -24.702 5.744   1.00 31.72 ?  276 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 42.271 -9.890  9.395   1.00 20.78 ?  277 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 56.901 -8.620  8.472   1.00 18.96 ?  278 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 46.589 -31.256 -4.769  1.00 20.94 ?  279 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 42.244 -10.006 -14.903 1.00 37.81 ?  280 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 49.728 -0.458  10.233  1.00 29.66 ?  281 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 27.571 -26.770 -15.722 1.00 31.62 ?  282 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 57.660 -22.138 3.043   1.00 28.29 ?  283 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 34.394 -12.789 2.659   1.00 23.17 ?  284 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 42.344 -34.706 3.786   1.00 24.99 ?  285 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 48.374 -25.038 3.126   1.00 12.40 ?  286 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 52.542 -10.403 13.013  1.00 21.62 ?  287 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 36.717 -12.758 -1.504  1.00 26.24 ?  288 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 45.324 -33.425 -15.900 1.00 21.61 ?  289 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 59.748 -15.321 8.167   1.00 31.45 ?  290 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 43.524 -15.395 18.250  1.00 30.73 ?  291 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 33.475 -15.299 -13.977 1.00 20.19 ?  292 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 57.058 -12.073 12.359  1.00 41.76 ?  293 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 41.130 -5.502  11.505  1.00 46.98 ?  294 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 37.311 -35.656 7.195   1.00 31.91 ?  295 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 48.664 -20.022 5.959   1.00 13.08 ?  296 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 44.002 -29.340 -4.710  1.00 22.66 ?  297 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 47.070 -33.953 -4.597  1.00 16.36 ?  298 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 51.242 -37.635 -9.545  1.00 25.47 ?  299 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 46.833 -29.491 9.851   1.00 30.95 ?  300 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 40.184 -10.813 -9.549  1.00 15.93 ?  301 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 53.471 -30.168 4.518   1.00 18.14 ?  302 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 53.212 -16.106 -12.683 1.00 28.56 ?  303 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 44.585 -27.428 1.998   1.00 14.26 ?  304 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 42.631 -12.348 -18.553 1.00 29.10 ?  305 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 59.927 -17.094 -10.413 1.00 31.41 ?  306 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 51.355 -32.961 -10.709 1.00 36.86 ?  307 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 62.672 -13.582 4.703   1.00 27.10 ?  308 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 52.598 -35.681 -8.581  1.00 28.05 ?  309 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 41.661 -8.077  1.324   1.00 24.98 ?  310 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 37.460 -18.179 13.160  1.00 26.94 ?  311 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 25.888 -21.479 -3.551  1.00 15.11 ?  312 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 52.516 -29.220 -13.033 1.00 23.73 ?  313 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 44.526 -24.611 9.601   1.00 18.96 ?  314 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 34.937 -33.570 4.458   1.00 27.28 ?  315 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 45.869 -40.396 -3.549  1.00 29.19 ?  316 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 48.053 -32.626 -16.602 1.00 40.52 ?  317 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 26.269 -21.017 -6.251  1.00 15.60 ?  318 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 32.783 -34.599 -5.936  1.00 16.00 ?  319 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 43.146 -21.408 10.703  1.00 15.13 ?  320 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 37.787 -10.226 -10.763 1.00 16.49 ?  321 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 44.154 -1.783  7.594   1.00 43.18 ?  322 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 38.302 -12.755 7.945   1.00 17.91 ?  323 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 27.933 -14.806 -9.369  1.00 30.75 ?  324 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 41.210 -24.524 15.819  1.00 41.95 ?  325 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 51.709 -5.991  -7.927  1.00 47.49 ?  326 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 38.326 -9.297  -13.262 1.00 25.59 ?  327 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 37.160 -30.539 -21.058 1.00 29.83 ?  328 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 53.621 -12.642 -22.226 1.00 31.39 ?  329 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 36.660 -12.411 4.272   1.00 17.25 ?  330 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 47.158 -24.487 8.178   1.00 23.28 ?  331 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 62.902 -20.080 -0.756  1.00 35.79 ?  332 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 43.116 -34.650 0.106   1.00 19.04 ?  333 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 48.536 -11.875 -13.783 1.00 26.07 ?  334 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 33.546 -31.248 11.088  1.00 33.11 ?  335 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 47.420 -27.422 2.033   1.00 13.64 ?  336 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 42.838 -43.560 -14.353 1.00 39.72 ?  337 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 36.983 -15.096 -16.510 1.00 38.42 ?  338 HOH   B O    1 
HETATM 7093 O O    . HOH   F 4 .   ? 39.415 -23.625 -20.301 1.00 37.70 ?  339 HOH   B O    1 
HETATM 7094 O O    . HOH   F 4 .   ? 46.729 -19.893 12.323  1.00 29.35 ?  340 HOH   B O    1 
HETATM 7095 O O    . HOH   F 4 .   ? 45.657 -36.256 -16.106 1.00 33.53 ?  341 HOH   B O    1 
HETATM 7096 O O    . HOH   F 4 .   ? 37.091 -45.221 -9.786  1.00 37.14 ?  342 HOH   B O    1 
HETATM 7097 O O    . HOH   F 4 .   ? 32.947 -14.679 1.070   1.00 17.94 ?  343 HOH   B O    1 
HETATM 7098 O O    . HOH   F 4 .   ? 28.876 -43.023 -12.335 1.00 39.98 ?  344 HOH   B O    1 
HETATM 7099 O O    . HOH   F 4 .   ? 38.516 -22.346 15.044  1.00 40.07 ?  345 HOH   B O    1 
HETATM 7100 O O    . HOH   F 4 .   ? 39.815 -44.281 -11.245 1.00 37.55 ?  346 HOH   B O    1 
HETATM 7101 O O    . HOH   F 4 .   ? 38.456 -12.239 -16.232 1.00 40.97 ?  347 HOH   B O    1 
HETATM 7102 O O    . HOH   F 4 .   ? 27.673 -26.591 -0.609  1.00 28.90 ?  348 HOH   B O    1 
HETATM 7103 O O    . HOH   F 4 .   ? 40.430 -43.509 -9.125  1.00 26.16 ?  349 HOH   B O    1 
HETATM 7104 O O    . HOH   F 4 .   ? 33.694 -9.339  -8.874  1.00 31.66 ?  350 HOH   B O    1 
HETATM 7105 O O    . HOH   F 4 .   ? 62.535 -20.068 -4.867  1.00 41.07 ?  351 HOH   B O    1 
HETATM 7106 O O    . HOH   F 4 .   ? 55.635 -8.250  10.892  1.00 25.18 ?  352 HOH   B O    1 
HETATM 7107 O O    . HOH   F 4 .   ? 44.142 -37.311 -17.730 1.00 33.33 ?  353 HOH   B O    1 
HETATM 7108 O O    . HOH   F 4 .   ? 43.113 -12.703 -21.132 1.00 40.23 ?  354 HOH   B O    1 
HETATM 7109 O O    . HOH   F 4 .   ? 36.007 -8.560  -9.728  1.00 33.52 ?  355 HOH   B O    1 
HETATM 7110 O O    . HOH   F 4 .   ? 34.613 -10.302 7.499   1.00 23.78 ?  356 HOH   B O    1 
HETATM 7111 O O    . HOH   F 4 .   ? 56.496 -7.210  3.146   1.00 25.53 ?  357 HOH   B O    1 
HETATM 7112 O O    . HOH   F 4 .   ? 23.117 -23.672 6.836   1.00 33.76 ?  358 HOH   B O    1 
HETATM 7113 O O    . HOH   F 4 .   ? 34.070 -7.777  11.393  1.00 38.41 ?  359 HOH   B O    1 
HETATM 7114 O O    . HOH   F 4 .   ? 61.457 -19.861 1.672   1.00 33.34 ?  360 HOH   B O    1 
HETATM 7115 O O    . HOH   F 4 .   ? 56.917 -21.488 -16.356 1.00 38.11 ?  361 HOH   B O    1 
HETATM 7116 O O    . HOH   F 4 .   ? 40.181 -8.801  9.930   1.00 36.40 ?  362 HOH   B O    1 
HETATM 7117 O O    . HOH   F 4 .   ? 27.076 -25.981 -11.404 1.00 31.88 ?  363 HOH   B O    1 
HETATM 7118 O O    . HOH   F 4 .   ? 54.145 -5.669  3.092   1.00 33.47 ?  364 HOH   B O    1 
HETATM 7119 O O    . HOH   F 4 .   ? 36.098 -8.664  9.043   1.00 34.48 ?  365 HOH   B O    1 
HETATM 7120 O O    . HOH   F 4 .   ? 48.300 -26.556 8.883   1.00 40.07 ?  366 HOH   B O    1 
HETATM 7121 O O    . HOH   F 4 .   ? 58.913 -10.446 9.267   1.00 36.50 ?  367 HOH   B O    1 
HETATM 7122 O O    . HOH   F 4 .   ? 32.478 -23.609 14.128  1.00 38.53 ?  368 HOH   B O    1 
HETATM 7123 O O    . HOH   F 4 .   ? 41.820 -10.097 -17.422 1.00 52.74 ?  369 HOH   B O    1 
HETATM 7124 O O    . HOH   F 4 .   ? 40.023 -11.377 -13.985 1.00 29.60 ?  370 HOH   B O    1 
HETATM 7125 O O    . HOH   F 4 .   ? 39.816 -6.979  7.917   1.00 40.73 ?  371 HOH   B O    1 
HETATM 7126 O O    . HOH   F 4 .   ? 56.015 -7.754  -0.606  1.00 33.58 ?  372 HOH   B O    1 
HETATM 7127 O O    . HOH   F 4 .   ? 52.033 -12.860 13.368  1.00 32.87 ?  373 HOH   B O    1 
HETATM 7128 O O    . HOH   F 4 .   ? 62.978 -12.361 6.969   1.00 37.56 ?  374 HOH   B O    1 
HETATM 7129 O O    . HOH   F 4 .   ? 37.975 -10.649 10.071  1.00 30.99 ?  375 HOH   B O    1 
HETATM 7130 O O    . HOH   F 4 .   ? 36.518 -22.770 13.312  1.00 23.86 ?  376 HOH   B O    1 
HETATM 7131 O O    . HOH   F 4 .   ? 44.113 -5.530  -3.545  1.00 41.50 ?  377 HOH   B O    1 
HETATM 7132 O O    . HOH   F 4 .   ? 41.825 -6.661  -4.829  1.00 46.36 ?  378 HOH   B O    1 
HETATM 7133 O O    . HOH   F 4 .   ? 42.657 -17.232 -23.154 1.00 41.80 ?  379 HOH   B O    1 
HETATM 7134 O O    . HOH   F 4 .   ? 39.693 -14.079 15.680  1.00 49.67 ?  380 HOH   B O    1 
HETATM 7135 O O    . HOH   F 4 .   ? 39.957 -7.630  3.283   1.00 33.49 ?  381 HOH   B O    1 
HETATM 7136 O O    . HOH   F 4 .   ? 52.848 -29.908 7.170   1.00 22.37 ?  382 HOH   B O    1 
HETATM 7137 O O    . HOH   F 4 .   ? 60.454 -22.264 2.825   1.00 46.13 ?  383 HOH   B O    1 
HETATM 7138 O O    . HOH   F 4 .   ? 25.790 -18.758 -11.913 1.00 38.27 ?  384 HOH   B O    1 
HETATM 7139 O O    . HOH   F 4 .   ? 46.663 -5.381  2.954   1.00 40.90 ?  385 HOH   B O    1 
HETATM 7140 O O    . HOH   F 4 .   ? 23.838 -20.769 -7.654  1.00 25.84 ?  386 HOH   B O    1 
HETATM 7141 O O    . HOH   F 4 .   ? 40.934 -9.828  15.817  1.00 43.51 ?  387 HOH   B O    1 
HETATM 7142 O O    . HOH   F 4 .   ? 35.234 -20.279 13.293  1.00 29.31 ?  388 HOH   B O    1 
HETATM 7143 O O    . HOH   F 4 .   ? 35.316 -33.697 7.291   1.00 39.55 ?  389 HOH   B O    1 
HETATM 7144 O O    . HOH   F 4 .   ? 40.686 -6.606  -0.883  1.00 22.73 ?  390 HOH   B O    1 
HETATM 7145 O O    . HOH   F 4 .   ? 44.017 -31.833 -3.870  1.00 31.72 ?  391 HOH   B O    1 
HETATM 7146 O O    . HOH   F 4 .   ? 26.629 -28.014 -13.563 1.00 32.87 ?  392 HOH   B O    1 
HETATM 7147 O O    . HOH   F 4 .   ? 27.804 -27.075 2.186   1.00 29.13 ?  393 HOH   B O    1 
HETATM 7148 O O    . HOH   F 4 .   ? 34.271 -33.423 9.621   1.00 33.95 ?  394 HOH   B O    1 
HETATM 7149 O O    . HOH   F 4 .   ? 24.555 -20.638 -10.521 1.00 33.55 ?  395 HOH   B O    1 
HETATM 7150 O O    . HOH   F 4 .   ? 45.701 -20.301 15.190  1.00 50.15 ?  396 HOH   B O    1 
HETATM 7151 O O    . HOH   F 4 .   ? 26.853 -30.675 -12.646 1.00 27.55 ?  397 HOH   B O    1 
HETATM 7152 O O    . HOH   F 4 .   ? 50.618 -30.754 8.747   1.00 25.94 ?  398 HOH   B O    1 
HETATM 7153 O O    . HOH   F 4 .   ? 57.545 -6.428  -2.350  1.00 32.63 ?  399 HOH   B O    1 
HETATM 7154 O O    . HOH   F 4 .   ? 40.977 -11.753 -22.345 1.00 38.83 ?  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   ? 0.5418 0.5603 0.6410 0.0013  -0.0181 0.0698  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5339 0.5396 0.6169 -0.0048 -0.0122 0.0419  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5386 0.5569 0.6289 -0.0012 -0.0177 0.0702  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5309 0.5361 0.6071 -0.0060 -0.0121 0.0421  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5225 0.5470 0.5902 -0.0109 -0.0218 0.0742  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5160 0.5242 0.5726 -0.0122 -0.0147 0.0430  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5248 0.5491 0.6025 -0.0097 -0.0240 0.0752  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5186 0.5268 0.5835 -0.0116 -0.0163 0.0442  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.5489 0.5618 0.6462 0.0032  -0.0142 0.0675  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5402 0.5425 0.6241 -0.0029 -0.0100 0.0415  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.5526 0.5633 0.6486 0.0052  -0.0134 0.0662  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5434 0.5444 0.6272 -0.0015 -0.0096 0.0411  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.5519 0.5634 0.6494 0.0043  -0.0129 0.0674  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5430 0.5447 0.6277 -0.0018 -0.0093 0.0418  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.5016 0.5329 0.5315 -0.0224 -0.0235 0.0769  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.4962 0.5077 0.5216 -0.0193 -0.0162 0.0425  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.4781 0.5167 0.4655 -0.0348 -0.0252 0.0779  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.4741 0.4895 0.4652 -0.0268 -0.0179 0.0410  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.4472 0.4977 0.4249 -0.0483 -0.0220 0.0563  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.4449 0.4693 0.4305 -0.0360 -0.0146 0.0319  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.4485 0.4985 0.4192 -0.0476 -0.0236 0.0586  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.4460 0.4706 0.4290 -0.0352 -0.0142 0.0340  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.4828 0.5182 0.4323 -0.0342 -0.0297 0.1001  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.4790 0.4904 0.4401 -0.0257 -0.0226 0.0490  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.4854 0.5174 0.3979 -0.0349 -0.0338 0.1226  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.4822 0.4901 0.4168 -0.0252 -0.0272 0.0568  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.4880 0.5167 0.3825 -0.0351 -0.0367 0.1323  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.4841 0.4891 0.4078 -0.0250 -0.0312 0.0608  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.4853 0.5168 0.3899 -0.0348 -0.0346 0.1318  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.4827 0.4907 0.4135 -0.0246 -0.0271 0.0598  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.4143 0.4757 0.3846 -0.0629 -0.0167 0.0327  5   SER   A N   
60   N N   B SER   A 5   ? 0.4137 0.4465 0.3959 -0.0465 -0.0115 0.0202  5   SER   A N   
61   C CA  A SER   A 5   ? 0.3808 0.4535 0.3486 -0.0767 -0.0059 0.0094  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.3820 0.4236 0.3659 -0.0562 -0.0051 0.0089  5   SER   A CA  
63   C C   A SER   A 5   ? 0.3428 0.4220 0.2925 -0.0875 0.0052  -0.0064 5   SER   A C   
64   C C   B SER   A 5   ? 0.3477 0.3961 0.3219 -0.0632 0.0054  -0.0001 5   SER   A C   
65   O O   A SER   A 5   ? 0.3462 0.4277 0.2896 -0.0795 0.0068  -0.0191 5   SER   A O   
66   O O   B SER   A 5   ? 0.3512 0.4009 0.3221 -0.0592 0.0070  -0.0058 5   SER   A O   
67   C CB  A SER   A 5   ? 0.3866 0.4619 0.3744 -0.0796 -0.0024 0.0030  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.3846 0.4281 0.3849 -0.0584 -0.0068 0.0067  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.3897 0.4653 0.3855 -0.0828 0.0010  -0.0005 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.3854 0.4298 0.3922 -0.0608 -0.0088 0.0057  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.2984 0.3835 0.2271 -0.1057 0.0203  -0.0050 6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3087 0.3640 0.2773 -0.0743 0.0166  -0.0006 6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2617 0.3470 0.1787 -0.1155 0.0324  0.0082  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.2723 0.3327 0.2408 -0.0801 0.0253  0.0035  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2609 0.3440 0.1758 -0.1226 0.0538  0.0049  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.2614 0.3236 0.2423 -0.0804 0.0379  -0.0031 6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2690 0.3491 0.2074 -0.1243 0.0590  0.0127  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.2639 0.3241 0.2645 -0.0791 0.0422  -0.0004 6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2389 0.3147 0.1483 -0.1064 0.0283  0.0263  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2528 0.3129 0.2115 -0.0788 0.0255  0.0159  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2195 0.2863 0.1495 -0.0933 0.0191  0.0313  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2388 0.2983 0.1972 -0.0737 0.0172  0.0214  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2085 0.2772 0.1527 -0.0842 0.0149  0.0354  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2343 0.2930 0.1938 -0.0693 0.0134  0.0270  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2236 0.2772 0.1771 -0.0745 0.0202  0.0298  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2380 0.2930 0.2052 -0.0679 0.0146  0.0212  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2099 0.2745 0.1662 -0.0789 0.0247  0.0354  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2338 0.2911 0.1971 -0.0672 0.0140  0.0279  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2218 0.2757 0.1925 -0.0648 0.0223  0.0236  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2367 0.2929 0.2086 -0.0627 0.0118  0.0207  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2142 0.2720 0.1769 -0.0717 0.0215  0.0238  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2347 0.2904 0.2006 -0.0647 0.0101  0.0234  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2555 0.3377 0.1639 -0.1180 0.0715  -0.0017 7   SER   A N   
122  N N   B SER   A 7   ? 0.2509 0.3138 0.2300 -0.0779 0.0449  -0.0086 7   SER   A N   
123  C CA  A SER   A 7   ? 0.2585 0.3383 0.1957 -0.0989 0.0719  -0.0126 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2454 0.3065 0.2304 -0.0681 0.0462  -0.0133 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2403 0.3050 0.1756 -0.0926 0.0748  -0.0116 7   SER   A C   
126  C C   B SER   A 7   ? 0.2242 0.2794 0.1973 -0.0627 0.0501  -0.0017 7   SER   A C   
127  O O   A SER   A 7   ? 0.2503 0.3048 0.1768 -0.0963 0.0769  -0.0133 7   SER   A O   
128  O O   B SER   A 7   ? 0.2278 0.2778 0.1989 -0.0670 0.0538  0.0024  7   SER   A O   
129  C CB  A SER   A 7   ? 0.2791 0.3661 0.2515 -0.0836 0.0697  -0.0158 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.2633 0.3244 0.2663 -0.0608 0.0441  -0.0213 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2944 0.3763 0.2896 -0.0752 0.0653  -0.0160 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.2762 0.3347 0.2941 -0.0552 0.0420  -0.0263 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2169 0.2751 0.1765 -0.0804 0.0601  -0.0193 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2012 0.2575 0.1777 -0.0508 0.0440  0.0023  8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1999 0.2482 0.1885 -0.0587 0.0536  -0.0135 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.1891 0.2364 0.1800 -0.0373 0.0328  0.0116  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1709 0.2232 0.1747 -0.0397 0.0487  -0.0100 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1672 0.2157 0.1681 -0.0249 0.0280  0.0227  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1768 0.2241 0.1829 -0.0322 0.0395  -0.0284 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1704 0.2149 0.1781 -0.0175 0.0237  0.0161  8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1452 0.2110 0.1663 -0.0294 0.0469  0.0067  9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1515 0.2054 0.1672 -0.0191 0.0185  0.0304  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1376 0.1953 0.1395 -0.0280 0.0261  0.0073  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1457 0.1930 0.1493 -0.0195 0.0062  0.0282  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1338 0.1816 0.1277 -0.0186 0.0287  0.0347  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1426 0.1843 0.1450 -0.0178 0.0110  0.0300  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1463 0.1960 0.1541 -0.0127 0.0106  0.0421  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1455 0.1972 0.1497 -0.0209 0.0145  0.0355  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1354 0.1966 0.1399 -0.0228 0.0230  0.0029  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1408 0.1893 0.1396 -0.0167 0.0018  0.0272  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1392 0.1916 0.1590 -0.0117 0.0247  -0.0069 9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1383 0.1816 0.1378 -0.0090 0.0069  0.0206  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1368 0.1883 0.1665 -0.0118 0.0217  -0.0159 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1386 0.1754 0.1457 -0.0096 0.0175  0.0147  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1467 0.1873 0.1724 -0.0102 0.0230  0.0023  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1338 0.1773 0.1278 -0.0028 0.0083  0.0219  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1455 0.1902 0.1809 -0.0107 0.0253  -0.0219 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1334 0.1673 0.1460 -0.0110 0.0310  0.0193  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1533 0.1896 0.1743 -0.0117 0.0216  -0.0025 9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1328 0.1723 0.1265 0.0002  0.0219  0.0179  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1528 0.1913 0.1903 -0.0180 0.0298  -0.0070 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1288 0.1626 0.1437 -0.0085 0.0427  0.0169  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1657 0.1890 0.2145 -0.0287 0.0302  -0.0093 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1263 0.1584 0.1729 -0.0180 0.0425  0.0178  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1342 0.1693 0.1353 -0.0207 0.0231  0.0321  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1388 0.1719 0.1457 -0.0120 0.0062  0.0236  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1268 0.1628 0.1451 -0.0258 0.0196  0.0488  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1305 0.1565 0.1407 -0.0118 0.0048  0.0287  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1261 0.1579 0.1577 -0.0251 0.0163  0.0435  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1287 0.1410 0.1396 -0.0129 0.0021  0.0298  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1244 0.1466 0.1562 -0.0209 0.0175  0.0418  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1274 0.1262 0.1496 -0.0117 0.0068  0.0344  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1361 0.1674 0.1822 -0.0178 0.0056  0.0586  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1327 0.1522 0.1566 -0.0095 -0.0057 0.0345  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1454 0.1715 0.2346 -0.0126 -0.0180 0.0613  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1341 0.1534 0.1941 -0.0126 -0.0193 0.0360  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1518 0.1834 0.2682 -0.0138 0.0025  0.0607  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1272 0.1602 0.2159 -0.0100 -0.0090 0.0414  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1660 0.1831 0.2530 -0.0040 -0.0154 0.0522  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1469 0.1540 0.1938 -0.0093 -0.0189 0.0212  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1317 0.1606 0.1560 -0.0270 0.0118  0.0411  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1277 0.1403 0.1213 -0.0159 -0.0103 0.0376  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1391 0.1597 0.1665 -0.0365 0.0155  0.0363  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1358 0.1321 0.1299 -0.0169 -0.0073 0.0363  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1397 0.1694 0.1762 -0.0369 0.0235  0.0311  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1281 0.1211 0.1236 -0.0204 -0.0078 0.0313  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1413 0.1692 0.2181 -0.0519 0.0327  0.0187  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1162 0.1083 0.1375 -0.0156 -0.0113 0.0118  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1553 0.1577 0.1655 -0.0411 0.0013  0.0224  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1521 0.1293 0.1413 -0.0180 -0.0085 0.0306  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1673 0.1601 0.1579 -0.0372 0.0003  0.0235  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1617 0.1282 0.1470 -0.0123 -0.0061 0.0424  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1837 0.1642 0.1558 -0.0296 0.0056  0.0256  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1707 0.1293 0.1644 -0.0044 0.0017  0.0446  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1945 0.1638 0.1526 -0.0294 0.0061  0.0288  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1761 0.1260 0.1768 -0.0030 0.0045  0.0481  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1958 0.1658 0.1593 -0.0225 -0.0016 0.0278  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1754 0.1239 0.1900 0.0037  0.0007  0.0457  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1307 0.1731 0.1466 -0.0350 0.0168  0.0335  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1260 0.1354 0.1206 -0.0254 -0.0144 0.0390  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1302 0.1826 0.1487 -0.0280 0.0092  0.0299  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1256 0.1553 0.1271 -0.0202 -0.0086 0.0383  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1358 0.1733 0.1601 -0.0371 0.0027  0.0270  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1305 0.1587 0.1420 -0.0252 0.0035  0.0444  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1464 0.1835 0.1747 -0.0412 -0.0095 0.0077  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1335 0.1590 0.1344 -0.0197 0.0135  0.0581  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1379 0.1816 0.1514 -0.0182 0.0094  0.0212  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1304 0.1567 0.1298 -0.0106 -0.0075 0.0348  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1545 0.1799 0.1587 -0.0156 0.0082  0.0182  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1344 0.1467 0.1107 -0.0098 -0.0017 0.0318  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1669 0.1714 0.1508 -0.0145 0.0154  0.0247  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1404 0.1437 0.1099 -0.0077 0.0087  0.0233  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1553 0.1830 0.1706 -0.0167 0.0048  0.0162  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1329 0.1388 0.1043 -0.0098 -0.0003 0.0229  12  LEU   A CD2 
319  N N   . THR   A 13  ? 0.1311 0.1547 0.1675 -0.0274 0.0030  0.0314  13  THR   A N   
320  C CA  . THR   A 13  ? 0.1340 0.1575 0.1686 -0.0270 0.0142  0.0259  13  THR   A CA  
321  C C   . THR   A 13  ? 0.1389 0.1534 0.1772 -0.0309 0.0037  0.0399  13  THR   A C   
322  O O   . THR   A 13  ? 0.1379 0.1584 0.1742 -0.0235 -0.0075 0.0399  13  THR   A O   
323  C CB  . THR   A 13  ? 0.1390 0.1807 0.1794 -0.0293 0.0112  0.0336  13  THR   A CB  
324  O OG1 . THR   A 13  ? 0.1355 0.1758 0.1880 -0.0313 0.0117  0.0401  13  THR   A OG1 
325  C CG2 . THR   A 13  ? 0.1549 0.1995 0.1865 -0.0234 0.0155  0.0278  13  THR   A CG2 
334  N N   . ASP   A 14  ? 0.1442 0.1541 0.1992 -0.0333 0.0007  0.0458  14  ASP   A N   
335  C CA  . ASP   A 14  ? 0.1418 0.1593 0.2091 -0.0233 -0.0067 0.0490  14  ASP   A CA  
336  C C   . ASP   A 14  ? 0.1343 0.1648 0.1902 -0.0267 -0.0236 0.0567  14  ASP   A C   
337  O O   . ASP   A 14  ? 0.1669 0.1725 0.1939 -0.0382 -0.0198 0.0548  14  ASP   A O   
338  C CB  . ASP   A 14  ? 0.1741 0.1831 0.2813 -0.0214 -0.0076 0.0592  14  ASP   A CB  
339  C CG  . ASP   A 14  ? 0.2035 0.2336 0.3666 -0.0180 0.0006  0.0585  14  ASP   A CG  
340  O OD1 . ASP   A 14  ? 0.2164 0.2436 0.3849 -0.0071 -0.0059 0.0577  14  ASP   A OD1 
341  O OD2 . ASP   A 14  ? 0.2230 0.2764 0.4106 -0.0071 -0.0231 0.0493  14  ASP   A OD2 
346  N N   . ASN   A 15  ? 0.1273 0.1478 0.1890 -0.0267 -0.0028 0.0533  15  ASN   A N   
347  C CA  . ASN   A 15  ? 0.1293 0.1471 0.1933 -0.0189 -0.0107 0.0434  15  ASN   A CA  
348  C C   . ASN   A 15  ? 0.1216 0.1424 0.2123 -0.0181 0.0005  0.0406  15  ASN   A C   
349  O O   . ASN   A 15  ? 0.1344 0.1422 0.2649 -0.0224 -0.0207 0.0415  15  ASN   A O   
350  C CB  . ASN   A 15  ? 0.1257 0.1421 0.1890 -0.0175 -0.0039 0.0326  15  ASN   A CB  
351  C CG  . ASN   A 15  ? 0.1291 0.1478 0.1947 -0.0100 -0.0006 0.0213  15  ASN   A CG  
352  O OD1 . ASN   A 15  ? 0.1471 0.1577 0.2217 -0.0271 0.0028  0.0302  15  ASN   A OD1 
353  N ND2 . ASN   A 15  ? 0.1319 0.1625 0.1879 -0.0184 0.0077  0.0275  15  ASN   A ND2 
360  N N   A VAL   A 16  ? 0.1199 0.1437 0.1955 -0.0191 -0.0030 0.0400  16  VAL   A N   
361  N N   B VAL   A 16  ? 0.1221 0.1438 0.1953 -0.0158 0.0007  0.0401  16  VAL   A N   
362  C CA  A VAL   A 16  ? 0.1267 0.1513 0.1853 -0.0178 0.0032  0.0433  16  VAL   A CA  
363  C CA  B VAL   A 16  ? 0.1271 0.1495 0.1827 -0.0105 0.0068  0.0412  16  VAL   A CA  
364  C C   A VAL   A 16  ? 0.1226 0.1444 0.1673 -0.0189 -0.0027 0.0390  16  VAL   A C   
365  C C   B VAL   A 16  ? 0.1241 0.1449 0.1725 -0.0123 0.0059  0.0400  16  VAL   A C   
366  O O   A VAL   A 16  ? 0.1175 0.1428 0.1797 -0.0209 -0.0001 0.0331  16  VAL   A O   
367  O O   B VAL   A 16  ? 0.1190 0.1467 0.1836 -0.0096 0.0097  0.0338  16  VAL   A O   
368  C CB  A VAL   A 16  ? 0.1385 0.1664 0.1868 -0.0078 0.0221  0.0479  16  VAL   A CB  
369  C CB  B VAL   A 16  ? 0.1351 0.1600 0.1766 0.0011  0.0190  0.0401  16  VAL   A CB  
370  C CG1 A VAL   A 16  ? 0.1498 0.1733 0.2017 -0.0024 0.0330  0.0461  16  VAL   A CG1 
371  C CG1 B VAL   A 16  ? 0.1421 0.1639 0.1787 0.0108  0.0262  0.0412  16  VAL   A CG1 
372  C CG2 A VAL   A 16  ? 0.1487 0.1745 0.2030 -0.0072 0.0354  0.0449  16  VAL   A CG2 
373  C CG2 B VAL   A 16  ? 0.1429 0.1665 0.1899 0.0003  0.0275  0.0345  16  VAL   A CG2 
392  N N   . TYR   A 17  ? 0.1244 0.1365 0.1753 -0.0139 0.0091  0.0438  17  TYR   A N   
393  C CA  . TYR   A 17  ? 0.1312 0.1413 0.1596 -0.0188 0.0083  0.0412  17  TYR   A CA  
394  C C   . TYR   A 17  ? 0.1239 0.1358 0.1612 -0.0192 0.0081  0.0326  17  TYR   A C   
395  O O   . TYR   A 17  ? 0.1213 0.1384 0.1889 -0.0180 0.0125  0.0533  17  TYR   A O   
396  C CB  . TYR   A 17  ? 0.1443 0.1473 0.1641 -0.0303 -0.0088 0.0336  17  TYR   A CB  
397  C CG  . TYR   A 17  ? 0.1707 0.1511 0.1622 -0.0356 -0.0234 0.0335  17  TYR   A CG  
398  C CD1 . TYR   A 17  ? 0.1888 0.1539 0.1932 -0.0185 -0.0270 0.0363  17  TYR   A CD1 
399  C CD2 . TYR   A 17  ? 0.1912 0.1663 0.1595 -0.0441 -0.0182 0.0389  17  TYR   A CD2 
400  C CE1 . TYR   A 17  ? 0.2052 0.1549 0.1989 -0.0204 -0.0376 0.0414  17  TYR   A CE1 
401  C CE2 . TYR   A 17  ? 0.2068 0.1668 0.1751 -0.0438 -0.0264 0.0348  17  TYR   A CE2 
402  C CZ  . TYR   A 17  ? 0.2189 0.1589 0.1782 -0.0325 -0.0399 0.0455  17  TYR   A CZ  
403  O OH  . TYR   A 17  ? 0.2412 0.1657 0.1883 -0.0317 -0.0354 0.0341  17  TYR   A OH  
414  N N   A ILE   A 18  ? 0.1261 0.1373 0.1526 -0.0217 0.0119  0.0395  18  ILE   A N   
415  N N   B ILE   A 18  ? 0.1256 0.1323 0.1424 -0.0202 0.0134  0.0304  18  ILE   A N   
416  C CA  A ILE   A 18  ? 0.1268 0.1345 0.1415 -0.0120 0.0193  0.0337  18  ILE   A CA  
417  C CA  B ILE   A 18  ? 0.1214 0.1247 0.1255 -0.0135 0.0126  0.0218  18  ILE   A CA  
418  C C   A ILE   A 18  ? 0.1302 0.1409 0.1618 -0.0250 0.0163  0.0272  18  ILE   A C   
419  C C   B ILE   A 18  ? 0.1212 0.1338 0.0996 -0.0179 0.0038  0.0227  18  ILE   A C   
420  O O   A ILE   A 18  ? 0.1290 0.1524 0.1523 -0.0377 0.0153  0.0234  18  ILE   A O   
421  O O   B ILE   A 18  ? 0.1233 0.1390 0.1026 -0.0244 -0.0005 0.0189  18  ILE   A O   
422  C CB  A ILE   A 18  ? 0.1394 0.1337 0.1328 -0.0007 0.0224  0.0254  18  ILE   A CB  
423  C CB  B ILE   A 18  ? 0.1243 0.1288 0.1288 -0.0069 0.0268  0.0186  18  ILE   A CB  
424  C CG1 A ILE   A 18  ? 0.1452 0.1450 0.1221 0.0069  0.0164  0.0236  18  ILE   A CG1 
425  C CG1 B ILE   A 18  ? 0.1412 0.1367 0.1402 -0.0118 0.0316  0.0216  18  ILE   A CG1 
426  C CG2 A ILE   A 18  ? 0.1407 0.1289 0.1277 0.0027  0.0169  0.0155  18  ILE   A CG2 
427  C CG2 B ILE   A 18  ? 0.1265 0.1312 0.1386 -0.0109 0.0207  0.0131  18  ILE   A CG2 
428  C CD1 A ILE   A 18  ? 0.1660 0.1556 0.1223 0.0272  0.0157  0.0284  18  ILE   A CD1 
429  C CD1 B ILE   A 18  ? 0.1627 0.1467 0.1613 -0.0112 0.0303  0.0086  18  ILE   A CD1 
452  N N   A LYS   A 19  ? 0.1373 0.1443 0.1666 -0.0108 0.0284  0.0297  19  LYS   A N   
453  N N   B LYS   A 19  ? 0.1203 0.1290 0.0943 -0.0067 0.0219  0.0257  19  LYS   A N   
454  C CA  A LYS   A 19  ? 0.1615 0.1514 0.1779 -0.0108 0.0326  0.0333  19  LYS   A CA  
455  C CA  B LYS   A 19  ? 0.1302 0.1380 0.1089 -0.0039 0.0396  0.0227  19  LYS   A CA  
456  C C   A LYS   A 19  ? 0.1512 0.1410 0.1929 -0.0118 0.0420  0.0414  19  LYS   A C   
457  C C   B LYS   A 19  ? 0.1254 0.1369 0.1313 0.0054  0.0323  0.0201  19  LYS   A C   
458  O O   A LYS   A 19  ? 0.1463 0.1489 0.2049 -0.0094 0.0437  0.0522  19  LYS   A O   
459  O O   B LYS   A 19  ? 0.1191 0.1390 0.1424 0.0083  0.0298  0.0222  19  LYS   A O   
460  C CB  A LYS   A 19  ? 0.1861 0.1774 0.1916 -0.0107 0.0343  0.0338  19  LYS   A CB  
461  C CB  B LYS   A 19  ? 0.1394 0.1448 0.1074 -0.0102 0.0451  0.0108  19  LYS   A CB  
462  C CG  A LYS   A 19  ? 0.2110 0.1901 0.2039 -0.0076 0.0367  0.0259  19  LYS   A CG  
463  C CG  B LYS   A 19  ? 0.1652 0.1602 0.1237 -0.0040 0.0452  -0.0023 19  LYS   A CG  
464  C CD  A LYS   A 19  ? 0.2265 0.2033 0.2166 -0.0002 0.0474  0.0088  19  LYS   A CD  
465  C CD  B LYS   A 19  ? 0.1825 0.1770 0.1559 -0.0013 0.0511  -0.0099 19  LYS   A CD  
466  C CE  A LYS   A 19  ? 0.2338 0.2061 0.2241 -0.0016 0.0551  0.0056  19  LYS   A CE  
467  C CE  B LYS   A 19  ? 0.1914 0.1898 0.1782 -0.0063 0.0552  -0.0097 19  LYS   A CE  
468  N NZ  A LYS   A 19  ? 0.2381 0.2022 0.2077 -0.0110 0.0660  0.0012  19  LYS   A NZ  
469  N NZ  B LYS   A 19  ? 0.1961 0.1914 0.1804 -0.0061 0.0563  -0.0155 19  LYS   A NZ  
496  N N   A ASN   A 20  ? 0.1517 0.1414 0.2061 -0.0194 0.0439  0.0404  20  ASN   A N   
497  N N   B ASN   A 20  ? 0.1294 0.1407 0.1372 0.0059  0.0311  0.0115  20  ASN   A N   
498  C CA  A ASN   A 20  ? 0.1648 0.1528 0.2177 -0.0047 0.0566  0.0337  20  ASN   A CA  
499  C CA  B ASN   A 20  ? 0.1261 0.1471 0.1480 0.0070  0.0290  0.0101  20  ASN   A CA  
500  C C   A ASN   A 20  ? 0.1795 0.1574 0.2127 -0.0088 0.0686  0.0308  20  ASN   A C   
501  C C   B ASN   A 20  ? 0.1422 0.1497 0.1512 0.0076  0.0392  0.0027  20  ASN   A C   
502  O O   A ASN   A 20  ? 0.1909 0.1600 0.2078 -0.0124 0.0709  0.0204  20  ASN   A O   
503  O O   B ASN   A 20  ? 0.1473 0.1466 0.1610 0.0207  0.0368  -0.0032 20  ASN   A O   
504  C CB  A ASN   A 20  ? 0.1732 0.1611 0.2237 0.0093  0.0662  0.0351  20  ASN   A CB  
505  C CB  B ASN   A 20  ? 0.1172 0.1499 0.1519 0.0089  0.0233  0.0135  20  ASN   A CB  
506  C CG  A ASN   A 20  ? 0.1907 0.1630 0.2435 0.0228  0.0671  0.0299  20  ASN   A CG  
507  C CG  B ASN   A 20  ? 0.1176 0.1424 0.1582 0.0088  0.0103  0.0151  20  ASN   A CG  
508  O OD1 A ASN   A 20  ? 0.2184 0.1839 0.2906 0.0252  0.0789  0.0135  20  ASN   A OD1 
509  O OD1 B ASN   A 20  ? 0.1169 0.1219 0.1553 0.0081  0.0210  -0.0022 20  ASN   A OD1 
510  N ND2 A ASN   A 20  ? 0.1889 0.1489 0.2350 0.0287  0.0601  0.0334  20  ASN   A ND2 
511  N ND2 B ASN   A 20  ? 0.1268 0.1544 0.1731 0.0074  0.0011  0.0307  20  ASN   A ND2 
524  N N   A ALA   A 21  ? 0.1811 0.1610 0.2189 -0.0062 0.0589  0.0274  21  ALA   A N   
525  N N   B ALA   A 21  ? 0.1516 0.1585 0.1571 0.0038  0.0231  -0.0022 21  ALA   A N   
526  C CA  A ALA   A 21  ? 0.1822 0.1607 0.2153 -0.0088 0.0523  0.0299  21  ALA   A CA  
527  C CA  B ALA   A 21  ? 0.1610 0.1639 0.1647 -0.0043 0.0182  0.0001  21  ALA   A CA  
528  C C   A ALA   A 21  ? 0.1656 0.1640 0.2096 -0.0102 0.0452  0.0277  21  ALA   A C   
529  C C   B ALA   A 21  ? 0.1507 0.1593 0.1446 -0.0068 0.0377  0.0003  21  ALA   A C   
530  O O   A ALA   A 21  ? 0.1627 0.1747 0.2067 -0.0009 0.0324  0.0282  21  ALA   A O   
531  O O   B ALA   A 21  ? 0.1505 0.1620 0.1489 0.0004  0.0436  -0.0043 21  ALA   A O   
532  C CB  A ALA   A 21  ? 0.1897 0.1591 0.2115 -0.0121 0.0563  0.0278  21  ALA   A CB  
533  C CB  B ALA   A 21  ? 0.1690 0.1692 0.1878 -0.0011 0.0108  -0.0020 21  ALA   A CB  
544  N N   A ASP   A 22  ? 0.1639 0.1544 0.2285 -0.0128 0.0374  0.0252  22  ASP   A N   
545  N N   B ASP   A 22  ? 0.1500 0.1512 0.1555 -0.0131 0.0353  0.0064  22  ASP   A N   
546  C CA  A ASP   A 22  ? 0.1619 0.1493 0.2272 -0.0044 0.0300  0.0310  22  ASP   A CA  
547  C CA  B ASP   A 22  ? 0.1507 0.1475 0.1566 -0.0067 0.0285  0.0092  22  ASP   A CA  
548  C C   A ASP   A 22  ? 0.1545 0.1477 0.1887 -0.0028 0.0263  0.0383  22  ASP   A C   
549  C C   B ASP   A 22  ? 0.1413 0.1398 0.1253 -0.0081 0.0253  0.0099  22  ASP   A C   
550  O O   A ASP   A 22  ? 0.1647 0.1428 0.1945 -0.0047 0.0262  0.0382  22  ASP   A O   
551  O O   B ASP   A 22  ? 0.1383 0.1412 0.1308 -0.0063 0.0266  0.0163  22  ASP   A O   
552  C CB  A ASP   A 22  ? 0.1799 0.1550 0.2797 -0.0067 0.0183  0.0187  22  ASP   A CB  
553  C CB  B ASP   A 22  ? 0.1597 0.1525 0.1846 0.0043  0.0321  -0.0044 22  ASP   A CB  
554  C CG  A ASP   A 22  ? 0.1968 0.1693 0.3290 -0.0122 -0.0066 0.0270  22  ASP   A CG  
555  C CG  B ASP   A 22  ? 0.1656 0.1536 0.2042 0.0098  0.0477  -0.0009 22  ASP   A CG  
556  O OD1 A ASP   A 22  ? 0.1946 0.1723 0.3434 -0.0328 -0.0152 0.0396  22  ASP   A OD1 
557  O OD1 B ASP   A 22  ? 0.1690 0.1394 0.1798 0.0103  0.0515  0.0104  22  ASP   A OD1 
558  O OD2 A ASP   A 22  ? 0.2129 0.1806 0.3646 0.0017  -0.0019 0.0216  22  ASP   A OD2 
559  O OD2 B ASP   A 22  ? 0.1683 0.1709 0.2342 0.0013  0.0498  -0.0018 22  ASP   A OD2 
568  N N   A ILE   A 23  ? 0.1548 0.1594 0.1723 0.0005  0.0238  0.0291  23  ILE   A N   
569  N N   B ILE   A 23  ? 0.1387 0.1347 0.0994 -0.0025 0.0223  0.0100  23  ILE   A N   
570  C CA  A ILE   A 23  ? 0.1564 0.1540 0.1527 0.0013  0.0244  0.0245  23  ILE   A CA  
571  C CA  B ILE   A 23  ? 0.1298 0.1410 0.0968 -0.0047 0.0133  0.0151  23  ILE   A CA  
572  C C   A ILE   A 23  ? 0.1564 0.1543 0.1532 0.0010  0.0386  0.0276  23  ILE   A C   
573  C C   B ILE   A 23  ? 0.1272 0.1474 0.0951 -0.0103 0.0167  0.0057  23  ILE   A C   
574  O O   A ILE   A 23  ? 0.1668 0.1650 0.1558 0.0036  0.0339  0.0146  23  ILE   A O   
575  O O   B ILE   A 23  ? 0.1294 0.1440 0.0976 -0.0009 0.0129  0.0015  23  ILE   A O   
576  C CB  A ILE   A 23  ? 0.1589 0.1527 0.1372 0.0044  0.0166  0.0057  23  ILE   A CB  
577  C CB  B ILE   A 23  ? 0.1267 0.1373 0.1041 -0.0032 0.0131  0.0195  23  ILE   A CB  
578  C CG1 A ILE   A 23  ? 0.1653 0.1535 0.1386 0.0071  0.0129  0.0018  23  ILE   A CG1 
579  C CG1 B ILE   A 23  ? 0.1343 0.1391 0.0998 -0.0010 0.0161  0.0218  23  ILE   A CG1 
580  C CG2 A ILE   A 23  ? 0.1613 0.1615 0.1358 0.0096  0.0205  0.0183  23  ILE   A CG2 
581  C CG2 B ILE   A 23  ? 0.1245 0.1374 0.1208 0.0053  0.0116  0.0230  23  ILE   A CG2 
582  C CD1 A ILE   A 23  ? 0.1704 0.1529 0.1355 0.0070  0.0028  -0.0114 23  ILE   A CD1 
583  C CD1 B ILE   A 23  ? 0.1381 0.1445 0.1058 0.0071  0.0099  0.0143  23  ILE   A CD1 
606  N N   A VAL   A 24  ? 0.1615 0.1556 0.1550 0.0008  0.0335  0.0284  24  VAL   A N   
607  N N   B VAL   A 24  ? 0.1365 0.1568 0.1224 -0.0207 0.0093  -0.0005 24  VAL   A N   
608  C CA  A VAL   A 24  ? 0.1782 0.1640 0.1854 -0.0079 0.0343  0.0028  24  VAL   A CA  
609  C CA  B VAL   A 24  ? 0.1504 0.1625 0.1487 -0.0263 0.0067  0.0021  24  VAL   A CA  
610  C C   A VAL   A 24  ? 0.1909 0.1814 0.1952 -0.0164 0.0367  -0.0031 24  VAL   A C   
611  C C   B VAL   A 24  ? 0.1531 0.1737 0.1513 -0.0304 0.0138  -0.0176 24  VAL   A C   
612  O O   A VAL   A 24  ? 0.2042 0.1875 0.1952 -0.0202 0.0381  0.0043  24  VAL   A O   
613  O O   B VAL   A 24  ? 0.1575 0.1760 0.1674 -0.0226 0.0130  -0.0212 24  VAL   A O   
614  C CB  A VAL   A 24  ? 0.1813 0.1639 0.2146 -0.0076 0.0323  -0.0011 24  VAL   A CB  
615  C CB  B VAL   A 24  ? 0.1629 0.1663 0.1942 -0.0211 0.0059  0.0227  24  VAL   A CB  
616  C CG1 A VAL   A 24  ? 0.1874 0.1665 0.2350 -0.0023 0.0233  -0.0160 24  VAL   A CG1 
617  C CG1 B VAL   A 24  ? 0.1776 0.1747 0.2169 -0.0206 -0.0052 0.0241  24  VAL   A CG1 
618  C CG2 A VAL   A 24  ? 0.1944 0.1681 0.2262 -0.0037 0.0455  0.0143  24  VAL   A CG2 
619  C CG2 B VAL   A 24  ? 0.1724 0.1654 0.2132 -0.0135 0.0116  0.0363  24  VAL   A CG2 
638  N N   A GLU   A 25  ? 0.1957 0.1963 0.1952 -0.0169 0.0492  -0.0140 25  GLU   A N   
639  N N   B GLU   A 25  ? 0.1581 0.1852 0.1492 -0.0336 0.0383  -0.0251 25  GLU   A N   
640  C CA  A GLU   A 25  ? 0.2132 0.2164 0.1934 -0.0113 0.0530  -0.0151 25  GLU   A CA  
641  C CA  B GLU   A 25  ? 0.1800 0.2067 0.1662 -0.0378 0.0569  -0.0262 25  GLU   A CA  
642  C C   A GLU   A 25  ? 0.2042 0.2193 0.1630 -0.0180 0.0600  -0.0131 25  GLU   A C   
643  C C   B GLU   A 25  ? 0.1756 0.2100 0.1264 -0.0386 0.0612  -0.0245 25  GLU   A C   
644  O O   A GLU   A 25  ? 0.2067 0.2275 0.1912 -0.0093 0.0507  -0.0133 25  GLU   A O   
645  O O   B GLU   A 25  ? 0.1784 0.2116 0.1202 -0.0338 0.0594  -0.0279 25  GLU   A O   
646  C CB  A GLU   A 25  ? 0.2390 0.2409 0.2391 -0.0166 0.0491  -0.0062 25  GLU   A CB  
647  C CB  B GLU   A 25  ? 0.2018 0.2210 0.2001 -0.0394 0.0747  -0.0273 25  GLU   A CB  
648  C CG  A GLU   A 25  ? 0.2681 0.2630 0.3073 -0.0230 0.0339  -0.0088 25  GLU   A CG  
649  C CG  B GLU   A 25  ? 0.2269 0.2412 0.2549 -0.0407 0.0742  -0.0197 25  GLU   A CG  
650  C CD  A GLU   A 25  ? 0.2879 0.2813 0.3637 -0.0308 0.0209  -0.0056 25  GLU   A CD  
651  C CD  B GLU   A 25  ? 0.2482 0.2575 0.3087 -0.0467 0.0637  -0.0114 25  GLU   A CD  
652  O OE1 A GLU   A 25  ? 0.2932 0.2893 0.3702 -0.0270 0.0062  -0.0133 25  GLU   A OE1 
653  O OE1 B GLU   A 25  ? 0.2543 0.2598 0.3236 -0.0489 0.0622  -0.0109 25  GLU   A OE1 
654  O OE2 A GLU   A 25  ? 0.2946 0.2892 0.3948 -0.0406 0.0176  -0.0094 25  GLU   A OE2 
655  O OE2 B GLU   A 25  ? 0.2623 0.2649 0.3368 -0.0456 0.0629  -0.0043 25  GLU   A OE2 
668  N N   A GLU   A 26  ? 0.1992 0.2203 0.1688 -0.0352 0.0547  -0.0109 26  GLU   A N   
669  N N   B GLU   A 26  ? 0.1725 0.2104 0.1310 -0.0409 0.0546  -0.0300 26  GLU   A N   
670  C CA  A GLU   A 26  ? 0.2009 0.2271 0.1571 -0.0496 0.0562  -0.0061 26  GLU   A CA  
671  C CA  B GLU   A 26  ? 0.1754 0.2145 0.1142 -0.0437 0.0494  -0.0283 26  GLU   A CA  
672  C C   A GLU   A 26  ? 0.1952 0.2222 0.1533 -0.0469 0.0473  -0.0013 26  GLU   A C   
673  C C   B GLU   A 26  ? 0.1723 0.2102 0.0917 -0.0453 0.0399  -0.0325 26  GLU   A C   
674  O O   A GLU   A 26  ? 0.2030 0.2229 0.1619 -0.0436 0.0508  0.0028  26  GLU   A O   
675  O O   B GLU   A 26  ? 0.1755 0.2082 0.1007 -0.0411 0.0403  -0.0240 26  GLU   A O   
676  C CB  A GLU   A 26  ? 0.2164 0.2332 0.1724 -0.0614 0.0505  0.0011  26  GLU   A CB  
677  C CB  B GLU   A 26  ? 0.1912 0.2273 0.1369 -0.0474 0.0446  -0.0342 26  GLU   A CB  
678  C CG  A GLU   A 26  ? 0.2399 0.2518 0.2342 -0.0631 0.0481  -0.0132 26  GLU   A CG  
679  C CG  B GLU   A 26  ? 0.2049 0.2374 0.1643 -0.0562 0.0499  -0.0308 26  GLU   A CG  
680  C CD  A GLU   A 26  ? 0.2577 0.2634 0.2702 -0.0746 0.0556  -0.0203 26  GLU   A CD  
681  C CD  B GLU   A 26  ? 0.2152 0.2460 0.1616 -0.0690 0.0607  -0.0260 26  GLU   A CD  
