data_7HEL
# 
_entry.id   7HEL 
# 
_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   7HEL         pdb_00007hel 10.2210/pdb7hel/pdb 
WWPDB D_1001407375 ?            ?                   
# 
_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                        7HEL 
_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 '(2S)-3-(4-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 282.340   1   ? ? ? ? 
3 non-polymer syn '(2R)-3-(4-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 282.340   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                  35.453    1   ? ? ? ? 
5 water       nat water                                                                           18.015    424 ? ? ? ? 
# 
_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 '(2S)-3-(4-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9Z 
3 '(2R)-3-(4-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9Y 
4 'CHLORIDE ION'                                                                  CL    
5 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 
A1A9Y non-polymer         . '(2R)-3-(4-methylphenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C16 H18 N4 O'   
282.340 
A1A9Z non-polymer         . '(2S)-3-(4-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 
CL    non-polymer         . 'CHLORIDE ION'                                                                  ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                        ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                           ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                   ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                         ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                          ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                        ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A9Z 1   201 201  A1A9Z LA1 A . 
D 3 A1A9Y 1   202 301  A1A9Y LA2 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 115  HOH   HOH A . 
F 5 HOH   3   303 109  HOH   HOH A . 
F 5 HOH   4   304 625  HOH   HOH A . 
F 5 HOH   5   305 153  HOH   HOH A . 
F 5 HOH   6   306 136  HOH   HOH A . 
F 5 HOH   7   307 1289 HOH   HOH A . 
F 5 HOH   8   308 1313 HOH   HOH A . 
F 5 HOH   9   309 199  HOH   HOH A . 
F 5 HOH   10  310 196  HOH   HOH A . 
F 5 HOH   11  311 229  HOH   HOH A . 
F 5 HOH   12  312 105  HOH   HOH A . 
F 5 HOH   13  313 209  HOH   HOH A . 
F 5 HOH   14  314 393  HOH   HOH A . 
F 5 HOH   15  315 337  HOH   HOH A . 
F 5 HOH   16  316 36   HOH   HOH A . 
F 5 HOH   17  317 86   HOH   HOH A . 
F 5 HOH   18  318 1310 HOH   HOH A . 
F 5 HOH   19  319 124  HOH   HOH A . 
F 5 HOH   20  320 76   HOH   HOH A . 
F 5 HOH   21  321 155  HOH   HOH A . 
F 5 HOH   22  322 192  HOH   HOH A . 
F 5 HOH   23  323 57   HOH   HOH A . 
F 5 HOH   24  324 93   HOH   HOH A . 
F 5 HOH   25  325 1295 HOH   HOH A . 
F 5 HOH   26  326 1283 HOH   HOH A . 
F 5 HOH   27  327 247  HOH   HOH A . 
F 5 HOH   28  328 225  HOH   HOH A . 
F 5 HOH   29  329 96   HOH   HOH A . 
F 5 HOH   30  330 236  HOH   HOH A . 
F 5 HOH   31  331 241  HOH   HOH A . 
F 5 HOH   32  332 151  HOH   HOH A . 
F 5 HOH   33  333 140  HOH   HOH A . 
F 5 HOH   34  334 469  HOH   HOH A . 
F 5 HOH   35  335 18   HOH   HOH A . 
F 5 HOH   36  336 17   HOH   HOH A . 
F 5 HOH   37  337 21   HOH   HOH A . 
F 5 HOH   38  338 320  HOH   HOH A . 
F 5 HOH   39  339 164  HOH   HOH A . 
F 5 HOH   40  340 42   HOH   HOH A . 
F 5 HOH   41  341 49   HOH   HOH A . 
F 5 HOH   42  342 102  HOH   HOH A . 
F 5 HOH   43  343 18   HOH   HOH A . 
F 5 HOH   44  344 1300 HOH   HOH A . 
F 5 HOH   45  345 5    HOH   HOH A . 
F 5 HOH   46  346 26   HOH   HOH A . 
F 5 HOH   47  347 15   HOH   HOH A . 
F 5 HOH   48  348 1309 HOH   HOH A . 
F 5 HOH   49  349 964  HOH   HOH A . 
F 5 HOH   50  350 165  HOH   HOH A . 
F 5 HOH   51  351 39   HOH   HOH A . 
F 5 HOH   52  352 132  HOH   HOH A . 
F 5 HOH   53  353 630  HOH   HOH A . 
F 5 HOH   54  354 139  HOH   HOH A . 
F 5 HOH   55  355 92   HOH   HOH A . 
F 5 HOH   56  356 2    HOH   HOH A . 
F 5 HOH   57  357 45   HOH   HOH A . 
F 5 HOH   58  358 354  HOH   HOH A . 
F 5 HOH   59  359 66   HOH   HOH A . 
F 5 HOH   60  360 162  HOH   HOH A . 
F 5 HOH   61  361 396  HOH   HOH A . 
F 5 HOH   62  362 169  HOH   HOH A . 
F 5 HOH   63  363 12   HOH   HOH A . 
F 5 HOH   64  364 662  HOH   HOH A . 
F 5 HOH   65  365 1290 HOH   HOH A . 
F 5 HOH   66  366 19   HOH   HOH A . 
F 5 HOH   67  367 27   HOH   HOH A . 
F 5 HOH   68  368 461  HOH   HOH A . 
F 5 HOH   69  369 159  HOH   HOH A . 
F 5 HOH   70  370 56   HOH   HOH A . 
F 5 HOH   71  371 939  HOH   HOH A . 
F 5 HOH   72  372 218  HOH   HOH A . 
F 5 HOH   73  373 138  HOH   HOH A . 
F 5 HOH   74  374 5    HOH   HOH A . 
F 5 HOH   75  375 70   HOH   HOH A . 
F 5 HOH   76  376 81   HOH   HOH A . 
F 5 HOH   77  377 186  HOH   HOH A . 
F 5 HOH   78  378 134  HOH   HOH A . 
F 5 HOH   79  379 46   HOH   HOH A . 
F 5 HOH   80  380 3    HOH   HOH A . 
F 5 HOH   81  381 493  HOH   HOH A . 
F 5 HOH   82  382 333  HOH   HOH A . 
F 5 HOH   83  383 4    HOH   HOH A . 
F 5 HOH   84  384 8    HOH   HOH A . 
F 5 HOH   85  385 12   HOH   HOH A . 
F 5 HOH   86  386 366  HOH   HOH A . 
F 5 HOH   87  387 2    HOH   HOH A . 
F 5 HOH   88  388 154  HOH   HOH A . 
F 5 HOH   89  389 351  HOH   HOH A . 
F 5 HOH   90  390 74   HOH   HOH A . 
F 5 HOH   91  391 14   HOH   HOH A . 
F 5 HOH   92  392 381  HOH   HOH A . 
F 5 HOH   93  393 35   HOH   HOH A . 
F 5 HOH   94  394 78   HOH   HOH A . 
F 5 HOH   95  395 1308 HOH   HOH A . 
F 5 HOH   96  396 122  HOH   HOH A . 
F 5 HOH   97  397 1275 HOH   HOH A . 
F 5 HOH   98  398 121  HOH   HOH A . 
F 5 HOH   99  399 148  HOH   HOH A . 
F 5 HOH   100 400 58   HOH   HOH A . 
F 5 HOH   101 401 195  HOH   HOH A . 
F 5 HOH   102 402 116  HOH   HOH A . 
F 5 HOH   103 403 33   HOH   HOH A . 
F 5 HOH   104 404 296  HOH   HOH A . 
F 5 HOH   105 405 68   HOH   HOH A . 
F 5 HOH   106 406 67   HOH   HOH A . 
F 5 HOH   107 407 409  HOH   HOH A . 
F 5 HOH   108 408 83   HOH   HOH A . 
F 5 HOH   109 409 1315 HOH   HOH A . 
F 5 HOH   110 410 4    HOH   HOH A . 
F 5 HOH   111 411 582  HOH   HOH A . 
F 5 HOH   112 412 6    HOH   HOH A . 
F 5 HOH   113 413 24   HOH   HOH A . 
F 5 HOH   114 414 34   HOH   HOH A . 
F 5 HOH   115 415 1279 HOH   HOH A . 
F 5 HOH   116 416 661  HOH   HOH A . 
F 5 HOH   117 417 303  HOH   HOH A . 
F 5 HOH   118 418 51   HOH   HOH A . 
F 5 HOH   119 419 281  HOH   HOH A . 
F 5 HOH   120 420 25   HOH   HOH A . 
F 5 HOH   121 421 125  HOH   HOH A . 
F 5 HOH   122 422 7    HOH   HOH A . 
F 5 HOH   123 423 85   HOH   HOH A . 
F 5 HOH   124 424 123  HOH   HOH A . 
F 5 HOH   125 425 53   HOH   HOH A . 
F 5 HOH   126 426 278  HOH   HOH A . 
F 5 HOH   127 427 95   HOH   HOH A . 
F 5 HOH   128 428 397  HOH   HOH A . 
F 5 HOH   129 429 156  HOH   HOH A . 
F 5 HOH   130 430 7    HOH   HOH A . 
F 5 HOH   131 431 1286 HOH   HOH A . 
F 5 HOH   132 432 1068 HOH   HOH A . 
F 5 HOH   133 433 10   HOH   HOH A . 
F 5 HOH   134 434 16   HOH   HOH A . 
F 5 HOH   135 435 1222 HOH   HOH A . 
F 5 HOH   136 436 188  HOH   HOH A . 
F 5 HOH   137 437 1296 HOH   HOH A . 
F 5 HOH   138 438 1238 HOH   HOH A . 
F 5 HOH   139 439 212  HOH   HOH A . 
F 5 HOH   140 440 405  HOH   HOH A . 
F 5 HOH   141 441 1094 HOH   HOH A . 
F 5 HOH   142 442 71   HOH   HOH A . 
F 5 HOH   143 443 944  HOH   HOH A . 
F 5 HOH   144 444 80   HOH   HOH A . 
F 5 HOH   145 445 94   HOH   HOH A . 
F 5 HOH   146 446 40   HOH   HOH A . 
F 5 HOH   147 447 952  HOH   HOH A . 
F 5 HOH   148 448 73   HOH   HOH A . 
F 5 HOH   149 449 9    HOH   HOH A . 
F 5 HOH   150 450 97   HOH   HOH A . 
F 5 HOH   151 451 104  HOH   HOH A . 
F 5 HOH   152 452 1189 HOH   HOH A . 
F 5 HOH   153 453 1301 HOH   HOH A . 
F 5 HOH   154 454 576  HOH   HOH A . 
F 5 HOH   155 455 330  HOH   HOH A . 
F 5 HOH   156 456 79   HOH   HOH A . 
F 5 HOH   157 457 3    HOH   HOH A . 
F 5 HOH   158 458 1119 HOH   HOH A . 
F 5 HOH   159 459 1134 HOH   HOH A . 
F 5 HOH   160 460 17   HOH   HOH A . 
F 5 HOH   161 461 107  HOH   HOH A . 
F 5 HOH   162 462 509  HOH   HOH A . 
F 5 HOH   163 463 163  HOH   HOH A . 
F 5 HOH   164 464 408  HOH   HOH A . 
F 5 HOH   165 465 726  HOH   HOH A . 
F 5 HOH   166 466 319  HOH   HOH A . 
F 5 HOH   167 467 756  HOH   HOH A . 
F 5 HOH   168 468 280  HOH   HOH A . 
F 5 HOH   169 469 1276 HOH   HOH A . 
F 5 HOH   170 470 370  HOH   HOH A . 
F 5 HOH   171 471 361  HOH   HOH A . 
F 5 HOH   172 472 126  HOH   HOH A . 
F 5 HOH   173 473 556  HOH   HOH A . 
F 5 HOH   174 474 63   HOH   HOH A . 
F 5 HOH   175 475 342  HOH   HOH A . 
F 5 HOH   176 476 801  HOH   HOH A . 
F 5 HOH   177 477 250  HOH   HOH A . 
F 5 HOH   178 478 1307 HOH   HOH A . 
F 5 HOH   179 479 135  HOH   HOH A . 
F 5 HOH   180 480 1306 HOH   HOH A . 
F 5 HOH   181 481 224  HOH   HOH A . 
F 5 HOH   182 482 1287 HOH   HOH A . 
F 5 HOH   183 483 202  HOH   HOH A . 
F 5 HOH   184 484 711  HOH   HOH A . 
F 5 HOH   185 485 674  HOH   HOH A . 
F 5 HOH   186 486 267  HOH   HOH A . 
F 5 HOH   187 487 919  HOH   HOH A . 
F 5 HOH   188 488 695  HOH   HOH A . 
F 5 HOH   189 489 315  HOH   HOH A . 
F 5 HOH   190 490 13   HOH   HOH A . 
F 5 HOH   191 491 1299 HOH   HOH A . 
F 5 HOH   192 492 318  HOH   HOH A . 
F 5 HOH   193 493 309  HOH   HOH A . 
F 5 HOH   194 494 521  HOH   HOH A . 
F 5 HOH   195 495 1314 HOH   HOH A . 
F 5 HOH   196 496 331  HOH   HOH A . 
F 5 HOH   197 497 805  HOH   HOH A . 
F 5 HOH   198 498 326  HOH   HOH A . 
F 5 HOH   199 499 152  HOH   HOH A . 
F 5 HOH   200 500 263  HOH   HOH A . 
F 5 HOH   201 501 1284 HOH   HOH A . 
F 5 HOH   202 502 981  HOH   HOH A . 
F 5 HOH   203 503 941  HOH   HOH A . 
F 5 HOH   204 504 208  HOH   HOH A . 
F 5 HOH   205 505 1071 HOH   HOH A . 
F 5 HOH   206 506 6    HOH   HOH A . 
F 5 HOH   207 507 350  HOH   HOH A . 
F 5 HOH   208 508 180  HOH   HOH A . 
F 5 HOH   209 509 356  HOH   HOH A . 
F 5 HOH   210 510 363  HOH   HOH A . 
F 5 HOH   211 511 313  HOH   HOH A . 
F 5 HOH   212 512 11   HOH   HOH A . 
F 5 HOH   213 513 371  HOH   HOH A . 
F 5 HOH   214 514 185  HOH   HOH A . 
F 5 HOH   215 515 429  HOH   HOH A . 
F 5 HOH   216 516 772  HOH   HOH A . 
F 5 HOH   217 517 16   HOH   HOH A . 
F 5 HOH   218 518 376  HOH   HOH A . 
F 5 HOH   219 519 1074 HOH   HOH A . 
F 5 HOH   220 520 346  HOH   HOH A . 
F 5 HOH   221 521 8    HOH   HOH A . 
F 5 HOH   222 522 1292 HOH   HOH A . 
F 5 HOH   223 523 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 531  HOH   HOH B . 
G 5 HOH   3   203 549  HOH   HOH B . 
G 5 HOH   4   204 240  HOH   HOH B . 
G 5 HOH   5   205 364  HOH   HOH B . 
G 5 HOH   6   206 358  HOH   HOH B . 
G 5 HOH   7   207 758  HOH   HOH B . 
G 5 HOH   8   208 232  HOH   HOH B . 
G 5 HOH   9   209 398  HOH   HOH B . 
G 5 HOH   10  210 120  HOH   HOH B . 
G 5 HOH   11  211 1249 HOH   HOH B . 
G 5 HOH   12  212 900  HOH   HOH B . 
G 5 HOH   13  213 743  HOH   HOH B . 
G 5 HOH   14  214 264  HOH   HOH B . 
G 5 HOH   15  215 343  HOH   HOH B . 
G 5 HOH   16  216 654  HOH   HOH B . 
G 5 HOH   17  217 452  HOH   HOH B . 
G 5 HOH   18  218 15   HOH   HOH B . 
G 5 HOH   19  219 50   HOH   HOH B . 
G 5 HOH   20  220 353  HOH   HOH B . 
G 5 HOH   21  221 444  HOH   HOH B . 
G 5 HOH   22  222 1140 HOH   HOH B . 
G 5 HOH   23  223 131  HOH   HOH B . 
G 5 HOH   24  224 332  HOH   HOH B . 
G 5 HOH   25  225 166  HOH   HOH B . 
G 5 HOH   26  226 54   HOH   HOH B . 
G 5 HOH   27  227 1312 HOH   HOH B . 
G 5 HOH   28  228 276  HOH   HOH B . 
G 5 HOH   29  229 75   HOH   HOH B . 
G 5 HOH   30  230 128  HOH   HOH B . 
G 5 HOH   31  231 282  HOH   HOH B . 
G 5 HOH   32  232 127  HOH   HOH B . 
G 5 HOH   33  233 60   HOH   HOH B . 
G 5 HOH   34  234 205  HOH   HOH B . 
G 5 HOH   35  235 82   HOH   HOH B . 
G 5 HOH   36  236 133  HOH   HOH B . 
G 5 HOH   37  237 69   HOH   HOH B . 
G 5 HOH   38  238 1278 HOH   HOH B . 
G 5 HOH   39  239 272  HOH   HOH B . 
G 5 HOH   40  240 110  HOH   HOH B . 
G 5 HOH   41  241 300  HOH   HOH B . 
G 5 HOH   42  242 14   HOH   HOH B . 
G 5 HOH   43  243 181  HOH   HOH B . 
G 5 HOH   44  244 325  HOH   HOH B . 
G 5 HOH   45  245 143  HOH   HOH B . 
G 5 HOH   46  246 1    HOH   HOH B . 
G 5 HOH   47  247 9    HOH   HOH B . 
G 5 HOH   48  248 129  HOH   HOH B . 
G 5 HOH   49  249 172  HOH   HOH B . 
G 5 HOH   50  250 231  HOH   HOH B . 
G 5 HOH   51  251 30   HOH   HOH B . 
G 5 HOH   52  252 144  HOH   HOH B . 
G 5 HOH   53  253 723  HOH   HOH B . 
G 5 HOH   54  254 72   HOH   HOH B . 
G 5 HOH   55  255 41   HOH   HOH B . 
G 5 HOH   56  256 52   HOH   HOH B . 
G 5 HOH   57  257 1277 HOH   HOH B . 
G 5 HOH   58  258 31   HOH   HOH B . 
G 5 HOH   59  259 47   HOH   HOH B . 
G 5 HOH   60  260 150  HOH   HOH B . 
G 5 HOH   61  261 10   HOH   HOH B . 
G 5 HOH   62  262 271  HOH   HOH B . 
G 5 HOH   63  263 302  HOH   HOH B . 
G 5 HOH   64  264 62   HOH   HOH B . 
G 5 HOH   65  265 347  HOH   HOH B . 
G 5 HOH   66  266 59   HOH   HOH B . 
G 5 HOH   67  267 416  HOH   HOH B . 
G 5 HOH   68  268 391  HOH   HOH B . 
G 5 HOH   69  269 117  HOH   HOH B . 
G 5 HOH   70  270 20   HOH   HOH B . 
G 5 HOH   71  271 243  HOH   HOH B . 
G 5 HOH   72  272 11   HOH   HOH B . 
G 5 HOH   73  273 84   HOH   HOH B . 
G 5 HOH   74  274 61   HOH   HOH B . 
G 5 HOH   75  275 103  HOH   HOH B . 
G 5 HOH   76  276 242  HOH   HOH B . 
G 5 HOH   77  277 77   HOH   HOH B . 
G 5 HOH   78  278 114  HOH   HOH B . 
G 5 HOH   79  279 175  HOH   HOH B . 
G 5 HOH   80  280 287  HOH   HOH B . 
G 5 HOH   81  281 1305 HOH   HOH B . 
G 5 HOH   82  282 22   HOH   HOH B . 
G 5 HOH   83  283 43   HOH   HOH B . 
G 5 HOH   84  284 147  HOH   HOH B . 
G 5 HOH   85  285 387  HOH   HOH B . 
G 5 HOH   86  286 13   HOH   HOH B . 
G 5 HOH   87  287 89   HOH   HOH B . 
G 5 HOH   88  288 106  HOH   HOH B . 
G 5 HOH   89  289 221  HOH   HOH B . 
G 5 HOH   90  290 1106 HOH   HOH B . 
G 5 HOH   91  291 137  HOH   HOH B . 
G 5 HOH   92  292 635  HOH   HOH B . 
G 5 HOH   93  293 252  HOH   HOH B . 
G 5 HOH   94  294 1066 HOH   HOH B . 
G 5 HOH   95  295 235  HOH   HOH B . 
G 5 HOH   96  296 88   HOH   HOH B . 
G 5 HOH   97  297 112  HOH   HOH B . 
G 5 HOH   98  298 316  HOH   HOH B . 
G 5 HOH   99  299 311  HOH   HOH B . 
G 5 HOH   100 300 160  HOH   HOH B . 
G 5 HOH   101 301 216  HOH   HOH B . 
G 5 HOH   102 302 32   HOH   HOH B . 
G 5 HOH   103 303 297  HOH   HOH B . 
G 5 HOH   104 304 299  HOH   HOH B . 
G 5 HOH   105 305 99   HOH   HOH B . 
G 5 HOH   106 306 220  HOH   HOH B . 
G 5 HOH   107 307 38   HOH   HOH B . 
G 5 HOH   108 308 1274 HOH   HOH B . 
G 5 HOH   109 309 170  HOH   HOH B . 
G 5 HOH   110 310 101  HOH   HOH B . 
G 5 HOH   111 311 142  HOH   HOH B . 
G 5 HOH   112 312 91   HOH   HOH B . 
G 5 HOH   113 313 215  HOH   HOH B . 
G 5 HOH   114 314 1126 HOH   HOH B . 
G 5 HOH   115 315 37   HOH   HOH B . 
G 5 HOH   116 316 48   HOH   HOH B . 
G 5 HOH   117 317 141  HOH   HOH B . 
G 5 HOH   118 318 118  HOH   HOH B . 
G 5 HOH   119 319 1285 HOH   HOH B . 
G 5 HOH   120 320 23   HOH   HOH B . 
G 5 HOH   121 321 44   HOH   HOH B . 
G 5 HOH   122 322 197  HOH   HOH B . 
G 5 HOH   123 323 177  HOH   HOH B . 
G 5 HOH   124 324 1291 HOH   HOH B . 
G 5 HOH   125 325 704  HOH   HOH B . 
G 5 HOH   126 326 28   HOH   HOH B . 
G 5 HOH   127 327 100  HOH   HOH B . 
G 5 HOH   128 328 29   HOH   HOH B . 
G 5 HOH   129 329 341  HOH   HOH B . 
G 5 HOH   130 330 334  HOH   HOH B . 
G 5 HOH   131 331 55   HOH   HOH B . 
G 5 HOH   132 332 161  HOH   HOH B . 
G 5 HOH   133 333 182  HOH   HOH B . 
G 5 HOH   134 334 445  HOH   HOH B . 
G 5 HOH   135 335 98   HOH   HOH B . 
G 5 HOH   136 336 717  HOH   HOH B . 
G 5 HOH   137 337 1294 HOH   HOH B . 
G 5 HOH   138 338 207  HOH   HOH B . 
G 5 HOH   139 339 234  HOH   HOH B . 
G 5 HOH   140 340 65   HOH   HOH B . 
G 5 HOH   141 341 339  HOH   HOH B . 
G 5 HOH   142 342 1293 HOH   HOH B . 
G 5 HOH   143 343 619  HOH   HOH B . 
G 5 HOH   144 344 362  HOH   HOH B . 
G 5 HOH   145 345 960  HOH   HOH B . 
G 5 HOH   146 346 178  HOH   HOH B . 
G 5 HOH   147 347 90   HOH   HOH B . 
G 5 HOH   148 348 463  HOH   HOH B . 
G 5 HOH   149 349 1304 HOH   HOH B . 
G 5 HOH   150 350 335  HOH   HOH B . 
G 5 HOH   151 351 191  HOH   HOH B . 
G 5 HOH   152 352 623  HOH   HOH B . 
G 5 HOH   153 353 1046 HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 304  HOH   HOH B . 
G 5 HOH   156 356 87   HOH   HOH B . 
G 5 HOH   157 357 203  HOH   HOH B . 
G 5 HOH   158 358 541  HOH   HOH B . 
G 5 HOH   159 359 290  HOH   HOH B . 
G 5 HOH   160 360 479  HOH   HOH B . 
G 5 HOH   161 361 1077 HOH   HOH B . 
G 5 HOH   162 362 389  HOH   HOH B . 
G 5 HOH   163 363 283  HOH   HOH B . 
G 5 HOH   164 364 718  HOH   HOH B . 
G 5 HOH   165 365 1072 HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 1316 HOH   HOH B . 
G 5 HOH   168 368 373  HOH   HOH B . 
G 5 HOH   169 369 615  HOH   HOH B . 
G 5 HOH   170 370 291  HOH   HOH B . 
G 5 HOH   171 371 340  HOH   HOH B . 
G 5 HOH   172 372 1303 HOH   HOH B . 
G 5 HOH   173 373 190  HOH   HOH B . 
G 5 HOH   174 374 667  HOH   HOH B . 
G 5 HOH   175 375 310  HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 431  HOH   HOH B . 
G 5 HOH   178 378 1173 HOH   HOH B . 
G 5 HOH   179 379 1163 HOH   HOH B . 
G 5 HOH   180 380 183  HOH   HOH B . 
G 5 HOH   181 381 418  HOH   HOH B . 
G 5 HOH   182 382 1000 HOH   HOH B . 
G 5 HOH   183 383 176  HOH   HOH B . 
G 5 HOH   184 384 1311 HOH   HOH B . 
G 5 HOH   185 385 424  HOH   HOH B . 
G 5 HOH   186 386 1298 HOH   HOH B . 
G 5 HOH   187 387 491  HOH   HOH B . 
G 5 HOH   188 388 265  HOH   HOH B . 
G 5 HOH   189 389 470  HOH   HOH B . 
G 5 HOH   190 390 248  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 355  HOH   HOH B . 
G 5 HOH   195 395 566  HOH   HOH B . 
G 5 HOH   196 396 274  HOH   HOH B . 
G 5 HOH   197 397 314  HOH   HOH B . 
G 5 HOH   198 398 157  HOH   HOH B . 
G 5 HOH   199 399 792  HOH   HOH B . 
G 5 HOH   200 400 321  HOH   HOH B . 
G 5 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEL 
_cell.length_a           88.809 
_cell.length_b           88.809 
_cell.length_c           39.499 
_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                         7HEL 
_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          7HEL 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.68 
_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                     7HEL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175515 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.049 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.300 
_reflns.B_iso_Wilson_estimate        11.740 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.053 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1079667 
_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 0.980 1.000  ? 26560 7992 ? 1.381 ? ? ? 3.300 ? 0.600  ? ? ? ? ? ? 91.600 1.635 0.848 0.462 
1 2 5.370 44.400 ? 8020  1164 ? 0.025 ? ? ? 6.900 ? 50.500 ? ? ? ? ? ? 99.800 0.028 0.010 0.999 
# 
_refine.entry_id                                 7HEL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3900 
_refine.ls_number_reflns_obs                     175290 
_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                          0.1447 
_refine.ls_R_factor_R_work                       0.1440 
_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                  8463 
_refine.ls_number_reflns_R_work                  166827 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.8412 
_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                            0.1200 
_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                                74.560 
_refine.B_iso_min                                8.790 
_refine.pdbx_overall_phase_error                 17.6700 
_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                       0.9800 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         79 
_refine_hist.number_atoms_solvent             424 
_refine_hist.number_atoms_total               3045 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.83 
_refine_hist.pdbx_B_iso_mean_solvent          30.39 
_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 
0.9800 0.9900  30 87.0000  4851 . 0.4298 0.4309 . 261 0.0000 5112 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 97.0000  5375 . 0.3877 0.3733 . 275 0.0000 5650 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 99.0000  5538 . 0.3443 0.3064 . 279 0.0000 5817 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5580 . 0.2895 0.2704 . 247 0.0000 5827 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5549 . 0.2620 0.2791 . 310 0.0000 5859 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5558 . 0.2259 0.2203 . 290 0.0000 5848 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5532 . 0.2120 0.2309 . 327 0.0000 5859 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5551 . 0.2002 0.2099 . 245 0.0000 5796 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5607 . 0.1813 0.1946 . 284 0.0000 5891 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5578 . 0.1688 0.1874 . 292 0.0000 5870 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5579 . 0.1579 0.1639 . 244 0.0000 5823 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5588 . 0.1466 0.1630 . 272 0.0000 5860 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5581 . 0.1389 0.1649 . 283 0.0000 5864 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5498 . 0.1293 0.1566 . 317 0.0000 5815 . 'X-RAY DIFFRACTION' 
1.2100 1.2400  30 100.0000 5658 . 0.1213 0.1427 . 240 0.0000 5898 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 5545 . 0.1232 0.1444 . 282 0.0000 5827 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5569 . 0.1231 0.1440 . 286 0.0000 5855 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5572 . 0.1250 0.1397 . 303 0.0000 5875 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5591 . 0.1317 0.1501 . 297 0.0000 5888 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5636 . 0.1252 0.1602 . 249 0.0000 5885 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5570 . 0.1239 0.1362 . 302 0.0000 5872 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5586 . 0.1176 0.1267 . 263 0.0000 5849 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5590 . 0.1154 0.1299 . 307 0.0000 5897 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5606 . 0.1187 0.1316 . 277 0.0000 5883 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5627 . 0.1263 0.1447 . 262 0.0000 5889 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5587 . 0.1300 0.1357 . 304 0.0000 5891 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5625 . 0.1336 0.1390 . 283 0.0000 5908 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5620 . 0.1355 0.1337 . 310 0.0000 5930 . 'X-RAY DIFFRACTION' 
2.4200 3.0500  30 100.0000 5682 . 0.1458 0.1701 . 290 0.0000 5972 . 'X-RAY DIFFRACTION' 
3.0500 44.4000 30 100.0000 5798 . 0.1460 0.1689 . 282 0.0000 6080 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEL 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003683' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEL 
_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 5 ? 
G N N 5 ? 
# 
_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 7HEL A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEL 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 7HEL SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEL MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEL SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEL 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,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O ALA A 154 ? O ALA A 154 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HEL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    304 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.31 -133.36 
2 1 SER A 128 ? B 67.75 -0.78   
3 1 HIS B 86  ? ? 57.30 -127.64 
# 
_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 520 ? 5.93 . 
2 1 O B A HOH 521 ? 5.94 . 
3 1 O ? A HOH 522 ? 6.04 . 
4 1 O ? A HOH 523 ? 7.59 . 
5 1 O ? B HOH 401 ? 6.27 . 
# 
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 
A1A9Y O1   O  N N 1   
A1A9Y C1   C  N N 2   
A1A9Y C2   C  Y N 3   
A1A9Y C3   C  Y N 4   
A1A9Y C4   C  Y N 5   
A1A9Y C5   C  Y N 6   
A1A9Y C6   C  N N 7   
A1A9Y C7   C  N R 8   
A1A9Y C8   C  N N 9   
A1A9Y C10  C  Y N 10  
A1A9Y C11  C  Y N 11  
A1A9Y C12  C  Y N 12  
A1A9Y C13  C  Y N 13  
A1A9Y C14  C  Y N 14  
A1A9Y C15  C  Y N 15  
A1A9Y C16  C  Y N 16  
A1A9Y C9   C  Y N 17  
A1A9Y N1   N  N N 18  
A1A9Y N2   N  Y N 19  
A1A9Y N3   N  Y N 20  
A1A9Y N4   N  Y N 21  
A1A9Y H11  H  N N 22  
A1A9Y H2   H  N N 23  
A1A9Y H4   H  N N 24  
A1A9Y H3   H  N N 25  
A1A9Y H5   H  N N 26  
A1A9Y H6   H  N N 27  
A1A9Y H8   H  N N 28  
A1A9Y H7   H  N N 29  
A1A9Y H1   H  N N 30  
A1A9Y H10  H  N N 31  
A1A9Y H9   H  N N 32  
A1A9Y H13  H  N N 33  
A1A9Y H14  H  N N 34  
A1A9Y H15  H  N N 35  
A1A9Y H17  H  N N 36  
A1A9Y H18  H  N N 37  
A1A9Y H12  H  N N 38  
A1A9Y H16  H  N N 39  
A1A9Z N2   N  Y N 40  
A1A9Z C3   C  Y N 41  
A1A9Z C6   C  N N 42  
A1A9Z C9   C  Y N 43  
A1A9Z C12  C  Y N 44  
A1A9Z C14  C  Y N 45  
A1A9Z C1   C  N N 46  
A1A9Z C10  C  Y N 47  
A1A9Z C11  C  Y N 48  
A1A9Z C13  C  Y N 49  
A1A9Z C15  C  Y N 50  
A1A9Z C16  C  Y N 51  
A1A9Z C2   C  Y N 52  
A1A9Z C4   C  Y N 53  
A1A9Z C5   C  Y N 54  
A1A9Z C7   C  N S 55  
A1A9Z C8   C  N N 56  
A1A9Z N1   N  N N 57  
A1A9Z N3   N  Y N 58  
A1A9Z N4   N  Y N 59  
A1A9Z O1   O  N N 60  
A1A9Z H5   H  N N 61  
A1A9Z H7   H  N N 62  
A1A9Z H8   H  N N 63  
A1A9Z H15  H  N N 64  
A1A9Z H3   H  N N 65  
A1A9Z H4   H  N N 66  
A1A9Z H2   H  N N 67  
A1A9Z H13  H  N N 68  
A1A9Z H14  H  N N 69  
A1A9Z H17  H  N N 70  
A1A9Z H18  H  N N 71  
A1A9Z H6   H  N N 72  
A1A9Z H1   H  N N 73  
A1A9Z H10  H  N N 74  
A1A9Z H9   H  N N 75  
A1A9Z H12  H  N N 76  
A1A9Z H16  H  N N 77  
A1A9Z H11  H  N N 78  
ALA   N    N  N N 79  
ALA   CA   C  N S 80  
ALA   C    C  N N 81  
ALA   O    O  N N 82  
ALA   CB   C  N N 83  
ALA   OXT  O  N N 84  
ALA   H    H  N N 85  
ALA   H2   H  N N 86  
ALA   HA   H  N N 87  
ALA   HB1  H  N N 88  
ALA   HB2  H  N N 89  
ALA   HB3  H  N N 90  
ALA   HXT  H  N N 91  
ARG   N    N  N N 92  
ARG   CA   C  N S 93  
ARG   C    C  N N 94  
ARG   O    O  N N 95  
ARG   CB   C  N N 96  
ARG   CG   C  N N 97  
ARG   CD   C  N N 98  
ARG   NE   N  N N 99  
ARG   CZ   C  N N 100 
ARG   NH1  N  N N 101 
ARG   NH2  N  N N 102 
ARG   OXT  O  N N 103 
ARG   H    H  N N 104 
ARG   H2   H  N N 105 
ARG   HA   H  N N 106 
ARG   HB2  H  N N 107 
ARG   HB3  H  N N 108 
ARG   HG2  H  N N 109 
ARG   HG3  H  N N 110 
ARG   HD2  H  N N 111 
ARG   HD3  H  N N 112 
ARG   HE   H  N N 113 
ARG   HH11 H  N N 114 
ARG   HH12 H  N N 115 
ARG   HH21 H  N N 116 
ARG   HH22 H  N N 117 
ARG   HXT  H  N N 118 
ASN   N    N  N N 119 
ASN   CA   C  N S 120 
ASN   C    C  N N 121 
ASN   O    O  N N 122 
ASN   CB   C  N N 123 
ASN   CG   C  N N 124 
ASN   OD1  O  N N 125 
ASN   ND2  N  N N 126 
ASN   OXT  O  N N 127 
ASN   H    H  N N 128 
ASN   H2   H  N N 129 
ASN   HA   H  N N 130 
ASN   HB2  H  N N 131 
ASN   HB3  H  N N 132 
ASN   HD21 H  N N 133 
ASN   HD22 H  N N 134 
ASN   HXT  H  N N 135 
ASP   N    N  N N 136 
ASP   CA   C  N S 137 
ASP   C    C  N N 138 
ASP   O    O  N N 139 
ASP   CB   C  N N 140 
ASP   CG   C  N N 141 
ASP   OD1  O  N N 142 
ASP   OD2  O  N N 143 
ASP   OXT  O  N N 144 
ASP   H    H  N N 145 
ASP   H2   H  N N 146 
ASP   HA   H  N N 147 
ASP   HB2  H  N N 148 
ASP   HB3  H  N N 149 
ASP   HD2  H  N N 150 
ASP   HXT  H  N N 151 
CL    CL   CL N N 152 
CYS   N    N  N N 153 
CYS   CA   C  N R 154 
CYS   C    C  N N 155 
CYS   O    O  N N 156 
CYS   CB   C  N N 157 
CYS   SG   S  N N 158 
CYS   OXT  O  N N 159 
CYS   H    H  N N 160 
CYS   H2   H  N N 161 
CYS   HA   H  N N 162 
CYS   HB2  H  N N 163 
CYS   HB3  H  N N 164 
CYS   HG   H  N N 165 
CYS   HXT  H  N N 166 
GLN   N    N  N N 167 
GLN   CA   C  N S 168 
GLN   C    C  N N 169 
GLN   O    O  N N 170 
GLN   CB   C  N N 171 
GLN   CG   C  N N 172 
GLN   CD   C  N N 173 
GLN   OE1  O  N N 174 
GLN   NE2  N  N N 175 
GLN   OXT  O  N N 176 
GLN   H    H  N N 177 
GLN   H2   H  N N 178 
GLN   HA   H  N N 179 
GLN   HB2  H  N N 180 
GLN   HB3  H  N N 181 
GLN   HG2  H  N N 182 
GLN   HG3  H  N N 183 
GLN   HE21 H  N N 184 
GLN   HE22 H  N N 185 
GLN   HXT  H  N N 186 
GLU   N    N  N N 187 
GLU   CA   C  N S 188 
GLU   C    C  N N 189 
GLU   O    O  N N 190 
GLU   CB   C  N N 191 
GLU   CG   C  N N 192 
GLU   CD   C  N N 193 
GLU   OE1  O  N N 194 
GLU   OE2  O  N N 195 
GLU   OXT  O  N N 196 
GLU   H    H  N N 197 
GLU   H2   H  N N 198 
GLU   HA   H  N N 199 
GLU   HB2  H  N N 200 
GLU   HB3  H  N N 201 
GLU   HG2  H  N N 202 
GLU   HG3  H  N N 203 
GLU   HE2  H  N N 204 
GLU   HXT  H  N N 205 
GLY   N    N  N N 206 
GLY   CA   C  N N 207 
GLY   C    C  N N 208 
GLY   O    O  N N 209 
GLY   OXT  O  N N 210 
GLY   H    H  N N 211 
GLY   H2   H  N N 212 
GLY   HA2  H  N N 213 
GLY   HA3  H  N N 214 
GLY   HXT  H  N N 215 
HIS   N    N  N N 216 
HIS   CA   C  N S 217 
HIS   C    C  N N 218 
HIS   O    O  N N 219 
HIS   CB   C  N N 220 
HIS   CG   C  Y N 221 
HIS   ND1  N  Y N 222 
HIS   CD2  C  Y N 223 
HIS   CE1  C  Y N 224 
HIS   NE2  N  Y N 225 
HIS   OXT  O  N N 226 
HIS   H    H  N N 227 
HIS   H2   H  N N 228 
HIS   HA   H  N N 229 
HIS   HB2  H  N N 230 
HIS   HB3  H  N N 231 
HIS   HD1  H  N N 232 
HIS   HD2  H  N N 233 
HIS   HE1  H  N N 234 
HIS   HE2  H  N N 235 
HIS   HXT  H  N N 236 
HOH   O    O  N N 237 
HOH   H1   H  N N 238 
HOH   H2   H  N N 239 
ILE   N    N  N N 240 
ILE   CA   C  N S 241 
ILE   C    C  N N 242 
ILE   O    O  N N 243 
ILE   CB   C  N S 244 
ILE   CG1  C  N N 245 
ILE   CG2  C  N N 246 
ILE   CD1  C  N N 247 
ILE   OXT  O  N N 248 
ILE   H    H  N N 249 
ILE   H2   H  N N 250 
ILE   HA   H  N N 251 
ILE   HB   H  N N 252 
ILE   HG12 H  N N 253 
ILE   HG13 H  N N 254 
ILE   HG21 H  N N 255 
ILE   HG22 H  N N 256 
ILE   HG23 H  N N 257 
ILE   HD11 H  N N 258 
ILE   HD12 H  N N 259 
ILE   HD13 H  N N 260 
ILE   HXT  H  N N 261 
LEU   N    N  N N 262 
LEU   CA   C  N S 263 
LEU   C    C  N N 264 
LEU   O    O  N N 265 
LEU   CB   C  N N 266 
LEU   CG   C  N N 267 
LEU   CD1  C  N N 268 
LEU   CD2  C  N N 269 
LEU   OXT  O  N N 270 
LEU   H    H  N N 271 
LEU   H2   H  N N 272 
LEU   HA   H  N N 273 
LEU   HB2  H  N N 274 
LEU   HB3  H  N N 275 
LEU   HG   H  N N 276 
LEU   HD11 H  N N 277 
LEU   HD12 H  N N 278 
LEU   HD13 H  N N 279 
LEU   HD21 H  N N 280 
LEU   HD22 H  N N 281 
LEU   HD23 H  N N 282 
LEU   HXT  H  N N 283 
LYS   N    N  N N 284 
LYS   CA   C  N S 285 
LYS   C    C  N N 286 
LYS   O    O  N N 287 
LYS   CB   C  N N 288 
LYS   CG   C  N N 289 
LYS   CD   C  N N 290 
LYS   CE   C  N N 291 
LYS   NZ   N  N N 292 
LYS   OXT  O  N N 293 
LYS   H    H  N N 294 
LYS   H2   H  N N 295 
LYS   HA   H  N N 296 
LYS   HB2  H  N N 297 
LYS   HB3  H  N N 298 
LYS   HG2  H  N N 299 
LYS   HG3  H  N N 300 
LYS   HD2  H  N N 301 
LYS   HD3  H  N N 302 
LYS   HE2  H  N N 303 
LYS   HE3  H  N N 304 
LYS   HZ1  H  N N 305 
LYS   HZ2  H  N N 306 
LYS   HZ3  H  N N 307 
LYS   HXT  H  N N 308 
MET   N    N  N N 309 
MET   CA   C  N S 310 
MET   C    C  N N 311 
MET   O    O  N N 312 
MET   CB   C  N N 313 
MET   CG   C  N N 314 
MET   SD   S  N N 315 
MET   CE   C  N N 316 
MET   OXT  O  N N 317 
MET   H    H  N N 318 
MET   H2   H  N N 319 
MET   HA   H  N N 320 
MET   HB2  H  N N 321 
MET   HB3  H  N N 322 
MET   HG2  H  N N 323 
MET   HG3  H  N N 324 
MET   HE1  H  N N 325 
MET   HE2  H  N N 326 
MET   HE3  H  N N 327 
MET   HXT  H  N N 328 
PHE   N    N  N N 329 
PHE   CA   C  N S 330 
PHE   C    C  N N 331 
PHE   O    O  N N 332 
PHE   CB   C  N N 333 
PHE   CG   C  Y N 334 
PHE   CD1  C  Y N 335 
PHE   CD2  C  Y N 336 
PHE   CE1  C  Y N 337 
PHE   CE2  C  Y N 338 
PHE   CZ   C  Y N 339 
PHE   OXT  O  N N 340 
PHE   H    H  N N 341 
PHE   H2   H  N N 342 
PHE   HA   H  N N 343 
PHE   HB2  H  N N 344 
PHE   HB3  H  N N 345 
PHE   HD1  H  N N 346 
PHE   HD2  H  N N 347 
PHE   HE1  H  N N 348 
PHE   HE2  H  N N 349 
PHE   HZ   H  N N 350 
PHE   HXT  H  N N 351 
PRO   N    N  N N 352 
PRO   CA   C  N S 353 
PRO   C    C  N N 354 
PRO   O    O  N N 355 
PRO   CB   C  N N 356 
PRO   CG   C  N N 357 
PRO   CD   C  N N 358 
PRO   OXT  O  N N 359 
PRO   H    H  N N 360 
PRO   HA   H  N N 361 
PRO   HB2  H  N N 362 
PRO   HB3  H  N N 363 
PRO   HG2  H  N N 364 
PRO   HG3  H  N N 365 
PRO   HD2  H  N N 366 
PRO   HD3  H  N N 367 
PRO   HXT  H  N N 368 
SER   N    N  N N 369 
SER   CA   C  N S 370 
SER   C    C  N N 371 
SER   O    O  N N 372 
SER   CB   C  N N 373 
SER   OG   O  N N 374 
SER   OXT  O  N N 375 
SER   H    H  N N 376 
SER   H2   H  N N 377 
SER   HA   H  N N 378 
SER   HB2  H  N N 379 
SER   HB3  H  N N 380 
SER   HG   H  N N 381 
SER   HXT  H  N N 382 
THR   N    N  N N 383 
THR   CA   C  N S 384 
THR   C    C  N N 385 
THR   O    O  N N 386 
THR   CB   C  N R 387 
THR   OG1  O  N N 388 
THR   CG2  C  N N 389 
THR   OXT  O  N N 390 
THR   H    H  N N 391 
THR   H2   H  N N 392 
THR   HA   H  N N 393 
THR   HB   H  N N 394 
THR   HG1  H  N N 395 
THR   HG21 H  N N 396 
THR   HG22 H  N N 397 
THR   HG23 H  N N 398 
THR   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
# 
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 
A1A9Y C1  C2   sing N N 1   
A1A9Y C3  C2   doub Y N 2   
A1A9Y C3  C4   sing Y N 3   
A1A9Y C2  C16  sing Y N 4   
A1A9Y C4  C5   doub Y N 5   
A1A9Y C16 C15  doub Y N 6   
A1A9Y C5  C15  sing Y N 7   
A1A9Y C5  C6   sing N N 8   
A1A9Y O1  C8   sing N N 9   
A1A9Y C6  C7   sing N N 10  
A1A9Y C7  C8   sing N N 11  
A1A9Y C7  N1   sing N N 12  
A1A9Y N1  C9   sing N N 13  
A1A9Y C9  C12  doub Y N 14  
A1A9Y C9  N2   sing Y N 15  
A1A9Y C13 C12  sing Y N 16  
A1A9Y C13 C14  doub Y N 17  
A1A9Y C12 C11  sing Y N 18  
A1A9Y N2  C10  doub Y N 19  
A1A9Y C14 N4   sing Y N 20  
A1A9Y C10 N3   sing Y N 21  
A1A9Y C11 N4   sing Y N 22  
A1A9Y C11 N3   doub Y N 23  
A1A9Y O1  H11  sing N N 24  
A1A9Y C1  H2   sing N N 25  
A1A9Y C1  H4   sing N N 26  
A1A9Y C1  H3   sing N N 27  
A1A9Y C3  H5   sing N N 28  
A1A9Y C4  H6   sing N N 29  
A1A9Y C6  H8   sing N N 30  
A1A9Y C6  H7   sing N N 31  
A1A9Y C7  H1   sing N N 32  
A1A9Y C8  H10  sing N N 33  
A1A9Y C8  H9   sing N N 34  
A1A9Y C10 H13  sing N N 35  
A1A9Y C13 H14  sing N N 36  
A1A9Y C14 H15  sing N N 37  
A1A9Y C15 H17  sing N N 38  
A1A9Y C16 H18  sing N N 39  
A1A9Y N1  H12  sing N N 40  
A1A9Y N4  H16  sing N N 41  
A1A9Z C3  C4   doub Y N 42  
A1A9Z C3  C2   sing Y N 43  
A1A9Z C1  C2   sing N N 44  
A1A9Z C4  C5   sing Y N 45  
A1A9Z C2  C16  doub Y N 46  
A1A9Z C5  C6   sing N N 47  
A1A9Z C5  C15  doub Y N 48  
A1A9Z C16 C15  sing Y N 49  
A1A9Z C6  C7   sing N N 50  
A1A9Z O1  C8   sing N N 51  
A1A9Z C8  C7   sing N N 52  
A1A9Z C7  N1   sing N N 53  
A1A9Z N1  C9   sing N N 54  
A1A9Z C9  C12  doub Y N 55  
A1A9Z C9  N2   sing Y N 56  
A1A9Z C13 C12  sing Y N 57  
A1A9Z C13 C14  doub Y N 58  
A1A9Z C12 C11  sing Y N 59  
A1A9Z N2  C10  doub Y N 60  
A1A9Z C14 N4   sing Y N 61  
A1A9Z C11 N4   sing Y N 62  
A1A9Z C11 N3   doub Y N 63  
A1A9Z C10 N3   sing Y N 64  
A1A9Z C3  H5   sing N N 65  
A1A9Z C6  H7   sing N N 66  
A1A9Z C6  H8   sing N N 67  
A1A9Z C14 H15  sing N N 68  
A1A9Z C1  H3   sing N N 69  
A1A9Z C1  H4   sing N N 70  
A1A9Z C1  H2   sing N N 71  
A1A9Z C10 H13  sing N N 72  
A1A9Z C13 H14  sing N N 73  
A1A9Z C15 H17  sing N N 74  
A1A9Z C16 H18  sing N N 75  
A1A9Z C4  H6   sing N N 76  
A1A9Z C7  H1   sing N N 77  
A1A9Z C8  H10  sing N N 78  
A1A9Z C8  H9   sing N N 79  
A1A9Z N1  H12  sing N N 80  
A1A9Z N4  H16  sing N N 81  
A1A9Z O1  H11  sing N N 82  
ALA   N   CA   sing N N 83  
ALA   N   H    sing N N 84  
ALA   N   H2   sing N N 85  
ALA   CA  C    sing N N 86  
ALA   CA  CB   sing N N 87  
ALA   CA  HA   sing N N 88  
ALA   C   O    doub N N 89  
ALA   C   OXT  sing N N 90  
ALA   CB  HB1  sing N N 91  
ALA   CB  HB2  sing N N 92  
ALA   CB  HB3  sing N N 93  
ALA   OXT HXT  sing N N 94  
ARG   N   CA   sing N N 95  
ARG   N   H    sing N N 96  
ARG   N   H2   sing N N 97  
ARG   CA  C    sing N N 98  
ARG   CA  CB   sing N N 99  
ARG   CA  HA   sing N N 100 
ARG   C   O    doub N N 101 
ARG   C   OXT  sing N N 102 
ARG   CB  CG   sing N N 103 
ARG   CB  HB2  sing N N 104 
ARG   CB  HB3  sing N N 105 
ARG   CG  CD   sing N N 106 
ARG   CG  HG2  sing N N 107 
ARG   CG  HG3  sing N N 108 
ARG   CD  NE   sing N N 109 
ARG   CD  HD2  sing N N 110 
ARG   CD  HD3  sing N N 111 
ARG   NE  CZ   sing N N 112 
ARG   NE  HE   sing N N 113 
ARG   CZ  NH1  sing N N 114 
ARG   CZ  NH2  doub N N 115 
ARG   NH1 HH11 sing N N 116 
ARG   NH1 HH12 sing N N 117 
ARG   NH2 HH21 sing N N 118 
ARG   NH2 HH22 sing N N 119 
ARG   OXT HXT  sing N N 120 
ASN   N   CA   sing N N 121 
ASN   N   H    sing N N 122 
ASN   N   H2   sing N N 123 
ASN   CA  C    sing N N 124 
ASN   CA  CB   sing N N 125 
ASN   CA  HA   sing N N 126 
ASN   C   O    doub N N 127 
ASN   C   OXT  sing N N 128 
ASN   CB  CG   sing N N 129 
ASN   CB  HB2  sing N N 130 
ASN   CB  HB3  sing N N 131 
ASN   CG  OD1  doub N N 132 
ASN   CG  ND2  sing N N 133 
ASN   ND2 HD21 sing N N 134 
ASN   ND2 HD22 sing N N 135 
ASN   OXT HXT  sing N N 136 
ASP   N   CA   sing N N 137 
ASP   N   H    sing N N 138 
ASP   N   H2   sing N N 139 
ASP   CA  C    sing N N 140 
ASP   CA  CB   sing N N 141 
ASP   CA  HA   sing N N 142 
ASP   C   O    doub N N 143 
ASP   C   OXT  sing N N 144 
ASP   CB  CG   sing N N 145 
ASP   CB  HB2  sing N N 146 
ASP   CB  HB3  sing N N 147 
ASP   CG  OD1  doub N N 148 
ASP   CG  OD2  sing N N 149 
ASP   OD2 HD2  sing N N 150 
ASP   OXT HXT  sing N N 151 
CYS   N   CA   sing N N 152 
CYS   N   H    sing N N 153 
CYS   N   H2   sing N N 154 
CYS   CA  C    sing N N 155 
CYS   CA  CB   sing N N 156 
CYS   CA  HA   sing N N 157 
CYS   C   O    doub N N 158 
CYS   C   OXT  sing N N 159 
CYS   CB  SG   sing N N 160 
CYS   CB  HB2  sing N N 161 
CYS   CB  HB3  sing N N 162 
CYS   SG  HG   sing N N 163 
CYS   OXT HXT  sing N N 164 
GLN   N   CA   sing N N 165 
GLN   N   H    sing N N 166 
GLN   N   H2   sing N N 167 
GLN   CA  C    sing N N 168 
GLN   CA  CB   sing N N 169 
GLN   CA  HA   sing N N 170 
GLN   C   O    doub N N 171 
GLN   C   OXT  sing N N 172 
GLN   CB  CG   sing N N 173 
GLN   CB  HB2  sing N N 174 
GLN   CB  HB3  sing N N 175 
GLN   CG  CD   sing N N 176 
GLN   CG  HG2  sing N N 177 
GLN   CG  HG3  sing N N 178 
GLN   CD  OE1  doub N N 179 
GLN   CD  NE2  sing N N 180 
GLN   NE2 HE21 sing N N 181 
GLN   NE2 HE22 sing N N 182 
GLN   OXT HXT  sing N N 183 
GLU   N   CA   sing N N 184 
GLU   N   H    sing N N 185 
GLU   N   H2   sing N N 186 
GLU   CA  C    sing N N 187 
GLU   CA  CB   sing N N 188 
GLU   CA  HA   sing N N 189 
GLU   C   O    doub N N 190 
GLU   C   OXT  sing N N 191 
GLU   CB  CG   sing N N 192 
GLU   CB  HB2  sing N N 193 
GLU   CB  HB3  sing N N 194 
GLU   CG  CD   sing N N 195 
GLU   CG  HG2  sing N N 196 
GLU   CG  HG3  sing N N 197 
GLU   CD  OE1  doub N N 198 
GLU   CD  OE2  sing N N 199 
GLU   OE2 HE2  sing N N 200 
GLU   OXT HXT  sing N N 201 
GLY   N   CA   sing N N 202 
GLY   N   H    sing N N 203 
GLY   N   H2   sing N N 204 
GLY   CA  C    sing N N 205 
GLY   CA  HA2  sing N N 206 
GLY   CA  HA3  sing N N 207 
GLY   C   O    doub N N 208 
GLY   C   OXT  sing N N 209 
GLY   OXT HXT  sing N N 210 
HIS   N   CA   sing N N 211 
HIS   N   H    sing N N 212 
HIS   N   H2   sing N N 213 
HIS   CA  C    sing N N 214 
HIS   CA  CB   sing N N 215 
HIS   CA  HA   sing N N 216 
HIS   C   O    doub N N 217 
HIS   C   OXT  sing N N 218 
HIS   CB  CG   sing N N 219 
HIS   CB  HB2  sing N N 220 
HIS   CB  HB3  sing N N 221 
HIS   CG  ND1  sing Y N 222 
HIS   CG  CD2  doub Y N 223 
HIS   ND1 CE1  doub Y N 224 
HIS   ND1 HD1  sing N N 225 
HIS   CD2 NE2  sing Y N 226 
HIS   CD2 HD2  sing N N 227 
HIS   CE1 NE2  sing Y N 228 
HIS   CE1 HE1  sing N N 229 
HIS   NE2 HE2  sing N N 230 
HIS   OXT HXT  sing N N 231 
HOH   O   H1   sing N N 232 
HOH   O   H2   sing N N 233 
ILE   N   CA   sing N N 234 
ILE   N   H    sing N N 235 
ILE   N   H2   sing N N 236 
ILE   CA  C    sing N N 237 
ILE   CA  CB   sing N N 238 
ILE   CA  HA   sing N N 239 
ILE   C   O    doub N N 240 
ILE   C   OXT  sing N N 241 
ILE   CB  CG1  sing N N 242 
ILE   CB  CG2  sing N N 243 
ILE   CB  HB   sing N N 244 
ILE   CG1 CD1  sing N N 245 
ILE   CG1 HG12 sing N N 246 
ILE   CG1 HG13 sing N N 247 
ILE   CG2 HG21 sing N N 248 
ILE   CG2 HG22 sing N N 249 
ILE   CG2 HG23 sing N N 250 
ILE   CD1 HD11 sing N N 251 
ILE   CD1 HD12 sing N N 252 
ILE   CD1 HD13 sing N N 253 
ILE   OXT HXT  sing N N 254 
LEU   N   CA   sing N N 255 
LEU   N   H    sing N N 256 
LEU   N   H2   sing N N 257 
LEU   CA  C    sing N N 258 
LEU   CA  CB   sing N N 259 
LEU   CA  HA   sing N N 260 
LEU   C   O    doub N N 261 
LEU   C   OXT  sing N N 262 
LEU   CB  CG   sing N N 263 
LEU   CB  HB2  sing N N 264 
LEU   CB  HB3  sing N N 265 
LEU   CG  CD1  sing N N 266 
LEU   CG  CD2  sing N N 267 
LEU   CG  HG   sing N N 268 
LEU   CD1 HD11 sing N N 269 
LEU   CD1 HD12 sing N N 270 
LEU   CD1 HD13 sing N N 271 
LEU   CD2 HD21 sing N N 272 
LEU   CD2 HD22 sing N N 273 
LEU   CD2 HD23 sing N N 274 
LEU   OXT HXT  sing N N 275 
LYS   N   CA   sing N N 276 
LYS   N   H    sing N N 277 
LYS   N   H2   sing N N 278 
LYS   CA  C    sing N N 279 
LYS   CA  CB   sing N N 280 
LYS   CA  HA   sing N N 281 
LYS   C   O    doub N N 282 
LYS   C   OXT  sing N N 283 
LYS   CB  CG   sing N N 284 
LYS   CB  HB2  sing N N 285 
LYS   CB  HB3  sing N N 286 
LYS   CG  CD   sing N N 287 
LYS   CG  HG2  sing N N 288 
LYS   CG  HG3  sing N N 289 
LYS   CD  CE   sing N N 290 
LYS   CD  HD2  sing N N 291 
LYS   CD  HD3  sing N N 292 
LYS   CE  NZ   sing N N 293 
LYS   CE  HE2  sing N N 294 
LYS   CE  HE3  sing N N 295 
LYS   NZ  HZ1  sing N N 296 
LYS   NZ  HZ2  sing N N 297 
LYS   NZ  HZ3  sing N N 298 
LYS   OXT HXT  sing N N 299 
MET   N   CA   sing N N 300 
MET   N   H    sing N N 301 
MET   N   H2   sing N N 302 
MET   CA  C    sing N N 303 
MET   CA  CB   sing N N 304 
MET   CA  HA   sing N N 305 
MET   C   O    doub N N 306 
MET   C   OXT  sing N N 307 
MET   CB  CG   sing N N 308 
MET   CB  HB2  sing N N 309 
MET   CB  HB3  sing N N 310 
MET   CG  SD   sing N N 311 
MET   CG  HG2  sing N N 312 
MET   CG  HG3  sing N N 313 
MET   SD  CE   sing N N 314 
MET   CE  HE1  sing N N 315 
MET   CE  HE2  sing N N 316 
MET   CE  HE3  sing N N 317 
MET   OXT HXT  sing N N 318 
PHE   N   CA   sing N N 319 
PHE   N   H    sing N N 320 
PHE   N   H2   sing N N 321 
PHE   CA  C    sing N N 322 
PHE   CA  CB   sing N N 323 
PHE   CA  HA   sing N N 324 
PHE   C   O    doub N N 325 
PHE   C   OXT  sing N N 326 
PHE   CB  CG   sing N N 327 
PHE   CB  HB2  sing N N 328 
PHE   CB  HB3  sing N N 329 
PHE   CG  CD1  doub Y N 330 
PHE   CG  CD2  sing Y N 331 
PHE   CD1 CE1  sing Y N 332 
PHE   CD1 HD1  sing N N 333 
PHE   CD2 CE2  doub Y N 334 
PHE   CD2 HD2  sing N N 335 
PHE   CE1 CZ   doub Y N 336 
PHE   CE1 HE1  sing N N 337 
PHE   CE2 CZ   sing Y N 338 
PHE   CE2 HE2  sing N N 339 
PHE   CZ  HZ   sing N N 340 
PHE   OXT HXT  sing N N 341 
PRO   N   CA   sing N N 342 
PRO   N   CD   sing N N 343 
PRO   N   H    sing N N 344 
PRO   CA  C    sing N N 345 
PRO   CA  CB   sing N N 346 
PRO   CA  HA   sing N N 347 
PRO   C   O    doub N N 348 
PRO   C   OXT  sing N N 349 
PRO   CB  CG   sing N N 350 
PRO   CB  HB2  sing N N 351 
PRO   CB  HB3  sing N N 352 
PRO   CG  CD   sing N N 353 
PRO   CG  HG2  sing N N 354 
PRO   CG  HG3  sing N N 355 
PRO   CD  HD2  sing N N 356 
PRO   CD  HD3  sing N N 357 
PRO   OXT HXT  sing N N 358 
SER   N   CA   sing N N 359 
SER   N   H    sing N N 360 
SER   N   H2   sing N N 361 
SER   CA  C    sing N N 362 
SER   CA  CB   sing N N 363 
SER   CA  HA   sing N N 364 
SER   C   O    doub N N 365 
SER   C   OXT  sing N N 366 
SER   CB  OG   sing N N 367 
SER   CB  HB2  sing N N 368 
SER   CB  HB3  sing N N 369 
SER   OG  HG   sing N N 370 
SER   OXT HXT  sing N N 371 
THR   N   CA   sing N N 372 
THR   N   H    sing N N 373 
THR   N   H2   sing N N 374 
THR   CA  C    sing N N 375 
THR   CA  CB   sing N N 376 
THR   CA  HA   sing N N 377 
THR   C   O    doub N N 378 
THR   C   OXT  sing N N 379 
THR   CB  OG1  sing N N 380 
THR   CB  CG2  sing N N 381 
THR   CB  HB   sing N N 382 
THR   OG1 HG1  sing N N 383 
THR   CG2 HG21 sing N N 384 
THR   CG2 HG22 sing N N 385 
THR   CG2 HG23 sing N N 386 
THR   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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                    7HEL 
_atom_sites.fract_transf_matrix[1][1]   0.011260 
_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]   0.011260 
_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]   0.025317 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.726 -16.188 22.230  0.50 54.56 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.649 -16.153 22.338  0.50 54.67 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.750 -15.118 22.401  0.50 54.27 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.695 -15.064 22.507  0.50 54.35 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.393 -13.767 22.103  0.50 52.96 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.352 -13.728 22.176  0.50 53.01 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.502 -13.485 22.556  0.50 53.41 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.436 -13.422 22.672  0.50 53.48 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.128 -15.149 23.813  0.50 54.96 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.098 -15.056 23.929  0.50 55.05 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.096 -14.039 23.966  0.50 55.13 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.112 -13.907 24.088  0.50 55.22 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.498 -16.508 24.087  0.50 55.12 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.426 -16.388 24.232  0.50 55.22 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.032 -15.246 21.766  0.50 65.13 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.962 -15.191 21.888  0.50 65.24 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.824 -15.004 24.472  0.50 65.96 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.812 -14.929 24.573  0.50 66.07 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.600 -14.182 24.788  0.50 66.17 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.610 -14.034 24.908  0.50 66.28 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.552 -13.184 24.002  0.50 66.17 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.602 -13.071 24.129  0.50 66.28 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.492 -14.063 23.208  0.50 66.17 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.508 -13.902 23.329  0.50 66.28 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.048 -16.480 24.946  0.50 66.16 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.003 -16.337 25.104  0.50 66.28 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.859 -16.706 23.385  0.50 66.16 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.759 -16.567 23.551  0.50 66.28 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.195 -17.183 24.100  0.50 66.16 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.097 -17.088 24.232  0.50 66.28 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.692 -12.940 21.328  1.00 50.91 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.145 -11.597 20.986  1.00 46.40 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 18.023 -10.600 21.267  1.00 41.68 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.906 -10.976 21.634  1.00 41.76 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.666 -11.511 19.541  1.00 46.13 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.630 -11.913 18.518  1.00 45.60 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.503 -11.417 18.528  1.00 45.45 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.008 -12.820 17.621  1.00 45.52 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.931 -13.144 20.981  0.50 61.10 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.964 -13.170 20.931  0.50 61.10 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.886 -11.369 21.559  1.00 55.69 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.934 -10.596 19.355  1.00 55.37 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.430 -12.103 19.444  1.00 55.37 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.459 -13.082 17.014  1.00 54.63 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.805 -13.146 17.647  1.00 54.63 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.309 -9.314  21.065  0.50 38.86 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.347 -9.317  21.107  0.50 39.15 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.391 -8.246  21.444  0.50 35.80 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.473 -8.225  21.513  0.50 36.40 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.528 -7.745  20.287  0.50 32.20 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.600 -7.705  20.379  0.50 33.04 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.924 -6.673  20.402  0.50 32.43 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.887 -6.714  20.571  0.50 33.21 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.157 -7.076  22.065  0.50 36.37 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.300 -7.081  22.110  0.50 37.08 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.127 -6.566  21.167  0.50 36.59 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.175 -6.523  21.146  0.50 37.34 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 19.035 -9.035  20.699  0.50 46.64 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 19.080 -9.051  20.747  0.50 46.99 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.798 -8.590  22.132  0.50 42.97 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.884 -8.544  22.210  0.50 43.69 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.528 -6.367  22.282  0.50 43.66 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.699 -6.389  22.430  0.50 44.51 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.600 -7.380  22.872  0.50 43.66 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.827 -7.426  22.851  0.50 44.51 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.540 -5.926  21.525  0.50 43.92 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.621 -5.898  21.490  0.50 44.82 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.455 -8.481  19.181  0.50 28.01 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.640 -8.336  19.209  0.50 29.20 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.573 -8.102  18.084  0.50 23.90 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.689 -8.012  18.154  0.50 25.56 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.131 -8.450  18.434  0.50 23.08 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.298 -8.431  18.604  0.50 25.43 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.857 -9.508  19.005  0.50 24.03 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 14.066 -9.608  18.896  0.50 25.86 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.995 -8.806  16.795  0.50 21.59 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 16.057 -8.750  16.872  0.50 23.19 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.259 -8.253  16.191  0.50 19.67 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.353 -8.301  16.260  0.50 21.19 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.243 -7.054  15.496  0.50 18.88 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.408 -7.154  15.487  0.50 20.41 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.458 -8.933  16.318  0.50 19.52 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.513 -9.036  16.447  0.50 20.99 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.402 -6.543  14.941  0.50 18.71 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.599 -6.741  14.917  0.50 20.14 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.618 -8.428  15.763  0.50 19.17 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.706 -8.629  15.878  0.50 20.59 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.590 -7.231  15.073  0.50 18.85 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.749 -7.479  15.112  0.50 20.21 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.904 -9.202  19.043  0.50 33.63 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 17.204 -8.953  19.006  0.50 35.05 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.624 -7.150  17.945  0.50 28.70 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.692 -7.059  17.990  0.50 30.68 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.144 -9.747  16.986  0.50 25.93 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 16.131 -9.698  17.072  0.50 27.84 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.286 -8.714  16.140  0.50 25.93 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.352 -8.607  16.223  0.50 27.84 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.443 -6.586  15.404  0.50 22.67 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.636 -6.654  15.353  0.50 24.50 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.482 -9.739  16.783  0.50 23.44 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.488 -9.810  16.964  0.50 25.20 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.380 -5.736  14.476  0.50 22.47 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.625 -5.968  14.401  0.50 24.18 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.418 -8.892  15.857  0.50 23.02 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.480 -9.127  16.012  0.50 24.72 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.369 -6.887  14.702  0.50 22.63 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.551 -7.203  14.728  0.50 24.27 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.204 -7.550  18.096  0.50 21.21 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.371 -7.479  18.659  0.50 24.81 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.826 -7.639  18.566  0.50 20.45 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 12.036 -7.729  19.181  0.50 24.59 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.839 -7.397  17.431  0.50 18.38 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 10.994 -7.412  18.118  0.50 22.38 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 11.045 -6.516  16.593  0.50 17.68 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 11.127 -6.438  17.372  0.50 22.35 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.585 -6.607  19.678  0.50 21.82 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.776 -6.894  20.440  0.50 26.25 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.254 -6.659  20.158  0.50 22.76 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 10.663 -7.393  21.161  0.50 27.52 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.354 -6.873  17.590  0.50 25.46 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.492 -6.671  18.389  0.50 29.78 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.662 -8.524  18.928  0.50 24.55 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.948 -8.664  19.419  0.50 29.53 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.194 -6.791  20.411  0.50 26.20 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 12.565 -6.924  21.008  0.50 31.52 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.754 -5.721  19.324  0.50 26.20 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 11.591 -5.979  20.182  0.50 31.52 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.149 -6.091  20.769  0.50 27.33 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.539 -6.936  21.855  0.50 33.04 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.759  -8.181  17.410  0.50 17.19 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 9.966  -8.251  18.042  0.50 20.49 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.674  -7.939  16.477  0.50 16.07 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.855  -8.004  17.152  0.50 18.86 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.877  -8.465  15.073  0.50 15.16 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 9.025  -8.486  15.732  0.50 17.30 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.166  -8.041  14.157  0.50 15.18 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.186  -8.157  14.885  0.50 17.24 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.637  -8.859  17.927  0.50 20.64 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.899  -8.975  18.497  0.50 24.60 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.860  -8.328  16.843  0.50 19.30 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 8.070  -8.440  17.505  0.50 22.64 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.533  -6.982  16.408  0.50 19.30 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.685  -7.051  17.120  0.50 22.64 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.822  -9.378  14.870  0.50 14.00 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.069 -9.255  15.437  0.50 16.10 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.091 -9.936  13.553  0.50 12.90 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.272 -9.741  14.081  0.50 15.01 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.213  -11.151 13.280  0.50 12.73 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.415  -10.971 13.810  0.50 13.81 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 8.871  -11.918 14.184  0.50 14.36 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 9.184  -11.799 14.698  0.50 14.94 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.564 -10.350 13.434  0.50 13.11 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.750 -10.068 13.841  0.50 15.33 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.511 -9.181  13.301  0.50 13.78 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.601 -8.837  13.605  0.50 15.11 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.872 -8.426  14.409  0.50 14.26 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 12.889 -7.963  14.642  0.50 15.44 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 13.029 -8.822  12.065  0.50 14.17 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.097 -8.542  12.342  0.50 14.80 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.724 -7.342  14.292  0.50 15.07 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.649 -6.832  14.431  0.50 15.31 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.881 -7.744  11.936  0.50 14.47 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.863 -7.411  12.120  0.50 14.77 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.224 -7.007  13.051  0.50 15.47 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.132 -6.563  13.168  0.50 15.17 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 15.072 -5.935  12.921  0.50 16.52 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 14.883 -5.436  12.947  0.50 15.64 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.321 -9.696  15.488  0.50 16.81 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.677 -9.505  16.001  0.50 19.34 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.906  -9.271  12.873  0.50 15.49 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 10.019 -9.044  13.457  0.50 18.03 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.819 -10.854 14.222  0.50 15.74 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 12.106 -10.536 14.612  0.50 18.41 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.661 -10.900 12.643  0.50 15.74 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.817 -10.631 13.052  0.50 18.41 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.526 -8.651  15.245  0.50 17.12 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.562 -8.142  15.493  0.50 18.54 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.798 -9.318  11.310  0.50 17.02 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.915 -9.114  11.632  0.50 17.78 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.959 -6.849  15.044  0.50 18.10 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 13.838 -6.255  15.135  0.50 18.39 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.228 -7.521  11.103  0.50 17.38 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.194 -7.224  11.269  0.50 17.74 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.207 -5.585  13.672  0.50 19.84 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 14.984 -5.004  13.660  0.50 18.78 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.858  -11.323 12.009  0.50 11.94 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 8.935  -11.071 12.573  0.50 13.02 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.250  -12.556 11.529  0.50 11.38 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.273  -12.267 12.076  0.50 13.35 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.361  -13.497 11.076  0.50 11.40 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.339  -13.235 11.577  0.50 12.65 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.290 -13.076 10.379  0.50 11.24 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.244 -12.842 10.836  0.50 12.52 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.322  -12.248 10.355  0.50 11.94 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.334  -11.894 10.929  0.50 13.99 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.630  -13.447 9.709   0.50 13.78 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.542  -13.031 10.284  0.50 14.84 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.580  -14.021 10.640  0.50 14.66 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.563  -13.643 11.274  0.50 15.90 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 6.019  -13.041 8.388   0.50 14.44 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 5.818  -12.508 9.054   0.50 16.15 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.966  -10.733 11.389  0.50 14.34 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 8.979  -10.429 11.993  0.50 15.64 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.741  -12.983 12.236  0.50 13.67 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.762  -12.679 12.789  0.50 16.03 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.623  -11.652 10.667  0.50 14.35 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.689  -11.248 11.260  0.50 16.80 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.837  -11.810 9.663   0.50 14.35 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.865  -11.481 10.229  0.50 16.80 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.285  -14.144 9.533   0.50 16.55 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 7.158  -13.725 10.001  0.50 17.82 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.184  -14.804 10.228  0.50 17.60 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 5.105  -14.384 10.846  0.50 19.10 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 6.001  -14.267 11.480  0.50 17.60 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.051  -13.961 12.050  0.50 19.10 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.899  -13.348 10.799  0.50 17.60 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 4.921  -12.968 11.541  0.50 19.10 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.576  -13.810 8.001   0.50 17.34 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 5.286  -13.224 8.675   0.50 19.39 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.380  -12.332 8.549   0.50 17.34 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 5.244  -11.771 9.317   0.50 19.39 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.725  -12.731 7.802   0.50 17.34 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.473  -12.203 8.408   0.50 19.39 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.264  -14.766 11.468  0.50 11.31 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.241  -14.490 11.991  0.50 13.26 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.267 -15.770 11.134  0.50 11.62 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.203 -15.496 11.568  0.50 13.14 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.916  -16.375 9.781   0.50 11.98 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.808  -16.024 10.197  0.50 12.25 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.861  -16.998 9.639   0.50 13.55 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.669  -16.460 9.997   0.50 12.67 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.288 -16.840 12.228  0.50 11.78 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.238 -16.634 12.585  0.50 13.69 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.377 -17.909 12.121  0.50 12.08 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.191 -17.764 12.242  0.50 14.11 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.457 -18.715 13.429  0.50 11.94 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.241 -18.785 13.371  0.50 14.92 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.475 -19.853 13.374  0.50 11.90 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.233 -19.908 13.091  0.50 15.26 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.854 -19.367 13.095  0.50 11.84 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.640 -19.418 12.981  0.50 15.44 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.606  -15.074 11.931  0.50 13.58 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.617  -14.777 12.505  0.50 15.93 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.136 -15.361 11.073  0.50 13.96 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 11.082 -15.093 11.505  0.50 15.78 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.409 -16.395 13.080  0.50 14.14 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.508 -16.267 13.441  0.50 16.44 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.435  -17.301 12.226  0.50 14.14 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.347  -17.006 12.655  0.50 16.44 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 11.166 -18.523 11.398  0.50 14.51 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 10.884 -18.211 11.437  0.50 16.95 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.238 -17.490 11.969  0.50 14.51 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 12.082 -17.405 12.110  0.50 16.95 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.710 -18.121 14.151  0.50 14.35 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.509 -18.338 14.189  0.50 17.92 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.586 -19.106 13.612  0.50 14.35 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.360 -19.178 13.481  0.50 17.92 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.487 -20.311 14.229  0.50 14.30 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.195 -20.552 13.814  0.50 18.32 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 12.227 -20.469 12.669  0.50 14.30 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 11.999 -20.335 12.252  0.50 18.32 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.418 -20.057 13.060  0.50 14.22 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.188 -20.100 12.809  0.50 18.54 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.874 -18.938 12.316  0.50 14.22 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.707 -18.822 12.323  0.50 18.54 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.118 -18.812 13.739  0.50 14.22 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 13.891 -19.034 13.745  0.50 18.54 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.790 -16.197 8.788   0.50 11.05 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.738 -15.972 9.246   0.50 12.23 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.548 -16.797 7.477   0.50 11.15 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.478 -16.489 7.907   0.50 12.79 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.153 -18.190 7.353   0.50 11.55 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 11.042 -17.886 7.688   0.50 12.60 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.536 -19.077 6.753   0.50 11.86 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.369 -18.734 7.092   0.50 12.90 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 11.100 -15.913 6.357   0.50 11.26 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 11.032 -15.540 6.842   0.50 13.51 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.447 -14.544 6.154   0.50 12.66 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.351 -14.175 6.744   0.50 13.70 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.176 -13.790 5.064   0.50 13.46 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.970 -13.367 5.618   0.50 14.10 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.969  -14.689 5.809   0.50 13.27 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.852  -14.343 6.540   0.50 14.39 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.517 -15.736 8.844   0.50 13.28 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.526 -15.627 9.349   0.50 14.70 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.593  -16.884 7.348   0.50 13.39 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.520  -16.545 7.781   0.50 15.36 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 12.040 -15.761 6.530   0.50 13.53 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.969 -15.377 7.029   0.50 16.23 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 11.005 -16.402 5.521   0.50 13.53 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.944 -15.964 5.976   0.50 16.23 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.519 -14.036 6.975   0.50 15.20 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.488 -13.688 7.574   0.50 16.46 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.757 -12.926 4.944   0.50 16.16 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.528 -12.504 5.568   0.50 16.93 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.104 -13.677 5.327   0.50 16.16 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.914 -13.246 5.801   0.50 16.93 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.129 -14.301 4.240   0.50 16.16 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.851 -13.849 4.785   0.50 16.93 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.609  -13.816 5.594   0.50 15.93 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.475  -13.499 6.248   0.50 17.28 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.880  -15.281 5.044   0.50 15.93 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.701  -15.025 5.869   0.50 17.28 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.500  -15.064 6.571   0.50 15.93 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.447  -14.612 7.381   0.50 17.28 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.360 -18.379 7.878   0.50 11.94 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.268 -18.136 8.141   0.50 12.13 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.066 -19.655 7.856   0.50 12.58 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.920 -19.428 7.975   0.50 12.66 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.807 -19.812 9.180   0.50 12.84 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.726 -19.726 9.231   0.50 13.39 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.663 -19.004 10.101  0.50 13.16 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.687 -18.986 10.218  0.50 13.78 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 14.058 -19.748 6.685   0.50 13.07 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.860 -19.439 6.762   0.50 12.81 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.136 -18.827 6.893   0.50 13.50 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.935 -18.526 6.999   0.50 12.83 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.392 -19.450 5.351   0.50 13.75 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 13.135 -19.064 5.472   0.50 13.42 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.815 -17.755 8.251   0.50 14.34 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.757 -17.550 8.548   0.50 14.57 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.431 -20.382 7.774   0.50 15.11 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.254 -20.117 7.858   0.50 15.20 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.420 -20.651 6.642   0.50 15.70 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.231 -20.325 6.651   0.50 15.39 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.686 -18.879 6.251   0.50 16.22 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.456 -18.508 6.335   0.50 15.41 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 14.014 -19.621 4.623   0.50 16.51 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.739 -19.142 4.715   0.50 16.12 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.615 -20.019 5.236   0.50 16.51 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.384 -19.667 5.331   0.50 16.12 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.115 -18.523 5.317   0.50 16.51 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.804 -18.157 5.521   0.50 16.12 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.649 -20.843 9.251   0.50 12.78 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.501 -20.807 9.168   0.50 13.78 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.446 -21.078 10.445  0.50 13.11 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.401 -21.135 10.261  0.50 14.30 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.227 -19.836 10.871  0.50 12.85 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.298 -19.960 10.632  0.50 13.02 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.342 -19.547 12.068  0.50 13.42 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.645 -19.799 11.808  0.50 13.12 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.407 -22.231 10.169  0.50 14.94 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.262 -22.341 9.883   0.50 16.97 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.255 -22.565 11.360  0.50 18.12 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.284 -22.679 10.948  0.50 19.76 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.709 -23.169 12.311  0.50 18.84 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.904 -22.717 12.137  0.50 21.06 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.454 -22.220 11.340  0.50 19.82 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.460 -22.908 10.603  0.50 21.14 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.792 -21.407 8.621   0.50 15.35 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.522 -21.349 8.505   0.50 16.55 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.865 -21.335 11.177  0.50 15.75 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.878 -21.374 11.042  0.50 17.17 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.890 -23.022 9.934   0.50 17.94 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.686 -23.117 9.763   0.50 20.38 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.994 -21.993 9.435   0.50 17.94 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.729 -22.150 9.053   0.50 20.38 ?  14  ASP   A HB3  1 
ATOM   358  N  N    A ASN   A 1 15  ? 16.767 -19.082 9.906   0.50 12.91 ?  15  ASN   A N    1 
ATOM   359  N  N    B ASN   A 1 15  ? 16.678 -19.120 9.656   0.50 12.10 ?  15  ASN   A N    1 
ATOM   360  C  CA   A ASN   A 1 15  ? 17.726 -18.020 10.188  0.50 13.13 ?  15  ASN   A CA   1 
ATOM   361  C  CA   B ASN   A 1 15  ? 17.700 -18.104 9.903   0.50 12.42 ?  15  ASN   A CA   1 
ATOM   362  C  C    A ASN   A 1 15  ? 17.330 -16.647 9.663   0.50 12.69 ?  15  ASN   A C    1 
ATOM   363  C  C    B ASN   A 1 15  ? 17.352 -16.701 9.406   0.50 12.78 ?  15  ASN   A C    1 
ATOM   364  O  O    A ASN   A 1 15  ? 18.000 -15.668 10.012  0.50 12.19 ?  15  ASN   A O    1 
ATOM   365  O  O    B ASN   A 1 15  ? 18.219 -15.820 9.455   0.50 12.80 ?  15  ASN   A O    1 
ATOM   366  C  CB   A ASN   A 1 15  ? 19.102 -18.370 9.593   0.50 12.99 ?  15  ASN   A CB   1 
ATOM   367  C  CB   B ASN   A 1 15  ? 19.064 -18.540 9.340   0.50 11.54 ?  15  ASN   A CB   1 
ATOM   368  C  CG   A ASN   A 1 15  ? 19.059 -18.528 8.087   0.50 13.07 ?  15  ASN   A CG   1 
ATOM   369  C  CG   B ASN   A 1 15  ? 19.079 -18.600 7.830   0.50 12.22 ?  15  ASN   A CG   1 
ATOM   370  O  OD1  A ASN   A 1 15  ? 18.250 -19.292 7.555   0.50 13.49 ?  15  ASN   A OD1  1 
ATOM   371  O  OD1  B ASN   A 1 15  ? 18.442 -19.466 7.224   0.50 12.75 ?  15  ASN   A OD1  1 
ATOM   372  N  ND2  A ASN   A 1 15  ? 19.912 -17.782 7.386   0.50 13.34 ?  15  ASN   A ND2  1 
ATOM   373  N  ND2  B ASN   A 1 15  ? 19.811 -17.680 7.208   0.50 12.71 ?  15  ASN   A ND2  1 
ATOM   374  H  H    A ASN   A 1 15  ? 16.587 -19.166 9.080   0.50 15.51 ?  15  ASN   A H    1 
ATOM   375  H  H    B ASN   A 1 15  ? 16.354 -19.127 8.858   0.50 14.54 ?  15  ASN   A H    1 
ATOM   376  H  HA   A ASN   A 1 15  ? 17.841 -17.943 11.155  0.50 15.77 ?  15  ASN   A HA   1 
ATOM   377  H  HA   B ASN   A 1 15  ? 17.809 -18.035 10.859  0.50 14.92 ?  15  ASN   A HA   1 
ATOM   378  H  HB2  A ASN   A 1 15  ? 19.731 -17.661 9.811   0.50 15.60 ?  15  ASN   A HB2  1 
ATOM   379  H  HB2  B ASN   A 1 15  ? 19.740 -17.901 9.627   0.50 13.87 ?  15  ASN   A HB2  1 
ATOM   380  H  HB3  A ASN   A 1 15  ? 19.407 -19.208 9.975   0.50 15.60 ?  15  ASN   A HB3  1 
ATOM   381  H  HB3  B ASN   A 1 15  ? 19.287 -19.424 9.683   0.50 13.87 ?  15  ASN   A HB3  1 
ATOM   382  H  HD21 A ASN   A 1 15  ? 19.921 -17.830 6.526   0.50 16.03 ?  15  ASN   A HD21 1 
ATOM   383  H  HD21 B ASN   A 1 15  ? 19.856 -17.676 6.351   0.50 15.26 ?  15  ASN   A HD21 1 
ATOM   384  H  HD22 A ASN   A 1 15  ? 20.459 -17.252 7.789   0.50 16.03 ?  15  ASN   A HD22 1 
ATOM   385  H  HD22 B ASN   A 1 15  ? 20.239 -17.086 7.664   0.50 15.26 ?  15  ASN   A HD22 1 
ATOM   386  N  N    A VAL   A 1 16  ? 16.297 -16.543 8.822   0.50 12.30 ?  16  VAL   A N    1 
ATOM   387  N  N    B VAL   A 1 16  ? 16.117 -16.447 8.971   0.50 12.78 ?  16  VAL   A N    1 
ATOM   388  C  CA   A VAL   A 1 16  ? 15.873 -15.278 8.224   0.50 12.49 ?  16  VAL   A CA   1 
ATOM   389  C  CA   B VAL   A 1 16  ? 15.749 -15.152 8.404   0.50 12.70 ?  16  VAL   A CA   1 
ATOM   390  C  C    A VAL   A 1 16  ? 14.581 -14.803 8.876   0.50 11.92 ?  16  VAL   A C    1 
ATOM   391  C  C    B VAL   A 1 16  ? 14.495 -14.631 9.097   0.50 12.59 ?  16  VAL   A C    1 
ATOM   392  O  O    A VAL   A 1 16  ? 13.582 -15.536 8.925   0.50 12.05 ?  16  VAL   A O    1 
ATOM   393  O  O    B VAL   A 1 16  ? 13.496 -15.351 9.222   0.50 12.86 ?  16  VAL   A O    1 
ATOM   394  C  CB   A VAL   A 1 16  ? 15.704 -15.374 6.698   0.50 13.36 ?  16  VAL   A CB   1 
ATOM   395  C  CB   B VAL   A 1 16  ? 15.558 -15.223 6.876   0.50 13.03 ?  16  VAL   A CB   1 
ATOM   396  C  CG1  A VAL   A 1 16  ? 15.269 -14.019 6.136   0.50 14.03 ?  16  VAL   A CG1  1 
ATOM   397  C  CG1  B VAL   A 1 16  ? 15.143 -13.862 6.313   0.50 13.41 ?  16  VAL   A CG1  1 
ATOM   398  C  CG2  A VAL   A 1 16  ? 16.990 -15.838 6.034   0.50 13.88 ?  16  VAL   A CG2  1 
ATOM   399  C  CG2  B VAL   A 1 16  ? 16.832 -15.724 6.191   0.50 14.16 ?  16  VAL   A CG2  1 
ATOM   400  H  H    A VAL   A 1 16  ? 15.835 -17.219 8.574   0.50 14.77 ?  16  VAL   A H    1 
ATOM   401  H  H    B VAL   A 1 16  ? 15.463 -17.008 9.011   0.50 15.35 ?  16  VAL   A H    1 
ATOM   402  H  HA   A VAL   A 1 16  ? 16.560 -14.614 8.399   0.50 15.00 ?  16  VAL   A HA   1 
ATOM   403  H  HA   B VAL   A 1 16  ? 16.465 -14.520 8.582   0.50 15.25 ?  16  VAL   A HA   1 
ATOM   404  H  HB   A VAL   A 1 16  ? 15.013 -16.025 6.499   0.50 16.04 ?  16  VAL   A HB   1 
ATOM   405  H  HB   B VAL   A 1 16  ? 14.853 -15.855 6.682   0.50 15.65 ?  16  VAL   A HB   1 
ATOM   406  H  HG11 A VAL   A 1 16  ? 15.364 -14.034 5.172   0.50 16.85 ?  16  VAL   A HG11 1 
ATOM   407  H  HG11 B VAL   A 1 16  ? 15.217 -13.892 5.345   0.50 16.11 ?  16  VAL   A HG11 1 
ATOM   408  H  HG12 A VAL   A 1 16  ? 14.341 -13.860 6.373   0.50 16.85 ?  16  VAL   A HG12 1 
ATOM   409  H  HG12 B VAL   A 1 16  ? 14.224 -13.685 6.566   0.50 16.11 ?  16  VAL   A HG12 1 
ATOM   410  H  HG13 A VAL   A 1 16  ? 15.831 -13.325 6.514   0.50 16.85 ?  16  VAL   A HG13 1 
ATOM   411  H  HG13 B VAL   A 1 16  ? 15.727 -13.180 6.670   0.50 16.11 ?  16  VAL   A HG13 1 
ATOM   412  H  HG21 A VAL   A 1 16  ? 16.872 -15.810 5.071   0.50 16.66 ?  16  VAL   A HG21 1 
ATOM   413  H  HG21 B VAL   A 1 16  ? 16.705 -15.696 5.229   0.50 17.01 ?  16  VAL   A HG21 1 
ATOM   414  H  HG22 A VAL   A 1 16  ? 17.711 -15.245 6.295   0.50 16.66 ?  16  VAL   A HG22 1 
ATOM   415  H  HG22 B VAL   A 1 16  ? 17.576 -15.155 6.442   0.50 17.01 ?  16  VAL   A HG22 1 
ATOM   416  H  HG23 A VAL   A 1 16  ? 17.186 -16.743 6.318   0.50 16.66 ?  16  VAL   A HG23 1 
ATOM   417  H  HG23 B VAL   A 1 16  ? 17.007 -16.636 6.474   0.50 17.01 ?  16  VAL   A HG23 1 
ATOM   418  N  N    A TYR   A 1 17  ? 14.596 -13.547 9.313   0.50 11.87 ?  17  TYR   A N    1 
ATOM   419  N  N    B TYR   A 1 17  ? 14.552 -13.364 9.517   0.50 12.44 ?  17  TYR   A N    1 
ATOM   420  C  CA   A TYR   A 1 17  ? 13.490 -12.872 9.971   0.50 12.09 ?  17  TYR   A CA   1 
ATOM   421  C  CA   B TYR   A 1 17  ? 13.505 -12.691 10.272  0.50 11.72 ?  17  TYR   A CA   1 
ATOM   422  C  C    A TYR   A 1 17  ? 13.230 -11.557 9.234   0.50 11.95 ?  17  TYR   A C    1 
ATOM   423  C  C    B TYR   A 1 17  ? 13.230 -11.348 9.618   0.50 11.58 ?  17  TYR   A C    1 
ATOM   424  O  O    A TYR   A 1 17  ? 14.131 -11.013 8.591   0.50 12.27 ?  17  TYR   A O    1 
ATOM   425  O  O    B TYR   A 1 17  ? 14.130 -10.757 9.020   0.50 11.93 ?  17  TYR   A O    1 
ATOM   426  C  CB   A TYR   A 1 17  ? 13.872 -12.596 11.434  0.50 12.95 ?  17  TYR   A CB   1 
ATOM   427  C  CB   B TYR   A 1 17  ? 13.981 -12.455 11.697  0.50 12.28 ?  17  TYR   A CB   1 
ATOM   428  C  CG   A TYR   A 1 17  ? 14.158 -13.849 12.258  0.50 14.15 ?  17  TYR   A CG   1 
ATOM   429  C  CG   B TYR   A 1 17  ? 14.089 -13.733 12.472  0.50 13.07 ?  17  TYR   A CG   1 
ATOM   430  C  CD1  A TYR   A 1 17  ? 15.389 -14.505 12.190  0.50 14.79 ?  17  TYR   A CD1  1 
ATOM   431  C  CD1  B TYR   A 1 17  ? 15.202 -14.558 12.348  0.50 13.46 ?  17  TYR   A CD1  1 
ATOM   432  C  CD2  A TYR   A 1 17  ? 13.194 -14.374 13.111  0.50 14.74 ?  17  TYR   A CD2  1 
ATOM   433  C  CD2  B TYR   A 1 17  ? 13.065 -14.133 13.312  0.50 13.44 ?  17  TYR   A CD2  1 
ATOM   434  C  CE1  A TYR   A 1 17  ? 15.641 -15.656 12.947  0.50 15.31 ?  17  TYR   A CE1  1 
ATOM   435  C  CE1  B TYR   A 1 17  ? 15.291 -15.745 13.053  0.50 13.88 ?  17  TYR   A CE1  1 
ATOM   436  C  CE2  A TYR   A 1 17  ? 13.437 -15.519 13.868  0.50 15.22 ?  17  TYR   A CE2  1 
ATOM   437  C  CE2  B TYR   A 1 17  ? 13.141 -15.317 14.019  0.50 13.93 ?  17  TYR   A CE2  1 
ATOM   438  C  CZ   A TYR   A 1 17  ? 14.658 -16.155 13.782  0.50 15.17 ?  17  TYR   A CZ   1 
ATOM   439  C  CZ   B TYR   A 1 17  ? 14.256 -16.121 13.889  0.50 13.44 ?  17  TYR   A CZ   1 
ATOM   440  O  OH   A TYR   A 1 17  ? 14.890 -17.286 14.540  0.50 15.10 ?  17  TYR   A OH   1 
ATOM   441  O  OH   B TYR   A 1 17  ? 14.330 -17.293 14.603  0.50 13.90 ?  17  TYR   A OH   1 
ATOM   442  H  H    A TYR   A 1 17  ? 15.282 -13.044 9.221   0.50 14.26 ?  17  TYR   A H    1 
ATOM   443  H  H    B TYR   A 1 17  ? 15.222 -12.837 9.356   0.50 14.94 ?  17  TYR   A H    1 
ATOM   444  H  HA   A TYR   A 1 17  ? 12.696 -13.434 9.944   0.50 14.52 ?  17  TYR   A HA   1 
ATOM   445  H  HA   B TYR   A 1 17  ? 12.689 -13.209 10.282  0.50 14.08 ?  17  TYR   A HA   1 
ATOM   446  H  HB2  A TYR   A 1 17  ? 14.668 -12.044 11.447  0.50 15.55 ?  17  TYR   A HB2  1 
ATOM   447  H  HB2  B TYR   A 1 17  ? 14.861 -12.044 11.675  0.50 14.76 ?  17  TYR   A HB2  1 
ATOM   448  H  HB3  A TYR   A 1 17  ? 13.141 -12.130 11.858  0.50 15.55 ?  17  TYR   A HB3  1 
ATOM   449  H  HB3  B TYR   A 1 17  ? 13.356 -11.878 12.157  0.50 14.76 ?  17  TYR   A HB3  1 
ATOM   450  H  HD1  A TYR   A 1 17  ? 16.055 -14.183 11.631  0.50 17.77 ?  17  TYR   A HD1  1 
ATOM   451  H  HD1  B TYR   A 1 17  ? 15.899 -14.310 11.781  0.50 16.17 ?  17  TYR   A HD1  1 
ATOM   452  H  HD2  A TYR   A 1 17  ? 12.369 -13.958 13.178  0.50 17.70 ?  17  TYR   A HD2  1 
ATOM   453  H  HD2  B TYR   A 1 17  ? 12.313 -13.594 13.401  0.50 16.14 ?  17  TYR   A HD2  1 
ATOM   454  H  HE1  A TYR   A 1 17  ? 16.467 -16.092 12.894  0.50 18.38 ?  17  TYR   A HE1  1 
ATOM   455  H  HE1  B TYR   A 1 17  ? 16.042 -16.290 12.960  0.50 16.66 ?  17  TYR   A HE1  1 
ATOM   456  H  HE2  A TYR   A 1 17  ? 12.778 -15.858 14.435  0.50 18.28 ?  17  TYR   A HE2  1 
ATOM   457  H  HE2  B TYR   A 1 17  ? 12.445 -15.566 14.581  0.50 16.73 ?  17  TYR   A HE2  1 
ATOM   458  H  HH   A TYR   A 1 17  ? 15.651 -17.608 14.372  0.50 18.13 ?  17  TYR   A HH   1 
ATOM   459  H  HH   B TYR   A 1 17  ? 13.574 -17.475 14.920  0.50 16.70 ?  17  TYR   A HH   1 
ATOM   460  N  N    A ILE   A 1 18  ? 12.001 -11.034 9.322   0.50 11.71 ?  18  ILE   A N    1 
ATOM   461  N  N    B ILE   A 1 18  ? 11.998 -10.844 9.743   0.50 11.69 ?  18  ILE   A N    1 
ATOM   462  C  CA   A ILE   A 1 18  ? 11.616 -9.851  8.544   0.50 12.40 ?  18  ILE   A CA   1 
ATOM   463  C  CA   B ILE   A 1 18  ? 11.612 -9.635  9.020   0.50 11.79 ?  18  ILE   A CA   1 
ATOM   464  C  C    A ILE   A 1 18  ? 10.638 -8.992  9.342   0.50 13.25 ?  18  ILE   A C    1 
ATOM   465  C  C    B ILE   A 1 18  ? 10.675 -8.769  9.847   0.50 12.51 ?  18  ILE   A C    1 
ATOM   466  O  O    A ILE   A 1 18  ? 9.801  -9.507  10.087  0.50 12.87 ?  18  ILE   A O    1 
ATOM   467  O  O    B ILE   A 1 18  ? 9.856  -9.265  10.629  0.50 12.61 ?  18  ILE   A O    1 
ATOM   468  C  CB   A ILE   A 1 18  ? 11.062 -10.264 7.157   0.50 12.30 ?  18  ILE   A CB   1 
ATOM   469  C  CB   B ILE   A 1 18  ? 10.996 -9.980  7.650   0.50 11.63 ?  18  ILE   A CB   1 
ATOM   470  C  CG1  A ILE   A 1 18  ? 10.988 -9.058  6.218   0.50 12.48 ?  18  ILE   A CG1  1 
ATOM   471  C  CG1  B ILE   A 1 18  ? 10.931 -8.744  6.752   0.50 12.47 ?  18  ILE   A CG1  1 
ATOM   472  C  CG2  A ILE   A 1 18  ? 9.714  -10.984 7.292   0.50 12.16 ?  18  ILE   A CG2  1 
ATOM   473  C  CG2  B ILE   A 1 18  ? 9.622  -10.614 7.826   0.50 12.34 ?  18  ILE   A CG2  1 
ATOM   474  C  CD1  A ILE   A 1 18  ? 10.735 -9.442  4.781   0.50 13.85 ?  18  ILE   A CD1  1 
ATOM   475  C  CD1  B ILE   A 1 18  ? 10.570 -9.083  5.329   0.50 13.73 ?  18  ILE   A CD1  1 
ATOM   476  H  H    A ILE   A 1 18  ? 11.382 -11.354 9.828   0.50 14.06 ?  18  ILE   A H    1 
ATOM   477  H  H    B ILE   A 1 18  ? 11.370 -11.183 10.235  0.50 14.04 ?  18  ILE   A H    1 
ATOM   478  H  HA   A ILE   A 1 18  ? 12.409 -9.327  8.385   0.50 14.89 ?  18  ILE   A HA   1 
ATOM   479  H  HA   B ILE   A 1 18  ? 12.412 -9.114  8.860   0.50 14.16 ?  18  ILE   A HA   1 
ATOM   480  H  HB   A ILE   A 1 18  ? 11.687 -10.897 6.767   0.50 14.77 ?  18  ILE   A HB   1 
ATOM   481  H  HB   B ILE   A 1 18  ? 11.577 -10.624 7.228   0.50 13.97 ?  18  ILE   A HB   1 
ATOM   482  H  HG12 A ILE   A 1 18  ? 10.269 -8.478  6.504   0.50 14.99 ?  18  ILE   A HG12 1 
ATOM   483  H  HG12 B ILE   A 1 18  ? 10.261 -8.133  7.095   0.50 14.98 ?  18  ILE   A HG12 1 
ATOM   484  H  HG13 A ILE   A 1 18  ? 11.834 -8.582  6.252   0.50 14.99 ?  18  ILE   A HG13 1 
ATOM   485  H  HG13 B ILE   A 1 18  ? 11.802 -8.309  6.745   0.50 14.98 ?  18  ILE   A HG13 1 
ATOM   486  H  HG21 A ILE   A 1 18  ? 9.471  -11.366 6.430   0.50 14.61 ?  18  ILE   A HG21 1 
ATOM   487  H  HG21 B ILE   A 1 18  ? 9.355  -11.012 6.983   0.50 14.82 ?  18  ILE   A HG21 1 
ATOM   488  H  HG22 A ILE   A 1 18  ? 9.797  -11.692 7.949   0.50 14.61 ?  18  ILE   A HG22 1 
ATOM   489  H  HG22 B ILE   A 1 18  ? 9.675  -11.292 8.513   0.50 14.82 ?  18  ILE   A HG22 1 
ATOM   490  H  HG23 A ILE   A 1 18  ? 9.039  -10.349 7.571   0.50 14.61 ?  18  ILE   A HG23 1 
ATOM   491  H  HG23 B ILE   A 1 18  ? 8.986  -9.927  8.085   0.50 14.82 ?  18  ILE   A HG23 1 
ATOM   492  H  HD11 A ILE   A 1 18  ? 10.757 -8.640  4.233   0.50 16.63 ?  18  ILE   A HD11 1 
ATOM   493  H  HD11 B ILE   A 1 18  ? 10.590 -8.275  4.793   0.50 16.49 ?  18  ILE   A HD11 1 
ATOM   494  H  HD12 A ILE   A 1 18  ? 11.423 -10.059 4.491   0.50 16.63 ?  18  ILE   A HD12 1 
ATOM   495  H  HD12 B ILE   A 1 18  ? 11.214 -9.723  4.983   0.50 16.49 ?  18  ILE   A HD12 1 
ATOM   496  H  HD13 A ILE   A 1 18  ? 9.862  -9.860  4.715   0.50 16.63 ?  18  ILE   A HD13 1 
ATOM   497  H  HD13 B ILE   A 1 18  ? 9.681  -9.469  5.310   0.50 16.49 ?  18  ILE   A HD13 1 
ATOM   498  N  N    A LYS   A 1 19  ? 10.732 -7.668  9.162   0.50 13.64 ?  19  LYS   A N    1 
ATOM   499  N  N    B LYS   A 1 19  ? 10.795 -7.455  9.645   0.50 13.16 ?  19  LYS   A N    1 
ATOM   500  C  CA   A LYS   A 1 19  ? 9.945  -6.715  9.943   0.50 14.95 ?  19  LYS   A CA   1 
ATOM   501  C  CA   B LYS   A 1 19  ? 9.985  -6.471  10.347  0.50 14.76 ?  19  LYS   A CA   1 
ATOM   502  C  C    A LYS   A 1 19  ? 9.752  -5.423  9.160   0.50 15.28 ?  19  LYS   A C    1 
ATOM   503  C  C    B LYS   A 1 19  ? 9.784  -5.270  9.430   0.50 15.32 ?  19  LYS   A C    1 
ATOM   504  O  O    A LYS   A 1 19  ? 10.574 -5.067  8.308   0.50 14.66 ?  19  LYS   A O    1 
ATOM   505  O  O    B LYS   A 1 19  ? 10.731 -4.828  8.775   0.50 15.04 ?  19  LYS   A O    1 
ATOM   506  C  CB   A LYS   A 1 19  ? 10.663 -6.391  11.265  0.50 16.02 ?  19  LYS   A CB   1 
ATOM   507  C  CB   B LYS   A 1 19  ? 10.701 -6.041  11.632  0.50 15.43 ?  19  LYS   A CB   1 
ATOM   508  C  CG   A LYS   A 1 19  ? 9.976  -5.402  12.223  0.50 17.18 ?  19  LYS   A CG   1 
ATOM   509  C  CG   B LYS   A 1 19  ? 9.885  -5.173  12.546  0.50 16.98 ?  19  LYS   A CG   1 
ATOM   510  C  CD   A LYS   A 1 19  ? 10.877 -5.150  13.449  0.50 17.71 ?  19  LYS   A CD   1 
ATOM   511  C  CD   B LYS   A 1 19  ? 10.703 -4.799  13.754  0.50 18.31 ?  19  LYS   A CD   1 
ATOM   512  C  CE   A LYS   A 1 19  ? 10.287 -4.158  14.452  0.50 18.26 ?  19  LYS   A CE   1 
ATOM   513  C  CE   B LYS   A 1 19  ? 9.928  -3.894  14.675  0.50 19.43 ?  19  LYS   A CE   1 
ATOM   514  N  NZ   A LYS   A 1 19  ? 11.158 -3.997  15.664  0.50 18.30 ?  19  LYS   A NZ   1 
ATOM   515  N  NZ   B LYS   A 1 19  ? 10.771 -3.488  15.818  0.50 19.82 ?  19  LYS   A NZ   1 
ATOM   516  H  H    A LYS   A 1 19  ? 11.251 -7.303  8.584   0.50 16.38 ?  19  LYS   A H    1 
ATOM   517  H  H    B LYS   A 1 19  ? 11.363 -7.093  9.100   0.50 15.81 ?  19  LYS   A H    1 
ATOM   518  H  HA   A LYS   A 1 19  ? 9.073  -7.101  10.137  0.50 17.95 ?  19  LYS   A HA   1 
ATOM   519  H  HA   B LYS   A 1 19  ? 9.126  -6.851  10.584  0.50 17.72 ?  19  LYS   A HA   1 
ATOM   520  H  HB2  A LYS   A 1 19  ? 10.773 -7.222  11.749  0.50 19.23 ?  19  LYS   A HB2  1 
ATOM   521  H  HB2  B LYS   A 1 19  ? 10.948 -6.833  12.139  0.50 18.53 ?  19  LYS   A HB2  1 
ATOM   522  H  HB3  A LYS   A 1 19  ? 11.529 -6.025  11.048  0.50 19.23 ?  19  LYS   A HB3  1 
ATOM   523  H  HB3  B LYS   A 1 19  ? 11.501 -5.543  11.399  0.50 18.53 ?  19  LYS   A HB3  1 
ATOM   524  H  HG2  A LYS   A 1 19  ? 9.829  -4.553  11.778  0.50 20.63 ?  19  LYS   A HG2  1 
ATOM   525  H  HG2  B LYS   A 1 19  ? 9.631  -4.360  12.083  0.50 20.39 ?  19  LYS   A HG2  1 
ATOM   526  H  HG3  A LYS   A 1 19  ? 9.133  -5.771  12.536  0.50 20.63 ?  19  LYS   A HG3  1 
ATOM   527  H  HG3  B LYS   A 1 19  ? 9.099  -5.659  12.843  0.50 20.39 ?  19  LYS   A HG3  1 
ATOM   528  H  HD2  A LYS   A 1 19  ? 11.017 -5.989  13.918  0.50 21.26 ?  19  LYS   A HD2  1 
ATOM   529  H  HD2  B LYS   A 1 19  ? 10.938 -5.607  14.241  0.50 21.98 ?  19  LYS   A HD2  1 
ATOM   530  H  HD3  A LYS   A 1 19  ? 11.727 -4.795  13.151  0.50 21.26 ?  19  LYS   A HD3  1 
ATOM   531  H  HD3  B LYS   A 1 19  ? 11.505 -4.336  13.465  0.50 21.98 ?  19  LYS   A HD3  1 
ATOM   532  H  HE2  A LYS   A 1 19  ? 10.201 -3.285  14.033  0.50 21.92 ?  19  LYS   A HE2  1 
ATOM   533  H  HE2  B LYS   A 1 19  ? 9.659  -3.098  14.189  0.50 23.33 ?  19  LYS   A HE2  1 
ATOM   534  H  HE3  A LYS   A 1 19  ? 9.419  -4.471  14.750  0.50 21.92 ?  19  LYS   A HE3  1 
ATOM   535  H  HE3  B LYS   A 1 19  ? 9.151  -4.365  15.012  0.50 23.33 ?  19  LYS   A HE3  1 
ATOM   536  H  HZ1  A LYS   A 1 19  ? 10.808 -3.393  16.217  0.50 21.98 ?  19  LYS   A HZ1  1 
ATOM   537  H  HZ1  B LYS   A 1 19  ? 10.311 -2.953  16.357  0.50 23.80 ?  19  LYS   A HZ1  1 
ATOM   538  H  HZ2  A LYS   A 1 19  ? 11.227 -4.774  16.094  0.50 21.98 ?  19  LYS   A HZ2  1 
ATOM   539  H  HZ2  B LYS   A 1 19  ? 11.030 -4.208  16.272  0.50 23.80 ?  19  LYS   A HZ2  1 
ATOM   540  H  HZ3  A LYS   A 1 19  ? 11.971 -3.729  15.422  0.50 21.98 ?  19  LYS   A HZ3  1 
ATOM   541  H  HZ3  B LYS   A 1 19  ? 11.492 -3.056  15.524  0.50 23.80 ?  19  LYS   A HZ3  1 
ATOM   542  N  N    A ASN   A 1 20  ? 8.663  -4.714  9.473   0.50 16.15 ?  20  ASN   A N    1 
ATOM   543  N  N    B ASN   A 1 20  ? 8.551  -4.758  9.359   0.50 16.45 ?  20  ASN   A N    1 
ATOM   544  C  CA   A ASN   A 1 20  ? 8.433  -3.361  8.972   0.50 16.75 ?  20  ASN   A CA   1 
ATOM   545  C  CA   B ASN   A 1 20  ? 8.290  -3.499  8.654   0.50 17.22 ?  20  ASN   A CA   1 
ATOM   546  C  C    A ASN   A 1 20  ? 9.056  -2.396  9.972   0.50 16.56 ?  20  ASN   A C    1 
ATOM   547  C  C    B ASN   A 1 20  ? 8.877  -2.372  9.488   0.50 17.41 ?  20  ASN   A C    1 
ATOM   548  O  O    A ASN   A 1 20  ? 8.548  -2.230  11.085  0.50 16.46 ?  20  ASN   A O    1 
ATOM   549  O  O    B ASN   A 1 20  ? 8.268  -1.924  10.463  0.50 18.14 ?  20  ASN   A O    1 
ATOM   550  C  CB   A ASN   A 1 20  ? 6.938  -3.092  8.801   0.50 17.44 ?  20  ASN   A CB   1 
ATOM   551  C  CB   B ASN   A 1 20  ? 6.792  -3.292  8.444   0.50 17.79 ?  20  ASN   A CB   1 
ATOM   552  C  CG   A ASN   A 1 20  ? 6.627  -1.630  8.498   0.50 18.01 ?  20  ASN   A CG   1 
ATOM   553  C  CG   B ASN   A 1 20  ? 6.446  -1.903  7.908   0.50 18.35 ?  20  ASN   A CG   1 
ATOM   554  O  OD1  A ASN   A 1 20  ? 5.723  -1.042  9.097   0.50 19.85 ?  20  ASN   A OD1  1 
ATOM   555  O  OD1  B ASN   A 1 20  ? 5.464  -1.286  8.341   0.50 19.69 ?  20  ASN   A OD1  1 
ATOM   556  N  ND2  A ASN   A 1 20  ? 7.375  -1.039  7.570   0.50 17.53 ?  20  ASN   A ND2  1 
ATOM   557  N  ND2  B ASN   A 1 20  ? 7.240  -1.414  6.952   0.50 18.98 ?  20  ASN   A ND2  1 
ATOM   558  H  H    A ASN   A 1 20  ? 8.043  -4.995  9.993   0.50 19.39 ?  20  ASN   A H    1 
ATOM   559  H  H    B ASN   A 1 20  ? 7.853  -5.130  9.700   0.50 19.75 ?  20  ASN   A H    1 
ATOM   560  H  HA   A ASN   A 1 20  ? 8.869  -3.251  8.117   0.50 20.12 ?  20  ASN   A HA   1 
ATOM   561  H  HA   B ASN   A 1 20  ? 8.735  -3.515  7.791   0.50 20.68 ?  20  ASN   A HA   1 
ATOM   562  H  HB2  A ASN   A 1 20  ? 6.608  -3.632  8.065   0.50 20.95 ?  20  ASN   A HB2  1 
ATOM   563  H  HB2  B ASN   A 1 20  ? 6.470  -3.920  7.800   0.50 21.36 ?  20  ASN   A HB2  1 
ATOM   564  H  HB3  A ASN   A 1 20  ? 6.479  -3.331  9.620   0.50 20.95 ?  20  ASN   A HB3  1 
ATOM   565  H  HB3  B ASN   A 1 20  ? 6.335  -3.420  9.287   0.50 21.36 ?  20  ASN   A HB3  1 
ATOM   566  H  HD21 A ASN   A 1 20  ? 7.229  -0.221  7.362   0.50 21.05 ?  20  ASN   A HD21 1 
ATOM   567  H  HD21 B ASN   A 1 20  ? 7.088  -0.636  6.627   0.50 22.79 ?  20  ASN   A HD21 1 
ATOM   568  H  HD22 A ASN   A 1 20  ? 8.001  -1.481  7.177   0.50 21.05 ?  20  ASN   A HD22 1 
ATOM   569  H  HD22 B ASN   A 1 20  ? 7.909  -1.878  6.664   0.50 22.79 ?  20  ASN   A HD22 1 
ATOM   570  N  N    A ALA   A 1 21  ? 10.167 -1.777  9.589   0.50 16.79 ?  21  ALA   A N    1 
ATOM   571  N  N    B ALA   A 1 21  ? 10.066 -1.906  9.114   0.50 16.96 ?  21  ALA   A N    1 
ATOM   572  C  CA   A ALA   A 1 21  ? 10.866 -0.900  10.512  0.50 16.72 ?  21  ALA   A CA   1 
ATOM   573  C  CA   B ALA   A 1 21  ? 10.742 -0.899  9.917   0.50 16.31 ?  21  ALA   A CA   1 
ATOM   574  C  C    A ALA   A 1 21  ? 11.844 -0.041  9.734   0.50 16.21 ?  21  ALA   A C    1 
ATOM   575  C  C    B ALA   A 1 21  ? 11.792 -0.189  9.079   0.50 14.94 ?  21  ALA   A C    1 
ATOM   576  O  O    A ALA   A 1 21  ? 12.332 -0.437  8.672   0.50 16.38 ?  21  ALA   A O    1 
ATOM   577  O  O    B ALA   A 1 21  ? 12.250 -0.698  8.053   0.50 15.05 ?  21  ALA   A O    1 
ATOM   578  C  CB   A ALA   A 1 21  ? 11.605 -1.707  11.582  0.50 18.00 ?  21  ALA   A CB   1 
ATOM   579  C  CB   B ALA   A 1 21  ? 11.395 -1.511  11.159  0.50 17.46 ?  21  ALA   A CB   1 
ATOM   580  H  H    A ALA   A 1 21  ? 10.534 -1.843  8.811   0.50 20.16 ?  21  ALA   A H    1 
ATOM   581  H  H    B ALA   A 1 21  ? 10.490 -2.152  8.406   0.50 20.36 ?  21  ALA   A H    1 
ATOM   582  H  HA   A ALA   A 1 21  ? 10.228 -0.311  10.951  0.50 20.08 ?  21  ALA   A HA   1 
ATOM   583  H  HA   B ALA   A 1 21  ? 10.088 -0.245  10.210  0.50 19.59 ?  21  ALA   A HA   1 
ATOM   584  H  HB1  A ALA   A 1 21  ? 11.972 -1.093  12.232  0.50 21.61 ?  21  ALA   A HB1  1 
ATOM   585  H  HB1  B ALA   A 1 21  ? 11.829 -0.808  11.664  0.50 20.97 ?  21  ALA   A HB1  1 
ATOM   586  H  HB2  A ALA   A 1 21  ? 10.971 -2.304  12.011  0.50 21.61 ?  21  ALA   A HB2  1 
ATOM   587  H  HB2  B ALA   A 1 21  ? 10.708 -1.933  11.702  0.50 20.97 ?  21  ALA   A HB2  1 
ATOM   588  H  HB3  A ALA   A 1 21  ? 12.309 -2.217  11.159  0.50 21.61 ?  21  ALA   A HB3  1 
ATOM   589  H  HB3  B ALA   A 1 21  ? 12.046 -2.172  10.879  0.50 20.97 ?  21  ALA   A HB3  1 
ATOM   590  N  N    A ASP   A 1 22  ? 12.097 1.150   10.268  0.50 15.95 ?  22  ASP   A N    1 
ATOM   591  N  N    B ASP   A 1 22  ? 12.147 1.010   9.540   0.50 14.53 ?  22  ASP   A N    1 
ATOM   592  C  CA   A ASP   A 1 22  ? 13.136 2.038   9.762   0.50 16.12 ?  22  ASP   A CA   1 
ATOM   593  C  CA   B ASP   A 1 22  ? 13.286 1.760   9.024   0.50 14.22 ?  22  ASP   A CA   1 
ATOM   594  C  C    A ASP   A 1 22  ? 14.473 1.546   10.300  0.50 15.23 ?  22  ASP   A C    1 
ATOM   595  C  C    B ASP   A 1 22  ? 14.550 1.199   9.669   0.50 13.13 ?  22  ASP   A C    1 
ATOM   596  O  O    A ASP   A 1 22  ? 14.710 1.581   11.512  0.50 15.86 ?  22  ASP   A O    1 
ATOM   597  O  O    B ASP   A 1 22  ? 14.654 1.159   10.899  0.50 13.15 ?  22  ASP   A O    1 
ATOM   598  C  CB   A ASP   A 1 22  ? 12.851 3.458   10.241  0.50 17.75 ?  22  ASP   A CB   1 
ATOM   599  C  CB   B ASP   A 1 22  ? 13.111 3.234   9.398   0.50 15.39 ?  22  ASP   A CB   1 
ATOM   600  C  CG   A ASP   A 1 22  ? 13.843 4.474   9.704   0.50 19.28 ?  22  ASP   A CG   1 
ATOM   601  C  CG   B ASP   A 1 22  ? 14.150 4.144   8.758   0.50 16.11 ?  22  ASP   A CG   1 
ATOM   602  O  OD1  A ASP   A 1 22  ? 14.873 4.077   9.127   0.50 19.53 ?  22  ASP   A OD1  1 
ATOM   603  O  OD1  B ASP   A 1 22  ? 15.221 3.655   8.339   0.50 14.99 ?  22  ASP   A OD1  1 
ATOM   604  O  OD2  A ASP   A 1 22  ? 13.587 5.686   9.867   0.50 20.51 -1 22  ASP   A OD2  1 
ATOM   605  O  OD2  B ASP   A 1 22  ? 13.896 5.367   8.683   0.50 17.86 -1 22  ASP   A OD2  1 
ATOM   606  H  H    A ASP   A 1 22  ? 11.651 1.484   10.924  0.50 19.15 ?  22  ASP   A H    1 
ATOM   607  H  H    B ASP   A 1 22  ? 11.721 1.421   10.166  0.50 17.44 ?  22  ASP   A H    1 
ATOM   608  H  HA   A ASP   A 1 22  ? 13.152 2.018   8.789   0.50 19.35 ?  22  ASP   A HA   1 
ATOM   609  H  HA   B ASP   A 1 22  ? 13.340 1.670   8.057   0.50 17.08 ?  22  ASP   A HA   1 
ATOM   610  H  HB2  A ASP   A 1 22  ? 11.960 3.714   9.959   0.50 21.32 ?  22  ASP   A HB2  1 
ATOM   611  H  HB2  B ASP   A 1 22  ? 12.236 3.531   9.112   0.50 18.48 ?  22  ASP   A HB2  1 
ATOM   612  H  HB3  A ASP   A 1 22  ? 12.912 3.479   11.209  0.50 21.32 ?  22  ASP   A HB3  1 
ATOM   613  H  HB3  B ASP   A 1 22  ? 13.193 3.319   10.362  0.50 18.48 ?  22  ASP   A HB3  1 
ATOM   614  N  N    A ILE   A 1 23  ? 15.348 1.088   9.400   0.50 14.63 ?  23  ILE   A N    1 
ATOM   615  N  N    B ILE   A 1 23  ? 15.501 0.744   8.847   0.50 13.05 ?  23  ILE   A N    1 
ATOM   616  C  CA   A ILE   A 1 23  ? 16.619 0.496   9.812   0.50 13.75 ?  23  ILE   A CA   1 
ATOM   617  C  CA   B ILE   A 1 23  ? 16.729 0.155   9.377   0.50 12.64 ?  23  ILE   A CA   1 
ATOM   618  C  C    A ILE   A 1 23  ? 17.435 1.468   10.651  0.50 14.03 ?  23  ILE   A C    1 
ATOM   619  C  C    B ILE   A 1 23  ? 17.450 1.130   10.296  0.50 13.26 ?  23  ILE   A C    1 
ATOM   620  O  O    A ILE   A 1 23  ? 18.199 1.051   11.532  0.50 14.41 ?  23  ILE   A O    1 
ATOM   621  O  O    B ILE   A 1 23  ? 18.098 0.718   11.267  0.50 13.44 ?  23  ILE   A O    1 
ATOM   622  C  CB   A ILE   A 1 23  ? 17.389 -0.013  8.574   0.50 13.38 ?  23  ILE   A CB   1 
ATOM   623  C  CB   B ILE   A 1 23  ? 17.644 -0.366  8.243   0.50 12.25 ?  23  ILE   A CB   1 
ATOM   624  C  CG1  A ILE   A 1 23  ? 18.582 -0.874  8.995   0.50 13.90 ?  23  ILE   A CG1  1 
ATOM   625  C  CG1  B ILE   A 1 23  ? 18.705 -1.312  8.818   0.50 12.14 ?  23  ILE   A CG1  1 
ATOM   626  C  CG2  A ILE   A 1 23  ? 17.811 1.155   7.677   0.50 13.40 ?  23  ILE   A CG2  1 
ATOM   627  C  CG2  B ILE   A 1 23  ? 18.294 0.786   7.474   0.50 11.74 ?  23  ILE   A CG2  1 
ATOM   628  C  CD1  A ILE   A 1 23  ? 19.228 -1.613  7.841   0.50 14.15 ?  23  ILE   A CD1  1 
ATOM   629  C  CD1  B ILE   A 1 23  ? 19.615 -1.926  7.773   0.50 11.80 ?  23  ILE   A CD1  1 
ATOM   630  H  H    A ILE   A 1 23  ? 15.225 1.108   8.551   0.50 17.57 ?  23  ILE   A H    1 
ATOM   631  H  H    B ILE   A 1 23  ? 15.459 0.757   8.001   0.50 15.68 ?  23  ILE   A H    1 
ATOM   632  H  HA   A ILE   A 1 23  ? 16.431 -0.277  10.364  0.50 16.51 ?  23  ILE   A HA   1 
ATOM   633  H  HA   B ILE   A 1 23  ? 16.480 -0.616  9.910   0.50 15.18 ?  23  ILE   A HA   1 
ATOM   634  H  HB   A ILE   A 1 23  ? 16.788 -0.573  8.060   0.50 16.07 ?  23  ILE   A HB   1 
ATOM   635  H  HB   B ILE   A 1 23  ? 17.100 -0.876  7.620   0.50 14.71 ?  23  ILE   A HB   1 
ATOM   636  H  HG12 A ILE   A 1 23  ? 19.257 -0.308  9.397   0.50 16.69 ?  23  ILE   A HG12 1 
ATOM   637  H  HG12 B ILE   A 1 23  ? 19.260 -0.819  9.442   0.50 14.58 ?  23  ILE   A HG12 1 
ATOM   638  H  HG13 A ILE   A 1 23  ? 18.280 -1.538  9.636   0.50 16.69 ?  23  ILE   A HG13 1 
ATOM   639  H  HG13 B ILE   A 1 23  ? 18.258 -2.039  9.283   0.50 14.58 ?  23  ILE   A HG13 1 
ATOM   640  H  HG21 A ILE   A 1 23  ? 18.164 0.804   6.844   0.50 16.09 ?  23  ILE   A HG21 1 
ATOM   641  H  HG21 B ILE   A 1 23  ? 18.687 0.437   6.654   0.50 14.11 ?  23  ILE   A HG21 1 
ATOM   642  H  HG22 A ILE   A 1 23  ? 17.033 1.709   7.494   0.50 16.09 ?  23  ILE   A HG22 1 
ATOM   643  H  HG22 B ILE   A 1 23  ? 17.620 1.444   7.261   0.50 14.11 ?  23  ILE   A HG22 1 
ATOM   644  H  HG23 A ILE   A 1 23  ? 18.488 1.678   8.130   0.50 16.09 ?  23  ILE   A HG23 1 
ATOM   645  H  HG23 B ILE   A 1 23  ? 18.988 1.183   8.024   0.50 14.11 ?  23  ILE   A HG23 1 
ATOM   646  H  HD11 A ILE   A 1 23  ? 19.930 -2.185  8.186   0.50 17.00 ?  23  ILE   A HD11 1 
ATOM   647  H  HD11 B ILE   A 1 23  ? 20.178 -2.593  8.199   0.50 14.17 ?  23  ILE   A HD11 1 
ATOM   648  H  HD12 A ILE   A 1 23  ? 18.554 -2.147  7.393   0.50 17.00 ?  23  ILE   A HD12 1 
ATOM   649  H  HD12 B ILE   A 1 23  ? 19.072 -2.340  7.087   0.50 14.17 ?  23  ILE   A HD12 1 
ATOM   650  H  HD13 A ILE   A 1 23  ? 19.601 -0.965  7.223   0.50 17.00 ?  23  ILE   A HD13 1 
ATOM   651  H  HD13 B ILE   A 1 23  ? 20.167 -1.229  7.387   0.50 14.17 ?  23  ILE   A HD13 1 
ATOM   652  N  N    A VAL   A 1 24  ? 17.293 2.770   10.402  0.50 14.68 ?  24  VAL   A N    1 
ATOM   653  N  N    B VAL   A 1 24  ? 17.351 2.430   10.014  0.50 13.68 ?  24  VAL   A N    1 
ATOM   654  C  CA   A VAL   A 1 24  ? 17.972 3.765   11.228  0.50 15.77 ?  24  VAL   A CA   1 
ATOM   655  C  CA   B VAL   A 1 24  ? 17.992 3.423   10.870  0.50 14.75 ?  24  VAL   A CA   1 
ATOM   656  C  C    A VAL   A 1 24  ? 17.486 3.674   12.668  0.50 16.38 ?  24  VAL   A C    1 
ATOM   657  C  C    B VAL   A 1 24  ? 17.389 3.390   12.267  0.50 15.88 ?  24  VAL   A C    1 
ATOM   658  O  O    A VAL   A 1 24  ? 18.283 3.599   13.613  0.50 16.07 ?  24  VAL   A O    1 
ATOM   659  O  O    B VAL   A 1 24  ? 18.110 3.411   13.272  0.50 16.22 ?  24  VAL   A O    1 
ATOM   660  C  CB   A VAL   A 1 24  ? 17.757 5.174   10.650  0.50 16.19 ?  24  VAL   A CB   1 
ATOM   661  C  CB   B VAL   A 1 24  ? 17.892 4.818   10.230  0.50 15.71 ?  24  VAL   A CB   1 
ATOM   662  C  CG1  A VAL   A 1 24  ? 18.244 6.235   11.631  0.50 16.38 ?  24  VAL   A CG1  1 
ATOM   663  C  CG1  B VAL   A 1 24  ? 18.532 5.859   11.130  0.50 17.31 ?  24  VAL   A CG1  1 
ATOM   664  C  CG2  A VAL   A 1 24  ? 18.462 5.311   9.306   0.50 16.74 ?  24  VAL   A CG2  1 
ATOM   665  C  CG2  B VAL   A 1 24  ? 18.545 4.810   8.861   0.50 15.63 ?  24  VAL   A CG2  1 
ATOM   666  H  H    A VAL   A 1 24  ? 16.819 3.097   9.763   0.50 17.62 ?  24  VAL   A H    1 
ATOM   667  H  H    B VAL   A 1 24  ? 16.919 2.755   9.350   0.50 16.43 ?  24  VAL   A H    1 
ATOM   668  H  HA   A VAL   A 1 24  ? 18.924 3.583   11.222  0.50 18.94 ?  24  VAL   A HA   1 
ATOM   669  H  HA   B VAL   A 1 24  ? 18.930 3.201   10.956  0.50 17.71 ?  24  VAL   A HA   1 
ATOM   670  H  HB   A VAL   A 1 24  ? 16.808 5.316   10.503  0.50 19.44 ?  24  VAL   A HB   1 
ATOM   671  H  HB   B VAL   A 1 24  ? 16.956 5.048   10.117  0.50 18.86 ?  24  VAL   A HB   1 
ATOM   672  H  HG11 A VAL   A 1 24  ? 18.365 7.070   11.154  0.50 19.67 ?  24  VAL   A HG11 1 
ATOM   673  H  HG11 B VAL   A 1 24  ? 18.650 6.678   10.627  0.50 20.78 ?  24  VAL   A HG11 1 
ATOM   674  H  HG12 A VAL   A 1 24  ? 17.585 6.345   12.332  0.50 19.67 ?  24  VAL   A HG12 1 
ATOM   675  H  HG12 B VAL   A 1 24  ? 17.948 6.020   11.889  0.50 20.78 ?  24  VAL   A HG12 1 
ATOM   676  H  HG13 A VAL   A 1 24  ? 19.090 5.946   12.009  0.50 19.67 ?  24  VAL   A HG13 1 
ATOM   677  H  HG13 B VAL   A 1 24  ? 19.390 5.528   11.435  0.50 20.78 ?  24  VAL   A HG13 1 
ATOM   678  H  HG21 A VAL   A 1 24  ? 18.197 6.149   8.895   0.50 20.10 ?  24  VAL   A HG21 1 
ATOM   679  H  HG21 B VAL   A 1 24  ? 18.618 5.720   8.542   0.50 18.76 ?  24  VAL   A HG21 1 
ATOM   680  H  HG22 A VAL   A 1 24  ? 19.421 5.303   9.450   0.50 20.10 ?  24  VAL   A HG22 1 
ATOM   681  H  HG22 B VAL   A 1 24  ? 19.428 4.414   8.938   0.50 18.76 ?  24  VAL   A HG22 1 
ATOM   682  H  HG23 A VAL   A 1 24  ? 18.205 4.569   8.735   0.50 20.10 ?  24  VAL   A HG23 1 
ATOM   683  H  HG23 B VAL   A 1 24  ? 18.001 4.285   8.254   0.50 18.76 ?  24  VAL   A HG23 1 
ATOM   684  N  N    A GLU   A 1 25  ? 16.165 3.685   12.855  0.50 17.27 ?  25  GLU   A N    1 
ATOM   685  N  N    B GLU   A 1 25  ? 16.058 3.322   12.353  0.50 16.76 ?  25  GLU   A N    1 
ATOM   686  C  CA   A GLU   A 1 25  ? 15.604 3.613   14.199  0.50 18.46 ?  25  GLU   A CA   1 
ATOM   687  C  CA   B GLU   A 1 25  ? 15.403 3.271   13.657  0.50 18.12 ?  25  GLU   A CA   1 
ATOM   688  C  C    A GLU   A 1 25  ? 15.843 2.244   14.824  0.50 17.66 ?  25  GLU   A C    1 
ATOM   689  C  C    B GLU   A 1 25  ? 15.684 1.951   14.368  0.50 18.10 ?  25  GLU   A C    1 
ATOM   690  O  O    A GLU   A 1 25  ? 16.087 2.143   16.032  0.50 18.09 ?  25  GLU   A O    1 
ATOM   691  O  O    B GLU   A 1 25  ? 15.896 1.932   15.586  0.50 18.75 ?  25  GLU   A O    1 
ATOM   692  C  CB   A GLU   A 1 25  ? 14.113 3.953   14.156  0.50 20.68 ?  25  GLU   A CB   1 
ATOM   693  C  CB   B GLU   A 1 25  ? 13.900 3.517   13.504  0.50 19.94 ?  25  GLU   A CB   1 
ATOM   694  C  CG   A GLU   A 1 25  ? 13.837 5.395   13.757  0.50 22.89 ?  25  GLU   A CG   1 
ATOM   695  C  CG   B GLU   A 1 25  ? 13.569 4.903   12.973  0.50 22.52 ?  25  GLU   A CG   1 
ATOM   696  C  CD   A GLU   A 1 25  ? 14.623 6.393   14.595  0.50 24.80 ?  25  GLU   A CD   1 
ATOM   697  C  CD   B GLU   A 1 25  ? 14.136 6.003   13.842  0.50 24.79 ?  25  GLU   A CD   1 
ATOM   698  O  OE1  A GLU   A 1 25  ? 14.664 6.232   15.834  0.50 25.44 ?  25  GLU   A OE1  1 
ATOM   699  O  OE1  B GLU   A 1 25  ? 14.171 5.821   15.078  0.50 26.14 ?  25  GLU   A OE1  1 
ATOM   700  O  OE2  A GLU   A 1 25  ? 15.222 7.320   14.011  0.50 25.74 -1 25  GLU   A OE2  1 
ATOM   701  O  OE2  B GLU   A 1 25  ? 14.556 7.042   13.292  0.50 25.61 -1 25  GLU   A OE2  1 
ATOM   702  H  H    A GLU   A 1 25  ? 15.582 3.741   12.224  0.50 20.73 ?  25  GLU   A H    1 
ATOM   703  H  H    B GLU   A 1 25  ? 15.519 3.304   11.683  0.50 20.13 ?  25  GLU   A H    1 
ATOM   704  H  HA   A GLU   A 1 25  ? 16.045 4.267   14.759  0.50 22.16 ?  25  GLU   A HA   1 
ATOM   705  H  HA   B GLU   A 1 25  ? 15.761 3.976   14.214  0.50 21.75 ?  25  GLU   A HA   1 
ATOM   706  H  HB2  A GLU   A 1 25  ? 13.672 3.379   13.507  0.50 24.83 ?  25  GLU   A HB2  1 
ATOM   707  H  HB2  B GLU   A 1 25  ? 13.532 2.869   12.883  0.50 23.94 ?  25  GLU   A HB2  1 
ATOM   708  H  HB3  A GLU   A 1 25  ? 13.726 3.812   15.034  0.50 24.83 ?  25  GLU   A HB3  1 
ATOM   709  H  HB3  B GLU   A 1 25  ? 13.471 3.422   14.370  0.50 23.94 ?  25  GLU   A HB3  1 
ATOM   710  H  HG2  A GLU   A 1 25  ? 14.097 5.522   12.833  0.50 27.48 ?  25  GLU   A HG2  1 
ATOM   711  H  HG2  B GLU   A 1 25  ? 13.946 5.002   12.086  0.50 27.03 ?  25  GLU   A HG2  1 
ATOM   712  H  HG3  A GLU   A 1 25  ? 12.887 5.576   13.863  0.50 27.48 ?  25  GLU   A HG3  1 
ATOM   713  H  HG3  B GLU   A 1 25  ? 12.606 5.013   12.942  0.50 27.03 ?  25  GLU   A HG3  1 
ATOM   714  N  N    A GLU   A 1 26  ? 15.786 1.181   14.020  0.50 17.41 ?  26  GLU   A N    1 
ATOM   715  N  N    B GLU   A 1 26  ? 15.689 0.839   13.630  0.50 18.08 ?  26  GLU   A N    1 
ATOM   716  C  CA   A GLU   A 1 26  ? 16.087 -0.152  14.533  0.50 17.09 ?  26  GLU   A CA   1 
ATOM   717  C  CA   B GLU   A 1 26  ? 16.053 -0.442  14.233  0.50 18.50 ?  26  GLU   A CA   1 
ATOM   718  C  C    A GLU   A 1 26  ? 17.514 -0.222  15.062  0.50 15.88 ?  26  GLU   A C    1 
ATOM   719  C  C    B GLU   A 1 26  ? 17.472 -0.404  14.786  0.50 17.42 ?  26  GLU   A C    1 
ATOM   720  O  O    A GLU   A 1 26  ? 17.757 -0.719  16.168  0.50 15.76 ?  26  GLU   A O    1 
ATOM   721  O  O    B GLU   A 1 26  ? 17.741 -0.940  15.867  0.50 17.57 ?  26  GLU   A O    1 
ATOM   722  C  CB   A GLU   A 1 26  ? 15.888 -1.196  13.433  0.50 18.20 ?  26  GLU   A CB   1 
ATOM   723  C  CB   B GLU   A 1 26  ? 15.922 -1.566  13.205  0.50 19.94 ?  26  GLU   A CB   1 
ATOM   724  C  CG   A GLU   A 1 26  ? 14.495 -1.767  13.334  0.50 20.22 ?  26  GLU   A CG   1 
ATOM   725  C  CG   B GLU   A 1 26  ? 14.496 -1.969  12.903  0.50 20.92 ?  26  GLU   A CG   1 
ATOM   726  C  CD   A GLU   A 1 26  ? 14.116 -2.592  14.555  0.50 21.45 ?  26  GLU   A CD   1 
ATOM   727  C  CD   B GLU   A 1 26  ? 13.788 -2.554  14.106  0.50 21.52 ?  26  GLU   A CD   1 
ATOM   728  O  OE1  A GLU   A 1 26  ? 14.551 -3.761  14.674  0.50 22.14 ?  26  GLU   A OE1  1 
ATOM   729  O  OE1  B GLU   A 1 26  ? 14.282 -3.552  14.676  0.50 22.54 ?  26  GLU   A OE1  1 
ATOM   730  O  OE2  A GLU   A 1 26  ? 13.390 -2.054  15.406  0.50 21.92 -1 26  GLU   A OE2  1 
ATOM   731  O  OE2  B GLU   A 1 26  ? 12.738 -2.003  14.484  0.50 20.45 -1 26  GLU   A OE2  1 
ATOM   732  H  H    A GLU   A 1 26  ? 15.587 1.211   13.184  0.50 20.91 ?  26  GLU   A H    1 
ATOM   733  H  H    B GLU   A 1 26  ? 15.487 0.797   12.796  0.50 21.70 ?  26  GLU   A H    1 
ATOM   734  H  HA   A GLU   A 1 26  ? 15.486 -0.352  15.263  0.50 20.52 ?  26  GLU   A HA   1 
ATOM   735  H  HA   B GLU   A 1 26  ? 15.452 -0.631  14.969  0.50 22.22 ?  26  GLU   A HA   1 
ATOM   736  H  HB2  A GLU   A 1 26  ? 16.103 -0.787  12.580  0.50 21.85 ?  26  GLU   A HB2  1 
ATOM   737  H  HB2  B GLU   A 1 26  ? 16.330 -1.277  12.373  0.50 23.94 ?  26  GLU   A HB2  1 
ATOM   738  H  HB3  A GLU   A 1 26  ? 16.495 -1.932  13.602  0.50 21.85 ?  26  GLU   A HB3  1 
ATOM   739  H  HB3  B GLU   A 1 26  ? 16.387 -2.351  13.540  0.50 23.94 ?  26  GLU   A HB3  1 
ATOM   740  H  HG2  A GLU   A 1 26  ? 13.871 -1.028  13.245  0.50 24.28 ?  26  GLU   A HG2  1 
ATOM   741  H  HG2  B GLU   A 1 26  ? 14.001 -1.187  12.613  0.50 25.11 ?  26  GLU   A HG2  1 
ATOM   742  H  HG3  A GLU   A 1 26  ? 14.445 -2.337  12.551  0.50 24.28 ?  26  GLU   A HG3  1 
ATOM   743  H  HG3  B GLU   A 1 26  ? 14.496 -2.642  12.207  0.50 25.11 ?  26  GLU   A HG3  1 
ATOM   744  N  N    A ALA   A 1 27  ? 18.477 0.273   14.278  0.50 15.16 ?  27  ALA   A N    1 
ATOM   745  N  N    B ALA   A 1 27  ? 18.398 0.219   14.055  0.50 16.38 ?  27  ALA   A N    1 
ATOM   746  C  CA   A ALA   A 1 27  ? 19.874 0.195   14.692  0.50 15.13 ?  27  ALA   A CA   1 
ATOM   747  C  CA   B ALA   A 1 27  ? 19.776 0.300   14.529  0.50 16.14 ?  27  ALA   A CA   1 
ATOM   748  C  C    A ALA   A 1 27  ? 20.110 0.980   15.976  0.50 16.52 ?  27  ALA   A C    1 
ATOM   749  C  C    B ALA   A 1 27  ? 19.871 1.145   15.795  0.50 17.17 ?  27  ALA   A C    1 
ATOM   750  O  O    A ALA   A 1 27  ? 20.787 0.498   16.892  0.50 16.83 ?  27  ALA   A O    1 
ATOM   751  O  O    B ALA   A 1 27  ? 20.531 0.756   16.765  0.50 17.01 ?  27  ALA   A O    1 
ATOM   752  C  CB   A ALA   A 1 27  ? 20.788 0.694   13.569  0.50 14.88 ?  27  ALA   A CB   1 
ATOM   753  C  CB   B ALA   A 1 27  ? 20.677 0.859   13.427  0.50 15.52 ?  27  ALA   A CB   1 
ATOM   754  H  H    A ALA   A 1 27  ? 18.349 0.661   13.520  0.50 18.20 ?  27  ALA   A H    1 
ATOM   755  H  H    B ALA   A 1 27  ? 18.255 0.592   13.292  0.50 19.67 ?  27  ALA   A H    1 
ATOM   756  H  HA   A ALA   A 1 27  ? 20.099 -0.730  14.864  0.50 18.17 ?  27  ALA   A HA   1 
ATOM   757  H  HA   B ALA   A 1 27  ? 20.085 -0.592  14.742  0.50 19.38 ?  27  ALA   A HA   1 
ATOM   758  H  HB1  A ALA   A 1 27  ? 21.714 0.630   13.860  0.50 17.87 ?  27  ALA   A HB1  1 
ATOM   759  H  HB1  B ALA   A 1 27  ? 21.587 0.904   13.759  0.50 18.64 ?  27  ALA   A HB1  1 
ATOM   760  H  HB2  A ALA   A 1 27  ? 20.655 0.139   12.783  0.50 17.87 ?  27  ALA   A HB2  1 
ATOM   761  H  HB2  B ALA   A 1 27  ? 20.634 0.272   12.656  0.50 18.64 ?  27  ALA   A HB2  1 
ATOM   762  H  HB3  A ALA   A 1 27  ? 20.571 1.615   13.363  0.50 17.87 ?  27  ALA   A HB3  1 
ATOM   763  H  HB3  B ALA   A 1 27  ? 20.369 1.746   13.185  0.50 18.64 ?  27  ALA   A HB3  1 
ATOM   764  N  N    A LYS   A 1 28  ? 19.550 2.188   16.068  0.50 18.42 ?  28  LYS   A N    1 
ATOM   765  N  N    B LYS   A 1 28  ? 19.203 2.301   15.811  0.50 19.06 ?  28  LYS   A N    1 
ATOM   766  C  CA   A LYS   A 1 28  ? 19.709 2.984   17.281  0.50 20.85 ?  28  LYS   A CA   1 
ATOM   767  C  CA   B LYS   A 1 28  ? 19.280 3.182   16.973  0.50 21.52 ?  28  LYS   A CA   1 
ATOM   768  C  C    A LYS   A 1 28  ? 19.155 2.251   18.495  0.50 22.05 ?  28  LYS   A C    1 
ATOM   769  C  C    B LYS   A 1 28  ? 18.769 2.505   18.238  0.50 22.88 ?  28  LYS   A C    1 
ATOM   770  O  O    A LYS   A 1 28  ? 19.764 2.266   19.571  0.50 22.93 ?  28  LYS   A O    1 
ATOM   771  O  O    B LYS   A 1 28  ? 19.209 2.846   19.341  0.50 23.53 ?  28  LYS   A O    1 
ATOM   772  C  CB   A LYS   A 1 28  ? 19.040 4.351   17.111  0.50 22.02 ?  28  LYS   A CB   1 
ATOM   773  C  CB   B LYS   A 1 28  ? 18.497 4.470   16.711  0.50 22.88 ?  28  LYS   A CB   1 
ATOM   774  C  CG   A LYS   A 1 28  ? 19.820 5.308   16.219  0.50 23.03 ?  28  LYS   A CG   1 
ATOM   775  C  CG   B LYS   A 1 28  ? 19.128 5.380   15.676  0.50 24.20 ?  28  LYS   A CG   1 
ATOM   776  C  CD   A LYS   A 1 28  ? 19.277 6.729   16.283  0.50 24.56 ?  28  LYS   A CD   1 
ATOM   777  C  CD   B LYS   A 1 28  ? 18.334 6.666   15.513  0.50 25.90 ?  28  LYS   A CD   1 
ATOM   778  C  CE   A LYS   A 1 28  ? 17.964 6.865   15.534  0.50 25.72 ?  28  LYS   A CE   1 
ATOM   779  C  CE   B LYS   A 1 28  ? 18.951 7.568   14.456  0.50 27.26 ?  28  LYS   A CE   1 
ATOM   780  N  NZ   A LYS   A 1 28  ? 17.509 8.281   15.483  0.50 26.37 ?  28  LYS   A NZ   1 
ATOM   781  N  NZ   B LYS   A 1 28  ? 18.239 8.873   14.339  0.50 28.03 ?  28  LYS   A NZ   1 
ATOM   782  H  H    A LYS   A 1 28  ? 19.084 2.558   15.454  0.50 22.11 ?  28  LYS   A H    1 
ATOM   783  H  H    B LYS   A 1 28  ? 18.705 2.591   15.176  0.50 22.88 ?  28  LYS   A H    1 
ATOM   784  H  HA   A LYS   A 1 28  ? 20.653 3.137   17.440  0.50 25.03 ?  28  LYS   A HA   1 
ATOM   785  H  HA   B LYS   A 1 28  ? 20.204 3.424   17.126  0.50 25.84 ?  28  LYS   A HA   1 
ATOM   786  H  HB2  A LYS   A 1 28  ? 18.165 4.226   16.712  0.50 26.44 ?  28  LYS   A HB2  1 
ATOM   787  H  HB2  B LYS   A 1 28  ? 17.609 4.239   16.396  0.50 27.47 ?  28  LYS   A HB2  1 
ATOM   788  H  HB3  A LYS   A 1 28  ? 18.949 4.770   17.981  0.50 26.44 ?  28  LYS   A HB3  1 
ATOM   789  H  HB3  B LYS   A 1 28  ? 18.431 4.971   17.539  0.50 27.47 ?  28  LYS   A HB3  1 
ATOM   790  H  HG2  A LYS   A 1 28  ? 20.746 5.328   16.504  0.50 27.65 ?  28  LYS   A HG2  1 
ATOM   791  H  HG2  B LYS   A 1 28  ? 20.026 5.612   15.958  0.50 29.06 ?  28  LYS   A HG2  1 
ATOM   792  H  HG3  A LYS   A 1 28  ? 19.760 5.006   15.299  0.50 27.65 ?  28  LYS   A HG3  1 
ATOM   793  H  HG3  B LYS   A 1 28  ? 19.153 4.926   14.819  0.50 29.06 ?  28  LYS   A HG3  1 
ATOM   794  H  HD2  A LYS   A 1 28  ? 19.123 6.972   17.210  0.50 29.48 ?  28  LYS   A HD2  1 
ATOM   795  H  HD2  B LYS   A 1 28  ? 17.428 6.451   15.239  0.50 31.09 ?  28  LYS   A HD2  1 
ATOM   796  H  HD3  A LYS   A 1 28  ? 19.919 7.336   15.881  0.50 29.48 ?  28  LYS   A HD3  1 
ATOM   797  H  HD3  B LYS   A 1 28  ? 18.325 7.147   16.356  0.50 31.09 ?  28  LYS   A HD3  1 
ATOM   798  H  HE2  A LYS   A 1 28  ? 18.082 6.550   14.624  0.50 30.88 ?  28  LYS   A HE2  1 
ATOM   799  H  HE2  B LYS   A 1 28  ? 19.874 7.747   14.692  0.50 32.73 ?  28  LYS   A HE2  1 
ATOM   800  H  HE3  A LYS   A 1 28  ? 17.283 6.343   15.985  0.50 30.88 ?  28  LYS   A HE3  1 
ATOM   801  H  HE3  B LYS   A 1 28  ? 18.909 7.123   13.595  0.50 32.73 ?  28  LYS   A HE3  1 
ATOM   802  H  HZ1  A LYS   A 1 28  ? 16.740 8.337   15.040  0.50 31.66 ?  28  LYS   A HZ1  1 
ATOM   803  H  HZ1  B LYS   A 1 28  ? 18.625 9.375   13.713  0.50 33.65 ?  28  LYS   A HZ1  1 
ATOM   804  H  HZ2  A LYS   A 1 28  ? 17.392 8.592   16.308  0.50 31.66 ?  28  LYS   A HZ2  1 
ATOM   805  H  HZ2  B LYS   A 1 28  ? 17.388 8.737   14.117  0.50 33.65 ?  28  LYS   A HZ2  1 
ATOM   806  H  HZ3  A LYS   A 1 28  ? 18.119 8.781   15.069  0.50 31.66 ?  28  LYS   A HZ3  1 
ATOM   807  H  HZ3  B LYS   A 1 28  ? 18.269 9.306   15.116  0.50 33.65 ?  28  LYS   A HZ3  1 
ATOM   808  N  N    A LYS   A 1 29  ? 18.008 1.588   18.339  0.50 22.87 ?  29  LYS   A N    1 
ATOM   809  N  N    B LYS   A 1 29  ? 17.851 1.548   18.104  0.50 24.02 ?  29  LYS   A N    1 
ATOM   810  C  CA   A LYS   A 1 29  ? 17.409 0.866   19.458  0.50 24.54 ?  29  LYS   A CA   1 
ATOM   811  C  CA   B LYS   A 1 29  ? 17.226 0.921   19.263  0.50 25.73 ?  29  LYS   A CA   1 
ATOM   812  C  C    A LYS   A 1 29  ? 18.235 -0.361  19.822  0.50 23.90 ?  29  LYS   A C    1 
ATOM   813  C  C    B LYS   A 1 29  ? 17.944 -0.343  19.718  0.50 25.05 ?  29  LYS   A C    1 
ATOM   814  O  O    A LYS   A 1 29  ? 18.638 -0.533  20.978  0.50 24.24 ?  29  LYS   A O    1 
ATOM   815  O  O    B LYS   A 1 29  ? 17.948 -0.642  20.918  0.50 25.34 ?  29  LYS   A O    1 
ATOM   816  C  CB   A LYS   A 1 29  ? 15.980 0.455   19.097  0.50 27.05 ?  29  LYS   A CB   1 
ATOM   817  C  CB   B LYS   A 1 29  ? 15.759 0.600   18.950  0.50 28.14 ?  29  LYS   A CB   1 
ATOM   818  C  CG   A LYS   A 1 29  ? 15.240 -0.280  20.205  0.50 29.80 ?  29  LYS   A CG   1 
ATOM   819  C  CG   B LYS   A 1 29  ? 14.970 -0.006  20.107  0.50 30.82 ?  29  LYS   A CG   1 
ATOM   820  C  CD   A LYS   A 1 29  ? 14.847 0.664   21.328  0.50 32.38 ?  29  LYS   A CD   1 
ATOM   821  C  CD   B LYS   A 1 29  ? 14.850 0.955   21.281  0.50 33.26 ?  29  LYS   A CD   1 
ATOM   822  C  CE   A LYS   A 1 29  ? 13.956 -0.024  22.349  0.50 34.02 ?  29  LYS   A CE   1 
ATOM   823  C  CE   B LYS   A 1 29  ? 13.990 0.363   22.388  0.50 34.86 ?  29  LYS   A CE   1 
ATOM   824  N  NZ   A LYS   A 1 29  ? 13.442 0.934   23.366  0.50 35.06 ?  29  LYS   A NZ   1 
ATOM   825  N  NZ   B LYS   A 1 29  ? 13.922 1.250   23.581  0.50 35.86 ?  29  LYS   A NZ   1 
ATOM   826  H  H    A LYS   A 1 29  ? 17.568 1.534   17.604  0.50 27.45 ?  29  LYS   A H    1 
ATOM   827  H  H    B LYS   A 1 29  ? 17.574 1.244   17.350  0.50 28.83 ?  29  LYS   A H    1 
ATOM   828  H  HA   A LYS   A 1 29  ? 17.369 1.448   20.233  0.50 29.46 ?  29  LYS   A HA   1 
ATOM   829  H  HA   B LYS   A 1 29  ? 17.239 1.545   20.002  0.50 30.89 ?  29  LYS   A HA   1 
ATOM   830  H  HB2  A LYS   A 1 29  ? 15.469 1.252   18.886  0.50 32.47 ?  29  LYS   A HB2  1 
ATOM   831  H  HB2  B LYS   A 1 29  ? 15.310 1.422   18.693  0.50 33.78 ?  29  LYS   A HB2  1 
ATOM   832  H  HB3  A LYS   A 1 29  ? 16.008 -0.131  18.326  0.50 32.47 ?  29  LYS   A HB3  1 
ATOM   833  H  HB3  B LYS   A 1 29  ? 15.727 -0.031  18.215  0.50 33.78 ?  29  LYS   A HB3  1 
ATOM   834  H  HG2  A LYS   A 1 29  ? 14.431 -0.672  19.841  0.50 35.78 ?  29  LYS   A HG2  1 
ATOM   835  H  HG2  B LYS   A 1 29  ? 14.073 -0.220  19.803  0.50 36.99 ?  29  LYS   A HG2  1 
ATOM   836  H  HG3  A LYS   A 1 29  ? 15.807 -0.976  20.576  0.50 35.78 ?  29  LYS   A HG3  1 
ATOM   837  H  HG3  B LYS   A 1 29  ? 15.414 -0.810  20.418  0.50 36.99 ?  29  LYS   A HG3  1 
ATOM   838  H  HD2  A LYS   A 1 29  ? 15.647 0.975   21.780  0.50 38.87 ?  29  LYS   A HD2  1 
ATOM   839  H  HD2  B LYS   A 1 29  ? 15.731 1.133   21.644  0.50 39.92 ?  29  LYS   A HD2  1 
ATOM   840  H  HD3  A LYS   A 1 29  ? 14.359 1.416   20.956  0.50 38.87 ?  29  LYS   A HD3  1 
ATOM   841  H  HD3  B LYS   A 1 29  ? 14.435 1.779   20.981  0.50 39.92 ?  29  LYS   A HD3  1 
ATOM   842  H  HE2  A LYS   A 1 29  ? 13.196 -0.421  21.895  0.50 40.83 ?  29  LYS   A HE2  1 
ATOM   843  H  HE2  B LYS   A 1 29  ? 13.087 0.234   22.056  0.50 41.84 ?  29  LYS   A HE2  1 
ATOM   844  H  HE3  A LYS   A 1 29  ? 14.467 -0.709  22.808  0.50 40.83 ?  29  LYS   A HE3  1 
ATOM   845  H  HE3  B LYS   A 1 29  ? 14.367 -0.488  22.664  0.50 41.84 ?  29  LYS   A HE3  1 
ATOM   846  H  HZ1  A LYS   A 1 29  ? 12.925 0.507   23.951  0.50 42.09 ?  29  LYS   A HZ1  1 
ATOM   847  H  HZ1  B LYS   A 1 29  ? 13.386 0.892   24.195  0.50 43.05 ?  29  LYS   A HZ1  1 
ATOM   848  H  HZ2  A LYS   A 1 29  ? 14.122 1.309   23.801  0.50 42.09 ?  29  LYS   A HZ2  1 
ATOM   849  H  HZ2  B LYS   A 1 29  ? 14.734 1.350   23.930  0.50 43.05 ?  29  LYS   A HZ2  1 
ATOM   850  H  HZ3  A LYS   A 1 29  ? 12.965 1.572   22.969  0.50 42.09 ?  29  LYS   A HZ3  1 
ATOM   851  H  HZ3  B LYS   A 1 29  ? 13.605 2.048   23.349  0.50 43.05 ?  29  LYS   A HZ3  1 
ATOM   852  N  N    A VAL   A 1 30  ? 18.485 -1.233  18.845  0.50 22.91 ?  30  VAL   A N    1 
ATOM   853  N  N    B VAL   A 1 30  ? 18.564 -1.085  18.800  0.50 24.01 ?  30  VAL   A N    1 
ATOM   854  C  CA   A VAL   A 1 30  ? 19.151 -2.503  19.116  0.50 22.25 ?  30  VAL   A CA   1 
ATOM   855  C  CA   B VAL   A 1 30  ? 19.124 -2.397  19.111  0.50 23.21 ?  30  VAL   A CA   1 
ATOM   856  C  C    A VAL   A 1 30  ? 20.649 -2.312  19.336  0.50 21.37 ?  30  VAL   A C    1 
ATOM   857  C  C    B VAL   A 1 30  ? 20.631 -2.303  19.327  0.50 21.84 ?  30  VAL   A C    1 
ATOM   858  O  O    A VAL   A 1 30  ? 21.253 -3.001  20.165  0.50 21.77 ?  30  VAL   A O    1 
ATOM   859  O  O    B VAL   A 1 30  ? 21.204 -3.049  20.128  0.50 22.12 ?  30  VAL   A O    1 
ATOM   860  C  CB   A VAL   A 1 30  ? 18.858 -3.501  17.979  0.50 22.75 ?  30  VAL   A CB   1 
ATOM   861  C  CB   B VAL   A 1 30  ? 18.794 -3.399  17.989  0.50 23.93 ?  30  VAL   A CB   1 
ATOM   862  C  CG1  A VAL   A 1 30  ? 19.652 -4.788  18.171  0.50 22.95 ?  30  VAL   A CG1  1 
ATOM   863  C  CG1  B VAL   A 1 30  ? 19.493 -4.729  18.230  0.50 24.30 ?  30  VAL   A CG1  1 
ATOM   864  C  CG2  A VAL   A 1 30  ? 17.366 -3.800  17.897  0.50 23.31 ?  30  VAL   A CG2  1 
ATOM   865  C  CG2  B VAL   A 1 30  ? 17.290 -3.593  17.877  0.50 24.45 ?  30  VAL   A CG2  1 
ATOM   866  H  H    A VAL   A 1 30  ? 18.265 -1.116  18.023  0.50 27.51 ?  30  VAL   A H    1 
ATOM   867  H  H    B VAL   A 1 30  ? 18.672 -0.847  17.980  0.50 28.82 ?  30  VAL   A H    1 
ATOM   868  H  HA   A VAL   A 1 30  ? 18.774 -2.877  19.930  0.50 26.72 ?  30  VAL   A HA   1 
ATOM   869  H  HA   B VAL   A 1 30  ? 18.718 -2.724  19.932  0.50 27.86 ?  30  VAL   A HA   1 
ATOM   870  H  HB   A VAL   A 1 30  ? 19.130 -3.108  17.136  0.50 27.31 ?  30  VAL   A HB   1 
ATOM   871  H  HB   B VAL   A 1 30  ? 19.114 -3.044  17.145  0.50 28.73 ?  30  VAL   A HB   1 
ATOM   872  H  HG11 A VAL   A 1 30  ? 19.292 -5.470  17.581  0.50 27.56 ?  30  VAL   A HG11 1 
ATOM   873  H  HG11 B VAL   A 1 30  ? 19.089 -5.403  17.661  0.50 29.18 ?  30  VAL   A HG11 1 
ATOM   874  H  HG12 A VAL   A 1 30  ? 20.582 -4.624  17.956  0.50 27.56 ?  30  VAL   A HG12 1 
ATOM   875  H  HG12 B VAL   A 1 30  ? 20.434 -4.638  18.013  0.50 29.18 ?  30  VAL   A HG12 1 
ATOM   876  H  HG13 A VAL   A 1 30  ? 19.568 -5.076  19.094  0.50 27.56 ?  30  VAL   A HG13 1 
ATOM   877  H  HG13 B VAL   A 1 30  ? 19.387 -4.977  19.161  0.50 29.18 ?  30  VAL   A HG13 1 
ATOM   878  H  HG21 A VAL   A 1 30  ? 17.213 -4.454  17.196  0.50 27.99 ?  30  VAL   A HG21 1 
ATOM   879  H  HG21 B VAL   A 1 30  ? 17.108 -4.248  17.185  0.50 29.36 ?  30  VAL   A HG21 1 
ATOM   880  H  HG22 A VAL   A 1 30  ? 17.067 -4.154  18.749  0.50 27.99 ?  30  VAL   A HG22 1 
ATOM   881  H  HG22 B VAL   A 1 30  ? 16.949 -3.909  18.729  0.50 29.36 ?  30  VAL   A HG22 1 
ATOM   882  H  HG23 A VAL   A 1 30  ? 16.891 -2.980  17.692  0.50 27.99 ?  30  VAL   A HG23 1 
ATOM   883  H  HG23 B VAL   A 1 30  ? 16.880 -2.746  17.648  0.50 29.36 ?  30  VAL   A HG23 1 
ATOM   884  N  N    . LYS   A 1 31  ? 21.276 -1.390  18.610  1.00 20.84 ?  31  LYS   A N    1 
ATOM   885  C  CA   . LYS   A 1 31  ? 22.729 -1.270  18.584  1.00 21.05 ?  31  LYS   A CA   1 
ATOM   886  C  C    . LYS   A 1 31  ? 23.351 -2.630  18.252  1.00 19.04 ?  31  LYS   A C    1 
ATOM   887  O  O    . LYS   A 1 31  ? 24.127 -3.178  19.041  1.00 20.28 ?  31  LYS   A O    1 
ATOM   888  C  CB   . LYS   A 1 31  ? 23.291 -0.710  19.883  1.00 26.01 ?  31  LYS   A CB   1 
ATOM   889  C  CG   . LYS   A 1 31  ? 22.630 0.583   20.329  1.00 31.75 ?  31  LYS   A CG   1 
ATOM   890  C  CD   . LYS   A 1 31  ? 23.651 1.599   20.817  1.00 36.20 ?  31  LYS   A CD   1 
ATOM   891  C  CE   . LYS   A 1 31  ? 23.011 2.637   21.727  1.00 39.13 ?  31  LYS   A CE   1 
ATOM   892  N  NZ   . LYS   A 1 31  ? 21.809 3.267   21.117  1.00 40.79 ?  31  LYS   A NZ   1 
ATOM   893  H  H    A LYS   A 1 31  ? 20.873 -0.814  18.118  0.50 25.02 ?  31  LYS   A H    1 
ATOM   894  H  H    B LYS   A 1 31  ? 20.879 -0.813  18.114  0.50 25.02 ?  31  LYS   A H    1 
ATOM   895  H  HA   . LYS   A 1 31  ? 22.968 -0.654  17.879  1.00 25.27 ?  31  LYS   A HA   1 
ATOM   896  H  HB2  . LYS   A 1 31  ? 23.163 -1.369  20.574  1.00 31.23 ?  31  LYS   A HB2  1 
ATOM   897  H  HB3  . LYS   A 1 31  ? 24.241 -0.537  19.762  1.00 31.23 ?  31  LYS   A HB3  1 
ATOM   898  H  HG2  . LYS   A 1 31  ? 22.149 0.971   19.581  1.00 38.12 ?  31  LYS   A HG2  1 
ATOM   899  H  HG3  . LYS   A 1 31  ? 22.020 0.393   21.058  1.00 38.12 ?  31  LYS   A HG3  1 
ATOM   900  H  HD2  . LYS   A 1 31  ? 24.345 1.142   21.317  1.00 43.46 ?  31  LYS   A HD2  1 
ATOM   901  H  HD3  . LYS   A 1 31  ? 24.035 2.059   20.053  1.00 43.46 ?  31  LYS   A HD3  1 
ATOM   902  H  HE2  . LYS   A 1 31  ? 22.740 2.209   22.554  1.00 46.97 ?  31  LYS   A HE2  1 
ATOM   903  H  HE3  . LYS   A 1 31  ? 23.656 3.338   21.911  1.00 46.97 ?  31  LYS   A HE3  1 
ATOM   904  H  HZ1  . LYS   A 1 31  ? 21.486 3.895   21.659  1.00 48.96 ?  31  LYS   A HZ1  1 
ATOM   905  H  HZ2  . LYS   A 1 31  ? 22.022 3.638   20.337  1.00 48.96 ?  31  LYS   A HZ2  1 
ATOM   906  H  HZ3  . LYS   A 1 31  ? 21.179 2.652   20.981  1.00 48.96 ?  31  LYS   A HZ3  1 
ATOM   907  N  N    . PRO   A 1 32  ? 23.022 -3.194  17.096  1.00 16.56 ?  32  PRO   A N    1 
ATOM   908  C  CA   . PRO   A 1 32  ? 23.493 -4.538  16.765  1.00 16.58 ?  32  PRO   A CA   1 
ATOM   909  C  C    . PRO   A 1 32  ? 24.993 -4.556  16.556  1.00 16.52 ?  32  PRO   A C    1 
ATOM   910  O  O    . PRO   A 1 32  ? 25.635 -3.529  16.336  1.00 16.44 ?  32  PRO   A O    1 
ATOM   911  C  CB   . PRO   A 1 32  ? 22.765 -4.843  15.453  1.00 16.66 ?  32  PRO   A CB   1 
ATOM   912  C  CG   . PRO   A 1 32  ? 22.592 -3.490  14.820  1.00 15.47 ?  32  PRO   A CG   1 
ATOM   913  C  CD   . PRO   A 1 32  ? 22.293 -2.579  15.975  1.00 15.72 ?  32  PRO   A CD   1 
ATOM   914  H  HA   . PRO   A 1 32  ? 23.242 -5.178  17.447  1.00 19.91 ?  32  PRO   A HA   1 
ATOM   915  H  HB2  . PRO   A 1 32  ? 23.312 -5.423  14.896  1.00 20.00 ?  32  PRO   A HB2  1 
ATOM   916  H  HB3  . PRO   A 1 32  ? 21.906 -5.257  15.640  1.00 20.00 ?  32  PRO   A HB3  1 
ATOM   917  H  HG2  . PRO   A 1 32  ? 23.408 -3.239  14.370  1.00 18.58 ?  32  PRO   A HG2  1 
ATOM   918  H  HG3  . PRO   A 1 32  ? 21.846 -3.524  14.196  1.00 18.58 ?  32  PRO   A HG3  1 
ATOM   919  H  HD2  . PRO   A 1 32  ? 22.636 -1.692  15.782  1.00 18.87 ?  32  PRO   A HD2  1 
ATOM   920  H  HD3  . PRO   A 1 32  ? 21.342 -2.565  16.150  1.00 18.87 ?  32  PRO   A HD3  1 
ATOM   921  N  N    . THR   A 1 33  ? 25.546 -5.766  16.596  1.00 16.08 ?  33  THR   A N    1 
ATOM   922  C  CA   . THR   A 1 33  ? 26.956 -5.932  16.276  1.00 16.44 ?  33  THR   A CA   1 
ATOM   923  C  C    . THR   A 1 33  ? 27.250 -5.477  14.853  1.00 14.74 ?  33  THR   A C    1 
ATOM   924  O  O    . THR   A 1 33  ? 28.281 -4.837  14.600  1.00 15.23 ?  33  THR   A O    1 
ATOM   925  C  CB   . THR   A 1 33  ? 27.359 -7.392  16.486  1.00 18.23 ?  33  THR   A CB   1 
ATOM   926  O  OG1  . THR   A 1 33  ? 27.046 -7.778  17.828  1.00 19.97 ?  33  THR   A OG1  1 
ATOM   927  C  CG2  . THR   A 1 33  ? 28.850 -7.583  16.246  1.00 19.18 ?  33  THR   A CG2  1 
ATOM   928  H  H    . THR   A 1 33  ? 25.133 -6.495  16.791  1.00 19.31 ?  33  THR   A H    1 
ATOM   929  H  HA   . THR   A 1 33  ? 27.485 -5.391  16.880  1.00 19.74 ?  33  THR   A HA   1 
ATOM   930  H  HB   . THR   A 1 33  ? 26.873 -7.962  15.867  1.00 21.89 ?  33  THR   A HB   1 
ATOM   931  H  HG1  . THR   A 1 33  ? 27.467 -7.293  18.375  1.00 23.98 ?  33  THR   A HG1  1 
ATOM   932  H  HG21 . THR   A 1 33  ? 29.121 -8.473  16.529  1.00 23.03 ?  33  THR   A HG21 1 
ATOM   933  H  HG22 . THR   A 1 33  ? 29.054 -7.478  15.306  1.00 23.03 ?  33  THR   A HG22 1 
ATOM   934  H  HG23 . THR   A 1 33  ? 29.353 -6.929  16.756  1.00 23.03 ?  33  THR   A HG23 1 
ATOM   935  N  N    . VAL   A 1 34  ? 26.359 -5.793  13.912  1.00 13.51 ?  34  VAL   A N    1 
ATOM   936  C  CA   . VAL   A 1 34  ? 26.552 -5.465  12.504  1.00 12.16 ?  34  VAL   A CA   1 
ATOM   937  C  C    . VAL   A 1 34  ? 25.253 -4.905  11.939  1.00 11.77 ?  34  VAL   A C    1 
ATOM   938  O  O    . VAL   A 1 34  ? 24.213 -5.577  11.979  1.00 12.78 ?  34  VAL   A O    1 
ATOM   939  C  CB   . VAL   A 1 34  ? 26.999 -6.678  11.664  1.00 12.87 ?  34  VAL   A CB   1 
ATOM   940  C  CG1  . VAL   A 1 34  ? 27.183 -6.259  10.212  1.00 13.02 ?  34  VAL   A CG1  1 
ATOM   941  C  CG2  . VAL   A 1 34  ? 28.277 -7.297  12.223  1.00 14.31 ?  34  VAL   A CG2  1 
ATOM   942  H  H    . VAL   A 1 34  ? 25.622 -6.214  14.071  1.00 16.23 ?  34  VAL   A H    1 
ATOM   943  H  HA   . VAL   A 1 34  ? 27.232 -4.778  12.427  1.00 14.61 ?  34  VAL   A HA   1 
ATOM   944  H  HB   . VAL   A 1 34  ? 26.301 -7.351  11.693  1.00 15.45 ?  34  VAL   A HB   1 
ATOM   945  H  HG11 . VAL   A 1 34  ? 27.687 -6.945  9.749   1.00 15.64 ?  34  VAL   A HG11 1 
ATOM   946  H  HG12 . VAL   A 1 34  ? 26.313 -6.150  9.797   1.00 15.64 ?  34  VAL   A HG12 1 
ATOM   947  H  HG13 . VAL   A 1 34  ? 27.670 -5.419  10.185  1.00 15.64 ?  34  VAL   A HG13 1 
ATOM   948  H  HG21 . VAL   A 1 34  ? 28.542 -8.037  11.654  1.00 17.18 ?  34  VAL   A HG21 1 
ATOM   949  H  HG22 . VAL   A 1 34  ? 28.974 -6.625  12.240  1.00 17.18 ?  34  VAL   A HG22 1 
ATOM   950  H  HG23 . VAL   A 1 34  ? 28.104 -7.620  13.123  1.00 17.18 ?  34  VAL   A HG23 1 
ATOM   951  N  N    . VAL   A 1 35  ? 25.320 -3.696  11.379  1.00 11.30 ?  35  VAL   A N    1 
ATOM   952  C  CA   . VAL   A 1 35  ? 24.284 -3.182  10.492  1.00 10.88 ?  35  VAL   A CA   1 
ATOM   953  C  C    . VAL   A 1 35  ? 24.833 -3.192  9.075   1.00 10.25 ?  35  VAL   A C    1 
ATOM   954  O  O    . VAL   A 1 35  ? 25.977 -2.784  8.839   1.00 11.12 ?  35  VAL   A O    1 
ATOM   955  C  CB   . VAL   A 1 35  ? 23.758 -1.788  10.899  1.00 11.28 ?  35  VAL   A CB   1 
ATOM   956  C  CG1  . VAL   A 1 35  ? 24.829 -0.697  10.761  1.00 11.71 ?  35  VAL   A CG1  1 
ATOM   957  C  CG2  . VAL   A 1 35  ? 22.516 -1.438  10.082  1.00 12.21 ?  35  VAL   A CG2  1 
ATOM   958  H  H    . VAL   A 1 35  ? 25.970 -3.146  11.492  1.00 13.57 ?  35  VAL   A H    1 
ATOM   959  H  HA   . VAL   A 1 35  ? 23.526 -3.794  10.513  1.00 13.07 ?  35  VAL   A HA   1 
ATOM   960  H  HB   . VAL   A 1 35  ? 23.485 -1.818  11.826  1.00 13.55 ?  35  VAL   A HB   1 
ATOM   961  H  HG11 . VAL   A 1 35  ? 24.482 0.135   11.130  1.00 14.07 ?  35  VAL   A HG11 1 
ATOM   962  H  HG12 . VAL   A 1 35  ? 25.618 -0.968  11.250  1.00 14.07 ?  35  VAL   A HG12 1 
ATOM   963  H  HG13 . VAL   A 1 35  ? 25.043 -0.572  9.823   1.00 14.07 ?  35  VAL   A HG13 1 
ATOM   964  H  HG21 . VAL   A 1 35  ? 22.161 -0.592  10.390  1.00 14.67 ?  35  VAL   A HG21 1 
ATOM   965  H  HG22 . VAL   A 1 35  ? 22.764 -1.369  9.143   1.00 14.67 ?  35  VAL   A HG22 1 
ATOM   966  H  HG23 . VAL   A 1 35  ? 21.855 -2.139  10.195  1.00 14.67 ?  35  VAL   A HG23 1 
ATOM   967  N  N    . VAL   A 1 36  ? 24.014 -3.650  8.129   1.00 10.03 ?  36  VAL   A N    1 
ATOM   968  C  CA   . VAL   A 1 36  ? 24.382 -3.660  6.720   1.00 9.64  ?  36  VAL   A CA   1 
ATOM   969  C  C    . VAL   A 1 36  ? 23.923 -2.366  6.062   1.00 9.74  ?  36  VAL   A C    1 
ATOM   970  O  O    . VAL   A 1 36  ? 22.763 -1.960  6.208   1.00 10.53 ?  36  VAL   A O    1 
ATOM   971  C  CB   . VAL   A 1 36  ? 23.774 -4.870  6.001   1.00 9.70  ?  36  VAL   A CB   1 
ATOM   972  C  CG1  . VAL   A 1 36  ? 24.037 -4.794  4.519   1.00 10.22 ?  36  VAL   A CG1  1 
ATOM   973  C  CG2  . VAL   A 1 36  ? 24.319 -6.164  6.580   1.00 10.70 ?  36  VAL   A CG2  1 
ATOM   974  H  H    . VAL   A 1 36  ? 23.223 -3.963  8.280   1.00 12.05 ?  36  VAL   A H    1 
ATOM   975  H  HA   . VAL   A 1 36  ? 25.353 -3.719  6.647   1.00 11.58 ?  36  VAL   A HA   1 
ATOM   976  H  HB   . VAL   A 1 36  ? 22.816 -4.860  6.135   1.00 11.66 ?  36  VAL   A HB   1 
ATOM   977  H  HG11 . VAL   A 1 36  ? 23.907 -5.671  4.132   1.00 12.28 ?  36  VAL   A HG11 1 
ATOM   978  H  HG12 . VAL   A 1 36  ? 23.422 -4.160  4.119   1.00 12.28 ?  36  VAL   A HG12 1 
ATOM   979  H  HG13 . VAL   A 1 36  ? 24.954 -4.503  4.376   1.00 12.28 ?  36  VAL   A HG13 1 
ATOM   980  H  HG21 . VAL   A 1 36  ? 23.924 -6.915  6.103   1.00 12.85 ?  36  VAL   A HG21 1 
ATOM   981  H  HG22 . VAL   A 1 36  ? 25.282 -6.182  6.478   1.00 12.85 ?  36  VAL   A HG22 1 
ATOM   982  H  HG23 . VAL   A 1 36  ? 24.085 -6.218  7.521   1.00 12.85 ?  36  VAL   A HG23 1 
ATOM   983  N  N    . ASN   A 1 37  ? 24.837 -1.729  5.325   1.00 9.28  ?  37  ASN   A N    1 
ATOM   984  C  CA   . ASN   A 1 37  ? 24.502 -0.609  4.461   1.00 9.18  ?  37  ASN   A CA   1 
ATOM   985  C  C    . ASN   A 1 37  ? 24.361 -1.081  3.025   1.00 9.25  ?  37  ASN   A C    1 
ATOM   986  O  O    . ASN   A 1 37  ? 25.143 -1.909  2.542   1.00 9.78  ?  37  ASN   A O    1 
ATOM   987  C  CB   . ASN   A 1 37  ? 25.580 0.468   4.534   1.00 9.46  ?  37  ASN   A CB   1 
ATOM   988  C  CG   . ASN   A 1 37  ? 25.253 1.670   3.680   1.00 9.96  ?  37  ASN   A CG   1 
ATOM   989  O  OD1  . ASN   A 1 37  ? 24.082 2.012   3.501   1.00 10.48 ?  37  ASN   A OD1  1 
ATOM   990  N  ND2  . ASN   A 1 37  ? 26.287 2.328   3.161   1.00 10.17 ?  37  ASN   A ND2  1 
ATOM   991  H  H    . ASN   A 1 37  ? 25.675 -1.937  5.316   1.00 11.15 ?  37  ASN   A H    1 
ATOM   992  H  HA   . ASN   A 1 37  ? 23.663 -0.224  4.749   1.00 11.03 ?  37  ASN   A HA   1 
ATOM   993  H  HB2  . ASN   A 1 37  ? 25.671 0.765   5.456   1.00 11.37 ?  37  ASN   A HB2  1 
ATOM   994  H  HB3  . ASN   A 1 37  ? 26.426 0.095   4.227   1.00 11.37 ?  37  ASN   A HB3  1 
ATOM   995  H  HD21 . ASN   A 1 37  ? 26.149 3.017   2.666   1.00 12.21 ?  37  ASN   A HD21 1 
ATOM   996  H  HD22 . ASN   A 1 37  ? 27.085 2.063   3.307   1.00 12.21 ?  37  ASN   A HD22 1 
ATOM   997  N  N    A ALA   A 1 38  ? 23.347 -0.531  2.351   0.50 9.59  ?  38  ALA   A N    1 
ATOM   998  N  N    B ALA   A 1 38  ? 23.346 -0.553  2.336   0.50 10.01 ?  38  ALA   A N    1 
ATOM   999  C  CA   A ALA   A 1 38  ? 23.153 -0.650  0.907   0.50 9.62  ?  38  ALA   A CA   1 
ATOM   1000 C  CA   B ALA   A 1 38  ? 23.162 -0.794  0.903   0.50 10.62 ?  38  ALA   A CA   1 
ATOM   1001 C  C    A ALA   A 1 38  ? 24.090 0.345   0.225   0.50 9.39  ?  38  ALA   A C    1 
ATOM   1002 C  C    B ALA   A 1 38  ? 24.005 0.218   0.126   0.50 10.38 ?  38  ALA   A C    1 
ATOM   1003 O  O    A ALA   A 1 38  ? 23.712 1.458   -0.147  0.50 8.89  ?  38  ALA   A O    1 
ATOM   1004 O  O    B ALA   A 1 38  ? 23.531 1.254   -0.346  0.50 10.26 ?  38  ALA   A O    1 
ATOM   1005 C  CB   A ALA   A 1 38  ? 21.697 -0.373  0.550   0.50 10.16 ?  38  ALA   A CB   1 
ATOM   1006 C  CB   B ALA   A 1 38  ? 21.686 -0.712  0.536   0.50 11.48 ?  38  ALA   A CB   1 
ATOM   1007 H  H    A ALA   A 1 38  ? 22.746 -0.047  2.729   0.50 11.52 ?  38  ALA   A H    1 
ATOM   1008 H  H    B ALA   A 1 38  ? 22.748 -0.040  2.684   0.50 12.03 ?  38  ALA   A H    1 
ATOM   1009 H  HA   A ALA   A 1 38  ? 23.388 -1.541  0.617   0.50 11.56 ?  38  ALA   A HA   1 
ATOM   1010 H  HA   B ALA   A 1 38  ? 23.483 -1.687  0.689   0.50 12.76 ?  38  ALA   A HA   1 
ATOM   1011 H  HB1  A ALA   A 1 38  ? 21.586 -0.456  -0.409  0.50 12.20 ?  38  ALA   A HB1  1 
ATOM   1012 H  HB1  B ALA   A 1 38  ? 21.597 -0.838  -0.420  0.50 13.79 ?  38  ALA   A HB1  1 
ATOM   1013 H  HB2  A ALA   A 1 38  ? 21.136 -1.016  1.008   0.50 12.20 ?  38  ALA   A HB2  1 
ATOM   1014 H  HB2  B ALA   A 1 38  ? 21.202 -1.406  1.011   0.50 13.79 ?  38  ALA   A HB2  1 
ATOM   1015 H  HB3  A ALA   A 1 38  ? 21.467 0.528   0.833   0.50 12.20 ?  38  ALA   A HB3  1 
ATOM   1016 H  HB3  B ALA   A 1 38  ? 21.350 0.161   0.787   0.50 13.79 ?  38  ALA   A HB3  1 
ATOM   1017 N  N    A ALA   A 1 39  ? 25.346 -0.063  0.072   0.50 9.26  ?  39  ALA   A N    1 
ATOM   1018 N  N    B ALA   A 1 39  ? 25.286 -0.101  -0.013  0.50 10.72 ?  39  ALA   A N    1 
ATOM   1019 C  CA   A ALA   A 1 39  ? 26.419 0.800   -0.396  0.50 9.02  ?  39  ALA   A CA   1 
ATOM   1020 C  CA   B ALA   A 1 39  ? 26.283 0.831   -0.518  0.50 10.60 ?  39  ALA   A CA   1 
ATOM   1021 C  C    A ALA   A 1 39  ? 26.540 0.762   -1.915  0.50 9.48  ?  39  ALA   A C    1 
ATOM   1022 C  C    B ALA   A 1 39  ? 26.411 0.749   -2.037  0.50 10.46 ?  39  ALA   A C    1 
ATOM   1023 O  O    A ALA   A 1 39  ? 26.040 -0.146  -2.583  0.50 9.53  ?  39  ALA   A O    1 
ATOM   1024 O  O    B ALA   A 1 39  ? 25.952 -0.201  -2.679  0.50 11.03 ?  39  ALA   A O    1 
ATOM   1025 C  CB   A ALA   A 1 39  ? 27.741 0.361   0.237   0.50 10.08 ?  39  ALA   A CB   1 
ATOM   1026 C  CB   B ALA   A 1 39  ? 27.633 0.532   0.134   0.50 11.60 ?  39  ALA   A CB   1 
ATOM   1027 H  H    A ALA   A 1 39  ? 25.607 -0.867  0.238   0.50 11.12 ?  39  ALA   A H    1 
ATOM   1028 H  H    B ALA   A 1 39  ? 25.605 -0.878  0.184   0.50 12.88 ?  39  ALA   A H    1 
ATOM   1029 H  HA   A ALA   A 1 39  ? 26.239 1.713   -0.129  0.50 10.84 ?  39  ALA   A HA   1 
ATOM   1030 H  HA   B ALA   A 1 39  ? 26.019 1.733   -0.277  0.50 12.73 ?  39  ALA   A HA   1 
ATOM   1031 H  HB1  A ALA   A 1 39  ? 28.451 0.943   -0.077  0.50 12.11 ?  39  ALA   A HB1  1 
ATOM   1032 H  HB1  B ALA   A 1 39  ? 28.289 1.158   -0.206  0.50 13.93 ?  39  ALA   A HB1  1 
ATOM   1033 H  HB2  A ALA   A 1 39  ? 27.663 0.431   1.204   0.50 12.11 ?  39  ALA   A HB2  1 
ATOM   1034 H  HB2  B ALA   A 1 39  ? 27.549 0.634   1.099   0.50 13.93 ?  39  ALA   A HB2  1 
ATOM   1035 H  HB3  A ALA   A 1 39  ? 27.925 -0.555  -0.013  0.50 12.11 ?  39  ALA   A HB3  1 
ATOM   1036 H  HB3  B ALA   A 1 39  ? 27.894 -0.376  -0.078  0.50 13.93 ?  39  ALA   A HB3  1 
ATOM   1037 N  N    A ASN   A 1 40  ? 27.241 1.762   -2.453  0.50 9.69  ?  40  ASN   A N    1 
ATOM   1038 N  N    B ASN   A 1 40  ? 27.047 1.772   -2.608  0.50 10.43 ?  40  ASN   A N    1 
ATOM   1039 C  CA   A ASN   A 1 40  ? 27.765 1.723   -3.813  0.50 9.88  ?  40  ASN   A CA   1 
ATOM   1040 C  CA   B ASN   A 1 40  ? 27.565 1.717   -3.968  0.50 10.45 ?  40  ASN   A CA   1 
ATOM   1041 C  C    A ASN   A 1 40  ? 29.286 1.599   -3.768  0.50 9.91  ?  40  ASN   A C    1 
ATOM   1042 C  C    B ASN   A 1 40  ? 29.091 1.619   -3.924  0.50 9.74  ?  40  ASN   A C    1 
ATOM   1043 O  O    A ASN   A 1 40  ? 29.905 1.730   -2.709  0.50 10.39 ?  40  ASN   A O    1 
ATOM   1044 O  O    B ASN   A 1 40  ? 29.707 1.700   -2.861  0.50 9.51  ?  40  ASN   A O    1 
ATOM   1045 C  CB   A ASN   A 1 40  ? 27.296 2.924   -4.654  0.50 10.87 ?  40  ASN   A CB   1 
ATOM   1046 C  CB   B ASN   A 1 40  ? 27.077 2.908   -4.810  0.50 10.93 ?  40  ASN   A CB   1 
ATOM   1047 C  CG   A ASN   A 1 40  ? 27.685 4.269   -4.060  0.50 12.31 ?  40  ASN   A CG   1 
ATOM   1048 C  CG   B ASN   A 1 40  ? 27.441 4.251   -4.208  0.50 11.45 ?  40  ASN   A CG   1 
ATOM   1049 O  OD1  A ASN   A 1 40  ? 28.845 4.496   -3.707  0.50 12.35 ?  40  ASN   A OD1  1 
ATOM   1050 O  OD1  B ASN   A 1 40  ? 28.621 4.568   -4.034  0.50 11.71 ?  40  ASN   A OD1  1 
ATOM   1051 N  ND2  A ASN   A 1 40  ? 26.711 5.177   -3.970  0.50 13.06 ?  40  ASN   A ND2  1 
ATOM   1052 N  ND2  B ASN   A 1 40  ? 26.427 5.061   -3.916  0.50 12.16 ?  40  ASN   A ND2  1 
ATOM   1053 H  H    A ASN   A 1 40  ? 27.451 2.481   -2.033  0.50 11.64 ?  40  ASN   A H    1 
ATOM   1054 H  H    B ASN   A 1 40  ? 27.187 2.520   -2.215  0.50 12.52 ?  40  ASN   A H    1 
ATOM   1055 H  HA   A ASN   A 1 40  ? 27.439 0.922   -4.247  0.50 11.87 ?  40  ASN   A HA   1 
ATOM   1056 H  HA   B ASN   A 1 40  ? 27.221 0.903   -4.389  0.50 12.56 ?  40  ASN   A HA   1 
ATOM   1057 H  HB2  A ASN   A 1 40  ? 27.690 2.856   -5.545  0.50 13.06 ?  40  ASN   A HB2  1 
ATOM   1058 H  HB2  B ASN   A 1 40  ? 27.478 2.848   -5.689  0.50 13.13 ?  40  ASN   A HB2  1 
ATOM   1059 H  HB3  A ASN   A 1 40  ? 26.333 2.895   -4.722  0.50 13.06 ?  40  ASN   A HB3  1 
ATOM   1060 H  HB3  B ASN   A 1 40  ? 26.108 2.861   -4.889  0.50 13.13 ?  40  ASN   A HB3  1 
ATOM   1061 H  HD21 A ASN   A 1 40  ? 26.878 5.959   -3.655  0.50 15.68 ?  40  ASN   A HD21 1 
ATOM   1062 H  HD21 B ASN   A 1 40  ? 26.583 5.833   -3.576  0.50 14.60 ?  40  ASN   A HD21 1 
ATOM   1063 H  HD22 A ASN   A 1 40  ? 25.915 4.974   -4.221  0.50 15.68 ?  40  ASN   A HD22 1 
ATOM   1064 H  HD22 B ASN   A 1 40  ? 25.617 4.808   -4.059  0.50 14.60 ?  40  ASN   A HD22 1 
ATOM   1065 N  N    A VAL   A 1 41  ? 29.887 1.304   -4.926  0.50 10.22 ?  41  VAL   A N    1 
ATOM   1066 N  N    B VAL   A 1 41  ? 29.701 1.418   -5.095  0.50 10.38 ?  41  VAL   A N    1 
ATOM   1067 C  CA   A VAL   A 1 41  ? 31.319 1.028   -4.956  0.50 10.78 ?  41  VAL   A CA   1 
ATOM   1068 C  CA   B VAL   A 1 41  ? 31.127 1.081   -5.159  0.50 11.26 ?  41  VAL   A CA   1 
ATOM   1069 C  C    A VAL   A 1 41  ? 32.124 2.225   -4.505  0.50 11.03 ?  41  VAL   A C    1 
ATOM   1070 C  C    B VAL   A 1 41  ? 32.048 2.190   -4.645  0.50 11.06 ?  41  VAL   A C    1 
ATOM   1071 O  O    A VAL   A 1 41  ? 33.256 2.056   -4.034  0.50 11.72 ?  41  VAL   A O    1 
ATOM   1072 O  O    B VAL   A 1 41  ? 33.198 1.916   -4.279  0.50 11.00 ?  41  VAL   A O    1 
ATOM   1073 C  CB   A VAL   A 1 41  ? 31.824 0.515   -6.329  0.50 10.76 ?  41  VAL   A CB   1 
ATOM   1074 C  CB   B VAL   A 1 41  ? 31.522 0.647   -6.589  0.50 12.33 ?  41  VAL   A CB   1 
ATOM   1075 C  CG1  A VAL   A 1 41  ? 31.090 -0.751  -6.732  0.50 11.47 ?  41  VAL   A CG1  1 
ATOM   1076 C  CG1  B VAL   A 1 41  ? 30.882 -0.688  -6.938  0.50 13.53 ?  41  VAL   A CG1  1 
ATOM   1077 C  CG2  A VAL   A 1 41  ? 31.723 1.592   -7.412  0.50 10.22 ?  41  VAL   A CG2  1 
ATOM   1078 C  CG2  B VAL   A 1 41  ? 31.151 1.720   -7.613  0.50 12.31 ?  41  VAL   A CG2  1 
ATOM   1079 H  H    A VAL   A 1 41  ? 29.506 1.252   -5.692  0.50 12.28 ?  41  VAL   A H    1 
ATOM   1080 H  H    B VAL   A 1 41  ? 29.297 1.441   -5.856  0.50 12.47 ?  41  VAL   A H    1 
ATOM   1081 H  HA   A VAL   A 1 41  ? 31.514 0.325   -4.322  0.50 12.95 ?  41  VAL   A HA   1 
ATOM   1082 H  HA   B VAL   A 1 41  ? 31.270 0.314   -4.589  0.50 13.53 ?  41  VAL   A HA   1 
ATOM   1083 H  HB   A VAL   A 1 41  ? 32.767 0.284   -6.249  0.50 12.93 ?  41  VAL   A HB   1 
ATOM   1084 H  HB   B VAL   A 1 41  ? 32.481 0.527   -6.620  0.50 14.81 ?  41  VAL   A HB   1 
ATOM   1085 H  HG11 A VAL   A 1 41  ? 31.440 -1.069  -7.580  0.50 13.78 ?  41  VAL   A HG11 1 
ATOM   1086 H  HG11 B VAL   A 1 41  ? 31.176 -0.958  -7.823  0.50 16.25 ?  41  VAL   A HG11 1 
ATOM   1087 H  HG12 A VAL   A 1 41  ? 31.223 -1.426  -6.047  0.50 13.78 ?  41  VAL   A HG12 1 
ATOM   1088 H  HG12 B VAL   A 1 41  ? 31.156 -1.351  -6.283  0.50 16.25 ?  41  VAL   A HG12 1 
ATOM   1089 H  HG13 A VAL   A 1 41  ? 30.144 -0.552  -6.820  0.50 13.78 ?  41  VAL   A HG13 1 
ATOM   1090 H  HG13 B VAL   A 1 41  ? 29.917 -0.592  -6.925  0.50 16.25 ?  41  VAL   A HG13 1 
ATOM   1091 H  HG21 A VAL   A 1 41  ? 31.909 1.188   -8.278  0.50 12.28 ?  41  VAL   A HG21 1 
ATOM   1092 H  HG21 B VAL   A 1 41  ? 31.528 1.475   -8.473  0.50 14.79 ?  41  VAL   A HG21 1 
ATOM   1093 H  HG22 A VAL   A 1 41  ? 30.831 1.961   -7.404  0.50 12.28 ?  41  VAL   A HG22 1 
ATOM   1094 H  HG22 B VAL   A 1 41  ? 30.183 1.773   -7.684  0.50 14.79 ?  41  VAL   A HG22 1 
ATOM   1095 H  HG23 A VAL   A 1 41  ? 32.376 2.287   -7.230  0.50 12.28 ?  41  VAL   A HG23 1 
ATOM   1096 H  HG23 B VAL   A 1 41  ? 31.511 2.570   -7.324  0.50 14.79 ?  41  VAL   A HG23 1 
ATOM   1097 N  N    . TYR   A 1 42  ? 31.580 3.437   -4.638  1.00 11.32 ?  42  TYR   A N    1 
ATOM   1098 C  CA   . TYR   A 1 42  ? 32.326 4.619   -4.224  1.00 11.20 ?  42  TYR   A CA   1 
ATOM   1099 C  C    . TYR   A 1 42  ? 32.069 4.998   -2.776  1.00 10.82 ?  42  TYR   A C    1 
ATOM   1100 O  O    . TYR   A 1 42  ? 32.644 5.986   -2.292  1.00 11.34 ?  42  TYR   A O    1 
ATOM   1101 C  CB   . TYR   A 1 42  ? 31.988 5.811   -5.140  1.00 11.98 ?  42  TYR   A CB   1 
ATOM   1102 C  CG   . TYR   A 1 42  ? 32.173 5.500   -6.610  1.00 12.77 ?  42  TYR   A CG   1 
ATOM   1103 C  CD1  . TYR   A 1 42  ? 33.435 5.302   -7.142  1.00 13.43 ?  42  TYR   A CD1  1 
ATOM   1104 C  CD2  . TYR   A 1 42  ? 31.086 5.378   -7.463  1.00 14.19 ?  42  TYR   A CD2  1 
ATOM   1105 C  CE1  . TYR   A 1 42  ? 33.610 4.991   -8.484  1.00 13.74 ?  42  TYR   A CE1  1 
ATOM   1106 C  CE2  . TYR   A 1 42  ? 31.256 5.080   -8.806  1.00 15.42 ?  42  TYR   A CE2  1 
ATOM   1107 C  CZ   . TYR   A 1 42  ? 32.522 4.887   -9.311  1.00 14.61 ?  42  TYR   A CZ   1 
ATOM   1108 O  OH   . TYR   A 1 42  ? 32.695 4.590   -10.640 1.00 16.63 ?  42  TYR   A OH   1 
ATOM   1109 H  H    A TYR   A 1 42  ? 30.793 3.593   -4.952  0.50 13.60 ?  42  TYR   A H    1 
ATOM   1110 H  H    B TYR   A 1 42  ? 30.782 3.634   -4.896  0.50 13.60 ?  42  TYR   A H    1 
ATOM   1111 H  HA   . TYR   A 1 42  ? 33.272 4.446   -4.319  1.00 13.46 ?  42  TYR   A HA   1 
ATOM   1112 H  HB2  . TYR   A 1 42  ? 31.061 6.069   -5.003  1.00 14.39 ?  42  TYR   A HB2  1 
ATOM   1113 H  HB3  . TYR   A 1 42  ? 32.570 6.558   -4.919  1.00 14.39 ?  42  TYR   A HB3  1 
ATOM   1114 H  HD1  . TYR   A 1 42  ? 34.178 5.363   -6.585  1.00 16.13 ?  42  TYR   A HD1  1 
ATOM   1115 H  HD2  . TYR   A 1 42  ? 30.226 5.512   -7.128  1.00 17.04 ?  42  TYR   A HD2  1 
ATOM   1116 H  HE1  . TYR   A 1 42  ? 34.466 4.859   -8.822  1.00 16.50 ?  42  TYR   A HE1  1 
ATOM   1117 H  HE2  . TYR   A 1 42  ? 30.515 5.008   -9.366  1.00 18.51 ?  42  TYR   A HE2  1 
ATOM   1118 H  HH   . TYR   A 1 42  ? 33.517 4.489   -10.808 1.00 19.97 ?  42  TYR   A HH   1 
ATOM   1119 N  N    A LEU   A 1 43  ? 31.224 4.242   -2.074  0.50 10.50 ?  43  LEU   A N    1 
ATOM   1120 N  N    B LEU   A 1 43  ? 31.213 4.245   -2.084  0.50 10.62 ?  43  LEU   A N    1 
ATOM   1121 C  CA   A LEU   A 1 43  ? 30.825 4.563   -0.703  0.50 10.16 ?  43  LEU   A CA   1 
ATOM   1122 C  CA   B LEU   A 1 43  ? 30.743 4.599   -0.749  0.50 10.45 ?  43  LEU   A CA   1 
ATOM   1123 C  C    A LEU   A 1 43  ? 30.320 6.002   -0.580  0.50 10.12 ?  43  LEU   A C    1 
ATOM   1124 C  C    B LEU   A 1 43  ? 30.299 6.059   -0.689  0.50 10.37 ?  43  LEU   A C    1 
ATOM   1125 O  O    A LEU   A 1 43  ? 30.516 6.668   0.440   0.50 10.46 ?  43  LEU   A O    1 
ATOM   1126 O  O    B LEU   A 1 43  ? 30.659 6.808   0.221   0.50 11.19 ?  43  LEU   A O    1 
ATOM   1127 C  CB   A LEU   A 1 43  ? 31.929 4.260   0.311   0.50 10.62 ?  43  LEU   A CB   1 
ATOM   1128 C  CB   B LEU   A 1 43  ? 31.776 4.282   0.331   0.50 10.35 ?  43  LEU   A CB   1 
ATOM   1129 C  CG   A LEU   A 1 43  ? 32.430 2.813   0.422   0.50 10.81 ?  43  LEU   A CG   1 
ATOM   1130 C  CG   B LEU   A 1 43  ? 32.242 2.826   0.412   0.50 10.76 ?  43  LEU   A CG   1 
ATOM   1131 C  CD1  A LEU   A 1 43  ? 33.509 2.730   1.488   0.50 11.47 ?  43  LEU   A CD1  1 
ATOM   1132 C  CD1  B LEU   A 1 43  ? 33.272 2.686   1.516   0.50 11.73 ?  43  LEU   A CD1  1 
ATOM   1133 C  CD2  A LEU   A 1 43  ? 31.310 1.838   0.735   0.50 10.71 ?  43  LEU   A CD2  1 
ATOM   1134 C  CD2  B LEU   A 1 43  ? 31.074 1.869   0.631   0.50 11.28 ?  43  LEU   A CD2  1 
ATOM   1135 H  H    A LEU   A 1 43  ? 30.858 3.517   -2.373  0.50 12.61 ?  43  LEU   A H    1 
ATOM   1136 H  H    B LEU   A 1 43  ? 30.875 3.503   -2.378  0.50 12.75 ?  43  LEU   A H    1 
ATOM   1137 H  HA   A LEU   A 1 43  ? 30.075 3.990   -0.474  0.50 12.20 ?  43  LEU   A HA   1 
ATOM   1138 H  HA   B LEU   A 1 43  ? 29.961 4.051   -0.556  0.50 12.55 ?  43  LEU   A HA   1 
ATOM   1139 H  HB2  A LEU   A 1 43  ? 32.697 4.812   0.096   0.50 12.76 ?  43  LEU   A HB2  1 
ATOM   1140 H  HB2  B LEU   A 1 43  ? 32.559 4.831   0.172   0.50 12.43 ?  43  LEU   A HB2  1 
ATOM   1141 H  HB3  A LEU   A 1 43  ? 31.596 4.505   1.188   0.50 12.76 ?  43  LEU   A HB3  1 
ATOM   1142 H  HB3  B LEU   A 1 43  ? 31.392 4.512   1.194   0.50 12.43 ?  43  LEU   A HB3  1 
ATOM   1143 H  HG   A LEU   A 1 43  ? 32.830 2.548   -0.422  0.50 12.98 ?  43  LEU   A HG   1 
ATOM   1144 H  HG   B LEU   A 1 43  ? 32.667 2.588   -0.426  0.50 12.93 ?  43  LEU   A HG   1 
ATOM   1145 H  HD11 A LEU   A 1 43  ? 33.821 1.814   1.552   0.50 13.78 ?  43  LEU   A HD11 1 
ATOM   1146 H  HD11 B LEU   A 1 43  ? 33.562 1.763   1.559   0.50 14.08 ?  43  LEU   A HD11 1 
ATOM   1147 H  HD12 A LEU   A 1 43  ? 34.242 3.314   1.242   0.50 13.78 ?  43  LEU   A HD12 1 
ATOM   1148 H  HD12 B LEU   A 1 43  ? 34.026 3.263   1.316   0.50 14.08 ?  43  LEU   A HD12 1 
ATOM   1149 H  HD13 A LEU   A 1 43  ? 33.132 3.011   2.338   0.50 13.78 ?  43  LEU   A HD13 1 
ATOM   1150 H  HD13 B LEU   A 1 43  ? 32.868 2.948   2.358   0.50 14.08 ?  43  LEU   A HD13 1 
ATOM   1151 H  HD21 A LEU   A 1 43  ? 31.688 0.956   0.874   0.50 12.87 ?  43  LEU   A HD21 1 
ATOM   1152 H  HD21 B LEU   A 1 43  ? 31.422 0.981   0.798   0.50 13.55 ?  43  LEU   A HD21 1 
ATOM   1153 H  HD22 A LEU   A 1 43  ? 30.855 2.133   1.541   0.50 12.87 ?  43  LEU   A HD22 1 
ATOM   1154 H  HD22 B LEU   A 1 43  ? 30.557 2.172   1.395   0.50 13.55 ?  43  LEU   A HD22 1 
ATOM   1155 H  HD23 A LEU   A 1 43  ? 30.690 1.822   -0.008  0.50 12.87 ?  43  LEU   A HD23 1 
ATOM   1156 H  HD23 B LEU   A 1 43  ? 30.516 1.863   -0.163  0.50 13.55 ?  43  LEU   A HD23 1 
ATOM   1157 N  N    A LYS   A 1 44  ? 29.642 6.475   -1.626  0.50 10.44 ?  44  LYS   A N    1 
ATOM   1158 N  N    B LYS   A 1 44  ? 29.509 6.464   -1.685  0.50 10.30 ?  44  LYS   A N    1 
ATOM   1159 C  CA   A LYS   A 1 44  ? 28.995 7.784   -1.610  0.50 11.08 ?  44  LYS   A CA   1 
ATOM   1160 C  CA   B LYS   A 1 44  ? 28.864 7.777   -1.696  0.50 11.04 ?  44  LYS   A CA   1 
ATOM   1161 C  C    A LYS   A 1 44  ? 27.562 7.585   -1.131  0.50 10.28 ?  44  LYS   A C    1 
ATOM   1162 C  C    B LYS   A 1 44  ? 27.450 7.603   -1.156  0.50 10.53 ?  44  LYS   A C    1 
ATOM   1163 O  O    A LYS   A 1 44  ? 26.717 7.051   -1.860  0.50 11.02 ?  44  LYS   A O    1 
ATOM   1164 O  O    B LYS   A 1 44  ? 26.552 7.130   -1.859  0.50 10.98 ?  44  LYS   A O    1 
ATOM   1165 C  CB   A LYS   A 1 44  ? 29.034 8.426   -2.993  0.50 13.14 ?  44  LYS   A CB   1 
ATOM   1166 C  CB   B LYS   A 1 44  ? 28.878 8.382   -3.095  0.50 13.36 ?  44  LYS   A CB   1 
ATOM   1167 C  CG   A LYS   A 1 44  ? 30.425 8.849   -3.437  0.50 16.00 ?  44  LYS   A CG   1 
ATOM   1168 C  CG   B LYS   A 1 44  ? 30.243 8.909   -3.526  0.50 16.76 ?  44  LYS   A CG   1 
ATOM   1169 C  CD   A LYS   A 1 44  ? 31.069 9.840   -2.469  0.50 20.53 ?  44  LYS   A CD   1 
ATOM   1170 C  CD   B LYS   A 1 44  ? 30.964 9.625   -2.384  0.50 21.42 ?  44  LYS   A CD   1 
ATOM   1171 C  CE   A LYS   A 1 44  ? 32.415 10.318  -2.984  0.50 23.67 ?  44  LYS   A CE   1 
ATOM   1172 C  CE   B LYS   A 1 44  ? 32.197 10.362  -2.866  0.50 24.10 ?  44  LYS   A CE   1 
ATOM   1173 N  NZ   A LYS   A 1 44  ? 33.187 11.038  -1.938  0.50 25.28 ?  44  LYS   A NZ   1 
ATOM   1174 N  NZ   B LYS   A 1 44  ? 33.064 10.793  -1.733  0.50 25.26 ?  44  LYS   A NZ   1 
ATOM   1175 H  H    A LYS   A 1 44  ? 29.534 6.048   -2.365  0.50 12.54 ?  44  LYS   A H    1 
ATOM   1176 H  H    B LYS   A 1 44  ? 29.335 5.992   -2.386  0.50 12.38 ?  44  LYS   A H    1 
ATOM   1177 H  HA   A LYS   A 1 44  ? 29.445 8.365   -0.976  0.50 13.31 ?  44  LYS   A HA   1 
ATOM   1178 H  HA   B LYS   A 1 44  ? 29.320 8.363   -1.076  0.50 13.27 ?  44  LYS   A HA   1 
ATOM   1179 H  HB2  A LYS   A 1 44  ? 28.698 7.794   -3.643  0.50 15.78 ?  44  LYS   A HB2  1 
ATOM   1180 H  HB2  B LYS   A 1 44  ? 28.610 7.704   -3.735  0.50 16.05 ?  44  LYS   A HB2  1 
ATOM   1181 H  HB3  A LYS   A 1 44  ? 28.476 9.222   -2.986  0.50 15.78 ?  44  LYS   A HB3  1 
ATOM   1182 H  HB3  B LYS   A 1 44  ? 28.253 9.125   -3.124  0.50 16.05 ?  44  LYS   A HB3  1 
ATOM   1183 H  HG2  A LYS   A 1 44  ? 30.996 8.067   -3.490  0.50 19.21 ?  44  LYS   A HG2  1 
ATOM   1184 H  HG2  B LYS   A 1 44  ? 30.797 8.168   -3.816  0.50 20.13 ?  44  LYS   A HG2  1 
ATOM   1185 H  HG3  A LYS   A 1 44  ? 30.367 9.279   -4.306  0.50 19.21 ?  44  LYS   A HG3  1 
ATOM   1186 H  HG3  B LYS   A 1 44  ? 30.129 9.545   -4.252  0.50 20.13 ?  44  LYS   A HG3  1 
ATOM   1187 H  HD2  A LYS   A 1 44  ? 30.483 10.604  -2.360  0.50 24.65 ?  44  LYS   A HD2  1 
ATOM   1188 H  HD2  B LYS   A 1 44  ? 30.357 10.263  -1.972  0.50 25.72 ?  44  LYS   A HD2  1 
ATOM   1189 H  HD3  A LYS   A 1 44  ? 31.212 9.400   -1.613  0.50 24.65 ?  44  LYS   A HD3  1 
ATOM   1190 H  HD3  B LYS   A 1 44  ? 31.253 8.967   -1.729  0.50 25.72 ?  44  LYS   A HD3  1 
ATOM   1191 H  HE2  A LYS   A 1 44  ? 32.933 9.550   -3.270  0.50 28.42 ?  44  LYS   A HE2  1 
ATOM   1192 H  HE2  B LYS   A 1 44  ? 32.716 9.774   -3.436  0.50 28.93 ?  44  LYS   A HE2  1 
ATOM   1193 H  HE3  A LYS   A 1 44  ? 32.269 10.921  -3.727  0.50 28.42 ?  44  LYS   A HE3  1 
ATOM   1194 H  HE3  B LYS   A 1 44  ? 31.924 11.151  -3.357  0.50 28.93 ?  44  LYS   A HE3  1 
ATOM   1195 H  HZ1  A LYS   A 1 44  ? 33.979 11.278  -2.260  0.50 30.35 ?  44  LYS   A HZ1  1 
ATOM   1196 H  HZ1  B LYS   A 1 44  ? 33.779 11.224  -2.043  0.50 30.33 ?  44  LYS   A HZ1  1 
ATOM   1197 H  HZ2  A LYS   A 1 44  ? 32.744 11.767  -1.683  0.50 30.35 ?  44  LYS   A HZ2  1 
ATOM   1198 H  HZ2  B LYS   A 1 44  ? 32.611 11.340  -1.194  0.50 30.33 ?  44  LYS   A HZ2  1 
ATOM   1199 H  HZ3  A LYS   A 1 44  ? 33.307 10.511  -1.231  0.50 30.35 ?  44  LYS   A HZ3  1 
ATOM   1200 H  HZ3  B LYS   A 1 44  ? 33.332 10.086  -1.266  0.50 30.33 ?  44  LYS   A HZ3  1 
ATOM   1201 N  N    A HIS   A 1 45  ? 27.298 7.988   0.106   0.50 9.61  ?  45  HIS   A N    1 
ATOM   1202 N  N    B HIS   A 1 45  ? 27.261 7.973   0.110   0.50 10.60 ?  45  HIS   A N    1 
ATOM   1203 C  CA   A HIS   A 1 45  ? 26.061 7.622   0.791   0.50 9.39  ?  45  HIS   A CA   1 
ATOM   1204 C  CA   B HIS   A 1 45  ? 26.023 7.682   0.833   0.50 10.87 ?  45  HIS   A CA   1 
ATOM   1205 C  C    A HIS   A 1 45  ? 25.026 8.741   0.653   0.50 9.65  ?  45  HIS   A C    1 
ATOM   1206 C  C    B HIS   A 1 45  ? 25.040 8.834   0.640   0.50 11.62 ?  45  HIS   A C    1 
ATOM   1207 O  O    A HIS   A 1 45  ? 24.646 9.414   1.614   0.50 10.37 ?  45  HIS   A O    1 
ATOM   1208 O  O    B HIS   A 1 45  ? 24.886 9.713   1.491   0.50 12.83 ?  45  HIS   A O    1 
ATOM   1209 C  CB   A HIS   A 1 45  ? 26.359 7.311   2.248   0.50 9.17  ?  45  HIS   A CB   1 
ATOM   1210 C  CB   B HIS   A 1 45  ? 26.323 7.474   2.308   0.50 10.32 ?  45  HIS   A CB   1 
ATOM   1211 C  CG   A HIS   A 1 45  ? 27.482 6.344   2.438   0.50 8.79  ?  45  HIS   A CG   1 
ATOM   1212 C  CG   B HIS   A 1 45  ? 27.434 6.510   2.564   0.50 10.02 ?  45  HIS   A CG   1 
ATOM   1213 N  ND1  A HIS   A 1 45  ? 27.469 5.068   1.913   0.50 8.99  ?  45  HIS   A ND1  1 
ATOM   1214 N  ND1  B HIS   A 1 45  ? 27.420 5.212   2.097   0.50 10.68 ?  45  HIS   A ND1  1 
ATOM   1215 C  CD2  A HIS   A 1 45  ? 28.661 6.475   3.090   0.50 10.06 ?  45  HIS   A CD2  1 
ATOM   1216 C  CD2  B HIS   A 1 45  ? 28.600 6.663   3.233   0.50 9.66  ?  45  HIS   A CD2  1 
ATOM   1217 C  CE1  A HIS   A 1 45  ? 28.591 4.453   2.246   0.50 9.69  ?  45  HIS   A CE1  1 
ATOM   1218 C  CE1  B HIS   A 1 45  ? 28.533 4.608   2.474   0.50 9.55  ?  45  HIS   A CE1  1 
ATOM   1219 N  NE2  A HIS   A 1 45  ? 29.332 5.284   2.959   0.50 10.48 ?  45  HIS   A NE2  1 
ATOM   1220 N  NE2  B HIS   A 1 45  ? 29.265 5.464   3.167   0.50 9.17  ?  45  HIS   A NE2  1 
ATOM   1221 H  H    A HIS   A 1 45  ? 27.821 8.485   0.579   0.50 11.54 ?  45  HIS   A H    1 
ATOM   1222 H  H    B HIS   A 1 45  ? 27.838 8.409   0.579   0.50 12.73 ?  45  HIS   A H    1 
ATOM   1223 H  HA   A HIS   A 1 45  ? 25.696 6.821   0.382   0.50 11.28 ?  45  HIS   A HA   1 
ATOM   1224 H  HA   B HIS   A 1 45  ? 25.622 6.873   0.479   0.50 13.06 ?  45  HIS   A HA   1 
ATOM   1225 H  HB2  A HIS   A 1 45  ? 26.590 8.129   2.708   0.50 11.02 ?  45  HIS   A HB2  1 
ATOM   1226 H  HB2  B HIS   A 1 45  ? 26.567 8.327   2.699   0.50 12.40 ?  45  HIS   A HB2  1 
ATOM   1227 H  HB3  A HIS   A 1 45  ? 25.563 6.920   2.656   0.50 11.02 ?  45  HIS   A HB3  1 
ATOM   1228 H  HB3  B HIS   A 1 45  ? 25.525 7.129   2.741   0.50 12.40 ?  45  HIS   A HB3  1 
ATOM   1229 H  HD2  A HIS   A 1 45  ? 28.965 7.229   3.543   0.50 12.08 ?  45  HIS   A HD2  1 
ATOM   1230 H  HD2  B HIS   A 1 45  ? 28.897 7.438   3.658   0.50 11.60 ?  45  HIS   A HD2  1 
ATOM   1231 H  HE1  A HIS   A 1 45  ? 28.823 3.575   2.027   0.50 11.65 ?  45  HIS   A HE1  1 
ATOM   1232 H  HE1  B HIS   A 1 45  ? 28.758 3.726   2.289   0.50 11.47 ?  45  HIS   A HE1  1 
ATOM   1233 H  HE2  A HIS   A 1 45  ? 30.113 5.107   3.287   0.50 12.59 ?  45  HIS   A HE2  1 
ATOM   1234 H  HE2  B HIS   A 1 45  ? 30.033 5.299   3.513   0.50 11.02 ?  45  HIS   A HE2  1 
ATOM   1235 N  N    A GLY   A 1 46  ? 24.555 8.919   -0.579  0.50 10.72 ?  46  GLY   A N    1 
ATOM   1236 N  N    B GLY   A 1 46  ? 24.347 8.817   -0.494  0.50 11.84 ?  46  GLY   A N    1 
ATOM   1237 C  CA   A GLY   A 1 46  ? 23.767 10.093  -0.914  0.50 11.57 ?  46  GLY   A CA   1 
ATOM   1238 C  CA   B GLY   A 1 46  ? 23.514 9.951   -0.850  0.50 12.03 ?  46  GLY   A CA   1 
ATOM   1239 C  C    A GLY   A 1 46  ? 22.267 9.968   -0.719  0.50 11.17 ?  46  GLY   A C    1 
ATOM   1240 C  C    B GLY   A 1 46  ? 22.059 9.835   -0.442  0.50 11.61 ?  46  GLY   A C    1 
ATOM   1241 O  O    A GLY   A 1 46  ? 21.587 10.970  -0.468  0.50 11.22 ?  46  GLY   A O    1 
ATOM   1242 O  O    B GLY   A 1 46  ? 21.458 10.811  0.022   0.50 12.04 ?  46  GLY   A O    1 
ATOM   1243 H  H    A GLY   A 1 46  ? 24.675 8.373   -1.232  0.50 12.88 ?  46  GLY   A H    1 
ATOM   1244 H  H    B GLY   A 1 46  ? 24.341 8.171   -1.066  0.50 14.22 ?  46  GLY   A H    1 
ATOM   1245 H  HA2  A GLY   A 1 46  ? 24.081 10.838  -0.374  0.50 13.90 ?  46  GLY   A HA2  1 
ATOM   1246 H  HA2  B GLY   A 1 46  ? 23.871 10.750  -0.428  0.50 14.44 ?  46  GLY   A HA2  1 
ATOM   1247 H  HA3  A GLY   A 1 46  ? 23.928 10.315  -1.844  0.50 13.90 ?  46  GLY   A HA3  1 
ATOM   1248 H  HA3  B GLY   A 1 46  ? 23.552 10.081  -1.809  0.50 14.44 ?  46  GLY   A HA3  1 
ATOM   1249 N  N    A GLY   A 1 47  ? 21.734 8.759   -0.854  0.50 10.89 ?  47  GLY   A N    1 
ATOM   1250 N  N    B GLY   A 1 47  ? 21.478 8.653   -0.616  0.50 11.48 ?  47  GLY   A N    1 
ATOM   1251 C  CA   A GLY   A 1 47  ? 20.301 8.551   -0.805  0.50 10.90 ?  47  GLY   A CA   1 
ATOM   1252 C  CA   B GLY   A 1 47  ? 20.054 8.475   -0.400  0.50 11.53 ?  47  GLY   A CA   1 
ATOM   1253 C  C    A GLY   A 1 47  ? 19.990 7.108   -0.467  0.50 10.71 ?  47  GLY   A C    1 
ATOM   1254 C  C    B GLY   A 1 47  ? 19.726 7.036   -0.067  0.50 10.29 ?  47  GLY   A C    1 
ATOM   1255 O  O    A GLY   A 1 47  ? 20.884 6.291   -0.237  0.50 11.14 ?  47  GLY   A O    1 
ATOM   1256 O  O    B GLY   A 1 47  ? 20.611 6.187   0.072   0.50 10.19 ?  47  GLY   A O    1 
ATOM   1257 H  H    A GLY   A 1 47  ? 22.192 8.040   -0.966  0.50 13.08 ?  47  GLY   A H    1 
ATOM   1258 H  H    B GLY   A 1 47  ? 21.893 7.938   -0.851  0.50 13.79 ?  47  GLY   A H    1 
ATOM   1259 H  HA2  A GLY   A 1 47  ? 19.905 9.133   -0.136  0.50 13.09 ?  47  GLY   A HA2  1 
ATOM   1260 H  HA2  B GLY   A 1 47  ? 19.760 9.025   0.338   0.50 13.84 ?  47  GLY   A HA2  1 
ATOM   1261 H  HA3  A GLY   A 1 47  ? 19.914 8.756   -1.669  0.50 13.09 ?  47  GLY   A HA3  1 
ATOM   1262 H  HA3  B GLY   A 1 47  ? 19.565 8.730   -1.197  0.50 13.84 ?  47  GLY   A HA3  1 
ATOM   1263 N  N    A GLY   A 1 48  ? 18.699 6.794   -0.459  0.50 10.41 ?  48  GLY   A N    1 
ATOM   1264 N  N    B GLY   A 1 48  ? 18.427 6.769   0.057   0.50 10.59 ?  48  GLY   A N    1 
ATOM   1265 C  CA   A GLY   A 1 48  ? 18.299 5.452   -0.093  0.50 10.60 ?  48  GLY   A CA   1 
ATOM   1266 C  CA   B GLY   A 1 48  ? 18.008 5.440   0.449   0.50 10.09 ?  48  GLY   A CA   1 
ATOM   1267 C  C    A GLY   A 1 48  ? 18.685 5.137   1.339   0.50 10.02 ?  48  GLY   A C    1 
ATOM   1268 C  C    B GLY   A 1 48  ? 18.605 5.060   1.791   0.50 10.07 ?  48  GLY   A C    1 
ATOM   1269 O  O    A GLY   A 1 48  ? 18.832 6.026   2.184   0.50 10.66 ?  48  GLY   A O    1 
ATOM   1270 O  O    B GLY   A 1 48  ? 18.807 5.895   2.683   0.50 10.55 ?  48  GLY   A O    1 
ATOM   1271 H  H    A GLY   A 1 48  ? 18.059 7.328   -0.657  0.50 12.51 ?  48  GLY   A H    1 
ATOM   1272 H  H    B GLY   A 1 48  ? 17.780 7.328   -0.077  0.50 12.72 ?  48  GLY   A H    1 
ATOM   1273 H  HA2  A GLY   A 1 48  ? 17.342 5.355   -0.188  0.50 12.73 ?  48  GLY   A HA2  1 
ATOM   1274 H  HA2  B GLY   A 1 48  ? 17.036 5.399   0.509   0.50 12.13 ?  48  GLY   A HA2  1 
ATOM   1275 H  HA3  A GLY   A 1 48  ? 18.739 4.807   -0.669  0.50 12.73 ?  48  GLY   A HA3  1 
ATOM   1276 H  HA3  B GLY   A 1 48  ? 18.297 4.790   -0.215  0.50 12.13 ?  48  GLY   A HA3  1 
ATOM   1277 N  N    A VAL   A 1 49  ? 18.860 3.843   1.618   0.50 10.75 ?  49  VAL   A N    1 
ATOM   1278 N  N    B VAL   A 1 49  ? 18.880 3.763   1.939   0.50 9.76  ?  49  VAL   A N    1 
ATOM   1279 C  CA   A VAL   A 1 49  ? 19.289 3.424   2.949   0.50 11.29 ?  49  VAL   A CA   1 
ATOM   1280 C  CA   B VAL   A 1 49  ? 19.489 3.248   3.164   0.50 9.91  ?  49  VAL   A CA   1 
ATOM   1281 C  C    A VAL   A 1 49  ? 20.622 4.066   3.317   0.50 10.69 ?  49  VAL   A C    1 
ATOM   1282 C  C    B VAL   A 1 49  ? 20.759 4.018   3.505   0.50 9.31  ?  49  VAL   A C    1 
ATOM   1283 O  O    A VAL   A 1 49  ? 20.830 4.477   4.463   0.50 10.98 ?  49  VAL   A O    1 
ATOM   1284 O  O    B VAL   A 1 49  ? 20.965 4.434   4.651   0.50 9.41  ?  49  VAL   A O    1 
ATOM   1285 C  CB   A VAL   A 1 49  ? 19.352 1.887   3.035   0.50 12.39 ?  49  VAL   A CB   1 
ATOM   1286 C  CB   B VAL   A 1 49  ? 19.780 1.743   3.012   0.50 10.50 ?  49  VAL   A CB   1 
ATOM   1287 C  CG1  A VAL   A 1 49  ? 20.042 1.453   4.320   0.50 12.75 ?  49  VAL   A CG1  1 
ATOM   1288 C  CG1  B VAL   A 1 49  ? 20.625 1.257   4.172   0.50 9.83  ?  49  VAL   A CG1  1 
ATOM   1289 C  CG2  A VAL   A 1 49  ? 17.952 1.288   2.953   0.50 13.67 ?  49  VAL   A CG2  1 
ATOM   1290 C  CG2  B VAL   A 1 49  ? 18.487 0.942   2.894   0.50 11.24 ?  49  VAL   A CG2  1 
ATOM   1291 H  H    A VAL   A 1 49  ? 18.733 3.196   1.065   0.50 12.91 ?  49  VAL   A H    1 
ATOM   1292 H  H    B VAL   A 1 49  ? 18.717 3.160   1.346   0.50 11.72 ?  49  VAL   A H    1 
ATOM   1293 H  HA   A VAL   A 1 49  ? 18.633 3.716   3.599   0.50 13.57 ?  49  VAL   A HA   1 
ATOM   1294 H  HA   B VAL   A 1 49  ? 18.869 3.356   3.898   0.50 11.91 ?  49  VAL   A HA   1 
ATOM   1295 H  HB   A VAL   A 1 49  ? 19.875 1.544   2.291   0.50 14.88 ?  49  VAL   A HB   1 
ATOM   1296 H  HB   B VAL   A 1 49  ? 20.285 1.601   2.197   0.50 12.62 ?  49  VAL   A HB   1 
ATOM   1297 H  HG11 A VAL   A 1 49  ? 19.829 0.522   4.493   0.50 15.32 ?  49  VAL   A HG11 1 
ATOM   1298 H  HG11 B VAL   A 1 49  ? 20.548 0.292   4.238   0.50 11.81 ?  49  VAL   A HG11 1 
ATOM   1299 H  HG12 A VAL   A 1 49  ? 21.000 1.560   4.224   0.50 15.32 ?  49  VAL   A HG12 1 
ATOM   1300 H  HG12 B VAL   A 1 49  ? 21.554 1.498   4.013   0.50 11.81 ?  49  VAL   A HG12 1 
ATOM   1301 H  HG13 A VAL   A 1 49  ? 19.717 2.004   5.052   0.50 15.32 ?  49  VAL   A HG13 1 
ATOM   1302 H  HG13 B VAL   A 1 49  ? 20.310 1.669   4.990   0.50 11.81 ?  49  VAL   A HG13 1 
ATOM   1303 H  HG21 A VAL   A 1 49  ? 18.019 0.322   3.007   0.50 16.41 ?  49  VAL   A HG21 1 
ATOM   1304 H  HG21 B VAL   A 1 49  ? 18.701 0.004   2.777   0.50 13.50 ?  49  VAL   A HG21 1 
ATOM   1305 H  HG22 A VAL   A 1 49  ? 17.424 1.626   3.692   0.50 16.41 ?  49  VAL   A HG22 1 
ATOM   1306 H  HG22 B VAL   A 1 49  ? 17.964 1.063   3.704   0.50 13.50 ?  49  VAL   A HG22 1 
ATOM   1307 H  HG23 A VAL   A 1 49  ? 17.552 1.547   2.111   0.50 16.41 ?  49  VAL   A HG23 1 
ATOM   1308 H  HG23 B VAL   A 1 49  ? 17.982 1.263   2.128   0.50 13.50 ?  49  VAL   A HG23 1 
ATOM   1309 N  N    A ALA   A 1 50  ? 21.552 4.137   2.362   0.50 10.31 ?  50  ALA   A N    1 
ATOM   1310 N  N    B ALA   A 1 50  ? 21.649 4.173   2.524   0.50 9.10  ?  50  ALA   A N    1 
ATOM   1311 C  CA   A ALA   A 1 50  ? 22.879 4.673   2.654   0.50 10.28 ?  50  ALA   A CA   1 
ATOM   1312 C  CA   B ALA   A 1 50  ? 22.965 4.739   2.805   0.50 9.07  ?  50  ALA   A CA   1 
ATOM   1313 C  C    A ALA   A 1 50  ? 22.810 6.138   3.058   0.50 10.09 ?  50  ALA   A C    1 
ATOM   1314 C  C    B ALA   A 1 50  ? 22.855 6.188   3.256   0.50 9.09  ?  50  ALA   A C    1 
ATOM   1315 O  O    A ALA   A 1 50  ? 23.482 6.563   4.004   0.50 10.48 ?  50  ALA   A O    1 
ATOM   1316 O  O    B ALA   A 1 50  ? 23.455 6.584   4.263   0.50 9.42  ?  50  ALA   A O    1 
ATOM   1317 C  CB   A ALA   A 1 50  ? 23.778 4.508   1.434   0.50 10.24 ?  50  ALA   A CB   1 
ATOM   1318 C  CB   B ALA   A 1 50  ? 23.854 4.621   1.571   0.50 8.94  ?  50  ALA   A CB   1 
ATOM   1319 H  H    A ALA   A 1 50  ? 21.441 3.879   1.555   0.50 12.39 ?  50  ALA   A H    1 
ATOM   1320 H  H    B ALA   A 1 50  ? 21.517 3.961   1.698   0.50 10.93 ?  50  ALA   A H    1 
ATOM   1321 H  HA   A ALA   A 1 50  ? 23.271 4.180   3.393   0.50 12.35 ?  50  ALA   A HA   1 
ATOM   1322 H  HA   B ALA   A 1 50  ? 23.375 4.241   3.523   0.50 10.90 ?  50  ALA   A HA   1 
ATOM   1323 H  HB1  A ALA   A 1 50  ? 24.651 4.873   1.638   0.50 12.31 ?  50  ALA   A HB1  1 
ATOM   1324 H  HB1  B ALA   A 1 50  ? 24.722 5.004   1.772   0.50 10.75 ?  50  ALA   A HB1  1 
ATOM   1325 H  HB2  A ALA   A 1 50  ? 23.846 3.569   1.221   0.50 12.31 ?  50  ALA   A HB2  1 
ATOM   1326 H  HB2  B ALA   A 1 50  ? 23.949 3.685   1.341   0.50 10.75 ?  50  ALA   A HB2  1 
ATOM   1327 H  HB3  A ALA   A 1 50  ? 23.381 4.993   0.691   0.50 12.31 ?  50  ALA   A HB3  1 
ATOM   1328 H  HB3  B ALA   A 1 50  ? 23.441 5.103   0.836   0.50 10.75 ?  50  ALA   A HB3  1 
ATOM   1329 N  N    A GLY   A 1 51  ? 22.019 6.932   2.340   0.50 10.00 ?  51  GLY   A N    1 
ATOM   1330 N  N    B GLY   A 1 51  ? 22.093 6.996   2.519   0.50 9.97  ?  51  GLY   A N    1 
ATOM   1331 C  CA   A GLY   A 1 51  ? 21.876 8.328   2.708   0.50 10.33 ?  51  GLY   A CA   1 
ATOM   1332 C  CA   B GLY   A 1 51  ? 21.913 8.378   2.923   0.50 9.97  ?  51  GLY   A CA   1 
ATOM   1333 C  C    A GLY   A 1 51  ? 21.276 8.501   4.088   0.50 10.20 ?  51  GLY   A C    1 
ATOM   1334 C  C    B GLY   A 1 51  ? 21.288 8.492   4.301   0.50 9.80  ?  51  GLY   A C    1 
ATOM   1335 O  O    A GLY   A 1 51  ? 21.669 9.398   4.836   0.50 10.35 ?  51  GLY   A O    1 
ATOM   1336 O  O    B GLY   A 1 51  ? 21.653 9.367   5.089   0.50 10.26 ?  51  GLY   A O    1 
ATOM   1337 H  H    A GLY   A 1 51  ? 21.575 6.693   1.648   0.50 12.02 ?  51  GLY   A H    1 
ATOM   1338 H  H    B GLY   A 1 51  ? 21.681 6.771   1.797   0.50 11.98 ?  51  GLY   A H    1 
ATOM   1339 H  HA2  A GLY   A 1 51  ? 22.743 8.761   2.705   0.50 12.41 ?  51  GLY   A HA2  1 
ATOM   1340 H  HA2  B GLY   A 1 51  ? 22.773 8.828   2.933   0.50 11.98 ?  51  GLY   A HA2  1 
ATOM   1341 H  HA3  A GLY   A 1 51  ? 21.302 8.780   2.072   0.50 12.41 ?  51  GLY   A HA3  1 
ATOM   1342 H  HA3  B GLY   A 1 51  ? 21.341 8.831   2.278   0.50 11.98 ?  51  GLY   A HA3  1 
ATOM   1343 N  N    A ALA   A 1 52  ? 20.307 7.651   4.440   0.50 10.70 ?  52  ALA   A N    1 
ATOM   1344 N  N    B ALA   A 1 52  ? 20.345 7.599   4.612   0.50 9.94  ?  52  ALA   A N    1 
ATOM   1345 C  CA   A ALA   A 1 52  ? 19.659 7.750   5.744   0.50 11.04 ?  52  ALA   A CA   1 
ATOM   1346 C  CA   B ALA   A 1 52  ? 19.679 7.640   5.909   0.50 10.35 ?  52  ALA   A CA   1 
ATOM   1347 C  C    A ALA   A 1 52  ? 20.605 7.338   6.868   0.50 10.36 ?  52  ALA   A C    1 
ATOM   1348 C  C    B ALA   A 1 52  ? 20.621 7.214   7.032   0.50 9.86  ?  52  ALA   A C    1 
ATOM   1349 O  O    A ALA   A 1 52  ? 20.700 8.021   7.893   0.50 11.15 ?  52  ALA   A O    1 
ATOM   1350 O  O    B ALA   A 1 52  ? 20.670 7.853   8.090   0.50 10.60 ?  52  ALA   A O    1 
ATOM   1351 C  CB   A ALA   A 1 52  ? 18.385 6.900   5.755   0.50 12.14 ?  52  ALA   A CB   1 
ATOM   1352 C  CB   B ALA   A 1 52  ? 18.426 6.763   5.870   0.50 11.42 ?  52  ALA   A CB   1 
ATOM   1353 H  H    A ALA   A 1 52  ? 20.020 7.010   3.948   0.50 12.85 ?  52  ALA   A H    1 
ATOM   1354 H  H    B ALA   A 1 52  ? 20.089 6.960   4.092   0.50 11.94 ?  52  ALA   A H    1 
ATOM   1355 H  HA   A ALA   A 1 52  ? 19.399 8.668   5.897   0.50 13.27 ?  52  ALA   A HA   1 
ATOM   1356 H  HA   B ALA   A 1 52  ? 19.402 8.547   6.083   0.50 12.44 ?  52  ALA   A HA   1 
ATOM   1357 H  HB1  A ALA   A 1 52  ? 17.959 6.974   6.624   0.50 14.59 ?  52  ALA   A HB1  1 
ATOM   1358 H  HB1  B ALA   A 1 52  ? 17.962 6.842   6.716   0.50 13.72 ?  52  ALA   A HB1  1 
ATOM   1359 H  HB2  A ALA   A 1 52  ? 17.783 7.225   5.065   0.50 14.59 ?  52  ALA   A HB2  1 
ATOM   1360 H  HB2  B ALA   A 1 52  ? 17.851 7.071   5.149   0.50 13.72 ?  52  ALA   A HB2  1 
ATOM   1361 H  HB3  A ALA   A 1 52  ? 18.616 5.974   5.579   0.50 14.59 ?  52  ALA   A HB3  1 
ATOM   1362 H  HB3  B ALA   A 1 52  ? 18.684 5.842   5.713   0.50 13.72 ?  52  ALA   A HB3  1 
ATOM   1363 N  N    A LEU   A 1 53  ? 21.317 6.219   6.698   0.50 10.45 ?  53  LEU   A N    1 
ATOM   1364 N  N    B LEU   A 1 53  ? 21.370 6.124   6.833   0.50 9.62  ?  53  LEU   A N    1 
ATOM   1365 C  CA   A LEU   A 1 53  ? 22.253 5.782   7.732   0.50 10.80 ?  53  LEU   A CA   1 
ATOM   1366 C  CA   B LEU   A 1 53  ? 22.373 5.748   7.826   0.50 9.53  ?  53  LEU   A CA   1 
ATOM   1367 C  C    A LEU   A 1 53  ? 23.348 6.817   7.943   0.50 10.65 ?  53  LEU   A C    1 
ATOM   1368 C  C    B LEU   A 1 53  ? 23.385 6.869   8.013   0.50 9.24  ?  53  LEU   A C    1 
ATOM   1369 O  O    A LEU   A 1 53  ? 23.739 7.100   9.080   0.50 11.31 ?  53  LEU   A O    1 
ATOM   1370 O  O    B LEU   A 1 53  ? 23.668 7.289   9.140   0.50 10.13 ?  53  LEU   A O    1 
ATOM   1371 C  CB   A LEU   A 1 53  ? 22.869 4.429   7.359   0.50 11.41 ?  53  LEU   A CB   1 
ATOM   1372 C  CB   B LEU   A 1 53  ? 23.083 4.448   7.424   0.50 9.33  ?  53  LEU   A CB   1 
ATOM   1373 C  CG   A LEU   A 1 53  ? 21.947 3.205   7.400   0.50 11.35 ?  53  LEU   A CG   1 
ATOM   1374 C  CG   B LEU   A 1 53  ? 22.297 3.134   7.508   0.50 9.58  ?  53  LEU   A CG   1 
ATOM   1375 C  CD1  A LEU   A 1 53  ? 22.665 1.992   6.833   0.50 11.20 ?  53  LEU   A CD1  1 
ATOM   1376 C  CD1  B LEU   A 1 53  ? 23.099 2.006   6.866   0.50 10.14 ?  53  LEU   A CD1  1 
ATOM   1377 C  CD2  A LEU   A 1 53  ? 21.469 2.926   8.814   0.50 12.34 ?  53  LEU   A CD2  1 
ATOM   1378 C  CD2  B LEU   A 1 53  ? 21.934 2.777   8.942   0.50 10.07 ?  53  LEU   A CD2  1 
ATOM   1379 H  H    A LEU   A 1 53  ? 21.276 5.709   6.011   0.50 12.55 ?  53  LEU   A H    1 
ATOM   1380 H  H    B LEU   A 1 53  ? 21.311 5.590   6.153   0.50 11.55 ?  53  LEU   A H    1 
ATOM   1381 H  HA   A LEU   A 1 53  ? 21.777 5.671   8.572   0.50 12.98 ?  53  LEU   A HA   1 
ATOM   1382 H  HA   B LEU   A 1 53  ? 21.931 5.593   8.674   0.50 11.45 ?  53  LEU   A HA   1 
ATOM   1383 H  HB2  A LEU   A 1 53  ? 23.216 4.492   6.454   0.50 13.70 ?  53  LEU   A HB2  1 
ATOM   1384 H  HB2  B LEU   A 1 53  ? 23.378 4.540   6.503   0.50 11.21 ?  53  LEU   A HB2  1 
ATOM   1385 H  HB3  A LEU   A 1 53  ? 23.603 4.248   7.968   0.50 13.70 ?  53  LEU   A HB3  1 
ATOM   1386 H  HB3  B LEU   A 1 53  ? 23.862 4.345   7.993   0.50 11.21 ?  53  LEU   A HB3  1 
ATOM   1387 H  HG   A LEU   A 1 53  ? 21.167 3.378   6.845   0.50 13.63 ?  53  LEU   A HG   1 
ATOM   1388 H  HG   B LEU   A 1 53  ? 21.478 3.226   7.002   0.50 11.51 ?  53  LEU   A HG   1 
ATOM   1389 H  HD11 A LEU   A 1 53  ? 22.068 1.228   6.865   0.50 13.45 ?  53  LEU   A HD11 1 
ATOM   1390 H  HD11 B LEU   A 1 53  ? 22.591 1.180   6.927   0.50 12.19 ?  53  LEU   A HD11 1 
ATOM   1391 H  HD12 A LEU   A 1 53  ? 22.920 2.175   5.915   0.50 13.45 ?  53  LEU   A HD12 1 
ATOM   1392 H  HD12 B LEU   A 1 53  ? 23.264 2.221   5.933   0.50 12.19 ?  53  LEU   A HD12 1 
ATOM   1393 H  HD13 A LEU   A 1 53  ? 23.455 1.817   7.368   0.50 13.45 ?  53  LEU   A HD13 1 
ATOM   1394 H  HD13 B LEU   A 1 53  ? 23.944 1.908   7.334   0.50 12.19 ?  53  LEU   A HD13 1 
ATOM   1395 H  HD21 A LEU   A 1 53  ? 20.965 2.098   8.818   0.50 14.82 ?  53  LEU   A HD21 1 
ATOM   1396 H  HD21 B LEU   A 1 53  ? 21.390 1.973   8.938   0.50 12.09 ?  53  LEU   A HD21 1 
ATOM   1397 H  HD22 A LEU   A 1 53  ? 22.242 2.847   9.395   0.50 14.82 ?  53  LEU   A HD22 1 
ATOM   1398 H  HD22 B LEU   A 1 53  ? 22.745 2.626   9.448   0.50 12.09 ?  53  LEU   A HD22 1 
ATOM   1399 H  HD23 A LEU   A 1 53  ? 20.907 3.658   9.108   0.50 14.82 ?  53  LEU   A HD23 1 
ATOM   1400 H  HD23 B LEU   A 1 53  ? 21.432 3.511   9.330   0.50 12.09 ?  53  LEU   A HD23 1 
ATOM   1401 N  N    A ASN   A 1 54  ? 23.856 7.394   6.860   0.50 10.12 ?  54  ASN   A N    1 
ATOM   1402 N  N    B ASN   A 1 54  ? 23.931 7.381   6.912   0.50 9.26  ?  54  ASN   A N    1 
ATOM   1403 C  CA   A ASN   A 1 54  ? 24.928 8.369   7.006   0.50 10.12 ?  54  ASN   A CA   1 
ATOM   1404 C  CA   B ASN   A 1 54  ? 24.966 8.398   7.039   0.50 9.54  ?  54  ASN   A CA   1 
ATOM   1405 C  C    A ASN   A 1 54  ? 24.435 9.623   7.728   0.50 10.60 ?  54  ASN   A C    1 
ATOM   1406 C  C    B ASN   A 1 54  ? 24.435 9.638   7.753   0.50 10.14 ?  54  ASN   A C    1 
ATOM   1407 O  O    A ASN   A 1 54  ? 25.135 10.173  8.586   0.50 11.02 ?  54  ASN   A O    1 
ATOM   1408 O  O    B ASN   A 1 54  ? 25.105 10.197  8.630   0.50 10.16 ?  54  ASN   A O    1 
ATOM   1409 C  CB   A ASN   A 1 54  ? 25.503 8.715   5.641   0.50 10.16 ?  54  ASN   A CB   1 
ATOM   1410 C  CB   B ASN   A 1 54  ? 25.533 8.769   5.677   0.50 9.74  ?  54  ASN   A CB   1 
ATOM   1411 C  CG   A ASN   A 1 54  ? 26.566 9.774   5.737   0.50 10.55 ?  54  ASN   A CG   1 
ATOM   1412 C  CG   B ASN   A 1 54  ? 26.506 9.915   5.782   0.50 9.59  ?  54  ASN   A CG   1 
ATOM   1413 O  OD1  A ASN   A 1 54  ? 27.547 9.616   6.468   0.50 10.88 ?  54  ASN   A OD1  1 
ATOM   1414 O  OD1  B ASN   A 1 54  ? 27.543 9.794   6.441   0.50 9.36  ?  54  ASN   A OD1  1 
ATOM   1415 N  ND2  A ASN   A 1 54  ? 26.377 10.870  5.021   0.50 10.81 ?  54  ASN   A ND2  1 
ATOM   1416 N  ND2  B ASN   A 1 54  ? 26.166 11.048  5.180   0.50 10.10 ?  54  ASN   A ND2  1 
ATOM   1417 H  H    A ASN   A 1 54  ? 23.596 7.242   6.056   0.50 12.16 ?  54  ASN   A H    1 
ATOM   1418 H  H    B ASN   A 1 54  ? 23.719 7.164   6.107   0.50 11.12 ?  54  ASN   A H    1 
ATOM   1419 H  HA   A ASN   A 1 54  ? 25.630 7.974   7.540   0.50 12.15 ?  54  ASN   A HA   1 
ATOM   1420 H  HA   B ASN   A 1 54  ? 25.683 8.039   7.574   0.50 11.46 ?  54  ASN   A HA   1 
ATOM   1421 H  HB2  A ASN   A 1 54  ? 25.897 7.911   5.257   0.50 12.20 ?  54  ASN   A HB2  1 
ATOM   1422 H  HB2  B ASN   A 1 54  ? 26.002 7.998   5.312   0.50 11.70 ?  54  ASN   A HB2  1 
ATOM   1423 H  HB3  A ASN   A 1 54  ? 24.792 9.040   5.070   0.50 12.20 ?  54  ASN   A HB3  1 
ATOM   1424 H  HB3  B ASN   A 1 54  ? 24.809 9.028   5.087   0.50 11.70 ?  54  ASN   A HB3  1 
ATOM   1425 H  HD21 A ASN   A 1 54  ? 26.959 11.497  5.047   0.50 12.98 ?  54  ASN   A HD21 1 
ATOM   1426 H  HD21 B ASN   A 1 54  ? 26.687 11.728  5.223   0.50 12.13 ?  54  ASN   A HD21 1 
ATOM   1427 H  HD22 A ASN   A 1 54  ? 25.676 10.943  4.531   0.50 12.98 ?  54  ASN   A HD22 1 
ATOM   1428 H  HD22 B ASN   A 1 54  ? 25.428 11.097  4.739   0.50 12.13 ?  54  ASN   A HD22 1 
ATOM   1429 N  N    . LYS   A 1 55  ? 23.224 10.080  7.398   1.00 10.60 ?  55  LYS   A N    1 
ATOM   1430 C  CA   . LYS   A 1 55  ? 22.640 11.233  8.074   1.00 11.12 ?  55  LYS   A CA   1 
ATOM   1431 C  C    . LYS   A 1 55  ? 22.549 10.995  9.576   1.00 11.27 ?  55  LYS   A C    1 
ATOM   1432 O  O    . LYS   A 1 55  ? 22.833 11.897  10.375  1.00 12.01 ?  55  LYS   A O    1 
ATOM   1433 C  CB   . LYS   A 1 55  ? 21.266 11.535  7.469   1.00 11.97 ?  55  LYS   A CB   1 
ATOM   1434 C  CG   . LYS   A 1 55  ? 20.515 12.698  8.110   1.00 13.70 ?  55  LYS   A CG   1 
ATOM   1435 C  CD   . LYS   A 1 55  ? 19.191 12.959  7.381   1.00 15.25 ?  55  LYS   A CD   1 
ATOM   1436 C  CE   . LYS   A 1 55  ? 18.339 14.021  8.062   1.00 17.08 ?  55  LYS   A CE   1 
ATOM   1437 N  NZ   . LYS   A 1 55  ? 17.006 14.163  7.405   1.00 17.96 ?  55  LYS   A NZ   1 
ATOM   1438 H  H    A LYS   A 1 55  ? 22.718 9.738   6.788   0.50 12.73 ?  55  LYS   A H    1 
ATOM   1439 H  H    B LYS   A 1 55  ? 22.720 9.725   6.794   0.50 12.73 ?  55  LYS   A H    1 
ATOM   1440 H  HA   . LYS   A 1 55  ? 23.207 12.004  7.928   1.00 13.35 ?  55  LYS   A HA   1 
ATOM   1441 H  HB2  . LYS   A 1 55  ? 21.383 11.748  6.530   1.00 14.37 ?  55  LYS   A HB2  1 
ATOM   1442 H  HB3  . LYS   A 1 55  ? 20.709 10.746  7.556   1.00 14.37 ?  55  LYS   A HB3  1 
ATOM   1443 H  HG2  . LYS   A 1 55  ? 20.315 12.483  9.035   1.00 16.45 ?  55  LYS   A HG2  1 
ATOM   1444 H  HG3  . LYS   A 1 55  ? 21.057 13.500  8.058   1.00 16.45 ?  55  LYS   A HG3  1 
ATOM   1445 H  HD2  . LYS   A 1 55  ? 19.385 13.260  6.478   1.00 18.31 ?  55  LYS   A HD2  1 
ATOM   1446 H  HD3  . LYS   A 1 55  ? 18.681 12.134  7.351   1.00 18.31 ?  55  LYS   A HD3  1 
ATOM   1447 H  HE2  . LYS   A 1 55  ? 18.197 13.769  8.988   1.00 20.50 ?  55  LYS   A HE2  1 
ATOM   1448 H  HE3  . LYS   A 1 55  ? 18.795 14.875  8.013   1.00 20.50 ?  55  LYS   A HE3  1 
ATOM   1449 H  HZ1  . LYS   A 1 55  ? 16.462 14.644  7.921   1.00 21.57 ?  55  LYS   A HZ1  1 
ATOM   1450 H  HZ2  . LYS   A 1 55  ? 17.093 14.573  6.620   1.00 21.57 ?  55  LYS   A HZ2  1 
ATOM   1451 H  HZ3  . LYS   A 1 55  ? 16.641 13.361  7.274   1.00 21.57 ?  55  LYS   A HZ3  1 
ATOM   1452 N  N    . ALA   A 1 56  ? 22.166 9.779   9.979   1.00 11.41 ?  56  ALA   A N    1 
ATOM   1453 C  CA   . ALA   A 1 56  ? 22.053 9.454   11.393  1.00 12.10 ?  56  ALA   A CA   1 
ATOM   1454 C  C    . ALA   A 1 56  ? 23.398 9.489   12.110  1.00 12.09 ?  56  ALA   A C    1 
ATOM   1455 O  O    . ALA   A 1 56  ? 23.423 9.680   13.329  1.00 13.68 ?  56  ALA   A O    1 
ATOM   1456 C  CB   . ALA   A 1 56  ? 21.368 8.094   11.575  1.00 13.06 ?  56  ALA   A CB   1 
ATOM   1457 H  H    . ALA   A 1 56  ? 21.969 9.133   9.448   1.00 13.70 ?  56  ALA   A H    1 
ATOM   1458 H  HA   . ALA   A 1 56  ? 21.492 10.114  11.816  1.00 14.53 ?  56  ALA   A HA   1 
ATOM   1459 H  HB1  . ALA   A 1 56  ? 21.305 7.897   12.526  1.00 15.69 ?  56  ALA   A HB1  1 
ATOM   1460 H  HB2  . ALA   A 1 56  ? 20.478 8.136   11.191  1.00 15.69 ?  56  ALA   A HB2  1 
ATOM   1461 H  HB3  . ALA   A 1 56  ? 21.889 7.409   11.131  1.00 15.69 ?  56  ALA   A HB3  1 
ATOM   1462 N  N    . THR   A 1 57  ? 24.507 9.308   11.388  1.00 11.34 ?  57  THR   A N    1 
ATOM   1463 C  CA   . THR   A 1 57  ? 25.847 9.435   11.963  1.00 11.52 ?  57  THR   A CA   1 
ATOM   1464 C  C    . THR   A 1 57  ? 26.397 10.854  11.883  1.00 11.88 ?  57  THR   A C    1 
ATOM   1465 O  O    . THR   A 1 57  ? 27.581 11.066  12.176  1.00 12.34 ?  57  THR   A O    1 
ATOM   1466 C  CB   . THR   A 1 57  ? 26.857 8.488   11.289  1.00 11.43 ?  57  THR   A CB   1 
ATOM   1467 O  OG1  . THR   A 1 57  ? 27.240 8.991   9.995   1.00 10.91 ?  57  THR   A OG1  1 
ATOM   1468 C  CG2  . THR   A 1 57  ? 26.326 7.069   11.178  1.00 11.60 ?  57  THR   A CG2  1 
ATOM   1469 H  H    . THR   A 1 57  ? 24.509 9.090   10.553  1.00 13.62 ?  57  THR   A H    1 
ATOM   1470 H  HA   . THR   A 1 57  ? 25.801 9.180   12.903  1.00 13.83 ?  57  THR   A HA   1 
ATOM   1471 H  HB   . THR   A 1 57  ? 27.656 8.445   11.849  1.00 13.73 ?  57  THR   A HB   1 
ATOM   1472 H  HG1  . THR   A 1 57  ? 26.558 9.055   9.508   1.00 13.11 ?  57  THR   A HG1  1 
ATOM   1473 H  HG21 . THR   A 1 57  ? 27.010 6.481   10.813  1.00 13.94 ?  57  THR   A HG21 1 
ATOM   1474 H  HG22 . THR   A 1 57  ? 26.063 6.735   12.050  1.00 13.94 ?  57  THR   A HG22 1 
ATOM   1475 H  HG23 . THR   A 1 57  ? 25.555 7.047   10.591  1.00 13.94 ?  57  THR   A HG23 1 
ATOM   1476 N  N    . ASN   A 1 58  ? 25.581 11.827  11.482  1.00 12.13 ?  58  ASN   A N    1 
ATOM   1477 C  CA   . ASN   A 1 58  ? 26.045 13.207  11.383  1.00 13.18 ?  58  ASN   A CA   1 
ATOM   1478 C  C    . ASN   A 1 58  ? 27.192 13.335  10.375  1.00 12.13 ?  58  ASN   A C    1 
ATOM   1479 O  O    . ASN   A 1 58  ? 28.087 14.171  10.535  1.00 12.54 ?  58  ASN   A O    1 
ATOM   1480 C  CB   . ASN   A 1 58  ? 26.418 13.746  12.779  1.00 15.79 ?  58  ASN   A CB   1 
ATOM   1481 C  CG   . ASN   A 1 58  ? 26.830 15.201  12.776  1.00 19.49 ?  58  ASN   A CG   1 
ATOM   1482 O  OD1  . ASN   A 1 58  ? 26.205 16.030  12.126  1.00 21.20 ?  58  ASN   A OD1  1 
ATOM   1483 N  ND2  . ASN   A 1 58  ? 27.884 15.527  13.530  1.00 20.73 ?  58  ASN   A ND2  1 
ATOM   1484 H  H    . ASN   A 1 58  ? 24.761 11.702  11.249  1.00 14.57 ?  58  ASN   A H    1 
ATOM   1485 H  HA   . ASN   A 1 58  ? 25.309 13.739  11.053  1.00 15.84 ?  58  ASN   A HA   1 
ATOM   1486 H  HB2  . ASN   A 1 58  ? 25.642 13.653  13.365  1.00 18.96 ?  58  ASN   A HB2  1 
ATOM   1487 H  HB3  . ASN   A 1 58  ? 27.154 13.232  13.134  1.00 18.96 ?  58  ASN   A HB3  1 
ATOM   1488 H  HD21 . ASN   A 1 58  ? 28.150 16.343  13.564  1.00 24.89 ?  58  ASN   A HD21 1 
ATOM   1489 H  HD22 . ASN   A 1 58  ? 28.291 14.919  13.975  1.00 24.89 ?  58  ASN   A HD22 1 
ATOM   1490 N  N    . ASN   A 1 59  ? 27.171 12.515  9.319   1.00 11.02 ?  59  ASN   A N    1 
ATOM   1491 C  CA   . ASN   A 1 59  ? 28.147 12.488  8.223   1.00 10.73 ?  59  ASN   A CA   1 
ATOM   1492 C  C    . ASN   A 1 59  ? 29.464 11.812  8.611   1.00 10.45 ?  59  ASN   A C    1 
ATOM   1493 O  O    . ASN   A 1 59  ? 30.380 11.771  7.783   1.00 10.82 ?  59  ASN   A O    1 
ATOM   1494 C  CB   . ASN   A 1 59  ? 28.430 13.874  7.617   1.00 11.04 ?  59  ASN   A CB   1 
ATOM   1495 C  CG   . ASN   A 1 59  ? 28.782 13.810  6.147   1.00 11.36 ?  59  ASN   A CG   1 
ATOM   1496 O  OD1  . ASN   A 1 59  ? 28.078 13.188  5.351   1.00 11.56 ?  59  ASN   A OD1  1 
ATOM   1497 N  ND2  . ASN   A 1 59  ? 29.875 14.470  5.771   1.00 12.01 ?  59  ASN   A ND2  1 
ATOM   1498 H  H    . ASN   A 1 59  ? 26.557 11.924  9.207   1.00 13.24 ?  59  ASN   A H    1 
ATOM   1499 H  HA   . ASN   A 1 59  ? 27.767 11.957  7.513   1.00 12.89 ?  59  ASN   A HA   1 
ATOM   1500 H  HB2  . ASN   A 1 59  ? 27.641 14.430  7.704   1.00 13.26 ?  59  ASN   A HB2  1 
ATOM   1501 H  HB3  . ASN   A 1 59  ? 29.177 14.283  8.079   1.00 13.26 ?  59  ASN   A HB3  1 
ATOM   1502 H  HD21 . ASN   A 1 59  ? 30.121 14.473  4.947   1.00 14.42 ?  59  ASN   A HD21 1 
ATOM   1503 H  HD22 . ASN   A 1 59  ? 30.346 14.899  6.357   1.00 14.42 ?  59  ASN   A HD22 1 
ATOM   1504 N  N    . ALA   A 1 60  ? 29.591 11.267  9.821   1.00 10.58 ?  60  ALA   A N    1 
ATOM   1505 C  CA   . ALA   A 1 60  ? 30.828 10.580  10.178  1.00 10.77 ?  60  ALA   A CA   1 
ATOM   1506 C  C    . ALA   A 1 60  ? 31.052 9.344   9.312   1.00 10.93 ?  60  ALA   A C    1 
ATOM   1507 O  O    . ALA   A 1 60  ? 32.196 9.022   8.970   1.00 11.28 ?  60  ALA   A O    1 
ATOM   1508 C  CB   . ALA   A 1 60  ? 30.822 10.211  11.659  1.00 11.60 ?  60  ALA   A CB   1 
ATOM   1509 H  H    . ALA   A 1 60  ? 28.992 11.274  10.433  1.00 12.71 ?  60  ALA   A H    1 
ATOM   1510 H  HA   . ALA   A 1 60  ? 31.574 11.183  10.029  1.00 12.94 ?  60  ALA   A HA   1 
ATOM   1511 H  HB1  . ALA   A 1 60  ? 31.650 9.761   11.880  1.00 13.94 ?  60  ALA   A HB1  1 
ATOM   1512 H  HB2  . ALA   A 1 60  ? 30.740 11.028  12.186  1.00 13.94 ?  60  ALA   A HB2  1 
ATOM   1513 H  HB3  . ALA   A 1 60  ? 30.067 9.631   11.839  1.00 13.94 ?  60  ALA   A HB3  1 
ATOM   1514 N  N    . MET   A 1 61  ? 29.979 8.645   8.938   1.00 10.36 ?  61  MET   A N    1 
ATOM   1515 C  CA   . MET   A 1 61  ? 30.116 7.509   8.029   1.00 10.20 ?  61  MET   A CA   1 
ATOM   1516 C  C    . MET   A 1 61  ? 30.746 7.934   6.704   1.00 10.15 ?  61  MET   A C    1 
ATOM   1517 O  O    . MET   A 1 61  ? 31.641 7.255   6.186   1.00 10.61 ?  61  MET   A O    1 
ATOM   1518 C  CB   . MET   A 1 61  ? 28.751 6.848   7.814   1.00 10.11 ?  61  MET   A CB   1 
ATOM   1519 C  CG   . MET   A 1 61  ? 28.759 5.679   6.835   1.00 10.92 ?  61  MET   A CG   1 
ATOM   1520 S  SD   . MET   A 1 61  ? 27.139 4.936   6.626   1.00 11.85 ?  61  MET   A SD   1 
ATOM   1521 C  CE   . MET   A 1 61  ? 27.019 4.037   8.183   1.00 13.05 ?  61  MET   A CE   1 
ATOM   1522 H  H    . MET   A 1 61  ? 29.173 8.813   9.186   1.00 12.45 ?  61  MET   A H    1 
ATOM   1523 H  HA   . MET   A 1 61  ? 30.694 6.853   8.447   1.00 12.26 ?  61  MET   A HA   1 
ATOM   1524 H  HB2  . MET   A 1 61  ? 28.433 6.516   8.667   1.00 12.14 ?  61  MET   A HB2  1 
ATOM   1525 H  HB3  . MET   A 1 61  ? 28.134 7.514   7.474   1.00 12.14 ?  61  MET   A HB3  1 
ATOM   1526 H  HG2  . MET   A 1 61  ? 29.051 5.991   5.967   1.00 13.12 ?  61  MET   A HG2  1 
ATOM   1527 H  HG3  . MET   A 1 61  ? 29.358 4.995   7.165   1.00 13.12 ?  61  MET   A HG3  1 
ATOM   1528 H  HE1  . MET   A 1 61  ? 26.182 3.545   8.206   1.00 15.67 ?  61  MET   A HE1  1 
ATOM   1529 H  HE2  . MET   A 1 61  ? 27.765 3.419   8.252   1.00 15.67 ?  61  MET   A HE2  1 
ATOM   1530 H  HE3  . MET   A 1 61  ? 27.048 4.669   8.920   1.00 15.67 ?  61  MET   A HE3  1 
ATOM   1531 N  N    . GLN   A 1 62  ? 30.302 9.065   6.148   1.00 10.16 ?  62  GLN   A N    1 
ATOM   1532 C  CA   . GLN   A 1 62  ? 30.862 9.535   4.885   1.00 10.30 ?  62  GLN   A CA   1 
ATOM   1533 C  C    . GLN   A 1 62  ? 32.333 9.914   5.028   1.00 10.43 ?  62  GLN   A C    1 
ATOM   1534 O  O    . GLN   A 1 62  ? 33.140 9.598   4.147   1.00 10.80 ?  62  GLN   A O    1 
ATOM   1535 C  CB   . GLN   A 1 62  ? 30.057 10.719  4.350   1.00 10.29 ?  62  GLN   A CB   1 
ATOM   1536 C  CG   . GLN   A 1 62  ? 30.432 11.086  2.926   1.00 10.28 ?  62  GLN   A CG   1 
ATOM   1537 C  CD   . GLN   A 1 62  ? 30.100 9.958   1.974   1.00 10.64 ?  62  GLN   A CD   1 
ATOM   1538 O  OE1  . GLN   A 1 62  ? 28.924 9.647   1.766   1.00 11.20 ?  62  GLN   A OE1  1 
ATOM   1539 N  NE2  . GLN   A 1 62  ? 31.114 9.289   1.449   1.00 11.17 ?  62  GLN   A NE2  1 
ATOM   1540 H  H    . GLN   A 1 62  ? 29.682 9.564   6.476   1.00 12.20 ?  62  GLN   A H    1 
ATOM   1541 H  HA   . GLN   A 1 62  ? 30.808 8.817   4.238   1.00 12.37 ?  62  GLN   A HA   1 
ATOM   1542 H  HB2  . GLN   A 1 62  ? 29.116 10.496  4.367   1.00 12.37 ?  62  GLN   A HB2  1 
ATOM   1543 H  HB3  . GLN   A 1 62  ? 30.227 11.494  4.912   1.00 12.37 ?  62  GLN   A HB3  1 
ATOM   1544 H  HG2  . GLN   A 1 62  ? 29.933 11.865  2.653   1.00 12.34 ?  62  GLN   A HG2  1 
ATOM   1545 H  HG3  . GLN   A 1 62  ? 31.387 11.255  2.875   1.00 12.34 ?  62  GLN   A HG3  1 
ATOM   1546 H  HE21 . GLN   A 1 62  ? 31.923 9.520   1.632   1.00 13.42 ?  62  GLN   A HE21 1 
ATOM   1547 H  HE22 . GLN   A 1 62  ? 30.965 8.631   0.916   1.00 13.42 ?  62  GLN   A HE22 1 
ATOM   1548 N  N    . VAL   A 1 63  ? 32.694 10.602  6.116   1.00 10.86 ?  63  VAL   A N    1 