682  O OE1 A GLU   A 26  ? 0.2577 0.2838 0.2627 -0.0618 0.0795  -0.0467 26  GLU   A OE1 
683  O OE1 B GLU   A 26  ? 0.2204 0.2698 0.1466 -0.0633 0.0788  -0.0259 26  GLU   A OE1 
684  O OE2 A GLU   A 26  ? 0.2805 0.2666 0.2795 -0.0830 0.0461  -0.0090 26  GLU   A OE2 
685  O OE2 B GLU   A 26  ? 0.2189 0.2373 0.1203 -0.0737 0.0719  -0.0254 26  GLU   A OE2 
698  N N   A ALA   A 27  ? 0.1818 0.2105 0.1462 -0.0571 0.0495  0.0011  27  ALA   A N   
699  N N   B ALA   A 27  ? 0.1698 0.2129 0.0978 -0.0479 0.0270  -0.0355 27  ALA   A N   
700  C CA  A ALA   A 27  ? 0.1920 0.2253 0.1444 -0.0566 0.0481  0.0032  27  ALA   A CA  
701  C CA  B ALA   A 27  ? 0.1820 0.2272 0.1173 -0.0439 0.0078  -0.0316 27  ALA   A CA  
702  C C   A ALA   A 27  ? 0.2167 0.2453 0.1462 -0.0625 0.0514  -0.0164 27  ALA   A C   
703  C C   B ALA   A 27  ? 0.2049 0.2454 0.1356 -0.0413 0.0036  -0.0377 27  ALA   A C   
704  O O   A ALA   A 27  ? 0.2217 0.2421 0.1462 -0.0659 0.0393  -0.0180 27  ALA   A O   
705  O O   B ALA   A 27  ? 0.2067 0.2460 0.1270 -0.0412 -0.0110 -0.0373 27  ALA   A O   
706  C CB  A ALA   A 27  ? 0.1806 0.2213 0.1365 -0.0556 0.0433  0.0061  27  ALA   A CB  
707  C CB  B ALA   A 27  ? 0.1757 0.2250 0.1180 -0.0452 -0.0006 -0.0283 27  ALA   A CB  
718  N N   A LYS   A 28  ? 0.2453 0.2686 0.1540 -0.0621 0.0382  -0.0495 28  LYS   A N   
719  N N   B LYS   A 28  ? 0.2312 0.2632 0.1586 -0.0387 0.0032  -0.0546 28  LYS   A N   
720  C CA  A LYS   A 28  ? 0.2795 0.2983 0.1771 -0.0605 0.0332  -0.0745 28  LYS   A CA  
721  C CA  B LYS   A 28  ? 0.2612 0.2880 0.1901 -0.0353 0.0080  -0.0632 28  LYS   A CA  
722  C C   A LYS   A 28  ? 0.2966 0.3264 0.1529 -0.0656 0.0462  -0.0668 28  LYS   A C   
723  C C   B LYS   A 28  ? 0.2865 0.3152 0.1917 -0.0414 0.0163  -0.0546 28  LYS   A C   
724  O O   A LYS   A 28  ? 0.3022 0.3363 0.1971 -0.0639 0.0255  -0.0622 28  LYS   A O   
725  O O   B LYS   A 28  ? 0.2941 0.3223 0.2099 -0.0381 0.0059  -0.0534 28  LYS   A O   
726  C CB  A LYS   A 28  ? 0.2985 0.3086 0.2303 -0.0459 0.0203  -0.0928 28  LYS   A CB  
727  C CB  B LYS   A 28  ? 0.2685 0.2905 0.2204 -0.0235 0.0051  -0.0731 28  LYS   A CB  
728  C CG  A LYS   A 28  ? 0.3156 0.3158 0.2861 -0.0351 0.0151  -0.0981 28  LYS   A CG  
729  C CG  B LYS   A 28  ? 0.2780 0.2950 0.2594 -0.0130 0.0013  -0.0758 28  LYS   A CG  
730  C CD  A LYS   A 28  ? 0.3320 0.3301 0.3569 -0.0257 0.0089  -0.0936 28  LYS   A CD  
731  C CD  B LYS   A 28  ? 0.2908 0.3064 0.3168 -0.0024 -0.0029 -0.0709 28  LYS   A CD  
732  C CE  A LYS   A 28  ? 0.3466 0.3412 0.4027 -0.0195 0.0038  -0.0941 28  LYS   A CE  
733  C CE  B LYS   A 28  ? 0.3046 0.3161 0.3615 0.0021  -0.0054 -0.0693 28  LYS   A CE  
734  N NZ  A LYS   A 28  ? 0.3544 0.3474 0.4364 -0.0159 0.0031  -0.0963 28  LYS   A NZ  
735  N NZ  B LYS   A 28  ? 0.3114 0.3213 0.3866 0.0041  -0.0067 -0.0692 28  LYS   A NZ  
762  N N   A LYS   A 29  ? 0.3064 0.3453 0.1372 -0.0756 0.0755  -0.0467 29  LYS   A N   
763  N N   B LYS   A 29  ? 0.3026 0.3350 0.1971 -0.0534 0.0391  -0.0388 29  LYS   A N   
764  C CA  A LYS   A 29  ? 0.3249 0.3699 0.1660 -0.0824 0.0905  -0.0313 29  LYS   A CA  
765  C CA  B LYS   A 29  ? 0.3213 0.3562 0.2205 -0.0651 0.0563  -0.0262 29  LYS   A CA  
766  C C   A LYS   A 29  ? 0.3289 0.3671 0.1547 -0.0885 0.0785  -0.0249 29  LYS   A C   
767  C C   B LYS   A 29  ? 0.3262 0.3585 0.1867 -0.0806 0.0633  -0.0214 29  LYS   A C   
768  O O   A LYS   A 29  ? 0.3384 0.3794 0.1580 -0.0808 0.0776  -0.0248 29  LYS   A O   
769  O O   B LYS   A 29  ? 0.3327 0.3644 0.1905 -0.0775 0.0669  -0.0180 29  LYS   A O   
770  C CB  A LYS   A 29  ? 0.3396 0.3956 0.2332 -0.0762 0.1090  -0.0260 29  LYS   A CB  
771  C CB  B LYS   A 29  ? 0.3349 0.3736 0.2833 -0.0578 0.0619  -0.0210 29  LYS   A CB  
772  C CG  A LYS   A 29  ? 0.3568 0.4177 0.3076 -0.0707 0.1152  -0.0224 29  LYS   A CG  
773  C CG  B LYS   A 29  ? 0.3498 0.3896 0.3433 -0.0506 0.0638  -0.0174 29  LYS   A CG  
774  C CD  A LYS   A 29  ? 0.3726 0.4346 0.3829 -0.0650 0.1139  -0.0223 29  LYS   A CD  
775  C CD  B LYS   A 29  ? 0.3625 0.4024 0.3979 -0.0443 0.0641  -0.0153 29  LYS   A CD  
776  C CE  A LYS   A 29  ? 0.3843 0.4478 0.4308 -0.0605 0.1162  -0.0222 29  LYS   A CE  
777  C CE  B LYS   A 29  ? 0.3712 0.4115 0.4338 -0.0390 0.0659  -0.0145 29  LYS   A CE  
778  N NZ  A LYS   A 29  ? 0.3895 0.4547 0.4572 -0.0578 0.1163  -0.0222 29  LYS   A NZ  
779  N NZ  B LYS   A 29  ? 0.3758 0.4169 0.4547 -0.0361 0.0658  -0.0132 29  LYS   A NZ  
806  N N   . VAL   A 30  ? 0.3211 0.3529 0.1582 -0.0943 0.0754  -0.0161 30  VAL   A N   
807  C CA  . VAL   A 30  ? 0.3200 0.3373 0.1501 -0.1090 0.0530  0.0029  30  VAL   A CA  
808  C C   . VAL   A 30  ? 0.3239 0.3263 0.1252 -0.1097 0.0371  0.0173  30  VAL   A C   
809  O O   . VAL   A 30  ? 0.3317 0.3327 0.1327 -0.1049 0.0288  0.0246  30  VAL   A O   
810  C CB  . VAL   A 30  ? 0.3186 0.3363 0.2034 -0.1191 0.0378  0.0042  30  VAL   A CB  
811  C CG1 . VAL   A 30  ? 0.3279 0.3365 0.2307 -0.1204 0.0257  0.0161  30  VAL   A CG1 
812  C CG2 . VAL   A 30  ? 0.3148 0.3374 0.2288 -0.1300 0.0370  -0.0027 30  VAL   A CG2 
823  N N   . LYS   A 31  ? 0.3087 0.3035 0.1073 -0.1097 0.0165  0.0077  31  LYS   A N   
824  C CA  . LYS   A 31  ? 0.3225 0.3019 0.1191 -0.0949 -0.0098 0.0080  31  LYS   A CA  
825  C C   . LYS   A 31  ? 0.2919 0.2719 0.0984 -0.0694 -0.0132 0.0407  31  LYS   A C   
826  O O   . LYS   A 31  ? 0.3056 0.2904 0.1106 -0.0602 -0.0258 0.0584  31  LYS   A O   
827  C CB  . LYS   A 31  ? 0.3781 0.3367 0.2202 -0.0909 -0.0384 -0.0031 31  LYS   A CB  
828  C CG  . LYS   A 31  ? 0.4348 0.3787 0.3764 -0.0814 -0.0572 -0.0046 31  LYS   A CG  
829  C CD  . LYS   A 31  ? 0.4738 0.4159 0.4952 -0.0704 -0.0718 -0.0092 31  LYS   A CD  
830  C CE  . LYS   A 31  ? 0.5019 0.4426 0.5662 -0.0645 -0.0825 -0.0142 31  LYS   A CE  
831  N NZ  . LYS   A 31  ? 0.5248 0.4489 0.6074 -0.0618 -0.0885 -0.0201 31  LYS   A NZ  
845  N N   . PRO   A 32  ? 0.2566 0.2436 0.0831 -0.0623 -0.0048 0.0264  32  PRO   A N   
846  C CA  . PRO   A 32  ? 0.2541 0.2306 0.1117 -0.0598 -0.0128 0.0396  32  PRO   A CA  
847  C C   . PRO   A 32  ? 0.2545 0.2256 0.1079 -0.0553 -0.0302 0.0464  32  PRO   A C   
848  O O   . PRO   A 32  ? 0.2488 0.2179 0.1375 -0.0554 -0.0421 0.0523  32  PRO   A O   
849  C CB  . PRO   A 32  ? 0.2418 0.2351 0.1223 -0.0593 -0.0091 0.0275  32  PRO   A CB  
850  C CG  . PRO   A 32  ? 0.2317 0.2366 0.0755 -0.0573 -0.0129 0.0172  32  PRO   A CG  
851  C CD  . PRO   A 32  ? 0.2300 0.2337 0.0756 -0.0544 -0.0039 0.0237  32  PRO   A CD  
859  N N   . THR   A 33  ? 0.2639 0.2255 0.1048 -0.0511 -0.0218 0.0477  33  THR   A N   
860  C CA  . THR   A 33  ? 0.2539 0.2260 0.1261 -0.0426 -0.0304 0.0510  33  THR   A CA  
861  C C   . THR   A 33  ? 0.2185 0.2026 0.1180 -0.0431 -0.0284 0.0372  33  THR   A C   
862  O O   . THR   A 33  ? 0.2129 0.2054 0.1307 -0.0426 -0.0432 0.0441  33  THR   A O   
863  C CB  . THR   A 33  ? 0.2754 0.2525 0.1400 -0.0340 -0.0422 0.0711  33  THR   A CB  
864  O OG1 . THR   A 33  ? 0.2979 0.2730 0.1700 -0.0185 -0.0346 0.0867  33  THR   A OG1 
865  C CG2 . THR   A 33  ? 0.2796 0.2646 0.1749 -0.0299 -0.0560 0.0627  33  THR   A CG2 
873  N N   . VAL   A 34  ? 0.1943 0.1882 0.0977 -0.0411 -0.0261 0.0322  34  VAL   A N   
874  C CA  . VAL   A 34  ? 0.1743 0.1716 0.0948 -0.0326 -0.0126 0.0309  34  VAL   A CA  
875  C C   . VAL   A 34  ? 0.1645 0.1655 0.0971 -0.0255 -0.0031 0.0248  34  VAL   A C   
876  O O   . VAL   A 34  ? 0.1651 0.1715 0.1167 -0.0344 -0.0005 0.0293  34  VAL   A O   
877  C CB  . VAL   A 34  ? 0.1758 0.1722 0.1180 -0.0324 -0.0105 0.0198  34  VAL   A CB  
878  C CG1 . VAL   A 34  ? 0.1862 0.1780 0.1160 -0.0345 -0.0004 0.0175  34  VAL   A CG1 
879  C CG2 . VAL   A 34  ? 0.1904 0.1821 0.1551 -0.0234 -0.0152 0.0261  34  VAL   A CG2 
889  N N   . VAL   A 35  ? 0.1504 0.1549 0.0923 -0.0295 -0.0073 0.0204  35  VAL   A N   
890  C CA  . VAL   A 35  ? 0.1394 0.1470 0.0854 -0.0285 -0.0059 0.0151  35  VAL   A CA  
891  C C   . VAL   A 35  ? 0.1285 0.1364 0.0955 -0.0185 -0.0030 0.0146  35  VAL   A C   
892  O O   . VAL   A 35  ? 0.1254 0.1444 0.1091 -0.0263 0.0099  0.0090  35  VAL   A O   
893  C CB  . VAL   A 35  ? 0.1489 0.1553 0.1034 -0.0210 0.0136  0.0045  35  VAL   A CB  
894  C CG1 . VAL   A 35  ? 0.1587 0.1582 0.1195 -0.0176 0.0086  0.0028  35  VAL   A CG1 
895  C CG2 . VAL   A 35  ? 0.1529 0.1600 0.1102 -0.0121 0.0178  -0.0055 35  VAL   A CG2 
905  N N   . VAL   A 36  ? 0.1149 0.1329 0.0874 -0.0180 0.0037  0.0167  36  VAL   A N   
906  C CA  . VAL   A 36  ? 0.1123 0.1254 0.0926 -0.0141 0.0072  0.0088  36  VAL   A CA  
907  C C   . VAL   A 36  ? 0.1108 0.1227 0.0953 -0.0134 0.0093  0.0049  36  VAL   A C   
908  O O   . VAL   A 36  ? 0.1208 0.1249 0.1122 -0.0096 0.0204  0.0069  36  VAL   A O   
909  C CB  . VAL   A 36  ? 0.1148 0.1218 0.0981 -0.0119 0.0029  0.0098  36  VAL   A CB  
910  C CG1 . VAL   A 36  ? 0.1209 0.1193 0.1085 -0.0157 0.0080  0.0076  36  VAL   A CG1 
911  C CG2 . VAL   A 36  ? 0.1237 0.1251 0.1186 -0.0097 0.0088  0.0235  36  VAL   A CG2 
921  N N   . ASN   A 37  ? 0.1102 0.1207 0.0873 -0.0018 0.0077  0.0126  37  ASN   A N   
922  C CA  . ASN   A 37  ? 0.1151 0.1164 0.0888 0.0016  0.0066  0.0162  37  ASN   A CA  
923  C C   . ASN   A 37  ? 0.1141 0.1121 0.0953 -0.0049 0.0106  0.0207  37  ASN   A C   
924  O O   . ASN   A 37  ? 0.1247 0.1227 0.0950 0.0035  0.0093  0.0081  37  ASN   A O   
925  C CB  . ASN   A 37  ? 0.1138 0.1185 0.0938 -0.0041 0.0052  0.0110  37  ASN   A CB  
926  C CG  . ASN   A 37  ? 0.1137 0.1116 0.1085 -0.0007 0.0077  0.0060  37  ASN   A CG  
927  O OD1 . ASN   A 37  ? 0.1123 0.1181 0.1168 0.0005  0.0066  0.0111  37  ASN   A OD1 
928  N ND2 . ASN   A 37  ? 0.1154 0.1153 0.1188 -0.0036 -0.0018 0.0231  37  ASN   A ND2 
935  N N   A ALA   A 38  ? 0.1114 0.1169 0.0948 -0.0003 0.0075  0.0063  38  ALA   A N   
936  N N   B ALA   A 38  ? 0.1169 0.1143 0.1032 -0.0006 -0.0004 0.0151  38  ALA   A N   
937  C CA  A ALA   A 38  ? 0.1152 0.1198 0.0918 -0.0030 0.0044  0.0025  38  ALA   A CA  
938  C CA  B ALA   A 38  ? 0.1251 0.1194 0.1115 -0.0020 -0.0086 0.0190  38  ALA   A CA  
939  C C   A ALA   A 38  ? 0.1052 0.1243 0.0889 0.0016  -0.0051 -0.0013 38  ALA   A C   
940  C C   B ALA   A 38  ? 0.1218 0.1247 0.1194 -0.0026 -0.0118 0.0108  38  ALA   A C   
941  O O   A ALA   A 38  ? 0.0991 0.1169 0.0999 0.0039  -0.0094 -0.0065 38  ALA   A O   
942  O O   B ALA   A 38  ? 0.1242 0.1141 0.1342 -0.0128 -0.0183 0.0112  38  ALA   A O   
943  C CB  A ALA   A 38  ? 0.1157 0.1331 0.0984 -0.0151 0.0037  -0.0018 38  ALA   A CB  
944  C CB  B ALA   A 38  ? 0.1294 0.1296 0.1202 -0.0049 -0.0185 0.0078  38  ALA   A CB  
955  N N   A ALA   A 39  ? 0.1078 0.1154 0.0862 -0.0018 -0.0031 0.0043  39  ALA   A N   
956  N N   B ALA   A 39  ? 0.1237 0.1336 0.1311 -0.0018 -0.0062 0.0197  39  ALA   A N   
957  C CA  A ALA   A 39  ? 0.1151 0.1145 0.0874 0.0044  0.0022  0.0062  39  ALA   A CA  
958  C CA  B ALA   A 39  ? 0.1254 0.1385 0.1322 -0.0038 -0.0036 0.0183  39  ALA   A CA  
959  C C   A ALA   A 39  ? 0.1094 0.1160 0.0983 -0.0021 0.0063  0.0035  39  ALA   A C   
960  C C   B ALA   A 39  ? 0.1238 0.1318 0.1300 -0.0052 -0.0049 0.0140  39  ALA   A C   
961  O O   A ALA   A 39  ? 0.1294 0.1139 0.0962 -0.0096 0.0129  0.0008  39  ALA   A O   
962  O O   B ALA   A 39  ? 0.1333 0.1286 0.1310 -0.0058 -0.0024 0.0219  39  ALA   A O   
963  C CB  A ALA   A 39  ? 0.1204 0.1156 0.0917 0.0026  -0.0066 -0.0039 39  ALA   A CB  
964  C CB  B ALA   A 39  ? 0.1380 0.1490 0.1480 -0.0092 0.0002  0.0082  39  ALA   A CB  
975  N N   A ASN   A 40  ? 0.1100 0.1229 0.1001 -0.0062 0.0195  0.0041  40  ASN   A N   
976  N N   B ASN   A 40  ? 0.1268 0.1321 0.1321 -0.0077 0.0029  0.0023  40  ASN   A N   
977  C CA  A ASN   A 40  ? 0.1186 0.1238 0.0990 0.0027  0.0117  0.0081  40  ASN   A CA  
978  C CA  B ASN   A 40  ? 0.1329 0.1279 0.1281 -0.0024 -0.0036 -0.0005 40  ASN   A CA  
979  C C   A ASN   A 40  ? 0.1234 0.1176 0.0886 -0.0034 0.0258  0.0098  40  ASN   A C   
980  C C   B ASN   A 40  ? 0.1315 0.1219 0.1093 -0.0033 0.0142  0.0012  40  ASN   A C   
981  O O   A ASN   A 40  ? 0.1191 0.1157 0.1030 -0.0076 0.0238  0.0209  40  ASN   A O   
982  O O   B ASN   A 40  ? 0.1279 0.1216 0.1151 -0.0032 0.0153  0.0066  40  ASN   A O   
983  C CB  A ASN   A 40  ? 0.1299 0.1327 0.1201 0.0072  0.0032  0.0063  40  ASN   A CB  
984  C CB  B ASN   A 40  ? 0.1431 0.1289 0.1498 0.0020  -0.0210 -0.0041 40  ASN   A CB  
985  C CG  A ASN   A 40  ? 0.1330 0.1256 0.1392 -0.0020 0.0056  0.0129  40  ASN   A CG  
986  C CG  B ASN   A 40  ? 0.1510 0.1214 0.1752 0.0011  -0.0367 -0.0078 40  ASN   A CG  
987  O OD1 A ASN   A 40  ? 0.1371 0.1243 0.1352 -0.0048 0.0351  0.0152  40  ASN   A OD1 
988  O OD1 B ASN   A 40  ? 0.1644 0.1247 0.2007 0.0061  -0.0486 -0.0078 40  ASN   A OD1 
989  N ND2 A ASN   A 40  ? 0.1331 0.1369 0.1568 -0.0042 0.0002  0.0007  40  ASN   A ND2 
990  N ND2 B ASN   A 40  ? 0.1441 0.1163 0.1765 -0.0089 -0.0303 -0.0176 40  ASN   A ND2 
1003 N N   . VAL   A 41  ? 0.1339 0.1226 0.1085 -0.0056 0.0233  0.0076  41  VAL   A N   
1004 C CA  . VAL   A 41  ? 0.1382 0.1233 0.1229 -0.0036 0.0335  0.0047  41  VAL   A CA  
1005 C C   . VAL   A 41  ? 0.1329 0.1258 0.1295 0.0024  0.0356  0.0088  41  VAL   A C   
1006 O O   . VAL   A 41  ? 0.1410 0.1220 0.1459 -0.0002 0.0335  0.0037  41  VAL   A O   
1007 C CB  . VAL   A 41  ? 0.1577 0.1362 0.1336 -0.0096 0.0413  -0.0036 41  VAL   A CB  
1008 C CG1 . VAL   A 41  ? 0.1727 0.1420 0.1346 -0.0078 0.0458  -0.0032 41  VAL   A CG1 
1009 C CG2 . VAL   A 41  ? 0.1859 0.1536 0.1203 -0.0182 0.0480  0.0039  41  VAL   A CG2 
1020 N N   A TYR   A 42  ? 0.1221 0.1193 0.1366 -0.0019 0.0237  0.0132  42  TYR   A N   
1021 N N   B TYR   A 42  ? 0.1247 0.1230 0.1291 -0.0031 0.0310  0.0154  42  TYR   A N   
1022 C CA  A TYR   A 42  ? 0.1198 0.1102 0.1500 -0.0015 0.0225  0.0103  42  TYR   A CA  
1023 C CA  B TYR   A 42  ? 0.1206 0.1179 0.1337 -0.0058 0.0338  0.0148  42  TYR   A CA  
1024 C C   A TYR   A 42  ? 0.1149 0.1142 0.1452 -0.0038 0.0180  0.0222  42  TYR   A C   
1025 C C   B TYR   A 42  ? 0.1195 0.1193 0.1295 -0.0072 0.0245  0.0204  42  TYR   A C   
1026 O O   A TYR   A 42  ? 0.1159 0.1164 0.1689 -0.0157 0.0160  0.0039  42  TYR   A O   
1027 O O   B TYR   A 42  ? 0.1155 0.1222 0.1390 -0.0138 0.0221  0.0085  42  TYR   A O   
1028 C CB  A TYR   A 42  ? 0.1428 0.1247 0.1507 -0.0024 0.0231  0.0280  42  TYR   A CB  
1029 C CB  B TYR   A 42  ? 0.1283 0.1258 0.1282 -0.0074 0.0493  0.0256  42  TYR   A CB  
1030 C CG  A TYR   A 42  ? 0.1538 0.1413 0.1522 0.0113  0.0059  0.0345  42  TYR   A CG  
1031 C CG  B TYR   A 42  ? 0.1332 0.1339 0.1328 -0.0033 0.0376  0.0221  42  TYR   A CG  
1032 C CD1 A TYR   A 42  ? 0.1606 0.1513 0.1435 0.0052  0.0129  0.0379  42  TYR   A CD1 
1033 C CD1 B TYR   A 42  ? 0.1397 0.1439 0.1365 -0.0077 0.0286  0.0127  42  TYR   A CD1 
1034 C CD2 A TYR   A 42  ? 0.1605 0.1662 0.1749 0.0127  0.0113  0.0263  42  TYR   A CD2 
1035 C CD2 B TYR   A 42  ? 0.1341 0.1467 0.1402 -0.0027 0.0354  0.0127  42  TYR   A CD2 
1036 C CE1 A TYR   A 42  ? 0.1639 0.1681 0.1351 0.0010  0.0205  0.0310  42  TYR   A CE1 
1037 C CE1 B TYR   A 42  ? 0.1432 0.1545 0.1420 -0.0079 0.0263  0.0041  42  TYR   A CE1 
1038 C CE2 A TYR   A 42  ? 0.1719 0.1785 0.1684 0.0164  0.0156  0.0261  42  TYR   A CE2 
1039 C CE2 B TYR   A 42  ? 0.1366 0.1534 0.1411 -0.0092 0.0297  0.0134  42  TYR   A CE2 
1040 C CZ  A TYR   A 42  ? 0.1717 0.1827 0.1506 0.0050  0.0245  0.0246  42  TYR   A CZ  
1041 C CZ  B TYR   A 42  ? 0.1415 0.1536 0.1396 -0.0090 0.0298  0.0118  42  TYR   A CZ  
1042 O OH  A TYR   A 42  ? 0.1721 0.2046 0.1691 -0.0015 0.0234  0.0053  42  TYR   A OH  
1043 O OH  B TYR   A 42  ? 0.1505 0.1604 0.1662 -0.0046 0.0131  0.0047  42  TYR   A OH  
1062 N N   . LEU   A 43  ? 0.1232 0.1166 0.1274 -0.0055 0.0181  0.0090  43  LEU   A N   
1063 C CA  . LEU   A 43  ? 0.1118 0.1208 0.1166 -0.0049 0.0117  0.0087  43  LEU   A CA  
1064 C C   . LEU   A 43  ? 0.1196 0.1178 0.1207 -0.0043 0.0092  0.0068  43  LEU   A C   
1065 O O   . LEU   A 43  ? 0.1387 0.1226 0.1434 0.0024  -0.0062 -0.0006 43  LEU   A O   
1066 C CB  . LEU   A 43  ? 0.1211 0.1200 0.1335 -0.0070 0.0157  0.0108  43  LEU   A CB  
1067 C CG  . LEU   A 43  ? 0.1256 0.1168 0.1372 0.0014  0.0099  0.0069  43  LEU   A CG  
1068 C CD1 . LEU   A 43  ? 0.1355 0.1251 0.1641 -0.0018 0.0001  0.0157  43  LEU   A CD1 
1069 C CD2 . LEU   A 43  ? 0.1473 0.1174 0.1401 -0.0084 0.0092  0.0167  43  LEU   A CD2 
1082 N N   . LYS   A 44  ? 0.1316 0.1201 0.1227 -0.0014 0.0131  0.0137  44  LYS   A N   
1083 C CA  . LYS   A 44  ? 0.1344 0.1211 0.1200 -0.0024 0.0109  0.0159  44  LYS   A CA  
1084 C C   . LYS   A 44  ? 0.1192 0.1204 0.1137 0.0014  -0.0006 0.0095  44  LYS   A C   
1085 O O   . LYS   A 44  ? 0.1264 0.1289 0.1338 0.0022  0.0023  0.0017  44  LYS   A O   
1086 C CB  . LYS   A 44  ? 0.1635 0.1308 0.1587 0.0028  0.0212  0.0241  44  LYS   A CB  
1087 C CG  . LYS   A 44  ? 0.1945 0.1638 0.2249 -0.0058 0.0443  0.0286  44  LYS   A CG  
1088 C CD  . LYS   A 44  ? 0.2384 0.2266 0.3389 -0.0133 0.0408  0.0184  44  LYS   A CD  
1089 C CE  . LYS   A 44  ? 0.2485 0.2513 0.4060 -0.0179 0.0360  0.0214  44  LYS   A CE  
1090 N NZ  . LYS   A 44  ? 0.2579 0.2687 0.4360 -0.0243 0.0344  0.0255  44  LYS   A NZ  
1104 N N   . HIS   A 45  ? 0.1119 0.1136 0.1181 -0.0009 0.0052  0.0114  45  HIS   A N   
1105 C CA  . HIS   A 45  ? 0.1183 0.1183 0.1234 -0.0004 -0.0049 0.0069  45  HIS   A CA  
1106 C C   . HIS   A 45  ? 0.1256 0.1292 0.1314 0.0046  0.0080  0.0125  45  HIS   A C   
1107 O O   . HIS   A 45  ? 0.1480 0.1396 0.1741 0.0185  0.0026  -0.0098 45  HIS   A O   
1108 C CB  . HIS   A 45  ? 0.1184 0.1194 0.1208 -0.0039 0.0034  0.0049  45  HIS   A CB  
1109 C CG  . HIS   A 45  ? 0.1187 0.1180 0.1030 -0.0091 0.0041  0.0076  45  HIS   A CG  
1110 N ND1 . HIS   A 45  ? 0.1108 0.1199 0.1206 -0.0064 0.0000  0.0029  45  HIS   A ND1 
1111 C CD2 . HIS   A 45  ? 0.1179 0.1223 0.1163 -0.0154 0.0005  0.0165  45  HIS   A CD2 
1112 C CE1 . HIS   A 45  ? 0.1057 0.1227 0.1083 -0.0078 -0.0031 0.0128  45  HIS   A CE1 
1113 N NE2 . HIS   A 45  ? 0.1084 0.1311 0.1158 -0.0059 0.0031  0.0198  45  HIS   A NE2 
1121 N N   A GLY   A 46  ? 0.1442 0.1385 0.1497 0.0097  -0.0059 0.0177  46  GLY   A N   
1122 N N   B GLY   A 46  ? 0.1267 0.1367 0.1477 0.0216  -0.0061 0.0246  46  GLY   A N   
1123 C CA  A GLY   A 46  ? 0.1469 0.1477 0.1706 0.0088  -0.0045 0.0195  46  GLY   A CA  
1124 C CA  B GLY   A 46  ? 0.1283 0.1372 0.1668 0.0281  -0.0109 0.0336  46  GLY   A CA  
1125 C C   A GLY   A 46  ? 0.1458 0.1407 0.1669 0.0110  -0.0071 0.0213  46  GLY   A C   
1126 C C   B GLY   A 46  ? 0.1298 0.1248 0.1587 0.0289  -0.0230 0.0344  46  GLY   A C   
1127 O O   A GLY   A 46  ? 0.1506 0.1449 0.1934 0.0049  -0.0143 0.0131  46  GLY   A O   
1128 O O   B GLY   A 46  ? 0.1328 0.1159 0.1839 0.0257  -0.0202 0.0502  46  GLY   A O   
1135 N N   A GLY   A 47  ? 0.1560 0.1382 0.1500 0.0112  -0.0074 0.0085  47  GLY   A N   
1136 N N   B GLY   A 47  ? 0.1224 0.1247 0.1404 0.0247  -0.0349 0.0157  47  GLY   A N   
1137 C CA  A GLY   A 47  ? 0.1548 0.1405 0.1356 0.0103  -0.0282 -0.0046 47  GLY   A CA  
1138 C CA  B GLY   A 47  ? 0.1328 0.1333 0.1510 0.0170  -0.0473 0.0113  47  GLY   A CA  
1139 C C   A GLY   A 47  ? 0.1375 0.1284 0.1400 0.0067  -0.0301 -0.0058 47  GLY   A C   
1140 C C   B GLY   A 47  ? 0.1333 0.1328 0.1496 0.0145  -0.0304 -0.0087 47  GLY   A C   
1141 O O   A GLY   A 47  ? 0.1298 0.1217 0.1503 0.0083  -0.0289 0.0112  47  GLY   A O   
1142 O O   B GLY   A 47  ? 0.1302 0.1322 0.1605 0.0187  -0.0270 0.0014  47  GLY   A O   
1149 N N   A GLY   A 48  ? 0.1327 0.1371 0.1430 0.0083  -0.0411 -0.0017 48  GLY   A N   
1150 N N   B GLY   A 48  ? 0.1331 0.1386 0.1534 0.0058  -0.0290 -0.0142 48  GLY   A N   
1151 C CA  A GLY   A 48  ? 0.1263 0.1388 0.1621 0.0053  -0.0366 -0.0013 48  GLY   A CA  
1152 C CA  B GLY   A 48  ? 0.1267 0.1422 0.1518 0.0031  -0.0267 -0.0145 48  GLY   A CA  
1153 C C   A GLY   A 48  ? 0.1232 0.1350 0.1431 0.0041  -0.0149 0.0043  48  GLY   A C   
1154 C C   B GLY   A 48  ? 0.1237 0.1457 0.1292 0.0034  -0.0038 -0.0075 48  GLY   A C   
1155 O O   A GLY   A 48  ? 0.1306 0.1358 0.1612 0.0104  -0.0182 -0.0125 48  GLY   A O   
1156 O O   B GLY   A 48  ? 0.1272 0.1517 0.1388 0.0093  -0.0101 -0.0166 48  GLY   A O   
1163 N N   A VAL   A 49  ? 0.1107 0.1260 0.1500 -0.0029 -0.0157 0.0078  49  VAL   A N   
1164 N N   B VAL   A 49  ? 0.1102 0.1361 0.1115 -0.0060 -0.0025 -0.0158 49  VAL   A N   
1165 C CA  A VAL   A 49  ? 0.1221 0.1240 0.1483 -0.0070 -0.0029 0.0037  49  VAL   A CA  
1166 C CA  B VAL   A 49  ? 0.1166 0.1301 0.0995 -0.0059 0.0113  -0.0110 49  VAL   A CA  
1167 C C   A VAL   A 49  ? 0.1218 0.1115 0.1282 -0.0022 0.0022  0.0103  49  VAL   A C   
1168 C C   B VAL   A 49  ? 0.1170 0.1179 0.0774 -0.0027 0.0169  -0.0106 49  VAL   A C   
1169 O O   A VAL   A 49  ? 0.1222 0.1156 0.1322 -0.0076 0.0020  0.0055  49  VAL   A O   
1170 O O   B VAL   A 49  ? 0.1137 0.1153 0.0833 0.0061  0.0213  -0.0106 49  VAL   A O   
1171 C CB  A VAL   A 49  ? 0.1418 0.1267 0.1563 -0.0125 0.0029  -0.0043 49  VAL   A CB  
1172 C CB  B VAL   A 49  ? 0.1207 0.1311 0.1053 -0.0018 0.0156  -0.0066 49  VAL   A CB  
1173 C CG1 A VAL   A 49  ? 0.1569 0.1290 0.1583 -0.0095 0.0022  -0.0019 49  VAL   A CG1 
1174 C CG1 B VAL   A 49  ? 0.1222 0.1297 0.0898 0.0059  0.0193  0.0022  49  VAL   A CG1 
1175 C CG2 A VAL   A 49  ? 0.1606 0.1381 0.1934 -0.0357 -0.0050 0.0040  49  VAL   A CG2 
1176 C CG2 B VAL   A 49  ? 0.1381 0.1391 0.1374 -0.0179 0.0083  0.0017  49  VAL   A CG2 
1195 N N   A ALA   A 50  ? 0.1140 0.1101 0.1210 -0.0075 -0.0151 0.0170  50  ALA   A N   
1196 N N   B ALA   A 50  ? 0.1189 0.1146 0.0775 -0.0027 0.0101  -0.0114 50  ALA   A N   
1197 C CA  A ALA   A 50  ? 0.1105 0.1118 0.1191 -0.0090 -0.0152 0.0221  50  ALA   A CA  
1198 C CA  B ALA   A 50  ? 0.1215 0.1149 0.0827 0.0003  0.0049  -0.0148 50  ALA   A CA  
1199 C C   A ALA   A 50  ? 0.1006 0.1129 0.1180 -0.0099 -0.0087 0.0079  50  ALA   A C   
1200 C C   B ALA   A 50  ? 0.1214 0.1114 0.0810 0.0082  0.0091  -0.0194 50  ALA   A C   
1201 O O   A ALA   A 50  ? 0.1018 0.1187 0.1395 -0.0120 -0.0116 0.0103  50  ALA   A O   
1202 O O   B ALA   A 50  ? 0.1261 0.1112 0.0901 0.0122  0.0128  -0.0112 50  ALA   A O   
1203 C CB  A ALA   A 50  ? 0.1066 0.1144 0.1146 -0.0065 -0.0086 0.0165  50  ALA   A CB  
1204 C CB  B ALA   A 50  ? 0.1243 0.1150 0.0871 0.0035  0.0181  -0.0242 50  ALA   A CB  
1215 N N   A GLY   A 51  ? 0.1092 0.1111 0.1288 -0.0018 -0.0142 0.0125  51  GLY   A N   
1216 N N   B GLY   A 51  ? 0.1235 0.1149 0.1045 0.0107  -0.0021 -0.0148 51  GLY   A N   
1217 C CA  A GLY   A 51  ? 0.1289 0.1149 0.1310 0.0054  -0.0140 0.0148  51  GLY   A CA  
1218 C CA  B GLY   A 51  ? 0.1332 0.1181 0.1165 0.0106  -0.0078 -0.0107 51  GLY   A CA  
1219 C C   A GLY   A 51  ? 0.1195 0.1258 0.1326 0.0039  -0.0057 -0.0004 51  GLY   A C   
1220 C C   B GLY   A 51  ? 0.1256 0.1279 0.1245 0.0083  -0.0055 -0.0130 51  GLY   A C   
1221 O O   A GLY   A 51  ? 0.1206 0.1306 0.1466 -0.0015 -0.0035 -0.0101 51  GLY   A O   
1222 O O   B GLY   A 51  ? 0.1289 0.1316 0.1366 0.0078  -0.0088 -0.0208 51  GLY   A O   
1229 N N   . ALA   A 52  ? 0.1209 0.1318 0.1212 0.0024  -0.0013 -0.0156 52  ALA   A N   
1230 C CA  . ALA   A 52  ? 0.1172 0.1442 0.1385 -0.0002 0.0035  -0.0197 52  ALA   A CA  
1231 C C   . ALA   A 52  ? 0.1155 0.1421 0.1228 -0.0067 0.0111  -0.0146 52  ALA   A C   
1232 O O   . ALA   A 52  ? 0.1267 0.1437 0.1296 -0.0063 0.0116  -0.0183 52  ALA   A O   
1233 C CB  . ALA   A 52  ? 0.1286 0.1674 0.1721 -0.0074 -0.0015 -0.0198 52  ALA   A CB  
1240 N N   A LEU   A 53  ? 0.1078 0.1367 0.1164 -0.0068 0.0087  -0.0102 53  LEU   A N   
1241 N N   B LEU   A 53  ? 0.1114 0.1375 0.1156 -0.0046 0.0076  -0.0115 53  LEU   A N   
1242 C CA  A LEU   A 53  ? 0.1256 0.1406 0.1035 -0.0063 0.0074  -0.0018 53  LEU   A CA  
1243 C CA  B LEU   A 53  ? 0.1222 0.1386 0.1053 -0.0028 0.0058  -0.0080 53  LEU   A CA  
1244 C C   A LEU   A 53  ? 0.1223 0.1337 0.0927 0.0043  0.0070  -0.0056 53  LEU   A C   
1245 C C   B LEU   A 53  ? 0.1209 0.1339 0.1025 -0.0005 0.0079  -0.0102 53  LEU   A C   
1246 O O   A LEU   A 53  ? 0.1356 0.1440 0.1017 -0.0056 0.0064  -0.0036 53  LEU   A O   
1247 O O   B LEU   A 53  ? 0.1259 0.1407 0.1217 -0.0157 0.0047  -0.0087 53  LEU   A O   
1248 C CB  A LEU   A 53  ? 0.1320 0.1371 0.1104 -0.0113 0.0009  0.0017  53  LEU   A CB  
1249 C CB  B LEU   A 53  ? 0.1252 0.1341 0.0984 -0.0011 -0.0007 -0.0116 53  LEU   A CB  
1250 C CG  A LEU   A 53  ? 0.1447 0.1399 0.1334 -0.0153 0.0061  0.0120  53  LEU   A CG  
1251 C CG  B LEU   A 53  ? 0.1312 0.1338 0.0991 -0.0026 -0.0040 -0.0138 53  LEU   A CG  
1252 C CD1 A LEU   A 53  ? 0.1541 0.1496 0.1358 -0.0078 0.0047  0.0153  53  LEU   A CD1 
1253 C CD1 B LEU   A 53  ? 0.1403 0.1422 0.1014 0.0003  0.0015  -0.0104 53  LEU   A CD1 
1254 C CD2 A LEU   A 53  ? 0.1426 0.1460 0.1426 -0.0205 0.0009  0.0159  53  LEU   A CD2 
1255 C CD2 B LEU   A 53  ? 0.1303 0.1333 0.0938 -0.0025 -0.0028 -0.0251 53  LEU   A CD2 
1278 N N   . ASN   A 54  ? 0.1187 0.1282 0.0995 -0.0017 0.0034  -0.0021 54  ASN   A N   
1279 C CA  . ASN   A 54  ? 0.1099 0.1258 0.1177 -0.0055 -0.0041 -0.0009 54  ASN   A CA  
1280 C C   . ASN   A 54  ? 0.1164 0.1264 0.1185 -0.0074 -0.0001 -0.0108 54  ASN   A C   
1281 O O   . ASN   A 54  ? 0.1174 0.1342 0.1274 -0.0068 0.0009  -0.0156 54  ASN   A O   
1282 C CB  . ASN   A 54  ? 0.1032 0.1262 0.1251 -0.0024 -0.0051 0.0002  54  ASN   A CB  
1283 C CG  . ASN   A 54  ? 0.1105 0.1310 0.1164 0.0005  -0.0066 -0.0031 54  ASN   A CG  
1284 O OD1 . ASN   A 54  ? 0.1134 0.1303 0.1209 -0.0061 -0.0035 -0.0033 54  ASN   A OD1 
1285 N ND2 . ASN   A 54  ? 0.1149 0.1393 0.1440 -0.0101 -0.0098 0.0091  54  ASN   A ND2 
1293 N N   . LYS   A 55  ? 0.1188 0.1276 0.1307 -0.0079 -0.0018 -0.0175 55  LYS   A N   
1294 C CA  . LYS   A 55  ? 0.1254 0.1357 0.1370 0.0038  -0.0057 -0.0207 55  LYS   A CA  
1295 C C   . LYS   A 55  ? 0.1206 0.1437 0.1358 -0.0040 0.0013  -0.0289 55  LYS   A C   
1296 O O   . LYS   A 55  ? 0.1313 0.1570 0.1432 0.0012  -0.0012 -0.0294 55  LYS   A O   
1297 C CB  . LYS   A 55  ? 0.1396 0.1471 0.1617 0.0150  -0.0080 -0.0225 55  LYS   A CB  
1298 C CG  . LYS   A 55  ? 0.1662 0.1805 0.1846 0.0321  -0.0213 -0.0232 55  LYS   A CG  
1299 C CD  . LYS   A 55  ? 0.1817 0.2155 0.1865 0.0523  -0.0109 -0.0291 55  LYS   A CD  
1300 C CE  . LYS   A 55  ? 0.2018 0.2494 0.2126 0.0579  -0.0235 -0.0320 55  LYS   A CE  
1301 N NZ  . LYS   A 55  ? 0.2131 0.2574 0.2272 0.0705  -0.0311 -0.0307 55  LYS   A NZ  
1315 N N   . ALA   A 56  ? 0.1289 0.1551 0.1336 -0.0104 0.0127  -0.0287 56  ALA   A N   
1316 C CA  . ALA   A 56  ? 0.1372 0.1749 0.1334 -0.0189 0.0175  -0.0278 56  ALA   A CA  
1317 C C   . ALA   A 56  ? 0.1460 0.1859 0.1163 -0.0213 0.0132  -0.0353 56  ALA   A C   
1318 O O   . ALA   A 56  ? 0.1531 0.2196 0.1229 -0.0044 0.0227  -0.0340 56  ALA   A O   
1319 C CB  . ALA   A 56  ? 0.1416 0.1920 0.1389 -0.0303 0.0196  -0.0132 56  ALA   A CB  
1325 N N   . THR   A 57  ? 0.1324 0.1619 0.1160 -0.0164 0.0163  -0.0225 57  THR   A N   
1326 C CA  . THR   A 57  ? 0.1316 0.1561 0.1196 -0.0188 0.0056  -0.0156 57  THR   A CA  
1327 C C   . THR   A 57  ? 0.1336 0.1633 0.1270 -0.0072 0.0012  -0.0242 57  THR   A C   
1328 O O   . THR   A 57  ? 0.1342 0.1681 0.1402 -0.0137 -0.0088 -0.0277 57  THR   A O   
1329 C CB  . THR   A 57  ? 0.1340 0.1562 0.1105 -0.0129 0.0122  -0.0196 57  THR   A CB  
1330 O OG1 . THR   A 57  ? 0.1232 0.1529 0.1197 -0.0078 0.0048  -0.0138 57  THR   A OG1 
1331 C CG2 . THR   A 57  ? 0.1422 0.1581 0.1148 -0.0191 -0.0008 -0.0102 57  THR   A CG2 
1339 N N   . ASN   A 58  ? 0.1353 0.1577 0.1481 -0.0144 0.0086  -0.0398 58  ASN   A N   
1340 C CA  . ASN   A 58  ? 0.1556 0.1569 0.1572 -0.0147 0.0181  -0.0524 58  ASN   A CA  
1341 C C   . ASN   A 58  ? 0.1332 0.1446 0.1525 -0.0064 0.0062  -0.0283 58  ASN   A C   
1342 O O   . ASN   A 58  ? 0.1375 0.1539 0.1683 -0.0206 -0.0026 -0.0347 58  ASN   A O   
1343 C CB  . ASN   A 58  ? 0.2024 0.1724 0.2028 -0.0219 0.0376  -0.0614 58  ASN   A CB  
1344 C CG  . ASN   A 58  ? 0.2405 0.1960 0.2782 -0.0189 0.0368  -0.0506 58  ASN   A CG  
1345 O OD1 . ASN   A 58  ? 0.2638 0.1943 0.3231 0.0159  0.0602  -0.0399 58  ASN   A OD1 
1346 N ND2 . ASN   A 58  ? 0.2508 0.2031 0.2992 -0.0257 0.0240  -0.0490 58  ASN   A ND2 
1353 N N   . ASN   A 59  ? 0.1224 0.1361 0.1420 -0.0065 -0.0039 -0.0236 59  ASN   A N   
1354 C CA  . ASN   A 59  ? 0.1257 0.1230 0.1397 -0.0038 -0.0021 -0.0158 59  ASN   A CA  
1355 C C   . ASN   A 59  ? 0.1264 0.1312 0.1219 -0.0083 -0.0093 -0.0114 59  ASN   A C   
1356 O O   . ASN   A 59  ? 0.1298 0.1351 0.1295 -0.0087 -0.0025 -0.0016 59  ASN   A O   
1357 C CB  . ASN   A 59  ? 0.1307 0.1241 0.1453 -0.0011 -0.0240 -0.0240 59  ASN   A CB  
1358 C CG  . ASN   A 59  ? 0.1289 0.1252 0.1501 -0.0007 -0.0263 -0.0027 59  ASN   A CG  
1359 O OD1 . ASN   A 59  ? 0.1407 0.1335 0.1395 -0.0095 -0.0214 -0.0014 59  ASN   A OD1 
1360 N ND2 . ASN   A 59  ? 0.1452 0.1282 0.1702 -0.0138 -0.0172 0.0005  59  ASN   A ND2 
1367 N N   . ALA   A 60  ? 0.1186 0.1335 0.1310 -0.0040 -0.0034 -0.0112 60  ALA   A N   
1368 C CA  . ALA   A 60  ? 0.1234 0.1332 0.1360 -0.0023 -0.0103 -0.0073 60  ALA   A CA  
1369 C C   . ALA   A 60  ? 0.1220 0.1293 0.1350 -0.0030 -0.0099 -0.0023 60  ALA   A C   
1370 O O   . ALA   A 60  ? 0.1129 0.1257 0.1643 -0.0028 -0.0129 -0.0127 60  ALA   A O   
1371 C CB  . ALA   A 60  ? 0.1339 0.1502 0.1356 -0.0042 -0.0189 -0.0215 60  ALA   A CB  
1377 N N   . MET   A 61  ? 0.1156 0.1255 0.1259 -0.0055 -0.0046 -0.0091 61  MET   A N   
1378 C CA  . MET   A 61  ? 0.1209 0.1230 0.1219 -0.0083 0.0060  -0.0029 61  MET   A CA  
1379 C C   . MET   A 61  ? 0.1134 0.1174 0.1299 -0.0079 0.0066  -0.0079 61  MET   A C   
1380 O O   . MET   A 61  ? 0.1173 0.1193 0.1367 -0.0064 0.0080  -0.0031 61  MET   A O   
1381 C CB  . MET   A 61  ? 0.1232 0.1220 0.1187 -0.0073 0.0018  -0.0064 61  MET   A CB  
1382 C CG  . MET   A 61  ? 0.1198 0.1295 0.1355 -0.0070 0.0050  0.0012  61  MET   A CG  
1383 S SD  . MET   A 61  ? 0.1260 0.1333 0.1573 -0.0115 0.0002  -0.0194 61  MET   A SD  
1384 C CE  . MET   A 61  ? 0.1476 0.1456 0.1635 -0.0192 0.0214  -0.0166 61  MET   A CE  
1394 N N   . GLN   A 62  ? 0.1094 0.1155 0.1313 -0.0043 0.0053  -0.0041 62  GLN   A N   
1395 C CA  . GLN   A 62  ? 0.1151 0.1175 0.1331 -0.0038 -0.0006 0.0002  62  GLN   A CA  
1396 C C   . GLN   A 62  ? 0.1195 0.1038 0.1408 0.0022  0.0045  0.0029  62  GLN   A C   
1397 O O   . GLN   A 62  ? 0.1229 0.1244 0.1278 -0.0026 0.0069  0.0002  62  GLN   A O   
1398 C CB  . GLN   A 62  ? 0.1146 0.1149 0.1426 -0.0047 -0.0005 0.0037  62  GLN   A CB  
1399 C CG  . GLN   A 62  ? 0.1207 0.1131 0.1450 -0.0066 0.0024  0.0107  62  GLN   A CG  
1400 C CD  . GLN   A 62  ? 0.1300 0.1168 0.1315 -0.0044 0.0049  0.0103  62  GLN   A CD  
1401 O OE1 . GLN   A 62  ? 0.1292 0.1300 0.1363 -0.0025 -0.0038 0.0023  62  GLN   A OE1 
1402 N NE2 . GLN   A 62  ? 0.1387 0.1195 0.1385 -0.0021 0.0046  -0.0067 62  GLN   A NE2 
1411 N N   . VAL   A 63  ? 0.1190 0.1184 0.1505 -0.0067 0.0073  -0.0200 63  VAL   A N   
1412 C CA  . VAL   A 63  ? 0.1209 0.1314 0.1680 -0.0159 -0.0012 -0.0223 63  VAL   A CA  
1413 C C   . VAL   A 63  ? 0.1121 0.1314 0.1471 -0.0203 0.0036  -0.0156 63  VAL   A C   
1414 O O   . VAL   A 63  ? 0.1137 0.1310 0.1637 -0.0176 0.0052  -0.0079 63  VAL   A O   
1415 C CB  . VAL   A 63  ? 0.1321 0.1480 0.1996 -0.0172 -0.0066 -0.0407 63  VAL   A CB  
1416 C CG1 . VAL   A 63  ? 0.1498 0.1630 0.2404 -0.0206 -0.0130 -0.0538 63  VAL   A CG1 
1417 C CG2 . VAL   A 63  ? 0.1381 0.1440 0.2185 -0.0129 0.0054  -0.0336 63  VAL   A CG2 
1427 N N   . GLU   A 64  ? 0.1100 0.1431 0.1452 -0.0079 -0.0022 -0.0142 64  GLU   A N   
1428 C CA  . GLU   A 64  ? 0.1133 0.1415 0.1420 -0.0059 -0.0029 0.0013  64  GLU   A CA  
1429 C C   . GLU   A 64  ? 0.1140 0.1266 0.1372 -0.0082 0.0032  0.0076  64  GLU   A C   
1430 O O   . GLU   A 64  ? 0.1159 0.1334 0.1519 -0.0020 0.0088  0.0008  64  GLU   A O   
1431 C CB  . GLU   A 64  ? 0.1183 0.1438 0.1467 -0.0091 0.0029  -0.0053 64  GLU   A CB  
1432 C CG  . GLU   A 64  ? 0.1342 0.1499 0.1640 -0.0105 0.0144  -0.0014 64  GLU   A CG  
1433 C CD  . GLU   A 64  ? 0.1439 0.1516 0.1574 -0.0176 0.0120  -0.0034 64  GLU   A CD  
1434 O OE1 . GLU   A 64  ? 0.1412 0.1624 0.1794 -0.0262 0.0204  -0.0015 64  GLU   A OE1 
1435 O OE2 . GLU   A 64  ? 0.1583 0.1578 0.1509 -0.0279 -0.0003 0.0023  64  GLU   A OE2 
1442 N N   . SER   A 65  ? 0.1137 0.1238 0.1194 -0.0032 0.0027  -0.0016 65  SER   A N   
1443 C CA  . SER   A 65  ? 0.1177 0.1198 0.1295 -0.0038 -0.0079 -0.0038 65  SER   A CA  
1444 C C   . SER   A 65  ? 0.1198 0.1190 0.1253 -0.0040 -0.0050 -0.0054 65  SER   A C   
1445 O O   . SER   A 65  ? 0.1310 0.1225 0.1555 -0.0009 0.0097  -0.0081 65  SER   A O   
1446 C CB  . SER   A 65  ? 0.1090 0.1192 0.1288 -0.0045 0.0046  -0.0013 65  SER   A CB  
1447 O OG  . SER   A 65  ? 0.1149 0.1319 0.1455 -0.0094 0.0014  0.0101  65  SER   A OG  
1453 N N   . ASP   A 66  ? 0.1172 0.1239 0.1286 -0.0050 0.0088  0.0058  66  ASP   A N   
1454 C CA  . ASP   A 66  ? 0.1225 0.1328 0.1450 -0.0031 0.0079  0.0125  66  ASP   A CA  
1455 C C   . ASP   A 66  ? 0.1187 0.1306 0.1464 -0.0093 0.0123  0.0112  66  ASP   A C   
1456 O O   . ASP   A 66  ? 0.1296 0.1436 0.1721 -0.0085 0.0274  0.0166  66  ASP   A O   
1457 C CB  . ASP   A 66  ? 0.1330 0.1483 0.1787 0.0105  0.0170  0.0244  66  ASP   A CB  
1458 C CG  . ASP   A 66  ? 0.1505 0.1619 0.2179 0.0007  0.0129  0.0509  66  ASP   A CG  
1459 O OD1 . ASP   A 66  ? 0.1544 0.1907 0.1912 -0.0029 -0.0063 0.0556  66  ASP   A OD1 
1460 O OD2 . ASP   A 66  ? 0.1694 0.1704 0.3010 0.0232  -0.0093 0.0348  66  ASP   A OD2 
1465 N N   . ASP   A 67  ? 0.1185 0.1343 0.1558 -0.0041 0.0065  0.0105  67  ASP   A N   
1466 C CA  . ASP   A 67  ? 0.1185 0.1465 0.1794 -0.0072 0.0004  0.0194  67  ASP   A CA  
1467 C C   . ASP   A 67  ? 0.1198 0.1434 0.1701 0.0023  0.0069  0.0259  67  ASP   A C   
1468 O O   . ASP   A 67  ? 0.1162 0.1540 0.1828 0.0023  0.0185  0.0289  67  ASP   A O   
1469 C CB  . ASP   A 67  ? 0.1295 0.1492 0.2040 -0.0056 -0.0182 0.0246  67  ASP   A CB  
1470 C CG  . ASP   A 67  ? 0.1331 0.1653 0.2418 -0.0109 -0.0334 0.0289  67  ASP   A CG  
1471 O OD1 . ASP   A 67  ? 0.1365 0.1820 0.3247 -0.0110 -0.0400 0.0407  67  ASP   A OD1 
1472 O OD2 . ASP   A 67  ? 0.1360 0.1721 0.2236 0.0065  -0.0207 0.0210  67  ASP   A OD2 
1477 N N   . TYR   A 68  ? 0.1224 0.1325 0.1728 0.0059  0.0150  0.0243  68  TYR   A N   
1478 C CA  . TYR   A 68  ? 0.1340 0.1344 0.1596 0.0029  0.0181  0.0233  68  TYR   A CA  
1479 C C   . TYR   A 68  ? 0.1233 0.1316 0.1596 -0.0002 0.0210  0.0191  68  TYR   A C   
1480 O O   . TYR   A 68  ? 0.1288 0.1382 0.1687 0.0078  0.0291  0.0220  68  TYR   A O   
1481 C CB  . TYR   A 68  ? 0.1329 0.1248 0.1652 0.0079  0.0332  0.0158  68  TYR   A CB  
1482 C CG  . TYR   A 68  ? 0.1334 0.1459 0.1968 0.0054  0.0508  0.0240  68  TYR   A CG  
1483 C CD1 . TYR   A 68  ? 0.1417 0.1575 0.2233 -0.0151 0.0478  -0.0123 68  TYR   A CD1 
1484 C CD2 . TYR   A 68  ? 0.1626 0.1504 0.2248 0.0214  0.0505  0.0330  68  TYR   A CD2 
1485 C CE1 . TYR   A 68  ? 0.1487 0.1674 0.2539 -0.0161 0.0461  -0.0126 68  TYR   A CE1 
1486 C CE2 . TYR   A 68  ? 0.1524 0.1563 0.2303 0.0103  0.0609  0.0096  68  TYR   A CE2 
1487 C CZ  . TYR   A 68  ? 0.1577 0.1608 0.2473 -0.0129 0.0467  -0.0089 68  TYR   A CZ  
1488 O OH  . TYR   A 68  ? 0.1818 0.1618 0.2578 -0.0041 0.0149  -0.0195 68  TYR   A OH  
1498 N N   . ILE   A 69  ? 0.1174 0.1265 0.1651 0.0010  0.0191  0.0153  69  ILE   A N   
1499 C CA  . ILE   A 69  ? 0.1274 0.1292 0.1555 0.0058  0.0147  0.0014  69  ILE   A CA  
1500 C C   . ILE   A 69  ? 0.1317 0.1299 0.1517 0.0049  0.0204  0.0103  69  ILE   A C   
1501 O O   . ILE   A 69  ? 0.1392 0.1398 0.1430 -0.0020 0.0221  0.0155  69  ILE   A O   
1502 C CB  . ILE   A 69  ? 0.1379 0.1466 0.1531 0.0050  0.0105  -0.0034 69  ILE   A CB  
1503 C CG1 . ILE   A 69  ? 0.1419 0.1588 0.1578 0.0052  0.0147  -0.0174 69  ILE   A CG1 
1504 C CG2 . ILE   A 69  ? 0.1563 0.1677 0.1703 0.0172  -0.0028 0.0021  69  ILE   A CG2 
1505 C CD1 . ILE   A 69  ? 0.1428 0.1683 0.1650 -0.0009 0.0124  -0.0186 69  ILE   A CD1 
1517 N N   . ALA   A 70  ? 0.1370 0.1349 0.1571 -0.0053 0.0198  0.0185  70  ALA   A N   
1518 C CA  . ALA   A 70  ? 0.1384 0.1422 0.1789 -0.0137 0.0288  0.0203  70  ALA   A CA  
1519 C C   . ALA   A 70  ? 0.1360 0.1591 0.1798 -0.0128 0.0294  0.0175  70  ALA   A C   
1520 O O   . ALA   A 70  ? 0.1508 0.1906 0.1956 -0.0015 0.0466  0.0337  70  ALA   A O   
1521 C CB  . ALA   A 70  ? 0.1364 0.1460 0.2088 -0.0158 0.0306  0.0109  70  ALA   A CB  
1527 N N   . THR   A 71  ? 0.1281 0.1549 0.1681 -0.0008 0.0216  0.0201  71  THR   A N   
1528 C CA  . THR   A 71  ? 0.1373 0.1687 0.1934 0.0067  0.0269  0.0252  71  THR   A CA  
1529 C C   . THR   A 71  ? 0.1349 0.1584 0.2205 0.0148  0.0359  0.0265  71  THR   A C   
1530 O O   . THR   A 71  ? 0.1412 0.1839 0.2571 0.0083  0.0418  -0.0015 71  THR   A O   
1531 C CB  . THR   A 71  ? 0.1614 0.1940 0.2167 0.0103  -0.0109 0.0290  71  THR   A CB  
1532 O OG1 . THR   A 71  ? 0.1824 0.2137 0.2149 -0.0000 -0.0284 0.0281  71  THR   A OG1 
1533 C CG2 . THR   A 71  ? 0.1838 0.2097 0.2395 0.0220  -0.0218 0.0347  71  THR   A CG2 
1541 N N   . ASN   A 72  ? 0.1377 0.1475 0.1900 0.0088  0.0304  0.0218  72  ASN   A N   
1542 C CA  . ASN   A 72  ? 0.1403 0.1469 0.1896 0.0180  0.0376  0.0253  72  ASN   A CA  
1543 C C   . ASN   A 72  ? 0.1492 0.1449 0.1864 0.0105  0.0451  0.0194  72  ASN   A C   
1544 O O   . ASN   A 72  ? 0.1653 0.1462 0.2233 0.0199  0.0380  0.0051  72  ASN   A O   
1545 C CB  . ASN   A 72  ? 0.1580 0.1550 0.1957 0.0160  0.0425  0.0283  72  ASN   A CB  
1546 C CG  . ASN   A 72  ? 0.1856 0.1691 0.1923 0.0236  0.0405  0.0336  72  ASN   A CG  
1547 O OD1 . ASN   A 72  ? 0.1927 0.2050 0.2115 0.0240  0.0477  0.0359  72  ASN   A OD1 
1548 N ND2 . ASN   A 72  ? 0.2009 0.1667 0.1970 0.0482  0.0089  0.0125  72  ASN   A ND2 
1555 N N   . GLY   A 73  ? 0.1479 0.1429 0.1697 0.0071  0.0383  0.0093  73  GLY   A N   
1556 C CA  . GLY   A 73  ? 0.1563 0.1437 0.1662 -0.0008 0.0385  0.0117  73  GLY   A CA  
1557 C C   . GLY   A 73  ? 0.1528 0.1337 0.1585 0.0007  0.0467  0.0199  73  GLY   A C   
1558 O O   . GLY   A 73  ? 0.1514 0.1342 0.1762 0.0065  0.0362  0.0268  73  GLY   A O   
1562 N N   . PRO   A 74  ? 0.1587 0.1370 0.1564 -0.0103 0.0436  0.0136  74  PRO   A N   
1563 C CA  . PRO   A 74  ? 0.1541 0.1401 0.1737 -0.0054 0.0398  0.0209  74  PRO   A CA  
1564 C C   . PRO   A 74  ? 0.1429 0.1236 0.1591 -0.0004 0.0281  0.0021  74  PRO   A C   
1565 O O   . PRO   A 74  ? 0.1552 0.1272 0.1753 0.0045  0.0272  -0.0111 74  PRO   A O   
1566 C CB  . PRO   A 74  ? 0.1698 0.1711 0.1892 0.0014  0.0455  0.0252  74  PRO   A CB  
1567 C CG  . PRO   A 74  ? 0.1954 0.1984 0.2407 -0.0209 0.0336  0.0133  74  PRO   A CG  
1568 C CD  . PRO   A 74  ? 0.1770 0.1679 0.1787 -0.0243 0.0340  0.0005  74  PRO   A CD  
1576 N N   . LEU   A 75  ? 0.1464 0.1172 0.1403 -0.0025 0.0208  0.0021  75  LEU   A N   
1577 C CA  . LEU   A 75  ? 0.1593 0.1176 0.1231 -0.0004 0.0102  0.0053  75  LEU   A CA  
1578 C C   . LEU   A 75  ? 0.1648 0.1296 0.1244 0.0024  0.0139  0.0085  75  LEU   A C   
1579 O O   . LEU   A 75  ? 0.1960 0.1412 0.1344 0.0084  0.0131  0.0016  75  LEU   A O   
1580 C CB  . LEU   A 75  ? 0.1607 0.1211 0.1215 -0.0085 0.0134  0.0119  75  LEU   A CB  
1581 C CG  . LEU   A 75  ? 0.1717 0.1501 0.1285 -0.0323 0.0045  0.0091  75  LEU   A CG  
1582 C CD1 . LEU   A 75  ? 0.1776 0.1984 0.1383 -0.0391 0.0104  0.0023  75  LEU   A CD1 
1583 C CD2 . LEU   A 75  ? 0.1914 0.1845 0.1928 -0.0167 0.0111  0.0139  75  LEU   A CD2 
1595 N N   . LYS   A 76  ? 0.1664 0.1306 0.1412 -0.0046 0.0156  -0.0077 76  LYS   A N   
1596 C CA  . LYS   A 76  ? 0.1644 0.1497 0.1453 -0.0101 0.0196  -0.0196 76  LYS   A CA  
1597 C C   . LYS   A 76  ? 0.1572 0.1288 0.1208 -0.0025 0.0139  0.0025  76  LYS   A C   
1598 O O   . LYS   A 76  ? 0.1583 0.1266 0.1173 -0.0058 0.0165  0.0050  76  LYS   A O   
1599 C CB  . LYS   A 76  ? 0.1668 0.1780 0.1978 -0.0028 0.0202  -0.0437 76  LYS   A CB  
1600 C CG  . LYS   A 76  ? 0.1718 0.1726 0.2524 0.0040  0.0186  -0.0431 76  LYS   A CG  
1601 C CD  . LYS   A 76  ? 0.1851 0.1748 0.3073 0.0116  0.0116  -0.0474 76  LYS   A CD  
1602 C CE  . LYS   A 76  ? 0.2004 0.1976 0.3693 0.0008  0.0240  -0.0537 76  LYS   A CE  
1603 N NZ  . LYS   A 76  ? 0.1990 0.1959 0.4071 -0.0154 0.0190  -0.0579 76  LYS   A NZ  
1617 N N   . VAL   A 77  ? 0.1682 0.1326 0.1207 -0.0045 0.0328  0.0071  77  VAL   A N   
1618 C CA  . VAL   A 77  ? 0.1657 0.1370 0.1207 0.0032  0.0206  0.0082  77  VAL   A CA  
1619 C C   . VAL   A 77  ? 0.1604 0.1308 0.1123 0.0082  0.0142  -0.0020 77  VAL   A C   
1620 O O   . VAL   A 77  ? 0.1695 0.1332 0.1151 0.0121  0.0292  -0.0069 77  VAL   A O   
1621 C CB  . VAL   A 77  ? 0.1836 0.1520 0.1272 0.0037  0.0163  0.0224  77  VAL   A CB  
1622 C CG1 . VAL   A 77  ? 0.1821 0.1704 0.1537 0.0130  0.0082  0.0067  77  VAL   A CG1 
1623 C CG2 . VAL   A 77  ? 0.2059 0.1593 0.1629 -0.0008 0.0038  0.0190  77  VAL   A CG2 
1633 N N   . GLY   A 78  ? 0.1613 0.1275 0.1124 0.0052  0.0224  0.0040  78  GLY   A N   
1634 C CA  . GLY   A 78  ? 0.1522 0.1286 0.1183 0.0015  0.0249  0.0113  78  GLY   A CA  
1635 C C   . GLY   A 78  ? 0.1428 0.1257 0.1168 0.0107  0.0241  0.0123  78  GLY   A C   
1636 O O   . GLY   A 78  ? 0.1408 0.1340 0.1342 0.0049  0.0260  0.0151  78  GLY   A O   
1640 N N   . GLY   A 79  ? 0.1446 0.1241 0.1191 0.0004  0.0173  0.0059  79  GLY   A N   
1641 C CA  . GLY   A 79  ? 0.1385 0.1262 0.1315 -0.0028 0.0230  0.0018  79  GLY   A CA  
1642 C C   . GLY   A 79  ? 0.1256 0.1180 0.1234 -0.0006 0.0192  0.0033  79  GLY   A C   
1643 O O   . GLY   A 79  ? 0.1322 0.1287 0.1328 0.0195  0.0149  0.0058  79  GLY   A O   
1647 N N   . SER   A 80  ? 0.1207 0.1330 0.1375 0.0033  0.0133  -0.0071 80  SER   A N   
1648 C CA  . SER   A 80  ? 0.1176 0.1254 0.1310 -0.0030 0.0071  -0.0005 80  SER   A CA  
1649 C C   . SER   A 80  ? 0.1263 0.1230 0.1328 -0.0000 0.0091  0.0121  80  SER   A C   
1650 O O   . SER   A 80  ? 0.1252 0.1480 0.1621 0.0092  0.0158  -0.0045 80  SER   A O   
1651 C CB  . SER   A 80  ? 0.1338 0.1324 0.1561 0.0002  0.0094  0.0025  80  SER   A CB  
1652 O OG  . SER   A 80  ? 0.1597 0.1323 0.1931 0.0001  0.0030  0.0214  80  SER   A OG  
1658 N N   . CYS   A 81  ? 0.1198 0.1262 0.1297 -0.0032 0.0021  0.0068  81  CYS   A N   
1659 C CA  . CYS   A 81  ? 0.1144 0.1287 0.1297 -0.0079 -0.0025 0.0187  81  CYS   A CA  
1660 C C   . CYS   A 81  ? 0.1162 0.1308 0.1262 -0.0097 -0.0015 0.0297  81  CYS   A C   
1661 O O   . CYS   A 81  ? 0.1151 0.1527 0.1435 0.0002  0.0030  0.0351  81  CYS   A O   
1662 C CB  . CYS   A 81  ? 0.1224 0.1426 0.1411 -0.0153 0.0053  0.0189  81  CYS   A CB  
1663 S SG  . CYS   A 81  ? 0.1346 0.1257 0.1405 -0.0130 0.0032  0.0128  81  CYS   A SG  
1669 N N   . VAL   A 82  ? 0.1163 0.1367 0.1283 0.0021  -0.0077 0.0163  82  VAL   A N   
1670 C CA  . VAL   A 82  ? 0.1274 0.1436 0.1233 -0.0028 -0.0017 0.0266  82  VAL   A CA  
1671 C C   . VAL   A 82  ? 0.1271 0.1464 0.1275 -0.0103 -0.0054 0.0208  82  VAL   A C   
1672 O O   . VAL   A 82  ? 0.1247 0.1534 0.1528 -0.0081 -0.0070 0.0007  82  VAL   A O   
1673 C CB  . VAL   A 82  ? 0.1603 0.1565 0.1276 0.0034  0.0004  0.0313  82  VAL   A CB  
1674 C CG1 . VAL   A 82  ? 0.1810 0.1707 0.1570 0.0081  0.0023  0.0255  82  VAL   A CG1 
1675 C CG2 . VAL   A 82  ? 0.1720 0.1647 0.1514 0.0005  -0.0006 0.0388  82  VAL   A CG2 
1685 N N   . LEU   A 83  ? 0.1208 0.1419 0.1256 -0.0114 -0.0031 0.0092  83  LEU   A N   