ATOM   1549 C  CA   . VAL   A 1 63  ? 34.087 10.996  6.321   1.00 11.89 ?  63  VAL   A CA   1 
ATOM   1550 C  C    . VAL   A 1 63  ? 34.982 9.762   6.381   1.00 11.29 ?  63  VAL   A C    1 
ATOM   1551 O  O    . VAL   A 1 63  ? 36.034 9.695   5.726   1.00 11.83 ?  63  VAL   A O    1 
ATOM   1552 C  CB   . VAL   A 1 63  ? 34.206 11.871  7.582   1.00 13.30 ?  63  VAL   A CB   1 
ATOM   1553 C  CG1  . VAL   A 1 63  ? 35.659 12.125  7.926   1.00 14.81 ?  63  VAL   A CG1  1 
ATOM   1554 C  CG2  . VAL   A 1 63  ? 33.467 13.196  7.373   1.00 13.48 ?  63  VAL   A CG2  1 
ATOM   1555 H  H    . VAL   A 1 63  ? 32.152 10.853  6.740   1.00 13.04 ?  63  VAL   A H    1 
ATOM   1556 H  HA   . VAL   A 1 63  ? 34.368 11.532  5.565   1.00 14.28 ?  63  VAL   A HA   1 
ATOM   1557 H  HB   . VAL   A 1 63  ? 33.797 11.413  8.331   1.00 15.97 ?  63  VAL   A HB   1 
ATOM   1558 H  HG11 . VAL   A 1 63  ? 35.708 12.858  8.559   1.00 17.79 ?  63  VAL   A HG11 1 
ATOM   1559 H  HG12 . VAL   A 1 63  ? 36.039 11.325  8.313   1.00 17.79 ?  63  VAL   A HG12 1 
ATOM   1560 H  HG13 . VAL   A 1 63  ? 36.136 12.362  7.112   1.00 17.79 ?  63  VAL   A HG13 1 
ATOM   1561 H  HG21 . VAL   A 1 63  ? 33.566 13.742  8.171   1.00 16.19 ?  63  VAL   A HG21 1 
ATOM   1562 H  HG22 . VAL   A 1 63  ? 33.852 13.657  6.610   1.00 16.19 ?  63  VAL   A HG22 1 
ATOM   1563 H  HG23 . VAL   A 1 63  ? 32.529 13.014  7.212   1.00 16.19 ?  63  VAL   A HG23 1 
ATOM   1564 N  N    . GLU   A 1 64  ? 34.567 8.757   7.157   1.00 11.17 ?  64  GLU   A N    1 
ATOM   1565 C  CA   . GLU   A 1 64  ? 35.328 7.518   7.248   1.00 11.26 ?  64  GLU   A CA   1 
ATOM   1566 C  C    . GLU   A 1 64  ? 35.412 6.832   5.892   1.00 10.70 ?  64  GLU   A C    1 
ATOM   1567 O  O    . GLU   A 1 64  ? 36.461 6.289   5.513   1.00 11.12 ?  64  GLU   A O    1 
ATOM   1568 C  CB   . GLU   A 1 64  ? 34.650 6.612   8.275   1.00 11.82 ?  64  GLU   A CB   1 
ATOM   1569 C  CG   . GLU   A 1 64  ? 35.305 5.263   8.434   1.00 12.35 ?  64  GLU   A CG   1 
ATOM   1570 C  CD   . GLU   A 1 64  ? 34.422 4.262   9.153   1.00 12.82 ?  64  GLU   A CD   1 
ATOM   1571 O  OE1  . GLU   A 1 64  ? 33.179 4.352   9.014   1.00 13.81 ?  64  GLU   A OE1  1 
ATOM   1572 O  OE2  . GLU   A 1 64  ? 34.970 3.366   9.836   1.00 13.18 -1 64  GLU   A OE2  1 
ATOM   1573 H  H    . GLU   A 1 64  ? 33.840 8.765   7.619   1.00 13.42 ?  64  GLU   A H    1 
ATOM   1574 H  HA   . GLU   A 1 64  ? 36.226 7.721   7.555   1.00 13.53 ?  64  GLU   A HA   1 
ATOM   1575 H  HB2  . GLU   A 1 64  ? 34.673 7.060   9.143   1.00 14.20 ?  64  GLU   A HB2  1 
ATOM   1576 H  HB3  . GLU   A 1 64  ? 33.730 6.479   8.007   1.00 14.20 ?  64  GLU   A HB3  1 
ATOM   1577 H  HG2  . GLU   A 1 64  ? 35.515 4.899   7.560   1.00 14.83 ?  64  GLU   A HG2  1 
ATOM   1578 H  HG3  . GLU   A 1 64  ? 36.116 5.367   8.952   1.00 14.83 ?  64  GLU   A HG3  1 
ATOM   1579 N  N    . SER   A 1 65  ? 34.293 6.823   5.162   1.00 10.47 ?  65  SER   A N    1 
ATOM   1580 C  CA   . SER   A 1 65  ? 34.245 6.160   3.865   1.00 10.33 ?  65  SER   A CA   1 
ATOM   1581 C  C    . SER   A 1 65  ? 35.168 6.828   2.857   1.00 10.64 ?  65  SER   A C    1 
ATOM   1582 O  O    . SER   A 1 65  ? 35.803 6.147   2.047   1.00 11.40 ?  65  SER   A O    1 
ATOM   1583 C  CB   . SER   A 1 65  ? 32.809 6.162   3.335   1.00 10.48 ?  65  SER   A CB   1 
ATOM   1584 O  OG   . SER   A 1 65  ? 31.960 5.347   4.135   1.00 11.23 ?  65  SER   A OG   1 
ATOM   1585 H  H    . SER   A 1 65  ? 33.555 7.196   5.398   1.00 12.58 ?  65  SER   A H    1 
ATOM   1586 H  HA   . SER   A 1 65  ? 34.528 5.240   3.965   1.00 12.41 ?  65  SER   A HA   1 
ATOM   1587 H  HB2  . SER   A 1 65  ? 32.470 7.069   3.340   1.00 12.59 ?  65  SER   A HB2  1 
ATOM   1588 H  HB3  . SER   A 1 65  ? 32.812 5.817   2.429   1.00 12.59 ?  65  SER   A HB3  1 
ATOM   1589 H  HG   . SER   A 1 65  ? 31.952 5.640   4.926   1.00 13.48 ?  65  SER   A HG   1 
ATOM   1590 N  N    . ASP   A 1 66  ? 35.241 8.160   2.876   1.00 10.85 ?  66  ASP   A N    1 
ATOM   1591 C  CA   . ASP   A 1 66  ? 36.098 8.854   1.922   1.00 11.58 ?  66  ASP   A CA   1 
ATOM   1592 C  C    . ASP   A 1 66  ? 37.563 8.503   2.154   1.00 11.49 ?  66  ASP   A C    1 
ATOM   1593 O  O    . ASP   A 1 66  ? 38.332 8.323   1.198   1.00 12.59 ?  66  ASP   A O    1 
ATOM   1594 C  CB   . ASP   A 1 66  ? 35.882 10.363  2.025   1.00 12.71 ?  66  ASP   A CB   1 
ATOM   1595 C  CG   . ASP   A 1 66  ? 34.542 10.823  1.440   1.00 14.38 ?  66  ASP   A CG   1 
ATOM   1596 O  OD1  . ASP   A 1 66  ? 33.829 10.030  0.787   1.00 14.92 ?  66  ASP   A OD1  1 
ATOM   1597 O  OD2  . ASP   A 1 66  ? 34.225 12.017  1.615   1.00 17.55 -1 66  ASP   A OD2  1 
ATOM   1598 H  H    . ASP   A 1 66  ? 34.805 8.674   3.415   1.00 13.04 ?  66  ASP   A H    1 
ATOM   1599 H  HA   . ASP   A 1 66  ? 35.859 8.578   1.025   1.00 13.92 ?  66  ASP   A HA   1 
ATOM   1600 H  HB2  . ASP   A 1 66  ? 35.903 10.622  2.961   1.00 15.27 ?  66  ASP   A HB2  1 
ATOM   1601 H  HB3  . ASP   A 1 66  ? 36.596 10.815  1.544   1.00 15.27 ?  66  ASP   A HB3  1 
ATOM   1602 N  N    . ASP   A 1 67  ? 37.965 8.376   3.418   1.00 11.60 ?  67  ASP   A N    1 
ATOM   1603 C  CA   . ASP   A 1 67  ? 39.319 7.926   3.715   1.00 12.35 ?  67  ASP   A CA   1 
ATOM   1604 C  C    . ASP   A 1 67  ? 39.534 6.489   3.251   1.00 12.39 ?  67  ASP   A C    1 
ATOM   1605 O  O    . ASP   A 1 67  ? 40.591 6.164   2.701   1.00 13.16 ?  67  ASP   A O    1 
ATOM   1606 C  CB   . ASP   A 1 67  ? 39.595 8.058   5.210   1.00 13.50 ?  67  ASP   A CB   1 
ATOM   1607 C  CG   . ASP   A 1 67  ? 40.888 7.394   5.625   1.00 15.03 ?  67  ASP   A CG   1 
ATOM   1608 O  OD1  . ASP   A 1 67  ? 41.966 8.020   5.480   1.00 18.05 ?  67  ASP   A OD1  1 
ATOM   1609 O  OD2  . ASP   A 1 67  ? 40.829 6.233   6.089   1.00 14.67 -1 67  ASP   A OD2  1 
ATOM   1610 H  H    . ASP   A 1 67  ? 37.485 8.544   4.108   1.00 13.93 ?  67  ASP   A H    1 
ATOM   1611 H  HA   . ASP   A 1 67  ? 39.953 8.486   3.242   1.00 14.84 ?  67  ASP   A HA   1 
ATOM   1612 H  HB2  . ASP   A 1 67  ? 39.650 8.991   5.437   1.00 16.21 ?  67  ASP   A HB2  1 
ATOM   1613 H  HB3  . ASP   A 1 67  ? 38.873 7.629   5.700   1.00 16.21 ?  67  ASP   A HB3  1 
ATOM   1614 N  N    . TYR   A 1 68  ? 38.538 5.616   3.447   1.00 12.12 ?  68  TYR   A N    1 
ATOM   1615 C  CA   . TYR   A 1 68  ? 38.657 4.235   2.973   1.00 11.99 ?  68  TYR   A CA   1 
ATOM   1616 C  C    . TYR   A 1 68  ? 38.892 4.186   1.463   1.00 11.69 ?  68  TYR   A C    1 
ATOM   1617 O  O    . TYR   A 1 68  ? 39.767 3.452   0.984   1.00 12.59 ?  68  TYR   A O    1 
ATOM   1618 C  CB   . TYR   A 1 68  ? 37.406 3.413   3.356   1.00 12.26 ?  68  TYR   A CB   1 
ATOM   1619 C  CG   . TYR   A 1 68  ? 37.427 2.028   2.722   1.00 13.68 ?  68  TYR   A CG   1 
ATOM   1620 C  CD1  . TYR   A 1 68  ? 36.974 1.844   1.423   1.00 14.96 ?  68  TYR   A CD1  1 
ATOM   1621 C  CD2  . TYR   A 1 68  ? 37.973 0.932   3.383   1.00 15.57 ?  68  TYR   A CD2  1 
ATOM   1622 C  CE1  . TYR   A 1 68  ? 37.033 0.627   0.801   1.00 16.27 ?  68  TYR   A CE1  1 
ATOM   1623 C  CE2  . TYR   A 1 68  ? 38.029 -0.329  2.759   1.00 15.72 ?  68  TYR   A CE2  1 
ATOM   1624 C  CZ   . TYR   A 1 68  ? 37.569 -0.450  1.467   1.00 16.38 ?  68  TYR   A CZ   1 
ATOM   1625 O  OH   . TYR   A 1 68  ? 37.643 -1.659  0.830   1.00 17.58 ?  68  TYR   A OH   1 
ATOM   1626 H  H    . TYR   A 1 68  ? 37.796 5.792   3.850   1.00 14.56 ?  68  TYR   A H    1 
ATOM   1627 H  HA   . TYR   A 1 68  ? 39.420 3.823   3.403   1.00 14.40 ?  68  TYR   A HA   1 
ATOM   1628 H  HB2  . TYR   A 1 68  ? 37.380 3.303   4.319   1.00 14.72 ?  68  TYR   A HB2  1 
ATOM   1629 H  HB3  . TYR   A 1 68  ? 36.612 3.875   3.047   1.00 14.72 ?  68  TYR   A HB3  1 
ATOM   1630 H  HD1  . TYR   A 1 68  ? 36.624 2.575   0.960   1.00 17.97 ?  68  TYR   A HD1  1 
ATOM   1631 H  HD2  . TYR   A 1 68  ? 38.306 1.030   4.245   1.00 18.70 ?  68  TYR   A HD2  1 
ATOM   1632 H  HE1  . TYR   A 1 68  ? 36.716 0.535   -0.068  1.00 19.54 ?  68  TYR   A HE1  1 
ATOM   1633 H  HE2  . TYR   A 1 68  ? 38.399 -1.062  3.194   1.00 18.88 ?  68  TYR   A HE2  1 
ATOM   1634 H  HH   . TYR   A 1 68  ? 37.978 -2.233  1.350   1.00 21.10 ?  68  TYR   A HH   1 
ATOM   1635 N  N    . ILE   A 1 69  ? 38.106 4.948   0.693   1.00 11.31 ?  69  ILE   A N    1 
ATOM   1636 C  CA   . ILE   A 1 69  ? 38.242 4.938   -0.763  1.00 11.79 ?  69  ILE   A CA   1 
ATOM   1637 C  C    . ILE   A 1 69  ? 39.577 5.543   -1.194  1.00 11.75 ?  69  ILE   A C    1 
ATOM   1638 O  O    . ILE   A 1 69  ? 40.229 5.050   -2.124  1.00 12.33 ?  69  ILE   A O    1 
ATOM   1639 C  CB   . ILE   A 1 69  ? 37.044 5.651   -1.421  1.00 12.56 ?  69  ILE   A CB   1 
ATOM   1640 C  CG1  . ILE   A 1 69  ? 35.729 4.917   -1.143  1.00 12.95 ?  69  ILE   A CG1  1 
ATOM   1641 C  CG2  . ILE   A 1 69  ? 37.289 5.849   -2.920  1.00 14.01 ?  69  ILE   A CG2  1 
ATOM   1642 C  CD1  . ILE   A 1 69  ? 35.577 3.614   -1.900  1.00 13.80 ?  69  ILE   A CD1  1 
ATOM   1643 H  H    . ILE   A 1 69  ? 37.496 5.477   0.991   1.00 13.59 ?  69  ILE   A H    1 
ATOM   1644 H  HA   . ILE   A 1 69  ? 38.235 4.016   -1.059  1.00 14.16 ?  69  ILE   A HA   1 
ATOM   1645 H  HB   . ILE   A 1 69  ? 36.976 6.529   -1.022  1.00 15.08 ?  69  ILE   A HB   1 
ATOM   1646 H  HG12 . ILE   A 1 69  ? 35.684 4.717   -0.195  1.00 15.55 ?  69  ILE   A HG12 1 
ATOM   1647 H  HG13 . ILE   A 1 69  ? 34.995 5.495   -1.393  1.00 15.55 ?  69  ILE   A HG13 1 
ATOM   1648 H  HG21 . ILE   A 1 69  ? 36.443 6.060   -3.351  1.00 16.83 ?  69  ILE   A HG21 1 
ATOM   1649 H  HG22 . ILE   A 1 69  ? 37.908 6.591   -3.047  1.00 16.83 ?  69  ILE   A HG22 1 
ATOM   1650 H  HG23 . ILE   A 1 69  ? 37.658 5.040   -3.296  1.00 16.83 ?  69  ILE   A HG23 1 
ATOM   1651 H  HD11 . ILE   A 1 69  ? 34.763 3.179   -1.609  1.00 16.57 ?  69  ILE   A HD11 1 
ATOM   1652 H  HD12 . ILE   A 1 69  ? 35.530 3.804   -2.850  1.00 16.57 ?  69  ILE   A HD12 1 
ATOM   1653 H  HD13 . ILE   A 1 69  ? 36.341 3.047   -1.713  1.00 16.57 ?  69  ILE   A HD13 1 
ATOM   1654 N  N    . ALA   A 1 70  ? 39.998 6.623   -0.540  1.00 12.03 ?  70  ALA   A N    1 
ATOM   1655 C  CA   . ALA   A 1 70  ? 41.278 7.228   -0.891  1.00 12.79 ?  70  ALA   A CA   1 
ATOM   1656 C  C    . ALA   A 1 70  ? 42.425 6.242   -0.716  1.00 13.15 ?  70  ALA   A C    1 
ATOM   1657 O  O    . ALA   A 1 70  ? 43.398 6.282   -1.476  1.00 15.09 ?  70  ALA   A O    1 
ATOM   1658 C  CB   . ALA   A 1 70  ? 41.513 8.478   -0.044  1.00 13.54 ?  70  ALA   A CB   1 
ATOM   1659 H  H    . ALA   A 1 70  ? 39.569 7.022   0.087   1.00 14.45 ?  70  ALA   A H    1 
ATOM   1660 H  HA   . ALA   A 1 70  ? 41.256 7.505   -1.823  1.00 15.37 ?  70  ALA   A HA   1 
ATOM   1661 H  HB1  . ALA   A 1 70  ? 42.371 8.868   -0.287  1.00 16.27 ?  70  ALA   A HB1  1 
ATOM   1662 H  HB2  . ALA   A 1 70  ? 40.804 9.115   -0.209  1.00 16.27 ?  70  ALA   A HB2  1 
ATOM   1663 H  HB3  . ALA   A 1 70  ? 41.524 8.226   0.893   1.00 16.27 ?  70  ALA   A HB3  1 
ATOM   1664 N  N    . THR   A 1 71  ? 42.326 5.347   0.268   1.00 12.64 ?  71  THR   A N    1 
ATOM   1665 C  CA   . THR   A 1 71  ? 43.373 4.362   0.512   1.00 14.09 ?  71  THR   A CA   1 
ATOM   1666 C  C    . THR   A 1 71  ? 43.245 3.140   -0.388  1.00 14.10 ?  71  THR   A C    1 
ATOM   1667 O  O    . THR   A 1 71  ? 44.256 2.634   -0.895  1.00 16.21 ?  71  THR   A O    1 
ATOM   1668 C  CB   . THR   A 1 71  ? 43.313 3.921   1.973   1.00 16.23 ?  71  THR   A CB   1 
ATOM   1669 O  OG1  . THR   A 1 71  ? 43.564 5.050   2.814   1.00 17.51 ?  71  THR   A OG1  1 
ATOM   1670 C  CG2  . THR   A 1 71  ? 44.328 2.819   2.263   1.00 17.80 ?  71  THR   A CG2  1 
ATOM   1671 H  H    . THR   A 1 71  ? 41.655 5.286   0.800   1.00 15.19 ?  71  THR   A H    1 
ATOM   1672 H  HA   . THR   A 1 71  ? 44.239 4.767   0.349   1.00 16.92 ?  71  THR   A HA   1 
ATOM   1673 H  HB   . THR   A 1 71  ? 42.426 3.570   2.159   1.00 19.50 ?  71  THR   A HB   1 
ATOM   1674 H  HG1  . THR   A 1 71  ? 42.978 5.638   2.679   1.00 21.02 ?  71  THR   A HG1  1 
ATOM   1675 H  HG21 . THR   A 1 71  ? 44.454 2.734   3.220   1.00 21.37 ?  71  THR   A HG21 1 
ATOM   1676 H  HG22 . THR   A 1 71  ? 44.017 1.972   1.909   1.00 21.37 ?  71  THR   A HG22 1 
ATOM   1677 H  HG23 . THR   A 1 71  ? 45.181 3.040   1.854   1.00 21.37 ?  71  THR   A HG23 1 
ATOM   1678 N  N    . ASN   A 1 72  ? 42.021 2.637   -0.579  1.00 13.46 ?  72  ASN   A N    1 
ATOM   1679 C  CA   . ASN   A 1 72  ? 41.803 1.311   -1.141  1.00 13.39 ?  72  ASN   A CA   1 
ATOM   1680 C  C    . ASN   A 1 72  ? 41.175 1.296   -2.522  1.00 13.68 ?  72  ASN   A C    1 
ATOM   1681 O  O    . ASN   A 1 72  ? 41.175 0.239   -3.167  1.00 15.20 ?  72  ASN   A O    1 
ATOM   1682 C  CB   . ASN   A 1 72  ? 40.921 0.487   -0.197  1.00 14.74 ?  72  ASN   A CB   1 
ATOM   1683 C  CG   . ASN   A 1 72  ? 41.539 0.335   1.169   1.00 15.85 ?  72  ASN   A CG   1 
ATOM   1684 O  OD1  . ASN   A 1 72  ? 41.084 0.936   2.141   1.00 17.63 ?  72  ASN   A OD1  1 
ATOM   1685 N  ND2  . ASN   A 1 72  ? 42.592 -0.448  1.247   1.00 16.20 ?  72  ASN   A ND2  1 
ATOM   1686 H  H    . ASN   A 1 72  ? 41.289 3.060   -0.391  1.00 16.17 ?  72  ASN   A H    1 
ATOM   1687 H  HA   . ASN   A 1 72  ? 42.659 0.865   -1.208  1.00 16.08 ?  72  ASN   A HA   1 
ATOM   1688 H  HB2  . ASN   A 1 72  ? 40.063 0.926   -0.097  1.00 17.70 ?  72  ASN   A HB2  1 
ATOM   1689 H  HB3  . ASN   A 1 72  ? 40.800 -0.400  -0.574  1.00 17.70 ?  72  ASN   A HB3  1 
ATOM   1690 H  HD21 . ASN   A 1 72  ? 42.985 -0.560  2.004   1.00 19.45 ?  72  ASN   A HD21 1 
ATOM   1691 H  HD22 . ASN   A 1 72  ? 42.892 -0.838  0.544   1.00 19.45 ?  72  ASN   A HD22 1 
ATOM   1692 N  N    . GLY   A 1 73  ? 40.628 2.412   -2.990  1.00 13.55 ?  73  GLY   A N    1 
ATOM   1693 C  CA   . GLY   A 1 73  ? 39.883 2.420   -4.224  1.00 13.30 ?  73  GLY   A CA   1 
ATOM   1694 C  C    . GLY   A 1 73  ? 38.488 1.841   -4.052  1.00 12.66 ?  73  GLY   A C    1 
ATOM   1695 O  O    . GLY   A 1 73  ? 38.102 1.381   -2.970  1.00 13.34 ?  73  GLY   A O    1 
ATOM   1696 H  H    . GLY   A 1 73  ? 40.684 3.189   -2.612  1.00 16.27 ?  73  GLY   A H    1 
ATOM   1697 H  HA2  . GLY   A 1 73  ? 39.803 3.334   -4.548  1.00 15.98 ?  73  GLY   A HA2  1 
ATOM   1698 H  HA3  . GLY   A 1 73  ? 40.354 1.900   -4.895  1.00 15.98 ?  73  GLY   A HA3  1 
ATOM   1699 N  N    . PRO   A 1 74  ? 37.705 1.866   -5.130  1.00 13.08 ?  74  PRO   A N    1 
ATOM   1700 C  CA   . PRO   A 1 74  ? 36.307 1.431   -5.045  1.00 13.00 ?  74  PRO   A CA   1 
ATOM   1701 C  C    . PRO   A 1 74  ? 36.160 -0.052  -4.727  1.00 12.35 ?  74  PRO   A C    1 
ATOM   1702 O  O    . PRO   A 1 74  ? 37.028 -0.885  -5.016  1.00 13.41 ?  74  PRO   A O    1 
ATOM   1703 C  CB   . PRO   A 1 74  ? 35.756 1.742   -6.444  1.00 14.60 ?  74  PRO   A CB   1 
ATOM   1704 C  CG   . PRO   A 1 74  ? 36.700 2.743   -7.038  1.00 17.38 ?  74  PRO   A CG   1 
ATOM   1705 C  CD   . PRO   A 1 74  ? 38.038 2.396   -6.462  1.00 15.01 ?  74  PRO   A CD   1 
ATOM   1706 H  HA   . PRO   A 1 74  ? 35.827 1.954   -4.383  1.00 15.62 ?  74  PRO   A HA   1 
ATOM   1707 H  HB2  . PRO   A 1 74  ? 35.731 0.929   -6.973  1.00 17.53 ?  74  PRO   A HB2  1 
ATOM   1708 H  HB3  . PRO   A 1 74  ? 34.860 2.119   -6.363  1.00 17.53 ?  74  PRO   A HB3  1 
ATOM   1709 H  HG2  . PRO   A 1 74  ? 36.708 2.654   -8.004  1.00 20.86 ?  74  PRO   A HG2  1 
ATOM   1710 H  HG3  . PRO   A 1 74  ? 36.438 3.639   -6.777  1.00 20.86 ?  74  PRO   A HG3  1 
ATOM   1711 H  HD2  . PRO   A 1 74  ? 38.477 1.714   -7.001  1.00 18.03 ?  74  PRO   A HD2  1 
ATOM   1712 H  HD3  . PRO   A 1 74  ? 38.589 3.194   -6.393  1.00 18.03 ?  74  PRO   A HD3  1 
ATOM   1713 N  N    . LEU   A 1 75  ? 35.016 -0.374  -4.131  1.00 11.57 ?  75  LEU   A N    1 
ATOM   1714 C  CA   . LEU   A 1 75  ? 34.615 -1.763  -3.980  1.00 11.56 ?  75  LEU   A CA   1 
ATOM   1715 C  C    . LEU   A 1 75  ? 34.229 -2.345  -5.339  1.00 11.81 ?  75  LEU   A C    1 
ATOM   1716 O  O    . LEU   A 1 75  ? 34.104 -1.638  -6.340  1.00 13.42 ?  75  LEU   A O    1 
ATOM   1717 C  CB   . LEU   A 1 75  ? 33.427 -1.886  -3.025  1.00 11.43 ?  75  LEU   A CB   1 
ATOM   1718 C  CG   . LEU   A 1 75  ? 33.647 -1.450  -1.581  1.00 13.12 ?  75  LEU   A CG   1 
ATOM   1719 C  CD1  . LEU   A 1 75  ? 32.362 -1.634  -0.779  1.00 14.95 ?  75  LEU   A CD1  1 
ATOM   1720 C  CD2  . LEU   A 1 75  ? 34.788 -2.168  -0.924  1.00 16.27 ?  75  LEU   A CD2  1 
ATOM   1721 H  H    . LEU   A 1 75  ? 34.455 0.192   -3.812  1.00 13.89 ?  75  LEU   A H    1 
ATOM   1722 H  HA   . LEU   A 1 75  ? 35.356 -2.278  -3.630  1.00 13.88 ?  75  LEU   A HA   1 
ATOM   1723 H  HB2  . LEU   A 1 75  ? 32.701 -1.352  -3.377  1.00 13.73 ?  75  LEU   A HB2  1 
ATOM   1724 H  HB3  . LEU   A 1 75  ? 33.157 -2.819  -3.003  1.00 13.73 ?  75  LEU   A HB3  1 
ATOM   1725 H  HG   . LEU   A 1 75  ? 33.868 -0.504  -1.578  1.00 15.76 ?  75  LEU   A HG   1 
ATOM   1726 H  HD11 . LEU   A 1 75  ? 32.521 -1.348  0.135   1.00 17.95 ?  75  LEU   A HD11 1 
ATOM   1727 H  HD12 . LEU   A 1 75  ? 31.667 -1.090  -1.180  1.00 17.95 ?  75  LEU   A HD12 1 
ATOM   1728 H  HD13 . LEU   A 1 75  ? 32.112 -2.567  -0.799  1.00 17.95 ?  75  LEU   A HD13 1 
ATOM   1729 H  HD21 . LEU   A 1 75  ? 34.839 -1.904  0.007   1.00 19.54 ?  75  LEU   A HD21 1 
ATOM   1730 H  HD22 . LEU   A 1 75  ? 34.645 -3.124  -0.991  1.00 19.54 ?  75  LEU   A HD22 1 
ATOM   1731 H  HD23 . LEU   A 1 75  ? 35.620 -1.930  -1.376  1.00 19.54 ?  75  LEU   A HD23 1 
ATOM   1732 N  N    . LYS   A 1 76  ? 34.051 -3.663  -5.360  1.00 12.53 ?  76  LYS   A N    1 
ATOM   1733 C  CA   . LYS   A 1 76  ? 33.456 -4.382  -6.480  1.00 12.78 ?  76  LYS   A CA   1 
ATOM   1734 C  C    . LYS   A 1 76  ? 31.945 -4.466  -6.287  1.00 11.64 ?  76  LYS   A C    1 
ATOM   1735 O  O    . LYS   A 1 76  ? 31.465 -4.584  -5.162  1.00 11.68 ?  76  LYS   A O    1 
ATOM   1736 C  CB   . LYS   A 1 76  ? 33.997 -5.823  -6.529  1.00 14.41 ?  76  LYS   A CB   1 
ATOM   1737 C  CG   . LYS   A 1 76  ? 35.503 -5.931  -6.733  1.00 15.81 ?  76  LYS   A CG   1 
ATOM   1738 C  CD   . LYS   A 1 76  ? 36.032 -7.331  -6.498  1.00 17.26 ?  76  LYS   A CD   1 
ATOM   1739 C  CE   . LYS   A 1 76  ? 37.524 -7.389  -6.728  1.00 19.75 ?  76  LYS   A CE   1 
ATOM   1740 N  NZ   . LYS   A 1 76  ? 38.068 -8.745  -6.530  1.00 20.99 ?  76  LYS   A NZ   1 
ATOM   1741 H  H    . LYS   A 1 76  ? 34.273 -4.181  -4.710  1.00 15.05 ?  76  LYS   A H    1 
ATOM   1742 H  HA   . LYS   A 1 76  ? 33.655 -3.934  -7.320  1.00 15.35 ?  76  LYS   A HA   1 
ATOM   1743 H  HB2  . LYS   A 1 76  ? 33.785 -6.263  -5.694  1.00 17.30 ?  76  LYS   A HB2  1 
ATOM   1744 H  HB3  . LYS   A 1 76  ? 33.571 -6.290  -7.265  1.00 17.30 ?  76  LYS   A HB3  1 
ATOM   1745 H  HG2  . LYS   A 1 76  ? 35.718 -5.679  -7.646  1.00 18.98 ?  76  LYS   A HG2  1 
ATOM   1746 H  HG3  . LYS   A 1 76  ? 35.951 -5.335  -6.112  1.00 18.98 ?  76  LYS   A HG3  1 
ATOM   1747 H  HD2  . LYS   A 1 76  ? 35.848 -7.594  -5.583  1.00 20.72 ?  76  LYS   A HD2  1 
ATOM   1748 H  HD3  . LYS   A 1 76  ? 35.600 -7.944  -7.117  1.00 20.72 ?  76  LYS   A HD3  1 
ATOM   1749 H  HE2  . LYS   A 1 76  ? 37.712 -7.115  -7.638  1.00 23.71 ?  76  LYS   A HE2  1 
ATOM   1750 H  HE3  . LYS   A 1 76  ? 37.959 -6.793  -6.100  1.00 23.71 ?  76  LYS   A HE3  1 
ATOM   1751 H  HZ1  . LYS   A 1 76  ? 38.944 -8.749  -6.672  1.00 25.20 ?  76  LYS   A HZ1  1 
ATOM   1752 H  HZ2  . LYS   A 1 76  ? 37.907 -9.024  -5.698  1.00 25.20 ?  76  LYS   A HZ2  1 
ATOM   1753 H  HZ3  . LYS   A 1 76  ? 37.681 -9.317  -7.099  1.00 25.20 ?  76  LYS   A HZ3  1 
ATOM   1754 N  N    . VAL   A 1 77  ? 31.194 -4.435  -7.392  1.00 12.16 ?  77  VAL   A N    1 
ATOM   1755 C  CA   . VAL   A 1 77  ? 29.788 -4.823  -7.302  1.00 11.90 ?  77  VAL   A CA   1 
ATOM   1756 C  C    . VAL   A 1 77  ? 29.724 -6.278  -6.858  1.00 11.44 ?  77  VAL   A C    1 
ATOM   1757 O  O    . VAL   A 1 77  ? 30.382 -7.147  -7.441  1.00 11.68 ?  77  VAL   A O    1 
ATOM   1758 C  CB   . VAL   A 1 77  ? 29.062 -4.611  -8.638  1.00 13.11 ?  77  VAL   A CB   1 
ATOM   1759 C  CG1  . VAL   A 1 77  ? 27.604 -5.047  -8.528  1.00 14.11 ?  77  VAL   A CG1  1 
ATOM   1760 C  CG2  . VAL   A 1 77  ? 29.142 -3.151  -9.067  1.00 14.39 ?  77  VAL   A CG2  1 
ATOM   1761 H  H    . VAL   A 1 77  ? 31.469 -4.207  -8.173  1.00 14.60 ?  77  VAL   A H    1 
ATOM   1762 H  HA   . VAL   A 1 77  ? 29.352 -4.280  -6.629  1.00 14.30 ?  77  VAL   A HA   1 
ATOM   1763 H  HB   . VAL   A 1 77  ? 29.492 -5.146  -9.324  1.00 15.75 ?  77  VAL   A HB   1 
ATOM   1764 H  HG11 . VAL   A 1 77  ? 27.128 -4.742  -9.314  1.00 16.95 ?  77  VAL   A HG11 1 
ATOM   1765 H  HG12 . VAL   A 1 77  ? 27.569 -6.013  -8.472  1.00 16.95 ?  77  VAL   A HG12 1 
ATOM   1766 H  HG13 . VAL   A 1 77  ? 27.220 -4.651  -7.732  1.00 16.95 ?  77  VAL   A HG13 1 
ATOM   1767 H  HG21 . VAL   A 1 77  ? 28.639 -3.037  -9.888  1.00 17.28 ?  77  VAL   A HG21 1 
ATOM   1768 H  HG22 . VAL   A 1 77  ? 28.761 -2.597  -8.366  1.00 17.28 ?  77  VAL   A HG22 1 
ATOM   1769 H  HG23 . VAL   A 1 77  ? 30.070 -2.911  -9.210  1.00 17.28 ?  77  VAL   A HG23 1 
ATOM   1770 N  N    . GLY   A 1 78  ? 28.937 -6.546  -5.812  1.00 11.01 ?  78  GLY   A N    1 
ATOM   1771 C  CA   . GLY   A 1 78  ? 28.912 -7.837  -5.152  1.00 11.31 ?  78  GLY   A CA   1 
ATOM   1772 C  C    . GLY   A 1 78  ? 29.835 -7.932  -3.956  1.00 10.74 ?  78  GLY   A C    1 
ATOM   1773 O  O    . GLY   A 1 78  ? 29.775 -8.932  -3.224  1.00 11.42 ?  78  GLY   A O    1 
ATOM   1774 H  H    . GLY   A 1 78  ? 28.381 -5.974  -5.474  1.00 13.23 ?  78  GLY   A H    1 
ATOM   1775 H  HA2  . GLY   A 1 78  ? 28.009 -8.022  -4.854  1.00 13.58 ?  78  GLY   A HA2  1 
ATOM   1776 H  HA3  . GLY   A 1 78  ? 29.168 -8.519  -5.789  1.00 13.58 ?  78  GLY   A HA3  1 
ATOM   1777 N  N    . GLY   A 1 79  ? 30.682 -6.921  -3.735  1.00 10.96 ?  79  GLY   A N    1 
ATOM   1778 C  CA   . GLY   A 1 79  ? 31.656 -6.933  -2.669  1.00 11.20 ?  79  GLY   A CA   1 
ATOM   1779 C  C    . GLY   A 1 79  ? 31.213 -6.141  -1.449  1.00 10.37 ?  79  GLY   A C    1 
ATOM   1780 O  O    . GLY   A 1 79  ? 30.095 -5.633  -1.366  1.00 11.18 ?  79  GLY   A O    1 
ATOM   1781 H  H    . GLY   A 1 79  ? 30.709 -6.199  -4.206  1.00 13.16 ?  79  GLY   A H    1 
ATOM   1782 H  HA2  . GLY   A 1 79  ? 31.816 -7.857  -2.395  1.00 13.46 ?  79  GLY   A HA2  1 
ATOM   1783 H  HA3  . GLY   A 1 79  ? 32.493 -6.567  -2.988  1.00 13.46 ?  79  GLY   A HA3  1 
ATOM   1784 N  N    . SER   A 1 80  ? 32.125 -6.051  -0.482  1.00 11.37 ?  80  SER   A N    1 
ATOM   1785 C  CA   . SER   A 1 80  ? 31.812 -5.415  0.789   1.00 10.66 ?  80  SER   A CA   1 
ATOM   1786 C  C    . SER   A 1 80  ? 33.085 -4.957  1.477   1.00 10.65 ?  80  SER   A C    1 
ATOM   1787 O  O    . SER   A 1 80  ? 34.194 -5.394  1.146   1.00 12.13 ?  80  SER   A O    1 
ATOM   1788 C  CB   . SER   A 1 80  ? 31.060 -6.371  1.725   1.00 11.72 ?  80  SER   A CB   1 
ATOM   1789 O  OG   . SER   A 1 80  ? 31.893 -7.424  2.194   1.00 13.43 ?  80  SER   A OG   1 
ATOM   1790 H  H    . SER   A 1 80  ? 32.934 -6.336  -0.545  1.00 13.66 ?  80  SER   A H    1 
ATOM   1791 H  HA   . SER   A 1 80  ? 31.258 -4.636  0.615   1.00 12.80 ?  80  SER   A HA   1 
ATOM   1792 H  HB2  . SER   A 1 80  ? 30.735 -5.869  2.487   1.00 14.08 ?  80  SER   A HB2  1 
ATOM   1793 H  HB3  . SER   A 1 80  ? 30.312 -6.755  1.240   1.00 14.08 ?  80  SER   A HB3  1 
ATOM   1794 H  HG   . SER   A 1 80  ? 32.184 -7.865  1.534   1.00 16.13 ?  80  SER   A HG   1 
ATOM   1795 N  N    . CYS   A 1 81  ? 32.898 -4.112  2.489   1.00 10.54 ?  81  CYS   A N    1 
ATOM   1796 C  CA   . CYS   A 1 81  ? 33.955 -3.826  3.449   1.00 10.66 ?  81  CYS   A CA   1 
ATOM   1797 C  C    . CYS   A 1 81  ? 33.317 -3.589  4.809   1.00 10.39 ?  81  CYS   A C    1 
ATOM   1798 O  O    . CYS   A 1 81  ? 32.150 -3.187  4.900   1.00 11.41 ?  81  CYS   A O    1 
ATOM   1799 C  CB   . CYS   A 1 81  ? 34.825 -2.633  3.032   1.00 11.54 ?  81  CYS   A CB   1 
ATOM   1800 S  SG   . CYS   A 1 81  ? 33.934 -1.061  3.046   1.00 11.44 ?  81  CYS   A SG   1 
ATOM   1801 H  H    . CYS   A 1 81  ? 32.165 -3.689  2.645   1.00 12.67 ?  81  CYS   A H    1 
ATOM   1802 H  HA   . CYS   A 1 81  ? 34.536 -4.602  3.517   1.00 12.81 ?  81  CYS   A HA   1 
ATOM   1803 H  HB2  . CYS   A 1 81  ? 35.578 -2.562  3.647   1.00 13.86 ?  81  CYS   A HB2  1 
ATOM   1804 H  HB3  . CYS   A 1 81  ? 35.160 -2.787  2.130   1.00 13.86 ?  81  CYS   A HB3  1 
ATOM   1805 H  HG   . CYS   A 1 81  ? 34.680 -0.182  2.710   1.00 13.74 ?  81  CYS   A HG   1 
ATOM   1806 N  N    . VAL   A 1 82  ? 34.089 -3.854  5.864   1.00 10.77 ?  82  VAL   A N    1 
ATOM   1807 C  CA   . VAL   A 1 82  ? 33.667 -3.608  7.236   1.00 11.00 ?  82  VAL   A CA   1 
ATOM   1808 C  C    . VAL   A 1 82  ? 34.273 -2.293  7.703   1.00 11.34 ?  82  VAL   A C    1 
ATOM   1809 O  O    . VAL   A 1 82  ? 35.498 -2.119  7.682   1.00 12.07 ?  82  VAL   A O    1 
ATOM   1810 C  CB   . VAL   A 1 82  ? 34.085 -4.750  8.176   1.00 12.76 ?  82  VAL   A CB   1 
ATOM   1811 C  CG1  . VAL   A 1 82  ? 33.640 -4.451  9.599   1.00 14.23 ?  82  VAL   A CG1  1 
ATOM   1812 C  CG2  . VAL   A 1 82  ? 33.526 -6.076  7.702   1.00 13.50 ?  82  VAL   A CG2  1 
ATOM   1813 H  H    . VAL   A 1 82  ? 34.886 -4.190  5.809   1.00 12.94 ?  82  VAL   A H    1 
ATOM   1814 H  HA   . VAL   A 1 82  ? 32.699 -3.527  7.262   1.00 13.21 ?  82  VAL   A HA   1 
ATOM   1815 H  HB   . VAL   A 1 82  ? 35.051 -4.812  8.177   1.00 15.32 ?  82  VAL   A HB   1 
ATOM   1816 H  HG11 . VAL   A 1 82  ? 33.727 -5.257  10.131  1.00 17.09 ?  82  VAL   A HG11 1 
ATOM   1817 H  HG12 . VAL   A 1 82  ? 34.198 -3.750  9.971   1.00 17.09 ?  82  VAL   A HG12 1 
ATOM   1818 H  HG13 . VAL   A 1 82  ? 32.711 -4.164  9.589   1.00 17.09 ?  82  VAL   A HG13 1 
ATOM   1819 H  HG21 . VAL   A 1 82  ? 33.770 -6.765  8.337   1.00 16.22 ?  82  VAL   A HG21 1 
ATOM   1820 H  HG22 . VAL   A 1 82  ? 32.560 -6.008  7.640   1.00 16.22 ?  82  VAL   A HG22 1 
ATOM   1821 H  HG23 . VAL   A 1 82  ? 33.900 -6.281  6.830   1.00 16.22 ?  82  VAL   A HG23 1 
ATOM   1822 N  N    . LEU   A 1 83  ? 33.419 -1.370  8.129   1.00 11.00 ?  83  LEU   A N    1 
ATOM   1823 C  CA   . LEU   A 1 83  ? 33.841 -0.107  8.711   1.00 10.84 ?  83  LEU   A CA   1 
ATOM   1824 C  C    . LEU   A 1 83  ? 33.126 0.075   10.043  1.00 11.24 ?  83  LEU   A C    1 
ATOM   1825 O  O    . LEU   A 1 83  ? 32.401 -0.813  10.504  1.00 11.61 ?  83  LEU   A O    1 
ATOM   1826 C  CB   . LEU   A 1 83  ? 33.596 1.055   7.736   1.00 11.53 ?  83  LEU   A CB   1 
ATOM   1827 C  CG   . LEU   A 1 83  ? 34.481 1.050   6.485   1.00 12.32 ?  83  LEU   A CG   1 
ATOM   1828 C  CD1  . LEU   A 1 83  ? 34.033 2.091   5.477   1.00 12.85 ?  83  LEU   A CD1  1 
ATOM   1829 C  CD2  . LEU   A 1 83  ? 35.955 1.267   6.851   1.00 13.07 ?  83  LEU   A CD2  1 
ATOM   1830 H  H    . LEU   A 1 83  ? 32.562 -1.454  8.085   1.00 13.21 ?  83  LEU   A H    1 
ATOM   1831 H  HA   . LEU   A 1 83  ? 34.790 -0.139  8.891   1.00 13.02 ?  83  LEU   A HA   1 
ATOM   1832 H  HB2  . LEU   A 1 83  ? 32.673 1.025   7.434   1.00 13.85 ?  83  LEU   A HB2  1 
ATOM   1833 H  HB3  . LEU   A 1 83  ? 33.753 1.895   8.199   1.00 13.85 ?  83  LEU   A HB3  1 
ATOM   1834 H  HG   . LEU   A 1 83  ? 34.414 0.182   6.065   1.00 14.80 ?  83  LEU   A HG   1 
ATOM   1835 H  HD11 . LEU   A 1 83  ? 34.619 2.047   4.702   1.00 15.43 ?  83  LEU   A HD11 1 
ATOM   1836 H  HD12 . LEU   A 1 83  ? 33.122 1.894   5.211   1.00 15.43 ?  83  LEU   A HD12 1 
ATOM   1837 H  HD13 . LEU   A 1 83  ? 34.083 2.967   5.881   1.00 15.43 ?  83  LEU   A HD13 1 
ATOM   1838 H  HD21 . LEU   A 1 83  ? 36.470 1.398   6.037   1.00 15.69 ?  83  LEU   A HD21 1 
ATOM   1839 H  HD22 . LEU   A 1 83  ? 36.031 2.055   7.416   1.00 15.69 ?  83  LEU   A HD22 1 
ATOM   1840 H  HD23 . LEU   A 1 83  ? 36.286 0.490   7.328   1.00 15.69 ?  83  LEU   A HD23 1 
ATOM   1841 N  N    . SER   A 1 84  ? 33.336 1.228   10.672  1.00 11.96 ?  84  SER   A N    1 
ATOM   1842 C  CA   . SER   A 1 84  ? 32.697 1.483   11.952  1.00 12.04 ?  84  SER   A CA   1 
ATOM   1843 C  C    . SER   A 1 84  ? 31.179 1.565   11.812  1.00 11.65 ?  84  SER   A C    1 
ATOM   1844 O  O    . SER   A 1 84  ? 30.646 2.024   10.801  1.00 11.94 ?  84  SER   A O    1 
ATOM   1845 C  CB   . SER   A 1 84  ? 33.201 2.798   12.535  1.00 13.02 ?  84  SER   A CB   1 
ATOM   1846 O  OG   . SER   A 1 84  ? 32.555 3.085   13.760  1.00 13.91 ?  84  SER   A OG   1 
ATOM   1847 H  H    . SER   A 1 84  ? 33.831 1.875   10.375  1.00 14.36 ?  84  SER   A H    1 
ATOM   1848 H  HA   . SER   A 1 84  ? 32.919 0.768   12.563  1.00 14.46 ?  84  SER   A HA   1 
ATOM   1849 H  HB2  . SER   A 1 84  ? 34.160 2.731   12.690  1.00 15.64 ?  84  SER   A HB2  1 
ATOM   1850 H  HB3  . SER   A 1 84  ? 33.022 3.517   11.907  1.00 15.64 ?  84  SER   A HB3  1 
ATOM   1851 H  HG   . SER   A 1 84  ? 32.843 3.811   14.076  1.00 16.70 ?  84  SER   A HG   1 
ATOM   1852 N  N    . GLY   A 1 85  ? 30.480 1.149   12.863  1.00 12.74 ?  85  GLY   A N    1 
ATOM   1853 C  CA   . GLY   A 1 85  ? 29.056 1.380   12.964  1.00 13.41 ?  85  GLY   A CA   1 
ATOM   1854 C  C    . GLY   A 1 85  ? 28.685 2.702   13.598  1.00 12.84 ?  85  GLY   A C    1 
ATOM   1855 O  O    . GLY   A 1 85  ? 27.496 3.021   13.713  1.00 13.31 ?  85  GLY   A O    1 
ATOM   1856 H  H    . GLY   A 1 85  ? 30.820 0.724   13.534  1.00 15.31 ?  85  GLY   A H    1 
ATOM   1857 H  HA2  . GLY   A 1 85  ? 28.673 1.350   12.076  1.00 16.11 ?  85  GLY   A HA2  1 
ATOM   1858 H  HA3  . GLY   A 1 85  ? 28.660 0.673   13.490  1.00 16.11 ?  85  GLY   A HA3  1 
ATOM   1859 N  N    . HIS   A 1 86  ? 29.668 3.487   14.026  1.00 12.73 ?  86  HIS   A N    1 
ATOM   1860 C  CA   . HIS   A 1 86  ? 29.437 4.821   14.594  1.00 13.14 ?  86  HIS   A CA   1 
ATOM   1861 C  C    . HIS   A 1 86  ? 28.461 4.701   15.758  1.00 13.70 ?  86  HIS   A C    1 
ATOM   1862 O  O    . HIS   A 1 86  ? 28.651 3.824   16.617  1.00 15.04 ?  86  HIS   A O    1 
ATOM   1863 C  CB   . HIS   A 1 86  ? 29.051 5.792   13.485  1.00 13.32 ?  86  HIS   A CB   1 
ATOM   1864 C  CG   . HIS   A 1 86  ? 30.108 5.897   12.445  1.00 13.20 ?  86  HIS   A CG   1 
ATOM   1865 N  ND1  . HIS   A 1 86  ? 31.190 6.742   12.574  1.00 14.18 ?  86  HIS   A ND1  1 
ATOM   1866 C  CD2  . HIS   A 1 86  ? 30.300 5.201   11.303  1.00 12.93 ?  86  HIS   A CD2  1 
ATOM   1867 C  CE1  . HIS   A 1 86  ? 31.986 6.580   11.532  1.00 13.78 ?  86  HIS   A CE1  1 
ATOM   1868 N  NE2  . HIS   A 1 86  ? 31.476 5.644   10.754  1.00 13.09 ?  86  HIS   A NE2  1 
ATOM   1869 H  H    . HIS   A 1 86  ? 30.496 3.271   14.008  1.00 15.29 ?  86  HIS   A H    1 
ATOM   1870 H  HA   . HIS   A 1 86  ? 30.274 5.143   14.962  1.00 15.79 ?  86  HIS   A HA   1 
ATOM   1871 H  HB2  . HIS   A 1 86  ? 28.234 5.489   13.056  1.00 16.00 ?  86  HIS   A HB2  1 
ATOM   1872 H  HB3  . HIS   A 1 86  ? 28.916 6.681   13.860  1.00 16.00 ?  86  HIS   A HB3  1 
ATOM   1873 H  HD2  . HIS   A 1 86  ? 29.746 4.534   10.954  1.00 15.53 ?  86  HIS   A HD2  1 
ATOM   1874 H  HE1  . HIS   A 1 86  ? 32.776 7.045   11.366  1.00 16.55 ?  86  HIS   A HE1  1 
ATOM   1875 H  HE2  . HIS   A 1 86  ? 31.818 5.367   10.005  1.00 15.73 ?  86  HIS   A HE2  1 
ATOM   1876 N  N    . ASN   A 1 87  ? 27.445 5.554   15.833  1.00 14.81 ?  87  ASN   A N    1 
ATOM   1877 C  CA   . ASN   A 1 87  ? 26.455 5.534   16.895  1.00 15.87 ?  87  ASN   A CA   1 
ATOM   1878 C  C    . ASN   A 1 87  ? 25.332 4.537   16.644  1.00 17.01 ?  87  ASN   A C    1 
ATOM   1879 O  O    . ASN   A 1 87  ? 24.405 4.462   17.455  1.00 19.32 ?  87  ASN   A O    1 
ATOM   1880 C  CB   . ASN   A 1 87  ? 25.855 6.938   17.064  1.00 16.93 ?  87  ASN   A CB   1 
ATOM   1881 C  CG   . ASN   A 1 87  ? 25.342 7.522   15.750  1.00 17.74 ?  87  ASN   A CG   1 
ATOM   1882 O  OD1  . ASN   A 1 87  ? 25.980 7.401   14.707  1.00 18.56 ?  87  ASN   A OD1  1 
ATOM   1883 N  ND2  . ASN   A 1 87  ? 24.191 8.163   15.802  1.00 18.94 ?  87  ASN   A ND2  1 
ATOM   1884 H  H    . ASN   A 1 87  ? 27.304 6.176   15.258  1.00 17.79 ?  87  ASN   A H    1 
ATOM   1885 H  HA   . ASN   A 1 87  ? 26.887 5.291   17.732  1.00 19.06 ?  87  ASN   A HA   1 
ATOM   1886 H  HB2  . ASN   A 1 87  ? 25.108 6.888   17.687  1.00 20.33 ?  87  ASN   A HB2  1 
ATOM   1887 H  HB3  . ASN   A 1 87  ? 26.536 7.530   17.416  1.00 20.33 ?  87  ASN   A HB3  1 
ATOM   1888 H  HD21 . ASN   A 1 87  ? 23.866 8.510   15.088  1.00 22.74 ?  87  ASN   A HD21 1 
ATOM   1889 H  HD22 . ASN   A 1 87  ? 23.774 8.242   16.551  1.00 22.74 ?  87  ASN   A HD22 1 
ATOM   1890 N  N    . LEU   A 1 88  ? 25.398 3.757   15.568  1.00 15.68 ?  88  LEU   A N    1 
ATOM   1891 C  CA   . LEU   A 1 88  ? 24.289 2.894   15.173  1.00 15.48 ?  88  LEU   A CA   1 
ATOM   1892 C  C    . LEU   A 1 88  ? 24.504 1.417   15.475  1.00 15.11 ?  88  LEU   A C    1 
ATOM   1893 O  O    . LEU   A 1 88  ? 23.525 0.682   15.633  1.00 16.46 ?  88  LEU   A O    1 
ATOM   1894 C  CB   . LEU   A 1 88  ? 24.037 3.046   13.673  1.00 16.10 ?  88  LEU   A CB   1 
ATOM   1895 C  CG   . LEU   A 1 88  ? 23.736 4.471   13.203  1.00 17.83 ?  88  LEU   A CG   1 
ATOM   1896 C  CD1  . LEU   A 1 88  ? 23.569 4.504   11.696  1.00 18.30 ?  88  LEU   A CD1  1 
ATOM   1897 C  CD2  . LEU   A 1 88  ? 22.494 5.022   13.894  1.00 19.71 ?  88  LEU   A CD2  1 
ATOM   1898 H  H    . LEU   A 1 88  ? 26.085 3.705   15.057  1.00 18.83 ?  88  LEU   A H    1 
ATOM   1899 H  HA   . LEU   A 1 88  ? 23.493 3.178   15.642  1.00 18.59 ?  88  LEU   A HA   1 
ATOM   1900 H  HB2  . LEU   A 1 88  ? 24.819 2.743   13.191  1.00 19.33 ?  88  LEU   A HB2  1 
ATOM   1901 H  HB3  . LEU   A 1 88  ? 23.272 2.498   13.433  1.00 19.33 ?  88  LEU   A HB3  1 
ATOM   1902 H  HG   . LEU   A 1 88  ? 24.484 5.044   13.431  1.00 21.41 ?  88  LEU   A HG   1 
ATOM   1903 H  HD11 . LEU   A 1 88  ? 23.385 5.416   11.416  1.00 21.97 ?  88  LEU   A HD11 1 
ATOM   1904 H  HD12 . LEU   A 1 88  ? 24.388 4.192   11.279  1.00 21.97 ?  88  LEU   A HD12 1 
ATOM   1905 H  HD13 . LEU   A 1 88  ? 22.830 3.928   11.444  1.00 21.97 ?  88  LEU   A HD13 1 
ATOM   1906 H  HD21 . LEU   A 1 88  ? 22.253 5.865   13.480  1.00 23.67 ?  88  LEU   A HD21 1 
ATOM   1907 H  HD22 . LEU   A 1 88  ? 21.771 4.385   13.795  1.00 23.67 ?  88  LEU   A HD22 1 
ATOM   1908 H  HD23 . LEU   A 1 88  ? 22.692 5.158   14.833  1.00 23.67 ?  88  LEU   A HD23 1 
ATOM   1909 N  N    . ALA   A 1 89  ? 25.750 0.966   15.531  1.00 14.30 ?  89  ALA   A N    1 
ATOM   1910 C  CA   . ALA   A 1 89  ? 26.094 -0.445  15.630  1.00 14.16 ?  89  ALA   A CA   1 
ATOM   1911 C  C    . ALA   A 1 89  ? 27.579 -0.505  15.948  1.00 14.42 ?  89  ALA   A C    1 
ATOM   1912 O  O    . ALA   A 1 89  ? 28.289 0.496   15.841  1.00 15.13 ?  89  ALA   A O    1 
ATOM   1913 C  CB   . ALA   A 1 89  ? 25.810 -1.165  14.312  1.00 13.85 ?  89  ALA   A CB   1 
ATOM   1914 H  H    . ALA   A 1 89  ? 26.437 1.479   15.504  1.00 17.18 ?  89  ALA   A H    1 
ATOM   1915 H  HA   . ALA   A 1 89  ? 25.590 -0.866  16.345  1.00 17.00 ?  89  ALA   A HA   1 
ATOM   1916 H  HB1  . ALA   A 1 89  ? 26.065 -2.099  14.399  1.00 16.64 ?  89  ALA   A HB1  1 
ATOM   1917 H  HB2  . ALA   A 1 89  ? 24.861 -1.103  14.111  1.00 16.64 ?  89  ALA   A HB2  1 
ATOM   1918 H  HB3  . ALA   A 1 89  ? 26.325 -0.750  13.604  1.00 16.64 ?  89  ALA   A HB3  1 
ATOM   1919 N  N    . LYS   A 1 90  ? 28.061 -1.684  16.328  1.00 15.09 ?  90  LYS   A N    1 
ATOM   1920 C  CA   . LYS   A 1 90  ? 29.506 -1.826  16.476  1.00 15.55 ?  90  LYS   A CA   1 
ATOM   1921 C  C    . LYS   A 1 90  ? 30.204 -1.643  15.132  1.00 14.56 ?  90  LYS   A C    1 
ATOM   1922 O  O    . LYS   A 1 90  ? 31.138 -0.833  15.001  1.00 15.80 ?  90  LYS   A O    1 
ATOM   1923 C  CB   . LYS   A 1 90  ? 29.852 -3.178  17.097  1.00 17.91 ?  90  LYS   A CB   1 
ATOM   1924 C  CG   . LYS   A 1 90  ? 31.327 -3.316  17.440  1.00 23.03 ?  90  LYS   A CG   1 
ATOM   1925 C  CD   . LYS   A 1 90  ? 31.587 -4.594  18.221  1.00 28.74 ?  90  LYS   A CD   1 
ATOM   1926 C  CE   . LYS   A 1 90  ? 32.976 -4.604  18.842  1.00 33.48 ?  90  LYS   A CE   1 
ATOM   1927 N  NZ   . LYS   A 1 90  ? 34.051 -4.789  17.832  1.00 36.48 ?  90  LYS   A NZ   1 
ATOM   1928 H  H    . LYS   A 1 90  ? 27.593 -2.380  16.505  1.00 18.12 ?  90  LYS   A H    1 
ATOM   1929 H  HA   . LYS   A 1 90  ? 29.828 -1.134  17.070  1.00 18.67 ?  90  LYS   A HA   1 
ATOM   1930 H  HB2  . LYS   A 1 90  ? 29.341 -3.286  17.917  1.00 21.50 ?  90  LYS   A HB2  1 
ATOM   1931 H  HB3  . LYS   A 1 90  ? 29.621 -3.882  16.471  1.00 21.50 ?  90  LYS   A HB3  1 
ATOM   1932 H  HG2  . LYS   A 1 90  ? 31.847 -3.346  16.622  1.00 27.65 ?  90  LYS   A HG2  1 
ATOM   1933 H  HG3  . LYS   A 1 90  ? 31.602 -2.562  17.987  1.00 27.65 ?  90  LYS   A HG3  1 
ATOM   1934 H  HD2  . LYS   A 1 90  ? 30.934 -4.671  18.936  1.00 34.50 ?  90  LYS   A HD2  1 
ATOM   1935 H  HD3  . LYS   A 1 90  ? 31.517 -5.355  17.623  1.00 34.50 ?  90  LYS   A HD3  1 
ATOM   1936 H  HE2  . LYS   A 1 90  ? 33.128 -3.758  19.292  1.00 40.18 ?  90  LYS   A HE2  1 
ATOM   1937 H  HE3  . LYS   A 1 90  ? 33.033 -5.333  19.480  1.00 40.18 ?  90  LYS   A HE3  1 
ATOM   1938 H  HZ1  . LYS   A 1 90  ? 34.847 -4.790  18.233  1.00 43.79 ?  90  LYS   A HZ1  1 
ATOM   1939 H  HZ2  . LYS   A 1 90  ? 33.941 -5.565  17.410  1.00 43.79 ?  90  LYS   A HZ2  1 
ATOM   1940 H  HZ3  . LYS   A 1 90  ? 34.027 -4.129  17.237  1.00 43.79 ?  90  LYS   A HZ3  1 
ATOM   1941 N  N    . HIS   A 1 91  ? 29.729 -2.362  14.114  1.00 12.83 ?  91  HIS   A N    1 
ATOM   1942 C  CA   . HIS   A 1 91  ? 30.301 -2.349  12.783  1.00 12.44 ?  91  HIS   A CA   1 
ATOM   1943 C  C    . HIS   A 1 91  ? 29.212 -2.076  11.764  1.00 11.06 ?  91  HIS   A C    1 
ATOM   1944 O  O    . HIS   A 1 91  ? 28.049 -2.443  11.960  1.00 12.04 ?  91  HIS   A O    1 
ATOM   1945 C  CB   . HIS   A 1 91  ? 30.889 -3.721  12.421  1.00 14.65 ?  91  HIS   A CB   1 
ATOM   1946 C  CG   . HIS   A 1 91  ? 31.878 -4.241  13.413  1.00 19.00 ?  91  HIS   A CG   1 
ATOM   1947 N  ND1  . HIS   A 1 91  ? 33.158 -3.743  13.517  1.00 21.12 ?  91  HIS   A ND1  1 
ATOM   1948 C  CD2  . HIS   A 1 91  ? 31.783 -5.226  14.339  1.00 20.89 ?  91  HIS   A CD2  1 
ATOM   1949 C  CE1  . HIS   A 1 91  ? 33.809 -4.396  14.465  1.00 22.02 ?  91  HIS   A CE1  1 
ATOM   1950 N  NE2  . HIS   A 1 91  ? 32.996 -5.301  14.980  1.00 22.27 ?  91  HIS   A NE2  1 
ATOM   1951 H  H    . HIS   A 1 91  ? 29.050 -2.901  14.182  1.00 15.41 ?  91  HIS   A H    1 
ATOM   1952 H  HA   . HIS   A 1 91  ? 30.992 -1.680  12.713  1.00 14.94 ?  91  HIS   A HA   1 
ATOM   1953 H  HB2  . HIS   A 1 91  ? 30.167 -4.370  12.361  1.00 17.60 ?  91  HIS   A HB2  1 
ATOM   1954 H  HB3  . HIS   A 1 91  ? 31.338 -3.656  11.562  1.00 17.60 ?  91  HIS   A HB3  1 
ATOM   1955 H  HD1  . HIS   A 1 91  ? 33.486 -3.108  13.034  1.00 25.36 ?  91  HIS   A HD1  1 
ATOM   1956 H  HD2  . HIS   A 1 91  ? 31.040 -5.755  14.509  1.00 25.08 ?  91  HIS   A HD2  1 
ATOM   1957 H  HE1  . HIS   A 1 91  ? 34.691 -4.238  14.723  1.00 26.44 ?  91  HIS   A HE1  1 
ATOM   1958 N  N    . CYS   A 1 92  ? 29.614 -1.481  10.648  1.00 10.91 ?  92  CYS   A N    1 
ATOM   1959 C  CA   . CYS   A 1 92  ? 28.782 -1.402  9.456   1.00 11.03 ?  92  CYS   A CA   1 
ATOM   1960 C  C    . CYS   A 1 92  ? 29.429 -2.225  8.349   1.00 10.41 ?  92  CYS   A C    1 
ATOM   1961 O  O    . CYS   A 1 92  ? 30.587 -1.974  7.977   1.00 11.20 ?  92  CYS   A O    1 
ATOM   1962 C  CB   . CYS   A 1 92  ? 28.572 0.042   8.997   1.00 11.31 ?  92  CYS   A CB   1 
ATOM   1963 S  SG   . CYS   A 1 92  ? 27.553 0.146   7.491   1.00 10.75 ?  92  CYS   A SG   1 
ATOM   1964 H  H    . CYS   A 1 92  ? 30.385 -1.101  10.548  1.00 13.10 ?  92  CYS   A H    1 
ATOM   1965 H  HA   . CYS   A 1 92  ? 27.914 -1.781  9.648   1.00 13.25 ?  92  CYS   A HA   1 
ATOM   1966 H  HB2  . CYS   A 1 92  ? 28.119 0.539   9.698   1.00 13.59 ?  92  CYS   A HB2  1 
ATOM   1967 H  HB3  . CYS   A 1 92  ? 29.430 0.449   8.803   1.00 13.59 ?  92  CYS   A HB3  1 
ATOM   1968 H  HG   . CYS   A 1 92  ? 27.411 1.298   7.194   1.00 12.91 ?  92  CYS   A HG   1 
ATOM   1969 N  N    . LEU   A 1 93  ? 28.695 -3.219  7.854   1.00 10.37 ?  93  LEU   A N    1 
ATOM   1970 C  CA   . LEU   A 1 93  ? 29.089 -3.971  6.669   1.00 10.11 ?  93  LEU   A CA   1 
ATOM   1971 C  C    . LEU   A 1 93  ? 28.490 -3.275  5.452   1.00 9.61  ?  93  LEU   A C    1 
ATOM   1972 O  O    . LEU   A 1 93  ? 27.273 -3.325  5.234   1.00 9.90  ?  93  LEU   A O    1 
ATOM   1973 C  CB   . LEU   A 1 93  ? 28.608 -5.415  6.774   1.00 10.29 ?  93  LEU   A CB   1 
ATOM   1974 C  CG   . LEU   A 1 93  ? 28.988 -6.314  5.602   1.00 10.54 ?  93  LEU   A CG   1 
ATOM   1975 C  CD1  . LEU   A 1 93  ? 30.490 -6.566  5.588   1.00 11.73 ?  93  LEU   A CD1  1 
ATOM   1976 C  CD2  . LEU   A 1 93  ? 28.217 -7.632  5.655   1.00 11.40 ?  93  LEU   A CD2  1 
ATOM   1977 H  H    . LEU   A 1 93  ? 27.946 -3.476  8.196   1.00 12.45 ?  93  LEU   A H    1 
ATOM   1978 H  HA   . LEU   A 1 93  ? 30.051 -3.966  6.592   1.00 12.14 ?  93  LEU   A HA   1 
ATOM   1979 H  HB2  . LEU   A 1 93  ? 28.983 -5.804  7.581   1.00 12.36 ?  93  LEU   A HB2  1 
ATOM   1980 H  HB3  . LEU   A 1 93  ? 27.639 -5.413  6.839   1.00 12.36 ?  93  LEU   A HB3  1 
ATOM   1981 H  HG   . LEU   A 1 93  ? 28.761 -5.868  4.777   1.00 12.67 ?  93  LEU   A HG   1 
ATOM   1982 H  HD11 . LEU   A 1 93  ? 30.704 -7.189  4.877   1.00 14.09 ?  93  LEU   A HD11 1 
ATOM   1983 H  HD12 . LEU   A 1 93  ? 30.958 -5.728  5.446   1.00 14.09 ?  93  LEU   A HD12 1 
ATOM   1984 H  HD13 . LEU   A 1 93  ? 30.759 -6.947  6.446   1.00 14.09 ?  93  LEU   A HD13 1 
ATOM   1985 H  HD21 . LEU   A 1 93  ? 28.483 -8.184  4.899   1.00 13.69 ?  93  LEU   A HD21 1 
ATOM   1986 H  HD22 . LEU   A 1 93  ? 28.423 -8.092  6.484   1.00 13.69 ?  93  LEU   A HD22 1 
ATOM   1987 H  HD23 . LEU   A 1 93  ? 27.267 -7.446  5.606   1.00 13.69 ?  93  LEU   A HD23 1 
ATOM   1988 N  N    . HIS   A 1 94  ? 29.338 -2.584  4.689   1.00 9.78  ?  94  HIS   A N    1 
ATOM   1989 C  CA   . HIS   A 1 94  ? 28.916 -1.911  3.465   1.00 9.51  ?  94  HIS   A CA   1 
ATOM   1990 C  C    . HIS   A 1 94  ? 28.918 -2.944  2.354   1.00 9.78  ?  94  HIS   A C    1 
ATOM   1991 O  O    . HIS   A 1 94  ? 29.977 -3.463  2.002   1.00 11.11 ?  94  HIS   A O    1 
ATOM   1992 C  CB   . HIS   A 1 94  ? 29.872 -0.767  3.131   1.00 9.66  ?  94  HIS   A CB   1 
ATOM   1993 C  CG   . HIS   A 1 94  ? 29.860 0.330   4.139   1.00 9.73  ?  94  HIS   A CG   1 
ATOM   1994 N  ND1  . HIS   A 1 94  ? 28.981 1.393   4.080   1.00 9.79  ?  94  HIS   A ND1  1 
ATOM   1995 C  CD2  . HIS   A 1 94  ? 30.595 0.499   5.262   1.00 10.66 ?  94  HIS   A CD2  1 
ATOM   1996 C  CE1  . HIS   A 1 94  ? 29.196 2.176   5.122   1.00 10.12 ?  94  HIS   A CE1  1 
ATOM   1997 N  NE2  . HIS   A 1 94  ? 30.168 1.658   5.854   1.00 10.50 ?  94  HIS   A NE2  1 
ATOM   1998 H  H    . HIS   A 1 94  ? 30.175 -2.489  4.869   1.00 11.74 ?  94  HIS   A H    1 
ATOM   1999 H  HA   . HIS   A 1 94  ? 28.017 -1.563  3.572   1.00 11.42 ?  94  HIS   A HA   1 
ATOM   2000 H  HB2  . HIS   A 1 94  ? 30.769 -1.116  3.078   1.00 11.60 ?  94  HIS   A HB2  1 
ATOM   2001 H  HB3  . HIS   A 1 94  ? 29.608 -0.386  2.278   1.00 11.60 ?  94  HIS   A HB3  1 
ATOM   2002 H  HD2  . HIS   A 1 94  ? 31.266 -0.056  5.578   1.00 12.81 ?  94  HIS   A HD2  1 
ATOM   2003 H  HE1  . HIS   A 1 94  ? 28.730 2.966   5.307   1.00 12.16 ?  94  HIS   A HE1  1 
ATOM   2004 H  HE2  . HIS   A 1 94  ? 30.477 2.006   6.580   1.00 12.61 ?  94  HIS   A HE2  1 
ATOM   2005 N  N    . VAL   A 1 95  ? 27.743 -3.268  1.815   1.00 9.06  ?  95  VAL   A N    1 
ATOM   2006 C  CA   . VAL   A 1 95  ? 27.595 -4.300  0.794   1.00 9.43  ?  95  VAL   A CA   1 
ATOM   2007 C  C    . VAL   A 1 95  ? 27.044 -3.666  -0.469  1.00 9.06  ?  95  VAL   A C    1 
ATOM   2008 O  O    . VAL   A 1 95  ? 26.038 -2.946  -0.415  1.00 9.99  ?  95  VAL   A O    1 
ATOM   2009 C  CB   . VAL   A 1 95  ? 26.665 -5.438  1.253   1.00 10.01 ?  95  VAL   A CB   1 
ATOM   2010 C  CG1  . VAL   A 1 95  ? 26.542 -6.474  0.153   1.00 10.68 ?  95  VAL   A CG1  1 
ATOM   2011 C  CG2  . VAL   A 1 95  ? 27.169 -6.064  2.535   1.00 10.21 ?  95  VAL   A CG2  1 
ATOM   2012 H  H    . VAL   A 1 95  ? 26.994 -2.895  2.033   1.00 10.89 ?  95  VAL   A H    1 
ATOM   2013 H  HA   . VAL   A 1 95  ? 28.459 -4.679  0.590   1.00 11.33 ?  95  VAL   A HA   1 
ATOM   2014 H  HB   . VAL   A 1 95  ? 25.782 -5.082  1.422   1.00 12.03 ?  95  VAL   A HB   1 
ATOM   2015 H  HG11 . VAL   A 1 95  ? 26.163 -7.290  0.522   1.00 12.83 ?  95  VAL   A HG11 1 
ATOM   2016 H  HG12 . VAL   A 1 95  ? 25.964 -6.135  -0.549  1.00 12.83 ?  95  VAL   A HG12 1 
ATOM   2017 H  HG13 . VAL   A 1 95  ? 27.425 -6.663  -0.210  1.00 12.83 ?  95  VAL   A HG13 1 
ATOM   2018 H  HG21 . VAL   A 1 95  ? 26.605 -6.823  2.758   1.00 12.26 ?  95  VAL   A HG21 1 
ATOM   2019 H  HG22 . VAL   A 1 95  ? 28.083 -6.361  2.404   1.00 12.26 ?  95  VAL   A HG22 1 
ATOM   2020 H  HG23 . VAL   A 1 95  ? 27.130 -5.404  3.242   1.00 12.26 ?  95  VAL   A HG23 1 
ATOM   2021 N  N    . VAL   A 1 96  ? 27.665 -3.960  -1.607  1.00 9.28  ?  96  VAL   A N    1 
ATOM   2022 C  CA   . VAL   A 1 96  ? 27.251 -3.405  -2.892  1.00 9.90  ?  96  VAL   A CA   1 
ATOM   2023 C  C    . VAL   A 1 96  ? 26.444 -4.452  -3.652  1.00 10.27 ?  96  VAL   A C    1 
ATOM   2024 O  O    . VAL   A 1 96  ? 27.004 -5.397  -4.219  1.00 11.21 ?  96  VAL   A O    1 
ATOM   2025 C  CB   . VAL   A 1 96  ? 28.444 -2.928  -3.721  1.00 10.47 ?  96  VAL   A CB   1 
ATOM   2026 C  CG1  . VAL   A 1 96  ? 27.936 -2.295  -5.001  1.00 10.72 ?  96  VAL   A CG1  1 
ATOM   2027 C  CG2  . VAL   A 1 96  ? 29.310 -1.955  -2.937  1.00 11.15 ?  96  VAL   A CG2  1 
ATOM   2028 H  H    . VAL   A 1 96  ? 28.357 -4.475  -1.663  1.00 11.15 ?  96  VAL   A H    1 
ATOM   2029 H  HA   . VAL   A 1 96  ? 26.679 -2.639  -2.736  1.00 11.89 ?  96  VAL   A HA   1 
ATOM   2030 H  HB   . VAL   A 1 96  ? 28.991 -3.686  -3.965  1.00 12.58 ?  96  VAL   A HB   1 
ATOM   2031 H  HG11 . VAL   A 1 96  ? 28.669 -1.812  -5.424  1.00 12.88 ?  96  VAL   A HG11 1 
ATOM   2032 H  HG12 . VAL   A 1 96  ? 27.614 -2.986  -5.594  1.00 12.88 ?  96  VAL   A HG12 1 
ATOM   2033 H  HG13 . VAL   A 1 96  ? 27.222 -1.675  -4.786  1.00 12.88 ?  96  VAL   A HG13 1 
ATOM   2034 H  HG21 . VAL   A 1 96  ? 30.015 -1.615  -3.513  1.00 13.39 ?  96  VAL   A HG21 1 
ATOM   2035 H  HG22 . VAL   A 1 96  ? 28.760 -1.216  -2.624  1.00 13.39 ?  96  VAL   A HG22 1 
ATOM   2036 H  HG23 . VAL   A 1 96  ? 29.700 -2.417  -2.178  1.00 13.39 ?  96  VAL   A HG23 1 
ATOM   2037 N  N    A GLY   A 1 97  ? 25.125 -4.300  -3.652  0.50 10.54 ?  97  GLY   A N    1 
ATOM   2038 N  N    B GLY   A 1 97  ? 25.125 -4.288  -3.685  0.50 10.19 ?  97  GLY   A N    1 
ATOM   2039 C  CA   A GLY   A 1 97  ? 24.290 -5.044  -4.558  0.50 11.22 ?  97  GLY   A CA   1 
ATOM   2040 C  CA   B GLY   A 1 97  ? 24.304 -5.062  -4.580  0.50 10.51 ?  97  GLY   A CA   1 
ATOM   2041 C  C    A GLY   A 1 97  ? 24.269 -4.357  -5.907  0.50 11.32 ?  97  GLY   A C    1 
ATOM   2042 C  C    B GLY   A 1 97  ? 24.332 -4.461  -5.974  0.50 10.69 ?  97  GLY   A C    1 
ATOM   2043 O  O    A GLY   A 1 97  ? 24.529 -3.154  -6.013  0.50 11.75 ?  97  GLY   A O    1 
ATOM   2044 O  O    B GLY   A 1 97  ? 24.672 -3.287  -6.158  0.50 11.38 ?  97  GLY   A O    1 
ATOM   2045 H  H    A GLY   A 1 97  ? 24.693 -3.762  -3.133  0.50 12.66 ?  97  GLY   A H    1 
ATOM   2046 H  H    B GLY   A 1 97  ? 24.687 -3.727  -3.194  0.50 12.24 ?  97  GLY   A H    1 
ATOM   2047 H  HA2  A GLY   A 1 97  ? 24.638 -5.944  -4.652  0.50 13.48 ?  97  GLY   A HA2  1 
ATOM   2048 H  HA2  B GLY   A 1 97  ? 24.643 -5.970  -4.622  0.50 12.63 ?  97  GLY   A HA2  1 
ATOM   2049 H  HA3  A GLY   A 1 97  ? 23.384 -5.086  -4.218  0.50 13.48 ?  97  GLY   A HA3  1 
ATOM   2050 H  HA3  B GLY   A 1 97  ? 23.390 -5.086  -4.250  0.50 12.63 ?  97  GLY   A HA3  1 
ATOM   2051 N  N    A PRO   A 1 98  ? 23.961 -5.100  -6.969  0.50 11.13 ?  98  PRO   A N    1 
ATOM   2052 N  N    B PRO   A 1 98  ? 23.977 -5.253  -6.985  0.50 11.35 ?  98  PRO   A N    1 
ATOM   2053 C  CA   A PRO   A 1 98  ? 23.832 -4.463  -8.284  0.50 11.51 ?  98  PRO   A CA   1 
ATOM   2054 C  CA   B PRO   A 1 98  ? 23.930 -4.718  -8.350  0.50 12.79 ?  98  PRO   A CA   1 
ATOM   2055 C  C    A PRO   A 1 98  ? 22.714 -3.428  -8.298  0.50 11.45 ?  98  PRO   A C    1 
ATOM   2056 C  C    B PRO   A 1 98  ? 22.837 -3.669  -8.496  0.50 13.17 ?  98  PRO   A C    1 
ATOM   2057 O  O    A PRO   A 1 98  ? 21.639 -3.630  -7.728  0.50 11.29 ?  98  PRO   A O    1 
ATOM   2058 O  O    B PRO   A 1 98  ? 21.755 -3.779  -7.914  0.50 14.18 ?  98  PRO   A O    1 
ATOM   2059 C  CB   A PRO   A 1 98  ? 23.526 -5.639  -9.220  0.50 11.86 ?  98  PRO   A CB   1 
ATOM   2060 C  CB   B PRO   A 1 98  ? 23.619 -5.955  -9.200  0.50 12.87 ?  98  PRO   A CB   1 
ATOM   2061 C  CG   A PRO   A 1 98  ? 22.983 -6.720  -8.327  0.50 12.51 ?  98  PRO   A CG   1 
ATOM   2062 C  CG   B PRO   A 1 98  ? 22.875 -6.865  -8.268  0.50 12.59 ?  98  PRO   A CG   1 
ATOM   2063 C  CD   A PRO   A 1 98  ? 23.739 -6.556  -7.034  0.50 11.56 ?  98  PRO   A CD   1 
ATOM   2064 C  CD   B PRO   A 1 98  ? 23.551 -6.664  -6.930  0.50 11.47 ?  98  PRO   A CD   1 
ATOM   2065 H  HA   A PRO   A 1 98  ? 24.664 -4.050  -8.538  0.50 13.83 ?  98  PRO   A HA   1 
ATOM   2066 H  HA   B PRO   A 1 98  ? 24.790 -4.350  -8.605  0.50 15.36 ?  98  PRO   A HA   1 
ATOM   2067 H  HB2  A PRO   A 1 98  ? 22.863 -5.376  -9.875  0.50 14.24 ?  98  PRO   A HB2  1 
ATOM   2068 H  HB2  B PRO   A 1 98  ? 23.063 -5.702  -9.952  0.50 15.45 ?  98  PRO   A HB2  1 
ATOM   2069 H  HB3  A PRO   A 1 98  ? 24.342 -5.934  -9.653  0.50 14.24 ?  98  PRO   A HB3  1 
ATOM   2070 H  HB3  B PRO   A 1 98  ? 24.444 -6.367  -9.498  0.50 15.45 ?  98  PRO   A HB3  1 
ATOM   2071 H  HG2  A PRO   A 1 98  ? 22.033 -6.589  -8.190  0.50 15.03 ?  98  PRO   A HG2  1 
ATOM   2072 H  HG2  B PRO   A 1 98  ? 21.944 -6.599  -8.226  0.50 15.13 ?  98  PRO   A HG2  1 
ATOM   2073 H  HG3  A PRO   A 1 98  ? 23.158 -7.591  -8.721  0.50 15.03 ?  98  PRO   A HG3  1 
ATOM   2074 H  HG3  B PRO   A 1 98  ? 22.962 -7.782  -8.567  0.50 15.13 ?  98  PRO   A HG3  1 
ATOM   2075 H  HD2  A PRO   A 1 98  ? 23.202 -6.863  -6.284  0.50 13.88 ?  98  PRO   A HD2  1 
ATOM   2076 H  HD2  B PRO   A 1 98  ? 22.920 -6.805  -6.205  0.50 13.78 ?  98  PRO   A HD2  1 
ATOM   2077 H  HD3  A PRO   A 1 98  ? 24.592 -7.023  -7.073  0.50 13.88 ?  98  PRO   A HD3  1 
ATOM   2078 H  HD3  B PRO   A 1 98  ? 24.320 -7.255  -6.846  0.50 13.78 ?  98  PRO   A HD3  1 
ATOM   2079 N  N    A ASN   A 1 99  ? 22.989 -2.304  -8.950  0.50 12.29 ?  99  ASN   A N    1 
ATOM   2080 N  N    B ASN   A 1 99  ? 23.130 -2.642  -9.285  0.50 13.71 ?  99  ASN   A N    1 
ATOM   2081 C  CA   A ASN   A 1 99  ? 22.005 -1.249  -9.162  0.50 13.03 ?  99  ASN   A CA   1 
ATOM   2082 C  CA   B ASN   A 1 99  ? 22.175 -1.584  -9.586  0.50 15.09 ?  99  ASN   A CA   1 
ATOM   2083 C  C    A ASN   A 1 99  ? 21.460 -1.399  -10.578 0.50 14.30 ?  99  ASN   A C    1 
ATOM   2084 C  C    B ASN   A 1 99  ? 21.605 -1.861  -10.972 0.50 16.13 ?  99  ASN   A C    1 
ATOM   2085 O  O    A ASN   A 1 99  ? 22.149 -1.085  -11.556 0.50 15.33 ?  99  ASN   A O    1 
ATOM   2086 O  O    B ASN   A 1 99  ? 22.313 -1.748  -11.980 0.50 16.15 ?  99  ASN   A O    1 
ATOM   2087 C  CB   A ASN   A 1 99  ? 22.644 0.124   -8.958  0.50 12.48 ?  99  ASN   A CB   1 
ATOM   2088 C  CB   B ASN   A 1 99  ? 22.864 -0.224  -9.540  0.50 16.75 ?  99  ASN   A CB   1 
ATOM   2089 C  CG   A ASN   A 1 99  ? 21.623 1.250   -8.941  0.50 12.73 ?  99  ASN   A CG   1 
ATOM   2090 C  CG   B ASN   A 1 99  ? 21.894 0.929   -9.706  0.50 18.20 ?  99  ASN   A CG   1 
ATOM   2091 O  OD1  A ASN   A 1 99  ? 20.622 1.203   -9.655  0.50 13.61 ?  99  ASN   A OD1  1 
ATOM   2092 O  OD1  B ASN   A 1 99  ? 20.896 0.817   -10.415 0.50 18.08 ?  99  ASN   A OD1  1 
ATOM   2093 N  ND2  A ASN   A 1 99  ? 21.877 2.270   -8.132  0.50 12.47 ?  99  ASN   A ND2  1 
ATOM   2094 N  ND2  B ASN   A 1 99  ? 22.182 2.046   -9.044  0.50 19.03 ?  99  ASN   A ND2  1 
ATOM   2095 H  H    A ASN   A 1 99  ? 23.761 -2.124  -9.271  0.50 14.77 ?  99  ASN   A H    1 
ATOM   2096 H  H    B ASN   A 1 99  ? 23.895 -2.534  -9.656  0.50 16.47 ?  99  ASN   A H    1 
ATOM   2097 H  HA   A ASN   A 1 99  ? 21.273 -1.352  -8.529  0.50 15.65 ?  99  ASN   A HA   1 
ATOM   2098 H  HA   B ASN   A 1 99  ? 21.450 -1.598  -8.935  0.50 18.12 ?  99  ASN   A HA   1 
ATOM   2099 H  HB2  A ASN   A 1 99  ? 23.116 0.132   -8.115  0.50 14.99 ?  99  ASN   A HB2  1 
ATOM   2100 H  HB2  B ASN   A 1 99  ? 23.316 -0.125  -8.687  0.50 20.11 ?  99  ASN   A HB2  1 
ATOM   2101 H  HB3  A ASN   A 1 99  ? 23.262 0.288   -9.690  0.50 14.99 ?  99  ASN   A HB3  1 
ATOM   2102 H  HB3  B ASN   A 1 99  ? 23.498 -0.184  -10.266 0.50 20.11 ?  99  ASN   A HB3  1 
ATOM   2103 H  HD21 A ASN   A 1 99  ? 21.327 2.930   -8.088  0.50 14.98 ?  99  ASN   A HD21 1 
ATOM   2104 H  HD21 B ASN   A 1 99  ? 21.663 2.728   -9.100  0.50 22.85 ?  99  ASN   A HD21 1 
ATOM   2105 H  HD22 A ASN   A 1 99  ? 22.587 2.267   -7.650  0.50 14.98 ?  99  ASN   A HD22 1 
ATOM   2106 H  HD22 B ASN   A 1 99  ? 22.892 2.085   -8.558  0.50 22.85 ?  99  ASN   A HD22 1 
ATOM   2107 N  N    A VAL   A 1 100 ? 20.219 -1.890  -10.680 0.50 14.84 ?  100 VAL   A N    1 
ATOM   2108 N  N    B VAL   A 1 100 ? 20.323 -2.228  -11.016 0.50 18.11 ?  100 VAL   A N    1 
ATOM   2109 C  CA   A VAL   A 1 100 ? 19.608 -2.130  -11.985 0.50 16.11 ?  100 VAL   A CA   1 
ATOM   2110 C  CA   B VAL   A 1 100 ? 19.681 -2.552  -12.286 0.50 20.70 ?  100 VAL   A CA   1 
ATOM   2111 C  C    A VAL   A 1 100 ? 19.475 -0.830  -12.770 0.50 16.78 ?  100 VAL   A C    1 
ATOM   2112 C  C    B VAL   A 1 100 ? 19.650 -1.338  -13.195 0.50 22.00 ?  100 VAL   A C    1 
ATOM   2113 O  O    A VAL   A 1 100 ? 19.555 -0.827  -14.004 0.50 17.37 ?  100 VAL   A O    1 
ATOM   2114 O  O    B VAL   A 1 100 ? 19.729 -1.468  -14.423 0.50 22.99 ?  100 VAL   A O    1 
ATOM   2115 C  CB   A VAL   A 1 100 ? 18.263 -2.874  -11.816 0.50 17.58 ?  100 VAL   A CB   1 
ATOM   2116 C  CB   B VAL   A 1 100 ? 18.266 -3.103  -12.042 0.50 22.52 ?  100 VAL   A CB   1 
ATOM   2117 C  CG1  A VAL   A 1 100 ? 17.513 -2.970  -13.140 0.50 17.71 ?  100 VAL   A CG1  1 
ATOM   2118 C  CG1  B VAL   A 1 100 ? 17.758 -3.820  -13.283 0.50 22.99 ?  100 VAL   A CG1  1 
ATOM   2119 C  CG2  A VAL   A 1 100 ? 18.504 -4.271  -11.252 0.50 18.21 ?  100 VAL   A CG2  1 
ATOM   2120 C  CG2  B VAL   A 1 100 ? 18.272 -4.020  -10.846 0.50 23.36 ?  100 VAL   A CG2  1 
ATOM   2121 H  H    A VAL   A 1 100 ? 19.711 -2.091  -10.007 0.50 17.82 ?  100 VAL   A H    1 
ATOM   2122 H  H    B VAL   A 1 100 ? 19.814 -2.293  -10.324 0.50 21.75 ?  100 VAL   A H    1 
ATOM   2123 H  HA   A VAL   A 1 100 ? 20.189 -2.718  -12.488 0.50 19.35 ?  100 VAL   A HA   1 
ATOM   2124 H  HA   B VAL   A 1 100 ? 20.194 -3.241  -12.734 0.50 24.86 ?  100 VAL   A HA   1 
ATOM   2125 H  HB   A VAL   A 1 100 ? 17.703 -2.394  -11.187 0.50 21.11 ?  100 VAL   A HB   1 
ATOM   2126 H  HB   B VAL   A 1 100 ? 17.667 -2.361  -11.856 0.50 27.03 ?  100 VAL   A HB   1 
ATOM   2127 H  HG11 A VAL   A 1 100 ? 16.792 -3.616  -13.050 0.50 21.26 ?  100 VAL   A HG11 1 
ATOM   2128 H  HG11 B VAL   A 1 100 ? 16.865 -4.154  -13.109 0.50 27.60 ?  100 VAL   A HG11 1 
ATOM   2129 H  HG12 A VAL   A 1 100 ? 17.148 -2.101  -13.361 0.50 21.26 ?  100 VAL   A HG12 1 
ATOM   2130 H  HG12 B VAL   A 1 100 ? 17.740 -3.196  -14.026 0.50 27.60 ?  100 VAL   A HG12 1 
ATOM   2131 H  HG13 A VAL   A 1 100 ? 18.129 -3.261  -13.831 0.50 21.26 ?  100 VAL   A HG13 1 
ATOM   2132 H  HG13 B VAL   A 1 100 ? 18.355 -4.558  -13.485 0.50 27.60 ?  100 VAL   A HG13 1 
ATOM   2133 H  HG21 A VAL   A 1 100 ? 17.654 -4.732  -11.166 0.50 21.87 ?  100 VAL   A HG21 1 
ATOM   2134 H  HG21 B VAL   A 1 100 ? 17.523 -4.622  -10.915 0.50 28.04 ?  100 VAL   A HG21 1 
ATOM   2135 H  HG22 A VAL   A 1 100 ? 19.085 -4.761  -11.856 0.50 21.87 ?  100 VAL   A HG22 1 
ATOM   2136 H  HG22 B VAL   A 1 100 ? 19.105 -4.517  -10.841 0.50 28.04 ?  100 VAL   A HG22 1 
ATOM   2137 H  HG23 A VAL   A 1 100 ? 18.924 -4.192  -10.381 0.50 21.87 ?  100 VAL   A HG23 1 
ATOM   2138 H  HG23 B VAL   A 1 100 ? 18.201 -3.484  -10.040 0.50 28.04 ?  100 VAL   A HG23 1 
ATOM   2139 N  N    A ASN   A 1 101 ? 19.290 0.292   -12.082 0.50 17.96 ?  101 ASN   A N    1 
ATOM   2140 N  N    B ASN   A 1 101 ? 19.514 -0.143  -12.616 0.50 22.86 ?  101 ASN   A N    1 
ATOM   2141 C  CA   A ASN   A 1 101 ? 19.220 1.574   -12.773 0.50 18.87 ?  101 ASN   A CA   1 
ATOM   2142 C  CA   B ASN   A 1 101 ? 19.511 1.085   -13.399 0.50 24.14 ?  101 ASN   A CA   1 
ATOM   2143 C  C    A ASN   A 1 101 ? 20.572 2.027   -13.326 0.50 20.64 ?  101 ASN   A C    1 
ATOM   2144 C  C    B ASN   A 1 101 ? 20.884 1.417   -13.969 0.50 25.50 ?  101 ASN   A C    1 
ATOM   2145 O  O    A ASN   A 1 101 ? 20.637 3.089   -13.958 0.50 22.41 ?  101 ASN   A O    1 
ATOM   2146 O  O    B ASN   A 1 101 ? 20.979 2.302   -14.827 0.50 25.96 ?  101 ASN   A O    1 
ATOM   2147 C  CB   A ASN   A 1 101 ? 18.604 2.624   -11.849 0.50 18.06 ?  101 ASN   A CB   1 
ATOM   2148 C  CB   B ASN   A 1 101 ? 18.974 2.238   -12.544 0.50 24.16 ?  101 ASN   A CB   1 
ATOM   2149 C  CG   A ASN   A 1 101 ? 17.223 2.219   -11.358 0.50 17.50 ?  101 ASN   A CG   1 
ATOM   2150 C  CG   B ASN   A 1 101 ? 17.674 1.882   -11.838 0.50 24.62 ?  101 ASN   A CG   1 
ATOM   2151 O  OD1  A ASN   A 1 101 ? 16.390 1.743   -12.134 0.50 17.63 ?  101 ASN   A OD1  1 
ATOM   2152 O  OD1  B ASN   A 1 101 ? 16.791 1.248   -12.417 0.50 25.40 ?  101 ASN   A OD1  1 
ATOM   2153 N  ND2  A ASN   A 1 101 ? 16.979 2.389   -10.064 0.50 16.99 ?  101 ASN   A ND2  1 
ATOM   2154 N  ND2  B ASN   A 1 101 ? 17.558 2.279   -10.575 0.50 24.61 ?  101 ASN   A ND2  1 
ATOM   2155 H  H    A ASN   A 1 101 ? 19.191 0.332   -11.231 0.50 21.56 ?  101 ASN   A H    1 
ATOM   2156 H  H    B ASN   A 1 101 ? 19.417 -0.021  -11.767 0.50 27.45 ?  101 ASN   A H    1 
ATOM   2157 H  HA   A ASN   A 1 101 ? 18.620 1.471   -13.529 0.50 22.66 ?  101 ASN   A HA   1 
ATOM   2158 H  HA   B ASN   A 1 101 ? 18.917 0.977   -14.150 0.50 28.99 ?  101 ASN   A HA   1 
ATOM   2159 H  HB2  A ASN   A 1 101 ? 19.177 2.744   -11.079 0.50 21.69 ?  101 ASN   A HB2  1 
ATOM   2160 H  HB2  B ASN   A 1 101 ? 19.625 2.470   -11.864 0.50 29.01 ?  101 ASN   A HB2  1 
ATOM   2161 H  HB3  A ASN   A 1 101 ? 18.517 3.458   -12.337 0.50 21.69 ?  101 ASN   A HB3  1 
ATOM   2162 H  HB3  B ASN   A 1 101 ? 18.799 3.005   -13.113 0.50 29.01 ?  101 ASN   A HB3  1 
ATOM   2163 H  HD21 A ASN   A 1 101 ? 16.212 2.171   -9.740  0.50 20.40 ?  101 ASN   A HD21 1 
ATOM   2164 H  HD21 B ASN   A 1 101 ? 16.842 2.100   -10.132 0.50 29.55 ?  101 ASN   A HD21 1 
ATOM   2165 H  HD22 A ASN   A 1 101 ? 17.582 2.724   -9.554  0.50 20.40 ?  101 ASN   A HD22 1 
ATOM   2166 H  HD22 B ASN   A 1 101 ? 18.196 2.717   -10.201 0.50 29.55 ?  101 ASN   A HD22 1 
ATOM   2167 N  N    A LYS   A 1 102 ? 21.637 1.248   -13.105 0.50 22.20 ?  102 LYS   A N    1 
ATOM   2168 N  N    B LYS   A 1 102 ? 21.935 0.723   -13.529 0.50 26.87 ?  102 LYS   A N    1 
ATOM   2169 C  CA   A LYS   A 1 102 ? 22.916 1.434   -13.778 0.50 23.94 ?  102 LYS   A CA   1 
ATOM   2170 C  CA   B LYS   A 1 102 ? 23.273 0.866   -14.088 0.50 27.66 ?  102 LYS   A CA   1 
ATOM   2171 C  C    A LYS   A 1 102 ? 23.211 0.336   -14.792 0.50 24.11 ?  102 LYS   A C    1 
ATOM   2172 C  C    B LYS   A 1 102 ? 23.617 -0.260  -15.057 0.50 27.29 ?  102 LYS   A C    1 
ATOM   2173 O  O    A LYS   A 1 102 ? 24.273 0.367   -15.422 0.50 24.68 ?  102 LYS   A O    1 
ATOM   2174 O  O    B LYS   A 1 102 ? 24.758 -0.337  -15.523 0.50 27.29 ?  102 LYS   A O    1 
ATOM   2175 C  CB   A LYS   A 1 102 ? 24.059 1.483   -12.757 0.50 25.74 ?  102 LYS   A CB   1 
ATOM   2176 C  CB   B LYS   A 1 102 ? 24.322 0.909   -12.969 0.50 29.10 ?  102 LYS   A CB   1 
ATOM   2177 C  CG   A LYS   A 1 102 ? 23.962 2.605   -11.743 0.50 27.06 ?  102 LYS   A CG   1 
ATOM   2178 C  CG   B LYS   A 1 102 ? 24.263 2.140   -12.073 0.50 30.11 ?  102 LYS   A CG   1 
ATOM   2179 C  CD   A LYS   A 1 102 ? 25.153 2.573   -10.795 0.50 28.29 ?  102 LYS   A CD   1 
ATOM   2180 C  CD   B LYS   A 1 102 ? 25.251 2.029   -10.912 0.50 31.19 ?  102 LYS   A CD   1 
ATOM   2181 C  CE   A LYS   A 1 102 ? 25.094 3.694   -9.771  0.50 29.18 ?  102 LYS   A CE   1 
ATOM   2182 C  CE   B LYS   A 1 102 ? 25.124 3.204   -9.953  0.50 32.08 ?  102 LYS   A CE   1 
ATOM   2183 N  NZ   A LYS   A 1 102 ? 26.234 3.623   -8.811  0.50 29.54 ?  102 LYS   A NZ   1 
ATOM   2184 N  NZ   B LYS   A 1 102 ? 25.427 2.816   -8.543  0.50 32.59 ?  102 LYS   A NZ   1 
ATOM   2185 H  H    A LYS   A 1 102 ? 21.641 0.586   -12.551 0.50 26.66 ?  102 LYS   A H    1 
ATOM   2186 H  H    B LYS   A 1 102 ? 21.891 0.137   -12.897 0.50 32.26 ?  102 LYS   A H    1 
ATOM   2187 H  HA   A LYS   A 1 102 ? 22.903 2.274   -14.253 0.50 28.74 ?  102 LYS   A HA   1 
ATOM   2188 H  HA   B LYS   A 1 102 ? 23.321 1.710   -14.565 0.50 33.20 ?  102 LYS   A HA   1 
ATOM   2189 H  HB2  A LYS   A 1 102 ? 24.074 0.646   -12.267 0.50 30.91 ?  102 LYS   A HB2  1 
ATOM   2190 H  HB2  B LYS   A 1 102 ? 24.205 0.130   -12.403 0.50 34.93 ?  102 LYS   A HB2  1 
ATOM   2191 H  HB3  A LYS   A 1 102 ? 24.895 1.594   -13.237 0.50 30.91 ?  102 LYS   A HB3  1 
ATOM   2192 H  HB3  B LYS   A 1 102 ? 25.205 0.886   -13.373 0.50 34.93 ?  102 LYS   A HB3  1 
ATOM   2193 H  HG2  A LYS   A 1 102 ? 23.959 3.458   -12.205 0.50 32.49 ?  102 LYS   A HG2  1 
ATOM   2194 H  HG2  B LYS   A 1 102 ? 24.495 2.927   -12.592 0.50 36.15 ?  102 LYS   A HG2  1 
ATOM   2195 H  HG3  A LYS   A 1 102 ? 23.150 2.499   -11.222 0.50 32.49 ?  102 LYS   A HG3  1 
ATOM   2196 H  HG3  B LYS   A 1 102 ? 23.371 2.229   -11.706 0.50 36.15 ?  102 LYS   A HG3  1 
ATOM   2197 H  HD2  A LYS   A 1 102 ? 25.158 1.727   -10.319 0.50 33.97 ?  102 LYS   A HD2  1 
ATOM   2198 H  HD2  B LYS   A 1 102 ? 25.083 1.213   -10.415 0.50 37.44 ?  102 LYS   A HD2  1 
ATOM   2199 H  HD3  A LYS   A 1 102 ? 25.971 2.672   -11.308 0.50 33.97 ?  102 LYS   A HD3  1 
ATOM   2200 H  HD3  B LYS   A 1 102 ? 26.155 2.021   -11.263 0.50 37.44 ?  102 LYS   A HD3  1 
ATOM   2201 H  HE2  A LYS   A 1 102 ? 25.136 4.548   -10.230 0.50 35.03 ?  102 LYS   A HE2  1 
ATOM   2202 H  HE2  B LYS   A 1 102 ? 25.751 3.897   -10.217 0.50 38.51 ?  102 LYS   A HE2  1 
ATOM   2203 H  HE3  A LYS   A 1 102 ? 24.268 3.624   -9.268  0.50 35.03 ?  102 LYS   A HE3  1 
ATOM   2204 H  HE3  B LYS   A 1 102 ? 24.218 3.546   -9.986  0.50 38.51 ?  102 LYS   A HE3  1 
ATOM   2205 H  HZ1  A LYS   A 1 102 ? 26.178 4.288   -8.224  0.50 35.46 ?  102 LYS   A HZ1  1 
ATOM   2206 H  HZ1  B LYS   A 1 102 ? 25.331 3.520   -8.007  0.50 39.12 ?  102 LYS   A HZ1  1 
ATOM   2207 H  HZ2  A LYS   A 1 102 ? 26.215 2.848   -8.375  0.50 35.46 ?  102 LYS   A HZ2  1 
ATOM   2208 H  HZ2  B LYS   A 1 102 ? 24.871 2.173   -8.279  0.50 39.12 ?  102 LYS   A HZ2  1 
ATOM   2209 H  HZ3  A LYS   A 1 102 ? 27.005 3.689   -9.251  0.50 35.46 ?  102 LYS   A HZ3  1 
ATOM   2210 H  HZ3  B LYS   A 1 102 ? 26.263 2.517   -8.482  0.50 39.12 ?  102 LYS   A HZ3  1 
ATOM   2211 N  N    A GLY   A 1 103 ? 22.314 -0.636  -14.956 0.50 24.66 ?  103 GLY   A N    1 
ATOM   2212 N  N    B GLY   A 1 103 ? 22.666 -1.142  -15.359 0.50 26.71 ?  103 GLY   A N    1 
ATOM   2213 C  CA   A GLY   A 1 103 ? 22.547 -1.731  -15.878 0.50 24.86 ?  103 GLY   A CA   1 
ATOM   2214 C  CA   B GLY   A 1 103 ? 22.936 -2.272  -16.227 0.50 25.81 ?  103 GLY   A CA   1 
ATOM   2215 C  C    A GLY   A 1 103 ? 23.415 -2.843  -15.339 0.50 25.06 ?  103 GLY   A C    1 
ATOM   2216 C  C    B GLY   A 1 103 ? 23.683 -3.418  -15.579 0.50 24.39 ?  103 GLY   A C    1 
ATOM   2217 O  O    A GLY   A 1 103 ? 23.991 -3.598  -16.127 0.50 26.14 ?  103 GLY   A O    1 
ATOM   2218 O  O    B GLY   A 1 103 ? 24.178 -4.299  -16.291 0.50 24.92 ?  103 GLY   A O    1 
ATOM   2219 H  H    A GLY   A 1 103 ? 21.565 -0.687  -14.542 0.50 29.60 ?  103 GLY   A H    1 
ATOM   2220 H  H    B GLY   A 1 103 ? 21.856 -1.098  -15.072 0.50 32.06 ?  103 GLY   A H    1 
ATOM   2221 H  HA2  A GLY   A 1 103 ? 21.693 -2.112  -16.143 0.50 29.84 ?  103 GLY   A HA2  1 
ATOM   2222 H  HA2  B GLY   A 1 103 ? 22.097 -2.617  -16.565 0.50 30.98 ?  103 GLY   A HA2  1 
ATOM   2223 H  HA3  A GLY   A 1 103 ? 22.979 -1.388  -16.677 0.50 29.84 ?  103 GLY   A HA3  1 
ATOM   2224 H  HA3  B GLY   A 1 103 ? 23.456 -1.949  -16.983 0.50 30.98 ?  103 GLY   A HA3  1 
ATOM   2225 N  N    A GLU   A 1 104 ? 23.530 -2.970  -14.021 0.50 23.86 ?  104 GLU   A N    1 
ATOM   2226 N  N    B GLU   A 1 104 ? 23.764 -3.449  -14.255 0.50 22.26 ?  104 GLU   A N    1 
ATOM   2227 C  CA   A GLU   A 1 104 ? 24.420 -3.959  -13.430 0.50 22.86 ?  104 GLU   A CA   1 
ATOM   2228 C  CA   B GLU   A 1 104 ? 24.624 -4.404  -13.572 0.50 20.22 ?  104 GLU   A CA   1 
ATOM   2229 C  C    A GLU   A 1 104 ? 23.746 -5.325  -13.325 0.50 23.36 ?  104 GLU   A C    1 
ATOM   2230 C  C    B GLU   A 1 104 ? 23.941 -5.764  -13.435 0.50 19.58 ?  104 GLU   A C    1 
ATOM   2231 O  O    A GLU   A 1 104 ? 22.536 -5.436  -13.105 0.50 23.69 ?  104 GLU   A O    1 
ATOM   2232 O  O    B GLU   A 1 104 ? 22.713 -5.869  -13.353 0.50 20.20 ?  104 GLU   A O    1 
ATOM   2233 C  CB   A GLU   A 1 104 ? 24.918 -3.469  -12.067 0.50 21.35 ?  104 GLU   A CB   1 
ATOM   2234 C  CB   B GLU   A 1 104 ? 25.052 -3.841  -12.215 0.50 19.60 ?  104 GLU   A CB   1 
ATOM   2235 C  CG   A GLU   A 1 104 ? 25.896 -2.303  -12.219 0.50 20.56 ?  104 GLU   A CG   1 
ATOM   2236 C  CG   B GLU   A 1 104 ? 25.870 -2.554  -12.364 0.50 20.21 ?  104 GLU   A CG   1 
ATOM   2237 C  CD   A GLU   A 1 104 ? 26.265 -1.601  -10.930 0.50 19.30 ?  104 GLU   A CD   1 
ATOM   2238 C  CD   B GLU   A 1 104 ? 26.146 -1.816  -11.066 0.50 20.45 ?  104 GLU   A CD   1 
ATOM   2239 O  OE1  A GLU   A 1 104 ? 25.627 -1.842  -9.888  0.50 17.38 ?  104 GLU   A OE1  1 
ATOM   2240 O  OE1  B GLU   A 1 104 ? 25.654 -2.232  -9.998  0.50 20.59 ?  104 GLU   A OE1  1 
ATOM   2241 O  OE2  A GLU   A 1 104 ? 27.212 -0.783  -10.973 0.50 20.22 -1 104 GLU   A OE2  1 
ATOM   2242 O  OE2  B GLU   A 1 104 ? 26.856 -0.788  -11.131 0.50 20.67 -1 104 GLU   A OE2  1 
ATOM   2243 H  H    A GLU   A 1 104 ? 23.110 -2.485  -13.450 0.50 28.65 ?  104 GLU   A H    1 
ATOM   2244 H  H    B GLU   A 1 104 ? 23.326 -2.921  -13.739 0.50 26.72 ?  104 GLU   A H    1 
ATOM   2245 H  HA   A GLU   A 1 104 ? 25.195 -4.057  -14.004 0.50 27.44 ?  104 GLU   A HA   1 
ATOM   2246 H  HA   B GLU   A 1 104 ? 25.426 -4.526  -14.107 0.50 24.28 ?  104 GLU   A HA   1 
ATOM   2247 H  HB2  A GLU   A 1 104 ? 24.161 -3.169  -11.539 0.50 25.63 ?  104 GLU   A HB2  1 
ATOM   2248 H  HB2  B GLU   A 1 104 ? 24.263 -3.643  -11.693 0.50 23.53 ?  104 GLU   A HB2  1 
ATOM   2249 H  HB3  A GLU   A 1 104 ? 25.376 -4.194  -11.615 0.50 25.63 ?  104 GLU   A HB3  1 
ATOM   2250 H  HB3  B GLU   A 1 104 ? 25.601 -4.500  -11.765 0.50 23.53 ?  104 GLU   A HB3  1 
ATOM   2251 H  HG2  A GLU   A 1 104 ? 26.719 -2.636  -12.599 0.50 24.69 ?  104 GLU   A HG2  1 
ATOM   2252 H  HG2  B GLU   A 1 104 ? 26.723 -2.773  -12.767 0.50 24.27 ?  104 GLU   A HG2  1 
ATOM   2253 H  HG3  A GLU   A 1 104 ? 25.500 -1.643  -12.807 0.50 24.69 ?  104 GLU   A HG3  1 
ATOM   2254 H  HG3  B GLU   A 1 104 ? 25.384 -1.939  -12.934 0.50 24.27 ?  104 GLU   A HG3  1 
ATOM   2255 N  N    A ASP   A 1 105 ? 24.557 -6.369  -13.483 0.50 23.88 ?  105 ASP   A N    1 
ATOM   2256 N  N    B ASP   A 1 105 ? 24.767 -6.808  -13.405 0.50 19.76 ?  105 ASP   A N    1 
ATOM   2257 C  CA   A ASP   A 1 105 ? 24.056 -7.734  -13.590 0.50 24.74 ?  105 ASP   A CA   1 
ATOM   2258 C  CA   B ASP   A 1 105 ? 24.306 -8.189  -13.513 0.50 20.15 ?  105 ASP   A CA   1 
ATOM   2259 C  C    A ASP   A 1 105 ? 23.388 -8.164  -12.289 0.50 23.39 ?  105 ASP   A C    1 
ATOM   2260 C  C    B ASP   A 1 105 ? 23.529 -8.594  -12.265 0.50 18.59 ?  105 ASP   A C    1 
ATOM   2261 O  O    A ASP   A 1 105 ? 24.009 -8.133  -11.223 0.50 22.82 ?  105 ASP   A O    1 
ATOM   2262 O  O    B ASP   A 1 105 ? 24.085 -8.622  -11.164 0.50 15.95 ?  105 ASP   A O    1 
ATOM   2263 C  CB   A ASP   A 1 105 ? 25.223 -8.665  -13.917 0.50 26.98 ?  105 ASP   A CB   1 
ATOM   2264 C  CB   B ASP   A 1 105 ? 25.529 -9.088  -13.695 0.50 22.12 ?  105 ASP   A CB   1 
ATOM   2265 C  CG   A ASP   A 1 105 ? 24.768 -10.073 -14.232 0.50 28.83 ?  105 ASP   A CG   1 
ATOM   2266 C  CG   B ASP   A 1 105 ? 25.180 -10.556 -13.830 0.50 23.58 ?  105 ASP   A CG   1 
ATOM   2267 O  OD1  A ASP   A 1 105 ? 23.541 -10.294 -14.304 0.50 29.10 ?  105 ASP   A OD1  1 
ATOM   2268 O  OD1  B ASP   A 1 105 ? 23.983 -10.889 -13.951 0.50 23.71 ?  105 ASP   A OD1  1 
ATOM   2269 O  OD2  A ASP   A 1 105 ? 25.634 -10.954 -14.420 0.50 30.16 -1 105 ASP   A OD2  1 
ATOM   2270 O  OD2  B ASP   A 1 105 ? 26.124 -11.382 -13.813 0.50 24.78 -1 105 ASP   A OD2  1 
ATOM   2271 H  H    A ASP   A 1 105 ? 25.413 -6.310  -13.527 0.50 28.67 ?  105 ASP   A H    1 
ATOM   2272 H  H    B ASP   A 1 105 ? 25.618 -6.734  -13.315 0.50 23.73 ?  105 ASP   A H    1 
ATOM   2273 H  HA   A ASP   A 1 105 ? 23.409 -7.794  -14.310 0.50 29.70 ?  105 ASP   A HA   1 
ATOM   2274 H  HA   B ASP   A 1 105 ? 23.726 -8.281  -14.282 0.50 24.19 ?  105 ASP   A HA   1 
ATOM   2275 H  HB2  A ASP   A 1 105 ? 25.689 -8.333  -14.702 0.50 32.39 ?  105 ASP   A HB2  1 
ATOM   2276 H  HB2  B ASP   A 1 105 ? 26.003 -8.809  -14.494 0.50 26.56 ?  105 ASP   A HB2  1 
ATOM   2277 H  HB3  A ASP   A 1 105 ? 25.835 -8.687  -13.160 0.50 32.39 ?  105 ASP   A HB3  1 
ATOM   2278 H  HB3  B ASP   A 1 105 ? 26.102 -9.000  -12.920 0.50 26.56 ?  105 ASP   A HB3  1 
ATOM   2279 N  N    A ILE   A 1 106 ? 22.125 -8.588  -12.384 0.50 22.41 ?  106 ILE   A N    1 
ATOM   2280 N  N    B ILE   A 1 106 ? 22.248 -8.931  -12.439 0.50 19.57 ?  106 ILE   A N    1 
ATOM   2281 C  CA   A ILE   A 1 106 ? 21.366 -8.971  -11.198 0.50 21.10 ?  106 ILE   A CA   1 
ATOM   2282 C  CA   B ILE   A 1 106 ? 21.422 -9.348  -11.308 0.50 20.26 ?  106 ILE   A CA   1 
ATOM   2283 C  C    A ILE   A 1 106 ? 21.882 -10.267 -10.582 0.50 20.14 ?  106 ILE   A C    1 
ATOM   2284 C  C    B ILE   A 1 106 ? 22.010 -10.572 -10.628 0.50 20.05 ?  106 ILE   A C    1 
ATOM   2285 O  O    A ILE   A 1 106 ? 21.623 -10.531 -9.402  0.50 19.26 ?  106 ILE   A O    1 
ATOM   2286 O  O    B ILE   A 1 106 ? 21.819 -10.770 -9.421  0.50 19.79 ?  106 ILE   A O    1 
ATOM   2287 C  CB   A ILE   A 1 106 ? 19.861 -9.046  -11.533 0.50 21.82 ?  106 ILE   A CB   1 
ATOM   2288 C  CB   B ILE   A 1 106 ? 19.967 -9.589  -11.759 0.50 21.49 ?  106 ILE   A CB   1 
ATOM   2289 C  CG1  A ILE   A 1 106 ? 19.017 -9.131  -10.258 0.50 21.86 ?  106 ILE   A CG1  1 
ATOM   2290 C  CG1  B ILE   A 1 106 ? 19.046 -9.773  -10.551 0.50 21.51 ?  106 ILE   A CG1  1 
ATOM   2291 C  CG2  A ILE   A 1 106 ? 19.571 -10.238 -12.439 0.50 22.43 ?  106 ILE   A CG2  1 
ATOM   2292 C  CG2  B ILE   A 1 106 ? 19.879 -10.823 -12.630 0.50 22.03 ?  106 ILE   A CG2  1 
ATOM   2293 C  CD1  A ILE   A 1 106 ? 19.189 -7.947  -9.328  0.50 21.79 ?  106 ILE   A CD1  1 
ATOM   2294 C  CD1  B ILE   A 1 106 ? 18.965 -8.564  -9.653  0.50 21.48 ?  106 ILE   A CD1  1 
ATOM   2295 H  H    A ILE   A 1 106 ? 21.691 -8.657  -13.121 0.50 26.91 ?  106 ILE   A H    1 
ATOM   2296 H  H    B ILE   A 1 106 ? 21.842 -8.924  -13.192 0.50 23.50 ?  106 ILE   A H    1 
ATOM   2297 H  HA   A ILE   A 1 106 ? 21.483 -8.275  -10.538 0.50 25.33 ?  106 ILE   A HA   1 
ATOM   2298 H  HA   B ILE   A 1 106 ? 21.417 -8.638  -10.654 0.50 24.33 ?  106 ILE   A HA   1 
ATOM   2299 H  HB   A ILE   A 1 106 ? 19.614 -8.238  -12.009 0.50 26.20 ?  106 ILE   A HB   1 
ATOM   2300 H  HB   B ILE   A 1 106 ? 19.665 -8.822  -12.270 0.50 25.80 ?  106 ILE   A HB   1 
ATOM   2301 H  HG12 A ILE   A 1 106 ? 18.080 -9.173  -10.507 0.50 26.24 ?  106 ILE   A HG12 1 
ATOM   2302 H  HG12 B ILE   A 1 106 ? 18.149 -9.965  -10.871 0.50 25.82 ?  106 ILE   A HG12 1 
ATOM   2303 H  HG13 A ILE   A 1 106 ? 19.263 -9.930  -9.769  0.50 26.24 ?  106 ILE   A HG13 1 
ATOM   2304 H  HG13 B ILE   A 1 106 ? 19.367 -10.519 -10.020 0.50 25.82 ?  106 ILE   A HG13 1 
ATOM   2305 H  HG21 A ILE   A 1 106 ? 18.666 -10.163 -12.778 0.50 26.93 ?  106 ILE   A HG21 1 
ATOM   2306 H  HG21 B ILE   A 1 106 ? 19.013 -10.837 -13.064 0.50 26.45 ?  106 ILE   A HG21 1 
ATOM   2307 H  HG22 A ILE   A 1 106 ? 20.201 -10.232 -13.178 0.50 26.93 ?  106 ILE   A HG22 1 
ATOM   2308 H  HG22 B ILE   A 1 106 ? 20.584 -10.789 -13.292 0.50 26.45 ?  106 ILE   A HG22 1 
ATOM   2309 H  HG23 A ILE   A 1 106 ? 19.668 -11.056 -11.929 0.50 26.93 ?  106 ILE   A HG23 1 
ATOM   2310 H  HG23 B ILE   A 1 106 ? 19.983 -11.610 -12.072 0.50 26.45 ?  106 ILE   A HG23 1 
ATOM   2311 H  HD11 A ILE   A 1 106 ? 18.457 -7.936  -8.694  0.50 26.16 ?  106 ILE   A HD11 1 
ATOM   2312 H  HD11 B ILE   A 1 106 ? 18.205 -8.666  -9.061  0.50 25.79 ?  106 ILE   A HD11 1 
ATOM   2313 H  HD12 A ILE   A 1 106 ? 20.034 -8.035  -8.857  0.50 26.16 ?  106 ILE   A HD12 1 
ATOM   2314 H  HD12 B ILE   A 1 106 ? 19.783 -8.502  -9.136  0.50 25.79 ?  106 ILE   A HD12 1 
ATOM   2315 H  HD13 A ILE   A 1 106 ? 19.186 -7.131  -9.853  0.50 26.16 ?  106 ILE   A HD13 1 
ATOM   2316 H  HD13 B ILE   A 1 106 ? 18.855 -7.774  -10.203 0.50 25.79 ?  106 ILE   A HD13 1 
ATOM   2317 N  N    A GLN   A 1 107 ? 22.622 -11.077 -11.347 0.50 21.01 ?  107 GLN   A N    1 
ATOM   2318 N  N    B GLN   A 1 107 ? 22.734 -11.410 -11.378 0.50 20.52 ?  107 GLN   A N    1 
ATOM   2319 C  CA   A GLN   A 1 107 ? 23.186 -12.313 -10.806 0.50 22.43 ?  107 GLN   A CA   1 
ATOM   2320 C  CA   B GLN   A 1 107 ? 23.399 -12.557 -10.774 0.50 22.19 ?  107 GLN   A CA   1 
ATOM   2321 C  C    A GLN   A 1 107 ? 24.152 -12.032 -9.659  0.50 20.06 ?  107 GLN   A C    1 
ATOM   2322 C  C    B GLN   A 1 107 ? 24.392 -12.137 -9.704  0.50 20.14 ?  107 GLN   A C    1 
ATOM   2323 O  O    A GLN   A 1 107 ? 24.305 -12.858 -8.751  0.50 20.13 ?  107 GLN   A O    1 
ATOM   2324 O  O    B GLN   A 1 107 ? 24.786 -12.969 -8.879  0.50 21.12 ?  107 GLN   A O    1 
ATOM   2325 C  CB   A GLN   A 1 107 ? 23.896 -13.084 -11.922 0.50 26.28 ?  107 GLN   A CB   1 
ATOM   2326 C  CB   B GLN   A 1 107 ? 24.104 -13.391 -11.849 0.50 25.46 ?  107 GLN   A CB   1 
ATOM   2327 C  CG   A GLN   A 1 107 ? 23.056 -13.273 -13.179 0.50 30.03 ?  107 GLN   A CG   1 
ATOM   2328 C  CG   B GLN   A 1 107 ? 23.149 -14.080 -12.809 0.50 28.59 ?  107 GLN   A CG   1 
ATOM   2329 C  CD   A GLN   A 1 107 ? 21.768 -14.025 -12.911 0.50 33.05 ?  107 GLN   A CD   1 
ATOM   2330 C  CD   B GLN   A 1 107 ? 22.190 -15.014 -12.099 0.50 31.44 ?  107 GLN   A CD   1 
ATOM   2331 O  OE1  A GLN   A 1 107 ? 21.773 -15.082 -12.280 0.50 34.40 ?  107 GLN   A OE1  1 
ATOM   2332 O  OE1  B GLN   A 1 107 ? 22.602 -15.861 -11.306 0.50 32.23 ?  107 GLN   A OE1  1 
ATOM   2333 N  NE2  A GLN   A 1 107 ? 20.655 -13.478 -13.383 0.50 33.96 ?  107 GLN   A NE2  1 
ATOM   2334 N  NE2  B GLN   A 1 107 ? 20.899 -14.856 -12.371 0.50 32.38 ?  107 GLN   A NE2  1 
ATOM   2335 H  H    A GLN   A 1 107 ? 22.813 -10.926 -12.172 0.50 25.22 ?  107 GLN   A H    1 
ATOM   2336 H  H    B GLN   A 1 107 ? 22.860 -11.334 -12.225 0.50 24.63 ?  107 GLN   A H    1 
ATOM   2337 H  HA   A GLN   A 1 107 ? 22.470 -12.868 -10.468 0.50 26.93 ?  107 GLN   A HA   1 
ATOM   2338 H  HA   B GLN   A 1 107 ? 22.735 -13.118 -10.351 0.50 26.64 ?  107 GLN   A HA   1 
ATOM   2339 H  HB2  A GLN   A 1 107 ? 24.701 -12.604 -12.176 0.50 31.55 ?  107 GLN   A HB2  1 
ATOM   2340 H  HB2  B GLN   A 1 107 ? 24.683 -12.813 -12.370 0.50 30.57 ?  107 GLN   A HB2  1 
ATOM   2341 H  HB3  A GLN   A 1 107 ? 24.132 -13.966 -11.594 0.50 31.55 ?  107 GLN   A HB3  1 
ATOM   2342 H  HB3  B GLN   A 1 107 ? 24.636 -14.080 -11.416 0.50 30.57 ?  107 GLN   A HB3  1 
ATOM   2343 H  HG2  A GLN   A 1 107 ? 22.825 -12.405 -13.546 0.50 36.05 ?  107 GLN   A HG2  1 
ATOM   2344 H  HG2  B GLN   A 1 107 ? 22.628 -13.407 -13.273 0.50 34.32 ?  107 GLN   A HG2  1 
ATOM   2345 H  HG3  A GLN   A 1 107 ? 23.570 -13.777 -13.828 0.50 36.05 ?  107 GLN   A HG3  1 
ATOM   2346 H  HG3  B GLN   A 1 107 ? 23.661 -14.602 -13.447 0.50 34.32 ?  107 GLN   A HG3  1 
ATOM   2347 H  HE21 A GLN   A 1 107 ? 20.689 -12.737 -13.817 0.50 40.76 ?  107 GLN   A HE21 1 
ATOM   2348 H  HE21 B GLN   A 1 107 ? 20.648 -14.252 -12.928 0.50 38.87 ?  107 GLN   A HE21 1 
ATOM   2349 H  HE22 A GLN   A 1 107 ? 19.899 -13.868 -13.255 0.50 40.76 ?  107 GLN   A HE22 1 
ATOM   2350 H  HE22 B GLN   A 1 107 ? 20.315 -15.361 -11.991 0.50 38.87 ?  107 GLN   A HE22 1 
ATOM   2351 N  N    . LEU   A 1 108 ? 24.800 -10.867 -9.682  1.00 17.36 ?  108 LEU   A N    1 
ATOM   2352 C  CA   . LEU   A 1 108 ? 25.702 -10.432 -8.627  1.00 14.97 ?  108 LEU   A CA   1 
ATOM   2353 C  C    . LEU   A 1 108 ? 24.989 -10.249 -7.298  1.00 13.28 ?  108 LEU   A C    1 
ATOM   2354 O  O    . LEU   A 1 108 ? 25.663 -10.081 -6.279  1.00 13.69 ?  108 LEU   A O    1 
ATOM   2355 C  CB   . LEU   A 1 108 ? 26.423 -9.141  -9.035  1.00 14.72 ?  108 LEU   A CB   1 
ATOM   2356 C  CG   . LEU   A 1 108 ? 27.414 -9.345  -10.180 1.00 16.60 ?  108 LEU   A CG   1 
ATOM   2357 C  CD1  . LEU   A 1 108 ? 27.886 -8.014  -10.742 1.00 17.27 ?  108 LEU   A CD1  1 
ATOM   2358 C  CD2  . LEU   A 1 108 ? 28.604 -10.170 -9.715  1.00 18.59 ?  108 LEU   A CD2  1 
ATOM   2359 H  H    A LEU   A 1 108 ? 24.732 -10.300 -10.321 0.50 20.85 ?  108 LEU   A H    1 
ATOM   2360 H  H    B LEU   A 1 108 ? 24.585 -10.266 -10.252 0.50 20.85 ?  108 LEU   A H    1 
ATOM   2361 H  HA   . LEU   A 1 108 ? 26.376 -11.114 -8.493  1.00 17.98 ?  108 LEU   A HA   1 
ATOM   2362 H  HB2  . LEU   A 1 108 ? 25.764 -8.491  -9.324  1.00 17.68 ?  108 LEU   A HB2  1 
ATOM   2363 H  HB3  . LEU   A 1 108 ? 26.914 -8.800  -8.274  1.00 17.68 ?  108 LEU   A HB3  1 
ATOM   2364 H  HG   . LEU   A 1 108 ? 26.976 -9.832  -10.897 1.00 19.94 ?  108 LEU   A HG   1 
ATOM   2365 H  HD11 . LEU   A 1 108 ? 28.483 -8.180  -11.491 1.00 20.74 ?  108 LEU   A HD11 1 
ATOM   2366 H  HD12 . LEU   A 1 108 ? 27.117 -7.505  -11.040 1.00 20.74 ?  108 LEU   A HD12 1 
ATOM   2367 H  HD13 . LEU   A 1 108 ? 28.358 -7.528  -10.048 1.00 20.74 ?  108 LEU   A HD13 1 
ATOM   2368 H  HD21 . LEU   A 1 108 ? 29.298 -10.128 -10.389 1.00 22.32 ?  108 LEU   A HD21 1 
ATOM   2369 H  HD22 . LEU   A 1 108 ? 28.930 -9.803  -8.879  1.00 22.32 ?  108 LEU   A HD22 1 
ATOM   2370 H  HD23 . LEU   A 1 108 ? 28.320 -11.088 -9.586  1.00 22.32 ?  108 LEU   A HD23 1 
ATOM   2371 N  N    . LEU   A 1 109 ? 23.652 -10.297 -7.276  1.00 12.81 ?  109 LEU   A N    1 
ATOM   2372 C  CA   . LEU   A 1 109 ? 22.946 -10.174 -6.010  1.00 12.16 ?  109 LEU   A CA   1 
ATOM   2373 C  C    . LEU   A 1 109 ? 23.288 -11.327 -5.075  1.00 11.56 ?  109 LEU   A C    1 
ATOM   2374 O  O    . LEU   A 1 109 ? 23.425 -11.133 -3.864  1.00 12.09 ?  109 LEU   A O    1 
ATOM   2375 C  CB   . LEU   A 1 109 ? 21.444 -10.093 -6.267  1.00 13.17 ?  109 LEU   A CB   1 
ATOM   2376 C  CG   . LEU   A 1 109 ? 20.547 -9.800  -5.064  1.00 13.11 ?  109 LEU   A CG   1 
ATOM   2377 C  CD1  . LEU   A 1 109 ? 20.986 -8.536  -4.343  1.00 13.60 ?  109 LEU   A CD1  1 
ATOM   2378 C  CD2  . LEU   A 1 109 ? 19.097 -9.680  -5.508  1.00 14.14 ?  109 LEU   A CD2  1 
ATOM   2379 H  H    . LEU   A 1 109 ? 23.144 -10.392 -7.964  1.00 15.39 ?  109 LEU   A H    1 
ATOM   2380 H  HA   . LEU   A 1 109 ? 23.221 -9.351  -5.578  1.00 14.60 ?  109 LEU   A HA   1 
ATOM   2381 H  HB2  . LEU   A 1 109 ? 21.287 -9.391  -6.916  1.00 15.82 ?  109 LEU   A HB2  1 
ATOM   2382 H  HB3  . LEU   A 1 109 ? 21.154 -10.941 -6.636  1.00 15.82 ?  109 LEU   A HB3  1 
ATOM   2383 H  HG   . LEU   A 1 109 ? 20.608 -10.537 -4.438  1.00 15.74 ?  109 LEU   A HG   1 
ATOM   2384 H  HD11 . LEU   A 1 109 ? 20.303 -8.278  -3.709  1.00 16.33 ?  109 LEU   A HD11 1 
ATOM   2385 H  HD12 . LEU   A 1 109 ? 21.823 -8.707  -3.881  1.00 16.33 ?  109 LEU   A HD12 1 
ATOM   2386 H  HD13 . LEU   A 1 109 ? 21.113 -7.826  -4.998  1.00 16.33 ?  109 LEU   A HD13 1 
ATOM   2387 H  HD21 . LEU   A 1 109 ? 18.556 -9.392  -4.754  1.00 16.99 ?  109 LEU   A HD21 1 
ATOM   2388 H  HD22 . LEU   A 1 109 ? 19.035 -9.030  -6.224  1.00 16.99 ?  109 LEU   A HD22 1 
ATOM   2389 H  HD23 . LEU   A 1 109 ? 18.787 -10.546 -5.822  1.00 16.99 ?  109 LEU   A HD23 1 
ATOM   2390 N  N    . LYS   A 1 110 ? 23.437 -12.539 -5.614  1.00 11.60 ?  110 LYS   A N    1 
ATOM   2391 C  CA   . LYS   A 1 110 ? 23.812 -13.657 -4.756  1.00 11.34 ?  110 LYS   A CA   1 
ATOM   2392 C  C    . LYS   A 1 110 ? 25.194 -13.438 -4.149  1.00 10.72 ?  110 LYS   A C    1 
ATOM   2393 O  O    . LYS   A 1 110 ? 25.392 -13.642 -2.951  1.00 10.98 ?  110 LYS   A O    1 
ATOM   2394 C  CB   . LYS   A 1 110 ? 23.736 -14.980 -5.521  1.00 12.34 ?  110 LYS   A CB   1 
ATOM   2395 C  CG   . LYS   A 1 110 ? 23.933 -16.196 -4.618  1.00 12.61 ?  110 LYS   A CG   1 
ATOM   2396 C  CD   . LYS   A 1 110 ? 23.718 -17.512 -5.344  1.00 13.47 ?  110 LYS   A CD   1 
ATOM   2397 C  CE   . LYS   A 1 110 ? 23.827 -18.701 -4.402  1.00 14.39 ?  110 LYS   A CE   1 
ATOM   2398 N  NZ   . LYS   A 1 110 ? 22.648 -18.839 -3.508  1.00 14.77 ?  110 LYS   A NZ   1 
ATOM   2399 H  H    . LYS   A 1 110 ? 23.331 -12.735 -6.443  1.00 13.94 ?  110 LYS   A H    1 
ATOM   2400 H  HA   . LYS   A 1 110 ? 23.174 -13.711 -4.023  1.00 13.62 ?  110 LYS   A HA   1 
ATOM   2401 H  HB2  . LYS   A 1 110 ? 22.862 -15.058 -5.937  1.00 14.82 ?  110 LYS   A HB2  1 
ATOM   2402 H  HB3  . LYS   A 1 110 ? 24.429 -14.997 -6.195  1.00 14.82 ?  110 LYS   A HB3  1 
ATOM   2403 H  HG2  . LYS   A 1 110 ? 24.835 -16.190 -4.265  1.00 15.14 ?  110 LYS   A HG2  1 
ATOM   2404 H  HG3  . LYS   A 1 110 ? 23.293 -16.153 -3.885  1.00 15.14 ?  110 LYS   A HG3  1 
ATOM   2405 H  HD2  . LYS   A 1 110 ? 22.835 -17.522 -5.737  1.00 16.18 ?  110 LYS   A HD2  1 
ATOM   2406 H  HD3  . LYS   A 1 110 ? 24.396 -17.609 -6.030  1.00 16.18 ?  110 LYS   A HD3  1 
ATOM   2407 H  HE2  . LYS   A 1 110 ? 23.906 -19.515 -4.926  1.00 17.28 ?  110 LYS   A HE2  1 
ATOM   2408 H  HE3  . LYS   A 1 110 ? 24.616 -18.593 -3.843  1.00 17.28 ?  110 LYS   A HE3  1 
ATOM   2409 H  HZ1  . LYS   A 1 110 ? 22.746 -19.543 -2.976  1.00 17.74 ?  110 LYS   A HZ1  1 
ATOM   2410 H  HZ2  . LYS   A 1 110 ? 22.557 -18.107 -3.010  1.00 17.74 ?  110 LYS   A HZ2  1 
ATOM   2411 H  HZ3  . LYS   A 1 110 ? 21.910 -18.947 -3.998  1.00 17.74 ?  110 LYS   A HZ3  1 
ATOM   2412 N  N    . SER   A 1 111 ? 26.155 -12.992 -4.963  1.00 11.08 ?  111 SER   A N    1 
ATOM   2413 C  CA   . SER   A 1 111 ? 27.491 -12.683 -4.453  1.00 11.11 ?  111 SER   A CA   1 
ATOM   2414 C  C    . SER   A 1 111 ? 27.426 -11.642 -3.341  1.00 10.65 ?  111 SER   A C    1 
ATOM   2415 O  O    . SER   A 1 111 ? 28.121 -11.751 -2.324  1.00 11.30 ?  111 SER   A O    1 
ATOM   2416 C  CB   . SER   A 1 111 ? 28.371 -12.185 -5.602  1.00 12.72 ?  111 SER   A CB   1 
ATOM   2417 O  OG   . SER   A 1 111 ? 28.464 -13.172 -6.617  1.00 14.79 ?  111 SER   A OG   1 
ATOM   2418 H  H    . SER   A 1 111 ? 26.052 -12.852 -5.804  1.00 13.31 ?  111 SER   A H    1 
ATOM   2419 H  HA   . SER   A 1 111 ? 27.889 -13.490 -4.093  1.00 13.35 ?  111 SER   A HA   1 
ATOM   2420 H  HB2  . SER   A 1 111 ? 27.969 -11.387 -5.983  1.00 15.28 ?  111 SER   A HB2  1 
ATOM   2421 H  HB3  . SER   A 1 111 ? 29.253 -11.980 -5.258  1.00 15.28 ?  111 SER   A HB3  1 
ATOM   2422 H  HG   . SER   A 1 111 ? 28.967 -12.890 -7.239  1.00 17.76 ?  111 SER   A HG   1 
ATOM   2423 N  N    . ALA   A 1 112 ? 26.582 -10.623 -3.518  1.00 10.81 ?  112 ALA   A N    1 
ATOM   2424 C  CA   . ALA   A 1 112 ? 26.427 -9.587  -2.497  1.00 10.62 ?  112 ALA   A CA   1 
ATOM   2425 C  C    . ALA   A 1 112 ? 25.949 -10.191 -1.178  1.00 10.41 ?  112 ALA   A C    1 
ATOM   2426 O  O    . ALA   A 1 112 ? 26.495 -9.901  -0.109  1.00 10.86 ?  112 ALA   A O    1 
ATOM   2427 C  CB   . ALA   A 1 112 ? 25.457 -8.504  -2.986  1.00 11.04 ?  112 ALA   A CB   1 
ATOM   2428 H  H    . ALA   A 1 112 ? 26.091 -10.507 -4.213  1.00 12.98 ?  112 ALA   A H    1 
ATOM   2429 H  HA   . ALA   A 1 112 ? 27.283 -9.163  -2.339  1.00 12.76 ?  112 ALA   A HA   1 
ATOM   2430 H  HB1  . ALA   A 1 112 ? 25.377 -7.814  -2.302  1.00 13.26 ?  112 ALA   A HB1  1 
ATOM   2431 H  HB2  . ALA   A 1 112 ? 25.799 -8.113  -3.804  1.00 13.26 ?  112 ALA   A HB2  1 
ATOM   2432 H  HB3  . ALA   A 1 112 ? 24.586 -8.902  -3.148  1.00 13.26 ?  112 ALA   A HB3  1 
ATOM   2433 N  N    . TYR   A 1 113 ? 24.911 -11.032 -1.227  1.00 10.63 ?  113 TYR   A N    1 
ATOM   2434 C  CA   . TYR   A 1 113 ? 24.405 -11.644 0.002   1.00 10.53 ?  113 TYR   A CA   1 
ATOM   2435 C  C    . TYR   A 1 113 ? 25.412 -12.598 0.644   1.00 10.07 ?  113 TYR   A C    1 
ATOM   2436 O  O    . TYR   A 1 113 ? 25.382 -12.778 1.866   1.00 10.65 ?  113 TYR   A O    1 
ATOM   2437 C  CB   . TYR   A 1 113 ? 23.084 -12.371 -0.269  1.00 10.86 ?  113 TYR   A CB   1 
ATOM   2438 C  CG   . TYR   A 1 113 ? 21.869 -11.479 -0.187  1.00 10.93 ?  113 TYR   A CG   1 
ATOM   2439 C  CD1  . TYR   A 1 113 ? 21.501 -10.889 1.016   1.00 11.06 ?  113 TYR   A CD1  1 
ATOM   2440 C  CD2  . TYR   A 1 113 ? 21.069 -11.247 -1.300  1.00 11.37 ?  113 TYR   A CD2  1 
ATOM   2441 C  CE1  . TYR   A 1 113 ? 20.380 -10.085 1.109   1.00 11.69 ?  113 TYR   A CE1  1 
ATOM   2442 C  CE2  . TYR   A 1 113 ? 19.922 -10.443 -1.213  1.00 11.83 ?  113 TYR   A CE2  1 
ATOM   2443 C  CZ   . TYR   A 1 113 ? 19.587 -9.872  -0.000  1.00 11.55 ?  113 TYR   A CZ   1 
ATOM   2444 O  OH   . TYR   A 1 113 ? 18.467 -9.073  0.121   1.00 12.54 ?  113 TYR   A OH   1 
ATOM   2445 H  H    . TYR   A 1 113 ? 24.495 -11.256 -1.944  1.00 12.77 ?  113 TYR   A H    1 
ATOM   2446 H  HA   . TYR   A 1 113 ? 24.232 -10.941 0.642   1.00 12.65 ?  113 TYR   A HA   1 
ATOM   2447 H  HB2  . TYR   A 1 113 ? 23.108 -12.741 -1.164  1.00 13.05 ?  113 TYR   A HB2  1 
ATOM   2448 H  HB3  . TYR   A 1 113 ? 22.974 -13.074 0.381   1.00 13.05 ?  113 TYR   A HB3  1 
ATOM   2449 H  HD1  . TYR   A 1 113 ? 22.027 -11.036 1.774   1.00 13.29 ?  113 TYR   A HD1  1 
ATOM   2450 H  HD2  . TYR   A 1 113 ? 21.287 -11.638 -2.112  1.00 13.66 ?  113 TYR   A HD2  1 
ATOM   2451 H  HE1  . TYR   A 1 113 ? 20.154 -9.703  1.929   1.00 14.04 ?  113 TYR   A HE1  1 
ATOM   2452 H  HE2  . TYR   A 1 113 ? 19.389 -10.290 -1.961  1.00 14.21 ?  113 TYR   A HE2  1 
ATOM   2453 H  HH   . TYR   A 1 113 ? 18.075 -9.024  -0.626  1.00 15.07 ?  113 TYR   A HH   1 
ATOM   2454 N  N    . GLU   A 1 114 ? 26.309 -13.207 -0.145  1.00 10.46 ?  114 GLU   A N    1 
ATOM   2455 C  CA   . GLU   A 1 114 ? 27.308 -14.103 0.441   1.00 10.50 ?  114 GLU   A CA   1 
ATOM   2456 C  C    . GLU   A 1 114 ? 28.162 -13.395 1.488   1.00 10.64 ?  114 GLU   A C    1 
ATOM   2457 O  O    . GLU   A 1 114 ? 28.642 -14.034 2.436   1.00 10.96 ?  114 GLU   A O    1 
ATOM   2458 C  CB   . GLU   A 1 114 ? 28.174 -14.734 -0.654  1.00 10.87 ?  114 GLU   A CB   1 
ATOM   2459 C  CG   . GLU   A 1 114 ? 27.414 -15.788 -1.431  1.00 11.12 ?  114 GLU   A CG   1 
ATOM   2460 C  CD   . GLU   A 1 114 ? 28.123 -16.321 -2.666  1.00 11.66 ?  114 GLU   A CD   1 
ATOM   2461 O  OE1  . GLU   A 1 114 ? 29.071 -15.685 -3.168  1.00 12.02 ?  114 GLU   A OE1  1 
ATOM   2462 O  OE2  . GLU   A 1 114 ? 27.685 -17.387 -3.149  1.00 13.15 -1 114 GLU   A OE2  1 
ATOM   2463 H  H    . GLU   A 1 114 ? 26.357 -13.119 -1.008  1.00 12.56 ?  114 GLU   A H    1 
ATOM   2464 H  HA   . GLU   A 1 114 ? 26.840 -14.821 0.883   1.00 12.61 ?  114 GLU   A HA   1 
ATOM   2465 H  HB2  . GLU   A 1 114 ? 28.455 -14.045 -1.282  1.00 13.06 ?  114 GLU   A HB2  1 
ATOM   2466 H  HB3  . GLU   A 1 114 ? 28.946 -15.153 -0.251  1.00 13.06 ?  114 GLU   A HB3  1 
ATOM   2467 H  HG2  . GLU   A 1 114 ? 27.248 -16.545 -0.844  1.00 13.36 ?  114 GLU   A HG2  1 
ATOM   2468 H  HG3  . GLU   A 1 114 ? 26.565 -15.415 -1.720  1.00 13.36 ?  114 GLU   A HG3  1 
ATOM   2469 N  N    . ASN   A 1 115 ? 28.344 -12.076 1.359   1.00 10.33 ?  115 ASN   A N    1 
ATOM   2470 C  CA   . ASN   A 1 115 ? 29.112 -11.345 2.363   1.00 10.60 ?  115 ASN   A CA   1 
ATOM   2471 C  C    . ASN   A 1 115 ? 28.494 -11.473 3.751   1.00 10.38 ?  115 ASN   A C    1 
ATOM   2472 O  O    . ASN   A 1 115 ? 29.205 -11.407 4.760   1.00 10.83 ?  115 ASN   A O    1 
ATOM   2473 C  CB   . ASN   A 1 115 ? 29.216 -9.868  1.986   1.00 11.11 ?  115 ASN   A CB   1 
ATOM   2474 C  CG   . ASN   A 1 115 ? 30.008 -9.648  0.718   1.00 11.81 ?  115 ASN   A CG   1 
ATOM   2475 O  OD1  . ASN   A 1 115 ? 31.227 -9.763  0.720   1.00 15.11 ?  115 ASN   A OD1  1 
ATOM   2476 N  ND2  . ASN   A 1 115 ? 29.327 -9.342  -0.364  1.00 11.33 ?  115 ASN   A ND2  1 
ATOM   2477 H  H    . ASN   A 1 115 ? 28.038 -11.587 0.716   1.00 12.41 ?  115 ASN   A H    1 
ATOM   2478 H  HA   . ASN   A 1 115 ? 30.009 -11.710 2.402   1.00 12.73 ?  115 ASN   A HA   1 
ATOM   2479 H  HB2  . ASN   A 1 115 ? 28.324 -9.512  1.862   1.00 13.35 ?  115 ASN   A HB2  1 
ATOM   2480 H  HB3  . ASN   A 1 115 ? 29.661 -9.393  2.711   1.00 13.35 ?  115 ASN   A HB3  1 
ATOM   2481 H  HD21 . ASN   A 1 115 ? 29.734 -9.204  -1.106  1.00 13.61 ?  115 ASN   A HD21 1 
ATOM   2482 H  HD22 . ASN   A 1 115 ? 28.465 -9.285  -0.331  1.00 13.61 ?  115 ASN   A HD22 1 
ATOM   2483 N  N    . PHE   A 1 116 ? 27.168 -11.645 3.829   1.00 10.40 ?  116 PHE   A N    1 
ATOM   2484 C  CA   . PHE   A 1 116 ? 26.523 -11.742 5.136   1.00 10.48 ?  116 PHE   A CA   1 
ATOM   2485 C  C    . PHE   A 1 116 ? 26.997 -12.976 5.906   1.00 10.78 ?  116 PHE   A C    1 
ATOM   2486 O  O    . PHE   A 1 116 ? 26.930 -12.994 7.135   1.00 11.42 ?  116 PHE   A O    1 
ATOM   2487 C  CB   . PHE   A 1 116 ? 24.997 -11.871 5.007   1.00 10.78 ?  116 PHE   A CB   1 
ATOM   2488 C  CG   . PHE   A 1 116 ? 24.243 -10.628 4.540   1.00 10.62 ?  116 PHE   A CG   1 
ATOM   2489 C  CD1  . PHE   A 1 116 ? 24.810 -9.604  3.786   1.00 10.97 ?  116 PHE   A CD1  1 
ATOM   2490 C  CD2  . PHE   A 1 116 ? 22.892 -10.527 4.865   1.00 11.39 ?  116 PHE   A CD2  1 
ATOM   2491 C  CE1  . PHE   A 1 116 ? 24.035 -8.532  3.363   1.00 11.27 ?  116 PHE   A CE1  1 
ATOM   2492 C  CE2  . PHE   A 1 116 ? 22.123 -9.454  4.451   1.00 11.52 ?  116 PHE   A CE2  1 
ATOM   2493 C  CZ   . PHE   A 1 116 ? 22.692 -8.453  3.702   1.00 10.89 ?  116 PHE   A CZ   1 
ATOM   2494 H  H    . PHE   A 1 116 ? 26.635 -11.706 3.152   1.00 12.49 ?  116 PHE   A H    1 
ATOM   2495 H  HA   . PHE   A 1 116 ? 26.724 -10.951 5.656   1.00 12.59 ?  116 PHE   A HA   1 
ATOM   2496 H  HB2  . PHE   A 1 116 ? 24.806 -12.580 4.370   1.00 12.95 ?  116 PHE   A HB2  1 
ATOM   2497 H  HB3  . PHE   A 1 116 ? 24.643 -12.121 5.875   1.00 12.95 ?  116 PHE   A HB3  1 
ATOM   2498 H  HD1  . PHE   A 1 116 ? 25.701 -9.663  3.546   1.00 13.18 ?  116 PHE   A HD1  1 
ATOM   2499 H  HD2  . PHE   A 1 116 ? 22.492 -11.210 5.365   1.00 13.68 ?  116 PHE   A HD2  1 
ATOM   2500 H  HE1  . PHE   A 1 116 ? 24.425 -7.857  2.864   1.00 13.54 ?  116 PHE   A HE1  1 
ATOM   2501 H  HE2  . PHE   A 1 116 ? 21.224 -9.414  4.688   1.00 13.84 ?  116 PHE   A HE2  1 
ATOM   2502 H  HZ   . PHE   A 1 116 ? 22.181 -7.727  3.434   1.00 13.08 ?  116 PHE   A HZ   1 
ATOM   2503 N  N    . ASN   A 1 117 ? 27.443 -14.025 5.205   1.00 10.94 ?  117 ASN   A N    1 
ATOM   2504 C  CA   . ASN   A 1 117 ? 27.811 -15.271 5.875   1.00 10.92 ?  117 ASN   A CA   1 
ATOM   2505 C  C    . ASN   A 1 117 ? 29.073 -15.151 6.709   1.00 11.35 ?  117 ASN   A C    1 
ATOM   2506 O  O    . ASN   A 1 117 ? 29.371 -16.066 7.483   1.00 12.59 ?  117 ASN   A O    1 
ATOM   2507 C  CB   . ASN   A 1 117 ? 27.927 -16.398 4.852   1.00 11.29 ?  117 ASN   A CB   1 
ATOM   2508 C  CG   . ASN   A 1 117 ? 26.575 -16.786 4.315   1.00 11.21 ?  117 ASN   A CG   1 
ATOM   2509 O  OD1  . ASN   A 1 117 ? 25.603 -16.810 5.066   1.00 12.19 ?  117 ASN   A OD1  1 
ATOM   2510 N  ND2  . ASN   A 1 117 ? 26.490 -17.038 3.023   1.00 11.33 ?  117 ASN   A ND2  1 
ATOM   2511 H  H    . ASN   A 1 117 ? 27.527 -14.040 4.346   1.00 13.14 ?  117 ASN   A H    1 
ATOM   2512 H  HA   . ASN   A 1 117 ? 27.088 -15.503 6.478   1.00 13.12 ?  117 ASN   A HA   1 
ATOM   2513 H  HB2  . ASN   A 1 117 ? 28.481 -16.103 4.111   1.00 13.56 ?  117 ASN   A HB2  1 
ATOM   2514 H  HB3  . ASN   A 1 117 ? 28.315 -17.173 5.279   1.00 13.56 ?  117 ASN   A HB3  1 
ATOM   2515 H  HD21 . ASN   A 1 117 ? 25.736 -17.253 2.678   1.00 13.60 ?  117 ASN   A HD21 1 
ATOM   2516 H  HD22 . ASN   A 1 117 ? 27.195 -16.994 2.529   1.00 13.60 ?  117 ASN   A HD22 1 
ATOM   2517 N  N    . GLN   A 1 118 ? 29.802 -14.044 6.585   1.00 11.50 ?  118 GLN   A N    1 
ATOM   2518 C  CA   . GLN   A 1 118 ? 30.981 -13.806 7.407   1.00 12.19 ?  118 GLN   A CA   1 
ATOM   2519 C  C    . GLN   A 1 118 ? 30.642 -13.230 8.777   1.00 11.91 ?  118 GLN   A C    1 
ATOM   2520 O  O    . GLN   A 1 118 ? 31.560 -12.945 9.556   1.00 13.53 ?  118 GLN   A O    1 
ATOM   2521 C  CB   . GLN   A 1 118 ? 31.969 -12.894 6.670   1.00 12.34 ?  118 GLN   A CB   1 
ATOM   2522 C  CG   . GLN   A 1 118 ? 32.445 -13.478 5.350   1.00 12.62 ?  118 GLN   A CG   1 
ATOM   2523 C  CD   . GLN   A 1 118 ? 33.270 -14.743 5.528   1.00 12.69 ?  118 GLN   A CD   1 
ATOM   2524 O  OE1  . GLN   A 1 118 ? 34.138 -14.817 6.409   1.00 13.39 ?  118 GLN   A OE1  1 
ATOM   2525 N  NE2  . GLN   A 1 118 ? 33.015 -15.742 4.681   1.00 13.09 ?  118 GLN   A NE2  1 
ATOM   2526 H  H    . GLN   A 1 118 ? 29.629 -13.400 6.030   1.00 13.81 ?  118 GLN   A H    1 
ATOM   2527 H  HA   . GLN   A 1 118 ? 31.418 -14.660 7.551   1.00 14.65 ?  118 GLN   A HA   1 
ATOM   2528 H  HB2  . GLN   A 1 118 ? 31.539 -12.048 6.489   1.00 14.83 ?  118 GLN   A HB2  1 
ATOM   2529 H  HB3  . GLN   A 1 118 ? 32.747 -12.761 7.235   1.00 14.83 ?  118 GLN   A HB3  1 
ATOM   2530 H  HG2  . GLN   A 1 118 ? 31.676 -13.693 4.796   1.00 15.16 ?  118 GLN   A HG2  1 
ATOM   2531 H  HG3  . GLN   A 1 118 ? 33.002 -12.823 4.894   1.00 15.16 ?  118 GLN   A HG3  1 
ATOM   2532 H  HE21 . GLN   A 1 118 ? 32.397 -15.651 4.079   1.00 15.72 ?  118 GLN   A HE21 1 
ATOM   2533 H  HE22 . GLN   A 1 118 ? 33.447 -16.478 4.735   1.00 15.72 ?  118 GLN   A HE22 1 
ATOM   2534 N  N    . HIS   A 1 119 ? 29.353 -13.073 9.091   1.00 11.76 ?  119 HIS   A N    1 
ATOM   2535 C  CA   . HIS   A 1 119 ? 28.900 -12.467 10.338  1.00 12.19 ?  119 HIS   A CA   1 
ATOM   2536 C  C    . HIS   A 1 119 ? 27.762 -13.295 10.910  1.00 12.61 ?  119 HIS   A C    1 
ATOM   2537 O  O    . HIS   A 1 119 ? 26.811 -13.620 10.195  1.00 13.05 ?  119 HIS   A O    1 
ATOM   2538 C  CB   . HIS   A 1 119 ? 28.439 -11.034 10.064  1.00 12.49 ?  119 HIS   A CB   1 
ATOM   2539 C  CG   . HIS   A 1 119 ? 29.519 -10.218 9.457   1.00 14.16 ?  119 HIS   A CG   1 
ATOM   2540 N  ND1  . HIS   A 1 119 ? 30.492 -9.614  10.218  1.00 16.49 ?  119 HIS   A ND1  1 
ATOM   2541 C  CD2  . HIS   A 1 119 ? 29.863 -10.017 8.165   1.00 15.12 ?  119 HIS   A CD2  1 