1686 C CA  . LEU   A 83  ? 0.1274 0.1459 0.1214 -0.0139 -0.0099 0.0061  83  LEU   A CA  
1687 C C   . LEU   A 83  ? 0.1319 0.1494 0.1126 -0.0143 -0.0159 0.0155  83  LEU   A C   
1688 O O   . LEU   A 83  ? 0.1379 0.1502 0.1291 -0.0219 -0.0016 0.0189  83  LEU   A O   
1689 C CB  . LEU   A 83  ? 0.1353 0.1478 0.1155 -0.0103 -0.0111 0.0137  83  LEU   A CB  
1690 C CG  . LEU   A 83  ? 0.1480 0.1516 0.1239 -0.0063 0.0047  0.0063  83  LEU   A CG  
1691 C CD1 . LEU   A 83  ? 0.1566 0.1544 0.1355 -0.0198 0.0023  0.0237  83  LEU   A CD1 
1692 C CD2 . LEU   A 83  ? 0.1483 0.1677 0.1477 -0.0054 0.0157  0.0144  83  LEU   A CD2 
1704 N N   . SER   A 84  ? 0.1426 0.1537 0.1220 -0.0185 -0.0113 0.0151  84  SER   A N   
1705 C CA  . SER   A 84  ? 0.1537 0.1602 0.1053 -0.0151 -0.0057 0.0123  84  SER   A CA  
1706 C C   . SER   A 84  ? 0.1497 0.1531 0.1012 -0.0227 0.0035  0.0102  84  SER   A C   
1707 O O   . SER   A 84  ? 0.1469 0.1631 0.1078 -0.0137 -0.0035 0.0043  84  SER   A O   
1708 C CB  . SER   A 84  ? 0.1523 0.1766 0.1165 -0.0167 -0.0013 0.0008  84  SER   A CB  
1709 O OG  . SER   A 84  ? 0.1558 0.1997 0.1221 -0.0140 -0.0212 -0.0131 84  SER   A OG  
1715 N N   . GLY   A 85  ? 0.1675 0.1661 0.1084 -0.0248 0.0073  0.0004  85  GLY   A N   
1716 C CA  . GLY   A 85  ? 0.1700 0.1812 0.1186 -0.0303 0.0135  -0.0147 85  GLY   A CA  
1717 C C   . GLY   A 85  ? 0.1612 0.1862 0.0996 -0.0284 0.0032  -0.0038 85  GLY   A C   
1718 O O   . GLY   A 85  ? 0.1662 0.1896 0.1220 -0.0319 0.0184  -0.0152 85  GLY   A O   
1722 N N   . HIS   A 86  ? 0.1585 0.1799 0.1033 -0.0276 -0.0054 0.0022  86  HIS   A N   
1723 C CA  . HIS   A 86  ? 0.1808 0.1828 0.1053 -0.0314 -0.0002 0.0027  86  HIS   A CA  
1724 C C   . HIS   A 86  ? 0.2025 0.1912 0.1020 -0.0320 -0.0049 0.0000  86  HIS   A C   
1725 O O   . HIS   A 86  ? 0.2090 0.2156 0.1069 -0.0256 0.0111  0.0022  86  HIS   A O   
1726 C CB  . HIS   A 86  ? 0.1731 0.1725 0.1103 -0.0231 0.0134  -0.0012 86  HIS   A CB  
1727 C CG  . HIS   A 86  ? 0.1687 0.1688 0.1207 -0.0153 0.0005  0.0020  86  HIS   A CG  
1728 N ND1 . HIS   A 86  ? 0.1825 0.1691 0.1637 -0.0205 -0.0020 0.0012  86  HIS   A ND1 
1729 C CD2 . HIS   A 86  ? 0.1699 0.1570 0.1127 -0.0025 0.0129  0.0068  86  HIS   A CD2 
1730 C CE1 . HIS   A 86  ? 0.1777 0.1675 0.1526 -0.0122 0.0241  0.0058  86  HIS   A CE1 
1731 N NE2 . HIS   A 86  ? 0.1730 0.1584 0.1242 0.0047  0.0241  0.0187  86  HIS   A NE2 
1739 N N   . ASN   A 87  ? 0.2128 0.2042 0.1147 -0.0285 0.0202  -0.0122 87  ASN   A N   
1740 C CA  . ASN   A 87  ? 0.2329 0.2139 0.1214 -0.0189 0.0470  -0.0232 87  ASN   A CA  
1741 C C   . ASN   A 87  ? 0.2267 0.2213 0.1597 -0.0285 0.0625  -0.0074 87  ASN   A C   
1742 O O   . ASN   A 87  ? 0.2567 0.2346 0.2039 -0.0403 0.0965  -0.0167 87  ASN   A O   
1743 C CB  . ASN   A 87  ? 0.2568 0.2210 0.1216 -0.0074 0.0544  -0.0342 87  ASN   A CB  
1744 C CG  . ASN   A 87  ? 0.2686 0.2308 0.1310 -0.0045 0.0613  -0.0232 87  ASN   A CG  
1745 O OD1 . ASN   A 87  ? 0.2859 0.2287 0.1389 0.0137  0.0583  -0.0058 87  ASN   A OD1 
1746 N ND2 . ASN   A 87  ? 0.2680 0.2539 0.1472 -0.0052 0.0645  -0.0123 87  ASN   A ND2 
1753 N N   A LEU   A 88  ? 0.2052 0.2136 0.1531 -0.0372 0.0355  0.0038  88  LEU   A N   
1754 N N   B LEU   A 88  ? 0.2125 0.2165 0.1567 -0.0287 0.0445  -0.0041 88  LEU   A N   
1755 C CA  A LEU   A 88  ? 0.1868 0.2151 0.1612 -0.0442 0.0287  0.0238  88  LEU   A CA  
1756 C CA  B LEU   A 88  ? 0.1988 0.2174 0.1626 -0.0285 0.0392  0.0054  88  LEU   A CA  
1757 C C   A LEU   A 88  ? 0.1845 0.2188 0.1475 -0.0395 0.0274  0.0255  88  LEU   A C   
1758 C C   B LEU   A 88  ? 0.1914 0.2185 0.1475 -0.0306 0.0317  0.0148  88  LEU   A C   
1759 O O   A LEU   A 88  ? 0.1896 0.2253 0.1919 -0.0385 0.0263  0.0339  88  LEU   A O   
1760 O O   B LEU   A 88  ? 0.1951 0.2231 0.1728 -0.0294 0.0327  0.0268  88  LEU   A O   
1761 C CB  A LEU   A 88  ? 0.1865 0.2194 0.1781 -0.0531 -0.0064 0.0274  88  LEU   A CB  
1762 C CB  B LEU   A 88  ? 0.2005 0.2204 0.1779 -0.0258 0.0261  -0.0015 88  LEU   A CB  
1763 C CG  A LEU   A 88  ? 0.2028 0.2316 0.2127 -0.0531 -0.0115 0.0303  88  LEU   A CG  
1764 C CG  B LEU   A 88  ? 0.2077 0.2262 0.1950 -0.0212 0.0206  -0.0080 88  LEU   A CG  
1765 C CD1 A LEU   A 88  ? 0.2117 0.2355 0.2197 -0.0514 -0.0152 0.0231  88  LEU   A CD1 
1766 C CD1 B LEU   A 88  ? 0.2091 0.2267 0.1940 -0.0171 0.0200  -0.0196 88  LEU   A CD1 
1767 C CD2 A LEU   A 88  ? 0.2167 0.2427 0.2489 -0.0502 -0.0078 0.0262  88  LEU   A CD2 
1768 C CD2 B LEU   A 88  ? 0.2157 0.2332 0.2176 -0.0203 0.0191  -0.0093 88  LEU   A CD2 
1791 N N   . ALA   A 89  ? 0.1848 0.2129 0.1171 -0.0305 0.0221  0.0070  89  ALA   A N   
1792 C CA  . ALA   A 89  ? 0.1933 0.2068 0.0911 -0.0277 0.0172  0.0135  89  ALA   A CA  
1793 C C   . ALA   A 89  ? 0.2003 0.2105 0.1069 -0.0263 0.0017  0.0108  89  ALA   A C   
1794 O O   . ALA   A 89  ? 0.1896 0.2047 0.1476 -0.0317 -0.0099 -0.0119 89  ALA   A O   
1795 C CB  . ALA   A 89  ? 0.1879 0.1962 0.0946 -0.0265 0.0113  0.0138  89  ALA   A CB  
1802 N N   . LYS   A 90  ? 0.2060 0.2198 0.1007 -0.0333 -0.0202 0.0115  90  LYS   A N   
1803 C CA  . LYS   A 90  ? 0.2107 0.2315 0.1142 -0.0248 -0.0379 0.0242  90  LYS   A CA  
1804 C C   . LYS   A 90  ? 0.1931 0.2161 0.1166 -0.0296 -0.0306 0.0119  90  LYS   A C   
1805 O O   . LYS   A 90  ? 0.1950 0.2327 0.1437 -0.0379 -0.0325 -0.0022 90  LYS   A O   
1806 C CB  . LYS   A 90  ? 0.2331 0.2598 0.1542 -0.0200 -0.0440 0.0414  90  LYS   A CB  
1807 C CG  . LYS   A 90  ? 0.2616 0.2848 0.2521 -0.0158 -0.0516 0.0439  90  LYS   A CG  
1808 C CD  . LYS   A 90  ? 0.3010 0.3131 0.3507 -0.0178 -0.0449 0.0452  90  LYS   A CD  
1809 C CE  . LYS   A 90  ? 0.3304 0.3404 0.4221 -0.0193 -0.0329 0.0427  90  LYS   A CE  
1810 N NZ  . LYS   A 90  ? 0.3368 0.3495 0.4725 -0.0198 -0.0265 0.0368  90  LYS   A NZ  
1824 N N   . HIS   A 91  ? 0.1779 0.1860 0.1029 -0.0268 -0.0410 0.0165  91  HIS   A N   
1825 C CA  . HIS   A 91  ? 0.1665 0.1695 0.1056 -0.0197 -0.0281 0.0123  91  HIS   A CA  
1826 C C   . HIS   A 91  ? 0.1504 0.1567 0.0920 -0.0215 -0.0103 0.0165  91  HIS   A C   
1827 O O   . HIS   A 91  ? 0.1489 0.1695 0.1056 -0.0283 -0.0082 0.0178  91  HIS   A O   
1828 C CB  . HIS   A 91  ? 0.1773 0.1955 0.1452 0.0033  -0.0417 0.0153  91  HIS   A CB  
1829 C CG  . HIS   A 91  ? 0.2305 0.2438 0.2283 0.0157  -0.0728 0.0014  91  HIS   A CG  
1830 N ND1 . HIS   A 91  ? 0.2409 0.2713 0.2769 0.0244  -0.0883 -0.0202 91  HIS   A ND1 
1831 C CD2 . HIS   A 91  ? 0.2575 0.2638 0.2632 0.0269  -0.0908 0.0124  91  HIS   A CD2 
1832 C CE1 . HIS   A 91  ? 0.2555 0.2792 0.2954 0.0263  -0.0930 -0.0130 91  HIS   A CE1 
1833 N NE2 . HIS   A 91  ? 0.2682 0.2803 0.2931 0.0306  -0.0989 0.0033  91  HIS   A NE2 
1841 N N   . CYS   A 92  ? 0.1370 0.1594 0.1012 -0.0200 -0.0097 0.0164  92  CYS   A N   
1842 C CA  . CYS   A 92  ? 0.1303 0.1475 0.1026 -0.0186 -0.0008 0.0154  92  CYS   A CA  
1843 C C   . CYS   A 92  ? 0.1231 0.1451 0.0978 -0.0212 0.0076  0.0162  92  CYS   A C   
1844 O O   . CYS   A 92  ? 0.1281 0.1449 0.1176 -0.0183 0.0017  0.0075  92  CYS   A O   
1845 C CB  . CYS   A 92  ? 0.1343 0.1487 0.1195 -0.0117 -0.0018 0.0105  92  CYS   A CB  
1846 S SG  . CYS   A 92  ? 0.1304 0.1338 0.1124 -0.0138 -0.0038 0.0097  92  CYS   A SG  
1852 N N   . LEU   A 93  ? 0.1232 0.1254 0.1078 -0.0145 0.0125  0.0140  93  LEU   A N   
1853 C CA  . LEU   A 93  ? 0.1148 0.1154 0.1016 -0.0094 0.0063  0.0135  93  LEU   A CA  
1854 C C   . LEU   A 93  ? 0.1106 0.1148 0.0986 -0.0047 0.0038  0.0072  93  LEU   A C   
1855 O O   . LEU   A 93  ? 0.1090 0.1260 0.1022 -0.0053 0.0012  0.0149  93  LEU   A O   
1856 C CB  . LEU   A 93  ? 0.1224 0.1227 0.1149 -0.0050 0.0001  0.0219  93  LEU   A CB  
1857 C CG  . LEU   A 93  ? 0.1298 0.1198 0.1246 -0.0067 0.0034  0.0248  93  LEU   A CG  
1858 C CD1 . LEU   A 93  ? 0.1399 0.1279 0.1429 0.0012  0.0101  0.0136  93  LEU   A CD1 
1859 C CD2 . LEU   A 93  ? 0.1451 0.1167 0.1430 -0.0031 0.0022  0.0155  93  LEU   A CD2 
1871 N N   . HIS   A 94  ? 0.1014 0.1148 0.1024 -0.0045 0.0071  0.0146  94  HIS   A N   
1872 C CA  . HIS   A 94  ? 0.1049 0.1188 0.1017 -0.0072 -0.0004 0.0133  94  HIS   A CA  
1873 C C   . HIS   A 94  ? 0.1119 0.1118 0.1093 -0.0038 0.0087  0.0099  94  HIS   A C   
1874 O O   . HIS   A 94  ? 0.1199 0.1238 0.1449 0.0001  0.0066  -0.0119 94  HIS   A O   
1875 C CB  . HIS   A 94  ? 0.1102 0.1193 0.1080 0.0006  -0.0003 0.0113  94  HIS   A CB  
1876 C CG  . HIS   A 94  ? 0.1131 0.1152 0.1020 -0.0034 -0.0019 0.0122  94  HIS   A CG  
1877 N ND1 . HIS   A 94  ? 0.1157 0.1121 0.1063 0.0012  0.0030  0.0156  94  HIS   A ND1 
1878 C CD2 . HIS   A 94  ? 0.1170 0.1261 0.1122 -0.0026 -0.0069 0.0045  94  HIS   A CD2 
1879 C CE1 . HIS   A 94  ? 0.1156 0.1213 0.1010 -0.0073 -0.0075 0.0058  94  HIS   A CE1 
1880 N NE2 . HIS   A 94  ? 0.1204 0.1224 0.1143 -0.0101 -0.0037 0.0006  94  HIS   A NE2 
1888 N N   . VAL   A 95  ? 0.1099 0.1101 0.0890 -0.0055 0.0067  -0.0013 95  VAL   A N   
1889 C CA  . VAL   A 95  ? 0.1183 0.1161 0.0960 -0.0038 0.0128  0.0072  95  VAL   A CA  
1890 C C   . VAL   A 95  ? 0.1126 0.1040 0.0848 -0.0087 0.0042  0.0076  95  VAL   A C   
1891 O O   . VAL   A 95  ? 0.1206 0.1230 0.0986 0.0067  0.0083  0.0061  95  VAL   A O   
1892 C CB  . VAL   A 95  ? 0.1186 0.1208 0.1094 -0.0082 0.0055  0.0080  95  VAL   A CB  
1893 C CG1 . VAL   A 95  ? 0.1314 0.1228 0.1246 -0.0103 -0.0025 0.0007  95  VAL   A CG1 
1894 C CG2 . VAL   A 95  ? 0.1207 0.1183 0.1141 -0.0191 0.0074  0.0110  95  VAL   A CG2 
1904 N N   . VAL   A 96  ? 0.1212 0.1113 0.0805 -0.0062 0.0071  0.0096  96  VAL   A N   
1905 C CA  . VAL   A 96  ? 0.1275 0.1142 0.1027 -0.0028 0.0112  0.0067  96  VAL   A CA  
1906 C C   . VAL   A 96  ? 0.1290 0.1229 0.1024 0.0001  0.0147  0.0120  96  VAL   A C   
1907 O O   . VAL   A 96  ? 0.1408 0.1278 0.1174 -0.0075 0.0179  -0.0044 96  VAL   A O   
1908 C CB  . VAL   A 96  ? 0.1274 0.1190 0.1066 -0.0046 0.0147  0.0094  96  VAL   A CB  
1909 C CG1 . VAL   A 96  ? 0.1341 0.1268 0.0987 -0.0057 0.0139  0.0103  96  VAL   A CG1 
1910 C CG2 . VAL   A 96  ? 0.1360 0.1277 0.1151 -0.0163 0.0196  0.0051  96  VAL   A CG2 
1920 N N   A GLY   A 97  ? 0.1285 0.1251 0.0961 -0.0069 0.0072  0.0067  97  GLY   A N   
1921 N N   B GLY   A 97  ? 0.1361 0.1290 0.1124 -0.0017 0.0061  0.0090  97  GLY   A N   
1922 C CA  A GLY   A 97  ? 0.1347 0.1386 0.0950 -0.0079 0.0001  0.0065  97  GLY   A CA  
1923 C CA  B GLY   A 97  ? 0.1459 0.1389 0.1263 -0.0036 -0.0048 0.0099  97  GLY   A CA  
1924 C C   A GLY   A 97  ? 0.1288 0.1452 0.0774 -0.0082 0.0101  0.0058  97  GLY   A C   
1925 C C   B GLY   A 97  ? 0.1515 0.1458 0.1301 -0.0036 -0.0093 0.0083  97  GLY   A C   
1926 O O   A GLY   A 97  ? 0.1346 0.1470 0.1003 -0.0096 0.0078  0.0143  97  GLY   A O   
1927 O O   B GLY   A 97  ? 0.1445 0.1447 0.1412 -0.0012 -0.0145 0.0173  97  GLY   A O   
1934 N N   A PRO   A 98  ? 0.1267 0.1466 0.0779 -0.0051 0.0047  0.0184  98  PRO   A N   
1935 N N   B PRO   A 98  ? 0.1567 0.1453 0.1202 -0.0035 -0.0102 0.0057  98  PRO   A N   
1936 C CA  A PRO   A 98  ? 0.1426 0.1746 0.0914 -0.0101 0.0060  0.0071  98  PRO   A CA  
1937 C CA  B PRO   A 98  ? 0.1643 0.1608 0.1159 -0.0009 -0.0017 -0.0021 98  PRO   A CA  
1938 C C   A PRO   A 98  ? 0.1513 0.1810 0.0988 -0.0168 0.0000  0.0258  98  PRO   A C   
1939 C C   B PRO   A 98  ? 0.1605 0.1641 0.1134 0.0043  -0.0032 0.0031  98  PRO   A C   
1940 O O   A PRO   A 98  ? 0.1495 0.1651 0.1265 -0.0129 -0.0086 0.0222  98  PRO   A O   
1941 O O   B PRO   A 98  ? 0.1503 0.1537 0.1091 0.0131  -0.0038 0.0072  98  PRO   A O   
1942 C CB  A PRO   A 98  ? 0.1552 0.1843 0.0876 0.0049  0.0016  -0.0016 98  PRO   A CB  
1943 C CB  B PRO   A 98  ? 0.1737 0.1673 0.1217 0.0019  -0.0046 -0.0046 98  PRO   A CB  
1944 C CG  A PRO   A 98  ? 0.1536 0.1763 0.0938 0.0057  0.0041  -0.0081 98  PRO   A CG  
1945 C CG  B PRO   A 98  ? 0.1701 0.1617 0.1176 -0.0007 -0.0013 -0.0104 98  PRO   A CG  
1946 C CD  A PRO   A 98  ? 0.1370 0.1550 0.0802 0.0043  0.0167  -0.0007 98  PRO   A CD  
1947 C CD  B PRO   A 98  ? 0.1621 0.1493 0.1119 -0.0038 0.0029  -0.0031 98  PRO   A CD  
1962 N N   A ASN   A 99  ? 0.1579 0.2003 0.1047 -0.0148 0.0117  0.0463  99  ASN   A N   
1963 N N   B ASN   A 99  ? 0.1650 0.1782 0.1246 0.0100  -0.0115 0.0069  99  ASN   A N   
1964 C CA  A ASN   A 99  ? 0.1774 0.2149 0.0961 -0.0124 0.0120  0.0629  99  ASN   A CA  
1965 C CA  B ASN   A 99  ? 0.1723 0.1853 0.1179 0.0115  -0.0175 0.0009  99  ASN   A CA  
1966 C C   A ASN   A 99  ? 0.1915 0.2290 0.0937 -0.0118 0.0228  0.0634  99  ASN   A C   
1967 C C   B ASN   A 99  ? 0.1846 0.1954 0.1239 0.0098  -0.0091 -0.0029 99  ASN   A C   
1968 O O   A ASN   A 99  ? 0.1941 0.2542 0.1000 -0.0009 0.0186  0.0560  99  ASN   A O   
1969 O O   B ASN   A 99  ? 0.1902 0.2090 0.1377 0.0227  -0.0115 0.0035  99  ASN   A O   
1970 C CB  A ASN   A 99  ? 0.1823 0.2033 0.1419 -0.0083 -0.0015 0.0673  99  ASN   A CB  
1971 C CB  B ASN   A 99  ? 0.1734 0.1836 0.1037 0.0083  -0.0161 0.0027  99  ASN   A CB  
1972 C CG  A ASN   A 99  ? 0.1896 0.2063 0.1739 -0.0046 -0.0044 0.0601  99  ASN   A CG  
1973 C CG  B ASN   A 99  ? 0.1770 0.1857 0.0983 0.0108  -0.0174 -0.0106 99  ASN   A CG  
1974 O OD1 A ASN   A 99  ? 0.2017 0.2133 0.1841 -0.0051 -0.0116 0.0574  99  ASN   A OD1 
1975 O OD1 B ASN   A 99  ? 0.1787 0.1936 0.0982 0.0153  -0.0151 -0.0284 99  ASN   A OD1 
1976 N ND2 A ASN   A 99  ? 0.1913 0.2053 0.1890 0.0035  -0.0007 0.0593  99  ASN   A ND2 
1977 N ND2 B ASN   A 99  ? 0.1806 0.1812 0.1091 0.0135  -0.0152 -0.0026 99  ASN   A ND2 
1990 N N   A VAL   A 100 ? 0.2055 0.2501 0.0934 -0.0187 0.0067  0.0644  100 VAL   A N   
1991 N N   B VAL   A 100 ? 0.1922 0.1887 0.1117 -0.0021 -0.0202 -0.0213 100 VAL   A N   
1992 C CA  A VAL   A 100 ? 0.2319 0.2728 0.1253 -0.0165 0.0011  0.0546  100 VAL   A CA  
1993 C CA  B VAL   A 100 ? 0.2025 0.1856 0.1237 -0.0089 -0.0208 -0.0226 100 VAL   A CA  
1994 C C   A VAL   A 100 ? 0.2410 0.2892 0.1217 -0.0180 -0.0045 0.0677  100 VAL   A C   
1995 C C   B VAL   A 100 ? 0.1928 0.1800 0.0892 -0.0031 -0.0149 -0.0145 100 VAL   A C   
1996 O O   A VAL   A 100 ? 0.2478 0.2982 0.1536 -0.0145 0.0089  0.0649  100 VAL   A O   
1997 O O   B VAL   A 100 ? 0.2010 0.1731 0.1069 0.0011  -0.0057 -0.0114 100 VAL   A O   
1998 C CB  A VAL   A 100 ? 0.2520 0.2788 0.1619 -0.0207 -0.0090 0.0412  100 VAL   A CB  
1999 C CB  B VAL   A 100 ? 0.2221 0.1875 0.1666 -0.0236 -0.0255 -0.0308 100 VAL   A CB  
2000 C CG1 A VAL   A 100 ? 0.2532 0.2860 0.1811 -0.0242 -0.0024 0.0418  100 VAL   A CG1 
2001 C CG1 B VAL   A 100 ? 0.2239 0.1904 0.1830 -0.0237 -0.0179 -0.0353 100 VAL   A CG1 
2002 C CG2 A VAL   A 100 ? 0.2648 0.2831 0.1821 -0.0236 -0.0106 0.0275  100 VAL   A CG2 
2003 C CG2 B VAL   A 100 ? 0.2363 0.1913 0.1884 -0.0311 -0.0250 -0.0272 100 VAL   A CG2 
2022 N N   A ASN   A 101 ? 0.2472 0.2952 0.1410 -0.0223 -0.0066 0.0845  101 ASN   A N   
2023 N N   B ASN   A 101 ? 0.1765 0.1849 0.0757 -0.0036 -0.0009 -0.0092 101 ASN   A N   
2024 C CA  A ASN   A 101 ? 0.2651 0.3033 0.1670 -0.0242 -0.0040 0.0969  101 ASN   A CA  
2025 C CA  B ASN   A 101 ? 0.1756 0.1944 0.0777 -0.0062 -0.0097 0.0018  101 ASN   A CA  
2026 C C   A ASN   A 101 ? 0.2906 0.3281 0.1870 -0.0305 0.0111  0.1154  101 ASN   A C   
2027 C C   B ASN   A 101 ? 0.1833 0.2125 0.0940 -0.0207 0.0020  0.0231  101 ASN   A C   
2028 O O   A ASN   A 101 ? 0.3069 0.3344 0.2195 -0.0255 0.0106  0.1099  101 ASN   A O   
2029 O O   B ASN   A 101 ? 0.1979 0.2201 0.1412 -0.0183 0.0032  0.0179  101 ASN   A O   
2030 C CB  A ASN   A 101 ? 0.2556 0.2864 0.1722 -0.0193 -0.0112 0.0855  101 ASN   A CB  
2031 C CB  B ASN   A 101 ? 0.1732 0.1974 0.0952 -0.0011 -0.0229 -0.0060 101 ASN   A CB  
2032 C CG  A ASN   A 101 ? 0.2482 0.2714 0.1781 -0.0198 -0.0155 0.0633  101 ASN   A CG  
2033 C CG  B ASN   A 101 ? 0.1693 0.2021 0.1274 0.0056  -0.0376 -0.0089 101 ASN   A CG  
2034 O OD1 A ASN   A 101 ? 0.2422 0.2742 0.1877 -0.0114 -0.0081 0.0343  101 ASN   A OD1 
2035 O OD1 B ASN   A 101 ? 0.1709 0.2172 0.1503 0.0136  -0.0470 -0.0158 101 ASN   A OD1 
2036 N ND2 A ASN   A 101 ? 0.2515 0.2581 0.1750 -0.0295 -0.0153 0.0696  101 ASN   A ND2 
2037 N ND2 B ASN   A 101 ? 0.1630 0.1975 0.1275 0.0053  -0.0294 -0.0064 101 ASN   A ND2 
2050 N N   A LYS   A 102 ? 0.2962 0.3476 0.2198 -0.0390 0.0205  0.1076  102 LYS   A N   
2051 N N   B LYS   A 102 ? 0.1779 0.2293 0.0931 -0.0380 0.0133  0.0195  102 LYS   A N   
2052 C CA  A LYS   A 102 ? 0.3082 0.3669 0.2290 -0.0436 0.0205  0.0910  102 LYS   A CA  
2053 C CA  B LYS   A 102 ? 0.1916 0.2539 0.1152 -0.0406 0.0223  0.0279  102 LYS   A CA  
2054 C C   A LYS   A 102 ? 0.3147 0.3798 0.2124 -0.0376 0.0285  0.0850  102 LYS   A C   
2055 C C   B LYS   A 102 ? 0.2029 0.2721 0.1156 -0.0267 0.0450  0.0188  102 LYS   A C   
2056 O O   A LYS   A 102 ? 0.3174 0.3857 0.2175 -0.0341 0.0383  0.0900  102 LYS   A O   
2057 O O   B LYS   A 102 ? 0.2058 0.2739 0.1277 -0.0145 0.0520  0.0164  102 LYS   A O   
2058 C CB  A LYS   A 102 ? 0.3159 0.3739 0.2616 -0.0539 0.0105  0.0763  102 LYS   A CB  
2059 C CB  B LYS   A 102 ? 0.1989 0.2567 0.1364 -0.0482 0.0063  0.0303  102 LYS   A CB  
2060 C CG  A LYS   A 102 ? 0.3232 0.3789 0.2781 -0.0631 0.0020  0.0621  102 LYS   A CG  
2061 C CG  B LYS   A 102 ? 0.2096 0.2583 0.1488 -0.0573 -0.0095 0.0319  102 LYS   A CG  
2062 C CD  A LYS   A 102 ? 0.3337 0.3864 0.2982 -0.0680 -0.0025 0.0442  102 LYS   A CD  
2063 C CD  B LYS   A 102 ? 0.2211 0.2631 0.1669 -0.0634 -0.0203 0.0286  102 LYS   A CD  
2064 C CE  A LYS   A 102 ? 0.3429 0.3924 0.3148 -0.0700 -0.0061 0.0315  102 LYS   A CE  
2065 C CE  B LYS   A 102 ? 0.2314 0.2654 0.1780 -0.0637 -0.0284 0.0267  102 LYS   A CE  
2066 N NZ  A LYS   A 102 ? 0.3476 0.3947 0.3229 -0.0731 -0.0056 0.0228  102 LYS   A NZ  
2067 N NZ  B LYS   A 102 ? 0.2386 0.2652 0.1789 -0.0644 -0.0347 0.0249  102 LYS   A NZ  
2094 N N   A GLY   A 103 ? 0.3198 0.3884 0.2172 -0.0314 0.0189  0.0575  103 GLY   A N   
2095 N N   B GLY   A 103 ? 0.2172 0.2911 0.1287 -0.0207 0.0443  -0.0070 103 GLY   A N   
2096 C CA  A GLY   A 103 ? 0.3221 0.3918 0.1975 -0.0288 0.0202  0.0398  103 GLY   A CA  
2097 C CA  B GLY   A 103 ? 0.2294 0.3056 0.1485 -0.0090 0.0490  -0.0238 103 GLY   A CA  
2098 C C   A GLY   A 103 ? 0.3189 0.3945 0.1844 -0.0315 0.0264  0.0255  103 GLY   A C   
2099 C C   B GLY   A 103 ? 0.2386 0.3167 0.1699 -0.0024 0.0628  -0.0400 103 GLY   A C   
2100 O O   A GLY   A 103 ? 0.3265 0.3989 0.2002 -0.0326 0.0194  0.0108  103 GLY   A O   
2101 O O   B GLY   A 103 ? 0.2468 0.3192 0.1875 -0.0006 0.0681  -0.0490 103 GLY   A O   
2108 N N   A GLU   A 104 ? 0.3069 0.3889 0.1460 -0.0345 0.0304  0.0224  104 GLU   A N   
2109 N N   B GLU   A 104 ? 0.2406 0.3265 0.1700 -0.0002 0.0606  -0.0384 104 GLU   A N   
2110 C CA  A GLU   A 104 ? 0.2886 0.3802 0.1230 -0.0441 0.0286  0.0091  104 GLU   A CA  
2111 C CA  B GLU   A 104 ? 0.2368 0.3328 0.1901 -0.0004 0.0585  -0.0368 104 GLU   A CA  
2112 C C   A GLU   A 104 ? 0.2925 0.3892 0.1151 -0.0467 0.0411  -0.0059 104 GLU   A C   
2113 C C   B GLU   A 104 ? 0.2572 0.3516 0.2107 -0.0080 0.0482  -0.0456 104 GLU   A C   
2114 O O   A GLU   A 104 ? 0.2897 0.3894 0.1487 -0.0455 0.0361  -0.0155 104 GLU   A O   
2115 O O   B GLU   A 104 ? 0.2592 0.3566 0.2211 -0.0139 0.0358  -0.0589 104 GLU   A O   
2116 C CB  A GLU   A 104 ? 0.2644 0.3624 0.1146 -0.0505 0.0218  0.0249  104 GLU   A CB  
2117 C CB  B GLU   A 104 ? 0.2129 0.3171 0.1908 0.0012  0.0592  -0.0220 104 GLU   A CB  
2118 C CG  A GLU   A 104 ? 0.2507 0.3446 0.1253 -0.0536 0.0161  0.0403  104 GLU   A CG  
2119 C CG  B GLU   A 104 ? 0.1947 0.3017 0.2020 0.0035  0.0529  -0.0121 104 GLU   A CG  
2120 C CD  A GLU   A 104 ? 0.2321 0.3245 0.1161 -0.0569 0.0188  0.0493  104 GLU   A CD  
2121 C CD  B GLU   A 104 ? 0.1769 0.2847 0.2031 0.0093  0.0516  -0.0029 104 GLU   A CD  
2122 O OE1 A GLU   A 104 ? 0.2252 0.3161 0.1016 -0.0533 0.0020  0.0534  104 GLU   A OE1 
2123 O OE1 B GLU   A 104 ? 0.1566 0.2684 0.1756 0.0158  0.0504  -0.0111 104 GLU   A OE1 
2124 O OE2 A GLU   A 104 ? 0.2314 0.3145 0.1281 -0.0610 0.0206  0.0517  104 GLU   A OE2 
2125 O OE2 B GLU   A 104 ? 0.1881 0.2877 0.2255 0.0081  0.0495  0.0046  104 GLU   A OE2 
2138 N N   A ASP   A 105 ? 0.2995 0.3962 0.1265 -0.0495 0.0458  -0.0217 105 ASP   A N   
2139 N N   B ASP   A 105 ? 0.2727 0.3623 0.2195 -0.0082 0.0426  -0.0466 105 ASP   A N   
2140 C CA  A ASP   A 105 ? 0.2995 0.3980 0.1773 -0.0445 0.0501  -0.0437 105 ASP   A CA  
2141 C CA  B ASP   A 105 ? 0.2864 0.3716 0.2363 -0.0120 0.0344  -0.0528 105 ASP   A CA  
2142 C C   A ASP   A 105 ? 0.2687 0.3789 0.1437 -0.0537 0.0344  -0.0525 105 ASP   A C   
2143 C C   B ASP   A 105 ? 0.2778 0.3648 0.2173 -0.0175 0.0266  -0.0551 105 ASP   A C   
2144 O O   A ASP   A 105 ? 0.2458 0.3450 0.1189 -0.0470 0.0268  -0.0725 105 ASP   A O   
2145 O O   B ASP   A 105 ? 0.2741 0.3630 0.1995 -0.0182 0.0311  -0.0617 105 ASP   A O   
2146 C CB  A ASP   A 105 ? 0.3254 0.4205 0.2537 -0.0331 0.0622  -0.0496 105 ASP   A CB  
2147 C CB  B ASP   A 105 ? 0.3036 0.3849 0.2739 -0.0097 0.0295  -0.0600 105 ASP   A CB  
2148 C CG  A ASP   A 105 ? 0.3481 0.4366 0.3246 -0.0198 0.0612  -0.0640 105 ASP   A CG  
2149 C CG  B ASP   A 105 ? 0.3166 0.3946 0.3050 -0.0095 0.0215  -0.0722 105 ASP   A CG  
2150 O OD1 A ASP   A 105 ? 0.3561 0.4444 0.3463 -0.0179 0.0573  -0.0732 105 ASP   A OD1 
2151 O OD1 B ASP   A 105 ? 0.3220 0.3997 0.3073 -0.0123 0.0184  -0.0852 105 ASP   A OD1 
2152 O OD2 A ASP   A 105 ? 0.3565 0.4420 0.3595 -0.0161 0.0677  -0.0636 105 ASP   A OD2 
2153 O OD2 B ASP   A 105 ? 0.3202 0.3976 0.3282 -0.0078 0.0188  -0.0719 105 ASP   A OD2 
2162 N N   A ILE   A 106 ? 0.2561 0.3815 0.1700 -0.0640 0.0169  -0.0519 106 ILE   A N   
2163 N N   B ILE   A 106 ? 0.2719 0.3607 0.2296 -0.0236 0.0081  -0.0520 106 ILE   A N   
2164 C CA  A ILE   A 106 ? 0.2311 0.3717 0.1901 -0.0794 -0.0049 -0.0692 106 ILE   A CA  
2165 C CA  B ILE   A 106 ? 0.2570 0.3463 0.2378 -0.0290 -0.0055 -0.0606 106 ILE   A CA  
2166 C C   A ILE   A 106 ? 0.2142 0.3506 0.2085 -0.0947 0.0002  -0.0898 106 ILE   A C   
2167 C C   B ILE   A 106 ? 0.2447 0.3224 0.2351 -0.0326 0.0033  -0.0949 106 ILE   A C   
2168 O O   A ILE   A 106 ? 0.1911 0.3448 0.2156 -0.1003 0.0128  -0.0892 106 ILE   A O   
2169 O O   B ILE   A 106 ? 0.2322 0.3103 0.2182 -0.0348 0.0038  -0.1086 106 ILE   A O   
2170 C CB  A ILE   A 106 ? 0.2322 0.3795 0.2371 -0.0692 -0.0267 -0.0470 106 ILE   A CB  
2171 C CB  B ILE   A 106 ? 0.2581 0.3536 0.2616 -0.0267 -0.0229 -0.0311 106 ILE   A CB  
2172 C CG1 A ILE   A 106 ? 0.2225 0.3785 0.2713 -0.0585 -0.0258 -0.0240 106 ILE   A CG1 
2173 C CG1 B ILE   A 106 ? 0.2553 0.3512 0.2835 -0.0256 -0.0263 -0.0123 106 ILE   A CG1 
2174 C CG2 A ILE   A 106 ? 0.2401 0.3842 0.2571 -0.0674 -0.0329 -0.0431 106 ILE   A CG2 
2175 C CG2 B ILE   A 106 ? 0.2617 0.3591 0.2716 -0.0255 -0.0289 -0.0262 106 ILE   A CG2 
2176 C CD1 A ILE   A 106 ? 0.2213 0.3767 0.2835 -0.0478 -0.0162 -0.0129 106 ILE   A CD1 
2177 C CD1 B ILE   A 106 ? 0.2569 0.3490 0.2948 -0.0226 -0.0233 -0.0016 106 ILE   A CD1 
2200 N N   A GLN   A 107 ? 0.2316 0.3339 0.2276 -0.0931 0.0067  -0.1089 107 GLN   A N   
2201 N N   B GLN   A 107 ? 0.2501 0.3122 0.2630 -0.0296 0.0167  -0.1053 107 GLN   A N   
2202 C CA  A GLN   A 107 ? 0.2515 0.3183 0.2996 -0.0746 0.0352  -0.1038 107 GLN   A CA  
2203 C CA  B GLN   A 107 ? 0.2531 0.2973 0.3029 -0.0184 0.0332  -0.0982 107 GLN   A CA  
2204 C C   A GLN   A 107 ? 0.2292 0.2739 0.2898 -0.0666 0.0579  -0.0774 107 GLN   A C   
2205 C C   B GLN   A 107 ? 0.2282 0.2615 0.2898 -0.0101 0.0525  -0.0745 107 GLN   A C   
2206 O O   A GLN   A 107 ? 0.2408 0.2738 0.3604 -0.0621 0.0680  -0.0684 107 GLN   A O   
2207 O O   B GLN   A 107 ? 0.2283 0.2595 0.3398 -0.0031 0.0651  -0.0742 107 GLN   A O   
2208 C CB  A GLN   A 107 ? 0.2856 0.3429 0.3902 -0.0714 0.0285  -0.1094 107 GLN   A CB  
2209 C CB  B GLN   A 107 ? 0.2780 0.3170 0.3730 -0.0193 0.0200  -0.0948 107 GLN   A CB  
2210 C CG  A GLN   A 107 ? 0.3235 0.3680 0.4846 -0.0632 0.0213  -0.1046 107 GLN   A CG  
2211 C CG  B GLN   A 107 ? 0.3023 0.3358 0.4447 -0.0176 0.0062  -0.0808 107 GLN   A CG  
2212 C CD  A GLN   A 107 ? 0.3542 0.3871 0.5651 -0.0551 0.0204  -0.0926 107 GLN   A CD  
2213 C CD  B GLN   A 107 ? 0.3210 0.3492 0.5038 -0.0153 -0.0030 -0.0644 107 GLN   A CD  
2214 O OE1 A GLN   A 107 ? 0.3609 0.3916 0.5977 -0.0512 0.0217  -0.0914 107 GLN   A OE1 
2215 O OE1 B GLN   A 107 ? 0.3301 0.3536 0.5298 -0.0140 -0.0053 -0.0577 107 GLN   A OE1 
2216 N NE2 A GLN   A 107 ? 0.3606 0.3938 0.5936 -0.0528 0.0173  -0.0889 107 GLN   A NE2 
2217 N NE2 B GLN   A 107 ? 0.3253 0.3535 0.5217 -0.0148 -0.0044 -0.0598 107 GLN   A NE2 
2234 N N   A LEU   A 108 ? 0.1959 0.2244 0.2232 -0.0657 0.0527  -0.0682 108 LEU   A N   
2235 N N   B LEU   A 108 ? 0.2043 0.2208 0.2322 -0.0043 0.0554  -0.0549 108 LEU   A N   
2236 C CA  A LEU   A 108 ? 0.1772 0.1822 0.1978 -0.0354 0.0458  -0.0321 108 LEU   A CA  
2237 C CA  B LEU   A 108 ? 0.1838 0.1837 0.1981 0.0122  0.0472  -0.0190 108 LEU   A CA  
2238 C C   A LEU   A 108 ? 0.1573 0.1463 0.1822 -0.0158 0.0413  -0.0003 108 LEU   A C   
2239 C C   B LEU   A 108 ? 0.1627 0.1546 0.1809 0.0117  0.0359  -0.0003 108 LEU   A C   
2240 O O   A LEU   A 108 ? 0.1526 0.1423 0.1931 -0.0110 0.0509  0.0082  108 LEU   A O   
2241 O O   B LEU   A 108 ? 0.1599 0.1514 0.1886 0.0183  0.0352  0.0029  108 LEU   A O   
2242 C CB  A LEU   A 108 ? 0.1746 0.1860 0.1851 -0.0371 0.0500  -0.0226 108 LEU   A CB  
2243 C CB  B LEU   A 108 ? 0.1812 0.1825 0.1825 0.0220  0.0509  -0.0036 108 LEU   A CB  
2244 C CG  A LEU   A 108 ? 0.1794 0.2024 0.2092 -0.0340 0.0510  -0.0210 108 LEU   A CG  
2245 C CG  B LEU   A 108 ? 0.1845 0.1870 0.1862 0.0292  0.0499  0.0099  108 LEU   A CG  
2246 C CD1 A LEU   A 108 ? 0.1828 0.2042 0.1985 -0.0324 0.0551  -0.0175 108 LEU   A CD1 
2247 C CD1 B LEU   A 108 ? 0.1875 0.1888 0.1706 0.0320  0.0474  0.0151  108 LEU   A CD1 
2248 C CD2 A LEU   A 108 ? 0.1862 0.2082 0.2423 -0.0310 0.0511  -0.0067 108 LEU   A CD2 
2249 C CD2 B LEU   A 108 ? 0.1881 0.1900 0.2115 0.0307  0.0467  0.0225  108 LEU   A CD2 
2272 N N   . LEU   A 109 ? 0.1457 0.1460 0.1717 0.0032  0.0303  0.0059  109 LEU   A N   
2273 C CA  . LEU   A 109 ? 0.1371 0.1335 0.1515 -0.0017 0.0112  0.0090  109 LEU   A CA  
2274 C C   . LEU   A 109 ? 0.1310 0.1258 0.1443 -0.0024 0.0181  0.0009  109 LEU   A C   
2275 O O   . LEU   A 109 ? 0.1394 0.1183 0.1649 -0.0016 0.0040  -0.0069 109 LEU   A O   
2276 C CB  . LEU   A 109 ? 0.1455 0.1389 0.1601 0.0090  0.0059  0.0222  109 LEU   A CB  
2277 C CG  . LEU   A 109 ? 0.1371 0.1441 0.1625 0.0058  0.0107  0.0248  109 LEU   A CG  
2278 C CD1 . LEU   A 109 ? 0.1368 0.1366 0.1796 0.0061  0.0180  0.0078  109 LEU   A CD1 
2279 C CD2 . LEU   A 109 ? 0.1343 0.1649 0.1763 0.0012  0.0076  0.0244  109 LEU   A CD2 
2292 N N   . LYS   A 110 ? 0.1289 0.1304 0.1371 0.0002  0.0016  -0.0018 110 LYS   A N   
2293 C CA  . LYS   A 110 ? 0.1333 0.1213 0.1488 -0.0068 -0.0019 0.0015  110 LYS   A CA  
2294 C C   . LYS   A 110 ? 0.1356 0.1141 0.1281 -0.0099 0.0073  -0.0123 110 LYS   A C   
2295 O O   . LYS   A 110 ? 0.1273 0.1175 0.1399 -0.0111 0.0099  -0.0041 110 LYS   A O   
2296 C CB  . LYS   A 110 ? 0.1374 0.1241 0.1791 0.0002  -0.0100 -0.0057 110 LYS   A CB  
2297 C CG  . LYS   A 110 ? 0.1387 0.1225 0.1869 0.0050  -0.0057 -0.0089 110 LYS   A CG  
2298 C CD  . LYS   A 110 ? 0.1404 0.1367 0.1828 -0.0050 0.0044  -0.0134 110 LYS   A CD  
2299 C CE  . LYS   A 110 ? 0.1521 0.1430 0.1997 -0.0043 0.0073  -0.0137 110 LYS   A CE  
2300 N NZ  . LYS   A 110 ? 0.1581 0.1342 0.2120 -0.0201 0.0153  -0.0060 110 LYS   A NZ  
2314 N N   . SER   A 111 ? 0.1348 0.1122 0.1541 -0.0028 0.0025  0.0031  111 SER   A N   
2315 C CA  . SER   A 111 ? 0.1289 0.1194 0.1530 -0.0030 0.0076  0.0043  111 SER   A CA  
2316 C C   . SER   A 111 ? 0.1248 0.1157 0.1445 -0.0059 0.0099  -0.0003 111 SER   A C   
2317 O O   . SER   A 111 ? 0.1304 0.1130 0.1617 -0.0076 0.0060  -0.0010 111 SER   A O   
2318 C CB  . SER   A 111 ? 0.1399 0.1453 0.1490 0.0008  0.0129  -0.0115 111 SER   A CB  
2319 O OG  . SER   A 111 ? 0.1840 0.1703 0.1692 0.0053  0.0229  -0.0106 111 SER   A OG  
2325 N N   . ALA   A 112 ? 0.1277 0.1134 0.1478 0.0001  0.0127  0.0009  112 ALA   A N   
2326 C CA  . ALA   A 112 ? 0.1314 0.1106 0.1444 -0.0051 0.0197  -0.0057 112 ALA   A CA  
2327 C C   . ALA   A 112 ? 0.1240 0.1097 0.1370 0.0043  0.0129  -0.0030 112 ALA   A C   
2328 O O   . ALA   A 112 ? 0.1234 0.1155 0.1437 -0.0134 0.0111  0.0018  112 ALA   A O   
2329 C CB  . ALA   A 112 ? 0.1354 0.1129 0.1668 -0.0073 0.0094  0.0026  112 ALA   A CB  
2335 N N   . TYR   A 113 ? 0.1172 0.1108 0.1478 -0.0037 0.0103  0.0041  113 TYR   A N   
2336 C CA  . TYR   A 113 ? 0.1158 0.1059 0.1526 -0.0005 0.0171  0.0079  113 TYR   A CA  
2337 C C   . TYR   A 113 ? 0.1181 0.1078 0.1387 -0.0072 0.0128  0.0098  113 TYR   A C   
2338 O O   . TYR   A 113 ? 0.1171 0.1162 0.1531 -0.0036 0.0145  0.0057  113 TYR   A O   
2339 C CB  . TYR   A 113 ? 0.1205 0.1199 0.1454 -0.0080 0.0063  0.0151  113 TYR   A CB  
2340 C CG  . TYR   A 113 ? 0.1180 0.1170 0.1324 -0.0107 0.0112  0.0129  113 TYR   A CG  
2341 C CD1 . TYR   A 113 ? 0.1238 0.1243 0.1332 -0.0015 0.0122  0.0146  113 TYR   A CD1 
2342 C CD2 . TYR   A 113 ? 0.1237 0.1245 0.1299 -0.0114 0.0028  0.0131  113 TYR   A CD2 
2343 C CE1 . TYR   A 113 ? 0.1238 0.1304 0.1262 -0.0041 0.0123  0.0150  113 TYR   A CE1 
2344 C CE2 . TYR   A 113 ? 0.1202 0.1265 0.1353 -0.0123 -0.0019 0.0149  113 TYR   A CE2 
2345 C CZ  . TYR   A 113 ? 0.1219 0.1263 0.1291 -0.0016 0.0129  0.0163  113 TYR   A CZ  
2346 O OH  . TYR   A 113 ? 0.1197 0.1367 0.1489 0.0060  0.0133  0.0200  113 TYR   A OH  
2356 N N   . GLU   A 114 ? 0.1220 0.1102 0.1447 -0.0020 0.0149  0.0070  114 GLU   A N   
2357 C CA  . GLU   A 114 ? 0.1250 0.1035 0.1522 0.0047  0.0062  0.0038  114 GLU   A CA  
2358 C C   . GLU   A 114 ? 0.1101 0.1127 0.1447 0.0071  0.0141  0.0047  114 GLU   A C   
2359 O O   . GLU   A 114 ? 0.1204 0.1146 0.1472 0.0020  0.0043  0.0093  114 GLU   A O   
2360 C CB  . GLU   A 114 ? 0.1231 0.1137 0.1478 -0.0061 0.0026  0.0079  114 GLU   A CB  
2361 C CG  . GLU   A 114 ? 0.1299 0.1181 0.1482 0.0005  0.0121  -0.0015 114 GLU   A CG  
2362 C CD  . GLU   A 114 ? 0.1385 0.1183 0.1584 -0.0090 0.0061  0.0013  114 GLU   A CD  
2363 O OE1 . GLU   A 114 ? 0.1404 0.1082 0.1729 -0.0062 0.0190  -0.0032 114 GLU   A OE1 
2364 O OE2 . GLU   A 114 ? 0.1549 0.1237 0.1811 -0.0123 0.0091  -0.0150 114 GLU   A OE2 
2371 N N   . ASN   A 115 ? 0.1186 0.1134 0.1317 -0.0015 0.0078  0.0046  115 ASN   A N   
2372 C CA  . ASN   A 115 ? 0.1199 0.1194 0.1395 -0.0095 0.0094  0.0119  115 ASN   A CA  
2373 C C   . ASN   A 115 ? 0.1197 0.1183 0.1253 -0.0084 0.0030  0.0102  115 ASN   A C   
2374 O O   . ASN   A 115 ? 0.1227 0.1288 0.1422 -0.0067 0.0076  0.0156  115 ASN   A O   
2375 C CB  . ASN   A 115 ? 0.1252 0.1223 0.1301 -0.0175 0.0125  -0.0008 115 ASN   A CB  
2376 C CG  . ASN   A 115 ? 0.1263 0.1481 0.1457 -0.0158 0.0238  0.0089  115 ASN   A CG  
2377 O OD1 . ASN   A 115 ? 0.1326 0.2457 0.1685 -0.0194 0.0266  0.0207  115 ASN   A OD1 
2378 N ND2 . ASN   A 115 ? 0.1278 0.1306 0.1441 -0.0091 0.0282  0.0118  115 ASN   A ND2 
2385 N N   . PHE   A 116 ? 0.1167 0.1229 0.1416 -0.0037 0.0076  0.0165  116 PHE   A N   
2386 C CA  . PHE   A 116 ? 0.1158 0.1303 0.1272 -0.0042 0.0134  0.0131  116 PHE   A CA  
2387 C C   . PHE   A 116 ? 0.1096 0.1366 0.1351 -0.0064 0.0200  0.0177  116 PHE   A C   
2388 O O   . PHE   A 116 ? 0.1259 0.1358 0.1484 0.0008  0.0192  0.0265  116 PHE   A O   
2389 C CB  . PHE   A 116 ? 0.1226 0.1251 0.1311 -0.0069 0.0165  0.0093  116 PHE   A CB  
2390 C CG  . PHE   A 116 ? 0.1181 0.1233 0.1209 -0.0097 0.0204  0.0045  116 PHE   A CG  
2391 C CD1 . PHE   A 116 ? 0.1263 0.1236 0.1212 -0.0086 0.0176  0.0079  116 PHE   A CD1 
2392 C CD2 . PHE   A 116 ? 0.1211 0.1268 0.1430 -0.0056 0.0194  0.0051  116 PHE   A CD2 
2393 C CE1 . PHE   A 116 ? 0.1241 0.1149 0.1331 -0.0152 0.0112  0.0090  116 PHE   A CE1 
2394 C CE2 . PHE   A 116 ? 0.1229 0.1232 0.1484 0.0020  0.0193  0.0062  116 PHE   A CE2 
2395 C CZ  . PHE   A 116 ? 0.1290 0.1111 0.1321 0.0012  0.0029  0.0062  116 PHE   A CZ  
2405 N N   . ASN   A 117 ? 0.1143 0.1254 0.1567 0.0003  0.0165  0.0188  117 ASN   A N   
2406 C CA  . ASN   A 117 ? 0.1165 0.1273 0.1621 -0.0010 0.0217  0.0282  117 ASN   A CA  
2407 C C   . ASN   A 117 ? 0.1139 0.1370 0.1651 -0.0030 0.0120  0.0198  117 ASN   A C   
2408 O O   . ASN   A 117 ? 0.1321 0.1353 0.1827 -0.0058 -0.0091 0.0324  117 ASN   A O   
2409 C CB  . ASN   A 117 ? 0.1207 0.1230 0.1645 -0.0009 0.0161  0.0276  117 ASN   A CB  
2410 C CG  . ASN   A 117 ? 0.1226 0.1211 0.1656 -0.0052 0.0193  0.0285  117 ASN   A CG  
2411 O OD1 . ASN   A 117 ? 0.1254 0.1390 0.1705 -0.0144 0.0147  0.0126  117 ASN   A OD1 
2412 N ND2 . ASN   A 117 ? 0.1209 0.1195 0.1686 0.0004  0.0163  0.0197  117 ASN   A ND2 
2419 N N   . GLN   A 118 ? 0.1114 0.1365 0.1693 -0.0118 -0.0004 0.0268  118 GLN   A N   
2420 C CA  . GLN   A 118 ? 0.1264 0.1469 0.1602 -0.0080 -0.0030 0.0293  118 GLN   A CA  
2421 C C   . GLN   A 118 ? 0.1279 0.1428 0.1540 -0.0096 -0.0032 0.0300  118 GLN   A C   
2422 O O   . GLN   A 118 ? 0.1337 0.1749 0.1847 -0.0050 -0.0117 0.0112  118 GLN   A O   
2423 C CB  . GLN   A 118 ? 0.1219 0.1433 0.1721 -0.0043 0.0122  0.0251  118 GLN   A CB  
2424 C CG  . GLN   A 118 ? 0.1190 0.1445 0.1798 -0.0048 0.0109  0.0245  118 GLN   A CG  
2425 C CD  . GLN   A 118 ? 0.1244 0.1563 0.1883 -0.0024 0.0068  0.0130  118 GLN   A CD  
2426 O OE1 . GLN   A 118 ? 0.1329 0.1645 0.2009 0.0097  0.0029  0.0087  118 GLN   A OE1 
2427 N NE2 . GLN   A 118 ? 0.1320 0.1538 0.1847 0.0036  0.0051  0.0219  118 GLN   A NE2 
2436 N N   . HIS   A 119 ? 0.1290 0.1427 0.1491 -0.0106 0.0036  0.0301  119 HIS   A N   
2437 C CA  . HIS   A 119 ? 0.1308 0.1566 0.1467 -0.0095 0.0038  0.0327  119 HIS   A CA  
2438 C C   . HIS   A 119 ? 0.1416 0.1638 0.1471 -0.0060 0.0028  0.0390  119 HIS   A C   
2439 O O   . HIS   A 119 ? 0.1460 0.1697 0.1488 -0.0208 -0.0009 0.0393  119 HIS   A O   
2440 C CB  . HIS   A 119 ? 0.1377 0.1519 0.1660 -0.0052 0.0183  0.0311  119 HIS   A CB  
2441 C CG  . HIS   A 119 ? 0.1434 0.1536 0.2169 0.0052  0.0166  0.0412  119 HIS   A CG  
2442 N ND1 . HIS   A 119 ? 0.1579 0.1716 0.2732 -0.0072 0.0135  0.0260  119 HIS   A ND1 
2443 C CD2 . HIS   A 119 ? 0.1572 0.1547 0.2340 0.0132  0.0331  0.0636  119 HIS   A CD2 
2444 C CE1 . HIS   A 119 ? 0.1569 0.1666 0.2873 -0.0156 0.0278  0.0432  119 HIS   A CE1 
2445 N NE2 . HIS   A 119 ? 0.1701 0.1600 0.2799 -0.0006 0.0427  0.0674  119 HIS   A NE2 
2453 N N   . GLU   A 120 ? 0.1487 0.1800 0.1566 -0.0076 -0.0037 0.0595  120 GLU   A N   
2454 C CA  . GLU   A 120 ? 0.1746 0.2088 0.1810 0.0011  -0.0011 0.0955  120 GLU   A CA  
2455 C C   . GLU   A 120 ? 0.1550 0.1920 0.1578 -0.0104 0.0023  0.0817  120 GLU   A C   
2456 O O   . GLU   A 120 ? 0.1564 0.1851 0.1740 -0.0198 0.0017  0.0762  120 GLU   A O   
2457 C CB  . GLU   A 120 ? 0.2439 0.2810 0.2510 0.0142  0.0047  0.1472  120 GLU   A CB  
2458 C CG  . GLU   A 120 ? 0.3366 0.3511 0.3756 0.0270  -0.0034 0.1562  120 GLU   A CG  
2459 C CD  . GLU   A 120 ? 0.4219 0.4204 0.5086 0.0361  0.0030  0.1417  120 GLU   A CD  
2460 O OE1 . GLU   A 120 ? 0.4487 0.4428 0.5397 0.0377  0.0051  0.1338  120 GLU   A OE1 
2461 O OE2 . GLU   A 120 ? 0.4627 0.4627 0.5667 0.0399  0.0043  0.1379  120 GLU   A OE2 
2468 N N   . VAL   A 121 ? 0.1482 0.1933 0.1325 -0.0113 0.0085  0.0581  121 VAL   A N   
2469 C CA  . VAL   A 121 ? 0.1582 0.2017 0.1201 -0.0146 0.0167  0.0534  121 VAL   A CA  
2470 C C   . VAL   A 121 ? 0.1490 0.1793 0.1058 -0.0251 0.0070  0.0412  121 VAL   A C   
2471 O O   . VAL   A 121 ? 0.1534 0.1842 0.1300 -0.0327 -0.0025 0.0338  121 VAL   A O   
2472 C CB  . VAL   A 121 ? 0.1913 0.2412 0.1657 0.0029  0.0252  0.0674  121 VAL   A CB  
2473 C CG1 . VAL   A 121 ? 0.1979 0.2576 0.1680 0.0130  0.0331  0.0739  121 VAL   A CG1 
2474 C CG2 . VAL   A 121 ? 0.2117 0.2553 0.2028 -0.0051 0.0191  0.0560  121 VAL   A CG2 
2484 N N   . LEU   A 122 ? 0.1370 0.1607 0.1177 -0.0221 0.0027  0.0319  122 LEU   A N   
2485 C CA  . LEU   A 122 ? 0.1450 0.1459 0.1149 -0.0215 0.0168  0.0260  122 LEU   A CA  
2486 C C   . LEU   A 122 ? 0.1407 0.1413 0.1200 -0.0247 0.0080  0.0251  122 LEU   A C   
2487 O O   . LEU   A 122 ? 0.1405 0.1603 0.1527 -0.0308 0.0013  0.0272  122 LEU   A O   
2488 C CB  . LEU   A 122 ? 0.1566 0.1507 0.1495 -0.0109 0.0109  0.0417  122 LEU   A CB  
2489 C CG  . LEU   A 122 ? 0.1587 0.1549 0.1423 -0.0113 0.0176  0.0291  122 LEU   A CG  
2490 C CD1 . LEU   A 122 ? 0.1826 0.1579 0.1644 -0.0187 0.0188  0.0325  122 LEU   A CD1 
2491 C CD2 . LEU   A 122 ? 0.1593 0.1478 0.1446 -0.0015 0.0318  0.0164  122 LEU   A CD2 
2503 N N   A LEU   A 123 ? 0.1345 0.1429 0.1145 -0.0239 0.0074  0.0225  123 LEU   A N   
2504 N N   B LEU   A 123 ? 0.1384 0.1399 0.1149 -0.0277 0.0030  0.0166  123 LEU   A N   
2505 C CA  A LEU   A 123 ? 0.1307 0.1420 0.1040 -0.0218 0.0097  0.0213  123 LEU   A CA  
2506 C CA  B LEU   A 123 ? 0.1386 0.1359 0.1133 -0.0272 0.0056  0.0097  123 LEU   A CA  
2507 C C   A LEU   A 123 ? 0.1270 0.1322 0.0967 -0.0166 0.0080  0.0194  123 LEU   A C   
2508 C C   B LEU   A 123 ? 0.1379 0.1321 0.1034 -0.0210 0.0067  0.0034  123 LEU   A C   
2509 O O   A LEU   A 123 ? 0.1172 0.1283 0.0963 -0.0160 0.0160  0.0175  123 LEU   A O   
2510 O O   B LEU   A 123 ? 0.1341 0.1356 0.1112 -0.0160 0.0063  -0.0006 123 LEU   A O   
2511 C CB  A LEU   A 123 ? 0.1424 0.1639 0.0976 -0.0186 0.0235  0.0171  123 LEU   A CB  
2512 C CB  B LEU   A 123 ? 0.1472 0.1451 0.1193 -0.0276 0.0062  0.0072  123 LEU   A CB  
2513 C CG  A LEU   A 123 ? 0.1511 0.1776 0.1150 -0.0084 0.0211  0.0053  123 LEU   A CG  
2514 C CG  B LEU   A 123 ? 0.1531 0.1476 0.1149 -0.0282 0.0094  0.0095  123 LEU   A CG  
2515 C CD1 A LEU   A 123 ? 0.1437 0.1877 0.1358 -0.0050 0.0255  -0.0045 123 LEU   A CD1 
2516 C CD1 B LEU   A 123 ? 0.1530 0.1463 0.1313 -0.0281 0.0088  0.0126  123 LEU   A CD1 
2517 C CD2 A LEU   A 123 ? 0.1614 0.1794 0.1196 -0.0127 0.0064  0.0002  123 LEU   A CD2 
2518 C CD2 B LEU   A 123 ? 0.1553 0.1501 0.1138 -0.0350 0.0086  0.0074  123 LEU   A CD2 
2541 N N   A ALA   A 124 ? 0.1179 0.1142 0.0958 -0.0112 0.0048  0.0204  124 ALA   A N   
2542 N N   B ALA   A 124 ? 0.1331 0.1191 0.0932 -0.0177 0.0093  0.0021  124 ALA   A N   
2543 C CA  A ALA   A 124 ? 0.1156 0.1135 0.0910 -0.0023 0.0037  0.0190  124 ALA   A CA  
2544 C CA  B ALA   A 124 ? 0.1332 0.1324 0.1083 -0.0199 -0.0020 0.0128  124 ALA   A CA  
2545 C C   A ALA   A 124 ? 0.1092 0.1161 0.1014 -0.0079 0.0074  0.0203  124 ALA   A C   
2546 C C   B ALA   A 124 ? 0.1362 0.1397 0.1083 -0.0149 -0.0021 0.0135  124 ALA   A C   
2547 O O   A ALA   A 124 ? 0.1105 0.1221 0.1193 -0.0216 0.0192  0.0298  124 ALA   A O   
2548 O O   B ALA   A 124 ? 0.1457 0.1504 0.1298 -0.0032 -0.0062 0.0165  124 ALA   A O   
2549 C CB  A ALA   A 124 ? 0.1145 0.1079 0.1054 -0.0017 0.0140  0.0115  124 ALA   A CB  
2550 C CB  B ALA   A 124 ? 0.1353 0.1366 0.1283 -0.0277 -0.0011 0.0069  124 ALA   A CB  
2561 N N   A PRO   A 125 ? 0.1049 0.1258 0.1126 -0.0027 0.0111  0.0218  125 PRO   A N   
2562 N N   B PRO   A 125 ? 0.1235 0.1295 0.0833 -0.0119 0.0025  0.0198  125 PRO   A N   
2563 C CA  A PRO   A 125 ? 0.1170 0.1298 0.1142 -0.0029 0.0019  0.0162  125 PRO   A CA  
2564 C CA  B PRO   A 125 ? 0.1218 0.1317 0.0873 -0.0171 -0.0002 0.0142  125 PRO   A CA  
2565 C C   A PRO   A 125 ? 0.1211 0.1261 0.1105 -0.0029 0.0171  0.0213  125 PRO   A C   
2566 C C   B PRO   A 125 ? 0.1262 0.1351 0.1020 -0.0143 -0.0024 0.0101  125 PRO   A C   
2567 O O   A PRO   A 125 ? 0.1256 0.1192 0.1229 0.0032  0.0171  0.0146  125 PRO   A O   
2568 O O   B PRO   A 125 ? 0.1233 0.1336 0.1258 -0.0176 -0.0044 0.0104  125 PRO   A O   
2569 C CB  A PRO   A 125 ? 0.1235 0.1310 0.1283 -0.0125 -0.0028 0.0165  125 PRO   A CB  
2570 C CB  B PRO   A 125 ? 0.1149 0.1267 0.0850 -0.0173 0.0007  0.0171  125 PRO   A CB  
2571 C CG  A PRO   A 125 ? 0.1209 0.1267 0.1251 -0.0065 0.0048  0.0282  125 PRO   A CG  
2572 C CG  B PRO   A 125 ? 0.1081 0.1214 0.0859 -0.0097 0.0128  0.0189  125 PRO   A CG  
2573 C CD  A PRO   A 125 ? 0.1070 0.1263 0.1233 -0.0032 0.0194  0.0118  125 PRO   A CD  
2574 C CD  B PRO   A 125 ? 0.1124 0.1165 0.0822 -0.0081 0.0125  0.0263  125 PRO   A CD  
2589 N N   A LEU   A 126 ? 0.1168 0.1314 0.1157 -0.0074 0.0150  0.0240  126 LEU   A N   
2590 N N   B LEU   A 126 ? 0.1289 0.1373 0.1122 -0.0050 -0.0096 0.0051  126 LEU   A N   
2591 C CA  A LEU   A 126 ? 0.1186 0.1326 0.1100 -0.0055 0.0150  0.0218  126 LEU   A CA  
2592 C CA  B LEU   A 126 ? 0.1206 0.1333 0.1168 -0.0069 -0.0017 0.0056  126 LEU   A CA  
2593 C C   A LEU   A 126 ? 0.1252 0.1210 0.1060 0.0046  0.0003  0.0116  126 LEU   A C   
2594 C C   B LEU   A 126 ? 0.1131 0.1279 0.1218 0.0045  -0.0079 -0.0064 126 LEU   A C   
2595 O O   A LEU   A 126 ? 0.1311 0.1294 0.1210 0.0099  0.0163  0.0242  126 LEU   A O   
2596 O O   B LEU   A 126 ? 0.1180 0.1340 0.1527 -0.0017 -0.0291 -0.0035 126 LEU   A O   
2597 C CB  A LEU   A 126 ? 0.1255 0.1439 0.1257 -0.0050 0.0076  0.0198  126 LEU   A CB  
2598 C CB  B LEU   A 126 ? 0.1263 0.1451 0.1544 -0.0172 -0.0065 0.0015  126 LEU   A CB  
2599 C CG  A LEU   A 126 ? 0.1213 0.1603 0.1456 -0.0096 0.0131  0.0089  126 LEU   A CG  
2600 C CG  B LEU   A 126 ? 0.1339 0.1587 0.1687 -0.0238 -0.0204 0.0081  126 LEU   A CG  
2601 C CD1 A LEU   A 126 ? 0.1274 0.1757 0.1805 -0.0087 0.0093  0.0089  126 LEU   A CD1 
2602 C CD1 B LEU   A 126 ? 0.1372 0.1675 0.1758 -0.0244 -0.0200 0.0079  126 LEU   A CD1 
2603 C CD2 A LEU   A 126 ? 0.1190 0.1610 0.1341 -0.0159 0.0130  0.0205  126 LEU   A CD2 
2604 C CD2 B LEU   A 126 ? 0.1347 0.1583 0.1615 -0.0267 -0.0231 0.0136  126 LEU   A CD2 
2627 N N   A LEU   A 127 ? 0.1274 0.1182 0.0998 0.0045  0.0062  0.0192  127 LEU   A N   
2628 N N   B LEU   A 127 ? 0.1190 0.1242 0.1106 0.0187  0.0026  -0.0043 127 LEU   A N   
2629 C CA  A LEU   A 127 ? 0.1239 0.1264 0.1056 -0.0020 0.0051  0.0119  127 LEU   A CA  
2630 C CA  B LEU   A 127 ? 0.1299 0.1280 0.1083 0.0174  -0.0009 0.0064  127 LEU   A CA  
2631 C C   A LEU   A 127 ? 0.1178 0.1243 0.1072 -0.0048 0.0100  0.0050  127 LEU   A C   
2632 C C   B LEU   A 127 ? 0.1338 0.1275 0.0927 0.0124  -0.0106 0.0025  127 LEU   A C   
2633 O O   A LEU   A 127 ? 0.1245 0.1310 0.1023 -0.0167 0.0098  0.0058  127 LEU   A O   
2634 O O   B LEU   A 127 ? 0.1450 0.1338 0.1053 0.0074  -0.0046 -0.0030 127 LEU   A O   
2635 C CB  A LEU   A 127 ? 0.1322 0.1318 0.1178 0.0048  0.0090  0.0016  127 LEU   A CB  
2636 C CB  B LEU   A 127 ? 0.1413 0.1299 0.1144 0.0175  0.0114  0.0047  127 LEU   A CB  
2637 C CG  A LEU   A 127 ? 0.1428 0.1282 0.1251 0.0069  0.0006  0.0140  127 LEU   A CG  
2638 C CG  B LEU   A 127 ? 0.1477 0.1388 0.1174 0.0189  0.0082  0.0177  127 LEU   A CG  
2639 C CD1 A LEU   A 127 ? 0.1443 0.1173 0.1381 0.0124  -0.0050 0.0076  127 LEU   A CD1 
2640 C CD1 B LEU   A 127 ? 0.1565 0.1414 0.1293 0.0188  0.0142  0.0263  127 LEU   A CD1 
2641 C CD2 A LEU   A 127 ? 0.1549 0.1253 0.1324 0.0151  -0.0126 0.0209  127 LEU   A CD2 
2642 C CD2 B LEU   A 127 ? 0.1491 0.1493 0.1111 0.0204  -0.0087 0.0157  127 LEU   A CD2 
2665 N N   A SER   A 128 ? 0.1198 0.1261 0.1223 -0.0139 0.0058  0.0168  128 SER   A N   
2666 N N   B SER   A 128 ? 0.1316 0.1217 0.0914 0.0094  -0.0069 0.0109  128 SER   A N   
2667 C CA  A SER   A 128 ? 0.1287 0.1292 0.1205 -0.0074 0.0011  0.0087  128 SER   A CA  
2668 C CA  B SER   A 128 ? 0.1397 0.1219 0.0865 0.0069  -0.0072 0.0138  128 SER   A CA  
2669 C C   A SER   A 128 ? 0.1316 0.1251 0.1074 -0.0025 -0.0056 0.0114  128 SER   A C   
2670 C C   B SER   A 128 ? 0.1394 0.1219 0.0900 0.0056  -0.0130 0.0088  128 SER   A C   
2671 O O   A SER   A 128 ? 0.1391 0.1230 0.1174 -0.0109 -0.0081 0.0105  128 SER   A O   