ATOM   2542 C  CE1  . HIS   A 1 119 ? 31.363 -9.026  9.419   1.00 16.80 ?  119 HIS   A CE1  1 
ATOM   2543 N  NE2  . HIS   A 1 119 ? 31.017 -9.272  8.168   1.00 16.46 ?  119 HIS   A NE2  1 
ATOM   2544 H  H    . HIS   A 1 119 ? 28.701 -13.325 8.583   1.00 14.12 ?  119 HIS   A H    1 
ATOM   2545 H  HA   . HIS   A 1 119 ? 29.629 -12.451 10.978  1.00 14.64 ?  119 HIS   A HA   1 
ATOM   2546 H  HB2  . HIS   A 1 119 ? 27.689 -11.058 9.451   1.00 15.01 ?  119 HIS   A HB2  1 
ATOM   2547 H  HB3  . HIS   A 1 119 ? 28.178 -10.624 10.902  1.00 15.01 ?  119 HIS   A HB3  1 
ATOM   2548 H  HD1  . HIS   A 1 119 ? 30.515 -9.602  11.078  1.00 19.80 ?  119 HIS   A HD1  1 
ATOM   2549 H  HD2  . HIS   A 1 119 ? 29.412 -10.333 7.415   1.00 18.16 ?  119 HIS   A HD2  1 
ATOM   2550 H  HE1  . HIS   A 1 119 ? 32.097 -8.523  9.692   1.00 20.18 ?  119 HIS   A HE1  1 
ATOM   2551 N  N    A GLU   A 1 120 ? 27.853 -13.617 12.203  0.50 13.25 ?  120 GLU   A N    1 
ATOM   2552 N  N    B GLU   A 1 120 ? 27.858 -13.626 12.201  0.50 13.47 ?  120 GLU   A N    1 
ATOM   2553 C  CA   A GLU   A 1 120 ? 26.898 -14.546 12.805  0.50 14.53 ?  120 GLU   A CA   1 
ATOM   2554 C  CA   B GLU   A 1 120 ? 26.899 -14.550 12.804  0.50 15.01 ?  120 GLU   A CA   1 
ATOM   2555 C  C    A GLU   A 1 120 ? 25.486 -13.974 12.874  0.50 13.65 ?  120 GLU   A C    1 
ATOM   2556 C  C    B GLU   A 1 120 ? 25.487 -13.973 12.867  0.50 13.99 ?  120 GLU   A C    1 
ATOM   2557 O  O    A GLU   A 1 120 ? 24.510 -14.732 12.779  0.50 13.88 ?  120 GLU   A O    1 
ATOM   2558 O  O    B GLU   A 1 120 ? 24.511 -14.727 12.752  0.50 14.42 ?  120 GLU   A O    1 
ATOM   2559 C  CB   A GLU   A 1 120 ? 27.367 -14.956 14.203  0.50 17.48 ?  120 GLU   A CB   1 
ATOM   2560 C  CB   B GLU   A 1 120 ? 27.367 -14.959 14.203  0.50 18.19 ?  120 GLU   A CB   1 
ATOM   2561 C  CG   A GLU   A 1 120 ? 28.522 -15.943 14.204  0.50 21.75 ?  120 GLU   A CG   1 
ATOM   2562 C  CG   B GLU   A 1 120 ? 28.592 -15.860 14.214  0.50 22.46 ?  120 GLU   A CG   1 
ATOM   2563 C  CD   A GLU   A 1 120 ? 28.640 -16.705 15.509  0.50 25.84 ?  120 GLU   A CD   1 
ATOM   2564 C  CD   B GLU   A 1 120 ? 28.885 -16.430 15.586  0.50 26.38 ?  120 GLU   A CD   1 
ATOM   2565 O  OE1  A GLU   A 1 120 ? 28.400 -16.104 16.578  0.50 27.51 ?  120 GLU   A OE1  1 
ATOM   2566 O  OE1  B GLU   A 1 120 ? 28.207 -16.020 16.556  0.50 28.03 ?  120 GLU   A OE1  1 
ATOM   2567 O  OE2  A GLU   A 1 120 ? 28.957 -17.912 15.462  0.50 26.98 -1 120 GLU   A OE2  1 
ATOM   2568 O  OE2  B GLU   A 1 120 ? 29.793 -17.281 15.695  0.50 27.45 -1 120 GLU   A OE2  1 
ATOM   2569 H  H    A GLU   A 1 120 ? 28.453 -13.318 12.744  0.50 15.91 ?  120 GLU   A H    1 
ATOM   2570 H  H    B GLU   A 1 120 ? 28.467 -13.339 12.740  0.50 16.18 ?  120 GLU   A H    1 
ATOM   2571 H  HA   A GLU   A 1 120 ? 26.867 -15.350 12.266  0.50 17.45 ?  120 GLU   A HA   1 
ATOM   2572 H  HA   B GLU   A 1 120 ? 26.865 -15.354 12.267  0.50 18.02 ?  120 GLU   A HA   1 
ATOM   2573 H  HB2  A GLU   A 1 120 ? 27.657 -14.165 14.685  0.50 20.99 ?  120 GLU   A HB2  1 
ATOM   2574 H  HB2  B GLU   A 1 120 ? 27.589 -14.163 14.710  0.50 21.84 ?  120 GLU   A HB2  1 
ATOM   2575 H  HB3  A GLU   A 1 120 ? 26.627 -15.371 14.675  0.50 20.99 ?  120 GLU   A HB3  1 
ATOM   2576 H  HB3  B GLU   A 1 120 ? 26.647 -15.438 14.648  0.50 21.84 ?  120 GLU   A HB3  1 
ATOM   2577 H  HG2  A GLU   A 1 120 ? 28.385 -16.593 13.501  0.50 26.12 ?  120 GLU   A HG2  1 
ATOM   2578 H  HG2  B GLU   A 1 120 ? 28.457 -16.587 13.583  0.50 26.96 ?  120 GLU   A HG2  1 
ATOM   2579 H  HG3  A GLU   A 1 120 ? 29.351 -15.461 14.060  0.50 26.12 ?  120 GLU   A HG3  1 
ATOM   2580 H  HG3  B GLU   A 1 120 ? 29.371 -15.346 13.972  0.50 26.96 ?  120 GLU   A HG3  1 
ATOM   2581 N  N    . VAL   A 1 121 ? 25.355 -12.664 13.081  1.00 13.42 ?  121 VAL   A N    1 
ATOM   2582 C  CA   . VAL   A 1 121 ? 24.059 -11.999 13.207  1.00 13.50 ?  121 VAL   A CA   1 
ATOM   2583 C  C    . VAL   A 1 121 ? 24.168 -10.618 12.571  1.00 12.43 ?  121 VAL   A C    1 
ATOM   2584 O  O    . VAL   A 1 121 ? 25.141 -9.893  12.809  1.00 13.30 ?  121 VAL   A O    1 
ATOM   2585 C  CB   . VAL   A 1 121 ? 23.625 -11.845 14.685  1.00 16.55 ?  121 VAL   A CB   1 
ATOM   2586 C  CG1  . VAL   A 1 121 ? 22.249 -11.198 14.776  1.00 17.17 ?  121 VAL   A CG1  1 
ATOM   2587 C  CG2  . VAL   A 1 121 ? 23.613 -13.171 15.428  1.00 19.17 ?  121 VAL   A CG2  1 
ATOM   2588 H  H    A VAL   A 1 121 ? 26.023 -12.127 13.160  0.50 16.11 ?  121 VAL   A H    1 
ATOM   2589 H  H    B VAL   A 1 121 ? 26.023 -12.126 13.156  0.50 16.11 ?  121 VAL   A H    1 
ATOM   2590 H  HA   . VAL   A 1 121 ? 23.384 -12.511 12.735  1.00 16.22 ?  121 VAL   A HA   1 
ATOM   2591 H  HB   . VAL   A 1 121 ? 24.250 -11.261 15.135  1.00 19.87 ?  121 VAL   A HB   1 
ATOM   2592 H  HG11 . VAL   A 1 121 ? 21.929 -11.261 15.690  1.00 20.62 ?  121 VAL   A HG11 1 
ATOM   2593 H  HG12 . VAL   A 1 121 ? 22.317 -10.265 14.516  1.00 20.62 ?  121 VAL   A HG12 1 
ATOM   2594 H  HG13 . VAL   A 1 121 ? 21.638 -11.663 14.182  1.00 20.62 ?  121 VAL   A HG13 1 
ATOM   2595 H  HG21 . VAL   A 1 121 ? 23.282 -13.023 16.335  1.00 23.02 ?  121 VAL   A HG21 1 
ATOM   2596 H  HG22 . VAL   A 1 121 ? 23.022 -13.790 14.968  1.00 23.02 ?  121 VAL   A HG22 1 
ATOM   2597 H  HG23 . VAL   A 1 121 ? 24.509 -13.527 15.462  1.00 23.02 ?  121 VAL   A HG23 1 
ATOM   2598 N  N    . LEU   A 1 122 ? 23.159 -10.230 11.782  1.00 11.89 ?  122 LEU   A N    1 
ATOM   2599 C  CA   . LEU   A 1 122 ? 23.159 -8.929  11.115  1.00 11.63 ?  122 LEU   A CA   1 
ATOM   2600 C  C    . LEU   A 1 122 ? 21.760 -8.340  11.086  1.00 11.64 ?  122 LEU   A C    1 
ATOM   2601 O  O    . LEU   A 1 122 ? 20.770 -9.060  10.948  1.00 12.55 ?  122 LEU   A O    1 
ATOM   2602 C  CB   . LEU   A 1 122 ? 23.578 -9.017  9.644   1.00 13.35 ?  122 LEU   A CB   1 
ATOM   2603 C  CG   . LEU   A 1 122 ? 24.785 -9.869  9.279   1.00 13.44 ?  122 LEU   A CG   1 
ATOM   2604 C  CD1  . LEU   A 1 122 ? 24.391 -11.320 9.056   1.00 14.16 ?  122 LEU   A CD1  1 
ATOM   2605 C  CD2  . LEU   A 1 122 ? 25.452 -9.298  8.043   1.00 12.65 ?  122 LEU   A CD2  1 
ATOM   2606 H  H    . LEU   A 1 122 ? 22.457 -10.702 11.618  1.00 14.28 ?  122 LEU   A H    1 
ATOM   2607 H  HA   . LEU   A 1 122 ? 23.756 -8.315  11.578  1.00 13.97 ?  122 LEU   A HA   1 
ATOM   2608 H  HB2  . LEU   A 1 122 ? 22.836 -9.371  9.143   1.00 16.03 ?  122 LEU   A HB2  1 
ATOM   2609 H  HB3  . LEU   A 1 122 ? 23.778 -8.121  9.336   1.00 16.03 ?  122 LEU   A HB3  1 
ATOM   2610 H  HG   . LEU   A 1 122 ? 25.439 -9.845  9.998   1.00 16.14 ?  122 LEU   A HG   1 
ATOM   2611 H  HD11 . LEU   A 1 122 ? 25.169 -11.826 8.768   1.00 17.01 ?  122 LEU   A HD11 1 
ATOM   2612 H  HD12 . LEU   A 1 122 ? 24.051 -11.686 9.887   1.00 17.01 ?  122 LEU   A HD12 1 
ATOM   2613 H  HD13 . LEU   A 1 122 ? 23.704 -11.359 8.372   1.00 17.01 ?  122 LEU   A HD13 1 
ATOM   2614 H  HD21 . LEU   A 1 122 ? 26.193 -9.871  7.778   1.00 15.19 ?  122 LEU   A HD21 1 
ATOM   2615 H  HD22 . LEU   A 1 122 ? 24.803 -9.249  7.324   1.00 15.19 ?  122 LEU   A HD22 1 
ATOM   2616 H  HD23 . LEU   A 1 122 ? 25.788 -8.407  8.244   1.00 15.19 ?  122 LEU   A HD23 1 
ATOM   2617 N  N    . LEU   A 1 123 ? 21.699 -7.013  11.184  1.00 11.30 ?  123 LEU   A N    1 
ATOM   2618 C  CA   . LEU   A 1 123 ? 20.529 -6.216  10.817  1.00 11.30 ?  123 LEU   A CA   1 
ATOM   2619 C  C    . LEU   A 1 123 ? 20.769 -5.689  9.410   1.00 10.49 ?  123 LEU   A C    1 
ATOM   2620 O  O    . LEU   A 1 123 ? 21.820 -5.097  9.157   1.00 11.36 ?  123 LEU   A O    1 
ATOM   2621 C  CB   . LEU   A 1 123 ? 20.403 -5.033  11.779  1.00 11.35 ?  123 LEU   A CB   1 
ATOM   2622 C  CG   . LEU   A 1 123 ? 19.356 -3.969  11.435  1.00 12.24 ?  123 LEU   A CG   1 
ATOM   2623 C  CD1  . LEU   A 1 123 ? 17.953 -4.560  11.440  1.00 13.22 ?  123 LEU   A CD1  1 
ATOM   2624 C  CD2  . LEU   A 1 123 ? 19.458 -2.798  12.408  1.00 13.68 ?  123 LEU   A CD2  1 
ATOM   2625 H  H    . LEU   A 1 123 ? 22.354 -6.528  11.469  1.00 13.58 ?  123 LEU   A H    1 
ATOM   2626 H  HA   . LEU   A 1 123 ? 19.722 -6.755  10.842  1.00 13.57 ?  123 LEU   A HA   1 
ATOM   2627 H  HB2  . LEU   A 1 123 ? 20.171 -5.375  12.656  1.00 13.63 ?  123 LEU   A HB2  1 
ATOM   2628 H  HB3  . LEU   A 1 123 ? 21.255 -4.582  11.823  1.00 13.63 ?  123 LEU   A HB3  1 
ATOM   2629 H  HG   . LEU   A 1 123 ? 19.525 -3.618  10.542  1.00 14.70 ?  123 LEU   A HG   1 
ATOM   2630 H  HD11 . LEU   A 1 123 ? 17.304 -3.849  11.345  1.00 15.88 ?  123 LEU   A HD11 1 
ATOM   2631 H  HD12 . LEU   A 1 123 ? 17.872 -5.184  10.700  1.00 15.88 ?  123 LEU   A HD12 1 
ATOM   2632 H  HD13 . LEU   A 1 123 ? 17.813 -5.027  12.280  1.00 15.88 ?  123 LEU   A HD13 1 
ATOM   2633 H  HD21 . LEU   A 1 123 ? 18.790 -2.135  12.179  1.00 16.43 ?  123 LEU   A HD21 1 
ATOM   2634 H  HD22 . LEU   A 1 123 ? 19.299 -3.131  13.308  1.00 16.43 ?  123 LEU   A HD22 1 
ATOM   2635 H  HD23 . LEU   A 1 123 ? 20.344 -2.417  12.347  1.00 16.43 ?  123 LEU   A HD23 1 
ATOM   2636 N  N    A ALA   A 1 124 ? 19.803 -5.855  8.512   0.50 10.09 ?  124 ALA   A N    1 
ATOM   2637 N  N    B ALA   A 1 124 ? 19.822 -5.912  8.498   0.50 10.75 ?  124 ALA   A N    1 
ATOM   2638 C  CA   A ALA   A 1 124 ? 20.070 -5.540  7.117   0.50 9.70  ?  124 ALA   A CA   1 
ATOM   2639 C  CA   B ALA   A 1 124 ? 20.108 -5.686  7.089   0.50 11.13 ?  124 ALA   A CA   1 
ATOM   2640 C  C    A ALA   A 1 124 ? 18.808 -5.058  6.421   0.50 9.84  ?  124 ALA   A C    1 
ATOM   2641 C  C    B ALA   A 1 124 ? 18.886 -5.201  6.322   0.50 10.69 ?  124 ALA   A C    1 
ATOM   2642 O  O    A ALA   A 1 124 ? 17.686 -5.376  6.845   0.50 10.21 ?  124 ALA   A O    1 
ATOM   2643 O  O    B ALA   A 1 124 ? 17.747 -5.552  6.664   0.50 10.91 ?  124 ALA   A O    1 
ATOM   2644 C  CB   A ALA   A 1 124 ? 20.626 -6.754  6.367   0.50 9.67  ?  124 ALA   A CB   1 
ATOM   2645 C  CB   B ALA   A 1 124 ? 20.657 -6.957  6.424   0.50 11.83 ?  124 ALA   A CB   1 
ATOM   2646 H  H    A ALA   A 1 124 ? 19.006 -6.142  8.680   0.50 12.12 ?  124 ALA   A H    1 
ATOM   2647 H  H    B ALA   A 1 124 ? 19.025 -6.195  8.667   0.50 12.91 ?  124 ALA   A H    1 
ATOM   2648 H  HA   A ALA   A 1 124 ? 20.735 -4.834  7.087   0.50 11.66 ?  124 ALA   A HA   1 
ATOM   2649 H  HA   B ALA   A 1 124 ? 20.792 -5.007  7.029   0.50 13.36 ?  124 ALA   A HA   1 
ATOM   2650 H  HB1  A ALA   A 1 124 ? 20.794 -6.502  5.446   0.50 11.62 ?  124 ALA   A HB1  1 
ATOM   2651 H  HB1  B ALA   A 1 124 ? 20.841 -6.775  5.488   0.50 14.21 ?  124 ALA   A HB1  1 
ATOM   2652 H  HB2  A ALA   A 1 124 ? 21.454 -7.031  6.790   0.50 11.62 ?  124 ALA   A HB2  1 
ATOM   2653 H  HB2  B ALA   A 1 124 ? 21.480 -7.220  6.872   0.50 14.21 ?  124 ALA   A HB2  1 
ATOM   2654 H  HB3  A ALA   A 1 124 ? 19.977 -7.470  6.404   0.50 11.62 ?  124 ALA   A HB3  1 
ATOM   2655 H  HB3  B ALA   A 1 124 ? 20.002 -7.667  6.500   0.50 14.21 ?  124 ALA   A HB3  1 
ATOM   2656 N  N    A PRO   A 1 125 ? 18.962 -4.297  5.339   0.50 10.29 ?  125 PRO   A N    1 
ATOM   2657 N  N    B PRO   A 1 125 ? 19.098 -4.427  5.262   0.50 10.01 ?  125 PRO   A N    1 
ATOM   2658 C  CA   A PRO   A 1 125 ? 17.883 -4.090  4.375   0.50 10.69 ?  125 PRO   A CA   1 
ATOM   2659 C  CA   B PRO   A 1 125 ? 18.022 -4.081  4.338   0.50 10.61 ?  125 PRO   A CA   1 
ATOM   2660 C  C    A PRO   A 1 125 ? 17.953 -5.157  3.284   0.50 9.83  ?  125 PRO   A C    1 
ATOM   2661 C  C    B PRO   A 1 125 ? 17.960 -5.132  3.234   0.50 11.48 ?  125 PRO   A C    1 
ATOM   2662 O  O    A PRO   A 1 125 ? 18.915 -5.922  3.188   0.50 10.82 ?  125 PRO   A O    1 
ATOM   2663 O  O    B PRO   A 1 125 ? 18.837 -5.990  3.105   0.50 12.03 ?  125 PRO   A O    1 
ATOM   2664 C  CB   A PRO   A 1 125 ? 18.248 -2.721  3.784   0.50 11.22 ?  125 PRO   A CB   1 
ATOM   2665 C  CB   B PRO   A 1 125 ? 18.532 -2.761  3.755   0.50 10.07 ?  125 PRO   A CB   1 
ATOM   2666 C  CG   A PRO   A 1 125 ? 19.754 -2.767  3.737   0.50 11.57 ?  125 PRO   A CG   1 
ATOM   2667 C  CG   B PRO   A 1 125 ? 20.015 -3.022  3.599   0.50 9.23  ?  125 PRO   A CG   1 
ATOM   2668 C  CD   A PRO   A 1 125 ? 20.168 -3.522  4.982   0.50 10.98 ?  125 PRO   A CD   1 
ATOM   2669 C  CD   B PRO   A 1 125 ? 20.394 -3.904  4.786   0.50 8.88  ?  125 PRO   A CD   1 
ATOM   2670 H  HA   A PRO   A 1 125 ? 17.010 -4.074  4.795   0.50 12.84 ?  125 PRO   A HA   1 
ATOM   2671 H  HA   B PRO   A 1 125 ? 17.164 -3.970  4.790   0.50 12.75 ?  125 PRO   A HA   1 
ATOM   2672 H  HB2  A PRO   A 1 125 ? 17.870 -2.627  2.894   0.50 13.48 ?  125 PRO   A HB2  1 
ATOM   2673 H  HB2  B PRO   A 1 125 ? 18.111 -2.596  2.897   0.50 12.10 ?  125 PRO   A HB2  1 
ATOM   2674 H  HB3  A PRO   A 1 125 ? 17.937 -2.012  4.371   0.50 13.48 ?  125 PRO   A HB3  1 
ATOM   2675 H  HB3  B PRO   A 1 125 ? 18.362 -2.034  4.376   0.50 12.10 ?  125 PRO   A HB3  1 
ATOM   2676 H  HG2  A PRO   A 1 125 ? 20.042 -3.239  2.939   0.50 13.90 ?  125 PRO   A HG2  1 
ATOM   2677 H  HG2  B PRO   A 1 125 ? 20.176 -3.484  2.759   0.50 11.09 ?  125 PRO   A HG2  1 
ATOM   2678 H  HG3  A PRO   A 1 125 ? 20.110 -1.863  3.746   0.50 13.90 ?  125 PRO   A HG3  1 
ATOM   2679 H  HG3  B PRO   A 1 125 ? 20.496 -2.181  3.623   0.50 11.09 ?  125 PRO   A HG3  1 
ATOM   2680 H  HD2  A PRO   A 1 125 ? 20.913 -4.108  4.788   0.50 13.18 ?  125 PRO   A HD2  1 
ATOM   2681 H  HD2  B PRO   A 1 125 ? 20.975 -4.629  4.496   0.50 10.67 ?  125 PRO   A HD2  1 
ATOM   2682 H  HD3  A PRO   A 1 125 ? 20.385 -2.896  5.695   0.50 13.18 ?  125 PRO   A HD3  1 
ATOM   2683 H  HD3  B PRO   A 1 125 ? 20.816 -3.371  5.478   0.50 10.67 ?  125 PRO   A HD3  1 
ATOM   2684 N  N    A LEU   A 1 126 ? 16.927 -5.169  2.435   0.50 9.61  ?  126 LEU   A N    1 
ATOM   2685 N  N    B LEU   A 1 126 ? 16.925 -5.022  2.409   0.50 12.83 ?  126 LEU   A N    1 
ATOM   2686 C  CA   A LEU   A 1 126 ? 16.967 -5.991  1.232   0.50 9.67  ?  126 LEU   A CA   1 
ATOM   2687 C  CA   B LEU   A 1 126 ? 16.804 -5.870  1.229   0.50 13.54 ?  126 LEU   A CA   1 
ATOM   2688 C  C    A LEU   A 1 126 ? 17.917 -5.376  0.210   0.50 9.82  ?  126 LEU   A C    1 
ATOM   2689 C  C    B LEU   A 1 126 ? 17.730 -5.328  0.141   0.50 12.94 ?  126 LEU   A C    1 
ATOM   2690 O  O    A LEU   A 1 126 ? 17.760 -4.213  -0.185  0.50 10.20 ?  126 LEU   A O    1 
ATOM   2691 O  O    B LEU   A 1 126 ? 17.456 -4.279  -0.454  0.50 13.03 ?  126 LEU   A O    1 
ATOM   2692 C  CB   A LEU   A 1 126 ? 15.574 -6.147  0.635   0.50 9.96  ?  126 LEU   A CB   1 
ATOM   2693 C  CB   B LEU   A 1 126 ? 15.349 -5.892  0.770   0.50 15.89 ?  126 LEU   A CB   1 
ATOM   2694 C  CG   A LEU   A 1 126 ? 14.632 -7.052  1.425   0.50 10.73 ?  126 LEU   A CG   1 
ATOM   2695 C  CG   B LEU   A 1 126 ? 14.837 -7.075  -0.051  0.50 17.80 ?  126 LEU   A CG   1 
ATOM   2696 C  CD1  A LEU   A 1 126 ? 13.221 -6.926  0.881   0.50 11.74 ?  126 LEU   A CD1  1 
ATOM   2697 C  CD1  B LEU   A 1 126 ? 15.096 -8.409  0.640   0.50 18.09 ?  126 LEU   A CD1  1 
ATOM   2698 C  CD2  A LEU   A 1 126 ? 15.099 -8.506  1.372   0.50 11.58 ?  126 LEU   A CD2  1 
ATOM   2699 C  CD2  B LEU   A 1 126 ? 13.348 -6.897  -0.328  0.50 18.53 ?  126 LEU   A CD2  1 
ATOM   2700 H  H    A LEU   A 1 126 ? 16.206 -4.706  2.521   0.50 11.54 ?  126 LEU   A H    1 
ATOM   2701 H  H    B LEU   A 1 126 ? 16.275 -4.459  2.510   0.50 15.41 ?  126 LEU   A H    1 
ATOM   2702 H  HA   A LEU   A 1 126 ? 17.304 -6.871  1.459   0.50 11.61 ?  126 LEU   A HA   1 
ATOM   2703 H  HA   B LEU   A 1 126 ? 17.080 -6.769  1.455   0.50 16.27 ?  126 LEU   A HA   1 
ATOM   2704 H  HB2  A LEU   A 1 126 ? 15.162 -5.272  0.580   0.50 11.96 ?  126 LEU   A HB2  1 
ATOM   2705 H  HB2  B LEU   A 1 126 ? 14.793 -5.841  1.560   0.50 19.09 ?  126 LEU   A HB2  1 
ATOM   2706 H  HB3  A LEU   A 1 126 ? 15.659 -6.521  -0.258  0.50 11.96 ?  126 LEU   A HB3  1 
ATOM   2707 H  HB3  B LEU   A 1 126 ? 15.203 -5.098  0.232   0.50 19.09 ?  126 LEU   A HB3  1 
ATOM   2708 H  HG   A LEU   A 1 126 ? 14.624 -6.770  2.350   0.50 12.89 ?  126 LEU   A HG   1 
ATOM   2709 H  HG   B LEU   A 1 126 ? 15.300 -7.074  -0.898  0.50 21.37 ?  126 LEU   A HG   1 
ATOM   2710 H  HD11 A LEU   A 1 126 ? 12.636 -7.507  1.386   0.50 14.11 ?  126 LEU   A HD11 1 
ATOM   2711 H  HD11 B LEU   A 1 126 ? 14.551 -9.091  0.219   0.50 21.72 ?  126 LEU   A HD11 1 
ATOM   2712 H  HD12 A LEU   A 1 126 ? 12.933 -6.004  0.964   0.50 14.11 ?  126 LEU   A HD12 1 
ATOM   2713 H  HD12 B LEU   A 1 126 ? 16.035 -8.633  0.553   0.50 21.72 ?  126 LEU   A HD12 1 
ATOM   2714 H  HD13 A LEU   A 1 126 ? 13.221 -7.188  -0.056  0.50 14.11 ?  126 LEU   A HD13 1 
ATOM   2715 H  HD13 B LEU   A 1 126 ? 14.857 -8.330  1.577   0.50 21.72 ?  126 LEU   A HD13 1 
ATOM   2716 H  HD21 A LEU   A 1 126 ? 14.411 -9.071  1.758   0.50 13.90 ?  126 LEU   A HD21 1 
ATOM   2717 H  HD21 B LEU   A 1 126 ? 13.029 -7.651  -0.850  0.50 22.25 ?  126 LEU   A HD21 1 
ATOM   2718 H  HD22 A LEU   A 1 126 ? 15.252 -8.756  0.447   0.50 13.90 ?  126 LEU   A HD22 1 
ATOM   2719 H  HD22 B LEU   A 1 126 ? 12.870 -6.858  0.517   0.50 22.25 ?  126 LEU   A HD22 1 
ATOM   2720 H  HD23 A LEU   A 1 126 ? 15.921 -8.593  1.879   0.50 13.90 ?  126 LEU   A HD23 1 
ATOM   2721 H  HD23 B LEU   A 1 126 ? 13.212 -6.073  -0.822  0.50 22.25 ?  126 LEU   A HD23 1 
ATOM   2722 N  N    A LEU   A 1 127 ? 18.900 -6.164  -0.219  0.50 10.91 ?  127 LEU   A N    1 
ATOM   2723 N  N    B LEU   A 1 127 ? 18.832 -6.031  -0.119  0.50 12.82 ?  127 LEU   A N    1 
ATOM   2724 C  CA   A LEU   A 1 127 ? 19.900 -5.684  -1.158  0.50 11.06 ?  127 LEU   A CA   1 
ATOM   2725 C  CA   B LEU   A 1 127 ? 19.816 -5.533  -1.071  0.50 12.20 ?  127 LEU   A CA   1 
ATOM   2726 C  C    A LEU   A 1 127 ? 19.279 -5.443  -2.523  0.50 11.09 ?  127 LEU   A C    1 
ATOM   2727 C  C    B LEU   A 1 127 ? 19.217 -5.417  -2.467  0.50 11.62 ?  127 LEU   A C    1 
ATOM   2728 O  O    A LEU   A 1 127 ? 18.431 -6.208  -2.993  0.50 11.30 ?  127 LEU   A O    1 
ATOM   2729 O  O    B LEU   A 1 127 ? 18.385 -6.226  -2.890  0.50 12.37 ?  127 LEU   A O    1 
ATOM   2730 C  CB   A LEU   A 1 127 ? 21.032 -6.705  -1.284  0.50 11.20 ?  127 LEU   A CB   1 
ATOM   2731 C  CB   B LEU   A 1 127 ? 21.044 -6.448  -1.113  0.50 12.32 ?  127 LEU   A CB   1 
ATOM   2732 C  CG   A LEU   A 1 127 ? 21.823 -6.996  -0.009  0.50 11.06 ?  127 LEU   A CG   1 
ATOM   2733 C  CG   B LEU   A 1 127 ? 21.887 -6.551  0.160   0.50 12.25 ?  127 LEU   A CG   1 
ATOM   2734 C  CD1  A LEU   A 1 127 ? 22.932 -7.975  -0.310  0.50 11.29 ?  127 LEU   A CD1  1 
ATOM   2735 C  CD1  B LEU   A 1 127 ? 23.014 -7.543  -0.042  0.50 12.64 ?  127 LEU   A CD1  1 
ATOM   2736 C  CD2  A LEU   A 1 127 ? 22.392 -5.716  0.581   0.50 11.99 ?  127 LEU   A CD2  1 
ATOM   2737 C  CD2  B LEU   A 1 127 ? 22.445 -5.196  0.567   0.50 13.43 ?  127 LEU   A CD2  1 
ATOM   2738 H  H    A LEU   A 1 127 ? 19.007 -6.987  0.020   0.50 13.11 ?  127 LEU   A H    1 
ATOM   2739 H  H    B LEU   A 1 127 ? 19.033 -6.791  0.241   0.50 15.40 ?  127 LEU   A H    1 
ATOM   2740 H  HA   A LEU   A 1 127 ? 20.273 -4.851  -0.836  0.50 13.29 ?  127 LEU   A HA   1 
ATOM   2741 H  HA   B LEU   A 1 127 ? 20.107 -4.653  -0.792  0.50 14.65 ?  127 LEU   A HA   1 
ATOM   2742 H  HB2  A LEU   A 1 127 ? 20.653 -7.546  -1.586  0.50 13.45 ?  127 LEU   A HB2  1 
ATOM   2743 H  HB2  B LEU   A 1 127 ? 20.747 -7.344  -1.329  0.50 14.80 ?  127 LEU   A HB2  1 
ATOM   2744 H  HB3  A LEU   A 1 127 ? 21.664 -6.382  -1.944  0.50 13.45 ?  127 LEU   A HB3  1 
ATOM   2745 H  HB3  B LEU   A 1 127 ? 21.632 -6.127  -1.815  0.50 14.80 ?  127 LEU   A HB3  1 
ATOM   2746 H  HG   A LEU   A 1 127 ? 21.232 -7.404  0.648   0.50 13.29 ?  127 LEU   A HG   1 
ATOM   2747 H  HG   B LEU   A 1 127 ? 21.330 -6.877  0.884   0.50 14.71 ?  127 LEU   A HG   1 
ATOM   2748 H  HD11 A LEU   A 1 127 ? 23.387 -8.202  0.517   0.50 13.56 ?  127 LEU   A HD11 1 
ATOM   2749 H  HD11 B LEU   A 1 127 ? 23.567 -7.561  0.757   0.50 15.18 ?  127 LEU   A HD11 1 
ATOM   2750 H  HD12 A LEU   A 1 127 ? 22.549 -8.777  -0.704  0.50 13.56 ?  127 LEU   A HD12 1 
ATOM   2751 H  HD12 B LEU   A 1 127 ? 22.638 -8.422  -0.203  0.50 15.18 ?  127 LEU   A HD12 1 
ATOM   2752 H  HD13 A LEU   A 1 127 ? 23.552 -7.566  -0.930  0.50 13.56 ?  127 LEU   A HD13 1 
ATOM   2753 H  HD13 B LEU   A 1 127 ? 23.548 -7.265  -0.803  0.50 15.18 ?  127 LEU   A HD13 1 
ATOM   2754 H  HD21 A LEU   A 1 127 ? 23.017 -5.943  1.286   0.50 14.41 ?  127 LEU   A HD21 1 
ATOM   2755 H  HD21 B LEU   A 1 127 ? 23.053 -5.317  1.314   0.50 16.12 ?  127 LEU   A HD21 1 
ATOM   2756 H  HD22 A LEU   A 1 127 ? 22.848 -5.224  -0.120  0.50 14.41 ?  127 LEU   A HD22 1 
ATOM   2757 H  HD22 B LEU   A 1 127 ? 22.918 -4.811  -0.186  0.50 16.12 ?  127 LEU   A HD22 1 
ATOM   2758 H  HD23 A LEU   A 1 127 ? 21.666 -5.183  0.939   0.50 14.41 ?  127 LEU   A HD23 1 
ATOM   2759 H  HD23 B LEU   A 1 127 ? 21.711 -4.619  0.829   0.50 16.12 ?  127 LEU   A HD23 1 
ATOM   2760 N  N    A SER   A 1 128 ? 19.736 -4.381  -3.170  0.50 11.38 ?  128 SER   A N    1 
ATOM   2761 N  N    B SER   A 1 128 ? 19.679 -4.401  -3.190  0.50 11.27 ?  128 SER   A N    1 
ATOM   2762 C  CA   A SER   A 1 128 ? 19.317 -3.977  -4.503  0.50 11.93 ?  128 SER   A CA   1 
ATOM   2763 C  CA   B SER   A 1 128 ? 19.316 -4.064  -4.562  0.50 11.44 ?  128 SER   A CA   1 
ATOM   2764 C  C    A SER   A 1 128 ? 17.852 -3.553  -4.570  0.50 12.46 ?  128 SER   A C    1 
ATOM   2765 C  C    B SER   A 1 128 ? 17.876 -3.588  -4.721  0.50 11.73 ?  128 SER   A C    1 
ATOM   2766 O  O    A SER   A 1 128 ? 17.347 -3.299  -5.667  0.50 14.31 ?  128 SER   A O    1 
ATOM   2767 O  O    B SER   A 1 128 ? 17.492 -3.230  -5.838  0.50 12.57 ?  128 SER   A O    1 
ATOM   2768 C  CB   A SER   A 1 128 ? 19.660 -5.019  -5.577  0.50 11.87 ?  128 SER   A CB   1 
ATOM   2769 C  CB   B SER   A 1 128 ? 19.648 -5.165  -5.583  0.50 11.46 ?  128 SER   A CB   1 
ATOM   2770 O  OG   A SER   A 1 128 ? 21.067 -5.222  -5.644  0.50 11.93 ?  128 SER   A OG   1 
ATOM   2771 O  OG   B SER   A 1 128 ? 21.054 -5.343  -5.680  0.50 11.66 ?  128 SER   A OG   1 
ATOM   2772 H  H    A SER   A 1 128 ? 20.332 -3.853  -2.836  0.50 13.67 ?  128 SER   A H    1 
ATOM   2773 H  H    B SER   A 1 128 ? 20.262 -3.849  -2.875  0.50 13.53 ?  128 SER   A H    1 
ATOM   2774 H  HA   A SER   A 1 128 ? 19.837 -3.197  -4.721  0.50 14.33 ?  128 SER   A HA   1 
ATOM   2775 H  HA   B SER   A 1 128 ? 19.858 -3.306  -4.809  0.50 13.74 ?  128 SER   A HA   1 
ATOM   2776 H  HB2  A SER   A 1 128 ? 19.227 -5.857  -5.363  0.50 14.26 ?  128 SER   A HB2  1 
ATOM   2777 H  HB2  B SER   A 1 128 ? 19.236 -5.993  -5.306  0.50 13.77 ?  128 SER   A HB2  1 
ATOM   2778 H  HB3  A SER   A 1 128 ? 19.349 -4.693  -6.439  0.50 14.26 ?  128 SER   A HB3  1 
ATOM   2779 H  HB3  B SER   A 1 128 ? 19.301 -4.895  -6.454  0.50 13.77 ?  128 SER   A HB3  1 
ATOM   2780 H  HG   A SER   A 1 128 ? 21.456 -4.499  -5.826  0.50 14.33 ?  128 SER   A HG   1 
ATOM   2781 H  HG   B SER   A 1 128 ? 21.416 -4.624  -5.921  0.50 14.00 ?  128 SER   A HG   1 
ATOM   2782 N  N    A ALA   A 1 129 ? 17.165 -3.448  -3.431  0.50 12.44 ?  129 ALA   A N    1 
ATOM   2783 N  N    B ALA   A 1 129 ? 17.085 -3.532  -3.650  0.50 12.41 ?  129 ALA   A N    1 
ATOM   2784 C  CA   A ALA   A 1 129 ? 15.807 -2.924  -3.390  0.50 12.44 ?  129 ALA   A CA   1 
ATOM   2785 C  CA   B ALA   A 1 129 ? 15.718 -3.043  -3.729  0.50 13.11 ?  129 ALA   A CA   1 
ATOM   2786 C  C    A ALA   A 1 129 ? 15.833 -1.395  -3.440  0.50 11.71 ?  129 ALA   A C    1 
ATOM   2787 C  C    B ALA   A 1 129 ? 15.689 -1.514  -3.633  0.50 13.40 ?  129 ALA   A C    1 
ATOM   2788 O  O    A ALA   A 1 129 ? 16.884 -0.766  -3.608  0.50 11.83 ?  129 ALA   A O    1 
ATOM   2789 O  O    B ALA   A 1 129 ? 16.719 -0.846  -3.485  0.50 13.93 ?  129 ALA   A O    1 
ATOM   2790 C  CB   A ALA   A 1 129 ? 15.078 -3.440  -2.149  0.50 13.64 ?  129 ALA   A CB   1 
ATOM   2791 C  CB   B ALA   A 1 129 ? 14.853 -3.710  -2.658  0.50 13.58 ?  129 ALA   A CB   1 
ATOM   2792 H  H    A ALA   A 1 129 ? 17.469 -3.677  -2.660  0.50 14.94 ?  129 ALA   A H    1 
ATOM   2793 H  H    B ALA   A 1 129 ? 17.324 -3.772  -2.858  0.50 14.90 ?  129 ALA   A H    1 
ATOM   2794 H  HA   A ALA   A 1 129 ? 15.328 -3.231  -4.169  0.50 14.94 ?  129 ALA   A HA   1 
ATOM   2795 H  HA   B ALA   A 1 129 ? 15.352 -3.284  -4.589  0.50 15.75 ?  129 ALA   A HA   1 
ATOM   2796 H  HB1  A ALA   A 1 129 ? 14.172 -3.089  -2.146  0.50 16.39 ?  129 ALA   A HB1  1 
ATOM   2797 H  HB1  B ALA   A 1 129 ? 13.963 -3.326  -2.686  0.50 16.31 ?  129 ALA   A HB1  1 
ATOM   2798 H  HB2  A ALA   A 1 129 ? 15.054 -4.409  -2.183  0.50 16.39 ?  129 ALA   A HB2  1 
ATOM   2799 H  HB2  B ALA   A 1 129 ? 14.811 -4.662  -2.832  0.50 16.31 ?  129 ALA   A HB2  1 
ATOM   2800 H  HB3  A ALA   A 1 129 ? 15.549 -3.146  -1.356  0.50 16.39 ?  129 ALA   A HB3  1 
ATOM   2801 H  HB3  B ALA   A 1 129 ? 15.251 -3.552  -1.786  0.50 16.31 ?  129 ALA   A HB3  1 
ATOM   2802 N  N    A GLY   A 1 130 ? 14.659 -0.784  -3.308  0.50 11.54 ?  130 GLY   A N    1 
ATOM   2803 N  N    B GLY   A 1 130 ? 14.489 -0.952  -3.745  0.50 13.50 ?  130 GLY   A N    1 
ATOM   2804 C  CA   A GLY   A 1 130 ? 14.605 0.671   -3.295  0.50 11.94 ?  130 GLY   A CA   1 
ATOM   2805 C  CA   B GLY   A 1 130 ? 14.340 0.492   -3.677  0.50 14.37 ?  130 GLY   A CA   1 
ATOM   2806 C  C    A GLY   A 1 130 ? 15.170 1.248   -4.578  0.50 12.30 ?  130 GLY   A C    1 
ATOM   2807 C  C    B GLY   A 1 130 ? 15.080 1.176   -4.801  0.50 15.03 ?  130 GLY   A C    1 
ATOM   2808 O  O    A GLY   A 1 130 ? 14.840 0.796   -5.681  0.50 12.37 ?  130 GLY   A O    1 
ATOM   2809 O  O    B GLY   A 1 130 ? 15.011 0.759   -5.963  0.50 15.57 ?  130 GLY   A O    1 
ATOM   2810 H  H    A GLY   A 1 130 ? 13.899 -1.172  -3.236  0.50 13.86 ?  130 GLY   A H    1 
ATOM   2811 H  H    B GLY   A 1 130 ? 13.755 -1.382  -3.869  0.50 16.21 ?  130 GLY   A H    1 
ATOM   2812 H  HA2  A GLY   A 1 130 ? 13.685 0.969   -3.196  0.50 14.35 ?  130 GLY   A HA2  1 
ATOM   2813 H  HA2  B GLY   A 1 130 ? 13.402 0.728   -3.744  0.50 17.26 ?  130 GLY   A HA2  1 
ATOM   2814 H  HA3  A GLY   A 1 130 ? 15.123 1.016   -2.551  0.50 14.35 ?  130 GLY   A HA3  1 
ATOM   2815 H  HA3  B GLY   A 1 130 ? 14.691 0.834   -2.851  0.50 17.26 ?  130 GLY   A HA3  1 
ATOM   2816 N  N    A ILE   A 1 131 ? 16.044 2.254   -4.438  0.50 12.87 ?  131 ILE   A N    1 
ATOM   2817 N  N    B ILE   A 1 131 ? 15.810 2.240   -4.452  0.50 15.31 ?  131 ILE   A N    1 
ATOM   2818 C  CA   A ILE   A 1 131 ? 16.579 2.980   -5.591  0.50 12.91 ?  131 ILE   A CA   1 
ATOM   2819 C  CA   B ILE   A 1 131 ? 16.476 3.061   -5.453  0.50 14.81 ?  131 ILE   A CA   1 
ATOM   2820 C  C    A ILE   A 1 131 ? 17.586 2.182   -6.406  0.50 12.84 ?  131 ILE   A C    1 
ATOM   2821 C  C    B ILE   A 1 131 ? 17.484 2.276   -6.279  0.50 14.45 ?  131 ILE   A C    1 
ATOM   2822 O  O    A ILE   A 1 131 ? 18.000 2.651   -7.473  0.50 13.73 ?  131 ILE   A O    1 
ATOM   2823 O  O    B ILE   A 1 131 ? 17.918 2.762   -7.327  0.50 15.15 ?  131 ILE   A O    1 
ATOM   2824 C  CB   A ILE   A 1 131 ? 17.172 4.357   -5.210  0.50 14.08 ?  131 ILE   A CB   1 
ATOM   2825 C  CB   B ILE   A 1 131 ? 17.101 4.329   -4.824  0.50 15.37 ?  131 ILE   A CB   1 
ATOM   2826 C  CG1  A ILE   A 1 131 ? 18.408 4.207   -4.314  0.50 14.53 ?  131 ILE   A CG1  1 
ATOM   2827 C  CG1  B ILE   A 1 131 ? 18.277 3.968   -3.911  0.50 16.45 ?  131 ILE   A CG1  1 
ATOM   2828 C  CG2  A ILE   A 1 131 ? 16.112 5.220   -4.540  0.50 14.29 ?  131 ILE   A CG2  1 
ATOM   2829 C  CG2  B ILE   A 1 131 ? 16.044 5.115   -4.054  0.50 15.44 ?  131 ILE   A CG2  1 
ATOM   2830 C  CD1  A ILE   A 1 131 ? 19.018 5.540   -3.883  0.50 15.36 ?  131 ILE   A CD1  1 
ATOM   2831 C  CD1  B ILE   A 1 131 ? 19.003 5.177   -3.338  0.50 17.33 ?  131 ILE   A CD1  1 
ATOM   2832 H  H    A ILE   A 1 131 ? 16.342 2.535   -3.686  0.50 15.46 ?  131 ILE   A H    1 
ATOM   2833 H  H    B ILE   A 1 131 ? 15.931 2.504   -3.640  0.50 18.38 ?  131 ILE   A H    1 
ATOM   2834 H  HA   A ILE   A 1 131 ? 15.843 3.160   -6.190  0.50 15.51 ?  131 ILE   A HA   1 
ATOM   2835 H  HA   B ILE   A 1 131 ? 15.802 3.370   -6.074  0.50 17.78 ?  131 ILE   A HA   1 
ATOM   2836 H  HB   A ILE   A 1 131 ? 17.446 4.803   -6.028  0.50 16.91 ?  131 ILE   A HB   1 
ATOM   2837 H  HB   B ILE   A 1 131 ? 17.430 4.894   -5.542  0.50 18.46 ?  131 ILE   A HB   1 
ATOM   2838 H  HG12 A ILE   A 1 131 ? 18.158 3.721   -3.514  0.50 17.45 ?  131 ILE   A HG12 1 
ATOM   2839 H  HG12 B ILE   A 1 131 ? 17.944 3.441   -3.170  0.50 19.75 ?  131 ILE   A HG12 1 
ATOM   2840 H  HG13 A ILE   A 1 131 ? 19.091 3.715   -4.798  0.50 17.45 ?  131 ILE   A HG13 1 
ATOM   2841 H  HG13 B ILE   A 1 131 ? 18.922 3.454   -4.419  0.50 19.75 ?  131 ILE   A HG13 1 
ATOM   2842 H  HG21 A ILE   A 1 131 ? 16.434 6.133   -4.490  0.50 17.16 ?  131 ILE   A HG21 1 
ATOM   2843 H  HG21 B ILE   A 1 131 ? 16.404 5.984   -3.821  0.50 18.54 ?  131 ILE   A HG21 1 
ATOM   2844 H  HG22 A ILE   A 1 131 ? 15.301 5.184   -5.069  0.50 17.16 ?  131 ILE   A HG22 1 
ATOM   2845 H  HG22 B ILE   A 1 131 ? 15.260 5.222   -4.616  0.50 18.54 ?  131 ILE   A HG22 1 
ATOM   2846 H  HG23 A ILE   A 1 131 ? 15.944 4.875   -3.651  0.50 17.16 ?  131 ILE   A HG23 1 
ATOM   2847 H  HG23 B ILE   A 1 131 ? 15.810 4.624   -3.251  0.50 18.54 ?  131 ILE   A HG23 1 
ATOM   2848 H  HD11 A ILE   A 1 131 ? 19.870 5.370   -3.450  0.50 18.44 ?  131 ILE   A HD11 1 
ATOM   2849 H  HD11 B ILE   A 1 131 ? 19.795 4.874   -2.868  0.50 20.81 ?  131 ILE   A HD11 1 
ATOM   2850 H  HD12 A ILE   A 1 131 ? 19.151 6.094   -4.667  0.50 18.44 ?  131 ILE   A HD12 1 
ATOM   2851 H  HD12 B ILE   A 1 131 ? 19.256 5.769   -4.065  0.50 20.81 ?  131 ILE   A HD12 1 
ATOM   2852 H  HD13 A ILE   A 1 131 ? 18.415 5.979   -3.264  0.50 18.44 ?  131 ILE   A HD13 1 
ATOM   2853 H  HD13 B ILE   A 1 131 ? 18.412 5.642   -2.725  0.50 20.81 ?  131 ILE   A HD13 1 
ATOM   2854 N  N    A PHE   A 1 132 ? 17.992 0.993   -5.945  0.50 12.39 ?  132 PHE   A N    1 
ATOM   2855 N  N    B PHE   A 1 132 ? 17.857 1.068   -5.844  0.50 14.16 ?  132 PHE   A N    1 
ATOM   2856 C  CA   A PHE   A 1 132 ? 18.838 0.127   -6.762  0.50 12.60 ?  132 PHE   A CA   1 
ATOM   2857 C  CA   B PHE   A 1 132 ? 18.740 0.221   -6.637  0.50 14.42 ?  132 PHE   A CA   1 
ATOM   2858 C  C    A PHE   A 1 132 ? 18.045 -0.648  -7.812  0.50 13.23 ?  132 PHE   A C    1 
ATOM   2859 C  C    B PHE   A 1 132 ? 18.021 -0.492  -7.781  0.50 15.14 ?  132 PHE   A C    1 
ATOM   2860 O  O    A PHE   A 1 132 ? 18.652 -1.341  -8.635  0.50 13.77 ?  132 PHE   A O    1 
ATOM   2861 O  O    B PHE   A 1 132 ? 18.691 -1.013  -8.678  0.50 15.62 ?  132 PHE   A O    1 
ATOM   2862 C  CB   A PHE   A 1 132 ? 19.658 -0.836  -5.893  0.50 11.89 ?  132 PHE   A CB   1 
ATOM   2863 C  CB   B PHE   A 1 132 ? 19.474 -0.785  -5.744  0.50 13.84 ?  132 PHE   A CB   1 
ATOM   2864 C  CG   A PHE   A 1 132 ? 20.888 -0.216  -5.254  0.50 11.63 ?  132 PHE   A CG   1 
ATOM   2865 C  CG   B PHE   A 1 132 ? 20.678 -0.214  -5.032  0.50 13.15 ?  132 PHE   A CG   1 
ATOM   2866 C  CD1  A PHE   A 1 132 ? 20.776 0.823   -4.343  0.50 12.41 ?  132 PHE   A CD1  1 
ATOM   2867 C  CD1  B PHE   A 1 132 ? 20.534 0.756   -4.054  0.50 13.42 ?  132 PHE   A CD1  1 
ATOM   2868 C  CD2  A PHE   A 1 132 ? 22.156 -0.713  -5.535  0.50 12.83 ?  132 PHE   A CD2  1 
ATOM   2869 C  CD2  B PHE   A 1 132 ? 21.953 -0.680  -5.320  0.50 13.18 ?  132 PHE   A CD2  1 
ATOM   2870 C  CE1  A PHE   A 1 132 ? 21.905 1.373   -3.747  0.50 12.23 ?  132 PHE   A CE1  1 
ATOM   2871 C  CE1  B PHE   A 1 132 ? 21.642 1.266   -3.394  0.50 13.23 ?  132 PHE   A CE1  1 
ATOM   2872 C  CE2  A PHE   A 1 132 ? 23.285 -0.170  -4.940  0.50 13.33 ?  132 PHE   A CE2  1 
ATOM   2873 C  CE2  B PHE   A 1 132 ? 23.062 -0.176  -4.661  0.50 12.83 ?  132 PHE   A CE2  1 
ATOM   2874 C  CZ   A PHE   A 1 132 ? 23.158 0.876   -4.046  0.50 12.84 ?  132 PHE   A CZ   1 
ATOM   2875 C  CZ   B PHE   A 1 132 ? 22.903 0.801   -3.698  0.50 12.63 ?  132 PHE   A CZ   1 
ATOM   2876 H  H    A PHE   A 1 132 ? 17.798 0.672   -5.171  0.50 14.88 ?  132 PHE   A H    1 
ATOM   2877 H  H    B PHE   A 1 132 ? 17.615 0.721   -5.091  0.50 17.00 ?  132 PHE   A H    1 
ATOM   2878 H  HA   A PHE   A 1 132 ? 19.470 0.682   -7.239  0.50 15.14 ?  132 PHE   A HA   1 
ATOM   2879 H  HA   B PHE   A 1 132 ? 19.413 0.786   -7.038  0.50 17.32 ?  132 PHE   A HA   1 
ATOM   2880 H  HB2  A PHE   A 1 132 ? 19.096 -1.165  -5.176  0.50 14.28 ?  132 PHE   A HB2  1 
ATOM   2881 H  HB2  B PHE   A 1 132 ? 18.861 -1.105  -5.066  0.50 16.63 ?  132 PHE   A HB2  1 
ATOM   2882 H  HB3  A PHE   A 1 132 ? 19.958 -1.583  -6.441  0.50 14.28 ?  132 PHE   A HB3  1 
ATOM   2883 H  HB3  B PHE   A 1 132 ? 19.779 -1.525  -6.291  0.50 16.63 ?  132 PHE   A HB3  1 
ATOM   2884 H  HD1  A PHE   A 1 132 ? 19.938 1.162   -4.134  0.50 14.90 ?  132 PHE   A HD1  1 
ATOM   2885 H  HD1  B PHE   A 1 132 ? 19.687 1.077   -3.843  0.50 16.12 ?  132 PHE   A HD1  1 
ATOM   2886 H  HD2  A PHE   A 1 132 ? 22.251 -1.418  -6.137  0.50 15.41 ?  132 PHE   A HD2  1 
ATOM   2887 H  HD2  B PHE   A 1 132 ? 22.066 -1.336  -5.971  0.50 15.83 ?  132 PHE   A HD2  1 
ATOM   2888 H  HE1  A PHE   A 1 132 ? 21.819 2.076   -3.141  0.50 14.69 ?  132 PHE   A HE1  1 
ATOM   2889 H  HE1  B PHE   A 1 132 ? 21.532 1.924   -2.744  0.50 15.88 ?  132 PHE   A HE1  1 
ATOM   2890 H  HE2  A PHE   A 1 132 ? 24.128 -0.508  -5.147  0.50 16.01 ?  132 PHE   A HE2  1 
ATOM   2891 H  HE2  B PHE   A 1 132 ? 23.910 -0.491  -4.874  0.50 15.41 ?  132 PHE   A HE2  1 
ATOM   2892 H  HZ   A PHE   A 1 132 ? 23.916 1.244   -3.647  0.50 15.42 ?  132 PHE   A HZ   1 
ATOM   2893 H  HZ   B PHE   A 1 132 ? 23.643 1.145   -3.256  0.50 15.17 ?  132 PHE   A HZ   1 
ATOM   2894 N  N    A GLY   A 1 133 ? 16.713 -0.565  -7.797  0.50 13.44 ?  133 GLY   A N    1 
ATOM   2895 N  N    B GLY   A 1 133 ? 16.690 -0.540  -7.776  0.50 15.31 ?  133 GLY   A N    1 
ATOM   2896 C  CA   A GLY   A 1 133 ? 15.908 -0.955  -8.935  0.50 13.98 ?  133 GLY   A CA   1 
ATOM   2897 C  CA   B GLY   A 1 133 ? 15.945 -0.884  -8.972  0.50 15.61 ?  133 GLY   A CA   1 
ATOM   2898 C  C    A GLY   A 1 133 ? 15.493 -2.409  -9.021  0.50 13.99 ?  133 GLY   A C    1 
ATOM   2899 C  C    B GLY   A 1 133 ? 15.660 -2.349  -9.226  0.50 15.34 ?  133 GLY   A C    1 
ATOM   2900 O  O    A GLY   A 1 133 ? 14.710 -2.746  -9.917  0.50 15.04 ?  133 GLY   A O    1 
ATOM   2901 O  O    B GLY   A 1 133 ? 15.115 -2.666  -10.290 0.50 15.26 ?  133 GLY   A O    1 
ATOM   2902 H  H    A GLY   A 1 133 ? 16.252 -0.278  -7.129  0.50 16.14 ?  133 GLY   A H    1 
ATOM   2903 H  H    B GLY   A 1 133 ? 16.193 -0.370  -7.094  0.50 18.39 ?  133 GLY   A H    1 
ATOM   2904 H  HA2  A GLY   A 1 133 ? 15.090 -0.439  -8.931  0.50 16.79 ?  133 GLY   A HA2  1 
ATOM   2905 H  HA2  B GLY   A 1 133 ? 15.094 -0.426  -8.949  0.50 18.75 ?  133 GLY   A HA2  1 
ATOM   2906 H  HA3  A GLY   A 1 133 ? 16.391 -0.744  -9.747  0.50 16.79 ?  133 GLY   A HA3  1 
ATOM   2907 H  HA3  B GLY   A 1 133 ? 16.435 -0.563  -9.745  0.50 18.75 ?  133 GLY   A HA3  1 
ATOM   2908 N  N    A ALA   A 1 134 ? 15.974 -3.282  -8.138  0.50 13.36 ?  134 ALA   A N    1 
ATOM   2909 N  N    B ALA   A 1 134 ? 16.001 -3.252  -8.309  0.50 15.70 ?  134 ALA   A N    1 
ATOM   2910 C  CA   A ALA   A 1 134 ? 15.587 -4.681  -8.246  0.50 13.46 ?  134 ALA   A CA   1 
ATOM   2911 C  CA   B ALA   A 1 134 ? 15.739 -4.666  -8.537  0.50 16.61 ?  134 ALA   A CA   1 
ATOM   2912 C  C    A ALA   A 1 134 ? 14.251 -4.928  -7.552  0.50 13.52 ?  134 ALA   A C    1 
ATOM   2913 C  C    B ALA   A 1 134 ? 14.371 -5.074  -7.991  0.50 17.33 ?  134 ALA   A C    1 
ATOM   2914 O  O    A ALA   A 1 134 ? 13.783 -4.128  -6.736  0.50 13.95 ?  134 ALA   A O    1 
ATOM   2915 O  O    B ALA   A 1 134 ? 13.720 -4.343  -7.245  0.50 17.92 ?  134 ALA   A O    1 
ATOM   2916 C  CB   A ALA   A 1 134 ? 16.651 -5.605  -7.656  0.50 13.86 ?  134 ALA   A CB   1 
ATOM   2917 C  CB   B ALA   A 1 134 ? 16.839 -5.534  -7.925  0.50 17.01 ?  134 ALA   A CB   1 
ATOM   2918 H  H    A ALA   A 1 134 ? 16.504 -3.094  -7.482  0.50 16.04 ?  134 ALA   A H    1 
ATOM   2919 H  H    B ALA   A 1 134 ? 16.392 -3.074  -7.558  0.50 18.85 ?  134 ALA   A H    1 
ATOM   2920 H  HA   A ALA   A 1 134 ? 15.481 -4.905  -9.180  0.50 16.16 ?  134 ALA   A HA   1 
ATOM   2921 H  HA   B ALA   A 1 134 ? 15.731 -4.833  -9.488  0.50 19.95 ?  134 ALA   A HA   1 
ATOM   2922 H  HB1  A ALA   A 1 134 ? 16.360 -6.525  -7.765  0.50 16.64 ?  134 ALA   A HB1  1 
ATOM   2923 H  HB1  B ALA   A 1 134 ? 16.644 -6.467  -8.111  0.50 20.43 ?  134 ALA   A HB1  1 
ATOM   2924 H  HB2  A ALA   A 1 134 ? 17.484 -5.462  -8.128  0.50 16.64 ?  134 ALA   A HB2  1 
ATOM   2925 H  HB2  B ALA   A 1 134 ? 17.689 -5.289  -8.323  0.50 20.43 ?  134 ALA   A HB2  1 
ATOM   2926 H  HB3  A ALA   A 1 134 ? 16.760 -5.402  -6.715  0.50 16.64 ?  134 ALA   A HB3  1 
ATOM   2927 H  HB3  B ALA   A 1 134 ? 16.866 -5.387  -6.968  0.50 20.43 ?  134 ALA   A HB3  1 
ATOM   2928 N  N    A ASP   A 1 135 ? 13.640 -6.056  -7.900  0.50 13.65 ?  135 ASP   A N    1 
ATOM   2929 N  N    B ASP   A 1 135 ? 13.941 -6.266  -8.388  0.50 18.29 ?  135 ASP   A N    1 
ATOM   2930 C  CA   A ASP   A 1 135 ? 12.390 -6.501  -7.291  0.50 14.21 ?  135 ASP   A CA   1 
ATOM   2931 C  CA   B ASP   A 1 135 ? 12.681 -6.834  -7.928  0.50 19.31 ?  135 ASP   A CA   1 
ATOM   2932 C  C    A ASP   A 1 135 ? 12.662 -6.943  -5.857  0.50 13.45 ?  135 ASP   A C    1 
ATOM   2933 C  C    B ASP   A 1 135 ? 12.831 -7.270  -6.475  0.50 18.06 ?  135 ASP   A C    1 
ATOM   2934 O  O    A ASP   A 1 135 ? 13.435 -7.890  -5.649  0.50 13.45 ?  135 ASP   A O    1 
ATOM   2935 O  O    B ASP   A 1 135 ? 13.627 -8.174  -6.190  0.50 17.66 ?  135 ASP   A O    1 
ATOM   2936 C  CB   A ASP   A 1 135 ? 11.869 -7.681  -8.114  0.50 15.79 ?  135 ASP   A CB   1 
ATOM   2937 C  CB   B ASP   A 1 135 ? 12.321 -8.030  -8.809  0.50 21.78 ?  135 ASP   A CB   1 
ATOM   2938 C  CG   A ASP   A 1 135 ? 10.550 -8.248  -7.590  0.50 17.69 ?  135 ASP   A CG   1 
ATOM   2939 C  CG   B ASP   A 1 135 ? 10.964 -8.641  -8.454  0.50 23.89 ?  135 ASP   A CG   1 
ATOM   2940 O  OD1  A ASP   A 1 135 ? 10.012 -7.720  -6.595  0.50 18.30 ?  135 ASP   A OD1  1 
ATOM   2941 O  OD1  B ASP   A 1 135 ? 10.815 -9.158  -7.329  0.50 24.13 ?  135 ASP   A OD1  1 
ATOM   2942 O  OD2  A ASP   A 1 135 ? 10.052 -9.227  -8.188  0.50 19.90 -1 135 ASP   A OD2  1 
ATOM   2943 O  OD2  B ASP   A 1 135 ? 10.042 -8.600  -9.298  0.50 25.42 -1 135 ASP   A OD2  1 
ATOM   2944 H  H    A ASP   A 1 135 ? 13.930 -6.587  -8.501  0.50 16.39 ?  135 ASP   A H    1 
ATOM   2945 H  H    B ASP   A 1 135 ? 14.367 -6.770  -8.931  0.50 21.96 ?  135 ASP   A H    1 
ATOM   2946 H  HA   A ASP   A 1 135 ? 11.727 -5.785  -7.314  0.50 17.06 ?  135 ASP   A HA   1 
ATOM   2947 H  HA   B ASP   A 1 135 ? 11.979 -6.170  -8.006  0.50 23.18 ?  135 ASP   A HA   1 
ATOM   2948 H  HB2  A ASP   A 1 135 ? 11.724 -7.385  -9.025  0.50 18.96 ?  135 ASP   A HB2  1 
ATOM   2949 H  HB2  B ASP   A 1 135 ? 12.310 -7.738  -9.738  0.50 26.14 ?  135 ASP   A HB2  1 
ATOM   2950 H  HB3  A ASP   A 1 135 ? 12.540 -8.383  -8.098  0.50 18.96 ?  135 ASP   A HB3  1 
ATOM   2951 H  HB3  B ASP   A 1 135 ? 12.999 -8.716  -8.693  0.50 26.14 ?  135 ASP   A HB3  1 
ATOM   2952 N  N    A PRO   A 1 136 ? 12.078 -6.293  -4.846  0.50 12.92 ?  136 PRO   A N    1 
ATOM   2953 N  N    B PRO   A 1 136 ? 12.108 -6.660  -5.532  0.50 17.32 ?  136 PRO   A N    1 
ATOM   2954 C  CA   A PRO   A 1 136 ? 12.329 -6.725  -3.458  0.50 13.03 ?  136 PRO   A CA   1 
ATOM   2955 C  CA   B PRO   A 1 136 ? 12.326 -7.003  -4.115  0.50 16.98 ?  136 PRO   A CA   1 
ATOM   2956 C  C    A PRO   A 1 136 ? 11.898 -8.158  -3.167  0.50 12.56 ?  136 PRO   A C    1 
ATOM   2957 C  C    B PRO   A 1 136 ? 11.916 -8.418  -3.758  0.50 16.84 ?  136 PRO   A C    1 
ATOM   2958 O  O    A PRO   A 1 136 ? 12.482 -8.806  -2.289  0.50 11.45 ?  136 PRO   A O    1 
ATOM   2959 O  O    B PRO   A 1 136 ? 12.561 -9.044  -2.910  0.50 16.55 ?  136 PRO   A O    1 
ATOM   2960 C  CB   A PRO   A 1 136 ? 11.561 -5.688  -2.620  0.50 13.72 ?  136 PRO   A CB   1 
ATOM   2961 C  CB   B PRO   A 1 136 ? 11.492 -5.954  -3.368  0.50 17.25 ?  136 PRO   A CB   1 
ATOM   2962 C  CG   A PRO   A 1 136 ? 10.540 -5.111  -3.561  0.50 14.56 ?  136 PRO   A CG   1 
ATOM   2963 C  CG   B PRO   A 1 136 ? 10.442 -5.539  -4.352  0.50 17.51 ?  136 PRO   A CG   1 
ATOM   2964 C  CD   A PRO   A 1 136 ? 11.196 -5.113  -4.906  0.50 13.54 ?  136 PRO   A CD   1 
ATOM   2965 C  CD   B PRO   A 1 136 ? 11.068 -5.633  -5.707  0.50 17.59 ?  136 PRO   A CD   1 
ATOM   2966 H  HA   A PRO   A 1 136 ? 13.273 -6.630  -3.253  0.50 15.65 ?  136 PRO   A HA   1 
ATOM   2967 H  HA   B PRO   A 1 136 ? 13.261 -6.886  -3.880  0.50 20.39 ?  136 PRO   A HA   1 
ATOM   2968 H  HB2  A PRO   A 1 136 ? 11.125 -6.117  -1.871  0.50 16.48 ?  136 PRO   A HB2  1 
ATOM   2969 H  HB2  B PRO   A 1 136 ? 11.090 -6.354  -2.580  0.50 20.71 ?  136 PRO   A HB2  1 
ATOM   2970 H  HB3  A PRO   A 1 136 ? 12.164 -4.987  -2.311  0.50 16.48 ?  136 PRO   A HB3  1 
ATOM   2971 H  HB3  B PRO   A 1 136 ? 12.057 -5.204  -3.122  0.50 20.71 ?  136 PRO   A HB3  1 
ATOM   2972 H  HG2  A PRO   A 1 136 ? 9.750  -5.674  -3.571  0.50 17.49 ?  136 PRO   A HG2  1 
ATOM   2973 H  HG2  B PRO   A 1 136 ? 9.687  -6.139  -4.288  0.50 21.02 ?  136 PRO   A HG2  1 
ATOM   2974 H  HG3  A PRO   A 1 136 ? 10.310 -4.206  -3.293  0.50 17.49 ?  136 PRO   A HG3  1 
ATOM   2975 H  HG3  B PRO   A 1 136 ? 10.176 -4.627  -4.169  0.50 21.02 ?  136 PRO   A HG3  1 
ATOM   2976 H  HD2  A PRO   A 1 136 ? 10.524 -5.220  -5.604  0.50 16.27 ?  136 PRO   A HD2  1 
ATOM   2977 H  HD2  B PRO   A 1 136 ? 10.417 -5.930  -6.362  0.50 21.12 ?  136 PRO   A HD2  1 
ATOM   2978 H  HD3  A PRO   A 1 136 ? 11.709 -4.297  -5.037  0.50 16.27 ?  136 PRO   A HD3  1 
ATOM   2979 H  HD3  B PRO   A 1 136 ? 11.470 -4.788  -5.960  0.50 21.12 ?  136 PRO   A HD3  1 
ATOM   2980 N  N    A ILE   A 1 137 ? 10.884 -8.670  -3.868  0.50 13.36 ?  137 ILE   A N    1 
ATOM   2981 N  N    B ILE   A 1 137 ? 10.846 -8.936  -4.357  0.50 17.24 ?  137 ILE   A N    1 
ATOM   2982 C  CA   A ILE   A 1 137 ? 10.486 -10.066 -3.689  0.50 14.19 ?  137 ILE   A CA   1 
ATOM   2983 C  CA   B ILE   A 1 137 ? 10.486 -10.332 -4.128  0.50 18.04 ?  137 ILE   A CA   1 
ATOM   2984 C  C    A ILE   A 1 137 ? 11.627 -10.995 -4.096  0.50 14.13 ?  137 ILE   A C    1 
ATOM   2985 C  C    B ILE   A 1 137 ? 11.665 -11.226 -4.476  0.50 17.65 ?  137 ILE   A C    1 
ATOM   2986 O  O    A ILE   A 1 137 ? 11.954 -11.964 -3.394  0.50 13.95 ?  137 ILE   A O    1 
ATOM   2987 O  O    B ILE   A 1 137 ? 11.961 -12.201 -3.773  0.50 17.32 ?  137 ILE   A O    1 
ATOM   2988 C  CB   A ILE   A 1 137 ? 9.201  -10.359 -4.488  0.50 14.99 ?  137 ILE   A CB   1 
ATOM   2989 C  CB   B ILE   A 1 137 ? 9.223  -10.702 -4.928  0.50 19.43 ?  137 ILE   A CB   1 
ATOM   2990 C  CG1  A ILE   A 1 137 ? 8.000  -9.594  -3.910  0.50 15.63 ?  137 ILE   A CG1  1 
ATOM   2991 C  CG1  B ILE   A 1 137 ? 8.165  -9.598  -4.812  0.50 20.25 ?  137 ILE   A CG1  1 
ATOM   2992 C  CG2  A ILE   A 1 137 ? 8.930  -11.859 -4.536  0.50 16.13 ?  137 ILE   A CG2  1 
ATOM   2993 C  CG2  B ILE   A 1 137 ? 8.657  -12.022 -4.430  0.50 20.08 ?  137 ILE   A CG2  1 
ATOM   2994 C  CD1  A ILE   A 1 137 ? 6.708  -9.834  -4.666  0.50 16.71 ?  137 ILE   A CD1  1 
ATOM   2995 C  CD1  B ILE   A 1 137 ? 6.894  -9.882  -5.575  0.50 20.81 ?  137 ILE   A CD1  1 
ATOM   2996 H  H    A ILE   A 1 137 ? 10.420 -8.224  -4.445  0.50 16.05 ?  137 ILE   A H    1 
ATOM   2997 H  H    B ILE   A 1 137 ? 10.338 -8.506  -4.891  0.50 20.70 ?  137 ILE   A H    1 
ATOM   2998 H  HA   A ILE   A 1 137 ? 10.295 -10.207 -2.751  0.50 17.05 ?  137 ILE   A HA   1 
ATOM   2999 H  HA   B ILE   A 1 137 ? 10.289 -10.464 -3.189  0.50 21.66 ?  137 ILE   A HA   1 
ATOM   3000 H  HB   A ILE   A 1 137 ? 9.336  -10.042 -5.394  0.50 18.00 ?  137 ILE   A HB   1 
ATOM   3001 H  HB   B ILE   A 1 137 ? 9.462  -10.806 -5.861  0.50 23.32 ?  137 ILE   A HB   1 
ATOM   3002 H  HG12 A ILE   A 1 137 ? 7.862  -9.866  -2.989  0.50 18.77 ?  137 ILE   A HG12 1 
ATOM   3003 H  HG12 B ILE   A 1 137 ? 7.942  -9.479  -3.875  0.50 24.32 ?  137 ILE   A HG12 1 
ATOM   3004 H  HG13 A ILE   A 1 137 ? 8.187  -8.636  -3.941  0.50 18.77 ?  137 ILE   A HG13 1 
ATOM   3005 H  HG13 B ILE   A 1 137 ? 8.522  -8.770  -5.171  0.50 24.32 ?  137 ILE   A HG13 1 
ATOM   3006 H  HG21 A ILE   A 1 137 ? 8.121  -12.021 -5.041  0.50 19.36 ?  137 ILE   A HG21 1 
ATOM   3007 H  HG21 B ILE   A 1 137 ? 7.951  -12.311 -5.028  0.50 24.11 ?  137 ILE   A HG21 1 
ATOM   3008 H  HG22 A ILE   A 1 137 ? 9.667  -12.302 -4.974  0.50 19.36 ?  137 ILE   A HG22 1 
ATOM   3009 H  HG22 B ILE   A 1 137 ? 9.365  -12.682 -4.413  0.50 24.11 ?  137 ILE   A HG22 1 
ATOM   3010 H  HG23 A ILE   A 1 137 ? 8.828  -12.184 -3.631  0.50 19.36 ?  137 ILE   A HG23 1 
ATOM   3011 H  HG23 B ILE   A 1 137 ? 8.303  -11.893 -3.536  0.50 24.11 ?  137 ILE   A HG23 1 
ATOM   3012 H  HD11 A ILE   A 1 137 ? 6.013  -9.337  -4.225  0.50 20.07 ?  137 ILE   A HD11 1 
ATOM   3013 H  HD11 B ILE   A 1 137 ? 6.602  -9.066  -6.011  0.50 24.99 ?  137 ILE   A HD11 1 
ATOM   3014 H  HD12 A ILE   A 1 137 ? 6.812  -9.532  -5.585  0.50 20.07 ?  137 ILE   A HD12 1 
ATOM   3015 H  HD12 B ILE   A 1 137 ? 7.072  -10.564 -6.239  0.50 24.99 ?  137 ILE   A HD12 1 
ATOM   3016 H  HD13 A ILE   A 1 137 ? 6.488  -10.778 -4.650  0.50 20.07 ?  137 ILE   A HD13 1 
ATOM   3017 H  HD13 B ILE   A 1 137 ? 6.218  -10.190 -4.953  0.50 24.99 ?  137 ILE   A HD13 1 
ATOM   3018 N  N    A HIS   A 1 138 ? 12.231 -10.724 -5.256  0.50 14.47 ?  138 HIS   A N    1 
ATOM   3019 N  N    B HIS   A 1 138 ? 12.372 -10.891 -5.555  0.50 17.67 ?  138 HIS   A N    1 
ATOM   3020 C  CA   A HIS   A 1 138 ? 13.362 -11.522 -5.724  0.50 14.66 ?  138 HIS   A CA   1 
ATOM   3021 C  CA   B HIS   A 1 138 ? 13.585 -11.621 -5.893  0.50 17.09 ?  138 HIS   A CA   1 
ATOM   3022 C  C    A HIS   A 1 138 ? 14.537 -11.425 -4.763  0.50 14.58 ?  138 HIS   A C    1 
ATOM   3023 C  C    B HIS   A 1 138 ? 14.667 -11.436 -4.832  0.50 15.70 ?  138 HIS   A C    1 
ATOM   3024 O  O    A HIS   A 1 138 ? 15.174 -12.433 -4.436  0.50 15.00 ?  138 HIS   A O    1 
ATOM   3025 O  O    B HIS   A 1 138 ? 15.357 -12.398 -4.474  0.50 15.64 ?  138 HIS   A O    1 
ATOM   3026 C  CB   A HIS   A 1 138 ? 13.777 -11.056 -7.121  0.50 14.52 ?  138 HIS   A CB   1 
ATOM   3027 C  CB   B HIS   A 1 138 ? 14.092 -11.207 -7.273  0.50 18.10 ?  138 HIS   A CB   1 
ATOM   3028 C  CG   A HIS   A 1 138 ? 15.070 -11.649 -7.593  0.50 15.00 ?  138 HIS   A CG   1 
ATOM   3029 C  CG   B HIS   A 1 138 ? 15.277 -11.995 -7.734  0.50 19.30 ?  138 HIS   A CG   1 
ATOM   3030 N  ND1  A HIS   A 1 138 ? 15.215 -12.992 -7.867  0.50 16.04 ?  138 HIS   A ND1  1 
ATOM   3031 N  ND1  B HIS   A 1 138 ? 15.212 -13.343 -8.017  0.50 20.26 ?  138 HIS   A ND1  1 
ATOM   3032 C  CD2  A HIS   A 1 138 ? 16.282 -11.086 -7.822  0.50 14.32 ?  138 HIS   A CD2  1 
ATOM   3033 C  CD2  B HIS   A 1 138 ? 16.562 -11.628 -7.946  0.50 19.72 ?  138 HIS   A CD2  1 
ATOM   3034 C  CE1  A HIS   A 1 138 ? 16.455 -13.228 -8.256  0.50 15.68 ?  138 HIS   A CE1  1 
ATOM   3035 C  CE1  B HIS   A 1 138 ? 16.404 -13.769 -8.393  0.50 20.48 ?  138 HIS   A CE1  1 
ATOM   3036 N  NE2  A HIS   A 1 138 ? 17.125 -12.090 -8.236  0.50 14.59 ?  138 HIS   A NE2  1 
ATOM   3037 N  NE2  B HIS   A 1 138 ? 17.242 -12.748 -8.357  0.50 19.88 ?  138 HIS   A NE2  1 
ATOM   3038 H  H    A HIS   A 1 138 ? 12.006 -10.080 -5.787  0.50 17.38 ?  138 HIS   A H    1 
ATOM   3039 H  H    B HIS   A 1 138 ? 12.162 -10.259 -6.106  0.50 21.22 ?  138 HIS   A H    1 
ATOM   3040 H  HA   A HIS   A 1 138 ? 13.090 -12.448 -5.781  0.50 17.60 ?  138 HIS   A HA   1 
ATOM   3041 H  HA   B HIS   A 1 138 ? 13.371 -12.563 -5.935  0.50 20.52 ?  138 HIS   A HA   1 
ATOM   3042 H  HB2  A HIS   A 1 138 ? 13.084 -11.310 -7.755  0.50 17.44 ?  138 HIS   A HB2  1 
ATOM   3043 H  HB2  B HIS   A 1 138 ? 13.380 -11.334 -7.921  0.50 21.73 ?  138 HIS   A HB2  1 
ATOM   3044 H  HB3  A HIS   A 1 138 ? 13.874 -10.090 -7.116  0.50 17.44 ?  138 HIS   A HB3  1 
ATOM   3045 H  HB3  B HIS   A 1 138 ? 14.350 -10.273 -7.248  0.50 21.73 ?  138 HIS   A HB3  1 
ATOM   3046 H  HD1  A HIS   A 1 138 ? 14.591 -13.581 -7.803  0.50 19.26 ?  138 HIS   A HD1  1 
ATOM   3047 H  HD1  B HIS   A 1 138 ? 14.500 -13.828 -7.964  0.50 24.32 ?  138 HIS   A HD1  1 
ATOM   3048 H  HD2  A HIS   A 1 138 ? 16.496 -10.185 -7.722  0.50 17.19 ?  138 HIS   A HD2  1 
ATOM   3049 H  HD2  B HIS   A 1 138 ? 16.917 -10.778 -7.834  0.50 23.67 ?  138 HIS   A HD2  1 
ATOM   3050 H  HE1  A HIS   A 1 138 ? 16.798 -14.056 -8.499  0.50 18.83 ?  138 HIS   A HE1  1 
ATOM   3051 H  HE1  B HIS   A 1 138 ? 16.613 -14.641 -8.637  0.50 24.59 ?  138 HIS   A HE1  1 
ATOM   3052 N  N    . SER   A 1 139 ? 14.844 -10.212 -4.316  1.00 14.84 ?  139 SER   A N    1 
ATOM   3053 C  CA   . SER   A 1 139 ? 15.915 -10.010 -3.350  1.00 14.36 ?  139 SER   A CA   1 
ATOM   3054 C  C    . SER   A 1 139 ? 15.700 -10.847 -2.093  1.00 13.70 ?  139 SER   A C    1 
ATOM   3055 O  O    . SER   A 1 139 ? 16.649 -11.428 -1.557  1.00 13.71 ?  139 SER   A O    1 
ATOM   3056 C  CB   . SER   A 1 139 ? 16.046 -8.527  -3.015  1.00 14.33 ?  139 SER   A CB   1 
ATOM   3057 O  OG   . SER   A 1 139 ? 17.123 -8.348  -2.110  1.00 14.53 ?  139 SER   A OG   1 
ATOM   3058 H  H    A SER   A 1 139 ? 14.436 -9.488  -4.549  0.50 17.82 ?  139 SER   A H    1 
ATOM   3059 H  H    B SER   A 1 139 ? 14.378 -9.511  -4.506  0.50 17.82 ?  139 SER   A H    1 
ATOM   3060 H  HA   . SER   A 1 139 ? 16.752 -10.287 -3.748  1.00 17.24 ?  139 SER   A HA   1 
ATOM   3061 H  HB2  . SER   A 1 139 ? 16.227 -8.023  -3.829  1.00 17.20 ?  139 SER   A HB2  1 
ATOM   3062 H  HB3  . SER   A 1 139 ? 15.218 -8.214  -2.615  1.00 17.20 ?  139 SER   A HB3  1 
ATOM   3063 H  HG   . SER   A 1 139 ? 17.212 -7.527  -1.921  1.00 17.45 ?  139 SER   A HG   1 
ATOM   3064 N  N    . LEU   A 1 140 ? 14.458 -10.921 -1.610  1.00 13.78 ?  140 LEU   A N    1 
ATOM   3065 C  CA   . LEU   A 1 140 ? 14.189 -11.727 -0.424  1.00 13.36 ?  140 LEU   A CA   1 
ATOM   3066 C  C    . LEU   A 1 140 ? 14.448 -13.206 -0.697  1.00 13.43 ?  140 LEU   A C    1 
ATOM   3067 O  O    . LEU   A 1 140 ? 14.999 -13.919 0.154   1.00 13.77 ?  140 LEU   A O    1 
ATOM   3068 C  CB   . LEU   A 1 140 ? 12.751 -11.503 0.038   1.00 13.64 ?  140 LEU   A CB   1 
ATOM   3069 C  CG   . LEU   A 1 140 ? 12.298 -12.360 1.221   1.00 13.90 ?  140 LEU   A CG   1 
ATOM   3070 C  CD1  . LEU   A 1 140 ? 13.205 -12.165 2.425   1.00 13.92 ?  140 LEU   A CD1  1 
ATOM   3071 C  CD2  . LEU   A 1 140 ? 10.839 -12.063 1.578   1.00 14.92 ?  140 LEU   A CD2  1 
ATOM   3072 H  H    . LEU   A 1 140 ? 13.772 -10.511 -1.936  1.00 16.55 ?  140 LEU   A H    1 
ATOM   3073 H  HA   . LEU   A 1 140 ? 14.778 -11.446 0.292   1.00 16.05 ?  140 LEU   A HA   1 
ATOM   3074 H  HB2  . LEU   A 1 140 ? 12.649 -10.580 0.303   1.00 16.38 ?  140 LEU   A HB2  1 
ATOM   3075 H  HB3  . LEU   A 1 140 ? 12.155 -11.701 -0.701  1.00 16.38 ?  140 LEU   A HB3  1 
ATOM   3076 H  HG   . LEU   A 1 140 ? 12.342 -13.299 0.968   1.00 16.69 ?  140 LEU   A HG   1 
ATOM   3077 H  HD11 . LEU   A 1 140 ? 12.827 -12.641 3.183   1.00 16.71 ?  140 LEU   A HD11 1 
ATOM   3078 H  HD12 . LEU   A 1 140 ? 14.082 -12.528 2.216   1.00 16.71 ?  140 LEU   A HD12 1 
ATOM   3079 H  HD13 . LEU   A 1 140 ? 13.269 -11.223 2.620   1.00 16.71 ?  140 LEU   A HD13 1 
ATOM   3080 H  HD21 . LEU   A 1 140 ? 10.576 -12.624 2.330   1.00 17.91 ?  140 LEU   A HD21 1 
ATOM   3081 H  HD22 . LEU   A 1 140 ? 10.756 -11.130 1.819   1.00 17.91 ?  140 LEU   A HD22 1 
ATOM   3082 H  HD23 . LEU   A 1 140 ? 10.278 -12.263 0.812   1.00 17.91 ?  140 LEU   A HD23 1 
ATOM   3083 N  N    . ARG   A 1 141 ? 14.057 -13.679 -1.883  1.00 14.32 ?  141 ARG   A N    1 
ATOM   3084 C  CA   . ARG   A 1 141 ? 14.304 -15.066 -2.258  1.00 15.29 ?  141 ARG   A CA   1 
ATOM   3085 C  C    . ARG   A 1 141 ? 15.798 -15.370 -2.265  1.00 14.13 ?  141 ARG   A C    1 
ATOM   3086 O  O    . ARG   A 1 141 ? 16.247 -16.379 -1.706  1.00 14.12 ?  141 ARG   A O    1 
ATOM   3087 C  CB   . ARG   A 1 141 ? 13.694 -15.318 -3.639  1.00 17.80 ?  141 ARG   A CB   1 
ATOM   3088 C  CG   . ARG   A 1 141 ? 13.680 -16.763 -4.082  1.00 20.72 ?  141 ARG   A CG   1 
ATOM   3089 C  CD   . ARG   A 1 141 ? 12.638 -17.530 -3.325  1.00 23.11 ?  141 ARG   A CD   1 
ATOM   3090 N  NE   . ARG   A 1 141 ? 13.244 -18.374 -2.309  1.00 23.98 ?  141 ARG   A NE   1 
ATOM   3091 C  CZ   . ARG   A 1 141 ? 12.567 -18.948 -1.323  1.00 24.59 ?  141 ARG   A CZ   1 
ATOM   3092 N  NH1  . ARG   A 1 141 ? 11.284 -18.691 -1.122  1.00 24.26 ?  141 ARG   A NH1  1 
ATOM   3093 N  NH2  . ARG   A 1 141 ? 13.196 -19.789 -0.507  1.00 25.30 ?  141 ARG   A NH2  1 
ATOM   3094 H  H    . ARG   A 1 141 ? 13.650 -13.215 -2.485  1.00 17.20 ?  141 ARG   A H    1 
ATOM   3095 H  HA   . ARG   A 1 141 ? 13.878 -15.653 -1.620  1.00 18.36 ?  141 ARG   A HA   1 
ATOM   3096 H  HB2  . ARG   A 1 141 ? 12.779 -14.999 -3.635  1.00 21.38 ?  141 ARG   A HB2  1 
ATOM   3097 H  HB3  . ARG   A 1 141 ? 14.206 -14.818 -4.295  1.00 21.38 ?  141 ARG   A HB3  1 
ATOM   3098 H  HG2  . ARG   A 1 141 ? 13.473 -16.810 -5.030  1.00 24.87 ?  141 ARG   A HG2  1 
ATOM   3099 H  HG3  . ARG   A 1 141 ? 14.548 -17.167 -3.909  1.00 24.87 ?  141 ARG   A HG3  1 
ATOM   3100 H  HD2  . ARG   A 1 141 ? 12.041 -16.910 -2.877  1.00 27.75 ?  141 ARG   A HD2  1 
ATOM   3101 H  HD3  . ARG   A 1 141 ? 12.135 -18.086 -3.945  1.00 27.75 ?  141 ARG   A HD3  1 
ATOM   3102 H  HE   . ARG   A 1 141 ? 14.057 -18.620 -2.425  1.00 28.79 ?  141 ARG   A HE   1 
ATOM   3103 H  HH11 . ARG   A 1 141 ? 10.857 -18.161 -1.650  1.00 29.13 ?  141 ARG   A HH11 1 
ATOM   3104 H  HH12 . ARG   A 1 141 ? 10.862 -19.072 -0.473  1.00 29.13 ?  141 ARG   A HH12 1 
ATOM   3105 H  HH21 . ARG   A 1 141 ? 14.027 -19.963 -0.629  1.00 30.38 ?  141 ARG   A HH21 1 
ATOM   3106 H  HH22 . ARG   A 1 141 ? 12.769 -20.159 0.144   1.00 30.38 ?  141 ARG   A HH22 1 
ATOM   3107 N  N    . VAL   A 1 142 ? 16.590 -14.505 -2.899  1.00 13.58 ?  142 VAL   A N    1 
ATOM   3108 C  CA   . VAL   A 1 142 ? 18.036 -14.714 -2.924  1.00 13.44 ?  142 VAL   A CA   1 
ATOM   3109 C  C    . VAL   A 1 142 ? 18.602 -14.693 -1.511  1.00 12.68 ?  142 VAL   A C    1 
ATOM   3110 O  O    . VAL   A 1 142 ? 19.477 -15.499 -1.166  1.00 12.84 ?  142 VAL   A O    1 
ATOM   3111 C  CB   . VAL   A 1 142 ? 18.728 -13.690 -3.841  1.00 13.42 ?  142 VAL   A CB   1 
ATOM   3112 C  CG1  . VAL   A 1 142 ? 20.239 -13.895 -3.804  1.00 13.12 ?  142 VAL   A CG1  1 
ATOM   3113 C  CG2  . VAL   A 1 142 ? 18.221 -13.821 -5.264  1.00 14.81 ?  142 VAL   A CG2  1 
ATOM   3114 H  H    . VAL   A 1 142 ? 16.324 -13.791 -3.314  1.00 16.32 ?  142 VAL   A H    1 
ATOM   3115 H  HA   . VAL   A 1 142 ? 18.213 -15.585 -3.295  1.00 16.14 ?  142 VAL   A HA   1 
ATOM   3116 H  HB   . VAL   A 1 142 ? 18.544 -12.784 -3.532  1.00 16.11 ?  142 VAL   A HB   1 
ATOM   3117 H  HG11 . VAL   A 1 142 ? 20.647 -13.408 -4.539  1.00 15.76 ?  142 VAL   A HG11 1 
ATOM   3118 H  HG12 . VAL   A 1 142 ? 20.589 -13.561 -2.960  1.00 15.76 ?  142 VAL   A HG12 1 
ATOM   3119 H  HG13 . VAL   A 1 142 ? 20.431 -14.841 -3.891  1.00 15.76 ?  142 VAL   A HG13 1 
ATOM   3120 H  HG21 . VAL   A 1 142 ? 18.687 -13.181 -5.828  1.00 17.78 ?  142 VAL   A HG21 1 
ATOM   3121 H  HG22 . VAL   A 1 142 ? 18.398 -14.722 -5.574  1.00 17.78 ?  142 VAL   A HG22 1 
ATOM   3122 H  HG23 . VAL   A 1 142 ? 17.272 -13.643 -5.275  1.00 17.78 ?  142 VAL   A HG23 1 
ATOM   3123 N  N    . CYS   A 1 143 ? 18.134 -13.763 -0.677  1.00 12.72 ?  143 CYS   A N    1 
ATOM   3124 C  CA   . CYS   A 1 143 ? 18.597 -13.711 0.705   1.00 12.64 ?  143 CYS   A CA   1 
ATOM   3125 C  C    . CYS   A 1 143 ? 18.373 -15.051 1.399   1.00 12.56 ?  143 CYS   A C    1 
ATOM   3126 O  O    . CYS   A 1 143 ? 19.293 -15.636 1.979   1.00 12.39 ?  143 CYS   A O    1 
ATOM   3127 C  CB   . CYS   A 1 143 ? 17.854 -12.602 1.444   1.00 13.00 ?  143 CYS   A CB   1 
ATOM   3128 S  SG   . CYS   A 1 143 ? 18.349 -12.410 3.162   1.00 13.27 ?  143 CYS   A SG   1 
ATOM   3129 H  H    . CYS   A 1 143 ? 17.558 -13.160 -0.886  1.00 15.28 ?  143 CYS   A H    1 
ATOM   3130 H  HA   . CYS   A 1 143 ? 19.544 -13.518 0.722   1.00 15.18 ?  143 CYS   A HA   1 
ATOM   3131 H  HB2  . CYS   A 1 143 ? 18.016 -11.761 0.990   1.00 15.62 ?  143 CYS   A HB2  1 
ATOM   3132 H  HB3  . CYS   A 1 143 ? 16.907 -12.800 1.433   1.00 15.62 ?  143 CYS   A HB3  1 
ATOM   3133 H  HG   . CYS   A 1 143 ? 17.772 -11.469 3.624   1.00 15.94 ?  143 CYS   A HG   1 
ATOM   3134 N  N    . VAL   A 1 144 ? 17.143 -15.555 1.339   1.00 13.15 ?  144 VAL   A N    1 
ATOM   3135 C  CA   . VAL   A 1 144 ? 16.805 -16.790 2.037   1.00 14.42 ?  144 VAL   A CA   1 
ATOM   3136 C  C    . VAL   A 1 144 ? 17.624 -17.961 1.512   1.00 13.69 ?  144 VAL   A C    1 
ATOM   3137 O  O    . VAL   A 1 144 ? 17.994 -18.867 2.273   1.00 14.29 ?  144 VAL   A O    1 
ATOM   3138 C  CB   . VAL   A 1 144 ? 15.289 -17.034 1.915   1.00 17.12 ?  144 VAL   A CB   1 
ATOM   3139 C  CG1  . VAL   A 1 144 ? 14.930 -18.466 2.253   1.00 18.89 ?  144 VAL   A CG1  1 
ATOM   3140 C  CG2  . VAL   A 1 144 ? 14.536 -16.037 2.797   1.00 17.14 ?  144 VAL   A CG2  1 
ATOM   3141 H  H    . VAL   A 1 144 ? 16.485 -15.202 0.899   1.00 15.79 ?  144 VAL   A H    1 
ATOM   3142 H  HA   . VAL   A 1 144 ? 17.005 -16.680 2.973   1.00 17.32 ?  144 VAL   A HA   1 
ATOM   3143 H  HB   . VAL   A 1 144 ? 15.013 -16.871 0.997   1.00 20.56 ?  144 VAL   A HB   1 
ATOM   3144 H  HG11 . VAL   A 1 144 ? 13.976 -18.519 2.440   1.00 22.68 ?  144 VAL   A HG11 1 
ATOM   3145 H  HG12 . VAL   A 1 144 ? 15.147 -19.036 1.500   1.00 22.68 ?  144 VAL   A HG12 1 
ATOM   3146 H  HG13 . VAL   A 1 144 ? 15.431 -18.740 3.036   1.00 22.68 ?  144 VAL   A HG13 1 
ATOM   3147 H  HG21 . VAL   A 1 144 ? 13.580 -16.211 2.739   1.00 20.58 ?  144 VAL   A HG21 1 
ATOM   3148 H  HG22 . VAL   A 1 144 ? 14.831 -16.133 3.715   1.00 20.58 ?  144 VAL   A HG22 1 
ATOM   3149 H  HG23 . VAL   A 1 144 ? 14.718 -15.132 2.486   1.00 20.58 ?  144 VAL   A HG23 1 
ATOM   3150 N  N    . ASP   A 1 145 ? 17.889 -17.986 0.211   1.00 13.85 ?  145 ASP   A N    1 
ATOM   3151 C  CA   . ASP   A 1 145 ? 18.607 -19.093 -0.412  1.00 14.54 ?  145 ASP   A CA   1 
ATOM   3152 C  C    . ASP   A 1 145 ? 20.130 -18.937 -0.369  1.00 14.36 ?  145 ASP   A C    1 
ATOM   3153 O  O    . ASP   A 1 145 ? 20.840 -19.833 -0.845  1.00 16.54 ?  145 ASP   A O    1 
ATOM   3154 C  CB   . ASP   A 1 145 ? 18.161 -19.251 -1.867  1.00 16.44 ?  145 ASP   A CB   1 
ATOM   3155 C  CG   . ASP   A 1 145 ? 16.713 -19.685 -1.996  1.00 18.96 ?  145 ASP   A CG   1 
ATOM   3156 O  OD1  . ASP   A 1 145 ? 16.145 -20.224 -1.020  1.00 19.56 ?  145 ASP   A OD1  1 
ATOM   3157 O  OD2  . ASP   A 1 145 ? 16.143 -19.477 -3.083  1.00 20.50 -1 145 ASP   A OD2  1 
ATOM   3158 H  H    . ASP   A 1 145 ? 17.655 -17.367 -0.343  1.00 16.63 ?  145 ASP   A H    1 
ATOM   3159 H  HA   . ASP   A 1 145 ? 18.379 -19.909 0.055   1.00 17.46 ?  145 ASP   A HA   1 
ATOM   3160 H  HB2  . ASP   A 1 145 ? 18.268 -18.404 -2.327  1.00 19.74 ?  145 ASP   A HB2  1 
ATOM   3161 H  HB3  . ASP   A 1 145 ? 18.705 -19.931 -2.292  1.00 19.74 ?  145 ASP   A HB3  1 
ATOM   3162 N  N    . THR   A 1 146 ? 20.651 -17.845 0.181   1.00 12.42 ?  146 THR   A N    1 
ATOM   3163 C  CA   . THR   A 1 146 ? 22.091 -17.591 0.191   1.00 12.04 ?  146 THR   A CA   1 
ATOM   3164 C  C    . THR   A 1 146 ? 22.653 -17.396 1.586   1.00 11.89 ?  146 THR   A C    1 
ATOM   3165 O  O    . THR   A 1 146 ? 23.733 -17.914 1.898   1.00 12.87 ?  146 THR   A O    1 
ATOM   3166 C  CB   . THR   A 1 146 ? 22.403 -16.339 -0.646  1.00 12.02 ?  146 THR   A CB   1 
ATOM   3167 O  OG1  . THR   A 1 146 ? 21.874 -16.501 -1.961  1.00 12.76 ?  146 THR   A OG1  1 
ATOM   3168 C  CG2  . THR   A 1 146 ? 23.907 -16.103 -0.748  1.00 12.67 ?  146 THR   A CG2  1 
ATOM   3169 H  H    . THR   A 1 146 ? 20.184 -17.219 0.547   1.00 14.92 ?  146 THR   A H    1 
ATOM   3170 H  HA   . THR   A 1 146 ? 22.549 -18.337 -0.214  1.00 14.46 ?  146 THR   A HA   1 
ATOM   3171 H  HB   . THR   A 1 146 ? 22.004 -15.558 -0.233  1.00 14.44 ?  146 THR   A HB   1 
ATOM   3172 H  HG1  . THR   A 1 146 ? 21.038 -16.580 -1.929  1.00 15.33 ?  146 THR   A HG1  1 
ATOM   3173 H  HG21 . THR   A 1 146 ? 24.092 -15.440 -1.429  1.00 15.21 ?  146 THR   A HG21 1 
ATOM   3174 H  HG22 . THR   A 1 146 ? 24.251 -15.790 0.101   1.00 15.21 ?  146 THR   A HG22 1 
ATOM   3175 H  HG23 . THR   A 1 146 ? 24.353 -16.932 -0.986  1.00 15.21 ?  146 THR   A HG23 1 
ATOM   3176 N  N    . VAL   A 1 147 ? 21.966 -16.624 2.419   1.00 11.61 ?  147 VAL   A N    1 
ATOM   3177 C  CA   . VAL   A 1 147 ? 22.452 -16.323 3.757   1.00 11.71 ?  147 VAL   A CA   1 
ATOM   3178 C  C    . VAL   A 1 147 ? 22.130 -17.491 4.674   1.00 12.40 ?  147 VAL   A C    1 
ATOM   3179 O  O    . VAL   A 1 147 ? 20.986 -17.969 4.720   1.00 13.05 ?  147 VAL   A O    1 
ATOM   3180 C  CB   . VAL   A 1 147 ? 21.831 -15.018 4.276   1.00 11.97 ?  147 VAL   A CB   1 
ATOM   3181 C  CG1  . VAL   A 1 147 ? 22.372 -14.702 5.647   1.00 13.00 ?  147 VAL   A CG1  1 
ATOM   3182 C  CG2  . VAL   A 1 147 ? 22.071 -13.871 3.304   1.00 12.04 ?  147 VAL   A CG2  1 
ATOM   3183 H  H    . VAL   A 1 147 ? 21.203 -16.265 2.236   1.00 13.95 ?  147 VAL   A H    1 
ATOM   3184 H  HA   . VAL   A 1 147 ? 23.414 -16.211 3.727   1.00 14.06 ?  147 VAL   A HA   1 
ATOM   3185 H  HB   . VAL   A 1 147 ? 20.873 -15.138 4.362   1.00 14.38 ?  147 VAL   A HB   1 
ATOM   3186 H  HG11 . VAL   A 1 147 ? 22.129 -13.795 5.883   1.00 15.61 ?  147 VAL   A HG11 1 
ATOM   3187 H  HG12 . VAL   A 1 147 ? 21.996 -15.323 6.290   1.00 15.61 ?  147 VAL   A HG12 1 
ATOM   3188 H  HG13 . VAL   A 1 147 ? 23.341 -14.789 5.632   1.00 15.61 ?  147 VAL   A HG13 1 
ATOM   3189 H  HG21 . VAL   A 1 147 ? 21.736 -13.048 3.699   1.00 14.46 ?  147 VAL   A HG21 1 
ATOM   3190 H  HG22 . VAL   A 1 147 ? 23.020 -13.794 3.133   1.00 14.46 ?  147 VAL   A HG22 1 
ATOM   3191 H  HG23 . VAL   A 1 147 ? 21.596 -14.054 2.478   1.00 14.46 ?  147 VAL   A HG23 1 
ATOM   3192 N  N    . ARG   A 1 148 ? 23.153 -17.963 5.391   1.00 12.46 ?  148 ARG   A N    1 
ATOM   3193 C  CA   . ARG   A 1 148 ? 23.027 -19.039 6.359   1.00 12.54 ?  148 ARG   A CA   1 
ATOM   3194 C  C    . ARG   A 1 148 ? 23.152 -18.564 7.795   1.00 12.84 ?  148 ARG   A C    1 
ATOM   3195 O  O    . ARG   A 1 148 ? 22.749 -19.292 8.711   1.00 14.46 ?  148 ARG   A O    1 
ATOM   3196 C  CB   . ARG   A 1 148 ? 24.067 -20.135 6.086   1.00 13.17 ?  148 ARG   A CB   1 
ATOM   3197 C  CG   . ARG   A 1 148 ? 23.894 -20.779 4.725   1.00 14.58 ?  148 ARG   A CG   1 
ATOM   3198 C  CD   . ARG   A 1 148 ? 24.981 -21.807 4.421   1.00 15.27 ?  148 ARG   A CD   1 
ATOM   3199 N  NE   . ARG   A 1 148 ? 26.318 -21.223 4.444   1.00 15.05 ?  148 ARG   A NE   1 
ATOM   3200 C  CZ   . ARG   A 1 148 ? 26.830 -20.489 3.467   1.00 14.37 ?  148 ARG   A CZ   1 
ATOM   3201 N  NH1  . ARG   A 1 148 ? 26.154 -20.254 2.354   1.00 14.72 ?  148 ARG   A NH1  1 
ATOM   3202 N  NH2  . ARG   A 1 148 ? 28.048 -19.962 3.615   1.00 15.07 ?  148 ARG   A NH2  1 
ATOM   3203 H  H    . ARG   A 1 148 ? 23.960 -17.663 5.318   1.00 14.96 ?  148 ARG   A H    1 
ATOM   3204 H  HA   . ARG   A 1 148 ? 22.152 -19.440 6.258   1.00 15.06 ?  148 ARG   A HA   1 
ATOM   3205 H  HB2  . ARG   A 1 148 ? 24.955 -19.754 6.127   1.00 15.82 ?  148 ARG   A HB2  1 
ATOM   3206 H  HB3  . ARG   A 1 148 ? 23.973 -20.834 6.756   1.00 15.82 ?  148 ARG   A HB3  1 
ATOM   3207 H  HG2  . ARG   A 1 148 ? 23.033 -21.221 4.696   1.00 17.51 ?  148 ARG   A HG2  1 
ATOM   3208 H  HG3  . ARG   A 1 148 ? 23.936 -20.084 4.048   1.00 17.51 ?  148 ARG   A HG3  1 
ATOM   3209 H  HD2  . ARG   A 1 148 ? 24.946 -22.511 5.091   1.00 18.34 ?  148 ARG   A HD2  1 
ATOM   3210 H  HD3  . ARG   A 1 148 ? 24.821 -22.183 3.539   1.00 18.34 ?  148 ARG   A HD3  1 
ATOM   3211 H  HE   . ARG   A 1 148 ? 26.803 -21.366 5.133   1.00 18.07 ?  148 ARG   A HE   1 
ATOM   3212 H  HH11 . ARG   A 1 148 ? 25.369 -20.585 2.246   1.00 17.68 ?  148 ARG   A HH11 1 
ATOM   3213 H  HH12 . ARG   A 1 148 ? 26.506 -19.773 1.733   1.00 17.68 ?  148 ARG   A HH12 1 
ATOM   3214 H  HH21 . ARG   A 1 148 ? 28.490 -20.103 4.338   1.00 18.09 ?  148 ARG   A HH21 1 
ATOM   3215 H  HH22 . ARG   A 1 148 ? 28.389 -19.479 2.990   1.00 18.09 ?  148 ARG   A HH22 1 
ATOM   3216 N  N    . THR   A 1 149 ? 23.702 -17.374 8.008   1.00 13.01 ?  149 THR   A N    1 
ATOM   3217 C  CA   . THR   A 1 149 ? 23.780 -16.771 9.324   1.00 13.02 ?  149 THR   A CA   1 
ATOM   3218 C  C    . THR   A 1 149 ? 22.455 -16.071 9.632   1.00 12.29 ?  149 THR   A C    1 
ATOM   3219 O  O    . THR   A 1 149 ? 21.516 -16.073 8.824   1.00 13.16 ?  149 THR   A O    1 
ATOM   3220 C  CB   . THR   A 1 149 ? 24.984 -15.839 9.376   1.00 13.27 ?  149 THR   A CB   1 
ATOM   3221 O  OG1  . THR   A 1 149 ? 24.847 -14.902 8.307   1.00 13.33 ?  149 THR   A OG1  1 
ATOM   3222 C  CG2  . THR   A 1 149 ? 26.290 -16.633 9.239   1.00 13.64 ?  149 THR   A CG2  1 
ATOM   3223 H  H    . THR   A 1 149 ? 24.050 -16.890 7.386   1.00 15.63 ?  149 THR   A H    1 
ATOM   3224 H  HA   . THR   A 1 149 ? 23.909 -17.473 9.981   1.00 15.63 ?  149 THR   A HA   1 
ATOM   3225 H  HB   . THR   A 1 149 ? 24.984 -15.369 10.219  1.00 15.93 ?  149 THR   A HB   1 
ATOM   3226 H  HG1  . THR   A 1 149 ? 25.503 -14.374 8.301   1.00 16.01 ?  149 THR   A HG1  1 
ATOM   3227 H  HG21 . THR   A 1 149 ? 27.050 -16.034 9.293   1.00 16.38 ?  149 THR   A HG21 1 
ATOM   3228 H  HG22 . THR   A 1 149 ? 26.357 -17.292 9.951   1.00 16.38 ?  149 THR   A HG22 1 
ATOM   3229 H  HG23 . THR   A 1 149 ? 26.317 -17.097 8.384   1.00 16.38 ?  149 THR   A HG23 1 
ATOM   3230 N  N    . ASN   A 1 150 ? 22.336 -15.533 10.840  1.00 12.93 ?  150 ASN   A N    1 
ATOM   3231 C  CA   . ASN   A 1 150 ? 21.053 -15.018 11.322  1.00 13.32 ?  150 ASN   A CA   1 
ATOM   3232 C  C    . ASN   A 1 150 ? 20.869 -13.583 10.855  1.00 12.50 ?  150 ASN   A C    1 
ATOM   3233 O  O    . ASN   A 1 150 ? 21.618 -12.686 11.263  1.00 13.95 ?  150 ASN   A O    1 
ATOM   3234 C  CB   . ASN   A 1 150 ? 20.990 -15.123 12.840  1.00 16.20 ?  150 ASN   A CB   1 
ATOM   3235 C  CG   . ASN   A 1 150 ? 20.885 -16.554 13.304  1.00 20.58 ?  150 ASN   A CG   1 
ATOM   3236 O  OD1  . ASN   A 1 150 ? 20.283 -17.387 12.625  1.00 21.58 ?  150 ASN   A OD1  1 
ATOM   3237 N  ND2  . ASN   A 1 150 ? 21.486 -16.859 14.450  1.00 22.80 ?  150 ASN   A ND2  1 
ATOM   3238 H  H    . ASN   A 1 150 ? 22.981 -15.457 11.403  1.00 15.52 ?  150 ASN   A H    1 
ATOM   3239 H  HA   . ASN   A 1 150 ? 20.333 -15.558 10.955  1.00 15.99 ?  150 ASN   A HA   1 
ATOM   3240 H  HB2  . ASN   A 1 150 ? 21.795 -14.745 13.225  1.00 19.45 ?  150 ASN   A HB2  1 
ATOM   3241 H  HB3  . ASN   A 1 150 ? 20.208 -14.651 13.165  1.00 19.45 ?  150 ASN   A HB3  1 
ATOM   3242 H  HD21 . ASN   A 1 150 ? 21.458 -17.667 14.758  1.00 27.37 ?  150 ASN   A HD21 1 
ATOM   3243 H  HD22 . ASN   A 1 150 ? 21.899 -16.251 14.898  1.00 27.37 ?  150 ASN   A HD22 1 
ATOM   3244 N  N    . VAL   A 1 151 ? 19.875 -13.360 10.003  1.00 12.49 ?  151 VAL   A N    1 
ATOM   3245 C  CA   . VAL   A 1 151 ? 19.660 -12.056 9.399   1.00 12.55 ?  151 VAL   A CA   1 
ATOM   3246 C  C    . VAL   A 1 151 ? 18.281 -11.532 9.769   1.00 12.21 ?  151 VAL   A C    1 
ATOM   3247 O  O    . VAL   A 1 151 ? 17.265 -12.237 9.634   1.00 13.86 ?  151 VAL   A O    1 
ATOM   3248 C  CB   . VAL   A 1 151 ? 19.945 -12.046 7.882   1.00 13.63 ?  151 VAL   A CB   1 
ATOM   3249 C  CG1  . VAL   A 1 151 ? 19.112 -13.058 7.135   1.00 14.76 ?  151 VAL   A CG1  1 
ATOM   3250 C  CG2  . VAL   A 1 151 ? 19.756 -10.640 7.308   1.00 13.79 ?  151 VAL   A CG2  1 
ATOM   3251 H  H    . VAL   A 1 151 ? 19.311 -13.960 9.751   1.00 15.00 ?  151 VAL   A H    1 
ATOM   3252 H  HA   . VAL   A 1 151 ? 20.306 -11.444 9.787   1.00 15.07 ?  151 VAL   A HA   1 
ATOM   3253 H  HB   . VAL   A 1 151 ? 20.877 -12.289 7.739   1.00 16.37 ?  151 VAL   A HB   1 
ATOM   3254 H  HG11 . VAL   A 1 151 ? 19.312 -13.010 6.186   1.00 17.72 ?  151 VAL   A HG11 1 
ATOM   3255 H  HG12 . VAL   A 1 151 ? 19.321 -13.952 7.466   1.00 17.72 ?  151 VAL   A HG12 1 
ATOM   3256 H  HG13 . VAL   A 1 151 ? 18.170 -12.872 7.282   1.00 17.72 ?  151 VAL   A HG13 1 
ATOM   3257 H  HG21 . VAL   A 1 151 ? 20.079 -10.629 6.390   1.00 16.56 ?  151 VAL   A HG21 1 
ATOM   3258 H  HG22 . VAL   A 1 151 ? 18.814 -10.415 7.327   1.00 16.56 ?  151 VAL   A HG22 1 
ATOM   3259 H  HG23 . VAL   A 1 151 ? 20.263 -10.013 7.842   1.00 16.56 ?  151 VAL   A HG23 1 
ATOM   3260 N  N    A TYR   A 1 152 ? 18.260 -10.293 10.235  0.50 12.22 ?  152 TYR   A N    1 
ATOM   3261 N  N    B TYR   A 1 152 ? 18.272 -10.274 10.228  0.50 12.01 ?  152 TYR   A N    1 
ATOM   3262 C  CA   A TYR   A 1 152 ? 17.045 -9.571  10.563  0.50 12.24 ?  152 TYR   A CA   1 
ATOM   3263 C  CA   B TYR   A 1 152 ? 17.096 -9.538  10.672  0.50 11.70 ?  152 TYR   A CA   1 
ATOM   3264 C  C    A TYR   A 1 152 ? 16.851 -8.500  9.496   0.50 11.63 ?  152 TYR   A C    1 
ATOM   3265 C  C    B TYR   A 1 152 ? 16.891 -8.394  9.698   0.50 11.30 ?  152 TYR   A C    1 
ATOM   3266 O  O    A TYR   A 1 152 ? 17.610 -7.525  9.438   0.50 11.58 ?  152 TYR   A O    1 
ATOM   3267 O  O    B TYR   A 1 152 ? 17.675 -7.438  9.677   0.50 11.83 ?  152 TYR   A O    1 
ATOM   3268 C  CB   A TYR   A 1 152 ? 17.171 -9.008  11.974  0.50 13.27 ?  152 TYR   A CB   1 
ATOM   3269 C  CB   B TYR   A 1 152 ? 17.305 -9.030  12.095  0.50 12.53 ?  152 TYR   A CB   1 
ATOM   3270 C  CG   A TYR   A 1 152 ? 17.214 -10.120 13.007  0.50 13.99 ?  152 TYR   A CG   1 
ATOM   3271 C  CG   B TYR   A 1 152 ? 17.195 -10.162 13.070  0.50 13.24 ?  152 TYR   A CG   1 
ATOM   3272 C  CD1  A TYR   A 1 152 ? 18.415 -10.715 13.383  0.50 14.63 ?  152 TYR   A CD1  1 
ATOM   3273 C  CD1  B TYR   A 1 152 ? 18.240 -11.055 13.238  0.50 13.88 ?  152 TYR   A CD1  1 
ATOM   3274 C  CD2  A TYR   A 1 152 ? 16.045 -10.610 13.575  0.50 14.45 ?  152 TYR   A CD2  1 
ATOM   3275 C  CD2  B TYR   A 1 152 ? 16.025 -10.380 13.782  0.50 13.21 ?  152 TYR   A CD2  1 
ATOM   3276 C  CE1  A TYR   A 1 152 ? 18.452 -11.751 14.309  0.50 15.68 ?  152 TYR   A CE1  1 
ATOM   3277 C  CE1  B TYR   A 1 152 ? 18.140 -12.121 14.105  0.50 14.43 ?  152 TYR   A CE1  1 
ATOM   3278 C  CE2  A TYR   A 1 152 ? 16.071 -11.650 14.503  0.50 15.59 ?  152 TYR   A CE2  1 
ATOM   3279 C  CE2  B TYR   A 1 152 ? 15.911 -11.448 14.659  0.50 14.32 ?  152 TYR   A CE2  1 
ATOM   3280 C  CZ   A TYR   A 1 152 ? 17.278 -12.211 14.863  0.50 16.24 ?  152 TYR   A CZ   1 
ATOM   3281 C  CZ   B TYR   A 1 152 ? 16.975 -12.316 14.815  0.50 14.54 ?  152 TYR   A CZ   1 
ATOM   3282 O  OH   A TYR   A 1 152 ? 17.319 -13.238 15.784  0.50 18.23 ?  152 TYR   A OH   1 
ATOM   3283 O  OH   B TYR   A 1 152 ? 16.878 -13.387 15.676  0.50 16.02 ?  152 TYR   A OH   1 
ATOM   3284 H  H    A TYR   A 1 152 ? 18.978 -9.832  10.374  0.50 14.67 ?  152 TYR   A H    1 
ATOM   3285 H  H    B TYR   A 1 152 ? 18.988 -9.789  10.269  0.50 14.43 ?  152 TYR   A H    1 
ATOM   3286 H  HA   A TYR   A 1 152 ? 16.294 -10.187 10.534  0.50 14.70 ?  152 TYR   A HA   1 
ATOM   3287 H  HA   B TYR   A 1 152 ? 16.318 -10.111 10.651  0.50 14.06 ?  152 TYR   A HA   1 
ATOM   3288 H  HB2  A TYR   A 1 152 ? 17.991 -8.504  12.046  0.50 15.94 ?  152 TYR   A HB2  1 
ATOM   3289 H  HB2  B TYR   A 1 152 ? 18.188 -8.645  12.177  0.50 15.04 ?  152 TYR   A HB2  1 
ATOM   3290 H  HB3  A TYR   A 1 152 ? 16.409 -8.446  12.164  0.50 15.94 ?  152 TYR   A HB3  1 
ATOM   3291 H  HB3  B TYR   A 1 152 ? 16.624 -8.375  12.310  0.50 15.04 ?  152 TYR   A HB3  1 
ATOM   3292 H  HD1  A TYR   A 1 152 ? 19.208 -10.416 13.013  0.50 17.57 ?  152 TYR   A HD1  1 
ATOM   3293 H  HD1  B TYR   A 1 152 ? 19.025 -10.927 12.755  0.50 16.66 ?  152 TYR   A HD1  1 
ATOM   3294 H  HD2  A TYR   A 1 152 ? 15.226 -10.242 13.336  0.50 17.35 ?  152 TYR   A HD2  1 
ATOM   3295 H  HD2  B TYR   A 1 152 ? 15.303 -9.796  13.675  0.50 15.86 ?  152 TYR   A HD2  1 
ATOM   3296 H  HE1  A TYR   A 1 152 ? 19.263 -12.138 14.557  0.50 18.83 ?  152 TYR   A HE1  1 
ATOM   3297 H  HE1  B TYR   A 1 152 ? 18.858 -12.700 14.209  0.50 17.33 ?  152 TYR   A HE1  1 
ATOM   3298 H  HE2  A TYR   A 1 152 ? 15.277 -11.964 14.881  0.50 18.72 ?  152 TYR   A HE2  1 
ATOM   3299 H  HE2  B TYR   A 1 152 ? 15.125 -11.576 15.140  0.50 17.19 ?  152 TYR   A HE2  1 
ATOM   3300 H  HH   A TYR   A 1 152 ? 16.539 -13.429 16.049  0.50 21.89 ?  152 TYR   A HH   1 
ATOM   3301 H  HH   B TYR   A 1 152 ? 16.150 -13.351 16.086  0.50 19.24 ?  152 TYR   A HH   1 
ATOM   3302 N  N    A LEU   A 1 153 ? 15.866 -8.717  8.625   0.50 11.50 ?  153 LEU   A N    1 
ATOM   3303 N  N    B LEU   A 1 153 ? 15.852 -8.506  8.883   0.50 11.38 ?  153 LEU   A N    1 
ATOM   3304 C  CA   A LEU   A 1 153 ? 15.597 -7.835  7.494   0.50 11.54 ?  153 LEU   A CA   1 
ATOM   3305 C  CA   B LEU   A 1 153 ? 15.594 -7.569  7.803   0.50 11.19 ?  153 LEU   A CA   1 
ATOM   3306 C  C    A LEU   A 1 153 ? 14.604 -6.752  7.892   0.50 11.32 ?  153 LEU   A C    1 
ATOM   3307 C  C    B LEU   A 1 153 ? 14.597 -6.510  8.251   0.50 11.55 ?  153 LEU   A C    1 
ATOM   3308 O  O    A LEU   A 1 153 ? 13.488 -7.054  8.330   0.50 12.69 ?  153 LEU   A O    1 
ATOM   3309 O  O    B LEU   A 1 153 ? 13.510 -6.838  8.742   0.50 12.16 ?  153 LEU   A O    1 
ATOM   3310 C  CB   A LEU   A 1 153 ? 15.026 -8.636  6.327   0.50 11.70 ?  153 LEU   A CB   1 
ATOM   3311 C  CB   B LEU   A 1 153 ? 15.031 -8.311  6.592   0.50 11.10 ?  153 LEU   A CB   1 
ATOM   3312 C  CG   A LEU   A 1 153 ? 15.995 -9.600  5.648   0.50 12.03 ?  153 LEU   A CG   1 
ATOM   3313 C  CG   B LEU   A 1 153 ? 15.927 -9.382  5.972   0.50 11.36 ?  153 LEU   A CG   1 
ATOM   3314 C  CD1  A LEU   A 1 153 ? 15.234 -10.509 4.709   0.50 12.33 ?  153 LEU   A CD1  1 
ATOM   3315 C  CD1  B LEU   A 1 153 ? 15.118 -10.212 4.978   0.50 11.69 ?  153 LEU   A CD1  1 
ATOM   3316 C  CD2  A LEU   A 1 153 ? 17.050 -8.819  4.892   0.50 11.84 ?  153 LEU   A CD2  1 
ATOM   3317 C  CD2  B LEU   A 1 153 ? 17.148 -8.758  5.306   0.50 12.06 ?  153 LEU   A CD2  1 
ATOM   3318 H  H    A LEU   A 1 153 ? 15.325 -9.393  8.673   0.50 13.81 ?  153 LEU   A H    1 
ATOM   3319 H  H    B LEU   A 1 153 ? 15.263 -9.133  8.939   0.50 13.67 ?  153 LEU   A H    1 
ATOM   3320 H  HA   A LEU   A 1 153 ? 16.419 -7.416  7.210   0.50 13.87 ?  153 LEU   A HA   1 
ATOM   3321 H  HA   B LEU   A 1 153 ? 16.421 -7.137  7.555   0.50 13.44 ?  153 LEU   A HA   1 
ATOM   3322 H  HB2  A LEU   A 1 153 ? 14.271 -9.159  6.650   0.50 14.05 ?  153 LEU   A HB2  1 
ATOM   3323 H  HB2  B LEU   A 1 153 ? 14.206 -8.741  6.863   0.50 13.33 ?  153 LEU   A HB2  1 
ATOM   3324 H  HB3  A LEU   A 1 153 ? 14.717 -8.015  5.649   0.50 14.05 ?  153 LEU   A HB3  1 
ATOM   3325 H  HB3  B LEU   A 1 153 ? 14.842 -7.657  5.903   0.50 13.33 ?  153 LEU   A HB3  1 
ATOM   3326 H  HG   A LEU   A 1 153 ? 16.432 -10.152 6.322   0.50 14.45 ?  153 LEU   A HG   1 
ATOM   3327 H  HG   B LEU   A 1 153 ? 16.237 -9.977  6.674   0.50 13.65 ?  153 LEU   A HG   1 
ATOM   3328 H  HD11 A LEU   A 1 153 ? 15.783 -11.279 4.499   0.50 14.82 ?  153 LEU   A HD11 1 
ATOM   3329 H  HD11 B LEU   A 1 153 ? 15.691 -10.889 4.588   0.50 14.04 ?  153 LEU   A HD11 1 
ATOM   3330 H  HD12 A LEU   A 1 153 ? 14.416 -10.799 5.142   0.50 14.82 ?  153 LEU   A HD12 1 
ATOM   3331 H  HD12 B LEU   A 1 153 ? 14.377 -10.634 5.444   0.50 14.04 ?  153 LEU   A HD12 1 
ATOM   3332 H  HD13 A LEU   A 1 153 ? 15.025 -10.017 3.902   0.50 14.82 ?  153 LEU   A HD13 1 
ATOM   3333 H  HD13 B LEU   A 1 153 ? 14.776 -9.627  4.282   0.50 14.04 ?  153 LEU   A HD13 1 
ATOM   3334 H  HD21 A LEU   A 1 153 ? 17.618 -9.442  4.418   0.50 14.22 ?  153 LEU   A HD21 1 
ATOM   3335 H  HD21 B LEU   A 1 153 ? 17.676 -9.462  4.898   0.50 14.49 ?  153 LEU   A HD21 1 
ATOM   3336 H  HD22 A LEU   A 1 153 ? 16.605 -8.229  4.267   0.50 14.22 ?  153 LEU   A HD22 1 
ATOM   3337 H  HD22 B LEU   A 1 153 ? 16.851 -8.131  4.630   0.50 14.49 ?  153 LEU   A HD22 1 
ATOM   3338 H  HD23 A LEU   A 1 153 ? 17.571 -8.308  5.526   0.50 14.22 ?  153 LEU   A HD23 1 
ATOM   3339 H  HD23 B LEU   A 1 153 ? 17.673 -8.297  5.979   0.50 14.49 ?  153 LEU   A HD23 1 
ATOM   3340 N  N    A ALA   A 1 154 ? 14.994 -5.499  7.690   0.50 10.93 ?  154 ALA   A N    1 
ATOM   3341 N  N    B ALA   A 1 154 ? 14.975 -5.246  8.085   0.50 11.32 ?  154 ALA   A N    1 
ATOM   3342 C  CA   A ALA   A 1 154 ? 14.156 -4.347  7.983   0.50 12.09 ?  154 ALA   A CA   1 
ATOM   3343 C  CA   B ALA   A 1 154 ? 14.078 -4.113  8.275   0.50 12.64 ?  154 ALA   A CA   1 
ATOM   3344 C  C    A ALA   A 1 154 ? 13.634 -3.783  6.674   0.50 12.96 ?  154 ALA   A C    1 
ATOM   3345 C  C    B ALA   A 1 154 ? 13.648 -3.613  6.899   0.50 12.99 ?  154 ALA   A C    1 
ATOM   3346 O  O    A ALA   A 1 154 ? 14.418 -3.438  5.781   0.50 13.41 ?  154 ALA   A O    1 
ATOM   3347 O  O    B ALA   A 1 154 ? 14.488 -3.170  6.106   0.50 12.59 ?  154 ALA   A O    1 
ATOM   3348 C  CB   A ALA   A 1 154 ? 14.945 -3.278  8.733   0.50 12.26 ?  154 ALA   A CB   1 
ATOM   3349 C  CB   B ALA   A 1 154 ? 14.782 -3.002  9.058   0.50 12.96 ?  154 ALA   A CB   1 
ATOM   3350 H  H    A ALA   A 1 154 ? 15.757 -5.295  7.361   0.50 13.13 ?  154 ALA   A H    1 
ATOM   3351 H  H    B ALA   A 1 154 ? 15.776 -5.009  7.869   0.50 13.60 ?  154 ALA   A H    1 
ATOM   3352 H  HA   A ALA   A 1 154 ? 13.399 -4.622  8.523   0.50 14.52 ?  154 ALA   A HA   1 
ATOM   3353 H  HA   B ALA   A 1 154 ? 13.295 -4.388  8.779   0.50 15.18 ?  154 ALA   A HA   1 
ATOM   3354 H  HB1  A ALA   A 1 154 ? 14.359 -2.527  8.908   0.50 14.72 ?  154 ALA   A HB1  1 
ATOM   3355 H  HB1  B ALA   A 1 154 ? 14.170 -2.255  9.175   0.50 15.57 ?  154 ALA   A HB1  1 
ATOM   3356 H  HB2  A ALA   A 1 154 ? 15.267 -3.655  9.563   0.50 14.72 ?  154 ALA   A HB2  1 
ATOM   3357 H  HB2  B ALA   A 1 154 ? 15.054 -3.339  9.929   0.50 15.57 ?  154 ALA   A HB2  1 
ATOM   3358 H  HB3  A ALA   A 1 154 ? 15.691 -2.998  8.181   0.50 14.72 ?  154 ALA   A HB3  1 
ATOM   3359 H  HB3  B ALA   A 1 154 ? 15.565 -2.708  8.563   0.50 15.57 ?  154 ALA   A HB3  1 
ATOM   3360 N  N    A VAL   A 1 155 ? 12.315 -3.680  6.572   0.50 14.36 ?  155 VAL   A N    1 
ATOM   3361 N  N    B VAL   A 1 155 ? 12.347 -3.684  6.619   0.50 14.10 ?  155 VAL   A N    1 
ATOM   3362 C  CA   A VAL   A 1 155 ? 11.639 -3.158  5.396   0.50 15.49 ?  155 VAL   A CA   1 
ATOM   3363 C  CA   B VAL   A 1 155 ? 11.772 -3.305  5.328   0.50 14.96 ?  155 VAL   A CA   1 
ATOM   3364 C  C    A VAL   A 1 155 ? 10.933 -1.878  5.815   0.50 16.60 ?  155 VAL   A C    1 
ATOM   3365 C  C    B VAL   A 1 155 ? 11.007 -2.000  5.501   0.50 15.39 ?  155 VAL   A C    1 
ATOM   3366 O  O    A VAL   A 1 155 ? 10.005 -1.913  6.633   0.50 17.19 ?  155 VAL   A O    1 
ATOM   3367 O  O    B VAL   A 1 155 ? 10.031 -1.944  6.261   0.50 16.17 ?  155 VAL   A O    1 
ATOM   3368 C  CB   A VAL   A 1 155 ? 10.660 -4.184  4.812   0.50 15.83 ?  155 VAL   A CB   1 
ATOM   3369 C  CB   B VAL   A 1 155 ? 10.848 -4.402  4.778   0.50 15.30 ?  155 VAL   A CB   1 
ATOM   3370 C  CG1  A VAL   A 1 155 ? 9.930  -3.598  3.625   0.50 16.31 ?  155 VAL   A CG1  1 
ATOM   3371 C  CG1  B VAL   A 1 155 ? 10.182 -3.941  3.479   0.50 15.81 ?  155 VAL   A CG1  1 
ATOM   3372 C  CG2  A VAL   A 1 155 ? 11.417 -5.447  4.410   0.50 16.40 ?  155 VAL   A CG2  1 
ATOM   3373 C  CG2  B VAL   A 1 155 ? 11.630 -5.678  4.556   0.50 16.05 ?  155 VAL   A CG2  1 
ATOM   3374 H  H    A VAL   A 1 155 ? 11.772 -3.915  7.199   0.50 17.25 ?  155 VAL   A H    1 
ATOM   3375 H  H    B VAL   A 1 155 ? 11.762 -3.959  7.185   0.50 16.93 ?  155 VAL   A H    1 
ATOM   3376 H  HA   A VAL   A 1 155 ? 12.288 -2.931  4.718   0.50 18.61 ?  155 VAL   A HA   1 
ATOM   3377 H  HA   B VAL   A 1 155 ? 12.490 -3.162  4.690   0.50 17.96 ?  155 VAL   A HA   1 
ATOM   3378 H  HB   A VAL   A 1 155 ? 10.002 -4.420  5.489   0.50 19.01 ?  155 VAL   A HB   1 
ATOM   3379 H  HB   B VAL   A 1 155 ? 10.150 -4.583  5.430   0.50 18.38 ?  155 VAL   A HB   1 
ATOM   3380 H  HG11 A VAL   A 1 155 ? 9.456  -4.310  3.170   0.50 19.59 ?  155 VAL   A HG11 1 
ATOM   3381 H  HG11 B VAL   A 1 155 ? 9.790  -4.710  3.035   0.50 18.98 ?  155 VAL   A HG11 1 
ATOM   3382 H  HG12 A VAL   A 1 155 ? 9.300  -2.929  3.937   0.50 19.59 ?  155 VAL   A HG12 1 
ATOM   3383 H  HG12 B VAL   A 1 155 ? 9.490  -3.294  3.686   0.50 18.98 ?  155 VAL   A HG12 1 
ATOM   3384 H  HG13 A VAL   A 1 155 ? 10.577 -3.194  3.029   0.50 19.59 ?  155 VAL   A HG13 1 
ATOM   3385 H  HG13 B VAL   A 1 155 ? 10.853 -3.538  2.906   0.50 18.98 ?  155 VAL   A HG13 1 
ATOM   3386 H  HG21 A VAL   A 1 155 ? 10.800 -6.066  3.994   0.50 19.69 ?  155 VAL   A HG21 1 
ATOM   3387 H  HG21 B VAL   A 1 155 ? 11.101 -6.275  4.008   0.50 19.28 ?  155 VAL   A HG21 1 
ATOM   3388 H  HG22 A VAL   A 1 155 ? 12.120 -5.206  3.785   0.50 19.69 ?  155 VAL   A HG22 1 
ATOM   3389 H  HG22 B VAL   A 1 155 ? 12.459 -5.459  4.106   0.50 19.28 ?  155 VAL   A HG22 1 
ATOM   3390 H  HG23 A VAL   A 1 155 ? 11.807 -5.849  5.203   0.50 19.69 ?  155 VAL   A HG23 1 
ATOM   3391 H  HG23 B VAL   A 1 155 ? 11.815 -6.086  5.415   0.50 19.28 ?  155 VAL   A HG23 1 
ATOM   3392 N  N    A PHE   A 1 156 ? 11.386 -0.745  5.266   0.50 16.60 ?  156 PHE   A N    1 
ATOM   3393 N  N    B PHE   A 1 156 ? 11.419 -0.969  4.754   0.50 15.66 ?  156 PHE   A N    1 
ATOM   3394 C  CA   A PHE   A 1 156 ? 10.855 0.556   5.665   0.50 17.16 ?  156 PHE   A CA   1 
ATOM   3395 C  CA   B PHE   A 1 156 ? 10.906 0.384   4.973   0.50 16.16 ?  156 PHE   A CA   1 
ATOM   3396 C  C    A PHE   A 1 156 ? 9.392  0.710   5.274   0.50 16.88 ?  156 PHE   A C    1 
ATOM   3397 C  C    B PHE   A 1 156 ? 9.439  0.518   4.559   0.50 16.43 ?  156 PHE   A C    1 
ATOM   3398 O  O    A PHE   A 1 156 ? 8.587  1.234   6.054   0.50 17.58 ?  156 PHE   A O    1 
ATOM   3399 O  O    B PHE   A 1 156 ? 8.651  1.168   5.259   0.50 17.52 ?  156 PHE   A O    1 
ATOM   3400 C  CB   A PHE   A 1 156 ? 11.697 1.666   5.028   0.50 18.21 ?  156 PHE   A CB   1 
ATOM   3401 C  CB   B PHE   A 1 156 ? 11.796 1.377   4.212   0.50 15.80 ?  156 PHE   A CB   1 
ATOM   3402 C  CG   A PHE   A 1 156 ? 11.177 3.049   5.294   0.50 19.72 ?  156 PHE   A CG   1 
ATOM   3403 C  CG   B PHE   A 1 156 ? 11.479 2.836   4.466   0.50 15.90 ?  156 PHE   A CG   1 
ATOM   3404 C  CD1  A PHE   A 1 156 ? 11.078 3.521   6.588   0.50 20.58 ?  156 PHE   A CD1  1 
ATOM   3405 C  CD1  B PHE   A 1 156 ? 12.045 3.511   5.544   0.50 16.45 ?  156 PHE   A CD1  1 
ATOM   3406 C  CD2  A PHE   A 1 156 ? 10.803 3.881   4.248   0.50 20.63 ?  156 PHE   A CD2  1 
ATOM   3407 C  CD2  B PHE   A 1 156 ? 10.662 3.542   3.600   0.50 16.69 ?  156 PHE   A CD2  1 
ATOM   3408 C  CE1  A PHE   A 1 156 ? 10.604 4.791   6.842   0.50 21.41 ?  156 PHE   A CE1  1 
ATOM   3409 C  CE1  B PHE   A 1 156 ? 11.771 4.854   5.769   0.50 17.04 ?  156 PHE   A CE1  1 
ATOM   3410 C  CE2  A PHE   A 1 156 ? 10.326 5.156   4.494   0.50 21.44 ?  156 PHE   A CE2  1 
ATOM   3411 C  CE2  B PHE   A 1 156 ? 10.384 4.884   3.820   0.50 17.54 ?  156 PHE   A CE2  1 
ATOM   3412 C  CZ   A PHE   A 1 156 ? 10.230 5.613   5.792   0.50 21.62 ?  156 PHE   A CZ   1 
ATOM   3413 C  CZ   B PHE   A 1 156 ? 10.943 5.541   4.907   0.50 17.28 ?  156 PHE   A CZ   1 
ATOM   3414 H  H    A PHE   A 1 156 ? 11.994 -0.703  4.660   0.50 19.93 ?  156 PHE   A H    1 
ATOM   3415 H  H    B PHE   A 1 156 ? 11.996 -1.033  4.113   0.50 18.81 ?  156 PHE   A H    1 
ATOM   3416 H  HA   A PHE   A 1 156 ? 10.919 0.656   6.623   0.50 20.61 ?  156 PHE   A HA   1 
ATOM   3417 H  HA   B PHE   A 1 156 ? 10.978 0.589   5.917   0.50 19.40 ?  156 PHE   A HA   1 
ATOM   3418 H  HB2  A PHE   A 1 156 ? 12.601 1.622   5.381   0.50 21.87 ?  156 PHE   A HB2  1 
ATOM   3419 H  HB2  B PHE   A 1 156 ? 12.718 1.232   4.480   0.50 18.97 ?  156 PHE   A HB2  1 
ATOM   3420 H  HB3  A PHE   A 1 156 ? 11.717 1.541   4.065   0.50 21.87 ?  156 PHE   A HB3  1 
ATOM   3421 H  HB3  B PHE   A 1 156 ? 11.706 1.217   3.261   0.50 18.97 ?  156 PHE   A HB3  1 
ATOM   3422 H  HD1  A PHE   A 1 156 ? 11.331 2.975   7.296   0.50 24.71 ?  156 PHE   A HD1  1 
ATOM   3423 H  HD1  B PHE   A 1 156 ? 12.602 3.045   6.132   0.50 19.76 ?  156 PHE   A HD1  1 
ATOM   3424 H  HD2  A PHE   A 1 156 ? 10.869 3.575   3.371   0.50 24.77 ?  156 PHE   A HD2  1 
ATOM   3425 H  HD2  B PHE   A 1 156 ? 10.286 3.106   2.872   0.50 20.04 ?  156 PHE   A HD2  1 
ATOM   3426 H  HE1  A PHE   A 1 156 ? 10.539 5.099   7.717   0.50 25.70 ?  156 PHE   A HE1  1 
ATOM   3427 H  HE1  B PHE   A 1 156 ? 12.147 5.281   6.504   0.50 20.46 ?  156 PHE   A HE1  1 
ATOM   3428 H  HE2  A PHE   A 1 156 ? 10.076 5.703   3.784   0.50 25.74 ?  156 PHE   A HE2  1 
ATOM   3429 H  HE2  B PHE   A 1 156 ? 9.826  5.343   3.239   0.50 21.06 ?  156 PHE   A HE2  1 
ATOM   3430 H  HZ   A PHE   A 1 156 ? 9.909  6.469   5.961   0.50 25.95 ?  156 PHE   A HZ   1 
ATOM   3431 H  HZ   B PHE   A 1 156 ? 10.756 6.437   5.060   0.50 20.75 ?  156 PHE   A HZ   1 
ATOM   3432 N  N    A ASP   A 1 157 ? 9.034  0.280   4.068   0.50 16.50 ?  157 ASP   A N    1 
ATOM   3433 N  N    B ASP   A 1 157 ? 9.054  -0.078  3.431   0.50 16.80 ?  157 ASP   A N    1 
ATOM   3434 C  CA   A ASP   A 1 157 ? 7.710  0.527   3.512   0.50 17.22 ?  157 ASP   A CA   1 
ATOM   3435 C  CA   B ASP   A 1 157 ? 7.742  0.159   2.832   0.50 17.66 ?  157 ASP   A CA   1 
ATOM   3436 C  C    A ASP   A 1 157 ? 6.739  -0.532  4.019   0.50 17.20 ?  157 ASP   A C    1 
ATOM   3437 C  C    B ASP   A 1 157 ? 6.707  -0.853  3.321   0.50 17.75 ?  157 ASP   A C    1 
ATOM   3438 O  O    A ASP   A 1 157 ? 6.950  -1.727  3.795   0.50 16.59 ?  157 ASP   A O    1 
ATOM   3439 O  O    B ASP   A 1 157 ? 6.904  -2.063  3.193   0.50 17.64 ?  157 ASP   A O    1 
ATOM   3440 C  CB   A ASP   A 1 157 ? 7.795  0.468   1.991   0.50 18.08 ?  157 ASP   A CB   1 
ATOM   3441 C  CB   B ASP   A 1 157 ? 7.846  0.078   1.310   0.50 18.56 ?  157 ASP   A CB   1 
ATOM   3442 C  CG   A ASP   A 1 157 ? 6.556  1.004   1.325   0.50 19.65 ?  157 ASP   A CG   1 
ATOM   3443 C  CG   B ASP   A 1 157 ? 6.587  0.550   0.608   0.50 19.21 ?  157 ASP   A CG   1 
ATOM   3444 O  OD1  A ASP   A 1 157 ? 6.452  2.240   1.179   0.50 21.13 ?  157 ASP   A OD1  1 
ATOM   3445 O  OD1  B ASP   A 1 157 ? 6.324  1.768   0.623   0.50 20.03 ?  157 ASP   A OD1  1 
ATOM   3446 O  OD2  A ASP   A 1 157 ? 5.677  0.196   0.963   0.50 19.88 -1 157 ASP   A OD2  1 
ATOM   3447 O  OD2  B ASP   A 1 157 ? 5.865  -0.292  0.031   0.50 19.13 -1 157 ASP   A OD2  1 
ATOM   3448 H  H    A ASP   A 1 157 ? 9.543  -0.169  3.547   0.50 19.81 ?  157 ASP   A H    1 
ATOM   3449 H  H    B ASP   A 1 157 ? 9.542  -0.631  2.990   0.50 20.17 ?  157 ASP   A H    1 
ATOM   3450 H  HA   A ASP   A 1 157 ? 7.385  1.405   3.770   0.50 20.68 ?  157 ASP   A HA   1 
ATOM   3451 H  HA   B ASP   A 1 157 ? 7.438  1.047   3.078   0.50 21.21 ?  157 ASP   A HA   1 
ATOM   3452 H  HB2  A ASP   A 1 157 ? 8.535  1.008   1.685   0.50 21.71 ?  157 ASP   A HB2  1 
ATOM   3453 H  HB2  B ASP   A 1 157 ? 8.591  0.621   1.021   0.50 22.29 ?  157 ASP   A HB2  1 
ATOM   3454 H  HB3  A ASP   A 1 157 ? 7.925  -0.456  1.712   0.50 21.71 ?  157 ASP   A HB3  1 
ATOM   3455 H  HB3  B ASP   A 1 157 ? 7.981  -0.844  1.056   0.50 22.29 ?  157 ASP   A HB3  1 
ATOM   3456 N  N    A LYS   A 1 158 ? 5.661  -0.100  4.681   0.50 17.88 ?  158 LYS   A N    1 
ATOM   3457 N  N    B LYS   A 1 158 ? 5.580  -0.338  3.825   0.50 18.39 ?  158 LYS   A N    1 
ATOM   3458 C  CA   A LYS   A 1 158 ? 4.708  -1.058  5.237   0.50 18.71 ?  158 LYS   A CA   1 
ATOM   3459 C  CA   B LYS   A 1 158 ? 4.526  -1.171  4.406   0.50 20.08 ?  158 LYS   A CA   1 
ATOM   3460 C  C    A LYS   A 1 158 ? 3.977  -1.816  4.139   0.50 18.62 ?  158 LYS   A C    1 
ATOM   3461 C  C    B LYS   A 1 158 ? 3.932  -2.132  3.380   0.50 19.16 ?  158 LYS   A C    1 
ATOM   3462 O  O    A LYS   A 1 158 ? 3.764  -3.029  4.252   0.50 18.98 ?  158 LYS   A O    1 
ATOM   3463 O  O    B LYS   A 1 158 ? 3.844  -3.345  3.616   0.50 19.08 ?  158 LYS   A O    1 
ATOM   3464 C  CB   A LYS   A 1 158 ? 3.709  -0.345  6.148   0.50 19.42 ?  158 LYS   A CB   1 
ATOM   3465 C  CB   B LYS   A 1 158 ? 3.420  -0.256  4.941   0.50 22.80 ?  158 LYS   A CB   1 
ATOM   3466 C  CG   A LYS   A 1 158 ? 2.474  -1.178  6.509   0.50 20.14 ?  158 LYS   A CG   1 
ATOM   3467 C  CG   B LYS   A 1 158 ? 3.428  -0.014  6.435   0.50 25.72 ?  158 LYS   A CG   1 
ATOM   3468 C  CD   A LYS   A 1 158 ? 2.833  -2.434  7.299   0.50 20.35 ?  158 LYS   A CD   1 
ATOM   3469 C  CD   B LYS   A 1 158 ? 2.454  -0.949  7.127   0.50 27.85 ?  158 LYS   A CD   1 
ATOM   3470 C  CE   A LYS   A 1 158 ? 1.578  -3.178  7.743   0.50 20.49 ?  158 LYS   A CE   1 
ATOM   3471 C  CE   B LYS   A 1 158 ? 2.384  -0.695  8.621   0.50 29.33 ?  158 LYS   A CE   1 
ATOM   3472 N  NZ   A LYS   A 1 158 ? 1.894  -4.484  8.385   0.50 20.45 ?  158 LYS   A NZ   1 
ATOM   3473 N  NZ   B LYS   A 1 158 ? 1.715  -1.825  9.320   0.50 30.21 ?  158 LYS   A NZ   1 
ATOM   3474 H  H    A LYS   A 1 158 ? 5.461  0.727   4.810   0.50 21.47 ?  158 LYS   A H    1 
ATOM   3475 H  H    B LYS   A 1 158 ? 5.405  0.502   3.838   0.50 22.08 ?  158 LYS   A H    1 
ATOM   3476 H  HA   A LYS   A 1 158 ? 5.186  -1.701  5.775   0.50 22.47 ?  158 LYS   A HA   1 
ATOM   3477 H  HA   B LYS   A 1 158 ? 4.884  -1.684  5.149   0.50 24.11 ?  158 LYS   A HA   1 
ATOM   3478 H  HB2  A LYS   A 1 158 ? 4.151  -0.112  6.981   0.50 23.32 ?  158 LYS   A HB2  1 
ATOM   3479 H  HB2  B LYS   A 1 158 ? 3.496  0.612   4.512   0.50 27.37 ?  158 LYS   A HB2  1 
ATOM   3480 H  HB3  A LYS   A 1 158 ? 3.396  0.463   5.710   0.50 23.32 ?  158 LYS   A HB3  1 
ATOM   3481 H  HB3  B LYS   A 1 158 ? 2.563  -0.648  4.721   0.50 27.37 ?  158 LYS   A HB3  1 
ATOM   3482 H  HG2  A LYS   A 1 158 ? 1.885  -0.641  7.062   0.50 24.18 ?  158 LYS   A HG2  1 
ATOM   3483 H  HG2  B LYS   A 1 158 ? 4.318  -0.171  6.781   0.50 30.88 ?  158 LYS   A HG2  1 
ATOM   3484 H  HG3  A LYS   A 1 158 ? 2.000  -1.446  5.703   0.50 24.18 ?  158 LYS   A HG3  1 
ATOM   3485 H  HG3  B LYS   A 1 158 ? 3.156  0.901   6.617   0.50 30.88 ?  158 LYS   A HG3  1 
ATOM   3486 H  HD2  A LYS   A 1 158 ? 3.357  -3.028  6.744   0.50 24.43 ?  158 LYS   A HD2  1 
ATOM   3487 H  HD2  B LYS   A 1 158 ? 1.566  -0.814  6.756   0.50 33.44 ?  158 LYS   A HD2  1 
ATOM   3488 H  HD3  A LYS   A 1 158 ? 3.331  -2.181  8.092   0.50 24.43 ?  158 LYS   A HD3  1 
ATOM   3489 H  HD3  B LYS   A 1 158 ? 2.738  -1.865  6.987   0.50 33.44 ?  158 LYS   A HD3  1 
ATOM   3490 H  HE2  A LYS   A 1 158 ? 1.095  -2.637  8.388   0.50 24.60 ?  158 LYS   A HE2  1 
ATOM   3491 H  HE2  B LYS   A 1 158 ? 3.281  -0.601  8.976   0.50 35.21 ?  158 LYS   A HE2  1 
ATOM   3492 H  HE3  A LYS   A 1 158 ? 1.018  -3.352  6.970   0.50 24.60 ?  158 LYS   A HE3  1 
ATOM   3493 H  HE3  B LYS   A 1 158 ? 1.871  0.113   8.785   0.50 35.21 ?  158 LYS   A HE3  1 
ATOM   3494 H  HZ1  A LYS   A 1 158 ? 1.140  -4.894  8.633   0.50 24.56 ?  158 LYS   A HZ1  1 
ATOM   3495 H  HZ1  B LYS   A 1 158 ? 1.618  -1.634  10.183  0.50 36.27 ?  158 LYS   A HZ1  1 
ATOM   3496 H  HZ2  A LYS   A 1 158 ? 2.330  -5.009  7.814   0.50 24.56 ?  158 LYS   A HZ2  1 
ATOM   3497 H  HZ2  B LYS   A 1 158 ? 0.913  -1.970  8.962   0.50 36.27 ?  158 LYS   A HZ2  1 
ATOM   3498 H  HZ3  A LYS   A 1 158 ? 2.400  -4.357  9.106   0.50 24.56 ?  158 LYS   A HZ3  1 
ATOM   3499 H  HZ3  B LYS   A 1 158 ? 2.205  -2.564  9.239   0.50 36.27 ?  158 LYS   A HZ3  1 
ATOM   3500 N  N    A ASN   A 1 159 ? 3.557  -1.117  3.083   0.50 18.62 ?  159 ASN   A N    1 
ATOM   3501 N  N    B ASN   A 1 159 ? 3.462  -1.597  2.251   0.50 19.41 ?  159 ASN   A N    1 
ATOM   3502 C  CA   A ASN   A 1 159 ? 2.888  -1.801  1.982   0.50 19.21 ?  159 ASN   A CA   1 
ATOM   3503 C  CA   B ASN   A 1 159 ? 2.835  -2.458  1.255   0.50 19.61 ?  159 ASN   A CA   1 
ATOM   3504 C  C    A ASN   A 1 159 ? 3.788  -2.877  1.388   0.50 18.54 ?  159 ASN   A C    1 
ATOM   3505 C  C    B ASN   A 1 159 ? 3.822  -3.484  0.715   0.50 18.21 ?  159 ASN   A C    1 
ATOM   3506 O  O    A ASN   A 1 159 ? 3.342  -4.005  1.148   0.50 17.83 ?  159 ASN   A O    1 
ATOM   3507 O  O    B ASN   A 1 159 ? 3.432  -4.610  0.382   0.50 18.39 ?  159 ASN   A O    1 
ATOM   3508 C  CB   A ASN   A 1 159 ? 2.452  -0.793  0.916   0.50 20.42 ?  159 ASN   A CB   1 
ATOM   3509 C  CB   B ASN   A 1 159 ? 2.210  -1.616  0.140   0.50 21.55 ?  159 ASN   A CB   1 
ATOM   3510 C  CG   A ASN   A 1 159 ? 1.188  -0.043  1.304   0.50 22.70 ?  159 ASN   A CG   1 
ATOM   3511 C  CG   B ASN   A 1 159 ? 0.917  -0.956  0.573   0.50 23.77 ?  159 ASN   A CG   1 
ATOM   3512 O  OD1  A ASN   A 1 159 ? 0.292  -0.604  1.936   0.50 24.03 ?  159 ASN   A OD1  1 
ATOM   3513 O  OD1  B ASN   A 1 159 ? 0.785  -0.514  1.715   0.50 25.17 ?  159 ASN   A OD1  1 
ATOM   3514 N  ND2  A ASN   A 1 159 ? 1.106  1.226   0.922   0.50 23.26 ?  159 ASN   A ND2  1 
ATOM   3515 N  ND2  B ASN   A 1 159 ? -0.049 -0.891  -0.337  0.50 24.76 ?  159 ASN   A ND2  1 
ATOM   3516 H  H    A ASN   A 1 159 ? 3.645  -0.268  2.980   0.50 22.35 ?  159 ASN   A H    1 
ATOM   3517 H  H    B ASN   A 1 159 ? 3.489  -0.759  2.051   0.50 23.30 ?  159 ASN   A H    1 
ATOM   3518 H  HA   A ASN   A 1 159 ? 2.088  -2.238  2.318   0.50 23.06 ?  159 ASN   A HA   1 
ATOM   3519 H  HA   B ASN   A 1 159 ? 2.114  -2.941  1.684   0.50 23.55 ?  159 ASN   A HA   1 
ATOM   3520 H  HB2  A ASN   A 1 159 ? 3.153  -0.139  0.787   0.50 24.52 ?  159 ASN   A HB2  1 
ATOM   3521 H  HB2  B ASN   A 1 159 ? 2.825  -0.913  -0.118  0.50 25.88 ?  159 ASN   A HB2  1 
ATOM   3522 H  HB3  A ASN   A 1 159 ? 2.276  -1.263  0.083   0.50 24.52 ?  159 ASN   A HB3  1 
ATOM   3523 H  HB3  B ASN   A 1 159 ? 2.012  -2.185  -0.616  0.50 25.88 ?  159 ASN   A HB3  1 
ATOM   3524 H  HD21 A ASN   A 1 159 ? 0.408  1.689   1.117   0.50 27.93 ?  159 ASN   A HD21 1 
ATOM   3525 H  HD21 B ASN   A 1 159 ? -0.808 -0.529  -0.141  0.50 29.72 ?  159 ASN   A HD21 1 
ATOM   3526 H  HD22 A ASN   A 1 159 ? 1.752  1.583   0.483   0.50 27.93 ?  159 ASN   A HD22 1 
ATOM   3527 H  HD22 B ASN   A 1 159 ? 0.077  -1.216  -1.123  0.50 29.72 ?  159 ASN   A HD22 1 
ATOM   3528 N  N    A LEU   A 1 160 ? 5.064  -2.557  1.170   0.50 18.28 ?  160 LEU   A N    1 
ATOM   3529 N  N    B LEU   A 1 160 ? 5.108  -3.129  0.651   0.50 17.50 ?  160 LEU   A N    1 
ATOM   3530 C  CA   A LEU   A 1 160 ? 5.974  -3.535  0.586   0.50 18.14 ?  160 LEU   A CA   1 
ATOM   3531 C  CA   B LEU   A 1 160 ? 6.120  -4.120  0.303   0.50 17.45 ?  160 LEU   A CA   1 
ATOM   3532 C  C    A LEU   A 1 160 ? 6.147  -4.735  1.503   0.50 17.84 ?  160 LEU   A C    1 
ATOM   3533 C  C    B LEU   A 1 160 ? 6.289  -5.151  1.419   0.50 17.54 ?  160 LEU   A C    1 
ATOM   3534 O  O    A LEU   A 1 160 ? 6.175  -5.882  1.041   0.50 18.39 ?  160 LEU   A O    1 
ATOM   3535 O  O    B LEU   A 1 160 ? 6.308  -6.358  1.154   0.50 17.81 ?  160 LEU   A O    1 
ATOM   3536 C  CB   A LEU   A 1 160 ? 7.324  -2.888  0.291   0.50 17.97 ?  160 LEU   A CB   1 
ATOM   3537 C  CB   B LEU   A 1 160 ? 7.451  -3.443  -0.031  0.50 17.46 ?  160 LEU   A CB   1 
ATOM   3538 C  CG   A LEU   A 1 160 ? 8.373  -3.905  -0.152  0.50 17.93 ?  160 LEU   A CG   1 
ATOM   3539 C  CG   B LEU   A 1 160 ? 8.549  -4.413  -0.482  0.50 17.75 ?  160 LEU   A CG   1 
ATOM   3540 C  CD1  A LEU   A 1 160 ? 7.888  -4.668  -1.377  0.50 18.59 ?  160 LEU   A CD1  1 
ATOM   3541 C  CD1  B LEU   A 1 160 ? 8.106  -5.173  -1.719  0.50 18.23 ?  160 LEU   A CD1  1 
ATOM   3542 C  CD2  A LEU   A 1 160 ? 9.698  -3.232  -0.423  0.50 17.64 ?  160 LEU   A CD2  1 
ATOM   3543 C  CD2  B LEU   A 1 160 ? 9.865  -3.689  -0.733  0.50 18.06 ?  160 LEU   A CD2  1 
ATOM   3544 H  H    A LEU   A 1 160 ? 5.418  -1.798  1.359   0.50 21.95 ?  160 LEU   A H    1 
ATOM   3545 H  H    B LEU   A 1 160 ? 5.407  -2.340  0.800   0.50 21.01 ?  160 LEU   A H    1 
ATOM   3546 H  HA   A LEU   A 1 160 ? 5.598  -3.849  -0.246  0.50 21.78 ?  160 LEU   A HA   1 
ATOM   3547 H  HA   B LEU   A 1 160 ? 5.818  -4.592  -0.489  0.50 20.95 ?  160 LEU   A HA   1 
ATOM   3548 H  HB2  A LEU   A 1 160 ? 7.216  -2.230  -0.418  0.50 21.58 ?  160 LEU   A HB2  1 
ATOM   3549 H  HB2  B LEU   A 1 160 ? 7.305  -2.801  -0.745  0.50 20.97 ?  160 LEU   A HB2  1 
ATOM   3550 H  HB3  A LEU   A 1 160 ? 7.650  -2.460  1.096   0.50 21.58 ?  160 LEU   A HB3  1 
ATOM   3551 H  HB3  B LEU   A 1 160 ? 7.771  -2.988  0.761   0.50 20.97 ?  160 LEU   A HB3  1 
ATOM   3552 H  HG   A LEU   A 1 160 ? 8.518  -4.548  0.560   0.50 21.53 ?  160 LEU   A HG   1 
ATOM   3553 H  HG   B LEU   A 1 160 ? 8.699  -5.061  0.221   0.50 21.32 ?  160 LEU   A HG   1 
ATOM   3554 H  HD11 A LEU   A 1 160 ? 8.606  -5.234  -1.694  0.50 22.32 ?  160 LEU   A HD11 1 
ATOM   3555 H  HD11 B LEU   A 1 160 ? 8.869  -5.632  -2.093  0.50 21.89 ?  160 LEU   A HD11 1 
ATOM   3556 H  HD12 A LEU   A 1 160 ? 7.124  -5.218  -1.136  0.50 22.32 ?  160 LEU   A HD12 1 
ATOM   3557 H  HD12 B LEU   A 1 160 ? 7.421  -5.813  -1.469  0.50 21.89 ?  160 LEU   A HD12 1 
ATOM   3558 H  HD13 A LEU   A 1 160 ? 7.635  -4.034  -2.066  0.50 22.32 ?  160 LEU   A HD13 1 
ATOM   3559 H  HD13 B LEU   A 1 160 ? 7.748  -4.540  -2.365  0.50 21.89 ?  160 LEU   A HD13 1 
ATOM   3560 H  HD21 A LEU   A 1 160 ? 10.340 -3.907  -0.698  0.50 21.19 ?  160 LEU   A HD21 1 
ATOM   3561 H  HD21 B LEU   A 1 160 ? 10.532 -4.338  -1.010  0.50 21.68 ?  160 LEU   A HD21 1 
ATOM   3562 H  HD22 A LEU   A 1 160 ? 9.581  -2.579  -1.127  0.50 21.19 ?  160 LEU   A HD22 1 
ATOM   3563 H  HD22 B LEU   A 1 160 ? 9.735  -3.029  -1.431  0.50 21.68 ?  160 LEU   A HD22 1 
ATOM   3564 H  HD23 A LEU   A 1 160 ? 10.001 -2.799  0.389   0.50 21.19 ?  160 LEU   A HD23 1 
ATOM   3565 H  HD23 B LEU   A 1 160 ? 10.147 -3.255  0.087   0.50 21.68 ?  160 LEU   A HD23 1 
ATOM   3566 N  N    A TYR   A 1 161 ? 6.261  -4.490  2.806   0.50 18.02 ?  161 TYR   A N    1 
ATOM   3567 N  N    B TYR   A 1 161 ? 6.413  -4.699  2.676   0.50 17.70 ?  161 TYR   A N    1 
ATOM   3568 C  CA   A TYR   A 1 161 ? 6.437  -5.583  3.753   0.50 18.03 ?  161 TYR   A CA   1 
ATOM   3569 C  CA   B TYR   A 1 161 ? 6.493  -5.645  3.794   0.50 17.51 ?  161 TYR   A CA   1 
ATOM   3570 C  C    A TYR   A 1 161 ? 5.315  -6.610  3.634   0.50 18.45 ?  161 TYR   A C    1 
ATOM   3571 C  C    B TYR   A 1 161 ? 5.298  -6.586  3.791   0.50 18.63 ?  161 TYR   A C    1 
ATOM   3572 O  O    A TYR   A 1 161 ? 5.567  -7.819  3.574   0.50 18.27 ?  161 TYR   A O    1 
ATOM   3573 O  O    B TYR   A 1 161 ? 5.452  -7.809  3.876   0.50 18.47 ?  161 TYR   A O    1 
ATOM   3574 C  CB   A TYR   A 1 161 ? 6.509  -5.012  5.165   0.50 18.55 ?  161 TYR   A CB   1 
ATOM   3575 C  CB   B TYR   A 1 161 ? 6.587  -4.922  5.147   0.50 17.26 ?  161 TYR   A CB   1 
ATOM   3576 C  CG   A TYR   A 1 161 ? 6.390  -6.055  6.231   0.50 18.45 ?  161 TYR   A CG   1 
ATOM   3577 C  CG   B TYR   A 1 161 ? 6.439  -5.852  6.362   0.50 16.34 ?  161 TYR   A CG   1 
ATOM   3578 C  CD1  A TYR   A 1 161 ? 7.494  -6.791  6.628   0.50 18.34 ?  161 TYR   A CD1  1 
ATOM   3579 C  CD1  B TYR   A 1 161 ? 7.530  -6.547  6.879   0.50 15.87 ?  161 TYR   A CD1  1 
ATOM   3580 C  CD2  A TYR   A 1 161 ? 5.169  -6.312  6.839   0.50 18.39 ?  161 TYR   A CD2  1 
ATOM   3581 C  CD2  B TYR   A 1 161 ? 5.210  -6.001  7.011   0.50 15.92 ?  161 TYR   A CD2  1 
ATOM   3582 C  CE1  A TYR   A 1 161 ? 7.387  -7.749  7.599   0.50 18.04 ?  161 TYR   A CE1  1 
ATOM   3583 C  CE1  B TYR   A 1 161 ? 7.395  -7.388  7.987   0.50 15.91 ?  161 TYR   A CE1  1 
ATOM   3584 C  CE2  A TYR   A 1 161 ? 5.052  -7.269  7.812   0.50 18.11 ?  161 TYR   A CE2  1 
ATOM   3585 C  CE2  B TYR   A 1 161 ? 5.071  -6.835  8.124   0.50 15.90 ?  161 TYR   A CE2  1 
ATOM   3586 C  CZ   A TYR   A 1 161 ? 6.167  -7.984  8.189   0.50 18.01 ?  161 TYR   A CZ   1 
ATOM   3587 C  CZ   B TYR   A 1 161 ? 6.166  -7.525  8.605   0.50 16.23 ?  161 TYR   A CZ   1 
ATOM   3588 O  OH   A TYR   A 1 161 ? 6.072  -8.941  9.165   0.50 18.01 ?  161 TYR   A OH   1 
ATOM   3589 O  OH   B TYR   A 1 161 ? 6.036  -8.361  9.703   0.50 17.00 ?  161 TYR   A OH   1 
ATOM   3590 H  H    A TYR   A 1 161 ? 6.235  -3.711  3.168   0.50 21.63 ?  161 TYR   A H    1 
ATOM   3591 H  H    B TYR   A 1 161 ? 6.445  -3.875  2.899   0.50 21.26 ?  161 TYR   A H    1 
ATOM   3592 H  HA   A TYR   A 1 161 ? 7.269  -6.037  3.571   0.50 21.65 ?  161 TYR   A HA   1 
ATOM   3593 H  HA   B TYR   A 1 161 ? 7.287  -6.182  3.695   0.50 21.03 ?  161 TYR   A HA   1 
ATOM   3594 H  HB2  A TYR   A 1 161 ? 7.364  -4.570  5.278   0.50 22.27 ?  161 TYR   A HB2  1 
ATOM   3595 H  HB2  B TYR   A 1 161 ? 7.453  -4.491  5.212   0.50 20.73 ?  161 TYR   A HB2  1 
ATOM   3596 H  HB3  A TYR   A 1 161 ? 5.787  -4.377  5.287   0.50 22.27 ?  161 TYR   A HB3  1 
ATOM   3597 H  HB3  B TYR   A 1 161 ? 5.885  -4.252  5.199   0.50 20.73 ?  161 TYR   A HB3  1 
ATOM   3598 H  HD1  A TYR   A 1 161 ? 8.317  -6.634  6.227   0.50 22.03 ?  161 TYR   A HD1  1 
ATOM   3599 H  HD1  B TYR   A 1 161 ? 8.357  -6.460  6.475   0.50 19.06 ?  161 TYR   A HD1  1 
ATOM   3600 H  HD2  A TYR   A 1 161 ? 4.415  -5.828  6.582   0.50 22.08 ?  161 TYR   A HD2  1 
ATOM   3601 H  HD2  B TYR   A 1 161 ? 4.463  -5.540  6.703   0.50 19.12 ?  161 TYR   A HD2  1 
ATOM   3602 H  HE1  A TYR   A 1 161 ? 8.131  -8.240  7.857   0.50 21.66 ?  161 TYR   A HE1  1 
ATOM   3603 H  HE1  B TYR   A 1 161 ? 8.134  -7.849  8.318   0.50 19.11 ?  161 TYR   A HE1  1 
ATOM   3604 H  HE2  A TYR   A 1 161 ? 4.225  -7.434  8.213   0.50 21.74 ?  161 TYR   A HE2  1 
ATOM   3605 H  HE2  B TYR   A 1 161 ? 4.239  -6.928  8.546   0.50 19.10 ?  161 TYR   A HE2  1 
ATOM   3606 H  HH   A TYR   A 1 161 ? 5.277  -8.991  9.445   0.50 21.63 ?  161 TYR   A HH   1 
ATOM   3607 H  HH   B TYR   A 1 161 ? 5.238  -8.354  9.988   0.50 20.42 ?  161 TYR   A HH   1 
ATOM   3608 N  N    A ASP   A 1 162 ? 4.063  -6.147  3.593   0.50 19.15 ?  162 ASP   A N    1 
ATOM   3609 N  N    B ASP   A 1 162 ? 4.090  -6.024  3.708   0.50 20.00 ?  162 ASP   A N    1 
ATOM   3610 C  CA   A ASP   A 1 162 ? 2.931  -7.071  3.541   0.50 19.41 ?  162 ASP   A CA   1 
ATOM   3611 C  CA   B ASP   A 1 162 ? 2.890  -6.851  3.642   0.50 21.29 ?  162 ASP   A CA   1 
ATOM   3612 C  C    A ASP   A 1 162 ? 2.964  -7.912  2.269   0.50 19.54 ?  162 ASP   A C    1 
ATOM   3613 C  C    B ASP   A 1 162 ? 2.941  -7.800  2.450   0.50 21.53 ?  162 ASP   A C    1 
ATOM   3614 O  O    A ASP   A 1 162 ? 2.614  -9.100  2.289   0.50 19.72 ?  162 ASP   A O    1 
ATOM   3615 O  O    B ASP   A 1 162 ? 2.533  -8.964  2.554   0.50 21.91 ?  162 ASP   A O    1 
ATOM   3616 C  CB   A ASP   A 1 162 ? 1.608  -6.299  3.633   0.50 19.93 ?  162 ASP   A CB   1 
ATOM   3617 C  CB   B ASP   A 1 162 ? 1.646  -5.961  3.553   0.50 22.58 ?  162 ASP   A CB   1 
ATOM   3618 C  CG   A ASP   A 1 162 ? 1.323  -5.753  5.027   0.50 20.59 ?  162 ASP   A CG   1 
ATOM   3619 C  CG   B ASP   A 1 162 ? 1.359  -5.210  4.842   0.50 23.89 ?  162 ASP   A CG   1 
ATOM   3620 O  OD1  A ASP   A 1 162 ? 2.047  -6.107  5.979   0.50 21.48 ?  162 ASP   A OD1  1 
ATOM   3621 O  OD1  B ASP   A 1 162 ? 1.932  -5.564  5.891   0.50 24.45 ?  162 ASP   A OD1  1 
ATOM   3622 O  OD2  A ASP   A 1 162 ? 0.347  -4.970  5.164   0.50 20.94 -1 162 ASP   A OD2  1 
ATOM   3623 O  OD2  B ASP   A 1 162 ? 0.546  -4.263  4.802   0.50 24.58 -1 162 ASP   A OD2  1 
ATOM   3624 H  H    A ASP   A 1 162 ? 3.838  -5.322  3.586   0.50 23.00 ?  162 ASP   A H    1 
ATOM   3625 H  H    B ASP   A 1 162 ? 3.939  -5.178  3.697   0.50 24.02 ?  162 ASP   A H    1 
ATOM   3626 H  HA   A ASP   A 1 162 ? 2.970  -7.684  4.289   0.50 23.30 ?  162 ASP   A HA   1 
ATOM   3627 H  HA   B ASP   A 1 162 ? 2.816  -7.383  4.450   0.50 25.56 ?  162 ASP   A HA   1 
ATOM   3628 H  HB2  A ASP   A 1 162 ? 1.632  -5.551  3.022   0.50 23.93 ?  162 ASP   A HB2  1 
ATOM   3629 H  HB2  B ASP   A 1 162 ? 1.769  -5.308  2.848   0.50 27.11 ?  162 ASP   A HB2  1 
ATOM   3630 H  HB3  A ASP   A 1 162 ? 0.871  -6.891  3.409   0.50 23.93 ?  162 ASP   A HB3  1 
ATOM   3631 H  HB3  B ASP   A 1 162 ? 0.870  -6.511  3.367   0.50 27.11 ?  162 ASP   A HB3  1 
ATOM   3632 N  N    A LYS   A 1 163 ? 3.373  -7.312  1.149   0.50 20.13 ?  163 LYS   A N    1 
ATOM   3633 N  N    B LYS   A 1 163 ? 3.440  -7.323  1.306   0.50 22.21 ?  163 LYS   A N    1 
ATOM   3634 C  CA   A LYS   A 1 163 ? 3.477  -8.068  -0.096  0.50 20.53 ?  163 LYS   A CA   1 
ATOM   3635 C  CA   B LYS   A 1 163 ? 3.486  -8.164  0.113   0.50 22.47 ?  163 LYS   A CA   1 
ATOM   3636 C  C    A LYS   A 1 163 ? 4.580  -9.115  -0.016  0.50 19.59 ?  163 LYS   A C    1 
ATOM   3637 C  C    B LYS   A 1 163 ? 4.561  -9.240  0.229   0.50 21.48 ?  163 LYS   A C    1 
ATOM   3638 O  O    A LYS   A 1 163 ? 4.447  -10.210 -0.574  0.50 19.75 ?  163 LYS   A O    1 
ATOM   3639 O  O    B LYS   A 1 163 ? 4.333  -10.396 -0.149  0.50 21.91 ?  163 LYS   A O    1 
ATOM   3640 C  CB   A LYS   A 1 163 ? 3.732  -7.116  -1.263  0.50 22.93 ?  163 LYS   A CB   1 
ATOM   3641 C  CB   B LYS   A 1 163 ? 3.694  -7.297  -1.131  0.50 24.71 ?  163 LYS   A CB   1 
ATOM   3642 C  CG   A LYS   A 1 163 ? 3.723  -7.803  -2.615  0.50 25.19 ?  163 LYS   A CG   1 
ATOM   3643 C  CG   B LYS   A 1 163 ? 3.782  -8.079  -2.433  0.50 26.81 ?  163 LYS   A CG   1 
ATOM   3644 C  CD   A LYS   A 1 163 ? 4.128  -6.857  -3.728  0.50 27.34 ?  163 LYS   A CD   1 
ATOM   3645 C  CD   B LYS   A 1 163 ? 3.693  -7.160  -3.643  0.50 28.88 ?  163 LYS   A CD   1 
ATOM   3646 C  CE   A LYS   A 1 163 ? 4.012  -7.532  -5.084  0.50 29.14 ?  163 LYS   A CE   1 
ATOM   3647 C  CE   B LYS   A 1 163 ? 5.024  -7.058  -4.368  0.50 30.45 ?  163 LYS   A CE   1 
ATOM   3648 N  NZ   A LYS   A 1 163 ? 4.642  -6.732  -6.165  0.50 30.20 ?  163 LYS   A NZ   1 
ATOM   3649 N  NZ   B LYS   A 1 163 ? 4.914  -6.289  -5.639  0.50 31.46 ?  163 LYS   A NZ   1 
ATOM   3650 H  H    A LYS   A 1 163 ? 3.585  -6.480  1.085   0.50 24.16 ?  163 LYS   A H    1 
ATOM   3651 H  H    B LYS   A 1 163 ? 3.751  -6.527  1.199   0.50 26.66 ?  163 LYS   A H    1 
ATOM   3652 H  HA   A LYS   A 1 163 ? 2.633  -8.522  -0.260  0.50 24.65 ?  163 LYS   A HA   1 
ATOM   3653 H  HA   B LYS   A 1 163 ? 2.631  -8.610  0.015   0.50 26.97 ?  163 LYS   A HA   1 
ATOM   3654 H  HB2  A LYS   A 1 163 ? 3.039  -6.434  -1.273  0.50 27.53 ?  163 LYS   A HB2  1 
ATOM   3655 H  HB2  B LYS   A 1 163 ? 2.945  -6.681  -1.212  0.50 29.67 ?  163 LYS   A HB2  1 
ATOM   3656 H  HB3  A LYS   A 1 163 ? 4.599  -6.701  -1.146  0.50 27.53 ?  163 LYS   A HB3  1 
ATOM   3657 H  HB3  B LYS   A 1 163 ? 4.518  -6.797  -1.035  0.50 29.67 ?  163 LYS   A HB3  1 
ATOM   3658 H  HG2  A LYS   A 1 163 ? 4.351  -8.541  -2.604  0.50 30.25 ?  163 LYS   A HG2  1 
ATOM   3659 H  HG2  B LYS   A 1 163 ? 4.631  -8.546  -2.470  0.50 32.19 ?  163 LYS   A HG2  1 
ATOM   3660 H  HG3  A LYS   A 1 163 ? 2.827  -8.127  -2.801  0.50 30.25 ?  163 LYS   A HG3  1 
ATOM   3661 H  HG3  B LYS   A 1 163 ? 3.048  -8.712  -2.479  0.50 32.19 ?  163 LYS   A HG3  1 
ATOM   3662 H  HD2  A LYS   A 1 163 ? 3.540  -6.084  -3.721  0.50 32.82 ?  163 LYS   A HD2  1 
ATOM   3663 H  HD2  B LYS   A 1 163 ? 3.035  -7.510  -4.263  0.50 34.67 ?  163 LYS   A HD2  1 
ATOM   3664 H  HD3  A LYS   A 1 163 ? 5.048  -6.582  -3.596  0.50 32.82 ?  163 LYS   A HD3  1 
ATOM   3665 H  HD3  B LYS   A 1 163 ? 3.439  -6.269  -3.353  0.50 34.67 ?  163 LYS   A HD3  1 
ATOM   3666 H  HE2  A LYS   A 1 163 ? 4.434  -8.404  -5.057  0.50 34.98 ?  163 LYS   A HE2  1 
ATOM   3667 H  HE2  B LYS   A 1 163 ? 5.666  -6.609  -3.797  0.50 36.56 ?  163 LYS   A HE2  1 
ATOM   3668 H  HE3  A LYS   A 1 163 ? 3.075  -7.634  -5.298  0.50 34.98 ?  163 LYS   A HE3  1 
ATOM   3669 H  HE3  B LYS   A 1 163 ? 5.334  -7.951  -4.581  0.50 36.56 ?  163 LYS   A HE3  1 
ATOM   3670 H  HZ1  A LYS   A 1 163 ? 4.561  -7.155  -6.942  0.50 36.26 ?  163 LYS   A HZ1  1 
ATOM   3671 H  HZ1  B LYS   A 1 163 ? 5.708  -6.248  -6.040  0.50 37.77 ?  163 LYS   A HZ1  1 
ATOM   3672 H  HZ2  A LYS   A 1 163 ? 4.245  -5.938  -6.223  0.50 36.26 ?  163 LYS   A HZ2  1 
ATOM   3673 H  HZ2  B LYS   A 1 163 ? 4.334  -6.686  -6.186  0.50 37.77 ?  163 LYS   A HZ2  1 
ATOM   3674 H  HZ3  A LYS   A 1 163 ? 5.507  -6.611  -5.990  0.50 36.26 ?  163 LYS   A HZ3  1 
ATOM   3675 H  HZ3  B LYS   A 1 163 ? 4.633  -5.462  -5.471  0.50 37.77 ?  163 LYS   A HZ3  1 
ATOM   3676 N  N    A LEU   A 1 164 ? 5.688  -8.783  0.652   0.50 18.42 ?  164 LEU   A N    1 
ATOM   3677 N  N    B LEU   A 1 164 ? 5.737  -8.884  0.754   0.50 20.09 ?  164 LEU   A N    1 
ATOM   3678 C  CA   A LEU   A 1 164 ? 6.786  -9.734  0.808   0.50 17.65 ?  164 LEU   A CA   1 
ATOM   3679 C  CA   B LEU   A 1 164 ? 6.802  -9.872  0.919   0.50 19.07 ?  164 LEU   A CA   1 
ATOM   3680 C  C    A LEU   A 1 164 ? 6.339  -10.955 1.597   0.50 17.86 ?  164 LEU   A C    1 
ATOM   3681 C  C    B LEU   A 1 164 ? 6.368  -10.987 1.858   0.50 18.94 ?  164 LEU   A C    1 
ATOM   3682 O  O    A LEU   A 1 164 ? 6.597  -12.099 1.204   0.50 18.06 ?  164 LEU   A O    1 
ATOM   3683 O  O    B LEU   A 1 164 ? 6.712  -12.158 1.651   0.50 19.12 ?  164 LEU   A O    1 
ATOM   3684 C  CB   A LEU   A 1 164 ? 7.954  -9.047  1.515   0.50 17.19 ?  164 LEU   A CB   1 
ATOM   3685 C  CB   B LEU   A 1 164 ? 8.061  -9.203  1.465   0.50 18.74 ?  164 LEU   A CB   1 
ATOM   3686 C  CG   A LEU   A 1 164 ? 8.687  -7.980  0.701   0.50 17.03 ?  164 LEU   A CG   1 
ATOM   3687 C  CG   B LEU   A 1 164 ? 8.831  -8.281  0.524   0.50 18.75 ?  164 LEU   A CG   1 
ATOM   3688 C  CD1  A LEU   A 1 164 ? 9.595  -7.126  1.584   0.50 16.15 ?  164 LEU   A CD1  1 
ATOM   3689 C  CD1  B LEU   A 1 164 ? 9.894  -7.533  1.305   0.50 18.84 ?  164 LEU   A CD1  1 
ATOM   3690 C  CD2  A LEU   A 1 164 ? 9.485  -8.636  -0.412  0.50 17.17 ?  164 LEU   A CD2  1 
ATOM   3691 C  CD2  B LEU   A 1 164 ? 9.461  -9.061  -0.617  0.50 18.84 ?  164 LEU   A CD2  1 
ATOM   3692 H  H    A LEU   A 1 164 ? 5.826  -8.014  1.017   0.50 22.12 ?  164 LEU   A H    1 
ATOM   3693 H  H    B LEU   A 1 164 ? 5.936  -8.092  1.025   0.50 24.13 ?  164 LEU   A H    1 
ATOM   3694 H  HA   A LEU   A 1 164 ? 7.078  -10.028 -0.064  0.50 21.20 ?  164 LEU   A HA   1 
ATOM   3695 H  HA   B LEU   A 1 164 ? 7.010  -10.265 0.060   0.50 22.90 ?  164 LEU   A HA   1 
ATOM   3696 H  HB2  A LEU   A 1 164 ? 7.617  -8.619  2.318   0.50 20.64 ?  164 LEU   A HB2  1 
ATOM   3697 H  HB2  B LEU   A 1 164 ? 7.809  -8.676  2.238   0.50 22.50 ?  164 LEU   A HB2  1 
ATOM   3698 H  HB3  A LEU   A 1 164 ? 8.603  -9.722  1.756   0.50 20.64 ?  164 LEU   A HB3  1 
ATOM   3699 H  HB3  B LEU   A 1 164 ? 8.673  -9.902  1.742   0.50 22.50 ?  164 LEU   A HB3  1 
ATOM   3700 H  HG   A LEU   A 1 164 ? 8.032  -7.387  0.295   0.50 20.45 ?  164 LEU   A HG   1 
ATOM   3701 H  HG   B LEU   A 1 164 ? 8.222  -7.629  0.146   0.50 22.51 ?  164 LEU   A HG   1 
ATOM   3702 H  HD11 A LEU   A 1 164 ? 10.042 -6.463  1.034   0.50 19.40 ?  164 LEU   A HD11 1 
ATOM   3703 H  HD11 B LEU   A 1 164 ? 10.385 -6.957  0.700   0.50 22.62 ?  164 LEU   A HD11 1 
ATOM   3704 H  HD12 A LEU   A 1 164 ? 9.058  -6.683  2.262   0.50 19.40 ?  164 LEU   A HD12 1 
ATOM   3705 H  HD12 B LEU   A 1 164 ? 9.467  -7.005  1.996   0.50 22.62 ?  164 LEU   A HD12 1 
ATOM   3706 H  HD13 A LEU   A 1 164 ? 10.253 -7.699  2.009   0.50 19.40 ?  164 LEU   A HD13 1 
ATOM   3707 H  HD13 B LEU   A 1 164 ? 10.500 -8.178  1.710   0.50 22.62 ?  164 LEU   A HD13 1 
ATOM   3708 H  HD21 A LEU   A 1 164 ? 10.011 -7.959  -0.863  0.50 20.61 ?  164 LEU   A HD21 1 
ATOM   3709 H  HD21 B LEU   A 1 164 ? 10.000 -8.458  -1.151  0.50 22.62 ?  164 LEU   A HD21 1 
ATOM   3710 H  HD22 A LEU   A 1 164 ? 10.065 -9.308  -0.026  0.50 20.61 ?  164 LEU   A HD22 1 
ATOM   3711 H  HD22 B LEU   A 1 164 ? 10.016 -9.765  -0.249  0.50 22.62 ?  164 LEU   A HD22 1 
ATOM   3712 H  HD23 A LEU   A 1 164 ? 8.868  -9.048  -1.038  0.50 20.61 ?  164 LEU   A HD23 1 
ATOM   3713 H  HD23 B LEU   A 1 164 ? 8.756  -9.446  -1.162  0.50 22.62 ?  164 LEU   A HD23 1 
ATOM   3714 N  N    A VAL   A 1 165 ? 5.665  -10.723 2.721   0.50 17.52 ?  165 VAL   A N    1 
ATOM   3715 N  N    B VAL   A 1 165 ? 5.635  -10.636 2.914   0.50 18.56 ?  165 VAL   A N    1 
ATOM   3716 C  CA   A VAL   A 1 165 ? 5.210  -11.817 3.570   0.50 17.33 ?  165 VAL   A CA   1 
ATOM   3717 C  CA   B VAL   A 1 165 ? 5.111  -11.653 3.820   0.50 18.25 ?  165 VAL   A CA   1 
ATOM   3718 C  C    A VAL   A 1 165 ? 4.141  -12.635 2.855   0.50 17.19 ?  165 VAL   A C    1 
ATOM   3719 C  C    B VAL   A 1 165 ? 4.117  -12.550 3.091   0.50 17.74 ?  165 VAL   A C    1 
ATOM   3720 O  O    A VAL   A 1 165 ? 4.250  -13.862 2.729   0.50 16.60 ?  165 VAL   A O    1 
ATOM   3721 O  O    B VAL   A 1 165 ? 4.191  -13.782 3.170   0.50 17.52 ?  165 VAL   A O    1 
ATOM   3722 C  CB   A VAL   A 1 165 ? 4.697  -11.252 4.907   0.50 17.61 ?  165 VAL   A CB   1 
ATOM   3723 C  CB   B VAL   A 1 165 ? 4.494  -10.997 5.070   0.50 18.53 ?  165 VAL   A CB   1 
ATOM   3724 C  CG1  A VAL   A 1 165 ? 3.950  -12.318 5.694   0.50 17.79 ?  165 VAL   A CG1  1 
ATOM   3725 C  CG1  B VAL   A 1 165 ? 3.751  -12.029 5.909   0.50 19.03 ?  165 VAL   A CG1  1 
ATOM   3726 C  CG2  A VAL   A 1 165 ? 5.852  -10.667 5.713   0.50 17.71 ?  165 VAL   A CG2  1 
ATOM   3727 C  CG2  B VAL   A 1 165 ? 5.574  -10.313 5.902   0.50 18.24 ?  165 VAL   A CG2  1 
ATOM   3728 H  H    A VAL   A 1 165 ? 5.449  -9.947  3.012   0.50 21.03 ?  165 VAL   A H    1 
ATOM   3729 H  H    B VAL   A 1 165 ? 5.434  -9.827  3.130   0.50 22.29 ?  165 VAL   A H    1 
ATOM   3730 H  HA   A VAL   A 1 165 ? 5.955  -12.408 3.765   0.50 20.81 ?  165 VAL   A HA   1 
ATOM   3731 H  HA   B VAL   A 1 165 ? 5.841  -12.212 4.120   0.50 21.91 ?  165 VAL   A HA   1 
ATOM   3732 H  HB   A VAL   A 1 165 ? 4.076  -10.533 4.724   0.50 21.14 ?  165 VAL   A HB   1 
ATOM   3733 H  HB   B VAL   A 1 165 ? 3.856  -10.318 4.797   0.50 22.25 ?  165 VAL   A HB   1 
ATOM   3734 H  HG11 A VAL   A 1 165 ? 3.894  -12.041 6.622   0.50 21.36 ?  165 VAL   A HG11 1 
ATOM   3735 H  HG11 B VAL   A 1 165 ? 3.606  -11.668 6.799   0.50 22.85 ?  165 VAL   A HG11 1 
ATOM   3736 H  HG12 A VAL   A 1 165 ? 3.055  -12.412 5.326   0.50 21.36 ?  165 VAL   A HG12 1 
ATOM   3737 H  HG12 B VAL   A 1 165 ? 2.898  -12.223 5.491   0.50 22.85 ?  165 VAL   A HG12 1 
ATOM   3738 H  HG13 A VAL   A 1 165 ? 4.429  -13.156 5.626   0.50 21.36 ?  165 VAL   A HG13 1 
ATOM   3739 H  HG13 B VAL   A 1 165 ? 4.288  -12.834 5.965   0.50 22.85 ?  165 VAL   A HG13 1 
ATOM   3740 H  HG21 A VAL   A 1 165 ? 5.512  -10.327 6.555   0.50 21.27 ?  165 VAL   A HG21 1 
ATOM   3741 H  HG21 B VAL   A 1 165 ? 5.155  -9.843  6.642   0.50 21.90 ?  165 VAL   A HG21 1 
ATOM   3742 H  HG22 A VAL   A 1 165 ? 6.507  -11.364 5.878   0.50 21.27 ?  165 VAL   A HG22 1 
ATOM   3743 H  HG22 B VAL   A 1 165 ? 6.184  -10.985 6.241   0.50 21.90 ?  165 VAL   A HG22 1 
ATOM   3744 H  HG23 A VAL   A 1 165 ? 6.257  -9.947  5.204   0.50 21.27 ?  165 VAL   A HG23 1 
ATOM   3745 H  HG23 B VAL   A 1 165 ? 6.053  -9.682  5.342   0.50 21.90 ?  165 VAL   A HG23 1 
ATOM   3746 N  N    A SER   A 1 166 ? 3.090  -11.964 2.374   0.50 18.50 ?  166 SER   A N    1 
ATOM   3747 N  N    B SER   A 1 166 ? 3.180  -11.945 2.352   0.50 17.82 ?  166 SER   A N    1 
ATOM   3748 C  CA   A SER   A 1 166 ? 1.964  -12.664 1.767   0.50 19.68 ?  166 SER   A CA   1 
ATOM   3749 C  CA   B SER   A 1 166 ? 2.057  -12.716 1.821   0.50 18.28 ?  166 SER   A CA   1 
ATOM   3750 C  C    A SER   A 1 166 ? 2.363  -13.406 0.502   0.50 19.66 ?  166 SER   A C    1 
ATOM   3751 C  C    B SER   A 1 166 ? 2.478  -13.670 0.706   0.50 18.82 ?  166 SER   A C    1 
ATOM   3752 O  O    A SER   A 1 166 ? 1.649  -14.326 0.086   0.50 20.00 ?  166 SER   A O    1 
ATOM   3753 O  O    B SER   A 1 166 ? 1.871  -14.738 0.552   0.50 19.50 ?  166 SER   A O    1 
ATOM   3754 C  CB   A SER   A 1 166 ? 0.856  -11.672 1.414   0.50 21.09 ?  166 SER   A CB   1 
ATOM   3755 C  CB   B SER   A 1 166 ? 0.916  -11.787 1.384   0.50 19.15 ?  166 SER   A CB   1 
ATOM   3756 O  OG   A SER   A 1 166 ? 0.326  -11.055 2.574   0.50 22.17 ?  166 SER   A OG   1 
ATOM   3757 O  OG   B SER   A 1 166 ? 1.260  -10.987 0.270   0.50 19.74 ?  166 SER   A OG   1 
ATOM   3758 H  H    A SER   A 1 166 ? 3.013  -11.112 2.386   0.50 22.22 ?  166 SER   A H    1 
ATOM   3759 H  H    B SER   A 1 166 ? 3.167  -11.108 2.157   0.50 21.40 ?  166 SER   A H    1 
ATOM   3760 H  HA   A SER   A 1 166 ? 1.605  -13.305 2.406   0.50 23.63 ?  166 SER   A HA   1 
ATOM   3761 H  HA   B SER   A 1 166 ? 1.707  -13.268 2.530   0.50 21.95 ?  166 SER   A HA   1 
ATOM   3762 H  HB2  A SER   A 1 166 ? 1.224  -10.993 0.829   0.50 25.32 ?  166 SER   A HB2  1 
ATOM   3763 H  HB2  B SER   A 1 166 ? 0.142  -12.326 1.147   0.50 23.00 ?  166 SER   A HB2  1 
ATOM   3764 H  HB3  A SER   A 1 166 ? 0.144  -12.151 0.959   0.50 25.32 ?  166 SER   A HB3  1 
ATOM   3765 H  HB3  B SER   A 1 166 ? 0.685  -11.203 2.128   0.50 23.00 ?  166 SER   A HB3  1 
ATOM   3766 H  HG   A SER   A 1 166 ? 0.937  -10.637 2.975   0.50 26.61 ?  166 SER   A HG   1 
ATOM   3767 H  HG   B SER   A 1 166 ? 1.956  -10.542 0.438   0.50 23.70 ?  166 SER   A HG   1 
ATOM   3768 N  N    A SER   A 1 167 ? 3.460  -13.007 -0.136  0.50 19.34 ?  167 SER   A N    1 
ATOM   3769 N  N    B SER   A 1 167 ? 3.524  -13.335 -0.053  0.50 19.36 ?  167 SER   A N    1 
ATOM   3770 C  CA   A SER   A 1 167 ? 3.952  -13.679 -1.329  0.50 19.35 ?  167 SER   A CA   1 
ATOM   3771 C  CA   B SER   A 1 167 ? 3.927  -14.135 -1.204  0.50 20.24 ?  167 SER   A CA   1 
ATOM   3772 C  C    A SER   A 1 167 ? 5.133  -14.600 -1.055  0.50 19.10 ?  167 SER   A C    1 
ATOM   3773 C  C    B SER   A 1 167 ? 5.058  -15.108 -0.890  0.50 20.78 ?  167 SER   A C    1 
ATOM   3774 O  O    A SER   A 1 167 ? 5.669  -15.188 -1.999  0.50 19.55 ?  167 SER   A O    1 
ATOM   3775 O  O    B SER   A 1 167 ? 5.573  -15.757 -1.806  0.50 21.29 ?  167 SER   A O    1 
ATOM   3776 C  CB   A SER   A 1 167 ? 4.348  -12.650 -2.395  0.50 19.42 ?  167 SER   A CB   1 
ATOM   3777 C  CB   B SER   A 1 167 ? 4.318  -13.231 -2.378  0.50 20.93 ?  167 SER   A CB   1 
ATOM   3778 O  OG   A SER   A 1 167 ? 5.380  -11.796 -1.930  0.50 19.21 ?  167 SER   A OG   1 
ATOM   3779 O  OG   B SER   A 1 167 ? 5.536  -12.553 -2.127  0.50 21.09 ?  167 SER   A OG   1 
ATOM   3780 H  H    A SER   A 1 167 ? 3.927  -12.323 0.099   0.50 23.22 ?  167 SER   A H    1 
ATOM   3781 H  H    B SER   A 1 167 ? 4.029  -12.644 0.085   0.50 23.24 ?  167 SER   A H    1 
ATOM   3782 H  HA   A SER   A 1 167 ? 3.235  -14.217 -1.693  0.50 23.23 ?  167 SER   A HA   1 
ATOM   3783 H  HA   B SER   A 1 167 ? 3.168  -14.660 -1.489  0.50 24.30 ?  167 SER   A HA   1 
ATOM   3784 H  HB2  A SER   A 1 167 ? 4.671  -13.123 -3.177  0.50 23.31 ?  167 SER   A HB2  1 
ATOM   3785 H  HB2  B SER   A 1 167 ? 4.419  -13.777 -3.175  0.50 25.13 ?  167 SER   A HB2  1 
ATOM   3786 H  HB3  A SER   A 1 167 ? 3.562  -12.127 -2.629  0.50 23.31 ?  167 SER   A HB3  1 
ATOM   3787 H  HB3  B SER   A 1 167 ? 3.616  -12.574 -2.518  0.50 25.13 ?  167 SER   A HB3  1 
ATOM   3788 H  HG   A SER   A 1 167 ? 5.561  -11.225 -2.520  0.50 23.07 ?  167 SER   A HG   1 
ATOM   3789 H  HG   B SER   A 1 167 ? 5.462  -12.074 -1.444  0.50 25.33 ?  167 SER   A HG   1 
ATOM   3790 N  N    A PHE   A 1 168 ? 5.562  -14.738 0.198   0.50 18.44 ?  168 PHE   A N    1 
ATOM   3791 N  N    B PHE   A 1 168 ? 5.439  -15.243 0.377   0.50 21.61 ?  168 PHE   A N    1 
ATOM   3792 C  CA   A PHE   A 1 168 ? 6.736  -15.555 0.472   0.50 18.62 ?  168 PHE   A CA   1 
ATOM   3793 C  CA   B PHE   A 1 168 ? 6.603  -16.042 0.749   0.50 23.21 ?  168 PHE   A CA   1 
ATOM   3794 C  C    A PHE   A 1 168 ? 6.408  -17.038 0.364   0.50 20.33 ?  168 PHE   A C    1 
ATOM   3795 C  C    B PHE   A 1 168 ? 6.236  -17.520 0.687   0.50 27.18 ?  168 PHE   A C    1 
ATOM   3796 O  O    A PHE   A 1 168 ? 5.380  -17.510 0.865   0.50 21.49 ?  168 PHE   A O    1 
ATOM   3797 O  O    B PHE   A 1 168 ? 5.437  -18.005 1.493   0.50 26.60 ?  168 PHE   A O    1 
ATOM   3798 C  CB   A PHE   A 1 168 ? 7.309  -15.268 1.858   0.50 17.48 ?  168 PHE   A CB   1 
ATOM   3799 C  CB   B PHE   A 1 168 ? 7.079  -15.656 2.145   0.50 21.80 ?  168 PHE   A CB   1 
ATOM   3800 C  CG   A PHE   A 1 168 ? 8.538  -16.083 2.164   0.50 16.43 ?  168 PHE   A CG   1 
ATOM   3801 C  CG   B PHE   A 1 168 ? 8.420  -16.224 2.497   0.50 20.84 ?  168 PHE   A CG   1 
ATOM   3802 C  CD1  A PHE   A 1 168 ? 9.727  -15.822 1.505   0.50 16.27 ?  168 PHE   A CD1  1 
ATOM   3803 C  CD1  B PHE   A 1 168 ? 9.575  -15.650 1.998   0.50 20.77 ?  168 PHE   A CD1  1 
ATOM   3804 C  CD2  A PHE   A 1 168 ? 8.502  -17.127 3.075   0.50 16.10 ?  168 PHE   A CD2  1 
ATOM   3805 C  CD2  B PHE   A 1 168 ? 8.529  -17.335 3.318   0.50 20.63 ?  168 PHE   A CD2  1 
ATOM   3806 C  CE1  A PHE   A 1 168 ? 10.863 -16.569 1.762   0.50 15.64 ?  168 PHE   A CE1  1 
ATOM   3807 C  CE1  B PHE   A 1 168 ? 10.816 -16.168 2.313   0.50 20.81 ?  168 PHE   A CE1  1 
ATOM   3808 C  CE2  A PHE   A 1 168 ? 9.640  -17.876 3.339   0.50 16.31 ?  168 PHE   A CE2  1 
ATOM   3809 C  CE2  B PHE   A 1 168 ? 9.770  -17.857 3.637   0.50 20.54 ?  168 PHE   A CE2  1 
ATOM   3810 C  CZ   A PHE   A 1 168 ? 10.819 -17.595 2.679   0.50 16.00 ?  168 PHE   A CZ   1 
ATOM   3811 C  CZ   B PHE   A 1 168 ? 10.913 -17.274 3.133   0.50 20.66 ?  168 PHE   A CZ   1 
ATOM   3812 H  H    A PHE   A 1 168 ? 5.207  -14.369 0.890   0.50 22.14 ?  168 PHE   A H    1 
ATOM   3813 H  H    B PHE   A 1 168 ? 5.037  -14.883 1.043   0.50 25.95 ?  168 PHE   A H    1 
ATOM   3814 H  HA   A PHE   A 1 168 ? 7.427  -15.341 -0.182  0.50 22.36 ?  168 PHE   A HA   1 
ATOM   3815 H  HA   B PHE   A 1 168 ? 7.323  -15.881 0.121   0.50 27.87 ?  168 PHE   A HA   1 
ATOM   3816 H  HB2  A PHE   A 1 168 ? 7.555  -14.327 1.914   0.50 20.99 ?  168 PHE   A HB2  1 
ATOM   3817 H  HB2  B PHE   A 1 168 ? 7.143  -14.690 2.196   0.50 26.17 ?  168 PHE   A HB2  1 
ATOM   3818 H  HB3  A PHE   A 1 168 ? 6.641  -15.474 2.525   0.50 20.99 ?  168 PHE   A HB3  1 
ATOM   3819 H  HB3  B PHE   A 1 168 ? 6.438  -15.981 2.796   0.50 26.17 ?  168 PHE   A HB3  1 
ATOM   3820 H  HD1  A PHE   A 1 168 ? 9.771  -15.128 0.886   0.50 19.54 ?  168 PHE   A HD1  1 
ATOM   3821 H  HD1  B PHE   A 1 168 ? 9.516  -14.905 1.443   0.50 24.94 ?  168 PHE   A HD1  1 
ATOM   3822 H  HD2  A PHE   A 1 168 ? 7.709  -17.317 3.523   0.50 19.33 ?  168 PHE   A HD2  1 
ATOM   3823 H  HD2  B PHE   A 1 168 ? 7.759  -17.732 3.658   0.50 24.76 ?  168 PHE   A HD2  1 
ATOM   3824 H  HE1  A PHE   A 1 168 ? 11.659 -16.380 1.317   0.50 18.78 ?  168 PHE   A HE1  1 
ATOM   3825 H  HE1  B PHE   A 1 168 ? 11.586 -15.773 1.973   0.50 24.98 ?  168 PHE   A HE1  1 
ATOM   3826 H  HE2  A PHE   A 1 168 ? 9.602  -18.573 3.956   0.50 19.59 ?  168 PHE   A HE2  1 
ATOM   3827 H  HE2  B PHE   A 1 168 ? 9.829  -18.604 4.190   0.50 24.66 ?  168 PHE   A HE2  1 
ATOM   3828 H  HZ   A PHE   A 1 168 ? 11.579 -18.103 2.852   0.50 19.21 ?  168 PHE   A HZ   1 
ATOM   3829 H  HZ   B PHE   A 1 168 ? 11.746 -17.624 3.347   0.50 24.80 ?  168 PHE   A HZ   1 
ATOM   3830 N  N    A LEU   A 1 169 ? 7.307  -17.776 -0.286  0.50 22.41 ?  169 LEU   A N    1 
ATOM   3831 N  N    B LEU   A 1 169 ? 6.840  -18.241 -0.251  0.50 32.19 ?  169 LEU   A N    1 
ATOM   3832 C  CA   A LEU   A 1 169 ? 7.160  -19.214 -0.413  0.50 26.31 ?  169 LEU   A CA   1 
ATOM   3833 C  CA   B LEU   A 1 169 ? 6.467  -19.626 -0.508  0.50 36.75 ?  169 LEU   A CA   1 
ATOM   3834 C  C    A LEU   A 1 169 ? 8.088  -19.898 0.576   0.50 27.72 ?  169 LEU   A C    1 
ATOM   3835 C  C    B LEU   A 1 169 ? 7.070  -20.574 0.525   0.50 38.89 ?  169 LEU   A C    1 
ATOM   3836 O  O    A LEU   A 1 169 ? 7.701  -20.162 1.715   0.50 28.58 ?  169 LEU   A O    1 
ATOM   3837 O  O    B LEU   A 1 169 ? 6.348  -21.319 1.188   0.50 39.63 ?  169 LEU   A O    1 
ATOM   3838 C  CB   A LEU   A 1 169 ? 7.463  -19.665 -1.844  0.50 28.32 ?  169 LEU   A CB   1 
ATOM   3839 C  CB   B LEU   A 1 169 ? 6.911  -20.029 -1.916  0.50 38.62 ?  169 LEU   A CB   1 
ATOM   3840 C  CG   A LEU   A 1 169 ? 7.167  -21.132 -2.167  0.50 30.06 ?  169 LEU   A CG   1 
ATOM   3841 C  CG   B LEU   A 1 169 ? 6.390  -21.357 -2.467  0.50 40.06 ?  169 LEU   A CG   1 
ATOM   3842 C  CD1  A LEU   A 1 169 ? 5.750  -21.499 -1.752  0.50 30.66 ?  169 LEU   A CD1  1 
ATOM   3843 C  CD1  B LEU   A 1 169 ? 4.881  -21.443 -2.325  0.50 40.49 ?  169 LEU   A CD1  1 
ATOM   3844 C  CD2  A LEU   A 1 169 ? 7.375  -21.408 -3.650  0.50 30.59 ?  169 LEU   A CD2  1 
ATOM   3845 C  CD2  B LEU   A 1 169 ? 6.800  -21.506 -3.924  0.50 40.57 ?  169 LEU   A CD2  1 
ATOM   3846 O  OXT  A LEU   A 1 169 ? 9.242  -20.186 0.270   0.50 27.40 -1 169 LEU   A OXT  1 
ATOM   3847 O  OXT  B LEU   A 1 169 ? 8.286  -20.618 0.722   0.50 39.78 -1 169 LEU   A OXT  1 
ATOM   3848 H  H    A LEU   A 1 169 ? 8.019  -17.463 -0.666  0.50 26.91 ?  169 LEU   A H    1 
ATOM   3849 H  H    B LEU   A 1 169 ? 7.472  -17.951 -0.754  0.50 38.65 ?  169 LEU   A H    1 
ATOM   3850 H  HA   A LEU   A 1 169 ? 6.251  -19.458 -0.196  0.50 31.59 ?  169 LEU   A HA   1 
ATOM   3851 H  HA   B LEU   A 1 169 ? 5.503  -19.698 -0.458  0.50 44.12 ?  169 LEU   A HA   1 
ATOM   3852 H  HB2  A LEU   A 1 169 ? 6.932  -19.127 -2.451  0.50 34.00 ?  169 LEU   A HB2  1 
ATOM   3853 H  HB2  B LEU   A 1 169 ? 6.623  -19.337 -2.529  0.50 46.35 ?  169 LEU   A HB2  1 
ATOM   3854 H  HB3  A LEU   A 1 169 ? 8.404  -19.518 -2.021  0.50 34.00 ?  169 LEU   A HB3  1 
ATOM   3855 H  HB3  B LEU   A 1 169 ? 7.879  -20.080 -1.922  0.50 46.35 ?  169 LEU   A HB3  1 
ATOM   3856 H  HG   A LEU   A 1 169 ? 7.780  -21.697 -1.671  0.50 36.09 ?  169 LEU   A HG   1 
ATOM   3857 H  HG   B LEU   A 1 169 ? 6.785  -22.089 -1.966  0.50 48.09 ?  169 LEU   A HG   1 
ATOM   3858 H  HD11 A LEU   A 1 169 ? 5.511  -22.346 -2.157  0.50 36.80 ?  169 LEU   A HD11 1 
ATOM   3859 H  HD11 B LEU   A 1 169 ? 4.558  -22.191 -2.848  0.50 48.60 ?  169 LEU   A HD11 1 
ATOM   3860 H  HD12 A LEU   A 1 169 ? 5.713  -21.573 -0.785  0.50 36.80 ?  169 LEU   A HD12 1 
ATOM   3861 H  HD12 B LEU   A 1 169 ? 4.659  -21.572 -1.389  0.50 48.60 ?  169 LEU   A HD12 1 
ATOM   3862 H  HD13 A LEU   A 1 169 ? 5.143  -20.805 -2.055  0.50 36.80 ?  169 LEU   A HD13 1 
ATOM   3863 H  HD13 B LEU   A 1 169 ? 4.488  -20.617 -2.649  0.50 48.60 ?  169 LEU   A HD13 1 
ATOM   3864 H  HD21 A LEU   A 1 169 ? 7.188  -22.343 -3.828  0.50 36.72 ?  169 LEU   A HD21 1 
ATOM   3865 H  HD21 B LEU   A 1 169 ? 6.469  -22.353 -4.260  0.50 48.70 ?  169 LEU   A HD21 1 
ATOM   3866 H  HD22 A LEU   A 1 169 ? 6.772  -20.847 -4.163  0.50 36.72 ?  169 LEU   A HD22 1 
ATOM   3867 H  HD22 B LEU   A 1 169 ? 6.418  -20.775 -4.435  0.50 48.70 ?  169 LEU   A HD22 1 
ATOM   3868 H  HD23 A LEU   A 1 169 ? 8.294  -21.204 -3.883  0.50 36.72 ?  169 LEU   A HD23 1 
ATOM   3869 H  HD23 B LEU   A 1 169 ? 7.768  -21.482 -3.984  0.50 48.70 ?  169 LEU   A HD23 1 
ATOM   3870 N  N    A SER   B 1 1   ? 50.788 -9.214  -23.715 0.50 30.25 ?  1   SER   B N    1 
ATOM   3871 N  N    B SER   B 1 1   ? 50.802 -9.260  -23.725 0.50 28.04 ?  1   SER   B N    1 
ATOM   3872 C  CA   A SER   B 1 1   ? 51.322 -10.285 -22.849 0.50 30.25 ?  1   SER   B CA   1 
ATOM   3873 C  CA   B SER   B 1 1   ? 51.255 -10.252 -22.728 0.50 27.98 ?  1   SER   B CA   1 
ATOM   3874 C  C    A SER   B 1 1   ? 50.262 -11.343 -22.590 0.50 29.11 ?  1   SER   B C    1 
ATOM   3875 C  C    B SER   B 1 1   ? 50.173 -11.291 -22.470 0.50 26.55 ?  1   SER   B C    1 
ATOM   3876 O  O    A SER   B 1 1   ? 49.067 -11.130 -22.820 0.50 29.10 ?  1   SER   B O    1 
ATOM   3877 O  O    B SER   B 1 1   ? 48.997 -11.105 -22.810 0.50 26.25 ?  1   SER   B O    1 
ATOM   3878 C  CB   A SER   B 1 1   ? 51.809 -9.713  -21.522 0.50 30.73 ?  1   SER   B CB   1 
ATOM   3879 C  CB   B SER   B 1 1   ? 51.627 -9.569  -21.416 0.50 28.66 ?  1   SER   B CB   1 
ATOM   3880 O  OG   A SER   B 1 1   ? 50.718 -9.363  -20.693 0.50 32.04 ?  1   SER   B OG   1 
ATOM   3881 O  OG   B SER   B 1 1   ? 50.504 -9.492  -20.558 0.50 30.07 ?  1   SER   B OG   1 
ATOM   3882 H  H1   A SER   B 1 1   ? 50.529 -9.568  -24.487 0.50 36.32 ?  1   SER   B H1   1 
ATOM   3883 H  H1   B SER   B 1 1   ? 51.493 -8.755  -23.961 0.50 33.66 ?  1   SER   B H1   1 
ATOM   3884 H  H2   A SER   B 1 1   ? 50.099 -8.832  -23.310 0.50 36.32 ?  1   SER   B H2   1 
ATOM   3885 H  H2   B SER   B 1 1   ? 50.485 -9.688  -24.435 0.50 33.66 ?  1   SER   B H2   1 
ATOM   3886 H  H3   A SER   B 1 1   ? 51.428 -8.616  -23.856 0.50 36.32 ?  1   SER   B H3   1 
ATOM   3887 H  H3   B SER   B 1 1   ? 50.168 -8.757  -23.364 0.50 33.66 ?  1   SER   B H3   1 
ATOM   3888 H  HA   A SER   B 1 1   ? 52.069 -10.698 -23.302 0.50 36.31 ?  1   SER   B HA   1 
ATOM   3889 H  HA   B SER   B 1 1   ? 52.040 -10.696 -23.077 0.50 33.59 ?  1   SER   B HA   1 
ATOM   3890 H  HB2  A SER   B 1 1   ? 52.348 -10.385 -21.078 0.50 36.89 ?  1   SER   B HB2  1 
ATOM   3891 H  HB2  B SER   B 1 1   ? 52.327 -10.085 -20.988 0.50 34.41 ?  1   SER   B HB2  1 
ATOM   3892 H  HB3  A SER   B 1 1   ? 52.338 -8.921  -21.694 0.50 36.89 ?  1   SER   B HB3  1 
ATOM   3893 H  HB3  B SER   B 1 1   ? 51.943 -8.671  -21.604 0.50 34.41 ?  1   SER   B HB3  1 
ATOM   3894 H  HG   A SER   B 1 1   ? 50.990 -8.898  -20.049 0.50 38.46 ?  1   SER   B HG   1 
ATOM   3895 H  HG   B SER   B 1 1   ? 50.573 -8.818  -20.061 0.50 36.09 ?  1   SER   B HG   1 
ATOM   3896 N  N    A MET   B 1 2   ? 50.719 -12.484 -22.092 0.50 27.71 ?  2   MET   B N    1 
ATOM   3897 N  N    B MET   B 1 2   ? 50.589 -12.384 -21.845 0.50 25.20 ?  2   MET   B N    1 
ATOM   3898 C  CA   A MET   B 1 2   ? 49.890 -13.665 -21.913 0.50 27.09 ?  2   MET   B CA   1 
ATOM   3899 C  CA   B MET   B 1 2   ? 49.771 -13.578 -21.688 0.50 24.71 ?  2   MET   B CA   1 
ATOM   3900 C  C    A MET   B 1 2   ? 49.652 -13.866 -20.425 0.50 24.04 ?  2   MET   B C    1 
ATOM   3901 C  C    B MET   B 1 2   ? 49.495 -13.771 -20.203 0.50 22.64 ?  2   MET   B C    1 
ATOM   3902 O  O    A MET   B 1 2   ? 50.602 -14.076 -19.664 0.50 23.81 ?  2   MET   B O    1 
ATOM   3903 O  O    B MET   B 1 2   ? 50.387 -14.170 -19.447 0.50 23.00 ?  2   MET   B O    1 
ATOM   3904 C  CB   A MET   B 1 2   ? 50.589 -14.877 -22.519 0.50 30.31 ?  2   MET   B CB   1 
ATOM   3905 C  CB   B MET   B 1 2   ? 50.534 -14.765 -22.260 0.50 27.22 ?  2   MET   B CB   1 
ATOM   3906 C  CG   A MET   B 1 2   ? 49.721 -16.119 -22.634 0.50 33.25 ?  2   MET   B CG   1 
ATOM   3907 C  CG   B MET   B 1 2   ? 49.681 -15.932 -22.734 0.50 29.25 ?  2   MET   B CG   1 
ATOM   3908 S  SD   A MET   B 1 2   ? 50.535 -17.406 -23.598 0.50 36.21 ?  2   MET   B SD   1 
ATOM   3909 S  SD   B MET   B 1 2   ? 50.608 -16.984 -23.862 0.50 31.24 ?  2   MET   B SD   1 
ATOM   3910 C  CE   A MET   B 1 2   ? 51.099 -16.419 -24.983 0.50 36.54 ?  2   MET   B CE   1 
ATOM   3911 C  CE   B MET   B 1 2   ? 51.438 -15.747 -24.833 0.50 31.70 ?  2   MET   B CE   1 
ATOM   3912 H  H    A MET   B 1 2   ? 51.532 -12.602 -21.837 0.50 33.26 ?  2   MET   B H    1 
ATOM   3913 H  H    B MET   B 1 2   ? 51.370 -12.466 -21.493 0.50 30.25 ?  2   MET   B H    1 
ATOM   3914 H  HA   A MET   B 1 2   ? 49.042 -13.551 -22.368 0.50 32.52 ?  2   MET   B HA   1 
ATOM   3915 H  HA   B MET   B 1 2   ? 48.943 -13.491 -22.182 0.50 29.67 ?  2   MET   B HA   1 
ATOM   3916 H  HB2  A MET   B 1 2   ? 50.881 -14.611 -23.403 0.50 36.38 ?  2   MET   B HB2  1 
ATOM   3917 H  HB2  B MET   B 1 2   ? 51.054 -14.410 -22.990 0.50 32.67 ?  2   MET   B HB2  1 
ATOM   3918 H  HB3  A MET   B 1 2   ? 51.357 -15.114 -21.980 0.50 36.38 ?  2   MET   B HB3  1 
ATOM   3919 H  HB3  B MET   B 1 2   ? 51.129 -15.127 -21.597 0.50 32.67 ?  2   MET   B HB3  1 
ATOM   3920 H  HG2  A MET   B 1 2   ? 49.545 -16.465 -21.743 0.50 39.92 ?  2   MET   B HG2  1 
ATOM   3921 H  HG2  B MET   B 1 2   ? 49.411 -16.468 -21.966 0.50 35.12 ?  2   MET   B HG2  1 
ATOM   3922 H  HG3  A MET   B 1 2   ? 48.889 -15.893 -23.078 0.50 39.92 ?  2   MET   B HG3  1 
ATOM   3923 H  HG3  B MET   B 1 2   ? 48.901 -15.612 -23.205 0.50 35.12 ?  2   MET   B HG3  1 
ATOM   3924 H  HE1  A MET   B 1 2   ? 51.262 -17.000 -25.729 0.50 43.87 ?  2   MET   B HE1  1 
ATOM   3925 H  HE1  B MET   B 1 2   ? 51.646 -16.140 -25.672 0.50 38.06 ?  2   MET   B HE1  1 
ATOM   3926 H  HE2  A MET   B 1 2   ? 50.407 -15.770 -25.205 0.50 43.87 ?  2   MET   B HE2  1 
ATOM   3927 H  HE2  B MET   B 1 2   ? 50.841 -14.989 -24.961 0.50 38.06 ?  2   MET   B HE2  1 
ATOM   3928 H  HE3  A MET   B 1 2   ? 51.918 -15.950 -24.738 0.50 43.87 ?  2   MET   B HE3  1 
ATOM   3929 H  HE3  B MET   B 1 2   ? 52.251 -15.464 -24.373 0.50 38.06 ?  2   MET   B HE3  1 
ATOM   3930 N  N    A VAL   B 1 3   ? 48.389 -13.770 -20.012 0.50 21.29 ?  3   VAL   B N    1 
ATOM   3931 N  N    B VAL   B 1 3   ? 48.269 -13.469 -19.784 0.50 20.57 ?  3   VAL   B N    1 
ATOM   3932 C  CA   A VAL   B 1 3   ? 47.983 -14.008 -18.635 0.50 19.56 ?  3   VAL   B CA   1 
ATOM   3933 C  CA   B VAL   B 1 3   ? 47.816 -13.729 -18.423 0.50 19.36 ?  3   VAL   B CA   1 
ATOM   3934 C  C    A VAL   B 1 3   ? 46.745 -14.896 -18.649 0.50 17.50 ?  3   VAL   B C    1 
ATOM   3935 C  C    B VAL   B 1 3   ? 46.574 -14.606 -18.475 0.50 17.70 ?  3   VAL   B C    1 
ATOM   3936 O  O    A VAL   B 1 3   ? 46.063 -15.036 -19.667 0.50 17.03 ?  3   VAL   B O    1 
ATOM   3937 O  O    B VAL   B 1 3   ? 45.759 -14.496 -19.397 0.50 18.06 ?  3   VAL   B O    1 
ATOM   3938 C  CB   A VAL   B 1 3   ? 47.693 -12.694 -17.876 0.50 20.85 ?  3   VAL   B CB   1 
ATOM   3939 C  CB   B VAL   B 1 3   ? 47.555 -12.438 -17.614 0.50 20.36 ?  3   VAL   B CB   1 
ATOM   3940 C  CG1  A VAL   B 1 3   ? 48.948 -11.832 -17.789 0.50 21.55 ?  3   VAL   B CG1  1 
ATOM   3941 C  CG1  B VAL   B 1 3   ? 48.835 -11.620 -17.483 0.50 20.89 ?  3   VAL   B CG1  1 
ATOM   3942 C  CG2  A VAL   B 1 3   ? 46.560 -11.934 -18.551 0.50 21.65 ?  3   VAL   B CG2  1 
ATOM   3943 C  CG2  B VAL   B 1 3   ? 46.444 -11.615 -18.244 0.50 20.85 ?  3   VAL   B CG2  1 
ATOM   3944 H  H    A VAL   B 1 3   ? 47.737 -13.555 -20.528 0.50 25.57 ?  3   VAL   B H    1 
ATOM   3945 H  H    B VAL   B 1 3   ? 47.670 -13.107 -20.287 0.50 24.70 ?  3   VAL   B H    1 
ATOM   3946 H  HA   A VAL   B 1 3   ? 48.700 -14.476 -18.169 0.50 23.48 ?  3   VAL   B HA   1 
ATOM   3947 H  HA   B VAL   B 1 3   ? 48.497 -14.230 -17.959 0.50 23.24 ?  3   VAL   B HA   1 
ATOM   3948 H  HB   A VAL   B 1 3   ? 47.416 -12.912 -16.971 0.50 25.03 ?  3   VAL   B HB   1 
ATOM   3949 H  HB   B VAL   B 1 3   ? 47.272 -12.684 -16.719 0.50 24.44 ?  3   VAL   B HB   1 
ATOM   3950 H  HG11 A VAL   B 1 3   ? 48.739 -11.024 -17.294 0.50 25.87 ?  3   VAL   B HG11 1 
ATOM   3951 H  HG11 B VAL   B 1 3   ? 48.649 -10.824 -16.960 0.50 25.09 ?  3   VAL   B HG11 1 
ATOM   3952 H  HG12 A VAL   B 1 3   ? 49.642 -12.331 -17.330 0.50 25.87 ?  3   VAL   B HG12 1 
ATOM   3953 H  HG12 B VAL   B 1 3   ? 49.509 -12.158 -17.039 0.50 25.09 ?  3   VAL   B HG12 1 
ATOM   3954 H  HG13 A VAL   B 1 3   ? 49.238 -11.608 -18.685 0.50 25.87 ?  3   VAL   B HG13 1 
ATOM   3955 H  HG13 B VAL   B 1 3   ? 49.141 -11.370 -18.369 0.50 25.09 ?  3   VAL   B HG13 1 
ATOM   3956 H  HG21 A VAL   B 1 3   ? 46.486 -11.057 -18.146 0.50 25.99 ?  3   VAL   B HG21 1 
ATOM   3957 H  HG21 B VAL   B 1 3   ? 46.404 -10.752 -17.805 0.50 25.03 ?  3   VAL   B HG21 1 
ATOM   3958 H  HG22 A VAL   B 1 3   ? 46.754 -11.848 -19.496 0.50 25.99 ?  3   VAL   B HG22 1 
ATOM   3959 H  HG22 B VAL   B 1 3   ? 46.631 -11.502 -19.187 0.50 25.03 ?  3   VAL   B HG22 1 
ATOM   3960 H  HG23 A VAL   B 1 3   ? 45.731 -12.425 -18.427 0.50 25.99 ?  3   VAL   B HG23 1 
ATOM   3961 H  HG23 B VAL   B 1 3   ? 45.600 -12.083 -18.127 0.50 25.03 ?  3   VAL   B HG23 1 
ATOM   3962 N  N    . ASN   B 1 4   ? 46.452 -15.491 -17.492 1.00 16.40 ?  4   ASN   B N    1 
ATOM   3963 C  CA   . ASN   B 1 4   ? 45.316 -16.406 -17.376 1.00 15.37 ?  4   ASN   B CA   1 
ATOM   3964 C  C    . ASN   B 1 4   ? 45.270 -17.369 -18.557 1.00 15.51 ?  4   ASN   B C    1 
ATOM   3965 O  O    . ASN   B 1 4   ? 44.210 -17.621 -19.126 1.00 16.30 ?  4   ASN   B O    1 
ATOM   3966 C  CB   . ASN   B 1 4   ? 43.992 -15.654 -17.211 1.00 15.02 ?  4   ASN   B CB   1 
ATOM   3967 C  CG   . ASN   B 1 4   ? 43.947 -14.832 -15.938 1.00 14.37 ?  4   ASN   B CG   1 
ATOM   3968 O  OD1  . ASN   B 1 4   ? 44.240 -15.331 -14.854 1.00 14.09 ?  4   ASN   B OD1  1 
ATOM   3969 N  ND2  . ASN   B 1 4   ? 43.600 -13.555 -16.068 1.00 15.54 ?  4   ASN   B ND2  1 
ATOM   3970 H  H    A ASN   B 1 4   ? 46.891 -15.376 -16.767 0.50 19.69 ?  4   ASN   B H    1 
ATOM   3971 H  H    B ASN   B 1 4   ? 47.042 -15.593 -16.879 0.50 19.69 ?  4   ASN   B H    1 
ATOM   3972 H  HA   . ASN   B 1 4   ? 45.447 -16.937 -16.576 1.00 18.46 ?  4   ASN   B HA   1 
ATOM   3973 H  HB2  . ASN   B 1 4   ? 43.865 -15.059 -17.962 1.00 18.04 ?  4   ASN   B HB2  1 
ATOM   3974 H  HB3  . ASN   B 1 4   ? 43.269 -16.305 -17.177 1.00 18.04 ?  4   ASN   B HB3  1 
ATOM   3975 H  HD21 . ASN   B 1 4   ? 43.564 -13.047 -15.372 1.00 18.67 ?  4   ASN   B HD21 1 
ATOM   3976 H  HD22 . ASN   B 1 4   ? 43.409 -13.235 -16.841 1.00 18.67 ?  4   ASN   B HD22 1 
ATOM   3977 N  N    . SER   B 1 5   ? 46.429 -17.905 -18.934 1.00 16.78 ?  5   SER   B N    1 
ATOM   3978 C  CA   . SER   B 1 5   ? 46.531 -18.810 -20.077 1.00 19.17 ?  5   SER   B CA   1 
ATOM   3979 C  C    . SER   B 1 5   ? 46.506 -20.249 -19.572 1.00 20.85 ?  5   SER   B C    1 
ATOM   3980 O  O    . SER   B 1 5   ? 47.504 -20.963 -19.575 1.00 23.60 ?  5   SER   B O    1 
ATOM   3981 C  CB   . SER   B 1 5   ? 47.797 -18.516 -20.878 1.00 20.57 ?  5   SER   B CB   1 
ATOM   3982 O  OG   . SER   B 1 5   ? 48.960 -18.704 -20.087 1.00 23.48 ?  5   SER   B OG   1 
ATOM   3983 H  H    . SER   B 1 5   ? 47.180 -17.761 -18.537 1.00 20.15 ?  5   SER   B H    1 
ATOM   3984 H  HA   . SER   B 1 5   ? 45.769 -18.682 -20.658 1.00 23.02 ?  5   SER   B HA   1 
ATOM   3985 H  HB2  . SER   B 1 5   ? 47.830 -19.112 -21.646 1.00 24.70 ?  5   SER   B HB2  1 
ATOM   3986 H  HB3  . SER   B 1 5   ? 47.756 -17.596 -21.177 1.00 24.70 ?  5   SER   B HB3  1 
ATOM   3987 H  HG   . SER   B 1 5   ? 49.012 -19.507 -19.845 1.00 28.19 ?  5   SER   B HG   1 
ATOM   3988 N  N    . PHE   B 1 6   ? 45.327 -20.649 -19.109 1.00 20.98 ?  6   PHE   B N    1 
ATOM   3989 C  CA   . PHE   B 1 6   ? 45.122 -21.998 -18.607 1.00 20.22 ?  6   PHE   B CA   1 
ATOM   3990 C  C    . PHE   B 1 6   ? 45.039 -22.966 -19.778 1.00 23.49 ?  6   PHE   B C    1 
ATOM   3991 O  O    . PHE   B 1 6   ? 44.382 -22.682 -20.783 1.00 26.16 ?  6   PHE   B O    1 
ATOM   3992 C  CB   . PHE   B 1 6   ? 43.831 -22.055 -17.789 1.00 18.23 ?  6   PHE   B CB   1 
ATOM   3993 C  CG   . PHE   B 1 6   ? 43.854 -21.196 -16.552 1.00 16.47 ?  6   PHE   B CG   1 
ATOM   3994 C  CD1  . PHE   B 1 6   ? 44.367 -21.688 -15.367 1.00 15.35 ?  6   PHE   B CD1  1 
ATOM   3995 C  CD2  . PHE   B 1 6   ? 43.371 -19.894 -16.581 1.00 16.00 ?  6   PHE   B CD2  1 
ATOM   3996 C  CE1  . PHE   B 1 6   ? 44.383 -20.905 -14.224 1.00 14.97 ?  6   PHE   B CE1  1 
ATOM   3997 C  CE2  . PHE   B 1 6   ? 43.386 -19.106 -15.445 1.00 16.57 ?  6   PHE   B CE2  1 
ATOM   3998 C  CZ   . PHE   B 1 6   ? 43.904 -19.602 -14.269 1.00 15.35 ?  6   PHE   B CZ   1 
ATOM   3999 H  H    . PHE   B 1 6   ? 44.622 -20.158 -19.083 1.00 25.19 ?  6   PHE   B H    1 
ATOM   4000 H  HA   . PHE   B 1 6   ? 45.860 -22.258 -18.037 1.00 24.28 ?  6   PHE   B HA   1 
ATOM   4001 H  HB2  . PHE   B 1 6   ? 43.094 -21.752 -18.344 1.00 21.89 ?  6   PHE   B HB2  1 
ATOM   4002 H  HB3  . PHE   B 1 6   ? 43.674 -22.971 -17.508 1.00 21.89 ?  6   PHE   B HB3  1 
ATOM   4003 H  HD1  . PHE   B 1 6   ? 44.702 -22.556 -15.334 1.00 18.43 ?  6   PHE   B HD1  1 
ATOM   4004 H  HD2  . PHE   B 1 6   ? 43.019 -19.555 -17.372 1.00 19.21 ?  6   PHE   B HD2  1 
ATOM   4005 H  HE1  . PHE   B 1 6   ? 44.743 -21.239 -13.431 1.00 17.98 ?  6   PHE   B HE1  1 
ATOM   4006 H  HE2  . PHE   B 1 6   ? 43.057 -18.236 -15.479 1.00 19.90 ?  6   PHE   B HE2  1 
ATOM   4007 H  HZ   . PHE   B 1 6   ? 43.918 -19.074 -13.504 1.00 18.44 ?  6   PHE   B HZ   1 
ATOM   4008 N  N    . SER   B 1 7   ? 45.726 -24.103 -19.652 1.00 24.80 ?  7   SER   B N    1 
ATOM   4009 C  CA   . SER   B 1 7   ? 45.798 -25.087 -20.723 1.00 27.37 ?  7   SER   B CA   1 
ATOM   4010 C  C    . SER   B 1 7   ? 45.744 -26.493 -20.146 1.00 26.57 ?  7   SER   B C    1 
ATOM   4011 O  O    . SER   B 1 7   ? 46.351 -26.776 -19.110 1.00 27.69 ?  7   SER   B O    1 
ATOM   4012 C  CB   . SER   B 1 7   ? 47.088 -24.919 -21.538 1.00 30.26 ?  7   SER   B CB   1 
ATOM   4013 O  OG   . SER   B 1 7   ? 47.102 -25.787 -22.658 1.00 32.38 ?  7   SER   B OG   1 
ATOM   4014 H  H    . SER   B 1 7   ? 46.172 -24.326 -18.946 1.00 29.77 ?  7   SER   B H    1 
ATOM   4015 H  HA   . SER   B 1 7   ? 45.045 -24.977 -21.316 1.00 32.86 ?  7   SER   B HA   1 
ATOM   4016 H  HB2  . SER   B 1 7   ? 47.144 -24.002 -21.851 1.00 36.33 ?  7   SER   B HB2  1 
ATOM   4017 H  HB3  . SER   B 1 7   ? 47.850 -25.122 -20.972 1.00 36.33 ?  7   SER   B HB3  1 
ATOM   4018 H  HG   . SER   B 1 7   ? 47.813 -25.684 -23.095 1.00 38.87 ?  7   SER   B HG   1 
ATOM   4019 N  N    . GLY   B 1 8   ? 45.017 -27.373 -20.834 1.00 26.73 ?  8   GLY   B N    1 
ATOM   4020 C  CA   . GLY   B 1 8   ? 44.979 -28.771 -20.463 1.00 25.91 ?  8   GLY   B CA   1 
ATOM   4021 C  C    . GLY   B 1 8   ? 44.049 -29.105 -19.327 1.00 24.19 ?  8   GLY   B C    1 
ATOM   4022 O  O    . GLY   B 1 8   ? 44.201 -30.169 -18.713 1.00 25.75 ?  8   GLY   B O    1 
ATOM   4023 H  H    . GLY   B 1 8   ? 44.541 -27.175 -21.519 1.00 32.08 ?  8   GLY   B H    1 
ATOM   4024 H  HA2  . GLY   B 1 8   ? 44.707 -29.292 -21.234 1.00 31.10 ?  8   GLY   B HA2  1 
ATOM   4025 H  HA3  . GLY   B 1 8   ? 45.866 -29.055 -20.204 1.00 31.10 ?  8   GLY   B HA3  1 
ATOM   4026 N  N    . TYR   B 1 9   ? 43.073 -28.250 -19.035 1.00 22.22 ?  9   TYR   B N    1 
ATOM   4027 C  CA   . TYR   B 1 9   ? 42.127 -28.531 -17.969 1.00 19.82 ?  9   TYR   B CA   1 
ATOM   4028 C  C    . TYR   B 1 9   ? 40.943 -29.326 -18.485 1.00 19.42 ?  9   TYR   B C    1 
ATOM   4029 O  O    . TYR   B 1 9   ? 40.517 -29.182 -19.635 1.00 21.85 ?  9   TYR   B O    1 
ATOM   4030 C  CB   . TYR   B 1 9   ? 41.612 -27.247 -17.323 1.00 18.90 ?  9   TYR   B CB   1 
ATOM   4031 C  CG   . TYR   B 1 9   ? 42.637 -26.620 -16.413 1.00 18.09 ?  9   TYR   B CG   1 
ATOM   4032 C  CD1  . TYR   B 1 9   ? 43.721 -25.936 -16.938 1.00 18.81 ?  9   TYR   B CD1  1 
ATOM   4033 C  CD2  . TYR   B 1 9   ? 42.542 -26.735 -15.034 1.00 17.47 ?  9   TYR   B CD2  1 
ATOM   4034 C  CE1  . TYR   B 1 9   ? 44.679 -25.369 -16.115 1.00 19.17 ?  9   TYR   B CE1  1 
ATOM   4035 C  CE2  . TYR   B 1 9   ? 43.495 -26.169 -14.201 1.00 17.96 ?  9   TYR   B CE2  1 
ATOM   4036 C  CZ   . TYR   B 1 9   ? 44.565 -25.488 -14.749 1.00 18.89 ?  9   TYR   B CZ   1 
ATOM   4037 O  OH   . TYR   B 1 9   ? 45.519 -24.938 -13.928 1.00 19.61 ?  9   TYR   B OH   1 
ATOM   4038 H  H    . TYR   B 1 9   ? 42.920 -27.515 -19.454 1.00 26.68 ?  9   TYR   B H    1 
ATOM   4039 H  HA   . TYR   B 1 9   ? 42.559 -29.056 -17.283 1.00 23.80 ?  9   TYR   B HA   1 
ATOM   4040 H  HB2  . TYR   B 1 9   ? 41.378 -26.602 -18.012 1.00 22.70 ?  9   TYR   B HB2  1 
ATOM   4041 H  HB3  . TYR   B 1 9   ? 40.835 -27.463 -16.790 1.00 22.70 ?  9   TYR   B HB3  1 
ATOM   4042 H  HD1  . TYR   B 1 9   ? 43.802 -25.851 -17.861 1.00 22.59 ?  9   TYR   B HD1  1 
ATOM   4043 H  HD2  . TYR   B 1 9   ? 41.819 -27.199 -14.665 1.00 20.98 ?  9   TYR   B HD2  1 
ATOM   4044 H  HE1  . TYR   B 1 9   ? 45.392 -24.914 -16.483 1.00 23.01 ?  9   TYR   B HE1  1 
ATOM   4045 H  HE2  . TYR   B 1 9   ? 43.408 -26.262 -13.278 1.00 21.56 ?  9   TYR   B HE2  1 
ATOM   4046 H  HH   . TYR   B 1 9   ? 46.098 -24.555 -14.388 1.00 23.55 ?  9   TYR   B HH   1 
ATOM   4047 N  N    . LEU   B 1 10  ? 40.428 -30.185 -17.614 1.00 17.79 ?  10  LEU   B N    1 
ATOM   4048 C  CA   . LEU   B 1 10  ? 39.219 -30.943 -17.875 1.00 17.56 ?  10  LEU   B CA   1 
ATOM   4049 C  C    . LEU   B 1 10  ? 38.033 -30.173 -17.310 1.00 17.38 ?  10  LEU   B C    1 
ATOM   4050 O  O    . LEU   B 1 10  ? 38.050 -29.758 -16.148 1.00 16.96 ?  10  LEU   B O    1 
ATOM   4051 C  CB   . LEU   B 1 10  ? 39.328 -32.310 -17.200 1.00 18.68 ?  10  LEU   B CB   1 
ATOM   4052 C  CG   . LEU   B 1 10  ? 38.179 -33.265 -17.497 1.00 20.75 ?  10  LEU   B CG   1 
ATOM   4053 C  CD1  . LEU   B 1 10  ? 38.258 -33.773 -18.930 1.00 22.27 ?  10  LEU   B CD1  1 
ATOM   4054 C  CD2  . LEU   B 1 10  ? 38.169 -34.421 -16.510 1.00 21.78 ?  10  LEU   B CD2  1 
ATOM   4055 H  H    . LEU   B 1 10  ? 40.769 -30.351 -16.837 1.00 21.36 ?  10  LEU   B H    1 
ATOM   4056 H  HA   . LEU   B 1 10  ? 39.094 -31.071 -18.824 1.00 21.08 ?  10  LEU   B HA   1 
ATOM   4057 H  HB2  . LEU   B 1 10  ? 40.146 -32.744 -17.497 1.00 22.43 ?  10  LEU   B HB2  1 
ATOM   4058 H  HB3  . LEU   B 1 10  ? 39.360 -32.189 -16.236 1.00 22.43 ?  10  LEU   B HB3  1 
ATOM   4059 H  HG   . LEU   B 1 10  ? 37.339 -32.791 -17.398 1.00 24.92 ?  10  LEU   B HG   1 
ATOM   4060 H  HD11 . LEU   B 1 10  ? 37.552 -34.422 -19.074 1.00 26.74 ?  10  LEU   B HD11 1 
ATOM   4061 H  HD12 . LEU   B 1 10  ? 38.145 -33.023 -19.534 1.00 26.74 ?  10  LEU   B HD12 1 
ATOM   4062 H  HD13 . LEU   B 1 10  ? 39.123 -34.186 -19.070 1.00 26.74 ?  10  LEU   B HD13 1 
ATOM   4063 H  HD21 . LEU   B 1 10  ? 37.432 -35.011 -16.726 1.00 26.15 ?  10  LEU   B HD21 1 
ATOM   4064 H  HD22 . LEU   B 1 10  ? 39.010 -34.894 -16.576 1.00 26.15 ?  10  LEU   B HD22 1 
ATOM   4065 H  HD23 . LEU   B 1 10  ? 38.056 -34.062 -15.615 1.00 26.15 ?  10  LEU   B HD23 1 
ATOM   4066 N  N    . LYS   B 1 11  ? 37.004 -29.996 -18.127 1.00 18.36 ?  11  LYS   B N    1 
ATOM   4067 C  CA   . LYS   B 1 11  ? 35.810 -29.278 -17.709 1.00 20.53 ?  11  LYS   B CA   1 
ATOM   4068 C  C    . LYS   B 1 11  ? 34.930 -30.199 -16.871 1.00 19.75 ?  11  LYS   B C    1 
ATOM   4069 O  O    . LYS   B 1 11  ? 34.537 -31.279 -17.329 1.00 21.65 ?  11  LYS   B O    1 
ATOM   4070 C  CB   . LYS   B 1 11  ? 35.059 -28.804 -18.951 1.00 24.55 ?  11  LYS   B CB   1 
ATOM   4071 C  CG   . LYS   B 1 11  ? 33.907 -27.854 -18.688 1.00 28.25 ?  11  LYS   B CG   1 
ATOM   4072 C  CD   . LYS   B 1 11  ? 33.136 -27.592 -19.976 1.00 31.33 ?  11  LYS   B CD   1 
ATOM   4073 C  CE   . LYS   B 1 11  ? 32.126 -26.471 -19.814 1.00 33.57 ?  11  LYS   B CE   1 
ATOM   4074 N  NZ   . LYS   B 1 11  ? 32.784 -25.142 -19.699 1.00 34.89 ?  11  LYS   B NZ   1 
ATOM   4075 H  H    . LYS   B 1 11  ? 36.967 -30.295 -18.932 1.00 22.04 ?  11  LYS   B H    1 
ATOM   4076 H  HA   . LYS   B 1 11  ? 36.058 -28.509 -17.175 1.00 24.65 ?  11  LYS   B HA   1 
ATOM   4077 H  HB2  . LYS   B 1 11  ? 35.687 -28.345 -19.531 1.00 29.47 ?  11  LYS   B HB2  1 
ATOM   4078 H  HB3  . LYS   B 1 11  ? 34.700 -29.578 -19.410 1.00 29.47 ?  11  LYS   B HB3  1 
ATOM   4079 H  HG2  . LYS   B 1 11  ? 33.301 -28.251 -18.043 1.00 33.91 ?  11  LYS   B HG2  1 
ATOM   4080 H  HG3  . LYS   B 1 11  ? 34.251 -27.010 -18.359 1.00 33.91 ?  11  LYS   B HG3  1 
ATOM   4081 H  HD2  . LYS   B 1 11  ? 33.761 -27.339 -20.675 1.00 37.60 ?  11  LYS   B HD2  1 
ATOM   4082 H  HD3  . LYS   B 1 11  ? 32.659 -28.397 -20.232 1.00 37.60 ?  11  LYS   B HD3  1 
ATOM   4083 H  HE2  . LYS   B 1 11  ? 31.541 -26.454 -20.588 1.00 40.29 ?  11  LYS   B HE2  1 
ATOM   4084 H  HE3  . LYS   B 1 11  ? 31.609 -26.629 -19.009 1.00 40.29 ?  11  LYS   B HE3  1 
ATOM   4085 H  HZ1  . LYS   B 1 11  ? 32.169 -24.505 -19.611 1.00 41.88 ?  11  LYS   B HZ1  1 
ATOM   4086 H  HZ2  . LYS   B 1 11  ? 33.320 -25.128 -18.989 1.00 41.88 ?  11  LYS   B HZ2  1 
ATOM   4087 H  HZ3  . LYS   B 1 11  ? 33.267 -24.979 -20.430 1.00 41.88 ?  11  LYS   B HZ3  1 
ATOM   4088 N  N    . LEU   B 1 12  ? 34.614 -29.774 -15.647 1.00 18.09 ?  12  LEU   B N    1 
ATOM   4089 C  CA   . LEU   B 1 12  ? 33.655 -30.482 -14.804 1.00 17.60 ?  12  LEU   B CA   1 
ATOM   4090 C  C    . LEU   B 1 12  ? 32.263 -29.876 -14.891 1.00 17.43 ?  12  LEU   B C    1 
ATOM   4091 O  O    . LEU   B 1 12  ? 31.276 -30.598 -15.062 1.00 17.94 ?  12  LEU   B O    1 
ATOM   4092 C  CB   . LEU   B 1 12  ? 34.124 -30.502 -13.344 1.00 17.13 ?  12  LEU   B CB   1 
ATOM   4093 C  CG   . LEU   B 1 12  ? 35.464 -31.187 -13.076 1.00 17.04 ?  12  LEU   B CG   1 
ATOM   4094 C  CD1  . LEU   B 1 12  ? 35.817 -31.131 -11.600 1.00 16.90 ?  12  LEU   B CD1  1 
ATOM   4095 C  CD2  . LEU   B 1 12  ? 35.452 -32.628 -13.575 1.00 17.73 ?  12  LEU   B CD2  1 
ATOM   4096 H  H    . LEU   B 1 12  ? 34.939 -29.067 -15.282 1.00 21.73 ?  12  LEU   B H    1 
ATOM   4097 H  HA   . LEU   B 1 12  ? 33.585 -31.396 -15.107 1.00 21.13 ?  12  LEU   B HA   1 
ATOM   4098 H  HB2  . LEU   B 1 12  ? 34.197 -29.587 -13.034 1.00 20.57 ?  12  LEU   B HB2  1 
ATOM   4099 H  HB3  . LEU   B 1 12  ? 33.452 -30.966 -12.816 1.00 20.57 ?  12  LEU   B HB3  1 
ATOM   4100 H  HG   . LEU   B 1 12  ? 36.154 -30.712 -13.563 1.00 20.46 ?  12  LEU   B HG   1 
ATOM   4101 H  HD11 . LEU   B 1 12  ? 36.675 -31.568 -11.465 1.00 20.29 ?  12  LEU   B HD11 1 
ATOM   4102 H  HD12 . LEU   B 1 12  ? 35.877 -30.202 -11.323 1.00 20.29 ?  12  LEU   B HD12 1 
ATOM   4103 H  HD13 . LEU   B 1 12  ? 35.131 -31.585 -11.090 1.00 20.29 ?  12  LEU   B HD13 1 
ATOM   4104 H  HD21 . LEU   B 1 12  ? 36.255 -33.072 -13.269 1.00 21.29 ?  12  LEU   B HD21 1 
ATOM   4105 H  HD22 . LEU   B 1 12  ? 34.667 -33.076 -13.223 1.00 21.29 ?  12  LEU   B HD22 1 
ATOM   4106 H  HD23 . LEU   B 1 12  ? 35.423 -32.624 -14.545 1.00 21.29 ?  12  LEU   B HD23 1 
ATOM   4107 N  N    . THR   B 1 13  ? 32.173 -28.556 -14.773 1.00 17.30 ?  13  THR   B N    1 
ATOM   4108 C  CA   . THR   B 1 13  ? 30.946 -27.804 -14.975 1.00 17.05 ?  13  THR   B CA   1 
ATOM   4109 C  C    . THR   B 1 13  ? 31.276 -26.608 -15.860 1.00 19.07 ?  13  THR   B C    1 
ATOM   4110 O  O    . THR   B 1 13  ? 32.422 -26.415 -16.284 1.00 19.78 ?  13  THR   B O    1 
ATOM   4111 C  CB   . THR   B 1 13  ? 30.352 -27.323 -13.648 1.00 16.81 ?  13  THR   B CB   1 
ATOM   4112 O  OG1  . THR   B 1 13  ? 31.212 -26.319 -13.098 1.00 16.32 ?  13  THR   B OG1  1 
ATOM   4113 C  CG2  . THR   B 1 13  ? 30.210 -28.474 -12.662 1.00 17.18 ?  13  THR   B CG2  1 
ATOM   4114 H  H    . THR   B 1 13  ? 32.841 -28.052 -14.570 1.00 20.77 ?  13  THR   B H    1 
ATOM   4115 H  HA   . THR   B 1 13  ? 30.291 -28.363 -15.421 1.00 20.47 ?  13  THR   B HA   1 
ATOM   4116 H  HB   . THR   B 1 13  ? 29.464 -26.949 -13.803 1.00 20.18 ?  13  THR   B HB   1 
ATOM   4117 H  HG1  . THR   B 1 13  ? 30.912 -25.552 -13.284 1.00 19.59 ?  13  THR   B HG1  1 
ATOM   4118 H  HG21 . THR   B 1 13  ? 29.723 -28.184 -11.874 1.00 20.63 ?  13  THR   B HG21 1 
ATOM   4119 H  HG22 . THR   B 1 13  ? 29.725 -29.208 -13.075 1.00 20.63 ?  13  THR   B HG22 1 
ATOM   4120 H  HG23 . THR   B 1 13  ? 31.086 -28.790 -12.393 1.00 20.63 ?  13  THR   B HG23 1 
ATOM   4121 N  N    A ASP   B 1 14  ? 30.263 -25.785 -16.125 0.50 19.96 ?  14  ASP   B N    1 
ATOM   4122 N  N    B ASP   B 1 14  ? 30.266 -25.777 -16.123 0.50 19.92 ?  14  ASP   B N    1 
ATOM   4123 C  CA   A ASP   B 1 14  ? 30.478 -24.625 -16.981 0.50 21.42 ?  14  ASP   B CA   1 
ATOM   4124 C  CA   B ASP   B 1 14  ? 30.471 -24.620 -16.989 0.50 21.29 ?  14  ASP   B CA   1 
ATOM   4125 C  C    A ASP   B 1 14  ? 31.589 -23.728 -16.449 0.50 19.59 ?  14  ASP   B C    1 
ATOM   4126 C  C    B ASP   B 1 14  ? 31.478 -23.627 -16.425 0.50 19.56 ?  14  ASP   B C    1 
ATOM   4127 O  O    A ASP   B 1 14  ? 32.281 -23.073 -17.237 0.50 20.19 ?  14  ASP   B O    1 
ATOM   4128 O  O    B ASP   B 1 14  ? 31.943 -22.755 -17.168 0.50 20.11 ?  14  ASP   B O    1 
ATOM   4129 C  CB   A ASP   B 1 14  ? 29.174 -23.844 -17.150 0.50 24.91 ?  14  ASP   B CB   1 
ATOM   4130 C  CB   B ASP   B 1 14  ? 29.151 -23.893 -17.234 0.50 24.65 ?  14  ASP   B CB   1 
ATOM   4131 C  CG   A ASP   B 1 14  ? 28.197 -24.530 -18.081 0.50 27.88 ?  14  ASP   B CG   1 
ATOM   4132 C  CG   B ASP   B 1 14  ? 28.256 -24.630 -18.207 0.50 27.56 ?  14  ASP   B CG   1 
ATOM   4133 O  OD1  A ASP   B 1 14  ? 28.524 -25.614 -18.613 0.50 28.84 ?  14  ASP   B OD1  1 
ATOM   4134 O  OD1  B ASP   B 1 14  ? 28.792 -25.325 -19.096 0.50 28.42 ?  14  ASP   B OD1  1 
ATOM   4135 O  OD2  A ASP   B 1 14  ? 27.095 -23.979 -18.278 0.50 29.05 -1 14  ASP   B OD2  1 
ATOM   4136 O  OD2  B ASP   B 1 14  ? 27.019 -24.519 -18.085 0.50 28.72 -1 14  ASP   B OD2  1 
ATOM   4137 H  H    A ASP   B 1 14  ? 29.464 -25.864 -15.815 0.50 23.97 ?  14  ASP   B H    1 
ATOM   4138 H  H    B ASP   B 1 14  ? 29.467 -25.858 -15.814 0.50 23.92 ?  14  ASP   B H    1 
ATOM   4139 H  HA   A ASP   B 1 14  ? 30.755 -24.926 -17.855 0.50 25.71 ?  14  ASP   B HA   1 
ATOM   4140 H  HA   B ASP   B 1 14  ? 30.801 -24.929 -17.846 0.50 25.56 ?  14  ASP   B HA   1 
ATOM   4141 H  HB2  A ASP   B 1 14  ? 28.731 -23.760 -16.293 0.50 29.90 ?  14  ASP   B HB2  1 
ATOM   4142 H  HB2  B ASP   B 1 14  ? 28.677 -23.805 -16.392 0.50 29.59 ?  14  ASP   B HB2  1 
ATOM   4143 H  HB3  A ASP   B 1 14  ? 29.364 -22.969 -17.519 0.50 29.90 ?  14  ASP   B HB3  1 
ATOM   4144 H  HB3  B ASP   B 1 14  ? 29.342 -23.010 -17.597 0.50 29.59 ?  14  ASP   B HB3  1 
ATOM   4145 N  N    . ASN   B 1 15  ? 31.798 -23.706 -15.130 1.00 17.41 ?  15  ASN   B N    1 
ATOM   4146 C  CA   . ASN   B 1 15  ? 32.758 -22.785 -14.526 1.00 14.95 ?  15  ASN   B CA   1 
ATOM   4147 C  C    . ASN   B 1 15  ? 33.851 -23.439 -13.693 1.00 13.87 ?  15  ASN   B C    1 
ATOM   4148 O  O    . ASN   B 1 15  ? 34.699 -22.711 -13.166 1.00 13.95 ?  15  ASN   B O    1 
ATOM   4149 C  CB   . ASN   B 1 15  ? 32.044 -21.732 -13.662 1.00 15.38 ?  15  ASN   B CB   1 
ATOM   4150 C  CG   . ASN   B 1 15  ? 31.427 -22.332 -12.420 1.00 14.63 ?  15  ASN   B CG   1 
ATOM   4151 O  OD1  . ASN   B 1 15  ? 30.482 -23.127 -12.505 1.00 16.56 ?  15  ASN   B OD1  1 
ATOM   4152 N  ND2  . ASN   B 1 15  ? 31.954 -21.977 -11.260 1.00 14.05 ?  15  ASN   B ND2  1 
ATOM   4153 H  H    A ASN   B 1 15  ? 31.401 -24.225 -14.566 0.50 20.91 ?  15  ASN   B H    1 
ATOM   4154 H  H    B ASN   B 1 15  ? 31.444 -24.263 -14.575 0.50 20.91 ?  15  ASN   B H    1 
ATOM   4155 H  HA   . ASN   B 1 15  ? 33.199 -22.301 -15.232 1.00 17.95 ?  15  ASN   B HA   1 
ATOM   4156 H  HB2  . ASN   B 1 15  ? 32.689 -21.054 -13.388 1.00 18.47 ?  15  ASN   B HB2  1 
ATOM   4157 H  HB3  . ASN   B 1 15  ? 31.334 -21.314 -14.179 1.00 18.47 ?  15  ASN   B HB3  1 
ATOM   4158 H  HD21 . ASN   B 1 15  ? 31.638 -22.294 -10.523 1.00 16.87 ?  15  ASN   B HD21 1 
ATOM   4159 H  HD22 . ASN   B 1 15  ? 32.620 -21.426 -11.232 1.00 16.87 ?  15  ASN   B HD22 1 
ATOM   4160 N  N    . VAL   B 1 16  ? 33.866 -24.762 -13.546 1.00 14.10 ?  16  VAL   B N    1 
ATOM   4161 C  CA   . VAL   B 1 16  ? 34.866 -25.454 -12.736 1.00 13.65 ?  16  VAL   B CA   1 
ATOM   4162 C  C    . VAL   B 1 16  ? 35.659 -26.389 -13.634 1.00 13.74 ?  16  VAL   B C    1 
ATOM   4163 O  O    . VAL   B 1 16  ? 35.082 -27.265 -14.298 1.00 14.89 ?  16  VAL   B O    1 
ATOM   4164 C  CB   . VAL   B 1 16  ? 34.238 -26.223 -11.564 1.00 13.97 ?  16  VAL   B CB   1 
ATOM   4165 C  CG1  . VAL   B 1 16  ? 35.315 -26.972 -10.775 1.00 14.31 ?  16  VAL   B CG1  1 
ATOM   4166 C  CG2  . VAL   B 1 16  ? 33.447 -25.279 -10.664 1.00 14.63 ?  16  VAL   B CG2  1 
ATOM   4167 H  H    . VAL   B 1 16  ? 33.290 -25.290 -13.907 1.00 16.93 ?  16  VAL   B H    1 
ATOM   4168 H  HA   . VAL   B 1 16  ? 35.479 -24.796 -12.366 1.00 16.40 ?  16  VAL   B HA   1 
ATOM   4169 H  HB   . VAL   B 1 16  ? 33.620 -26.881 -11.921 1.00 16.78 ?  16  VAL   B HB   1 
ATOM   4170 H  HG11 . VAL   B 1 16  ? 34.933 -27.276 -9.937  1.00 17.18 ?  16  VAL   B HG11 1 
ATOM   4171 H  HG12 . VAL   B 1 16  ? 35.619 -27.732 -11.294 1.00 17.18 ?  16  VAL   B HG12 1 
ATOM   4172 H  HG13 . VAL   B 1 16  ? 36.054 -26.368 -10.601 1.00 17.18 ?  16  VAL   B HG13 1 
ATOM   4173 H  HG21 . VAL   B 1 16  ? 33.104 -25.780 -9.909  1.00 17.56 ?  16  VAL   B HG21 1 
ATOM   4174 H  HG22 . VAL   B 1 16  ? 34.033 -24.572 -10.359 1.00 17.56 ?  16  VAL   B HG22 1 
ATOM   4175 H  HG23 . VAL   B 1 16  ? 32.712 -24.903 -11.175 1.00 17.56 ?  16  VAL   B HG23 1 
ATOM   4176 N  N    . TYR   B 1 17  ? 36.984 -26.222 -13.612 1.00 14.18 ?  17  TYR   B N    1 
ATOM   4177 C  CA   . TYR   B 1 17  ? 37.926 -26.975 -14.422 1.00 14.65 ?  17  TYR   B CA   1 
ATOM   4178 C  C    . TYR   B 1 17  ? 38.977 -27.586 -13.506 1.00 13.87 ?  17  TYR   B C    1 
ATOM   4179 O  O    . TYR   B 1 17  ? 39.254 -27.056 -12.426 1.00 14.08 ?  17  TYR   B O    1 
ATOM   4180 C  CB   . TYR   B 1 17  ? 38.635 -26.057 -15.426 1.00 17.39 ?  17  TYR   B CB   1 
ATOM   4181 C  CG   . TYR   B 1 17  ? 37.709 -25.283 -16.333 1.00 20.28 ?  17  TYR   B CG   1 
ATOM   4182 C  CD1  . TYR   B 1 17  ? 37.126 -24.092 -15.918 1.00 21.60 ?  17  TYR   B CD1  1 
ATOM   4183 C  CD2  . TYR   B 1 17  ? 37.422 -25.744 -17.610 1.00 22.31 ?  17  TYR   B CD2  1 
ATOM   4184 C  CE1  . TYR   B 1 17  ? 36.276 -23.382 -16.750 1.00 23.07 ?  17  TYR   B CE1  1 
ATOM   4185 C  CE2  . TYR   B 1 17  ? 36.580 -25.043 -18.450 1.00 23.58 ?  17  TYR   B CE2  1 
ATOM   4186 C  CZ   . TYR   B 1 17  ? 36.008 -23.864 -18.014 1.00 24.25 ?  17  TYR   B CZ   1 
ATOM   4187 O  OH   . TYR   B 1 17  ? 35.170 -23.164 -18.847 1.00 25.69 ?  17  TYR   B OH   1 
ATOM   4188 H  H    . TYR   B 1 17  ? 37.380 -25.640 -13.109 1.00 17.03 ?  17  TYR   B H    1 
ATOM   4189 H  HA   . TYR   B 1 17  ? 37.465 -27.683 -14.902 1.00 17.60 ?  17  TYR   B HA   1 
ATOM   4190 H  HB2  . TYR   B 1 17  ? 39.181 -25.421 -14.941 1.00 20.88 ?  17  TYR   B HB2  1 
ATOM   4191 H  HB3  . TYR   B 1 17  ? 39.194 -26.605 -15.993 1.00 20.88 ?  17  TYR   B HB3  1 
ATOM   4192 H  HD1  . TYR   B 1 17  ? 37.310 -23.767 -15.067 1.00 25.93 ?  17  TYR   B HD1  1 
ATOM   4193 H  HD2  . TYR   B 1 17  ? 37.801 -26.539 -17.908 1.00 26.79 ?  17  TYR   B HD2  1 
ATOM   4194 H  HE1  . TYR   B 1 17  ? 35.894 -22.584 -16.460 1.00 27.70 ?  17  TYR   B HE1  1 
ATOM   4195 H  HE2  . TYR   B 1 17  ? 36.389 -25.364 -19.305 1.00 28.31 ?  17  TYR   B HE2  1 
ATOM   4196 H  HH   . TYR   B 1 17  ? 35.086 -23.560 -19.583 1.00 30.84 ?  17  TYR   B HH   1 
ATOM   4197 N  N    . ILE   B 1 18  ? 39.589 -28.688 -13.942 1.00 13.65 ?  18  ILE   B N    1 
ATOM   4198 C  CA   . ILE   B 1 18  ? 40.522 -29.409 -13.081 1.00 13.76 ?  18  ILE   B CA   1 
ATOM   4199 C  C    . ILE   B 1 18  ? 41.682 -29.957 -13.903 1.00 14.24 ?  18  ILE   B C    1 
ATOM   4200 O  O    . ILE   B 1 18  ? 41.522 -30.343 -15.065 1.00 15.29 ?  18  ILE   B O    1 
ATOM   4201 C  CB   . ILE   B 1 18  ? 39.772 -30.507 -12.280 1.00 14.18 ?  18  ILE   B CB   1 
ATOM   4202 C  CG1  . ILE   B 1 18  ? 40.627 -31.047 -11.129 1.00 14.62 ?  18  ILE   B CG1  1 
ATOM   4203 C  CG2  . ILE   B 1 18  ? 39.270 -31.622 -13.208 1.00 14.45 ?  18  ILE   B CG2  1 
ATOM   4204 C  CD1  . ILE   B 1 18  ? 39.823 -31.861 -10.126 1.00 15.99 ?  18  ILE   B CD1  1 
ATOM   4205 H  H    . ILE   B 1 18  ? 39.486 -29.032 -14.720 1.00 16.40 ?  18  ILE   B H    1 
ATOM   4206 H  HA   . ILE   B 1 18  ? 40.885 -28.794 -12.431 1.00 16.53 ?  18  ILE   B HA   1 
ATOM   4207 H  HB   . ILE   B 1 18  ? 38.988 -30.101 -11.878 1.00 17.02 ?  18  ILE   B HB   1 
ATOM   4208 H  HG12 . ILE   B 1 18  ? 41.320 -31.619 -11.486 1.00 17.55 ?  18  ILE   B HG12 1 
ATOM   4209 H  HG13 . ILE   B 1 18  ? 41.021 -30.299 -10.653 1.00 17.55 ?  18  ILE   B HG13 1 
ATOM   4210 H  HG21 . ILE   B 1 18  ? 38.680 -32.212 -12.708 1.00 17.35 ?  18  ILE   B HG21 1 
ATOM   4211 H  HG22 . ILE   B 1 18  ? 38.783 -31.218 -13.943 1.00 17.35 ?  18  ILE   B HG22 1 
ATOM   4212 H  HG23 . ILE   B 1 18  ? 40.028 -32.121 -13.544 1.00 17.35 ?  18  ILE   B HG23 1 
ATOM   4213 H  HD11 . ILE   B 1 18  ? 40.404 -32.134 -9.399  1.00 19.21 ?  18  ILE   B HD11 1 
ATOM   4214 H  HD12 . ILE   B 1 18  ? 39.098 -31.315 -9.782  1.00 19.21 ?  18  ILE   B HD12 1 
ATOM   4215 H  HD13 . ILE   B 1 18  ? 39.461 -32.645 -10.571 1.00 19.21 ?  18  ILE   B HD13 1 
ATOM   4216 N  N    . LYS   B 1 19  ? 42.864 -29.996 -13.283 1.00 14.50 ?  19  LYS   B N    1 
ATOM   4217 C  CA   . LYS   B 1 19  ? 44.072 -30.467 -13.942 1.00 15.49 ?  19  LYS   B CA   1 
ATOM   4218 C  C    . LYS   B 1 19  ? 44.970 -31.149 -12.922 1.00 15.37 ?  19  LYS   B C    1 
ATOM   4219 O  O    . LYS   B 1 19  ? 45.054 -30.719 -11.770 1.00 14.68 ?  19  LYS   B O    1 
ATOM   4220 C  CB   . LYS   B 1 19  ? 44.843 -29.304 -14.577 1.00 16.80 ?  19  LYS   B CB   1 
ATOM   4221 C  CG   . LYS   B 1 19  ? 46.035 -29.708 -15.431 1.00 18.69 ?  19  LYS   B CG   1 
ATOM   4222 C  CD   . LYS   B 1 19  ? 46.762 -28.470 -15.945 1.00 20.68 ?  19  LYS   B CD   1 
ATOM   4223 C  CE   . LYS   B 1 19  ? 47.918 -28.825 -16.861 1.00 22.54 ?  19  LYS   B CE   1 
ATOM   4224 N  NZ   . LYS   B 1 19  ? 48.625 -27.611 -17.341 1.00 23.23 ?  19  LYS   B NZ   1 
ATOM   4225 H  H    . LYS   B 1 19  ? 42.983 -29.742 -12.464 1.00 17.41 ?  19  LYS   B H    1 
ATOM   4226 H  HA   . LYS   B 1 19  ? 43.834 -31.105 -14.632 1.00 18.60 ?  19  LYS   B HA   1 
ATOM   4227 H  HB2  . LYS   B 1 19  ? 44.232 -28.810 -15.144 1.00 20.17 ?  19  LYS   B HB2  1 
ATOM   4228 H  HB3  . LYS   B 1 19  ? 45.166 -28.727 -13.866 1.00 20.17 ?  19  LYS   B HB3  1 
ATOM   4229 H  HG2  . LYS   B 1 19  ? 46.648 -30.233 -14.896 1.00 22.44 ?  19  LYS   B HG2  1 
ATOM   4230 H  HG3  . LYS   B 1 19  ? 45.719 -30.223 -16.191 1.00 22.44 ?  19  LYS   B HG3  1 
ATOM   4231 H  HD2  . LYS   B 1 19  ? 46.137 -27.918 -16.441 1.00 24.83 ?  19  LYS   B HD2  1 
ATOM   4232 H  HD3  . LYS   B 1 19  ? 47.115 -27.975 -15.188 1.00 24.83 ?  19  LYS   B HD3  1 
ATOM   4233 H  HE2  . LYS   B 1 19  ? 48.550 -29.379 -16.376 1.00 27.07 ?  19  LYS   B HE2  1 
ATOM   4234 H  HE3  . LYS   B 1 19  ? 47.575 -29.307 -17.632 1.00 27.07 ?  19  LYS   B HE3  1 
ATOM   4235 H  HZ1  . LYS   B 1 19  ? 49.245 -27.838 -17.940 1.00 27.89 ?  19  LYS   B HZ1  1 
ATOM   4236 H  HZ2  . LYS   B 1 19  ? 48.048 -27.052 -17.723 1.00 27.89 ?  19  LYS   B HZ2  1 
ATOM   4237 H  HZ3  . LYS   B 1 19  ? 49.020 -27.199 -16.660 1.00 27.89 ?  19  LYS   B HZ3  1 
ATOM   4238 N  N    . ASN   B 1 20  ? 45.661 -32.196 -13.361 1.00 16.87 ?  20  ASN   B N    1 
ATOM   4239 C  CA   . ASN   B 1 20  ? 46.688 -32.834 -12.544 1.00 17.46 ?  20  ASN   B CA   1 
ATOM   4240 C  C    . ASN   B 1 20  ? 47.961 -32.015 -12.721 1.00 17.94 ?  20  ASN   B C    1 
ATOM   4241 O  O    . ASN   B 1 20  ? 48.614 -32.084 -13.767 1.00 19.70 ?  20  ASN   B O    1 
ATOM   4242 C  CB   . ASN   B 1 20  ? 46.864 -34.285 -12.990 1.00 19.34 ?  20  ASN   B CB   1 
ATOM   4243 C  CG   . ASN   B 1 20  ? 48.026 -34.993 -12.307 1.00 20.83 ?  20  ASN   B CG   1 
ATOM   4244 O  OD1  . ASN   B 1 20  ? 48.689 -35.842 -12.916 1.00 23.14 ?  20  ASN   B OD1  1 
ATOM   4245 N  ND2  . ASN   B 1 20  ? 48.270 -34.671 -11.046 1.00 20.31 ?  20  ASN   B ND2  1 
ATOM   4246 H  H    . ASN   B 1 20  ? 45.554 -32.553 -14.135 1.00 20.25 ?  20  ASN   B H    1 
ATOM   4247 H  HA   . ASN   B 1 20  ? 46.415 -32.821 -11.612 1.00 20.97 ?  20  ASN   B HA   1 
ATOM   4248 H  HB2  . ASN   B 1 20  ? 46.050 -34.777 -12.781 1.00 23.22 ?  20  ASN   B HB2  1 
ATOM   4249 H  HB3  . ASN   B 1 20  ? 47.017 -34.299 -13.946 1.00 23.22 ?  20  ASN   B HB3  1 
ATOM   4250 H  HD21 . ASN   B 1 20  ? 48.920 -35.041 -10.630 1.00 24.39 ?  20  ASN   B HD21 1 
ATOM   4251 H  HD22 . ASN   B 1 20  ? 47.786 -34.078 -10.647 1.00 24.39 ?  20  ASN   B HD22 1 
ATOM   4252 N  N    . ALA   B 1 21  ? 48.313 -31.217 -11.709 1.00 17.25 ?  21  ALA   B N    1 
ATOM   4253 C  CA   . ALA   B 1 21  ? 49.422 -30.289 -11.857 1.00 18.04 ?  21  ALA   B CA   1 
ATOM   4254 C  C    . ALA   B 1 21  ? 49.886 -29.794 -10.495 1.00 17.05 ?  21  ALA   B C    1 
ATOM   4255 O  O    . ALA   B 1 21  ? 49.144 -29.819 -9.510  1.00 16.78 ?  21  ALA   B O    1 
ATOM   4256 C  CB   . ALA   B 1 21  ? 49.020 -29.117 -12.749 1.00 19.29 ?  21  ALA   B CB   1 
ATOM   4257 H  H    . ALA   B 1 21  ? 47.924 -31.206 -10.935 1.00 20.71 ?  21  ALA   B H    1 
ATOM   4258 H  HA   . ALA   B 1 21  ? 50.160 -30.757 -12.276 1.00 21.66 ?  21  ALA   B HA   1 
ATOM   4259 H  HB1  . ALA   B 1 21  ? 49.805 -28.587 -12.920 1.00 23.17 ?  21  ALA   B HB1  1 
ATOM   4260 H  HB2  . ALA   B 1 21  ? 48.666 -29.473 -13.580 1.00 23.17 ?  21  ALA   B HB2  1 
ATOM   4261 H  HB3  . ALA   B 1 21  ? 48.341 -28.598 -12.295 1.00 23.17 ?  21  ALA   B HB3  1 
ATOM   4262 N  N    . ASP   B 1 22  ? 51.146 -29.354 -10.474 1.00 16.17 ?  22  ASP   B N    1 
ATOM   4263 C  CA   . ASP   B 1 22  ? 51.765 -28.655 -9.351  1.00 15.67 ?  22  ASP   B CA   1 
ATOM   4264 C  C    . ASP   B 1 22  ? 51.356 -27.185 -9.429  1.00 14.16 ?  22  ASP   B C    1 
ATOM   4265 O  O    . ASP   B 1 22  ? 51.662 -26.509 -10.417 1.00 14.50 ?  22  ASP   B O    1 
ATOM   4266 C  CB   . ASP   B 1 22  ? 53.282 -28.826 -9.511  1.00 17.09 ?  22  ASP   B CB   1 
ATOM   4267 C  CG   . ASP   B 1 22  ? 54.109 -28.076 -8.475  1.00 18.76 ?  22  ASP   B CG   1 
ATOM   4268 O  OD1  . ASP   B 1 22  ? 53.738 -26.963 -8.070  1.00 18.77 ?  22  ASP   B OD1  1 
ATOM   4269 O  OD2  . ASP   B 1 22  ? 55.187 -28.593 -8.101  1.00 21.25 -1 22  ASP   B OD2  1 
ATOM   4270 H  H    . ASP   B 1 22  ? 51.687 -29.458 -11.140 1.00 19.42 ?  22  ASP   B H    1 
ATOM   4271 H  HA   . ASP   B 1 22  ? 51.476 -29.042 -8.507  1.00 18.82 ?  22  ASP   B HA   1 
ATOM   4272 H  HB2  . ASP   B 1 22  ? 53.504 -29.761 -9.443  1.00 20.52 ?  22  ASP   B HB2  1 
ATOM   4273 H  HB3  . ASP   B 1 22  ? 53.539 -28.483 -10.382 1.00 20.52 ?  22  ASP   B HB3  1 
ATOM   4274 N  N    . ILE   B 1 23  ? 50.650 -26.696 -8.403  1.00 13.37 ?  23  ILE   B N    1 
ATOM   4275 C  CA   . ILE   B 1 23  ? 50.053 -25.360 -8.473  1.00 12.64 ?  23  ILE   B CA   1 
ATOM   4276 C  C    . ILE   B 1 23  ? 51.106 -24.269 -8.609  1.00 12.61 ?  23  ILE   B C    1 
ATOM   4277 O  O    . ILE   B 1 23  ? 50.840 -23.224 -9.211  1.00 12.13 ?  23  ILE   B O    1 
ATOM   4278 C  CB   . ILE   B 1 23  ? 49.112 -25.118 -7.278  1.00 13.06 ?  23  ILE   B CB   1 
ATOM   4279 C  CG1  . ILE   B 1 23  ? 48.297 -23.843 -7.482  1.00 13.70 ?  23  ILE   B CG1  1 
ATOM   4280 C  CG2  . ILE   B 1 23  ? 49.877 -25.083 -5.969  1.00 13.77 ?  23  ILE   B CG2  1 
ATOM   4281 C  CD1  . ILE   B 1 23  ? 47.174 -23.679 -6.468  1.00 14.49 ?  23  ILE   B CD1  1 
ATOM   4282 H  H    . ILE   B 1 23  ? 50.502 -27.119 -7.670  1.00 16.06 ?  23  ILE   B H    1 
ATOM   4283 H  HA   . ILE   B 1 23  ? 49.507 -25.322 -9.272  1.00 15.18 ?  23  ILE   B HA   1 
ATOM   4284 H  HB   . ILE   B 1 23  ? 48.488 -25.860 -7.239  1.00 15.68 ?  23  ILE   B HB   1 
ATOM   4285 H  HG12 . ILE   B 1 23  ? 48.885 -23.075 -7.400  1.00 16.45 ?  23  ILE   B HG12 1 
ATOM   4286 H  HG13 . ILE   B 1 23  ? 47.899 -23.858 -8.369  1.00 16.45 ?  23  ILE   B HG13 1 
ATOM   4287 H  HG21 . ILE   B 1 23  ? 49.247 -25.082 -5.233  1.00 16.54 ?  23  ILE   B HG21 1 
ATOM   4288 H  HG22 . ILE   B 1 23  ? 50.445 -25.869 -5.917  1.00 16.54 ?  23  ILE   B HG22 1 
ATOM   4289 H  HG23 . ILE   B 1 23  ? 50.422 -24.281 -5.942  1.00 16.54 ?  23  ILE   B HG23 1 
ATOM   4290 H  HD11 . ILE   B 1 23  ? 46.645 -22.903 -6.707  1.00 17.40 ?  23  ILE   B HD11 1 
ATOM   4291 H  HD12 . ILE   B 1 23  ? 46.619 -24.476 -6.487  1.00 17.40 ?  23  ILE   B HD12 1 
ATOM   4292 H  HD13 . ILE   B 1 23  ? 47.559 -23.564 -5.588  1.00 17.40 ?  23  ILE   B HD13 1 
ATOM   4293 N  N    . VAL   B 1 24  ? 52.299 -24.475 -8.050  1.00 12.82 ?  24  VAL   B N    1 
ATOM   4294 C  CA   . VAL   B 1 24  ? 53.377 -23.500 -8.216  1.00 13.36 ?  24  VAL   B CA   1 
ATOM   4295 C  C    . VAL   B 1 24  ? 53.831 -23.450 -9.669  1.00 13.54 ?  24  VAL   B C    1 
ATOM   4296 O  O    . VAL   B 1 24  ? 53.966 -22.370 -10.259 1.00 14.00 ?  24  VAL   B O    1 
ATOM   4297 C  CB   . VAL   B 1 24  ? 54.551 -23.824 -7.270  1.00 14.59 ?  24  VAL   B CB   1 
ATOM   4298 C  CG1  . VAL   B 1 24  ? 55.755 -22.949 -7.594  1.00 15.51 ?  24  VAL   B CG1  1 
ATOM   4299 C  CG2  . VAL   B 1 24  ? 54.131 -23.646 -5.829  1.00 15.46 ?  24  VAL   B CG2  1 
ATOM   4300 H  H    . VAL   B 1 24  ? 52.508 -25.162 -7.576  1.00 15.39 ?  24  VAL   B H    1 
ATOM   4301 H  HA   . VAL   B 1 24  ? 53.045 -22.623 -7.978  1.00 16.05 ?  24  VAL   B HA   1 
ATOM   4302 H  HB   . VAL   B 1 24  ? 54.814 -24.751 -7.389  1.00 17.52 ?  24  VAL   B HB   1 
ATOM   4303 H  HG11 . VAL   B 1 24  ? 56.345 -22.929 -6.823  1.00 18.62 ?  24  VAL   B HG11 1 
ATOM   4304 H  HG12 . VAL   B 1 24  ? 56.220 -23.323 -8.356  1.00 18.62 ?  24  VAL   B HG12 1 
ATOM   4305 H  HG13 . VAL   B 1 24  ? 55.446 -22.052 -7.794  1.00 18.62 ?  24  VAL   B HG13 1 
ATOM   4306 H  HG21 . VAL   B 1 24  ? 54.854 -23.928 -5.248  1.00 18.56 ?  24  VAL   B HG21 1 
ATOM   4307 H  HG22 . VAL   B 1 24  ? 53.928 -22.710 -5.673  1.00 18.56 ?  24  VAL   B HG22 1 
ATOM   4308 H  HG23 . VAL   B 1 24  ? 53.342 -24.187 -5.659  1.00 18.56 ?  24  VAL   B HG23 1 
ATOM   4309 N  N    . GLU   B 1 25  ? 54.094 -24.619 -10.263 1.00 14.62 ?  25  GLU   B N    1 
ATOM   4310 C  CA   . GLU   B 1 25  ? 54.486 -24.648 -11.668 1.00 16.15 ?  25  GLU   B CA   1 
ATOM   4311 C  C    . GLU   B 1 25  ? 53.377 -24.101 -12.554 1.00 14.96 ?  25  GLU   B C    1 
ATOM   4312 O  O    . GLU   B 1 25  ? 53.646 -23.387 -13.530 1.00 15.60 ?  25  GLU   B O    1 
ATOM   4313 C  CB   . GLU   B 1 25  ? 54.881 -26.067 -12.072 1.00 19.67 ?  25  GLU   B CB   1 
ATOM   4314 C  CG   . GLU   B 1 25  ? 56.164 -26.527 -11.407 1.00 25.21 ?  25  GLU   B CG   1 
ATOM   4315 C  CD   . GLU   B 1 25  ? 57.284 -25.497 -11.492 1.00 30.53 ?  25  GLU   B CD   1 
ATOM   4316 O  OE1  . GLU   B 1 25  ? 57.658 -25.109 -12.620 1.00 32.41 ?  25  GLU   B OE1  1 
ATOM   4317 O  OE2  . GLU   B 1 25  ? 57.785 -25.058 -10.429 1.00 32.44 -1 25  GLU   B OE2  1 
ATOM   4318 H  H    . GLU   B 1 25  ? 54.049 -25.387 -9.882  1.00 17.56 ?  25  GLU   B H    1 
ATOM   4319 H  HA   . GLU   B 1 25  ? 55.244 -24.061 -11.791 1.00 19.39 ?  25  GLU   B HA   1 
ATOM   4320 H  HB2  . GLU   B 1 25  ? 54.173 -26.679 -11.812 1.00 23.62 ?  25  GLU   B HB2  1 
ATOM   4321 H  HB3  . GLU   B 1 25  ? 55.007 -26.098 -13.034 1.00 23.62 ?  25  GLU   B HB3  1 
ATOM   4322 H  HG2  . GLU   B 1 25  ? 55.998 -26.683 -10.471 1.00 30.27 ?  25  GLU   B HG2  1 
ATOM   4323 H  HG3  . GLU   B 1 25  ? 56.469 -27.338 -11.841 1.00 30.27 ?  25  GLU   B HG3  1 
ATOM   4324 N  N    A GLU   B 1 26  ? 52.122 -24.412 -12.224 0.50 14.17 ?  26  GLU   B N    1 
ATOM   4325 N  N    B GLU   B 1 26  ? 52.121 -24.420 -12.226 0.50 14.68 ?  26  GLU   B N    1 
ATOM   4326 C  CA   A GLU   B 1 26  ? 51.000 -23.880 -12.991 0.50 14.33 ?  26  GLU   B CA   1 
ATOM   4327 C  CA   B GLU   B 1 26  ? 50.990 -23.890 -12.982 0.50 15.30 ?  26  GLU   B CA   1 
ATOM   4328 C  C    A GLU   B 1 26  ? 50.950 -22.364 -12.909 0.50 13.92 ?  26  GLU   B C    1 
ATOM   4329 C  C    B GLU   B 1 26  ? 50.945 -22.371 -12.907 0.50 14.31 ?  26  GLU   B C    1 
ATOM   4330 O  O    A GLU   B 1 26  ? 50.759 -21.682 -13.922 0.50 15.12 ?  26  GLU   B O    1 
ATOM   4331 O  O    B GLU   B 1 26  ? 50.752 -21.694 -13.923 0.50 15.33 ?  26  GLU   B O    1 
ATOM   4332 C  CB   A GLU   B 1 26  ? 49.687 -24.470 -12.477 0.50 15.53 ?  26  GLU   B CB   1 
ATOM   4333 C  CB   B GLU   B 1 26  ? 49.677 -24.472 -12.446 0.50 17.24 ?  26  GLU   B CB   1 
ATOM   4334 C  CG   A GLU   B 1 26  ? 49.377 -25.840 -13.017 0.50 17.49 ?  26  GLU   B CG   1 
ATOM   4335 C  CG   B GLU   B 1 26  ? 49.137 -25.672 -13.208 0.50 19.80 ?  26  GLU   B CG   1 
ATOM   4336 C  CD   A GLU   B 1 26  ? 49.191 -25.855 -14.525 0.50 17.87 ?  26  GLU   B CD   1 
ATOM   4337 C  CD   B GLU   B 1 26  ? 48.825 -25.359 -14.665 0.50 20.42 ?  26  GLU   B CD   1 
ATOM   4338 O  OE1  A GLU   B 1 26  ? 48.346 -25.089 -15.039 0.50 17.03 ?  26  GLU   B OE1  1 
ATOM   4339 O  OE1  B GLU   B 1 26  ? 47.772 -24.751 -14.961 0.50 21.04 ?  26  GLU   B OE1  1 
ATOM   4340 O  OE2  A GLU   B 1 26  ? 49.892 -26.633 -15.194 0.50 19.40 -1 26  GLU   B OE2  1 
ATOM   4341 O  OE2  B GLU   B 1 26  ? 49.645 -25.733 -15.520 0.50 20.28 -1 26  GLU   B OE2  1 
ATOM   4342 H  H    A GLU   B 1 26  ? 51.892 -24.922 -11.568 0.50 17.01 ?  26  GLU   B H    1 
ATOM   4343 H  H    B GLU   B 1 26  ? 51.897 -24.937 -11.573 0.50 17.62 ?  26  GLU   B H    1 
ATOM   4344 H  HA   A GLU   B 1 26  ? 51.101 -24.127 -13.920 0.50 17.21 ?  26  GLU   B HA   1 
ATOM   4345 H  HA   B GLU   B 1 26  ? 51.079 -24.143 -13.911 0.50 18.38 ?  26  GLU   B HA   1 
ATOM   4346 H  HB2  A GLU   B 1 26  ? 49.730 -24.536 -11.508 0.50 18.65 ?  26  GLU   B HB2  1 
ATOM   4347 H  HB2  B GLU   B 1 26  ? 49.810 -24.747 -11.526 0.50 20.70 ?  26  GLU   B HB2  1 
ATOM   4348 H  HB3  A GLU   B 1 26  ? 48.956 -23.878 -12.727 0.50 18.65 ?  26  GLU   B HB3  1 
ATOM   4349 H  HB3  B GLU   B 1 26  ? 48.995 -23.780 -12.479 0.50 20.70 ?  26  GLU   B HB3  1 
ATOM   4350 H  HG2  A GLU   B 1 26  ? 50.114 -26.421 -12.805 0.50 21.00 ?  26  GLU   B HG2  1 
ATOM   4351 H  HG2  B GLU   B 1 26  ? 49.797 -26.382 -13.172 0.50 23.77 ?  26  GLU   B HG2  1 
ATOM   4352 H  HG3  A GLU   B 1 26  ? 48.560 -26.158 -12.603 0.50 21.00 ?  26  GLU   B HG3  1 
ATOM   4353 H  HG3  B GLU   B 1 26  ? 48.312 -25.966 -12.791 0.50 23.77 ?  26  GLU   B HG3  1 
ATOM   4354 N  N    . ALA   B 1 27  ? 51.094 -21.817 -11.702 1.00 13.22 ?  27  ALA   B N    1 
ATOM   4355 C  CA   . ALA   B 1 27  ? 51.058 -20.369 -11.551 1.00 13.25 ?  27  ALA   B CA   1 
ATOM   4356 C  C    . ALA   B 1 27  ? 52.131 -19.706 -12.403 1.00 14.29 ?  27  ALA   B C    1 
ATOM   4357 O  O    . ALA   B 1 27  ? 51.873 -18.697 -13.077 1.00 15.11 ?  27  ALA   B O    1 
ATOM   4358 C  CB   . ALA   B 1 27  ? 51.219 -19.994 -10.079 1.00 13.30 ?  27  ALA   B CB   1 
ATOM   4359 H  H    A ALA   B 1 27  ? 51.204 -22.253 -10.969 0.50 15.88 ?  27  ALA   B H    1 
ATOM   4360 H  H    B ALA   B 1 27  ? 51.207 -22.251 -10.968 0.50 15.88 ?  27  ALA   B H    1 
ATOM   4361 H  HA   . ALA   B 1 27  ? 50.202 -20.035 -11.849 1.00 15.91 ?  27  ALA   B HA   1 
ATOM   4362 H  HB1  . ALA   B 1 27  ? 51.189 -19.027 -9.993  1.00 15.97 ?  27  ALA   B HB1  1 
ATOM   4363 H  HB2  . ALA   B 1 27  ? 50.490 -20.389 -9.573  1.00 15.97 ?  27  ALA   B HB2  1 
ATOM   4364 H  HB3  . ALA   B 1 27  ? 52.067 -20.329 -9.755  1.00 15.97 ?  27  ALA   B HB3  1 
ATOM   4365 N  N    . LYS   B 1 28  ? 53.344 -20.261 -12.400 1.00 15.67 ?  28  LYS   B N    1 
ATOM   4366 C  CA   . LYS   B 1 28  ? 54.422 -19.646 -13.165 1.00 17.88 ?  28  LYS   B CA   1 
ATOM   4367 C  C    . LYS   B 1 28  ? 54.164 -19.721 -14.666 1.00 18.49 ?  28  LYS   B C    1 
ATOM   4368 O  O    . LYS   B 1 28  ? 54.575 -18.821 -15.407 1.00 19.84 ?  28  LYS   B O    1 
ATOM   4369 C  CB   . LYS   B 1 28  ? 55.773 -20.254 -12.770 1.00 20.71 ?  28  LYS   B CB   1 
ATOM   4370 C  CG   . LYS   B 1 28  ? 56.177 -19.907 -11.337 1.00 23.76 ?  28  LYS   B CG   1 
ATOM   4371 C  CD   . LYS   B 1 28  ? 57.603 -20.318 -11.000 1.00 28.20 ?  28  LYS   B CD   1 
ATOM   4372 C  CE   . LYS   B 1 28  ? 57.689 -21.776 -10.622 1.00 32.06 ?  28  LYS   B CE   1 
ATOM   4373 N  NZ   . LYS   B 1 28  ? 59.037 -22.113 -10.082 1.00 33.75 ?  28  LYS   B NZ   1 
ATOM   4374 H  H    . LYS   B 1 28  ? 53.565 -20.979 -11.974 1.00 18.82 ?  28  LYS   B H    1 
ATOM   4375 H  HA   . LYS   B 1 28  ? 54.462 -18.709 -12.932 1.00 21.46 ?  28  LYS   B HA   1 
ATOM   4376 H  HB2  . LYS   B 1 28  ? 55.726 -21.220 -12.835 1.00 24.87 ?  28  LYS   B HB2  1 
ATOM   4377 H  HB3  . LYS   B 1 28  ? 56.465 -19.914 -13.360 1.00 24.87 ?  28  LYS   B HB3  1 
ATOM   4378 H  HG2  . LYS   B 1 28  ? 56.103 -18.945 -11.217 1.00 28.52 ?  28  LYS   B HG2  1 
ATOM   4379 H  HG3  . LYS   B 1 28  ? 55.579 -20.362 -10.724 1.00 28.52 ?  28  LYS   B HG3  1 
ATOM   4380 H  HD2  . LYS   B 1 28  ? 58.166 -20.166 -11.774 1.00 33.85 ?  28  LYS   B HD2  1 
ATOM   4381 H  HD3  . LYS   B 1 28  ? 57.914 -19.787 -10.250 1.00 33.85 ?  28  LYS   B HD3  1 
ATOM   4382 H  HE2  . LYS   B 1 28  ? 57.028 -21.971 -9.939  1.00 38.48 ?  28  LYS   B HE2  1 
ATOM   4383 H  HE3  . LYS   B 1 28  ? 57.530 -22.323 -11.408 1.00 38.48 ?  28  LYS   B HE3  1 
ATOM   4384 H  HZ1  . LYS   B 1 28  ? 59.070 -22.975 -9.864  1.00 40.52 ?  28  LYS   B HZ1  1 
ATOM   4385 H  HZ2  . LYS   B 1 28  ? 59.660 -21.944 -10.693 1.00 40.52 ?  28  LYS   B HZ2  1 
ATOM   4386 H  HZ3  . LYS   B 1 28  ? 59.203 -21.625 -9.356  1.00 40.52 ?  28  LYS   B HZ3  1 
ATOM   4387 N  N    . LYS   B 1 29  ? 53.461 -20.758 -15.126 1.00 19.57 ?  29  LYS   B N    1 
ATOM   4388 C  CA   . LYS   B 1 29  ? 53.175 -20.899 -16.552 1.00 22.29 ?  29  LYS   B CA   1 
ATOM   4389 C  C    . LYS   B 1 29  ? 51.935 -20.116 -16.977 1.00 21.06 ?  29  LYS   B C    1 
ATOM   4390 O  O    . LYS   B 1 29  ? 51.940 -19.473 -18.034 1.00 22.40 ?  29  LYS   B O    1 
ATOM   4391 C  CB   . LYS   B 1 29  ? 53.004 -22.378 -16.904 1.00 27.23 ?  29  LYS   B CB   1 
ATOM   4392 C  CG   . LYS   B 1 29  ? 52.913 -22.652 -18.397 1.00 32.29 ?  29  LYS   B CG   1 
ATOM   4393 C  CD   . LYS   B 1 29  ? 53.135 -24.128 -18.709 1.00 36.11 ?  29  LYS   B CD   1 
ATOM   4394 C  CE   . LYS   B 1 29  ? 52.035 -25.002 -18.125 1.00 38.85 ?  29  LYS   B CE   1 
ATOM   4395 N  NZ   . LYS   B 1 29  ? 52.269 -26.446 -18.408 1.00 40.57 ?  29  LYS   B NZ   1 
ATOM   4396 H  H    . LYS   B 1 29  ? 53.154 -21.394 -14.633 1.00 23.50 ?  29  LYS   B H    1 
ATOM   4397 H  HA   . LYS   B 1 29  ? 53.929 -20.559 -17.054 1.00 26.76 ?  29  LYS   B HA   1 
ATOM   4398 H  HB2  . LYS   B 1 29  ? 53.765 -22.872 -16.560 1.00 32.69 ?  29  LYS   B HB2  1 
ATOM   4399 H  HB3  . LYS   B 1 29  ? 52.189 -22.704 -16.494 1.00 32.69 ?  29  LYS   B HB3  1 
ATOM   4400 H  HG2  . LYS   B 1 29  ? 52.031 -22.403 -18.715 1.00 38.76 ?  29  LYS   B HG2  1 
ATOM   4401 H  HG3  . LYS   B 1 29  ? 53.594 -22.137 -18.860 1.00 38.76 ?  29  LYS   B HG3  1 
ATOM   4402 H  HD2  . LYS   B 1 29  ? 53.143 -24.254 -19.671 1.00 43.34 ?  29  LYS   B HD2  1 
ATOM   4403 H  HD3  . LYS   B 1 29  ? 53.981 -24.411 -18.328 1.00 43.34 ?  29  LYS   B HD3  1 
ATOM   4404 H  HE2  . LYS   B 1 29  ? 52.008 -24.885 -17.163 1.00 46.64 ?  29  LYS   B HE2  1 
ATOM   4405 H  HE3  . LYS   B 1 29  ? 51.185 -24.749 -18.518 1.00 46.64 ?  29  LYS   B HE3  1 
ATOM   4406 H  HZ1  . LYS   B 1 29  ? 51.613 -26.935 -18.057 1.00 48.70 ?  29  LYS   B HZ1  1 
ATOM   4407 H  HZ2  . LYS   B 1 29  ? 52.293 -26.584 -19.287 1.00 48.70 ?  29  LYS   B HZ2  1 
ATOM   4408 H  HZ3  . LYS   B 1 29  ? 53.044 -26.704 -18.053 1.00 48.70 ?  29  LYS   B HZ3  1 
ATOM   4409 N  N    . VAL   B 1 30  ? 50.866 -20.182 -16.178 1.00 19.15 ?  30  VAL   B N    1 
ATOM   4410 C  CA   . VAL   B 1 30  ? 49.576 -19.593 -16.544 1.00 19.86 ?  30  VAL   B CA   1 
ATOM   4411 C  C    . VAL   B 1 30  ? 49.573 -18.081 -16.383 1.00 18.93 ?  30  VAL   B C    1 
ATOM   4412 O  O    . VAL   B 1 30  ? 48.830 -17.374 -17.082 1.00 19.87 ?  30  VAL   B O    1 
ATOM   4413 C  CB   . VAL   B 1 30  ? 48.470 -20.219 -15.671 1.00 21.35 ?  30  VAL   B CB   1 
ATOM   4414 C  CG1  . VAL   B 1 30  ? 47.172 -19.418 -15.758 1.00 22.00 ?  30  VAL   B CG1  1 
ATOM   4415 C  CG2  . VAL   B 1 30  ? 48.243 -21.671 -16.059 1.00 22.34 ?  30  VAL   B CG2  1 
ATOM   4416 H  H    . VAL   B 1 30  ? 50.855 -20.593 -15.410 1.00 22.99 ?  30  VAL   B H    1 
ATOM   4417 H  HA   . VAL   B 1 30  ? 49.381 -19.819 -17.468 1.00 23.84 ?  30  VAL   B HA   1 
ATOM   4418 H  HB   . VAL   B 1 30  ? 48.754 -20.213 -14.744 1.00 25.64 ?  30  VAL   B HB   1 
ATOM   4419 H  HG11 . VAL   B 1 30  ? 46.432 -20.003 -15.535 1.00 26.41 ?  30  VAL   B HG11 1 
ATOM   4420 H  HG12 . VAL   B 1 30  ? 47.208 -18.682 -15.129 1.00 26.41 ?  30  VAL   B HG12 1 
ATOM   4421 H  HG13 . VAL   B 1 30  ? 47.061 -19.090 -16.660 1.00 26.41 ?  30  VAL   B HG13 1 
ATOM   4422 H  HG21 . VAL   B 1 30  ? 47.548 -22.049 -15.491 1.00 26.83 ?  30  VAL   B HG21 1 
ATOM   4423 H  HG22 . VAL   B 1 30  ? 47.960 -21.710 -16.987 1.00 26.83 ?  30  VAL   B HG22 1 
ATOM   4424 H  HG23 . VAL   B 1 30  ? 49.067 -22.164 -15.942 1.00 26.83 ?  30  VAL   B HG23 1 
ATOM   4425 N  N    . LYS   B 1 31  ? 50.355 -17.575 -15.442 1.00 18.49 ?  31  LYS   B N    1 
ATOM   4426 C  CA   . LYS   B 1 31  ? 50.384 -16.164 -15.085 1.00 19.06 ?  31  LYS   B CA   1 
ATOM   4427 C  C    . LYS   B 1 31  ? 48.982 -15.692 -14.697 1.00 16.86 ?  31  LYS   B C    1 
ATOM   4428 O  O    . LYS   B 1 31  ? 48.442 -14.772 -15.323 1.00 17.76 ?  31  LYS   B O    1 
ATOM   4429 C  CB   . LYS   B 1 31  ? 51.011 -15.345 -16.223 1.00 22.34 ?  31  LYS   B CB   1 
ATOM   4430 C  CG   . LYS   B 1 31  ? 52.435 -15.796 -16.562 1.00 25.58 ?  31  LYS   B CG   1 
ATOM   4431 C  CD   . LYS   B 1 31  ? 53.041 -14.976 -17.688 1.00 29.42 ?  31  LYS   B CD   1 
ATOM   4432 C  CE   . LYS   B 1 31  ? 54.523 -15.255 -17.845 1.00 32.40 ?  31  LYS   B CE   1 
ATOM   4433 N  NZ   . LYS   B 1 31  ? 55.262 -14.897 -16.604 1.00 34.41 ?  31  LYS   B NZ   1 
ATOM   4434 H  H    . LYS   B 1 31  ? 50.900 -18.064 -14.989 1.00 22.20 ?  31  LYS   B H    1 
ATOM   4435 H  HA   . LYS   B 1 31  ? 50.941 -16.076 -14.308 1.00 22.88 ?  31  LYS   B HA   1 
ATOM   4436 H  HB2  . LYS   B 1 31  ? 50.471 -15.441 -17.024 1.00 26.82 ?  31  LYS   B HB2  1 
ATOM   4437 H  HB3  . LYS   B 1 31  ? 51.047 -14.418 -15.953 1.00 26.82 ?  31  LYS   B HB3  1 
ATOM   4438 H  HG2  . LYS   B 1 31  ? 52.986 -15.699 -15.770 1.00 30.71 ?  31  LYS   B HG2  1 
ATOM   4439 H  HG3  . LYS   B 1 31  ? 52.412 -16.729 -16.838 1.00 30.71 ?  31  LYS   B HG3  1 
ATOM   4440 H  HD2  . LYS   B 1 31  ? 52.595 -15.204 -18.517 1.00 35.32 ?  31  LYS   B HD2  1 
ATOM   4441 H  HD3  . LYS   B 1 31  ? 52.924 -14.036 -17.488 1.00 35.32 ?  31  LYS   B HD3  1 
ATOM   4442 H  HE2  . LYS   B 1 31  ? 54.662 -16.200 -18.021 1.00 38.90 ?  31  LYS   B HE2  1 
ATOM   4443 H  HE3  . LYS   B 1 31  ? 54.877 -14.722 -18.576 1.00 38.90 ?  31  LYS   B HE3  1 
ATOM   4444 H  HZ1  . LYS   B 1 31  ? 56.138 -14.941 -16.747 1.00 41.30 ?  31  LYS   B HZ1  1 
ATOM   4445 H  HZ2  . LYS   B 1 31  ? 55.050 -14.069 -16.355 1.00 41.30 ?  31  LYS   B HZ2  1 
ATOM   4446 H  HZ3  . LYS   B 1 31  ? 55.046 -15.459 -15.949 1.00 41.30 ?  31  LYS   B HZ3  1 
ATOM   4447 N  N    . PRO   B 1 32  ? 48.370 -16.289 -13.668 1.00 14.29 ?  32  PRO   B N    1 
ATOM   4448 C  CA   . PRO   B 1 32  ? 46.992 -15.931 -13.314 1.00 13.37 ?  32  PRO   B CA   1 
ATOM   4449 C  C    . PRO   B 1 32  ? 46.911 -14.589 -12.604 1.00 13.40 ?  32  PRO   B C    1 
ATOM   4450 O  O    . PRO   B 1 32  ? 47.842 -14.166 -11.909 1.00 14.63 ?  32  PRO   B O    1 
ATOM   4451 C  CB   . PRO   B 1 32  ? 46.589 -17.053 -12.352 1.00 13.61 ?  32  PRO   B CB   1 
ATOM   4452 C  CG   . PRO   B 1 32  ? 47.889 -17.395 -11.664 1.00 13.83 ?  32  PRO   B CG   1 
ATOM   4453 C  CD   . PRO   B 1 32  ? 48.945 -17.272 -12.727 1.00 14.16 ?  32  PRO   B CD   1 
ATOM   4454 H  HA   . PRO   B 1 32  ? 46.416 -15.939 -14.099 1.00 16.05 ?  32  PRO   B HA   1 
ATOM   4455 H  HB2  . PRO   B 1 32  ? 45.931 -16.724 -11.719 1.00 16.34 ?  32  PRO   B HB2  1 
ATOM   4456 H  HB3  . PRO   B 1 32  ? 46.246 -17.811 -12.851 1.00 16.34 ?  32  PRO   B HB3  1 
ATOM   4457 H  HG2  . PRO   B 1 32  ? 48.054 -16.763 -10.943 1.00 16.61 ?  32  PRO   B HG2  1 
ATOM   4458 H  HG3  . PRO   B 1 32  ? 47.852 -18.301 -11.323 1.00 16.61 ?  32  PRO   B HG3  1 
ATOM   4459 H  HD2  . PRO   B 1 32  ? 49.769 -16.930 -12.344 1.00 17.01 ?  32  PRO   B HD2  1 
ATOM   4460 H  HD3  . PRO   B 1 32  ? 49.078 -18.121 -13.166 1.00 17.01 ?  32  PRO   B HD3  1 
ATOM   4461 N  N    . THR   B 1 33  ? 45.757 -13.932 -12.770 1.00 12.95 ?  33  THR   B N    1 
ATOM   4462 C  CA   . THR   B 1 33  ? 45.460 -12.755 -11.960 1.00 13.30 ?  33  THR   B CA   1 
ATOM   4463 C  C    . THR   B 1 33  ? 45.413 -13.108 -10.478 1.00 12.76 ?  33  THR   B C    1 
ATOM   4464 O  O    . THR   B 1 33  ? 45.889 -12.331 -9.636  1.00 13.86 ?  33  THR   B O    1 
ATOM   4465 C  CB   . THR   B 1 33  ? 44.139 -12.120 -12.410 1.00 13.61 ?  33  THR   B CB   1 
ATOM   4466 O  OG1  . THR   B 1 33  ? 44.188 -11.854 -13.814 1.00 13.93 ?  33  THR   B OG1  1 
ATOM   4467 C  CG2  . THR   B 1 33  ? 43.877 -10.830 -11.653 1.00 14.99 ?  33  THR   B CG2  1 
ATOM   4468 H  H    . THR   B 1 33  ? 45.135 -14.148 -13.333 1.00 15.55 ?  33  THR   B H    1 
ATOM   4469 H  HA   . THR   B 1 33  ? 46.158 -12.098 -12.095 1.00 15.98 ?  33  THR   B HA   1 
ATOM   4470 H  HB   . THR   B 1 33  ? 43.406 -12.736 -12.230 1.00 16.34 ?  33  THR   B HB   1 
ATOM   4471 H  HG1  . THR   B 1 33  ? 43.464 -11.496 -14.069 1.00 16.72 ?  33  THR   B HG1  1 
ATOM   4472 H  HG21 . THR   B 1 33  ? 43.128 -10.361 -12.048 1.00 18.00 ?  33  THR   B HG21 1 
ATOM   4473 H  HG22 . THR   B 1 33  ? 43.674 -11.026 -10.725 1.00 18.00 ?  33  THR   B HG22 1 
ATOM   4474 H  HG23 . THR   B 1 33  ? 44.662 -10.263 -11.693 1.00 18.00 ?  33  THR   B HG23 1 
ATOM   4475 N  N    . VAL   B 1 34  ? 44.865 -14.277 -10.139 1.00 11.97 ?  34  VAL   B N    1 
ATOM   4476 C  CA   . VAL   B 1 34  ? 44.675 -14.677 -8.750  1.00 11.28 ?  34  VAL   B CA   1 
ATOM   4477 C  C    . VAL   B 1 34  ? 45.103 -16.125 -8.590  1.00 10.43 ?  34  VAL   B C    1 
ATOM   4478 O  O    . VAL   B 1 34  ? 44.584 -17.013 -9.277  1.00 11.55 ?  34  VAL   B O    1 
ATOM   4479 C  CB   . VAL   B 1 34  ? 43.207 -14.536 -8.298  1.00 12.60 ?  34  VAL   B CB   1 
ATOM   4480 C  CG1  . VAL   B 1 34  ? 43.052 -14.987 -6.854  1.00 12.77 ?  34  VAL   B CG1  1 
ATOM   4481 C  CG2  . VAL   B 1 34  ? 42.707 -13.113 -8.493  1.00 13.42 ?  34  VAL   B CG2  1 
ATOM   4482 H  H    . VAL   B 1 34  ? 44.607 -14.870 -10.709 1.00 14.38 ?  34  VAL   B H    1 
ATOM   4483 H  HA   . VAL   B 1 34  ? 45.230 -14.126 -8.174  1.00 13.55 ?  34  VAL   B HA   1 
ATOM   4484 H  HB   . VAL   B 1 34  ? 42.659 -15.115 -8.853  1.00 15.14 ?  34  VAL   B HB   1 
ATOM   4485 H  HG11 . VAL   B 1 34  ? 42.198 -14.669 -6.515  1.00 15.34 ?  34  VAL   B HG11 1 
ATOM   4486 H  HG12 . VAL   B 1 34  ? 43.077 -15.957 -6.817  1.00 15.34 ?  34  VAL   B HG12 1 
ATOM   4487 H  HG13 . VAL   B 1 34  ? 43.774 -14.615 -6.326  1.00 15.34 ?  34  VAL   B HG13 1 
ATOM   4488 H  HG21 . VAL   B 1 34  ? 41.792 -13.054 -8.177  1.00 16.12 ?  34  VAL   B HG21 1 
ATOM   4489 H  HG22 . VAL   B 1 34  ? 43.272 -12.507 -7.991  1.00 16.12 ?  34  VAL   B HG22 1 
ATOM   4490 H  HG23 . VAL   B 1 34  ? 42.742 -12.890 -9.439  1.00 16.12 ?  34  VAL   B HG23 1 
ATOM   4491 N  N    . VAL   B 1 35  ? 46.007 -16.376 -7.649  1.00 10.35 ?  35  VAL   B N    1 
ATOM   4492 C  CA   . VAL   B 1 35  ? 46.244 -17.720 -7.131  1.00 10.20 ?  35  VAL   B CA   1 
ATOM   4493 C  C    . VAL   B 1 35  ? 45.709 -17.773 -5.710  1.00 9.70  ?  35  VAL   B C    1 
ATOM   4494 O  O    . VAL   B 1 35  ? 45.932 -16.848 -4.921  1.00 10.37 ?  35  VAL   B O    1 
ATOM   4495 C  CB   . VAL   B 1 35  ? 47.726 -18.138 -7.217  1.00 10.77 ?  35  VAL   B CB   1 
ATOM   4496 C  CG1  . VAL   B 1 35  ? 48.630 -17.297 -6.308  1.00 11.45 ?  35  VAL   B CG1  1 
ATOM   4497 C  CG2  . VAL   B 1 35  ? 47.879 -19.634 -6.897  1.00 11.30 ?  35  VAL   B CG2  1 
ATOM   4498 H  H    . VAL   B 1 35  ? 46.510 -15.775 -7.293  1.00 12.43 ?  35  VAL   B H    1 
ATOM   4499 H  HA   . VAL   B 1 35  ? 45.728 -18.351 -7.657  1.00 12.25 ?  35  VAL   B HA   1 
ATOM   4500 H  HB   . VAL   B 1 35  ? 48.028 -18.013 -8.133  1.00 12.93 ?  35  VAL   B HB   1 
ATOM   4501 H  HG11 . VAL   B 1 35  ? 49.552 -17.524 -6.490  1.00 13.75 ?  35  VAL   B HG11 1 
ATOM   4502 H  HG12 . VAL   B 1 35  ? 48.468 -16.363 -6.492  1.00 13.75 ?  35  VAL   B HG12 1 
ATOM   4503 H  HG13 . VAL   B 1 35  ? 48.412 -17.500 -5.383  1.00 13.75 ?  35  VAL   B HG13 1 
ATOM   4504 H  HG21 . VAL   B 1 35  ? 48.803 -19.894 -7.006  1.00 13.57 ?  35  VAL   B HG21 1 
ATOM   4505 H  HG22 . VAL   B 1 35  ? 47.595 -19.793 -5.980  1.00 13.57 ?  35  VAL   B HG22 1 
ATOM   4506 H  HG23 . VAL   B 1 35  ? 47.317 -20.151 -7.503  1.00 13.57 ?  35  VAL   B HG23 1 
ATOM   4507 N  N    . VAL   B 1 36  ? 44.989 -18.845 -5.394  1.00 9.91  ?  36  VAL   B N    1 
ATOM   4508 C  CA   . VAL   B 1 36  ? 44.447 -19.055 -4.060  1.00 9.69  ?  36  VAL   B CA   1 
ATOM   4509 C  C    . VAL   B 1 36  ? 45.457 -19.817 -3.212  1.00 9.37  ?  36  VAL   B C    1 
ATOM   4510 O  O    . VAL   B 1 36  ? 45.998 -20.853 -3.634  1.00 10.57 ?  36  VAL   B O    1 
ATOM   4511 C  CB   . VAL   B 1 36  ? 43.111 -19.815 -4.132  1.00 9.95  ?  36  VAL   B CB   1 
ATOM   4512 C  CG1  . VAL   B 1 36  ? 42.607 -20.173 -2.743  1.00 10.42 ?  36  VAL   B CG1  1 
ATOM   4513 C  CG2  . VAL   B 1 36  ? 42.082 -18.985 -4.872  1.00 10.70 ?  36  VAL   B CG2  1 
ATOM   4514 H  H    . VAL   B 1 36  ? 44.806 -19.480 -5.941  1.00 11.91 ?  36  VAL   B H    1 
ATOM   4515 H  HA   . VAL   B 1 36  ? 44.282 -18.196 -3.639  1.00 11.64 ?  36  VAL   B HA   1 
ATOM   4516 H  HB   . VAL   B 1 36  ? 43.242 -20.640 -4.628  1.00 11.96 ?  36  VAL   B HB   1 
ATOM   4517 H  HG11 . VAL   B 1 36  ? 41.669 -20.411 -2.799  1.00 12.52 ?  36  VAL   B HG11 1 
ATOM   4518 H  HG12 . VAL   B 1 36  ? 43.120 -20.917 -2.398  1.00 12.52 ?  36  VAL   B HG12 1 
ATOM   4519 H  HG13 . VAL   B 1 36  ? 42.713 -19.398 -2.163  1.00 12.52 ?  36  VAL   B HG13 1 
ATOM   4520 H  HG21 . VAL   B 1 36  ? 41.241 -19.467 -4.894  1.00 12.85 ?  36  VAL   B HG21 1 
ATOM   4521 H  HG22 . VAL   B 1 36  ? 41.968 -18.139 -4.413  1.00 12.85 ?  36  VAL   B HG22 1 
ATOM   4522 H  HG23 . VAL   B 1 36  ? 42.394 -18.827 -5.780  1.00 12.85 ?  36  VAL   B HG23 1 
ATOM   4523 N  N    . ASN   B 1 37  ? 45.679 -19.325 -1.995  1.00 9.61  ?  37  ASN   B N    1 
ATOM   4524 C  CA   . ASN   B 1 37  ? 46.436 -20.048 -0.986  1.00 9.91  ?  37  ASN   B CA   1 
ATOM   4525 C  C    . ASN   B 1 37  ? 45.489 -20.722 0.002   1.00 9.69  ?  37  ASN   B C    1 
ATOM   4526 O  O    . ASN   B 1 37  ? 44.480 -20.143 0.414   1.00 10.42 ?  37  ASN   B O    1 
ATOM   4527 C  CB   . ASN   B 1 37  ? 47.372 -19.102 -0.232  1.00 10.05 ?  37  ASN   B CB   1 