2672 O O   B SER   A 128 ? 0.1503 0.1308 0.1249 0.0005  -0.0083 -0.0000 128 SER   A O   
2673 C CB  A SER   A 128 ? 0.1251 0.1316 0.1208 -0.0186 0.0030  0.0058  128 SER   A CB  
2674 C CB  B SER   A 128 ? 0.1432 0.1306 0.0841 0.0044  0.0051  0.0094  128 SER   A CB  
2675 O OG  A SER   A 128 ? 0.1190 0.1486 0.1471 -0.0097 -0.0019 0.0023  128 SER   A OG  
2676 O OG  B SER   A 128 ? 0.1524 0.1384 0.0971 0.0010  0.0095  0.0187  128 SER   A OG  
2687 N N   A ALA   A 129 ? 0.1280 0.1353 0.1317 0.0010  -0.0068 0.0197  129 ALA   A N   
2688 N N   B ALA   A 129 ? 0.1354 0.1240 0.0973 0.0017  -0.0108 0.0118  129 ALA   A N   
2689 C CA  A ALA   A 129 ? 0.1280 0.1390 0.1427 -0.0064 -0.0008 0.0225  129 ALA   A CA  
2690 C CA  B ALA   A 129 ? 0.1282 0.1259 0.1090 -0.0017 -0.0083 0.0224  129 ALA   A CA  
2691 C C   A ALA   A 129 ? 0.1391 0.1385 0.1409 -0.0096 -0.0018 0.0096  129 ALA   A C   
2692 C C   B ALA   A 129 ? 0.1276 0.1301 0.1045 0.0022  0.0132  0.0183  129 ALA   A C   
2693 O O   A ALA   A 129 ? 0.1428 0.1475 0.1604 -0.0088 0.0063  0.0192  129 ALA   A O   
2694 O O   B ALA   A 129 ? 0.1305 0.1368 0.1042 0.0038  0.0154  0.0162  129 ALA   A O   
2695 C CB  A ALA   A 129 ? 0.1263 0.1541 0.1763 0.0012  0.0035  0.0219  129 ALA   A CB  
2696 C CB  B ALA   A 129 ? 0.1228 0.1322 0.1187 -0.0063 -0.0174 0.0236  129 ALA   A CB  
2707 N N   A GLY   A 130 ? 0.1489 0.1389 0.1554 -0.0072 -0.0161 0.0073  130 GLY   A N   
2708 N N   B GLY   A 130 ? 0.1255 0.1327 0.1069 -0.0014 0.0049  0.0217  130 GLY   A N   
2709 C CA  A GLY   A 130 ? 0.1614 0.1397 0.1697 -0.0022 -0.0066 0.0009  130 GLY   A CA  
2710 C CA  B GLY   A 130 ? 0.1282 0.1332 0.0863 -0.0001 0.0053  0.0201  130 GLY   A CA  
2711 C C   A GLY   A 130 ? 0.1547 0.1411 0.1555 0.0036  -0.0155 0.0050  130 GLY   A C   
2712 C C   B GLY   A 130 ? 0.1340 0.1338 0.0760 -0.0011 0.0001  0.0190  130 GLY   A C   
2713 O O   A GLY   A 130 ? 0.1563 0.1441 0.1633 0.0142  -0.0185 0.0047  130 GLY   A O   
2714 O O   B GLY   A 130 ? 0.1378 0.1399 0.0775 -0.0097 -0.0016 0.0267  130 GLY   A O   
2721 N N   A ILE   A 131 ? 0.1622 0.1394 0.1538 -0.0042 -0.0130 0.0083  131 ILE   A N   
2722 N N   B ILE   A 131 ? 0.1353 0.1276 0.0877 0.0029  -0.0001 0.0157  131 ILE   A N   
2723 C CA  A ILE   A 131 ? 0.1638 0.1342 0.1214 -0.0074 -0.0264 0.0143  131 ILE   A CA  
2724 C CA  B ILE   A 131 ? 0.1323 0.1271 0.1040 0.0060  -0.0085 0.0091  131 ILE   A CA  
2725 C C   A ILE   A 131 ? 0.1557 0.1297 0.1165 -0.0076 -0.0160 0.0286  131 ILE   A C   
2726 C C   B ILE   A 131 ? 0.1445 0.1317 0.1041 0.0076  0.0029  0.0150  131 ILE   A C   
2727 O O   A ILE   A 131 ? 0.1745 0.1423 0.1428 -0.0062 -0.0172 0.0363  131 ILE   A O   
2728 O O   B ILE   A 131 ? 0.1574 0.1398 0.0976 0.0098  0.0059  0.0213  131 ILE   A O   
2729 C CB  A ILE   A 131 ? 0.1749 0.1535 0.1468 -0.0132 -0.0294 0.0133  131 ILE   A CB  
2730 C CB  B ILE   A 131 ? 0.1211 0.1213 0.1242 0.0132  -0.0183 -0.0004 131 ILE   A CB  
2731 C CG1 A ILE   A 131 ? 0.1817 0.1889 0.1600 -0.0188 -0.0376 0.0046  131 ILE   A CG1 
2732 C CG1 B ILE   A 131 ? 0.1243 0.1404 0.1367 0.0218  -0.0164 0.0005  131 ILE   A CG1 
2733 C CG2 A ILE   A 131 ? 0.1830 0.1426 0.1745 -0.0108 -0.0203 0.0048  131 ILE   A CG2 
2734 C CG2 B ILE   A 131 ? 0.1143 0.1055 0.1365 0.0194  -0.0245 0.0009  131 ILE   A CG2 
2735 C CD1 A ILE   A 131 ? 0.1896 0.1998 0.1896 -0.0211 -0.0385 -0.0102 131 ILE   A CD1 
2736 C CD1 B ILE   A 131 ? 0.1229 0.1476 0.1420 0.0212  -0.0358 -0.0093 131 ILE   A CD1 
2759 N N   A PHE   A 132 ? 0.1390 0.1268 0.1104 -0.0057 -0.0151 0.0245  132 PHE   A N   
2760 N N   B PHE   A 132 ? 0.1501 0.1387 0.1184 0.0088  0.0048  0.0035  132 PHE   A N   
2761 C CA  A PHE   A 132 ? 0.1501 0.1347 0.1076 -0.0119 -0.0006 0.0111  132 PHE   A CA  
2762 C CA  B PHE   A 132 ? 0.1513 0.1510 0.1181 0.0049  -0.0005 -0.0008 132 PHE   A CA  
2763 C C   A PHE   A 132 ? 0.1657 0.1523 0.0999 -0.0064 -0.0009 0.0108  132 PHE   A C   
2764 C C   B PHE   A 132 ? 0.1583 0.1644 0.1196 0.0055  -0.0039 0.0047  132 PHE   A C   
2765 O O   A PHE   A 132 ? 0.1803 0.1699 0.1098 -0.0014 0.0028  0.0090  132 PHE   A O   
2766 O O   B PHE   A 132 ? 0.1610 0.1781 0.1208 0.0115  -0.0131 0.0076  132 PHE   A O   
2767 C CB  A PHE   A 132 ? 0.1449 0.1264 0.0847 -0.0062 0.0054  0.0213  132 PHE   A CB  
2768 C CB  B PHE   A 132 ? 0.1461 0.1497 0.1184 0.0137  -0.0007 -0.0102 132 PHE   A CB  
2769 C CG  A PHE   A 132 ? 0.1425 0.1292 0.0916 0.0016  0.0026  0.0140  132 PHE   A CG  
2770 C CG  B PHE   A 132 ? 0.1464 0.1514 0.1114 0.0186  -0.0008 0.0016  132 PHE   A CG  
2771 C CD1 A PHE   A 132 ? 0.1433 0.1370 0.1296 0.0084  0.0009  -0.0044 132 PHE   A CD1 
2772 C CD1 B PHE   A 132 ? 0.1505 0.1572 0.1125 0.0218  -0.0021 -0.0004 132 PHE   A CD1 
2773 C CD2 A PHE   A 132 ? 0.1354 0.1421 0.1091 -0.0004 -0.0086 0.0024  132 PHE   A CD2 
2774 C CD2 B PHE   A 132 ? 0.1494 0.1553 0.1179 0.0165  0.0055  -0.0005 132 PHE   A CD2 
2775 C CE1 A PHE   A 132 ? 0.1407 0.1502 0.1398 0.0026  0.0039  -0.0024 132 PHE   A CE1 
2776 C CE1 B PHE   A 132 ? 0.1593 0.1624 0.1142 0.0163  -0.0045 0.0052  132 PHE   A CE1 
2777 C CE2 A PHE   A 132 ? 0.1379 0.1473 0.1229 0.0073  -0.0154 0.0018  132 PHE   A CE2 
2778 C CE2 B PHE   A 132 ? 0.1561 0.1592 0.1235 0.0177  0.0086  0.0029  132 PHE   A CE2 
2779 C CZ  A PHE   A 132 ? 0.1394 0.1507 0.1289 0.0030  -0.0048 0.0031  132 PHE   A CZ  
2780 C CZ  B PHE   A 132 ? 0.1571 0.1619 0.1132 0.0131  -0.0052 0.0077  132 PHE   A CZ  
2799 N N   A GLY   A 133 ? 0.1663 0.1532 0.1035 -0.0099 -0.0173 0.0149  133 GLY   A N   
2800 N N   B GLY   A 133 ? 0.1635 0.1674 0.1249 0.0020  -0.0129 0.0055  133 GLY   A N   
2801 C CA  A GLY   A 133 ? 0.1667 0.1582 0.1100 -0.0042 -0.0189 0.0088  133 GLY   A CA  
2802 C CA  B GLY   A 133 ? 0.1668 0.1716 0.1303 0.0007  -0.0153 0.0025  133 GLY   A CA  
2803 C C   A GLY   A 133 ? 0.1711 0.1687 0.1004 -0.0060 -0.0227 -0.0016 133 GLY   A C   
2804 C C   B GLY   A 133 ? 0.1728 0.1795 0.1338 -0.0027 -0.0126 -0.0046 133 GLY   A C   
2805 O O   A GLY   A 133 ? 0.1831 0.1859 0.1147 0.0052  -0.0280 -0.0195 133 GLY   A O   
2806 O O   B GLY   A 133 ? 0.1879 0.1887 0.1376 0.0055  -0.0048 -0.0177 133 GLY   A O   
2813 N N   A ALA   A 134 ? 0.1717 0.1606 0.1034 -0.0101 -0.0100 -0.0026 134 ALA   A N   
2814 N N   B ALA   A 134 ? 0.1696 0.1780 0.1386 -0.0104 -0.0129 -0.0028 134 ALA   A N   
2815 C CA  A ALA   A 134 ? 0.1703 0.1535 0.1344 -0.0033 -0.0094 -0.0144 134 ALA   A CA  
2816 C CA  B ALA   A 134 ? 0.1677 0.1774 0.1385 -0.0128 -0.0109 -0.0089 134 ALA   A CA  
2817 C C   A ALA   A 134 ? 0.1671 0.1522 0.1423 -0.0054 0.0002  0.0037  134 ALA   A C   
2818 C C   B ALA   A 134 ? 0.1647 0.1784 0.1287 -0.0169 -0.0007 -0.0100 134 ALA   A C   
2819 O O   A ALA   A 134 ? 0.1821 0.1547 0.1625 -0.0036 0.0155  0.0007  134 ALA   A O   
2820 O O   B ALA   A 134 ? 0.1807 0.1805 0.1366 -0.0170 0.0035  -0.0254 134 ALA   A O   
2821 C CB  A ALA   A 134 ? 0.1760 0.1408 0.1660 -0.0046 -0.0090 -0.0283 134 ALA   A CB  
2822 C CB  B ALA   A 134 ? 0.1726 0.1718 0.1610 -0.0111 -0.0183 -0.0205 134 ALA   A CB  
2833 N N   A ASP   A 135 ? 0.1688 0.1608 0.1463 -0.0138 -0.0103 0.0143  135 ASP   A N   
2834 N N   B ASP   A 135 ? 0.1587 0.1750 0.1375 -0.0149 0.0029  -0.0006 135 ASP   A N   
2835 C CA  A ASP   A 135 ? 0.1679 0.1747 0.1746 -0.0179 -0.0297 0.0228  135 ASP   A CA  
2836 C CA  B ASP   A 135 ? 0.1576 0.1774 0.1381 -0.0141 -0.0077 0.0054  135 ASP   A CA  
2837 C C   A ASP   A 135 ? 0.1561 0.1615 0.1808 -0.0072 -0.0139 0.0251  135 ASP   A C   
2838 C C   B ASP   A 135 ? 0.1561 0.1636 0.1302 -0.0109 0.0007  0.0049  135 ASP   A C   
2839 O O   A ASP   A 135 ? 0.1530 0.1616 0.1707 -0.0026 -0.0138 0.0293  135 ASP   A O   
2840 O O   B ASP   A 135 ? 0.1569 0.1593 0.1431 -0.0082 -0.0068 0.0114  135 ASP   A O   
2841 C CB  A ASP   A 135 ? 0.1876 0.2083 0.2233 -0.0245 -0.0495 0.0179  135 ASP   A CB  
2842 C CB  B ASP   A 135 ? 0.1653 0.2004 0.1702 -0.0172 -0.0243 -0.0037 135 ASP   A CB  
2843 C CG  A ASP   A 135 ? 0.2068 0.2370 0.2830 -0.0369 -0.0516 0.0122  135 ASP   A CG  
2844 C CG  B ASP   A 135 ? 0.1731 0.2183 0.2053 -0.0215 -0.0331 -0.0158 135 ASP   A CG  
2845 O OD1 A ASP   A 135 ? 0.2050 0.2413 0.2867 -0.0383 -0.0540 0.0204  135 ASP   A OD1 
2846 O OD1 B ASP   A 135 ? 0.1724 0.2250 0.2021 -0.0293 -0.0438 -0.0123 135 ASP   A OD1 
2847 O OD2 A ASP   A 135 ? 0.2244 0.2576 0.3342 -0.0410 -0.0435 0.0041  135 ASP   A OD2 
2848 O OD2 B ASP   A 135 ? 0.1900 0.2293 0.2430 -0.0222 -0.0236 -0.0218 135 ASP   A OD2 
2857 N N   A PRO   A 136 ? 0.1475 0.1499 0.1830 -0.0008 -0.0020 0.0249  136 PRO   A N   
2858 N N   B PRO   A 136 ? 0.1557 0.1590 0.1281 -0.0067 0.0027  -0.0009 136 PRO   A N   
2859 C CA  A PRO   A 136 ? 0.1395 0.1521 0.1856 -0.0022 0.0039  0.0079  136 PRO   A CA  
2860 C CA  B PRO   A 136 ? 0.1504 0.1511 0.1323 -0.0093 0.0024  -0.0078 136 PRO   A CA  
2861 C C   A PRO   A 136 ? 0.1284 0.1508 0.1585 -0.0016 0.0052  0.0083  136 PRO   A C   
2862 C C   B PRO   A 136 ? 0.1395 0.1407 0.1414 -0.0056 0.0007  -0.0024 136 PRO   A C   
2863 O O   A PRO   A 136 ? 0.1277 0.1486 0.1451 -0.0085 0.0103  0.0049  136 PRO   A O   
2864 O O   B PRO   A 136 ? 0.1384 0.1454 0.1430 -0.0032 0.0007  -0.0020 136 PRO   A O   
2865 C CB  A PRO   A 136 ? 0.1549 0.1476 0.2083 0.0017  -0.0001 0.0076  136 PRO   A CB  
2866 C CB  B PRO   A 136 ? 0.1581 0.1503 0.1434 -0.0087 -0.0041 -0.0080 136 PRO   A CB  
2867 C CG  A PRO   A 136 ? 0.1700 0.1542 0.2298 0.0133  -0.0019 0.0113  136 PRO   A CG  
2868 C CG  B PRO   A 136 ? 0.1621 0.1552 0.1396 -0.0080 -0.0155 -0.0158 136 PRO   A CG  
2869 C CD  A PRO   A 136 ? 0.1619 0.1485 0.2154 0.0102  0.0023  0.0280  136 PRO   A CD  
2870 C CD  B PRO   A 136 ? 0.1637 0.1583 0.1404 -0.0029 -0.0045 -0.0128 136 PRO   A CD  
2885 N N   A ILE   A 137 ? 0.1296 0.1602 0.1636 -0.0027 -0.0049 0.0043  137 ILE   A N   
2886 N N   B ILE   A 137 ? 0.1295 0.1358 0.1428 -0.0059 -0.0038 -0.0091 137 ILE   A N   
2887 C CA  A ILE   A 137 ? 0.1322 0.1600 0.1600 -0.0045 -0.0045 -0.0029 137 ILE   A CA  
2888 C CA  B ILE   A 137 ? 0.1293 0.1378 0.1524 -0.0115 -0.0008 0.0026  137 ILE   A CA  
2889 C C   A ILE   A 137 ? 0.1292 0.1519 0.1537 -0.0055 0.0014  0.0010  137 ILE   A C   
2890 C C   B ILE   A 137 ? 0.1348 0.1393 0.1487 -0.0072 -0.0048 0.0119  137 ILE   A C   
2891 O O   A ILE   A 137 ? 0.1281 0.1562 0.1578 -0.0089 0.0083  -0.0008 137 ILE   A O   
2892 O O   B ILE   A 137 ? 0.1460 0.1414 0.1581 -0.0087 -0.0019 0.0063  137 ILE   A O   
2893 C CB  A ILE   A 137 ? 0.1435 0.1646 0.1738 -0.0019 -0.0120 -0.0123 137 ILE   A CB  
2894 C CB  B ILE   A 137 ? 0.1335 0.1429 0.1770 -0.0108 -0.0127 -0.0172 137 ILE   A CB  
2895 C CG1 A ILE   A 137 ? 0.1552 0.1754 0.2201 0.0038  -0.0263 -0.0046 137 ILE   A CG1 
2896 C CG1 B ILE   A 137 ? 0.1330 0.1468 0.1904 -0.0087 -0.0153 -0.0206 137 ILE   A CG1 
2897 C CG2 A ILE   A 137 ? 0.1516 0.1625 0.1800 -0.0028 -0.0124 -0.0227 137 ILE   A CG2 
2898 C CG2 B ILE   A 137 ? 0.1368 0.1427 0.1869 -0.0110 -0.0079 -0.0287 137 ILE   A CG2 
2899 C CD1 A ILE   A 137 ? 0.1686 0.1894 0.2545 0.0085  -0.0302 -0.0085 137 ILE   A CD1 
2900 C CD1 B ILE   A 137 ? 0.1372 0.1532 0.2060 -0.0006 -0.0168 -0.0324 137 ILE   A CD1 
2923 N N   A HIS   A 138 ? 0.1332 0.1520 0.1603 -0.0077 0.0091  -0.0028 138 HIS   A N   
2924 N N   B HIS   A 138 ? 0.1400 0.1430 0.1419 -0.0037 -0.0038 0.0136  138 HIS   A N   
2925 C CA  A HIS   A 138 ? 0.1467 0.1446 0.1438 -0.0092 0.0113  -0.0042 138 HIS   A CA  
2926 C CA  B HIS   A 138 ? 0.1502 0.1490 0.1489 0.0020  0.0058  -0.0014 138 HIS   A CA  
2927 C C   A HIS   A 138 ? 0.1394 0.1322 0.1349 -0.0012 0.0066  0.0011  138 HIS   A C   
2928 C C   B HIS   A 138 ? 0.1461 0.1398 0.1480 0.0020  0.0052  0.0037  138 HIS   A C   
2929 O O   A HIS   A 138 ? 0.1393 0.1296 0.1349 -0.0082 0.0112  0.0024  138 HIS   A O   
2930 O O   B HIS   A 138 ? 0.1517 0.1428 0.1640 0.0025  0.0046  0.0022  138 HIS   A O   
2931 C CB  A HIS   A 138 ? 0.1540 0.1623 0.1388 -0.0031 0.0021  -0.0140 138 HIS   A CB  
2932 C CB  B HIS   A 138 ? 0.1640 0.1569 0.1520 0.0064  0.0001  -0.0017 138 HIS   A CB  
2933 C CG  A HIS   A 138 ? 0.1626 0.1717 0.1525 -0.0085 -0.0001 -0.0164 138 HIS   A CG  
2934 C CG  B HIS   A 138 ? 0.1749 0.1633 0.1536 0.0067  0.0020  0.0029  138 HIS   A CG  
2935 N ND1 A HIS   A 138 ? 0.1751 0.1844 0.1778 -0.0034 -0.0017 -0.0307 138 HIS   A ND1 
2936 N ND1 B HIS   A 138 ? 0.1798 0.1684 0.1725 0.0052  0.0065  -0.0061 138 HIS   A ND1 
2937 C CD2 A HIS   A 138 ? 0.1648 0.1754 0.1598 -0.0003 0.0065  -0.0106 138 HIS   A CD2 
2938 C CD2 B HIS   A 138 ? 0.1798 0.1672 0.1563 0.0063  0.0022  0.0071  138 HIS   A CD2 
2939 C CE1 A HIS   A 138 ? 0.1782 0.1888 0.1793 0.0090  0.0011  -0.0303 138 HIS   A CE1 
2940 C CE1 B HIS   A 138 ? 0.1842 0.1735 0.1828 0.0097  0.0055  -0.0039 138 HIS   A CE1 
2941 N NE2 A HIS   A 138 ? 0.1723 0.1876 0.1620 0.0145  0.0062  -0.0172 138 HIS   A NE2 
2942 N NE2 B HIS   A 138 ? 0.1820 0.1749 0.1684 0.0091  0.0082  0.0014  138 HIS   A NE2 
2957 N N   A SER   A 139 ? 0.1295 0.1199 0.1276 0.0002  0.0029  0.0097  139 SER   A N   
2958 N N   B SER   A 139 ? 0.1345 0.1328 0.1323 -0.0001 0.0016  0.0042  139 SER   A N   
2959 C CA  A SER   A 139 ? 0.1245 0.1233 0.1377 0.0031  0.0002  0.0028  139 SER   A CA  
2960 C CA  B SER   A 139 ? 0.1269 0.1223 0.1305 -0.0087 0.0070  0.0084  139 SER   A CA  
2961 C C   A SER   A 139 ? 0.1193 0.1260 0.1402 0.0007  -0.0020 -0.0077 139 SER   A C   
2962 C C   B SER   A 139 ? 0.1200 0.1235 0.1352 -0.0121 0.0144  0.0098  139 SER   A C   
2963 O O   A SER   A 139 ? 0.1174 0.1178 0.1671 -0.0028 -0.0109 0.0063  139 SER   A O   
2964 O O   B SER   A 139 ? 0.1069 0.1144 0.1387 -0.0148 0.0277  0.0029  139 SER   A O   
2965 C CB  A SER   A 139 ? 0.1277 0.1230 0.1353 0.0018  -0.0005 0.0041  139 SER   A CB  
2966 C CB  B SER   A 139 ? 0.1214 0.1099 0.1134 -0.0056 0.0181  0.0017  139 SER   A CB  
2967 O OG  A SER   A 139 ? 0.1342 0.1250 0.1435 -0.0013 -0.0054 0.0054  139 SER   A OG  
2968 O OG  B SER   A 139 ? 0.1129 0.1017 0.1103 -0.0028 0.0273  0.0106  139 SER   A OG  
2979 N N   A LEU   A 140 ? 0.1160 0.1321 0.1281 -0.0016 0.0009  0.0097  140 LEU   A N   
2980 N N   B LEU   A 140 ? 0.1237 0.1309 0.1356 -0.0122 0.0074  0.0123  140 LEU   A N   
2981 C CA  A LEU   A 140 ? 0.1173 0.1360 0.1198 -0.0043 0.0018  0.0071  140 LEU   A CA  
2982 C CA  B LEU   A 140 ? 0.1271 0.1384 0.1369 -0.0170 -0.0027 0.0175  140 LEU   A CA  
2983 C C   A LEU   A 140 ? 0.1091 0.1404 0.1382 -0.0073 -0.0039 0.0119  140 LEU   A C   
2984 C C   B LEU   A 140 ? 0.1238 0.1422 0.1309 -0.0190 0.0040  0.0226  140 LEU   A C   
2985 O O   A LEU   A 140 ? 0.1143 0.1454 0.1651 -0.0075 -0.0019 0.0153  140 LEU   A O   
2986 O O   B LEU   A 140 ? 0.1236 0.1383 0.1460 -0.0133 0.0057  0.0232  140 LEU   A O   
2987 C CB  A LEU   A 140 ? 0.1224 0.1495 0.1217 -0.0052 0.0101  0.0078  140 LEU   A CB  
2988 C CB  B LEU   A 140 ? 0.1284 0.1378 0.1485 -0.0199 -0.0016 0.0166  140 LEU   A CB  
2989 C CG  A LEU   A 140 ? 0.1291 0.1564 0.1384 -0.0119 0.0133  0.0198  140 LEU   A CG  
2990 C CG  B LEU   A 140 ? 0.1259 0.1276 0.1352 -0.0230 0.0076  0.0191  140 LEU   A CG  
2991 C CD1 A LEU   A 140 ? 0.1258 0.1485 0.1518 -0.0031 -0.0012 0.0192  140 LEU   A CD1 
2992 C CD1 B LEU   A 140 ? 0.1252 0.1280 0.1317 -0.0139 0.0138  0.0290  140 LEU   A CD1 
2993 C CD2 A LEU   A 140 ? 0.1334 0.1613 0.1524 -0.0145 0.0137  0.0318  140 LEU   A CD2 
2994 C CD2 B LEU   A 140 ? 0.1227 0.1233 0.1433 -0.0265 0.0122  0.0334  140 LEU   A CD2 
3017 N N   A ARG   A 141 ? 0.1216 0.1435 0.1471 -0.0044 -0.0009 0.0070  141 ARG   A N   
3018 N N   B ARG   A 141 ? 0.1308 0.1435 0.1321 -0.0238 0.0022  0.0195  141 ARG   A N   
3019 C CA  A ARG   A 141 ? 0.1318 0.1567 0.1668 -0.0146 -0.0044 -0.0119 141 ARG   A CA  
3020 C CA  B ARG   A 141 ? 0.1415 0.1475 0.1464 -0.0320 -0.0013 0.0156  141 ARG   A CA  
3021 C C   A ARG   A 141 ? 0.1308 0.1475 0.1625 -0.0124 -0.0035 -0.0029 141 ARG   A C   
3022 C C   B ARG   A 141 ? 0.1347 0.1456 0.1435 -0.0185 -0.0014 0.0076  141 ARG   A C   
3023 O O   A ARG   A 141 ? 0.1295 0.1426 0.1808 -0.0150 0.0048  -0.0076 141 ARG   A O   
3024 O O   B ARG   A 141 ? 0.1319 0.1417 0.1392 -0.0105 0.0084  -0.0104 141 ARG   A O   
3025 C CB  A ARG   A 141 ? 0.1460 0.1719 0.1901 -0.0215 -0.0035 -0.0254 141 ARG   A CB  
3026 C CB  B ARG   A 141 ? 0.1604 0.1554 0.1659 -0.0414 -0.0032 0.0146  141 ARG   A CB  
3027 C CG  A ARG   A 141 ? 0.1689 0.1995 0.2189 -0.0254 0.0022  -0.0244 141 ARG   A CG  
3028 C CG  B ARG   A 141 ? 0.1864 0.1721 0.1930 -0.0373 -0.0017 0.0095  141 ARG   A CG  
3029 C CD  A ARG   A 141 ? 0.1909 0.2250 0.2487 -0.0330 0.0084  -0.0280 141 ARG   A CD  
3030 C CD  B ARG   A 141 ? 0.2161 0.1945 0.2395 -0.0340 -0.0005 -0.0007 141 ARG   A CD  
3031 N NE  A ARG   A 141 ? 0.1805 0.2374 0.2600 -0.0410 0.0090  -0.0146 141 ARG   A NE  
3032 N NE  B ARG   A 141 ? 0.2290 0.2242 0.2819 -0.0251 -0.0024 -0.0067 141 ARG   A NE  
3033 C CZ  A ARG   A 141 ? 0.1843 0.2577 0.2566 -0.0511 0.0250  -0.0062 141 ARG   A CZ  
3034 C CZ  B ARG   A 141 ? 0.2387 0.2389 0.2982 -0.0208 -0.0025 -0.0061 141 ARG   A CZ  
3035 N NH1 A ARG   A 141 ? 0.1754 0.2624 0.2341 -0.0667 0.0472  -0.0147 141 ARG   A NH1 
3036 N NH1 B ARG   A 141 ? 0.2415 0.2452 0.2976 -0.0198 -0.0024 -0.0128 141 ARG   A NH1 
3037 N NH2 A ARG   A 141 ? 0.1973 0.2647 0.2746 -0.0409 0.0121  0.0050  141 ARG   A NH2 
3038 N NH2 B ARG   A 141 ? 0.2432 0.2425 0.3174 -0.0185 -0.0010 0.0026  141 ARG   A NH2 
3065 N N   . VAL   A 142 ? 0.1254 0.1455 0.1531 -0.0153 0.0031  0.0021  142 VAL   A N   
3066 C CA  . VAL   A 142 ? 0.1291 0.1466 0.1521 -0.0048 0.0167  0.0047  142 VAL   A CA  
3067 C C   . VAL   A 142 ? 0.1185 0.1410 0.1541 -0.0111 0.0095  0.0067  142 VAL   A C   
3068 O O   . VAL   A 142 ? 0.1235 0.1378 0.1725 -0.0003 0.0108  0.0065  142 VAL   A O   
3069 C CB  . VAL   A 142 ? 0.1360 0.1522 0.1524 -0.0053 0.0151  0.0083  142 VAL   A CB  
3070 C CG1 . VAL   A 142 ? 0.1455 0.1426 0.1564 -0.0130 0.0239  0.0078  142 VAL   A CG1 
3071 C CG2 . VAL   A 142 ? 0.1525 0.1685 0.1650 0.0055  0.0096  0.0166  142 VAL   A CG2 
3082 N N   . CYS   A 143 ? 0.1208 0.1338 0.1464 -0.0164 0.0069  0.0033  143 CYS   A N   
3083 C CA  . CYS   A 143 ? 0.1229 0.1346 0.1500 -0.0105 0.0071  0.0109  143 CYS   A CA  
3084 C C   . CYS   A 143 ? 0.1263 0.1307 0.1544 -0.0129 0.0069  0.0191  143 CYS   A C   
3085 O O   . CYS   A 143 ? 0.1212 0.1337 0.1613 -0.0030 0.0072  0.0254  143 CYS   A O   
3086 C CB  . CYS   A 143 ? 0.1273 0.1352 0.1607 -0.0159 0.0164  0.0147  143 CYS   A CB  
3087 S SG  . CYS   A 143 ? 0.1479 0.1486 0.1404 0.0004  0.0116  0.0126  143 CYS   A SG  
3093 N N   . VAL   A 144 ? 0.1250 0.1436 0.1637 -0.0131 0.0101  0.0297  144 VAL   A N   
3094 C CA  . VAL   A 144 ? 0.1315 0.1504 0.2065 -0.0173 0.0242  0.0328  144 VAL   A CA  
3095 C C   . VAL   A 144 ? 0.1288 0.1446 0.1994 -0.0206 -0.0145 0.0321  144 VAL   A C   
3096 O O   . VAL   A 144 ? 0.1401 0.1485 0.2221 -0.0097 -0.0070 0.0389  144 VAL   A O   
3097 C CB  . VAL   A 144 ? 0.1587 0.1766 0.2899 -0.0047 0.0445  0.0443  144 VAL   A CB  
3098 C CG1 . VAL   A 144 ? 0.1860 0.2055 0.3493 -0.0153 0.0245  0.0457  144 VAL   A CG1 
3099 C CG2 . VAL   A 144 ? 0.1463 0.1836 0.2889 -0.0016 0.0468  0.0550  144 VAL   A CG2 
3109 N N   . ASP   A 145 ? 0.1419 0.1397 0.2116 -0.0203 -0.0038 0.0206  145 ASP   A N   
3110 C CA  . ASP   A 145 ? 0.1496 0.1435 0.2325 -0.0197 -0.0114 0.0094  145 ASP   A CA  
3111 C C   . ASP   A 145 ? 0.1457 0.1332 0.2248 -0.0107 -0.0058 -0.0065 145 ASP   A C   
3112 O O   . ASP   A 145 ? 0.1629 0.1407 0.2734 -0.0115 -0.0065 -0.0358 145 ASP   A O   
3113 C CB  . ASP   A 145 ? 0.1640 0.1684 0.2633 -0.0296 -0.0291 0.0078  145 ASP   A CB  
3114 C CG  . ASP   A 145 ? 0.1890 0.1989 0.3006 -0.0511 -0.0462 0.0256  145 ASP   A CG  
3115 O OD1 . ASP   A 145 ? 0.1832 0.2241 0.3052 -0.0681 -0.0309 0.0253  145 ASP   A OD1 
3116 O OD2 . ASP   A 145 ? 0.2064 0.2192 0.3181 -0.0531 -0.0664 0.0306  145 ASP   A OD2 
3121 N N   . THR   A 146 ? 0.1320 0.1279 0.1785 -0.0169 0.0100  -0.0033 146 THR   A N   
3122 C CA  . THR   A 146 ? 0.1286 0.1320 0.1717 -0.0034 0.0074  -0.0046 146 THR   A CA  
3123 C C   . THR   A 146 ? 0.1281 0.1291 0.1680 0.0010  0.0089  0.0116  146 THR   A C   
3124 O O   . THR   A 146 ? 0.1465 0.1383 0.1805 0.0040  0.0013  0.0088  146 THR   A O   
3125 C CB  . THR   A 146 ? 0.1269 0.1334 0.1606 -0.0053 0.0050  0.0027  146 THR   A CB  
3126 O OG1 . THR   A 146 ? 0.1269 0.1451 0.1660 -0.0006 -0.0020 0.0004  146 THR   A OG1 
3127 C CG2 . THR   A 146 ? 0.1286 0.1372 0.1783 -0.0049 0.0095  0.0024  146 THR   A CG2 
3135 N N   . VAL   A 147 ? 0.1182 0.1310 0.1585 -0.0025 0.0045  0.0135  147 VAL   A N   
3136 C CA  . VAL   A 147 ? 0.1221 0.1374 0.1648 -0.0098 0.0213  0.0198  147 VAL   A CA  
3137 C C   . VAL   A 147 ? 0.1257 0.1275 0.1708 -0.0123 0.0227  0.0171  147 VAL   A C   
3138 O O   . VAL   A 147 ? 0.1329 0.1407 0.1869 -0.0170 0.0190  0.0186  147 VAL   A O   
3139 C CB  . VAL   A 147 ? 0.1303 0.1359 0.1539 -0.0091 0.0199  0.0224  147 VAL   A CB  
3140 C CG1 . VAL   A 147 ? 0.1599 0.1363 0.1589 -0.0018 0.0185  0.0209  147 VAL   A CG1 
3141 C CG2 . VAL   A 147 ? 0.1374 0.1393 0.1500 -0.0135 0.0042  0.0188  147 VAL   A CG2 
3151 N N   . ARG   A 148 ? 0.1301 0.1295 0.1782 -0.0112 0.0155  0.0326  148 ARG   A N   
3152 C CA  . ARG   A 148 ? 0.1368 0.1303 0.1834 -0.0167 0.0182  0.0427  148 ARG   A CA  
3153 C C   . ARG   A 148 ? 0.1455 0.1365 0.1739 -0.0188 0.0137  0.0537  148 ARG   A C   
3154 O O   . ARG   A 148 ? 0.1712 0.1544 0.1957 -0.0254 0.0153  0.0439  148 ARG   A O   
3155 C CB  . ARG   A 148 ? 0.1463 0.1330 0.1935 -0.0100 0.0231  0.0404  148 ARG   A CB  
3156 C CG  . ARG   A 148 ? 0.1621 0.1449 0.2218 -0.0129 0.0301  0.0286  148 ARG   A CG  
3157 C CD  . ARG   A 148 ? 0.1757 0.1408 0.2436 -0.0064 0.0417  0.0474  148 ARG   A CD  
3158 N NE  . ARG   A 148 ? 0.1651 0.1385 0.2455 0.0070  0.0448  0.0447  148 ARG   A NE  
3159 C CZ  . ARG   A 148 ? 0.1588 0.1364 0.2338 0.0020  0.0449  0.0359  148 ARG   A CZ  
3160 N NH1 . ARG   A 148 ? 0.1568 0.1348 0.2470 -0.0014 0.0435  0.0118  148 ARG   A NH1 
3161 N NH2 . ARG   A 148 ? 0.1611 0.1522 0.2275 0.0171  0.0464  0.0443  148 ARG   A NH2 
3175 N N   . THR   A 149 ? 0.1473 0.1464 0.1643 -0.0229 -0.0010 0.0411  149 THR   A N   
3176 C CA  . THR   A 149 ? 0.1437 0.1524 0.1717 -0.0152 -0.0028 0.0458  149 THR   A CA  
3177 C C   . THR   A 149 ? 0.1417 0.1562 0.1503 -0.0220 0.0037  0.0462  149 THR   A C   
3178 O O   . THR   A 149 ? 0.1385 0.1644 0.1682 -0.0266 0.0021  0.0416  149 THR   A O   
3179 C CB  . THR   A 149 ? 0.1435 0.1678 0.1704 -0.0181 0.0005  0.0346  149 THR   A CB  
3180 O OG1 . THR   A 149 ? 0.1456 0.1524 0.1712 -0.0277 0.0071  0.0285  149 THR   A OG1 
3181 C CG2 . THR   A 149 ? 0.1349 0.1769 0.1811 -0.0135 -0.0004 0.0276  149 THR   A CG2 
3189 N N   . ASN   A 150 ? 0.1421 0.1590 0.1594 -0.0095 -0.0005 0.0595  150 ASN   A N   
3190 C CA  . ASN   A 150 ? 0.1491 0.1645 0.1625 -0.0149 0.0091  0.0539  150 ASN   A CA  
3191 C C   . ASN   A 150 ? 0.1286 0.1583 0.1614 -0.0181 0.0077  0.0408  150 ASN   A C   
3192 O O   . ASN   A 150 ? 0.1421 0.1647 0.1938 -0.0188 -0.0158 0.0380  150 ASN   A O   
3193 C CB  . ASN   A 150 ? 0.1926 0.1925 0.1945 -0.0239 0.0245  0.0650  150 ASN   A CB  
3194 C CG  . ASN   A 150 ? 0.2501 0.2303 0.2718 -0.0206 0.0083  0.0726  150 ASN   A CG  
3195 O OD1 . ASN   A 150 ? 0.2708 0.2438 0.2943 -0.0274 0.0130  0.0834  150 ASN   A OD1 
3196 N ND2 . ASN   A 150 ? 0.2809 0.2499 0.3141 -0.0134 -0.0128 0.0728  150 ASN   A ND2 
3203 N N   . VAL   A 151 ? 0.1330 0.1484 0.1545 -0.0185 0.0004  0.0371  151 VAL   A N   
3204 C CA  . VAL   A 151 ? 0.1388 0.1416 0.1480 -0.0148 0.0078  0.0433  151 VAL   A CA  
3205 C C   . VAL   A 151 ? 0.1297 0.1361 0.1514 -0.0236 0.0064  0.0375  151 VAL   A C   
3206 O O   . VAL   A 151 ? 0.1467 0.1488 0.1913 -0.0194 0.0112  0.0274  151 VAL   A O   
3207 C CB  . VAL   A 151 ? 0.1691 0.1658 0.1640 -0.0034 0.0105  0.0369  151 VAL   A CB  
3208 C CG1 . VAL   A 151 ? 0.1718 0.1913 0.1922 -0.0103 -0.0018 0.0318  151 VAL   A CG1 
3209 C CG2 . VAL   A 151 ? 0.1867 0.1660 0.1642 -0.0024 0.0212  0.0317  151 VAL   A CG2 
3219 N N   . TYR   A 152 ? 0.1305 0.1422 0.1496 -0.0240 0.0100  0.0376  152 TYR   A N   
3220 C CA  . TYR   A 152 ? 0.1295 0.1506 0.1327 -0.0157 0.0096  0.0313  152 TYR   A CA  
3221 C C   . TYR   A 152 ? 0.1230 0.1422 0.1286 -0.0169 0.0180  0.0283  152 TYR   A C   
3222 O O   . TYR   A 152 ? 0.1308 0.1438 0.1332 -0.0216 0.0146  0.0279  152 TYR   A O   
3223 C CB  . TYR   A 152 ? 0.1501 0.1493 0.1359 -0.0172 0.0159  0.0384  152 TYR   A CB  
3224 C CG  . TYR   A 152 ? 0.1641 0.1737 0.1354 -0.0252 0.0225  0.0454  152 TYR   A CG  
3225 C CD1 . TYR   A 152 ? 0.1764 0.1936 0.1592 -0.0172 0.0157  0.0598  152 TYR   A CD1 
3226 C CD2 . TYR   A 152 ? 0.1676 0.1838 0.1399 -0.0409 0.0147  0.0402  152 TYR   A CD2 
3227 C CE1 . TYR   A 152 ? 0.2070 0.2132 0.1752 -0.0123 0.0040  0.0632  152 TYR   A CE1 
3228 C CE2 . TYR   A 152 ? 0.1950 0.2013 0.1623 -0.0377 0.0097  0.0492  152 TYR   A CE2 
3229 C CZ  . TYR   A 152 ? 0.2171 0.2083 0.1577 -0.0244 0.0021  0.0741  152 TYR   A CZ  
3230 O OH  . TYR   A 152 ? 0.2473 0.2367 0.1863 -0.0197 0.0050  0.0887  152 TYR   A OH  
3240 N N   A LEU   A 153 ? 0.1231 0.1339 0.1265 -0.0259 0.0167  0.0266  153 LEU   A N   
3241 N N   B LEU   A 153 ? 0.1294 0.1396 0.1239 -0.0155 0.0093  0.0311  153 LEU   A N   
3242 C CA  A LEU   A 153 ? 0.1194 0.1309 0.1402 -0.0189 0.0220  0.0251  153 LEU   A CA  
3243 C CA  B LEU   A 153 ? 0.1305 0.1399 0.1256 -0.0047 0.0090  0.0351  153 LEU   A CA  
3244 C C   A LEU   A 153 ? 0.1242 0.1251 0.1426 -0.0205 0.0265  0.0218  153 LEU   A C   
3245 C C   B LEU   A 153 ? 0.1286 0.1384 0.1173 -0.0038 0.0143  0.0356  153 LEU   A C   
3246 O O   A LEU   A 153 ? 0.1331 0.1350 0.1714 -0.0164 0.0356  0.0081  153 LEU   A O   
3247 O O   B LEU   A 153 ? 0.1355 0.1401 0.1417 -0.0073 0.0333  0.0348  153 LEU   A O   
3248 C CB  A LEU   A 153 ? 0.1120 0.1271 0.1467 -0.0191 0.0164  0.0256  153 LEU   A CB  
3249 C CB  B LEU   A 153 ? 0.1329 0.1420 0.1319 -0.0020 0.0057  0.0386  153 LEU   A CB  
3250 C CG  A LEU   A 153 ? 0.1152 0.1337 0.1431 -0.0135 0.0160  0.0108  153 LEU   A CG  
3251 C CG  B LEU   A 153 ? 0.1419 0.1483 0.1360 -0.0023 0.0054  0.0319  153 LEU   A CG  
3252 C CD1 A LEU   A 153 ? 0.1273 0.1345 0.1499 -0.0142 0.0093  0.0062  153 LEU   A CD1 
3253 C CD1 B LEU   A 153 ? 0.1482 0.1484 0.1464 -0.0046 0.0046  0.0347  153 LEU   A CD1 
3254 C CD2 A LEU   A 153 ? 0.1153 0.1347 0.1368 -0.0115 0.0130  0.0065  153 LEU   A CD2 
3255 C CD2 B LEU   A 153 ? 0.1472 0.1541 0.1449 -0.0030 -0.0011 0.0294  153 LEU   A CD2 
3278 N N   A ALA   A 154 ? 0.1285 0.1278 0.1362 -0.0141 0.0245  0.0193  154 ALA   A N   
3279 N N   B ALA   A 154 ? 0.1225 0.1381 0.0936 0.0020  0.0113  0.0222  154 ALA   A N   
3280 C CA  A ALA   A 154 ? 0.1294 0.1301 0.1354 -0.0172 0.0243  0.0137  154 ALA   A CA  
3281 C CA  B ALA   A 154 ? 0.1203 0.1360 0.1069 -0.0025 0.0078  0.0151  154 ALA   A CA  
3282 C C   A ALA   A 154 ? 0.1283 0.1240 0.1203 -0.0117 0.0229  0.0094  154 ALA   A C   
3283 C C   B ALA   A 154 ? 0.1188 0.1281 0.0962 -0.0047 0.0057  0.0228  154 ALA   A C   
3284 O O   A ALA   A 154 ? 0.1346 0.1382 0.1304 -0.0141 0.0221  0.0070  154 ALA   A O   
3285 O O   B ALA   A 154 ? 0.1269 0.1369 0.0828 -0.0103 0.0019  0.0124  154 ALA   A O   
3286 C CB  A ALA   A 154 ? 0.1444 0.1383 0.1373 -0.0160 0.0175  0.0073  154 ALA   A CB  
3287 C CB  B ALA   A 154 ? 0.1265 0.1393 0.1195 -0.0035 -0.0077 0.0007  154 ALA   A CB  
3298 N N   A VAL   A 155 ? 0.1116 0.1016 0.0811 -0.0095 0.0288  0.0214  155 VAL   A N   
3299 N N   B VAL   A 155 ? 0.1122 0.1231 0.1041 -0.0029 0.0117  0.0353  155 VAL   A N   
3300 C CA  A VAL   A 155 ? 0.1309 0.1211 0.1291 -0.0023 0.0206  0.0230  155 VAL   A CA  
3301 C CA  B VAL   A 155 ? 0.1224 0.1419 0.1310 -0.0102 0.0006  0.0207  155 VAL   A CA  
3302 C CA  T VAL   A 155 ? 0.1572 0.1629 0.1537 -0.0062 0.0330  0.0346  155 VAL   A CA  
3303 C C   A VAL   A 155 ? 0.1423 0.1276 0.1606 0.0114  0.0280  0.0384  155 VAL   A C   
3304 C C   B VAL   A 155 ? 0.1275 0.1463 0.1502 -0.0064 -0.0094 0.0155  155 VAL   A C   
3305 C C   T VAL   A 155 ? 0.1592 0.1605 0.1465 0.0029  0.0417  0.0448  155 VAL   A C   
3306 O O   A VAL   A 155 ? 0.1425 0.1315 0.1790 0.0166  0.0461  0.0389  155 VAL   A O   
3307 O O   B VAL   A 155 ? 0.1307 0.1544 0.1707 -0.0020 -0.0048 0.0112  155 VAL   A O   
3308 O O   T VAL   A 155 ? 0.1595 0.1692 0.1390 0.0053  0.0543  0.0425  155 VAL   A O   
3309 C CB  A VAL   A 155 ? 0.1364 0.1268 0.1381 -0.0020 0.0055  0.0220  155 VAL   A CB  
3310 C CB  B VAL   A 155 ? 0.1293 0.1464 0.1396 -0.0168 -0.0057 0.0211  155 VAL   A CB  
3311 C CB  T VAL   A 155 ? 0.1554 0.1623 0.1560 -0.0105 0.0203  0.0353  155 VAL   A CB  
3312 C CG1 A VAL   A 155 ? 0.1458 0.1261 0.1453 0.0000  0.0073  0.0211  155 VAL   A CG1 
3313 C CG1 B VAL   A 155 ? 0.1331 0.1479 0.1577 -0.0178 -0.0158 0.0219  155 VAL   A CG1 
3314 C CG1 T VAL   A 155 ? 0.1596 0.1620 0.1597 -0.0117 0.0227  0.0387  155 VAL   A CG1 
3315 C CG2 A VAL   A 155 ? 0.1429 0.1332 0.1558 -0.0017 -0.0045 0.0208  155 VAL   A CG2 
3316 C CG2 B VAL   A 155 ? 0.1275 0.1442 0.1422 -0.0244 -0.0050 0.0096  155 VAL   A CG2 
3317 C CG2 T VAL   A 155 ? 0.1583 0.1639 0.1668 -0.0118 0.0116  0.0353  155 VAL   A CG2 
3343 N N   A PHE   A 156 ? 0.1570 0.1346 0.1861 0.0197  0.0268  0.0444  156 PHE   A N   
3344 N N   B PHE   A 156 ? 0.1310 0.1399 0.1501 -0.0066 -0.0092 0.0129  156 PHE   A N   
3345 N N   T PHE   A 156 ? 0.1645 0.1524 0.1569 0.0078  0.0431  0.0525  156 PHE   A N   
3346 C CA  A PHE   A 156 ? 0.1768 0.1459 0.2136 0.0292  0.0255  0.0421  156 PHE   A CA  
3347 C CA  B PHE   A 156 ? 0.1510 0.1452 0.1720 -0.0021 -0.0073 0.0078  156 PHE   A CA  
3348 C CA  T PHE   A 156 ? 0.1741 0.1457 0.1567 0.0182  0.0454  0.0572  156 PHE   A CA  
3349 C C   A PHE   A 156 ? 0.1806 0.1541 0.2063 0.0344  0.0403  0.0407  156 PHE   A C   
3350 C C   B PHE   A 156 ? 0.1479 0.1430 0.1690 -0.0034 -0.0086 0.0137  156 PHE   A C   
3351 C C   T PHE   A 156 ? 0.1751 0.1528 0.1629 0.0148  0.0627  0.0577  156 PHE   A C   
3352 O O   A PHE   A 156 ? 0.1864 0.1558 0.2100 0.0344  0.0544  0.0338  156 PHE   A O   
3353 O O   B PHE   A 156 ? 0.1566 0.1460 0.1846 -0.0052 -0.0020 0.0057  156 PHE   A O   
3354 O O   T PHE   A 156 ? 0.1809 0.1537 0.1763 0.0212  0.0646  0.0521  156 PHE   A O   
3355 C CB  A PHE   A 156 ? 0.1928 0.1614 0.2489 0.0222  0.0214  0.0403  156 PHE   A CB  
3356 C CB  B PHE   A 156 ? 0.1685 0.1670 0.1966 -0.0054 -0.0053 0.0005  156 PHE   A CB  
3357 C CB  T PHE   A 156 ? 0.1760 0.1358 0.1425 0.0205  0.0472  0.0611  156 PHE   A CB  
3358 C CG  A PHE   A 156 ? 0.2075 0.1738 0.2598 0.0225  0.0238  0.0409  156 PHE   A CG  
3359 C CG  B PHE   A 156 ? 0.1897 0.1876 0.2364 -0.0040 0.0067  -0.0025 156 PHE   A CG  
3360 C CG  T PHE   A 156 ? 0.1834 0.1350 0.1485 0.0236  0.0339  0.0742  156 PHE   A CG  
3361 C CD1 A PHE   A 156 ? 0.2121 0.1814 0.2617 0.0251  0.0330  0.0447  156 PHE   A CD1 
3362 C CD1 B PHE   A 156 ? 0.1994 0.1985 0.2532 0.0022  0.0013  -0.0055 156 PHE   A CD1 
3363 C CD1 T PHE   A 156 ? 0.1907 0.1436 0.1736 0.0222  0.0251  0.0679  156 PHE   A CD1 
3364 C CD2 A PHE   A 156 ? 0.2192 0.1825 0.2618 0.0270  0.0252  0.0361  156 PHE   A CD2 
3365 C CD2 B PHE   A 156 ? 0.2017 0.1951 0.2593 -0.0070 0.0141  -0.0018 156 PHE   A CD2 
3366 C CD2 T PHE   A 156 ? 0.1925 0.1410 0.1653 0.0320  0.0253  0.0812  156 PHE   A CD2 
3367 C CE1 A PHE   A 156 ? 0.2179 0.1858 0.2630 0.0290  0.0393  0.0402  156 PHE   A CE1 
3368 C CE1 B PHE   A 156 ? 0.2093 0.2054 0.2639 0.0002  0.0035  -0.0073 156 PHE   A CE1 
3369 C CE1 T PHE   A 156 ? 0.1937 0.1453 0.1952 0.0219  0.0200  0.0535  156 PHE   A CE1 
3370 C CE2 A PHE   A 156 ? 0.2272 0.1911 0.2619 0.0303  0.0301  0.0258  156 PHE   A CE2 
3371 C CE2 B PHE   A 156 ? 0.2101 0.1978 0.2672 -0.0123 0.0095  -0.0023 156 PHE   A CE2 
3372 C CE2 T PHE   A 156 ? 0.1971 0.1459 0.1853 0.0264  0.0193  0.0706  156 PHE   A CE2 
3373 C CZ  A PHE   A 156 ? 0.2257 0.1939 0.2595 0.0317  0.0397  0.0292  156 PHE   A CZ  
3374 C CZ  B PHE   A 156 ? 0.2114 0.2060 0.2683 -0.0058 0.0037  -0.0125 156 PHE   A CZ  
3375 C CZ  T PHE   A 156 ? 0.1932 0.1396 0.1967 0.0140  0.0171  0.0623  156 PHE   A CZ  
3403 N N   A ASP   A 157 ? 0.1806 0.1620 0.2122 0.0391  0.0363  0.0385  157 ASP   A N   
3404 N N   B ASP   A 157 ? 0.1366 0.1333 0.1652 -0.0025 -0.0034 0.0089  157 ASP   A N   
3405 N N   T ASP   A 157 ? 0.1692 0.1581 0.1712 0.0112  0.0568  0.0591  157 ASP   A N   
3406 C CA  A ASP   A 157 ? 0.1943 0.1786 0.2255 0.0368  0.0324  0.0397  157 ASP   A CA  
3407 C CA  B ASP   A 157 ? 0.1356 0.1317 0.1642 -0.0027 -0.0056 0.0199  157 ASP   A CA  
3408 C CA  T ASP   A 157 ? 0.1732 0.1667 0.1775 0.0102  0.0470  0.0615  157 ASP   A CA  
3409 C C   A ASP   A 157 ? 0.1974 0.1880 0.2437 0.0316  0.0360  0.0474  157 ASP   A C   
3410 C C   B ASP   A 157 ? 0.1412 0.1305 0.1584 0.0011  -0.0034 0.0213  157 ASP   A C   
3411 C C   T ASP   A 157 ? 0.1789 0.1717 0.1876 0.0090  0.0568  0.0702  157 ASP   A C   
3412 O O   A ASP   A 157 ? 0.1951 0.1884 0.2453 0.0305  0.0351  0.0450  157 ASP   A O   
3413 O O   B ASP   A 157 ? 0.1471 0.1371 0.1655 -0.0007 -0.0064 0.0117  157 ASP   A O   
3414 O O   T ASP   A 157 ? 0.1759 0.1727 0.1904 0.0096  0.0589  0.0593  157 ASP   A O   
3415 C CB  A ASP   A 157 ? 0.2074 0.1874 0.2380 0.0407  0.0283  0.0353  157 ASP   A CB  
3416 C CB  B ASP   A 157 ? 0.1281 0.1255 0.1651 -0.0082 -0.0085 0.0261  157 ASP   A CB  
3417 C CB  T ASP   A 157 ? 0.1748 0.1726 0.1939 0.0119  0.0352  0.0573  157 ASP   A CB  
3418 C CG  A ASP   A 157 ? 0.2203 0.1938 0.2518 0.0421  0.0207  0.0387  157 ASP   A CG  
3419 C CG  B ASP   A 157 ? 0.1295 0.1273 0.1893 -0.0080 -0.0025 0.0319  157 ASP   A CG  
3420 C CG  T ASP   A 157 ? 0.1730 0.1732 0.2087 0.0177  0.0191  0.0564  157 ASP   A CG  
3421 O OD1 A ASP   A 157 ? 0.2306 0.2047 0.2714 0.0431  0.0189  0.0304  157 ASP   A OD1 
3422 O OD1 B ASP   A 157 ? 0.1311 0.1315 0.2095 -0.0069 -0.0098 0.0176  157 ASP   A OD1 
3423 O OD1 T ASP   A 157 ? 0.1706 0.1762 0.2255 0.0210  0.0103  0.0423  157 ASP   A OD1 
3424 O OD2 A ASP   A 157 ? 0.2213 0.1916 0.2474 0.0443  0.0174  0.0491  157 ASP   A OD2 
3425 O OD2 B ASP   A 157 ? 0.1355 0.1346 0.2020 -0.0050 -0.0108 0.0495  157 ASP   A OD2 
3426 O OD2 T ASP   A 157 ? 0.1753 0.1750 0.2133 0.0233  0.0125  0.0594  157 ASP   A OD2 
3439 N N   A LYS   A 158 ? 0.2053 0.1994 0.2612 0.0245  0.0438  0.0499  158 LYS   A N   
3440 N N   B LYS   A 158 ? 0.1434 0.1232 0.1537 0.0061  0.0043  0.0378  158 LYS   A N   
3441 N N   T LYS   A 158 ? 0.1911 0.1815 0.2089 0.0041  0.0618  0.0697  158 LYS   A N   
3442 C CA  A LYS   A 158 ? 0.2092 0.2146 0.2810 0.0183  0.0507  0.0543  158 LYS   A CA  
3443 C CA  B LYS   A 158 ? 0.1358 0.1328 0.1532 0.0052  0.0066  0.0524  158 LYS   A CA  
3444 C CA  T LYS   A 158 ? 0.2002 0.1993 0.2410 -0.0011 0.0602  0.0658  158 LYS   A CA  
3445 C C   A LYS   A 158 ? 0.1991 0.2148 0.2743 0.0137  0.0368  0.0606  158 LYS   A C   
3446 C C   B LYS   A 158 ? 0.1292 0.1221 0.1565 -0.0027 0.0009  0.0438  158 LYS   A C   
3447 C C   T LYS   A 158 ? 0.1968 0.2004 0.2393 -0.0081 0.0453  0.0666  158 LYS   A C   
3448 O O   A LYS   A 158 ? 0.1980 0.2154 0.2787 0.0076  0.0335  0.0627  158 LYS   A O   
3449 O O   B LYS   A 158 ? 0.1383 0.1272 0.1736 -0.0064 0.0184  0.0317  158 LYS   A O   
3450 O O   T LYS   A 158 ? 0.1979 0.1997 0.2472 -0.0121 0.0377  0.0704  158 LYS   A O   
3451 C CB  A LYS   A 158 ? 0.2265 0.2275 0.3091 0.0139  0.0658  0.0561  158 LYS   A CB  
3452 C CB  B LYS   A 158 ? 0.1483 0.1588 0.1698 0.0075  0.0225  0.0606  158 LYS   A CB  
3453 C CB  T LYS   A 158 ? 0.2177 0.2164 0.2826 -0.0020 0.0672  0.0582  158 LYS   A CB  
3454 C CG  A LYS   A 158 ? 0.2462 0.2422 0.3362 0.0119  0.0766  0.0610  158 LYS   A CG  
3455 C CG  B LYS   A 158 ? 0.1611 0.1852 0.2038 0.0059  0.0328  0.0580  158 LYS   A CG  
3456 C CG  T LYS   A 158 ? 0.2341 0.2330 0.3211 -0.0047 0.0722  0.0577  158 LYS   A CG  
3457 C CD  A LYS   A 158 ? 0.2621 0.2578 0.3621 0.0148  0.0859  0.0629  158 LYS   A CD  
3458 C CD  B LYS   A 158 ? 0.1676 0.2113 0.2324 0.0010  0.0395  0.0441  158 LYS   A CD  
3459 C CD  T LYS   A 158 ? 0.2464 0.2461 0.3598 -0.0047 0.0736  0.0560  158 LYS   A CD  
3460 C CE  A LYS   A 158 ? 0.2729 0.2665 0.3717 0.0163  0.0942  0.0696  158 LYS   A CE  
3461 C CE  B LYS   A 158 ? 0.1741 0.2249 0.2416 0.0010  0.0367  0.0345  158 LYS   A CE  
3462 C CE  T LYS   A 158 ? 0.2559 0.2533 0.3826 -0.0072 0.0749  0.0553  158 LYS   A CE  
3463 N NZ  A LYS   A 158 ? 0.2768 0.2704 0.3762 0.0179  0.0983  0.0723  158 LYS   A NZ  
3464 N NZ  B LYS   A 158 ? 0.1830 0.2296 0.2499 0.0031  0.0346  0.0278  158 LYS   A NZ  
3465 N NZ  T LYS   A 158 ? 0.2596 0.2552 0.3905 -0.0073 0.0776  0.0574  158 LYS   A NZ  
3505 N N   A ASN   A 159 ? 0.1891 0.2138 0.2697 0.0114  0.0222  0.0599  159 ASN   A N   
3506 N N   B ASN   A 159 ? 0.1267 0.1232 0.1563 -0.0028 -0.0073 0.0409  159 ASN   A N   
3507 N N   T ASN   A 159 ? 0.1951 0.2040 0.2438 -0.0117 0.0302  0.0574  159 ASN   A N   
3508 C CA  A ASN   A 159 ? 0.1848 0.2105 0.2549 0.0077  0.0134  0.0609  159 ASN   A CA  
3509 C CA  B ASN   A 159 ? 0.1339 0.1342 0.1906 -0.0059 -0.0086 0.0275  159 ASN   A CA  
3510 C CA  T ASN   A 159 ? 0.1981 0.2078 0.2415 -0.0146 0.0198  0.0508  159 ASN   A CA  
3511 C C   A ASN   A 159 ? 0.1738 0.2042 0.2418 0.0008  0.0174  0.0573  159 ASN   A C   
3512 C C   B ASN   A 159 ? 0.1394 0.1387 0.1955 -0.0106 -0.0053 0.0152  159 ASN   A C   
3513 C C   T ASN   A 159 ? 0.1984 0.2097 0.2416 -0.0185 0.0238  0.0388  159 ASN   A C   
3514 O O   A ASN   A 159 ? 0.1639 0.2017 0.2426 0.0038  0.0071  0.0534  159 ASN   A O   
3515 O O   B ASN   A 159 ? 0.1279 0.1392 0.2046 -0.0137 -0.0118 0.0002  159 ASN   A O   
3516 O O   T ASN   A 159 ? 0.1957 0.2102 0.2443 -0.0187 0.0189  0.0318  159 ASN   A O   
3517 C CB  A ASN   A 159 ? 0.1879 0.2137 0.2609 0.0059  0.0051  0.0683  159 ASN   A CB  
3518 C CB  B ASN   A 159 ? 0.1488 0.1562 0.2205 -0.0073 -0.0217 0.0333  159 ASN   A CB  
3519 C CB  T ASN   A 159 ? 0.1995 0.2109 0.2479 -0.0166 0.0089  0.0595  159 ASN   A CB  
3520 C CG  A ASN   A 159 ? 0.1938 0.2179 0.2791 0.0047  0.0019  0.0696  159 ASN   A CG  
3521 C CG  B ASN   A 159 ? 0.1565 0.1763 0.2425 -0.0015 -0.0177 0.0368  159 ASN   A CG  
3522 C CG  T ASN   A 159 ? 0.2029 0.2141 0.2636 -0.0176 0.0050  0.0657  159 ASN   A CG  
3523 O OD1 A ASN   A 159 ? 0.1971 0.2234 0.2950 0.0056  0.0118  0.0733  159 ASN   A OD1 
3524 O OD1 B ASN   A 159 ? 0.1612 0.1884 0.2630 0.0063  -0.0024 0.0373  159 ASN   A OD1 
3525 O OD1 T ASN   A 159 ? 0.2051 0.2201 0.2790 -0.0159 0.0152  0.0710  159 ASN   A OD1 
3526 N ND2 A ASN   A 159 ? 0.1949 0.2178 0.2805 0.0059  -0.0085 0.0675  159 ASN   A ND2 
3527 N ND2 B ASN   A 159 ? 0.1582 0.1866 0.2442 0.0073  -0.0257 0.0377  159 ASN   A ND2 
3528 N ND2 T ASN   A 159 ? 0.2037 0.2147 0.2644 -0.0162 -0.0053 0.0644  159 ASN   A ND2 
3547 N N   A LEU   A 160 ? 0.1668 0.1980 0.2268 0.0006  0.0237  0.0654  160 LEU   A N   
3548 N N   B LEU   A 160 ? 0.1449 0.1361 0.1904 -0.0028 -0.0007 0.0177  160 LEU   A N   
3549 N N   T LEU   A 160 ? 0.1987 0.2108 0.2400 -0.0159 0.0289  0.0391  160 LEU   A N   
3550 C CA  A LEU   A 160 ? 0.1672 0.1952 0.2097 0.0016  0.0301  0.0639  160 LEU   A CA  
3551 C CA  B LEU   A 160 ? 0.1593 0.1508 0.1912 0.0018  0.0068  0.0151  160 LEU   A CA  
3552 C CA  T LEU   A 160 ? 0.2047 0.2131 0.2326 -0.0150 0.0339  0.0343  160 LEU   A CA  
3553 C C   A LEU   A 160 ? 0.1548 0.1883 0.1917 -0.0005 0.0321  0.0715  160 LEU   A C   
3554 C C   B LEU   A 160 ? 0.1558 0.1444 0.1739 0.0041  0.0136  0.0210  160 LEU   A C   
3555 O O   A LEU   A 160 ? 0.1481 0.1855 0.1781 -0.0064 0.0267  0.0846  160 LEU   A O   
3556 O O   B LEU   A 160 ? 0.1475 0.1438 0.1672 -0.0018 0.0065  0.0114  160 LEU   A O   
3557 C CB  A LEU   A 160 ? 0.1758 0.1987 0.2100 0.0012  0.0332  0.0573  160 LEU   A CB  
3558 C CB  B LEU   A 160 ? 0.1764 0.1686 0.2025 -0.0008 0.0082  0.0052  160 LEU   A CB  
3559 C CB  T LEU   A 160 ? 0.2081 0.2141 0.2267 -0.0159 0.0392  0.0315  160 LEU   A CB  
3560 C CG  A LEU   A 160 ? 0.1816 0.2028 0.2276 0.0011  0.0314  0.0346  160 LEU   A CG  
3561 C CG  B LEU   A 160 ? 0.1940 0.1872 0.2199 -0.0005 -0.0002 -0.0100 160 LEU   A CG  
3562 C CG  T LEU   A 160 ? 0.2109 0.2152 0.2318 -0.0191 0.0412  0.0197  160 LEU   A CG  
3563 C CD1 A LEU   A 160 ? 0.1842 0.2023 0.2369 -0.0004 0.0326  0.0266  160 LEU   A CD1 
3564 C CD1 B LEU   A 160 ? 0.1944 0.1898 0.2228 -0.0036 0.0006  -0.0111 160 LEU   A CD1 
3565 C CD1 T LEU   A 160 ? 0.2133 0.2166 0.2378 -0.0185 0.0411  0.0145  160 LEU   A CD1 
3566 C CD2 A LEU   A 160 ? 0.1845 0.2037 0.2312 0.0009  0.0329  0.0297  160 LEU   A CD2 
3567 C CD2 B LEU   A 160 ? 0.2031 0.1978 0.2251 0.0005  -0.0050 -0.0130 160 LEU   A CD2 
3568 C CD2 T LEU   A 160 ? 0.2120 0.2123 0.2314 -0.0227 0.0443  0.0188  160 LEU   A CD2 
3601 N N   A TYR   A 161 ? 0.1617 0.1875 0.2118 0.0010  0.0305  0.0621  161 TYR   A N   
3602 N N   B TYR   A 161 ? 0.1648 0.1452 0.1882 0.0061  0.0174  0.0238  161 TYR   A N   
3603 C CA  A TYR   A 161 ? 0.1607 0.1900 0.2102 0.0026  0.0339  0.0504  161 TYR   A CA  
3604 C CA  B TYR   A 161 ? 0.1684 0.1497 0.1879 0.0046  0.0182  0.0209  161 TYR   A CA  
3605 C C   A TYR   A 161 ? 0.1584 0.2024 0.2155 0.0061  0.0349  0.0507  161 TYR   A C   
3606 C C   B TYR   A 161 ? 0.1742 0.1565 0.1944 0.0028  0.0120  0.0242  161 TYR   A C   
3607 O O   A TYR   A 161 ? 0.1467 0.2000 0.2029 -0.0004 0.0351  0.0543  161 TYR   A O   
3608 O O   B TYR   A 161 ? 0.1672 0.1581 0.1884 0.0018  0.0050  0.0216  161 TYR   A O   
3609 C CB  A TYR   A 161 ? 0.1618 0.1929 0.2068 0.0086  0.0368  0.0343  161 TYR   A CB  
3610 C CB  B TYR   A 161 ? 0.1679 0.1581 0.1774 0.0091  0.0228  0.0197  161 TYR   A CB  
3611 C CG  A TYR   A 161 ? 0.1507 0.1893 0.1972 0.0133  0.0309  0.0189  161 TYR   A CG  
3612 C CG  B TYR   A 161 ? 0.1556 0.1592 0.1707 0.0087  0.0270  0.0172  161 TYR   A CG  
3613 C CD1 A TYR   A 161 ? 0.1517 0.1863 0.2057 0.0133  0.0236  0.0165  161 TYR   A CD1 
3614 C CD1 B TYR   A 161 ? 0.1550 0.1597 0.1762 0.0077  0.0241  0.0213  161 TYR   A CD1 
3615 C CD2 A TYR   A 161 ? 0.1461 0.1854 0.1911 0.0170  0.0210  0.0137  161 TYR   A CD2 
3616 C CD2 B TYR   A 161 ? 0.1515 0.1607 0.1727 0.0072  0.0291  0.0118  161 TYR   A CD2 
3617 C CE1 A TYR   A 161 ? 0.1507 0.1798 0.2065 0.0116  0.0188  0.0234  161 TYR   A CE1 
3618 C CE1 B TYR   A 161 ? 0.1540 0.1617 0.1785 0.0043  0.0255  0.0272  161 TYR   A CE1 
3619 C CE2 A TYR   A 161 ? 0.1497 0.1750 0.1902 0.0062  0.0169  0.0224  161 TYR   A CE2 
3620 C CE2 B TYR   A 161 ? 0.1518 0.1593 0.1735 -0.0034 0.0310  0.0190  161 TYR   A CE2 
3621 C CZ  A TYR   A 161 ? 0.1572 0.1736 0.1981 0.0016  0.0078  0.0329  161 TYR   A CZ  
3622 C CZ  B TYR   A 161 ? 0.1581 0.1638 0.1756 -0.0056 0.0251  0.0288  161 TYR   A CZ  
3623 O OH  A TYR   A 161 ? 0.1725 0.1818 0.2173 -0.0046 -0.0022 0.0474  161 TYR   A OH  
3624 O OH  B TYR   A 161 ? 0.1675 0.1762 0.1823 -0.0134 0.0264  0.0373  161 TYR   A OH  
3643 N N   A ASP   A 162 ? 0.1568 0.2247 0.2256 0.0049  0.0428  0.0591  162 ASP   A N   
3644 N N   B ASP   A 162 ? 0.1784 0.1620 0.2075 -0.0010 0.0142  0.0338  162 ASP   A N   
3645 C CA  A ASP   A 162 ? 0.1562 0.2465 0.2351 0.0092  0.0394  0.0627  162 ASP   A CA  
3646 C CA  B ASP   A 162 ? 0.1802 0.1698 0.2118 0.0047  0.0137  0.0435  162 ASP   A CA  
3647 C C   A ASP   A 162 ? 0.1497 0.2366 0.2334 -0.0016 0.0255  0.0688  162 ASP   A C   
3648 C C   B ASP   A 162 ? 0.1872 0.1623 0.2189 0.0096  -0.0001 0.0357  162 ASP   A C   
3649 O O   A ASP   A 162 ? 0.1423 0.2320 0.2304 -0.0056 0.0156  0.0728  162 ASP   A O   