ATOM   4528 C  CG   . ASN   B 1 37  ? 48.222 -19.820 0.787   1.00 10.38 ?  37  ASN   B CG   1 
ATOM   4529 O  OD1  . ASN   B 1 37  ? 48.556 -21.001 0.613   1.00 11.12 ?  37  ASN   B OD1  1 
ATOM   4530 N  ND2  . ASN   B 1 37  ? 48.563 -19.123 1.863   1.00 10.56 ?  37  ASN   B ND2  1 
ATOM   4531 H  H    . ASN   B 1 37  ? 45.398 -18.558 -1.722  1.00 11.55 ?  37  ASN   B H    1 
ATOM   4532 H  HA   . ASN   B 1 37  ? 46.967 -20.741 -1.406  1.00 11.90 ?  37  ASN   B HA   1 
ATOM   4533 H  HB2  . ASN   B 1 37  ? 47.967 -18.681 -0.869  1.00 12.07 ?  37  ASN   B HB2  1 
ATOM   4534 H  HB3  . ASN   B 1 37  ? 46.849 -18.437 0.234   1.00 12.07 ?  37  ASN   B HB3  1 
ATOM   4535 H  HD21 . ASN   B 1 37  ? 49.053 -19.487 2.473   1.00 12.68 ?  37  ASN   B HD21 1 
ATOM   4536 H  HD22 . ASN   B 1 37  ? 48.313 -18.313 1.948   1.00 12.68 ?  37  ASN   B HD22 1 
ATOM   4537 N  N    . ALA   B 1 38  ? 45.835 -21.962 0.373   1.00 10.11 ?  38  ALA   B N    1 
ATOM   4538 C  CA   . ALA   B 1 38  ? 45.186 -22.705 1.456   1.00 10.73 ?  38  ALA   B CA   1 
ATOM   4539 C  C    . ALA   B 1 38  ? 45.776 -22.221 2.780   1.00 10.43 ?  38  ALA   B C    1 
ATOM   4540 O  O    . ALA   B 1 38  ? 46.686 -22.825 3.361   1.00 11.16 ?  38  ALA   B O    1 
ATOM   4541 C  CB   . ALA   B 1 38  ? 45.410 -24.200 1.263   1.00 11.99 ?  38  ALA   B CB   1 
ATOM   4542 H  H    . ALA   B 1 38  ? 46.478 -22.399 0.012   1.00 12.15 ?  38  ALA   B H    1 
ATOM   4543 H  HA   . ALA   B 1 38  ? 44.230 -22.527 1.455   1.00 12.89 ?  38  ALA   B HA   1 
ATOM   4544 H  HB1  . ALA   B 1 38  ? 44.965 -24.683 1.986   1.00 14.40 ?  38  ALA   B HB1  1 
ATOM   4545 H  HB2  . ALA   B 1 38  ? 45.025 -24.470 0.412   1.00 14.40 ?  38  ALA   B HB2  1 
ATOM   4546 H  HB3  . ALA   B 1 38  ? 46.356 -24.387 1.277   1.00 14.40 ?  38  ALA   B HB3  1 
ATOM   4547 N  N    . ALA   B 1 39  ? 45.260 -21.077 3.241   1.00 10.29 ?  39  ALA   B N    1 
ATOM   4548 C  CA   . ALA   B 1 39  ? 45.807 -20.341 4.371   1.00 10.49 ?  39  ALA   B CA   1 
ATOM   4549 C  C    . ALA   B 1 39  ? 45.188 -20.791 5.694   1.00 10.68 ?  39  ALA   B C    1 
ATOM   4550 O  O    . ALA   B 1 39  ? 44.160 -21.472 5.738   1.00 11.57 ?  39  ALA   B O    1 
ATOM   4551 C  CB   . ALA   B 1 39  ? 45.562 -18.842 4.178   1.00 11.16 ?  39  ALA   B CB   1 
ATOM   4552 H  H    . ALA   B 1 39  ? 44.567 -20.705 2.896   1.00 12.37 ?  39  ALA   B H    1 
ATOM   4553 H  HA   . ALA   B 1 39  ? 46.760 -20.491 4.418   1.00 12.60 ?  39  ALA   B HA   1 
ATOM   4554 H  HB1  . ALA   B 1 39  ? 45.929 -18.362 4.936   1.00 13.40 ?  39  ALA   B HB1  1 
ATOM   4555 H  HB2  . ALA   B 1 39  ? 46.000 -18.554 3.361   1.00 13.40 ?  39  ALA   B HB2  1 
ATOM   4556 H  HB3  . ALA   B 1 39  ? 44.607 -18.680 4.114   1.00 13.40 ?  39  ALA   B HB3  1 
ATOM   4557 N  N    . ASN   B 1 40  ? 45.826 -20.366 6.783   1.00 11.43 ?  40  ASN   B N    1 
ATOM   4558 C  CA   . ASN   B 1 40  ? 45.268 -20.415 8.123   1.00 12.02 ?  40  ASN   B CA   1 
ATOM   4559 C  C    . ASN   B 1 40  ? 45.087 -18.988 8.648   1.00 11.69 ?  40  ASN   B C    1 
ATOM   4560 O  O    . ASN   B 1 40  ? 45.496 -18.006 8.016   1.00 11.46 ?  40  ASN   B O    1 
ATOM   4561 C  CB   . ASN   B 1 40  ? 46.120 -21.292 9.058   1.00 13.15 ?  40  ASN   B CB   1 
ATOM   4562 C  CG   . ASN   B 1 40  ? 47.574 -20.884 9.084   1.00 14.24 ?  40  ASN   B CG   1 
ATOM   4563 O  OD1  . ASN   B 1 40  ? 47.896 -19.704 9.164   1.00 16.21 ?  40  ASN   B OD1  1 
ATOM   4564 N  ND2  . ASN   B 1 40  ? 48.467 -21.860 9.023   1.00 14.08 ?  40  ASN   B ND2  1 
ATOM   4565 H  H    . ASN   B 1 40  ? 46.615 -20.029 6.759   1.00 13.73 ?  40  ASN   B H    1 
ATOM   4566 H  HA   . ASN   B 1 40  ? 44.388 -20.815 8.079   1.00 14.44 ?  40  ASN   B HA   1 
ATOM   4567 H  HB2  . ASN   B 1 40  ? 45.774 -21.220 9.961   1.00 15.79 ?  40  ASN   B HB2  1 
ATOM   4568 H  HB3  . ASN   B 1 40  ? 46.073 -22.211 8.756   1.00 15.79 ?  40  ASN   B HB3  1 
ATOM   4569 H  HD21 . ASN   B 1 40  ? 49.309 -21.677 9.034   1.00 16.90 ?  40  ASN   B HD21 1 
ATOM   4570 H  HD22 . ASN   B 1 40  ? 48.208 -22.678 8.966   1.00 16.90 ?  40  ASN   B HD22 1 
ATOM   4571 N  N    . VAL   B 1 41  ? 44.434 -18.862 9.807   1.00 12.23 ?  41  VAL   B N    1 
ATOM   4572 C  CA   . VAL   B 1 41  ? 43.976 -17.543 10.254  1.00 12.84 ?  41  VAL   B CA   1 
ATOM   4573 C  C    . VAL   B 1 41  ? 45.128 -16.591 10.546  1.00 12.35 ?  41  VAL   B C    1 
ATOM   4574 O  O    . VAL   B 1 41  ? 44.949 -15.370 10.473  1.00 12.94 ?  41  VAL   B O    1 
ATOM   4575 C  CB   . VAL   B 1 41  ? 42.999 -17.624 11.447  1.00 14.39 ?  41  VAL   B CB   1 
ATOM   4576 C  CG1  . VAL   B 1 41  ? 41.698 -18.309 11.044  1.00 14.66 ?  41  VAL   B CG1  1 
ATOM   4577 C  CG2  . VAL   B 1 41  ? 43.647 -18.314 12.634  1.00 15.48 ?  41  VAL   B CG2  1 
ATOM   4578 H  H    . VAL   B 1 41  ? 44.247 -19.507 10.336  1.00 14.69 ?  41  VAL   B H    1 
ATOM   4579 H  HA   . VAL   B 1 41  ? 43.476 -17.147 9.525   1.00 15.42 ?  41  VAL   B HA   1 
ATOM   4580 H  HB   . VAL   B 1 41  ? 42.774 -16.722 11.723  1.00 17.29 ?  41  VAL   B HB   1 
ATOM   4581 H  HG11 . VAL   B 1 41  ? 41.097 -18.316 11.806  1.00 17.61 ?  41  VAL   B HG11 1 
ATOM   4582 H  HG12 . VAL   B 1 41  ? 41.297 -17.816 10.311  1.00 17.61 ?  41  VAL   B HG12 1 
ATOM   4583 H  HG13 . VAL   B 1 41  ? 41.893 -19.217 10.767  1.00 17.61 ?  41  VAL   B HG13 1 
ATOM   4584 H  HG21 . VAL   B 1 41  ? 43.012 -18.345 13.366  1.00 18.59 ?  41  VAL   B HG21 1 
ATOM   4585 H  HG22 . VAL   B 1 41  ? 43.900 -19.215 12.377  1.00 18.59 ?  41  VAL   B HG22 1 
ATOM   4586 H  HG23 . VAL   B 1 41  ? 44.433 -17.812 12.899  1.00 18.59 ?  41  VAL   B HG23 1 
ATOM   4587 N  N    . TYR   B 1 42  ? 46.299 -17.108 10.917  1.00 12.91 ?  42  TYR   B N    1 
ATOM   4588 C  CA   . TYR   B 1 42  ? 47.453 -16.261 11.192  1.00 13.50 ?  42  TYR   B CA   1 
ATOM   4589 C  C    . TYR   B 1 42  ? 48.419 -16.184 10.014  1.00 12.82 ?  42  TYR   B C    1 
ATOM   4590 O  O    . TYR   B 1 42  ? 49.509 -15.616 10.149  1.00 13.79 ?  42  TYR   B O    1 
ATOM   4591 C  CB   . TYR   B 1 42  ? 48.146 -16.675 12.497  1.00 15.21 ?  42  TYR   B CB   1 
ATOM   4592 C  CG   . TYR   B 1 42  ? 47.552 -15.984 13.723  1.00 15.62 ?  42  TYR   B CG   1 
ATOM   4593 C  CD1  . TYR   B 1 42  ? 47.774 -14.627 13.951  1.00 14.75 ?  42  TYR   B CD1  1 
ATOM   4594 C  CD2  . TYR   B 1 42  ? 46.774 -16.677 14.636  1.00 17.52 ?  42  TYR   B CD2  1 
ATOM   4595 C  CE1  . TYR   B 1 42  ? 47.241 -13.984 15.046  1.00 16.05 ?  42  TYR   B CE1  1 
ATOM   4596 C  CE2  . TYR   B 1 42  ? 46.238 -16.039 15.743  1.00 18.02 ?  42  TYR   B CE2  1 
ATOM   4597 C  CZ   . TYR   B 1 42  ? 46.475 -14.690 15.944  1.00 18.19 ?  42  TYR   B CZ   1 
ATOM   4598 O  OH   . TYR   B 1 42  ? 45.953 -14.041 17.044  1.00 21.33 ?  42  TYR   B OH   1 
ATOM   4599 H  H    . TYR   B 1 42  ? 46.447 -17.955 11.006  1.00 15.51 ?  42  TYR   B H    1 
ATOM   4600 H  HA   . TYR   B 1 42  ? 47.123 -15.362 11.328  1.00 16.21 ?  42  TYR   B HA   1 
ATOM   4601 H  HB2  . TYR   B 1 42  ? 48.051 -17.632 12.614  1.00 18.26 ?  42  TYR   B HB2  1 
ATOM   4602 H  HB3  . TYR   B 1 42  ? 49.084 -16.437 12.439  1.00 18.26 ?  42  TYR   B HB3  1 
ATOM   4603 H  HD1  . TYR   B 1 42  ? 48.296 -14.149 13.334  1.00 17.71 ?  42  TYR   B HD1  1 
ATOM   4604 H  HD2  . TYR   B 1 42  ? 46.614 -17.586 14.500  1.00 21.04 ?  42  TYR   B HD2  1 
ATOM   4605 H  HE1  . TYR   B 1 42  ? 47.407 -13.079 15.174  1.00 19.27 ?  42  TYR   B HE1  1 
ATOM   4606 H  HE2  . TYR   B 1 42  ? 45.720 -16.518 16.347  1.00 21.64 ?  42  TYR   B HE2  1 
ATOM   4607 H  HH   . TYR   B 1 42  ? 46.180 -13.236 17.027  1.00 25.61 ?  42  TYR   B HH   1 
ATOM   4608 N  N    . LEU   B 1 43  ? 48.023 -16.702 8.854   1.00 11.74 ?  43  LEU   B N    1 
ATOM   4609 C  CA   . LEU   B 1 43  ? 48.835 -16.629 7.644   1.00 11.83 ?  43  LEU   B CA   1 
ATOM   4610 C  C    . LEU   B 1 43  ? 50.248 -17.137 7.896   1.00 12.08 ?  43  LEU   B C    1 
ATOM   4611 O  O    . LEU   B 1 43  ? 51.228 -16.537 7.449   1.00 12.80 ?  43  LEU   B O    1 
ATOM   4612 C  CB   . LEU   B 1 43  ? 48.848 -15.223 7.041   1.00 11.73 ?  43  LEU   B CB   1 
ATOM   4613 C  CG   . LEU   B 1 43  ? 47.490 -14.614 6.666   1.00 12.04 ?  43  LEU   B CG   1 
ATOM   4614 C  CD1  . LEU   B 1 43  ? 47.689 -13.217 6.094   1.00 13.26 ?  43  LEU   B CD1  1 
ATOM   4615 C  CD2  . LEU   B 1 43  ? 46.723 -15.501 5.691   1.00 12.19 ?  43  LEU   B CD2  1 
ATOM   4616 H  H    . LEU   B 1 43  ? 47.281 -17.119 8.740   1.00 14.10 ?  43  LEU   B H    1 
ATOM   4617 H  HA   . LEU   B 1 43  ? 48.439 -17.218 6.981   1.00 14.21 ?  43  LEU   B HA   1 
ATOM   4618 H  HB2  . LEU   B 1 43  ? 49.263 -14.625 7.682   1.00 14.09 ?  43  LEU   B HB2  1 
ATOM   4619 H  HB3  . LEU   B 1 43  ? 49.382 -15.249 6.233   1.00 14.09 ?  43  LEU   B HB3  1 
ATOM   4620 H  HG   . LEU   B 1 43  ? 46.956 -14.531 7.468   1.00 14.46 ?  43  LEU   B HG   1 
ATOM   4621 H  HD11 . LEU   B 1 43  ? 46.825 -12.844 5.862   1.00 15.93 ?  43  LEU   B HD11 1 
ATOM   4622 H  HD12 . LEU   B 1 43  ? 48.118 -12.661 6.767   1.00 15.93 ?  43  LEU   B HD12 1 
ATOM   4623 H  HD13 . LEU   B 1 43  ? 48.250 -13.272 5.306   1.00 15.93 ?  43  LEU   B HD13 1 
ATOM   4624 H  HD21 . LEU   B 1 43  ? 45.915 -15.040 5.410   1.00 14.64 ?  43  LEU   B HD21 1 
ATOM   4625 H  HD22 . LEU   B 1 43  ? 47.282 -15.685 4.919   1.00 14.64 ?  43  LEU   B HD22 1 
ATOM   4626 H  HD23 . LEU   B 1 43  ? 46.489 -16.333 6.133   1.00 14.64 ?  43  LEU   B HD23 1 
ATOM   4627 N  N    . LYS   B 1 44  ? 50.354 -18.263 8.609   1.00 12.05 ?  44  LYS   B N    1 
ATOM   4628 C  CA   . LYS   B 1 44  ? 51.624 -18.938 8.847   1.00 12.61 ?  44  LYS   B CA   1 
ATOM   4629 C  C    . LYS   B 1 44  ? 51.739 -20.057 7.822   1.00 11.78 ?  44  LYS   B C    1 
ATOM   4630 O  O    . LYS   B 1 44  ? 51.039 -21.072 7.910   1.00 13.14 ?  44  LYS   B O    1 
ATOM   4631 C  CB   . LYS   B 1 44  ? 51.683 -19.458 10.281  1.00 14.32 ?  44  LYS   B CB   1 
ATOM   4632 C  CG   . LYS   B 1 44  ? 51.862 -18.351 11.314  1.00 16.84 ?  44  LYS   B CG   1 
ATOM   4633 C  CD   . LYS   B 1 44  ? 53.067 -17.479 10.937  1.00 19.99 ?  44  LYS   B CD   1 
ATOM   4634 C  CE   . LYS   B 1 44  ? 53.545 -16.590 12.053  1.00 22.62 ?  44  LYS   B CE   1 
ATOM   4635 N  NZ   . LYS   B 1 44  ? 54.728 -15.782 11.660  1.00 24.13 ?  44  LYS   B NZ   1 
ATOM   4636 H  H    . LYS   B 1 44  ? 49.682 -18.653 8.978   1.00 14.47 ?  44  LYS   B H    1 
ATOM   4637 H  HA   . LYS   B 1 44  ? 52.353 -18.320 8.687   1.00 15.14 ?  44  LYS   B HA   1 
ATOM   4638 H  HB2  . LYS   B 1 44  ? 50.847 -19.918 10.480  1.00 17.19 ?  44  LYS   B HB2  1 
ATOM   4639 H  HB3  . LYS   B 1 44  ? 52.424 -20.071 10.364  1.00 17.19 ?  44  LYS   B HB3  1 
ATOM   4640 H  HG2  . LYS   B 1 44  ? 51.068 -17.797 11.339  1.00 20.22 ?  44  LYS   B HG2  1 
ATOM   4641 H  HG3  . LYS   B 1 44  ? 52.028 -18.749 12.185  1.00 20.22 ?  44  LYS   B HG3  1 
ATOM   4642 H  HD2  . LYS   B 1 44  ? 53.796 -18.062 10.660  1.00 24.00 ?  44  LYS   B HD2  1 
ATOM   4643 H  HD3  . LYS   B 1 44  ? 52.809 -16.905 10.196  1.00 24.00 ?  44  LYS   B HD3  1 
ATOM   4644 H  HE2  . LYS   B 1 44  ? 52.840 -15.970 12.259  1.00 27.15 ?  44  LYS   B HE2  1 
ATOM   4645 H  HE3  . LYS   B 1 44  ? 53.773 -17.134 12.826  1.00 27.15 ?  44  LYS   B HE3  1 
ATOM   4646 H  HZ1  . LYS   B 1 44  ? 54.982 -15.269 12.340  1.00 28.97 ?  44  LYS   B HZ1  1 
ATOM   4647 H  HZ2  . LYS   B 1 44  ? 55.400 -16.314 11.427  1.00 28.97 ?  44  LYS   B HZ2  1 
ATOM   4648 H  HZ3  . LYS   B 1 44  ? 54.519 -15.260 10.967  1.00 28.97 ?  44  LYS   B HZ3  1 
ATOM   4649 N  N    . HIS   B 1 45  ? 52.586 -19.842 6.820   1.00 12.03 ?  45  HIS   B N    1 
ATOM   4650 C  CA   . HIS   B 1 45  ? 52.597 -20.672 5.617   1.00 11.97 ?  45  HIS   B CA   1 
ATOM   4651 C  C    . HIS   B 1 45  ? 53.614 -21.797 5.773   1.00 14.25 ?  45  HIS   B C    1 
ATOM   4652 O  O    . HIS   B 1 45  ? 54.674 -21.810 5.157   1.00 16.39 ?  45  HIS   B O    1 
ATOM   4653 C  CB   . HIS   B 1 45  ? 52.916 -19.820 4.402   1.00 11.95 ?  45  HIS   B CB   1 
ATOM   4654 C  CG   . HIS   B 1 45  ? 52.048 -18.615 4.289   1.00 11.64 ?  45  HIS   B CG   1 
ATOM   4655 N  ND1  . HIS   B 1 45  ? 50.671 -18.692 4.256   1.00 12.04 ?  45  HIS   B ND1  1 
ATOM   4656 C  CD2  . HIS   B 1 45  ? 52.368 -17.302 4.219   1.00 12.51 ?  45  HIS   B CD2  1 
ATOM   4657 C  CE1  . HIS   B 1 45  ? 50.186 -17.466 4.154   1.00 11.53 ?  45  HIS   B CE1  1 
ATOM   4658 N  NE2  . HIS   B 1 45  ? 51.192 -16.607 4.124   1.00 12.04 ?  45  HIS   B NE2  1 
ATOM   4659 H  H    . HIS   B 1 45  ? 53.159 -19.200 6.802   1.00 14.45 ?  45  HIS   B H    1 
ATOM   4660 H  HA   . HIS   B 1 45  ? 51.715 -21.065 5.489   1.00 14.38 ?  45  HIS   B HA   1 
ATOM   4661 H  HB2  . HIS   B 1 45  ? 53.834 -19.527 4.453   1.00 14.35 ?  45  HIS   B HB2  1 
ATOM   4662 H  HB3  . HIS   B 1 45  ? 52.785 -20.361 3.599   1.00 14.35 ?  45  HIS   B HB3  1 
ATOM   4663 H  HD2  . HIS   B 1 45  ? 53.225 -16.942 4.221   1.00 15.03 ?  45  HIS   B HD2  1 
ATOM   4664 H  HE1  . HIS   B 1 45  ? 49.284 -17.245 4.100   1.00 13.85 ?  45  HIS   B HE1  1 
ATOM   4665 H  HE2  . HIS   B 1 45  ? 51.118 -15.753 4.069   1.00 14.46 ?  45  HIS   B HE2  1 
ATOM   4666 N  N    A GLY   B 1 46  ? 53.246 -22.773 6.599   0.50 15.13 ?  46  GLY   B N    1 
ATOM   4667 N  N    B GLY   B 1 46  ? 53.261 -22.757 6.618   0.50 15.08 ?  46  GLY   B N    1 
ATOM   4668 C  CA   A GLY   B 1 46  ? 54.172 -23.820 6.991   0.50 16.87 ?  46  GLY   B CA   1 
ATOM   4669 C  CA   B GLY   B 1 46  ? 54.187 -23.818 6.954   0.50 16.71 ?  46  GLY   B CA   1 
ATOM   4670 C  C    A GLY   B 1 46  ? 54.228 -25.056 6.114   0.50 18.43 ?  46  GLY   B C    1 
ATOM   4671 C  C    B GLY   B 1 46  ? 54.216 -24.974 5.976   0.50 18.35 ?  46  GLY   B C    1 
ATOM   4672 O  O    A GLY   B 1 46  ? 55.315 -25.516 5.753   0.50 20.61 ?  46  GLY   B O    1 
ATOM   4673 O  O    B GLY   B 1 46  ? 55.256 -25.276 5.382   0.50 20.05 ?  46  GLY   B O    1 
ATOM   4674 H  H    A GLY   B 1 46  ? 52.463 -22.834 6.962   0.50 18.17 ?  46  GLY   B H    1 
ATOM   4675 H  H    B GLY   B 1 46  ? 52.495 -22.804 7.019   0.50 18.11 ?  46  GLY   B H    1 
ATOM   4676 H  HA2  A GLY   B 1 46  ? 55.063 -23.439 7.029   0.50 20.26 ?  46  GLY   B HA2  1 
ATOM   4677 H  HA2  B GLY   B 1 46  ? 55.080 -23.443 7.008   0.50 20.06 ?  46  GLY   B HA2  1 
ATOM   4678 H  HA3  A GLY   B 1 46  ? 53.939 -24.118 7.882   0.50 20.26 ?  46  GLY   B HA3  1 
ATOM   4679 H  HA3  B GLY   B 1 46  ? 53.956 -24.168 7.828   0.50 20.06 ?  46  GLY   B HA3  1 
ATOM   4680 N  N    . GLY   B 1 47  ? 53.073 -25.629 5.787   1.00 18.13 ?  47  GLY   B N    1 
ATOM   4681 C  CA   . GLY   B 1 47  ? 53.018 -26.896 5.088   1.00 16.00 ?  47  GLY   B CA   1 
ATOM   4682 C  C    . GLY   B 1 47  ? 52.101 -26.874 3.882   1.00 13.54 ?  47  GLY   B C    1 
ATOM   4683 O  O    . GLY   B 1 47  ? 51.446 -25.874 3.591   1.00 13.83 ?  47  GLY   B O    1 
ATOM   4684 H  H    A GLY   B 1 47  ? 52.300 -25.306 5.983   0.50 21.77 ?  47  GLY   B H    1 
ATOM   4685 H  H    B GLY   B 1 47  ? 52.307 -25.352 6.064   0.50 21.77 ?  47  GLY   B H    1 
ATOM   4686 H  HA2  . GLY   B 1 47  ? 53.906 -27.141 4.782   1.00 19.21 ?  47  GLY   B HA2  1 
ATOM   4687 H  HA3  . GLY   B 1 47  ? 52.708 -27.582 5.698   1.00 19.21 ?  47  GLY   B HA3  1 
ATOM   4688 N  N    . GLY   B 1 48  ? 52.052 -28.014 3.195   1.00 12.83 ?  48  GLY   B N    1 
ATOM   4689 C  CA   . GLY   B 1 48  ? 51.119 -28.155 2.094   1.00 12.77 ?  48  GLY   B CA   1 
ATOM   4690 C  C    . GLY   B 1 48  ? 51.259 -27.049 1.074   1.00 12.36 ?  48  GLY   B C    1 
ATOM   4691 O  O    . GLY   B 1 48  ? 52.363 -26.587 0.757   1.00 12.86 ?  48  GLY   B O    1 
ATOM   4692 H  H    . GLY   B 1 48  ? 52.548 -28.694 3.341   1.00 15.41 ?  48  GLY   B H    1 
ATOM   4693 H  HA2  . GLY   B 1 48  ? 51.272 -29.004 1.651   1.00 15.34 ?  48  GLY   B HA2  1 
ATOM   4694 H  HA3  . GLY   B 1 48  ? 50.212 -28.143 2.433   1.00 15.34 ?  48  GLY   B HA3  1 
ATOM   4695 N  N    . VAL   B 1 49  ? 50.113 -26.614 0.547   1.00 12.16 ?  49  VAL   B N    1 
ATOM   4696 C  CA   . VAL   B 1 49  ? 50.096 -25.590 -0.495  1.00 12.16 ?  49  VAL   B CA   1 
ATOM   4697 C  C    . VAL   B 1 49  ? 50.753 -24.304 -0.005  1.00 10.99 ?  49  VAL   B C    1 
ATOM   4698 O  O    . VAL   B 1 49  ? 51.541 -23.687 -0.726  1.00 11.83 ?  49  VAL   B O    1 
ATOM   4699 C  CB   . VAL   B 1 49  ? 48.655 -25.344 -0.985  1.00 13.49 ?  49  VAL   B CB   1 
ATOM   4700 C  CG1  . VAL   B 1 49  ? 48.584 -24.098 -1.859  1.00 13.40 ?  49  VAL   B CG1  1 
ATOM   4701 C  CG2  . VAL   B 1 49  ? 48.127 -26.563 -1.738  1.00 14.79 ?  49  VAL   B CG2  1 
ATOM   4702 H  H    . VAL   B 1 49  ? 49.330 -26.897 0.772   1.00 14.61 ?  49  VAL   B H    1 
ATOM   4703 H  HA   . VAL   B 1 49  ? 50.607 -25.910 -1.255  1.00 14.60 ?  49  VAL   B HA   1 
ATOM   4704 H  HB   . VAL   B 1 49  ? 48.081 -25.200 -0.218  1.00 16.20 ?  49  VAL   B HB   1 
ATOM   4705 H  HG11 . VAL   B 1 49  ? 47.756 -24.117 -2.366  1.00 16.10 ?  49  VAL   B HG11 1 
ATOM   4706 H  HG12 . VAL   B 1 49  ? 48.604 -23.310 -1.294  1.00 16.10 ?  49  VAL   B HG12 1 
ATOM   4707 H  HG13 . VAL   B 1 49  ? 49.340 -24.094 -2.466  1.00 16.10 ?  49  VAL   B HG13 1 
ATOM   4708 H  HG21 . VAL   B 1 49  ? 47.222 -26.385 -2.034  1.00 17.76 ?  49  VAL   B HG21 1 
ATOM   4709 H  HG22 . VAL   B 1 49  ? 48.699 -26.729 -2.507  1.00 17.76 ?  49  VAL   B HG22 1 
ATOM   4710 H  HG23 . VAL   B 1 49  ? 48.140 -27.328 -1.145  1.00 17.76 ?  49  VAL   B HG23 1 
ATOM   4711 N  N    . ALA   B 1 50  ? 50.409 -23.859 1.205   1.00 10.95 ?  50  ALA   B N    1 
ATOM   4712 C  CA   . ALA   B 1 50  ? 50.934 -22.583 1.684   1.00 10.81 ?  50  ALA   B CA   1 
ATOM   4713 C  C    . ALA   B 1 50  ? 52.453 -22.615 1.783   1.00 11.29 ?  50  ALA   B C    1 
ATOM   4714 O  O    . ALA   B 1 50  ? 53.131 -21.646 1.417   1.00 11.10 ?  50  ALA   B O    1 
ATOM   4715 C  CB   . ALA   B 1 50  ? 50.307 -22.224 3.031   1.00 11.28 ?  50  ALA   B CB   1 
ATOM   4716 H  H    . ALA   B 1 50  ? 49.890 -24.267 1.755   1.00 13.16 ?  50  ALA   B H    1 
ATOM   4717 H  HA   . ALA   B 1 50  ? 50.703 -21.892 1.055   1.00 12.98 ?  50  ALA   B HA   1 
ATOM   4718 H  HB1  . ALA   B 1 50  ? 50.670 -21.375 3.333   1.00 13.55 ?  50  ALA   B HB1  1 
ATOM   4719 H  HB2  . ALA   B 1 50  ? 49.347 -22.154 2.922   1.00 13.55 ?  50  ALA   B HB2  1 
ATOM   4720 H  HB3  . ALA   B 1 50  ? 50.517 -22.919 3.677   1.00 13.55 ?  50  ALA   B HB3  1 
ATOM   4721 N  N    . GLY   B 1 51  ? 53.007 -23.709 2.298   1.00 11.60 ?  51  GLY   B N    1 
ATOM   4722 C  CA   . GLY   B 1 51  ? 54.451 -23.804 2.375   1.00 12.37 ?  51  GLY   B CA   1 
ATOM   4723 C  C    . GLY   B 1 51  ? 55.098 -23.756 1.007   1.00 12.19 ?  51  GLY   B C    1 
ATOM   4724 O  O    . GLY   B 1 51  ? 56.140 -23.122 0.825   1.00 13.13 ?  51  GLY   B O    1 
ATOM   4725 H  H    . GLY   B 1 51  ? 52.584 -24.397 2.597   1.00 13.93 ?  51  GLY   B H    1 
ATOM   4726 H  HA2  . GLY   B 1 51  ? 54.800 -23.071 2.907   1.00 14.86 ?  51  GLY   B HA2  1 
ATOM   4727 H  HA3  . GLY   B 1 51  ? 54.703 -24.640 2.809   1.00 14.86 ?  51  GLY   B HA3  1 
ATOM   4728 N  N    . ALA   B 1 52  ? 54.487 -24.415 0.025   1.00 11.86 ?  52  ALA   B N    1 
ATOM   4729 C  CA   . ALA   B 1 52  ? 55.047 -24.425 -1.318  1.00 12.27 ?  52  ALA   B CA   1 
ATOM   4730 C  C    . ALA   B 1 52  ? 54.967 -23.048 -1.970  1.00 11.48 ?  52  ALA   B C    1 
ATOM   4731 O  O    . ALA   B 1 52  ? 55.936 -22.601 -2.603  1.00 12.37 ?  52  ALA   B O    1 
ATOM   4732 C  CB   . ALA   B 1 52  ? 54.333 -25.465 -2.172  1.00 12.73 ?  52  ALA   B CB   1 
ATOM   4733 H  H    . ALA   B 1 52  ? 53.748 -24.848 0.110   1.00 14.24 ?  52  ALA   B H    1 
ATOM   4734 H  HA   . ALA   B 1 52  ? 55.983 -24.671 -1.262  1.00 14.74 ?  52  ALA   B HA   1 
ATOM   4735 H  HB1  . ALA   B 1 52  ? 54.722 -25.459 -3.062  1.00 15.29 ?  52  ALA   B HB1  1 
ATOM   4736 H  HB2  . ALA   B 1 52  ? 54.452 -26.337 -1.766  1.00 15.29 ?  52  ALA   B HB2  1 
ATOM   4737 H  HB3  . ALA   B 1 52  ? 53.393 -25.243 -2.219  1.00 15.29 ?  52  ALA   B HB3  1 
ATOM   4738 N  N    . LEU   B 1 53  ? 53.822 -22.370 -1.856  1.00 11.30 ?  53  LEU   B N    1 
ATOM   4739 C  CA   . LEU   B 1 53  ? 53.712 -21.031 -2.427  1.00 11.54 ?  53  LEU   B CA   1 
ATOM   4740 C  C    . LEU   B 1 53  ? 54.721 -20.092 -1.778  1.00 11.43 ?  53  LEU   B C    1 
ATOM   4741 O  O    . LEU   B 1 53  ? 55.425 -19.342 -2.463  1.00 12.17 ?  53  LEU   B O    1 
ATOM   4742 C  CB   . LEU   B 1 53  ? 52.286 -20.497 -2.254  1.00 11.90 ?  53  LEU   B CB   1 
ATOM   4743 C  CG   . LEU   B 1 53  ? 51.152 -21.219 -2.991  1.00 12.24 ?  53  LEU   B CG   1 
ATOM   4744 C  CD1  . LEU   B 1 53  ? 49.811 -20.615 -2.633  1.00 13.67 ?  53  LEU   B CD1  1 
ATOM   4745 C  CD2  . LEU   B 1 53  ? 51.357 -21.206 -4.502  1.00 14.14 ?  53  LEU   B CD2  1 
ATOM   4746 H  H    . LEU   B 1 53  ? 53.117 -22.655 -1.459  1.00 13.58 ?  53  LEU   B H    1 
ATOM   4747 H  HA   . LEU   B 1 53  ? 53.908 -21.076 -3.379  1.00 13.86 ?  53  LEU   B HA   1 
ATOM   4748 H  HB2  . LEU   B 1 53  ? 52.072 -20.531 -1.311  1.00 14.29 ?  53  LEU   B HB2  1 
ATOM   4749 H  HB3  . LEU   B 1 53  ? 52.274 -19.580 -2.555  1.00 14.29 ?  53  LEU   B HB3  1 
ATOM   4750 H  HG   . LEU   B 1 53  ? 51.134 -22.144 -2.705  1.00 14.71 ?  53  LEU   B HG   1 
ATOM   4751 H  HD11 . LEU   B 1 53  ? 49.107 -21.093 -3.108  1.00 16.42 ?  53  LEU   B HD11 1 
ATOM   4752 H  HD12 . LEU   B 1 53  ? 49.667 -20.703 -1.673  1.00 16.42 ?  53  LEU   B HD12 1 
ATOM   4753 H  HD13 . LEU   B 1 53  ? 49.799 -19.680 -2.882  1.00 16.42 ?  53  LEU   B HD13 1 
ATOM   4754 H  HD21 . LEU   B 1 53  ? 50.638 -21.702 -4.924  1.00 16.98 ?  53  LEU   B HD21 1 
ATOM   4755 H  HD22 . LEU   B 1 53  ? 51.352 -20.288 -4.815  1.00 16.98 ?  53  LEU   B HD22 1 
ATOM   4756 H  HD23 . LEU   B 1 53  ? 52.209 -21.622 -4.709  1.00 16.98 ?  53  LEU   B HD23 1 
ATOM   4757 N  N    . ASN   B 1 54  ? 54.814 -20.122 -0.452  1.00 10.97 ?  54  ASN   B N    1 
ATOM   4758 C  CA   . ASN   B 1 54  ? 55.728 -19.209 0.216   1.00 11.69 ?  54  ASN   B CA   1 
ATOM   4759 C  C    . ASN   B 1 54  ? 57.169 -19.488 -0.184  1.00 12.48 ?  54  ASN   B C    1 
ATOM   4760 O  O    . ASN   B 1 54  ? 57.943 -18.550 -0.417  1.00 12.70 ?  54  ASN   B O    1 
ATOM   4761 C  CB   . ASN   B 1 54  ? 55.565 -19.284 1.724   1.00 12.41 ?  54  ASN   B CB   1 
ATOM   4762 C  CG   . ASN   B 1 54  ? 56.545 -18.379 2.434   1.00 12.45 ?  54  ASN   B CG   1 
ATOM   4763 O  OD1  . ASN   B 1 54  ? 56.557 -17.166 2.205   1.00 12.73 ?  54  ASN   B OD1  1 
ATOM   4764 N  ND2  . ASN   B 1 54  ? 57.393 -18.960 3.273   1.00 14.26 ?  54  ASN   B ND2  1 
ATOM   4765 H  H    . ASN   B 1 54  ? 54.371 -20.647 0.066   1.00 13.17 ?  54  ASN   B H    1 
ATOM   4766 H  HA   . ASN   B 1 54  ? 55.517 -18.305 -0.060  1.00 14.04 ?  54  ASN   B HA   1 
ATOM   4767 H  HB2  . ASN   B 1 54  ? 54.666 -19.004 1.962   1.00 14.91 ?  54  ASN   B HB2  1 
ATOM   4768 H  HB3  . ASN   B 1 54  ? 55.722 -20.193 2.020   1.00 14.91 ?  54  ASN   B HB3  1 
ATOM   4769 H  HD21 . ASN   B 1 54  ? 57.974 -18.485 3.694   1.00 17.13 ?  54  ASN   B HD21 1 
ATOM   4770 H  HD22 . ASN   B 1 54  ? 57.366 -19.811 3.395   1.00 17.13 ?  54  ASN   B HD22 1 
ATOM   4771 N  N    . LYS   B 1 55  ? 57.554 -20.768 -0.246  1.00 12.80 ?  55  LYS   B N    1 
ATOM   4772 C  CA   . LYS   B 1 55  ? 58.907 -21.110 -0.669  1.00 13.88 ?  55  LYS   B CA   1 
ATOM   4773 C  C    . LYS   B 1 55  ? 59.203 -20.565 -2.060  1.00 13.70 ?  55  LYS   B C    1 
ATOM   4774 O  O    . LYS   B 1 55  ? 60.300 -20.052 -2.311  1.00 14.17 ?  55  LYS   B O    1 
ATOM   4775 C  CB   . LYS   B 1 55  ? 59.099 -22.628 -0.620  1.00 15.46 ?  55  LYS   B CB   1 
ATOM   4776 C  CG   . LYS   B 1 55  ? 60.479 -23.092 -1.034  1.00 19.69 ?  55  LYS   B CG   1 
ATOM   4777 C  CD   . LYS   B 1 55  ? 60.649 -24.591 -0.830  1.00 23.18 ?  55  LYS   B CD   1 
ATOM   4778 C  CE   . LYS   B 1 55  ? 60.725 -24.959 0.651   1.00 26.44 ?  55  LYS   B CE   1 
ATOM   4779 N  NZ   . LYS   B 1 55  ? 61.047 -26.393 0.859   1.00 27.93 ?  55  LYS   B NZ   1 
ATOM   4780 H  H    . LYS   B 1 55  ? 57.052 -21.442 -0.053  1.00 15.38 ?  55  LYS   B H    1 
ATOM   4781 H  HA   . LYS   B 1 55  ? 59.536 -20.711 -0.053  1.00 16.67 ?  55  LYS   B HA   1 
ATOM   4782 H  HB2  . LYS   B 1 55  ? 58.943 -22.927 0.290   1.00 18.57 ?  55  LYS   B HB2  1 
ATOM   4783 H  HB3  . LYS   B 1 55  ? 58.457 -23.045 -1.215  1.00 18.57 ?  55  LYS   B HB3  1 
ATOM   4784 H  HG2  . LYS   B 1 55  ? 60.617 -22.898 -1.975  1.00 23.64 ?  55  LYS   B HG2  1 
ATOM   4785 H  HG3  . LYS   B 1 55  ? 61.147 -22.635 -0.497  1.00 23.64 ?  55  LYS   B HG3  1 
ATOM   4786 H  HD2  . LYS   B 1 55  ? 59.889 -25.055 -1.217  1.00 27.83 ?  55  LYS   B HD2  1 
ATOM   4787 H  HD3  . LYS   B 1 55  ? 61.471 -24.884 -1.255  1.00 27.83 ?  55  LYS   B HD3  1 
ATOM   4788 H  HE2  . LYS   B 1 55  ? 61.418 -24.423 1.072   1.00 31.74 ?  55  LYS   B HE2  1 
ATOM   4789 H  HE3  . LYS   B 1 55  ? 59.867 -24.775 1.067   1.00 31.74 ?  55  LYS   B HE3  1 
ATOM   4790 H  HZ1  . LYS   B 1 55  ? 61.059 -26.577 1.731   1.00 33.53 ?  55  LYS   B HZ1  1 
ATOM   4791 H  HZ2  . LYS   B 1 55  ? 60.430 -26.900 0.466   1.00 33.53 ?  55  LYS   B HZ2  1 
ATOM   4792 H  HZ3  . LYS   B 1 55  ? 61.842 -26.580 0.511   1.00 33.53 ?  55  LYS   B HZ3  1 
ATOM   4793 N  N    . ALA   B 1 56  ? 58.236 -20.655 -2.976  1.00 13.09 ?  56  ALA   B N    1 
ATOM   4794 C  CA   . ALA   B 1 56  ? 58.451 -20.149 -4.326  1.00 13.87 ?  56  ALA   B CA   1 
ATOM   4795 C  C    . ALA   B 1 56  ? 58.724 -18.651 -4.322  1.00 13.73 ?  56  ALA   B C    1 
ATOM   4796 O  O    . ALA   B 1 56  ? 59.457 -18.151 -5.189  1.00 14.90 ?  56  ALA   B O    1 
ATOM   4797 C  CB   . ALA   B 1 56  ? 57.249 -20.481 -5.212  1.00 14.42 ?  56  ALA   B CB   1 
ATOM   4798 H  H    . ALA   B 1 56  ? 57.454 -20.991 -2.840  1.00 15.72 ?  56  ALA   B H    1 
ATOM   4799 H  HA   . ALA   B 1 56  ? 59.227 -20.589 -4.703  1.00 16.66 ?  56  ALA   B HA   1 
ATOM   4800 H  HB1  . ALA   B 1 56  ? 57.417 -20.146 -6.110  1.00 17.32 ?  56  ALA   B HB1  1 
ATOM   4801 H  HB2  . ALA   B 1 56  ? 57.134 -21.445 -5.240  1.00 17.32 ?  56  ALA   B HB2  1 
ATOM   4802 H  HB3  . ALA   B 1 56  ? 56.457 -20.062 -4.847  1.00 17.32 ?  56  ALA   B HB3  1 
ATOM   4803 N  N    . THR   B 1 57  ? 58.159 -17.921 -3.355  1.00 13.56 ?  57  THR   B N    1 
ATOM   4804 C  CA   . THR   B 1 57  ? 58.396 -16.485 -3.227  1.00 13.38 ?  57  THR   B CA   1 
ATOM   4805 C  C    . THR   B 1 57  ? 59.650 -16.154 -2.418  1.00 13.80 ?  57  THR   B C    1 
ATOM   4806 O  O    . THR   B 1 57  ? 59.885 -14.977 -2.109  1.00 14.44 ?  57  THR   B O    1 
ATOM   4807 C  CB   . THR   B 1 57  ? 57.195 -15.759 -2.594  1.00 12.75 ?  57  THR   B CB   1 
ATOM   4808 O  OG1  . THR   B 1 57  ? 57.176 -15.967 -1.175  1.00 12.91 ?  57  THR   B OG1  1 
ATOM   4809 C  CG2  . THR   B 1 57  ? 55.874 -16.183 -3.229  1.00 12.98 ?  57  THR   B CG2  1 
ATOM   4810 H  H    . THR   B 1 57  ? 57.624 -18.240 -2.761  1.00 16.29 ?  57  THR   B H    1 
ATOM   4811 H  HA   . THR   B 1 57  ? 58.515 -16.119 -4.117  1.00 16.06 ?  57  THR   B HA   1 
ATOM   4812 H  HB   . THR   B 1 57  ? 57.296 -14.809 -2.761  1.00 15.32 ?  57  THR   B HB   1 
ATOM   4813 H  HG1  . THR   B 1 57  ? 57.113 -16.786 -1.007  1.00 15.50 ?  57  THR   B HG1  1 
ATOM   4814 H  HG21 . THR   B 1 57  ? 55.147 -15.655 -2.868  1.00 15.59 ?  57  THR   B HG21 1 
ATOM   4815 H  HG22 . THR   B 1 57  ? 55.911 -16.058 -4.190  1.00 15.59 ?  57  THR   B HG22 1 
ATOM   4816 H  HG23 . THR   B 1 57  ? 55.702 -17.120 -3.043  1.00 15.59 ?  57  THR   B HG23 1 
ATOM   4817 N  N    . ASN   B 1 58  ? 60.453 -17.155 -2.068  1.00 14.75 ?  58  ASN   B N    1 
ATOM   4818 C  CA   . ASN   B 1 58  ? 61.651 -16.940 -1.261  1.00 17.11 ?  58  ASN   B CA   1 
ATOM   4819 C  C    . ASN   B 1 58  ? 61.313 -16.231 0.049   1.00 15.36 ?  58  ASN   B C    1 
ATOM   4820 O  O    . ASN   B 1 58  ? 62.047 -15.353 0.513   1.00 16.14 ?  58  ASN   B O    1 
ATOM   4821 C  CB   . ASN   B 1 58  ? 62.736 -16.189 -2.038  1.00 24.15 ?  58  ASN   B CB   1 
ATOM   4822 C  CG   . ASN   B 1 58  ? 64.106 -16.328 -1.404  1.00 33.34 ?  58  ASN   B CG   1 
ATOM   4823 O  OD1  . ASN   B 1 58  ? 64.421 -17.356 -0.803  1.00 36.27 ?  58  ASN   B OD1  1 
ATOM   4824 N  ND2  . ASN   B 1 58  ? 64.925 -15.292 -1.530  1.00 36.17 ?  58  ASN   B ND2  1 
ATOM   4825 H  H    . ASN   B 1 58  ? 60.320 -17.981 -2.281  1.00 17.71 ?  58  ASN   B H    1 
ATOM   4826 H  HA   . ASN   B 1 58  ? 62.016 -17.811 -1.035  1.00 20.55 ?  58  ASN   B HA   1 
ATOM   4827 H  HB2  . ASN   B 1 58  ? 62.784 -16.544 -2.942  1.00 29.00 ?  58  ASN   B HB2  1 
ATOM   4828 H  HB3  . ASN   B 1 58  ? 62.513 -15.247 -2.065  1.00 29.00 ?  58  ASN   B HB3  1 
ATOM   4829 H  HD21 . ASN   B 1 58  ? 65.714 -15.323 -1.188  1.00 43.42 ?  58  ASN   B HD21 1 
ATOM   4830 H  HD22 . ASN   B 1 58  ? 64.668 -14.590 -1.954  1.00 43.42 ?  58  ASN   B HD22 1 
ATOM   4831 N  N    . ASN   B 1 59  ? 60.190 -16.621 0.654   1.00 14.33 ?  59  ASN   B N    1 
ATOM   4832 C  CA   . ASN   B 1 59  ? 59.710 -16.148 1.953   1.00 14.35 ?  59  ASN   B CA   1 
ATOM   4833 C  C    . ASN   B 1 59  ? 59.114 -14.739 1.897   1.00 13.76 ?  59  ASN   B C    1 
ATOM   4834 O  O    . ASN   B 1 59  ? 58.689 -14.233 2.941   1.00 14.08 ?  59  ASN   B O    1 
ATOM   4835 C  CB   . ASN   B 1 59  ? 60.780 -16.209 3.060   1.00 15.58 ?  59  ASN   B CB   1 
ATOM   4836 C  CG   . ASN   B 1 59  ? 60.190 -16.385 4.439   1.00 16.60 ?  59  ASN   B CG   1 
ATOM   4837 O  OD1  . ASN   B 1 59  ? 59.363 -17.273 4.665   1.00 16.74 ?  59  ASN   B OD1  1 
ATOM   4838 N  ND2  . ASN   B 1 59  ? 60.611 -15.543 5.376   1.00 17.30 ?  59  ASN   B ND2  1 
ATOM   4839 H  H    . ASN   B 1 59  ? 59.654 -17.203 0.309   1.00 17.21 ?  59  ASN   B H    1 
ATOM   4840 H  HA   . ASN   B 1 59  ? 58.999 -16.742 2.233   1.00 17.23 ?  59  ASN   B HA   1 
ATOM   4841 H  HB2  . ASN   B 1 59  ? 61.367 -16.964 2.900   1.00 18.71 ?  59  ASN   B HB2  1 
ATOM   4842 H  HB3  . ASN   B 1 59  ? 61.287 -15.386 3.064   1.00 18.71 ?  59  ASN   B HB3  1 
ATOM   4843 H  HD21 . ASN   B 1 59  ? 60.302 -15.600 6.179   1.00 20.77 ?  59  ASN   B HD21 1 
ATOM   4844 H  HD22 . ASN   B 1 59  ? 61.188 -14.938 5.181   1.00 20.77 ?  59  ASN   B HD22 1 
ATOM   4845 N  N    . ALA   B 1 60  ? 59.049 -14.094 0.728   1.00 13.64 ?  60  ALA   B N    1 
ATOM   4846 C  CA   . ALA   B 1 60  ? 58.454 -12.760 0.661   1.00 13.44 ?  60  ALA   B CA   1 
ATOM   4847 C  C    . ALA   B 1 60  ? 56.986 -12.789 1.066   1.00 12.78 ?  60  ALA   B C    1 
ATOM   4848 O  O    . ALA   B 1 60  ? 56.480 -11.840 1.678   1.00 13.37 ?  60  ALA   B O    1 
ATOM   4849 C  CB   . ALA   B 1 60  ? 58.613 -12.179 -0.744  1.00 14.58 ?  60  ALA   B CB   1 
ATOM   4850 H  H    . ALA   B 1 60  ? 59.335 -14.405 -0.020  1.00 16.38 ?  60  ALA   B H    1 
ATOM   4851 H  HA   . ALA   B 1 60  ? 58.918 -12.182 1.283   1.00 16.14 ?  60  ALA   B HA   1 
ATOM   4852 H  HB1  . ALA   B 1 60  ? 58.217 -11.297 -0.765  1.00 17.51 ?  60  ALA   B HB1  1 
ATOM   4853 H  HB2  . ALA   B 1 60  ? 59.562 -12.121 -0.953  1.00 17.51 ?  60  ALA   B HB2  1 
ATOM   4854 H  HB3  . ALA   B 1 60  ? 58.172 -12.761 -1.380  1.00 17.51 ?  60  ALA   B HB3  1 
ATOM   4855 N  N    . MET   B 1 61  ? 56.279 -13.863 0.718   1.00 12.33 ?  61  MET   B N    1 
ATOM   4856 C  CA   . MET   B 1 61  ? 54.883 -13.985 1.115   1.00 11.87 ?  61  MET   B CA   1 
ATOM   4857 C  C    . MET   B 1 61  ? 54.749 -13.996 2.638   1.00 11.93 ?  61  MET   B C    1 
ATOM   4858 O  O    . MET   B 1 61  ? 53.848 -13.353 3.193   1.00 11.90 ?  61  MET   B O    1 
ATOM   4859 C  CB   . MET   B 1 61  ? 54.295 -15.246 0.477   1.00 11.63 ?  61  MET   B CB   1 
ATOM   4860 C  CG   . MET   B 1 61  ? 52.852 -15.546 0.896   1.00 11.26 ?  61  MET   B CG   1 
ATOM   4861 S  SD   . MET   B 1 61  ? 52.219 -17.054 0.136   1.00 12.31 ?  61  MET   B SD   1 
ATOM   4862 C  CE   . MET   B 1 61  ? 51.955 -16.477 -1.539  1.00 13.41 ?  61  MET   B CE   1 
ATOM   4863 H  H    . MET   B 1 61  ? 56.582 -14.532 0.260   1.00 14.81 ?  61  MET   B H    1 
ATOM   4864 H  HA   . MET   B 1 61  ? 54.392 -13.228 0.759   1.00 14.25 ?  61  MET   B HA   1 
ATOM   4865 H  HB2  . MET   B 1 61  ? 54.301 -15.144 -0.491  1.00 13.96 ?  61  MET   B HB2  1 
ATOM   4866 H  HB3  . MET   B 1 61  ? 54.838 -16.009 0.725   1.00 13.96 ?  61  MET   B HB3  1 
ATOM   4867 H  HG2  . MET   B 1 61  ? 52.819 -15.661 1.859   1.00 13.53 ?  61  MET   B HG2  1 
ATOM   4868 H  HG3  . MET   B 1 61  ? 52.284 -14.809 0.628   1.00 13.53 ?  61  MET   B HG3  1 
ATOM   4869 H  HE1  . MET   B 1 61  ? 51.577 -17.197 -2.065  1.00 16.10 ?  61  MET   B HE1  1 
ATOM   4870 H  HE2  . MET   B 1 61  ? 51.345 -15.721 -1.524  1.00 16.10 ?  61  MET   B HE2  1 
ATOM   4871 H  HE3  . MET   B 1 61  ? 52.808 -16.203 -1.916  1.00 16.10 ?  61  MET   B HE3  1 
ATOM   4872 N  N    . GLN   B 1 62  ? 55.635 -14.712 3.335   1.00 11.72 ?  62  GLN   B N    1 
ATOM   4873 C  CA   . GLN   B 1 62  ? 55.527 -14.774 4.788   1.00 12.09 ?  62  GLN   B CA   1 
ATOM   4874 C  C    . GLN   B 1 62  ? 55.811 -13.421 5.423   1.00 12.29 ?  62  GLN   B C    1 
ATOM   4875 O  O    . GLN   B 1 62  ? 55.129 -13.026 6.374   1.00 12.87 ?  62  GLN   B O    1 
ATOM   4876 C  CB   . GLN   B 1 62  ? 56.477 -15.827 5.353   1.00 12.46 ?  62  GLN   B CB   1 
ATOM   4877 C  CG   . GLN   B 1 62  ? 56.257 -16.091 6.836   1.00 12.79 ?  62  GLN   B CG   1 
ATOM   4878 C  CD   . GLN   B 1 62  ? 54.885 -16.688 7.079   1.00 12.50 ?  62  GLN   B CD   1 
ATOM   4879 O  OE1  . GLN   B 1 62  ? 54.631 -17.836 6.724   1.00 12.89 ?  62  GLN   B OE1  1 
ATOM   4880 N  NE2  . GLN   B 1 62  ? 53.969 -15.892 7.624   1.00 12.77 ?  62  GLN   B NE2  1 
ATOM   4881 H  H    . GLN   B 1 62  ? 56.286 -15.165 2.992   1.00 14.07 ?  62  GLN   B H    1 
ATOM   4882 H  HA   . GLN   B 1 62  ? 54.621 -15.030 5.020   1.00 14.52 ?  62  GLN   B HA   1 
ATOM   4883 H  HB2  . GLN   B 1 62  ? 56.345 -16.663 4.877   1.00 14.96 ?  62  GLN   B HB2  1 
ATOM   4884 H  HB3  . GLN   B 1 62  ? 57.391 -15.522 5.236   1.00 14.96 ?  62  GLN   B HB3  1 
ATOM   4885 H  HG2  . GLN   B 1 62  ? 56.924 -16.726 7.148   1.00 15.36 ?  62  GLN   B HG2  1 
ATOM   4886 H  HG3  . GLN   B 1 62  ? 56.325 -15.262 7.329   1.00 15.36 ?  62  GLN   B HG3  1 
ATOM   4887 H  HE21 . GLN   B 1 62  ? 54.178 -15.088 7.842   1.00 15.34 ?  62  GLN   B HE21 1 
ATOM   4888 H  HE22 . GLN   B 1 62  ? 53.177 -16.189 7.771   1.00 15.34 ?  62  GLN   B HE22 1 
ATOM   4889 N  N    . VAL   B 1 63  ? 56.827 -12.708 4.933   1.00 13.04 ?  63  VAL   B N    1 
ATOM   4890 C  CA   . VAL   B 1 63  ? 57.134 -11.389 5.483   1.00 13.86 ?  63  VAL   B CA   1 
ATOM   4891 C  C    . VAL   B 1 63  ? 55.944 -10.452 5.304   1.00 13.03 ?  63  VAL   B C    1 
ATOM   4892 O  O    . VAL   B 1 63  ? 55.527 -9.756  6.240   1.00 13.81 ?  63  VAL   B O    1 
ATOM   4893 C  CB   . VAL   B 1 63  ? 58.422 -10.830 4.852   1.00 15.19 ?  63  VAL   B CB   1 
ATOM   4894 C  CG1  . VAL   B 1 63  ? 58.659 -9.388  5.303   1.00 15.92 ?  63  VAL   B CG1  1 
ATOM   4895 C  CG2  . VAL   B 1 63  ? 59.604 -11.712 5.233   1.00 15.72 ?  63  VAL   B CG2  1 
ATOM   4896 H  H    . VAL   B 1 63  ? 57.340 -12.961 4.284   1.00 15.66 ?  63  VAL   B H    1 
ATOM   4897 H  HA   . VAL   B 1 63  ? 57.297 -11.488 6.431   1.00 16.64 ?  63  VAL   B HA   1 
ATOM   4898 H  HB   . VAL   B 1 63  ? 58.346 -10.840 3.886   1.00 18.25 ?  63  VAL   B HB   1 
ATOM   4899 H  HG11 . VAL   B 1 63  ? 59.574 -9.140  5.101   1.00 19.12 ?  63  VAL   B HG11 1 
ATOM   4900 H  HG12 . VAL   B 1 63  ? 58.046 -8.806  4.831   1.00 19.12 ?  63  VAL   B HG12 1 
ATOM   4901 H  HG13 . VAL   B 1 63  ? 58.505 -9.331  6.260   1.00 19.12 ?  63  VAL   B HG13 1 
ATOM   4902 H  HG21 . VAL   B 1 63  ? 60.418 -11.335 4.859   1.00 18.88 ?  63  VAL   B HG21 1 
ATOM   4903 H  HG22 . VAL   B 1 63  ? 59.676 -11.743 6.203   1.00 18.88 ?  63  VAL   B HG22 1 
ATOM   4904 H  HG23 . VAL   B 1 63  ? 59.464 -12.605 4.886   1.00 18.88 ?  63  VAL   B HG23 1 
ATOM   4905 N  N    . GLU   B 1 64  ? 55.371 -10.439 4.101   1.00 12.65 ?  64  GLU   B N    1 
ATOM   4906 C  CA   . GLU   B 1 64  ? 54.202 -9.607  3.836   1.00 12.40 ?  64  GLU   B CA   1 
ATOM   4907 C  C    . GLU   B 1 64  ? 53.024 -10.013 4.715   1.00 12.12 ?  64  GLU   B C    1 
ATOM   4908 O  O    . GLU   B 1 64  ? 52.280 -9.157  5.219   1.00 12.62 ?  64  GLU   B O    1 
ATOM   4909 C  CB   . GLU   B 1 64  ? 53.835 -9.751  2.358   1.00 12.33 ?  64  GLU   B CB   1 
ATOM   4910 C  CG   . GLU   B 1 64  ? 52.568 -9.022  1.930   1.00 12.88 ?  64  GLU   B CG   1 
ATOM   4911 C  CD   . GLU   B 1 64  ? 52.036 -9.518  0.592   1.00 13.48 ?  64  GLU   B CD   1 
ATOM   4912 O  OE1  . GLU   B 1 64  ? 52.217 -10.725 0.266   1.00 14.29 ?  64  GLU   B OE1  1 
ATOM   4913 O  OE2  . GLU   B 1 64  ? 51.416 -8.704  -0.131  1.00 14.23 -1 64  GLU   B OE2  1 
ATOM   4914 H  H    . GLU   B 1 64  ? 55.639 -10.906 3.423   1.00 15.19 ?  64  GLU   B H    1 
ATOM   4915 H  HA   . GLU   B 1 64  ? 54.420 -8.679  4.012   1.00 14.90 ?  64  GLU   B HA   1 
ATOM   4916 H  HB2  . GLU   B 1 64  ? 54.563 -9.391  1.818   1.00 14.81 ?  64  GLU   B HB2  1 
ATOM   4917 H  HB3  . GLU   B 1 64  ? 53.716 -10.687 2.155   1.00 14.81 ?  64  GLU   B HB3  1 
ATOM   4918 H  HG2  . GLU   B 1 64  ? 51.869 -9.160  2.592   1.00 15.47 ?  64  GLU   B HG2  1 
ATOM   4919 H  HG3  . GLU   B 1 64  ? 52.755 -8.074  1.847   1.00 15.47 ?  64  GLU   B HG3  1 
ATOM   4920 N  N    . SER   B 1 65  ? 52.838 -11.321 4.897   1.00 11.91 ?  65  SER   B N    1 
ATOM   4921 C  CA   . SER   B 1 65  ? 51.725 -11.819 5.695   1.00 11.78 ?  65  SER   B CA   1 
ATOM   4922 C  C    . SER   B 1 65  ? 51.861 -11.422 7.158   1.00 11.98 ?  65  SER   B C    1 
ATOM   4923 O  O    . SER   B 1 65  ? 50.864 -11.061 7.797   1.00 12.50 ?  65  SER   B O    1 
ATOM   4924 C  CB   . SER   B 1 65  ? 51.634 -13.340 5.568   1.00 12.00 ?  65  SER   B CB   1 
ATOM   4925 O  OG   . SER   B 1 65  ? 51.297 -13.739 4.247   1.00 12.27 ?  65  SER   B OG   1 
ATOM   4926 H  H    . SER   B 1 65  ? 53.348 -11.942 4.577   1.00 14.31 ?  65  SER   B H    1 
ATOM   4927 H  HA   . SER   B 1 65  ? 50.899 -11.438 5.357   1.00 14.15 ?  65  SER   B HA   1 
ATOM   4928 H  HB2  . SER   B 1 65  ? 52.487 -13.729 5.801   1.00 14.41 ?  65  SER   B HB2  1 
ATOM   4929 H  HB3  . SER   B 1 65  ? 50.945 -13.662 6.175   1.00 14.41 ?  65  SER   B HB3  1 
ATOM   4930 H  HG   . SER   B 1 65  ? 51.878 -13.455 3.703   1.00 14.74 ?  65  SER   B HG   1 
ATOM   4931 N  N    . ASP   B 1 66  ? 53.071 -11.524 7.720   1.00 12.61 ?  66  ASP   B N    1 
ATOM   4932 C  CA   . ASP   B 1 66  ? 53.264 -11.127 9.112   1.00 12.83 ?  66  ASP   B CA   1 
ATOM   4933 C  C    . ASP   B 1 66  ? 52.947 -9.649  9.313   1.00 13.04 ?  66  ASP   B C    1 
ATOM   4934 O  O    . ASP   B 1 66  ? 52.375 -9.258  10.338  1.00 13.45 ?  66  ASP   B O    1 
ATOM   4935 C  CB   . ASP   B 1 66  ? 54.699 -11.430 9.550   1.00 14.08 ?  66  ASP   B CB   1 
ATOM   4936 C  CG   . ASP   B 1 66  ? 54.974 -12.923 9.714   1.00 15.80 ?  66  ASP   B CG   1 
ATOM   4937 O  OD1  . ASP   B 1 66  ? 54.029 -13.742 9.648   1.00 16.29 ?  66  ASP   B OD1  1 
ATOM   4938 O  OD2  . ASP   B 1 66  ? 56.156 -13.287 9.925   1.00 18.61 -1 66  ASP   B OD2  1 
ATOM   4939 H  H    . ASP   B 1 66  ? 53.776 -11.820 7.327   1.00 15.15 ?  66  ASP   B H    1 
ATOM   4940 H  HA   . ASP   B 1 66  ? 52.669 -11.636 9.677   1.00 15.41 ?  66  ASP   B HA   1 
ATOM   4941 H  HB2  . ASP   B 1 66  ? 55.316 -11.091 8.884   1.00 16.91 ?  66  ASP   B HB2  1 
ATOM   4942 H  HB3  . ASP   B 1 66  ? 54.868 -10.999 10.406  1.00 16.91 ?  66  ASP   B HB3  1 
ATOM   4943 N  N    . ASP   B 1 67  ? 53.323 -8.806  8.351   1.00 12.67 ?  67  ASP   B N    1 
ATOM   4944 C  CA   . ASP   B 1 67  ? 52.976 -7.395  8.442   1.00 13.22 ?  67  ASP   B CA   1 
ATOM   4945 C  C    . ASP   B 1 67  ? 51.465 -7.192  8.360   1.00 13.56 ?  67  ASP   B C    1 
ATOM   4946 O  O    . ASP   B 1 67  ? 50.903 -6.381  9.106   1.00 13.87 ?  67  ASP   B O    1 
ATOM   4947 C  CB   . ASP   B 1 67  ? 53.687 -6.625  7.338   1.00 14.89 ?  67  ASP   B CB   1 
ATOM   4948 C  CG   . ASP   B 1 67  ? 53.260 -5.184  7.293   1.00 16.11 ?  67  ASP   B CG   1 
ATOM   4949 O  OD1  . ASP   B 1 67  ? 53.772 -4.372  8.096   1.00 17.34 ?  67  ASP   B OD1  1 
ATOM   4950 O  OD2  . ASP   B 1 67  ? 52.375 -4.886  6.473   1.00 17.32 -1 67  ASP   B OD2  1 
ATOM   4951 H  H    . ASP   B 1 67  ? 53.781 -9.022  7.657   1.00 15.22 ?  67  ASP   B H    1 
ATOM   4952 H  HA   . ASP   B 1 67  ? 53.283 -7.043  9.292   1.00 15.87 ?  67  ASP   B HA   1 
ATOM   4953 H  HB2  . ASP   B 1 67  ? 54.646 -6.650  7.493   1.00 17.89 ?  67  ASP   B HB2  1 
ATOM   4954 H  HB3  . ASP   B 1 67  ? 53.485 -7.038  6.478   1.00 17.89 ?  67  ASP   B HB3  1 
ATOM   4955 N  N    . TYR   B 1 68  ? 50.787 -7.932  7.476   1.00 13.00 ?  68  TYR   B N    1 
ATOM   4956 C  CA   . TYR   B 1 68  ? 49.331 -7.851  7.404   1.00 13.67 ?  68  TYR   B CA   1 
ATOM   4957 C  C    . TYR   B 1 68  ? 48.698 -8.193  8.749   1.00 13.35 ?  68  TYR   B C    1 
ATOM   4958 O  O    . TYR   B 1 68  ? 47.764 -7.517  9.195   1.00 13.91 ?  68  TYR   B O    1 
ATOM   4959 C  CB   . TYR   B 1 68  ? 48.791 -8.781  6.307   1.00 14.18 ?  68  TYR   B CB   1 
ATOM   4960 C  CG   . TYR   B 1 68  ? 47.284 -8.932  6.364   1.00 15.04 ?  68  TYR   B CG   1 
ATOM   4961 C  CD1  . TYR   B 1 68  ? 46.696 -9.882  7.190   1.00 16.06 ?  68  TYR   B CD1  1 
ATOM   4962 C  CD2  . TYR   B 1 68  ? 46.452 -8.097  5.635   1.00 16.32 ?  68  TYR   B CD2  1 
ATOM   4963 C  CE1  . TYR   B 1 68  ? 45.330 -10.005 7.283   1.00 17.05 ?  68  TYR   B CE1  1 
ATOM   4964 C  CE2  . TYR   B 1 68  ? 45.070 -8.222  5.716   1.00 16.70 ?  68  TYR   B CE2  1 
ATOM   4965 C  CZ   . TYR   B 1 68  ? 44.531 -9.174  6.547   1.00 17.02 ?  68  TYR   B CZ   1 
ATOM   4966 O  OH   . TYR   B 1 68  ? 43.162 -9.296  6.645   1.00 17.87 ?  68  TYR   B OH   1 
ATOM   4967 H  H    . TYR   B 1 68  ? 51.144 -8.491  6.924   1.00 15.61 ?  68  TYR   B H    1 
ATOM   4968 H  HA   . TYR   B 1 68  ? 49.081 -6.946  7.180   1.00 16.42 ?  68  TYR   B HA   1 
ATOM   4969 H  HB2  . TYR   B 1 68  ? 49.018 -8.413  5.442   1.00 17.02 ?  68  TYR   B HB2  1 
ATOM   4970 H  HB3  . TYR   B 1 68  ? 49.183 -9.661  6.413   1.00 17.02 ?  68  TYR   B HB3  1 
ATOM   4971 H  HD1  . TYR   B 1 68  ? 47.234 -10.449 7.694   1.00 19.28 ?  68  TYR   B HD1  1 
ATOM   4972 H  HD2  . TYR   B 1 68  ? 46.825 -7.446  5.091   1.00 19.60 ?  68  TYR   B HD2  1 
ATOM   4973 H  HE1  . TYR   B 1 68  ? 44.949 -10.660 7.828   1.00 20.47 ?  68  TYR   B HE1  1 
ATOM   4974 H  HE2  . TYR   B 1 68  ? 44.517 -7.659  5.225   1.00 20.06 ?  68  TYR   B HE2  1 
ATOM   4975 H  HH   . TYR   B 1 68  ? 42.772 -8.745  6.133   1.00 21.45 ?  68  TYR   B HH   1 
ATOM   4976 N  N    . ILE   B 1 69  ? 49.180 -9.256  9.397   1.00 13.04 ?  69  ILE   B N    1 
ATOM   4977 C  CA   . ILE   B 1 69  ? 48.623 -9.686  10.677  1.00 13.61 ?  69  ILE   B CA   1 
ATOM   4978 C  C    . ILE   B 1 69  ? 48.877 -8.641  11.756  1.00 13.28 ?  69  ILE   B C    1 
ATOM   4979 O  O    . ILE   B 1 69  ? 48.006 -8.362  12.587  1.00 13.60 ?  69  ILE   B O    1 
ATOM   4980 C  CB   . ILE   B 1 69  ? 49.201 -11.063 11.064  1.00 14.51 ?  69  ILE   B CB   1 
ATOM   4981 C  CG1  . ILE   B 1 69  ? 48.667 -12.168 10.140  1.00 14.88 ?  69  ILE   B CG1  1 
ATOM   4982 C  CG2  . ILE   B 1 69  ? 48.928 -11.381 12.528  1.00 15.27 ?  69  ILE   B CG2  1 
ATOM   4983 C  CD1  . ILE   B 1 69  ? 47.190 -12.472 10.301  1.00 14.86 ?  69  ILE   B CD1  1 
ATOM   4984 H  H    . ILE   B 1 69  ? 49.826 -9.743  9.117   1.00 15.66 ?  69  ILE   B H    1 
ATOM   4985 H  HA   . ILE   B 1 69  ? 47.664 -9.785  10.586  1.00 16.34 ?  69  ILE   B HA   1 
ATOM   4986 H  HB   . ILE   B 1 69  ? 50.163 -11.024 10.949  1.00 17.43 ?  69  ILE   B HB   1 
ATOM   4987 H  HG12 . ILE   B 1 69  ? 48.816 -11.896 9.221   1.00 17.87 ?  69  ILE   B HG12 1 
ATOM   4988 H  HG13 . ILE   B 1 69  ? 49.159 -12.985 10.321  1.00 17.87 ?  69  ILE   B HG13 1 
ATOM   4989 H  HG21 . ILE   B 1 69  ? 49.066 -12.332 12.672  1.00 18.34 ?  69  ILE   B HG21 1 
ATOM   4990 H  HG22 . ILE   B 1 69  ? 49.540 -10.875 13.084  1.00 18.34 ?  69  ILE   B HG22 1 
ATOM   4991 H  HG23 . ILE   B 1 69  ? 48.012 -11.147 12.738  1.00 18.34 ?  69  ILE   B HG23 1 
ATOM   4992 H  HD11 . ILE   B 1 69  ? 46.954 -13.195 9.701   1.00 17.85 ?  69  ILE   B HD11 1 
ATOM   4993 H  HD12 . ILE   B 1 69  ? 47.017 -12.735 11.219  1.00 17.85 ?  69  ILE   B HD12 1 
ATOM   4994 H  HD13 . ILE   B 1 69  ? 46.676 -11.679 10.082  1.00 17.85 ?  69  ILE   B HD13 1 
ATOM   4995 N  N    . ALA   B 1 70  ? 50.074 -8.059  11.781  1.00 13.36 ?  70  ALA   B N    1 
ATOM   4996 C  CA   . ALA   B 1 70  ? 50.356 -7.017  12.763  1.00 13.23 ?  70  ALA   B CA   1 
ATOM   4997 C  C    . ALA   B 1 70  ? 49.357 -5.874  12.652  1.00 13.36 ?  70  ALA   B C    1 
ATOM   4998 O  O    . ALA   B 1 70  ? 48.925 -5.319  13.668  1.00 14.00 ?  70  ALA   B O    1 
ATOM   4999 C  CB   . ALA   B 1 70  ? 51.783 -6.504  12.584  1.00 14.08 ?  70  ALA   B CB   1 
ATOM   5000 H  H    . ALA   B 1 70  ? 50.720 -8.251  11.258  1.00 16.05 ?  70  ALA   B H    1 
ATOM   5001 H  HA   . ALA   B 1 70  ? 50.287 -7.394  13.657  1.00 15.89 ?  70  ALA   B HA   1 
ATOM   5002 H  HB1  . ALA   B 1 70  ? 51.969 -5.839  13.267  1.00 16.91 ?  70  ALA   B HB1  1 
ATOM   5003 H  HB2  . ALA   B 1 70  ? 52.402 -7.248  12.674  1.00 16.91 ?  70  ALA   B HB2  1 
ATOM   5004 H  HB3  . ALA   B 1 70  ? 51.870 -6.109  11.703  1.00 16.91 ?  70  ALA   B HB3  1 
ATOM   5005 N  N    . THR   B 1 71  ? 48.979 -5.511  11.429  1.00 13.77 ?  71  THR   B N    1 
ATOM   5006 C  CA   . THR   B 1 71  ? 48.090 -4.375  11.219  1.00 15.23 ?  71  THR   B CA   1 
ATOM   5007 C  C    . THR   B 1 71  ? 46.620 -4.742  11.420  1.00 15.62 ?  71  THR   B C    1 
ATOM   5008 O  O    . THR   B 1 71  ? 45.839 -3.926  11.927  1.00 17.04 ?  71  THR   B O    1 
ATOM   5009 C  CB   . THR   B 1 71  ? 48.314 -3.808  9.815   1.00 17.09 ?  71  THR   B CB   1 
ATOM   5010 O  OG1  . THR   B 1 71  ? 49.644 -3.284  9.718   1.00 18.99 ?  71  THR   B OG1  1 
ATOM   5011 C  CG2  . THR   B 1 71  ? 47.305 -2.713  9.490   1.00 18.34 ?  71  THR   B CG2  1 
ATOM   5012 H  H    . THR   B 1 71  ? 49.222 -5.910  10.711  1.00 16.53 ?  71  THR   B H    1 
ATOM   5013 H  HA   . THR   B 1 71  ? 48.314 -3.679  11.857  1.00 18.29 ?  71  THR   B HA   1 
ATOM   5014 H  HB   . THR   B 1 71  ? 48.216 -4.517  9.161   1.00 20.52 ?  71  THR   B HB   1 
ATOM   5015 H  HG1  . THR   B 1 71  ? 49.773 -2.954  8.950   1.00 22.80 ?  71  THR   B HG1  1 
ATOM   5016 H  HG21 . THR   B 1 71  ? 47.613 -2.193  8.731   1.00 22.02 ?  71  THR   B HG21 1 
ATOM   5017 H  HG22 . THR   B 1 71  ? 46.446 -3.105  9.273   1.00 22.02 ?  71  THR   B HG22 1 
ATOM   5018 H  HG23 . THR   B 1 71  ? 47.202 -2.121  10.252  1.00 22.02 ?  71  THR   B HG23 1 
ATOM   5019 N  N    . ASN   B 1 72  ? 46.225 -5.957  11.032  1.00 15.10 ?  72  ASN   B N    1 
ATOM   5020 C  CA   . ASN   B 1 72  ? 44.820 -6.314  10.907  1.00 15.73 ?  72  ASN   B CA   1 
ATOM   5021 C  C    . ASN   B 1 72  ? 44.348 -7.413  11.847  1.00 16.38 ?  72  ASN   B C    1 
ATOM   5022 O  O    . ASN   B 1 72  ? 43.131 -7.572  12.008  1.00 17.67 ?  72  ASN   B O    1 
ATOM   5023 C  CB   . ASN   B 1 72  ? 44.512 -6.739  9.464   1.00 16.51 ?  72  ASN   B CB   1 
ATOM   5024 C  CG   . ASN   B 1 72  ? 44.792 -5.636  8.473   1.00 17.60 ?  72  ASN   B CG   1 
ATOM   5025 O  OD1  . ASN   B 1 72  ? 45.807 -5.645  7.771   1.00 19.14 ?  72  ASN   B OD1  1 
ATOM   5026 N  ND2  . ASN   B 1 72  ? 43.909 -4.661  8.429   1.00 19.18 ?  72  ASN   B ND2  1 
ATOM   5027 H  H    . ASN   B 1 72  ? 46.768 -6.601  10.835  1.00 18.14 ?  72  ASN   B H    1 
ATOM   5028 H  HA   . ASN   B 1 72  ? 44.292 -5.525  11.095  1.00 18.90 ?  72  ASN   B HA   1 
ATOM   5029 H  HB2  . ASN   B 1 72  ? 45.066 -7.502  9.233   1.00 19.83 ?  72  ASN   B HB2  1 
ATOM   5030 H  HB3  . ASN   B 1 72  ? 43.575 -6.974  9.398   1.00 19.83 ?  72  ASN   B HB3  1 
ATOM   5031 H  HD21 . ASN   B 1 72  ? 44.017 -4.006  7.882   1.00 23.03 ?  72  ASN   B HD21 1 
ATOM   5032 H  HD22 . ASN   B 1 72  ? 43.211 -4.686  8.934   1.00 23.03 ?  72  ASN   B HD22 1 
ATOM   5033 N  N    . GLY   B 1 73  ? 45.251 -8.164  12.468  1.00 15.80 ?  73  GLY   B N    1 
ATOM   5034 C  CA   . GLY   B 1 73  ? 44.860 -9.308  13.255  1.00 15.59 ?  73  GLY   B CA   1 
ATOM   5035 C  C    . GLY   B 1 73  ? 44.494 -10.489 12.383  1.00 14.09 ?  73  GLY   B C    1 
ATOM   5036 O  O    . GLY   B 1 73  ? 44.484 -10.404 11.152  1.00 13.80 ?  73  GLY   B O    1 
ATOM   5037 H  H    . GLY   B 1 73  ? 46.101 -8.020  12.448  1.00 18.97 ?  73  GLY   B H    1 
ATOM   5038 H  HA2  . GLY   B 1 73  ? 45.596 -9.560  13.841  1.00 18.72 ?  73  GLY   B HA2  1 
ATOM   5039 H  HA3  . GLY   B 1 73  ? 44.097 -9.074  13.809  1.00 18.72 ?  73  GLY   B HA3  1 
ATOM   5040 N  N    . PRO   B 1 74  ? 44.182 -11.615 13.019  1.00 14.19 ?  74  PRO   B N    1 
ATOM   5041 C  CA   . PRO   B 1 74  ? 43.930 -12.848 12.272  1.00 13.56 ?  74  PRO   B CA   1 
ATOM   5042 C  C    . PRO   B 1 74  ? 42.629 -12.794 11.483  1.00 12.94 ?  74  PRO   B C    1 
ATOM   5043 O  O    . PRO   B 1 74  ? 41.686 -12.060 11.800  1.00 14.49 ?  74  PRO   B O    1 
ATOM   5044 C  CB   . PRO   B 1 74  ? 43.856 -13.912 13.371  1.00 14.73 ?  74  PRO   B CB   1 
ATOM   5045 C  CG   . PRO   B 1 74  ? 43.414 -13.161 14.587  1.00 16.09 ?  74  PRO   B CG   1 
ATOM   5046 C  CD   . PRO   B 1 74  ? 44.071 -11.815 14.475  1.00 15.28 ?  74  PRO   B CD   1 
ATOM   5047 H  HA   . PRO   B 1 74  ? 44.677 -13.038 11.675  1.00 16.29 ?  74  PRO   B HA   1 
ATOM   5048 H  HB2  . PRO   B 1 74  ? 43.205 -14.585 13.123  1.00 17.69 ?  74  PRO   B HB2  1 
ATOM   5049 H  HB3  . PRO   B 1 74  ? 44.731 -14.305 13.506  1.00 17.69 ?  74  PRO   B HB3  1 
ATOM   5050 H  HG2  . PRO   B 1 74  ? 42.447 -13.073 14.581  1.00 19.32 ?  74  PRO   B HG2  1 
ATOM   5051 H  HG3  . PRO   B 1 74  ? 43.713 -13.625 15.382  1.00 19.32 ?  74  PRO   B HG3  1 
ATOM   5052 H  HD2  . PRO   B 1 74  ? 43.507 -11.129 14.875  1.00 18.34 ?  74  PRO   B HD2  1 
ATOM   5053 H  HD3  . PRO   B 1 74  ? 44.950 -11.830 14.882  1.00 18.34 ?  74  PRO   B HD3  1 
ATOM   5054 N  N    . LEU   B 1 75  ? 42.599 -13.609 10.436  1.00 12.26 ?  75  LEU   B N    1 
ATOM   5055 C  CA   . LEU   B 1 75  ? 41.386 -13.823 9.669   1.00 12.57 ?  75  LEU   B CA   1 
ATOM   5056 C  C    . LEU   B 1 75  ? 40.413 -14.685 10.470  1.00 13.08 ?  75  LEU   B C    1 
ATOM   5057 O  O    . LEU   B 1 75  ? 40.756 -15.250 11.513  1.00 13.85 ?  75  LEU   B O    1 
ATOM   5058 C  CB   . LEU   B 1 75  ? 41.712 -14.540 8.358   1.00 12.55 ?  75  LEU   B CB   1 
ATOM   5059 C  CG   . LEU   B 1 75  ? 42.561 -13.792 7.326   1.00 14.45 ?  75  LEU   B CG   1 
ATOM   5060 C  CD1  . LEU   B 1 75  ? 42.764 -14.631 6.067   1.00 15.82 ?  75  LEU   B CD1  1 
ATOM   5061 C  CD2  . LEU   B 1 75  ? 41.961 -12.460 6.974   1.00 17.94 ?  75  LEU   B CD2  1 
ATOM   5062 H  H    . LEU   B 1 75  ? 43.272 -14.059 10.147  1.00 14.73 ?  75  LEU   B H    1 
ATOM   5063 H  HA   . LEU   B 1 75  ? 40.961 -12.973 9.466   1.00 15.09 ?  75  LEU   B HA   1 
ATOM   5064 H  HB2  . LEU   B 1 75  ? 42.188 -15.360 8.573   1.00 15.08 ?  75  LEU   B HB2  1 
ATOM   5065 H  HB3  . LEU   B 1 75  ? 40.876 -14.770 7.919   1.00 15.08 ?  75  LEU   B HB3  1 
ATOM   5066 H  HG   . LEU   B 1 75  ? 43.437 -13.630 7.709   1.00 17.35 ?  75  LEU   B HG   1 
ATOM   5067 H  HD11 . LEU   B 1 75  ? 43.311 -14.130 5.437   1.00 18.99 ?  75  LEU   B HD11 1 
ATOM   5068 H  HD12 . LEU   B 1 75  ? 43.213 -15.459 6.303   1.00 18.99 ?  75  LEU   B HD12 1 
ATOM   5069 H  HD13 . LEU   B 1 75  ? 41.901 -14.825 5.670   1.00 18.99 ?  75  LEU   B HD13 1 
ATOM   5070 H  HD21 . LEU   B 1 75  ? 42.468 -12.067 6.250   1.00 21.55 ?  75  LEU   B HD21 1 
ATOM   5071 H  HD22 . LEU   B 1 75  ? 41.039 -12.593 6.703   1.00 21.55 ?  75  LEU   B HD22 1 
ATOM   5072 H  HD23 . LEU   B 1 75  ? 41.995 -11.885 7.755   1.00 21.55 ?  75  LEU   B HD23 1 
ATOM   5073 N  N    . LYS   B 1 76  ? 39.182 -14.776 9.967   1.00 13.97 ?  76  LYS   B N    1 
ATOM   5074 C  CA   . LYS   B 1 76  ? 38.201 -15.742 10.442  1.00 15.09 ?  76  LYS   B CA   1 
ATOM   5075 C  C    . LYS   B 1 76  ? 38.293 -17.019 9.611   1.00 13.66 ?  76  LYS   B C    1 
ATOM   5076 O  O    . LYS   B 1 76  ? 38.567 -16.969 8.413   1.00 13.37 ?  76  LYS   B O    1 
ATOM   5077 C  CB   . LYS   B 1 76  ? 36.782 -15.175 10.263  1.00 17.98 ?  76  LYS   B CB   1 
ATOM   5078 C  CG   . LYS   B 1 76  ? 36.505 -13.789 10.881  1.00 19.89 ?  76  LYS   B CG   1 
ATOM   5079 C  CD   . LYS   B 1 76  ? 35.110 -13.251 10.505  1.00 20.99 ?  76  LYS   B CD   1 
ATOM   5080 C  CE   . LYS   B 1 76  ? 34.833 -11.895 11.137  1.00 22.97 ?  76  LYS   B CE   1 
ATOM   5081 N  NZ   . LYS   B 1 76  ? 33.552 -11.294 10.672  1.00 23.70 ?  76  LYS   B NZ   1 
ATOM   5082 H  H    . LYS   B 1 76  ? 38.889 -14.279 9.330   1.00 16.78 ?  76  LYS   B H    1 
ATOM   5083 H  HA   . LYS   B 1 76  ? 38.349 -15.953 11.377  1.00 18.12 ?  76  LYS   B HA   1 
ATOM   5084 H  HB2  . LYS   B 1 76  ? 36.600 -15.105 9.312   1.00 21.59 ?  76  LYS   B HB2  1 
ATOM   5085 H  HB3  . LYS   B 1 76  ? 36.152 -15.796 10.664  1.00 21.59 ?  76  LYS   B HB3  1 
ATOM   5086 H  HG2  . LYS   B 1 76  ? 36.554 -13.855 11.848  1.00 23.88 ?  76  LYS   B HG2  1 
ATOM   5087 H  HG3  . LYS   B 1 76  ? 37.170 -13.158 10.557  1.00 23.88 ?  76  LYS   B HG3  1 
ATOM   5088 H  HD2  . LYS   B 1 76  ? 35.055 -13.154 9.541   1.00 25.21 ?  76  LYS   B HD2  1 
ATOM   5089 H  HD3  . LYS   B 1 76  ? 34.435 -13.874 10.816  1.00 25.21 ?  76  LYS   B HD3  1 
ATOM   5090 H  HE2  . LYS   B 1 76  ? 34.785 -12.001 12.099  1.00 27.57 ?  76  LYS   B HE2  1 
ATOM   5091 H  HE3  . LYS   B 1 76  ? 35.554 -11.288 10.904  1.00 27.57 ?  76  LYS   B HE3  1 
ATOM   5092 H  HZ1  . LYS   B 1 76  ? 33.426 -10.504 11.061  1.00 28.45 ?  76  LYS   B HZ1  1 
ATOM   5093 H  HZ2  . LYS   B 1 76  ? 33.572 -11.180 9.788   1.00 28.45 ?  76  LYS   B HZ2  1 
ATOM   5094 H  HZ3  . LYS   B 1 76  ? 32.871 -11.830 10.877  1.00 28.45 ?  76  LYS   B HZ3  1 
ATOM   5095 N  N    . VAL   B 1 77  ? 38.042 -18.169 10.244  1.00 14.30 ?  77  VAL   B N    1 
ATOM   5096 C  CA   . VAL   B 1 77  ? 37.831 -19.381 9.460   1.00 14.58 ?  77  VAL   B CA   1 
ATOM   5097 C  C    . VAL   B 1 77  ? 36.637 -19.148 8.545   1.00 13.62 ?  77  VAL   B C    1 
ATOM   5098 O  O    . VAL   B 1 77  ? 35.573 -18.700 8.992   1.00 13.70 ?  77  VAL   B O    1 
ATOM   5099 C  CB   . VAL   B 1 77  ? 37.633 -20.600 10.372  1.00 15.97 ?  77  VAL   B CB   1 
ATOM   5100 C  CG1  . VAL   B 1 77  ? 37.350 -21.832 9.528   1.00 16.96 ?  77  VAL   B CG1  1 
ATOM   5101 C  CG2  . VAL   B 1 77  ? 38.867 -20.825 11.249  1.00 17.10 ?  77  VAL   B CG2  1 
ATOM   5102 H  H    . VAL   B 1 77  ? 37.996 -18.267 11.091  1.00 17.17 ?  77  VAL   B H    1 
ATOM   5103 H  HA   . VAL   B 1 77  ? 38.607 -19.541 8.903   1.00 17.51 ?  77  VAL   B HA   1 
ATOM   5104 H  HB   . VAL   B 1 77  ? 36.867 -20.443 10.951  1.00 19.18 ?  77  VAL   B HB   1 
ATOM   5105 H  HG11 . VAL   B 1 77  ? 37.407 -22.618 10.095  1.00 20.37 ?  77  VAL   B HG11 1 
ATOM   5106 H  HG12 . VAL   B 1 77  ? 36.456 -21.765 9.152   1.00 20.37 ?  77  VAL   B HG12 1 
ATOM   5107 H  HG13 . VAL   B 1 77  ? 38.005 -21.886 8.819   1.00 20.37 ?  77  VAL   B HG13 1 
ATOM   5108 H  HG21 . VAL   B 1 77  ? 38.727 -21.620 11.784  1.00 20.53 ?  77  VAL   B HG21 1 
ATOM   5109 H  HG22 . VAL   B 1 77  ? 39.638 -20.937 10.676  1.00 20.53 ?  77  VAL   B HG22 1 
ATOM   5110 H  HG23 . VAL   B 1 77  ? 38.987 -20.053 11.823  1.00 20.53 ?  77  VAL   B HG23 1 
ATOM   5111 N  N    . GLY   B 1 78  ? 36.820 -19.417 7.253   1.00 13.02 ?  78  GLY   B N    1 
ATOM   5112 C  CA   . GLY   B 1 78  ? 35.847 -19.099 6.231   1.00 12.75 ?  78  GLY   B CA   1 
ATOM   5113 C  C    . GLY   B 1 78  ? 36.086 -17.778 5.534   1.00 12.07 ?  78  GLY   B C    1 
ATOM   5114 O  O    . GLY   B 1 78  ? 35.400 -17.491 4.548   1.00 12.36 ?  78  GLY   B O    1 
ATOM   5115 H  H    . GLY   B 1 78  ? 37.528 -19.798 6.939   1.00 15.64 ?  78  GLY   B H    1 
ATOM   5116 H  HA2  . GLY   B 1 78  ? 35.851 -19.794 5.559   1.00 15.31 ?  78  GLY   B HA2  1 
ATOM   5117 H  HA3  . GLY   B 1 78  ? 34.966 -19.067 6.633   1.00 15.31 ?  78  GLY   B HA3  1 
ATOM   5118 N  N    . GLY   B 1 79  ? 37.041 -16.977 6.016   1.00 12.16 ?  79  GLY   B N    1 
ATOM   5119 C  CA   . GLY   B 1 79  ? 37.342 -15.681 5.444   1.00 11.95 ?  79  GLY   B CA   1 
ATOM   5120 C  C    . GLY   B 1 79  ? 38.573 -15.697 4.549   1.00 11.47 ?  79  GLY   B C    1 
ATOM   5121 O  O    . GLY   B 1 79  ? 39.186 -16.733 4.298   1.00 11.89 ?  79  GLY   B O    1 
ATOM   5122 H  H    . GLY   B 1 79  ? 37.543 -17.176 6.684   1.00 14.61 ?  79  GLY   B H    1 
ATOM   5123 H  HA2  . GLY   B 1 79  ? 36.588 -15.376 4.913   1.00 14.35 ?  79  GLY   B HA2  1 
ATOM   5124 H  HA3  . GLY   B 1 79  ? 37.491 -15.040 6.157   1.00 14.35 ?  79  GLY   B HA3  1 
ATOM   5125 N  N    . SER   B 1 80  ? 38.944 -14.501 4.080   1.00 11.22 ?  80  SER   B N    1 
ATOM   5126 C  CA   . SER   B 1 80  ? 40.055 -14.370 3.146   1.00 11.11 ?  80  SER   B CA   1 
ATOM   5127 C  C    . SER   B 1 80  ? 40.630 -12.962 3.204   1.00 11.23 ?  80  SER   B C    1 
ATOM   5128 O  O    . SER   B 1 80  ? 40.008 -12.029 3.717   1.00 12.37 ?  80  SER   B O    1 
ATOM   5129 C  CB   . SER   B 1 80  ? 39.616 -14.660 1.707   1.00 11.43 ?  80  SER   B CB   1 
ATOM   5130 O  OG   . SER   B 1 80  ? 38.765 -13.640 1.211   1.00 12.81 ?  80  SER   B OG   1 
ATOM   5131 H  H    . SER   B 1 80  ? 38.571 -13.758 4.289   1.00 13.48 ?  80  SER   B H    1 
ATOM   5132 H  HA   . SER   B 1 80  ? 40.748 -14.999 3.392   1.00 13.35 ?  80  SER   B HA   1 
ATOM   5133 H  HB2  . SER   B 1 80  ? 40.399 -14.711 1.138   1.00 13.73 ?  80  SER   B HB2  1 
ATOM   5134 H  HB3  . SER   B 1 80  ? 39.138 -15.507 1.685   1.00 13.73 ?  80  SER   B HB3  1 
ATOM   5135 H  HG   . SER   B 1 80  ? 38.070 -13.589 1.693   1.00 15.39 ?  80  SER   B HG   1 
ATOM   5136 N  N    . CYS   B 1 81  ? 41.818 -12.816 2.620   1.00 10.95 ?  81  CYS   B N    1 
ATOM   5137 C  CA   . CYS   B 1 81  ? 42.359 -11.501 2.314   1.00 11.25 ?  81  CYS   B CA   1 
ATOM   5138 C  C    . CYS   B 1 81  ? 43.123 -11.585 1.003   1.00 10.40 ?  81  CYS   B C    1 
ATOM   5139 O  O    . CYS   B 1 81  ? 43.638 -12.646 0.632   1.00 11.56 ?  81  CYS   B O    1 
ATOM   5140 C  CB   . CYS   B 1 81  ? 43.248 -10.949 3.438   1.00 11.98 ?  81  CYS   B CB   1 
ATOM   5141 S  SG   . CYS   B 1 81  ? 44.773 -11.885 3.672   1.00 12.14 ?  81  CYS   B SG   1 
ATOM   5142 H  H    . CYS   B 1 81  ? 42.333 -13.466 2.383   1.00 13.16 ?  81  CYS   B H    1 
ATOM   5143 H  HA   . CYS   B 1 81  ? 41.623 -10.880 2.187   1.00 13.52 ?  81  CYS   B HA   1 
ATOM   5144 H  HB2  . CYS   B 1 81  ? 43.488 -10.032 3.230   1.00 14.39 ?  81  CYS   B HB2  1 
ATOM   5145 H  HB3  . CYS   B 1 81  ? 42.744 -10.972 4.272   1.00 14.39 ?  81  CYS   B HB3  1 
ATOM   5146 H  HG   . CYS   B 1 81  ? 45.397 -11.392 4.575   1.00 14.58 ?  81  CYS   B HG   1 
ATOM   5147 N  N    . VAL   B 1 82  ? 43.223 -10.443 0.327   1.00 10.96 ?  82  VAL   B N    1 
ATOM   5148 C  CA   . VAL   B 1 82  ? 43.987 -10.315 -0.911  1.00 10.85 ?  82  VAL   B CA   1 
ATOM   5149 C  C    . VAL   B 1 82  ? 45.330 -9.675  -0.592  1.00 11.28 ?  82  VAL   B C    1 
ATOM   5150 O  O    . VAL   B 1 82  ? 45.383 -8.557  -0.062  1.00 12.60 ?  82  VAL   B O    1 
ATOM   5151 C  CB   . VAL   B 1 82  ? 43.240 -9.474  -1.955  1.00 12.19 ?  82  VAL   B CB   1 
ATOM   5152 C  CG1  . VAL   B 1 82  ? 44.094 -9.315  -3.213  1.00 13.58 ?  82  VAL   B CG1  1 
ATOM   5153 C  CG2  . VAL   B 1 82  ? 41.882 -10.077 -2.272  1.00 13.32 ?  82  VAL   B CG2  1 
ATOM   5154 H  H    . VAL   B 1 82  ? 42.847 -9.702  0.570   1.00 13.17 ?  82  VAL   B H    1 
ATOM   5155 H  HA   . VAL   B 1 82  ? 44.147 -11.193 -1.284  1.00 13.04 ?  82  VAL   B HA   1 
ATOM   5156 H  HB   . VAL   B 1 82  ? 43.090 -8.589  -1.592  1.00 14.64 ?  82  VAL   B HB   1 
ATOM   5157 H  HG11 . VAL   B 1 82  ? 43.534 -9.004  -3.941  1.00 16.30 ?  82  VAL   B HG11 1 
ATOM   5158 H  HG12 . VAL   B 1 82  ? 44.798 -8.663  -3.043  1.00 16.30 ?  82  VAL   B HG12 1 
ATOM   5159 H  HG13 . VAL   B 1 82  ? 44.488 -10.170 -3.443  1.00 16.30 ?  82  VAL   B HG13 1 
ATOM   5160 H  HG21 . VAL   B 1 82  ? 41.451 -9.550  -2.964  1.00 16.00 ?  82  VAL   B HG21 1 
ATOM   5161 H  HG22 . VAL   B 1 82  ? 42.003 -10.991 -2.583  1.00 16.00 ?  82  VAL   B HG22 1 
ATOM   5162 H  HG23 . VAL   B 1 82  ? 41.337 -10.075 -1.468  1.00 16.00 ?  82  VAL   B HG23 1 
ATOM   5163 N  N    . LEU   B 1 83  ? 46.411 -10.360 -0.959  1.00 10.88 ?  83  LEU   B N    1 
ATOM   5164 C  CA   . LEU   B 1 83  ? 47.770 -9.842  -0.842  1.00 10.87 ?  83  LEU   B CA   1 
ATOM   5165 C  C    . LEU   B 1 83  ? 48.470 -9.988  -2.194  1.00 10.95 ?  83  LEU   B C    1 
ATOM   5166 O  O    . LEU   B 1 83  ? 47.867 -10.406 -3.187  1.00 10.98 ?  83  LEU   B O    1 
ATOM   5167 C  CB   . LEU   B 1 83  ? 48.523 -10.516 0.310   1.00 11.70 ?  83  LEU   B CB   1 
ATOM   5168 C  CG   . LEU   B 1 83  ? 48.016 -10.160 1.714   1.00 12.86 ?  83  LEU   B CG   1 
ATOM   5169 C  CD1  . LEU   B 1 83  ? 48.658 -11.033 2.774   1.00 13.54 ?  83  LEU   B CD1  1 
ATOM   5170 C  CD2  . LEU   B 1 83  ? 48.213 -8.679  2.043   1.00 13.76 ?  83  LEU   B CD2  1 
ATOM   5171 H  H    . LEU   B 1 83  ? 46.372 -11.158 -1.287  1.00 13.07 ?  83  LEU   B H    1 
ATOM   5172 H  HA   . LEU   B 1 83  ? 47.713 -8.898  -0.648  1.00 13.05 ?  83  LEU   B HA   1 
ATOM   5173 H  HB2  . LEU   B 1 83  ? 48.457 -11.473 0.206   1.00 14.06 ?  83  LEU   B HB2  1 
ATOM   5174 H  HB3  . LEU   B 1 83  ? 49.454 -10.244 0.258   1.00 14.06 ?  83  LEU   B HB3  1 
ATOM   5175 H  HG   . LEU   B 1 83  ? 47.065 -10.334 1.741   1.00 15.44 ?  83  LEU   B HG   1 
ATOM   5176 H  HD11 . LEU   B 1 83  ? 48.306 -10.786 3.644   1.00 16.26 ?  83  LEU   B HD11 1 
ATOM   5177 H  HD12 . LEU   B 1 83  ? 48.442 -11.964 2.587   1.00 16.26 ?  83  LEU   B HD12 1 
ATOM   5178 H  HD13 . LEU   B 1 83  ? 49.617 -10.908 2.755   1.00 16.26 ?  83  LEU   B HD13 1 
ATOM   5179 H  HD21 . LEU   B 1 83  ? 47.995 -8.533  2.977   1.00 16.52 ?  83  LEU   B HD21 1 
ATOM   5180 H  HD22 . LEU   B 1 83  ? 49.134 -8.436  1.874   1.00 16.52 ?  83  LEU   B HD22 1 
ATOM   5181 H  HD23 . LEU   B 1 83  ? 47.621 -8.152  1.481   1.00 16.52 ?  83  LEU   B HD23 1 
ATOM   5182 N  N    . SER   B 1 84  ? 49.747 -9.614  -2.247  1.00 12.01 ?  84  SER   B N    1 
ATOM   5183 C  CA   . SER   B 1 84  ? 50.477 -9.726  -3.500  1.00 12.24 ?  84  SER   B CA   1 
ATOM   5184 C  C    . SER   B 1 84  ? 50.631 -11.184 -3.918  1.00 11.56 ?  84  SER   B C    1 
ATOM   5185 O  O    . SER   B 1 84  ? 50.751 -12.082 -3.088  1.00 11.61 ?  84  SER   B O    1 
ATOM   5186 C  CB   . SER   B 1 84  ? 51.870 -9.121  -3.356  1.00 14.10 ?  84  SER   B CB   1 
ATOM   5187 O  OG   . SER   B 1 84  ? 52.610 -9.336  -4.540  1.00 15.63 ?  84  SER   B OG   1 
ATOM   5188 H  H    . SER   B 1 84  ? 50.197 -9.296  -1.588  1.00 14.43 ?  84  SER   B H    1 
ATOM   5189 H  HA   . SER   B 1 84  ? 50.001 -9.256  -4.200  1.00 14.70 ?  84  SER   B HA   1 
ATOM   5190 H  HB2  . SER   B 1 84  ? 51.783 -8.166  -3.193  1.00 16.93 ?  84  SER   B HB2  1 
ATOM   5191 H  HB3  . SER   B 1 84  ? 52.328 -9.544  -2.616  1.00 16.93 ?  84  SER   B HB3  1 
ATOM   5192 H  HG   . SER   B 1 84  ? 53.377 -8.986  -4.466  1.00 18.77 ?  84  SER   B HG   1 
ATOM   5193 N  N    . GLY   B 1 85  ? 50.686 -11.405 -5.226  1.00 12.52 ?  85  GLY   B N    1 
ATOM   5194 C  CA   . GLY   B 1 85  ? 51.040 -12.700 -5.760  1.00 12.96 ?  85  GLY   B CA   1 
ATOM   5195 C  C    . GLY   B 1 85  ? 52.513 -12.892 -6.062  1.00 12.17 ?  85  GLY   B C    1 
ATOM   5196 O  O    . GLY   B 1 85  ? 52.890 -13.970 -6.523  1.00 12.80 ?  85  GLY   B O    1 
ATOM   5197 H  H    . GLY   B 1 85  ? 50.526 -10.816 -5.824  1.00 15.03 ?  85  GLY   B H    1 
ATOM   5198 H  HA2  . GLY   B 1 85  ? 50.781 -13.389 -5.126  1.00 15.57 ?  85  GLY   B HA2  1 
ATOM   5199 H  HA3  . GLY   B 1 85  ? 50.550 -12.851 -6.579  1.00 15.57 ?  85  GLY   B HA3  1 
ATOM   5200 N  N    . HIS   B 1 86  ? 53.367 -11.894 -5.837  1.00 12.36 ?  86  HIS   B N    1 
ATOM   5201 C  CA   . HIS   B 1 86  ? 54.831 -12.061 -5.927  1.00 12.43 ?  86  HIS   B CA   1 
ATOM   5202 C  C    . HIS   B 1 86  ? 55.201 -12.570 -7.318  1.00 12.74 ?  86  HIS   B C    1 
ATOM   5203 O  O    . HIS   B 1 86  ? 54.815 -11.947 -8.320  1.00 13.46 ?  86  HIS   B O    1 
ATOM   5204 C  CB   . HIS   B 1 86  ? 55.332 -12.902 -4.759  1.00 12.73 ?  86  HIS   B CB   1 
ATOM   5205 C  CG   . HIS   B 1 86  ? 55.016 -12.302 -3.432  1.00 12.66 ?  86  HIS   B CG   1 
ATOM   5206 N  ND1  . HIS   B 1 86  ? 55.829 -11.371 -2.820  1.00 14.19 ?  86  HIS   B ND1  1 
ATOM   5207 C  CD2  . HIS   B 1 86  ? 53.947 -12.468 -2.618  1.00 13.11 ?  86  HIS   B CD2  1 
ATOM   5208 C  CE1  . HIS   B 1 86  ? 55.269 -10.992 -1.684  1.00 14.05 ?  86  HIS   B CE1  1 
ATOM   5209 N  NE2  . HIS   B 1 86  ? 54.125 -11.638 -1.541  1.00 13.43 ?  86  HIS   B NE2  1 
ATOM   5210 H  H    . HIS   B 1 86  ? 53.125 -11.099 -5.629  1.00 14.85 ?  86  HIS   B H    1 
ATOM   5211 H  HA   . HIS   B 1 86  ? 55.236 -11.188 -5.836  1.00 14.93 ?  86  HIS   B HA   1 
ATOM   5212 H  HB2  . HIS   B 1 86  ? 54.927 -13.781 -4.797  1.00 15.29 ?  86  HIS   B HB2  1 
ATOM   5213 H  HB3  . HIS   B 1 86  ? 56.301 -12.986 -4.821  1.00 15.29 ?  86  HIS   B HB3  1 
ATOM   5214 H  HD2  . HIS   B 1 86  ? 53.215 -13.029 -2.772  1.00 15.75 ?  86  HIS   B HD2  1 
ATOM   5215 H  HE1  . HIS   B 1 86  ? 55.627 -10.389 -1.074  1.00 16.87 ?  86  HIS   B HE1  1 
ATOM   5216 H  HE2  . HIS   B 1 86  ? 53.587 -11.573 -0.869  1.00 16.13 ?  86  HIS   B HE2  1 
ATOM   5217 N  N    . ASN   B 1 87  ? 55.963 -13.655 -7.431  1.00 12.99 ?  87  ASN   B N    1 
ATOM   5218 C  CA   . ASN   B 1 87  ? 56.355 -14.227 -8.709  1.00 13.57 ?  87  ASN   B CA   1 
ATOM   5219 C  C    . ASN   B 1 87  ? 55.372 -15.274 -9.208  1.00 13.14 ?  87  ASN   B C    1 
ATOM   5220 O  O    . ASN   B 1 87  ? 55.687 -15.980 -10.172 1.00 15.07 ?  87  ASN   B O    1 
ATOM   5221 C  CB   . ASN   B 1 87  ? 57.752 -14.851 -8.597  1.00 15.57 ?  87  ASN   B CB   1 
ATOM   5222 C  CG   . ASN   B 1 87  ? 57.816 -15.970 -7.559  1.00 16.63 ?  87  ASN   B CG   1 
ATOM   5223 O  OD1  . ASN   B 1 87  ? 57.176 -15.900 -6.504  1.00 15.71 ?  87  ASN   B OD1  1 
ATOM   5224 N  ND2  . ASN   B 1 87  ? 58.578 -17.021 -7.871  1.00 18.85 ?  87  ASN   B ND2  1 
ATOM   5225 H  H    . ASN   B 1 87  ? 56.260 -14.102 -6.760  1.00 15.60 ?  87  ASN   B H    1 
ATOM   5226 H  HA   . ASN   B 1 87  ? 56.395 -13.522 -9.369  1.00 16.30 ?  87  ASN   B HA   1 
ATOM   5227 H  HB2  . ASN   B 1 87  ? 58.001 -15.224 -9.460  1.00 18.69 ?  87  ASN   B HB2  1 
ATOM   5228 H  HB3  . ASN   B 1 87  ? 58.383 -14.163 -8.341  1.00 18.69 ?  87  ASN   B HB3  1 
ATOM   5229 H  HD21 . ASN   B 1 87  ? 58.654 -17.673 -7.322  1.00 22.63 ?  87  ASN   B HD21 1 
ATOM   5230 H  HD22 . ASN   B 1 87  ? 59.008 -17.036 -8.621  1.00 22.63 ?  87  ASN   B HD22 1 
ATOM   5231 N  N    . LEU   B 1 88  ? 54.196 -15.381 -8.585  1.00 12.26 ?  88  LEU   B N    1 
ATOM   5232 C  CA   . LEU   B 1 88  ? 53.214 -16.409 -8.911  1.00 13.05 ?  88  LEU   B CA   1 
ATOM   5233 C  C    . LEU   B 1 88  ? 51.982 -15.887 -9.632  1.00 12.44 ?  88  LEU   B C    1 
ATOM   5234 O  O    . LEU   B 1 88  ? 51.376 -16.634 -10.408 1.00 14.08 ?  88  LEU   B O    1 
ATOM   5235 C  CB   . LEU   B 1 88  ? 52.751 -17.101 -7.625  1.00 13.62 ?  88  LEU   B CB   1 
ATOM   5236 C  CG   . LEU   B 1 88  ? 53.874 -17.747 -6.825  1.00 15.99 ?  88  LEU   B CG   1 
ATOM   5237 C  CD1  . LEU   B 1 88  ? 53.383 -18.100 -5.431  1.00 17.42 ?  88  LEU   B CD1  1 
ATOM   5238 C  CD2  . LEU   B 1 88  ? 54.362 -18.980 -7.552  1.00 18.96 ?  88  LEU   B CD2  1 
ATOM   5239 H  H    . LEU   B 1 88  ? 53.941 -14.855 -7.949  1.00 14.72 ?  88  LEU   B H    1 
ATOM   5240 H  HA   . LEU   B 1 88  ? 53.632 -17.074 -9.474  1.00 15.67 ?  88  LEU   B HA   1 
ATOM   5241 H  HB2  . LEU   B 1 88  ? 52.320 -16.449 -7.052  1.00 16.35 ?  88  LEU   B HB2  1 
ATOM   5242 H  HB3  . LEU   B 1 88  ? 52.119 -17.801 -7.858  1.00 16.35 ?  88  LEU   B HB3  1 
ATOM   5243 H  HG   . LEU   B 1 88  ? 54.614 -17.124 -6.742  1.00 19.20 ?  88  LEU   B HG   1 
ATOM   5244 H  HD11 . LEU   B 1 88  ? 54.043 -18.661 -4.996  1.00 20.92 ?  88  LEU   B HD11 1 
ATOM   5245 H  HD12 . LEU   B 1 88  ? 53.258 -17.282 -4.924  1.00 20.92 ?  88  LEU   B HD12 1 
ATOM   5246 H  HD13 . LEU   B 1 88  ? 52.542 -18.574 -5.507  1.00 20.92 ?  88  LEU   B HD13 1 
ATOM   5247 H  HD21 . LEU   B 1 88  ? 55.022 -19.429 -7.001  1.00 22.76 ?  88  LEU   B HD21 1 
ATOM   5248 H  HD22 . LEU   B 1 88  ? 53.609 -19.569 -7.714  1.00 22.76 ?  88  LEU   B HD22 1 
ATOM   5249 H  HD23 . LEU   B 1 88  ? 54.761 -18.713 -8.395  1.00 22.76 ?  88  LEU   B HD23 1 
ATOM   5250 N  N    . ALA   B 1 89  ? 51.580 -14.649 -9.368  1.00 11.75 ?  89  ALA   B N    1 
ATOM   5251 C  CA   . ALA   B 1 89  ? 50.285 -14.151 -9.807  1.00 11.16 ?  89  ALA   B CA   1 
ATOM   5252 C  C    . ALA   B 1 89  ? 50.259 -12.659 -9.528  1.00 11.90 ?  89  ALA   B C    1 
ATOM   5253 O  O    . ALA   B 1 89  ? 51.099 -12.141 -8.790  1.00 12.70 ?  89  ALA   B O    1 
ATOM   5254 C  CB   . ALA   B 1 89  ? 49.153 -14.825 -9.040  1.00 11.52 ?  89  ALA   B CB   1 
ATOM   5255 H  H    . ALA   B 1 89  ? 52.037 -14.070 -8.924  1.00 14.11 ?  89  ALA   B H    1 
ATOM   5256 H  HA   . ALA   B 1 89  ? 50.165 -14.305 -10.760 1.00 13.40 ?  89  ALA   B HA   1 
ATOM   5257 H  HB1  . ALA   B 1 89  ? 48.304 -14.489 -9.368  1.00 13.84 ?  89  ALA   B HB1  1 
ATOM   5258 H  HB2  . ALA   B 1 89  ? 49.203 -15.787 -9.191  1.00 13.84 ?  89  ALA   B HB2  1 
ATOM   5259 H  HB3  . ALA   B 1 89  ? 49.251 -14.633 -8.100  1.00 13.84 ?  89  ALA   B HB3  1 
ATOM   5260 N  N    . LYS   B 1 90  ? 49.265 -11.968 -10.087 1.00 12.53 ?  90  LYS   B N    1 
ATOM   5261 C  CA   . LYS   B 1 90  ? 49.070 -10.581 -9.686  1.00 12.88 ?  90  LYS   B CA   1 
ATOM   5262 C  C    . LYS   B 1 90  ? 48.754 -10.503 -8.200  1.00 12.41 ?  90  LYS   B C    1 
ATOM   5263 O  O    . LYS   B 1 90  ? 49.395 -9.746  -7.454  1.00 13.64 ?  90  LYS   B O    1 
ATOM   5264 C  CB   . LYS   B 1 90  ? 47.987 -9.922  -10.538 1.00 14.09 ?  90  LYS   B CB   1 
ATOM   5265 C  CG   . LYS   B 1 90  ? 47.698 -8.478  -10.147 1.00 14.71 ?  90  LYS   B CG   1 
ATOM   5266 C  CD   . LYS   B 1 90  ? 48.911 -7.591  -10.239 1.00 17.91 ?  90  LYS   B CD   1 
ATOM   5267 C  CE   . LYS   B 1 90  ? 48.479 -6.160  -10.033 1.00 19.92 ?  90  LYS   B CE   1 
ATOM   5268 N  NZ   . LYS   B 1 90  ? 49.631 -5.240  -9.897  1.00 20.15 ?  90  LYS   B NZ   1 
ATOM   5269 H  H    . LYS   B 1 90  ? 48.709 -12.273 -10.671 1.00 15.05 ?  90  LYS   B H    1 
ATOM   5270 H  HA   . LYS   B 1 90  ? 49.895 -10.104 -9.836  1.00 15.47 ?  90  LYS   B HA   1 
ATOM   5271 H  HB2  . LYS   B 1 90  ? 48.275 -9.926  -11.467 1.00 16.92 ?  90  LYS   B HB2  1 
ATOM   5272 H  HB3  . LYS   B 1 90  ? 47.163 -10.430 -10.452 1.00 16.92 ?  90  LYS   B HB3  1 
ATOM   5273 H  HG2  . LYS   B 1 90  ? 47.018 -8.123  -10.742 1.00 17.67 ?  90  LYS   B HG2  1 
ATOM   5274 H  HG3  . LYS   B 1 90  ? 47.370 -8.457  -9.231  1.00 17.67 ?  90  LYS   B HG3  1 
ATOM   5275 H  HD2  . LYS   B 1 90  ? 49.545 -7.829  -9.544  1.00 21.50 ?  90  LYS   B HD2  1 
ATOM   5276 H  HD3  . LYS   B 1 90  ? 49.314 -7.676  -11.116 1.00 21.50 ?  90  LYS   B HD3  1 
ATOM   5277 H  HE2  . LYS   B 1 90  ? 47.956 -5.868  -10.798 1.00 23.91 ?  90  LYS   B HE2  1 
ATOM   5278 H  HE3  . LYS   B 1 90  ? 47.951 -6.093  -9.224  1.00 23.91 ?  90  LYS   B HE3  1 
ATOM   5279 H  HZ1  . LYS   B 1 90  ? 49.346 -4.402  -9.781  1.00 24.20 ?  90  LYS   B HZ1  1 
ATOM   5280 H  HZ2  . LYS   B 1 90  ? 50.131 -5.473  -9.199  1.00 24.20 ?  90  LYS   B HZ2  1 
ATOM   5281 H  HZ3  . LYS   B 1 90  ? 50.135 -5.268  -10.634 1.00 24.20 ?  90  LYS   B HZ3  1 
ATOM   5282 N  N    . HIS   B 1 91  ? 47.801 -11.325 -7.748  1.00 11.04 ?  91  HIS   B N    1 
ATOM   5283 C  CA   . HIS   B 1 91  ? 47.342 -11.348 -6.374  1.00 11.14 ?  91  HIS   B CA   1 
ATOM   5284 C  C    . HIS   B 1 91  ? 47.347 -12.773 -5.854  1.00 10.42 ?  91  HIS   B C    1 
ATOM   5285 O  O    . HIS   B 1 91  ? 47.102 -13.724 -6.604  1.00 10.83 ?  91  HIS   B O    1 
ATOM   5286 C  CB   . HIS   B 1 91  ? 45.891 -10.871 -6.252  1.00 12.99 ?  91  HIS   B CB   1 
ATOM   5287 C  CG   . HIS   B 1 91  ? 45.676 -9.462  -6.685  1.00 16.11 ?  91  HIS   B CG   1 
ATOM   5288 N  ND1  . HIS   B 1 91  ? 46.273 -8.389  -6.059  1.00 18.63 ?  91  HIS   B ND1  1 
ATOM   5289 C  CD2  . HIS   B 1 91  ? 44.909 -8.945  -7.670  1.00 18.43 ?  91  HIS   B CD2  1 
ATOM   5290 C  CE1  . HIS   B 1 91  ? 45.893 -7.268  -6.649  1.00 19.51 ?  91  HIS   B CE1  1 
ATOM   5291 N  NE2  . HIS   B 1 91  ? 45.057 -7.579  -7.624  1.00 19.60 ?  91  HIS   B NE2  1 
ATOM   5292 H  H    . HIS   B 1 91  ? 47.391 -11.897 -8.244  1.00 13.26 ?  91  HIS   B H    1 
ATOM   5293 H  HA   . HIS   B 1 91  ? 47.910 -10.792 -5.812  1.00 13.39 ?  91  HIS   B HA   1 
ATOM   5294 H  HB2  . HIS   B 1 91  ? 45.327 -11.435 -6.802  1.00 15.60 ?  91  HIS   B HB2  1 
ATOM   5295 H  HB3  . HIS   B 1 91  ? 45.614 -10.937 -5.322  1.00 15.60 ?  91  HIS   B HB3  1 
ATOM   5296 H  HD1  . HIS   B 1 91  ? 46.810 -8.440  -5.387  1.00 22.37 ?  91  HIS   B HD1  1 
ATOM   5297 H  HD2  . HIS   B 1 91  ? 44.382 -9.410  -8.272  1.00 22.13 ?  91  HIS   B HD2  1 
ATOM   5298 H  HE1  . HIS   B 1 91  ? 46.166 -6.407  -6.408  1.00 23.42 ?  91  HIS   B HE1  1 
ATOM   5299 N  N    . CYS   B 1 92  ? 47.537 -12.909 -4.550  1.00 10.35 ?  92  CYS   B N    1 
ATOM   5300 C  CA   . CYS   B 1 92  ? 47.235 -14.144 -3.843  1.00 10.22 ?  92  CYS   B CA   1 
ATOM   5301 C  C    . CYS   B 1 92  ? 46.017 -13.911 -2.959  1.00 9.93  ?  92  CYS   B C    1 
ATOM   5302 O  O    . CYS   B 1 92  ? 46.015 -13.004 -2.113  1.00 10.80 ?  92  CYS   B O    1 
ATOM   5303 C  CB   . CYS   B 1 92  ? 48.415 -14.607 -2.994  1.00 10.77 ?  92  CYS   B CB   1 
ATOM   5304 S  SG   . CYS   B 1 92  ? 48.057 -16.142 -2.094  1.00 10.66 ?  92  CYS   B SG   1 
ATOM   5305 H  H    . CYS   B 1 92  ? 47.867 -12.290 -4.045  1.00 12.43 ?  92  CYS   B H    1 
ATOM   5306 H  HA   . CYS   B 1 92  ? 47.033 -14.839 -4.490  1.00 12.28 ?  92  CYS   B HA   1 
ATOM   5307 H  HB2  . CYS   B 1 92  ? 49.176 -14.762 -3.566  1.00 12.94 ?  92  CYS   B HB2  1 
ATOM   5308 H  HB3  . CYS   B 1 92  ? 48.615 -13.919 -2.341  1.00 12.94 ?  92  CYS   B HB3  1 
ATOM   5309 H  HG   . CYS   B 1 92  ? 49.035 -16.455 -1.469  1.00 12.81 ?  92  CYS   B HG   1 
ATOM   5310 N  N    . LEU   B 1 93  ? 44.982 -14.723 -3.169  1.00 9.72  ?  93  LEU   B N    1 
ATOM   5311 C  CA   . LEU   B 1 93  ? 43.808 -14.740 -2.307  1.00 10.13 ?  93  LEU   B CA   1 
ATOM   5312 C  C    . LEU   B 1 93  ? 44.034 -15.803 -1.240  1.00 9.38  ?  93  LEU   B C    1 
ATOM   5313 O  O    . LEU   B 1 93  ? 43.992 -17.005 -1.535  1.00 10.11 ?  93  LEU   B O    1 
ATOM   5314 C  CB   . LEU   B 1 93  ? 42.542 -15.026 -3.112  1.00 10.33 ?  93  LEU   B CB   1 
ATOM   5315 C  CG   . LEU   B 1 93  ? 41.244 -15.052 -2.302  1.00 10.84 ?  93  LEU   B CG   1 
ATOM   5316 C  CD1  . LEU   B 1 93  ? 40.886 -13.665 -1.795  1.00 11.11 ?  93  LEU   B CD1  1 
ATOM   5317 C  CD2  . LEU   B 1 93  ? 40.113 -15.636 -3.133  1.00 11.35 ?  93  LEU   B CD2  1 
ATOM   5318 H  H    . LEU   B 1 93  ? 44.943 -15.296 -3.824  1.00 11.68 ?  93  LEU   B H    1 
ATOM   5319 H  HA   . LEU   B 1 93  ? 43.719 -13.880 -1.878  1.00 12.17 ?  93  LEU   B HA   1 
ATOM   5320 H  HB2  . LEU   B 1 93  ? 42.446 -14.332 -3.788  1.00 12.41 ?  93  LEU   B HB2  1 
ATOM   5321 H  HB3  . LEU   B 1 93  ? 42.635 -15.886 -3.543  1.00 12.41 ?  93  LEU   B HB3  1 
ATOM   5322 H  HG   . LEU   B 1 93  ? 41.369 -15.625 -1.532  1.00 13.02 ?  93  LEU   B HG   1 
ATOM   5323 H  HD11 . LEU   B 1 93  ? 40.038 -13.709 -1.329  1.00 13.34 ?  93  LEU   B HD11 1 
ATOM   5324 H  HD12 . LEU   B 1 93  ? 41.581 -13.360 -1.191  1.00 13.34 ?  93  LEU   B HD12 1 
ATOM   5325 H  HD13 . LEU   B 1 93  ? 40.818 -13.060 -2.552  1.00 13.34 ?  93  LEU   B HD13 1 
ATOM   5326 H  HD21 . LEU   B 1 93  ? 39.301 -15.637 -2.602  1.00 13.64 ?  93  LEU   B HD21 1 
ATOM   5327 H  HD22 . LEU   B 1 93  ? 39.990 -15.091 -3.926  1.00 13.64 ?  93  LEU   B HD22 1 
ATOM   5328 H  HD23 . LEU   B 1 93  ? 40.344 -16.543 -3.387  1.00 13.64 ?  93  LEU   B HD23 1 
ATOM   5329 N  N    . HIS   B 1 94  ? 44.309 -15.364 -0.018  1.00 9.43  ?  94  HIS   B N    1 
ATOM   5330 C  CA   . HIS   B 1 94  ? 44.532 -16.270 1.102   1.00 9.73  ?  94  HIS   B CA   1 
ATOM   5331 C  C    . HIS   B 1 94  ? 43.172 -16.630 1.682   1.00 10.05 ?  94  HIS   B C    1 
ATOM   5332 O  O    . HIS   B 1 94  ? 42.501 -15.756 2.232   1.00 11.43 ?  94  HIS   B O    1 
ATOM   5333 C  CB   . HIS   B 1 94  ? 45.402 -15.585 2.158   1.00 10.16 ?  94  HIS   B CB   1 
ATOM   5334 C  CG   . HIS   B 1 94  ? 46.786 -15.286 1.688   1.00 10.31 ?  94  HIS   B CG   1 
ATOM   5335 N  ND1  . HIS   B 1 94  ? 47.810 -16.205 1.768   1.00 10.41 ?  94  HIS   B ND1  1 
ATOM   5336 C  CD2  . HIS   B 1 94  ? 47.298 -14.177 1.100   1.00 10.48 ?  94  HIS   B CD2  1 
ATOM   5337 C  CE1  . HIS   B 1 94  ? 48.899 -15.657 1.255   1.00 10.50 ?  94  HIS   B CE1  1 
ATOM   5338 N  NE2  . HIS   B 1 94  ? 48.617 -14.430 0.845   1.00 10.78 ?  94  HIS   B NE2  1 
ATOM   5339 H  H    . HIS   B 1 94  ? 44.379 -14.528 0.188   1.00 11.32 ?  94  HIS   B H    1 
ATOM   5340 H  HA   . HIS   B 1 94  ? 44.975 -17.077 0.796   1.00 11.69 ?  94  HIS   B HA   1 
ATOM   5341 H  HB2  . HIS   B 1 94  ? 44.985 -14.746 2.406   1.00 12.21 ?  94  HIS   B HB2  1 
ATOM   5342 H  HB3  . HIS   B 1 94  ? 45.468 -16.165 2.929   1.00 12.21 ?  94  HIS   B HB3  1 
ATOM   5343 H  HD2  . HIS   B 1 94  ? 46.846 -13.390 0.910   1.00 12.59 ?  94  HIS   B HD2  1 
ATOM   5344 H  HE1  . HIS   B 1 94  ? 49.731 -16.078 1.197   1.00 12.61 ?  94  HIS   B HE1  1 
ATOM   5345 H  HE2  . HIS   B 1 94  ? 49.179 -13.891 0.483   1.00 12.95 ?  94  HIS   B HE2  1 
ATOM   5346 N  N    . VAL   B 1 95  ? 42.737 -17.880 1.526   1.00 9.86  ?  95  VAL   B N    1 
ATOM   5347 C  CA   . VAL   B 1 95  ? 41.410 -18.320 1.961   1.00 10.31 ?  95  VAL   B CA   1 
ATOM   5348 C  C    . VAL   B 1 95  ? 41.581 -19.358 3.056   1.00 10.07 ?  95  VAL   B C    1 
ATOM   5349 O  O    . VAL   B 1 95  ? 42.358 -20.309 2.898   1.00 10.93 ?  95  VAL   B O    1 
ATOM   5350 C  CB   . VAL   B 1 95  ? 40.590 -18.927 0.806   1.00 10.25 ?  95  VAL   B CB   1 
ATOM   5351 C  CG1  . VAL   B 1 95  ? 39.210 -19.376 1.293   1.00 11.23 ?  95  VAL   B CG1  1 
ATOM   5352 C  CG2  . VAL   B 1 95  ? 40.469 -17.941 -0.334  1.00 10.69 ?  95  VAL   B CG2  1 
ATOM   5353 H  H    . VAL   B 1 95  ? 43.202 -18.505 1.162   1.00 11.84 ?  95  VAL   B H    1 
ATOM   5354 H  HA   . VAL   B 1 95  ? 40.917 -17.568 2.324   1.00 12.38 ?  95  VAL   B HA   1 
ATOM   5355 H  HB   . VAL   B 1 95  ? 41.051 -19.709 0.469   1.00 12.32 ?  95  VAL   B HB   1 
ATOM   5356 H  HG11 . VAL   B 1 95  ? 38.649 -19.577 0.521   1.00 13.49 ?  95  VAL   B HG11 1 
ATOM   5357 H  HG12 . VAL   B 1 95  ? 39.303 -20.173 1.839   1.00 13.49 ?  95  VAL   B HG12 1 
ATOM   5358 H  HG13 . VAL   B 1 95  ? 38.803 -18.665 1.811   1.00 13.49 ?  95  VAL   B HG13 1 
ATOM   5359 H  HG21 . VAL   B 1 95  ? 39.886 -18.320 -1.012  1.00 12.84 ?  95  VAL   B HG21 1 
ATOM   5360 H  HG22 . VAL   B 1 95  ? 40.088 -17.118 0.006   1.00 12.84 ?  95  VAL   B HG22 1 
ATOM   5361 H  HG23 . VAL   B 1 95  ? 41.348 -17.781 -0.700  1.00 12.84 ?  95  VAL   B HG23 1 
ATOM   5362 N  N    . VAL   B 1 96  ? 40.854 -19.188 4.153   1.00 10.73 ?  96  VAL   B N    1 
ATOM   5363 C  CA   . VAL   B 1 96  ? 40.938 -20.103 5.290   1.00 10.94 ?  96  VAL   B CA   1 
ATOM   5364 C  C    . VAL   B 1 96  ? 39.750 -21.065 5.242   1.00 11.34 ?  96  VAL   B C    1 
ATOM   5365 O  O    . VAL   B 1 96  ? 38.631 -20.705 5.616   1.00 11.96 ?  96  VAL   B O    1 
ATOM   5366 C  CB   . VAL   B 1 96  ? 40.990 -19.355 6.625   1.00 11.72 ?  96  VAL   B CB   1 
ATOM   5367 C  CG1  . VAL   B 1 96  ? 41.153 -20.351 7.774   1.00 12.74 ?  96  VAL   B CG1  1 
ATOM   5368 C  CG2  . VAL   B 1 96  ? 42.108 -18.323 6.638   1.00 12.29 ?  96  VAL   B CG2  1 
ATOM   5369 H  H    . VAL   B 1 96  ? 40.300 -18.543 4.269   1.00 12.89 ?  96  VAL   B H    1 
ATOM   5370 H  HA   . VAL   B 1 96  ? 41.751 -20.631 5.215   1.00 13.15 ?  96  VAL   B HA   1 
ATOM   5371 H  HB   . VAL   B 1 96  ? 40.151 -18.888 6.757   1.00 14.08 ?  96  VAL   B HB   1 
ATOM   5372 H  HG11 . VAL   B 1 96  ? 41.341 -19.863 8.595   1.00 15.30 ?  96  VAL   B HG11 1 
ATOM   5373 H  HG12 . VAL   B 1 96  ? 40.335 -20.861 7.879   1.00 15.30 ?  96  VAL   B HG12 1 
ATOM   5374 H  HG13 . VAL   B 1 96  ? 41.893 -20.949 7.577   1.00 15.30 ?  96  VAL   B HG13 1 
ATOM   5375 H  HG21 . VAL   B 1 96  ? 42.154 -17.913 7.519   1.00 14.76 ?  96  VAL   B HG21 1 
ATOM   5376 H  HG22 . VAL   B 1 96  ? 42.949 -18.759 6.434   1.00 14.76 ?  96  VAL   B HG22 1 
ATOM   5377 H  HG23 . VAL   B 1 96  ? 41.919 -17.642 5.971   1.00 14.76 ?  96  VAL   B HG23 1 
ATOM   5378 N  N    . GLY   B 1 97  ? 39.984 -22.299 4.800   1.00 11.39 ?  97  GLY   B N    1 
ATOM   5379 C  CA   . GLY   B 1 97  ? 39.009 -23.354 4.965   1.00 11.95 ?  97  GLY   B CA   1 
ATOM   5380 C  C    . GLY   B 1 97  ? 39.141 -23.965 6.343   1.00 13.21 ?  97  GLY   B C    1 
ATOM   5381 O  O    . GLY   B 1 97  ? 40.185 -23.842 6.997   1.00 13.72 ?  97  GLY   B O    1 
ATOM   5382 H  H    . GLY   B 1 97  ? 40.709 -22.542 4.403   1.00 13.68 ?  97  GLY   B H    1 
ATOM   5383 H  HA2  . GLY   B 1 97  ? 38.115 -22.982 4.855   1.00 14.36 ?  97  GLY   B HA2  1 
ATOM   5384 H  HA3  . GLY   B 1 97  ? 39.147 -24.035 4.289   1.00 14.36 ?  97  GLY   B HA3  1 
ATOM   5385 N  N    . PRO   B 1 98  ? 38.093 -24.647 6.809   1.00 13.98 ?  98  PRO   B N    1 
ATOM   5386 C  CA   . PRO   B 1 98  ? 38.185 -25.344 8.095   1.00 15.00 ?  98  PRO   B CA   1 
ATOM   5387 C  C    . PRO   B 1 98  ? 39.207 -26.469 8.048   1.00 14.51 ?  98  PRO   B C    1 
ATOM   5388 O  O    . PRO   B 1 98  ? 39.312 -27.203 7.065   1.00 14.61 ?  98  PRO   B O    1 
ATOM   5389 C  CB   . PRO   B 1 98  ? 36.764 -25.881 8.305   1.00 15.43 ?  98  PRO   B CB   1 
ATOM   5390 C  CG   . PRO   B 1 98  ? 36.205 -26.023 6.934   1.00 14.79 ?  98  PRO   B CG   1 
ATOM   5391 C  CD   . PRO   B 1 98  ? 36.776 -24.845 6.174   1.00 14.37 ?  98  PRO   B CD   1 
ATOM   5392 H  HA   . PRO   B 1 98  ? 38.412 -24.721 8.798   1.00 18.02 ?  98  PRO   B HA   1 
ATOM   5393 H  HB2  . PRO   B 1 98  ? 36.802 -26.742 8.750   1.00 18.54 ?  98  PRO   B HB2  1 
ATOM   5394 H  HB3  . PRO   B 1 98  ? 36.246 -25.246 8.820   1.00 18.54 ?  98  PRO   B HB3  1 
ATOM   5395 H  HG2  . PRO   B 1 98  ? 36.498 -26.864 6.543   1.00 17.77 ?  98  PRO   B HG2  1 
ATOM   5396 H  HG3  . PRO   B 1 98  ? 35.237 -25.978 6.965   1.00 17.77 ?  98  PRO   B HG3  1 
ATOM   5397 H  HD2  . PRO   B 1 98  ? 36.875 -25.069 5.228   1.00 17.26 ?  98  PRO   B HD2  1 
ATOM   5398 H  HD3  . PRO   B 1 98  ? 36.223 -24.060 6.293   1.00 17.26 ?  98  PRO   B HD3  1 
ATOM   5399 N  N    . ASN   B 1 99  ? 39.958 -26.596 9.131   1.00 15.54 ?  99  ASN   B N    1 
ATOM   5400 C  CA   . ASN   B 1 99  ? 40.936 -27.668 9.291   1.00 16.56 ?  99  ASN   B CA   1 
ATOM   5401 C  C    . ASN   B 1 99  ? 40.308 -28.749 10.170  1.00 19.09 ?  99  ASN   B C    1 
ATOM   5402 O  O    . ASN   B 1 99  ? 40.231 -28.603 11.392  1.00 20.03 ?  99  ASN   B O    1 
ATOM   5403 C  CB   . ASN   B 1 99  ? 42.212 -27.112 9.909   1.00 16.64 ?  99  ASN   B CB   1 
ATOM   5404 C  CG   . ASN   B 1 99  ? 43.343 -28.115 9.910   1.00 17.48 ?  99  ASN   B CG   1 
ATOM   5405 O  OD1  . ASN   B 1 99  ? 43.121 -29.304 10.084  1.00 18.33 ?  99  ASN   B OD1  1 
ATOM   5406 N  ND2  . ASN   B 1 99  ? 44.557 -27.638 9.708   1.00 17.90 ?  99  ASN   B ND2  1 
ATOM   5407 H  H    . ASN   B 1 99  ? 39.918 -26.060 9.801   1.00 18.66 ?  99  ASN   B H    1 
ATOM   5408 H  HA   . ASN   B 1 99  ? 41.142 -28.057 8.430   1.00 19.89 ?  99  ASN   B HA   1 
ATOM   5409 H  HB2  . ASN   B 1 99  ? 42.490 -26.340 9.408   1.00 19.98 ?  99  ASN   B HB2  1 
ATOM   5410 H  HB3  . ASN   B 1 99  ? 42.023 -26.864 10.833  1.00 19.98 ?  99  ASN   B HB3  1 
ATOM   5411 H  HD21 . ASN   B 1 99  ? 45.230 -28.169 9.702   1.00 21.49 ?  99  ASN   B HD21 1 
ATOM   5412 H  HD22 . ASN   B 1 99  ? 44.667 -26.795 9.591   1.00 21.49 ?  99  ASN   B HD22 1 
ATOM   5413 N  N    A VAL   B 1 100 ? 39.840 -29.831 9.540   0.50 21.05 ?  100 VAL   B N    1 
ATOM   5414 N  N    B VAL   B 1 100 ? 39.852 -29.833 9.535   0.50 21.03 ?  100 VAL   B N    1 
ATOM   5415 C  CA   A VAL   B 1 100 ? 39.229 -30.924 10.295  0.50 23.50 ?  100 VAL   B CA   1 
ATOM   5416 C  CA   B VAL   B 1 100 ? 39.235 -30.936 10.270  0.50 23.44 ?  100 VAL   B CA   1 
ATOM   5417 C  C    A VAL   B 1 100 ? 40.244 -31.578 11.224  0.50 23.93 ?  100 VAL   B C    1 
ATOM   5418 C  C    B VAL   B 1 100 ? 40.239 -31.599 11.204  0.50 23.86 ?  100 VAL   B C    1 
ATOM   5419 O  O    A VAL   B 1 100 ? 39.887 -32.058 12.307  0.50 24.69 ?  100 VAL   B O    1 
ATOM   5420 O  O    B VAL   B 1 100 ? 39.867 -32.108 12.268  0.50 24.52 ?  100 VAL   B O    1 
ATOM   5421 C  CB   A VAL   B 1 100 ? 38.571 -31.942 9.341   0.50 25.75 ?  100 VAL   B CB   1 
ATOM   5422 C  CB   B VAL   B 1 100 ? 38.607 -31.942 9.283   0.50 25.60 ?  100 VAL   B CB   1 
ATOM   5423 C  CG1  A VAL   B 1 100 ? 38.077 -33.159 10.111  0.50 26.64 ?  100 VAL   B CG1  1 
ATOM   5424 C  CG1  B VAL   B 1 100 ? 38.106 -33.178 10.018  0.50 26.45 ?  100 VAL   B CG1  1 
ATOM   5425 C  CG2  A VAL   B 1 100 ? 37.421 -31.294 8.584   0.50 26.37 ?  100 VAL   B CG2  1 
ATOM   5426 C  CG2  B VAL   B 1 100 ? 37.472 -31.285 8.513   0.50 26.17 ?  100 VAL   B CG2  1 
ATOM   5427 H  H    A VAL   B 1 100 ? 39.853 -29.949 8.686   0.50 25.28 ?  100 VAL   B H    1 
ATOM   5428 H  H    B VAL   B 1 100 ? 39.882 -29.948 8.682   0.50 25.26 ?  100 VAL   B H    1 
ATOM   5429 H  HA   A VAL   B 1 100 ? 38.522 -30.557 10.846  0.50 28.21 ?  100 VAL   B HA   1 
ATOM   5430 H  HA   B VAL   B 1 100 ? 38.515 -30.581 10.814  0.50 28.14 ?  100 VAL   B HA   1 
ATOM   5431 H  HB   A VAL   B 1 100 ? 39.225 -32.245 8.694   0.50 30.91 ?  100 VAL   B HB   1 
ATOM   5432 H  HB   B VAL   B 1 100 ? 39.279 -32.227 8.644   0.50 30.73 ?  100 VAL   B HB   1 
ATOM   5433 H  HG11 A VAL   B 1 100 ? 37.479 -33.671 9.542   0.50 31.98 ?  100 VAL   B HG11 1 
ATOM   5434 H  HG11 B VAL   B 1 100 ? 37.524 -33.683 9.426   0.50 31.75 ?  100 VAL   B HG11 1 
ATOM   5435 H  HG12 A VAL   B 1 100 ? 38.836 -33.707 10.365  0.50 31.98 ?  100 VAL   B HG12 1 
ATOM   5436 H  HG12 B VAL   B 1 100 ? 38.864 -33.725 10.278  0.50 31.75 ?  100 VAL   B HG12 1 
ATOM   5437 H  HG13 A VAL   B 1 100 ? 37.601 -32.862 10.902  0.50 31.98 ?  100 VAL   B HG13 1 
ATOM   5438 H  HG13 B VAL   B 1 100 ? 37.611 -32.899 10.805  0.50 31.75 ?  100 VAL   B HG13 1 
ATOM   5439 H  HG21 A VAL   B 1 100 ? 37.038 -31.946 7.975   0.50 31.66 ?  100 VAL   B HG21 1 
ATOM   5440 H  HG21 B VAL   B 1 100 ? 37.089 -31.933 7.901   0.50 31.42 ?  100 VAL   B HG21 1 
ATOM   5441 H  HG22 A VAL   B 1 100 ? 36.749 -31.003 9.220   0.50 31.66 ?  100 VAL   B HG22 1 
ATOM   5442 H  HG22 B VAL   B 1 100 ? 36.797 -30.985 9.143   0.50 31.42 ?  100 VAL   B HG22 1 
ATOM   5443 H  HG23 A VAL   B 1 100 ? 37.759 -30.536 8.086   0.50 31.66 ?  100 VAL   B HG23 1 
ATOM   5444 H  HG23 B VAL   B 1 100 ? 37.824 -30.530 8.019   0.50 31.42 ?  100 VAL   B HG23 1 
ATOM   5445 N  N    . ASN   B 1 101 ? 41.518 -31.619 10.822  1.00 24.51 ?  101 ASN   B N    1 
ATOM   5446 C  CA   . ASN   B 1 101 ? 42.559 -32.155 11.698  1.00 26.23 ?  101 ASN   B CA   1 
ATOM   5447 C  C    . ASN   B 1 101 ? 42.757 -31.315 12.953  1.00 28.21 ?  101 ASN   B C    1 
ATOM   5448 O  O    . ASN   B 1 101 ? 43.415 -31.781 13.893  1.00 29.61 ?  101 ASN   B O    1 
ATOM   5449 C  CB   . ASN   B 1 101 ? 43.882 -32.289 10.941  1.00 26.22 ?  101 ASN   B CB   1 
ATOM   5450 C  CG   . ASN   B 1 101 ? 43.865 -33.428 9.940   1.00 25.51 ?  101 ASN   B CG   1 
ATOM   5451 O  OD1  . ASN   B 1 101 ? 43.187 -34.432 10.142  1.00 26.43 ?  101 ASN   B OD1  1 
ATOM   5452 N  ND2  . ASN   B 1 101 ? 44.607 -33.273 8.850   1.00 25.20 ?  101 ASN   B ND2  1 
ATOM   5453 H  H    A ASN   B 1 101 ? 41.794 -31.357 10.050  0.50 29.43 ?  101 ASN   B H    1 
ATOM   5454 H  H    B ASN   B 1 101 ? 41.801 -31.338 10.059  0.50 29.43 ?  101 ASN   B H    1 
ATOM   5455 H  HA   . ASN   B 1 101 ? 42.293 -33.038 11.980  1.00 31.49 ?  101 ASN   B HA   1 
ATOM   5456 H  HB2  . ASN   B 1 101 ? 44.063 -31.467 10.457  1.00 31.47 ?  101 ASN   B HB2  1 
ATOM   5457 H  HB3  . ASN   B 1 101 ? 44.593 -32.460 11.577  1.00 31.47 ?  101 ASN   B HB3  1 
ATOM   5458 H  HD21 . ASN   B 1 101 ? 44.628 -33.891 8.253   1.00 30.25 ?  101 ASN   B HD21 1 
ATOM   5459 H  HD22 . ASN   B 1 101 ? 45.066 -32.554 8.740   1.00 30.25 ?  101 ASN   B HD22 1 
ATOM   5460 N  N    . LYS   B 1 102 ? 42.217 -30.095 12.984  1.00 30.43 ?  102 LYS   B N    1 
ATOM   5461 C  CA   . LYS   B 1 102 ? 42.193 -29.259 14.177  1.00 33.20 ?  102 LYS   B CA   1 
ATOM   5462 C  C    . LYS   B 1 102 ? 40.811 -29.206 14.819  1.00 32.45 ?  102 LYS   B C    1 
ATOM   5463 O  O    . LYS   B 1 102 ? 40.591 -28.396 15.724  1.00 33.45 ?  102 LYS   B O    1 
ATOM   5464 C  CB   . LYS   B 1 102 ? 42.637 -27.834 13.842  1.00 36.97 ?  102 LYS   B CB   1 
ATOM   5465 C  CG   . LYS   B 1 102 ? 44.096 -27.679 13.457  1.00 40.38 ?  102 LYS   B CG   1 
ATOM   5466 C  CD   . LYS   B 1 102 ? 44.346 -26.267 12.948  1.00 43.60 ?  102 LYS   B CD   1 
ATOM   5467 C  CE   . LYS   B 1 102 ? 45.824 -25.938 12.850  1.00 45.95 ?  102 LYS   B CE   1 
ATOM   5468 N  NZ   . LYS   B 1 102 ? 46.031 -24.534 12.388  1.00 47.27 ?  102 LYS   B NZ   1 
ATOM   5469 H  H    . LYS   B 1 102 ? 41.840 -29.719 12.304  1.00 36.53 ?  102 LYS   B H    1 
ATOM   5470 H  HA   . LYS   B 1 102 ? 42.817 -29.618 14.825  1.00 39.86 ?  102 LYS   B HA   1 
ATOM   5471 H  HB2  . LYS   B 1 102 ? 42.104 -27.511 13.099  1.00 44.38 ?  102 LYS   B HB2  1 
ATOM   5472 H  HB3  . LYS   B 1 102 ? 42.481 -27.271 14.619  1.00 44.38 ?  102 LYS   B HB3  1 
ATOM   5473 H  HG2  . LYS   B 1 102 ? 44.657 -27.831 14.235  1.00 48.47 ?  102 LYS   B HG2  1 
ATOM   5474 H  HG3  . LYS   B 1 102 ? 44.315 -28.307 12.751  1.00 48.47 ?  102 LYS   B HG3  1 
ATOM   5475 H  HD2  . LYS   B 1 102 ? 43.959 -26.177 12.063  1.00 52.33 ?  102 LYS   B HD2  1 
ATOM   5476 H  HD3  . LYS   B 1 102 ? 43.936 -25.633 13.557  1.00 52.33 ?  102 LYS   B HD3  1 
ATOM   5477 H  HE2  . LYS   B 1 102 ? 46.234 -26.035 13.725  1.00 55.16 ?  102 LYS   B HE2  1 
ATOM   5478 H  HE3  . LYS   B 1 102 ? 46.246 -26.535 12.213  1.00 55.16 ?  102 LYS   B HE3  1 
ATOM   5479 H  HZ1  . LYS   B 1 102 ? 46.900 -24.355 12.336  1.00 56.73 ?  102 LYS   B HZ1  1 
ATOM   5480 H  HZ2  . LYS   B 1 102 ? 45.663 -24.422 11.585  1.00 56.73 ?  102 LYS   B HZ2  1 
ATOM   5481 H  HZ3  . LYS   B 1 102 ? 45.652 -23.967 12.960  1.00 56.73 ?  102 LYS   B HZ3  1 
ATOM   5482 N  N    . GLY   B 1 103 ? 39.872 -30.028 14.356  1.00 31.47 ?  103 GLY   B N    1 
ATOM   5483 C  CA   . GLY   B 1 103 ? 38.544 -30.072 14.934  1.00 30.86 ?  103 GLY   B CA   1 
ATOM   5484 C  C    . GLY   B 1 103 ? 37.598 -28.989 14.468  1.00 29.83 ?  103 GLY   B C    1 
ATOM   5485 O  O    . GLY   B 1 103 ? 36.506 -28.859 15.033  1.00 30.53 ?  103 GLY   B O    1 
ATOM   5486 H  H    . GLY   B 1 103 ? 39.983 -30.568 13.699  1.00 37.78 ?  103 GLY   B H    1 
ATOM   5487 H  HA2  . GLY   B 1 103 ? 38.140 -30.927 14.723  1.00 37.05 ?  103 GLY   B HA2  1 
ATOM   5488 H  HA3  . GLY   B 1 103 ? 38.619 -30.006 15.899  1.00 37.05 ?  103 GLY   B HA3  1 
ATOM   5489 N  N    A GLU   B 1 104 ? 37.985 -28.199 13.470  0.50 28.91 ?  104 GLU   B N    1 
ATOM   5490 N  N    B GLU   B 1 104 ? 37.962 -28.223 13.444  0.50 28.55 ?  104 GLU   B N    1 
ATOM   5491 C  CA   A GLU   B 1 104 ? 37.153 -27.094 13.021  0.50 27.80 ?  104 GLU   B CA   1 
ATOM   5492 C  CA   B GLU   B 1 104 ? 37.106 -27.146 12.974  0.50 27.06 ?  104 GLU   B CA   1 
ATOM   5493 C  C    A GLU   B 1 104 ? 35.969 -27.610 12.207  0.50 28.44 ?  104 GLU   B C    1 
ATOM   5494 C  C    B GLU   B 1 104 ? 35.953 -27.694 12.137  0.50 27.42 ?  104 GLU   B C    1 
ATOM   5495 O  O    A GLU   B 1 104 ? 36.009 -28.697 11.622  0.50 29.16 ?  104 GLU   B O    1 
ATOM   5496 O  O    B GLU   B 1 104 ? 36.042 -28.774 11.544  0.50 28.15 ?  104 GLU   B O    1 
ATOM   5497 C  CB   A GLU   B 1 104 ? 37.993 -26.101 12.216  0.50 26.73 ?  104 GLU   B CB   1 
ATOM   5498 C  CB   B GLU   B 1 104 ? 37.930 -26.127 12.189  0.50 25.91 ?  104 GLU   B CB   1 
ATOM   5499 C  CG   A GLU   B 1 104 ? 39.103 -25.469 13.048  0.50 25.69 ?  104 GLU   B CG   1 
ATOM   5500 C  CG   B GLU   B 1 104 ? 39.008 -25.488 13.051  0.50 24.75 ?  104 GLU   B CG   1 
ATOM   5501 C  CD   A GLU   B 1 104 ? 40.031 -24.579 12.248  0.50 24.73 ?  104 GLU   B CD   1 
ATOM   5502 C  CD   B GLU   B 1 104 ? 39.986 -24.633 12.275  0.50 23.59 ?  104 GLU   B CD   1 
ATOM   5503 O  OE1  A GLU   B 1 104 ? 40.027 -24.655 11.002  0.50 23.06 ?  104 GLU   B OE1  1 
ATOM   5504 O  OE1  B GLU   B 1 104 ? 39.962 -24.652 11.026  0.50 22.19 ?  104 GLU   B OE1  1 
ATOM   5505 O  OE2  A GLU   B 1 104 ? 40.772 -23.799 12.881  0.50 25.11 -1 104 GLU   B OE2  1 
ATOM   5506 O  OE2  B GLU   B 1 104 ? 40.788 -23.940 12.932  0.50 23.55 -1 104 GLU   B OE2  1 
ATOM   5507 H  H    A GLU   B 1 104 ? 38.728 -28.278 13.046  0.50 34.70 ?  104 GLU   B H    1 
ATOM   5508 H  H    B GLU   B 1 104 ? 38.700 -28.304 13.012  0.50 34.27 ?  104 GLU   B H    1 
ATOM   5509 H  HA   A GLU   B 1 104 ? 36.806 -26.627 13.795  0.50 33.37 ?  104 GLU   B HA   1 
ATOM   5510 H  HA   B GLU   B 1 104 ? 36.727 -26.691 13.741  0.50 32.49 ?  104 GLU   B HA   1 
ATOM   5511 H  HB2  A GLU   B 1 104 ? 38.407 -26.559 11.469  0.50 32.09 ?  104 GLU   B HB2  1 
ATOM   5512 H  HB2  B GLU   B 1 104 ? 38.361 -26.570 11.443  0.50 31.10 ?  104 GLU   B HB2  1 
ATOM   5513 H  HB3  A GLU   B 1 104 ? 37.422 -25.386 11.893  0.50 32.09 ?  104 GLU   B HB3  1 
ATOM   5514 H  HB3  B GLU   B 1 104 ? 37.343 -25.423 11.868  0.50 31.10 ?  104 GLU   B HB3  1 
ATOM   5515 H  HG2  A GLU   B 1 104 ? 38.707 -24.921 13.744  0.50 30.84 ?  104 GLU   B HG2  1 
ATOM   5516 H  HG2  B GLU   B 1 104 ? 38.584 -24.921 13.716  0.50 29.71 ?  104 GLU   B HG2  1 
ATOM   5517 H  HG3  A GLU   B 1 104 ? 39.642 -26.169 13.447  0.50 30.84 ?  104 GLU   B HG3  1 
ATOM   5518 H  HG3  B GLU   B 1 104 ? 39.516 -26.186 13.493  0.50 29.71 ?  104 GLU   B HG3  1 
ATOM   5519 N  N    A ASP   B 1 105 ? 34.902 -26.815 12.186  0.50 28.27 ?  105 ASP   B N    1 
ATOM   5520 N  N    B ASP   B 1 105 ? 34.860 -26.934 12.103  0.50 26.81 ?  105 ASP   B N    1 
ATOM   5521 C  CA   A ASP   B 1 105 ? 33.627 -27.266 11.641  0.50 28.91 ?  105 ASP   B CA   1 
ATOM   5522 C  CA   B ASP   B 1 105 ? 33.598 -27.416 11.555  0.50 27.04 ?  105 ASP   B CA   1 
ATOM   5523 C  C    A ASP   B 1 105 ? 33.688 -27.322 10.119  0.50 27.24 ?  105 ASP   B C    1 
ATOM   5524 C  C    B ASP   B 1 105 ? 33.653 -27.422 10.032  0.50 25.76 ?  105 ASP   B C    1 
ATOM   5525 O  O    A ASP   B 1 105 ? 33.872 -26.295 9.458   0.50 26.87 ?  105 ASP   B O    1 
ATOM   5526 O  O    B ASP   B 1 105 ? 33.816 -26.371 9.404   0.50 25.30 ?  105 ASP   B O    1 
ATOM   5527 C  CB   A ASP   B 1 105 ? 32.516 -26.321 12.093  0.50 31.35 ?  105 ASP   B CB   1 
ATOM   5528 C  CB   B ASP   B 1 105 ? 32.449 -26.534 12.043  0.50 28.78 ?  105 ASP   B CB   1 
ATOM   5529 C  CG   A ASP   B 1 105 ? 31.142 -26.782 11.653  0.50 33.58 ?  105 ASP   B CG   1 
ATOM   5530 C  CG   B ASP   B 1 105 ? 31.088 -27.134 11.745  0.50 30.31 ?  105 ASP   B CG   1 
ATOM   5531 O  OD1  A ASP   B 1 105 ? 31.024 -27.919 11.151  0.50 33.94 ?  105 ASP   B OD1  1 
ATOM   5532 O  OD1  B ASP   B 1 105 ? 31.021 -28.105 10.962  0.50 30.47 ?  105 ASP   B OD1  1 
ATOM   5533 O  OD2  A ASP   B 1 105 ? 30.179 -25.998 11.799  0.50 34.70 -1 105 ASP   B OD2  1 
ATOM   5534 O  OD2  B ASP   B 1 105 ? 30.084 -26.642 12.304  0.50 30.66 -1 105 ASP   B OD2  1 
ATOM   5535 H  H    A ASP   B 1 105 ? 34.893 -26.009 12.485  0.50 33.94 ?  105 ASP   B H    1 
ATOM   5536 H  H    B ASP   B 1 105 ? 34.826 -26.127 12.394  0.50 32.18 ?  105 ASP   B H    1 
ATOM   5537 H  HA   A ASP   B 1 105 ? 33.432 -28.156 11.974  0.50 34.70 ?  105 ASP   B HA   1 
ATOM   5538 H  HA   B ASP   B 1 105 ? 33.434 -28.322 11.859  0.50 32.46 ?  105 ASP   B HA   1 
ATOM   5539 H  HB2  A ASP   B 1 105 ? 32.538 -26.251 13.063  0.50 37.63 ?  105 ASP   B HB2  1 
ATOM   5540 H  HB2  B ASP   B 1 105 ? 32.522 -26.420 13.004  0.50 34.55 ?  105 ASP   B HB2  1 
ATOM   5541 H  HB3  A ASP   B 1 105 ? 32.659 -25.451 11.695  0.50 37.63 ?  105 ASP   B HB3  1 
ATOM   5542 H  HB3  B ASP   B 1 105 ? 32.506 -25.668 11.604  0.50 34.55 ?  105 ASP   B HB3  1 
ATOM   5543 N  N    A ILE   B 1 106 ? 33.511 -28.525 9.567   0.50 26.34 ?  106 ILE   B N    1 
ATOM   5544 N  N    B ILE   B 1 106 ? 33.491 -28.610 9.441   0.50 25.21 ?  106 ILE   B N    1 
ATOM   5545 C  CA   A ILE   B 1 106 ? 33.517 -28.713 8.121   0.50 25.27 ?  106 ILE   B CA   1 
ATOM   5546 C  CA   B ILE   B 1 106 ? 33.490 -28.754 7.991   0.50 24.69 ?  106 ILE   B CA   1 
ATOM   5547 C  C    A ILE   B 1 106 ? 32.421 -27.902 7.439   0.50 24.27 ?  106 ILE   B C    1 
ATOM   5548 C  C    B ILE   B 1 106 ? 32.393 -27.922 7.339   0.50 23.97 ?  106 ILE   B C    1 
ATOM   5549 O  O    A ILE   B 1 106 ? 32.532 -27.591 6.249   0.50 23.58 ?  106 ILE   B O    1 
ATOM   5550 O  O    B ILE   B 1 106 ? 32.479 -27.609 6.147   0.50 23.30 ?  106 ILE   B O    1 
ATOM   5551 C  CB   A ILE   B 1 106 ? 33.421 -30.221 7.794   0.50 25.71 ?  106 ILE   B CB   1 
ATOM   5552 C  CB   B ILE   B 1 106 ? 33.386 -30.253 7.622   0.50 25.39 ?  106 ILE   B CB   1 
ATOM   5553 C  CG1  A ILE   B 1 106 ? 33.657 -30.478 6.304   0.50 25.84 ?  106 ILE   B CG1  1 
ATOM   5554 C  CG1  B ILE   B 1 106 ? 33.667 -30.475 6.135   0.50 25.88 ?  106 ILE   B CG1  1 
ATOM   5555 C  CG2  A ILE   B 1 106 ? 32.069 -30.777 8.219   0.50 26.29 ?  106 ILE   B CG2  1 
ATOM   5556 C  CG2  B ILE   B 1 106 ? 32.013 -30.803 7.988   0.50 25.96 ?  106 ILE   B CG2  1 
ATOM   5557 C  CD1  A ILE   B 1 106 ? 35.007 -30.009 5.816   0.50 25.70 ?  106 ILE   B CD1  1 
ATOM   5558 C  CD1  B ILE   B 1 106 ? 35.032 -29.998 5.702   0.50 25.94 ?  106 ILE   B CD1  1 
ATOM   5559 H  H    A ILE   B 1 106 ? 33.389 -29.247 10.015  0.50 31.62 ?  106 ILE   B H    1 
ATOM   5560 H  H    B ILE   B 1 106 ? 33.382 -29.348 9.866   0.50 30.26 ?  106 ILE   B H    1 
ATOM   5561 H  HA   A ILE   B 1 106 ? 34.364 -28.394 7.783   0.50 30.34 ?  106 ILE   B HA   1 
ATOM   5562 H  HA   B ILE   B 1 106 ? 34.335 -28.426 7.658   0.50 29.64 ?  106 ILE   B HA   1 
ATOM   5563 H  HB   A ILE   B 1 106 ? 34.108 -30.687 8.295   0.50 30.86 ?  106 ILE   B HB   1 
ATOM   5564 H  HB   B ILE   B 1 106 ? 34.050 -30.740 8.133   0.50 30.48 ?  106 ILE   B HB   1 
ATOM   5565 H  HG12 A ILE   B 1 106 ? 33.603 -31.434 6.139   0.50 31.02 ?  106 ILE   B HG12 1 
ATOM   5566 H  HG12 B ILE   B 1 106 ? 33.614 -31.427 5.945   0.50 31.07 ?  106 ILE   B HG12 1 
ATOM   5567 H  HG13 A ILE   B 1 106 ? 32.978 -30.018 5.790   0.50 31.02 ?  106 ILE   B HG13 1 
ATOM   5568 H  HG13 B ILE   B 1 106 ? 33.005 -30.000 5.612   0.50 31.07 ?  106 ILE   B HG13 1 
ATOM   5569 H  HG21 A ILE   B 1 106 ? 32.081 -31.742 8.124   0.50 31.56 ?  106 ILE   B HG21 1 
ATOM   5570 H  HG21 B ILE   B 1 106 ? 32.027 -31.769 7.901   0.50 31.17 ?  106 ILE   B HG21 1 
ATOM   5571 H  HG22 A ILE   B 1 106 ? 31.907 -30.538 9.145   0.50 31.56 ?  106 ILE   B HG22 1 
ATOM   5572 H  HG22 B ILE   B 1 106 ? 31.809 -30.557 8.904   0.50 31.17 ?  106 ILE   B HG22 1 
ATOM   5573 H  HG23 A ILE   B 1 106 ? 31.378 -30.399 7.654   0.50 31.56 ?  106 ILE   B HG23 1 
ATOM   5574 H  HG23 B ILE   B 1 106 ? 31.349 -30.427 7.389   0.50 31.17 ?  106 ILE   B HG23 1 
ATOM   5575 H  HD11 A ILE   B 1 106 ? 35.188 -30.411 4.953   0.50 30.85 ?  106 ILE   B HD11 1 
ATOM   5576 H  HD11 B ILE   B 1 106 ? 35.250 -30.399 4.848   0.50 31.14 ?  106 ILE   B HD11 1 
ATOM   5577 H  HD12 A ILE   B 1 106 ? 34.996 -29.042 5.734   0.50 30.85 ?  106 ILE   B HD12 1 
ATOM   5578 H  HD12 B ILE   B 1 106 ? 35.017 -29.031 5.618   0.50 31.14 ?  106 ILE   B HD12 1 
ATOM   5579 H  HD13 A ILE   B 1 106 ? 35.686 -30.279 6.455   0.50 30.85 ?  106 ILE   B HD13 1 
ATOM   5580 H  HD13 B ILE   B 1 106 ? 35.686 -30.264 6.368   0.50 31.14 ?  106 ILE   B HD13 1 
ATOM   5581 N  N    A GLN   B 1 107 ? 31.360 -27.545 8.167   0.50 24.40 ?  107 GLN   B N    1 
ATOM   5582 N  N    B GLN   B 1 107 ? 31.361 -27.545 8.096   0.50 24.36 ?  107 GLN   B N    1 
ATOM   5583 C  CA   A GLN   B 1 107 ? 30.288 -26.741 7.588   0.50 24.79 ?  107 GLN   B CA   1 
ATOM   5584 C  CA   B GLN   B 1 107 ? 30.283 -26.735 7.543   0.50 24.85 ?  107 GLN   B CA   1 
ATOM   5585 C  C    A GLN   B 1 107 ? 30.782 -25.396 7.068   0.50 22.42 ?  107 GLN   B C    1 
ATOM   5586 C  C    B GLN   B 1 107 ? 30.766 -25.367 7.079   0.50 22.54 ?  107 GLN   B C    1 
ATOM   5587 O  O    A GLN   B 1 107 ? 30.153 -24.827 6.171   0.50 22.81 ?  107 GLN   B O    1 
ATOM   5588 O  O    B GLN   B 1 107 ? 30.110 -24.751 6.235   0.50 23.16 ?  107 GLN   B O    1 
ATOM   5589 C  CB   A GLN   B 1 107 ? 29.183 -26.529 8.628   0.50 28.25 ?  107 GLN   B CB   1 
ATOM   5590 C  CB   B GLN   B 1 107 ? 29.165 -26.582 8.578   0.50 28.30 ?  107 GLN   B CB   1 
ATOM   5591 C  CG   A GLN   B 1 107 ? 27.856 -26.021 8.065   0.50 31.51 ?  107 GLN   B CG   1 
ATOM   5592 C  CG   B GLN   B 1 107 ? 27.831 -26.103 8.015   0.50 31.58 ?  107 GLN   B CG   1 
ATOM   5593 C  CD   A GLN   B 1 107 ? 27.795 -24.507 7.950   0.50 34.10 ?  107 GLN   B CD   1 
ATOM   5594 C  CD   B GLN   B 1 107 ? 27.702 -24.590 8.007   0.50 34.23 ?  107 GLN   B CD   1 
ATOM   5595 O  OE1  A GLN   B 1 107 ? 28.637 -23.795 8.501   0.50 35.02 ?  107 GLN   B OE1  1 
ATOM   5596 O  OE1  B GLN   B 1 107 ? 28.530 -23.879 8.577   0.50 35.16 ?  107 GLN   B OE1  1 
ATOM   5597 N  NE2  A GLN   B 1 107 ? 26.790 -24.007 7.234   0.50 34.92 ?  107 GLN   B NE2  1 
ATOM   5598 N  NE2  B GLN   B 1 107 ? 26.653 -24.090 7.361   0.50 35.09 ?  107 GLN   B NE2  1 
ATOM   5599 H  H    A GLN   B 1 107 ? 31.239 -27.757 8.988   0.50 29.30 ?  107 GLN   B H    1 
ATOM   5600 H  H    B GLN   B 1 107 ? 31.265 -27.741 8.923   0.50 29.25 ?  107 GLN   B H    1 
ATOM   5601 H  HA   A GLN   B 1 107 ? 29.905 -27.225 6.837   0.50 29.76 ?  107 GLN   B HA   1 
ATOM   5602 H  HA   B GLN   B 1 107 ? 29.909 -27.193 6.774   0.50 29.83 ?  107 GLN   B HA   1 
ATOM   5603 H  HB2  A GLN   B 1 107 ? 29.008 -27.374 9.066   0.50 33.91 ?  107 GLN   B HB2  1 
ATOM   5604 H  HB2  B GLN   B 1 107 ? 29.012 -27.443 8.990   0.50 33.97 ?  107 GLN   B HB2  1 
ATOM   5605 H  HB3  A GLN   B 1 107 ? 29.493 -25.882 9.281   0.50 33.91 ?  107 GLN   B HB3  1 
ATOM   5606 H  HB3  B GLN   B 1 107 ? 29.450 -25.944 9.249   0.50 33.97 ?  107 GLN   B HB3  1 
ATOM   5607 H  HG2  A GLN   B 1 107 ? 27.725 -26.392 7.180   0.50 37.82 ?  107 GLN   B HG2  1 
ATOM   5608 H  HG2  B GLN   B 1 107 ? 27.740 -26.414 7.101   0.50 37.91 ?  107 GLN   B HG2  1 
ATOM   5609 H  HG3  A GLN   B 1 107 ? 27.136 -26.308 8.653   0.50 37.82 ?  107 GLN   B HG3  1 
ATOM   5610 H  HG3  B GLN   B 1 107 ? 27.112 -26.465 8.560   0.50 37.91 ?  107 GLN   B HG3  1 
ATOM   5611 H  HE21 A GLN   B 1 107 ? 26.221 -24.535 6.862   0.50 41.92 ?  107 GLN   B HE21 1 
ATOM   5612 H  HE21 B GLN   B 1 107 ? 26.094 -24.617 6.972   0.50 42.12 ?  107 GLN   B HE21 1 
ATOM   5613 H  HE22 A GLN   B 1 107 ? 26.706 -23.155 7.142   0.50 41.92 ?  107 GLN   B HE22 1 
ATOM   5614 H  HE22 B GLN   B 1 107 ? 26.532 -23.239 7.331   0.50 42.12 ?  107 GLN   B HE22 1 
ATOM   5615 N  N    . LEU   B 1 108 ? 31.900 -24.884 7.591   1.00 20.46 ?  108 LEU   B N    1 
ATOM   5616 C  CA   . LEU   B 1 108 ? 32.441 -23.588 7.182   1.00 17.96 ?  108 LEU   B CA   1 
ATOM   5617 C  C    . LEU   B 1 108 ? 33.085 -23.611 5.805   1.00 15.80 ?  108 LEU   B C    1 
ATOM   5618 O  O    . LEU   B 1 108 ? 33.517 -22.557 5.318   1.00 15.09 ?  108 LEU   B O    1 
ATOM   5619 C  CB   . LEU   B 1 108 ? 33.449 -23.094 8.216   1.00 18.68 ?  108 LEU   B CB   1 
ATOM   5620 C  CG   . LEU   B 1 108 ? 32.817 -22.629 9.527   1.00 20.12 ?  108 LEU   B CG   1 
ATOM   5621 C  CD1  . LEU   B 1 108 ? 33.833 -22.619 10.655  1.00 20.19 ?  108 LEU   B CD1  1 
ATOM   5622 C  CD2  . LEU   B 1 108 ? 32.222 -21.245 9.343   1.00 21.49 ?  108 LEU   B CD2  1 
ATOM   5623 H  H    A LEU   B 1 108 ? 32.364 -25.277 8.196   0.50 24.57 ?  108 LEU   B H    1 
ATOM   5624 H  H    B LEU   B 1 108 ? 32.369 -25.290 8.184   0.50 24.57 ?  108 LEU   B H    1 
ATOM   5625 H  HA   . LEU   B 1 108 ? 31.713 -22.949 7.152   1.00 21.56 ?  108 LEU   B HA   1 
ATOM   5626 H  HB2  . LEU   B 1 108 ? 34.058 -23.817 8.426   1.00 22.43 ?  108 LEU   B HB2  1 
ATOM   5627 H  HB3  . LEU   B 1 108 ? 33.936 -22.347 7.844   1.00 22.43 ?  108 LEU   B HB3  1 
ATOM   5628 H  HG   . LEU   B 1 108 ? 32.097 -23.236 9.775   1.00 24.15 ?  108 LEU   B HG   1 
ATOM   5629 H  HD11 . LEU   B 1 108 ? 33.393 -22.343 11.476  1.00 24.24 ?  108 LEU   B HD11 1 
ATOM   5630 H  HD12 . LEU   B 1 108 ? 34.197 -23.511 10.759  1.00 24.24 ?  108 LEU   B HD12 1 
ATOM   5631 H  HD13 . LEU   B 1 108 ? 34.540 -21.994 10.434  1.00 24.24 ?  108 LEU   B HD13 1 
ATOM   5632 H  HD21 . LEU   B 1 108 ? 31.858 -20.940 10.189  1.00 25.80 ?  108 LEU   B HD21 1 
ATOM   5633 H  HD22 . LEU   B 1 108 ? 32.919 -20.641 9.046   1.00 25.80 ?  108 LEU   B HD22 1 
ATOM   5634 H  HD23 . LEU   B 1 108 ? 31.516 -21.289 8.678   1.00 25.80 ?  108 LEU   B HD23 1 
ATOM   5635 N  N    . LEU   B 1 109 ? 33.145 -24.777 5.169   1.00 14.60 ?  109 LEU   B N    1 
ATOM   5636 C  CA   . LEU   B 1 109 ? 33.779 -24.882 3.865   1.00 13.88 ?  109 LEU   B CA   1 
ATOM   5637 C  C    . LEU   B 1 109 ? 33.012 -24.102 2.804   1.00 13.10 ?  109 LEU   B C    1 
ATOM   5638 O  O    . LEU   B 1 109 ? 33.626 -23.509 1.909   1.00 12.90 ?  109 LEU   B O    1 
ATOM   5639 C  CB   . LEU   B 1 109 ? 33.901 -26.357 3.492   1.00 14.02 ?  109 LEU   B CB   1 
ATOM   5640 C  CG   . LEU   B 1 109 ? 34.689 -26.697 2.236   1.00 13.99 ?  109 LEU   B CG   1 
ATOM   5641 C  CD1  . LEU   B 1 109 ? 36.059 -26.043 2.262   1.00 13.86 ?  109 LEU   B CD1  1 
ATOM   5642 C  CD2  . LEU   B 1 109 ? 34.814 -28.207 2.100   1.00 14.95 ?  109 LEU   B CD2  1 
ATOM   5643 H  H    . LEU   B 1 109 ? 32.835 -25.517 5.469   1.00 17.53 ?  109 LEU   B H    1 
ATOM   5644 H  HA   . LEU   B 1 109 ? 34.672 -24.513 3.915   1.00 16.67 ?  109 LEU   B HA   1 
ATOM   5645 H  HB2  . LEU   B 1 109 ? 34.328 -26.821 4.229   1.00 16.84 ?  109 LEU   B HB2  1 
ATOM   5646 H  HB3  . LEU   B 1 109 ? 33.006 -26.715 3.370   1.00 16.84 ?  109 LEU   B HB3  1 
ATOM   5647 H  HG   . LEU   B 1 109 ? 34.210 -26.375 1.458   1.00 16.80 ?  109 LEU   B HG   1 
ATOM   5648 H  HD11 . LEU   B 1 109 ? 36.605 -26.418 1.552   1.00 16.64 ?  109 LEU   B HD11 1 
ATOM   5649 H  HD12 . LEU   B 1 109 ? 35.954 -25.089 2.128   1.00 16.64 ?  109 LEU   B HD12 1 
ATOM   5650 H  HD13 . LEU   B 1 109 ? 36.476 -26.215 3.122   1.00 16.64 ?  109 LEU   B HD13 1 
ATOM   5651 H  HD21 . LEU   B 1 109 ? 35.375 -28.413 1.332   1.00 17.96 ?  109 LEU   B HD21 1 
ATOM   5652 H  HD22 . LEU   B 1 109 ? 35.222 -28.567 2.905   1.00 17.96 ?  109 LEU   B HD22 1 
ATOM   5653 H  HD23 . LEU   B 1 109 ? 33.934 -28.594 1.976   1.00 17.96 ?  109 LEU   B HD23 1 
ATOM   5654 N  N    . LYS   B 1 110 ? 31.680 -24.065 2.889   1.00 12.93 ?  110 LYS   B N    1 
ATOM   5655 C  CA   . LYS   B 1 110 ? 30.922 -23.304 1.901   1.00 12.69 ?  110 LYS   B CA   1 
ATOM   5656 C  C    . LYS   B 1 110 ? 31.262 -21.816 1.986   1.00 12.41 ?  110 LYS   B C    1 
ATOM   5657 O  O    . LYS   B 1 110 ? 31.519 -21.165 0.967   1.00 12.33 ?  110 LYS   B O    1 
ATOM   5658 C  CB   . LYS   B 1 110 ? 29.417 -23.550 2.057   1.00 13.35 ?  110 LYS   B CB   1 
ATOM   5659 C  CG   . LYS   B 1 110 ? 28.613 -22.923 0.922   1.00 13.78 ?  110 LYS   B CG   1 
ATOM   5660 C  CD   . LYS   B 1 110 ? 27.146 -23.345 0.944   1.00 14.05 ?  110 LYS   B CD   1 
ATOM   5661 C  CE   . LYS   B 1 110 ? 26.384 -22.815 -0.276  1.00 14.93 ?  110 LYS   B CE   1 
ATOM   5662 N  NZ   . LYS   B 1 110 ? 26.709 -23.540 -1.538  1.00 15.07 ?  110 LYS   B NZ   1 
ATOM   5663 H  H    . LYS   B 1 110 ? 31.210 -24.465 3.486   1.00 15.53 ?  110 LYS   B H    1 
ATOM   5664 H  HA   . LYS   B 1 110 ? 31.177 -23.611 1.015   1.00 15.24 ?  110 LYS   B HA   1 
ATOM   5665 H  HB2  . LYS   B 1 110 ? 29.251 -24.509 2.052   1.00 16.03 ?  110 LYS   B HB2  1 
ATOM   5666 H  HB3  . LYS   B 1 110 ? 29.117 -23.166 2.892   1.00 16.03 ?  110 LYS   B HB3  1 
ATOM   5667 H  HG2  . LYS   B 1 110 ? 28.647 -21.959 1.005   1.00 16.55 ?  110 LYS   B HG2  1 
ATOM   5668 H  HG3  . LYS   B 1 110 ? 28.991 -23.201 0.073   1.00 16.55 ?  110 LYS   B HG3  1 
ATOM   5669 H  HD2  . LYS   B 1 110 ? 27.089 -24.317 0.940   1.00 16.87 ?  110 LYS   B HD2  1 
ATOM   5670 H  HD3  . LYS   B 1 110 ? 26.721 -22.994 1.745   1.00 16.87 ?  110 LYS   B HD3  1 
ATOM   5671 H  HE2  . LYS   B 1 110 ? 25.432 -22.905 -0.120  1.00 17.93 ?  110 LYS   B HE2  1 
ATOM   5672 H  HE3  . LYS   B 1 110 ? 26.612 -21.880 -0.404  1.00 17.93 ?  110 LYS   B HE3  1 
ATOM   5673 H  HZ1  . LYS   B 1 110 ? 26.250 -23.195 -2.215  1.00 18.09 ?  110 LYS   B HZ1  1 
ATOM   5674 H  HZ2  . LYS   B 1 110 ? 27.581 -23.467 -1.713  1.00 18.09 ?  110 LYS   B HZ2  1 
ATOM   5675 H  HZ3  . LYS   B 1 110 ? 26.505 -24.402 -1.454  1.00 18.09 ?  110 LYS   B HZ3  1 
ATOM   5676 N  N    . SER   B 1 111 ? 31.279 -21.262 3.202   1.00 12.67 ?  111 SER   B N    1 
ATOM   5677 C  CA   . SER   B 1 111 ? 31.672 -19.865 3.375   1.00 12.64 ?  111 SER   B CA   1 
ATOM   5678 C  C    . SER   B 1 111 ? 33.055 -19.605 2.790   1.00 11.84 ?  111 SER   B C    1 
ATOM   5679 O  O    . SER   B 1 111 ? 33.282 -18.574 2.143   1.00 12.15 ?  111 SER   B O    1 
ATOM   5680 C  CB   . SER   B 1 111 ? 31.667 -19.506 4.858   1.00 13.70 ?  111 SER   B CB   1 
ATOM   5681 O  OG   . SER   B 1 111 ? 30.361 -19.498 5.379   1.00 15.10 ?  111 SER   B OG   1 
ATOM   5682 H  H    . SER   B 1 111 ? 31.070 -21.671 3.930   1.00 15.21 ?  111 SER   B H    1 
ATOM   5683 H  HA   . SER   B 1 111 ? 31.037 -19.295 2.921   1.00 15.18 ?  111 SER   B HA   1 
ATOM   5684 H  HB2  . SER   B 1 111 ? 32.184 -20.165 5.348   1.00 16.45 ?  111 SER   B HB2  1 
ATOM   5685 H  HB3  . SER   B 1 111 ? 32.053 -18.628 4.974   1.00 16.45 ?  111 SER   B HB3  1 
ATOM   5686 H  HG   . SER   B 1 111 ? 30.369 -19.292 6.202   1.00 18.14 ?  111 SER   B HG   1 
ATOM   5687 N  N    . ALA   B 1 112 ? 33.995 -20.524 3.015   1.00 12.07 ?  112 ALA   B N    1 
ATOM   5688 C  CA   . ALA   B 1 112 ? 35.339 -20.353 2.469   1.00 11.82 ?  112 ALA   B CA   1 
ATOM   5689 C  C    . ALA   B 1 112 ? 35.301 -20.252 0.948   1.00 11.17 ?  112 ALA   B C    1 
ATOM   5690 O  O    . ALA   B 1 112 ? 35.931 -19.372 0.354   1.00 11.80 ?  112 ALA   B O    1 
ATOM   5691 C  CB   . ALA   B 1 112 ? 36.246 -21.498 2.934   1.00 12.37 ?  112 ALA   B CB   1 
ATOM   5692 H  H    . ALA   B 1 112 ? 33.884 -21.248 3.474   1.00 14.50 ?  112 ALA   B H    1 
ATOM   5693 H  HA   . ALA   B 1 112 ? 35.709 -19.528 2.812   1.00 14.20 ?  112 ALA   B HA   1 
ATOM   5694 H  HB1  . ALA   B 1 112 ? 37.139 -21.360 2.570   1.00 14.86 ?  112 ALA   B HB1  1 
ATOM   5695 H  HB2  . ALA   B 1 112 ? 36.289 -21.493 3.906   1.00 14.86 ?  112 ALA   B HB2  1 
ATOM   5696 H  HB3  . ALA   B 1 112 ? 35.888 -22.339 2.623   1.00 14.86 ?  112 ALA   B HB3  1 
ATOM   5697 N  N    . TYR   B 1 113 ? 34.571 -21.155 0.293   1.00 11.57 ?  113 TYR   B N    1 
ATOM   5698 C  CA   . TYR   B 1 113 ? 34.493 -21.110 -1.162  1.00 11.10 ?  113 TYR   B CA   1 
ATOM   5699 C  C    . TYR   B 1 113 ? 33.783 -19.859 -1.680  1.00 10.71 ?  113 TYR   B C    1 
ATOM   5700 O  O    . TYR   B 1 113 ? 34.056 -19.429 -2.806  1.00 10.93 ?  113 TYR   B O    1 
ATOM   5701 C  CB   . TYR   B 1 113 ? 33.821 -22.367 -1.709  1.00 11.45 ?  113 TYR   B CB   1 
ATOM   5702 C  CG   . TYR   B 1 113 ? 34.778 -23.518 -1.973  1.00 11.67 ?  113 TYR   B CG   1 
ATOM   5703 C  CD1  . TYR   B 1 113 ? 35.774 -23.415 -2.938  1.00 12.42 ?  113 TYR   B CD1  1 
ATOM   5704 C  CD2  . TYR   B 1 113 ? 34.687 -24.706 -1.262  1.00 12.16 ?  113 TYR   B CD2  1 
ATOM   5705 C  CE1  . TYR   B 1 113 ? 36.653 -24.450 -3.188  1.00 12.32 ?  113 TYR   B CE1  1 
ATOM   5706 C  CE2  . TYR   B 1 113 ? 35.564 -25.762 -1.511  1.00 12.33 ?  113 TYR   B CE2  1 
ATOM   5707 C  CZ   . TYR   B 1 113 ? 36.539 -25.627 -2.477  1.00 12.33 ?  113 TYR   B CZ   1 
ATOM   5708 O  OH   . TYR   B 1 113 ? 37.419 -26.641 -2.755  1.00 13.20 ?  113 TYR   B OH   1 
ATOM   5709 H  H    . TYR   B 1 113 ? 34.109 -21.782 0.668   1.00 13.90 ?  113 TYR   B H    1 
ATOM   5710 H  HA   . TYR   B 1 113 ? 35.393 -21.090 -1.501  1.00 13.33 ?  113 TYR   B HA   1 
ATOM   5711 H  HB2  . TYR   B 1 113 ? 33.160 -22.682 -1.066  1.00 13.76 ?  113 TYR   B HB2  1 
ATOM   5712 H  HB3  . TYR   B 1 113 ? 33.382 -22.150 -2.544  1.00 13.76 ?  113 TYR   B HB3  1 
ATOM   5713 H  HD1  . TYR   B 1 113 ? 35.855 -22.623 -3.427  1.00 14.91 ?  113 TYR   B HD1  1 
ATOM   5714 H  HD2  . TYR   B 1 113 ? 34.024 -24.799 -0.619  1.00 14.60 ?  113 TYR   B HD2  1 
ATOM   5715 H  HE1  . TYR   B 1 113 ? 37.309 -24.361 -3.846  1.00 14.80 ?  113 TYR   B HE1  1 
ATOM   5716 H  HE2  . TYR   B 1 113 ? 35.481 -26.554 -1.033  1.00 14.81 ?  113 TYR   B HE2  1 
ATOM   5717 H  HH   . TYR   B 1 113 ? 37.248 -27.308 -2.276  1.00 15.85 ?  113 TYR   B HH   1 
ATOM   5718 N  N    . GLU   B 1 114 ? 32.859 -19.282 -0.901  1.00 11.07 ?  114 GLU   B N    1 
ATOM   5719 C  CA   . GLU   B 1 114 ? 32.174 -18.073 -1.360  1.00 10.70 ?  114 GLU   B CA   1 
ATOM   5720 C  C    . GLU   B 1 114 ? 33.159 -16.952 -1.659  1.00 10.74 ?  114 GLU   B C    1 
ATOM   5721 O  O    . GLU   B 1 114 ? 32.883 -16.092 -2.500  1.00 11.36 ?  114 GLU   B O    1 
ATOM   5722 C  CB   . GLU   B 1 114 ? 31.119 -17.642 -0.341  1.00 11.44 ?  114 GLU   B CB   1 
ATOM   5723 C  CG   . GLU   B 1 114 ? 29.905 -18.569 -0.399  1.00 11.74 ?  114 GLU   B CG   1 
ATOM   5724 C  CD   . GLU   B 1 114 ? 28.883 -18.376 0.703   1.00 12.20 ?  114 GLU   B CD   1 
ATOM   5725 O  OE1  . GLU   B 1 114 ? 29.174 -17.761 1.747   1.00 12.26 ?  114 GLU   B OE1  1 
ATOM   5726 O  OE2  . GLU   B 1 114 ? 27.757 -18.916 0.532   1.00 12.94 -1 114 GLU   B OE2  1 
ATOM   5727 H  H    . GLU   B 1 114 ? 32.608 -19.572 -0.124  1.00 13.29 ?  114 GLU   B H    1 
ATOM   5728 H  HA   . GLU   B 1 114 ? 31.714 -18.278 -2.180  1.00 12.85 ?  114 GLU   B HA   1 
ATOM   5729 H  HB2  . GLU   B 1 114 ? 31.496 -17.687 0.556   1.00 13.74 ?  114 GLU   B HB2  1 
ATOM   5730 H  HB3  . GLU   B 1 114 ? 30.828 -16.743 -0.540  1.00 13.74 ?  114 GLU   B HB3  1 
ATOM   5731 H  HG2  . GLU   B 1 114 ? 29.458 -18.428 -1.243  1.00 14.10 ?  114 GLU   B HG2  1 
ATOM   5732 H  HG3  . GLU   B 1 114 ? 30.220 -19.486 -0.345  1.00 14.10 ?  114 GLU   B HG3  1 
ATOM   5733 N  N    . ASN   B 1 115 ? 34.325 -16.947 -1.006  1.00 10.58 ?  115 ASN   B N    1 
ATOM   5734 C  CA   . ASN   B 1 115 ? 35.324 -15.918 -1.303  1.00 10.69 ?  115 ASN   B CA   1 
ATOM   5735 C  C    . ASN   B 1 115 ? 35.728 -15.932 -2.771  1.00 10.60 ?  115 ASN   B C    1 
ATOM   5736 O  O    . ASN   B 1 115 ? 36.110 -14.891 -3.327  1.00 11.03 ?  115 ASN   B O    1 
ATOM   5737 C  CB   . ASN   B 1 115 ? 36.562 -16.098 -0.417  1.00 11.34 ?  115 ASN   B CB   1 
ATOM   5738 C  CG   . ASN   B 1 115 ? 36.294 -15.826 1.044   1.00 11.60 ?  115 ASN   B CG   1 
ATOM   5739 O  OD1  . ASN   B 1 115 ? 36.295 -14.676 1.479   1.00 13.35 ?  115 ASN   B OD1  1 
ATOM   5740 N  ND2  . ASN   B 1 115 ? 36.121 -16.891 1.828   1.00 11.70 ?  115 ASN   B ND2  1 
ATOM   5741 H  H    . ASN   B 1 115 ? 34.562 -17.510 -0.391  1.00 12.71 ?  115 ASN   B H    1 
ATOM   5742 H  HA   . ASN   B 1 115 ? 34.948 -15.048 -1.107  1.00 12.84 ?  115 ASN   B HA   1 
ATOM   5743 H  HB2  . ASN   B 1 115 ? 36.879 -17.012 -0.500  1.00 13.62 ?  115 ASN   B HB2  1 
ATOM   5744 H  HB3  . ASN   B 1 115 ? 37.252 -15.483 -0.712  1.00 13.62 ?  115 ASN   B HB3  1 
ATOM   5745 H  HD21 . ASN   B 1 115 ? 35.979 -16.784 2.674   1.00 14.06 ?  115 ASN   B HD21 1 
ATOM   5746 H  HD22 . ASN   B 1 115 ? 36.143 -17.682 1.498   1.00 14.06 ?  115 ASN   B HD22 1 
ATOM   5747 N  N    . PHE   B 1 116 ? 35.700 -17.110 -3.407  1.00 10.52 ?  116 PHE   B N    1 
ATOM   5748 C  CA   . PHE   B 1 116 ? 36.128 -17.204 -4.795  1.00 10.48 ?  116 PHE   B CA   1 
ATOM   5749 C  C    . PHE   B 1 116 ? 35.223 -16.383 -5.707  1.00 10.34 ?  116 PHE   B C    1 
ATOM   5750 O  O    . PHE   B 1 116 ? 35.656 -15.957 -6.782  1.00 10.98 ?  116 PHE   B O    1 
ATOM   5751 C  CB   . PHE   B 1 116 ? 36.097 -18.651 -5.314  1.00 10.40 ?  116 PHE   B CB   1 
ATOM   5752 C  CG   . PHE   B 1 116 ? 37.165 -19.601 -4.767  1.00 10.43 ?  116 PHE   B CG   1 
ATOM   5753 C  CD1  . PHE   B 1 116 ? 37.821 -19.417 -3.559  1.00 11.30 ?  116 PHE   B CD1  1 
ATOM   5754 C  CD2  . PHE   B 1 116 ? 37.462 -20.739 -5.506  1.00 10.72 ?  116 PHE   B CD2  1 
ATOM   5755 C  CE1  . PHE   B 1 116 ? 38.757 -20.356 -3.111  1.00 11.54 ?  116 PHE   B CE1  1 
ATOM   5756 C  CE2  . PHE   B 1 116 ? 38.394 -21.674 -5.067  1.00 11.20 ?  116 PHE   B CE2  1 
ATOM   5757 C  CZ   . PHE   B 1 116 ? 39.036 -21.488 -3.873  1.00 11.32 ?  116 PHE   B CZ   1 
ATOM   5758 H  H    . PHE   B 1 116 ? 35.441 -17.858 -3.058  1.00 12.64 ?  116 PHE   B H    1 
ATOM   5759 H  HA   . PHE   B 1 116 ? 37.035 -16.872 -4.880  1.00 12.59 ?  116 PHE   B HA   1 
ATOM   5760 H  HB2  . PHE   B 1 116 ? 35.227 -19.032 -5.094  1.00 12.49 ?  116 PHE   B HB2  1 
ATOM   5761 H  HB3  . PHE   B 1 116 ? 36.195 -18.630 -6.279  1.00 12.49 ?  116 PHE   B HB3  1 
ATOM   5762 H  HD1  . PHE   B 1 116 ? 37.627 -18.670 -3.040  1.00 13.58 ?  116 PHE   B HD1  1 
ATOM   5763 H  HD2  . PHE   B 1 116 ? 37.021 -20.880 -6.313  1.00 12.88 ?  116 PHE   B HD2  1 
ATOM   5764 H  HE1  . PHE   B 1 116 ? 39.196 -20.220 -2.305  1.00 13.86 ?  116 PHE   B HE1  1 
ATOM   5765 H  HE2  . PHE   B 1 116 ? 38.582 -22.421 -5.584  1.00 13.45 ?  116 PHE   B HE2  1 
ATOM   5766 H  HZ   . PHE   B 1 116 ? 39.671 -22.099 -3.583  1.00 13.60 ?  116 PHE   B HZ   1 
ATOM   5767 N  N    . ASN   B 1 117 ? 33.955 -16.181 -5.322  1.00 10.84 ?  117 ASN   B N    1 
ATOM   5768 C  CA   . ASN   B 1 117 ? 33.011 -15.474 -6.186  1.00 11.02 ?  117 ASN   B CA   1 
ATOM   5769 C  C    . ASN   B 1 117 ? 33.325 -13.995 -6.333  1.00 11.34 ?  117 ASN   B C    1 
ATOM   5770 O  O    . ASN   B 1 117 ? 32.725 -13.335 -7.186  1.00 12.53 ?  117 ASN   B O    1 
ATOM   5771 C  CB   . ASN   B 1 117 ? 31.584 -15.697 -5.697  1.00 11.41 ?  117 ASN   B CB   1 
ATOM   5772 C  CG   . ASN   B 1 117 ? 31.133 -17.108 -5.945  1.00 11.75 ?  117 ASN   B CG   1 
ATOM   5773 O  OD1  . ASN   B 1 117 ? 31.490 -17.696 -6.965  1.00 12.65 ?  117 ASN   B OD1  1 
ATOM   5774 N  ND2  . ASN   B 1 117 ? 30.398 -17.680 -5.002  1.00 11.62 ?  117 ASN   B ND2  1 
ATOM   5775 H  H    . ASN   B 1 117 ? 33.631 -16.444 -4.565  1.00 13.02 ?  117 ASN   B H    1 
ATOM   5776 H  HA   . ASN   B 1 117 ? 33.075 -15.864 -7.065  1.00 13.24 ?  117 ASN   B HA   1 
ATOM   5777 H  HB2  . ASN   B 1 117 ? 31.538 -15.528 -4.739  1.00 13.70 ?  117 ASN   B HB2  1 
ATOM   5778 H  HB3  . ASN   B 1 117 ? 30.989 -15.088 -6.167  1.00 13.70 ?  117 ASN   B HB3  1 
ATOM   5779 H  HD21 . ASN   B 1 117 ? 30.112 -18.482 -5.105  1.00 13.95 ?  117 ASN   B HD21 1 
ATOM   5780 H  HD22 . ASN   B 1 117 ? 30.174 -17.231 -4.298  1.00 13.95 ?  117 ASN   B HD22 1 
ATOM   5781 N  N    . GLN   B 1 118 ? 34.262 -13.469 -5.554  1.00 11.20 ?  118 GLN   B N    1 
ATOM   5782 C  CA   . GLN   B 1 118 ? 34.691 -12.084 -5.688  1.00 11.57 ?  118 GLN   B CA   1 
ATOM   5783 C  C    . GLN   B 1 118 ? 35.759 -11.889 -6.762  1.00 11.82 ?  118 GLN   B C    1 
ATOM   5784 O  O    . GLN   B 1 118 ? 36.231 -10.761 -6.943  1.00 13.13 ?  118 GLN   B O    1 
ATOM   5785 C  CB   . GLN   B 1 118 ? 35.163 -11.546 -4.331  1.00 11.98 ?  118 GLN   B CB   1 
ATOM   5786 C  CG   . GLN   B 1 118 ? 34.079 -11.587 -3.262  1.00 12.35 ?  118 GLN   B CG   1 
ATOM   5787 C  CD   . GLN   B 1 118 ? 32.909 -10.682 -3.598  1.00 11.97 ?  118 GLN   B CD   1 
ATOM   5788 O  OE1  . GLN   B 1 118 ? 33.097 -9.545  -4.047  1.00 12.94 ?  118 GLN   B OE1  1 
ATOM   5789 N  NE2  . GLN   B 1 118 ? 31.691 -11.177 -3.394  1.00 12.58 ?  118 GLN   B NE2  1 
ATOM   5790 H  H    . GLN   B 1 118 ? 34.688 -13.901 -4.937  1.00 13.45 ?  118 GLN   B H    1 
ATOM   5791 H  HA   . GLN   B 1 118 ? 33.924 -11.560 -5.957  1.00 13.90 ?  118 GLN   B HA   1 
ATOM   5792 H  HB2  . GLN   B 1 118 ? 35.910 -12.072 -4.021  1.00 14.40 ?  118 GLN   B HB2  1 
ATOM   5793 H  HB3  . GLN   B 1 118 ? 35.433 -10.617 -4.440  1.00 14.40 ?  118 GLN   B HB3  1 
ATOM   5794 H  HG2  . GLN   B 1 118 ? 33.747 -12.495 -3.180  1.00 14.84 ?  118 GLN   B HG2  1 
ATOM   5795 H  HG3  . GLN   B 1 118 ? 34.457 -11.294 -2.416  1.00 14.84 ?  118 GLN   B HG3  1 
ATOM   5796 H  HE21 . GLN   B 1 118 ? 31.601 -11.975 -3.080  1.00 15.11 ?  118 GLN   B HE21 1 
ATOM   5797 H  HE22 . GLN   B 1 118 ? 31.003 -10.702 -3.572  1.00 15.11 ?  118 GLN   B HE22 1 
ATOM   5798 N  N    . HIS   B 1 119 ? 36.106 -12.945 -7.502  1.00 11.46 ?  119 HIS   B N    1 
ATOM   5799 C  CA   . HIS   B 1 119 ? 37.151 -12.903 -8.517  1.00 11.68 ?  119 HIS   B CA   1 
ATOM   5800 C  C    . HIS   B 1 119 ? 36.668 -13.631 -9.757  1.00 11.70 ?  119 HIS   B C    1 
ATOM   5801 O  O    . HIS   B 1 119 ? 36.160 -14.747 -9.660  1.00 12.47 ?  119 HIS   B O    1 
ATOM   5802 C  CB   . HIS   B 1 119 ? 38.431 -13.535 -7.972  1.00 12.16 ?  119 HIS   B CB   1 
ATOM   5803 C  CG   . HIS   B 1 119 ? 38.913 -12.839 -6.746  1.00 13.38 ?  119 HIS   B CG   1 
ATOM   5804 N  ND1  . HIS   B 1 119 ? 39.712 -11.716 -6.799  1.00 14.82 ?  119 HIS   B ND1  1 
ATOM   5805 C  CD2  . HIS   B 1 119 ? 38.622 -13.036 -5.439  1.00 14.26 ?  119 HIS   B CD2  1 
ATOM   5806 C  CE1  . HIS   B 1 119 ? 39.921 -11.275 -5.571  1.00 16.10 ?  119 HIS   B CE1  1 
ATOM   5807 N  NE2  . HIS   B 1 119 ? 39.266 -12.053 -4.728  1.00 16.00 ?  119 HIS   B NE2  1 
ATOM   5808 H  H    . HIS   B 1 119 ? 35.729 -13.719 -7.440  1.00 13.76 ?  119 HIS   B H    1 
ATOM   5809 H  HA   . HIS   B 1 119 ? 37.336 -11.979 -8.756  1.00 14.03 ?  119 HIS   B HA   1 
ATOM   5810 H  HB2  . HIS   B 1 119 ? 38.260 -14.460 -7.752  1.00 14.60 ?  119 HIS   B HB2  1 
ATOM   5811 H  HB3  . HIS   B 1 119 ? 39.127 -13.473 -8.649  1.00 14.60 ?  119 HIS   B HB3  1 
ATOM   5812 H  HD2  . HIS   B 1 119 ? 38.089 -13.714 -5.091  1.00 17.12 ?  119 HIS   B HD2  1 
ATOM   5813 H  HE1  . HIS   B 1 119 ? 40.456 -10.551 -5.332  1.00 19.33 ?  119 HIS   B HE1  1 
ATOM   5814 H  HE2  . HIS   B 1 119 ? 39.271 -11.981 -3.869  1.00 19.22 ?  119 HIS   B HE2  1 
ATOM   5815 N  N    . GLU   B 1 120 ? 36.820 -13.008 -10.926 1.00 12.23 ?  120 GLU   B N    1 
ATOM   5816 C  CA   . GLU   B 1 120 ? 36.229 -13.588 -12.129 1.00 13.32 ?  120 GLU   B CA   1 
ATOM   5817 C  C    . GLU   B 1 120 ? 36.901 -14.890 -12.546 1.00 12.21 ?  120 GLU   B C    1 
ATOM   5818 O  O    . GLU   B 1 120 ? 36.234 -15.764 -13.111 1.00 12.80 ?  120 GLU   B O    1 
ATOM   5819 C  CB   . GLU   B 1 120 ? 36.244 -12.575 -13.272 1.00 17.88 ?  120 GLU   B CB   1 
ATOM   5820 C  CG   . GLU   B 1 120 ? 35.278 -11.420 -13.055 1.00 24.24 ?  120 GLU   B CG   1 
ATOM   5821 C  CD   . GLU   B 1 120 ? 35.121 -10.536 -14.275 1.00 30.60 ?  120 GLU   B CD   1 
ATOM   5822 O  OE1  . GLU   B 1 120 ? 36.111 -10.358 -15.016 1.00 32.87 ?  120 GLU   B OE1  1 
ATOM   5823 O  OE2  . GLU   B 1 120 ? 34.005 -10.017 -14.488 1.00 33.96 -1 120 GLU   B OE2  1 
ATOM   5824 H  H    . GLU   B 1 120 ? 37.238 -12.265 -11.049 1.00 14.69 ?  120 GLU   B H    1 
ATOM   5825 H  HA   . GLU   B 1 120 ? 35.303 -13.794 -11.944 1.00 16.00 ?  120 GLU   B HA   1 
ATOM   5826 H  HB2  . GLU   B 1 120 ? 37.134 -12.203 -13.359 1.00 21.47 ?  120 GLU   B HB2  1 
ATOM   5827 H  HB3  . GLU   B 1 120 ? 35.989 -13.022 -14.096 1.00 21.47 ?  120 GLU   B HB3  1 
ATOM   5828 H  HG2  . GLU   B 1 120 ? 34.404 -11.778 -12.827 1.00 29.10 ?  120 GLU   B HG2  1 
ATOM   5829 H  HG3  . GLU   B 1 120 ? 35.607 -10.864 -12.333 1.00 29.10 ?  120 GLU   B HG3  1 
ATOM   5830 N  N    . VAL   B 1 121 ? 38.200 -15.036 -12.284 1.00 11.96 ?  121 VAL   B N    1 
ATOM   5831 C  CA   . VAL   B 1 121 ? 38.950 -16.241 -12.632 1.00 11.90 ?  121 VAL   B CA   1 
ATOM   5832 C  C    . VAL   B 1 121 ? 40.065 -16.449 -11.611 1.00 11.48 ?  121 VAL   B C    1 
ATOM   5833 O  O    . VAL   B 1 121 ? 40.749 -15.497 -11.217 1.00 12.21 ?  121 VAL   B O    1 
ATOM   5834 C  CB   . VAL   B 1 121 ? 39.465 -16.196 -14.091 1.00 13.61 ?  121 VAL   B CB   1 
ATOM   5835 C  CG1  . VAL   B 1 121 ? 40.338 -14.971 -14.346 1.00 14.69 ?  121 VAL   B CG1  1 
ATOM   5836 C  CG2  . VAL   B 1 121 ? 40.193 -17.478 -14.446 1.00 14.89 ?  121 VAL   B CG2  1 
ATOM   5837 H  H    . VAL   B 1 121 ? 38.682 -14.434 -11.899 1.00 14.36 ?  121 VAL   B H    1 
ATOM   5838 H  HA   . VAL   B 1 121 ? 38.346 -16.996 -12.566 1.00 14.30 ?  121 VAL   B HA   1 
ATOM   5839 H  HB   . VAL   B 1 121 ? 38.695 -16.128 -14.682 1.00 16.35 ?  121 VAL   B HB   1 
ATOM   5840 H  HG11 . VAL   B 1 121 ? 40.638 -14.981 -15.268 1.00 17.64 ?  121 VAL   B HG11 1 
ATOM   5841 H  HG12 . VAL   B 1 121 ? 39.816 -14.167 -14.179 1.00 17.64 ?  121 VAL   B HG12 1 
ATOM   5842 H  HG13 . VAL   B 1 121 ? 41.102 -14.996 -13.749 1.00 17.64 ?  121 VAL   B HG13 1 
ATOM   5843 H  HG21 . VAL   B 1 121 ? 40.391 -17.474 -15.397 1.00 17.88 ?  121 VAL   B HG21 1 
ATOM   5844 H  HG22 . VAL   B 1 121 ? 41.019 -17.523 -13.939 1.00 17.88 ?  121 VAL   B HG22 1 
ATOM   5845 H  HG23 . VAL   B 1 121 ? 39.628 -18.234 -14.230 1.00 17.88 ?  121 VAL   B HG23 1 
ATOM   5846 N  N    . LEU   B 1 122 ? 40.244 -17.700 -11.177 1.00 10.98 ?  122 LEU   B N    1 
ATOM   5847 C  CA   . LEU   B 1 122 ? 41.229 -18.052 -10.156 1.00 10.62 ?  122 LEU   B CA   1 
ATOM   5848 C  C    . LEU   B 1 122 ? 41.884 -19.383 -10.485 1.00 10.52 ?  122 LEU   B C    1 
ATOM   5849 O  O    . LEU   B 1 122 ? 41.223 -20.302 -10.984 1.00 11.82 ?  122 LEU   B O    1 
ATOM   5850 C  CB   . LEU   B 1 122 ? 40.581 -18.279 -8.778  1.00 12.61 ?  122 LEU   B CB   1 
ATOM   5851 C  CG   . LEU   B 1 122 ? 39.548 -17.264 -8.287  1.00 12.56 ?  122 LEU   B CG   1 
ATOM   5852 C  CD1  . LEU   B 1 122 ? 38.153 -17.641 -8.752  1.00 13.25 ?  122 LEU   B CD1  1 
ATOM   5853 C  CD2  . LEU   B 1 122 ? 39.596 -17.157 -6.776  1.00 11.90 ?  122 LEU   B CD2  1 
ATOM   5854 H  H    . LEU   B 1 122 ? 39.802 -18.379 -11.468 1.00 13.19 ?  122 LEU   B H    1 
ATOM   5855 H  HA   . LEU   B 1 122 ? 41.908 -17.362 -10.082 1.00 12.76 ?  122 LEU   B HA   1 
ATOM   5856 H  HB2  . LEU   B 1 122 ? 40.139 -19.139 -8.796  1.00 15.14 ?  122 LEU   B HB2  1 
ATOM   5857 H  HB3  . LEU   B 1 122 ? 41.288 -18.297 -8.116  1.00 15.14 ?  122 LEU   B HB3  1 
ATOM   5858 H  HG   . LEU   B 1 122 ? 39.760 -16.392 -8.656  1.00 15.09 ?  122 LEU   B HG   1 
ATOM   5859 H  HD11 . LEU   B 1 122 ? 37.519 -16.997 -8.404  1.00 15.91 ?  122 LEU   B HD11 1 
ATOM   5860 H  HD12 . LEU   B 1 122 ? 38.130 -17.636 -9.723  1.00 15.91 ?  122 LEU   B HD12 1 
ATOM   5861 H  HD13 . LEU   B 1 122 ? 37.939 -18.528 -8.423  1.00 15.91 ?  122 LEU   B HD13 1 
ATOM   5862 H  HD21 . LEU   B 1 122 ? 38.913 -16.537 -6.478  1.00 14.29 ?  122 LEU   B HD21 1 
ATOM   5863 H  HD22 . LEU   B 1 122 ? 39.439 -18.034 -6.390  1.00 14.29 ?  122 LEU   B HD22 1 
ATOM   5864 H  HD23 . LEU   B 1 122 ? 40.473 -16.833 -6.509  1.00 14.29 ?  122 LEU   B HD23 1 
ATOM   5865 N  N    . LEU   B 1 123 ? 43.171 -19.494 -10.128 1.00 10.42 ?  123 LEU   B N    1 
ATOM   5866 C  CA   . LEU   B 1 123 ? 43.884 -20.764 -10.008 1.00 10.68 ?  123 LEU   B CA   1 
ATOM   5867 C  C    . LEU   B 1 123 ? 43.859 -21.156 -8.536  1.00 10.28 ?  123 LEU   B C    1 
ATOM   5868 O  O    . LEU   B 1 123 ? 44.210 -20.330 -7.684  1.00 10.86 ?  123 LEU   B O    1 
ATOM   5869 C  CB   . LEU   B 1 123 ? 45.331 -20.584 -10.476 1.00 11.02 ?  123 LEU   B CB   1 
ATOM   5870 C  CG   . LEU   B 1 123 ? 46.282 -21.763 -10.231 1.00 11.55 ?  123 LEU   B CG   1 
ATOM   5871 C  CD1  . LEU   B 1 123 ? 45.855 -23.007 -11.006 1.00 11.85 ?  123 LEU   B CD1  1 
ATOM   5872 C  CD2  . LEU   B 1 123 ? 47.704 -21.373 -10.598 1.00 12.49 ?  123 LEU   B CD2  1 
ATOM   5873 H  H    . LEU   B 1 123 ? 43.664 -18.815 -9.926  1.00 12.51 ?  123 LEU   B H    1 
ATOM   5874 H  HA   . LEU   B 1 123 ? 43.443 -21.450 -10.533 1.00 12.83 ?  123 LEU   B HA   1 
ATOM   5875 H  HB2  . LEU   B 1 123 ? 45.316 -20.424 -11.433 1.00 13.24 ?  123 LEU   B HB2  1 
ATOM   5876 H  HB3  . LEU   B 1 123 ? 45.704 -19.818 -10.023 1.00 13.24 ?  123 LEU   B HB3  1 
ATOM   5877 H  HG   . LEU   B 1 123 ? 46.273 -21.992 -9.288  1.00 13.87 ?  123 LEU   B HG   1 
ATOM   5878 H  HD11 . LEU   B 1 123 ? 46.489 -23.719 -10.835 1.00 14.23 ?  123 LEU   B HD11 1 
ATOM   5879 H  HD12 . LEU   B 1 123 ? 44.969 -23.275 -10.709 1.00 14.23 ?  123 LEU   B HD12 1 
ATOM   5880 H  HD13 . LEU   B 1 123 ? 45.836 -22.797 -11.952 1.00 14.23 ?  123 LEU   B HD13 1 
ATOM   5881 H  HD21 . LEU   B 1 123 ? 48.292 -22.129 -10.439 1.00 15.00 ?  123 LEU   B HD21 1 
ATOM   5882 H  HD22 . LEU   B 1 123 ? 47.731 -21.126 -11.536 1.00 15.00 ?  123 LEU   B HD22 1 
ATOM   5883 H  HD23 . LEU   B 1 123 ? 47.974 -20.622 -10.049 1.00 15.00 ?  123 LEU   B HD23 1 
ATOM   5884 N  N    . ALA   B 1 124 ? 43.424 -22.383 -8.226  1.00 10.24 ?  124 ALA   B N    1 
ATOM   5885 C  CA   . ALA   B 1 124 ? 43.173 -22.706 -6.828  1.00 10.46 ?  124 ALA   B CA   1 
ATOM   5886 C  C    . ALA   B 1 124 ? 43.454 -24.166 -6.507  1.00 10.27 ?  124 ALA   B C    1 
ATOM   5887 O  O    . ALA   B 1 124 ? 43.313 -25.044 -7.371  1.00 10.99 ?  124 ALA   B O    1 
ATOM   5888 C  CB   . ALA   B 1 124 ? 41.722 -22.396 -6.451  1.00 11.15 ?  124 ALA   B CB   1 
ATOM   5889 H  H    . ALA   B 1 124 ? 43.247 -23.016 -8.789  1.00 12.30 ?  124 ALA   B H    1 
ATOM   5890 H  HA   . ALA   B 1 124 ? 43.752 -22.157 -6.284  1.00 12.57 ?  124 ALA   B HA   1 
ATOM   5891 H  HB1  . ALA   B 1 124 ? 41.579 -22.614 -5.518  1.00 13.40 ?  124 ALA   B HB1  1 
ATOM   5892 H  HB2  . ALA   B 1 124 ? 41.559 -21.444 -6.593  1.00 13.40 ?  124 ALA   B HB2  1 
ATOM   5893 H  HB3  . ALA   B 1 124 ? 41.126 -22.914 -7.011  1.00 13.40 ?  124 ALA   B HB3  1 
ATOM   5894 N  N    . PRO   B 1 125 ? 43.749 -24.462 -5.242  1.00 10.51 ?  125 PRO   B N    1 
ATOM   5895 C  CA   . PRO   B 1 125 ? 43.684 -25.829 -4.724  1.00 11.05 ?  125 PRO   B CA   1 
ATOM   5896 C  C    . PRO   B 1 125 ? 42.283 -26.105 -4.177  1.00 11.16 ?  125 PRO   B C    1 
ATOM   5897 O  O    . PRO   B 1 125 ? 41.483 -25.188 -3.975  1.00 11.73 ?  125 PRO   B O    1 
ATOM   5898 C  CB   . PRO   B 1 125 ? 44.673 -25.761 -3.558  1.00 12.05 ?  125 PRO   B CB   1 
ATOM   5899 C  CG   . PRO   B 1 125 ? 44.420 -24.375 -2.979  1.00 12.11 ?  125 PRO   B CG   1 
ATOM   5900 C  CD   . PRO   B 1 125 ? 44.076 -23.498 -4.175  1.00 11.31 ?  125 PRO   B CD   1 
ATOM   5901 H  HA   . PRO   B 1 125 ? 43.954 -26.496 -5.375  1.00 13.28 ?  125 PRO   B HA   1 
ATOM   5902 H  HB2  . PRO   B 1 125 ? 44.472 -26.452 -2.904  1.00 14.48 ?  125 PRO   B HB2  1 
ATOM   5903 H  HB3  . PRO   B 1 125 ? 45.581 -25.843 -3.884  1.00 14.48 ?  125 PRO   B HB3  1 
ATOM   5904 H  HG2  . PRO   B 1 125 ? 43.675 -24.404 -2.356  1.00 14.55 ?  125 PRO   B HG2  1 
ATOM   5905 H  HG3  . PRO   B 1 125 ? 45.222 -24.050 -2.533  1.00 14.55 ?  125 PRO   B HG3  1 
ATOM   5906 H  HD2  . PRO   B 1 125 ? 43.317 -22.932 -3.978  1.00 13.58 ?  125 PRO   B HD2  1 
ATOM   5907 H  HD3  . PRO   B 1 125 ? 44.854 -22.968 -4.435  1.00 13.58 ?  125 PRO   B HD3  1 
ATOM   5908 N  N    . LEU   B 1 126 ? 42.015 -27.381 -3.894  1.00 11.69 ?  126 LEU   B N    1 
ATOM   5909 C  CA   . LEU   B 1 126 ? 40.792 -27.751 -3.187  1.00 12.40 ?  126 LEU   B CA   1 
ATOM   5910 C  C    . LEU   B 1 126 ? 40.911 -27.353 -1.723  1.00 12.65 ?  126 LEU   B C    1 
ATOM   5911 O  O    . LEU   B 1 126 ? 41.811 -27.806 -1.009  1.00 14.10 ?  126 LEU   B O    1 
ATOM   5912 C  CB   . LEU   B 1 126 ? 40.549 -29.248 -3.305  1.00 13.96 ?  126 LEU   B CB   1 
ATOM   5913 C  CG   . LEU   B 1 126 ? 40.015 -29.727 -4.657  1.00 14.63 ?  126 LEU   B CG   1 
ATOM   5914 C  CD1  . LEU   B 1 126 ? 40.074 -31.235 -4.747  1.00 16.38 ?  126 LEU   B CD1  1 
ATOM   5915 C  CD2  . LEU   B 1 126 ? 38.595 -29.238 -4.898  1.00 14.84 ?  126 LEU   B CD2  1 
ATOM   5916 H  H    . LEU   B 1 126 ? 42.525 -28.045 -4.089  1.00 14.04 ?  126 LEU   B H    1 
ATOM   5917 H  HA   . LEU   B 1 126 ? 40.040 -27.276 -3.576  1.00 14.90 ?  126 LEU   B HA   1 
ATOM   5918 H  HB2  . LEU   B 1 126 ? 41.387 -29.705 -3.143  1.00 16.76 ?  126 LEU   B HB2  1 
ATOM   5919 H  HB3  . LEU   B 1 126 ? 39.902 -29.505 -2.630  1.00 16.76 ?  126 LEU   B HB3  1 
ATOM   5920 H  HG   . LEU   B 1 126 ? 40.580 -29.363 -5.360  1.00 17.56 ?  126 LEU   B HG   1 
ATOM   5921 H  HD11 . LEU   B 1 126 ? 39.732 -31.514 -5.611  1.00 19.68 ?  126 LEU   B HD11 1 
ATOM   5922 H  HD12 . LEU   B 1 126 ? 40.992 -31.526 -4.644  1.00 19.68 ?  126 LEU   B HD12 1 
ATOM   5923 H  HD13 . LEU   B 1 126 ? 39.525 -31.615 -4.039  1.00 19.68 ?  126 LEU   B HD13 1 
ATOM   5924 H  HD21 . LEU   B 1 126 ? 38.254 -29.652 -5.705  1.00 17.82 ?  126 LEU   B HD21 1 
ATOM   5925 H  HD22 . LEU   B 1 126 ? 38.045 -29.483 -4.139  1.00 17.82 ?  126 LEU   B HD22 1 
ATOM   5926 H  HD23 . LEU   B 1 126 ? 38.604 -28.272 -5.001  1.00 17.82 ?  126 LEU   B HD23 1 
ATOM   5927 N  N    . LEU   B 1 127 ? 39.987 -26.518 -1.267  1.00 12.30 ?  127 LEU   B N    1 
ATOM   5928 C  CA   . LEU   B 1 127 ? 40.045 -26.027 0.097   1.00 12.80 ?  127 LEU   B CA   1 
ATOM   5929 C  C    . LEU   B 1 127 ? 39.774 -27.148 1.092   1.00 12.59 ?  127 LEU   B C    1 
ATOM   5930 O  O    . LEU   B 1 127 ? 38.951 -28.041 0.868   1.00 12.80 ?  127 LEU   B O    1 
ATOM   5931 C  CB   . LEU   B 1 127 ? 39.024 -24.906 0.306   1.00 13.12 ?  127 LEU   B CB   1 
ATOM   5932 C  CG   . LEU   B 1 127 ? 39.196 -23.638 -0.530  1.00 13.83 ?  127 LEU   B CG   1 
ATOM   5933 C  CD1  . LEU   B 1 127 ? 38.075 -22.667 -0.200  1.00 13.99 ?  127 LEU   B CD1  1 
ATOM   5934 C  CD2  . LEU   B 1 127 ? 40.563 -23.000 -0.297  1.00 14.66 ?  127 LEU   B CD2  1 
ATOM   5935 H  H    . LEU   B 1 127 ? 39.317 -26.214 -1.726  1.00 14.78 ?  127 LEU   B H    1 
ATOM   5936 H  HA   . LEU   B 1 127 ? 40.929 -25.663 0.268   1.00 15.37 ?  127 LEU   B HA   1 
ATOM   5937 H  HB2  . LEU   B 1 127 ? 38.140 -25.258 0.108   1.00 15.76 ?  127 LEU   B HB2  1 
ATOM   5938 H  HB3  . LEU   B 1 127 ? 39.054 -24.636 1.238   1.00 15.76 ?  127 LEU   B HB3  1 
ATOM   5939 H  HG   . LEU   B 1 127 ? 39.118 -23.859 -1.468  1.00 16.61 ?  127 LEU   B HG   1 
ATOM   5940 H  HD11 . LEU   B 1 127 ? 38.190 -21.855 -0.727  1.00 16.80 ?  127 LEU   B HD11 1 
ATOM   5941 H  HD12 . LEU   B 1 127 ? 37.222 -23.074 -0.407  1.00 16.80 ?  127 LEU   B HD12 1 
ATOM   5942 H  HD13 . LEU   B 1 127 ? 38.114 -22.444 0.747   1.00 16.80 ?  127 LEU   B HD13 1 
ATOM   5943 H  HD21 . LEU   B 1 127 ? 40.601 -22.144 -0.750  1.00 17.61 ?  127 LEU   B HD21 1 
ATOM   5944 H  HD22 . LEU   B 1 127 ? 40.699 -22.875 0.657   1.00 17.61 ?  127 LEU   B HD22 1 
ATOM   5945 H  HD23 . LEU   B 1 127 ? 41.248 -23.591 -0.651  1.00 17.61 ?  127 LEU   B HD23 1 
ATOM   5946 N  N    . SER   B 1 128 ? 40.457 -27.066 2.222   1.00 12.45 ?  128 SER   B N    1 
ATOM   5947 C  CA   . SER   B 1 128 ? 40.341 -27.981 3.345   1.00 12.90 ?  128 SER   B CA   1 
ATOM   5948 C  C    . SER   B 1 128 ? 40.833 -29.388 3.023   1.00 13.92 ?  128 SER   B C    1 
ATOM   5949 O  O    . SER   B 1 128 ? 40.743 -30.266 3.881   1.00 15.13 ?  128 SER   B O    1 
ATOM   5950 C  CB   . SER   B 1 128 ? 38.937 -27.994 3.967   1.00 13.18 ?  128 SER   B CB   1 
ATOM   5951 O  OG   . SER   B 1 128 ? 38.622 -26.716 4.523   1.00 14.19 ?  128 SER   B OG   1 
ATOM   5952 H  H    . SER   B 1 128 ? 41.034 -26.441 2.366   1.00 14.96 ?  128 SER   B H    1 
ATOM   5953 H  HA   . SER   B 1 128 ? 40.929 -27.646 4.033   1.00 15.49 ?  128 SER   B HA   1 
ATOM   5954 H  HB2  . SER   B 1 128 ? 38.283 -28.225 3.285   1.00 15.83 ?  128 SER   B HB2  1 
ATOM   5955 H  HB3  . SER   B 1 128 ? 38.914 -28.670 4.676   1.00 15.83 ?  128 SER   B HB3  1 
ATOM   5956 H  HG   . SER   B 1 128 ? 39.187 -26.525 5.111   1.00 17.04 ?  128 SER   B HG   1 
ATOM   5957 N  N    . ALA   B 1 129 ? 41.402 -29.613 1.837   1.00 15.10 ?  129 ALA   B N    1 
ATOM   5958 C  CA   . ALA   B 1 129 ? 41.946 -30.913 1.480   1.00 16.18 ?  129 ALA   B CA   1 
ATOM   5959 C  C    . ALA   B 1 129 ? 43.341 -31.089 2.069   1.00 15.48 ?  129 ALA   B C    1 
ATOM   5960 O  O    . ALA   B 1 129 ? 43.908 -30.186 2.702   1.00 15.03 ?  129 ALA   B O    1 
ATOM   5961 C  CB   . ALA   B 1 129 ? 41.986 -31.070 -0.039  1.00 18.31 ?  129 ALA   B CB   1 
ATOM   5962 H  H    . ALA   B 1 129 ? 41.492 -29.023 1.218   1.00 18.13 ?  129 ALA   B H    1 
ATOM   5963 H  HA   . ALA   B 1 129 ? 41.376 -31.609 1.837   1.00 19.43 ?  129 ALA   B HA   1 
ATOM   5964 H  HB1  . ALA   B 1 129 ? 42.343 -31.947 -0.258  1.00 21.98 ?  129 ALA   B HB1  1 
ATOM   5965 H  HB2  . ALA   B 1 129 ? 41.086 -30.983 -0.388  1.00 21.98 ?  129 ALA   B HB2  1 
ATOM   5966 H  HB3  . ALA   B 1 129 ? 42.555 -30.380 -0.414  1.00 21.98 ?  129 ALA   B HB3  1 
ATOM   5967 N  N    . GLY   B 1 130 ? 43.901 -32.279 1.847   1.00 15.32 ?  130 GLY   B N    1 
ATOM   5968 C  CA   . GLY   B 1 130 ? 45.290 -32.514 2.194   1.00 15.81 ?  130 GLY   B CA   1 
ATOM   5969 C  C    . GLY   B 1 130 ? 45.509 -32.425 3.686   1.00 15.63 ?  130 GLY   B C    1 
ATOM   5970 O  O    . GLY   B 1 130 ? 44.814 -33.073 4.485   1.00 16.65 ?  130 GLY   B O    1 
ATOM   5971 H  H    . GLY   B 1 130 ? 43.501 -32.957 1.495   1.00 18.40 ?  130 GLY   B H    1 
ATOM   5972 H  HA2  . GLY   B 1 130 ? 45.557 -33.399 1.892   1.00 18.98 ?  130 GLY   B HA2  1 
ATOM   5973 H  HA3  . GLY   B 1 130 ? 45.852 -31.857 1.755   1.00 18.98 ?  130 GLY   B HA3  1 
ATOM   5974 N  N    . ILE   B 1 131 ? 46.481 -31.591 4.073   1.00 16.14 ?  131 ILE   B N    1 
ATOM   5975 C  CA   . ILE   B 1 131 ? 46.843 -31.459 5.477   1.00 16.80 ?  131 ILE   B CA   1 
ATOM   5976 C  C    . ILE   B 1 131 ? 45.731 -30.855 6.314   1.00 16.22 ?  131 ILE   B C    1 
ATOM   5977 O  O    . ILE   B 1 131 ? 45.809 -30.916 7.544   1.00 17.56 ?  131 ILE   B O    1 
ATOM   5978 C  CB   . ILE   B 1 131 ? 48.165 -30.683 5.679   1.00 18.85 ?  131 ILE   B CB   1 
ATOM   5979 C  CG1  . ILE   B 1 131 ? 47.999 -29.201 5.311   1.00 19.79 ?  131 ILE   B CG1  1 
ATOM   5980 C  CG2  . ILE   B 1 131 ? 49.286 -31.323 4.867   1.00 20.03 ?  131 ILE   B CG2  1 
ATOM   5981 C  CD1  . ILE   B 1 131 ? 49.217 -28.342 5.627   1.00 20.65 ?  131 ILE   B CD1  1 
ATOM   5982 H  H    . ILE   B 1 131 ? 46.943 -31.097 3.541   1.00 19.38 ?  131 ILE   B H    1 
ATOM   5983 H  HA   . ILE   B 1 131 ? 46.985 -32.350 5.824   1.00 20.17 ?  131 ILE   B HA   1 
ATOM   5984 H  HB   . ILE   B 1 131 ? 48.396 -30.735 6.620   1.00 22.63 ?  131 ILE   B HB   1 
ATOM   5985 H  HG12 . ILE   B 1 131 ? 47.822 -29.138 4.359   1.00 23.77 ?  131 ILE   B HG12 1 
ATOM   5986 H  HG13 . ILE   B 1 131 ? 47.245 -28.831 5.805   1.00 23.77 ?  131 ILE   B HG13 1 
ATOM   5987 H  HG21 . ILE   B 1 131 ? 50.125 -30.918 5.125   1.00 24.04 ?  131 ILE   B HG21 1 
ATOM   5988 H  HG22 . ILE   B 1 131 ? 49.300 -32.272 5.050   1.00 24.04 ?  131 ILE   B HG22 1 
ATOM   5989 H  HG23 . ILE   B 1 131 ? 49.114 -31.168 3.925   1.00 24.04 ?  131 ILE   B HG23 1 
ATOM   5990 H  HD11 . ILE   B 1 131 ? 48.999 -27.413 5.455   1.00 24.79 ?  131 ILE   B HD11 1 
ATOM   5991 H  HD12 . ILE   B 1 131 ? 49.451 -28.460 6.561   1.00 24.79 ?  131 ILE   B HD12 1 
ATOM   5992 H  HD13 . ILE   B 1 131 ? 49.952 -28.621 5.062   1.00 24.79 ?  131 ILE   B HD13 1 
ATOM   5993 N  N    . PHE   B 1 132 ? 44.695 -30.280 5.687   1.00 15.21 ?  132 PHE   B N    1 
ATOM   5994 C  CA   . PHE   B 1 132 ? 43.542 -29.774 6.424   1.00 15.41 ?  132 PHE   B CA   1 
ATOM   5995 C  C    . PHE   B 1 132 ? 42.517 -30.861 6.752   1.00 16.59 ?  132 PHE   B C    1 
ATOM   5996 O  O    . PHE   B 1 132 ? 41.613 -30.607 7.554   1.00 18.43 ?  132 PHE   B O    1 
ATOM   5997 C  CB   . PHE   B 1 132 ? 42.869 -28.633 5.651   1.00 14.45 ?  132 PHE   B CB   1 
ATOM   5998 C  CG   . PHE   B 1 132 ? 43.571 -27.293 5.766   1.00 14.05 ?  132 PHE   B CG   1 
ATOM   5999 C  CD1  . PHE   B 1 132 ? 44.869 -27.113 5.314   1.00 15.42 ?  132 PHE   B CD1  1 
ATOM   6000 C  CD2  . PHE   B 1 132 ? 42.892 -26.192 6.274   1.00 13.54 ?  132 PHE   B CD2  1 
ATOM   6001 C  CE1  . PHE   B 1 132 ? 45.490 -25.871 5.412   1.00 15.87 ?  132 PHE   B CE1  1 
ATOM   6002 C  CE2  . PHE   B 1 132 ? 43.497 -24.950 6.362   1.00 14.28 ?  132 PHE   B CE2  1 
ATOM   6003 C  CZ   . PHE   B 1 132 ? 44.795 -24.792 5.931   1.00 15.49 ?  132 PHE   B CZ   1 
ATOM   6004 H  H    . PHE   B 1 132 ? 44.635 -30.177 4.830   1.00 18.27 ?  132 PHE   B H    1 
ATOM   6005 H  HA   . PHE   B 1 132 ? 43.857 -29.408 7.262   1.00 18.51 ?  132 PHE   B HA   1 
ATOM   6006 H  HB2  . PHE   B 1 132 ? 42.847 -28.868 4.713   1.00 17.35 ?  132 PHE   B HB2  1 
ATOM   6007 H  HB3  . PHE   B 1 132 ? 41.964 -28.522 5.985   1.00 17.35 ?  132 PHE   B HB3  1 
ATOM   6008 H  HD1  . PHE   B 1 132 ? 45.342 -27.839 4.970   1.00 18.52 ?  132 PHE   B HD1  1 
ATOM   6009 H  HD2  . PHE   B 1 132 ? 42.013 -26.295 6.568   1.00 16.26 ?  132 PHE   B HD2  1 
ATOM   6010 H  HE1  . PHE   B 1 132 ? 46.368 -25.765 5.122   1.00 19.06 ?  132 PHE   B HE1  1 
ATOM   6011 H  HE2  . PHE   B 1 132 ? 43.027 -24.228 6.721   1.00 17.15 ?  132 PHE   B HE2  1 
ATOM   6012 H  HZ   . PHE   B 1 132 ? 45.208 -23.958 6.001   1.00 18.61 ?  132 PHE   B HZ   1 
ATOM   6013 N  N    . GLY   B 1 133 ? 42.620 -32.054 6.155   1.00 16.05 ?  133 GLY   B N    1 
ATOM   6014 C  CA   . GLY   B 1 133 ? 41.903 -33.219 6.646   1.00 17.14 ?  133 GLY   B CA   1 
ATOM   6015 C  C    . GLY   B 1 133 ? 40.509 -33.480 6.105   1.00 17.52 ?  133 GLY   B C    1 
ATOM   6016 O  O    . GLY   B 1 133 ? 39.920 -34.502 6.469   1.00 19.43 ?  133 GLY   B O    1 
ATOM   6017 H  H    . GLY   B 1 133 ? 43.111 -32.208 5.465   1.00 19.27 ?  133 GLY   B H    1 
ATOM   6018 H  HA2  . GLY   B 1 133 ? 42.440 -34.003 6.458   1.00 20.59 ?  133 GLY   B HA2  1 
ATOM   6019 H  HA3  . GLY   B 1 133 ? 41.826 -33.141 7.609   1.00 20.59 ?  133 GLY   B HA3  1 
ATOM   6020 N  N    . ALA   B 1 134 ? 39.949 -32.611 5.273   1.00 16.31 ?  134 ALA   B N    1 
ATOM   6021 C  CA   . ALA   B 1 134 ? 38.626 -32.892 4.736   1.00 16.61 ?  134 ALA   B CA   1 
ATOM   6022 C  C    . ALA   B 1 134 ? 38.713 -33.881 3.577   1.00 16.91 ?  134 ALA   B C    1 
ATOM   6023 O  O    . ALA   B 1 134 ? 39.768 -34.076 2.966   1.00 18.03 ?  134 ALA   B O    1 
ATOM   6024 C  CB   . ALA   B 1 134 ? 37.942 -31.605 4.275   1.00 17.13 ?  134 ALA   B CB   1 
ATOM   6025 H  H    . ALA   B 1 134 ? 40.300 -31.865 5.015   1.00 19.58 ?  134 ALA   B H    1 
ATOM   6026 H  HA   . ALA   B 1 134 ? 38.080 -33.288 5.435   1.00 19.94 ?  134 ALA   B HA   1 
ATOM   6027 H  HB1  . ALA   B 1 134 ? 37.058 -31.823 3.941   1.00 20.56 ?  134 ALA   B HB1  1 
ATOM   6028 H  HB2  . ALA   B 1 134 ? 37.871 -30.999 5.029   1.00 20.56 ?  134 ALA   B HB2  1 
ATOM   6029 H  HB3  . ALA   B 1 134 ? 38.473 -31.201 3.573   1.00 20.56 ?  134 ALA   B HB3  1 
ATOM   6030 N  N    . ASP   B 1 135 ? 37.580 -34.509 3.284   1.00 17.08 ?  135 ASP   B N    1 
ATOM   6031 C  CA   . ASP   B 1 135 ? 37.485 -35.409 2.144   1.00 17.98 ?  135 ASP   B CA   1 
ATOM   6032 C  C    . ASP   B 1 135 ? 37.578 -34.575 0.874   1.00 16.66 ?  135 ASP   B C    1 
ATOM   6033 O  O    . ASP   B 1 135 ? 36.722 -33.705 0.655   1.00 16.56 ?  135 ASP   B O    1 
ATOM   6034 C  CB   . ASP   B 1 135 ? 36.146 -36.143 2.201   1.00 19.70 ?  135 ASP   B CB   1 
ATOM   6035 C  CG   . ASP   B 1 135 ? 35.963 -37.134 1.064   1.00 21.87 ?  135 ASP   B CG   1 
ATOM   6036 O  OD1  . ASP   B 1 135 ? 36.827 -37.182 0.161   1.00 21.37 ?  135 ASP   B OD1  1 
ATOM   6037 O  OD2  . ASP   B 1 135 ? 34.954 -37.879 1.084   1.00 24.95 -1 135 ASP   B OD2  1 
ATOM   6038 H  H    . ASP   B 1 135 ? 36.850 -34.430 3.731   1.00 20.51 ?  135 ASP   B H    1 
ATOM   6039 H  HA   . ASP   B 1 135 ? 38.208 -36.057 2.175   1.00 21.59 ?  135 ASP   B HA   1 
ATOM   6040 H  HB2  . ASP   B 1 135 ? 36.097 -36.633 3.035   1.00 23.66 ?  135 ASP   B HB2  1 
ATOM   6041 H  HB3  . ASP   B 1 135 ? 35.433 -35.494 2.149   1.00 23.66 ?  135 ASP   B HB3  1 
ATOM   6042 N  N    . PRO   B 1 136 ? 38.588 -34.776 0.026   1.00 16.98 ?  136 PRO   B N    1 
ATOM   6043 C  CA   . PRO   B 1 136 ? 38.681 -33.952 -1.189  1.00 16.23 ?  136 PRO   B CA   1 
ATOM   6044 C  C    . PRO   B 1 136 ? 37.488 -34.100 -2.110  1.00 15.42 ?  136 PRO   B C    1 
ATOM   6045 O  O    . PRO   B 1 136 ? 37.167 -33.156 -2.839  1.00 14.71 ?  136 PRO   B O    1 
ATOM   6046 C  CB   . PRO   B 1 136 ? 39.985 -34.428 -1.846  1.00 17.30 ?  136 PRO   B CB   1 
ATOM   6047 C  CG   . PRO   B 1 136 ? 40.190 -35.817 -1.310  1.00 18.57 ?  136 PRO   B CG   1 
ATOM   6048 C  CD   . PRO   B 1 136 ? 39.665 -35.777 0.096   1.00 17.97 ?  136 PRO   B CD   1 
ATOM   6049 H  HA   . PRO   B 1 136 ? 38.771 -33.017 -0.954  1.00 19.50 ?  136 PRO   B HA   1 
ATOM   6050 H  HB2  . PRO   B 1 136 ? 39.882 -34.443 -2.812  1.00 20.77 ?  136 PRO   B HB2  1 
ATOM   6051 H  HB3  . PRO   B 1 136 ? 40.713 -33.845 -1.586  1.00 20.77 ?  136 PRO   B HB3  1 
ATOM   6052 H  HG2  . PRO   B 1 136 ? 39.689 -36.454 -1.844  1.00 22.30 ?  136 PRO   B HG2  1 
ATOM   6053 H  HG3  . PRO   B 1 136 ? 41.136 -36.034 -1.315  1.00 22.30 ?  136 PRO   B HG3  1 
ATOM   6054 H  HD2  . PRO   B 1 136 ? 39.307 -36.642 0.349   1.00 21.58 ?  136 PRO   B HD2  1 
ATOM   6055 H  HD3  . PRO   B 1 136 ? 40.355 -35.482 0.712   1.00 21.58 ?  136 PRO   B HD3  1 
ATOM   6056 N  N    . ILE   B 1 137 ? 36.835 -35.266 -2.122  1.00 15.84 ?  137 ILE   B N    1 
ATOM   6057 C  CA   . ILE   B 1 137 ? 35.615 -35.432 -2.911  1.00 16.20 ?  137 ILE   B CA   1 
ATOM   6058 C  C    . ILE   B 1 137 ? 34.542 -34.464 -2.431  1.00 15.39 ?  137 ILE   B C    1 
ATOM   6059 O  O    . ILE   B 1 137 ? 33.820 -33.854 -3.230  1.00 15.32 ?  137 ILE   B O    1 
ATOM   6060 C  CB   . ILE   B 1 137 ? 35.143 -36.902 -2.851  1.00 18.61 ?  137 ILE   B CB   1 
ATOM   6061 C  CG1  . ILE   B 1 137 ? 36.137 -37.804 -3.588  1.00 21.33 ?  137 ILE   B CG1  1 
ATOM   6062 C  CG2  . ILE   B 1 137 ? 33.737 -37.049 -3.431  1.00 19.04 ?  137 ILE   B CG2  1 
ATOM   6063 C  CD1  . ILE   B 1 137 ? 35.849 -39.288 -3.448  1.00 23.74 ?  137 ILE   B CD1  1 
ATOM   6064 H  H    . ILE   B 1 137 ? 37.073 -35.972 -1.691  1.00 19.03 ?  137 ILE   B H    1 
ATOM   6065 H  HA   . ILE   B 1 137 ? 35.806 -35.228 -3.841  1.00 19.46 ?  137 ILE   B HA   1 
ATOM   6066 H  HB   . ILE   B 1 137 ? 35.113 -37.178 -1.926  1.00 22.35 ?  137 ILE   B HB   1 
ATOM   6067 H  HG12 . ILE   B 1 137 ? 36.115 -37.591 -4.534  1.00 25.62 ?  137 ILE   B HG12 1 
ATOM   6068 H  HG13 . ILE   B 1 137 ? 37.023 -37.643 -3.234  1.00 25.62 ?  137 ILE   B HG13 1 
ATOM   6069 H  HG21 . ILE   B 1 137 ? 33.508 -37.992 -3.500  1.00 22.86 ?  137 ILE   B HG21 1 
ATOM   6070 H  HG22 . ILE   B 1 137 ? 33.100 -36.613 -2.845  1.00 22.86 ?  137 ILE   B HG22 1 
ATOM   6071 H  HG23 . ILE   B 1 137 ? 33.710 -36.645 -4.312  1.00 22.86 ?  137 ILE   B HG23 1 
ATOM   6072 H  HD11 . ILE   B 1 137 ? 36.546 -39.780 -3.907  1.00 28.50 ?  137 ILE   B HD11 1 
ATOM   6073 H  HD12 . ILE   B 1 137 ? 35.839 -39.525 -2.507  1.00 28.50 ?  137 ILE   B HD12 1 
ATOM   6074 H  HD13 . ILE   B 1 137 ? 34.990 -39.495 -3.850  1.00 28.50 ?  137 ILE   B HD13 1 
ATOM   6075 N  N    . HIS   B 1 138 ? 34.415 -34.317 -1.116  1.00 15.57 ?  138 HIS   B N    1 
ATOM   6076 C  CA   . HIS   B 1 138 ? 33.467 -33.352 -0.578  1.00 16.19 ?  138 HIS   B CA   1 
ATOM   6077 C  C    . HIS   B 1 138 ? 33.883 -31.924 -0.901  1.00 15.35 ?  138 HIS   B C    1 
ATOM   6078 O  O    . HIS   B 1 138 ? 33.033 -31.084 -1.210  1.00 15.97 ?  138 HIS   B O    1 
ATOM   6079 C  CB   . HIS   B 1 138 ? 33.350 -33.533 0.927   1.00 17.51 ?  138 HIS   B CB   1 
ATOM   6080 C  CG   . HIS   B 1 138 ? 32.416 -32.560 1.566   1.00 18.73 ?  138 HIS   B CG   1 
ATOM   6081 N  ND1  . HIS   B 1 138 ? 31.075 -32.505 1.252   1.00 20.13 ?  138 HIS   B ND1  1 
ATOM   6082 C  CD2  . HIS   B 1 138 ? 32.633 -31.578 2.471   1.00 19.22 ?  138 HIS   B CD2  1 
ATOM   6083 C  CE1  . HIS   B 1 138 ? 30.502 -31.543 1.953   1.00 20.17 ?  138 HIS   B CE1  1 
ATOM   6084 N  NE2  . HIS   B 1 138 ? 31.426 -30.963 2.698   1.00 19.47 ?  138 HIS   B NE2  1 
ATOM   6085 H  H    . HIS   B 1 138 ? 34.865 -34.753 -0.531  1.00 18.70 ?  138 HIS   B H    1 
ATOM   6086 H  HA   . HIS   B 1 138 ? 32.594 -33.515 -0.974  1.00 19.44 ?  138 HIS   B HA   1 
ATOM   6087 H  HB2  . HIS   B 1 138 ? 33.017 -34.428 1.109   1.00 21.02 ?  138 HIS   B HB2  1 
ATOM   6088 H  HB3  . HIS   B 1 138 ? 34.223 -33.417 1.325   1.00 21.02 ?  138 HIS   B HB3  1 
ATOM   6089 H  HD1  . HIS   B 1 138 ? 30.674 -33.028 0.695   1.00 24.17 ?  138 HIS   B HD1  1 
ATOM   6090 H  HD2  . HIS   B 1 138 ? 33.441 -31.364 2.871   1.00 23.08 ?  138 HIS   B HD2  1 
ATOM   6091 H  HE1  . HIS   B 1 138 ? 29.597 -31.323 1.925   1.00 24.22 ?  138 HIS   B HE1  1 
ATOM   6092 N  N    . SER   B 1 139 ? 35.177 -31.618 -0.813  1.00 14.87 ?  139 SER   B N    1 
ATOM   6093 C  CA   . SER   B 1 139 ? 35.618 -30.271 -1.140  1.00 14.35 ?  139 SER   B CA   1 
ATOM   6094 C  C    . SER   B 1 139 ? 35.282 -29.921 -2.581  1.00 13.36 ?  139 SER   B C    1 
ATOM   6095 O  O    . SER   B 1 139 ? 34.838 -28.804 -2.863  1.00 13.47 ?  139 SER   B O    1 
ATOM   6096 C  CB   . SER   B 1 139 ? 37.114 -30.134 -0.880  1.00 14.78 ?  139 SER   B CB   1 
ATOM   6097 O  OG   . SER   B 1 139 ? 37.524 -28.801 -1.130  1.00 14.52 ?  139 SER   B OG   1 
ATOM   6098 H  H    . SER   B 1 139 ? 35.794 -32.157 -0.576  1.00 17.86 ?  139 SER   B H    1 
ATOM   6099 H  HA   . SER   B 1 139 ? 35.149 -29.642 -0.570  1.00 17.24 ?  139 SER   B HA   1 
ATOM   6100 H  HB2  . SER   B 1 139 ? 37.293 -30.357 0.046   1.00 17.74 ?  139 SER   B HB2  1 
ATOM   6101 H  HB3  . SER   B 1 139 ? 37.595 -30.733 -1.470  1.00 17.74 ?  139 SER   B HB3  1 
ATOM   6102 H  HG   . SER   B 1 139 ? 38.350 -28.725 -0.983  1.00 17.44 ?  139 SER   B HG   1 
ATOM   6103 N  N    . LEU   B 1 140 ? 35.463 -30.867 -3.504  1.00 13.32 ?  140 LEU   B N    1 
ATOM   6104 C  CA   . LEU   B 1 140 ? 35.100 -30.616 -4.892  1.00 13.17 ?  140 LEU   B CA   1 
ATOM   6105 C  C    . LEU   B 1 140 ? 33.596 -30.395 -5.024  1.00 13.58 ?  140 LEU   B C    1 
ATOM   6106 O  O    . LEU   B 1 140 ? 33.154 -29.513 -5.767  1.00 13.33 ?  140 LEU   B O    1 
ATOM   6107 C  CB   . LEU   B 1 140 ? 35.576 -31.775 -5.771  1.00 13.25 ?  140 LEU   B CB   1 
ATOM   6108 C  CG   . LEU   B 1 140 ? 35.204 -31.669 -7.242  1.00 13.45 ?  140 LEU   B CG   1 
ATOM   6109 C  CD1  . LEU   B 1 140 ? 35.778 -30.402 -7.844  1.00 14.59 ?  140 LEU   B CD1  1 
ATOM   6110 C  CD2  . LEU   B 1 140 ? 35.665 -32.903 -7.999  1.00 14.83 ?  140 LEU   B CD2  1 
ATOM   6111 H  H    . LEU   B 1 140 ? 35.784 -31.647 -3.355  1.00 16.00 ?  140 LEU   B H    1 
ATOM   6112 H  HA   . LEU   B 1 140 ? 35.551 -29.811 -5.192  1.00 15.82 ?  140 LEU   B HA   1 
ATOM   6113 H  HB2  . LEU   B 1 140 ? 36.545 -31.825 -5.721  1.00 15.91 ?  140 LEU   B HB2  1 
ATOM   6114 H  HB3  . LEU   B 1 140 ? 35.191 -32.598 -5.437  1.00 15.91 ?  140 LEU   B HB3  1 
ATOM   6115 H  HG   . LEU   B 1 140 ? 34.241 -31.613 -7.318  1.00 16.16 ?  140 LEU   B HG   1 
ATOM   6116 H  HD11 . LEU   B 1 140 ? 35.655 -30.425 -8.804  1.00 17.52 ?  140 LEU   B HD11 1 
ATOM   6117 H  HD12 . LEU   B 1 140 ? 35.314 -29.632 -7.471  1.00 17.52 ?  140 LEU   B HD12 1 
ATOM   6118 H  HD13 . LEU   B 1 140 ? 36.724 -30.350 -7.632  1.00 17.52 ?  140 LEU   B HD13 1 
ATOM   6119 H  HD21 . LEU   B 1 140 ? 35.410 -32.804 -8.931  1.00 17.81 ?  140 LEU   B HD21 1 
ATOM   6120 H  HD22 . LEU   B 1 140 ? 36.622 -32.980 -7.919  1.00 17.81 ?  140 LEU   B HD22 1 
ATOM   6121 H  HD23 . LEU   B 1 140 ? 35.227 -33.677 -7.616  1.00 17.81 ?  140 LEU   B HD23 1 
ATOM   6122 N  N    . ARG   B 1 141 ? 32.797 -31.183 -4.299  1.00 13.60 ?  141 ARG   B N    1 
ATOM   6123 C  CA   . ARG   B 1 141 ? 31.345 -31.010 -4.284  1.00 14.69 ?  141 ARG   B CA   1 
ATOM   6124 C  C    . ARG   B 1 141 ? 30.965 -29.596 -3.857  1.00 14.13 ?  141 ARG   B C    1 
ATOM   6125 O  O    . ARG   B 1 141 ? 30.153 -28.921 -4.511  1.00 14.22 ?  141 ARG   B O    1 
ATOM   6126 C  CB   . ARG   B 1 141 ? 30.766 -32.039 -3.307  1.00 16.04 ?  141 ARG   B CB   1 
ATOM   6127 C  CG   . ARG   B 1 141 ? 29.296 -31.938 -2.993  1.00 17.88 ?  141 ARG   B CG   1 
ATOM   6128 C  CD   . ARG   B 1 141 ? 28.516 -32.576 -4.074  1.00 19.84 ?  141 ARG   B CD   1 
ATOM   6129 N  NE   . ARG   B 1 141 ? 28.247 -31.656 -5.168  1.00 20.30 ?  141 ARG   B NE   1 
ATOM   6130 C  CZ   . ARG   B 1 141 ? 28.232 -31.994 -6.450  1.00 20.11 ?  141 ARG   B CZ   1 
ATOM   6131 N  NH1  . ARG   B 1 141 ? 28.666 -33.176 -6.860  1.00 19.83 ?  141 ARG   B NH1  1 
ATOM   6132 N  NH2  . ARG   B 1 141 ? 27.766 -31.124 -7.342  1.00 21.12 ?  141 ARG   B NH2  1 
ATOM   6133 H  H    . ARG   B 1 141 ? 33.079 -31.826 -3.805  1.00 16.34 ?  141 ARG   B H    1 
ATOM   6134 H  HA   . ARG   B 1 141 ? 30.986 -31.175 -5.167  1.00 17.64 ?  141 ARG   B HA   1 
ATOM   6135 H  HB2  . ARG   B 1 141 ? 30.937 -32.925 -3.672  1.00 19.26 ?  141 ARG   B HB2  1 
ATOM   6136 H  HB3  . ARG   B 1 141 ? 31.244 -31.955 -2.468  1.00 19.26 ?  141 ARG   B HB3  1 
ATOM   6137 H  HG2  . ARG   B 1 141 ? 29.118 -32.398 -2.162  1.00 21.47 ?  141 ARG   B HG2  1 
ATOM   6138 H  HG3  . ARG   B 1 141 ? 29.034 -31.004 -2.926  1.00 21.47 ?  141 ARG   B HG3  1 
ATOM   6139 H  HD2  . ARG   B 1 141 ? 29.013 -33.340 -4.418  1.00 23.82 ?  141 ARG   B HD2  1 
ATOM   6140 H  HD3  . ARG   B 1 141 ? 27.675 -32.877 -3.710  1.00 23.82 ?  141 ARG   B HD3  1 
ATOM   6141 H  HE   . ARG   B 1 141 ? 28.056 -30.844 -4.966  1.00 24.37 ?  141 ARG   B HE   1 
ATOM   6142 H  HH11 . ARG   B 1 141 ? 28.960 -33.755 -6.295  1.00 23.81 ?  141 ARG   B HH11 1 
ATOM   6143 H  HH12 . ARG   B 1 141 ? 28.657 -33.368 -7.696  1.00 23.81 ?  141 ARG   B HH12 1 
ATOM   6144 H  HH21 . ARG   B 1 141 ? 27.490 -30.350 -7.086  1.00 25.35 ?  141 ARG   B HH21 1 
ATOM   6145 H  HH22 . ARG   B 1 141 ? 27.772 -31.320 -8.181  1.00 25.35 ?  141 ARG   B HH22 1 
ATOM   6146 N  N    . VAL   B 1 142 ? 31.512 -29.149 -2.730  1.00 13.73 ?  142 VAL   B N    1 
ATOM   6147 C  CA   . VAL   B 1 142 ? 31.183 -27.814 -2.243  1.00 13.64 ?  142 VAL   B CA   1 
ATOM   6148 C  C    . VAL   B 1 142 ? 31.656 -26.756 -3.234  1.00 13.60 ?  142 VAL   B C    1 
ATOM   6149 O  O    . VAL   B 1 142 ? 30.955 -25.770 -3.492  1.00 13.94 ?  142 VAL   B O    1 
ATOM   6150 C  CB   . VAL   B 1 142 ? 31.734 -27.592 -0.821  1.00 14.33 ?  142 VAL   B CB   1 
ATOM   6151 C  CG1  . VAL   B 1 142 ? 31.419 -26.176 -0.333  1.00 14.54 ?  142 VAL   B CG1  1 
ATOM   6152 C  CG2  . VAL   B 1 142 ? 31.161 -28.624 0.133   1.00 15.09 ?  142 VAL   B CG2  1 
ATOM   6153 H  H    . VAL   B 1 142 ? 32.072 -29.584 -2.242  1.00 16.48 ?  142 VAL   B H    1 
ATOM   6154 H  HA   . VAL   B 1 142 ? 30.225 -27.740 -2.187  1.00 16.38 ?  142 VAL   B HA   1 
ATOM   6155 H  HB   . VAL   B 1 142 ? 32.701 -27.698 -0.830  1.00 17.21 ?  142 VAL   B HB   1 
ATOM   6156 H  HG11 . VAL   B 1 142 ? 31.618 -26.119 0.613   1.00 17.46 ?  142 VAL   B HG11 1 
ATOM   6157 H  HG12 . VAL   B 1 142 ? 31.970 -25.544 -0.824  1.00 17.46 ?  142 VAL   B HG12 1 
ATOM   6158 H  HG13 . VAL   B 1 142 ? 30.482 -25.993 -0.489  1.00 17.46 ?  142 VAL   B HG13 1 
ATOM   6159 H  HG21 . VAL   B 1 142 ? 31.477 -28.435 1.029   1.00 18.12 ?  142 VAL   B HG21 1 
ATOM   6160 H  HG22 . VAL   B 1 142 ? 30.194 -28.572 0.103   1.00 18.12 ?  142 VAL   B HG22 1 
ATOM   6161 H  HG23 . VAL   B 1 142 ? 31.455 -29.506 -0.144  1.00 18.12 ?  142 VAL   B HG23 1 
ATOM   6162 N  N    . CYS   B 1 143 ? 32.836 -26.951 -3.821  1.00 12.98 ?  143 CYS   B N    1 
ATOM   6163 C  CA   . CYS   B 1 143 ? 33.329 -26.014 -4.825  1.00 12.71 ?  143 CYS   B CA   1 
ATOM   6164 C  C    . CYS   B 1 143 ? 32.328 -25.868 -5.966  1.00 12.73 ?  143 CYS   B C    1 
ATOM   6165 O  O    . CYS   B 1 143 ? 31.925 -24.757 -6.326  1.00 13.07 ?  143 CYS   B O    1 
ATOM   6166 C  CB   . CYS   B 1 143 ? 34.688 -26.496 -5.348  1.00 13.15 ?  143 CYS   B CB   1 
ATOM   6167 S  SG   . CYS   B 1 143 ? 35.431 -25.397 -6.571  1.00 13.46 ?  143 CYS   B SG   1 
ATOM   6168 H  H    . CYS   B 1 143 ? 33.373 -27.601 -3.648  1.00 15.59 ?  143 CYS   B H    1 
ATOM   6169 H  HA   . CYS   B 1 143 ? 33.462 -25.143 -4.420  1.00 15.26 ?  143 CYS   B HA   1 
ATOM   6170 H  HB2  . CYS   B 1 143 ? 35.313 -26.569 -4.606  1.00 15.79 ?  143 CYS   B HB2  1 
ATOM   6171 H  HB3  . CYS   B 1 143 ? 34.578 -27.365 -5.760  1.00 15.79 ?  143 CYS   B HB3  1 
ATOM   6172 H  HG   . CYS   B 1 143 ? 36.506 -25.830 -6.895  1.00 16.16 ?  143 CYS   B HG   1 
ATOM   6173 N  N    . VAL   B 1 144 ? 31.920 -26.987 -6.556  1.00 13.17 ?  144 VAL   B N    1 
ATOM   6174 C  CA   . VAL   B 1 144 ? 31.012 -26.930 -7.696  1.00 14.24 ?  144 VAL   B CA   1 
ATOM   6175 C  C    . VAL   B 1 144 ? 29.672 -26.316 -7.318  1.00 14.24 ?  144 VAL   B C    1 
ATOM   6176 O  O    . VAL   B 1 144 ? 29.054 -25.610 -8.125  1.00 15.59 ?  144 VAL   B O    1 
ATOM   6177 C  CB   . VAL   B 1 144 ? 30.857 -28.347 -8.267  1.00 16.87 ?  144 VAL   B CB   1 
ATOM   6178 C  CG1  . VAL   B 1 144 ? 29.579 -28.482 -9.093  1.00 19.40 ?  144 VAL   B CG1  1 
ATOM   6179 C  CG2  . VAL   B 1 144 ? 32.104 -28.751 -9.061  1.00 17.09 ?  144 VAL   B CG2  1 
ATOM   6180 H  H    . VAL   B 1 144 ? 32.155 -27.780 -6.320  1.00 15.81 ?  144 VAL   B H    1 
ATOM   6181 H  HA   . VAL   B 1 144 ? 31.405 -26.378 -8.385  1.00 17.11 ?  144 VAL   B HA   1 
ATOM   6182 H  HB   . VAL   B 1 144 ? 30.784 -28.971 -7.526  1.00 20.26 ?  144 VAL   B HB   1 
ATOM   6183 H  HG11 . VAL   B 1 144 ? 29.653 -29.274 -9.653  1.00 23.29 ?  144 VAL   B HG11 1 
ATOM   6184 H  HG12 . VAL   B 1 144 ? 28.826 -28.577 -8.492  1.00 23.29 ?  144 VAL   B HG12 1 
ATOM   6185 H  HG13 . VAL   B 1 144 ? 29.477 -27.697 -9.647  1.00 23.29 ?  144 VAL   B HG13 1 
ATOM   6186 H  HG21 . VAL   B 1 144 ? 31.983 -29.651 -9.409  1.00 20.52 ?  144 VAL   B HG21 1 
ATOM   6187 H  HG22 . VAL   B 1 144 ? 32.226 -28.129 -9.796  1.00 20.52 ?  144 VAL   B HG22 1 
ATOM   6188 H  HG23 . VAL   B 1 144 ? 32.876 -28.726 -8.475  1.00 20.52 ?  144 VAL   B HG23 1 
ATOM   6189 N  N    . ASP   B 1 145 ? 29.202 -26.567 -6.100  1.00 14.33 ?  145 ASP   B N    1 
ATOM   6190 C  CA   . ASP   B 1 145 ? 27.899 -26.095 -5.656  1.00 15.22 ?  145 ASP   B CA   1 
ATOM   6191 C  C    . ASP   B 1 145 ? 27.927 -24.671 -5.115  1.00 14.58 ?  145 ASP   B C    1 
ATOM   6192 O  O    . ASP   B 1 145 ? 26.868 -24.133 -4.777  1.00 16.70 ?  145 ASP   B O    1 
ATOM   6193 C  CB   . ASP   B 1 145 ? 27.325 -27.017 -4.569  1.00 17.07 ?  145 ASP   B CB   1 
ATOM   6194 C  CG   . ASP   B 1 145 ? 26.952 -28.389 -5.081  1.00 18.56 ?  145 ASP   B CG   1 
ATOM   6195 O  OD1  . ASP   B 1 145 ? 26.830 -28.572 -6.309  1.00 18.83 ?  145 ASP   B OD1  1 
ATOM   6196 O  OD2  . ASP   B 1 145 ? 26.775 -29.281 -4.229  1.00 20.53 -1 145 ASP   B OD2  1 
ATOM   6197 H  H    . ASP   B 1 145 ? 29.636 -27.001 -5.502  1.00 17.21 ?  145 ASP   B H    1 
ATOM   6198 H  HA   . ASP   B 1 145 ? 27.294 -26.094 -6.407  1.00 18.28 ?  145 ASP   B HA   1 
ATOM   6199 H  HB2  . ASP   B 1 145 ? 27.984 -27.131 -3.873  1.00 20.50 ?  145 ASP   B HB2  1 
ATOM   6200 H  HB3  . ASP   B 1 145 ? 26.522 -26.608 -4.208  1.00 20.50 ?  145 ASP   B HB3  1 
ATOM   6201 N  N    . THR   B 1 146 ? 29.103 -24.053 -5.012  1.00 12.78 ?  146 THR   B N    1 
ATOM   6202 C  CA   . THR   B 1 146 ? 29.246 -22.736 -4.399  1.00 12.48 ?  146 THR   B CA   1 
ATOM   6203 C  C    . THR   B 1 146 ? 29.871 -21.705 -5.318  1.00 12.42 ?  146 THR   B C    1 
ATOM   6204 O  O    . THR   B 1 146 ? 29.409 -20.546 -5.367  1.00 12.80 ?  146 THR   B O    1 
ATOM   6205 C  CB   . THR   B 1 146 ? 30.077 -22.846 -3.114  1.00 13.02 ?  146 THR   B CB   1 
ATOM   6206 O  OG1  . THR   B 1 146 ? 29.495 -23.832 -2.255  1.00 13.32 ?  146 THR   B OG1  1 
ATOM   6207 C  CG2  . THR   B 1 146 ? 30.153 -21.504 -2.391  1.00 13.06 ?  146 THR   B CG2  1 
ATOM   6208 H  H    . THR   B 1 146 ? 29.852 -24.383 -5.295  1.00 15.36 ?  146 THR   B H    1 
ATOM   6209 H  HA   . THR   B 1 146 ? 28.374 -22.408 -4.155  1.00 14.99 ?  146 THR   B HA   1 
ATOM   6210 H  HB   . THR   B 1 146 ? 30.985 -23.108 -3.340  1.00 15.64 ?  146 THR   B HB   1 
ATOM   6211 H  HG1  . THR   B 1 146 ? 29.531 -24.591 -2.635  1.00 16.00 ?  146 THR   B HG1  1 
ATOM   6212 H  HG21 . THR   B 1 146 ? 30.510 -21.631 -1.500  1.00 15.68 ?  146 THR   B HG21 1 
ATOM   6213 H  HG22 . THR   B 1 146 ? 30.734 -20.897 -2.880  1.00 15.68 ?  146 THR   B HG22 1 
ATOM   6214 H  HG23 . THR   B 1 146 ? 29.269 -21.116 -2.328  1.00 15.68 ?  146 THR   B HG23 1 
ATOM   6215 N  N    . VAL   B 1 147 ? 30.933 -22.080 -6.021  1.00 12.35 ?  147 VAL   B N    1 
ATOM   6216 C  CA   . VAL   B 1 147 ? 31.653 -21.132 -6.857  1.00 12.15 ?  147 VAL   B CA   1 
ATOM   6217 C  C    . VAL   B 1 147 ? 30.920 -20.998 -8.177  1.00 12.21 ?  147 VAL   B C    1 
ATOM   6218 O  O    . VAL   B 1 147 ? 30.550 -21.999 -8.805  1.00 13.31 ?  147 VAL   B O    1 
ATOM   6219 C  CB   . VAL   B 1 147 ? 33.105 -21.586 -7.071  1.00 12.20 ?  147 VAL   B CB   1 
ATOM   6220 C  CG1  . VAL   B 1 147 ? 33.858 -20.562 -7.885  1.00 12.57 ?  147 VAL   B CG1  1 
ATOM   6221 C  CG2  . VAL   B 1 147 ? 33.786 -21.817 -5.737  1.00 12.33 ?  147 VAL   B CG2  1 
ATOM   6222 H  H    . VAL   B 1 147 ? 31.258 -22.882 -6.039  1.00 14.83 ?  147 VAL   B H    1 
ATOM   6223 H  HA   . VAL   B 1 147 ? 31.668 -20.267 -6.423  1.00 14.59 ?  147 VAL   B HA   1 
ATOM   6224 H  HB   . VAL   B 1 147 ? 33.109 -22.427 -7.566  1.00 14.65 ?  147 VAL   B HB   1 
ATOM   6225 H  HG11 . VAL   B 1 147 ? 34.801 -20.780 -7.872  1.00 15.10 ?  147 VAL   B HG11 1 
ATOM   6226 H  HG12 . VAL   B 1 147 ? 33.527 -20.571 -8.796  1.00 15.10 ?  147 VAL   B HG12 1 
ATOM   6227 H  HG13 . VAL   B 1 147 ? 33.716 -19.686 -7.490  1.00 15.10 ?  147 VAL   B HG13 1 
ATOM   6228 H  HG21 . VAL   B 1 147 ? 34.725 -22.003 -5.892  1.00 14.82 ?  147 VAL   B HG21 1 
ATOM   6229 H  HG22 . VAL   B 1 147 ? 33.692 -21.016 -5.198  1.00 14.82 ?  147 VAL   B HG22 1 
ATOM   6230 H  HG23 . VAL   B 1 147 ? 33.367 -22.568 -5.293  1.00 14.82 ?  147 VAL   B HG23 1 
ATOM   6231 N  N    . ARG   B 1 148 ? 30.716 -19.751 -8.600  1.00 12.07 ?  148 ARG   B N    1 
ATOM   6232 C  CA   . ARG   B 1 148 ? 30.086 -19.433 -9.869  1.00 12.40 ?  148 ARG   B CA   1 
ATOM   6233 C  C    . ARG   B 1 148 ? 31.041 -18.762 -10.845 1.00 12.57 ?  148 ARG   B C    1 
ATOM   6234 O  O    . ARG   B 1 148 ? 30.754 -18.740 -12.046 1.00 13.85 ?  148 ARG   B O    1 
ATOM   6235 C  CB   . ARG   B 1 148 ? 28.851 -18.545 -9.640  1.00 12.84 ?  148 ARG   B CB   1 
ATOM   6236 C  CG   . ARG   B 1 148 ? 27.770 -19.259 -8.836  1.00 13.64 ?  148 ARG   B CG   1 
ATOM   6237 C  CD   . ARG   B 1 148 ? 26.559 -18.376 -8.530  1.00 14.42 ?  148 ARG   B CD   1 
ATOM   6238 N  NE   . ARG   B 1 148 ? 26.944 -17.174 -7.801  1.00 14.17 ?  148 ARG   B NE   1 
ATOM   6239 C  CZ   . ARG   B 1 148 ? 27.258 -17.138 -6.512  1.00 13.26 ?  148 ARG   B CZ   1 
ATOM   6240 N  NH1  . ARG   B 1 148 ? 27.193 -18.220 -5.750  1.00 13.48 ?  148 ARG   B NH1  1 
ATOM   6241 N  NH2  . ARG   B 1 148 ? 27.657 -15.988 -5.974  1.00 13.56 ?  148 ARG   B NH2  1 
ATOM   6242 H  H    . ARG   B 1 148 ? 30.947 -19.050 -8.148  1.00 14.50 ?  148 ARG   B H    1 
ATOM   6243 H  HA   . ARG   B 1 148 ? 29.781 -20.254 -10.276 1.00 14.89 ?  148 ARG   B HA   1 
ATOM   6244 H  HB2  . ARG   B 1 148 ? 29.115 -17.750 -9.145  1.00 15.42 ?  148 ARG   B HB2  1 
ATOM   6245 H  HB3  . ARG   B 1 148 ? 28.475 -18.293 -10.496 1.00 15.42 ?  148 ARG   B HB3  1 
ATOM   6246 H  HG2  . ARG   B 1 148 ? 27.457 -20.027 -9.344  1.00 16.38 ?  148 ARG   B HG2  1 
ATOM   6247 H  HG3  . ARG   B 1 148 ? 28.144 -19.555 -7.992  1.00 16.38 ?  148 ARG   B HG3  1 
ATOM   6248 H  HD2  . ARG   B 1 148 ? 26.141 -18.107 -9.362  1.00 17.32 ?  148 ARG   B HD2  1 
ATOM   6249 H  HD3  . ARG   B 1 148 ? 25.928 -18.875 -7.984  1.00 17.32 ?  148 ARG   B HD3  1 
ATOM   6250 H  HE   . ARG   B 1 148 ? 26.976 -16.436 -8.238  1.00 17.02 ?  148 ARG   B HE   1 
ATOM   6251 H  HH11 . ARG   B 1 148 ? 26.932 -18.970 -6.081  1.00 16.18 ?  148 ARG   B HH11 1 
ATOM   6252 H  HH12 . ARG   B 1 148 ? 27.397 -18.172 -4.914  1.00 16.18 ?  148 ARG   B HH12 1 
ATOM   6253 H  HH21 . ARG   B 1 148 ? 27.714 -15.283 -6.462  1.00 16.29 ?  148 ARG   B HH21 1 
ATOM   6254 H  HH22 . ARG   B 1 148 ? 27.868 -15.952 -5.141  1.00 16.29 ?  148 ARG   B HH22 1 
ATOM   6255 N  N    . THR   B 1 149 ? 32.149 -18.204 -10.359 1.00 12.54 ?  149 THR   B N    1 
ATOM   6256 C  CA   . THR   B 1 149 ? 33.186 -17.641 -11.208 1.00 12.66 ?  149 THR   B CA   1 
ATOM   6257 C  C    . THR   B 1 149 ? 34.072 -18.777 -11.723 1.00 12.16 ?  149 THR   B C    1 
ATOM   6258 O  O    . THR   B 1 149 ? 33.883 -19.948 -11.380 1.00 12.96 ?  149 THR   B O    1 
ATOM   6259 C  CB   . THR   B 1 149 ? 33.960 -16.593 -10.421 1.00 12.63 ?  149 THR   B CB   1 
ATOM   6260 O  OG1  . THR   B 1 149 ? 34.415 -17.190 -9.206  1.00 12.47 ?  149 THR   B OG1  1 
ATOM   6261 C  CG2  . THR   B 1 149 ? 33.068 -15.392 -10.119 1.00 13.06 ?  149 THR   B CG2  1 
ATOM   6262 H  H    . THR   B 1 149 ? 32.314 -18.132 -9.518  1.00 15.06 ?  149 THR   B H    1 
ATOM   6263 H  HA   . THR   B 1 149 ? 32.774 -17.203 -11.969 1.00 15.20 ?  149 THR   B HA   1 
ATOM   6264 H  HB   . THR   B 1 149 ? 34.719 -16.295 -10.936 1.00 15.17 ?  149 THR   B HB   1 
ATOM   6265 H  HG1  . THR   B 1 149 ? 34.831 -16.612 -8.745  1.00 14.98 ?  149 THR   B HG1  1 
ATOM   6266 H  HG21 . THR   B 1 149 ? 33.570 -14.720 -9.637  1.00 15.68 ?  149 THR   B HG21 1 
ATOM   6267 H  HG22 . THR   B 1 149 ? 32.739 -15.008 -10.948 1.00 15.68 ?  149 THR   B HG22 1 
ATOM   6268 H  HG23 . THR   B 1 149 ? 32.309 -15.667 -9.580  1.00 15.68 ?  149 THR   B HG23 1 
ATOM   6269 N  N    . ASN   B 1 150 ? 35.038 -18.454 -12.574 1.00 12.15 ?  150 ASN   B N    1 
ATOM   6270 C  CA   . ASN   B 1 150 ? 35.800 -19.480 -13.275 1.00 12.80 ?  150 ASN   B CA   1 
ATOM   6271 C  C    . ASN   B 1 150 ? 36.966 -19.935 -12.405 1.00 12.31 ?  150 ASN   B C    1 
ATOM   6272 O  O    . ASN   B 1 150 ? 37.896 -19.166 -12.146 1.00 12.95 ?  150 ASN   B O    1 
ATOM   6273 C  CB   . ASN   B 1 150 ? 36.271 -18.945 -14.618 1.00 14.39 ?  150 ASN   B CB   1 
ATOM   6274 C  CG   . ASN   B 1 150 ? 35.127 -18.730 -15.569 1.00 17.15 ?  150 ASN   B CG   1 
ATOM   6275 O  OD1  . ASN   B 1 150 ? 34.223 -19.553 -15.646 1.00 18.33 ?  150 ASN   B OD1  1 
ATOM   6276 N  ND2  . ASN   B 1 150 ? 35.139 -17.615 -16.279 1.00 19.01 ?  150 ASN   B ND2  1 
ATOM   6277 H  H    . ASN   B 1 150 ? 35.281 -17.645 -12.751 1.00 14.60 ?  150 ASN   B H    1 
ATOM   6278 H  HA   . ASN   B 1 150 ? 35.216 -20.243 -13.439 1.00 15.37 ?  150 ASN   B HA   1 
ATOM   6279 H  HB2  . ASN   B 1 150 ? 36.713 -18.092 -14.482 1.00 17.29 ?  150 ASN   B HB2  1 
ATOM   6280 H  HB3  . ASN   B 1 150 ? 36.878 -19.580 -15.019 1.00 17.29 ?  150 ASN   B HB3  1 
ATOM   6281 H  HD21 . ASN   B 1 150 ? 34.504 -17.446 -16.838 1.00 22.82 ?  150 ASN   B HD21 1 
ATOM   6282 H  HD22 . ASN   B 1 150 ? 35.788 -17.054 -16.194 1.00 22.82 ?  150 ASN   B HD22 1 
ATOM   6283 N  N    . VAL   B 1 151 ? 36.924 -21.184 -11.953 1.00 11.91 ?  151 VAL   B N    1 
ATOM   6284 C  CA   . VAL   B 1 151 ? 37.942 -21.714 -11.062 1.00 12.10 ?  151 VAL   B CA   1 
ATOM   6285 C  C    . VAL   B 1 151 ? 38.648 -22.880 -11.739 1.00 11.96 ?  151 VAL   B C    1 
ATOM   6286 O  O    . VAL   B 1 151 ? 38.004 -23.818 -12.237 1.00 13.13 ?  151 VAL   B O    1 
ATOM   6287 C  CB   . VAL   B 1 151 ? 37.386 -22.053 -9.665  1.00 12.99 ?  151 VAL   B CB   1 
ATOM   6288 C  CG1  . VAL   B 1 151 ? 36.221 -23.045 -9.740  1.00 13.99 ?  151 VAL   B CG1  1 
ATOM   6289 C  CG2  . VAL   B 1 151 ? 38.496 -22.558 -8.762  1.00 13.54 ?  151 VAL   B CG2  1 
ATOM   6290 H  H    . VAL   B 1 151 ? 36.298 -21.749 -12.148 1.00 14.31 ?  151 VAL   B H    1 
ATOM   6291 H  HA   . VAL   B 1 151 ? 38.608 -21.017 -10.933 1.00 14.53 ?  151 VAL   B HA   1 
ATOM   6292 H  HB   . VAL   B 1 151 ? 37.042 -21.235 -9.267  1.00 15.60 ?  151 VAL   B HB   1 
ATOM   6293 H  HG11 . VAL   B 1 151 ? 35.909 -23.237 -8.842  1.00 16.81 ?  151 VAL   B HG11 1 
ATOM   6294 H  HG12 . VAL   B 1 151 ? 35.503 -22.655 -10.263 1.00 16.81 ?  151 VAL   B HG12 1 
ATOM   6295 H  HG13 . VAL   B 1 151 ? 36.529 -23.863 -10.164 1.00 16.81 ?  151 VAL   B HG13 1 
ATOM   6296 H  HG21 . VAL   B 1 151 ? 38.153 -22.627 -7.855  1.00 16.26 ?  151 VAL   B HG21 1 
ATOM   6297 H  HG22 . VAL   B 1 151 ? 38.784 -23.430 -9.071  1.00 16.26 ?  151 VAL   B HG22 1 
ATOM   6298 H  HG23 . VAL   B 1 151 ? 39.235 -21.933 -8.787  1.00 16.26 ?  151 VAL   B HG23 1 
ATOM   6299 N  N    . TYR   B 1 152 ? 39.979 -22.792 -11.757 1.00 11.66 ?  152 TYR   B N    1 
ATOM   6300 C  CA   . TYR   B 1 152 ? 40.885 -23.771 -12.340 1.00 11.87 ?  152 TYR   B CA   1 
ATOM   6301 C  C    . TYR   B 1 152 ? 41.604 -24.448 -11.177 1.00 11.01 ?  152 TYR   B C    1 
ATOM   6302 O  O    . TYR   B 1 152 ? 42.452 -23.835 -10.524 1.00 11.84 ?  152 TYR   B O    1 
ATOM   6303 C  CB   . TYR   B 1 152 ? 41.850 -23.056 -13.287 1.00 12.81 ?  152 TYR   B CB   1 
ATOM   6304 C  CG   . TYR   B 1 152 ? 41.168 -22.596 -14.554 1.00 13.30 ?  152 TYR   B CG   1 
ATOM   6305 C  CD1  . TYR   B 1 152 ? 40.501 -21.375 -14.619 1.00 13.74 ?  152 TYR   B CD1  1 
ATOM   6306 C  CD2  . TYR   B 1 152 ? 41.172 -23.399 -15.681 1.00 14.77 ?  152 TYR   B CD2  1 
ATOM   6307 C  CE1  . TYR   B 1 152 ? 39.859 -20.976 -15.778 1.00 15.00 ?  152 TYR   B CE1  1 
ATOM   6308 C  CE2  . TYR   B 1 152 ? 40.535 -23.014 -16.840 1.00 15.25 ?  152 TYR   B CE2  1 
ATOM   6309 C  CZ   . TYR   B 1 152 ? 39.882 -21.799 -16.889 1.00 15.59 ?  152 TYR   B CZ   1 
ATOM   6310 O  OH   . TYR   B 1 152 ? 39.251 -21.415 -18.050 1.00 18.18 ?  152 TYR   B OH   1 
ATOM   6311 H  H    . TYR   B 1 152 ? 40.408 -22.128 -11.408 1.00 14.01 ?  152 TYR   B H    1 
ATOM   6312 H  HA   . TYR   B 1 152 ? 40.379 -24.436 -12.836 1.00 14.25 ?  152 TYR   B HA   1 
ATOM   6313 H  HB2  . TYR   B 1 152 ? 42.212 -22.277 -12.837 1.00 15.39 ?  152 TYR   B HB2  1 
ATOM   6314 H  HB3  . TYR   B 1 152 ? 42.565 -23.663 -13.530 1.00 15.39 ?  152 TYR   B HB3  1 
ATOM   6315 H  HD1  . TYR   B 1 152 ? 40.479 -20.822 -13.869 1.00 16.51 ?  152 TYR   B HD1  1 
ATOM   6316 H  HD2  . TYR   B 1 152 ? 41.608 -24.223 -15.652 1.00 17.74 ?  152 TYR   B HD2  1 
ATOM   6317 H  HE1  . TYR   B 1 152 ? 39.419 -20.156 -15.812 1.00 18.01 ?  152 TYR   B HE1  1 
ATOM   6318 H  HE2  . TYR   B 1 152 ? 40.556 -23.566 -17.587 1.00 18.32 ?  152 TYR   B HE2  1 
ATOM   6319 H  HH   . TYR   B 1 152 ? 39.356 -22.012 -18.634 1.00 21.83 ?  152 TYR   B HH   1 
ATOM   6320 N  N    . LEU   B 1 153 ? 41.240 -25.704 -10.909 1.00 11.55 ?  153 LEU   B N    1 
ATOM   6321 C  CA   . LEU   B 1 153 ? 41.751 -26.456 -9.771  1.00 11.28 ?  153 LEU   B CA   1 
ATOM   6322 C  C    . LEU   B 1 153 ? 42.978 -27.260 -10.171 1.00 11.42 ?  153 LEU   B C    1 
ATOM   6323 O  O    . LEU   B 1 153 ? 42.957 -27.987 -11.164 1.00 12.75 ?  153 LEU   B O    1 
ATOM   6324 C  CB   . LEU   B 1 153 ? 40.674 -27.414 -9.253  1.00 11.65 ?  153 LEU   B CB   1 
ATOM   6325 C  CG   . LEU   B 1 153 ? 39.414 -26.761 -8.685  1.00 12.83 ?  153 LEU   B CG   1 
ATOM   6326 C  CD1  . LEU   B 1 153 ? 38.320 -27.802 -8.523  1.00 13.66 ?  153 LEU   B CD1  1 
ATOM   6327 C  CD2  . LEU   B 1 153 ? 39.720 -26.100 -7.349  1.00 13.16 ?  153 LEU   B CD2  1 
ATOM   6328 H  H    . LEU   B 1 153 ? 40.677 -26.154 -11.392 1.00 13.88 ?  153 LEU   B H    1 
ATOM   6329 H  HA   . LEU   B 1 153 ? 41.984 -25.840 -9.064  1.00 13.55 ?  153 LEU   B HA   1 
ATOM   6330 H  HB2  . LEU   B 1 153 ? 40.394 -27.988 -9.979  1.00 13.99 ?  153 LEU   B HB2  1 
ATOM   6331 H  HB3  . LEU   B 1 153 ? 41.060 -27.951 -8.543  1.00 13.99 ?  153 LEU   B HB3  1 
ATOM   6332 H  HG   . LEU   B 1 153 ? 39.099 -26.071 -9.295  1.00 15.40 ?  153 LEU   B HG   1 
ATOM   6333 H  HD11 . LEU   B 1 153 ? 37.517 -27.362 -8.200  1.00 16.41 ?  153 LEU   B HD11 1 
ATOM   6334 H  HD12 . LEU   B 1 153 ? 38.154 -28.211 -9.381  1.00 16.41 ?  153 LEU   B HD12 1 
ATOM   6335 H  HD13 . LEU   B 1 153 ? 38.617 -28.463 -7.883  1.00 16.41 ?  153 LEU   B HD13 1 
ATOM   6336 H  HD21 . LEU   B 1 153 ? 38.908 -25.725 -6.980  1.00 15.81 ?  153 LEU   B HD21 1 
ATOM   6337 H  HD22 . LEU   B 1 153 ? 40.084 -26.767 -6.743  1.00 15.81 ?  153 LEU   B HD22 1 
ATOM   6338 H  HD23 . LEU   B 1 153 ? 40.377 -25.394 -7.486  1.00 15.81 ?  153 LEU   B HD23 1 
ATOM   6339 N  N    . ALA   B 1 154 ? 44.033 -27.151 -9.369  1.00 11.83 ?  154 ALA   B N    1 
ATOM   6340 C  CA   . ALA   B 1 154 ? 45.265 -27.906 -9.555  1.00 12.81 ?  154 ALA   B CA   1 
ATOM   6341 C  C    . ALA   B 1 154 ? 45.332 -28.985 -8.484  1.00 13.48 ?  154 ALA   B C    1 
ATOM   6342 O  O    . ALA   B 1 154 ? 45.261 -28.689 -7.284  1.00 14.57 ?  154 ALA   B O    1 
ATOM   6343 C  CB   . ALA   B 1 154 ? 46.484 -26.988 -9.480  1.00 13.80 ?  154 ALA   B CB   1 
ATOM   6344 H  H    . ALA   B 1 154 ? 44.052 -26.625 -8.681  1.00 14.20 ?  154 ALA   B H    1 
ATOM   6345 H  HA   . ALA   B 1 154 ? 45.253 -28.331 -10.420 1.00 15.38 ?  154 ALA   B HA   1 
ATOM   6346 H  HB1  . ALA   B 1 154 ? 47.287 -27.517 -9.607  1.00 16.57 ?  154 ALA   B HB1  1 
ATOM   6347 H  HB2  . ALA   B 1 154 ? 46.418 -26.316 -10.179 1.00 16.57 ?  154 ALA   B HB2  1 
ATOM   6348 H  HB3  . ALA   B 1 154 ? 46.508 -26.555 -8.611  1.00 16.57 ?  154 ALA   B HB3  1 
ATOM   6349 N  N    . VAL   B 1 155 ? 45.452 -30.233 -8.920  1.00 13.01 ?  155 VAL   B N    1 
ATOM   6350 C  CA   . VAL   B 1 155 ? 45.559 -31.384 -8.031  1.00 13.23 ?  155 VAL   B CA   1 
ATOM   6351 C  C    . VAL   B 1 155 ? 46.897 -32.055 -8.314  1.00 13.41 ?  155 VAL   B C    1 
ATOM   6352 O  O    . VAL   B 1 155 ? 47.131 -32.545 -9.427  1.00 15.33 ?  155 VAL   B O    1 
ATOM   6353 C  CB   . VAL   B 1 155 ? 44.397 -32.374 -8.224  1.00 14.62 ?  155 VAL   B CB   1 
ATOM   6354 C  CG1  . VAL   B 1 155 ? 44.577 -33.581 -7.315  1.00 14.27 ?  155 VAL   B CG1  1 
ATOM   6355 C  CG2  . VAL   B 1 155 ? 43.065 -31.686 -7.950  1.00 15.92 ?  155 VAL   B CG2  1 
ATOM   6356 H  H    . VAL   B 1 155 ? 45.485 -30.444 -9.753  1.00 15.63 ?  155 VAL   B H    1 
ATOM   6357 H  HA   . VAL   B 1 155 ? 45.553 -31.089 -7.109  1.00 15.89 ?  155 VAL   B HA   1 
ATOM   6358 H  HB   . VAL   B 1 155 ? 44.388 -32.683 -9.145  1.00 17.56 ?  155 VAL   B HB   1 
ATOM   6359 H  HG11 . VAL   B 1 155 ? 43.748 -34.089 -7.292  1.00 17.14 ?  155 VAL   B HG11 1 
ATOM   6360 H  HG12 . VAL   B 1 155 ? 45.291 -34.141 -7.662  1.00 17.14 ?  155 VAL   B HG12 1 
ATOM   6361 H  HG13 . VAL   B 1 155 ? 44.798 -33.277 -6.421  1.00 17.14 ?  155 VAL   B HG13 1 
ATOM   6362 H  HG21 . VAL   B 1 155 ? 42.351 -32.334 -8.041  1.00 19.12 ?  155 VAL   B HG21 1 
ATOM   6363 H  HG22 . VAL   B 1 155 ? 43.078 -31.330 -7.048  1.00 19.12 ?  155 VAL   B HG22 1 
ATOM   6364 H  HG23 . VAL   B 1 155 ? 42.945 -30.966 -8.589  1.00 19.12 ?  155 VAL   B HG23 1 
ATOM   6365 N  N    . PHE   B 1 156 ? 47.764 -32.093 -7.302  1.00 13.82 ?  156 PHE   B N    1 
ATOM   6366 C  CA   . PHE   B 1 156 ? 49.142 -32.544 -7.505  1.00 14.70 ?  156 PHE   B CA   1 
ATOM   6367 C  C    . PHE   B 1 156 ? 49.242 -34.045 -7.787  1.00 15.81 ?  156 PHE   B C    1 
ATOM   6368 O  O    . PHE   B 1 156 ? 49.976 -34.471 -8.689  1.00 17.74 ?  156 PHE   B O    1 
ATOM   6369 C  CB   . PHE   B 1 156 ? 49.971 -32.176 -6.277  1.00 14.78 ?  156 PHE   B CB   1 
ATOM   6370 C  CG   . PHE   B 1 156 ? 51.391 -32.643 -6.332  1.00 15.28 ?  156 PHE   B CG   1 
ATOM   6371 C  CD1  . PHE   B 1 156 ? 52.273 -32.109 -7.251  1.00 16.84 ?  156 PHE   B CD1  1 
ATOM   6372 C  CD2  . PHE   B 1 156 ? 51.852 -33.597 -5.447  1.00 15.90 ?  156 PHE   B CD2  1 
ATOM   6373 C  CE1  . PHE   B 1 156 ? 53.591 -32.519 -7.298  1.00 17.96 ?  156 PHE   B CE1  1 
ATOM   6374 C  CE2  . PHE   B 1 156 ? 53.171 -34.016 -5.489  1.00 16.90 ?  156 PHE   B CE2  1 
ATOM   6375 C  CZ   . PHE   B 1 156 ? 54.035 -33.476 -6.421  1.00 17.60 ?  156 PHE   B CZ   1 
ATOM   6376 H  H    . PHE   B 1 156 ? 47.582 -31.872 -6.490  1.00 16.59 ?  156 PHE   B H    1 
ATOM   6377 H  HA   . PHE   B 1 156 ? 49.514 -32.074 -8.265  1.00 17.65 ?  156 PHE   B HA   1 
ATOM   6378 H  HB2  . PHE   B 1 156 ? 49.984 -31.210 -6.191  1.00 17.75 ?  156 PHE   B HB2  1 
ATOM   6379 H  HB3  . PHE   B 1 156 ? 49.561 -32.571 -5.492  1.00 17.75 ?  156 PHE   B HB3  1 
ATOM   6380 H  HD1  . PHE   B 1 156 ? 51.978 -31.458 -7.847  1.00 20.22 ?  156 PHE   B HD1  1 
ATOM   6381 H  HD2  . PHE   B 1 156 ? 51.263 -33.967 -4.824  1.00 19.09 ?  156 PHE   B HD2  1 
ATOM   6382 H  HE1  . PHE   B 1 156 ? 54.175 -32.153 -7.925  1.00 21.56 ?  156 PHE   B HE1  1 
ATOM   6383 H  HE2  . PHE   B 1 156 ? 53.468 -34.671 -4.896  1.00 20.29 ?  156 PHE   B HE2  1 
ATOM   6384 H  HZ   . PHE   B 1 156 ? 54.921 -33.760 -6.450  1.00 21.14 ?  156 PHE   B HZ   1 
ATOM   6385 N  N    . ASP   B 1 157 ? 48.567 -34.866 -6.993  1.00 16.16 ?  157 ASP   B N    1 
ATOM   6386 C  CA   . ASP   B 1 157 ? 48.721 -36.312 -7.085  1.00 17.23 ?  157 ASP   B CA   1 
ATOM   6387 C  C    . ASP   B 1 157 ? 47.803 -36.866 -8.169  1.00 17.27 ?  157 ASP   B C    1 
ATOM   6388 O  O    . ASP   B 1 157 ? 46.578 -36.737 -8.072  1.00 16.49 ?  157 ASP   B O    1 
ATOM   6389 C  CB   . ASP   B 1 157 ? 48.383 -36.927 -5.733  1.00 18.65 ?  157 ASP   B CB   1 
ATOM   6390 C  CG   . ASP   B 1 157 ? 48.504 -38.440 -5.726  1.00 20.91 ?  157 ASP   B CG   1 
ATOM   6391 O  OD1  . ASP   B 1 157 ? 48.846 -39.041 -6.774  1.00 21.52 ?  157 ASP   B OD1  1 
ATOM   6392 O  OD2  . ASP   B 1 157 ? 48.270 -39.029 -4.652  1.00 22.90 -1 157 ASP   B OD2  1 
ATOM   6393 H  H    . ASP   B 1 157 ? 48.024 -34.610 -6.383  1.00 19.41 ?  157 ASP   B H    1 
ATOM   6394 H  HA   . ASP   B 1 157 ? 49.642 -36.536 -7.309  1.00 20.70 ?  157 ASP   B HA   1 
ATOM   6395 H  HB2  . ASP   B 1 157 ? 48.977 -36.554 -5.064  1.00 22.39 ?  157 ASP   B HB2  1 
ATOM   6396 H  HB3  . ASP   B 1 157 ? 47.464 -36.704 -5.516  1.00 22.39 ?  157 ASP   B HB3  1 
ATOM   6397 N  N    A LYS   B 1 158 ? 48.396 -37.514 -9.178  0.50 17.95 ?  158 LYS   B N    1 
ATOM   6398 N  N    B LYS   B 1 158 ? 48.399 -37.471 -9.205  0.50 18.23 ?  158 LYS   B N    1 
ATOM   6399 C  CA   A LYS   B 1 158 ? 47.616 -38.123 -10.255 0.50 18.76 ?  158 LYS   B CA   1 
ATOM   6400 C  CA   B LYS   B 1 158 ? 47.623 -38.047 -10.301 0.50 19.39 ?  158 LYS   B CA   1 
ATOM   6401 C  C    A LYS   B 1 158 ? 46.561 -39.086 -9.717  0.50 18.74 ?  158 LYS   B C    1 
ATOM   6402 C  C    B LYS   B 1 158 ? 46.569 -39.026 -9.799  0.50 19.55 ?  158 LYS   B C    1 
ATOM   6403 O  O    A LYS   B 1 158 ? 45.449 -39.165 -10.251 0.50 18.61 ?  158 LYS   B O    1 
ATOM   6404 O  O    B LYS   B 1 158 ? 45.480 -39.121 -10.377 0.50 19.63 ?  158 LYS   B O    1 
ATOM   6405 C  CB   A LYS   B 1 158 ? 48.563 -38.838 -11.226 0.50 20.28 ?  158 LYS   B CB   1 
ATOM   6406 C  CB   B LYS   B 1 158 ? 48.574 -38.735 -11.291 0.50 20.87 ?  158 LYS   B CB   1 
ATOM   6407 C  CG   A LYS   B 1 158 ? 47.885 -39.751 -12.239 0.50 22.09 ?  158 LYS   B CG   1 
ATOM   6408 C  CG   B LYS   B 1 158 ? 47.907 -39.656 -12.306 0.50 22.53 ?  158 LYS   B CG   1 
ATOM   6409 C  CD   A LYS   B 1 158 ? 46.995 -38.986 -13.197 0.50 23.66 ?  158 LYS   B CD   1 
ATOM   6410 C  CD   B LYS   B 1 158 ? 47.017 -38.897 -13.269 0.50 24.12 ?  158 LYS   B CD   1 
ATOM   6411 C  CE   A LYS   B 1 158 ? 46.429 -39.910 -14.264 0.50 24.99 ?  158 LYS   B CE   1 
ATOM   6412 C  CE   B LYS   B 1 158 ? 46.433 -39.830 -14.318 0.50 25.47 ?  158 LYS   B CE   1 
ATOM   6413 N  NZ   A LYS   B 1 158 ? 45.349 -39.258 -15.057 0.50 25.24 ?  158 LYS   B NZ   1 
ATOM   6414 N  NZ   B LYS   B 1 158 ? 45.380 -39.165 -15.135 0.50 25.82 ?  158 LYS   B NZ   1 
ATOM   6415 H  H    A LYS   B 1 158 ? 49.248 -37.617 -9.258  0.50 21.55 ?  158 LYS   B H    1 
ATOM   6416 H  H    B LYS   B 1 158 ? 49.252 -37.564 -9.292  0.50 21.88 ?  158 LYS   B H    1 
ATOM   6417 H  HA   A LYS   B 1 158 ? 47.162 -37.423 -10.749 0.50 22.53 ?  158 LYS   B HA   1 
ATOM   6418 H  HA   B LYS   B 1 158 ? 47.172 -37.333 -10.778 0.50 23.28 ?  158 LYS   B HA   1 
ATOM   6419 H  HB2  A LYS   B 1 158 ? 49.059 -38.170 -11.729 0.50 24.35 ?  158 LYS   B HB2  1 
ATOM   6420 H  HB2  B LYS   B 1 158 ? 49.051 -38.052 -11.794 0.50 25.06 ?  158 LYS   B HB2  1 
ATOM   6421 H  HB3  A LYS   B 1 158 ? 49.183 -39.381 -10.715 0.50 24.35 ?  158 LYS   B HB3  1 
ATOM   6422 H  HB3  B LYS   B 1 158 ? 49.212 -39.268 -10.791 0.50 25.06 ?  158 LYS   B HB3  1 
ATOM   6423 H  HG2  A LYS   B 1 158 ? 48.570 -40.197 -12.763 0.50 26.52 ?  158 LYS   B HG2  1 
ATOM   6424 H  HG2  B LYS   B 1 158 ? 48.598 -40.096 -12.827 0.50 27.05 ?  158 LYS   B HG2  1 
ATOM   6425 H  HG3  A LYS   B 1 158 ? 47.346 -40.415 -11.780 0.50 26.52 ?  158 LYS   B HG3  1 
ATOM   6426 H  HG3  B LYS   B 1 158 ? 47.372 -40.326 -11.851 0.50 27.05 ?  158 LYS   B HG3  1 
ATOM   6427 H  HD2  A LYS   B 1 158 ? 46.255 -38.594 -12.708 0.50 28.40 ?  158 LYS   B HD2  1 
ATOM   6428 H  HD2  B LYS   B 1 158 ? 46.285 -38.491 -12.780 0.50 28.95 ?  158 LYS   B HD2  1 
ATOM   6429 H  HD3  A LYS   B 1 158 ? 47.514 -38.294 -13.637 0.50 28.40 ?  158 LYS   B HD3  1 
ATOM   6430 H  HD3  B LYS   B 1 158 ? 47.540 -38.218 -13.724 0.50 28.95 ?  158 LYS   B HD3  1 
ATOM   6431 H  HE2  A LYS   B 1 158 ? 47.138 -40.164 -14.874 0.50 30.01 ?  158 LYS   B HE2  1 
ATOM   6432 H  HE2  B LYS   B 1 158 ? 47.139 -40.122 -14.915 0.50 30.58 ?  158 LYS   B HE2  1 
ATOM   6433 H  HE3  A LYS   B 1 158 ? 46.058 -40.700 -13.839 0.50 30.01 ?  158 LYS   B HE3  1 
ATOM   6434 H  HE3  B LYS   B 1 158 ? 46.033 -40.597 -13.876 0.50 30.58 ?  158 LYS   B HE3  1 
ATOM   6435 H  HZ1  A LYS   B 1 158 ? 45.038 -39.822 -15.671 0.50 30.30 ?  158 LYS   B HZ1  1 
ATOM   6436 H  HZ1  B LYS   B 1 158 ? 45.057 -39.734 -15.738 0.50 31.00 ?  158 LYS   B HZ1  1 
ATOM   6437 H  HZ2  A LYS   B 1 158 ? 44.681 -39.016 -14.521 0.50 30.30 ?  158 LYS   B HZ2  1 
ATOM   6438 H  HZ2  B LYS   B 1 158 ? 44.715 -38.892 -14.610 0.50 31.00 ?  158 LYS   B HZ2  1 
ATOM   6439 H  HZ3  A LYS   B 1 158 ? 45.668 -38.533 -15.465 0.50 30.30 ?  158 LYS   B HZ3  1 
ATOM   6440 H  HZ3  B LYS   B 1 158 ? 45.724 -38.461 -15.557 0.50 31.00 ?  158 LYS   B HZ3  1 
ATOM   6441 N  N    A ASN   B 1 159 ? 46.893 -39.842 -8.668  0.50 18.77 ?  159 ASN   B N    1 
ATOM   6442 N  N    B ASN   B 1 159 ? 46.871 -39.769 -8.733  0.50 19.55 ?  159 ASN   B N    1 
ATOM   6443 C  CA   A ASN   B 1 159 ? 45.942 -40.817 -8.145  0.50 19.28 ?  159 ASN   B CA   1 
ATOM   6444 C  CA   B ASN   B 1 159 ? 45.923 -40.762 -8.238  0.50 19.85 ?  159 ASN   B CA   1 
ATOM   6445 C  C    A ASN   B 1 159 ? 44.744 -40.142 -7.481  0.50 18.73 ?  159 ASN   B C    1 
ATOM   6446 C  C    B ASN   B 1 159 ? 44.728 -40.102 -7.549  0.50 19.00 ?  159 ASN   B C    1 
ATOM   6447 O  O    A ASN   B 1 159 ? 43.621 -40.657 -7.560  0.50 19.15 ?  159 ASN   B O    1 
ATOM   6448 O  O    B ASN   B 1 159 ? 43.595 -40.586 -7.667  0.50 19.25 ?  159 ASN   B O    1 
ATOM   6449 C  CB   A ASN   B 1 159 ? 46.649 -41.775 -7.187  0.50 20.69 ?  159 ASN   B CB   1 
ATOM   6450 C  CB   B ASN   B 1 159 ? 46.639 -41.752 -7.320  0.50 21.04 ?  159 ASN   B CB   1 
ATOM   6451 C  CG   A ASN   B 1 159 ? 47.652 -42.665 -7.893  0.50 22.31 ?  159 ASN   B CG   1 
ATOM   6452 C  CG   B ASN   B 1 159 ? 47.679 -42.575 -8.058  0.50 22.45 ?  159 ASN   B CG   1 
ATOM   6453 O  OD1  A ASN   B 1 159 ? 47.374 -43.204 -8.969  0.50 22.82 ?  159 ASN   B OD1  1 
ATOM   6454 O  OD1  B ASN   B 1 159 ? 47.452 -43.006 -9.191  0.50 23.00 ?  159 ASN   B OD1  1 
ATOM   6455 N  ND2  A ASN   B 1 159 ? 48.827 -42.824 -7.294  0.50 22.96 ?  159 ASN   B ND2  1 
ATOM   6456 N  ND2  B ASN   B 1 159 ? 48.827 -42.792 -7.423  0.50 22.96 ?  159 ASN   B ND2  1 
ATOM   6457 H  H    A ASN   B 1 159 ? 47.645 -39.807 -8.256  0.50 22.54 ?  159 ASN   B H    1 
ATOM   6458 H  H    B ASN   B 1 159 ? 47.608 -39.718 -8.296  0.50 23.47 ?  159 ASN   B H    1 
ATOM   6459 H  HA   A ASN   B 1 159 ? 45.606 -41.344 -8.887  0.50 23.15 ?  159 ASN   B HA   1 
ATOM   6460 H  HA   B ASN   B 1 159 ? 45.586 -41.265 -8.997  0.50 23.83 ?  159 ASN   B HA   1 
ATOM   6461 H  HB2  A ASN   B 1 159 ? 47.121 -41.262 -6.515  0.50 24.84 ?  159 ASN   B HB2  1 
ATOM   6462 H  HB2  B ASN   B 1 159 ? 47.090 -41.266 -6.614  0.50 25.26 ?  159 ASN   B HB2  1 
ATOM   6463 H  HB3  A ASN   B 1 159 ? 45.988 -42.347 -6.772  0.50 24.84 ?  159 ASN   B HB3  1 
ATOM   6464 H  HB3  B ASN   B 1 159 ? 45.988 -42.364 -6.944  0.50 25.26 ?  159 ASN   B HB3  1 
ATOM   6465 H  HD21 A ASN   B 1 159 ? 49.432 -43.319 -7.657  0.50 27.56 ?  159 ASN   B HD21 1 
ATOM   6466 H  HD21 B ASN   B 1 159 ? 49.450 -43.255 -7.799  0.50 27.56 ?  159 ASN   B HD21 1 
ATOM   6467 H  HD22 A ASN   B 1 159 ? 48.982 -42.443 -6.539  0.50 27.56 ?  159 ASN   B HD22 1 
ATOM   6468 H  HD22 B ASN   B 1 159 ? 48.948 -42.480 -6.631  0.50 27.56 ?  159 ASN   B HD22 1 
ATOM   6469 N  N    . LEU   B 1 160 ? 44.947 -38.987 -6.843  1.00 18.37 ?  160 LEU   B N    1 
ATOM   6470 C  CA   . LEU   B 1 160 ? 43.816 -38.259 -6.280  1.00 17.32 ?  160 LEU   B CA   1 
ATOM   6471 C  C    . LEU   B 1 160 ? 43.021 -37.587 -7.384  1.00 16.60 ?  160 LEU   B C    1 
ATOM   6472 O  O    . LEU   B 1 160 ? 41.786 -37.594 -7.358  1.00 16.22 ?  160 LEU   B O    1 
ATOM   6473 C  CB   . LEU   B 1 160 ? 44.278 -37.236 -5.246  1.00 16.78 ?  160 LEU   B CB   1 
ATOM   6474 C  CG   . LEU   B 1 160 ? 43.156 -36.336 -4.711  1.00 16.74 ?  160 LEU   B CG   1 
ATOM   6475 C  CD1  . LEU   B 1 160 ? 42.037 -37.161 -4.086  1.00 17.26 ?  160 LEU   B CD1  1 
ATOM   6476 C  CD2  . LEU   B 1 160 ? 43.701 -35.334 -3.711  1.00 17.17 ?  160 LEU   B CD2  1 
ATOM   6477 H  H    A LEU   B 1 160 ? 45.715 -38.615 -6.732  0.50 22.06 ?  160 LEU   B H    1 
ATOM   6478 H  H    B LEU   B 1 160 ? 45.720 -38.644 -6.688  0.50 22.06 ?  160 LEU   B H    1 
ATOM   6479 H  HA   . LEU   B 1 160 ? 43.230 -38.890 -5.842  1.00 20.79 ?  160 LEU   B HA   1 
ATOM   6480 H  HB2  . LEU   B 1 160 ? 44.667 -37.717 -4.496  1.00 20.15 ?  160 LEU   B HB2  1 
ATOM   6481 H  HB3  . LEU   B 1 160 ? 44.954 -36.668 -5.652  1.00 20.15 ?  160 LEU   B HB3  1 
ATOM   6482 H  HG   . LEU   B 1 160 ? 42.778 -35.837 -5.448  1.00 20.10 ?  160 LEU   B HG   1 
ATOM   6483 H  HD11 . LEU   B 1 160 ? 41.401 -36.561 -3.670  1.00 20.73 ?  160 LEU   B HD11 1 
ATOM   6484 H  HD12 . LEU   B 1 160 ? 41.595 -37.680 -4.779  1.00 20.73 ?  160 LEU   B HD12 1 
ATOM   6485 H  HD13 . LEU   B 1 160 ? 42.415 -37.758 -3.419  1.00 20.73 ?  160 LEU   B HD13 1 
ATOM   6486 H  HD21 . LEU   B 1 160 ? 42.975 -34.768 -3.412  1.00 20.62 ?  160 LEU   B HD21 1 
ATOM   6487 H  HD22 . LEU   B 1 160 ? 44.082 -35.814 -2.960  1.00 20.62 ?  160 LEU   B HD22 1 
ATOM   6488 H  HD23 . LEU   B 1 160 ? 44.384 -34.799 -4.145  1.00 20.62 ?  160 LEU   B HD23 1 
ATOM   6489 N  N    . TYR   B 1 161 ? 43.715 -37.014 -8.371  1.00 16.79 ?  161 TYR   B N    1 
ATOM   6490 C  CA   . TYR   B 1 161 ? 43.045 -36.447 -9.536  1.00 16.54 ?  161 TYR   B CA   1 
ATOM   6491 C  C    . TYR   B 1 161 ? 42.102 -37.465 -10.162 1.00 16.46 ?  161 TYR   B C    1 
ATOM   6492 O  O    . TYR   B 1 161 ? 40.933 -37.166 -10.431 1.00 16.25 ?  161 TYR   B O    1 
ATOM   6493 C  CB   . TYR   B 1 161 ? 44.090 -35.972 -10.553 1.00 17.12 ?  161 TYR   B CB   1 
ATOM   6494 C  CG   . TYR   B 1 161 ? 43.511 -35.505 -11.869 1.00 17.65 ?  161 TYR   B CG   1 
ATOM   6495 C  CD1  . TYR   B 1 161 ? 43.119 -34.184 -12.041 1.00 17.71 ?  161 TYR   B CD1  1 
ATOM   6496 C  CD2  . TYR   B 1 161 ? 43.345 -36.381 -12.936 1.00 18.20 ?  161 TYR   B CD2  1 
ATOM   6497 C  CE1  . TYR   B 1 161 ? 42.584 -33.748 -13.230 1.00 18.79 ?  161 TYR   B CE1  1 
ATOM   6498 C  CE2  . TYR   B 1 161 ? 42.803 -35.953 -14.130 1.00 19.41 ?  161 TYR   B CE2  1 
ATOM   6499 C  CZ   . TYR   B 1 161 ? 42.427 -34.634 -14.272 1.00 19.61 ?  161 TYR   B CZ   1 
ATOM   6500 O  OH   . TYR   B 1 161 ? 41.887 -34.195 -15.458 1.00 21.50 ?  161 TYR   B OH   1 
ATOM   6501 H  H    . TYR   B 1 161 ? 44.569 -36.943 -8.395  1.00 20.16 ?  161 TYR   B H    1 
ATOM   6502 H  HA   . TYR   B 1 161 ? 42.519 -35.678 -9.267  1.00 19.86 ?  161 TYR   B HA   1 
ATOM   6503 H  HB2  . TYR   B 1 161 ? 44.582 -35.227 -10.172 1.00 20.56 ?  161 TYR   B HB2  1 
ATOM   6504 H  HB3  . TYR   B 1 161 ? 44.697 -36.702 -10.746 1.00 20.56 ?  161 TYR   B HB3  1 
ATOM   6505 H  HD1  . TYR   B 1 161 ? 43.224 -33.576 -11.343 1.00 21.26 ?  161 TYR   B HD1  1 
ATOM   6506 H  HD2  . TYR   B 1 161 ? 43.592 -37.273 -12.845 1.00 21.86 ?  161 TYR   B HD2  1 
ATOM   6507 H  HE1  . TYR   B 1 161 ? 42.328 -32.855 -13.328 1.00 22.56 ?  161 TYR   B HE1  1 
ATOM   6508 H  HE2  . TYR   B 1 161 ? 42.693 -36.548 -14.838 1.00 23.31 ?  161 TYR   B HE2  1 
ATOM   6509 H  HH   . TYR   B 1 161 ? 41.847 -34.833 -16.006 1.00 25.81 ?  161 TYR   B HH   1 
ATOM   6510 N  N    . ASP   B 1 162 ? 42.597 -38.683 -10.393 1.00 17.09 ?  162 ASP   B N    1 
ATOM   6511 C  CA   . ASP   B 1 162 ? 41.772 -39.720 -11.004 1.00 17.36 ?  162 ASP   B CA   1 
ATOM   6512 C  C    . ASP   B 1 162 ? 40.562 -40.055 -10.136 1.00 16.70 ?  162 ASP   B C    1 
ATOM   6513 O  O    . ASP   B 1 162 ? 39.458 -40.271 -10.651 1.00 17.44 ?  162 ASP   B O    1 