3650 O O   B ASP   A 162 ? 0.1818 0.1611 0.2257 0.0097  -0.0099 0.0289  162 ASP   A O   
3651 C CB  A ASP   A 162 ? 0.1643 0.2717 0.2609 0.0202  0.0446  0.0587  162 ASP   A CB  
3652 C CB  B ASP   A 162 ? 0.1758 0.1800 0.2207 0.0104  0.0220  0.0600  162 ASP   A CB  
3653 C CG  A ASP   A 162 ? 0.1829 0.2969 0.2881 0.0194  0.0477  0.0573  162 ASP   A CG  
3654 C CG  B ASP   A 162 ? 0.1720 0.1833 0.2156 0.0134  0.0294  0.0847  162 ASP   A CG  
3655 O OD1 A ASP   A 162 ? 0.1895 0.3035 0.2859 0.0211  0.0561  0.0641  162 ASP   A OD1 
3656 O OD1 B ASP   A 162 ? 0.1723 0.1889 0.2133 0.0220  0.0340  0.0971  162 ASP   A OD1 
3657 O OD2 A ASP   A 162 ? 0.1937 0.3105 0.3068 0.0217  0.0548  0.0463  162 ASP   A OD2 
3658 O OD2 B ASP   A 162 ? 0.1720 0.1851 0.2228 0.0159  0.0348  0.0804  162 ASP   A OD2 
3667 N N   A LYS   A 163 ? 0.1581 0.2433 0.2308 -0.0031 0.0196  0.0614  163 LYS   A N   
3668 N N   B LYS   A 163 ? 0.2022 0.1654 0.2143 0.0066  -0.0007 0.0387  163 LYS   A N   
3669 C CA  A LYS   A 163 ? 0.1698 0.2522 0.2351 -0.0051 0.0039  0.0488  163 LYS   A CA  
3670 C CA  B LYS   A 163 ? 0.2134 0.1756 0.2194 0.0092  -0.0036 0.0403  163 LYS   A CA  
3671 C C   A LYS   A 163 ? 0.1564 0.2390 0.2209 -0.0139 0.0089  0.0463  163 LYS   A C   
3672 C C   B LYS   A 163 ? 0.2073 0.1677 0.2033 0.0057  -0.0089 0.0207  163 LYS   A C   
3673 O O   A LYS   A 163 ? 0.1526 0.2398 0.2333 -0.0140 0.0088  0.0386  163 LYS   A O   
3674 O O   B LYS   A 163 ? 0.2045 0.1607 0.1970 -0.0028 -0.0111 -0.0015 163 LYS   A O   
3675 C CB  A LYS   A 163 ? 0.2016 0.2771 0.2711 0.0103  -0.0078 0.0401  163 LYS   A CB  
3676 C CB  B LYS   A 163 ? 0.2336 0.1967 0.2423 0.0140  0.0051  0.0522  163 LYS   A CB  
3677 C CG  A LYS   A 163 ? 0.2323 0.2993 0.3248 0.0164  -0.0102 0.0298  163 LYS   A CG  
3678 C CG  B LYS   A 163 ? 0.2557 0.2230 0.2805 0.0159  0.0101  0.0527  163 LYS   A CG  
3679 C CD  A LYS   A 163 ? 0.2549 0.3173 0.3816 0.0210  -0.0077 0.0195  163 LYS   A CD  
3680 C CD  B LYS   A 163 ? 0.2747 0.2457 0.3225 0.0203  0.0162  0.0481  163 LYS   A CD  
3681 C CE  A LYS   A 163 ? 0.2700 0.3276 0.4229 0.0250  -0.0006 0.0128  163 LYS   A CE  
3682 C CE  B LYS   A 163 ? 0.2881 0.2615 0.3540 0.0262  0.0187  0.0446  163 LYS   A CE  
3683 N NZ  A LYS   A 163 ? 0.2771 0.3344 0.4461 0.0276  0.0037  0.0111  163 LYS   A NZ  
3684 N NZ  B LYS   A 163 ? 0.2943 0.2689 0.3762 0.0288  0.0171  0.0429  163 LYS   A NZ  
3711 N N   A LEU   A 164 ? 0.1384 0.2209 0.1887 -0.0147 0.0106  0.0463  164 LEU   A N   
3712 N N   B LEU   A 164 ? 0.1994 0.1697 0.1901 0.0087  -0.0046 0.0184  164 LEU   A N   
3713 C CA  A LEU   A 164 ? 0.1360 0.2100 0.1770 -0.0225 0.0244  0.0326  164 LEU   A CA  
3714 C CA  B LEU   A 164 ? 0.1952 0.1723 0.1845 0.0069  0.0040  0.0198  164 LEU   A CA  
3715 C C   A LEU   A 164 ? 0.1347 0.2051 0.1765 -0.0207 0.0234  0.0251  164 LEU   A C   
3716 C C   B LEU   A 164 ? 0.1873 0.1604 0.1856 0.0087  -0.0007 0.0242  164 LEU   A C   
3717 O O   A LEU   A 164 ? 0.1347 0.2084 0.1638 -0.0257 0.0417  0.0188  164 LEU   A O   
3718 O O   B LEU   A 164 ? 0.1890 0.1617 0.1932 0.0068  -0.0016 0.0254  164 LEU   A O   
3719 C CB  A LEU   A 164 ? 0.1340 0.2008 0.1740 -0.0286 0.0347  0.0300  164 LEU   A CB  
3720 C CB  B LEU   A 164 ? 0.1945 0.1822 0.1831 0.0074  0.0152  0.0165  164 LEU   A CB  
3721 C CG  A LEU   A 164 ? 0.1418 0.1937 0.1852 -0.0243 0.0280  0.0269  164 LEU   A CG  
3722 C CG  B LEU   A 164 ? 0.1959 0.1890 0.1829 0.0061  0.0248  0.0152  164 LEU   A CG  
3723 C CD1 A LEU   A 164 ? 0.1373 0.1889 0.1935 -0.0231 0.0216  0.0317  164 LEU   A CD1 
3724 C CD1 B LEU   A 164 ? 0.1920 0.1921 0.1864 0.0084  0.0301  0.0193  164 LEU   A CD1 
3725 C CD2 A LEU   A 164 ? 0.1489 0.1915 0.1807 -0.0234 0.0264  0.0292  164 LEU   A CD2 
3726 C CD2 B LEU   A 164 ? 0.1992 0.1908 0.1800 -0.0001 0.0248  0.0146  164 LEU   A CD2 
3749 N N   A VAL   A 165 ? 0.1343 0.2028 0.1761 -0.0198 0.0218  0.0353  165 VAL   A N   
3750 N N   B VAL   A 165 ? 0.1781 0.1510 0.1692 0.0056  0.0019  0.0336  165 VAL   A N   
3751 C CA  A VAL   A 165 ? 0.1408 0.2118 0.1740 -0.0126 0.0256  0.0361  165 VAL   A CA  
3752 C CA  B VAL   A 165 ? 0.1705 0.1472 0.1632 0.0108  -0.0043 0.0335  165 VAL   A CA  
3753 C C   A VAL   A 165 ? 0.1424 0.2162 0.1773 -0.0151 0.0281  0.0382  165 VAL   A C   
3754 C C   B VAL   A 165 ? 0.1600 0.1451 0.1633 0.0035  0.0036  0.0293  165 VAL   A C   
3755 O O   A VAL   A 165 ? 0.1455 0.2200 0.1794 -0.0242 0.0384  0.0252  165 VAL   A O   
3756 O O   B VAL   A 165 ? 0.1574 0.1389 0.1671 0.0027  0.0065  0.0259  165 VAL   A O   
3757 C CB  A VAL   A 165 ? 0.1540 0.2159 0.1717 -0.0044 0.0293  0.0372  165 VAL   A CB  
3758 C CB  B VAL   A 165 ? 0.1886 0.1539 0.1747 0.0123  -0.0009 0.0265  165 VAL   A CB  
3759 C CG1 A VAL   A 165 ? 0.1545 0.2199 0.1596 0.0003  0.0353  0.0279  165 VAL   A CG1 
3760 C CG1 B VAL   A 165 ? 0.1923 0.1574 0.1671 0.0144  -0.0001 0.0187  165 VAL   A CG1 
3761 C CG2 A VAL   A 165 ? 0.1603 0.2181 0.1846 -0.0017 0.0265  0.0421  165 VAL   A CG2 
3762 C CG2 B VAL   A 165 ? 0.1932 0.1511 0.1911 0.0131  -0.0036 0.0295  165 VAL   A CG2 
3781 N N   A SER   A 166 ? 0.1359 0.2217 0.1893 -0.0136 0.0272  0.0465  166 SER   A N   
3782 N N   B SER   A 166 ? 0.1534 0.1594 0.1666 -0.0031 0.0087  0.0247  166 SER   A N   
3783 C CA  A SER   A 166 ? 0.1427 0.2343 0.2123 -0.0150 0.0245  0.0426  166 SER   A CA  
3784 C CA  B SER   A 166 ? 0.1583 0.1788 0.1759 -0.0035 0.0004  0.0137  166 SER   A CA  
3785 C C   A SER   A 166 ? 0.1449 0.2461 0.2152 -0.0131 0.0102  0.0440  166 SER   A C   
3786 C C   B SER   A 166 ? 0.1567 0.1843 0.1689 -0.0051 0.0014  0.0124  166 SER   A C   
3787 O O   A SER   A 166 ? 0.1526 0.2594 0.2310 -0.0106 0.0001  0.0375  166 SER   A O   
3788 O O   B SER   A 166 ? 0.1499 0.1861 0.1633 -0.0066 -0.0219 0.0140  166 SER   A O   
3789 C CB  A SER   A 166 ? 0.1533 0.2395 0.2441 -0.0088 0.0168  0.0312  166 SER   A CB  
3790 C CB  B SER   A 166 ? 0.1659 0.1964 0.2071 -0.0003 -0.0150 0.0078  166 SER   A CB  
3791 O OG  A SER   A 166 ? 0.1702 0.2506 0.2672 -0.0110 0.0174  0.0285  166 SER   A OG  
3792 O OG  B SER   A 166 ? 0.1740 0.2125 0.2404 -0.0037 -0.0176 0.0125  166 SER   A OG  
3803 N N   A SER   A 167 ? 0.1485 0.2492 0.1984 -0.0071 0.0091  0.0421  167 SER   A N   
3804 N N   B SER   A 167 ? 0.1628 0.1931 0.1554 0.0031  0.0104  0.0148  167 SER   A N   
3805 C CA  A SER   A 167 ? 0.1676 0.2543 0.2020 -0.0051 0.0026  0.0303  167 SER   A CA  
3806 C CA  B SER   A 167 ? 0.1808 0.2001 0.1540 0.0038  0.0107  0.0179  167 SER   A CA  
3807 C C   A SER   A 167 ? 0.1692 0.2515 0.1964 0.0004  0.0224  0.0271  167 SER   A C   
3808 C C   B SER   A 167 ? 0.1885 0.1986 0.1677 0.0085  0.0254  0.0200  167 SER   A C   
3809 O O   A SER   A 167 ? 0.1958 0.2585 0.2126 0.0024  0.0062  0.0301  167 SER   A O   
3810 O O   B SER   A 167 ? 0.2051 0.2071 0.1841 0.0081  0.0145  0.0166  167 SER   A O   
3811 C CB  A SER   A 167 ? 0.1846 0.2650 0.1998 -0.0065 0.0047  0.0374  167 SER   A CB  
3812 C CB  B SER   A 167 ? 0.1910 0.2122 0.1365 -0.0005 0.0145  0.0223  167 SER   A CB  
3813 O OG  A SER   A 167 ? 0.1888 0.2686 0.2155 -0.0094 0.0083  0.0370  167 SER   A OG  
3814 O OG  B SER   A 167 ? 0.1916 0.2181 0.1419 -0.0038 0.0310  0.0194  167 SER   A OG  
3825 N N   A PHE   A 168 ? 0.1585 0.2427 0.1894 0.0109  0.0226  0.0226  168 PHE   A N   
3826 N N   B PHE   A 168 ? 0.1858 0.1899 0.1692 0.0196  0.0330  0.0262  168 PHE   A N   
3827 C CA  A PHE   A 168 ? 0.1560 0.2380 0.1843 0.0014  0.0306  0.0200  168 PHE   A CA  
3828 C CA  B PHE   A 168 ? 0.1878 0.1879 0.1856 0.0219  0.0311  0.0299  168 PHE   A CA  
3829 C C   A PHE   A 168 ? 0.1714 0.2526 0.2082 -0.0039 0.0669  0.0151  168 PHE   A C   
3830 C C   B PHE   A 168 ? 0.1945 0.1871 0.1962 0.0200  0.0383  0.0117  168 PHE   A C   
3831 O O   A PHE   A 168 ? 0.1789 0.2584 0.2616 -0.0223 0.0780  0.0213  168 PHE   A O   
3832 O O   B PHE   A 168 ? 0.1989 0.1819 0.2180 0.0095  0.0459  -0.0049 168 PHE   A O   
3833 C CB  A PHE   A 168 ? 0.1546 0.2264 0.1700 -0.0035 0.0104  0.0136  168 PHE   A CB  
3834 C CB  B PHE   A 168 ? 0.1897 0.1923 0.1935 0.0243  0.0326  0.0460  168 PHE   A CB  
3835 C CG  A PHE   A 168 ? 0.1488 0.2193 0.1635 -0.0084 -0.0028 0.0025  168 PHE   A CG  
3836 C CG  B PHE   A 168 ? 0.1863 0.1945 0.2009 0.0220  0.0420  0.0589  168 PHE   A CG  
3837 C CD1 A PHE   A 168 ? 0.1463 0.2183 0.1639 -0.0128 -0.0064 0.0069  168 PHE   A CD1 
3838 C CD1 B PHE   A 168 ? 0.1868 0.1964 0.2126 0.0208  0.0417  0.0643  168 PHE   A CD1 
3839 C CD2 A PHE   A 168 ? 0.1499 0.2206 0.1723 -0.0110 0.0023  -0.0003 168 PHE   A CD2 
3840 C CD2 B PHE   A 168 ? 0.1842 0.1968 0.2044 0.0114  0.0565  0.0682  168 PHE   A CD2 
3841 C CE1 A PHE   A 168 ? 0.1409 0.2181 0.1602 -0.0162 -0.0026 0.0096  168 PHE   A CE1 
3842 C CE1 B PHE   A 168 ? 0.1861 0.1998 0.2212 0.0183  0.0451  0.0699  168 PHE   A CE1 
3843 C CE2 A PHE   A 168 ? 0.1576 0.2139 0.1842 -0.0106 0.0004  0.0083  168 PHE   A CE2 
3844 C CE2 B PHE   A 168 ? 0.1882 0.1943 0.2153 0.0110  0.0519  0.0745  168 PHE   A CE2 
3845 C CZ  A PHE   A 168 ? 0.1489 0.2130 0.1755 -0.0145 -0.0047 0.0041  168 PHE   A CZ  
3846 C CZ  B PHE   A 168 ? 0.1862 0.1974 0.2197 0.0135  0.0461  0.0723  168 PHE   A CZ  
3865 N N   A LEU   A 169 ? 0.2011 0.2594 0.2224 -0.0044 0.0677  0.0007  169 LEU   A N   
3866 N N   B LEU   A 169 ? 0.2106 0.1901 0.2070 0.0192  0.0298  0.0060  169 LEU   A N   
3867 C CA  A LEU   A 169 ? 0.2354 0.2739 0.2698 0.0082  0.0494  -0.0135 169 LEU   A CA  
3868 C CA  B LEU   A 169 ? 0.2239 0.1998 0.2256 0.0274  0.0192  0.0017  169 LEU   A CA  
3869 C C   A LEU   A 169 ? 0.2275 0.2757 0.2834 0.0083  0.0542  0.0036  169 LEU   A C   
3870 C C   B LEU   A 169 ? 0.2140 0.1966 0.2116 0.0233  0.0168  0.0323  169 LEU   A C   
3871 O O   A LEU   A 169 ? 0.2311 0.2853 0.3004 0.0120  0.0389  0.0031  169 LEU   A O   
3872 O O   B LEU   A 169 ? 0.2135 0.2075 0.2213 0.0242  0.0164  0.0381  169 LEU   A O   
3873 C CB  A LEU   A 169 ? 0.2667 0.2885 0.2971 0.0120  0.0327  -0.0386 169 LEU   A CB  
3874 C CB  B LEU   A 169 ? 0.2450 0.2194 0.2548 0.0267  0.0129  -0.0247 169 LEU   A CB  
3875 C CG  A LEU   A 169 ? 0.2935 0.3023 0.3261 0.0101  0.0181  -0.0620 169 LEU   A CG  
3876 C CG  B LEU   A 169 ? 0.2608 0.2370 0.2860 0.0217  0.0079  -0.0444 169 LEU   A CG  
3877 C CD1 A LEU   A 169 ? 0.3025 0.3050 0.3425 0.0051  0.0052  -0.0665 169 LEU   A CD1 
3878 C CD1 B LEU   A 169 ? 0.2664 0.2413 0.3044 0.0173  -0.0017 -0.0478 169 LEU   A CD1 
3879 C CD2 A LEU   A 169 ? 0.3023 0.3097 0.3341 0.0069  0.0180  -0.0695 169 LEU   A CD2 
3880 C CD2 B LEU   A 169 ? 0.2672 0.2440 0.2927 0.0185  0.0121  -0.0488 169 LEU   A CD2 
3881 O OXT A LEU   A 169 ? 0.2158 0.2777 0.2854 0.0054  0.0665  0.0109  169 LEU   A OXT 
3882 O OXT B LEU   A 169 ? 0.2133 0.1970 0.2002 0.0191  0.0149  0.0377  169 LEU   A OXT 
3905 N N   A SER   B 1   ? 0.3605 0.3539 0.3689 -0.0915 -0.0824 0.0472  1   SER   B N   
3906 N N   B SER   B 1   ? 0.3231 0.3378 0.3370 -0.0798 -0.0665 0.0438  1   SER   B N   
3907 C CA  A SER   B 1   ? 0.3548 0.3549 0.3739 -0.0943 -0.0828 0.0437  1   SER   B CA  
3908 C CA  B SER   B 1   ? 0.3172 0.3377 0.3371 -0.0812 -0.0670 0.0414  1   SER   B CA  
3909 C C   A SER   B 1   ? 0.3325 0.3525 0.3561 -0.0957 -0.0828 0.0594  1   SER   B C   
3910 C C   B SER   B 1   ? 0.2981 0.3324 0.3119 -0.0810 -0.0720 0.0515  1   SER   B C   
3911 O O   A SER   B 1   ? 0.3418 0.3551 0.3375 -0.0891 -0.0725 0.0592  1   SER   B O   
3912 O O   B SER   B 1   ? 0.2994 0.3327 0.2899 -0.0784 -0.0764 0.0528  1   SER   B O   
3913 C CB  A SER   B 1   ? 0.3665 0.3539 0.3840 -0.0932 -0.0777 0.0291  1   SER   B CB  
3914 C CB  B SER   B 1   ? 0.3262 0.3395 0.3514 -0.0808 -0.0588 0.0303  1   SER   B CB  
3915 O OG  A SER   B 1   ? 0.3802 0.3626 0.4275 -0.0893 -0.0696 0.0227  1   SER   B OG  
3916 O OG  B SER   B 1   ? 0.3363 0.3471 0.3870 -0.0790 -0.0523 0.0247  1   SER   B OG  
3931 N N   A MET   B 2   ? 0.3057 0.3441 0.3483 -0.0995 -0.0838 0.0918  2   MET   B N   
3932 N N   B MET   B 2   ? 0.2828 0.3246 0.3020 -0.0793 -0.0655 0.0716  2   MET   B N   
3933 C CA  A MET   B 2   ? 0.2871 0.3388 0.3579 -0.0836 -0.0837 0.1120  2   MET   B CA  
3934 C CA  B MET   B 2   ? 0.2740 0.3191 0.3034 -0.0645 -0.0582 0.0819  2   MET   B CA  
3935 C C   A MET   B 2   ? 0.2482 0.3099 0.3174 -0.0728 -0.0933 0.1406  2   MET   B C   
3936 C C   B MET   B 2   ? 0.2532 0.2966 0.2672 -0.0535 -0.0496 0.0861  2   MET   B C   
3937 O O   A MET   B 2   ? 0.2430 0.3196 0.3225 -0.0620 -0.1054 0.1429  2   MET   B O   
3938 O O   B MET   B 2   ? 0.2550 0.3043 0.2717 -0.0475 -0.0434 0.0816  2   MET   B O   
3939 C CB  A MET   B 2   ? 0.3170 0.3675 0.4380 -0.0636 -0.0623 0.0897  2   MET   B CB  
3940 C CB  B MET   B 2   ? 0.2945 0.3400 0.3581 -0.0508 -0.0538 0.0802  2   MET   B CB  
3941 C CG  A MET   B 2   ? 0.3439 0.3914 0.5113 -0.0437 -0.0412 0.0739  2   MET   B CG  
3942 C CG  B MET   B 2   ? 0.3115 0.3579 0.4042 -0.0387 -0.0467 0.0847  2   MET   B CG  
3943 S SD  A MET   B 2   ? 0.3696 0.4137 0.5823 -0.0273 -0.0285 0.0619  2   MET   B SD  
3944 S SD  B MET   B 2   ? 0.3285 0.3762 0.4501 -0.0271 -0.0440 0.0884  2   MET   B SD  
3945 C CE  A MET   B 2   ? 0.3728 0.4179 0.5847 -0.0257 -0.0213 0.0621  2   MET   B CE  
3946 C CE  B MET   B 2   ? 0.3295 0.3778 0.4493 -0.0264 -0.0424 0.0836  2   MET   B CE  
3965 N N   A VAL   B 3   ? 0.2180 0.2692 0.2891 -0.0763 -0.0862 0.1506  3   VAL   B N   
3966 N N   B VAL   B 3   ? 0.2326 0.2660 0.2352 -0.0502 -0.0453 0.0853  3   VAL   B N   
3967 C CA  A VAL   B 3   ? 0.2053 0.2373 0.2832 -0.0674 -0.0759 0.1298  3   VAL   B CA  
3968 C CA  B VAL   B 3   ? 0.2188 0.2400 0.2204 -0.0427 -0.0365 0.0674  3   VAL   B CA  
3969 C C   A VAL   B 3   ? 0.1850 0.2193 0.2472 -0.0591 -0.0622 0.1095  3   VAL   B C   
3970 C C   B VAL   B 3   ? 0.1993 0.2239 0.1969 -0.0380 -0.0323 0.0639  3   VAL   B C   
3971 O O   A VAL   B 3   ? 0.1767 0.2106 0.2616 -0.0618 -0.0639 0.1153  3   VAL   B O   
3972 O O   B VAL   B 3   ? 0.1991 0.2240 0.1732 -0.0238 -0.0281 0.0441  3   VAL   B O   
3973 C CB  A VAL   B 3   ? 0.2219 0.2311 0.3294 -0.0735 -0.0676 0.1073  3   VAL   B CB  
3974 C CB  B VAL   B 3   ? 0.2269 0.2301 0.2360 -0.0438 -0.0295 0.0535  3   VAL   B CB  
3975 C CG1 A VAL   B 3   ? 0.2281 0.2276 0.3482 -0.0761 -0.0648 0.0965  3   VAL   B CG1 
3976 C CG1 B VAL   B 3   ? 0.2297 0.2277 0.2467 -0.0451 -0.0281 0.0499  3   VAL   B CG1 
3977 C CG2 A VAL   B 3   ? 0.2271 0.2287 0.3464 -0.0772 -0.0567 0.1090  3   VAL   B CG2 
3978 C CG2 B VAL   B 3   ? 0.2297 0.2274 0.2371 -0.0436 -0.0266 0.0525  3   VAL   B CG2 
3997 N N   . ASN   B 4   ? 0.1842 0.2074 0.2034 -0.0510 -0.0456 0.0766  4   ASN   B N   
3998 C CA  . ASN   B 4   ? 0.1868 0.2072 0.1764 -0.0489 -0.0391 0.0429  4   ASN   B CA  
3999 C C   . ASN   B 4   ? 0.1971 0.2185 0.1725 -0.0543 -0.0243 0.0340  4   ASN   B C   
4000 O O   . ASN   B 4   ? 0.2033 0.2263 0.1943 -0.0539 -0.0245 0.0115  4   ASN   B O   
4001 C CB  . ASN   B 4   ? 0.1811 0.2006 0.1718 -0.0424 -0.0441 0.0373  4   ASN   B CB  
4002 C CG  . ASN   B 4   ? 0.1747 0.1840 0.1599 -0.0457 -0.0458 0.0349  4   ASN   B CG  
4003 O OD1 . ASN   B 4   ? 0.1764 0.1740 0.1607 -0.0405 -0.0452 0.0274  4   ASN   B OD1 
4004 N ND2 . ASN   B 4   ? 0.1916 0.1885 0.1727 -0.0281 -0.0413 0.0279  4   ASN   B ND2 
4012 N N   . SER   B 5   ? 0.2125 0.2376 0.1730 -0.0561 -0.0033 0.0346  5   SER   B N   
4013 C CA  . SER   B 5   ? 0.2375 0.2714 0.2090 -0.0438 0.0209  0.0317  5   SER   B CA  
4014 C C   . SER   B 5   ? 0.2514 0.2747 0.2418 -0.0545 0.0422  0.0303  5   SER   B C   
4015 O O   . SER   B 5   ? 0.2644 0.2681 0.3200 -0.0506 0.0670  0.0277  5   SER   B O   
4016 C CB  . SER   B 5   ? 0.2528 0.2944 0.2383 -0.0345 0.0255  0.0368  5   SER   B CB  
4017 O OG  . SER   B 5   ? 0.2683 0.3193 0.3008 -0.0262 0.0292  0.0369  5   SER   B OG  
4023 N N   . PHE   B 6   ? 0.2648 0.2897 0.2064 -0.0601 0.0431  0.0383  6   PHE   B N   
4024 C CA  . PHE   B 6   ? 0.2668 0.2918 0.1783 -0.0790 0.0386  0.0150  6   PHE   B CA  
4025 C C   . PHE   B 6   ? 0.3119 0.3245 0.2109 -0.0832 0.0561  -0.0156 6   PHE   B C   
4026 O O   . PHE   B 6   ? 0.3267 0.3594 0.2428 -0.0759 0.0383  -0.0338 6   PHE   B O   
4027 C CB  . PHE   B 6   ? 0.2344 0.2703 0.1605 -0.0673 0.0186  0.0139  6   PHE   B CB  
4028 C CG  . PHE   B 6   ? 0.2038 0.2402 0.1587 -0.0636 0.0043  0.0190  6   PHE   B CG  
4029 C CD1 . PHE   B 6   ? 0.2052 0.2116 0.1429 -0.0625 -0.0103 0.0194  6   PHE   B CD1 
4030 C CD2 . PHE   B 6   ? 0.1839 0.2405 0.1620 -0.0517 -0.0034 0.0400  6   PHE   B CD2 
4031 C CE1 . PHE   B 6   ? 0.2030 0.1979 0.1502 -0.0481 -0.0178 0.0226  6   PHE   B CE1 
4032 C CE2 . PHE   B 6   ? 0.1918 0.2294 0.1897 -0.0426 -0.0007 0.0384  6   PHE   B CE2 
4033 C CZ  . PHE   B 6   ? 0.1947 0.2083 0.1734 -0.0435 -0.0068 0.0232  6   PHE   B CZ  
4043 N N   . SER   B 7   ? 0.3441 0.3074 0.2192 -0.0966 0.0798  -0.0432 7   SER   B N   
4044 C CA  . SER   B 7   ? 0.3742 0.3111 0.2637 -0.0946 0.0953  -0.0505 7   SER   B CA  
4045 C C   . SER   B 7   ? 0.3678 0.2966 0.2625 -0.0954 0.1160  -0.0517 7   SER   B C   
4046 O O   . SER   B 7   ? 0.3741 0.3023 0.2933 -0.0960 0.1157  -0.0501 7   SER   B O   
4047 C CB  . SER   B 7   ? 0.4001 0.3257 0.3189 -0.0886 0.1005  -0.0535 7   SER   B CB  
4048 O OG  . SER   B 7   ? 0.4146 0.3379 0.3706 -0.0866 0.0973  -0.0476 7   SER   B OG  
4054 N N   A GLY   B 8   ? 0.3647 0.2879 0.2677 -0.0877 0.1252  -0.0549 8   GLY   B N   
4055 N N   B GLY   B 8   ? 0.3631 0.2868 0.2651 -0.0891 0.1192  -0.0546 8   GLY   B N   
4056 C CA  A GLY   B 8   ? 0.3555 0.2739 0.2732 -0.0857 0.1272  -0.0569 8   GLY   B CA  
4057 C CA  B GLY   B 8   ? 0.3543 0.2737 0.2685 -0.0862 0.1185  -0.0563 8   GLY   B CA  
4058 C C   A GLY   B 8   ? 0.3428 0.2501 0.2651 -0.0873 0.1273  -0.0534 8   GLY   B C   
4059 C C   B GLY   B 8   ? 0.3429 0.2539 0.2612 -0.0853 0.1169  -0.0553 8   GLY   B C   
4060 O O   A GLY   B 8   ? 0.3500 0.2504 0.2939 -0.0826 0.1285  -0.0566 8   GLY   B O   
4061 O O   B GLY   B 8   ? 0.3479 0.2570 0.2798 -0.0804 0.1149  -0.0579 8   GLY   B O   
4068 N N   . TYR   B 9   ? 0.3324 0.2382 0.2429 -0.0807 0.1101  -0.0628 9   TYR   B N   
4069 C CA  . TYR   B 9   ? 0.3096 0.2085 0.2148 -0.0666 0.0787  -0.0491 9   TYR   B CA  
4070 C C   . TYR   B 9   ? 0.3014 0.2100 0.1948 -0.0587 0.0519  -0.0429 9   TYR   B C   
4071 O O   . TYR   B 9   ? 0.3176 0.2244 0.2315 -0.0613 0.0433  -0.0325 9   TYR   B O   
4072 C CB  . TYR   B 9   ? 0.3001 0.1872 0.2206 -0.0579 0.0772  -0.0476 9   TYR   B CB  
4073 C CG  . TYR   B 9   ? 0.2894 0.1706 0.2310 -0.0634 0.0656  -0.0536 9   TYR   B CG  
4074 C CD1 . TYR   B 9   ? 0.2915 0.1759 0.2552 -0.0738 0.0657  -0.0508 9   TYR   B CD1 
4075 C CD2 . TYR   B 9   ? 0.2773 0.1593 0.2231 -0.0576 0.0668  -0.0546 9   TYR   B CD2 
4076 C CE1 . TYR   B 9   ? 0.2884 0.1817 0.2493 -0.0810 0.0738  -0.0633 9   TYR   B CE1 
4077 C CE2 . TYR   B 9   ? 0.2772 0.1591 0.2361 -0.0569 0.0732  -0.0544 9   TYR   B CE2 
4078 C CZ  . TYR   B 9   ? 0.2845 0.1803 0.2453 -0.0737 0.0735  -0.0721 9   TYR   B CZ  
4079 O OH  . TYR   B 9   ? 0.2834 0.1952 0.2563 -0.0868 0.0785  -0.0821 9   TYR   B OH  
4090 N N   . LEU   B 10  ? 0.2730 0.1881 0.1703 -0.0509 0.0332  -0.0441 10  LEU   B N   
4091 C CA  . LEU   B 10  ? 0.2672 0.1835 0.1761 -0.0610 -0.0058 -0.0361 10  LEU   B CA  
4092 C C   . LEU   B 10  ? 0.2437 0.1821 0.1720 -0.0642 -0.0171 -0.0396 10  LEU   B C   
4093 O O   . LEU   B 10  ? 0.2269 0.1870 0.1802 -0.0475 -0.0083 -0.0306 10  LEU   B O   
4094 C CB  . LEU   B 10  ? 0.2833 0.1827 0.1928 -0.0657 -0.0225 -0.0129 10  LEU   B CB  
4095 C CG  . LEU   B 10  ? 0.3034 0.1897 0.2377 -0.0606 -0.0506 -0.0012 10  LEU   B CG  
4096 C CD1 . LEU   B 10  ? 0.3205 0.2024 0.2731 -0.0575 -0.0464 -0.0032 10  LEU   B CD1 
4097 C CD2 . LEU   B 10  ? 0.3100 0.1969 0.2737 -0.0609 -0.0467 0.0206  10  LEU   B CD2 
4109 N N   . LYS   B 11  ? 0.2602 0.2091 0.1793 -0.0530 -0.0211 -0.0336 11  LYS   B N   
4110 C CA  . LYS   B 11  ? 0.2730 0.2354 0.2060 -0.0440 -0.0477 -0.0410 11  LYS   B CA  
4111 C C   . LYS   B 11  ? 0.2594 0.2174 0.2101 -0.0645 -0.0439 -0.0501 11  LYS   B C   
4112 O O   . LYS   B 11  ? 0.2784 0.2332 0.2439 -0.0758 -0.0315 -0.0810 11  LYS   B O   
4113 C CB  . LYS   B 11  ? 0.3062 0.2856 0.2781 -0.0135 -0.0534 -0.0324 11  LYS   B CB  
4114 C CG  . LYS   B 11  ? 0.3358 0.3187 0.3532 0.0045  -0.0566 -0.0317 11  LYS   B CG  
4115 C CD  . LYS   B 11  ? 0.3583 0.3421 0.4296 0.0137  -0.0542 -0.0351 11  LYS   B CD  
4116 C CE  . LYS   B 11  ? 0.3782 0.3581 0.4820 0.0158  -0.0519 -0.0387 11  LYS   B CE  
4117 N NZ  . LYS   B 11  ? 0.3859 0.3675 0.5104 0.0152  -0.0535 -0.0376 11  LYS   B NZ  
4131 N N   . LEU   B 12  ? 0.2316 0.1953 0.2214 -0.0578 -0.0395 -0.0401 12  LEU   B N   
4132 C CA  . LEU   B 12  ? 0.2205 0.1727 0.2359 -0.0534 -0.0411 -0.0327 12  LEU   B CA  
4133 C C   . LEU   B 12  ? 0.2106 0.1762 0.2366 -0.0573 -0.0468 -0.0322 12  LEU   B C   
4134 O O   . LEU   B 12  ? 0.2150 0.1815 0.2511 -0.0648 -0.0532 -0.0272 12  LEU   B O   
4135 C CB  . LEU   B 12  ? 0.2218 0.1514 0.2316 -0.0425 -0.0344 -0.0352 12  LEU   B CB  
4136 C CG  . LEU   B 12  ? 0.2168 0.1534 0.2317 -0.0430 -0.0200 -0.0313 12  LEU   B CG  
4137 C CD1 . LEU   B 12  ? 0.2248 0.1616 0.2261 -0.0338 -0.0140 -0.0113 12  LEU   B CD1 
4138 C CD2 . LEU   B 12  ? 0.2198 0.1608 0.2465 -0.0404 -0.0131 -0.0384 12  LEU   B CD2 
4150 N N   . THR   B 13  ? 0.1984 0.1773 0.2381 -0.0547 -0.0437 -0.0419 13  THR   B N   
4151 C CA  . THR   B 13  ? 0.1964 0.1840 0.2306 -0.0585 -0.0483 -0.0291 13  THR   B CA  
4152 C C   . THR   B 13  ? 0.2345 0.1975 0.2489 -0.0651 -0.0693 -0.0243 13  THR   B C   
4153 O O   . THR   B 13  ? 0.2570 0.1988 0.2653 -0.0643 -0.0327 -0.0231 13  THR   B O   
4154 C CB  . THR   B 13  ? 0.1746 0.1893 0.2321 -0.0497 -0.0441 -0.0215 13  THR   B CB  
4155 O OG1 . THR   B 13  ? 0.1720 0.1792 0.2358 -0.0411 -0.0367 -0.0239 13  THR   B OG1 
4156 C CG2 . THR   B 13  ? 0.1796 0.2035 0.2396 -0.0515 -0.0342 -0.0003 13  THR   B CG2 
4164 N N   A ASP   B 14  ? 0.2433 0.2141 0.2542 -0.0677 -0.1051 -0.0074 14  ASP   B N   
4165 N N   B ASP   B 14  ? 0.2417 0.2102 0.2630 -0.0607 -0.0818 -0.0086 14  ASP   B N   
4166 C CA  A ASP   B 14  ? 0.2559 0.2271 0.2918 -0.0654 -0.1028 0.0162  14  ASP   B CA  
4167 C CA  B ASP   B 14  ? 0.2490 0.2194 0.2889 -0.0551 -0.0756 0.0080  14  ASP   B CA  
4168 C C   A ASP   B 14  ? 0.2430 0.2067 0.2515 -0.0654 -0.0809 0.0123  14  ASP   B C   
4169 C C   B ASP   B 14  ? 0.2314 0.2003 0.2556 -0.0541 -0.0679 0.0071  14  ASP   B C   
4170 O O   A ASP   B 14  ? 0.2620 0.2116 0.2403 -0.0625 -0.0815 0.0232  14  ASP   B O   
4171 O O   B ASP   B 14  ? 0.2382 0.1974 0.2543 -0.0472 -0.0654 0.0111  14  ASP   B O   
4172 C CB  A ASP   B 14  ? 0.2742 0.2600 0.3700 -0.0624 -0.1228 0.0192  14  ASP   B CB  
4173 C CB  B ASP   B 14  ? 0.2692 0.2468 0.3466 -0.0498 -0.0777 0.0107  14  ASP   B CB  
4174 C CG  A ASP   B 14  ? 0.2998 0.2902 0.4541 -0.0538 -0.1199 0.0106  14  ASP   B CG  
4175 C CG  B ASP   B 14  ? 0.2911 0.2718 0.4036 -0.0414 -0.0721 0.0058  14  ASP   B CG  
4176 O OD1 A ASP   B 14  ? 0.3138 0.3012 0.4742 -0.0570 -0.1149 -0.0009 14  ASP   B OD1 
4177 O OD1 B ASP   B 14  ? 0.2989 0.2840 0.4181 -0.0388 -0.0633 0.0046  14  ASP   B OD1 
4178 O OD2 A ASP   B 14  ? 0.3023 0.2992 0.4939 -0.0514 -0.1197 0.0143  14  ASP   B OD2 
4179 O OD2 B ASP   B 14  ? 0.2969 0.2775 0.4260 -0.0445 -0.0754 0.0032  14  ASP   B OD2 
4188 N N   . ASN   B 15  ? 0.2076 0.1825 0.2248 -0.0543 -0.0700 0.0075  15  ASN   B N   
4189 C CA  . ASN   B 15  ? 0.1723 0.1568 0.2068 -0.0360 -0.0456 -0.0014 15  ASN   B CA  
4190 C C   . ASN   B 15  ? 0.1581 0.1446 0.1834 -0.0221 -0.0321 -0.0033 15  ASN   B C   
4191 O O   . ASN   B 15  ? 0.1577 0.1418 0.2083 -0.0194 -0.0390 -0.0174 15  ASN   B O   
4192 C CB  . ASN   B 15  ? 0.1679 0.1578 0.2245 -0.0187 -0.0492 -0.0035 15  ASN   B CB  
4193 C CG  . ASN   B 15  ? 0.1571 0.1521 0.2292 -0.0256 -0.0213 -0.0045 15  ASN   B CG  
4194 O OD1 . ASN   B 15  ? 0.1671 0.1809 0.2535 -0.0463 -0.0303 0.0055  15  ASN   B OD1 
4195 N ND2 . ASN   B 15  ? 0.1539 0.1330 0.2174 -0.0128 -0.0045 -0.0145 15  ASN   B ND2 
4203 N N   . VAL   B 16  ? 0.1643 0.1417 0.1864 -0.0270 -0.0486 -0.0070 16  VAL   B N   
4204 C CA  . VAL   B 16  ? 0.1659 0.1404 0.1689 -0.0269 -0.0272 -0.0247 16  VAL   B CA  
4205 C C   . VAL   B 16  ? 0.1557 0.1469 0.1693 -0.0417 -0.0278 -0.0089 16  VAL   B C   
4206 O O   . VAL   B 16  ? 0.1592 0.1663 0.2020 -0.0357 -0.0227 -0.0271 16  VAL   B O   
4207 C CB  . VAL   B 16  ? 0.1689 0.1388 0.1880 -0.0175 -0.0220 -0.0213 16  VAL   B CB  
4208 C CG1 . VAL   B 16  ? 0.1785 0.1303 0.1834 -0.0043 -0.0214 -0.0118 16  VAL   B CG1 
4209 C CG2 . VAL   B 16  ? 0.1679 0.1444 0.2083 -0.0111 -0.0153 -0.0205 16  VAL   B CG2 
4219 N N   . TYR   B 17  ? 0.1612 0.1565 0.1727 -0.0298 -0.0237 -0.0186 17  TYR   B N   
4220 C CA  . TYR   B 17  ? 0.1710 0.1658 0.1684 -0.0353 -0.0243 -0.0080 17  TYR   B CA  
4221 C C   . TYR   B 17  ? 0.1636 0.1450 0.1744 -0.0332 -0.0186 -0.0130 17  TYR   B C   
4222 O O   . TYR   B 17  ? 0.1606 0.1529 0.1723 -0.0281 -0.0249 -0.0312 17  TYR   B O   
4223 C CB  . TYR   B 17  ? 0.2025 0.2078 0.1887 -0.0270 -0.0259 0.0275  17  TYR   B CB  
4224 C CG  . TYR   B 17  ? 0.2297 0.2530 0.2287 -0.0216 -0.0355 0.0332  17  TYR   B CG  
4225 C CD1 . TYR   B 17  ? 0.2441 0.2651 0.2445 -0.0162 -0.0494 0.0498  17  TYR   B CD1 
4226 C CD2 . TYR   B 17  ? 0.2518 0.2817 0.2533 -0.0119 -0.0441 0.0327  17  TYR   B CD2 
4227 C CE1 . TYR   B 17  ? 0.2619 0.2889 0.2503 -0.0078 -0.0640 0.0418  17  TYR   B CE1 
4228 C CE2 . TYR   B 17  ? 0.2681 0.3014 0.2683 -0.0009 -0.0609 0.0386  17  TYR   B CE2 
4229 C CZ  . TYR   B 17  ? 0.2773 0.3073 0.2725 0.0006  -0.0701 0.0416  17  TYR   B CZ  
4230 O OH  . TYR   B 17  ? 0.2957 0.3221 0.3123 0.0093  -0.0721 0.0367  17  TYR   B OH  
4240 N N   . ILE   B 18  ? 0.1817 0.1422 0.1677 -0.0315 -0.0107 -0.0153 18  ILE   B N   
4241 C CA  . ILE   B 18  ? 0.1820 0.1341 0.1588 -0.0303 -0.0152 -0.0184 18  ILE   B CA  
4242 C C   . ILE   B 18  ? 0.1956 0.1440 0.1577 -0.0351 -0.0041 -0.0284 18  ILE   B C   
4243 O O   . ILE   B 18  ? 0.2158 0.1568 0.1721 -0.0363 0.0068  -0.0370 18  ILE   B O   
4244 C CB  . ILE   B 18  ? 0.1864 0.1400 0.1769 -0.0373 -0.0126 -0.0142 18  ILE   B CB  
4245 C CG1 . ILE   B 18  ? 0.1900 0.1436 0.1929 -0.0376 -0.0158 0.0059  18  ILE   B CG1 
4246 C CG2 . ILE   B 18  ? 0.1873 0.1435 0.1742 -0.0384 -0.0163 -0.0121 18  ILE   B CG2 
4247 C CD1 . ILE   B 18  ? 0.1973 0.1719 0.2164 -0.0334 -0.0257 0.0219  18  ILE   B CD1 
4259 N N   . LYS   B 19  ? 0.1917 0.1500 0.1795 -0.0210 0.0228  -0.0359 19  LYS   B N   
4260 C CA  . LYS   B 19  ? 0.1998 0.1486 0.2003 -0.0250 0.0290  -0.0379 19  LYS   B CA  
4261 C C   . LYS   B 19  ? 0.1843 0.1421 0.2105 -0.0265 0.0290  -0.0455 19  LYS   B C   
4262 O O   . LYS   B 19  ? 0.1740 0.1468 0.1978 -0.0183 0.0176  -0.0384 19  LYS   B O   
4263 C CB  . LYS   B 19  ? 0.2225 0.1684 0.2168 -0.0294 0.0454  -0.0251 19  LYS   B CB  
4264 C CG  . LYS   B 19  ? 0.2500 0.1912 0.2304 -0.0313 0.0475  -0.0248 19  LYS   B CG  
4265 C CD  . LYS   B 19  ? 0.2809 0.2218 0.2407 -0.0430 0.0510  -0.0200 19  LYS   B CD  
4266 C CE  . LYS   B 19  ? 0.3088 0.2491 0.2709 -0.0456 0.0521  -0.0232 19  LYS   B CE  
4267 N NZ  . LYS   B 19  ? 0.3247 0.2652 0.2759 -0.0511 0.0578  -0.0190 19  LYS   B NZ  
4281 N N   . ASN   B 20  ? 0.1858 0.1645 0.2362 -0.0197 0.0358  -0.0592 20  ASN   B N   
4282 C CA  . ASN   B 20  ? 0.1895 0.1755 0.2565 -0.0141 0.0395  -0.0662 20  ASN   B CA  
4283 C C   . ASN   B 20  ? 0.1815 0.1914 0.2553 -0.0197 0.0511  -0.0801 20  ASN   B C   
4284 O O   . ASN   B 20  ? 0.1980 0.2254 0.2794 -0.0338 0.0542  -0.0761 20  ASN   B O   
4285 C CB  . ASN   B 20  ? 0.2137 0.1773 0.2783 0.0061  0.0283  -0.0683 20  ASN   B CB  
4286 C CG  . ASN   B 20  ? 0.2367 0.1831 0.2966 0.0346  0.0321  -0.0923 20  ASN   B CG  
4287 O OD1 . ASN   B 20  ? 0.2642 0.2131 0.3310 0.0446  0.0253  -0.0886 20  ASN   B OD1 
4288 N ND2 . ASN   B 20  ? 0.2245 0.1866 0.2975 0.0339  0.0159  -0.0879 20  ASN   B ND2 
4295 N N   . ALA   B 21  ? 0.1792 0.1779 0.2524 -0.0232 0.0507  -0.0683 21  ALA   B N   
4296 C CA  . ALA   B 21  ? 0.1909 0.1838 0.2713 -0.0314 0.0296  -0.0522 21  ALA   B CA  
4297 C C   . ALA   B 21  ? 0.1912 0.1579 0.2545 -0.0204 0.0278  -0.0370 21  ALA   B C   
4298 O O   . ALA   B 21  ? 0.1922 0.1533 0.2623 -0.0302 0.0288  -0.0336 21  ALA   B O   
4299 C CB  . ALA   B 21  ? 0.2080 0.2118 0.2753 -0.0404 0.0353  -0.0358 21  ALA   B CB  
4305 N N   . ASP   B 22  ? 0.1832 0.1485 0.2528 -0.0193 0.0253  -0.0325 22  ASP   B N   
4306 C CA  . ASP   B 22  ? 0.1743 0.1462 0.2349 -0.0062 0.0216  -0.0232 22  ASP   B CA  
4307 C C   . ASP   B 22  ? 0.1671 0.1403 0.1933 -0.0170 0.0197  -0.0113 22  ASP   B C   
4308 O O   . ASP   B 22  ? 0.1711 0.1478 0.2035 -0.0106 0.0156  -0.0024 22  ASP   B O   
4309 C CB  . ASP   B 22  ? 0.1828 0.1581 0.2750 -0.0020 0.0135  -0.0044 22  ASP   B CB  
4310 C CG  . ASP   B 22  ? 0.1850 0.1746 0.3166 -0.0009 -0.0079 -0.0018 22  ASP   B CG  
4311 O OD1 . ASP   B 22  ? 0.1998 0.1673 0.3174 0.0020  -0.0263 0.0021  22  ASP   B OD1 
4312 O OD2 . ASP   B 22  ? 0.1965 0.2014 0.3672 0.0151  -0.0277 -0.0158 22  ASP   B OD2 
4317 N N   . ILE   B 23  ? 0.1675 0.1376 0.1729 -0.0036 0.0071  0.0143  23  ILE   B N   
4318 C CA  . ILE   B 23  ? 0.1633 0.1424 0.1538 -0.0056 -0.0001 0.0026  23  ILE   B CA  
4319 C C   . ILE   B 23  ? 0.1534 0.1398 0.1531 -0.0099 -0.0112 0.0066  23  ILE   B C   
4320 O O   . ILE   B 23  ? 0.1472 0.1420 0.1458 -0.0093 -0.0005 0.0087  23  ILE   B O   
4321 C CB  . ILE   B 23  ? 0.1591 0.1465 0.1740 -0.0097 -0.0024 0.0100  23  ILE   B CB  
4322 C CG1 . ILE   B 23  ? 0.1577 0.1564 0.1887 -0.0146 0.0057  0.0239  23  ILE   B CG1 
4323 C CG2 . ILE   B 23  ? 0.1700 0.1683 0.1806 -0.0170 0.0024  0.0082  23  ILE   B CG2 
4324 C CD1 . ILE   B 23  ? 0.1604 0.1717 0.1875 -0.0077 0.0115  0.0245  23  ILE   B CD1 
4336 N N   . VAL   B 24  ? 0.1559 0.1382 0.1666 -0.0111 -0.0115 0.0017  24  VAL   B N   
4337 C CA  . VAL   B 24  ? 0.1538 0.1481 0.1859 -0.0106 -0.0225 -0.0027 24  VAL   B CA  
4338 C C   . VAL   B 24  ? 0.1510 0.1517 0.1982 -0.0095 -0.0099 0.0050  24  VAL   B C   
4339 O O   . VAL   B 24  ? 0.1505 0.1564 0.2087 -0.0153 -0.0041 0.0160  24  VAL   B O   
4340 C CB  . VAL   B 24  ? 0.1652 0.1691 0.1910 -0.0006 -0.0261 -0.0073 24  VAL   B CB  
4341 C CG1 . VAL   B 24  ? 0.1649 0.1720 0.2302 -0.0087 -0.0295 -0.0023 24  VAL   B CG1 
4342 C CG2 . VAL   B 24  ? 0.1692 0.1937 0.2020 0.0064  -0.0281 -0.0140 24  VAL   B CG2 
4352 N N   . GLU   B 25  ? 0.1670 0.1590 0.1946 -0.0078 0.0031  -0.0027 25  GLU   B N   
4353 C CA  . GLU   B 25  ? 0.1867 0.1767 0.2132 -0.0032 0.0045  -0.0193 25  GLU   B CA  
4354 C C   . GLU   B 25  ? 0.1789 0.1688 0.1902 -0.0125 0.0053  -0.0121 25  GLU   B C   
4355 O O   . GLU   B 25  ? 0.1763 0.1933 0.2046 -0.0105 0.0159  0.0094  25  GLU   B O   
4356 C CB  . GLU   B 25  ? 0.2293 0.2228 0.2704 0.0182  0.0027  -0.0176 25  GLU   B CB  
4357 C CG  . GLU   B 25  ? 0.2638 0.2811 0.3775 0.0284  -0.0024 -0.0200 25  GLU   B CG  
4358 C CD  . GLU   B 25  ? 0.3076 0.3368 0.4685 0.0226  -0.0064 -0.0207 25  GLU   B CD  
4359 O OE1 . GLU   B 25  ? 0.3393 0.3622 0.4991 0.0247  0.0002  -0.0169 25  GLU   B OE1 
4360 O OE2 . GLU   B 25  ? 0.3373 0.3571 0.5000 0.0210  -0.0137 -0.0274 25  GLU   B OE2 
4367 N N   . GLU   B 26  ? 0.1784 0.1636 0.1723 -0.0323 -0.0038 -0.0025 26  GLU   B N   
4368 C CA  . GLU   B 26  ? 0.1775 0.1819 0.1673 -0.0444 -0.0044 0.0061  26  GLU   B CA  
4369 C C   . GLU   B 26  ? 0.1570 0.1756 0.1624 -0.0288 0.0067  0.0256  26  GLU   B C   
4370 O O   . GLU   B 26  ? 0.1764 0.2027 0.1654 -0.0243 -0.0022 0.0340  26  GLU   B O   
4371 C CB  . GLU   B 26  ? 0.2108 0.2096 0.1812 -0.0560 0.0058  0.0189  26  GLU   B CB  
4372 C CG  . GLU   B 26  ? 0.2523 0.2484 0.2432 -0.0579 0.0200  -0.0020 26  GLU   B CG  
4373 C CD  . GLU   B 26  ? 0.2750 0.2699 0.2616 -0.0801 0.0293  -0.0388 26  GLU   B CD  
4374 O OE1 . GLU   B 26  ? 0.2948 0.2561 0.2677 -0.0899 0.0713  -0.0398 26  GLU   B OE1 
4375 O OE2 . GLU   B 26  ? 0.2748 0.3068 0.2861 -0.0784 0.0315  -0.0240 26  GLU   B OE2 
4382 N N   . ALA   B 27  ? 0.1450 0.1613 0.1702 -0.0225 0.0090  0.0187  27  ALA   B N   
4383 C CA  . ALA   B 27  ? 0.1473 0.1549 0.1798 -0.0173 0.0086  0.0259  27  ALA   B CA  
4384 C C   . ALA   B 27  ? 0.1555 0.1642 0.1961 -0.0136 0.0191  0.0368  27  ALA   B C   
4385 O O   . ALA   B 27  ? 0.1597 0.1708 0.2201 -0.0017 0.0162  0.0452  27  ALA   B O   
4386 C CB  . ALA   B 27  ? 0.1605 0.1407 0.1833 -0.0163 -0.0015 0.0273  27  ALA   B CB  
4392 N N   . LYS   B 28  ? 0.1500 0.1762 0.2344 -0.0189 0.0170  0.0492  28  LYS   B N   
4393 C CA  . LYS   B 28  ? 0.1591 0.2106 0.2731 -0.0132 0.0483  0.0776  28  LYS   B CA  
4394 C C   . LYS   B 28  ? 0.1829 0.2333 0.2623 -0.0033 0.0533  0.0719  28  LYS   B C   
4395 O O   . LYS   B 28  ? 0.2123 0.2426 0.2719 -0.0005 0.0574  0.0758  28  LYS   B O   
4396 C CB  . LYS   B 28  ? 0.1788 0.2418 0.3298 0.0006  0.0716  0.0943  28  LYS   B CB  
4397 C CG  . LYS   B 28  ? 0.2079 0.2837 0.3722 0.0075  0.0746  0.1078  28  LYS   B CG  
4398 C CD  . LYS   B 28  ? 0.2677 0.3453 0.4291 0.0102  0.0917  0.1089  28  LYS   B CD  
4399 C CE  . LYS   B 28  ? 0.3111 0.3913 0.4776 0.0192  0.0978  0.1135  28  LYS   B CE  
4400 N NZ  . LYS   B 28  ? 0.3309 0.4004 0.4953 0.0252  0.0995  0.1200  28  LYS   B NZ  
4414 N N   . LYS   B 29  ? 0.2016 0.2575 0.2653 0.0160  0.0680  0.0577  29  LYS   B N   
4415 C CA  . LYS   B 29  ? 0.2473 0.2922 0.2905 0.0199  0.0685  0.0599  29  LYS   B CA  
4416 C C   . LYS   B 29  ? 0.2415 0.2963 0.2478 0.0206  0.0576  0.0730  29  LYS   B C   
4417 O O   . LYS   B 29  ? 0.2613 0.3202 0.2543 0.0233  0.0551  0.0785  29  LYS   B O   
4418 C CB  . LYS   B 29  ? 0.3036 0.3269 0.3674 0.0213  0.0641  0.0456  29  LYS   B CB  
4419 C CG  . LYS   B 29  ? 0.3515 0.3517 0.4507 0.0200  0.0645  0.0436  29  LYS   B CG  
4420 C CD  . LYS   B 29  ? 0.3938 0.3708 0.5161 0.0155  0.0700  0.0383  29  LYS   B CD  
4421 C CE  . LYS   B 29  ? 0.4221 0.3851 0.5596 0.0105  0.0773  0.0343  29  LYS   B CE  
4422 N NZ  . LYS   B 29  ? 0.4329 0.3880 0.5881 0.0071  0.0794  0.0306  29  LYS   B NZ  
4436 N N   . VAL   B 30  ? 0.2124 0.2772 0.2325 0.0136  0.0508  0.0776  30  VAL   B N   
4437 C CA  . VAL   B 30  ? 0.1984 0.2706 0.2555 0.0014  0.0171  0.0824  30  VAL   B CA  
4438 C C   . VAL   B 30  ? 0.1767 0.2676 0.2527 0.0024  0.0256  0.1092  30  VAL   B C   
4439 O O   . VAL   B 30  ? 0.1938 0.2881 0.2601 0.0120  0.0262  0.1216  30  VAL   B O   
4440 C CB  . VAL   B 30  ? 0.2038 0.2614 0.2775 -0.0138 -0.0174 0.0749  30  VAL   B CB  
4441 C CG1 . VAL   B 30  ? 0.2065 0.2639 0.2718 -0.0162 -0.0153 0.0619  30  VAL   B CG1 
4442 C CG2 . VAL   B 30  ? 0.2196 0.2661 0.3037 -0.0218 -0.0241 0.0589  30  VAL   B CG2 
4452 N N   . LYS   B 31  ? 0.1654 0.2314 0.2994 -0.0182 0.0185  0.1207  31  LYS   B N   
4453 C CA  . LYS   B 31  ? 0.1518 0.2283 0.3410 -0.0329 0.0119  0.1187  31  LYS   B CA  
4454 C C   . LYS   B 31  ? 0.1411 0.1885 0.2915 -0.0325 -0.0134 0.0994  31  LYS   B C   
4455 O O   . LYS   B 31  ? 0.1550 0.2076 0.3062 -0.0204 -0.0079 0.1166  31  LYS   B O   
4456 C CB  . LYS   B 31  ? 0.1727 0.2791 0.4001 -0.0310 0.0354  0.1373  31  LYS   B CB  
4457 C CG  . LYS   B 31  ? 0.2100 0.3310 0.4382 -0.0283 0.0442  0.1358  31  LYS   B CG  
4458 C CD  . LYS   B 31  ? 0.2621 0.3854 0.4759 -0.0188 0.0386  0.1210  31  LYS   B CD  
4459 C CE  . LYS   B 31  ? 0.2990 0.4160 0.5087 -0.0149 0.0327  0.1102  31  LYS   B CE  
4460 N NZ  . LYS   B 31  ? 0.3089 0.4351 0.5183 -0.0094 0.0242  0.1016  31  LYS   B NZ  
4474 N N   . PRO   B 32  ? 0.1544 0.1523 0.2131 -0.0274 -0.0338 0.0538  32  PRO   B N   
4475 C CA  . PRO   B 32  ? 0.1665 0.1477 0.1687 -0.0297 -0.0342 0.0324  32  PRO   B CA  
4476 C C   . PRO   B 32  ? 0.1756 0.1388 0.1692 -0.0340 -0.0505 0.0299  32  PRO   B C   
4477 O O   . PRO   B 32  ? 0.1913 0.1380 0.1930 -0.0351 -0.0699 0.0308  32  PRO   B O   
4478 C CB  . PRO   B 32  ? 0.1840 0.1455 0.1659 -0.0363 -0.0309 0.0221  32  PRO   B CB  
4479 C CG  . PRO   B 32  ? 0.2021 0.1358 0.1781 -0.0290 -0.0548 0.0319  32  PRO   B CG  
4480 C CD  . PRO   B 32  ? 0.1889 0.1387 0.1894 -0.0260 -0.0578 0.0325  32  PRO   B CD  
4488 N N   . THR   B 33  ? 0.1741 0.1314 0.1524 -0.0271 -0.0471 0.0231  33  THR   B N   
4489 C CA  . THR   B 33  ? 0.1803 0.1377 0.1509 -0.0304 -0.0465 0.0217  33  THR   B CA  
4490 C C   . THR   B 33  ? 0.1851 0.1275 0.1497 -0.0300 -0.0468 0.0182  33  THR   B C   
4491 O O   . THR   B 33  ? 0.2092 0.1298 0.1555 -0.0369 -0.0511 0.0200  33  THR   B O   
4492 C CB  . THR   B 33  ? 0.1910 0.1455 0.1633 -0.0152 -0.0485 0.0272  33  THR   B CB  
4493 O OG1 . THR   B 33  ? 0.1882 0.1540 0.1636 -0.0205 -0.0454 0.0348  33  THR   B OG1 
4494 C CG2 . THR   B 33  ? 0.2074 0.1516 0.1802 -0.0100 -0.0438 0.0274  33  THR   B CG2 
4502 N N   . VAL   B 34  ? 0.1710 0.1284 0.1351 -0.0323 -0.0413 0.0147  34  VAL   B N   
4503 C CA  . VAL   B 34  ? 0.1574 0.1227 0.1284 -0.0240 -0.0351 0.0104  34  VAL   B CA  
4504 C C   . VAL   B 34  ? 0.1451 0.1220 0.1220 -0.0269 -0.0227 0.0084  34  VAL   B C   
4505 O O   . VAL   B 34  ? 0.1633 0.1207 0.1302 -0.0277 -0.0349 0.0070  34  VAL   B O   
4506 C CB  . VAL   B 34  ? 0.1593 0.1339 0.1568 -0.0095 -0.0383 0.0031  34  VAL   B CB  
4507 C CG1 . VAL   B 34  ? 0.1634 0.1473 0.1691 -0.0093 -0.0211 0.0071  34  VAL   B CG1 
4508 C CG2 . VAL   B 34  ? 0.1687 0.1376 0.1854 -0.0074 -0.0316 -0.0044 34  VAL   B CG2 
4518 N N   . VAL   B 35  ? 0.1360 0.1189 0.1149 -0.0244 -0.0116 0.0034  35  VAL   B N   
4519 C CA  . VAL   B 35  ? 0.1292 0.1157 0.1051 -0.0197 -0.0030 0.0061  35  VAL   B CA  
4520 C C   . VAL   B 35  ? 0.1220 0.1134 0.1102 -0.0138 -0.0110 0.0043  35  VAL   B C   
4521 O O   . VAL   B 35  ? 0.1330 0.1193 0.1158 -0.0216 -0.0022 -0.0079 35  VAL   B O   
4522 C CB  . VAL   B 35  ? 0.1288 0.1274 0.1157 -0.0136 0.0007  0.0020  35  VAL   B CB  
4523 C CG1 . VAL   B 35  ? 0.1263 0.1489 0.1404 -0.0180 -0.0020 0.0001  35  VAL   B CG1 
4524 C CG2 . VAL   B 35  ? 0.1312 0.1271 0.1357 -0.0027 0.0002  -0.0034 35  VAL   B CG2 
4534 N N   . VAL   B 36  ? 0.1230 0.1126 0.1076 -0.0133 -0.0106 0.0119  36  VAL   B N   
4535 C CA  . VAL   B 36  ? 0.1259 0.1009 0.1021 -0.0067 -0.0058 0.0085  36  VAL   B CA  
4536 C C   . VAL   B 36  ? 0.1189 0.1066 0.1032 -0.0128 -0.0101 0.0045  36  VAL   B C   
4537 O O   . VAL   B 36  ? 0.1260 0.1181 0.1207 -0.0053 -0.0007 -0.0055 36  VAL   B O   
4538 C CB  . VAL   B 36  ? 0.1249 0.1096 0.1166 -0.0126 -0.0089 0.0044  36  VAL   B CB  
4539 C CG1 . VAL   B 36  ? 0.1266 0.1238 0.1273 -0.0227 -0.0093 0.0007  36  VAL   B CG1 
4540 C CG2 . VAL   B 36  ? 0.1385 0.1166 0.1279 -0.0104 -0.0069 0.0011  36  VAL   B CG2 
4550 N N   . ASN   B 37  ? 0.1238 0.1159 0.1070 -0.0065 -0.0068 0.0027  37  ASN   B N   
4551 C CA  . ASN   B 37  ? 0.1212 0.1166 0.1138 -0.0008 -0.0133 0.0036  37  ASN   B CA  
4552 C C   . ASN   B 37  ? 0.1161 0.1163 0.1197 0.0024  -0.0065 0.0086  37  ASN   B C   
4553 O O   . ASN   B 37  ? 0.1293 0.1273 0.1187 0.0013  -0.0044 0.0082  37  ASN   B O   
4554 C CB  . ASN   B 37  ? 0.1242 0.1164 0.1151 -0.0023 -0.0143 0.0003  37  ASN   B CB  
4555 C CG  . ASN   B 37  ? 0.1301 0.1259 0.1187 -0.0053 -0.0127 0.0010  37  ASN   B CG  
4556 O OD1 . ASN   B 37  ? 0.1399 0.1252 0.1402 0.0116  -0.0162 0.0003  37  ASN   B OD1 
4557 N ND2 . ASN   B 37  ? 0.1372 0.1187 0.1181 0.0032  -0.0184 0.0098  37  ASN   B ND2 
4564 N N   . ALA   B 38  ? 0.1223 0.1187 0.1187 0.0074  0.0051  0.0085  38  ALA   B N   
4565 C CA  . ALA   B 38  ? 0.1371 0.1167 0.1202 0.0019  0.0043  0.0040  38  ALA   B CA  
4566 C C   . ALA   B 38  ? 0.1382 0.1168 0.1223 0.0045  0.0036  0.0124  38  ALA   B C   
4567 O O   . ALA   B 38  ? 0.1502 0.1227 0.1329 0.0065  -0.0066 0.0051  38  ALA   B O   
4568 C CB  . ALA   B 38  ? 0.1540 0.1303 0.1275 -0.0036 0.0146  0.0019  38  ALA   B CB  
4574 N N   . ALA   B 39  ? 0.1342 0.1239 0.1170 0.0106  -0.0039 0.0068  39  ALA   B N   
4575 C CA  . ALA   B 39  ? 0.1432 0.1263 0.1106 0.0052  -0.0058 0.0090  39  ALA   B CA  
4576 C C   . ALA   B 39  ? 0.1458 0.1342 0.1008 0.0118  0.0002  0.0031  39  ALA   B C   
4577 O O   . ALA   B 39  ? 0.1461 0.1457 0.1364 0.0016  -0.0002 0.0068  39  ALA   B O   
4578 C CB  . ALA   B 39  ? 0.1432 0.1359 0.1327 -0.0008 0.0027  -0.0060 39  ALA   B CB  
4584 N N   . ASN   B 40  ? 0.1499 0.1570 0.1052 -0.0029 -0.0024 -0.0100 40  ASN   B N   
4585 C CA  . ASN   B 40  ? 0.1577 0.1652 0.1121 0.0014  -0.0088 -0.0099 40  ASN   B CA  
4586 C C   . ASN   B 40  ? 0.1601 0.1679 0.1055 0.0054  -0.0111 -0.0041 40  ASN   B C   
4587 O O   . ASN   B 40  ? 0.1596 0.1590 0.1106 0.0081  -0.0121 -0.0008 40  ASN   B O   
4588 C CB  . ASN   B 40  ? 0.1715 0.1608 0.1294 0.0097  -0.0066 0.0027  40  ASN   B CB  
4589 C CG  . ASN   B 40  ? 0.1744 0.1620 0.1576 0.0020  -0.0215 0.0075  40  ASN   B CG  
4590 O OD1 . ASN   B 40  ? 0.1720 0.1551 0.2409 0.0024  -0.0361 0.0103  40  ASN   B OD1 
4591 N ND2 . ASN   B 40  ? 0.1787 0.1632 0.1686 -0.0021 -0.0128 0.0172  40  ASN   B ND2 
4598 N N   . VAL   B 41  ? 0.1673 0.1679 0.1171 0.0076  0.0022  -0.0103 41  VAL   B N   
4599 C CA  . VAL   B 41  ? 0.1807 0.1756 0.1186 0.0109  -0.0022 -0.0128 41  VAL   B CA  
4600 C C   . VAL   B 41  ? 0.1796 0.1767 0.1078 0.0174  -0.0104 -0.0155 41  VAL   B C   
4601 O O   . VAL   B 41  ? 0.1727 0.1704 0.1318 0.0132  -0.0133 -0.0151 41  VAL   B O   
4602 C CB  . VAL   B 41  ? 0.1955 0.1927 0.1366 -0.0025 0.0114  -0.0260 41  VAL   B CB  
4603 C CG1 . VAL   B 41  ? 0.1963 0.1961 0.1530 -0.0041 0.0228  -0.0171 41  VAL   B CG1 
4604 C CG2 . VAL   B 41  ? 0.1997 0.2111 0.1442 -0.0140 0.0124  -0.0284 41  VAL   B CG2 
4614 N N   . TYR   B 42  ? 0.1800 0.1725 0.1162 0.0169  -0.0192 -0.0002 42  TYR   B N   
4615 C CA  . TYR   B 42  ? 0.1829 0.1805 0.1314 0.0135  -0.0278 -0.0122 42  TYR   B CA  
4616 C C   . TYR   B 42  ? 0.1716 0.1552 0.1320 0.0157  -0.0246 -0.0122 42  TYR   B C   
4617 O O   . TYR   B 42  ? 0.1824 0.1642 0.1684 0.0089  -0.0280 -0.0218 42  TYR   B O   
4618 C CB  . TYR   B 42  ? 0.2086 0.2106 0.1512 0.0085  -0.0395 -0.0055 42  TYR   B CB  
4619 C CG  . TYR   B 42  ? 0.2182 0.2303 0.1435 -0.0024 -0.0307 0.0097  42  TYR   B CG  
4620 C CD1 . TYR   B 42  ? 0.2161 0.2298 0.1093 -0.0068 -0.0104 0.0046  42  TYR   B CD1 
4621 C CD2 . TYR   B 42  ? 0.2368 0.2475 0.1804 -0.0056 -0.0126 0.0201  42  TYR   B CD2 
4622 C CE1 . TYR   B 42  ? 0.2310 0.2505 0.1204 -0.0032 -0.0074 0.0069  42  TYR   B CE1 
4623 C CE2 . TYR   B 42  ? 0.2415 0.2613 0.1676 -0.0046 0.0134  0.0340  42  TYR   B CE2 
4624 C CZ  . TYR   B 42  ? 0.2510 0.2735 0.1599 0.0070  0.0148  0.0181  42  TYR   B CZ  
4625 O OH  . TYR   B 42  ? 0.2849 0.2976 0.2074 0.0226  0.0270  0.0307  42  TYR   B OH  
4635 N N   . LEU   B 43  ? 0.1565 0.1431 0.1248 0.0063  -0.0141 -0.0094 43  LEU   B N   
4636 C CA  . LEU   B 43  ? 0.1572 0.1394 0.1282 0.0012  -0.0164 -0.0025 43  LEU   B CA  
4637 C C   . LEU   B 43  ? 0.1638 0.1427 0.1230 0.0016  -0.0153 -0.0074 43  LEU   B C   
4638 O O   . LEU   B 43  ? 0.1598 0.1485 0.1543 0.0022  -0.0226 0.0016  43  LEU   B O   
4639 C CB  . LEU   B 43  ? 0.1580 0.1396 0.1389 0.0027  -0.0242 -0.0120 43  LEU   B CB  
4640 C CG  . LEU   B 43  ? 0.1570 0.1353 0.1326 0.0051  -0.0212 -0.0089 43  LEU   B CG  
4641 C CD1 . LEU   B 43  ? 0.1672 0.1414 0.1754 0.0086  -0.0370 -0.0160 43  LEU   B CD1 
4642 C CD2 . LEU   B 43  ? 0.1540 0.1444 0.1366 -0.0025 -0.0175 -0.0028 43  LEU   B CD2 
4654 N N   . LYS   B 44  ? 0.1603 0.1439 0.1265 0.0088  -0.0120 -0.0089 44  LYS   B N   
4655 C CA  . LYS   B 44  ? 0.1710 0.1587 0.1279 0.0091  -0.0121 0.0018  44  LYS   B CA  
4656 C C   . LYS   B 44  ? 0.1609 0.1553 0.1302 0.0049  -0.0135 0.0082  44  LYS   B C   
4657 O O   . LYS   B 44  ? 0.1786 0.1549 0.1526 -0.0015 -0.0090 0.0047  44  LYS   B O   
4658 C CB  . LYS   B 44  ? 0.1996 0.1795 0.1516 0.0184  -0.0309 0.0011  44  LYS   B CB  
4659 C CG  . LYS   B 44  ? 0.2434 0.2068 0.1949 0.0087  -0.0561 0.0007  44  LYS   B CG  
4660 C CD  . LYS   B 44  ? 0.2826 0.2295 0.2474 -0.0102 -0.0715 -0.0098 44  LYS   B CD  
4661 C CE  . LYS   B 44  ? 0.3132 0.2518 0.2967 -0.0147 -0.0749 -0.0049 44  LYS   B CE  
4662 N NZ  . LYS   B 44  ? 0.3242 0.2615 0.3222 -0.0098 -0.0819 0.0102  44  LYS   B NZ  
4676 N N   . HIS   B 45  ? 0.1579 0.1546 0.1251 0.0020  -0.0160 0.0127  45  HIS   B N   
4677 C CA  . HIS   B 45  ? 0.1583 0.1475 0.1292 0.0078  -0.0161 0.0033  45  HIS   B CA  
4678 C C   . HIS   B 45  ? 0.1798 0.1624 0.1669 0.0168  -0.0256 -0.0095 45  HIS   B C   
4679 O O   . HIS   B 45  ? 0.1936 0.1944 0.2134 0.0440  0.0059  -0.0041 45  HIS   B O   
4680 C CB  . HIS   B 45  ? 0.1451 0.1519 0.1378 0.0053  -0.0073 -0.0032 45  HIS   B CB  
4681 C CG  . HIS   B 45  ? 0.1492 0.1470 0.1296 -0.0066 -0.0097 -0.0038 45  HIS   B CG  
4682 N ND1 . HIS   B 45  ? 0.1518 0.1450 0.1375 -0.0013 -0.0115 -0.0043 45  HIS   B ND1 
4683 C CD2 . HIS   B 45  ? 0.1608 0.1506 0.1354 -0.0169 -0.0215 -0.0016 45  HIS   B CD2 
4684 C CE1 . HIS   B 45  ? 0.1632 0.1320 0.1282 -0.0080 -0.0255 -0.0064 45  HIS   B CE1 
4685 N NE2 . HIS   B 45  ? 0.1688 0.1416 0.1317 -0.0094 -0.0187 -0.0053 45  HIS   B NE2 
4693 N N   A GLY   B 46  ? 0.1951 0.1566 0.2062 0.0170  -0.0391 0.0007  46  GLY   B N   
4694 N N   B GLY   B 46  ? 0.1931 0.1660 0.1948 0.0154  -0.0350 0.0048  46  GLY   B N   
4695 C CA  A GLY   B 46  ? 0.2082 0.1661 0.2467 0.0191  -0.0469 0.0054  46  GLY   B CA  
4696 C CA  B GLY   B 46  ? 0.2050 0.1775 0.2208 0.0150  -0.0434 0.0157  46  GLY   B CA  
4697 C C   A GLY   B 46  ? 0.2099 0.1817 0.2910 0.0290  -0.0409 0.0049  46  GLY   B C   
4698 C C   B GLY   B 46  ? 0.2107 0.1913 0.2485 0.0190  -0.0412 0.0252  46  GLY   B C   
4699 O O   A GLY   B 46  ? 0.2207 0.1890 0.3759 0.0404  -0.0261 -0.0213 46  GLY   B O   
4700 O O   B GLY   B 46  ? 0.2225 0.2032 0.2600 0.0210  -0.0424 0.0430  46  GLY   B O   
4707 N N   . GLY   B 47  ? 0.2050 0.1944 0.2564 0.0092  -0.0247 0.0060  47  GLY   B N   
4708 C CA  . GLY   B 47  ? 0.1907 0.1747 0.2147 0.0067  -0.0236 0.0056  47  GLY   B CA  
4709 C C   . GLY   B 47  ? 0.1720 0.1603 0.1701 0.0060  -0.0022 0.0045  47  GLY   B C   
4710 O O   . GLY   B 47  ? 0.1774 0.1445 0.1758 0.0039  -0.0086 0.0126  47  GLY   B O   
4715 N N   . GLY   B 48  ? 0.1553 0.1488 0.1661 0.0014  -0.0082 0.0133  48  GLY   B N   
4716 C CA  . GLY   B 48  ? 0.1526 0.1422 0.1641 -0.0061 -0.0006 0.0094  48  GLY   B CA  
4717 C C   . GLY   B 48  ? 0.1465 0.1300 0.1474 0.0007  0.0067  0.0054  48  GLY   B C   
4718 O O   . GLY   B 48  ? 0.1421 0.1288 0.1740 0.0011  -0.0053 0.0065  48  GLY   B O   
4722 N N   . VAL   B 49  ? 0.1459 0.1372 0.1389 0.0104  0.0020  0.0169  49  VAL   B N   
4723 C CA  . VAL   B 49  ? 0.1458 0.1493 0.1301 0.0065  -0.0111 -0.0082 49  VAL   B CA  
4724 C C   . VAL   B 49  ? 0.1295 0.1399 0.1185 0.0085  -0.0021 0.0039  49  VAL   B C   
4725 O O   . VAL   B 49  ? 0.1414 0.1421 0.1408 0.0047  -0.0066 0.0033  49  VAL   B O   
4726 C CB  . VAL   B 49  ? 0.1466 0.1594 0.1647 -0.0006 -0.0228 -0.0012 49  VAL   B CB  
4727 C CG1 . VAL   B 49  ? 0.1436 0.1615 0.1654 0.0090  -0.0299 0.0044  49  VAL   B CG1 
4728 C CG2 . VAL   B 49  ? 0.1589 0.1730 0.1868 -0.0072 -0.0345 0.0037  49  VAL   B CG2 
4738 N N   . ALA   B 50  ? 0.1261 0.1288 0.1334 0.0018  -0.0018 0.0039  50  ALA   B N   
4739 C CA  . ALA   B 50  ? 0.1321 0.1259 0.1322 0.0084  -0.0096 0.0085  50  ALA   B CA  
4740 C C   . ALA   B 50  ? 0.1312 0.1326 0.1315 0.0051  -0.0051 0.0036  50  ALA   B C   
4741 O O   . ALA   B 50  ? 0.1360 0.1327 0.1291 0.0016  -0.0036 -0.0037 50  ALA   B O   
4742 C CB  . ALA   B 50  ? 0.1396 0.1284 0.1421 0.0035  -0.0012 0.0001  50  ALA   B CB  
4748 N N   . GLY   B 51  ? 0.1351 0.1427 0.1353 0.0094  -0.0119 0.0156  51  GLY   B N   
4749 C CA  . GLY   B 51  ? 0.1422 0.1433 0.1469 0.0164  -0.0172 0.0130  51  GLY   B CA  
4750 C C   . GLY   B 51  ? 0.1402 0.1409 0.1513 0.0155  -0.0144 0.0109  51  GLY   B C   
4751 O O   . GLY   B 51  ? 0.1452 0.1502 0.1733 0.0068  -0.0116 -0.0001 51  GLY   B O   
4755 N N   . ALA   B 52  ? 0.1363 0.1318 0.1438 0.0215  -0.0110 0.0119  52  ALA   B N   
4756 C CA  . ALA   B 52  ? 0.1378 0.1417 0.1525 0.0218  -0.0006 -0.0011 52  ALA   B CA  
4757 C C   . ALA   B 52  ? 0.1283 0.1369 0.1361 0.0054  0.0012  0.0037  52  ALA   B C   
4758 O O   . ALA   B 52  ? 0.1386 0.1470 0.1591 0.0099  -0.0002 -0.0014 52  ALA   B O   
4759 C CB  . ALA   B 52  ? 0.1634 0.1495 0.1602 0.0090  0.0006  0.0015  52  ALA   B CB  
4765 N N   . LEU   B 53  ? 0.1291 0.1297 0.1406 0.0149  -0.0036 0.0031  53  LEU   B N   
4766 C CA  . LEU   B 53  ? 0.1292 0.1411 0.1311 0.0121  -0.0086 0.0021  53  LEU   B CA  
4767 C C   . LEU   B 53  ? 0.1345 0.1407 0.1319 0.0082  0.0034  0.0068  53  LEU   B C   
4768 O O   . LEU   B 53  ? 0.1307 0.1447 0.1501 -0.0036 0.0013  0.0129  53  LEU   B O   
4769 C CB  . LEU   B 53  ? 0.1321 0.1476 0.1418 0.0084  -0.0046 0.0131  53  LEU   B CB  
4770 C CG  . LEU   B 53  ? 0.1361 0.1612 0.1487 0.0032  -0.0042 0.0203  53  LEU   B CG  
4771 C CD1 . LEU   B 53  ? 0.1391 0.1823 0.1723 0.0176  -0.0089 0.0078  53  LEU   B CD1 
4772 C CD2 . LEU   B 53  ? 0.1503 0.1875 0.1712 -0.0111 -0.0033 -0.0087 53  LEU   B CD2 
4784 N N   . ASN   B 54  ? 0.1346 0.1316 0.1310 0.0063  -0.0045 0.0052  54  ASN   B N   
4785 C CA  . ASN   B 54  ? 0.1413 0.1390 0.1464 0.0069  -0.0011 0.0002  54  ASN   B CA  
4786 C C   . ASN   B 54  ? 0.1294 0.1488 0.1594 0.0033  -0.0056 0.0052  54  ASN   B C   
4787 O O   . ASN   B 54  ? 0.1344 0.1574 0.1689 -0.0006 0.0018  0.0005  54  ASN   B O   
4788 C CB  . ASN   B 54  ? 0.1409 0.1552 0.1470 0.0037  -0.0004 0.0050  54  ASN   B CB  
4789 C CG  . ASN   B 54  ? 0.1387 0.1646 0.1521 -0.0009 -0.0081 0.0002  54  ASN   B CG  
4790 O OD1 . ASN   B 54  ? 0.1375 0.1603 0.1677 -0.0019 -0.0141 -0.0003 54  ASN   B OD1 
4791 N ND2 . ASN   B 54  ? 0.1564 0.1836 0.1671 -0.0066 -0.0328 0.0147  54  ASN   B ND2 
4798 N N   . LYS   B 55  ? 0.1306 0.1524 0.1714 0.0151  -0.0037 0.0033  55  LYS   B N   
4799 C CA  . LYS   B 55  ? 0.1440 0.1652 0.1986 0.0192  -0.0045 0.0085  55  LYS   B CA  
4800 C C   . LYS   B 55  ? 0.1357 0.1637 0.1814 0.0119  0.0035  0.0006  55  LYS   B C   
4801 O O   . LYS   B 55  ? 0.1291 0.1772 0.1978 0.0099  0.0027  0.0079  55  LYS   B O   
4802 C CB  . LYS   B 55  ? 0.1508 0.1771 0.2351 0.0280  0.0028  0.0274  55  LYS   B CB  
4803 C CG  . LYS   B 55  ? 0.1910 0.1999 0.3265 0.0269  0.0165  0.0419  55  LYS   B CG  
4804 C CD  . LYS   B 55  ? 0.2271 0.2232 0.4010 0.0354  0.0372  0.0519  55  LYS   B CD  
4805 C CE  . LYS   B 55  ? 0.2588 0.2458 0.4707 0.0402  0.0499  0.0496  55  LYS   B CE  
4806 N NZ  . LYS   B 55  ? 0.2672 0.2612 0.5103 0.0417  0.0379  0.0556  55  LYS   B NZ  
4820 N N   . ALA   B 56  ? 0.1385 0.1664 0.1619 0.0029  -0.0024 -0.0047 56  ALA   B N   
4821 C CA  . ALA   B 56  ? 0.1532 0.1780 0.1622 0.0009  0.0079  0.0007  56  ALA   B CA  
4822 C C   . ALA   B 56  ? 0.1451 0.1756 0.1575 0.0022  0.0137  0.0093  56  ALA   B C   
4823 O O   . ALA   B 56  ? 0.1625 0.1854 0.1816 0.0081  0.0313  0.0112  56  ALA   B O   
4824 C CB  . ALA   B 56  ? 0.1587 0.1897 0.1603 -0.0137 0.0018  -0.0002 56  ALA   B CB  
4830 N N   . THR   B 57  ? 0.1396 0.1660 0.1631 -0.0019 0.0214  0.0101  57  THR   B N   
4831 C CA  . THR   B 57  ? 0.1501 0.1620 0.1637 -0.0028 0.0124  0.0178  57  THR   B CA  
4832 C C   . THR   B 57  ? 0.1491 0.1736 0.1829 -0.0073 0.0162  0.0220  57  THR   B C   
4833 O O   . THR   B 57  ? 0.1594 0.1794 0.2005 -0.0231 0.0146  0.0137  57  THR   B O   
4834 C CB  . THR   B 57  ? 0.1568 0.1459 0.1536 -0.0066 0.0068  0.0171  57  THR   B CB  
4835 O OG1 . THR   B 57  ? 0.1557 0.1479 0.1603 -0.0058 0.0075  0.0097  57  THR   B OG1 
4836 C CG2 . THR   B 57  ? 0.1497 0.1531 0.1528 -0.0052 0.0072  0.0069  57  THR   B CG2 
4844 N N   . ASN   B 58  ? 0.1396 0.1869 0.1993 -0.0155 -0.0019 -0.0004 58  ASN   B N   
4845 C CA  . ASN   B 58  ? 0.1584 0.2286 0.2411 -0.0275 0.0183  0.0059  58  ASN   B CA  
4846 C C   . ASN   B 58  ? 0.1395 0.2124 0.2065 -0.0207 -0.0093 0.0040  58  ASN   B C   
4847 O O   . ASN   B 58  ? 0.1487 0.2292 0.2242 -0.0219 -0.0137 -0.0093 58  ASN   B O   
4848 C CB  . ASN   B 58  ? 0.2513 0.3068 0.3569 -0.0464 0.0407  0.0117  58  ASN   B CB  
4849 C CG  . ASN   B 58  ? 0.3517 0.3824 0.4966 -0.0518 0.0569  0.0329  58  ASN   B CG  
4850 O OD1 . ASN   B 58  ? 0.3757 0.3971 0.5445 -0.0542 0.0627  0.0393  58  ASN   B OD1 
4851 N ND2 . ASN   B 58  ? 0.4245 0.4245 0.5429 -0.0546 0.0634  0.0391  58  ASN   B ND2 
4858 N N   . ASN   B 59  ? 0.1378 0.1989 0.1917 -0.0133 -0.0136 0.0108  59  ASN   B N   
4859 C CA  . ASN   B 59  ? 0.1458 0.1990 0.1834 -0.0132 -0.0206 0.0118  59  ASN   B CA  
4860 C C   . ASN   B 59  ? 0.1386 0.1873 0.1785 -0.0163 -0.0161 -0.0016 59  ASN   B C   
4861 O O   . ASN   B 59  ? 0.1437 0.1889 0.1791 -0.0182 -0.0130 0.0006  59  ASN   B O   
4862 C CB  . ASN   B 59  ? 0.1600 0.2182 0.1916 -0.0131 -0.0304 0.0120  59  ASN   B CB  
4863 C CG  . ASN   B 59  ? 0.1701 0.2355 0.2086 -0.0107 -0.0426 0.0088  59  ASN   B CG  
4864 O OD1 . ASN   B 59  ? 0.1724 0.2407 0.2059 -0.0102 -0.0346 0.0220  59  ASN   B OD1 
4865 N ND2 . ASN   B 59  ? 0.1775 0.2481 0.2215 -0.0148 -0.0435 0.0049  59  ASN   B ND2 
4872 N N   . ALA   B 60  ? 0.1417 0.1778 0.1761 -0.0160 -0.0113 0.0013  60  ALA   B N   
4873 C CA  . ALA   B 60  ? 0.1466 0.1629 0.1696 -0.0203 -0.0074 0.0090  60  ALA   B CA  
4874 C C   . ALA   B 60  ? 0.1432 0.1533 0.1639 -0.0176 -0.0113 0.0063  60  ALA   B C   
4875 O O   . ALA   B 60  ? 0.1464 0.1603 0.1747 -0.0234 -0.0042 -0.0048 60  ALA   B O   
4876 C CB  . ALA   B 60  ? 0.1656 0.1638 0.2014 -0.0227 -0.0008 0.0087  60  ALA   B CB  
4882 N N   . MET   B 61  ? 0.1389 0.1450 0.1671 -0.0115 -0.0066 0.0048  61  MET   B N   
4883 C CA  . MET   B 61  ? 0.1342 0.1390 0.1589 -0.0129 -0.0063 0.0093  61  MET   B CA  
4884 C C   . MET   B 61  ? 0.1493 0.1345 0.1585 -0.0091 -0.0118 0.0094  61  MET   B C   
4885 O O   . MET   B 61  ? 0.1481 0.1362 0.1527 -0.0040 -0.0183 -0.0107 61  MET   B O   
4886 C CB  . MET   B 61  ? 0.1380 0.1471 0.1590 -0.0056 -0.0099 0.0009  61  MET   B CB  
4887 C CG  . MET   B 61  ? 0.1269 0.1420 0.1464 -0.0024 -0.0090 -0.0000 61  MET   B CG  
4888 S SD  . MET   B 61  ? 0.1358 0.1446 0.1598 -0.0049 -0.0043 -0.0098 61  MET   B SD  
4889 C CE  . MET   B 61  ? 0.1432 0.1631 0.1839 0.0025  -0.0122 -0.0225 61  MET   B CE  
4899 N N   . GLN   B 62  ? 0.1401 0.1450 0.1453 -0.0041 -0.0173 0.0003  62  GLN   B N   
4900 C CA  . GLN   B 62  ? 0.1445 0.1521 0.1520 -0.0032 -0.0245 -0.0069 62  GLN   B CA  
4901 C C   . GLN   B 62  ? 0.1441 0.1569 0.1542 -0.0090 -0.0329 -0.0020 62  GLN   B C   
4902 O O   . GLN   B 62  ? 0.1581 0.1570 0.1620 -0.0070 -0.0321 -0.0124 62  GLN   B O   
4903 C CB  . GLN   B 62  ? 0.1428 0.1535 0.1531 0.0022  -0.0181 0.0077  62  GLN   B CB  
4904 C CG  . GLN   B 62  ? 0.1548 0.1573 0.1536 0.0002  -0.0292 0.0001  62  GLN   B CG  
4905 C CD  . GLN   B 62  ? 0.1536 0.1532 0.1543 0.0049  -0.0310 0.0073  62  GLN   B CD  
4906 O OE1 . GLN   B 62  ? 0.1526 0.1534 0.1658 -0.0003 -0.0260 -0.0047 62  GLN   B OE1 
4907 N NE2 . GLN   B 62  ? 0.1558 0.1653 0.1454 0.0001  -0.0270 -0.0054 62  GLN   B NE2 
4916 N N   . VAL   B 63  ? 0.1420 0.1639 0.1754 -0.0148 -0.0262 -0.0106 63  VAL   B N   
4917 C CA  . VAL   B 63  ? 0.1550 0.1627 0.1917 -0.0207 -0.0350 -0.0110 63  VAL   B CA  
4918 C C   . VAL   B 63  ? 0.1574 0.1507 0.1816 -0.0201 -0.0310 -0.0127 63  VAL   B C   
4919 O O   . VAL   B 63  ? 0.1704 0.1475 0.1897 -0.0142 -0.0444 -0.0111 63  VAL   B O   
4920 C CB  . VAL   B 63  ? 0.1579 0.1816 0.2321 -0.0294 -0.0341 -0.0198 63  VAL   B CB  
4921 C CG1 . VAL   B 63  ? 0.1620 0.1910 0.2464 -0.0347 -0.0265 -0.0210 63  VAL   B CG1 
4922 C CG2 . VAL   B 63  ? 0.1565 0.1952 0.2509 -0.0244 -0.0410 -0.0186 63  VAL   B CG2 
4932 N N   . GLU   B 64  ? 0.1507 0.1468 0.1725 -0.0136 -0.0249 -0.0071 64  GLU   B N   
4933 C CA  . GLU   B 64  ? 0.1547 0.1380 0.1671 -0.0154 -0.0336 -0.0057 64  GLU   B CA  
4934 C C   . GLU   B 64  ? 0.1510 0.1384 0.1542 -0.0058 -0.0341 -0.0141 64  GLU   B C   
4935 O O   . GLU   B 64  ? 0.1625 0.1454 0.1609 -0.0120 -0.0257 -0.0170 64  GLU   B O   
4936 C CB  . GLU   B 64  ? 0.1597 0.1436 0.1627 -0.0162 -0.0248 -0.0058 64  GLU   B CB  
4937 C CG  . GLU   B 64  ? 0.1667 0.1462 0.1640 -0.0217 -0.0341 -0.0186 64  GLU   B CG  
4938 C CD  . GLU   B 64  ? 0.1702 0.1622 0.1757 -0.0278 -0.0332 -0.0112 64  GLU   B CD  
4939 O OE1 . GLU   B 64  ? 0.1683 0.1823 0.1802 -0.0269 -0.0252 -0.0318 64  GLU   B OE1 
4940 O OE2 . GLU   B 64  ? 0.1833 0.1693 0.1827 -0.0356 -0.0466 -0.0072 64  GLU   B OE2 
4947 N N   . SER   B 65  ? 0.1534 0.1343 0.1490 -0.0087 -0.0198 -0.0156 65  SER   B N   
4948 C CA  . SER   B 65  ? 0.1561 0.1368 0.1463 -0.0062 -0.0164 -0.0195 65  SER   B CA  
4949 C C   . SER   B 65  ? 0.1589 0.1423 0.1564 -0.0047 -0.0266 -0.0247 65  SER   B C   
4950 O O   . SER   B 65  ? 0.1624 0.1454 0.1585 0.0006  -0.0248 -0.0283 65  SER   B O   
4951 C CB  . SER   B 65  ? 0.1541 0.1358 0.1338 -0.0118 -0.0187 -0.0129 65  SER   B CB  
4952 O OG  . SER   B 65  ? 0.1588 0.1361 0.1598 -0.0095 -0.0201 -0.0219 65  SER   B OG  
4958 N N   . ASP   B 66  ? 0.1624 0.1477 0.1479 -0.0025 -0.0323 -0.0243 66  ASP   B N   
4959 C CA  . ASP   B 66  ? 0.1641 0.1545 0.1451 0.0015  -0.0322 -0.0165 66  ASP   B CA  
4960 C C   . ASP   B 66  ? 0.1788 0.1594 0.1382 -0.0014 -0.0258 -0.0208 66  ASP   B C   
4961 O O   . ASP   B 66  ? 0.1815 0.1647 0.1522 0.0038  -0.0319 -0.0235 66  ASP   B O   
4962 C CB  . ASP   B 66  ? 0.1797 0.1657 0.1676 0.0118  -0.0408 -0.0131 66  ASP   B CB  
4963 C CG  . ASP   B 66  ? 0.2171 0.1875 0.1959 0.0196  -0.0582 -0.0026 66  ASP   B CG  
4964 O OD1 . ASP   B 66  ? 0.2419 0.1859 0.1967 0.0099  -0.0584 0.0079  66  ASP   B OD1 
4965 O OD2 . ASP   B 66  ? 0.2375 0.2118 0.2581 0.0366  -0.0566 0.0016  66  ASP   B OD2 
4970 N N   . ASP   B 67  ? 0.1723 0.1493 0.1333 -0.0070 -0.0276 -0.0213 67  ASP   B N   
4971 C CA  . ASP   B 67  ? 0.1865 0.1478 0.1532 -0.0132 -0.0269 -0.0136 67  ASP   B CA  
4972 C C   . ASP   B 67  ? 0.1830 0.1492 0.1655 -0.0032 -0.0229 -0.0244 67  ASP   B C   
4973 O O   . ASP   B 67  ? 0.1838 0.1553 0.1753 -0.0023 -0.0218 -0.0318 67  ASP   B O   
4974 C CB  . ASP   B 67  ? 0.2071 0.1576 0.1750 -0.0213 -0.0411 0.0002  67  ASP   B CB  
4975 C CG  . ASP   B 67  ? 0.2390 0.1672 0.1807 -0.0176 -0.0690 -0.0090 67  ASP   B CG  
4976 O OD1 . ASP   B 67  ? 0.2543 0.1740 0.1913 -0.0109 -0.0665 -0.0060 67  ASP   B OD1 
4977 O OD2 . ASP   B 67  ? 0.2560 0.1703 0.1998 -0.0020 -0.0750 -0.0145 67  ASP   B OD2 
4982 N N   . TYR   B 68  ? 0.1695 0.1462 0.1563 0.0010  -0.0354 -0.0336 68  TYR   B N   
4983 C CA  . TYR   B 68  ? 0.1645 0.1672 0.1697 0.0056  -0.0421 -0.0320 68  TYR   B CA  
4984 C C   . TYR   B 68  ? 0.1575 0.1637 0.1701 0.0055  -0.0342 -0.0430 68  TYR   B C   
4985 O O   . TYR   B 68  ? 0.1660 0.1696 0.1767 0.0102  -0.0327 -0.0581 68  TYR   B O   
4986 C CB  . TYR   B 68  ? 0.1759 0.1874 0.1659 0.0076  -0.0468 -0.0460 68  TYR   B CB  
4987 C CG  . TYR   B 68  ? 0.1883 0.2099 0.1803 0.0119  -0.0412 -0.0646 68  TYR   B CG  
4988 C CD1 . TYR   B 68  ? 0.1885 0.2107 0.2107 -0.0127 -0.0363 -0.0775 68  TYR   B CD1 
4989 C CD2 . TYR   B 68  ? 0.1904 0.2256 0.1937 0.0205  -0.0543 -0.0585 68  TYR   B CD2 
4990 C CE1 . TYR   B 68  ? 0.1913 0.2250 0.2328 -0.0102 -0.0354 -0.0773 68  TYR   B CE1 
4991 C CE2 . TYR   B 68  ? 0.1880 0.2294 0.2099 0.0131  -0.0462 -0.0735 68  TYR   B CE2 
4992 C CZ  . TYR   B 68  ? 0.1864 0.2314 0.2283 0.0027  -0.0393 -0.0820 68  TYR   B CZ  
4993 O OH  . TYR   B 68  ? 0.1842 0.2576 0.2559 -0.0017 -0.0307 -0.0583 68  TYR   B OH  
5003 N N   . ILE   B 69  ? 0.1557 0.1565 0.1699 0.0041  -0.0314 -0.0370 69  ILE   B N   
5004 C CA  . ILE   B 69  ? 0.1704 0.1645 0.1821 -0.0020 -0.0145 -0.0399 69  ILE   B CA  
5005 C C   . ILE   B 69  ? 0.1703 0.1639 0.1701 0.0061  -0.0316 -0.0308 69  ILE   B C   
5006 O O   . ILE   B 69  ? 0.1803 0.1727 0.1684 0.0056  -0.0261 -0.0384 69  ILE   B O   
5007 C CB  . ILE   B 69  ? 0.1815 0.1696 0.2046 -0.0059 -0.0017 -0.0343 69  ILE   B CB  
5008 C CG1 . ILE   B 69  ? 0.1825 0.1647 0.2152 -0.0095 0.0076  -0.0446 69  ILE   B CG1 
5009 C CG2 . ILE   B 69  ? 0.1983 0.1809 0.2199 -0.0041 0.0029  -0.0241 69  ILE   B CG2 
5010 C CD1 . ILE   B 69  ? 0.1782 0.1668 0.2249 -0.0181 0.0127  -0.0430 69  ILE   B CD1 
5022 N N   . ALA   B 70  ? 0.1694 0.1611 0.1613 0.0063  -0.0365 -0.0334 70  ALA   B N   
5023 C CA  . ALA   B 70  ? 0.1706 0.1624 0.1530 0.0057  -0.0400 -0.0262 70  ALA   B CA  
5024 C C   . ALA   B 70  ? 0.1742 0.1596 0.1617 0.0001  -0.0427 -0.0381 70  ALA   B C   
5025 O O   . ALA   B 70  ? 0.1814 0.1627 0.1719 -0.0025 -0.0375 -0.0418 70  ALA   B O   
5026 C CB  . ALA   B 70  ? 0.1714 0.1751 0.1644 -0.0040 -0.0465 -0.0253 70  ALA   B CB  
5032 N N   . THR   B 71  ? 0.1856 0.1674 0.1724 0.0064  -0.0493 -0.0411 71  THR   B N   
5033 C CA  . THR   B 71  ? 0.1962 0.1710 0.1888 0.0118  -0.0660 -0.0477 71  THR   B CA  
5034 C C   . THR   B 71  ? 0.1908 0.1674 0.2137 0.0286  -0.0623 -0.0578 71  THR   B C   
5035 O O   . THR   B 71  ? 0.2001 0.1758 0.2569 0.0330  -0.0581 -0.0676 71  THR   B O   
5036 C CB  . THR   B 71  ? 0.2224 0.1885 0.2180 -0.0001 -0.0715 -0.0207 71  THR   B CB  
5037 O OG1 . THR   B 71  ? 0.2391 0.2078 0.2555 -0.0202 -0.0784 0.0035  71  THR   B OG1 
5038 C CG2 . THR   B 71  ? 0.2414 0.1872 0.2449 0.0031  -0.0647 0.0006  71  THR   B CG2 
5046 N N   . ASN   B 72  ? 0.1795 0.1768 0.2109 0.0188  -0.0640 -0.0696 72  ASN   B N   
5047 C CA  . ASN   B 72  ? 0.1805 0.1898 0.2184 0.0142  -0.0544 -0.0779 72  ASN   B CA  
5048 C C   . ASN   B 72  ? 0.1807 0.2043 0.2199 0.0009  -0.0314 -0.0771 72  ASN   B C   
5049 O O   . ASN   B 72  ? 0.1839 0.2173 0.2493 0.0094  -0.0095 -0.0827 72  ASN   B O   
5050 C CB  . ASN   B 72  ? 0.1854 0.2069 0.2333 0.0105  -0.0615 -0.0678 72  ASN   B CB  
5051 C CG  . ASN   B 72  ? 0.1989 0.2208 0.2384 0.0271  -0.0516 -0.0462 72  ASN   B CG  
5052 O OD1 . ASN   B 72  ? 0.2230 0.2377 0.2396 0.0105  -0.0356 -0.0456 72  ASN   B OD1 
5053 N ND2 . ASN   B 72  ? 0.2086 0.2295 0.2818 0.0437  -0.0464 -0.0148 72  ASN   B ND2 
5060 N N   . GLY   B 73  ? 0.1835 0.2007 0.1947 -0.0018 -0.0339 -0.0667 73  GLY   B N   
5061 C CA  . GLY   B 73  ? 0.1793 0.2049 0.1840 -0.0043 -0.0243 -0.0485 73  GLY   B CA  
5062 C C   . GLY   B 73  ? 0.1767 0.2024 0.1332 0.0028  -0.0261 -0.0485 73  GLY   B C   
5063 O O   . GLY   B 73  ? 0.1711 0.1925 0.1546 0.0043  -0.0179 -0.0400 73  GLY   B O   
5067 N N   . PRO   B 74  ? 0.1839 0.2161 0.1325 -0.0013 -0.0266 -0.0436 74  PRO   B N   
5068 C CA  . PRO   B 74  ? 0.1751 0.2151 0.1302 0.0040  -0.0258 -0.0263 74  PRO   B CA  
5069 C C   . PRO   B 74  ? 0.1586 0.1948 0.1335 0.0086  -0.0139 -0.0167 74  PRO   B C   
5070 O O   . PRO   B 74  ? 0.1577 0.1915 0.1680 0.0105  -0.0090 -0.0244 74  PRO   B O   
5071 C CB  . PRO   B 74  ? 0.1863 0.2303 0.1273 0.0074  -0.0197 -0.0203 74  PRO   B CB  
5072 C CG  . PRO   B 74  ? 0.2083 0.2437 0.1454 0.0071  -0.0149 -0.0234 74  PRO   B CG  
5073 C CD  . PRO   B 74  ? 0.2046 0.2340 0.1334 0.0074  -0.0126 -0.0313 74  PRO   B CD  
5081 N N   . LEU   B 75  ? 0.1542 0.1821 0.1269 0.0037  -0.0178 -0.0227 75  LEU   B N   
5082 C CA  . LEU   B 75  ? 0.1544 0.1812 0.1237 0.0007  -0.0213 -0.0071 75  LEU   B CA  
5083 C C   . LEU   B 75  ? 0.1590 0.1907 0.1165 0.0085  -0.0151 -0.0118 75  LEU   B C   
5084 O O   . LEU   B 75  ? 0.1720 0.2073 0.1319 0.0064  -0.0079 -0.0070 75  LEU   B O   
5085 C CB  . LEU   B 75  ? 0.1672 0.1816 0.1159 -0.0044 -0.0187 0.0083  75  LEU   B CB  
5086 C CG  . LEU   B 75  ? 0.1996 0.1960 0.1300 -0.0231 -0.0014 0.0002  75  LEU   B CG  
5087 C CD1 . LEU   B 75  ? 0.2326 0.2079 0.1261 -0.0310 0.0176  -0.0007 75  LEU   B CD1 
5088 C CD2 . LEU   B 75  ? 0.2301 0.2154 0.2128 -0.0129 0.0152  0.0105  75  LEU   B CD2 
5100 N N   . LYS   B 76  ? 0.1596 0.2140 0.1372 0.0048  -0.0010 -0.0090 76  LYS   B N   
5101 C CA  . LYS   B 76  ? 0.1729 0.2223 0.1828 -0.0040 0.0223  -0.0109 76  LYS   B CA  
5102 C C   . LYS   B 76  ? 0.1616 0.1999 0.1434 0.0040  0.0078  0.0121  76  LYS   B C   
5103 O O   . LYS   B 76  ? 0.1551 0.1860 0.1443 -0.0008 -0.0052 0.0145  76  LYS   B O   
5104 C CB  . LYS   B 76  ? 0.1905 0.2358 0.2484 -0.0122 0.0468  -0.0424 76  LYS   B CB  
5105 C CG  . LYS   B 76  ? 0.1963 0.2533 0.2934 -0.0078 0.0415  -0.0479 76  LYS   B CG  
5106 C CD  . LYS   B 76  ? 0.1948 0.2621 0.3320 -0.0029 0.0246  -0.0631 76  LYS   B CD  
5107 C CE  . LYS   B 76  ? 0.2072 0.2818 0.3924 0.0037  0.0092  -0.0691 76  LYS   B CE  
5108 N NZ  . LYS   B 76  ? 0.2155 0.2918 0.4186 0.0027  -0.0171 -0.0868 76  LYS   B NZ  
5122 N N   . VAL   B 77  ? 0.1710 0.2108 0.1454 0.0107  0.0106  0.0170  77  VAL   B N   
5123 C CA  . VAL   B 77  ? 0.1700 0.2036 0.1573 0.0180  0.0092  0.0378  77  VAL   B CA  
5124 C C   . VAL   B 77  ? 0.1596 0.1813 0.1477 0.0181  0.0166  0.0254  77  VAL   B C   
5125 O O   . VAL   B 77  ? 0.1622 0.1781 0.1473 0.0228  0.0227  0.0198  77  VAL   B O   
5126 C CB  . VAL   B 77  ? 0.1811 0.2189 0.1859 0.0205  0.0181  0.0529  77  VAL   B CB  
5127 C CG1 . VAL   B 77  ? 0.1863 0.2136 0.2193 0.0179  0.0320  0.0590  77  VAL   B CG1 
5128 C CG2 . VAL   B 77  ? 0.1940 0.2346 0.2127 0.0123  0.0139  0.0558  77  VAL   B CG2 
5138 N N   . GLY   B 78  ? 0.1607 0.1719 0.1419 0.0163  0.0202  0.0179  78  GLY   B N   
5139 C CA  . GLY   B 78  ? 0.1579 0.1618 0.1340 0.0142  0.0261  0.0141  78  GLY   B CA  
5140 C C   . GLY   B 78  ? 0.1499 0.1541 0.1271 0.0114  0.0182  0.0126  78  GLY   B C   
5141 O O   . GLY   B 78  ? 0.1492 0.1530 0.1376 0.0168  0.0107  0.0151  78  GLY   B O   
5145 N N   . GLY   B 79  ? 0.1457 0.1569 0.1360 0.0090  0.0140  0.0141  79  GLY   B N   
5146 C CA  . GLY   B 79  ? 0.1420 0.1505 0.1410 0.0152  0.0085  0.0093  79  GLY   B CA  
5147 C C   . GLY   B 79  ? 0.1338 0.1428 0.1319 0.0120  0.0063  0.0021  79  GLY   B C   
5148 O O   . GLY   B 79  ? 0.1449 0.1424 0.1456 0.0154  0.0135  0.0128  79  GLY   B O   
5152 N N   . SER   B 80  ? 0.1392 0.1322 0.1467 0.0071  0.0155  -0.0036 80  SER   B N   
5153 C CA  . SER   B 80  ? 0.1322 0.1360 0.1453 0.0085  0.0112  -0.0024 80  SER   B CA  
5154 C C   . SER   B 80  ? 0.1323 0.1338 0.1441 0.0086  -0.0071 -0.0043 80  SER   B C   
5155 O O   . SER   B 80  ? 0.1443 0.1388 0.1690 0.0134  0.0028  -0.0163 80  SER   B O   
5156 C CB  . SER   B 80  ? 0.1315 0.1447 0.1418 0.0012  0.0013  -0.0031 80  SER   B CB  
5157 O OG  . SER   B 80  ? 0.1428 0.1542 0.1541 0.0008  -0.0145 0.0031  80  SER   B OG  
5163 N N   . CYS   B 81  ? 0.1329 0.1208 0.1467 0.0027  -0.0089 -0.0056 81  CYS   B N   
5164 C CA  . CYS   B 81  ? 0.1426 0.1164 0.1401 0.0053  -0.0162 0.0004  81  CYS   B CA  
5165 C C   . CYS   B 81  ? 0.1358 0.1208 0.1236 0.0084  -0.0166 -0.0011 81  CYS   B C   
5166 O O   . CYS   B 81  ? 0.1583 0.1230 0.1396 0.0161  -0.0035 -0.0054 81  CYS   B O   
5167 C CB  . CYS   B 81  ? 0.1491 0.1352 0.1464 -0.0039 -0.0173 -0.0061 81  CYS   B CB  
5168 S SG  . CYS   B 81  ? 0.1574 0.1533 0.1413 -0.0033 -0.0249 -0.0168 81  CYS   B SG  
5174 N N   . VAL   B 82  ? 0.1359 0.1179 0.1431 0.0050  -0.0115 -0.0073 82  VAL   B N   
5175 C CA  . VAL   B 82  ? 0.1480 0.1201 0.1354 -0.0073 -0.0148 -0.0010 82  VAL   B CA  
5176 C C   . VAL   B 82  ? 0.1517 0.1176 0.1448 0.0012  -0.0077 -0.0034 82  VAL   B C   
5177 O O   . VAL   B 82  ? 0.1566 0.1245 0.1705 -0.0002 -0.0149 -0.0188 82  VAL   B O   
5178 C CB  . VAL   B 82  ? 0.1552 0.1384 0.1553 -0.0064 -0.0115 0.0083  82  VAL   B CB  
5179 C CG1 . VAL   B 82  ? 0.1733 0.1640 0.1687 0.0005  -0.0198 0.0192  82  VAL   B CG1 
5180 C CG2 . VAL   B 82  ? 0.1631 0.1489 0.1581 -0.0056 -0.0214 0.0154  82  VAL   B CG2 
5190 N N   . LEU   B 83  ? 0.1381 0.1137 0.1405 -0.0104 -0.0141 -0.0076 83  LEU   B N   
5191 C CA  . LEU   B 83  ? 0.1405 0.1207 0.1246 -0.0133 -0.0151 -0.0014 83  LEU   B CA  
5192 C C   . LEU   B 83  ? 0.1408 0.1167 0.1257 -0.0186 -0.0217 -0.0010 83  LEU   B C   
5193 O O   . LEU   B 83  ? 0.1454 0.1289 0.1239 -0.0204 -0.0190 0.0087  83  LEU   B O   
5194 C CB  . LEU   B 83  ? 0.1509 0.1340 0.1255 -0.0166 -0.0207 -0.0025 83  LEU   B CB  
5195 C CG  . LEU   B 83  ? 0.1674 0.1524 0.1338 -0.0208 -0.0155 -0.0085 83  LEU   B CG  
5196 C CD1 . LEU   B 83  ? 0.1720 0.1622 0.1471 -0.0142 -0.0242 -0.0082 83  LEU   B CD1 
5197 C CD2 . LEU   B 83  ? 0.1820 0.1558 0.1548 -0.0107 -0.0117 -0.0232 83  LEU   B CD2 
5209 N N   . SER   B 84  ? 0.1428 0.1293 0.1537 -0.0204 -0.0231 -0.0017 84  SER   B N   
5210 C CA  . SER   B 84  ? 0.1474 0.1470 0.1525 -0.0246 -0.0141 0.0154  84  SER   B CA  
5211 C C   . SER   B 84  ? 0.1416 0.1620 0.1124 -0.0208 -0.0195 0.0194  84  SER   B C   
5212 O O   . SER   B 84  ? 0.1498 0.1492 0.1099 -0.0133 -0.0145 0.0064  84  SER   B O   
5213 C CB  . SER   B 84  ? 0.1672 0.1612 0.2009 -0.0252 0.0059  0.0022  84  SER   B CB  
5214 O OG  . SER   B 84  ? 0.1626 0.1702 0.2547 -0.0363 0.0017  0.0181  84  SER   B OG  
5220 N N   . GLY   B 85  ? 0.1385 0.1867 0.1241 -0.0223 -0.0148 0.0196  85  GLY   B N   
5221 C CA  . GLY   B 85  ? 0.1329 0.1981 0.1348 -0.0351 -0.0067 -0.0051 85  GLY   B CA  
5222 C C   . GLY   B 85  ? 0.1360 0.1810 0.1336 -0.0371 -0.0085 0.0098  85  GLY   B C   
5223 O O   . GLY   B 85  ? 0.1436 0.1770 0.1335 -0.0461 0.0117  -0.0030 85  GLY   B O   
5227 N N   . HIS   B 86  ? 0.1414 0.1614 0.1377 -0.0292 -0.0196 0.0236  86  HIS   B N   
5228 C CA  . HIS   B 86  ? 0.1454 0.1566 0.1354 -0.0347 -0.0220 0.0227  86  HIS   B CA  
5229 C C   . HIS   B 86  ? 0.1438 0.1676 0.1374 -0.0440 -0.0125 0.0347  86  HIS   B C   
5230 O O   . HIS   B 86  ? 0.1580 0.1780 0.1437 -0.0410 -0.0004 0.0354  86  HIS   B O   
5231 C CB  . HIS   B 86  ? 0.1478 0.1626 0.1447 -0.0212 -0.0202 0.0086  86  HIS   B CB  
5232 C CG  . HIS   B 86  ? 0.1555 0.1662 0.1514 -0.0141 -0.0269 0.0117  86  HIS   B CG  
5233 N ND1 . HIS   B 86  ? 0.1600 0.1879 0.1705 -0.0203 -0.0274 -0.0040 86  HIS   B ND1 
5234 C CD2 . HIS   B 86  ? 0.1551 0.1631 0.1539 -0.0110 -0.0284 0.0133  86  HIS   B CD2 
5235 C CE1 . HIS   B 86  ? 0.1732 0.1856 0.1611 -0.0204 -0.0119 -0.0239 86  HIS   B CE1 
5236 N NE2 . HIS   B 86  ? 0.1657 0.1768 0.1469 0.0016  -0.0122 -0.0009 86  HIS   B NE2 
5244 N N   . ASN   B 87  ? 0.1518 0.1695 0.1461 -0.0358 -0.0017 0.0277  87  ASN   B N   
5245 C CA  . ASN   B 87  ? 0.1546 0.1906 0.1447 -0.0342 0.0188  0.0207  87  ASN   B CA  
5246 C C   . ASN   B 87  ? 0.1632 0.1802 0.1368 -0.0309 0.0259  0.0171  87  ASN   B C   
5247 O O   . ASN   B 87  ? 0.1803 0.1947 0.1752 -0.0250 0.0388  0.0124  87  ASN   B O   
5248 C CB  . ASN   B 87  ? 0.1548 0.2317 0.1783 -0.0265 0.0229  0.0159  87  ASN   B CB  
5249 C CG  . ASN   B 87  ? 0.1597 0.2534 0.1905 0.0027  0.0187  0.0331  87  ASN   B CG  
5250 O OD1 . ASN   B 87  ? 0.1591 0.2381 0.1769 0.0036  0.0416  0.0533  87  ASN   B OD1 
5251 N ND2 . ASN   B 87  ? 0.1940 0.2696 0.2294 0.0028  0.0216  0.0325  87  ASN   B ND2 
5258 N N   . LEU   B 88  ? 0.1500 0.1657 0.1335 -0.0331 0.0161  0.0125  88  LEU   B N   
5259 C CA  . LEU   B 88  ? 0.1559 0.1598 0.1386 -0.0290 0.0067  0.0052  88  LEU   B CA  
5260 C C   . LEU   B 88  ? 0.1560 0.1498 0.1318 -0.0292 -0.0038 -0.0039 88  LEU   B C   
5261 O O   . LEU   B 88  ? 0.1811 0.1553 0.1671 -0.0170 -0.0299 -0.0055 88  LEU   B O   
5262 C CB  . LEU   B 88  ? 0.1766 0.1617 0.1485 -0.0358 -0.0056 0.0267  88  LEU   B CB  
5263 C CG  . LEU   B 88  ? 0.2116 0.1943 0.1704 -0.0259 -0.0239 0.0404  88  LEU   B CG  
5264 C CD1 . LEU   B 88  ? 0.2203 0.2300 0.1897 -0.0372 -0.0121 0.0515  88  LEU   B CD1 
5265 C CD2 . LEU   B 88  ? 0.2422 0.2227 0.2327 0.0161  -0.0475 0.0221  88  LEU   B CD2 
5277 N N   . ALA   B 89  ? 0.1455 0.1455 0.1157 -0.0320 0.0085  0.0040  89  ALA   B N   
5278 C CA  . ALA   B 89  ? 0.1471 0.1392 0.1033 -0.0319 0.0040  0.0096  89  ALA   B CA  
5279 C C   . ALA   B 89  ? 0.1621 0.1403 0.1133 -0.0386 0.0137  0.0094  89  ALA   B C   
5280 O O   . ALA   B 89  ? 0.1441 0.1539 0.1473 -0.0421 0.0097  -0.0223 89  ALA   B O   
5281 C CB  . ALA   B 89  ? 0.1410 0.1411 0.1238 -0.0339 0.0035  0.0092  89  ALA   B CB  
5287 N N   . LYS   B 90  ? 0.1928 0.1287 0.1262 -0.0387 -0.0036 0.0117  90  LYS   B N   
5288 C CA  . LYS   B 90  ? 0.2030 0.1301 0.1194 -0.0392 -0.0122 0.0134  90  LYS   B CA  
5289 C C   . LYS   B 90  ? 0.1867 0.1304 0.1268 -0.0435 -0.0156 0.0045  90  LYS   B C   
5290 O O   . LYS   B 90  ? 0.1996 0.1498 0.1466 -0.0584 -0.0066 -0.0031 90  LYS   B O   
5291 C CB  . LYS   B 90  ? 0.2228 0.1340 0.1581 -0.0324 0.0024  0.0216  90  LYS   B CB  
5292 C CG  . LYS   B 90  ? 0.2312 0.1559 0.1662 -0.0164 0.0334  0.0178  90  LYS   B CG  
5293 C CD  . LYS   B 90  ? 0.2697 0.1862 0.2327 -0.0191 0.0453  -0.0150 90  LYS   B CD  
5294 C CE  . LYS   B 90  ? 0.2850 0.2057 0.2866 -0.0296 0.0512  -0.0263 90  LYS   B CE  
5295 N NZ  . LYS   B 90  ? 0.2934 0.1966 0.2871 -0.0454 0.0666  -0.0340 90  LYS   B NZ  
5309 N N   . HIS   B 91  ? 0.1633 0.1189 0.1128 -0.0272 -0.0169 0.0027  91  HIS   B N   
5310 C CA  . HIS   B 91  ? 0.1547 0.1193 0.1289 -0.0185 -0.0191 -0.0035 91  HIS   B CA  
5311 C C   . HIS   B 91  ? 0.1445 0.1280 0.1106 -0.0257 -0.0051 -0.0031 91  HIS   B C   
5312 O O   . HIS   B 91  ? 0.1546 0.1296 0.1151 -0.0211 -0.0194 0.0042  91  HIS   B O   
5313 C CB  . HIS   B 91  ? 0.1687 0.1194 0.1660 -0.0015 -0.0130 0.0041  91  HIS   B CB  
5314 C CG  . HIS   B 91  ? 0.2098 0.1432 0.2454 0.0051  0.0258  0.0258  91  HIS   B CG  
5315 N ND1 . HIS   B 91  ? 0.2393 0.1601 0.2995 0.0036  0.0313  0.0148  91  HIS   B ND1 
5316 C CD2 . HIS   B 91  ? 0.2226 0.1689 0.3020 0.0197  0.0157  0.0593  91  HIS   B CD2 
5317 C CE1 . HIS   B 91  ? 0.2442 0.1711 0.3224 0.0202  0.0288  0.0249  91  HIS   B CE1 
5318 N NE2 . HIS   B 91  ? 0.2340 0.1819 0.3278 0.0289  0.0276  0.0700  91  HIS   B NE2 
5326 N N   . CYS   B 92  ? 0.1362 0.1262 0.1182 -0.0279 -0.0110 -0.0024 92  CYS   B N   
5327 C CA  . CYS   B 92  ? 0.1364 0.1140 0.1120 -0.0225 -0.0122 0.0015  92  CYS   B CA  
5328 C C   . CYS   B 92  ? 0.1314 0.1176 0.1022 -0.0162 -0.0096 -0.0014 92  CYS   B C   
5329 O O   . CYS   B 92  ? 0.1398 0.1200 0.1318 -0.0167 -0.0064 -0.0038 92  CYS   B O   
5330 C CB  . CYS   B 92  ? 0.1345 0.1267 0.1222 -0.0160 -0.0036 -0.0002 92  CYS   B CB  
5331 S SG  . CYS   B 92  ? 0.1337 0.1286 0.1286 -0.0125 -0.0108 0.0055  92  CYS   B SG  
5337 N N   . LEU   B 93  ? 0.1270 0.1222 0.1115 -0.0147 -0.0039 -0.0028 93  LEU   B N   
5338 C CA  . LEU   B 93  ? 0.1296 0.1208 0.1214 -0.0064 -0.0104 -0.0017 93  LEU   B CA  
5339 C C   . LEU   B 93  ? 0.1195 0.1131 0.1110 -0.0004 -0.0108 0.0077  93  LEU   B C   
5340 O O   . LEU   B 93  ? 0.1303 0.1117 0.1180 -0.0046 -0.0104 0.0014  93  LEU   B O   
5341 C CB  . LEU   B 93  ? 0.1304 0.1172 0.1328 -0.0084 -0.0120 -0.0026 93  LEU   B CB  
5342 C CG  . LEU   B 93  ? 0.1228 0.1248 0.1497 -0.0077 -0.0060 0.0096  93  LEU   B CG  
5343 C CD1 . LEU   B 93  ? 0.1287 0.1434 0.1449 0.0104  -0.0077 -0.0036 93  LEU   B CD1 
5344 C CD2 . LEU   B 93  ? 0.1263 0.1268 0.1438 -0.0011 -0.0059 0.0035  93  LEU   B CD2 
5356 N N   . HIS   B 94  ? 0.1224 0.1066 0.1053 -0.0072 -0.0135 0.0048  94  HIS   B N   
5357 C CA  . HIS   B 94  ? 0.1243 0.1117 0.1113 -0.0039 -0.0035 -0.0067 94  HIS   B CA  
5358 C C   . HIS   B 94  ? 0.1228 0.1105 0.1209 -0.0053 -0.0041 -0.0006 94  HIS   B C   
5359 O O   . HIS   B 94  ? 0.1284 0.1230 0.1593 -0.0035 0.0109  -0.0156 94  HIS   B O   
5360 C CB  . HIS   B 94  ? 0.1248 0.1133 0.1264 0.0003  -0.0017 0.0015  94  HIS   B CB  
5361 C CG  . HIS   B 94  ? 0.1313 0.1138 0.1166 -0.0044 -0.0175 -0.0049 94  HIS   B CG  
5362 N ND1 . HIS   B 94  ? 0.1354 0.1195 0.1154 -0.0071 -0.0212 -0.0003 94  HIS   B ND1 
5363 C CD2 . HIS   B 94  ? 0.1308 0.1207 0.1264 0.0007  -0.0162 0.0067  94  HIS   B CD2 
5364 C CE1 . HIS   B 94  ? 0.1307 0.1284 0.1149 -0.0103 -0.0120 0.0003  94  HIS   B CE1 
5365 N NE2 . HIS   B 94  ? 0.1245 0.1298 0.1288 -0.0161 -0.0132 0.0054  94  HIS   B NE2 
5373 N N   . VAL   B 95  ? 0.1148 0.1166 0.1229 -0.0015 -0.0023 -0.0019 95  VAL   B N   
5374 C CA  . VAL   B 95  ? 0.1189 0.1176 0.1227 0.0007  -0.0036 0.0015  95  VAL   B CA  
5375 C C   . VAL   B 95  ? 0.1277 0.1226 0.1229 -0.0035 0.0042  0.0043  95  VAL   B C   
5376 O O   . VAL   B 95  ? 0.1315 0.1212 0.1412 0.0066  0.0039  0.0131  95  VAL   B O   
5377 C CB  . VAL   B 95  ? 0.1252 0.1147 0.1349 -0.0006 -0.0027 -0.0010 95  VAL   B CB  
5378 C CG1 . VAL   B 95  ? 0.1418 0.1316 0.1500 -0.0032 0.0001  0.0131  95  VAL   B CG1 
5379 C CG2 . VAL   B 95  ? 0.1349 0.1163 0.1275 0.0046  -0.0099 0.0070  95  VAL   B CG2 
5389 N N   . VAL   B 96  ? 0.1353 0.1352 0.1167 0.0073  0.0058  0.0116  96  VAL   B N   
5390 C CA  . VAL   B 96  ? 0.1450 0.1430 0.1129 0.0095  0.0081  0.0124  96  VAL   B CA  
5391 C C   . VAL   B 96  ? 0.1484 0.1438 0.1234 0.0091  0.0076  0.0151  96  VAL   B C   
5392 O O   . VAL   B 96  ? 0.1453 0.1501 0.1502 0.0039  0.0195  0.0006  96  VAL   B O   
5393 C CB  . VAL   B 96  ? 0.1549 0.1572 0.1136 0.0081  0.0137  0.0106  96  VAL   B CB  
5394 C CG1 . VAL   B 96  ? 0.1517 0.1742 0.1256 0.0118  0.0087  0.0029  96  VAL   B CG1 
5395 C CG2 . VAL   B 96  ? 0.1605 0.1574 0.1286 -0.0017 0.0108  0.0018  96  VAL   B CG2 
5405 N N   . GLY   B 97  ? 0.1470 0.1422 0.1251 0.0060  0.0051  0.0171  97  GLY   B N   
5406 C CA  . GLY   B 97  ? 0.1642 0.1484 0.1313 -0.0038 0.0048  0.0182  97  GLY   B CA  
5407 C C   . GLY   B 97  ? 0.1770 0.1523 0.1312 0.0042  0.0023  0.0150  97  GLY   B C   
5408 O O   . GLY   B 97  ? 0.1847 0.1641 0.1300 0.0049  0.0046  0.0093  97  GLY   B O   
5412 N N   . PRO   B 98  ? 0.1866 0.1604 0.1442 0.0062  0.0233  0.0280  98  PRO   B N   
5413 C CA  . PRO   B 98  ? 0.1965 0.1683 0.1544 0.0098  0.0289  0.0239  98  PRO   B CA  
5414 C C   . PRO   B 98  ? 0.2094 0.1701 0.1239 0.0213  0.0231  0.0363  98  PRO   B C   
5415 O O   . PRO   B 98  ? 0.2063 0.1656 0.1487 0.0244  0.0220  0.0369  98  PRO   B O   
5416 C CB  . PRO   B 98  ? 0.1820 0.1720 0.1774 0.0050  0.0396  0.0235  98  PRO   B CB  
5417 C CG  . PRO   B 98  ? 0.1762 0.1705 0.1734 0.0049  0.0295  0.0316  98  PRO   B CG  
5418 C CD  . PRO   B 98  ? 0.1686 0.1609 0.1638 0.0062  0.0277  0.0371  98  PRO   B CD  
5426 N N   . ASN   B 99  ? 0.2199 0.1874 0.1312 0.0324  0.0283  0.0160  99  ASN   B N   
5427 C CA  . ASN   B 99  ? 0.2367 0.1905 0.1377 0.0378  0.0185  0.0304  99  ASN   B CA  
5428 C C   . ASN   B 99  ? 0.2615 0.2229 0.1677 0.0360  0.0365  0.0552  99  ASN   B C   
5429 O O   . ASN   B 99  ? 0.2740 0.2295 0.1782 0.0359  0.0311  0.0546  99  ASN   B O   
5430 C CB  . ASN   B 99  ? 0.2503 0.1859 0.1339 0.0382  0.0115  0.0324  99  ASN   B CB  
5431 C CG  . ASN   B 99  ? 0.2584 0.1926 0.1673 0.0369  0.0017  0.0261  99  ASN   B CG  
5432 O OD1 . ASN   B 99  ? 0.2616 0.1971 0.1946 0.0422  0.0026  0.0330  99  ASN   B OD1 
5433 N ND2 . ASN   B 99  ? 0.2604 0.1906 0.1839 0.0334  -0.0163 0.0242  99  ASN   B ND2 
5440 N N   A VAL   B 100 ? 0.2767 0.2320 0.2062 0.0278  0.0432  0.0802  100 VAL   B N   
5441 N N   B VAL   B 100 ? 0.2805 0.2351 0.2089 0.0313  0.0379  0.0746  100 VAL   B N   
5442 C CA  A VAL   B 100 ? 0.3062 0.2510 0.2611 0.0144  0.0496  0.0952  100 VAL   B CA  
5443 C CA  B VAL   B 100 ? 0.3080 0.2523 0.2573 0.0224  0.0391  0.0875  100 VAL   B CA  
5444 C C   A VAL   B 100 ? 0.3295 0.2550 0.2555 0.0246  0.0500  0.1131  100 VAL   B C   
5445 C C   B VAL   B 100 ? 0.3296 0.2565 0.2578 0.0297  0.0406  0.1070  100 VAL   B C   
5446 O O   A VAL   B 100 ? 0.3382 0.2641 0.2638 0.0236  0.0580  0.1042  100 VAL   B O   
5447 O O   B VAL   B 100 ? 0.3356 0.2629 0.2641 0.0287  0.0441  0.1013  100 VAL   B O   
5448 C CB  A VAL   B 100 ? 0.3138 0.2669 0.3280 -0.0091 0.0525  0.0968  100 VAL   B CB  
5449 C CB  B VAL   B 100 ? 0.3144 0.2649 0.3063 0.0064  0.0382  0.0842  100 VAL   B CB  
5450 C CG1 A VAL   B 100 ? 0.3190 0.2743 0.3556 -0.0096 0.0540  0.0934  100 VAL   B CG1 
5451 C CG1 B VAL   B 100 ? 0.3182 0.2701 0.3263 0.0056  0.0385  0.0821  100 VAL   B CG1 
5452 C CG2 A VAL   B 100 ? 0.3145 0.2725 0.3491 -0.0181 0.0565  0.1006  100 VAL   B CG2 
5453 C CG2 B VAL   B 100 ? 0.3156 0.2695 0.3232 0.0009  0.0391  0.0836  100 VAL   B CG2 
5472 N N   . ASN   B 101 ? 0.3449 0.2583 0.2573 0.0391  0.0365  0.1225  101 ASN   B N   
5473 C CA  . ASN   B 101 ? 0.3861 0.2834 0.2745 0.0459  0.0243  0.1265  101 ASN   B CA  
5474 C C   . ASN   B 101 ? 0.4285 0.3301 0.2814 0.0449  0.0050  0.1218  101 ASN   B C   
5475 O O   . ASN   B 101 ? 0.4373 0.3444 0.3078 0.0534  0.0047  0.1001  101 ASN   B O   
5476 C CB  . ASN   B 101 ? 0.3865 0.2690 0.2988 0.0420  0.0412  0.1190  101 ASN   B CB  
5477 C CG  . ASN   B 101 ? 0.3854 0.2551 0.2973 0.0439  0.0520  0.1244  101 ASN   B CG  
5478 O OD1 . ASN   B 101 ? 0.3938 0.2577 0.3343 0.0395  0.0653  0.1146  101 ASN   B OD1 
5479 N ND2 . ASN   B 101 ? 0.3792 0.2524 0.2908 0.0472  0.0480  0.1149  101 ASN   B ND2 
5487 N N   A LYS   B 102 ? 0.4458 0.3500 0.2908 0.0363  0.0050  0.1109  102 LYS   B N   
5488 N N   B LYS   B 102 ? 0.4425 0.3506 0.3005 0.0372  0.0050  0.1096  102 LYS   B N   
5489 C CA  A LYS   B 102 ? 0.4621 0.3752 0.3099 0.0257  0.0098  0.0853  102 LYS   B CA  
5490 C CA  B LYS   B 102 ? 0.4549 0.3730 0.3229 0.0283  0.0094  0.0881  102 LYS   B CA  
5491 C C   A LYS   B 102 ? 0.4591 0.3769 0.2871 0.0283  0.0167  0.0898  102 LYS   B C   
5492 C C   B LYS   B 102 ? 0.4541 0.3751 0.3022 0.0288  0.0173  0.0911  102 LYS   B C   
5493 O O   A LYS   B 102 ? 0.4672 0.3834 0.2937 0.0287  0.0071  0.0824  102 LYS   B O   
5494 O O   B LYS   B 102 ? 0.4598 0.3798 0.3137 0.0285  0.0108  0.0860  102 LYS   B O   
5495 C CB  A LYS   B 102 ? 0.4788 0.3973 0.3622 0.0141  0.0146  0.0503  102 LYS   B CB  
5496 C CB  B LYS   B 102 ? 0.4659 0.3913 0.3696 0.0201  0.0111  0.0600  102 LYS   B CB  
5497 C CG  A LYS   B 102 ? 0.4933 0.4169 0.4171 0.0044  0.0208  0.0169  102 LYS   B CG  
5498 C CG  B LYS   B 102 ? 0.4748 0.4068 0.4143 0.0134  0.0142  0.0326  102 LYS   B CG  
5499 C CD  A LYS   B 102 ? 0.5061 0.4334 0.4725 -0.0024 0.0278  -0.0078 102 LYS   B CD  
5500 C CD  B LYS   B 102 ? 0.4826 0.4196 0.4557 0.0088  0.0178  0.0119  102 LYS   B CD  
5501 C CE  A LYS   B 102 ? 0.5152 0.4447 0.5140 -0.0071 0.0330  -0.0264 102 LYS   B CE  
5502 C CE  B LYS   B 102 ? 0.4880 0.4284 0.4854 0.0058  0.0206  -0.0035 102 LYS   B CE  
5503 N NZ  A LYS   B 102 ? 0.5200 0.4518 0.5417 -0.0089 0.0349  -0.0372 102 LYS   B NZ  
5504 N NZ  B LYS   B 102 ? 0.4908 0.4338 0.5041 0.0049  0.0217  -0.0121 102 LYS   B NZ  
5531 N N   . GLY   B 103 ? 0.4449 0.3703 0.2794 0.0288  0.0329  0.0939  103 GLY   B N   
5532 C CA  . GLY   B 103 ? 0.4220 0.3616 0.2832 0.0272  0.0608  0.0785  103 GLY   B CA  
5533 C C   . GLY   B 103 ? 0.3953 0.3477 0.2741 0.0218  0.0818  0.0653  103 GLY   B C   
5534 O O   . GLY   B 103 ? 0.4028 0.3606 0.2868 0.0186  0.0837  0.0648  103 GLY   B O   
5539 N N   A GLU   B 104 ? 0.3743 0.3292 0.2530 0.0234  0.0991  0.0558  104 GLU   B N   
5540 N N   B GLU   B 104 ? 0.3792 0.3338 0.2729 0.0163  0.0746  0.0546  104 GLU   B N   
5541 C CA  A GLU   B 104 ? 0.3526 0.3133 0.2351 0.0292  0.1062  0.0408  104 GLU   B CA  
5542 C CA  B GLU   B 104 ? 0.3621 0.3207 0.2681 0.0122  0.0641  0.0412  104 GLU   B CA  
5543 C C   A GLU   B 104 ? 0.3583 0.3155 0.2526 0.0144  0.1314  0.0380  104 GLU   B C   
5544 C C   B GLU   B 104 ? 0.3573 0.3159 0.2787 0.0050  0.0769  0.0368  104 GLU   B C   
5545 O O   A GLU   B 104 ? 0.3625 0.3183 0.2893 0.0125  0.1211  0.0278  104 GLU   B O   
5546 O O   B GLU   B 104 ? 0.3598 0.3164 0.2961 0.0048  0.0721  0.0289  104 GLU   B O   
5547 C CB  A GLU   B 104 ? 0.3336 0.2946 0.2205 0.0477  0.0728  0.0194  104 GLU   B CB  
5548 C CB  B GLU   B 104 ? 0.3538 0.3117 0.2583 0.0132  0.0384  0.0278  104 GLU   B CB  
5549 C CG  A GLU   B 104 ? 0.3217 0.2812 0.2040 0.0624  0.0341  -0.0093 104 GLU   B CG  
5550 C CG  B GLU   B 104 ? 0.3496 0.3054 0.2497 0.0126  0.0133  0.0109  104 GLU   B CG  
5551 C CD  A GLU   B 104 ? 0.3102 0.2703 0.1796 0.0742  -0.0025 -0.0183 104 GLU   B CD  
5552 C CD  B GLU   B 104 ? 0.3475 0.3003 0.2393 0.0093  -0.0075 0.0032  104 GLU   B CD  
5553 O OE1 A GLU   B 104 ? 0.2889 0.2524 0.1444 0.0932  0.0035  -0.0105 104 GLU   B OE1 
5554 O OE1 B GLU   B 104 ? 0.3433 0.2941 0.2287 0.0064  -0.0071 0.0060  104 GLU   B OE1 
5555 O OE2 A GLU   B 104 ? 0.3181 0.2827 0.1906 0.0662  -0.0382 -0.0290 104 GLU   B OE2 
5556 O OE2 B GLU   B 104 ? 0.3502 0.3047 0.2413 0.0081  -0.0246 -0.0050 104 GLU   B OE2 
5569 N N   A ASP   B 105 ? 0.3561 0.3180 0.2515 0.0000  0.1551  0.0460  105 ASP   B N   
5570 N N   B ASP   B 105 ? 0.3482 0.3123 0.2717 -0.0035 0.0913  0.0410  105 ASP   B N   
5571 C CA  A ASP   B 105 ? 0.3594 0.3200 0.2810 -0.0140 0.1737  0.0374  105 ASP   B CA  
5572 C CA  B ASP   B 105 ? 0.3427 0.3085 0.2826 -0.0116 0.1043  0.0361  105 ASP   B CA  
5573 C C   A ASP   B 105 ? 0.3482 0.2928 0.2591 -0.0244 0.1691  0.0314  105 ASP   B C   
5574 C C   B ASP   B 105 ? 0.3372 0.2952 0.2722 -0.0144 0.0990  0.0238  105 ASP   B C   
5575 O O   A ASP   B 105 ? 0.3340 0.2813 0.2506 -0.0243 0.1632  0.0293  105 ASP   B O   
5576 O O   B ASP   B 105 ? 0.3328 0.2892 0.2601 -0.0159 0.0995  0.0231  105 ASP   B O   
5577 C CB  A ASP   B 105 ? 0.3745 0.3450 0.3596 -0.0106 0.1768  0.0194  105 ASP   B CB  
5578 C CB  B ASP   B 105 ? 0.3419 0.3162 0.3098 -0.0139 0.1173  0.0376  105 ASP   B CB  
5579 C CG  A ASP   B 105 ? 0.3852 0.3620 0.4303 -0.0124 0.1845  0.0077  105 ASP   B CG  
5580 C CG  B ASP   B 105 ? 0.3392 0.3195 0.3357 -0.0199 0.1346  0.0428  105 ASP   B CG  
5581 O OD1 A ASP   B 105 ? 0.3833 0.3671 0.4423 -0.0199 0.1970  0.0109  105 ASP   B OD1 
5582 O OD1 B ASP   B 105 ? 0.3356 0.3217 0.3384 -0.0275 0.1421  0.0451  105 ASP   B OD1 
5583 O OD2 A ASP   B 105 ? 0.3942 0.3697 0.4742 -0.0066 0.1700  -0.0035 105 ASP   B OD2 
5584 O OD2 B ASP   B 105 ? 0.3357 0.3193 0.3370 -0.0231 0.1474  0.0511  105 ASP   B OD2 
5593 N N   A ILE   B 106 ? 0.3452 0.2739 0.2684 -0.0289 0.1570  0.0288  106 ILE   B N   
5594 N N   B ILE   B 106 ? 0.3342 0.2861 0.2709 -0.0123 0.0903  0.0136  106 ILE   B N   
5595 C CA  A ILE   B 106 ? 0.3284 0.2507 0.2744 -0.0419 0.1595  0.0271  106 ILE   B CA  
5596 C CA  B ILE   B 106 ? 0.3242 0.2766 0.2726 -0.0129 0.0874  0.0048  106 ILE   B CA  
5597 C C   A ILE   B 106 ? 0.2981 0.2461 0.2755 -0.0399 0.1525  0.0144  106 ILE   B C   
5598 C C   B ILE   B 106 ? 0.3046 0.2751 0.2734 -0.0102 0.0830  -0.0057 106 ILE   B C   
5599 O O   A ILE   B 106 ? 0.2852 0.2282 0.2743 -0.0430 0.1524  0.0108  106 ILE   B O   
5600 O O   B ILE   B 106 ? 0.2987 0.2681 0.2666 -0.0119 0.0762  -0.0105 106 ILE   B O   
5601 C CB  A ILE   B 106 ? 0.3498 0.2437 0.2984 -0.0457 0.1503  0.0298  106 ILE   B CB  
5602 C CB  B ILE   B 106 ? 0.3357 0.2750 0.2836 -0.0134 0.0860  0.0061  106 ILE   B CB  
5603 C CG1 A ILE   B 106 ? 0.3616 0.2475 0.3063 -0.0326 0.1419  0.0163  106 ILE   B CG1 
5604 C CG1 B ILE   B 106 ? 0.3416 0.2760 0.2889 -0.0072 0.0817  0.0012  106 ILE   B CG1 
5605 C CG2 A ILE   B 106 ? 0.3589 0.2475 0.3241 -0.0518 0.1449  0.0358  106 ILE   B CG2 
5606 C CG2 B ILE   B 106 ? 0.3408 0.2787 0.2979 -0.0161 0.0860  0.0081  106 ILE   B CG2 
5607 C CD1 A ILE   B 106 ? 0.3659 0.2499 0.3005 -0.0260 0.1422  0.0172  106 ILE   B CD1 
5608 C CD1 B ILE   B 106 ? 0.3436 0.2762 0.2885 -0.0038 0.0809  0.0026  106 ILE   B CD1 
5631 N N   A GLN   B 107 ? 0.2871 0.2630 0.2935 -0.0364 0.1367  0.0172  107 GLN   B N   
5632 N N   B GLN   B 107 ? 0.2942 0.2831 0.2914 -0.0085 0.0811  -0.0062 107 GLN   B N   
5633 C CA  A GLN   B 107 ? 0.2729 0.2791 0.3157 -0.0290 0.1215  0.0128  107 GLN   B CA  
5634 C CA  B GLN   B 107 ? 0.2832 0.2887 0.3091 -0.0058 0.0791  -0.0050 107 GLN   B CA  
5635 C C   A GLN   B 107 ? 0.2464 0.2625 0.2881 -0.0131 0.0901  -0.0005 107 GLN   B C   
5636 C C   B GLN   B 107 ? 0.2552 0.2692 0.2800 0.0001  0.0738  -0.0093 107 GLN   B C   
5637 O O   A GLN   B 107 ? 0.2399 0.2631 0.3219 -0.0054 0.0646  -0.0183 107 GLN   B O   
5638 O O   B GLN   B 107 ? 0.2537 0.2721 0.2999 0.0037  0.0615  -0.0218 107 GLN   B O   
5639 C CB  A GLN   B 107 ? 0.2997 0.3133 0.3863 -0.0279 0.1061  0.0143  107 GLN   B CB  
5640 C CB  B GLN   B 107 ? 0.3048 0.3138 0.3665 -0.0058 0.0699  -0.0019 107 GLN   B CB  
5641 C CG  A GLN   B 107 ? 0.3305 0.3464 0.4610 -0.0230 0.0738  0.0142  107 GLN   B CG  
5642 C CG  B GLN   B 107 ? 0.3262 0.3372 0.4246 -0.0043 0.0525  0.0006  107 GLN   B CG  
5643 C CD  A GLN   B 107 ? 0.3531 0.3718 0.5187 -0.0226 0.0485  0.0147  107 GLN   B CD  
5644 C CD  B GLN   B 107 ? 0.3422 0.3548 0.4698 -0.0052 0.0381  0.0024  107 GLN   B CD  
5645 O OE1 A GLN   B 107 ? 0.3602 0.3800 0.5394 -0.0211 0.0440  0.0110  107 GLN   B OE1 
5646 O OE1 B GLN   B 107 ? 0.3474 0.3609 0.4835 -0.0052 0.0359  0.0022  107 GLN   B OE1 
5647 N NE2 A GLN   B 107 ? 0.3611 0.3790 0.5390 -0.0207 0.0380  0.0202  107 GLN   B NE2 
5648 N NE2 B GLN   B 107 ? 0.3489 0.3610 0.4865 -0.0040 0.0327  0.0053  107 GLN   B NE2 
5665 N N   . LEU   B 108 ? 0.2275 0.2450 0.2418 0.0100  0.0768  -0.0071 108 LEU   B N   
5666 C CA  . LEU   B 108 ? 0.2105 0.2193 0.1934 0.0236  0.0449  0.0112  108 LEU   B CA  
5667 C C   . LEU   B 108 ? 0.1832 0.1840 0.1865 0.0240  0.0247  0.0314  108 LEU   B C   
5668 O O   . LEU   B 108 ? 0.1859 0.1793 0.1843 0.0188  0.0229  0.0241  108 LEU   B O   
5669 C CB  . LEU   B 108 ? 0.2261 0.2378 0.1800 0.0139  0.0429  0.0194  108 LEU   B CB  
5670 C CG  . LEU   B 108 ? 0.2470 0.2690 0.1910 0.0104  0.0365  -0.0053 108 LEU   B CG  
5671 C CD1 . LEU   B 108 ? 0.2506 0.2824 0.1694 0.0004  0.0452  -0.0098 108 LEU   B CD1 
5672 C CD2 . LEU   B 108 ? 0.2632 0.2840 0.2138 0.0265  0.0273  -0.0249 108 LEU   B CD2 
5685 N N   . LEU   B 109 ? 0.1722 0.1626 0.1845 0.0148  0.0311  0.0193  109 LEU   B N   
5686 C CA  . LEU   B 109 ? 0.1590 0.1396 0.1931 0.0099  0.0334  0.0332  109 LEU   B CA  
5687 C C   . LEU   B 109 ? 0.1427 0.1229 0.1898 0.0004  0.0285  0.0145  109 LEU   B C   
5688 O O   . LEU   B 109 ? 0.1397 0.1248 0.1977 0.0011  0.0288  0.0242  109 LEU   B O   
5689 C CB  . LEU   B 109 ? 0.1646 0.1309 0.1996 0.0101  0.0273  0.0383  109 LEU   B CB  
5690 C CG  . LEU   B 109 ? 0.1620 0.1310 0.1995 0.0048  0.0210  0.0212  109 LEU   B CG  
5691 C CD1 . LEU   B 109 ? 0.1555 0.1471 0.1829 0.0134  0.0275  0.0198  109 LEU   B CD1 
5692 C CD2 . LEU   B 109 ? 0.1757 0.1366 0.2043 0.0006  0.0165  0.0147  109 LEU   B CD2 
5704 N N   . LYS   B 110 ? 0.1394 0.1242 0.1943 -0.0019 0.0278  0.0212  110 LYS   B N   
5705 C CA  . LYS   B 110 ? 0.1312 0.1231 0.1892 -0.0037 0.0268  0.0152  110 LYS   B CA  
5706 C C   . LYS   B 110 ? 0.1312 0.1297 0.1662 0.0036  0.0257  0.0115  110 LYS   B C   
5707 O O   . LYS   B 110 ? 0.1303 0.1344 0.1658 -0.0008 0.0162  0.0036  110 LYS   B O   
5708 C CB  . LYS   B 110 ? 0.1484 0.1241 0.2046 -0.0041 0.0239  0.0005  110 LYS   B CB  
5709 C CG  . LYS   B 110 ? 0.1419 0.1205 0.2252 0.0003  0.0127  0.0074  110 LYS   B CG  
5710 C CD  . LYS   B 110 ? 0.1476 0.1252 0.2332 -0.0025 0.0141  0.0164  110 LYS   B CD  
5711 C CE  . LYS   B 110 ? 0.1416 0.1439 0.2527 -0.0054 0.0205  0.0068  110 LYS   B CE  
5712 N NZ  . LYS   B 110 ? 0.1473 0.1538 0.2550 -0.0016 0.0094  -0.0000 110 LYS   B NZ  
5726 N N   . SER   B 111 ? 0.1416 0.1306 0.1828 -0.0046 0.0266  0.0148  111 SER   B N   
5727 C CA  . SER   B 111 ? 0.1426 0.1344 0.1782 0.0002  0.0246  0.0119  111 SER   B CA  
5728 C C   . SER   B 111 ? 0.1420 0.1225 0.1735 0.0015  0.0118  -0.0011 111 SER   B C   
5729 O O   . SER   B 111 ? 0.1399 0.1234 0.1785 -0.0020 0.0074  0.0086  111 SER   B O   
5730 C CB  . SER   B 111 ? 0.1548 0.1498 0.1894 0.0036  0.0431  0.0203  111 SER   B CB  
5731 O OG  . SER   B 111 ? 0.1748 0.1923 0.2032 0.0077  0.0387  0.0210  111 SER   B OG  
5737 N N   . ALA   B 112 ? 0.1341 0.1244 0.1780 0.0060  0.0132  0.0099  112 ALA   B N   
5738 C CA  . ALA   B 112 ? 0.1302 0.1359 0.1665 0.0032  0.0075  -0.0014 112 ALA   B CA  
5739 C C   . ALA   B 112 ? 0.1170 0.1314 0.1539 0.0028  0.0100  0.0023  112 ALA   B C   
5740 O O   . ALA   B 112 ? 0.1260 0.1325 0.1539 -0.0057 0.0060  -0.0075 112 ALA   B O   
5741 C CB  . ALA   B 112 ? 0.1372 0.1420 0.1812 0.0075  0.0101  0.0138  112 ALA   B CB  
5747 N N   . TYR   B 113 ? 0.1210 0.1198 0.1682 0.0005  0.0146  0.0067  113 TYR   B N   
5748 C CA  . TYR   B 113 ? 0.1181 0.1130 0.1616 -0.0009 0.0097  0.0021  113 TYR   B CA  
5749 C C   . TYR   B 113 ? 0.1159 0.1073 0.1601 -0.0073 0.0109  0.0024  113 TYR   B C   
5750 O O   . TYR   B 113 ? 0.1214 0.1107 0.1513 -0.0039 0.0092  -0.0019 113 TYR   B O   
5751 C CB  . TYR   B 113 ? 0.1200 0.1129 0.1751 -0.0073 0.0173  0.0031  113 TYR   B CB  
5752 C CG  . TYR   B 113 ? 0.1295 0.1203 0.1718 -0.0033 0.0095  0.0120  113 TYR   B CG  
5753 C CD1 . TYR   B 113 ? 0.1305 0.1262 0.1721 0.0001  0.0111  0.0174  113 TYR   B CD1 
5754 C CD2 . TYR   B 113 ? 0.1431 0.1184 0.1754 -0.0018 0.0084  0.0157  113 TYR   B CD2 
5755 C CE1 . TYR   B 113 ? 0.1333 0.1240 0.1719 -0.0023 0.0203  0.0055  113 TYR   B CE1 
5756 C CE2 . TYR   B 113 ? 0.1434 0.1163 0.1874 -0.0010 0.0057  0.0141  113 TYR   B CE2 
5757 C CZ  . TYR   B 113 ? 0.1309 0.1215 0.1864 0.0059  0.0074  0.0091  113 TYR   B CZ  
5758 O OH  . TYR   B 113 ? 0.1357 0.1168 0.2044 0.0095  0.0171  0.0050  113 TYR   B OH  
5768 N N   . GLU   B 114 ? 0.1166 0.1044 0.1661 -0.0012 0.0130  0.0098  114 GLU   B N   
5769 C CA  . GLU   B 114 ? 0.1184 0.1133 0.1675 0.0027  0.0121  -0.0053 114 GLU   B CA  
5770 C C   . GLU   B 114 ? 0.1175 0.1148 0.1505 -0.0009 0.0035  0.0023  114 GLU   B C   
5771 O O   . GLU   B 114 ? 0.1132 0.1191 0.1626 0.0023  0.0009  0.0056  114 GLU   B O   
5772 C CB  . GLU   B 114 ? 0.1222 0.1221 0.1731 -0.0028 0.0073  -0.0002 114 GLU   B CB  
5773 C CG  . GLU   B 114 ? 0.1265 0.1202 0.1690 0.0002  0.0033  0.0067  114 GLU   B CG  
5774 C CD  . GLU   B 114 ? 0.1269 0.1195 0.1733 -0.0061 0.0081  0.0079  114 GLU   B CD  
5775 O OE1 . GLU   B 114 ? 0.1233 0.1364 0.1744 -0.0072 0.0157  0.0064  114 GLU   B OE1 
5776 O OE2 . GLU   B 114 ? 0.1274 0.1405 0.1863 -0.0171 0.0079  0.0047  114 GLU   B OE2 
5783 N N   . ASN   B 115 ? 0.1247 0.1088 0.1430 -0.0036 0.0041  0.0012  115 ASN   B N   
5784 C CA  . ASN   B 115 ? 0.1248 0.1172 0.1395 -0.0073 0.0013  0.0050  115 ASN   B CA  
5785 C C   . ASN   B 115 ? 0.1182 0.1107 0.1400 -0.0084 -0.0010 -0.0054 115 ASN   B C   
5786 O O   . ASN   B 115 ? 0.1324 0.1195 0.1444 -0.0151 0.0037  0.0013  115 ASN   B O   
5787 C CB  . ASN   B 115 ? 0.1293 0.1304 0.1409 -0.0089 0.0010  0.0064  115 ASN   B CB  
5788 C CG  . ASN   B 115 ? 0.1432 0.1359 0.1492 0.0006  -0.0019 -0.0017 115 ASN   B CG  
5789 O OD1 . ASN   B 115 ? 0.1817 0.1479 0.1653 0.0029  0.0114  -0.0164 115 ASN   B OD1 
5790 N ND2 . ASN   B 115 ? 0.1455 0.1473 0.1407 -0.0012 0.0049  -0.0019 115 ASN   B ND2 
5797 N N   . PHE   B 116 ? 0.1196 0.1166 0.1287 -0.0056 0.0037  0.0017  116 PHE   B N   
5798 C CA  . PHE   B 116 ? 0.1300 0.1173 0.1374 -0.0105 0.0001  0.0013  116 PHE   B CA  
5799 C C   . PHE   B 116 ? 0.1296 0.1074 0.1379 -0.0112 0.0069  -0.0025 116 PHE   B C   
5800 O O   . PHE   B 116 ? 0.1204 0.1202 0.1454 -0.0016 -0.0004 0.0028  116 PHE   B O   
5801 C CB  . PHE   B 116 ? 0.1256 0.1077 0.1384 -0.0097 -0.0129 -0.0004 116 PHE   B CB  
5802 C CG  . PHE   B 116 ? 0.1149 0.1126 0.1365 -0.0050 0.0018  -0.0069 116 PHE   B CG  
5803 C CD1 . PHE   B 116 ? 0.1193 0.1197 0.1571 -0.0059 0.0000  -0.0054 116 PHE   B CD1 
5804 C CD2 . PHE   B 116 ? 0.1137 0.1222 0.1434 -0.0018 0.0003  -0.0077 116 PHE   B CD2 
5805 C CE1 . PHE   B 116 ? 0.1175 0.1197 0.1579 -0.0027 -0.0158 0.0013  116 PHE   B CE1 
5806 C CE2 . PHE   B 116 ? 0.1138 0.1247 0.1575 0.0001  0.0028  0.0005  116 PHE   B CE2 
5807 C CZ  . PHE   B 116 ? 0.1064 0.1153 0.1649 0.0016  -0.0096 0.0032  116 PHE   B CZ  
5817 N N   . ASN   B 117 ? 0.1291 0.1057 0.1506 -0.0087 -0.0024 0.0028  117 ASN   B N   
5818 C CA  . ASN   B 117 ? 0.1287 0.1118 0.1493 -0.0057 -0.0056 0.0015  117 ASN   B CA  
5819 C C   . ASN   B 117 ? 0.1295 0.1083 0.1655 -0.0011 -0.0087 0.0026  117 ASN   B C   
5820 O O   . ASN   B 117 ? 0.1368 0.1173 0.1825 -0.0051 -0.0229 0.0097  117 ASN   B O   
5821 C CB  . ASN   B 117 ? 0.1274 0.1171 0.1524 -0.0079 -0.0002 -0.0091 117 ASN   B CB  
5822 C CG  . ASN   B 117 ? 0.1197 0.1116 0.1622 -0.0021 0.0013  -0.0088 117 ASN   B CG  
5823 O OD1 . ASN   B 117 ? 0.1439 0.1164 0.1720 -0.0084 0.0076  -0.0102 117 ASN   B OD1 
5824 N ND2 . ASN   B 117 ? 0.1282 0.1131 0.1621 0.0007  0.0008  -0.0091 117 ASN   B ND2 
5831 N N   . GLN   B 118 ? 0.1267 0.1030 0.1662 -0.0050 -0.0099 0.0018  118 GLN   B N   
5832 C CA  . GLN   B 118 ? 0.1366 0.1122 0.1731 0.0026  -0.0077 -0.0012 118 GLN   B CA  
5833 C C   . GLN   B 118 ? 0.1390 0.1188 0.1816 0.0002  -0.0062 -0.0036 118 GLN   B C   
5834 O O   . GLN   B 118 ? 0.1553 0.1209 0.2040 -0.0086 0.0018  0.0031  118 GLN   B O   
5835 C CB  . GLN   B 118 ? 0.1437 0.1212 0.1864 0.0080  -0.0135 -0.0012 118 GLN   B CB  
5836 C CG  . GLN   B 118 ? 0.1524 0.1173 0.1747 0.0080  -0.0125 -0.0098 118 GLN   B CG  
5837 C CD  . GLN   B 118 ? 0.1597 0.1115 0.1692 0.0031  -0.0047 -0.0266 118 GLN   B CD  
5838 O OE1 . GLN   B 118 ? 0.1662 0.1128 0.1880 0.0089  0.0091  -0.0036 118 GLN   B OE1 
5839 N NE2 . GLN   B 118 ? 0.1599 0.1119 0.1765 -0.0023 -0.0060 -0.0074 118 GLN   B NE2 
5848 N N   . HIS   B 119 ? 0.1370 0.1211 0.1405 -0.0016 -0.0067 0.0013  119 HIS   B N   
5849 C CA  . HIS   B 119 ? 0.1457 0.1287 0.1376 -0.0021 -0.0139 0.0033  119 HIS   B CA  
5850 C C   . HIS   B 119 ? 0.1502 0.1229 0.1383 -0.0041 -0.0230 0.0068  119 HIS   B C   
5851 O O   . HIS   B 119 ? 0.1526 0.1250 0.1549 -0.0204 -0.0158 0.0069  119 HIS   B O   
5852 C CB  . HIS   B 119 ? 0.1487 0.1374 0.1497 -0.0032 -0.0134 -0.0055 119 HIS   B CB  
5853 C CG  . HIS   B 119 ? 0.1530 0.1643 0.1640 0.0117  -0.0291 -0.0238 119 HIS   B CG  
5854 N ND1 . HIS   B 119 ? 0.1660 0.1764 0.1937 0.0024  -0.0390 -0.0361 119 HIS   B ND1 
5855 C CD2 . HIS   B 119 ? 0.1651 0.1803 0.1784 0.0412  -0.0365 -0.0202 119 HIS   B CD2 
5856 C CE1 . HIS   B 119 ? 0.1879 0.1934 0.2039 0.0208  -0.0481 -0.0485 119 HIS   B CE1 
5857 N NE2 . HIS   B 119 ? 0.1850 0.2046 0.1983 0.0345  -0.0453 -0.0400 119 HIS   B NE2 
5865 N N   . GLU   B 120 ? 0.1660 0.1293 0.1437 -0.0111 -0.0278 0.0079  120 GLU   B N   
5866 C CA  . GLU   B 120 ? 0.1904 0.1501 0.1524 -0.0010 -0.0392 0.0232  120 GLU   B CA  
5867 C C   . GLU   B 120 ? 0.1692 0.1422 0.1345 -0.0130 -0.0290 0.0167  120 GLU   B C   
5868 O O   . GLU   B 120 ? 0.1649 0.1460 0.1383 -0.0140 -0.0262 0.0090  120 GLU   B O   
5869 C CB  . GLU   B 120 ? 0.2642 0.1881 0.2264 0.0270  -0.0719 0.0494  120 GLU   B CB  
5870 C CG  . GLU   B 120 ? 0.3257 0.2576 0.3351 0.0340  -0.0938 0.0689  120 GLU   B CG  
5871 C CD  . GLU   B 120 ? 0.3796 0.3333 0.4503 0.0360  -0.1041 0.0792  120 GLU   B CD  
5872 O OE1 . GLU   B 120 ? 0.4037 0.3610 0.4799 0.0312  -0.0998 0.0886  120 GLU   B OE1 
5873 O OE2 . GLU   B 120 ? 0.4011 0.3670 0.5103 0.0389  -0.1060 0.0758  120 GLU   B OE2 
5880 N N   . VAL   B 121 ? 0.1594 0.1284 0.1341 -0.0181 -0.0165 0.0177  121 VAL   B N   
5881 C CA  . VAL   B 121 ? 0.1571 0.1413 0.1338 -0.0143 -0.0104 0.0069  121 VAL   B CA  
5882 C C   . VAL   B 121 ? 0.1419 0.1355 0.1323 -0.0187 -0.0116 0.0128  121 VAL   B C   
5883 O O   . VAL   B 121 ? 0.1508 0.1297 0.1498 -0.0297 -0.0179 0.0023  121 VAL   B O   
5884 C CB  . VAL   B 121 ? 0.1729 0.1764 0.1411 -0.0001 -0.0176 0.0103  121 VAL   B CB  
5885 C CG1 . VAL   B 121 ? 0.1808 0.1909 0.1794 -0.0077 -0.0109 0.0072  121 VAL   B CG1 
5886 C CG2 . VAL   B 121 ? 0.1941 0.2031 0.1414 0.0064  -0.0118 -0.0022 121 VAL   B CG2 
5896 N N   . LEU   B 122 ? 0.1361 0.1323 0.1330 -0.0088 -0.0139 0.0137  122 LEU   B N   
5897 C CA  . LEU   B 122 ? 0.1297 0.1428 0.1150 -0.0167 -0.0114 0.0073  122 LEU   B CA  
5898 C C   . LEU   B 122 ? 0.1299 0.1276 0.1193 -0.0238 -0.0100 0.0022  122 LEU   B C   
5899 O O   . LEU   B 122 ? 0.1374 0.1294 0.1563 -0.0309 -0.0182 -0.0074 122 LEU   B O   
5900 C CB  . LEU   B 122 ? 0.1597 0.1465 0.1511 -0.0007 -0.0187 0.0114  122 LEU   B CB  
5901 C CG  . LEU   B 122 ? 0.1485 0.1463 0.1532 -0.0143 -0.0080 0.0088  122 LEU   B CG  
5902 C CD1 . LEU   B 122 ? 0.1506 0.1707 0.1582 -0.0137 -0.0184 0.0091  122 LEU   B CD1 
5903 C CD2 . LEU   B 122 ? 0.1498 0.1529 0.1277 -0.0073 -0.0049 -0.0106 122 LEU   B CD2 
5915 N N   . LEU   B 123 ? 0.1332 0.1201 0.1145 -0.0210 -0.0087 0.0040  123 LEU   B N   
5916 C CA  . LEU   B 123 ? 0.1374 0.1203 0.1189 -0.0231 -0.0152 0.0011  123 LEU   B CA  
5917 C C   . LEU   B 123 ? 0.1328 0.1175 0.1187 -0.0243 -0.0113 -0.0000 123 LEU   B C   
5918 O O   . LEU   B 123 ? 0.1466 0.1281 0.1177 -0.0292 -0.0126 -0.0000 123 LEU   B O   
5919 C CB  . LEU   B 123 ? 0.1421 0.1198 0.1276 -0.0190 -0.0083 -0.0033 123 LEU   B CB  
5920 C CG  . LEU   B 123 ? 0.1347 0.1288 0.1494 -0.0158 -0.0028 0.0069  123 LEU   B CG  
5921 C CD1 . LEU   B 123 ? 0.1409 0.1306 0.1544 -0.0112 0.0011  -0.0085 123 LEU   B CD1 
5922 C CD2 . LEU   B 123 ? 0.1420 0.1356 0.1587 -0.0174 -0.0054 0.0193  123 LEU   B CD2 
5934 N N   . ALA   B 124 ? 0.1295 0.1142 0.1224 -0.0166 -0.0034 0.0009  124 ALA   B N   
5935 C CA  . ALA   B 124 ? 0.1179 0.1181 0.1268 -0.0189 -0.0068 -0.0049 124 ALA   B CA  
5936 C C   . ALA   B 124 ? 0.1201 0.1138 0.1222 -0.0174 -0.0116 -0.0017 124 ALA   B C   
5937 O O   . ALA   B 124 ? 0.1315 0.1170 0.1337 -0.0127 -0.0045 -0.0031 124 ALA   B O   
5938 C CB  . ALA   B 124 ? 0.1299 0.1225 0.1287 -0.0022 0.0026  -0.0038 124 ALA   B CB  
5944 N N   . PRO   B 125 ? 0.1310 0.1175 0.1247 -0.0196 -0.0152 0.0066  125 PRO   B N   
5945 C CA  . PRO   B 125 ? 0.1433 0.1183 0.1373 -0.0128 -0.0139 0.0107  125 PRO   B CA  
5946 C C   . PRO   B 125 ? 0.1380 0.1101 0.1506 -0.0138 -0.0110 0.0066  125 PRO   B C   
5947 O O   . PRO   B 125 ? 0.1379 0.1119 0.1692 -0.0087 -0.0027 0.0135  125 PRO   B O   
5948 C CB  . PRO   B 125 ? 0.1440 0.1445 0.1508 -0.0241 -0.0167 0.0195  125 PRO   B CB  
5949 C CG  . PRO   B 125 ? 0.1475 0.1472 0.1407 -0.0287 -0.0166 0.0092  125 PRO   B CG  
5950 C CD  . PRO   B 125 ? 0.1393 0.1330 0.1225 -0.0276 -0.0096 0.0119  125 PRO   B CD  
5958 N N   . LEU   B 126 ? 0.1354 0.1096 0.1677 -0.0148 0.0048  0.0077  126 LEU   B N   
5959 C CA  . LEU   B 126 ? 0.1400 0.1171 0.1786 -0.0126 0.0134  0.0112  126 LEU   B CA  
5960 C C   . LEU   B 126 ? 0.1413 0.1260 0.1741 -0.0014 0.0078  0.0165  126 LEU   B C   
5961 O O   . LEU   B 126 ? 0.1599 0.1519 0.1961 0.0160  -0.0106 -0.0059 126 LEU   B O   
5962 C CB  . LEU   B 126 ? 0.1580 0.1232 0.2016 -0.0135 0.0263  0.0064  126 LEU   B CB  
5963 C CG  . LEU   B 126 ? 0.1806 0.1324 0.2112 -0.0204 0.0266  -0.0124 126 LEU   B CG  
5964 C CD1 . LEU   B 126 ? 0.1914 0.1436 0.2619 -0.0261 0.0199  -0.0228 126 LEU   B CD1 
5965 C CD2 . LEU   B 126 ? 0.1910 0.1401 0.2051 -0.0288 0.0253  -0.0086 126 LEU   B CD2 
5977 N N   . LEU   B 127 ? 0.1391 0.1144 0.1856 0.0018  0.0213  0.0053  127 LEU   B N   
5978 C CA  . LEU   B 127 ? 0.1388 0.1257 0.1925 -0.0083 0.0199  0.0135  127 LEU   B CA  
5979 C C   . LEU   B 127 ? 0.1269 0.1287 0.1903 -0.0047 0.0216  0.0132  127 LEU   B C   
5980 O O   . LEU   B 127 ? 0.1336 0.1352 0.1922 -0.0152 0.0134  0.0185  127 LEU   B O   
5981 C CB  . LEU   B 127 ? 0.1507 0.1273 0.1841 -0.0040 0.0133  0.0151  127 LEU   B CB  
5982 C CG  . LEU   B 127 ? 0.1653 0.1294 0.1926 0.0052  0.0203  0.0203  127 LEU   B CG  
5983 C CD1 . LEU   B 127 ? 0.1738 0.1272 0.1938 0.0100  0.0186  0.0219  127 LEU   B CD1 
5984 C CD2 . LEU   B 127 ? 0.1710 0.1402 0.2110 -0.0076 0.0256  0.0239  127 LEU   B CD2 
5996 N N   . SER   B 128 ? 0.1358 0.1335 0.1789 0.0056  -0.0030 0.0119  128 SER   B N   
5997 C CA  . SER   B 128 ? 0.1513 0.1349 0.1759 0.0132  -0.0098 0.0203  128 SER   B CA  
5998 C C   . SER   B 128 ? 0.1588 0.1358 0.1949 0.0090  -0.0174 0.0198  128 SER   B C   
5999 O O   . SER   B 128 ? 0.1769 0.1376 0.2393 0.0040  -0.0120 0.0332  128 SER   B O   
6000 C CB  . SER   B 128 ? 0.1621 0.1375 0.1862 0.0123  -0.0003 0.0311  128 SER   B CB  
6001 O OG  . SER   B 128 ? 0.1640 0.1464 0.1888 0.0151  0.0069  0.0300  128 SER   B OG  
6007 N N   . ALA   B 129 ? 0.1659 0.1439 0.2182 0.0231  -0.0110 0.0104  129 ALA   B N   
6008 C CA  . ALA   B 129 ? 0.1835 0.1491 0.2256 0.0320  -0.0058 0.0035  129 ALA   B CA  
6009 C C   . ALA   B 129 ? 0.1733 0.1441 0.2142 0.0204  0.0053  0.0007  129 ALA   B C   
6010 O O   . ALA   B 129 ? 0.1610 0.1445 0.2263 0.0135  -0.0012 0.0077  129 ALA   B O   
6011 C CB  . ALA   B 129 ? 0.2040 0.1702 0.2508 0.0336  0.0026  -0.0037 129 ALA   B CB  
6017 N N   . GLY   B 130 ? 0.1751 0.1418 0.2168 0.0261  0.0025  0.0020  130 GLY   B N   
6018 C CA  . GLY   B 130 ? 0.1796 0.1522 0.2325 0.0170  0.0172  0.0018  130 GLY   B CA  
6019 C C   . GLY   B 130 ? 0.1821 0.1477 0.2303 0.0169  0.0092  0.0131  130 GLY   B C   
6020 O O   . GLY   B 130 ? 0.2000 0.1559 0.2353 0.0161  0.0084  0.0188  130 GLY   B O   
6024 N N   . ILE   B 131 ? 0.1734 0.1592 0.2369 0.0324  0.0007  0.0086  131 ILE   B N   
6025 C CA  . ILE   B 131 ? 0.1951 0.1687 0.2407 0.0258  -0.0155 0.0174  131 ILE   B CA  
6026 C C   . ILE   B 131 ? 0.2089 0.1662 0.2070 0.0219  -0.0060 0.0213  131 ILE   B C   
6027 O O   . ILE   B 131 ? 0.2346 0.1842 0.2186 0.0213  -0.0234 0.0209  131 ILE   B O   
6028 C CB  . ILE   B 131 ? 0.1997 0.2045 0.2875 0.0228  -0.0222 0.0260  131 ILE   B CB  
6029 C CG1 . ILE   B 131 ? 0.1963 0.2178 0.3016 -0.0006 -0.0178 0.0336  131 ILE   B CG1 
6030 C CG2 . ILE   B 131 ? 0.2016 0.2234 0.3098 0.0262  -0.0092 0.0156  131 ILE   B CG2 
6031 C CD1 . ILE   B 131 ? 0.1998 0.2367 0.3169 -0.0220 -0.0178 0.0402  131 ILE   B CD1 
6043 N N   . PHE   B 132 ? 0.1885 0.1454 0.1972 0.0191  0.0118  0.0201  132 PHE   B N   
6044 C CA  . PHE   B 132 ? 0.1946 0.1567 0.1873 0.0088  0.0357  0.0130  132 PHE   B CA  
6045 C C   . PHE   B 132 ? 0.2143 0.1753 0.1997 0.0073  0.0344  0.0178  132 PHE   B C   
6046 O O   . PHE   B 132 ? 0.2348 0.1940 0.2322 -0.0010 0.0488  0.0255  132 PHE   B O   
6047 C CB  . PHE   B 132 ? 0.1768 0.1556 0.1727 0.0136  0.0301  0.0254  132 PHE   B CB  
6048 C CG  . PHE   B 132 ? 0.1811 0.1571 0.1686 0.0170  0.0209  0.0206  132 PHE   B CG  
6049 C CD1 . PHE   B 132 ? 0.1874 0.1535 0.2075 0.0102  0.0216  0.0173  132 PHE   B CD1 
6050 C CD2 . PHE   B 132 ? 0.1807 0.1551 0.1409 0.0267  0.0164  0.0251  132 PHE   B CD2 
6051 C CE1 . PHE   B 132 ? 0.1919 0.1597 0.2281 0.0109  0.0153  0.0235  132 PHE   B CE1 
6052 C CE2 . PHE   B 132 ? 0.1869 0.1585 0.1653 0.0275  0.0101  0.0179  132 PHE   B CE2 
6053 C CZ  . PHE   B 132 ? 0.1904 0.1622 0.2175 0.0124  0.0052  0.0231  132 PHE   B CZ  
6063 N N   . GLY   B 133 ? 0.2096 0.1676 0.1990 0.0036  0.0179  0.0443  133 GLY   B N   
6064 C CA  . GLY   B 133 ? 0.2178 0.1809 0.2217 -0.0167 0.0210  0.0446  133 GLY   B CA  
6065 C C   . GLY   B 133 ? 0.2234 0.1885 0.2168 -0.0313 0.0284  0.0497  133 GLY   B C   
6066 O O   . GLY   B 133 ? 0.2422 0.1991 0.2581 -0.0398 0.0294  0.0581  133 GLY   B O   
6070 N N   . ALA   B 134 ? 0.2094 0.1846 0.1978 -0.0300 0.0250  0.0361  134 ALA   B N   
6071 C CA  . ALA   B 134 ? 0.2030 0.1770 0.2221 -0.0190 0.0255  0.0208  134 ALA   B CA  
6072 C C   . ALA   B 134 ? 0.2093 0.1646 0.2283 -0.0104 0.0281  0.0237  134 ALA   B C   
6073 O O   . ALA   B 134 ? 0.2111 0.1836 0.2416 0.0035  0.0266  0.0212  134 ALA   B O   
6074 C CB  . ALA   B 134 ? 0.1912 0.1760 0.2375 -0.0085 0.0179  0.0171  134 ALA   B CB  
6080 N N   . ASP   B 135 ? 0.2240 0.1543 0.2304 -0.0148 0.0091  0.0320  135 ASP   B N   
6081 C CA  . ASP   B 135 ? 0.2368 0.1489 0.2531 -0.0135 0.0047  0.0330  135 ASP   B CA  
6082 C C   . ASP   B 135 ? 0.2134 0.1405 0.2350 -0.0016 -0.0052 0.0204  135 ASP   B C   
6083 O O   . ASP   B 135 ? 0.2053 0.1367 0.2458 0.0016  0.0004  0.0185  135 ASP   B O   
6084 C CB  . ASP   B 135 ? 0.2657 0.1657 0.2888 -0.0386 0.0060  0.0453  135 ASP   B CB  
6085 C CG  . ASP   B 135 ? 0.2929 0.1681 0.3322 -0.0576 0.0039  0.0417  135 ASP   B CG  
6086 O OD1 . ASP   B 135 ? 0.3056 0.1535 0.3213 -0.0379 -0.0156 0.0302  135 ASP   B OD1 
6087 O OD2 . ASP   B 135 ? 0.3136 0.2066 0.3808 -0.0765 0.0054  0.0210  135 ASP   B OD2 
6092 N N   . PRO   B 136 ? 0.2076 0.1471 0.2363 0.0184  -0.0169 0.0174  136 PRO   B N   
6093 C CA  . PRO   B 136 ? 0.1873 0.1368 0.2382 0.0128  -0.0183 0.0070  136 PRO   B CA  
6094 C C   . PRO   B 136 ? 0.1713 0.1294 0.2356 0.0118  -0.0052 -0.0008 136 PRO   B C   
6095 O O   . PRO   B 136 ? 0.1548 0.1304 0.2258 0.0087  0.0050  -0.0025 136 PRO   B O   
6096 C CB  . PRO   B 136 ? 0.1954 0.1602 0.2584 0.0244  -0.0210 -0.0016 136 PRO   B CB  
6097 C CG  . PRO   B 136 ? 0.2163 0.1675 0.2745 0.0299  -0.0118 -0.0015 136 PRO   B CG  
6098 C CD  . PRO   B 136 ? 0.2146 0.1607 0.2591 0.0400  -0.0018 0.0089  136 PRO   B CD  
6106 N N   . ILE   B 137 ? 0.1820 0.1266 0.2512 0.0123  -0.0060 0.0011  137 ILE   B N   
6107 C CA  . ILE   B 137 ? 0.1889 0.1219 0.2585 0.0018  0.0023  0.0063  137 ILE   B CA  
6108 C C   . ILE   B 137 ? 0.1784 0.1235 0.2476 -0.0054 0.0100  0.0132  137 ILE   B C   
6109 O O   . ILE   B 137 ? 0.1679 0.1279 0.2431 -0.0073 0.0062  0.0055  137 ILE   B O   
6110 C CB  . ILE   B 137 ? 0.2130 0.1274 0.3131 -0.0026 -0.0031 0.0063  137 ILE   B CB  
6111 C CG1 . ILE   B 137 ? 0.2378 0.1462 0.3581 0.0059  0.0045  -0.0064 137 ILE   B CG1 
6112 C CG2 . ILE   B 137 ? 0.2174 0.1246 0.3344 -0.0244 -0.0026 0.0151  137 ILE   B CG2 
6113 C CD1 . ILE   B 137 ? 0.2584 0.1734 0.4064 0.0190  0.0049  0.0036  137 ILE   B CD1 
6125 N N   . HIS   B 138 ? 0.1817 0.1256 0.2432 -0.0024 0.0162  0.0187  138 HIS   B N   
6126 C CA  . HIS   B 138 ? 0.1882 0.1364 0.2372 0.0001  0.0305  0.0188  138 HIS   B CA  
6127 C C   . HIS   B 138 ? 0.1774 0.1230 0.2304 -0.0062 0.0293  0.0180  138 HIS   B C   
6128 O O   . HIS   B 138 ? 0.1678 0.1358 0.2546 -0.0006 0.0293  0.0221  138 HIS   B O   
6129 C CB  . HIS   B 138 ? 0.2097 0.1565 0.2595 -0.0063 0.0416  0.0208  138 HIS   B CB  
6130 C CG  . HIS   B 138 ? 0.2263 0.1772 0.2629 -0.0129 0.0589  0.0369  138 HIS   B CG  
6131 N ND1 . HIS   B 138 ? 0.2353 0.1933 0.2992 -0.0102 0.0706  0.0270  138 HIS   B ND1 
6132 C CD2 . HIS   B 138 ? 0.2384 0.1880 0.2543 -0.0114 0.0675  0.0308  138 HIS   B CD2 
6133 C CE1 . HIS   B 138 ? 0.2379 0.1890 0.2917 -0.0134 0.0757  0.0265  138 HIS   B CE1 
6134 N NE2 . HIS   B 138 ? 0.2434 0.1811 0.2669 -0.0050 0.0735  0.0240  138 HIS   B NE2 
6142 N N   . SER   B 139 ? 0.1786 0.1137 0.2289 0.0025  0.0237  0.0090  139 SER   B N   
6143 C CA  . SER   B 139 ? 0.1617 0.1168 0.2095 0.0000  0.0245  -0.0005 139 SER   B CA  
6144 C C   . SER   B 139 ? 0.1470 0.1169 0.2111 0.0040  0.0204  0.0058  139 SER   B C   
6145 O O   . SER   B 139 ? 0.1480 0.1159 0.2089 0.0063  0.0092  0.0081  139 SER   B O   
6146 C CB  . SER   B 139 ? 0.1698 0.1205 0.2174 -0.0014 0.0018  -0.0022 139 SER   B CB  
6147 O OG  . SER   B 139 ? 0.1719 0.1191 0.2231 -0.0023 -0.0153 0.0156  139 SER   B OG  
6153 N N   . LEU   B 140 ? 0.1372 0.1086 0.1992 -0.0002 0.0176  0.0065  140 LEU   B N   
6154 C CA  . LEU   B 140 ? 0.1352 0.1116 0.2007 -0.0020 0.0104  0.0058  140 LEU   B CA  
6155 C C   . LEU   B 140 ? 0.1274 0.1151 0.2137 0.0005  0.0022  -0.0058 140 LEU   B C   
6156 O O   . LEU   B 140 ? 0.1337 0.1239 0.2136 -0.0001 -0.0011 0.0031  140 LEU   B O   
6157 C CB  . LEU   B 140 ? 0.1304 0.1176 0.2120 -0.0086 0.0136  -0.0064 140 LEU   B CB  
6158 C CG  . LEU   B 140 ? 0.1425 0.1196 0.2086 -0.0131 -0.0005 0.0028  140 LEU   B CG  
6159 C CD1 . LEU   B 140 ? 0.1531 0.1241 0.2252 -0.0143 0.0103  0.0044  140 LEU   B CD1 
6160 C CD2 . LEU   B 140 ? 0.1658 0.1355 0.2162 -0.0103 -0.0029 0.0021  140 LEU   B CD2 
6172 N N   . ARG   B 141 ? 0.1283 0.1159 0.2250 -0.0118 0.0064  -0.0030 141 ARG   B N   
6173 C CA  . ARG   B 141 ? 0.1331 0.1162 0.2658 -0.0155 0.0202  -0.0057 141 ARG   B CA  
6174 C C   . ARG   B 141 ? 0.1243 0.1099 0.2499 -0.0144 0.0088  -0.0021 141 ARG   B C   
6175 O O   . ARG   B 141 ? 0.1327 0.1211 0.2500 -0.0108 -0.0027 -0.0108 141 ARG   B O   
6176 C CB  . ARG   B 141 ? 0.1477 0.1295 0.3000 -0.0165 0.0374  -0.0024 141 ARG   B CB  
6177 C CG  . ARG   B 141 ? 0.1854 0.1536 0.3206 -0.0130 0.0339  -0.0005 141 ARG   B CG  
6178 C CD  . ARG   B 141 ? 0.2233 0.1776 0.3214 -0.0091 0.0191  -0.0145 141 ARG   B CD  
6179 N NE  . ARG   B 141 ? 0.2436 0.1807 0.3233 -0.0296 0.0142  -0.0180 141 ARG   B NE  
6180 C CZ  . ARG   B 141 ? 0.2486 0.1707 0.3016 -0.0262 0.0231  -0.0250 141 ARG   B CZ  
6181 N NH1 . ARG   B 141 ? 0.2616 0.1631 0.2868 -0.0242 0.0174  -0.0151 141 ARG   B NH1 
6182 N NH2 . ARG   B 141 ? 0.2559 0.1802 0.3153 -0.0172 0.0129  -0.0209 141 ARG   B NH2 
6196 N N   . VAL   B 142 ? 0.1299 0.1137 0.2382 -0.0028 0.0121  -0.0039 142 VAL   B N   
6197 C CA  . VAL   B 142 ? 0.1233 0.1171 0.2338 -0.0047 0.0218  -0.0054 142 VAL   B CA  
6198 C C   . VAL   B 142 ? 0.1211 0.1165 0.2323 -0.0059 0.0098  -0.0051 142 VAL   B C   
6199 O O   . VAL   B 142 ? 0.1266 0.1160 0.2435 -0.0025 0.0070  -0.0023 142 VAL   B O   
6200 C CB  . VAL   B 142 ? 0.1359 0.1321 0.2361 0.0024  0.0161  0.0067  142 VAL   B CB  
6201 C CG1 . VAL   B 142 ? 0.1442 0.1267 0.2479 0.0097  0.0174  0.0017  142 VAL   B CG1 
6202 C CG2 . VAL   B 142 ? 0.1525 0.1438 0.2326 0.0030  0.0175  0.0093  142 VAL   B CG2 
6212 N N   . CYS   B 143 ? 0.1250 0.1194 0.2161 -0.0028 0.0034  0.0111  143 CYS   B N   
6213 C CA  . CYS   B 143 ? 0.1229 0.1180 0.2185 -0.0058 -0.0050 0.0011  143 CYS   B CA  
6214 C C   . CYS   B 143 ? 0.1191 0.1173 0.2191 -0.0052 0.0079  -0.0062 143 CYS   B C   
6215 O O   . CYS   B 143 ? 0.1301 0.1214 0.2123 -0.0018 0.0010  -0.0033 143 CYS   B O   
6216 C CB  . CYS   B 143 ? 0.1276 0.1242 0.2128 -0.0042 0.0038  -0.0011 143 CYS   B CB  
6217 S SG  . CYS   B 143 ? 0.1331 0.1376 0.2037 -0.0049 0.0098  0.0034  143 CYS   B SG  
6223 N N   . VAL   B 144 ? 0.1296 0.1207 0.2280 -0.0056 -0.0039 -0.0147 144 VAL   B N   
6224 C CA  . VAL   B 144 ? 0.1333 0.1243 0.2464 -0.0101 -0.0129 -0.0258 144 VAL   B CA  
6225 C C   . VAL   B 144 ? 0.1256 0.1292 0.2553 -0.0123 -0.0157 0.0000  144 VAL   B C   
6226 O O   . VAL   B 144 ? 0.1394 0.1523 0.2749 0.0064  -0.0127 0.0238  144 VAL   B O   
6227 C CB  . VAL   B 144 ? 0.1525 0.1401 0.3045 -0.0155 -0.0174 -0.0351 144 VAL   B CB  
6228 C CG1 . VAL   B 144 ? 0.1786 0.1851 0.3299 -0.0011 -0.0213 -0.0295 144 VAL   B CG1 
6229 C CG2 . VAL   B 144 ? 0.1531 0.1427 0.3003 0.0049  -0.0322 -0.0434 144 VAL   B CG2 
6239 N N   . ASP   B 145 ? 0.1322 0.1236 0.2638 -0.0055 -0.0045 -0.0164 145 ASP   B N   
6240 C CA  . ASP   B 145 ? 0.1307 0.1346 0.2726 -0.0113 0.0089  -0.0110 145 ASP   B CA  
6241 C C   . ASP   B 145 ? 0.1334 0.1254 0.2612 -0.0053 0.0115  -0.0132 145 ASP   B C   
6242 O O   . ASP   B 145 ? 0.1345 0.1378 0.3127 -0.0115 0.0145  -0.0271 145 ASP   B O   
6243 C CB  . ASP   B 145 ? 0.1341 0.1423 0.3142 -0.0161 0.0233  -0.0073 145 ASP   B CB  
6244 C CG  . ASP   B 145 ? 0.1598 0.1438 0.3508 -0.0261 0.0279  -0.0093 145 ASP   B CG  
6245 O OD1 . ASP   B 145 ? 0.1623 0.1409 0.3558 -0.0239 -0.0036 -0.0133 145 ASP   B OD1 
6246 O OD2 . ASP   B 145 ? 0.1925 0.1590 0.3941 -0.0223 0.0551  -0.0026 145 ASP   B OD2 
6251 N N   . THR   B 146 ? 0.1239 0.1165 0.2191 -0.0098 -0.0005 -0.0018 146 THR   B N   
6252 C CA  . THR   B 146 ? 0.1264 0.1245 0.1968 -0.0043 0.0087  -0.0043 146 THR   B CA  
6253 C C   . THR   B 146 ? 0.1274 0.1242 0.1973 -0.0005 0.0010  -0.0003 146 THR   B C   
6254 O O   . THR   B 146 ? 0.1271 0.1219 0.2078 0.0007  0.0009  0.0013  146 THR   B O   
6255 C CB  . THR   B 146 ? 0.1316 0.1235 0.2088 0.0008  0.0214  -0.0056 146 THR   B CB  
6256 O OG1 . THR   B 146 ? 0.1346 0.1201 0.2241 -0.0057 0.0232  0.0116  146 THR   B OG1 
6257 C CG2 . THR   B 146 ? 0.1386 0.1297 0.1921 -0.0004 0.0191  -0.0055 146 THR   B CG2 
6265 N N   . VAL   B 147 ? 0.1310 0.1223 0.1850 -0.0002 0.0124  0.0006  147 VAL   B N   
6266 C CA  . VAL   B 147 ? 0.1358 0.1133 0.1735 -0.0062 -0.0013 0.0014  147 VAL   B CA  
6267 C C   . VAL   B 147 ? 0.1290 0.1248 0.1803 -0.0158 -0.0010 -0.0023 147 VAL   B C   
6268 O O   . VAL   B 147 ? 0.1359 0.1376 0.1990 -0.0211 -0.0231 -0.0172 147 VAL   B O   
6269 C CB  . VAL   B 147 ? 0.1398 0.1271 0.1647 -0.0044 -0.0054 0.0070  147 VAL   B CB  
6270 C CG1 . VAL   B 147 ? 0.1381 0.1451 0.1546 -0.0131 -0.0079 0.0009  147 VAL   B CG1 
6271 C CG2 . VAL   B 147 ? 0.1422 0.1260 0.1758 -0.0085 0.0020  0.0009  147 VAL   B CG2 
6281 N N   . ARG   B 148 ? 0.1293 0.1236 0.1741 -0.0110 -0.0124 -0.0054 148 ARG   B N   
6282 C CA  . ARG   B 148 ? 0.1365 0.1298 0.1693 -0.0078 -0.0213 -0.0081 148 ARG   B CA  
6283 C C   . ARG   B 148 ? 0.1381 0.1326 0.1617 -0.0075 -0.0199 -0.0060 148 ARG   B C   
6284 O O   . ARG   B 148 ? 0.1592 0.1677 0.1772 -0.0240 -0.0292 -0.0050 148 ARG   B O   
6285 C CB  . ARG   B 148 ? 0.1393 0.1377 0.1826 -0.0011 -0.0233 -0.0200 148 ARG   B CB  
6286 C CG  . ARG   B 148 ? 0.1384 0.1492 0.2005 -0.0131 -0.0196 -0.0396 148 ARG   B CG  
6287 C CD  . ARG   B 148 ? 0.1498 0.1661 0.2016 0.0071  -0.0272 -0.0342 148 ARG   B CD  
6288 N NE  . ARG   B 148 ? 0.1517 0.1665 0.1996 0.0214  -0.0309 -0.0329 148 ARG   B NE  
6289 C CZ  . ARG   B 148 ? 0.1433 0.1610 0.1800 0.0104  -0.0215 -0.0219 148 ARG   B CZ  
6290 N NH1 . ARG   B 148 ? 0.1442 0.1626 0.1858 -0.0032 -0.0055 -0.0167 148 ARG   B NH1 
6291 N NH2 . ARG   B 148 ? 0.1651 0.1476 0.1650 0.0147  -0.0149 -0.0194 148 ARG   B NH2 
6305 N N   . THR   B 149 ? 0.1389 0.1257 0.1662 -0.0112 -0.0168 -0.0074 149 THR   B N   
6306 C CA  . THR   B 149 ? 0.1439 0.1322 0.1640 -0.0106 -0.0201 -0.0003 149 THR   B CA  
6307 C C   . THR   B 149 ? 0.1439 0.1298 0.1517 -0.0146 -0.0220 -0.0005 149 THR   B C   
6308 O O   . THR   B 149 ? 0.1507 0.1268 0.1723 -0.0175 -0.0117 -0.0028 149 THR   B O   
6309 C CB  . THR   B 149 ? 0.1430 0.1300 0.1662 -0.0196 -0.0223 0.0070  149 THR   B CB  
6310 O OG1 . THR   B 149 ? 0.1440 0.1394 0.1599 -0.0245 -0.0236 -0.0003 149 THR   B OG1 
6311 C CG2 . THR   B 149 ? 0.1577 0.1344 0.1781 -0.0058 -0.0141 0.0033  149 THR   B CG2 
6319 N N   . ASN   B 150 ? 0.1513 0.1348 0.1517 -0.0140 -0.0306 -0.0019 150 ASN   B N   
6320 C CA  . ASN   B 150 ? 0.1553 0.1455 0.1506 -0.0162 -0.0276 -0.0116 150 ASN   B CA  
6321 C C   . ASN   B 150 ? 0.1479 0.1312 0.1555 -0.0137 -0.0214 -0.0097 150 ASN   B C   
6322 O O   . ASN   B 150 ? 0.1493 0.1329 0.1789 -0.0231 -0.0335 -0.0027 150 ASN   B O   
6323 C CB  . ASN   B 150 ? 0.1846 0.1758 0.1558 -0.0166 -0.0413 0.0002  150 ASN   B CB  
6324 C CG  . ASN   B 150 ? 0.2144 0.2184 0.1933 -0.0167 -0.0412 0.0186  150 ASN   B CG  
6325 O OD1 . ASN   B 150 ? 0.2225 0.2399 0.2104 -0.0273 -0.0525 0.0157  150 ASN   B OD1 
6326 N ND2 . ASN   B 150 ? 0.2275 0.2324 0.2363 -0.0056 -0.0453 0.0558  150 ASN   B ND2 
6333 N N   . VAL   B 151 ? 0.1459 0.1373 0.1458 -0.0181 -0.0261 -0.0047 151 VAL   B N   
6334 C CA  . VAL   B 151 ? 0.1451 0.1417 0.1489 -0.0253 -0.0191 -0.0016 151 VAL   B CA  
6335 C C   . VAL   B 151 ? 0.1429 0.1319 0.1516 -0.0303 -0.0216 -0.0062 151 VAL   B C   
6336 O O   . VAL   B 151 ? 0.1527 0.1376 0.1721 -0.0270 -0.0192 -0.0138 151 VAL   B O   
6337 C CB  . VAL   B 151 ? 0.1664 0.1634 0.1579 -0.0080 -0.0163 -0.0030 151 VAL   B CB  
6338 C CG1 . VAL   B 151 ? 0.1724 0.1663 0.1823 -0.0218 -0.0102 -0.0075 151 VAL   B CG1 
6339 C CG2 . VAL   B 151 ? 0.1766 0.1774 0.1485 0.0030  -0.0120 0.0128  151 VAL   B CG2 
6349 N N   . TYR   B 152 ? 0.1378 0.1193 0.1464 -0.0265 -0.0142 -0.0071 152 TYR   B N   
6350 C CA  . TYR   B 152 ? 0.1419 0.1349 0.1313 -0.0273 -0.0101 -0.0110 152 TYR   B CA  
6351 C C   . TYR   B 152 ? 0.1414 0.1240 0.1242 -0.0252 -0.0084 -0.0085 152 TYR   B C   
6352 O O   . TYR   B 152 ? 0.1455 0.1327 0.1348 -0.0264 -0.0090 0.0013  152 TYR   B O   
6353 C CB  . TYR   B 152 ? 0.1482 0.1486 0.1429 -0.0230 -0.0103 -0.0029 152 TYR   B CB  
6354 C CG  . TYR   B 152 ? 0.1679 0.1602 0.1418 -0.0325 -0.0109 -0.0024 152 TYR   B CG  
6355 C CD1 . TYR   B 152 ? 0.1797 0.1677 0.1306 -0.0286 -0.0245 -0.0010 152 TYR   B CD1 
6356 C CD2 . TYR   B 152 ? 0.1898 0.1785 0.1478 -0.0387 -0.0103 -0.0019 152 TYR   B CD2 
6357 C CE1 . TYR   B 152 ? 0.1912 0.1912 0.1495 -0.0290 -0.0282 0.0158  152 TYR   B CE1 
6358 C CE2 . TYR   B 152 ? 0.1997 0.2021 0.1573 -0.0362 -0.0158 -0.0042 152 TYR   B CE2 
6359 C CZ  . TYR   B 152 ? 0.2019 0.2085 0.1396 -0.0332 -0.0391 0.0172  152 TYR   B CZ  
6360 O OH  . TYR   B 152 ? 0.2238 0.2368 0.1776 -0.0179 -0.0398 0.0233  152 TYR   B OH  
6370 N N   . LEU   B 153 ? 0.1421 0.1185 0.1451 -0.0255 -0.0099 -0.0012 153 LEU   B N   
6371 C CA  . LEU   B 153 ? 0.1469 0.1143 0.1352 -0.0193 -0.0070 -0.0059 153 LEU   B CA  
6372 C C   . LEU   B 153 ? 0.1472 0.1188 0.1462 -0.0235 -0.0023 -0.0098 153 LEU   B C   
6373 O O   . LEU   B 153 ? 0.1552 0.1385 0.1586 -0.0170 0.0006  -0.0319 153 LEU   B O   
6374 C CB  . LEU   B 153 ? 0.1448 0.1161 0.1483 -0.0216 -0.0033 -0.0079 153 LEU   B CB  
6375 C CG  . LEU   B 153 ? 0.1411 0.1289 0.1744 -0.0245 -0.0036 -0.0027 153 LEU   B CG  
6376 C CD1 . LEU   B 153 ? 0.1489 0.1486 0.1792 -0.0273 -0.0008 0.0003  153 LEU   B CD1 
6377 C CD2 . LEU   B 153 ? 0.1511 0.1408 0.1882 -0.0266 0.0035  0.0043  153 LEU   B CD2 
6389 N N   . ALA   B 154 ? 0.1399 0.1215 0.1609 -0.0082 -0.0105 -0.0124 154 ALA   B N   
6390 C CA  . ALA   B 154 ? 0.1536 0.1304 0.1781 0.0018  -0.0131 -0.0237 154 ALA   B CA  
6391 C C   . ALA   B 154 ? 0.1624 0.1344 0.1769 0.0121  -0.0218 -0.0267 154 ALA   B C   
6392 O O   . ALA   B 154 ? 0.1975 0.1382 0.1918 0.0074  -0.0088 -0.0120 154 ALA   B O   
6393 C CB  . ALA   B 154 ? 0.1528 0.1408 0.2101 0.0040  -0.0153 -0.0280 154 ALA   B CB  
6399 N N   . VAL   B 155 ? 0.1375 0.1281 0.1852 0.0030  -0.0040 -0.0083 155 VAL   B N   
6400 C CA  . VAL   B 155 ? 0.1309 0.1291 0.1995 0.0041  -0.0167 -0.0060 155 VAL   B CA  
6401 C C   . VAL   B 155 ? 0.1311 0.1231 0.1941 -0.0020 -0.0106 -0.0116 155 VAL   B C   
6402 O O   . VAL   B 155 ? 0.1432 0.1410 0.2282 0.0010  -0.0063 -0.0352 155 VAL   B O   
6403 C CB  . VAL   B 155 ? 0.1360 0.1461 0.2306 -0.0056 -0.0228 0.0131  155 VAL   B CB  
6404 C CG1 . VAL   B 155 ? 0.1406 0.1393 0.2303 -0.0092 -0.0147 0.0042  155 VAL   B CG1 
6405 C CG2 . VAL   B 155 ? 0.1332 0.1544 0.2675 -0.0110 -0.0140 0.0301  155 VAL   B CG2 
6415 N N   . PHE   B 156 ? 0.1212 0.1347 0.2198 0.0033  -0.0061 -0.0161 156 PHE   B N   
6416 C CA  . PHE   B 156 ? 0.1274 0.1377 0.2550 0.0067  -0.0043 -0.0125 156 PHE   B CA  
6417 C C   . PHE   B 156 ? 0.1191 0.1483 0.2821 0.0113  -0.0075 -0.0331 156 PHE   B C   
6418 O O   . PHE   B 156 ? 0.1451 0.1632 0.3187 0.0230  0.0023  -0.0414 156 PHE   B O   
6419 C CB  . PHE   B 156 ? 0.1409 0.1356 0.2512 -0.0024 -0.0213 -0.0062 156 PHE   B CB  
6420 C CG  . PHE   B 156 ? 0.1340 0.1492 0.2611 -0.0033 -0.0168 0.0120  156 PHE   B CG  
6421 C CD1 . PHE   B 156 ? 0.1382 0.1722 0.3008 0.0004  -0.0074 0.0467  156 PHE   B CD1 
6422 C CD2 . PHE   B 156 ? 0.1399 0.1621 0.2553 0.0046  -0.0187 0.0114  156 PHE   B CD2 
6423 C CE1 . PHE   B 156 ? 0.1415 0.1883 0.3226 0.0034  -0.0063 0.0476  156 PHE   B CE1 
6424 C CE2 . PHE   B 156 ? 0.1468 0.1810 0.2836 0.0133  -0.0171 0.0145  156 PHE   B CE2 
6425 C CZ  . PHE   B 156 ? 0.1427 0.1884 0.3130 0.0141  -0.0175 0.0272  156 PHE   B CZ  
6435 N N   . ASP   B 157 ? 0.1309 0.1376 0.3026 0.0125  -0.0151 -0.0096 157 ASP   B N   
6436 C CA  . ASP   B 157 ? 0.1388 0.1411 0.3325 0.0117  -0.0228 -0.0187 157 ASP   B CA  
6437 C C   . ASP   B 157 ? 0.1386 0.1398 0.3383 0.0135  -0.0202 -0.0383 157 ASP   B C   
6438 O O   . ASP   B 157 ? 0.1375 0.1406 0.3190 0.0097  -0.0169 -0.0361 157 ASP   B O   
6439 C CB  . ASP   B 157 ? 0.1702 0.1621 0.3481 -0.0014 -0.0434 -0.0058 157 ASP   B CB  
6440 C CG  . ASP   B 157 ? 0.2049 0.1775 0.3784 -0.0044 -0.0284 -0.0092 157 ASP   B CG  
6441 O OD1 . ASP   B 157 ? 0.2140 0.1661 0.3955 0.0092  -0.0214 -0.0071 157 ASP   B OD1 
6442 O OD2 . ASP   B 157 ? 0.2323 0.1981 0.4054 -0.0122 -0.0091 -0.0087 157 ASP   B OD2 
6447 N N   . LYS   B 158 ? 0.1406 0.1654 0.3579 0.0086  -0.0091 -0.0684 158 LYS   B N   
6448 C CA  . LYS   B 158 ? 0.1627 0.1814 0.3640 0.0060  -0.0002 -0.0893 158 LYS   B CA  
6449 C C   . LYS   B 158 ? 0.1606 0.1661 0.3654 0.0101  0.0007  -0.0834 158 LYS   B C   
6450 O O   . LYS   B 158 ? 0.1581 0.1639 0.3632 -0.0031 0.0057  -0.0838 158 LYS   B O   
6451 C CB  . LYS   B 158 ? 0.1899 0.2187 0.3720 0.0060  0.0131  -0.1081 158 LYS   B CB  
6452 C CG  . LYS   B 158 ? 0.2235 0.2545 0.3831 0.0061  0.0200  -0.1114 158 LYS   B CG  
6453 C CD  . LYS   B 158 ? 0.2497 0.2995 0.3990 0.0019  0.0252  -0.1029 158 LYS   B CD  
6454 C CE  . LYS   B 158 ? 0.2699 0.3297 0.4098 0.0090  0.0303  -0.1050 158 LYS   B CE  
6455 N NZ  . LYS   B 158 ? 0.2710 0.3364 0.4015 0.0078  0.0340  -0.1106 158 LYS   B NZ  
6469 N N   . ASN   B 159 ? 0.1602 0.1549 0.3906 0.0113  -0.0142 -0.0656 159 ASN   B N   
6470 C CA  . ASN   B 159 ? 0.1730 0.1493 0.4121 0.0175  -0.0282 -0.0502 159 ASN   B CA  
6471 C C   . ASN   B 159 ? 0.1595 0.1366 0.3868 0.0184  -0.0427 -0.0378 159 ASN   B C   
6472 O O   . ASN   B 159 ? 0.1580 0.1327 0.3945 0.0056  -0.0478 -0.0294 159 ASN   B O   
6473 C CB  . ASN   B 159 ? 0.1950 0.1666 0.4564 0.0246  -0.0278 -0.0429 159 ASN   B CB  
6474 C CG  . ASN   B 159 ? 0.2195 0.1873 0.4921 0.0275  -0.0407 -0.0547 159 ASN   B CG  
6475 O OD1 . ASN   B 159 ? 0.2366 0.1949 0.4937 0.0350  -0.0398 -0.0720 159 ASN   B OD1 
6476 N ND2 . ASN   B 159 ? 0.2190 0.1969 0.5073 0.0312  -0.0501 -0.0448 159 ASN   B ND2 
6483 N N   . LEU   B 160 ? 0.1507 0.1347 0.3540 0.0092  -0.0396 -0.0321 160 LEU   B N   
6484 C CA  . LEU   B 160 ? 0.1510 0.1372 0.3187 0.0080  -0.0313 -0.0258 160 LEU   B CA  
6485 C C   . LEU   B 160 ? 0.1476 0.1292 0.3012 0.0010  -0.0205 -0.0272 160 LEU   B C   
6486 O O   . LEU   B 160 ? 0.1388 0.1307 0.2854 -0.0035 -0.0296 -0.0255 160 LEU   B O   
6487 C CB  . LEU   B 160 ? 0.1433 0.1472 0.2997 0.0057  -0.0346 -0.0091 160 LEU   B CB  
6488 C CG  . LEU   B 160 ? 0.1442 0.1652 0.2804 0.0116  -0.0303 -0.0082 160 LEU   B CG  
6489 C CD1 . LEU   B 160 ? 0.1633 0.1853 0.2833 -0.0022 -0.0253 -0.0054 160 LEU   B CD1 
6490 C CD2 . LEU   B 160 ? 0.1385 0.1709 0.2671 0.0231  -0.0297 -0.0097 160 LEU   B CD2 
6502 N N   . TYR   B 161 ? 0.1375 0.1339 0.3138 -0.0075 -0.0025 -0.0353 161 TYR   B N   
6503 C CA  . TYR   B 161 ? 0.1427 0.1312 0.3015 -0.0162 0.0092  -0.0397 161 TYR   B CA  
6504 C C   . TYR   B 161 ? 0.1533 0.1369 0.2931 -0.0069 0.0205  -0.0399 161 TYR   B C   
6505 O O   . TYR   B 161 ? 0.1611 0.1325 0.2784 -0.0158 0.0048  -0.0370 161 TYR   B O   
6506 C CB  . TYR   B 161 ? 0.1569 0.1425 0.3025 -0.0181 0.0307  -0.0423 161 TYR   B CB  
6507 C CG  . TYR   B 161 ? 0.1820 0.1533 0.2874 -0.0203 0.0376  -0.0533 161 TYR   B CG  
6508 C CD1 . TYR   B 161 ? 0.1870 0.1485 0.2849 -0.0311 0.0421  -0.0534 161 TYR   B CD1 
6509 C CD2 . TYR   B 161 ? 0.2052 0.1627 0.2834 -0.0158 0.0299  -0.0530 161 TYR   B CD2 
6510 C CE1 . TYR   B 161 ? 0.2087 0.1677 0.2957 -0.0323 0.0354  -0.0530 161 TYR   B CE1 
6511 C CE2 . TYR   B 161 ? 0.2256 0.1765 0.2930 -0.0239 0.0295  -0.0453 161 TYR   B CE2 
6512 C CZ  . TYR   B 161 ? 0.2237 0.1752 0.2939 -0.0381 0.0247  -0.0404 161 TYR   B CZ  
6513 O OH  . TYR   B 161 ? 0.2573 0.1940 0.3154 -0.0432 0.0262  -0.0370 161 TYR   B OH  
6523 N N   . ASP   B 162 ? 0.1514 0.1395 0.3032 -0.0067 0.0047  -0.0544 162 ASP   B N   
6524 C CA  . ASP   B 162 ? 0.1635 0.1492 0.3078 -0.0046 -0.0013 -0.0519 162 ASP   B CA  
6525 C C   . ASP   B 162 ? 0.1610 0.1305 0.3025 -0.0110 -0.0116 -0.0428 162 ASP   B C   
6526 O O   . ASP   B 162 ? 0.1657 0.1359 0.3009 -0.0129 -0.0217 -0.0320 162 ASP   B O   
6527 C CB  . ASP   B 162 ? 0.1794 0.1693 0.3306 0.0036  -0.0158 -0.0791 162 ASP   B CB  
6528 C CG  . ASP   B 162 ? 0.1875 0.1963 0.3638 0.0122  -0.0067 -0.0881 162 ASP   B CG  
6529 O OD1 . ASP   B 162 ? 0.1865 0.2080 0.3514 0.0044  0.0065  -0.0935 162 ASP   B OD1 
6530 O OD2 . ASP   B 162 ? 0.2018 0.2131 0.3955 0.0250  0.0041  -0.0856 162 ASP   B OD2 
6535 N N   A LYS   B 163 ? 0.1608 0.1207 0.2970 -0.0122 -0.0265 -0.0263 163 LYS   B N   
6536 N N   B LYS   B 163 ? 0.1632 0.1329 0.2965 -0.0113 -0.0204 -0.0261 163 LYS   B N   
6537 C CA  A LYS   B 163 ? 0.1648 0.1308 0.2913 -0.0111 -0.0254 -0.0064 163 LYS   B CA  
6538 C CA  B LYS   B 163 ? 0.1687 0.1465 0.2920 -0.0112 -0.0196 -0.0095 163 LYS   B CA  
6539 C C   A LYS   B 163 ? 0.1412 0.1231 0.2684 -0.0204 -0.0238 -0.0032 163 LYS   B C   
6540 C C   B LYS   B 163 ? 0.1454 0.1335 0.2718 -0.0161 -0.0197 -0.0052 163 LYS   B C   
6541 O O   A LYS   B 163 ? 0.1471 0.1259 0.2890 -0.0267 -0.0280 -0.0059 163 LYS   B O   
6542 O O   B LYS   B 163 ? 0.1495 0.1354 0.2880 -0.0179 -0.0215 -0.0031 163 LYS   B O   
6543 C CB  A LYS   B 163 ? 0.1920 0.1617 0.3233 -0.0041 -0.0357 0.0064  163 LYS   B CB  
6544 C CB  B LYS   B 163 ? 0.1963 0.1786 0.3183 -0.0082 -0.0254 0.0007  163 LYS   B CB  
6545 C CG  A LYS   B 163 ? 0.2388 0.2136 0.3686 -0.0044 -0.0303 0.0135  163 LYS   B CG  
6546 C CG  B LYS   B 163 ? 0.2281 0.2151 0.3531 -0.0073 -0.0235 0.0073  163 LYS   B CG  
6547 C CD  A LYS   B 163 ? 0.2836 0.2579 0.4120 -0.0096 -0.0222 0.0098  163 LYS   B CD  
6548 C CD  B LYS   B 163 ? 0.2607 0.2508 0.3890 -0.0089 -0.0192 0.0075  163 LYS   B CD  
6549 C CE  A LYS   B 163 ? 0.3112 0.2891 0.4342 -0.0132 -0.0149 0.0103  163 LYS   B CE  
6550 C CE  B LYS   B 163 ? 0.2899 0.2820 0.4115 -0.0117 -0.0143 0.0097  163 LYS   B CE  
6551 N NZ  A LYS   B 163 ? 0.3259 0.2997 0.4534 -0.0157 -0.0108 0.0063  163 LYS   B NZ  
6552 N NZ  B LYS   B 163 ? 0.2906 0.2825 0.4287 -0.0128 -0.0126 0.0097  163 LYS   B NZ  
6579 N N   . LEU   B 164 ? 0.1270 0.1261 0.2532 -0.0152 -0.0170 -0.0095 164 LEU   B N   
6580 C CA  . LEU   B 164 ? 0.1374 0.1264 0.2339 -0.0109 -0.0209 -0.0123 164 LEU   B CA  
6581 C C   . LEU   B 164 ? 0.1448 0.1268 0.2371 -0.0141 -0.0310 -0.0064 164 LEU   B C   
6582 O O   . LEU   B 164 ? 0.1464 0.1449 0.2644 -0.0143 -0.0339 -0.0084 164 LEU   B O   
6583 C CB  . LEU   B 164 ? 0.1282 0.1292 0.2261 -0.0123 -0.0176 -0.0128 164 LEU   B CB  
6584 C CG  . LEU   B 164 ? 0.1426 0.1424 0.2390 -0.0114 -0.0043 -0.0111 164 LEU   B CG  
6585 C CD1 . LEU   B 164 ? 0.1460 0.1372 0.2374 -0.0159 -0.0147 -0.0183 164 LEU   B CD1 
6586 C CD2 . LEU   B 164 ? 0.1604 0.1782 0.2519 -0.0138 0.0078  -0.0196 164 LEU   B CD2 
6599 N N   . VAL   B 165 ? 0.1712 0.1343 0.2586 -0.0186 -0.0387 -0.0188 165 VAL   B N   
6600 C CA  . VAL   B 165 ? 0.2053 0.1463 0.2697 -0.0313 -0.0511 -0.0137 165 VAL   B CA  
6601 C C   . VAL   B 165 ? 0.2261 0.1575 0.2988 -0.0384 -0.0713 -0.0138 165 VAL   B C   
6602 O O   . VAL   B 165 ? 0.2412 0.1771 0.3063 -0.0408 -0.0782 -0.0019 165 VAL   B O   
6603 C CB  . VAL   B 165 ? 0.2242 0.1669 0.2741 -0.0140 -0.0311 -0.0223 165 VAL   B CB  
6604 C CG1 . VAL   B 165 ? 0.2420 0.1769 0.3084 -0.0186 -0.0181 -0.0276 165 VAL   B CG1 
6605 C CG2 . VAL   B 165 ? 0.2207 0.1720 0.2715 -0.0101 -0.0269 -0.0175 165 VAL   B CG2 
6615 N N   . SER   B 166 ? 0.2327 0.1519 0.3321 -0.0313 -0.0790 -0.0331 166 SER   B N   
6616 C CA  . SER   B 166 ? 0.2262 0.1485 0.3755 -0.0303 -0.0718 -0.0388 166 SER   B CA  
6617 C C   . SER   B 166 ? 0.2126 0.1529 0.3920 -0.0355 -0.0662 -0.0129 166 SER   B C   
6618 O O   . SER   B 166 ? 0.2154 0.1824 0.4273 -0.0559 -0.0780 -0.0286 166 SER   B O   
6619 C CB  . SER   B 166 ? 0.2251 0.1666 0.3942 -0.0210 -0.0654 -0.0428 166 SER   B CB  
6620 O OG  . SER   B 166 ? 0.2082 0.1622 0.4053 -0.0169 -0.0674 -0.0216 166 SER   B OG  
6626 N N   . SER   B 167 ? 0.1954 0.1589 0.3594 -0.0364 -0.0709 0.0324  167 SER   B N   
6627 C CA  . SER   B 167 ? 0.1838 0.1655 0.3311 -0.0334 -0.0601 0.0360  167 SER   B CA  
6628 C C   . SER   B 167 ? 0.1784 0.1753 0.3167 -0.0473 -0.0504 0.0562  167 SER   B C   
6629 O O   . SER   B 167 ? 0.1842 0.1878 0.3127 -0.0538 -0.0458 0.0541  167 SER   B O   
6630 C CB  . SER   B 167 ? 0.1760 0.1700 0.3260 -0.0334 -0.0295 0.0339  167 SER   B CB  
6631 O OG  . SER   B 167 ? 0.1720 0.1806 0.3047 -0.0195 -0.0108 0.0313  167 SER   B OG  
6637 N N   . PHE   B 168 ? 0.1715 0.1761 0.3196 -0.0427 -0.0343 0.0569  168 PHE   B N   
6638 C CA  . PHE   B 168 ? 0.1847 0.1638 0.2901 -0.0447 -0.0295 0.0305  168 PHE   B CA  
6639 C C   . PHE   B 168 ? 0.1669 0.1495 0.2320 -0.0253 -0.0050 0.0130  168 PHE   B C   
6640 O O   . PHE   B 168 ? 0.1937 0.1464 0.2342 -0.0002 -0.0037 -0.0072 168 PHE   B O   
6641 C CB  . PHE   B 168 ? 0.2053 0.1660 0.3022 -0.0524 -0.0397 0.0397  168 PHE   B CB  
6642 C CG  . PHE   B 168 ? 0.2242 0.1490 0.2842 -0.0488 -0.0423 0.0221  168 PHE   B CG  
6643 C CD1 . PHE   B 168 ? 0.2532 0.1598 0.2971 -0.0411 -0.0492 0.0203  168 PHE   B CD1 
6644 C CD2 . PHE   B 168 ? 0.2122 0.1515 0.2872 -0.0388 -0.0406 0.0183  168 PHE   B CD2 
6645 C CE1 . PHE   B 168 ? 0.2654 0.1678 0.2963 -0.0310 -0.0431 0.0220  168 PHE   B CE1 
6646 C CE2 . PHE   B 168 ? 0.2394 0.1574 0.2873 -0.0267 -0.0509 0.0159  168 PHE   B CE2 
6647 C CZ  . PHE   B 168 ? 0.2565 0.1563 0.2899 -0.0135 -0.0528 0.0248  168 PHE   B CZ  
6657 N N   . LEU   B 169 ? 0.1751 0.1684 0.2263 -0.0046 0.0038  -0.0046 169 LEU   B N   
6658 C CA  . LEU   B 169 ? 0.1977 0.1996 0.2673 -0.0099 -0.0005 -0.0317 169 LEU   B CA  
6659 C C   . LEU   B 169 ? 0.2236 0.2228 0.3227 0.0058  -0.0086 -0.0520 169 LEU   B C   
6660 O O   . LEU   B 169 ? 0.2411 0.2475 0.3815 0.0012  -0.0073 -0.0667 169 LEU   B O   
6661 C CB  . LEU   B 169 ? 0.2180 0.2423 0.2885 -0.0205 -0.0016 -0.0075 169 LEU   B CB  
6662 C CG  . LEU   B 169 ? 0.2613 0.2783 0.3400 -0.0102 0.0035  -0.0011 169 LEU   B CG  
6663 C CD1 . LEU   B 169 ? 0.2750 0.2991 0.3502 -0.0122 -0.0005 0.0144  169 LEU   B CD1 
6664 C CD2 . LEU   B 169 ? 0.2590 0.2857 0.3442 0.0018  0.0270  -0.0163 169 LEU   B CD2 
6665 O OXT . LEU   B 169 ? 0.2405 0.2395 0.3225 0.0340  -0.0029 -0.0384 169 LEU   B OXT 
6677 C C1  T TFA   C .   ? 0.1442 0.1751 0.1134 0.0023  0.0257  0.0135  201 TFA   A C1  
6678 C C2  T TFA   C .   ? 0.1666 0.1928 0.1571 -0.0032 0.0242  0.0017  201 TFA   A C2  
6679 O O   T TFA   C .   ? 0.1227 0.1599 0.0927 0.0032  0.0136  0.0323  201 TFA   A O   
6680 F F1  T TFA   C .   ? 0.1807 0.2010 0.1866 -0.0005 0.0177  -0.0094 201 TFA   A F1  
6681 F F2  T TFA   C .   ? 0.1759 0.1937 0.1559 -0.0011 0.0283  0.0131  201 TFA   A F2  
6682 F F3  T TFA   C .   ? 0.1731 0.2035 0.1772 -0.0131 0.0279  -0.0110 201 TFA   A F3  
6683 O OXT T TFA   C .   ? 0.1434 0.1721 0.1220 0.0181  0.0291  0.0118  201 TFA   A OXT 
6684 N N2  B A1A9S D .   ? 0.1267 0.1398 0.1151 -0.0142 -0.0027 0.0016  202 A1A9S A N2  
6685 C C3  B A1A9S D .   ? 0.1760 0.1942 0.1446 -0.0133 -0.0006 -0.0243 202 A1A9S A C3  
6686 C C6  B A1A9S D .   ? 0.1706 0.1909 0.1449 0.0040  -0.0044 -0.0011 202 A1A9S A C6  
6687 C C9  B A1A9S D .   ? 0.1422 0.1576 0.1256 -0.0166 -0.0042 0.0100  202 A1A9S A C9  
6688 C C12 B A1A9S D .   ? 0.1251 0.1478 0.1096 -0.0055 -0.0068 0.0081  202 A1A9S A C12 
6689 C C14 B A1A9S D .   ? 0.1392 0.1358 0.1167 -0.0091 -0.0069 0.0078  202 A1A9S A C14 
6690 C C1  B A1A9S D .   ? 0.1722 0.2020 0.1558 -0.0156 -0.0107 -0.0109 202 A1A9S A C1  
6691 C C10 B A1A9S D .   ? 0.1355 0.1702 0.1366 -0.0076 0.0060  0.0167  202 A1A9S A C10 
6692 C C11 B A1A9S D .   ? 0.1293 0.1356 0.1075 -0.0141 -0.0022 0.0122  202 A1A9S A C11 
6693 C C13 B A1A9S D .   ? 0.1318 0.1369 0.1174 -0.0037 -0.0095 0.0108  202 A1A9S A C13 
6694 C C15 B A1A9S D .   ? 0.1557 0.1377 0.1335 -0.0166 -0.0187 0.0022  202 A1A9S A C15 
6695 C C16 B A1A9S D .   ? 0.1448 0.1312 0.1320 -0.0086 -0.0194 0.0094  202 A1A9S A C16 
6696 C C2  B A1A9S D .   ? 0.1712 0.1934 0.1542 -0.0124 -0.0095 -0.0069 202 A1A9S A C2  
6697 C C4  B A1A9S D .   ? 0.1756 0.1924 0.1465 -0.0047 0.0005  -0.0158 202 A1A9S A C4  
6698 C C5  B A1A9S D .   ? 0.1823 0.1974 0.1700 0.0053  0.0046  -0.0011 202 A1A9S A C5  
6699 C C7  B A1A9S D .   ? 0.1633 0.1859 0.1421 -0.0110 -0.0038 0.0006  202 A1A9S A C7  
6700 C C8  B A1A9S D .   ? 0.1475 0.1694 0.1309 -0.0179 -0.0012 0.0048  202 A1A9S A C8  
6701 N N1  B A1A9S D .   ? 0.1415 0.1369 0.1149 -0.0130 0.0002  0.0208  202 A1A9S A N1  
6702 N N3  B A1A9S D .   ? 0.1322 0.1475 0.1123 -0.0083 0.0057  0.0130  202 A1A9S A N3  
6703 N N4  B A1A9S D .   ? 0.1300 0.1254 0.1225 -0.0110 -0.0221 0.0261  202 A1A9S A N4  
6704 O O1  B A1A9S D .   ? 0.1352 0.1712 0.1685 0.0004  0.0170  0.0314  202 A1A9S A O1  
6723 O O   . HOH   E .   ? 0.4009 0.7384 0.5295 -0.1207 0.0352  0.1150  301 HOH   A O   
6724 O O   A HOH   E .   ? 0.2030 0.1317 0.3573 0.0250  -0.0112 0.0194  302 HOH   A O   
6725 O O   . HOH   E .   ? 0.2495 0.3613 0.4300 0.0116  -0.0953 0.0274  303 HOH   A O   
6726 O O   . HOH   E .   ? 0.5644 0.3587 0.4644 -0.1077 0.1305  0.0655  304 HOH   A O   
6727 O O   A HOH   E .   ? 0.2457 0.4073 0.4905 0.0686  0.0058  -0.0163 305 HOH   A O   
6728 O O   . HOH   E .   ? 0.5970 0.4706 0.3209 0.2077  -0.1221 0.0636  306 HOH   A O   
6729 O O   . HOH   E .   ? 0.2454 0.3422 0.1444 -0.0325 0.0202  0.0417  307 HOH   A O   
6730 O O   B HOH   E .   ? 0.2043 0.3082 0.3576 0.0695  -0.0673 0.1156  308 HOH   A O   
6731 O O   B HOH   E .   ? 0.1406 0.0967 0.2081 0.0244  -0.0037 0.0048  309 HOH   A O   
6732 O O   . HOH   E .   ? 0.4444 0.3293 0.3684 -0.0153 0.0945  0.0032  310 HOH   A O   
6733 O O   . HOH   E .   ? 0.1792 0.1798 0.1675 -0.0070 -0.0144 0.0445  311 HOH   A O   
6734 O O   . HOH   E .   ? 0.4154 0.4974 0.5109 0.1143  0.1276  -0.1320 312 HOH   A O   
6735 O O   . HOH   E .   ? 0.2641 0.3060 0.3015 -0.0123 -0.0369 -0.0909 313 HOH   A O   
6736 O O   . HOH   E .   ? 0.1929 0.3139 0.3315 -0.0461 0.0524  -0.0988 314 HOH   A O   
6737 O O   A HOH   E .   ? 0.3728 0.2861 0.2499 -0.0675 -0.0123 0.0330  315 HOH   A O   
6738 O O   . HOH   E .   ? 0.5663 0.5349 0.3000 0.0342  -0.0650 0.0992  316 HOH   A O   
6739 O O   . HOH   E .   ? 0.2104 0.1851 0.3704 -0.0496 0.0155  -0.0238 317 HOH   A O   
6740 O O   . HOH   E .   ? 0.2831 0.3047 0.2907 -0.0766 0.0112  -0.0430 318 HOH   A O   
6741 O O   . HOH   E .   ? 0.2991 0.2917 0.2568 -0.0794 0.0078  0.0839  319 HOH   A O   
6742 O O   . HOH   E .   ? 0.4754 0.3343 0.3743 0.0071  0.2162  0.0649  320 HOH   A O   
6743 O O   . HOH   E .   ? 0.5068 0.2639 0.2942 -0.0955 0.0801  0.0198  321 HOH   A O   
6744 O O   . HOH   E .   ? 0.4968 0.4818 0.2910 -0.1367 0.1393  0.0709  322 HOH   A O   
6745 O O   . HOH   E .   ? 0.5996 0.4834 0.6160 0.0655  -0.0090 -0.0353 323 HOH   A O   
6746 O O   . HOH   E .   ? 0.4123 0.2055 0.3731 0.0284  -0.1593 0.0041  324 HOH   A O   
6747 O O   . HOH   E .   ? 0.2227 0.1773 0.2301 -0.0004 -0.0273 0.0162  325 HOH   A O   
6748 O O   . HOH   E .   ? 0.1766 0.2613 0.2690 0.0265  -0.0101 -0.0089 326 HOH   A O   
6749 O O   . HOH   E .   ? 0.1528 0.1439 0.2096 -0.0181 0.0031  -0.0016 327 HOH   A O   
6750 O O   A HOH   E .   ? 0.1293 0.2531 0.1788 0.0405  0.0458  0.0635  328 HOH   A O   
6751 O O   . HOH   E .   ? 0.1711 0.1664 0.2128 0.0190  -0.0172 0.0246  329 HOH   A O   
6752 O O   A HOH   E .   ? 0.4550 0.3023 0.1777 -0.1067 0.0382  -0.0639 330 HOH   A O   
6753 O O   . HOH   E .   ? 0.2364 0.2271 0.2733 0.0359  0.0325  0.0328  331 HOH   A O   
6754 O O   . HOH   E .   ? 0.2992 0.3352 0.3420 0.0158  -0.0174 -0.1316 332 HOH   A O   
6755 O O   A HOH   E .   ? 0.2039 0.2861 0.1826 0.0641  -0.0127 0.0009  333 HOH   A O   
6756 O O   . HOH   E .   ? 0.2949 0.2605 0.4611 -0.0276 -0.1521 0.1164  334 HOH   A O   
6757 O O   . HOH   E .   ? 0.4977 0.2002 0.5545 0.0478  0.0883  0.0061  335 HOH   A O   
6758 O O   . HOH   E .   ? 0.4820 0.5065 0.4519 -0.0700 0.0663  0.2395  336 HOH   A O   
6759 O O   . HOH   E .   ? 0.1475 0.2164 0.1867 0.0038  -0.0096 0.0551  337 HOH   A O   
6760 O O   . HOH   E .   ? 0.1932 0.1937 0.3199 0.0150  0.0801  -0.0092 338 HOH   A O   
6761 O O   . HOH   E .   ? 0.3233 0.4114 0.3823 -0.1443 -0.0818 -0.0454 339 HOH   A O   
6762 O O   . HOH   E .   ? 0.2294 0.3953 0.3496 0.1034  -0.0741 -0.0114 340 HOH   A O   
6763 O O   . HOH   E .   ? 0.1269 0.1216 0.1112 -0.0036 0.0107  0.0032  341 HOH   A O   
6764 O O   . HOH   E .   ? 0.3096 0.4138 0.2653 -0.0002 0.0497  0.0330  342 HOH   A O   
6765 O O   A HOH   E .   ? 0.5004 0.2692 0.4626 -0.0094 -0.1294 0.0939  343 HOH   A O   
6766 O O   . HOH   E .   ? 0.6258 0.3443 0.2997 -0.0077 -0.0417 0.1045  344 HOH   A O   
6767 O O   . HOH   E .   ? 0.2717 0.3220 0.5556 -0.0487 -0.1096 -0.1096 345 HOH   A O   
6768 O O   . HOH   E .   ? 0.2289 0.5161 0.3864 0.0068  -0.0649 0.1818  346 HOH   A O   
6769 O O   . HOH   E .   ? 0.1501 0.2655 0.2247 0.0073  0.0304  0.0359  347 HOH   A O   
6770 O O   . HOH   E .   ? 0.2289 0.2520 0.2941 0.0161  -0.0304 -0.0803 348 HOH   A O   
6771 O O   . HOH   E .   ? 0.3565 0.3492 0.3161 0.1651  0.0711  0.0454  349 HOH   A O   
6772 O O   . HOH   E .   ? 0.3595 0.4822 0.3077 0.2412  -0.0034 -0.0383 350 HOH   A O   
6773 O O   . HOH   E .   ? 0.2248 0.1653 0.2377 0.0285  -0.0396 -0.0034 351 HOH   A O   
6774 O O   . HOH   E .   ? 0.5035 0.4545 0.4738 0.0858  0.2249  -0.0340 352 HOH   A O   
6775 O O   . HOH   E .   ? 0.3204 0.3848 0.2002 -0.0887 -0.0221 -0.0696 353 HOH   A O   
6776 O O   . HOH   E .   ? 0.4458 0.2754 0.4449 -0.1515 0.1677  -0.0255 354 HOH   A O   
6777 O O   B HOH   E .   ? 0.3518 0.2455 0.3671 0.0199  0.0829  -0.0226 355 HOH   A O   
6778 O O   . HOH   E .   ? 0.3361 0.7261 0.4441 -0.0461 -0.1389 0.0644  356 HOH   A O   
6779 O O   . HOH   E .   ? 0.2417 0.4437 0.2758 0.0587  0.0858  0.1725  357 HOH   A O   
6780 O O   . HOH   E .   ? 0.1458 0.1777 0.2430 0.0036  -0.0023 0.0149  358 HOH   A O   
6781 O O   . HOH   E .   ? 0.1487 0.1531 0.1772 0.0060  -0.0220 -0.0288 359 HOH   A O   
6782 O O   . HOH   E .   ? 0.5942 0.4531 0.3958 -0.1349 -0.1229 0.2208  360 HOH   A O   
6783 O O   . HOH   E .   ? 0.4726 0.6089 0.2702 0.1336  -0.0507 0.1157  361 HOH   A O   
6784 O O   . HOH   E .   ? 0.3272 0.2751 0.4594 -0.0914 -0.0615 0.0488  362 HOH   A O   
6785 O O   . HOH   E .   ? 0.3735 0.2031 0.2033 0.1039  0.0632  0.0161  363 HOH   A O   
6786 O O   . HOH   E .   ? 0.2027 0.3008 0.3093 0.0422  0.0649  -0.0874 364 HOH   A O   
6787 O O   . HOH   E .   ? 0.3478 0.5830 0.3038 0.0704  0.1066  -0.1100 365 HOH   A O   
6788 O O   . HOH   E .   ? 0.1497 0.1268 0.1885 -0.0051 0.0126  -0.0052 366 HOH   A O   
6789 O O   . HOH   E .   ? 0.3124 0.3581 0.3193 -0.1450 0.0896  -0.0169 367 HOH   A O   
6790 O O   . HOH   E .   ? 0.3370 0.7473 0.5796 -0.1070 -0.1143 0.1931  368 HOH   A O   
6791 O O   A HOH   E .   ? 0.2206 0.2483 0.3052 0.0529  0.0773  0.0837  369 HOH   A O   
6792 O O   . HOH   E .   ? 0.1346 0.1425 0.1343 -0.0044 -0.0103 -0.0053 370 HOH   A O   
6793 O O   . HOH   E .   ? 0.3057 0.5064 0.3865 0.0388  0.1252  -0.0181 371 HOH   A O   
6794 O O   . HOH   E .   ? 0.2513 0.4454 0.2944 -0.0508 0.0766  -0.0176 372 HOH   A O   
6795 O O   . HOH   E .   ? 0.3905 0.2391 0.3597 -0.1297 0.0807  0.0251  373 HOH   A O   
6796 O O   B HOH   E .   ? 0.1781 0.2353 0.2012 0.0106  0.0094  0.0213  374 HOH   A O   
6797 O O   . HOH   E .   ? 0.1871 0.1969 0.2130 -0.0380 0.0069  0.0358  375 HOH   A O   
6798 O O   . HOH   E .   ? 0.1856 0.2124 0.2108 -0.0317 -0.0473 0.0393  376 HOH   A O   
6799 O O   . HOH   E .   ? 0.1597 0.1753 0.2126 -0.0207 0.0057  0.0346  377 HOH   A O   
6800 O O   . HOH   E .   ? 0.7803 0.8154 0.7087 0.0308  -0.0208 -0.0519 378 HOH   A O   
6801 O O   . HOH   E .   ? 0.2508 0.2011 0.1634 -0.0669 0.0055  0.0266  379 HOH   A O   
6802 O O   A HOH   E .   ? 0.2284 0.2067 0.2918 0.0364  0.1164  0.1128  380 HOH   A O   
6803 O O   . HOH   E .   ? 0.1631 0.1720 0.1332 0.0033  0.0044  0.0084  381 HOH   A O   
6804 O O   . HOH   E .   ? 0.2070 0.2358 0.1902 0.0053  0.0346  0.0463  382 HOH   A O   
6805 O O   . HOH   E .   ? 0.1746 0.2722 0.2309 0.0508  0.0384  0.0757  383 HOH   A O   
6806 O O   T HOH   E .   ? 0.0955 0.1376 0.2483 -0.0236 0.0061  0.0607  384 HOH   A O   
6807 O O   B HOH   E .   ? 0.1322 0.1332 0.1518 -0.0213 -0.0067 0.0052  385 HOH   A O   
6808 O O   . HOH   E .   ? 0.2074 0.3747 0.2640 -0.0118 -0.0071 0.0534  386 HOH   A O   
6809 O O   A HOH   E .   ? 0.1726 0.1622 0.2016 -0.0147 -0.0279 0.0281  387 HOH   A O   
6810 O O   . HOH   E .   ? 0.2991 0.2638 0.1870 0.0232  0.0658  0.0038  388 HOH   A O   
6811 O O   B HOH   E .   ? 0.2407 0.2736 0.1895 -0.0550 0.0056  0.0323  389 HOH   A O   
6812 O O   . HOH   E .   ? 0.2619 0.3458 0.3352 -0.0534 0.1193  0.0086  390 HOH   A O   
6813 O O   B HOH   E .   ? 0.2481 0.2514 0.1611 0.0069  0.0527  0.0250  391 HOH   A O   
6814 O O   . HOH   E .   ? 0.1847 0.1976 0.1921 -0.0016 -0.0055 0.0428  392 HOH   A O   
6815 O O   . HOH   E .   ? 0.6115 0.5177 0.3916 -0.0900 0.0466  0.2078  393 HOH   A O   
6816 O O   . HOH   E .   ? 0.5642 0.3639 0.4356 0.1580  -0.0846 0.1303  394 HOH   A O   
6817 O O   . HOH   E .   ? 0.2428 0.3833 0.3110 -0.0353 0.0862  -0.0416 395 HOH   A O   
6818 O O   . HOH   E .   ? 0.3914 0.6325 0.5064 0.0889  -0.0218 0.1881  396 HOH   A O   
6819 O O   . HOH   E .   ? 0.3185 0.2624 0.3177 -0.0056 -0.0373 0.1061  397 HOH   A O   
6820 O O   . HOH   E .   ? 0.5197 0.5339 0.5779 -0.0495 0.0211  0.1448  398 HOH   A O   
6821 O O   A HOH   E .   ? 0.1308 0.1535 0.1686 0.0051  0.0018  -0.0154 399 HOH   A O   
6822 O O   A HOH   E .   ? 0.1876 0.1640 0.3430 -0.0078 0.0318  0.0044  400 HOH   A O   
6823 O O   . HOH   E .   ? 0.4297 0.3795 0.1698 -0.0283 0.0958  0.0520  401 HOH   A O   
6824 O O   . HOH   E .   ? 0.3985 0.6216 0.4084 -0.0422 0.0119  0.1364  402 HOH   A O   
6825 O O   . HOH   E .   ? 0.2309 0.2072 0.2310 -0.0551 -0.0105 0.0505  403 HOH   A O   
6826 O O   . HOH   E .   ? 0.1848 0.1942 0.3547 0.0470  0.1057  0.1048  404 HOH   A O   
6827 O O   . HOH   E .   ? 0.1357 0.1417 0.1742 0.0009  -0.0103 0.0059  405 HOH   A O   
6828 O O   . HOH   E .   ? 0.1861 0.2469 0.3600 -0.0174 -0.0202 0.0040  406 HOH   A O   
6829 O O   . HOH   E .   ? 0.1857 0.2236 0.2495 -0.0265 -0.0368 0.0838  407 HOH   A O   
6830 O O   . HOH   E .   ? 0.2589 0.2908 0.1857 -0.0258 -0.0386 0.0206  408 HOH   A O   
6831 O O   B HOH   E .   ? 0.5573 0.2436 0.2820 -0.0401 0.0418  0.0514  409 HOH   A O   
6832 O O   . HOH   E .   ? 0.4349 0.4493 0.3754 0.1965  -0.1122 -0.1486 410 HOH   A O   
6833 O O   B HOH   E .   ? 0.0942 0.1100 0.0889 -0.0188 0.0040  -0.0206 411 HOH   A O   
6834 O O   . HOH   E .   ? 0.6632 0.5627 0.3993 -0.1068 0.0074  0.2520  412 HOH   A O   
6835 O O   . HOH   E .   ? 0.1709 0.2055 0.2396 -0.0241 0.0584  0.0525  413 HOH   A O   
6836 O O   . HOH   E .   ? 0.5506 0.2760 0.4327 0.0478  0.0601  -0.0311 414 HOH   A O   
6837 O O   . HOH   E .   ? 0.6690 0.7155 0.4526 0.2188  -0.0421 0.0289  415 HOH   A O   
6838 O O   . HOH   E .   ? 0.2259 0.1866 0.2357 -0.0091 0.0002  0.0230  416 HOH   A O   
6839 O O   B HOH   E .   ? 0.1261 0.2292 0.3765 -0.0055 0.0247  0.1386  417 HOH   A O   
6840 O O   A HOH   E .   ? 0.4277 0.4868 0.4597 -0.0363 -0.1095 -0.0281 418 HOH   A O   
6841 O O   . HOH   E .   ? 0.2667 0.2455 0.1754 -0.0615 -0.0533 0.0152  419 HOH   A O   
6842 O O   . HOH   E .   ? 0.2082 0.1684 0.2733 0.0060  -0.0373 0.0166  420 HOH   A O   
6843 O O   . HOH   E .   ? 0.1449 0.1733 0.2616 0.0018  -0.0040 0.0136  421 HOH   A O   
6844 O O   . HOH   E .   ? 0.4831 0.6782 0.5188 0.0058  0.1098  0.1225  422 HOH   A O   
6845 O O   . HOH   E .   ? 0.1557 0.1377 0.1381 -0.0207 0.0075  -0.0024 423 HOH   A O   
6846 O O   . HOH   E .   ? 0.4608 0.3530 0.5130 -0.0190 0.1236  -0.1161 424 HOH   A O   
6847 O O   B HOH   E .   ? 0.1396 0.2544 0.2617 -0.0434 -0.0291 0.0794  425 HOH   A O   
6848 O O   . HOH   E .   ? 0.3044 0.5725 0.1619 -0.0388 0.0472  0.0151  426 HOH   A O   
6849 O O   . HOH   E .   ? 0.1871 0.2898 0.2357 -0.0188 -0.0511 0.0481  427 HOH   A O   
6850 O O   . HOH   E .   ? 0.1949 0.1550 0.1363 -0.0146 0.0174  0.0107  428 HOH   A O   
6851 O O   B HOH   E .   ? 0.4241 0.2032 0.2801 -0.0915 0.0113  -0.0240 429 HOH   A O   
6852 O O   . HOH   E .   ? 0.3362 0.2352 0.4178 -0.0588 0.1738  -0.0400 430 HOH   A O   
6853 O O   . HOH   E .   ? 0.3333 0.1208 0.1830 0.0038  -0.0419 0.0078  431 HOH   A O   
6854 O O   . HOH   E .   ? 0.3747 0.5898 0.5445 -0.0769 0.0616  -0.0120 432 HOH   A O   
6855 O O   . HOH   E .   ? 0.3429 0.3481 0.7125 -0.0001 0.1409  -0.0550 433 HOH   A O   
6856 O O   . HOH   E .   ? 0.3968 0.2330 0.5444 -0.0783 -0.2430 0.1177  434 HOH   A O   
6857 O O   . HOH   E .   ? 0.4891 0.5329 0.2942 -0.0847 -0.0142 0.0880  435 HOH   A O   
6858 O O   . HOH   E .   ? 0.2209 0.4113 0.2226 0.1460  -0.0064 0.0058  436 HOH   A O   
6859 O O   . HOH   E .   ? 0.1905 0.1812 0.2565 0.0114  -0.0438 0.0282  437 HOH   A O   
6860 O O   . HOH   E .   ? 0.5225 0.6617 0.4010 0.0654  0.2556  -0.0640 438 HOH   A O   
6861 O O   A HOH   E .   ? 0.2679 0.2595 0.1967 -0.0229 0.0541  -0.0131 439 HOH   A O   
6862 O O   B HOH   E .   ? 0.1506 0.1263 0.1197 0.0032  -0.0088 0.0042  440 HOH   A O   
6863 O O   . HOH   E .   ? 0.3157 0.3707 0.1981 -0.0221 -0.0514 0.0420  441 HOH   A O   
6864 O O   . HOH   E .   ? 0.1522 0.1811 0.2306 -0.0122 0.0075  0.0202  442 HOH   A O   
6865 O O   A HOH   E .   ? 0.1725 0.1810 0.3496 0.0157  -0.0419 -0.0695 443 HOH   A O   
6866 O O   A HOH   E .   ? 0.1776 0.1609 0.1735 0.0090  -0.0368 0.0067  444 HOH   A O   
6867 O O   . HOH   E .   ? 0.4311 0.4743 0.4168 -0.0029 -0.1185 -0.0004 445 HOH   A O   
6868 O O   . HOH   E .   ? 0.6753 0.5155 0.8166 0.0371  -0.1069 0.2180  446 HOH   A O   
6869 O O   . HOH   E .   ? 0.6189 0.6158 0.5901 -0.1065 -0.0255 -0.0566 447 HOH   A O   
6870 O O   B HOH   E .   ? 0.1743 0.2440 0.1451 -0.0625 0.0051  0.0163  448 HOH   A O   
6871 O O   . HOH   E .   ? 0.3615 0.2743 0.1533 -0.0686 0.0216  0.0620  449 HOH   A O   
6872 O O   . HOH   E .   ? 0.2407 0.1549 0.2438 0.0189  0.0102  0.0062  450 HOH   A O   
6873 O O   . HOH   E .   ? 0.2149 0.2604 0.2201 -0.0016 -0.0174 -0.0493 451 HOH   A O   
6874 O O   A HOH   E .   ? 0.3023 0.3239 0.4566 -0.0226 0.0811  -0.1103 452 HOH   A O   
6875 O O   . HOH   E .   ? 0.4987 0.4768 0.4928 -0.1245 -0.1083 -0.1426 453 HOH   A O   
6876 O O   A HOH   E .   ? 0.4869 0.1973 0.2537 -0.0114 0.0754  0.0487  454 HOH   A O   
6877 O O   B HOH   E .   ? 0.1751 0.1537 0.1240 0.0456  -0.0272 -0.0277 455 HOH   A O   
6878 O O   . HOH   E .   ? 0.4527 0.3741 0.2945 0.2421  -0.0567 -0.0432 456 HOH   A O   
6879 O O   A HOH   E .   ? 0.1721 0.1474 0.1540 -0.0062 -0.0100 -0.0194 457 HOH   A O   
6880 O O   . HOH   E .   ? 0.5871 0.6915 0.5613 0.1079  -0.1199 -0.0212 458 HOH   A O   
6881 O O   . HOH   E .   ? 0.2317 0.1948 0.2721 0.0132  0.0329  0.0302  459 HOH   A O   
6882 O O   A HOH   E .   ? 0.1895 0.1479 0.1736 0.0086  -0.0000 0.0046  460 HOH   A O   
6883 O O   . HOH   E .   ? 0.6864 0.6033 0.6596 -0.1368 -0.1261 -0.1234 461 HOH   A O   
6884 O O   . HOH   E .   ? 0.6004 0.3129 0.3840 0.0665  -0.0447 0.1156  462 HOH   A O   
6885 O O   . HOH   E .   ? 0.1897 0.2401 0.4663 -0.0222 -0.0958 0.0939  463 HOH   A O   
6886 O O   A HOH   E .   ? 0.6665 0.5075 0.4762 0.0946  0.0872  0.0936  464 HOH   A O   
6887 O O   . HOH   E .   ? 0.6161 0.5741 0.4393 -0.0895 0.0935  0.0909  465 HOH   A O   
6888 O O   B HOH   E .   ? 0.2626 0.3573 0.3601 -0.0134 0.0018  -0.0702 466 HOH   A O   
6889 O O   . HOH   E .   ? 0.5148 0.5842 0.5083 0.2059  -0.1442 0.1652  467 HOH   A O   
6890 O O   . HOH   E .   ? 0.4360 0.3490 0.5099 0.0523  0.0372  0.0641  468 HOH   A O   
6891 O O   B HOH   E .   ? 0.4287 0.2841 0.2492 -0.0912 -0.0047 -0.0015 469 HOH   A O   
6892 O O   . HOH   E .   ? 0.2616 0.2715 0.3646 -0.0365 0.0343  -0.0957 470 HOH   A O   
6893 O O   . HOH   E .   ? 0.7255 0.6778 0.4507 0.1149  -0.0463 -0.0746 471 HOH   A O   
6894 O O   . HOH   E .   ? 0.4600 0.4185 0.5262 0.1270  0.0094  0.0843  472 HOH   A O   
6895 O O   . HOH   E .   ? 0.4678 0.4425 0.4732 0.0411  -0.0368 0.1164  473 HOH   A O   
6896 O O   . HOH   E .   ? 0.3355 0.4500 0.5179 -0.1259 0.0639  -0.1963 474 HOH   A O   
6897 O O   . HOH   E .   ? 0.4333 0.5940 0.3004 -0.0991 -0.1156 0.1923  475 HOH   A O   
6898 O O   . HOH   E .   ? 0.3096 0.4751 0.5033 -0.0636 -0.0060 0.0381  476 HOH   A O   
6899 O O   . HOH   E .   ? 0.2995 0.3401 0.4252 -0.1472 0.1112  -0.1020 477 HOH   A O   
6900 O O   . HOH   E .   ? 0.3795 0.4893 0.3538 0.0107  -0.0088 -0.0668 478 HOH   A O   
6901 O O   . HOH   E .   ? 0.2788 0.4455 0.4508 0.0637  0.0120  -0.2020 479 HOH   A O   
6902 O O   . HOH   E .   ? 0.6619 0.6634 0.6423 -0.0517 0.1548  0.2243  480 HOH   A O   
6903 O O   . HOH   E .   ? 0.6153 0.3574 0.6182 0.1002  0.0073  0.1568  481 HOH   A O   
6904 O O   . HOH   E .   ? 0.5275 0.5419 0.4942 0.0771  -0.0072 -0.1042 482 HOH   A O   
6905 O O   . HOH   E .   ? 0.4644 0.5118 0.5049 0.0044  0.0975  0.0652  483 HOH   A O   
6906 O O   . HOH   E .   ? 0.3684 0.4621 0.2560 0.0100  0.0225  -0.0147 484 HOH   A O   
6907 O O   . HOH   E .   ? 0.2726 0.1668 0.2546 0.0331  -0.0883 -0.0318 485 HOH   A O   
6908 O O   . HOH   E .   ? 0.5145 0.3679 0.3850 0.0665  0.1089  0.0516  486 HOH   A O   
6909 O O   A HOH   E .   ? 0.2727 0.2607 0.5153 0.0913  -0.1244 -0.0478 487 HOH   A O   
6910 O O   B HOH   E .   ? 0.1410 0.1613 0.1214 0.0056  -0.0169 -0.0132 488 HOH   A O   
6911 O O   . HOH   E .   ? 0.4932 0.4551 0.3056 -0.0647 -0.0670 -0.0486 489 HOH   A O   
6912 O O   . HOH   E .   ? 0.4065 0.4938 0.5570 -0.2024 -0.0406 -0.0347 490 HOH   A O   
6913 O O   . HOH   E .   ? 0.2292 0.2174 0.2460 0.0180  -0.0095 -0.0141 491 HOH   A O   
6914 O O   . HOH   E .   ? 0.6446 0.5579 0.6429 -0.0798 0.0253  -0.0467 492 HOH   A O   
6915 O O   B HOH   E .   ? 0.2567 0.1262 0.3433 0.0153  0.1150  -0.0311 493 HOH   A O   
6916 O O   . HOH   E .   ? 0.4917 0.5525 0.5440 -0.1544 -0.1262 0.0102  494 HOH   A O   
6917 O O   . HOH   E .   ? 0.5986 0.4304 0.4721 -0.0024 0.0223  -0.1206 495 HOH   A O   
6918 O O   . HOH   E .   ? 0.5851 0.4901 0.4531 -0.1115 -0.0681 -0.0451 496 HOH   A O   
6919 O O   . HOH   E .   ? 0.8068 0.3900 0.3068 -0.0344 -0.1204 0.0653  497 HOH   A O   
6920 O O   . HOH   E .   ? 0.4740 0.2813 0.3287 -0.0919 -0.0978 0.0436  498 HOH   A O   
6921 O O   . HOH   E .   ? 0.5327 0.6783 0.3674 -0.0726 0.0335  0.1360  499 HOH   A O   
6922 O O   . HOH   E .   ? 0.5716 0.3689 0.2893 -0.0141 0.1258  -0.0054 500 HOH   A O   
6923 O O   . HOH   E .   ? 0.2571 0.2390 0.7581 -0.0094 -0.1299 0.0555  501 HOH   A O   
6924 O O   . HOH   E .   ? 0.5693 0.6203 0.6534 0.0549  0.2432  -0.1191 502 HOH   A O   
6925 O O   . HOH   E .   ? 0.2571 0.5093 0.3461 0.1141  0.0951  0.2296  503 HOH   A O   
6926 O O   . HOH   E .   ? 0.3075 0.3477 0.5033 -0.0145 0.1294  0.0888  504 HOH   A O   
6927 O O   . HOH   E .   ? 0.4197 0.3745 0.2489 -0.0989 0.1390  -0.0510 505 HOH   A O   
6928 O O   . HOH   E .   ? 0.4800 0.4783 0.6360 -0.0103 -0.1071 0.0292  506 HOH   A O   
6929 O O   B HOH   E .   ? 0.2887 0.2129 0.3280 0.0960  -0.0157 0.1091  507 HOH   A O   
6930 O O   . HOH   E .   ? 0.4958 0.3331 0.4734 -0.0527 0.2585  0.0212  508 HOH   A O   
6931 O O   . HOH   E .   ? 0.3895 0.2802 0.4678 -0.0962 -0.0229 0.1132  509 HOH   A O   
6932 O O   . HOH   E .   ? 0.2649 0.2360 0.4611 0.0010  0.0001  0.1039  510 HOH   A O   
6933 O O   . HOH   E .   ? 0.5766 0.2517 0.4040 -0.0886 0.0263  0.0625  511 HOH   A O   
6934 O O   . HOH   E .   ? 0.2821 0.4026 0.4766 0.0172  0.1347  -0.0511 512 HOH   A O   
6935 O O   . HOH   E .   ? 0.2345 0.2921 0.3434 0.0412  -0.0327 0.0559  513 HOH   A O   
6936 O O   . HOH   E .   ? 0.4127 0.8274 0.5262 -0.0936 -0.0615 0.2511  514 HOH   A O   
6937 O O   . HOH   E .   ? 0.4511 0.2915 0.3926 -0.1490 -0.0166 0.0761  515 HOH   A O   
6938 O O   . HOH   E .   ? 0.2701 0.4008 0.4014 0.0341  0.0095  0.0280  516 HOH   A O   
6939 O O   B HOH   E .   ? 0.2019 0.3044 0.2564 0.0551  0.0113  0.1269  517 HOH   A O   
6940 O O   . HOH   E .   ? 0.6540 0.4873 0.6193 0.1485  0.0935  0.0298  518 HOH   A O   
6941 O O   . HOH   E .   ? 0.5504 0.6810 0.5453 0.0669  -0.1058 -0.0325 519 HOH   A O   
6942 O O   . HOH   E .   ? 0.6612 0.6249 0.5174 0.0816  -0.1456 0.0398  520 HOH   A O   
6943 O O   . HOH   E .   ? 0.2738 0.4107 0.3024 -0.0006 -0.0272 -0.0869 521 HOH   A O   
6944 O O   B HOH   E .   ? 0.2788 0.2185 0.4809 0.0473  0.0168  0.0368  522 HOH   A O   
6945 O O   . HOH   E .   ? 0.2676 0.2286 0.5206 0.0218  0.0447  0.0995  523 HOH   A O   
6946 O O   . HOH   E .   ? 0.5377 0.6703 0.4680 0.3137  0.0152  0.1330  524 HOH   A O   
6947 O O   B HOH   E .   ? 0.2202 0.1639 0.2940 0.0149  0.0642  0.0489  525 HOH   A O   
6948 O O   A HOH   E .   ? 0.3895 0.7252 0.3921 0.1268  0.0971  -0.0747 526 HOH   A O   
6949 O O   . HOH   E .   ? 0.4992 0.4971 0.4489 -0.0178 -0.0241 -0.1376 527 HOH   A O   
6950 O O   T HOH   E .   ? 0.1082 0.0957 0.2185 -0.0263 -0.0150 0.0616  528 HOH   A O   
6951 O O   . HOH   E .   ? 0.3317 0.8134 0.5003 0.0209  0.0994  -0.1158 529 HOH   A O   
6952 O O   . HOH   E .   ? 0.4810 0.6643 0.5373 -0.0800 -0.0870 0.0796  530 HOH   A O   
6953 O O   . HOH   E .   ? 0.4912 0.4757 0.4296 0.1054  -0.0593 0.1088  531 HOH   A O   
6954 O O   . HOH   E .   ? 0.3521 0.4817 0.5677 0.0427  -0.0805 0.2725  532 HOH   A O   
6955 O O   . HOH   F .   ? 0.2282 0.2276 0.2975 0.0193  0.0776  0.0306  201 HOH   B O   
6956 O O   . HOH   F .   ? 0.4050 0.5521 0.2987 0.0295  -0.0495 -0.1520 202 HOH   B O   
6957 O O   . HOH   F .   ? 0.3344 0.3997 0.4681 -0.0901 0.0501  -0.1422 203 HOH   B O   
6958 O O   . HOH   F .   ? 0.5007 0.5598 0.3723 0.2574  -0.1568 -0.0358 204 HOH   B O   
6959 O O   . HOH   F .   ? 0.4454 0.3050 0.3825 -0.0441 -0.0008 -0.1389 205 HOH   B O   
6960 O O   . HOH   F .   ? 0.5997 0.5239 0.5863 0.1602  0.0772  0.0198  206 HOH   B O   
6961 O O   . HOH   F .   ? 0.7207 0.3132 0.3859 0.0331  0.0255  -0.0001 207 HOH   B O   
6962 O O   . HOH   F .   ? 0.4093 0.5860 0.3604 0.2512  -0.0578 0.0252  208 HOH   B O   
6963 O O   . HOH   F .   ? 0.3018 0.4871 0.4709 -0.0254 0.1689  -0.1777 209 HOH   B O   
6964 O O   . HOH   F .   ? 0.3199 0.6437 0.3094 0.0060  -0.0040 0.2052  210 HOH   B O   
6965 O O   . HOH   F .   ? 0.4429 0.4064 0.6438 0.0275  -0.1120 0.2611  211 HOH   B O   
6966 O O   . HOH   F .   ? 0.3689 0.4852 0.3889 0.2256  0.0535  0.0231  212 HOH   B O   
6967 O O   . HOH   F .   ? 0.1951 0.2205 0.2420 -0.0009 0.0154  -0.0219 213 HOH   B O   
6968 O O   . HOH   F .   ? 0.2669 0.3004 0.6584 0.0661  -0.1024 0.0684  214 HOH   B O   
6969 O O   . HOH   F .   ? 0.5042 0.3995 0.3513 0.0062  -0.1238 0.0749  215 HOH   B O   
6970 O O   . HOH   F .   ? 0.6614 0.3141 0.3749 -0.1695 0.0764  0.0349  216 HOH   B O   
6971 O O   . HOH   F .   ? 0.1567 0.1900 0.2452 -0.0132 -0.0010 0.0080  217 HOH   B O   
6972 O O   . HOH   F .   ? 0.3760 0.5801 0.3279 0.1476  -0.0073 0.0083  218 HOH   B O   
6973 O O   . HOH   F .   ? 0.2892 0.2345 0.5595 -0.0255 0.0275  0.0402  219 HOH   B O   
6974 O O   . HOH   F .   ? 0.4723 0.5416 0.5851 -0.0233 -0.1445 -0.1115 220 HOH   B O   
6975 O O   . HOH   F .   ? 0.3135 0.5038 0.6153 -0.0570 0.0360  -0.0922 221 HOH   B O   
6976 O O   . HOH   F .   ? 0.4822 0.2055 0.2795 0.0080  -0.1005 0.0048  222 HOH   B O   
6977 O O   . HOH   F .   ? 0.5080 0.4367 0.3832 0.0535  0.0928  -0.1718 223 HOH   B O   
6978 O O   . HOH   F .   ? 0.2419 0.1838 0.2578 -0.0386 0.1086  -0.0171 224 HOH   B O   
6979 O O   . HOH   F .   ? 0.1616 0.1964 0.2797 -0.0121 -0.0024 -0.0038 225 HOH   B O   
6980 O O   . HOH   F .   ? 0.2975 0.2128 0.3907 -0.0019 0.1404  0.0148  226 HOH   B O   
6981 O O   . HOH   F .   ? 0.2272 0.2114 0.3690 -0.0392 -0.0178 -0.0568 227 HOH   B O   
6982 O O   . HOH   F .   ? 0.3041 0.2099 0.5238 0.0360  0.1966  0.1029  228 HOH   B O   
6983 O O   . HOH   F .   ? 0.2547 0.3991 0.3155 -0.0808 0.0467  -0.1232 229 HOH   B O   
6984 O O   . HOH   F .   ? 0.4254 0.3360 0.3163 -0.0941 0.0610  -0.0941 230 HOH   B O   
6985 O O   . HOH   F .   ? 0.1919 0.2298 0.3011 -0.0508 -0.0012 -0.0332 231 HOH   B O   
6986 O O   . HOH   F .   ? 0.3280 0.4411 0.4922 0.0862  -0.1231 0.1018  232 HOH   B O   
6987 O O   . HOH   F .   ? 0.2097 0.1347 0.3498 0.0166  -0.0833 -0.0185 233 HOH   B O   
6988 O O   . HOH   F .   ? 0.3610 0.1818 0.1869 0.0063  -0.0639 -0.0035 234 HOH   B O   
6989 O O   . HOH   F .   ? 0.1478 0.1380 0.1487 -0.0163 -0.0103 0.0015  235 HOH   B O   
6990 O O   . HOH   F .   ? 0.5538 0.5554 0.3135 0.1184  -0.0056 0.0356  236 HOH   B O   
6991 O O   . HOH   F .   ? 0.3901 0.4383 0.4573 -0.1676 -0.0131 0.0755  237 HOH   B O   
6992 O O   . HOH   F .   ? 0.2997 0.4578 0.3664 -0.0064 -0.0954 0.0935  238 HOH   B O   
6993 O O   . HOH   F .   ? 0.4531 0.2969 0.4095 -0.2094 -0.0279 0.0260  239 HOH   B O   
6994 O O   . HOH   F .   ? 0.2142 0.3905 0.2969 -0.0548 -0.0537 -0.0584 240 HOH   B O   
6995 O O   . HOH   F .   ? 0.3809 0.2597 0.3969 0.1029  -0.0236 -0.0800 241 HOH   B O   
6996 O O   . HOH   F .   ? 0.3660 0.3359 0.2312 0.0378  0.0874  0.0484  242 HOH   B O   
6997 O O   . HOH   F .   ? 0.2715 0.2517 0.3345 0.0402  0.0164  -0.1099 243 HOH   B O   
6998 O O   . HOH   F .   ? 0.1593 0.1502 0.2296 -0.0016 0.0066  -0.0171 244 HOH   B O   
6999 O O   . HOH   F .   ? 0.1377 0.1273 0.1454 0.0002  -0.0057 0.0047  245 HOH   B O   
7000 O O   . HOH   F .   ? 0.2382 0.3338 0.6146 0.0886  -0.0978 -0.0930 246 HOH   B O   
7001 O O   . HOH   F .   ? 0.2840 0.3454 0.3051 -0.0871 -0.0298 -0.0230 247 HOH   B O   
7002 O O   . HOH   F .   ? 0.6810 0.4519 0.4678 0.1669  0.0089  -0.0731 248 HOH   B O   
7003 O O   . HOH   F .   ? 0.3844 0.2733 0.4106 0.0587  -0.1269 -0.1511 249 HOH   B O   
7004 O O   . HOH   F .   ? 0.3171 0.2308 0.3011 -0.0292 0.0079  -0.0585 250 HOH   B O   
7005 O O   . HOH   F .   ? 0.2008 0.3783 0.2355 -0.0395 -0.0306 0.0698  251 HOH   B O   
7006 O O   . HOH   F .   ? 0.5116 0.3579 0.2383 0.0915  0.0888  -0.0265 252 HOH   B O   
7007 O O   . HOH   F .   ? 0.2889 0.2124 0.3004 0.0866  0.0858  0.0100  253 HOH   B O   
7008 O O   . HOH   F .   ? 0.2305 0.2102 0.1666 0.0069  -0.0122 0.0017  254 HOH   B O   
7009 O O   . HOH   F .   ? 0.3032 0.1749 0.5822 -0.0276 -0.1323 -0.0316 255 HOH   B O   
7010 O O   . HOH   F .   ? 0.3099 0.3451 0.2094 0.0423  0.0756  0.0209  256 HOH   B O   
7011 O O   . HOH   F .   ? 0.2184 0.1928 0.1915 -0.0394 -0.0551 0.0156  257 HOH   B O   
7012 O O   . HOH   F .   ? 0.1527 0.1721 0.2645 -0.0219 -0.0143 0.0036  258 HOH   B O   
7013 O O   . HOH   F .   ? 0.2407 0.3347 0.2196 -0.0738 0.0196  0.0545  259 HOH   B O   
7014 O O   . HOH   F .   ? 0.2157 0.1877 0.3363 0.0096  -0.0523 -0.0362 260 HOH   B O   
7015 O O   . HOH   F .   ? 0.1918 0.1436 0.1946 -0.0226 -0.0252 0.0223  261 HOH   B O   
7016 O O   . HOH   F .   ? 0.2276 0.2206 0.2210 0.0825  -0.0725 -0.0637 262 HOH   B O   
7017 O O   . HOH   F .   ? 0.1353 0.1638 0.1845 -0.0069 0.0033  0.0092  263 HOH   B O   
7018 O O   . HOH   F .   ? 0.2319 0.3637 0.3427 0.0227  0.0949  0.0065  264 HOH   B O   
7019 O O   . HOH   F .   ? 0.2248 0.4907 0.5651 0.0059  0.0322  -0.0937 265 HOH   B O   
7020 O O   . HOH   F .   ? 0.2328 0.2212 0.1785 0.0074  -0.0198 -0.0014 266 HOH   B O   
7021 O O   . HOH   F .   ? 0.2537 0.1932 0.2860 -0.0715 0.0171  -0.0221 267 HOH   B O   
7022 O O   . HOH   F .   ? 0.2155 0.3906 0.4394 -0.0538 -0.0264 -0.1279 268 HOH   B O   
7023 O O   . HOH   F .   ? 0.1729 0.1756 0.1497 -0.0403 -0.0376 0.0092  269 HOH   B O   
7024 O O   . HOH   F .   ? 0.3112 0.3036 0.4807 -0.0286 0.0316  -0.1439 270 HOH   B O   
7025 O O   . HOH   F .   ? 0.1936 0.1522 0.1971 -0.0197 -0.0075 0.0184  271 HOH   B O   
7026 O O   . HOH   F .   ? 0.3956 0.6137 0.2341 -0.0108 -0.0495 0.0737  272 HOH   B O   
7027 O O   . HOH   F .   ? 0.4796 0.3228 0.2608 0.0469  -0.0258 -0.0623 273 HOH   B O   
7028 O O   . HOH   F .   ? 0.1690 0.1371 0.3900 -0.0104 -0.0086 -0.0176 274 HOH   B O   
7029 O O   . HOH   F .   ? 0.1587 0.1501 0.3184 -0.0153 0.0030  -0.0064 275 HOH   B O   
7030 O O   . HOH   F .   ? 0.5692 0.3550 0.2811 0.2458  0.0920  0.0791  276 HOH   B O   
7031 O O   . HOH   F .   ? 0.2419 0.2872 0.2602 -0.0536 -0.0852 0.0114  277 HOH   B O   
7032 O O   . HOH   F .   ? 0.2427 0.2613 0.2165 -0.0492 -0.0741 -0.0375 278 HOH   B O   
7033 O O   . HOH   F .   ? 0.2467 0.3302 0.2186 0.1263  -0.0323 -0.0464 279 HOH   B O   
7034 O O   . HOH   F .   ? 0.3448 0.7113 0.3805 0.1030  -0.0892 0.1661  280 HOH   B O   
7035 O O   . HOH   F .   ? 0.4113 0.3029 0.4127 0.0172  -0.1297 -0.0429 281 HOH   B O   
7036 O O   . HOH   F .   ? 0.2641 0.4739 0.4633 -0.0942 -0.1318 0.0859  282 HOH   B O   
7037 O O   . HOH   F .   ? 0.2499 0.3746 0.4503 -0.0527 -0.1392 0.1041  283 HOH   B O   
7038 O O   . HOH   F .   ? 0.2346 0.3344 0.3113 -0.0772 0.0624  -0.1148 284 HOH   B O   
7039 O O   . HOH   F .   ? 0.2615 0.2063 0.4818 0.0100  0.0592  0.0408  285 HOH   B O   
7040 O O   . HOH   F .   ? 0.1548 0.1506 0.1656 0.0049  0.0024  -0.0027 286 HOH   B O   
7041 O O   . HOH   F .   ? 0.3367 0.2918 0.1928 0.0414  -0.0672 -0.0208 287 HOH   B O   
7042 O O   . HOH   F .   ? 0.3822 0.2145 0.4004 -0.1036 -0.2161 0.0945  288 HOH   B O   
7043 O O   . HOH   F .   ? 0.3031 0.2702 0.2480 -0.0166 0.0237  -0.1140 289 HOH   B O   
7044 O O   . HOH   F .   ? 0.2332 0.7094 0.2525 0.0589  -0.0388 -0.0409 290 HOH   B O   
7045 O O   . HOH   F .   ? 0.3945 0.5556 0.2176 0.1247  -0.0435 0.0026  291 HOH   B O   
7046 O O   . HOH   F .   ? 0.2178 0.2659 0.2836 0.0244  -0.0830 0.0115  292 HOH   B O   
7047 O O   . HOH   F .   ? 0.4853 0.6078 0.4934 0.0746  -0.1562 0.0311  293 HOH   B O   
7048 O O   . HOH   F .   ? 0.3044 0.7077 0.7731 0.1516  -0.0763 -0.0896 294 HOH   B O   
7049 O O   . HOH   F .   ? 0.4471 0.2889 0.4763 -0.0653 0.0443  0.0911  295 HOH   B O   
7050 O O   . HOH   F .   ? 0.1509 0.2048 0.1415 -0.0143 -0.0138 0.0050  296 HOH   B O   
7051 O O   . HOH   F .   ? 0.3286 0.1988 0.3335 0.0713  0.1129  0.0483  297 HOH   B O   
7052 O O   . HOH   F .   ? 0.1603 0.1892 0.2719 0.0182  -0.0042 0.0185  298 HOH   B O   
7053 O O   . HOH   F .   ? 0.1745 0.3346 0.4587 0.0381  -0.0036 -0.1474 299 HOH   B O   
7054 O O   . HOH   F .   ? 0.3406 0.3770 0.4583 0.1245  -0.0830 -0.1042 300 HOH   B O   
7055 O O   . HOH   F .   ? 0.1904 0.1530 0.2620 -0.0215 -0.0348 -0.0053 301 HOH   B O   
7056 O O   . HOH   F .   ? 0.2125 0.1540 0.3228 0.0347  -0.1127 0.0029  302 HOH   B O   
7057 O O   . HOH   F .   ? 0.5664 0.2952 0.2236 -0.1797 0.1029  -0.0245 303 HOH   B O   
7058 O O   . HOH   F .   ? 0.1675 0.1515 0.2228 -0.0024 -0.0017 0.0229  304 HOH   B O   
7059 O O   . HOH   F .   ? 0.4695 0.3925 0.2436 0.1469  -0.0888 0.0411  305 HOH   B O   
7060 O O   . HOH   F .   ? 0.4047 0.3092 0.4794 0.0630  0.1700  0.1671  306 HOH   B O   
7061 O O   . HOH   F .   ? 0.3284 0.3893 0.6828 -0.0080 -0.0762 0.1894  307 HOH   B O   
7062 O O   . HOH   F .   ? 0.2347 0.3038 0.4910 -0.0353 -0.0488 0.0107  308 HOH   B O   
7063 O O   . HOH   F .   ? 0.2033 0.2619 0.6006 0.0580  -0.0248 -0.0909 309 HOH   B O   
7064 O O   . HOH   F .   ? 0.4274 0.2528 0.2687 0.1693  0.1149  0.0457  310 HOH   B O   
7065 O O   . HOH   F .   ? 0.4156 0.4197 0.1881 0.0093  0.0373  0.0524  311 HOH   B O   
7066 O O   . HOH   F .   ? 0.1450 0.1494 0.2798 0.0149  -0.0049 -0.0094 312 HOH   B O   
7067 O O   . HOH   F .   ? 0.2551 0.2866 0.3599 -0.0342 0.0995  -0.0852 313 HOH   B O   
7068 O O   . HOH   F .   ? 0.2667 0.2172 0.2365 0.0209  -0.0171 0.0250  314 HOH   B O   
7069 O O   . HOH   F .   ? 0.2684 0.3682 0.4000 -0.1242 0.1064  -0.0753 315 HOH   B O   
7070 O O   . HOH   F .   ? 0.2962 0.3077 0.5052 -0.0359 -0.0838 0.1256  316 HOH   B O   
7071 O O   . HOH   F .   ? 0.6234 0.3942 0.5220 0.1596  0.1237  0.0111  317 HOH   B O   
7072 O O   . HOH   F .   ? 0.1508 0.1538 0.2883 -0.0105 -0.0125 -0.0090 318 HOH   B O   
7073 O O   . HOH   F .   ? 0.1508 0.1842 0.2729 -0.0265 -0.0115 0.0111  319 HOH   B O   
7074 O O   . HOH   F .   ? 0.2116 0.1964 0.1670 -0.0052 0.0263  0.0175  320 HOH   B O   
7075 O O   . HOH   F .   ? 0.2379 0.1468 0.2418 -0.0109 -0.0122 0.0388  321 HOH   B O   
7076 O O   . HOH   F .   ? 0.5981 0.4237 0.6188 0.0571  -0.0807 0.1630  322 HOH   B O   
7077 O O   . HOH   F .   ? 0.1636 0.2784 0.2385 -0.0096 -0.0257 0.0710  323 HOH   B O   
7078 O O   . HOH   F .   ? 0.6676 0.2105 0.2903 0.0061  -0.0480 0.0014  324 HOH   B O   
7079 O O   . HOH   F .   ? 0.6213 0.4855 0.4873 -0.1047 -0.0285 0.1013  325 HOH   B O   
7080 O O   . HOH   F .   ? 0.6287 0.6756 0.5000 0.3038  -0.0394 -0.0618 326 HOH   B O   
7081 O O   . HOH   F .   ? 0.4450 0.2502 0.2774 0.0101  0.0378  0.0758  327 HOH   B O   
7082 O O   . HOH   F .   ? 0.4655 0.4567 0.2113 0.0622  -0.0457 -0.0579 328 HOH   B O   
7083 O O   . HOH   F .   ? 0.2253 0.5244 0.4430 -0.0934 -0.0315 -0.0384 329 HOH   B O   
7084 O O   . HOH   F .   ? 0.1860 0.1968 0.2725 0.0364  0.0490  0.0204  330 HOH   B O   
7085 O O   . HOH   F .   ? 0.2636 0.2036 0.4172 -0.0015 0.0158  0.0285  331 HOH   B O   
7086 O O   . HOH   F .   ? 0.4093 0.3715 0.5792 0.0770  -0.0271 0.1056  332 HOH   B O   
7087 O O   . HOH   F .   ? 0.1687 0.2641 0.2906 0.0290  -0.0205 -0.0661 333 HOH   B O   
7088 O O   . HOH   F .   ? 0.2287 0.2362 0.5258 -0.0623 -0.0334 0.1452  334 HOH   B O   
7089 O O   . HOH   F .   ? 0.5477 0.3593 0.3508 0.0114  0.1093  0.1307  335 HOH   B O   
7090 O O   . HOH   F .   ? 0.1612 0.1412 0.2157 0.0046  -0.0200 0.0030  336 HOH   B O   
7091 O O   . HOH   F .   ? 0.5277 0.4576 0.5240 -0.0375 -0.0317 -0.1277 337 HOH   B O   
7092 O O   . HOH   F .   ? 0.4035 0.7176 0.3387 -0.0017 -0.0283 0.1864  338 HOH   B O   
7093 O O   . HOH   F .   ? 0.4868 0.5927 0.3530 -0.0448 -0.1015 0.0503  339 HOH   B O   
7094 O O   . HOH   F .   ? 0.4394 0.3502 0.3255 0.0608  -0.1183 -0.0843 340 HOH   B O   
7095 O O   . HOH   F .   ? 0.5076 0.3454 0.4212 0.0182  0.0325  -0.1696 341 HOH   B O   
7096 O O   . HOH   F .   ? 0.4097 0.6077 0.3937 -0.1037 -0.1291 -0.0842 342 HOH   B O   
7097 O O   . HOH   F .   ? 0.2203 0.1871 0.2742 -0.0057 0.0531  -0.0093 343 HOH   B O   
7098 O O   . HOH   F .   ? 0.2704 0.6561 0.5927 0.0904  0.0759  0.0407  344 HOH   B O   
7099 O O   . HOH   F .   ? 0.4972 0.5829 0.4425 -0.1234 0.0738  0.1232  345 HOH   B O   
7100 O O   . HOH   F .   ? 0.3994 0.4517 0.5757 0.0291  -0.1042 0.0478  346 HOH   B O   
7101 O O   . HOH   F .   ? 0.6781 0.6098 0.2687 -0.0115 -0.0537 0.0920  347 HOH   B O   
7102 O O   . HOH   F .   ? 0.2405 0.3615 0.4960 0.0385  0.0414  0.0068  348 HOH   B O   
7103 O O   . HOH   F .   ? 0.2849 0.2308 0.4783 -0.0392 -0.0903 -0.0430 349 HOH   B O   
7104 O O   . HOH   F .   ? 0.2334 0.5793 0.3902 0.1454  -0.0497 -0.1621 350 HOH   B O   
7105 O O   . HOH   F .   ? 0.4526 0.5147 0.5934 0.0123  -0.0048 -0.0073 351 HOH   B O   
7106 O O   . HOH   F .   ? 0.3741 0.2287 0.3538 -0.0737 0.0508  -0.1135 352 HOH   B O   
7107 O O   . HOH   F .   ? 0.3502 0.4252 0.4911 -0.1555 0.0222  -0.0436 353 HOH   B O   
7108 O O   . HOH   F .   ? 0.5159 0.5134 0.4993 -0.0855 -0.0548 0.0291  354 HOH   B O   
7109 O O   . HOH   F .   ? 0.4888 0.3680 0.4167 0.0925  0.1222  -0.0780 355 HOH   B O   
7110 O O   . HOH   F .   ? 0.2891 0.1912 0.4233 0.0410  -0.1217 -0.0682 356 HOH   B O   
7111 O O   . HOH   F .   ? 0.3557 0.2564 0.3579 -0.0868 -0.0107 -0.0502 357 HOH   B O   
7112 O O   . HOH   F .   ? 0.4087 0.3593 0.5149 -0.1195 0.1164  0.0495  358 HOH   B O   
7113 O O   . HOH   F .   ? 0.4490 0.5261 0.4845 0.1843  -0.1213 0.1447  359 HOH   B O   
7114 O O   . HOH   F .   ? 0.4694 0.3219 0.4756 0.0096  -0.1618 0.0008  360 HOH   B O   
7115 O O   . HOH   F .   ? 0.4143 0.4242 0.6093 -0.0303 0.0640  0.1019  361 HOH   B O   
7116 O O   . HOH   F .   ? 0.4452 0.6402 0.2977 0.1689  -0.0097 0.0103  362 HOH   B O   
7117 O O   . HOH   F .   ? 0.2397 0.3373 0.6344 -0.0844 -0.0596 -0.0766 363 HOH   B O   
7118 O O   . HOH   F .   ? 0.4405 0.3542 0.4769 -0.1359 -0.0516 0.0378  364 HOH   B O   
7119 O O   . HOH   F .   ? 0.4282 0.3445 0.5375 0.0884  -0.1311 0.0353  365 HOH   B O   
7120 O O   . HOH   F .   ? 0.5007 0.5486 0.4730 -0.0902 -0.0853 -0.1023 366 HOH   B O   
7121 O O   . HOH   F .   ? 0.5161 0.4945 0.3761 0.0519  -0.1497 0.1009  367 HOH   B O   
7122 O O   . HOH   F .   ? 0.5735 0.4376 0.4527 0.0736  0.0802  0.0404  368 HOH   B O   
7123 O O   . HOH   F .   ? 0.7196 0.7648 0.5195 0.2331  -0.1185 0.0946  369 HOH   B O   
7124 O O   . HOH   F .   ? 0.5844 0.2180 0.3221 0.0090  0.0223  0.0517  370 HOH   B O   
7125 O O   . HOH   F .   ? 0.4369 0.5746 0.5360 0.2691  0.1458  0.1532  371 HOH   B O   
7126 O O   . HOH   F .   ? 0.5870 0.3786 0.3101 -0.1422 -0.0968 -0.0393 372 HOH   B O   
7127 O O   . HOH   F .   ? 0.4669 0.3638 0.4184 0.0709  -0.1423 -0.0611 373 HOH   B O   
7128 O O   . HOH   F .   ? 0.4003 0.5776 0.4490 -0.1220 -0.0478 0.0555  374 HOH   B O   
7129 O O   . HOH   F .   ? 0.2296 0.5364 0.4114 0.0085  -0.0468 -0.0899 375 HOH   B O   
7130 O O   . HOH   F .   ? 0.3171 0.3681 0.2212 0.0496  0.0435  0.0193  376 HOH   B O   
7131 O O   . HOH   F .   ? 0.6765 0.3803 0.5201 -0.1066 -0.0411 -0.0091 377 HOH   B O   
7132 O O   . HOH   F .   ? 0.4865 0.6363 0.6386 0.1360  0.0486  0.2537  378 HOH   B O   
7133 O O   . HOH   F .   ? 0.5201 0.6683 0.3996 -0.1474 0.0441  -0.1508 379 HOH   B O   
7134 O O   . HOH   F .   ? 0.5802 0.6886 0.6186 0.0111  0.2503  0.1160  380 HOH   B O   
7135 O O   . HOH   F .   ? 0.3563 0.4712 0.4448 0.1255  0.0481  0.0488  381 HOH   B O   
7136 O O   . HOH   F .   ? 0.2881 0.2481 0.3138 -0.0055 0.0115  0.0429  382 HOH   B O   
7137 O O   . HOH   F .   ? 0.4462 0.7898 0.5167 0.1000  0.1953  0.1112  383 HOH   B O   
7138 O O   . HOH   F .   ? 0.5028 0.5050 0.4461 0.0630  -0.0900 -0.0195 384 HOH   B O   
7139 O O   . HOH   F .   ? 0.6048 0.5239 0.4252 0.0989  0.0508  -0.1375 385 HOH   B O   
7140 O O   . HOH   F .   ? 0.2448 0.3940 0.3430 -0.0666 -0.0929 -0.0387 386 HOH   B O   
7141 O O   . HOH   F .   ? 0.6844 0.5437 0.4252 0.0992  0.0242  0.0420  387 HOH   B O   
7142 O O   . HOH   F .   ? 0.4288 0.3769 0.3080 -0.0159 0.0387  -0.0475 388 HOH   B O   
7143 O O   . HOH   F .   ? 0.5557 0.4459 0.5010 -0.0777 0.0535  0.0004  389 HOH   B O   
7144 O O   . HOH   F .   ? 0.3381 0.2214 0.3042 0.0477  -0.0187 0.0032  390 HOH   B O   
7145 O O   . HOH   F .   ? 0.4380 0.3624 0.4049 -0.0145 0.0602  0.0547  391 HOH   B O   
7146 O O   . HOH   F .   ? 0.2317 0.4119 0.6054 -0.1267 -0.0452 0.0238  392 HOH   B O   
7147 O O   . HOH   F .   ? 0.3815 0.2172 0.5081 -0.0295 0.0583  0.0545  393 HOH   B O   
7148 O O   . HOH   F .   ? 0.4185 0.4524 0.4190 -0.0196 0.0792  0.1156  394 HOH   B O   
7149 O O   . HOH   F .   ? 0.3619 0.5223 0.3904 0.0416  -0.0245 -0.0985 395 HOH   B O   
7150 O O   . HOH   F .   ? 0.5463 0.6577 0.7015 0.1406  -0.0810 0.2033  396 HOH   B O   
7151 O O   . HOH   F .   ? 0.1994 0.2786 0.5689 -0.0374 -0.1080 0.0073  397 HOH   B O   
7152 O O   . HOH   F .   ? 0.3039 0.3122 0.3697 0.0413  0.0116  -0.0176 398 HOH   B O   
7153 O O   . HOH   F .   ? 0.5195 0.3988 0.3217 -0.2071 -0.0592 0.1441  399 HOH   B O   
7154 O O   . HOH   F .   ? 0.5184 0.5991 0.3581 0.1688  0.0344  0.0041  400 HOH   B O   
# 