ATOM   6514 C  CB   . ASP   B 1 162 ? 42.606 -40.983 -11.249 1.00 18.74 ?  162 ASP   B CB   1 
ATOM   6515 C  CG   . ASP   B 1 162 ? 43.604 -40.831 -12.385 1.00 20.24 ?  162 ASP   B CG   1 
ATOM   6516 O  OD1  . ASP   B 1 162 ? 43.472 -39.893 -13.191 1.00 20.15 ?  162 ASP   B OD1  1 
ATOM   6517 O  OD2  . ASP   B 1 162 ? 44.510 -41.687 -12.488 1.00 22.02 -1 162 ASP   B OD2  1 
ATOM   6518 H  H    . ASP   B 1 162 ? 43.395 -38.927 -10.206 1.00 20.52 ?  162 ASP   B H    1 
ATOM   6519 H  HA   . ASP   B 1 162 ? 41.441 -39.403 -11.858 1.00 20.84 ?  162 ASP   B HA   1 
ATOM   6520 H  HB2  . ASP   B 1 162 ? 43.108 -41.188 -10.448 1.00 22.50 ?  162 ASP   B HB2  1 
ATOM   6521 H  HB3  . ASP   B 1 162 ? 42.011 -41.714 -11.470 1.00 22.50 ?  162 ASP   B HB3  1 
ATOM   6522 N  N    . LYS   B 1 163 ? 40.753 -40.133 -8.817  1.00 16.33 ?  163 LYS   B N    1 
ATOM   6523 C  CA   . LYS   B 1 163 ? 39.631 -40.413 -7.925  1.00 17.26 ?  163 LYS   B CA   1 
ATOM   6524 C  C    . LYS   B 1 163 ? 38.585 -39.306 -7.988  1.00 15.85 ?  163 LYS   B C    1 
ATOM   6525 O  O    . LYS   B 1 163 ? 37.377 -39.578 -7.989  1.00 16.64 ?  163 LYS   B O    1 
ATOM   6526 C  CB   . LYS   B 1 163 ? 40.126 -40.592 -6.491  1.00 20.65 ?  163 LYS   B CB   1 
ATOM   6527 C  CG   . LYS   B 1 163 ? 39.045 -41.085 -5.555  1.00 26.69 ?  163 LYS   B CG   1 
ATOM   6528 C  CD   . LYS   B 1 163 ? 39.536 -41.260 -4.131  1.00 33.03 ?  163 LYS   B CD   1 
ATOM   6529 C  CE   . LYS   B 1 163 ? 38.458 -41.915 -3.276  1.00 37.98 ?  163 LYS   B CE   1 
ATOM   6530 N  NZ   . LYS   B 1 163 ? 38.643 -41.651 -1.822  1.00 41.16 ?  163 LYS   B NZ   1 
ATOM   6531 H  H    . LYS   B 1 163 ? 41.513 -40.032 -8.423  1.00 19.61 ?  163 LYS   B H    1 
ATOM   6532 H  HA   . LYS   B 1 163 ? 39.211 -41.243 -8.202  1.00 20.72 ?  163 LYS   B HA   1 
ATOM   6533 H  HB2  . LYS   B 1 163 ? 40.849 -41.241 -6.483  1.00 24.79 ?  163 LYS   B HB2  1 
ATOM   6534 H  HB3  . LYS   B 1 163 ? 40.446 -39.739 -6.158  1.00 24.79 ?  163 LYS   B HB3  1 
ATOM   6535 H  HG2  . LYS   B 1 163 ? 38.319 -40.444 -5.544  1.00 32.04 ?  163 LYS   B HG2  1 
ATOM   6536 H  HG3  . LYS   B 1 163 ? 38.724 -41.946 -5.870  1.00 32.04 ?  163 LYS   B HG3  1 
ATOM   6537 H  HD2  . LYS   B 1 163 ? 40.321 -41.832 -4.127  1.00 39.65 ?  163 LYS   B HD2  1 
ATOM   6538 H  HD3  . LYS   B 1 163 ? 39.746 -40.393 -3.752  1.00 39.65 ?  163 LYS   B HD3  1 
ATOM   6539 H  HE2  . LYS   B 1 163 ? 37.588 -41.579 -3.541  1.00 45.60 ?  163 LYS   B HE2  1 
ATOM   6540 H  HE3  . LYS   B 1 163 ? 38.492 -42.875 -3.412  1.00 45.60 ?  163 LYS   B HE3  1 
ATOM   6541 H  HZ1  . LYS   B 1 163 ? 37.996 -42.047 -1.357  1.00 49.40 ?  163 LYS   B HZ1  1 
ATOM   6542 H  HZ2  . LYS   B 1 163 ? 39.429 -41.969 -1.554  1.00 49.40 ?  163 LYS   B HZ2  1 
ATOM   6543 H  HZ3  . LYS   B 1 163 ? 38.617 -40.775 -1.667  1.00 49.40 ?  163 LYS   B HZ3  1 
ATOM   6544 N  N    . LEU   B 1 164 ? 39.038 -38.054 -8.044  1.00 14.79 ?  164 LEU   B N    1 
ATOM   6545 C  CA   . LEU   B 1 164 ? 38.132 -36.911 -8.101  1.00 14.32 ?  164 LEU   B CA   1 
ATOM   6546 C  C    . LEU   B 1 164 ? 37.348 -36.894 -9.408  1.00 14.51 ?  164 LEU   B C    1 
ATOM   6547 O  O    . LEU   B 1 164 ? 36.125 -36.703 -9.404  1.00 15.48 ?  164 LEU   B O    1 
ATOM   6548 C  CB   . LEU   B 1 164 ? 38.935 -35.620 -7.940  1.00 13.91 ?  164 LEU   B CB   1 
ATOM   6549 C  CG   . LEU   B 1 164 ? 39.460 -35.343 -6.533  1.00 14.47 ?  164 LEU   B CG   1 
ATOM   6550 C  CD1  . LEU   B 1 164 ? 40.560 -34.292 -6.581  1.00 14.64 ?  164 LEU   B CD1  1 
ATOM   6551 C  CD2  . LEU   B 1 164 ? 38.348 -34.898 -5.608  1.00 16.18 ?  164 LEU   B CD2  1 
ATOM   6552 H  H    . LEU   B 1 164 ? 39.875 -37.839 -8.060  1.00 17.76 ?  164 LEU   B H    1 
ATOM   6553 H  HA   . LEU   B 1 164 ? 37.503 -36.969 -7.375  1.00 17.20 ?  164 LEU   B HA   1 
ATOM   6554 H  HB2  . LEU   B 1 164 ? 39.707 -35.659 -8.535  1.00 16.70 ?  164 LEU   B HB2  1 
ATOM   6555 H  HB3  . LEU   B 1 164 ? 38.376 -34.873 -8.195  1.00 16.70 ?  164 LEU   B HB3  1 
ATOM   6556 H  HG   . LEU   B 1 164 ? 39.848 -36.153 -6.178  1.00 17.38 ?  164 LEU   B HG   1 
ATOM   6557 H  HD11 . LEU   B 1 164 ? 40.877 -34.121 -5.679  1.00 17.59 ?  164 LEU   B HD11 1 
ATOM   6558 H  HD12 . LEU   B 1 164 ? 41.296 -34.621 -7.128  1.00 17.59 ?  164 LEU   B HD12 1 
ATOM   6559 H  HD13 . LEU   B 1 164 ? 40.209 -33.473 -6.967  1.00 17.59 ?  164 LEU   B HD13 1 
ATOM   6560 H  HD21 . LEU   B 1 164 ? 38.724 -34.681 -4.741  1.00 19.42 ?  164 LEU   B HD21 1 
ATOM   6561 H  HD22 . LEU   B 1 164 ? 37.912 -34.117 -5.984  1.00 19.42 ?  164 LEU   B HD22 1 
ATOM   6562 H  HD23 . LEU   B 1 164 ? 37.708 -35.622 -5.518  1.00 19.42 ?  164 LEU   B HD23 1 
ATOM   6563 N  N    . VAL   B 1 165 ? 38.036 -37.068 -10.539 1.00 16.09 ?  165 VAL   B N    1 
ATOM   6564 C  CA   . VAL   B 1 165 ? 37.375 -37.001 -11.838 1.00 17.38 ?  165 VAL   B CA   1 
ATOM   6565 C  C    . VAL   B 1 165 ? 36.452 -38.198 -12.021 1.00 18.99 ?  165 VAL   B C    1 
ATOM   6566 O  O    . VAL   B 1 165 ? 35.289 -38.059 -12.422 1.00 19.95 ?  165 VAL   B O    1 
ATOM   6567 C  CB   . VAL   B 1 165 ? 38.420 -36.922 -12.967 1.00 18.25 ?  165 VAL   B CB   1 
ATOM   6568 C  CG1  . VAL   B 1 165 ? 37.756 -37.025 -14.320 1.00 19.60 ?  165 VAL   B CG1  1 
ATOM   6569 C  CG2  . VAL   B 1 165 ? 39.222 -35.643 -12.864 1.00 17.88 ?  165 VAL   B CG2  1 
ATOM   6570 H  H    . VAL   B 1 165 ? 38.886 -37.211 -10.581 1.00 19.32 ?  165 VAL   B H    1 
ATOM   6571 H  HA   . VAL   B 1 165 ? 36.835 -36.199 -11.881 1.00 20.87 ?  165 VAL   B HA   1 
ATOM   6572 H  HB   . VAL   B 1 165 ? 39.039 -37.663 -12.880 1.00 21.92 ?  165 VAL   B HB   1 
ATOM   6573 H  HG11 . VAL   B 1 165 ? 38.377 -36.732 -15.001 1.00 23.54 ?  165 VAL   B HG11 1 
ATOM   6574 H  HG12 . VAL   B 1 165 ? 37.515 -37.954 -14.478 1.00 23.54 ?  165 VAL   B HG12 1 
ATOM   6575 H  HG13 . VAL   B 1 165 ? 36.963 -36.472 -14.327 1.00 23.54 ?  165 VAL   B HG13 1 
ATOM   6576 H  HG21 . VAL   B 1 165 ? 39.855 -35.602 -13.599 1.00 21.46 ?  165 VAL   B HG21 1 
ATOM   6577 H  HG22 . VAL   B 1 165 ? 38.616 -34.884 -12.912 1.00 21.46 ?  165 VAL   B HG22 1 
ATOM   6578 H  HG23 . VAL   B 1 165 ? 39.697 -35.630 -12.019 1.00 21.46 ?  165 VAL   B HG23 1 
ATOM   6579 N  N    . SER   B 1 166 ? 36.964 -39.397 -11.725 1.00 19.72 ?  166 SER   B N    1 
ATOM   6580 C  CA   . SER   B 1 166 ? 36.213 -40.612 -12.006 1.00 21.04 ?  166 SER   B CA   1 
ATOM   6581 C  C    . SER   B 1 166 ? 34.957 -40.707 -11.153 1.00 21.28 ?  166 SER   B C    1 
ATOM   6582 O  O    . SER   B 1 166 ? 33.984 -41.336 -11.572 1.00 22.90 ?  166 SER   B O    1 
ATOM   6583 C  CB   . SER   B 1 166 ? 37.087 -41.862 -11.833 1.00 22.14 ?  166 SER   B CB   1 
ATOM   6584 O  OG   . SER   B 1 166 ? 37.433 -42.081 -10.476 1.00 21.89 ?  166 SER   B OG   1 
ATOM   6585 H  H    . SER   B 1 166 ? 37.741 -39.530 -11.374 1.00 23.68 ?  166 SER   B H    1 
ATOM   6586 H  HA   . SER   B 1 166 ? 35.934 -40.590 -12.933 1.00 25.26 ?  166 SER   B HA   1 
ATOM   6587 H  HB2  . SER   B 1 166 ? 36.598 -42.634 -12.158 1.00 26.58 ?  166 SER   B HB2  1 
ATOM   6588 H  HB3  . SER   B 1 166 ? 37.902 -41.750 -12.350 1.00 26.58 ?  166 SER   B HB3  1 
ATOM   6589 H  HG   . SER   B 1 166 ? 37.867 -41.425 -10.182 1.00 26.28 ?  166 SER   B HG   1 
ATOM   6590 N  N    . SER   B 1 167 ? 34.946 -40.098 -9.968  1.00 19.94 ?  167 SER   B N    1 
ATOM   6591 C  CA   . SER   B 1 167 ? 33.790 -40.153 -9.081  1.00 19.62 ?  167 SER   B CA   1 
ATOM   6592 C  C    . SER   B 1 167 ? 32.872 -38.935 -9.182  1.00 19.27 ?  167 SER   B C    1 
ATOM   6593 O  O    . SER   B 1 167 ? 31.796 -38.938 -8.572  1.00 19.27 ?  167 SER   B O    1 
ATOM   6594 C  CB   . SER   B 1 167 ? 34.234 -40.336 -7.624  1.00 19.41 ?  167 SER   B CB   1 
ATOM   6595 O  OG   . SER   B 1 167 ? 34.906 -39.178 -7.152  1.00 18.87 ?  167 SER   B OG   1 
ATOM   6596 H  H    . SER   B 1 167 ? 35.605 -39.654 -9.652  1.00 23.94 ?  167 SER   B H    1 
ATOM   6597 H  HA   . SER   B 1 167 ? 33.260 -40.934 -9.320  1.00 23.56 ?  167 SER   B HA   1 
ATOM   6598 H  HB2  . SER   B 1 167 ? 33.449 -40.501 -7.076  1.00 23.30 ?  167 SER   B HB2  1 
ATOM   6599 H  HB3  . SER   B 1 167 ? 34.832 -41.104 -7.573  1.00 23.30 ?  167 SER   B HB3  1 
ATOM   6600 H  HG   . SER   B 1 167 ? 35.587 -39.041 -7.622  1.00 22.66 ?  167 SER   B HG   1 
ATOM   6601 N  N    . PHE   B 1 168 ? 33.247 -37.900 -9.934  1.00 18.94 ?  168 PHE   B N    1 
ATOM   6602 C  CA   . PHE   B 1 168 ? 32.411 -36.700 -9.990  1.00 18.25 ?  168 PHE   B CA   1 
ATOM   6603 C  C    . PHE   B 1 168 ? 31.095 -36.964 -10.719 1.00 16.20 ?  168 PHE   B C    1 
ATOM   6604 O  O    . PHE   B 1 168 ? 30.052 -36.372 -10.377 1.00 17.00 ?  168 PHE   B O    1 
ATOM   6605 C  CB   . PHE   B 1 168 ? 33.169 -35.558 -10.663 1.00 18.72 ?  168 PHE   B CB   1 
ATOM   6606 C  CG   . PHE   B 1 168 ? 32.363 -34.310 -10.790 1.00 18.43 ?  168 PHE   B CG   1 
ATOM   6607 C  CD1  . PHE   B 1 168 ? 32.038 -33.573 -9.662  1.00 19.49 ?  168 PHE   B CD1  1 
ATOM   6608 C  CD2  . PHE   B 1 168 ? 31.914 -33.881 -12.021 1.00 17.81 ?  168 PHE   B CD2  1 
ATOM   6609 C  CE1  . PHE   B 1 168 ? 31.275 -32.428 -9.757  1.00 19.99 ?  168 PHE   B CE1  1 
ATOM   6610 C  CE2  . PHE   B 1 168 ? 31.164 -32.717 -12.131 1.00 19.02 ?  168 PHE   B CE2  1 
ATOM   6611 C  CZ   . PHE   B 1 168 ? 30.839 -31.993 -10.993 1.00 19.33 ?  168 PHE   B CZ   1 
ATOM   6612 H  H    . PHE   B 1 168 ? 33.968 -37.868 -10.404 1.00 22.75 ?  168 PHE   B H    1 
ATOM   6613 H  HA   . PHE   B 1 168 ? 32.196 -36.428 -9.089  1.00 21.92 ?  168 PHE   B HA   1 
ATOM   6614 H  HB2  . PHE   B 1 168 ? 33.955 -35.352 -10.134 1.00 22.47 ?  168 PHE   B HB2  1 
ATOM   6615 H  HB3  . PHE   B 1 168 ? 33.433 -35.834 -11.553 1.00 22.47 ?  168 PHE   B HB3  1 
ATOM   6616 H  HD1  . PHE   B 1 168 ? 32.327 -33.870 -8.827  1.00 23.40 ?  168 PHE   B HD1  1 
ATOM   6617 H  HD2  . PHE   B 1 168 ? 32.131 -34.364 -12.784 1.00 21.38 ?  168 PHE   B HD2  1 
ATOM   6618 H  HE1  . PHE   B 1 168 ? 31.065 -31.946 -8.992  1.00 24.01 ?  168 PHE   B HE1  1 
ATOM   6619 H  HE2  . PHE   B 1 168 ? 30.864 -32.434 -12.966 1.00 22.84 ?  168 PHE   B HE2  1 
ATOM   6620 H  HZ   . PHE   B 1 168 ? 30.328 -31.220 -11.066 1.00 23.21 ?  168 PHE   B HZ   1 
ATOM   6621 N  N    . LEU   B 1 169 ? 31.128 -37.842 -11.718 1.00 16.34 ?  169 LEU   B N    1 
ATOM   6622 C  CA   . LEU   B 1 169 ? 29.950 -38.162 -12.518 1.00 18.53 ?  169 LEU   B CA   1 
ATOM   6623 C  C    . LEU   B 1 169 ? 29.946 -39.601 -13.017 1.00 21.25 ?  169 LEU   B C    1 
ATOM   6624 O  O    . LEU   B 1 169 ? 29.040 -40.010 -13.747 1.00 23.94 ?  169 LEU   B O    1 
ATOM   6625 C  CB   . LEU   B 1 169 ? 29.869 -37.219 -13.719 1.00 20.44 ?  169 LEU   B CB   1 
ATOM   6626 C  CG   . LEU   B 1 169 ? 28.615 -36.350 -13.809 1.00 23.72 ?  169 LEU   B CG   1 
ATOM   6627 C  CD1  . LEU   B 1 169 ? 28.560 -35.675 -15.162 1.00 24.81 ?  169 LEU   B CD1  1 
ATOM   6628 C  CD2  . LEU   B 1 169 ? 27.353 -37.160 -13.562 1.00 24.15 ?  169 LEU   B CD2  1 
ATOM   6629 O  OXT  . LEU   B 1 169 ? 30.852 -40.367 -12.710 1.00 22.09 -1 169 LEU   B OXT  1 
ATOM   6630 H  H    . LEU   B 1 169 ? 31.835 -38.272 -11.967 1.00 19.63 ?  169 LEU   B H    1 
ATOM   6631 H  HA   . LEU   B 1 169 ? 29.165 -38.030 -11.971 1.00 22.25 ?  169 LEU   B HA   1 
ATOM   6632 H  HB2  . LEU   B 1 169 ? 30.631 -36.619 -13.695 1.00 24.54 ?  169 LEU   B HB2  1 
ATOM   6633 H  HB3  . LEU   B 1 169 ? 29.905 -37.750 -14.532 1.00 24.54 ?  169 LEU   B HB3  1 
ATOM   6634 H  HG   . LEU   B 1 169 ? 28.662 -35.655 -13.133 1.00 28.48 ?  169 LEU   B HG   1 
ATOM   6635 H  HD11 . LEU   B 1 169 ? 27.777 -35.104 -15.198 1.00 29.79 ?  169 LEU   B HD11 1 
ATOM   6636 H  HD12 . LEU   B 1 169 ? 29.363 -35.144 -15.281 1.00 29.79 ?  169 LEU   B HD12 1 
ATOM   6637 H  HD13 . LEU   B 1 169 ? 28.507 -36.356 -15.850 1.00 29.79 ?  169 LEU   B HD13 1 
ATOM   6638 H  HD21 . LEU   B 1 169 ? 26.603 -36.719 -13.986 1.00 28.99 ?  169 LEU   B HD21 1 
ATOM   6639 H  HD22 . LEU   B 1 169 ? 27.473 -38.048 -13.938 1.00 28.99 ?  169 LEU   B HD22 1 
ATOM   6640 H  HD23 . LEU   B 1 169 ? 27.205 -37.225 -12.607 1.00 28.99 ?  169 LEU   B HD23 1 
HETATM 6641 N  N2   B A1A9Z C 2 .   ? 14.872 -0.175  3.950   0.25 12.40 ?  201 A1A9Z A N2   1 
HETATM 6642 C  C3   B A1A9Z C 2 .   ? 10.603 0.152   -1.581  0.25 15.28 ?  201 A1A9Z A C3   1 
HETATM 6643 C  C6   B A1A9Z C 2 .   ? 14.311 -0.228  -0.439  0.25 13.62 ?  201 A1A9Z A C6   1 
HETATM 6644 C  C9   B A1A9Z C 2 .   ? 15.074 0.933   3.153   0.25 11.72 ?  201 A1A9Z A C9   1 
HETATM 6645 C  C12  B A1A9Z C 2 .   ? 15.353 2.192   3.783   0.25 11.93 ?  201 A1A9Z A C12  1 
HETATM 6646 C  C14  B A1A9Z C 2 .   ? 15.806 4.266   4.646   0.25 12.62 ?  201 A1A9Z A C14  1 
HETATM 6647 C  C1   B A1A9Z C 2 .   ? 8.855  2.034   -1.479  0.25 15.95 ?  201 A1A9Z A C1   1 
HETATM 6648 C  C10  B A1A9Z C 2 .   ? 14.934 -0.051  5.315   0.25 12.29 ?  201 A1A9Z A C10  1 
HETATM 6649 C  C11  B A1A9Z C 2 .   ? 15.378 2.124   5.183   0.25 12.00 ?  201 A1A9Z A C11  1 
HETATM 6650 C  C13  B A1A9Z C 2 .   ? 15.630 3.562   3.469   0.25 12.54 ?  201 A1A9Z A C13  1 
HETATM 6651 C  C15  B A1A9Z C 2 .   ? 12.541 1.716   -0.312  0.25 15.35 ?  201 A1A9Z A C15  1 
HETATM 6652 C  C16  B A1A9Z C 2 .   ? 11.248 2.234   -0.561  0.25 16.05 ?  201 A1A9Z A C16  1 
HETATM 6653 C  C2   B A1A9Z C 2 .   ? 10.250 1.465   -1.205  0.25 15.67 ?  201 A1A9Z A C2   1 
HETATM 6654 C  C4   B A1A9Z C 2 .   ? 11.887 -0.367  -1.329  0.25 15.04 ?  201 A1A9Z A C4   1 
HETATM 6655 C  C5   B A1A9Z C 2 .   ? 12.895 0.391   -0.685  0.25 14.57 ?  201 A1A9Z A C5   1 
HETATM 6656 C  C7   B A1A9Z C 2 .   ? 14.763 -0.468  1.045   0.25 12.51 ?  201 A1A9Z A C7   1 
HETATM 6657 C  C8   B A1A9Z C 2 .   ? 16.064 -1.362  0.985   0.25 14.64 ?  201 A1A9Z A C8   1 
HETATM 6658 N  N1   B A1A9Z C 2 .   ? 15.007 0.784   1.768   0.25 11.72 ?  201 A1A9Z A N1   1 
HETATM 6659 N  N3   B A1A9Z C 2 .   ? 15.180 1.062   6.025   0.25 12.04 ?  201 A1A9Z A N3   1 
HETATM 6660 N  N4   B A1A9Z C 2 .   ? 15.656 3.382   5.775   0.25 12.53 ?  201 A1A9Z A N4   1 
HETATM 6661 O  O1   B A1A9Z C 2 .   ? 15.796 -2.504  0.243   0.25 16.18 ?  201 A1A9Z A O1   1 
HETATM 6662 H  H5   B A1A9Z C 2 .   ? 9.831  -0.487  -2.093  0.25 18.35 ?  201 A1A9Z A H5   1 
HETATM 6663 H  H7   B A1A9Z C 2 .   ? 15.099 0.380   -0.917  0.25 16.36 ?  201 A1A9Z A H7   1 
HETATM 6664 H  H8   B A1A9Z C 2 .   ? 14.402 -1.193  -0.987  0.25 16.36 ?  201 A1A9Z A H8   1 
HETATM 6665 H  H15  B A1A9Z C 2 .   ? 16.023 5.260   4.996   0.25 15.16 ?  201 A1A9Z A H15  1 
HETATM 6666 H  H3   B A1A9Z C 2 .   ? 8.149  1.353   -2.006  0.25 19.16 ?  201 A1A9Z A H3   1 
HETATM 6667 H  H4   B A1A9Z C 2 .   ? 8.838  2.950   -2.118  0.25 19.16 ?  201 A1A9Z A H4   1 
HETATM 6668 H  H2   B A1A9Z C 2 .   ? 8.288  2.350   -0.584  0.25 19.16 ?  201 A1A9Z A H2   1 
HETATM 6669 H  H13  B A1A9Z C 2 .   ? 14.755 -0.972  5.954   0.25 14.76 ?  201 A1A9Z A H13  1 
HETATM 6670 H  H14  B A1A9Z C 2 .   ? 15.707 4.067   2.513   0.25 15.06 ?  201 A1A9Z A H14  1 
HETATM 6671 H  H17  B A1A9Z C 2 .   ? 13.301 2.350   0.200   0.25 18.43 ?  201 A1A9Z A H17  1 
HETATM 6672 H  H18  B A1A9Z C 2 .   ? 11.008 3.277   -0.253  0.25 19.27 ?  201 A1A9Z A H18  1 
HETATM 6673 H  H6   B A1A9Z C 2 .   ? 12.120 -1.422  -1.645  0.25 18.06 ?  201 A1A9Z A H6   1 
HETATM 6674 H  H1   B A1A9Z C 2 .   ? 13.912 -1.049  1.498   0.25 15.02 ?  201 A1A9Z A H1   1 
HETATM 6675 H  H10  B A1A9Z C 2 .   ? 16.921 -0.756  0.589   0.25 17.59 ?  201 A1A9Z A H10  1 
HETATM 6676 H  H9   B A1A9Z C 2 .   ? 16.368 -1.643  2.016   0.25 17.59 ?  201 A1A9Z A H9   1 
HETATM 6677 H  H12  B A1A9Z C 2 .   ? 15.140 1.611   1.172   0.25 14.07 ?  201 A1A9Z A H12  1 
HETATM 6678 H  H16  B A1A9Z C 2 .   ? 15.727 3.617   6.670   0.25 15.05 ?  201 A1A9Z A H16  1 
HETATM 6679 H  H11  B A1A9Z C 2 .   ? 16.620 -2.945  -0.048  0.25 19.43 ?  201 A1A9Z A H11  1 
HETATM 6680 O  O1   C A1A9Y D 3 .   ? 15.750 -2.564  0.304   0.25 17.65 ?  202 A1A9Y A O1   1 
HETATM 6681 C  C1   C A1A9Y D 3 .   ? 9.334  2.249   -2.040  0.25 16.09 ?  202 A1A9Y A C1   1 
HETATM 6682 C  C2   C A1A9Y D 3 .   ? 10.417 1.463   -1.375  0.25 16.23 ?  202 A1A9Y A C2   1 
HETATM 6683 C  C3   C A1A9Y D 3 .   ? 10.655 0.138   -1.726  0.25 16.16 ?  202 A1A9Y A C3   1 
HETATM 6684 C  C4   C A1A9Y D 3 .   ? 11.660 -0.604  -1.113  0.25 16.33 ?  202 A1A9Y A C4   1 
HETATM 6685 C  C5   C A1A9Y D 3 .   ? 12.487 -0.068  -0.121  0.25 16.58 ?  202 A1A9Y A C5   1 
HETATM 6686 C  C6   C A1A9Y D 3 .   ? 13.569 -0.925  0.520   0.25 16.19 ?  202 A1A9Y A C6   1 
HETATM 6687 C  C7   C A1A9Y D 3 .   ? 15.014 -0.327  0.671   0.25 15.07 ?  202 A1A9Y A C7   1 
HETATM 6688 C  C8   C A1A9Y D 3 .   ? 16.011 -1.461  1.102   0.25 16.55 ?  202 A1A9Y A C8   1 
HETATM 6689 C  C10  C A1A9Y D 3 .   ? 14.912 -0.199  5.093   0.25 12.47 ?  202 A1A9Y A C10  1 
HETATM 6690 C  C11  C A1A9Y D 3 .   ? 15.377 2.016   5.126   0.25 11.84 ?  202 A1A9Y A C11  1 
HETATM 6691 C  C12  C A1A9Y D 3 .   ? 15.371 2.086   3.702   0.25 12.16 ?  202 A1A9Y A C12  1 
HETATM 6692 C  C13  C A1A9Y D 3 .   ? 15.657 3.460   3.397   0.25 12.33 ?  202 A1A9Y A C13  1 
HETATM 6693 C  C14  C A1A9Y D 3 .   ? 15.822 4.162   4.583   0.25 12.28 ?  202 A1A9Y A C14  1 
HETATM 6694 C  C15  C A1A9Y D 3 .   ? 12.239 1.273   0.227   0.25 16.71 ?  202 A1A9Y A C15  1 
HETATM 6695 C  C16  C A1A9Y D 3 .   ? 11.227 2.021   -0.386  0.25 16.51 ?  202 A1A9Y A C16  1 
HETATM 6696 C  C9   C A1A9Y D 3 .   ? 15.111 0.889   2.995   0.25 12.83 ?  202 A1A9Y A C9   1 
HETATM 6697 N  N1   C A1A9Y D 3 .   ? 15.082 0.855   1.592   0.25 13.50 ?  202 A1A9Y A N1   1 
HETATM 6698 N  N2   C A1A9Y D 3 .   ? 14.877 -0.265  3.710   0.25 13.40 ?  202 A1A9Y A N2   1 
HETATM 6699 N  N3   C A1A9Y D 3 .   ? 15.151 0.881   5.864   0.25 11.73 ?  202 A1A9Y A N3   1 
HETATM 6700 N  N4   C A1A9Y D 3 .   ? 15.649 3.270   5.642   0.25 12.07 ?  202 A1A9Y A N4   1 
HETATM 6701 H  H11  C A1A9Y D 3 .   ? 16.452 -3.198  0.474   0.25 21.19 ?  202 A1A9Y A H11  1 
HETATM 6702 H  H2   C A1A9Y D 3 .   ? 8.693  1.652   -2.710  0.25 19.33 ?  202 A1A9Y A H2   1 
HETATM 6703 H  H4   C A1A9Y D 3 .   ? 9.725  3.061   -2.673  0.25 19.33 ?  202 A1A9Y A H4   1 
HETATM 6704 H  H3   C A1A9Y D 3 .   ? 8.636  2.742   -1.343  0.25 19.33 ?  202 A1A9Y A H3   1 
HETATM 6705 H  H5   C A1A9Y D 3 .   ? 10.034 -0.324  -2.491  0.25 19.41 ?  202 A1A9Y A H5   1 
HETATM 6706 H  H6   C A1A9Y D 3 .   ? 11.796 -1.631  -1.431  0.25 19.60 ?  202 A1A9Y A H6   1 
HETATM 6707 H  H8   C A1A9Y D 3 .   ? 13.616 -1.871  -0.063  0.25 19.44 ?  202 A1A9Y A H8   1 
HETATM 6708 H  H7   C A1A9Y D 3 .   ? 13.213 -1.277  1.499   0.25 19.44 ?  202 A1A9Y A H7   1 
HETATM 6709 H  H1   C A1A9Y D 3 .   ? 15.334 0.005   -0.348  0.25 18.10 ?  202 A1A9Y A H1   1 
HETATM 6710 H  H10  C A1A9Y D 3 .   ? 17.068 -1.122  0.980   0.25 19.87 ?  202 A1A9Y A H10  1 
HETATM 6711 H  H9   C A1A9Y D 3 .   ? 15.913 -1.705  2.172   0.25 19.87 ?  202 A1A9Y A H9   1 
HETATM 6712 H  H13  C A1A9Y D 3 .   ? 14.724 -1.119  5.643   0.25 14.98 ?  202 A1A9Y A H13  1 
HETATM 6713 H  H14  C A1A9Y D 3 .   ? 15.737 3.909   2.415   0.25 14.81 ?  202 A1A9Y A H14  1 
HETATM 6714 H  H15  C A1A9Y D 3 .   ? 16.042 5.201   4.762   0.25 14.75 ?  202 A1A9Y A H15  1 
HETATM 6715 H  H17  C A1A9Y D 3 .   ? 12.843 1.770   0.984   0.25 20.06 ?  202 A1A9Y A H17  1 
HETATM 6716 H  H18  C A1A9Y D 3 .   ? 11.065 3.064   -0.098  0.25 19.83 ?  202 A1A9Y A H18  1 
HETATM 6717 H  H12  C A1A9Y D 3 .   ? 15.111 1.763   1.162   0.25 16.21 ?  202 A1A9Y A H12  1 
HETATM 6718 H  H16  C A1A9Y D 3 .   ? 15.707 3.487   6.633   0.25 14.50 ?  202 A1A9Y A H16  1 
HETATM 6719 CL CL   B CL    E 4 .   ? 16.016 2.773   -0.903  0.50 18.04 ?  203 CL    A CL   1 
HETATM 6720 O  O    . HOH   F 5 .   ? 14.800 -4.577  20.560  1.00 44.68 ?  301 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 5 .   ? 10.927 -0.765  2.094   1.00 26.62 ?  302 HOH   A O    1 
HETATM 6722 O  O    . HOH   F 5 .   ? 28.920 0.425   -9.732  1.00 21.90 ?  303 HOH   A O    1 
HETATM 6723 O  O    . HOH   F 5 .   ? 34.368 -1.893  12.490  1.00 36.30 ?  304 HOH   A O    1 
HETATM 6724 O  O    . HOH   F 5 .   ? 17.159 -18.047 15.015  1.00 28.32 ?  305 HOH   A O    1 
HETATM 6725 O  O    . HOH   F 5 .   ? 14.742 -13.974 16.700  1.00 24.92 ?  306 HOH   A O    1 
HETATM 6726 O  O    . HOH   F 5 .   ? 18.599 -2.378  -16.452 1.00 45.36 ?  307 HOH   A O    1 
HETATM 6727 O  O    . HOH   F 5 .   ? 15.960 2.168   24.715  1.00 50.30 ?  308 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 5 .   ? 23.942 -15.756 -9.181  1.00 35.94 ?  309 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 5 .   ? 4.617  3.913   0.706   1.00 23.92 ?  310 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 11.986 0.409   14.752  1.00 39.05 ?  311 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 7.969  -12.705 -0.855  1.00 23.19 ?  312 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 15.066 -12.193 18.685  1.00 40.78 ?  313 HOH   A O    1 
HETATM 6733 O  O    A HOH   F 5 .   ? 3.623  -9.470  9.751   0.50 32.70 ?  314 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 18.911 -21.988 6.909   1.00 31.65 ?  315 HOH   A O    1 
HETATM 6735 O  O    A HOH   F 5 .   ? 17.509 -1.719  0.448   0.50 17.00 ?  316 HOH   A O    1 
HETATM 6736 O  O    A HOH   F 5 .   ? 6.975  -8.168  11.865  0.50 16.08 ?  317 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 28.593 -10.624 -14.018 1.00 43.96 ?  318 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 30.243 -13.318 -8.501  1.00 21.69 ?  319 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 42.458 10.549  5.156   1.00 20.31 ?  320 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? 13.547 -15.276 -7.496  1.00 29.43 ?  321 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 14.159 -4.504  -11.868 1.00 35.16 ?  322 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 9.882  -21.378 5.708   1.00 18.87 ?  323 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 26.852 11.441  1.663   1.00 16.05 ?  324 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 28.326 -6.311  19.613  1.00 44.29 ?  325 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 15.163 4.069   17.596  1.00 43.38 ?  326 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 0.789  -4.645  0.111   1.00 32.72 ?  327 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 33.971 -1.062  -8.936  1.00 26.28 ?  328 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 15.268 -8.060  -9.847  1.00 26.45 ?  329 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 36.269 -5.098  -0.509  1.00 29.32 ?  330 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 27.303 13.784  2.863   1.00 29.92 ?  331 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 19.945 -12.587 -8.815  1.00 27.25 ?  332 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 31.037 -18.146 7.804   1.00 19.03 ?  333 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 38.285 10.127  7.124   1.00 41.08 ?  334 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 22.758 12.527  1.630   1.00 14.36 ?  335 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 21.268 -2.381  -2.215  1.00 16.44 ?  336 HOH   A O    1 
HETATM 6756 O  O    A HOH   F 5 .   ? 14.651 -3.660  3.106   0.50 16.17 ?  337 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 20.618 -19.738 -5.037  1.00 27.62 ?  338 HOH   A O    1 
HETATM 6758 O  O    . HOH   F 5 .   ? 37.579 2.773   10.169  1.00 25.93 ?  339 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 38.579 4.983   6.931   1.00 15.56 ?  340 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 17.030 -19.295 4.914   1.00 15.02 ?  341 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 31.718 8.248   14.769  1.00 23.27 ?  342 HOH   A O    1 
HETATM 6762 O  O    B HOH   F 5 .   ? 14.878 -2.856  3.437   0.50 17.20 ?  343 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 22.399 5.415   19.018  1.00 45.96 ?  344 HOH   A O    1 
HETATM 6764 O  O    B HOH   F 5 .   ? 22.653 5.614   -1.630  0.50 22.25 ?  345 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 25.701 -0.842  -7.359  1.00 16.26 ?  346 HOH   A O    1 
HETATM 6766 O  O    B HOH   F 5 .   ? 12.140 -2.194  -4.329  0.50 23.62 ?  347 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 10.333 -22.149 -1.266  1.00 48.86 ?  348 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 28.300 -0.151  -13.388 1.00 34.69 ?  349 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 44.363 7.103   6.400   1.00 26.33 ?  350 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 13.350 -1.435  -6.682  1.00 18.61 ?  351 HOH   A O    1 
HETATM 6771 O  O    A HOH   F 5 .   ? 11.062 1.546   12.764  0.50 18.50 ?  352 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 18.698 -19.390 13.599  1.00 32.89 ?  353 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 17.167 -17.823 -5.009  1.00 28.59 ?  354 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 39.760 -1.018  -5.204  1.00 20.53 ?  355 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 24.030 -2.114  -2.089  1.00 10.76 ?  356 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 33.668 -7.174  4.272   1.00 16.21 ?  357 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 42.583 4.260   5.336   1.00 30.37 ?  358 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 35.797 -12.672 6.847   1.00 15.33 ?  359 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 37.377 11.963  4.945   1.00 31.79 ?  360 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 22.158 -19.275 11.397  1.00 32.51 ?  361 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 14.386 -21.253 -4.239  1.00 31.18 ?  362 HOH   A O    1 
HETATM 6782 O  O    B HOH   F 5 .   ? 11.370 6.439   8.941   0.50 28.06 ?  363 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 8.169  -21.523 4.066   1.00 51.27 ?  364 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? -0.743 -8.542  2.194   1.00 46.47 ?  365 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 31.093 -13.944 -2.473  1.00 13.13 ?  366 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 24.414 3.552   -1.800  1.00 14.85 ?  367 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 22.647 -11.886 21.879  1.00 48.26 ?  368 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 43.916 8.447   -3.108  1.00 27.24 ?  369 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 18.610 9.447   9.017   1.00 21.10 ?  370 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 37.288 -2.867  9.656   1.00 42.65 ?  371 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 43.375 7.807   2.650   1.00 25.53 ?  372 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 21.883 -21.910 8.435   1.00 28.78 ?  373 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 30.824 3.086   8.247   1.00 11.71 ?  374 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 11.817 -10.711 17.038  1.00 28.50 ?  375 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 31.848 -9.377  -6.651  1.00 22.05 ?  376 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 16.539 -22.069 1.034   1.00 28.69 ?  377 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 31.802 -7.307  -9.838  1.00 20.83 ?  378 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 27.525 -10.627 14.067  1.00 16.61 ?  379 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 26.937 4.144   -0.675  1.00 12.67 ?  380 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 7.569  -6.238  -6.527  1.00 42.82 ?  381 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 21.774 -13.900 -8.157  1.00 48.45 ?  382 HOH   A O    1 
HETATM 6802 O  O    B HOH   F 5 .   ? 21.302 2.910   0.045   0.50 19.54 ?  383 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 27.903 0.813   -7.165  1.00 14.13 ?  384 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 23.500 11.389  4.079   1.00 12.10 ?  385 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 21.243 10.230  15.015  1.00 37.17 ?  386 HOH   A O    1 
HETATM 6806 O  O    B HOH   F 5 .   ? 18.553 -1.454  -1.442  0.50 30.07 ?  387 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 24.729 -17.536 12.706  1.00 23.96 ?  388 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 6.799  -3.312  13.021  1.00 34.31 ?  389 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 15.223 -21.570 14.215  1.00 17.01 ?  390 HOH   A O    1 
HETATM 6810 O  O    B HOH   F 5 .   ? 11.006 2.082   11.892  0.50 22.72 ?  391 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 5.250  2.655   5.163   1.00 32.92 ?  392 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 24.269 -7.763  14.451  1.00 16.52 ?  393 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 20.116 4.532   -7.540  1.00 21.72 ?  394 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 27.437 -6.083  -14.002 1.00 39.37 ?  395 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 24.005 3.905   -4.821  1.00 21.88 ?  396 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 14.451 -24.715 11.554  1.00 34.15 ?  397 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 30.113 -10.111 12.991  1.00 21.76 ?  398 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 13.965 -4.893  17.428  1.00 26.48 ?  399 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 32.811 -9.247  5.962   1.00 20.08 ?  400 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 14.571 -0.505  -12.118 1.00 29.31 ?  401 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 37.583 -2.010  5.750   1.00 25.95 ?  402 HOH   A O    1 
HETATM 6822 O  O    A HOH   F 5 .   ? 14.295 0.568   6.809   0.50 19.53 ?  403 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 15.478 11.804  7.878   1.00 38.10 ?  404 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 38.111 -1.346  -1.965  1.00 18.60 ?  405 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 20.594 -20.048 2.799   1.00 18.06 ?  406 HOH   A O    1 
HETATM 6826 O  O    A HOH   F 5 .   ? -0.461 -3.098  3.125   0.50 30.98 ?  407 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 30.740 1.866   16.675  1.00 20.58 ?  408 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 27.326 2.334   18.693  1.00 30.86 ?  409 HOH   A O    1 
HETATM 6829 O  O    A HOH   F 5 .   ? 18.969 -0.674  -1.622  0.50 9.63  ?  410 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 16.308 -14.118 20.204  1.00 49.87 ?  411 HOH   A O    1 
HETATM 6831 O  O    A HOH   F 5 .   ? 21.360 3.151   -0.347  0.50 9.14  ?  412 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 6.464  -5.489  11.221  1.00 21.03 ?  413 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 14.096 -23.085 7.434   1.00 18.16 ?  414 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 44.911 -0.659  2.964   1.00 40.69 ?  415 HOH   A O    1 
HETATM 6835 O  O    A HOH   F 5 .   ? 9.283  -10.234 19.396  0.50 31.21 ?  416 HOH   A O    1 
HETATM 6836 O  O    A HOH   F 5 .   ? 15.818 -0.951  5.278   0.50 23.18 ?  417 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 10.403 -13.747 -1.689  1.00 18.82 ?  418 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 30.932 6.219   -12.295 1.00 28.73 ?  419 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 23.948 -20.285 -1.335  1.00 16.14 ?  420 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 32.659 -4.334  -9.916  1.00 28.37 ?  421 HOH   A O    1 
HETATM 6841 O  O    B HOH   F 5 .   ? 8.098  3.947   1.428   0.50 20.24 ?  422 HOH   A O    1 
HETATM 6842 O  O    A HOH   F 5 .   ? 24.587 2.036   -6.989  0.50 14.22 ?  423 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 30.380 -12.940 13.516  1.00 19.41 ?  424 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 35.044 -5.229  -3.093  1.00 17.75 ?  425 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 16.241 16.666  8.721   1.00 33.70 ?  426 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 36.768 -4.955  5.356   1.00 23.42 ?  427 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 41.651 1.525   4.968   1.00 36.14 ?  428 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 32.524 -10.662 3.205   1.00 30.85 ?  429 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 16.070 6.982   2.923   1.00 19.08 ?  430 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 21.292 -9.178  21.327  1.00 52.22 ?  431 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 40.976 -8.279  -6.802  1.00 37.92 ?  432 HOH   A O    1 
HETATM 6852 O  O    B HOH   F 5 .   ? 9.239  2.388   7.901   0.50 27.74 ?  433 HOH   A O    1 
HETATM 6853 O  O    A HOH   F 5 .   ? 18.874 2.028   -0.747  0.50 9.33  ?  434 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 22.658 8.145   18.359  1.00 46.20 ?  435 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 23.226 7.634   -3.178  1.00 29.20 ?  436 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 19.213 -11.013 23.954  1.00 74.56 ?  437 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 18.564 4.937   -15.115 1.00 49.72 ?  438 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 27.127 -3.140  19.350  1.00 35.57 ?  439 HOH   A O    1 
HETATM 6859 O  O    A HOH   F 5 .   ? 9.040  -12.129 17.203  0.50 32.09 ?  440 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? -1.337 -5.082  7.684   1.00 45.13 ?  441 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 23.569 -8.022  17.086  1.00 21.29 ?  442 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 18.456 -16.008 16.317  1.00 37.19 ?  443 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 23.372 -20.969 1.337   1.00 18.04 ?  444 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 34.424 -8.092  -0.498  1.00 27.20 ?  445 HOH   A O    1 
HETATM 6865 O  O    A HOH   F 5 .   ? 16.269 2.942   -1.434  0.50 15.52 ?  446 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 9.475  -16.349 -2.017  1.00 51.82 ?  447 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 37.728 -8.829  -3.455  1.00 23.23 ?  448 HOH   A O    1 
HETATM 6868 O  O    B HOH   F 5 .   ? 7.397  3.762   4.127   0.50 25.49 ?  449 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 30.618 14.784  2.775   1.00 18.77 ?  450 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 31.345 -12.789 -0.002  1.00 18.51 ?  451 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 20.614 -17.762 24.856  1.00 57.85 ?  452 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 11.837 -11.054 -10.181 1.00 48.28 ?  453 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 21.563 -14.726 17.905  1.00 57.10 ?  454 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 29.845 -16.037 10.666  1.00 30.49 ?  455 HOH   A O    1 
HETATM 6875 O  O    A HOH   F 5 .   ? 14.044 -0.344  3.471   0.50 19.99 ?  456 HOH   A O    1 
HETATM 6876 O  O    B HOH   F 5 .   ? 18.839 1.541   -0.424  0.50 18.97 ?  457 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 27.740 6.968   -6.492  1.00 35.72 ?  458 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 29.762 -1.978  -12.676 1.00 45.90 ?  459 HOH   A O    1 
HETATM 6879 O  O    B HOH   F 5 .   ? 12.832 -3.380  1.505   0.50 23.98 ?  460 HOH   A O    1 
HETATM 6880 O  O    . HOH   F 5 .   ? 25.403 8.248   -4.803  1.00 24.08 ?  461 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 32.465 -15.937 10.822  1.00 31.50 ?  462 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 19.936 -17.355 -5.046  1.00 25.17 ?  463 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 23.199 -22.295 -3.368  1.00 35.30 ?  464 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 24.883 5.660   20.733  1.00 52.34 ?  465 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 18.763 10.798  11.372  1.00 33.60 ?  466 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 24.663 14.614  7.832   1.00 35.44 ?  467 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 21.993 5.221   -5.982  1.00 31.12 ?  468 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 12.034 -13.400 16.418  1.00 49.44 ?  469 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 18.116 -16.308 -8.812  1.00 41.49 ?  470 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 26.938 11.651  -1.341  1.00 31.16 ?  471 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 15.754 -21.515 3.699   1.00 22.27 ?  472 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 39.621 -7.062  -3.525  1.00 46.63 ?  473 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 23.520 13.728  5.499   1.00 18.40 ?  474 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 11.008 -15.046 -6.081  1.00 36.29 ?  475 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 27.500 -11.400 16.553  1.00 37.42 ?  476 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 25.858 10.804  -3.707  1.00 25.16 ?  477 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 12.377 1.621   17.287  1.00 40.65 ?  478 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 23.156 11.872  -4.016  1.00 19.27 ?  479 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 35.175 7.480   12.227  1.00 42.06 ?  480 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 15.792 -17.247 -6.956  1.00 32.90 ?  481 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 28.799 9.039   17.529  1.00 37.48 ?  482 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 16.849 -20.568 16.193  1.00 28.87 ?  483 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 16.092 -6.868  -11.908 1.00 50.21 ?  484 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 41.010 -3.976  -0.352  1.00 38.88 ?  485 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 14.044 -10.339 -10.902 1.00 35.11 ?  486 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 30.836 0.716   19.175  1.00 38.70 ?  487 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 17.401 -18.691 19.769  1.00 53.31 ?  488 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 31.491 -0.596  -10.592 1.00 26.90 ?  489 HOH   A O    1 
HETATM 6909 O  O    B HOH   F 5 .   ? 11.351 8.721   7.793   0.50 34.91 ?  490 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 23.291 -12.876 19.312  1.00 49.91 ?  491 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 44.546 10.454  -1.598  1.00 31.29 ?  492 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 41.722 9.367   -4.018  1.00 33.42 ?  493 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 28.526 -4.678  -12.351 1.00 39.47 ?  494 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 28.683 -7.963  -15.257 1.00 49.73 ?  495 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 39.194 2.407   7.499   1.00 32.28 ?  496 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 18.597 -23.208 1.935   1.00 40.62 ?  497 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 20.543 -15.983 -7.414  1.00 31.13 ?  498 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 20.062 -22.337 4.236   1.00 30.11 ?  499 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 40.517 -0.254  -7.860  1.00 32.10 ?  500 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 8.099  -3.166  -5.737  1.00 55.25 ?  501 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 25.793 -18.927 -11.896 1.00 38.63 ?  502 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 13.993 -25.260 8.979   1.00 32.11 ?  503 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 16.195 -23.431 5.751   1.00 27.26 ?  504 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 30.725 -5.884  -11.883 1.00 48.17 ?  505 HOH   A O    1 
HETATM 6925 O  O    B HOH   F 5 .   ? 14.682 7.892   4.869   0.50 31.14 ?  506 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 23.214 -23.793 1.744   1.00 29.31 ?  507 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 37.405 -6.678  7.508   1.00 23.92 ?  508 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 30.719 5.829   -14.756 1.00 36.48 ?  509 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 39.566 0.025   6.535   1.00 29.85 ?  510 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 38.065 13.917  6.701   1.00 48.96 ?  511 HOH   A O    1 
HETATM 6931 O  O    B HOH   F 5 .   ? 9.132  5.226   8.047   0.50 33.11 ?  512 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 29.069 14.443  0.806   1.00 46.14 ?  513 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 22.065 -24.072 4.474   1.00 24.49 ?  514 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 36.506 -6.535  10.130  1.00 45.75 ?  515 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 17.304 -6.918  -14.183 1.00 41.43 ?  516 HOH   A O    1 
HETATM 6936 O  O    B HOH   F 5 .   ? 9.490  0.237   -5.493  0.50 31.83 ?  517 HOH   A O    1 
HETATM 6937 O  O    A HOH   F 5 .   ? 14.867 8.645   4.898   0.50 27.05 ?  518 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 24.062 9.075   -7.220  1.00 36.69 ?  519 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 16.336 -21.150 18.802  1.00 36.62 ?  520 HOH   A O    1 
HETATM 6940 O  O    B HOH   F 5 .   ? 7.862  7.176   2.524   0.50 24.85 ?  521 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 15.920 -12.354 27.427  1.00 47.25 ?  522 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 14.731 -22.836 19.783  1.00 34.49 ?  523 HOH   A O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 29.836 -22.415 5.479   1.00 19.48 ?  201 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 52.917 -13.471 -20.349 1.00 35.18 ?  202 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 41.718 -36.028 -17.166 1.00 31.91 ?  203 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 27.688 -29.196 -1.855  1.00 39.16 ?  204 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 59.179 -18.692 6.776   1.00 38.75 ?  205 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 48.087 -6.911  15.521  1.00 36.16 ?  206 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 41.430 -7.768  5.474   1.00 37.49 ?  207 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 29.933 -26.306 4.037   1.00 26.69 ?  208 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 27.843 -41.863 -15.138 1.00 36.93 ?  209 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 54.499 -9.390  -8.766  1.00 18.50 ?  210 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 38.003 -39.496 -0.192  1.00 40.48 ?  211 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 49.445 -22.715 -19.787 1.00 48.90 ?  212 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 56.393 -19.722 7.253   1.00 32.70 ?  213 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 58.261 -12.906 8.378   1.00 31.79 ?  214 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 55.475 -16.569 -14.346 1.00 35.48 ?  215 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 47.465 -7.386  -3.915  1.00 40.89 ?  216 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 57.768 -24.481 5.062   1.00 37.58 ?  217 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 26.511 -19.338 -1.776  1.00 13.79 ?  218 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 30.225 -41.037 -8.126  1.00 16.35 ?  219 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 50.265 -3.331  7.127   1.00 35.95 ?  220 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 44.460 -7.211  2.048   1.00 33.88 ?  221 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 57.204 -26.877 -7.675  1.00 42.38 ?  222 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 50.765 -6.114  0.166   1.00 25.14 ?  223 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 56.714 -30.781 -7.762  1.00 29.83 ?  224 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 44.970 -43.560 -10.609 1.00 27.34 ?  225 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 57.430 -16.276 -12.209 1.00 18.80 ?  226 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 48.540 -36.559 -15.515 1.00 46.07 ?  227 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 29.763 -34.142 -0.461  1.00 35.54 ?  228 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 34.565 -36.394 -7.208  1.00 18.31 ?  229 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 40.610 -16.093 14.086  1.00 23.10 ?  230 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 35.989 -43.302 -8.532  1.00 31.53 ?  231 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 41.407 -9.657  13.039  1.00 21.39 ?  232 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 51.689 -6.494  4.387   1.00 19.79 ?  233 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 30.912 -28.793 4.262   1.00 26.47 ?  234 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 41.513 -39.180 -14.942 1.00 21.79 ?  235 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 44.528 -27.746 -0.701  1.00 22.07 ?  236 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 32.822 -43.805 -11.359 1.00 20.15 ?  237 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 37.065 -19.768 -18.087 1.00 39.43 ?  238 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 39.333 -10.891 6.116   1.00 24.59 ?  239 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 35.123 -8.017  -3.014  1.00 18.45 ?  240 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 25.407 -25.945 -1.318  1.00 32.38 ?  241 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 42.591 -25.387 2.617   1.00 14.66 ?  242 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 28.413 -19.699 -13.112 1.00 23.68 ?  243 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 46.401 -1.556  13.194  1.00 28.25 ?  244 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 43.158 -32.391 -17.099 1.00 23.87 ?  245 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 50.763 -12.987 -0.491  1.00 11.65 ?  246 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 42.660 -22.884 3.822   1.00 11.43 ?  247 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 43.116 -43.260 -8.305  1.00 29.20 ?  248 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 34.973 -24.631 13.867  1.00 32.26 ?  249 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 51.600 -13.882 10.964  1.00 27.03 ?  250 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 39.520 -11.126 0.330   1.00 16.76 ?  251 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 34.260 -18.504 11.422  1.00 24.47 ?  252 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 45.173 -35.025 6.772   1.00 39.69 ?  253 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 41.893 -23.523 9.286   1.00 17.26 ?  254 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 38.485 -11.055 -2.257  1.00 18.36 ?  255 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 57.633 -24.405 -3.864  1.00 21.36 ?  256 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 34.925 -33.255 -19.254 1.00 32.87 ?  257 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 40.347 -12.755 -11.535 1.00 14.98 ?  258 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 29.740 -25.236 -10.806 1.00 16.25 ?  259 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 58.214 -10.655 -4.084  1.00 19.47 ?  260 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 30.872 -15.733 2.643   1.00 13.25 ?  261 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 31.836 -17.965 -14.503 1.00 30.70 ?  262 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 49.780 -0.536  10.213  1.00 32.18 ?  263 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 33.542 -17.014 8.066   1.00 18.82 ?  264 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 38.942 -12.025 12.350  1.00 32.69 ?  265 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 48.016 -22.794 5.826   1.00 16.66 ?  266 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 42.910 -20.299 -20.752 1.00 39.86 ?  267 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 51.013 -39.963 -8.294  1.00 33.85 ?  268 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 42.396 -9.934  9.342   1.00 19.82 ?  269 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 49.352 -28.722 -6.936  1.00 15.39 ?  270 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 28.484 -30.817 -14.774 1.00 28.89 ?  271 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 43.379 -15.798 -12.179 1.00 13.95 ?  272 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 56.990 -8.637  8.376   1.00 19.61 ?  273 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 57.504 -9.227  1.391   1.00 19.64 ?  274 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 27.159 -31.838 -10.004 1.00 20.74 ?  275 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 56.184 -23.516 -14.761 1.00 26.15 ?  276 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 28.276 -34.378 -9.440  1.00 18.19 ?  277 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 46.652 -31.260 -4.828  1.00 19.78 ?  278 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 34.490 -12.794 2.610   1.00 25.06 ?  279 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 46.886 -29.596 9.822   1.00 31.40 ?  280 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 41.230 -5.511  11.506  1.00 44.92 ?  281 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 48.429 -25.063 3.088   1.00 13.23 ?  282 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 27.957 -22.888 -8.006  1.00 17.14 ?  283 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 42.432 -34.719 3.772   1.00 25.49 ?  284 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 42.321 -9.985  -14.934 1.00 37.32 ?  285 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 48.750 -20.047 5.906   1.00 13.59 ?  286 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 47.114 -33.992 -4.672  1.00 17.68 ?  287 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 33.523 -15.327 -13.965 1.00 21.06 ?  288 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 30.531 -42.294 -10.595 1.00 29.65 ?  289 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 57.194 -12.072 12.320  1.00 36.33 ?  290 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 51.249 -37.616 -9.613  1.00 25.47 ?  291 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 37.396 -35.696 7.188   1.00 32.87 ?  292 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 47.972 -24.449 -17.826 1.00 31.96 ?  293 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 36.831 -12.777 -1.499  1.00 26.15 ?  294 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 27.569 -26.726 -15.654 1.00 32.59 ?  295 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 52.579 -10.402 12.987  1.00 22.61 ?  296 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 44.651 -27.482 1.987   1.00 14.99 ?  297 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 52.605 -35.688 -8.636  1.00 30.02 ?  298 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 37.510 -18.231 13.095  1.00 29.18 ?  299 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 42.739 -12.233 -18.503 1.00 27.72 ?  300 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 59.831 -15.334 8.170   1.00 31.26 ?  301 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 40.265 -10.837 -9.520  1.00 16.78 ?  302 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 35.097 -33.626 4.531   1.00 28.57 ?  303 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 45.929 -40.453 -3.642  1.00 29.64 ?  304 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 45.384 -33.409 -16.003 1.00 23.60 ?  305 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 49.936 -24.724 5.813   1.00 33.04 ?  306 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 25.964 -21.483 -3.486  1.00 16.02 ?  307 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 51.390 -32.938 -10.760 1.00 37.61 ?  308 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 62.722 -13.592 4.746   1.00 27.60 ?  309 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 53.502 -30.224 4.489   1.00 18.64 ?  310 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 44.062 -29.368 -4.683  1.00 23.38 ?  311 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 41.769 -8.088  1.338   1.00 23.26 ?  312 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 53.199 -16.090 -12.700 1.00 27.96 ?  313 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 41.244 -24.458 15.801  1.00 43.12 ?  314 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 37.846 -10.245 -10.743 1.00 16.92 ?  315 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 32.835 -34.610 -5.915  1.00 16.78 ?  316 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 57.665 -22.096 3.144   1.00 28.34 ?  317 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 52.561 -29.219 -13.070 1.00 24.31 ?  318 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 51.720 -5.926  -7.913  1.00 44.81 ?  319 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 43.244 -21.445 10.657  1.00 15.71 ?  320 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 38.372 -12.770 7.933   1.00 17.96 ?  321 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 53.692 -12.528 -22.258 1.00 37.77 ?  322 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 37.147 -30.591 -21.045 1.00 30.69 ?  323 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 48.141 -32.605 -16.669 1.00 43.99 ?  324 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 62.911 -20.083 -0.849  1.00 38.44 ?  325 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 26.358 -21.053 -6.234  1.00 15.83 ?  326 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 44.633 -24.633 9.560   1.00 19.93 ?  327 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 36.747 -12.433 4.298   1.00 18.07 ?  328 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 43.499 -15.421 18.153  1.00 28.91 ?  329 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 27.772 -14.782 -9.463  1.00 34.55 ?  330 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 43.151 -34.609 0.063   1.00 20.96 ?  331 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 59.956 -17.273 -10.558 1.00 33.78 ?  332 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 38.381 -9.379  -13.258 1.00 26.93 ?  333 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 45.688 -36.296 -16.115 1.00 35.81 ?  334 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 47.225 -24.497 8.133   1.00 25.75 ?  335 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 33.663 -31.193 11.064  1.00 35.64 ?  336 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 44.203 -1.710  7.574   1.00 45.35 ?  337 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 48.614 -11.965 -13.949 1.00 27.04 ?  338 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 42.928 -43.548 -14.402 1.00 43.01 ?  339 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 47.506 -27.456 2.010   1.00 14.48 ?  340 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 39.544 -23.520 -20.369 1.00 36.46 ?  341 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 37.064 -15.132 -16.570 1.00 38.87 ?  342 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 46.837 -19.912 12.285  1.00 31.18 ?  343 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 28.900 -42.927 -12.366 1.00 38.25 ?  344 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 38.420 -12.267 -16.238 1.00 41.76 ?  345 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 37.085 -45.229 -9.756  1.00 37.45 ?  346 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 33.035 -14.704 1.032   1.00 17.99 ?  347 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 39.769 -44.338 -11.197 1.00 39.76 ?  348 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 38.611 -22.365 15.046  1.00 40.42 ?  349 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 27.823 -26.599 -0.554  1.00 29.00 ?  350 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 40.432 -43.511 -9.146  1.00 27.03 ?  351 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 33.777 -9.328  -8.837  1.00 31.84 ?  352 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 62.581 -20.149 -4.856  1.00 49.41 ?  353 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 44.181 -37.361 -17.812 1.00 33.31 ?  354 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 55.706 -8.273  10.800  1.00 24.91 ?  355 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 34.651 -10.321 7.525   1.00 23.76 ?  356 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 23.246 -23.709 6.799   1.00 33.03 ?  357 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 36.047 -8.571  -9.723  1.00 35.46 ?  358 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 56.568 -7.274  3.048   1.00 28.25 ?  359 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 43.171 -12.752 -21.214 1.00 36.61 ?  360 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 34.098 -7.800  11.498  1.00 39.58 ?  361 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 61.530 -19.914 1.621   1.00 34.95 ?  362 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 40.293 -8.798  9.911   1.00 38.21 ?  363 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 56.931 -21.600 -16.439 1.00 39.03 ?  364 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 27.164 -25.928 -11.446 1.00 33.45 ?  365 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 32.551 -23.633 14.028  1.00 40.20 ?  366 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 54.196 -5.724  2.959   1.00 35.41 ?  367 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 59.001 -10.503 9.135   1.00 37.79 ?  368 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 48.384 -26.504 8.838   1.00 40.25 ?  369 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 40.115 -11.362 -13.963 1.00 31.65 ?  370 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 36.231 -8.680  8.964   1.00 36.48 ?  371 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 41.892 -10.048 -17.468 1.00 53.85 ?  372 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 56.001 -7.798  -0.627  1.00 37.50 ?  373 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 39.836 -7.002  7.804   1.00 40.75 ?  374 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 52.114 -12.912 13.297  1.00 28.73 ?  375 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 38.083 -10.572 10.029  1.00 28.51 ?  376 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 63.080 -12.399 6.942   1.00 36.81 ?  377 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 41.844 -6.774  -4.888  1.00 49.22 ?  378 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 44.105 -5.589  -3.522  1.00 44.57 ?  379 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 36.534 -22.848 13.278  1.00 24.68 ?  380 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 40.150 -7.643  3.169   1.00 37.26 ?  381 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 42.677 -17.095 -23.250 1.00 42.60 ?  382 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 52.859 -29.892 7.143   1.00 23.69 ?  383 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 39.677 -14.008 15.709  1.00 49.11 ?  384 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 60.535 -22.266 2.817   1.00 50.11 ?  385 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 41.088 -9.794  15.787  1.00 44.10 ?  386 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 46.789 -5.418  2.910   1.00 40.47 ?  387 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 35.330 -20.340 13.303  1.00 30.44 ?  388 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 35.409 -33.651 7.302   1.00 41.19 ?  389 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 23.950 -20.916 -7.702  1.00 27.04 ?  390 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 40.767 -6.620  -0.856  1.00 24.16 ?  391 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 44.092 -31.801 -3.831  1.00 35.97 ?  392 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 27.915 -27.084 2.267   1.00 30.00 ?  393 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 26.614 -27.954 -13.491 1.00 35.10 ?  394 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 34.398 -33.511 9.588   1.00 33.65 ?  395 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 24.642 -20.713 -10.471 1.00 37.62 ?  396 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 50.678 -30.864 8.704   1.00 27.46 ?  397 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 26.837 -30.673 -12.627 1.00 28.15 ?  398 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 45.756 -20.176 15.223  1.00 51.17 ?  399 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 57.506 -6.411  -2.326  1.00 32.65 ?  400 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 40.904 -11.835 -22.338 1.00 45.33 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.6758 0.6729 0.7244 -0.0017 -0.0339 0.0852  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6778 0.6737 0.7256 -0.0029 -0.0359 0.0843  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6728 0.6704 0.7187 -0.0035 -0.0326 0.0848  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6747 0.6711 0.7194 -0.0046 -0.0343 0.0841  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6567 0.6580 0.6974 -0.0099 -0.0331 0.0885  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6578 0.6584 0.6979 -0.0106 -0.0341 0.0882  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6593 0.6606 0.7093 -0.0088 -0.0350 0.0907  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6607 0.6612 0.7099 -0.0096 -0.0363 0.0903  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6826 0.6778 0.7277 -0.0003 -0.0307 0.0809  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6850 0.6786 0.7280 -0.0016 -0.0331 0.0800  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6862 0.6803 0.7283 0.0012  -0.0305 0.0796  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6887 0.6809 0.7285 -0.0002 -0.0331 0.0786  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6856 0.6804 0.7285 0.0006  -0.0300 0.0799  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6882 0.6813 0.7287 -0.0009 -0.0327 0.0789  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6341 0.6401 0.6601 -0.0178 -0.0307 0.0893  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5837 0.6004 0.5786 -0.0341 -0.0222 0.0890  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5167 0.5533 0.5137 -0.0500 0.0045  0.0579  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5169 0.5552 0.5145 -0.0528 0.0035  0.0620  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5960 0.6051 0.5516 -0.0352 -0.0364 0.1188  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.6032 0.6068 0.5224 -0.0367 -0.0502 0.1442  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6060 0.6070 0.5141 -0.0375 -0.0552 0.1541  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6048 0.6066 0.5180 -0.0363 -0.0553 0.1536  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.4777 0.5249 0.4736 -0.0576 0.0166  0.0408  5   SER   A N   
47   N  N   B SER   A 5   ? 0.4850 0.5284 0.4741 -0.0561 0.0204  0.0415  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4359 0.4942 0.4301 -0.0657 0.0317  0.0237  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4503 0.5011 0.4317 -0.0626 0.0392  0.0253  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.3885 0.4529 0.3821 -0.0712 0.0490  0.0166  5   SER   A C   
51   C  C   B SER   A 5   ? 0.4083 0.4634 0.3837 -0.0669 0.0595  0.0180  5   SER   A C   
52   O  O   A SER   A 5   ? 0.3941 0.4578 0.3803 -0.0664 0.0486  0.0108  5   SER   A O   
53   O  O   B SER   A 5   ? 0.4137 0.4679 0.3803 -0.0620 0.0607  0.0118  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4402 0.5024 0.4394 -0.0681 0.0293  0.0157  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4559 0.5092 0.4438 -0.0647 0.0376  0.0181  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4425 0.5066 0.4410 -0.0698 0.0289  0.0118  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4589 0.5133 0.4466 -0.0662 0.0373  0.0142  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3333 0.4041 0.3270 -0.0813 0.0689  0.0213  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3583 0.4186 0.3327 -0.0764 0.0804  0.0218  6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2834 0.3532 0.2715 -0.0861 0.0794  0.0367  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3113 0.3711 0.2888 -0.0841 0.0940  0.0331  6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2693 0.3414 0.2662 -0.0859 0.0865  0.0330  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.2987 0.3630 0.3047 -0.0835 0.1001  0.0309  6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2717 0.3452 0.2959 -0.0883 0.0855  0.0391  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3004 0.3635 0.3187 -0.0907 0.1059  0.0432  6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2576 0.3179 0.2450 -0.0792 0.0683  0.0464  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.2866 0.3362 0.2583 -0.0802 0.0824  0.0342  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2396 0.2889 0.2188 -0.0664 0.0529  0.0484  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.2669 0.3067 0.2317 -0.0726 0.0700  0.0285  6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2310 0.2778 0.2087 -0.0582 0.0430  0.0483  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.2574 0.2953 0.2227 -0.0677 0.0610  0.0273  6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2421 0.2793 0.2204 -0.0519 0.0450  0.0470  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.2675 0.2950 0.2349 -0.0616 0.0639  0.0207  6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2294 0.2709 0.2106 -0.0518 0.0411  0.0502  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2540 0.2869 0.2244 -0.0641 0.0636  0.0261  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2380 0.2725 0.2180 -0.0471 0.0418  0.0461  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.2623 0.2859 0.2340 -0.0597 0.0656  0.0185  6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2327 0.2688 0.2147 -0.0492 0.0381  0.0455  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2562 0.2835 0.2282 -0.0618 0.0659  0.0193  6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2519 0.3226 0.2313 -0.0829 0.0928  0.0264  7   SER   A N   
109  N  N   B SER   A 7   ? 0.2843 0.3528 0.3055 -0.0742 0.0952  0.0174  7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2460 0.3099 0.2209 -0.0691 0.0865  0.0116  7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.2777 0.3458 0.3110 -0.0614 0.0855  0.0075  7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2247 0.2766 0.1971 -0.0659 0.0806  -0.0054 7   SER   A C   
113  C  C   B SER   A 7   ? 0.2575 0.3223 0.2703 -0.0601 0.0878  0.0100  7   SER   A C   
114  O  O   A SER   A 7   ? 0.2260 0.2647 0.1812 -0.0709 0.0904  -0.0140 7   SER   A O   
115  O  O   B SER   A 7   ? 0.2590 0.3212 0.2689 -0.0624 0.0840  0.0116  7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2641 0.3268 0.2382 -0.0550 0.0784  0.0150  7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.2922 0.3587 0.3466 -0.0510 0.0768  0.0030  7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2788 0.3370 0.2491 -0.0441 0.0693  0.0162  7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.3024 0.3661 0.3771 -0.0437 0.0691  0.0030  7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2077 0.2521 0.1933 -0.0614 0.0624  -0.0140 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2406 0.3011 0.2368 -0.0581 0.0899  0.0077  8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.1942 0.2274 0.1889 -0.0421 0.0603  -0.0090 8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2273 0.2773 0.2119 -0.0496 0.0806  0.0122  8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1765 0.2072 0.1924 -0.0264 0.0447  -0.0040 8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2090 0.2547 0.1936 -0.0442 0.0693  0.0161  8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1777 0.2080 0.1909 -0.0080 0.0401  -0.0169 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2085 0.2528 0.1938 -0.0345 0.0790  0.0159  8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1569 0.1861 0.1890 -0.0222 0.0338  0.0117  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.1890 0.2314 0.1914 -0.0397 0.0429  0.0168  9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1412 0.1687 0.1803 -0.0170 0.0202  0.0139  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1751 0.2051 0.1903 -0.0331 0.0329  0.0235  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1393 0.1562 0.1883 -0.0113 0.0158  0.0245  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1680 0.1844 0.1721 -0.0265 0.0301  0.0336  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1588 0.1794 0.2075 -0.0190 0.0072  0.0184  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1747 0.2016 0.1912 -0.0337 0.0093  0.0521  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1351 0.1709 0.1920 -0.0079 0.0228  -0.0015 9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1688 0.2048 0.2089 -0.0290 0.0256  0.0149  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1382 0.1703 0.2152 0.0027  0.0449  -0.0176 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1613 0.1995 0.2134 -0.0231 0.0329  0.0075  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1443 0.1688 0.2285 -0.0008 0.0538  -0.0310 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1674 0.1947 0.2245 -0.0247 0.0416  -0.0034 9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1438 0.1665 0.2282 0.0052  0.0395  -0.0095 9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1557 0.1941 0.2127 -0.0179 0.0309  0.0156  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1559 0.1714 0.2454 -0.0019 0.0488  -0.0393 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1667 0.1872 0.2280 -0.0200 0.0461  -0.0105 9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1465 0.1684 0.2349 0.0038  0.0497  -0.0243 9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1516 0.1922 0.2175 -0.0123 0.0449  0.0150  9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1560 0.1732 0.2585 -0.0082 0.0550  -0.0290 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1534 0.1852 0.2377 -0.0126 0.0609  0.0072  9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1719 0.1765 0.2794 -0.0198 0.0550  -0.0262 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1518 0.1850 0.2575 -0.0158 0.0694  0.0173  9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1317 0.1400 0.1820 -0.0097 0.0226  0.0224  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1632 0.1596 0.1720 -0.0200 0.0345  0.0227  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1240 0.1353 0.1732 -0.0125 0.0204  0.0320  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1588 0.1570 0.1914 -0.0171 0.0335  0.0076  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1267 0.1298 0.1768 -0.0160 0.0250  0.0282  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1611 0.1450 0.1748 -0.0194 0.0237  0.0189  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1324 0.1230 0.1716 -0.0136 0.0297  0.0216  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1634 0.1366 0.1756 -0.0184 0.0353  0.0207  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1233 0.1384 0.1921 -0.0079 0.0189  0.0355  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1592 0.1599 0.2124 -0.0210 0.0263  0.0010  10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1470 0.1471 0.2294 -0.0052 0.0045  0.0366  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1674 0.1676 0.2289 -0.0175 0.0177  -0.0004 10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1641 0.1506 0.2422 -0.0130 0.0054  0.0340  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.1780 0.1771 0.2491 -0.0310 0.0116  -0.0041 10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1593 0.1574 0.2321 0.0042  0.0197  0.0193  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.1825 0.1775 0.2534 -0.0048 0.0057  -0.0013 10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1282 0.1317 0.1697 -0.0165 0.0289  0.0302  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1707 0.1449 0.1883 -0.0233 0.0151  0.0228  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1276 0.1329 0.1810 -0.0198 0.0272  0.0258  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1699 0.1379 0.1916 -0.0322 0.0165  0.0315  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1248 0.1374 0.1929 -0.0160 0.0265  0.0078  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1540 0.1266 0.1848 -0.0336 0.0134  0.0203  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1382 0.1476 0.2292 -0.0379 0.0270  -0.0062 11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1465 0.1283 0.2065 -0.0242 0.0172  0.0007  11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1369 0.1365 0.1741 -0.0187 0.0175  0.0135  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1835 0.1376 0.1989 -0.0283 0.0148  0.0276  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1487 0.1413 0.1690 -0.0189 0.0151  0.0218  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1913 0.1437 0.2013 -0.0277 0.0166  0.0475  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1596 0.1457 0.1485 -0.0174 0.0084  0.0140  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.2016 0.1523 0.2130 -0.0273 0.0119  0.0512  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1664 0.1421 0.1437 -0.0107 0.0037  0.0245  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.2034 0.1509 0.2254 -0.0297 -0.0048 0.0563  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1583 0.1445 0.1471 -0.0014 0.0019  0.0244  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1995 0.1531 0.2340 -0.0253 -0.0170 0.0529  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1189 0.1338 0.1673 -0.0212 0.0267  0.0101  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1486 0.1379 0.1784 -0.0244 0.0037  0.0202  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1304 0.1383 0.1549 -0.0170 0.0143  0.0213  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1439 0.1537 0.1882 -0.0164 0.0097  0.0166  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1346 0.1333 0.1711 -0.0176 0.0123  0.0273  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1435 0.1548 0.1806 -0.0146 0.0211  0.0236  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1403 0.1338 0.1763 -0.0174 0.0128  0.0092  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1517 0.1548 0.1837 -0.0077 0.0228  0.0137  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1408 0.1330 0.1541 -0.0184 0.0036  0.0253  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1469 0.1628 0.2037 -0.0079 0.0047  0.0127  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1521 0.1433 0.1855 -0.0101 0.0143  0.0260  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1469 0.1591 0.2146 -0.0073 0.0097  0.0115  12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1614 0.1424 0.2076 0.0003  0.0232  0.0309  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1473 0.1648 0.2235 -0.0002 0.0226  0.0121  12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1547 0.1469 0.2026 -0.0059 0.0106  0.0192  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1472 0.1619 0.2377 -0.0044 -0.0003 0.0001  12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1296 0.1381 0.1858 -0.0170 0.0143  0.0263  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1313 0.1529 0.1767 -0.0117 0.0179  0.0215  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1367 0.1419 0.1992 -0.0126 0.0122  0.0366  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1357 0.1495 0.1956 -0.0146 0.0208  0.0214  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1370 0.1435 0.2072 -0.0193 0.0061  0.0561  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1390 0.1606 0.2093 -0.0218 0.0209  0.0248  13  THR   A C   
312  O  O   A THR   A 13  ? 0.1446 0.1477 0.2076 -0.0148 0.0054  0.0539  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1440 0.1642 0.2153 -0.0204 0.0106  0.0258  13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1417 0.1488 0.2062 -0.0095 0.0101  0.0377  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1337 0.1451 0.2081 -0.0101 0.0222  0.0277  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1498 0.1428 0.2205 -0.0093 0.0004  0.0387  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1282 0.1467 0.2127 -0.0121 0.0300  0.0346  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1439 0.1597 0.2188 -0.0040 0.0131  0.0260  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1351 0.1511 0.2237 -0.0014 0.0237  0.0219  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1340 0.1404 0.2112 -0.0250 -0.0015 0.0668  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1425 0.1642 0.2170 -0.0267 0.0188  0.0182  14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1429 0.1465 0.2087 -0.0186 -0.0056 0.0749  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1514 0.1712 0.2206 -0.0177 0.0071  0.0176  14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1419 0.1498 0.1965 -0.0149 -0.0116 0.0666  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1402 0.1574 0.1973 -0.0111 0.0041  0.0278  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1456 0.1560 0.2082 -0.0251 0.0007  0.0610  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1435 0.1638 0.1913 -0.0085 0.0125  0.0322  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1600 0.1550 0.2526 -0.0231 -0.0007 0.0808  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1769 0.1989 0.2691 -0.0134 0.0011  0.0143  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1837 0.1908 0.3141 -0.0252 0.0074  0.0592  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.2004 0.2338 0.3166 -0.0073 -0.0055 0.0161  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.1916 0.1958 0.3285 -0.0315 0.0046  0.0696  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.2174 0.2441 0.3385 0.0029  -0.0132 0.0316  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.1975 0.2061 0.3494 -0.0228 -0.0008 0.0238  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.2064 0.2505 0.3465 -0.0052 -0.0146 0.0014  14  ASP   A OD2 
358  N  N   A ASN   A 15  ? 0.1418 0.1472 0.2016 -0.0146 -0.0057 0.0617  15  ASN   A N   
359  N  N   B ASN   A 15  ? 0.1264 0.1429 0.1907 -0.0193 0.0059  0.0389  15  ASN   A N   
360  C  CA  A ASN   A 15  ? 0.1456 0.1479 0.2053 -0.0130 -0.0051 0.0529  15  ASN   A CA  
361  C  CA  B ASN   A 15  ? 0.1249 0.1392 0.2078 -0.0221 -0.0012 0.0246  15  ASN   A CA  
362  C  C   A ASN   A 15  ? 0.1378 0.1428 0.2015 -0.0118 0.0092  0.0475  15  ASN   A C   
363  C  C   B ASN   A 15  ? 0.1234 0.1361 0.2259 -0.0155 0.0083  0.0288  15  ASN   A C   
364  O  O   A ASN   A 15  ? 0.1343 0.1438 0.1849 -0.0114 0.0174  0.0438  15  ASN   A O   
365  O  O   B ASN   A 15  ? 0.1240 0.1343 0.2279 -0.0052 0.0129  0.0156  15  ASN   A O   
366  C  CB  A ASN   A 15  ? 0.1453 0.1518 0.1966 -0.0094 0.0002  0.0570  15  ASN   A CB  
367  C  CB  B ASN   A 15  ? 0.1168 0.1388 0.1830 -0.0225 0.0022  0.0211  15  ASN   A CB  
368  C  CG  A ASN   A 15  ? 0.1447 0.1594 0.1924 -0.0042 0.0149  0.0438  15  ASN   A CG  
369  C  CG  B ASN   A 15  ? 0.1195 0.1507 0.1939 -0.0134 0.0112  0.0107  15  ASN   A CG  
370  O  OD1 A ASN   A 15  ? 0.1503 0.1571 0.2053 -0.0133 0.0332  0.0395  15  ASN   A OD1 
371  O  OD1 B ASN   A 15  ? 0.1279 0.1523 0.2043 -0.0168 0.0198  0.0010  15  ASN   A OD1 
372  N  ND2 A ASN   A 15  ? 0.1495 0.1708 0.1867 -0.0022 0.0114  0.0490  15  ASN   A ND2 
373  N  ND2 B ASN   A 15  ? 0.1267 0.1599 0.1961 -0.0132 0.0093  0.0120  15  ASN   A ND2 
386  N  N   A VAL   A 16  ? 0.1343 0.1409 0.1921 -0.0037 0.0152  0.0405  16  VAL   A N   
387  N  N   B VAL   A 16  ? 0.1240 0.1392 0.2223 -0.0111 0.0092  0.0444  16  VAL   A N   
388  C  CA  A VAL   A 16  ? 0.1364 0.1448 0.1933 -0.0054 0.0118  0.0336  16  VAL   A CA  
389  C  CA  B VAL   A 16  ? 0.1291 0.1390 0.2144 -0.0103 0.0133  0.0579  16  VAL   A CA  
390  C  C   A VAL   A 16  ? 0.1292 0.1337 0.1898 -0.0131 0.0108  0.0230  16  VAL   A C   
391  C  C   B VAL   A 16  ? 0.1272 0.1438 0.2074 -0.0176 0.0058  0.0576  16  VAL   A C   
392  O  O   A VAL   A 16  ? 0.1229 0.1322 0.2026 -0.0137 0.0252  0.0067  16  VAL   A O   
393  O  O   B VAL   A 16  ? 0.1238 0.1441 0.2206 -0.0103 0.0138  0.0527  16  VAL   A O   
394  C  CB  A VAL   A 16  ? 0.1448 0.1617 0.2011 0.0107  0.0182  0.0346  16  VAL   A CB  
395  C  CB  B VAL   A 16  ? 0.1402 0.1444 0.2105 0.0026  0.0291  0.0603  16  VAL   A CB  
396  C  CG1 A VAL   A 16  ? 0.1574 0.1718 0.2040 0.0174  0.0239  0.0311  16  VAL   A CG1 
397  C  CG1 B VAL   A 16  ? 0.1515 0.1470 0.2111 0.0133  0.0288  0.0615  16  VAL   A CG1 
398  C  CG2 A VAL   A 16  ? 0.1490 0.1723 0.2059 0.0155  0.0303  0.0291  16  VAL   A CG2 
399  C  CG2 B VAL   A 16  ? 0.1473 0.1583 0.2325 0.0070  0.0398  0.0516  16  VAL   A CG2 
418  N  N   A TYR   A 17  ? 0.1240 0.1299 0.1973 -0.0068 0.0245  0.0230  17  TYR   A N   
419  N  N   B TYR   A 17  ? 0.1263 0.1413 0.2050 -0.0243 0.0080  0.0511  17  TYR   A N   
420  C  CA  A TYR   A 17  ? 0.1288 0.1393 0.1914 -0.0058 0.0273  0.0198  17  TYR   A CA  
421  C  CA  B TYR   A 17  ? 0.1284 0.1352 0.1817 -0.0309 0.0098  0.0484  17  TYR   A CA  
422  C  C   A TYR   A 17  ? 0.1327 0.1290 0.1921 -0.0048 0.0167  0.0177  17  TYR   A C   
423  C  C   B TYR   A 17  ? 0.1292 0.1317 0.1791 -0.0185 0.0138  0.0386  17  TYR   A C   
424  O  O   A TYR   A 17  ? 0.1339 0.1264 0.2059 0.0009  0.0191  0.0240  17  TYR   A O   
425  O  O   B TYR   A 17  ? 0.1284 0.1326 0.1921 -0.0261 0.0124  0.0402  17  TYR   A O   
426  C  CB  A TYR   A 17  ? 0.1434 0.1513 0.1973 -0.0066 0.0211  0.0215  17  TYR   A CB  
427  C  CB  B TYR   A 17  ? 0.1495 0.1326 0.1846 -0.0341 -0.0106 0.0493  17  TYR   A CB  
428  C  CG  A TYR   A 17  ? 0.1584 0.1685 0.2110 -0.0059 0.0205  0.0302  17  TYR   A CG  
429  C  CG  B TYR   A 17  ? 0.1691 0.1404 0.1871 -0.0344 -0.0161 0.0378  17  TYR   A CG  
430  C  CD1 A TYR   A 17  ? 0.1655 0.1732 0.2235 -0.0003 0.0172  0.0405  17  TYR   A CD1 
431  C  CD1 B TYR   A 17  ? 0.1745 0.1526 0.1845 -0.0243 -0.0144 0.0378  17  TYR   A CD1 
432  C  CD2 A TYR   A 17  ? 0.1630 0.1770 0.2200 -0.0052 0.0256  0.0318  17  TYR   A CD2 
433  C  CD2 B TYR   A 17  ? 0.1786 0.1404 0.1916 -0.0438 -0.0166 0.0279  17  TYR   A CD2 
434  C  CE1 A TYR   A 17  ? 0.1713 0.1744 0.2359 -0.0047 0.0150  0.0498  17  TYR   A CE1 
435  C  CE1 B TYR   A 17  ? 0.1741 0.1519 0.2012 -0.0308 -0.0166 0.0358  17  TYR   A CE1 
436  C  CE2 A TYR   A 17  ? 0.1706 0.1780 0.2298 -0.0039 0.0205  0.0362  17  TYR   A CE2 
437  C  CE2 B TYR   A 17  ? 0.1852 0.1450 0.1990 -0.0398 -0.0190 0.0258  17  TYR   A CE2 
438  C  CZ  A TYR   A 17  ? 0.1687 0.1787 0.2290 -0.0047 0.0077  0.0477  17  TYR   A CZ  
439  C  CZ  B TYR   A 17  ? 0.1786 0.1451 0.1870 -0.0418 -0.0210 0.0348  17  TYR   A CZ  
440  O  OH  A TYR   A 17  ? 0.1595 0.1832 0.2311 -0.0102 0.0024  0.0459  17  TYR   A OH  
441  O  OH  B TYR   A 17  ? 0.1903 0.1427 0.1953 -0.0410 -0.0229 0.0330  17  TYR   A OH  
460  N  N   A ILE   A 18  ? 0.1371 0.1331 0.1747 -0.0105 0.0182  0.0328  18  ILE   A N   
461  N  N   B ILE   A 18  ? 0.1292 0.1347 0.1803 -0.0176 0.0232  0.0398  18  ILE   A N   
462  C  CA  A ILE   A 18  ? 0.1467 0.1351 0.1892 -0.0133 0.0194  0.0297  18  ILE   A CA  
463  C  CA  B ILE   A 18  ? 0.1352 0.1342 0.1785 -0.0117 0.0324  0.0312  18  ILE   A CA  
464  C  C   A ILE   A 18  ? 0.1486 0.1373 0.2177 -0.0202 0.0298  0.0324  18  ILE   A C   
465  C  C   B ILE   A 18  ? 0.1398 0.1470 0.1884 -0.0092 0.0238  0.0229  18  ILE   A C   
466  O  O   A ILE   A 18  ? 0.1404 0.1350 0.2136 -0.0221 0.0302  0.0384  18  ILE   A O   
467  O  O   B ILE   A 18  ? 0.1339 0.1573 0.1880 -0.0153 0.0289  0.0203  18  ILE   A O   
468  C  CB  A ILE   A 18  ? 0.1527 0.1370 0.1776 -0.0021 0.0160  0.0239  18  ILE   A CB  
469  C  CB  B ILE   A 18  ? 0.1414 0.1361 0.1644 -0.0012 0.0280  0.0323  18  ILE   A CB  
470  C  CG1 A ILE   A 18  ? 0.1608 0.1402 0.1732 0.0106  -0.0001 0.0207  18  ILE   A CG1 
471  C  CG1 B ILE   A 18  ? 0.1548 0.1478 0.1712 -0.0044 0.0306  0.0392  18  ILE   A CG1 
472  C  CG2 A ILE   A 18  ? 0.1525 0.1274 0.1823 -0.0011 0.0183  0.0139  18  ILE   A CG2 
473  C  CG2 B ILE   A 18  ? 0.1458 0.1455 0.1777 -0.0075 0.0197  0.0347  18  ILE   A CG2 
474  C  CD1 A ILE   A 18  ? 0.1803 0.1500 0.1959 0.0249  -0.0021 0.0140  18  ILE   A CD1 
475  C  CD1 B ILE   A 18  ? 0.1747 0.1631 0.1840 -0.0007 0.0289  0.0238  18  ILE   A CD1 
498  N  N   A LYS   A 19  ? 0.1496 0.1359 0.2328 -0.0225 0.0512  0.0373  19  LYS   A N   
499  N  N   B LYS   A 19  ? 0.1452 0.1472 0.2077 -0.0000 0.0355  0.0189  19  LYS   A N   
500  C  CA  A LYS   A 19  ? 0.1580 0.1445 0.2654 -0.0148 0.0575  0.0411  19  LYS   A CA  
501  C  CA  B LYS   A 19  ? 0.1567 0.1587 0.2453 0.0140  0.0409  0.0200  19  LYS   A CA  
502  C  C   A LYS   A 19  ? 0.1508 0.1410 0.2889 -0.0091 0.0459  0.0500  19  LYS   A C   
503  C  C   B LYS   A 19  ? 0.1446 0.1603 0.2773 0.0181  0.0329  0.0362  19  LYS   A C   
504  O  O   A LYS   A 19  ? 0.1374 0.1366 0.2832 -0.0149 0.0320  0.0504  19  LYS   A O   
505  O  O   B LYS   A 19  ? 0.1409 0.1568 0.2736 0.0127  0.0153  0.0339  19  LYS   A O   
506  C  CB  A LYS   A 19  ? 0.1725 0.1575 0.2785 -0.0128 0.0705  0.0305  19  LYS   A CB  
507  C  CB  B LYS   A 19  ? 0.1733 0.1675 0.2455 0.0177  0.0542  -0.0015 19  LYS   A CB  
508  C  CG  A LYS   A 19  ? 0.1959 0.1712 0.2858 -0.0035 0.0780  0.0176  19  LYS   A CG  
509  C  CG  B LYS   A 19  ? 0.2027 0.1907 0.2517 0.0222  0.0658  -0.0166 19  LYS   A CG  
510  C  CD  A LYS   A 19  ? 0.2144 0.1822 0.2761 0.0045  0.0964  0.0105  19  LYS   A CD  
511  C  CD  B LYS   A 19  ? 0.2288 0.2088 0.2579 0.0234  0.0772  -0.0228 19  LYS   A CD  
512  C  CE  A LYS   A 19  ? 0.2269 0.1817 0.2851 0.0103  0.1034  -0.0018 19  LYS   A CE  
513  C  CE  B LYS   A 19  ? 0.2460 0.2249 0.2672 0.0180  0.0870  -0.0240 19  LYS   A CE  
514  N  NZ  A LYS   A 19  ? 0.2381 0.1829 0.2744 0.0055  0.1167  -0.0102 19  LYS   A NZ  
515  N  NZ  B LYS   A 19  ? 0.2525 0.2300 0.2705 0.0166  0.0896  -0.0333 19  LYS   A NZ  
542  N  N   A ASN   A 20  ? 0.1581 0.1479 0.3077 -0.0090 0.0497  0.0537  20  ASN   A N   
543  N  N   B ASN   A 20  ? 0.1443 0.1690 0.3118 0.0096  0.0399  0.0519  20  ASN   A N   
544  C  CA  A ASN   A 20  ? 0.1707 0.1613 0.3046 0.0082  0.0392  0.0360  20  ASN   A CA  
545  C  CA  B ASN   A 20  ? 0.1498 0.1832 0.3213 0.0188  0.0411  0.0512  20  ASN   A CA  
546  C  C   A ASN   A 20  ? 0.1826 0.1650 0.2817 0.0137  0.0371  0.0397  20  ASN   A C   
547  C  C   B ASN   A 20  ? 0.1692 0.1827 0.3098 0.0032  0.0553  0.0589  20  ASN   A C   
548  O  O   A ASN   A 20  ? 0.1911 0.1677 0.2668 0.0104  0.0344  0.0474  20  ASN   A O   
549  O  O   B ASN   A 20  ? 0.1882 0.1886 0.3126 -0.0009 0.0522  0.0558  20  ASN   A O   
550  C  CB  A ASN   A 20  ? 0.1789 0.1679 0.3160 0.0106  0.0373  0.0355  20  ASN   A CB  
551  C  CB  B ASN   A 20  ? 0.1476 0.1971 0.3311 0.0299  0.0330  0.0588  20  ASN   A CB  
552  C  CG  A ASN   A 20  ? 0.1879 0.1693 0.3270 0.0107  0.0382  0.0299  20  ASN   A CG  
553  C  CG  B ASN   A 20  ? 0.1528 0.2055 0.3390 0.0451  0.0275  0.0655  20  ASN   A CG  
554  O  OD1 A ASN   A 20  ? 0.2122 0.1925 0.3495 0.0151  0.0315  0.0246  20  ASN   A OD1 
555  O  OD1 B ASN   A 20  ? 0.1746 0.2104 0.3630 0.0483  0.0468  0.0565  20  ASN   A OD1 
556  N  ND2 A ASN   A 20  ? 0.1857 0.1536 0.3266 0.0023  0.0317  0.0300  20  ASN   A ND2 
557  N  ND2 B ASN   A 20  ? 0.1635 0.2100 0.3477 0.0469  0.0064  0.0744  20  ASN   A ND2 
570  N  N   A ALA   A 21  ? 0.1902 0.1683 0.2794 0.0185  0.0299  0.0217  21  ALA   A N   
571  N  N   B ALA   A 21  ? 0.1724 0.1773 0.2945 -0.0089 0.0574  0.0540  21  ALA   A N   
572  C  CA  A ALA   A 21  ? 0.2007 0.1740 0.2606 0.0186  0.0200  0.0261  21  ALA   A CA  
573  C  CA  B ALA   A 21  ? 0.1794 0.1711 0.2692 -0.0187 0.0524  0.0608  21  ALA   A CA  
574  C  C   A ALA   A 21  ? 0.2001 0.1802 0.2357 0.0128  0.0268  0.0126  21  ALA   A C   
575  C  C   B ALA   A 21  ? 0.1637 0.1572 0.2467 -0.0160 0.0434  0.0464  21  ALA   A C   
576  O  O   A ALA   A 21  ? 0.2052 0.1936 0.2234 0.0066  0.0225  0.0009  21  ALA   A O   
577  O  O   B ALA   A 21  ? 0.1581 0.1579 0.2560 -0.0183 0.0275  0.0300  21  ALA   A O   
578  C  CB  A ALA   A 21  ? 0.2163 0.1844 0.2831 0.0186  0.0054  0.0309  21  ALA   A CB  
579  C  CB  B ALA   A 21  ? 0.2002 0.1880 0.2753 -0.0270 0.0467  0.0639  21  ALA   A CB  
590  N  N   A ASP   A 22  ? 0.1990 0.1743 0.2327 0.0043  0.0348  0.0130  22  ASP   A N   
591  N  N   B ASP   A 22  ? 0.1655 0.1505 0.2359 -0.0113 0.0465  0.0414  22  ASP   A N   
592  C  CA  A ASP   A 22  ? 0.2029 0.1762 0.2332 0.0051  0.0315  0.0110  22  ASP   A CA  
593  C  CA  B ASP   A 22  ? 0.1752 0.1505 0.2146 -0.0047 0.0367  0.0389  22  ASP   A CA  
594  C  C   A ASP   A 22  ? 0.1959 0.1757 0.2070 0.0009  0.0261  0.0065  22  ASP   A C   
595  C  C   B ASP   A 22  ? 0.1567 0.1563 0.1859 -0.0132 0.0387  0.0301  22  ASP   A C   
596  O  O   A ASP   A 22  ? 0.1962 0.1854 0.2210 -0.0035 0.0284  0.0007  22  ASP   A O   
597  O  O   B ASP   A 22  ? 0.1483 0.1689 0.1823 -0.0206 0.0386  0.0077  22  ASP   A O   
598  C  CB  A ASP   A 22  ? 0.2165 0.1819 0.2761 0.0068  0.0283  0.0092  22  ASP   A CB  
599  C  CB  B ASP   A 22  ? 0.1994 0.1545 0.2309 0.0064  0.0387  0.0317  22  ASP   A CB  
600  C  CG  A ASP   A 22  ? 0.2293 0.1887 0.3144 0.0018  0.0234  0.0128  22  ASP   A CG  
601  C  CG  B ASP   A 22  ? 0.2159 0.1561 0.2401 0.0113  0.0486  0.0311  22  ASP   A CG  
602  O  OD1 A ASP   A 22  ? 0.2247 0.1802 0.3372 -0.0106 0.0133  0.0284  22  ASP   A OD1 
603  O  OD1 B ASP   A 22  ? 0.2090 0.1483 0.2122 0.0049  0.0526  0.0299  22  ASP   A OD1 
604  O  OD2 A ASP   A 22  ? 0.2448 0.2000 0.3344 0.0095  0.0294  -0.0030 22  ASP   A OD2 
605  O  OD2 B ASP   A 22  ? 0.2372 0.1708 0.2705 0.0118  0.0635  0.0276  22  ASP   A OD2 
614  N  N   A ILE   A 23  ? 0.1932 0.1724 0.1903 0.0008  0.0241  0.0016  23  ILE   A N   
615  N  N   B ILE   A 23  ? 0.1521 0.1547 0.1891 -0.0133 0.0342  0.0253  23  ILE   A N   
616  C  CA  A ILE   A 23  ? 0.1856 0.1622 0.1745 0.0045  0.0283  0.0104  23  ILE   A CA  
617  C  CA  B ILE   A 23  ? 0.1482 0.1566 0.1755 -0.0143 0.0260  0.0293  23  ILE   A CA  
618  C  C   A ILE   A 23  ? 0.1817 0.1724 0.1788 0.0037  0.0379  0.0127  23  ILE   A C   
619  C  C   B ILE   A 23  ? 0.1565 0.1683 0.1790 -0.0176 0.0294  0.0157  23  ILE   A C   
620  O  O   A ILE   A 23  ? 0.1844 0.1779 0.1852 0.0017  0.0355  0.0047  23  ILE   A O   
621  O  O   B ILE   A 23  ? 0.1556 0.1715 0.1835 -0.0223 0.0270  0.0109  23  ILE   A O   
622  C  CB  A ILE   A 23  ? 0.1905 0.1561 0.1617 0.0082  0.0226  0.0075  23  ILE   A CB  
623  C  CB  B ILE   A 23  ? 0.1456 0.1528 0.1671 -0.0067 0.0157  0.0180  23  ILE   A CB  
624  C  CG1 A ILE   A 23  ? 0.1965 0.1584 0.1732 0.0084  0.0253  0.0044  23  ILE   A CG1 
625  C  CG1 B ILE   A 23  ? 0.1509 0.1508 0.1596 -0.0080 0.0067  0.0042  23  ILE   A CG1 
626  C  CG2 A ILE   A 23  ? 0.1864 0.1556 0.1671 0.0062  0.0198  0.0109  23  ILE   A CG2 
627  C  CG2 B ILE   A 23  ? 0.1425 0.1519 0.1518 -0.0012 0.0128  0.0202  23  ILE   A CG2 
628  C  CD1 A ILE   A 23  ? 0.1994 0.1617 0.1766 0.0079  0.0188  -0.0000 23  ILE   A CD1 
629  C  CD1 B ILE   A 23  ? 0.1439 0.1494 0.1548 0.0013  0.0003  0.0017  23  ILE   A CD1 
652  N  N   A VAL   A 24  ? 0.1860 0.1833 0.1884 -0.0024 0.0367  0.0119  24  VAL   A N   
653  N  N   B VAL   A 24  ? 0.1657 0.1747 0.1795 -0.0270 0.0258  0.0156  24  VAL   A N   
654  C  CA  A VAL   A 24  ? 0.1985 0.1988 0.2021 -0.0094 0.0352  -0.0030 24  VAL   A CA  
655  C  CA  B VAL   A 24  ? 0.1900 0.1842 0.1863 -0.0247 0.0309  0.0072  24  VAL   A CA  
656  C  C   A VAL   A 24  ? 0.2030 0.2141 0.2053 -0.0214 0.0283  -0.0060 24  VAL   A C   
657  C  C   B VAL   A 24  ? 0.1986 0.2056 0.1990 -0.0242 0.0381  0.0030  24  VAL   A C   
658  O  O   A VAL   A 24  ? 0.2044 0.2108 0.1953 -0.0168 0.0341  -0.0045 24  VAL   A O   
659  O  O   B VAL   A 24  ? 0.2031 0.2061 0.2073 -0.0249 0.0375  0.0030  24  VAL   A O   
660  C  CB  A VAL   A 24  ? 0.2049 0.1996 0.2108 -0.0077 0.0545  -0.0118 24  VAL   A CB  
661  C  CB  B VAL   A 24  ? 0.2030 0.1837 0.2101 -0.0299 0.0326  0.0127  24  VAL   A CB  
662  C  CG1 A VAL   A 24  ? 0.2087 0.2058 0.2080 -0.0060 0.0713  -0.0256 24  VAL   A CG1 
663  C  CG1 B VAL   A 24  ? 0.2193 0.1924 0.2459 -0.0276 0.0235  0.0130  24  VAL   A CG1 
664  C  CG2 A VAL   A 24  ? 0.2138 0.1998 0.2223 -0.0012 0.0643  -0.0037 24  VAL   A CG2 
665  C  CG2 B VAL   A 24  ? 0.2107 0.1809 0.2020 -0.0336 0.0361  0.0047  24  VAL   A CG2 
684  N  N   A GLU   A 25  ? 0.2089 0.2384 0.2088 -0.0300 0.0340  -0.0155 25  GLU   A N   
685  N  N   B GLU   A 25  ? 0.2004 0.2271 0.2094 -0.0220 0.0569  -0.0085 25  GLU   A N   
686  C  CA  A GLU   A 25  ? 0.2204 0.2647 0.2162 -0.0296 0.0468  -0.0228 25  GLU   A CA  
687  C  CA  B GLU   A 25  ? 0.2124 0.2522 0.2237 -0.0286 0.0626  -0.0065 25  GLU   A CA  
688  C  C   A GLU   A 25  ? 0.2117 0.2688 0.1906 -0.0425 0.0610  -0.0175 25  GLU   A C   
689  C  C   B GLU   A 25  ? 0.2092 0.2625 0.2162 -0.0340 0.0709  -0.0035 25  GLU   A C   
690  O  O   A GLU   A 25  ? 0.2181 0.2795 0.1898 -0.0455 0.0636  -0.0177 25  GLU   A O   
691  O  O   B GLU   A 25  ? 0.2168 0.2684 0.2271 -0.0366 0.0648  -0.0005 25  GLU   A O   
692  C  CB  A GLU   A 25  ? 0.2429 0.2864 0.2564 -0.0239 0.0411  -0.0305 25  GLU   A CB  
693  C  CB  B GLU   A 25  ? 0.2318 0.2653 0.2605 -0.0301 0.0545  -0.0103 25  GLU   A CB  
694  C  CG  A GLU   A 25  ? 0.2645 0.3043 0.3009 -0.0224 0.0222  -0.0372 25  GLU   A CG  
695  C  CG  B GLU   A 25  ? 0.2571 0.2812 0.3172 -0.0325 0.0391  -0.0156 25  GLU   A CG  
696  C  CD  A GLU   A 25  ? 0.2812 0.3196 0.3414 -0.0172 0.0066  -0.0383 25  GLU   A CD  
697  C  CD  B GLU   A 25  ? 0.2756 0.2970 0.3693 -0.0351 0.0189  -0.0119 25  GLU   A CD  
698  O  OE1 A GLU   A 25  ? 0.2911 0.3271 0.3485 -0.0148 -0.0078 -0.0442 25  GLU   A OE1 
699  O  OE1 B GLU   A 25  ? 0.2858 0.3064 0.4010 -0.0355 0.0084  -0.0085 25  GLU   A OE1 
700  O  OE2 A GLU   A 25  ? 0.2847 0.3263 0.3669 -0.0119 0.0034  -0.0382 25  GLU   A OE2 
701  O  OE2 B GLU   A 25  ? 0.2825 0.3008 0.3898 -0.0364 0.0104  -0.0113 25  GLU   A OE2 
714  N  N   A GLU   A 26  ? 0.2046 0.2599 0.1971 -0.0535 0.0644  -0.0145 26  GLU   A N   
715  N  N   B GLU   A 26  ? 0.2047 0.2623 0.2198 -0.0395 0.0755  -0.0045 26  GLU   A N   
716  C  CA  A GLU   A 26  ? 0.2136 0.2548 0.1809 -0.0620 0.0533  -0.0037 26  GLU   A CA  
717  C  CA  B GLU   A 26  ? 0.2156 0.2649 0.2226 -0.0400 0.0685  0.0052  26  GLU   A CA  
718  C  C   A GLU   A 26  ? 0.2102 0.2417 0.1514 -0.0643 0.0438  -0.0032 26  GLU   A C   
719  C  C   B GLU   A 26  ? 0.2131 0.2538 0.1949 -0.0295 0.0681  0.0135  26  GLU   A C   
720  O  O   A GLU   A 26  ? 0.2148 0.2378 0.1463 -0.0702 0.0346  -0.0025 26  GLU   A O   
721  O  O   B GLU   A 26  ? 0.2203 0.2527 0.1946 -0.0316 0.0733  0.0117  26  GLU   A O   
722  C  CB  A GLU   A 26  ? 0.2293 0.2556 0.2065 -0.0668 0.0497  0.0097  26  GLU   A CB  
723  C  CB  B GLU   A 26  ? 0.2287 0.2734 0.2555 -0.0540 0.0543  0.0061  26  GLU   A CB  
724  C  CG  A GLU   A 26  ? 0.2447 0.2615 0.2620 -0.0651 0.0530  0.0078  26  GLU   A CG  
725  C  CG  B GLU   A 26  ? 0.2394 0.2803 0.2750 -0.0616 0.0615  -0.0027 26  GLU   A CG  
726  C  CD  A GLU   A 26  ? 0.2551 0.2657 0.2943 -0.0638 0.0717  0.0135  26  GLU   A CD  
727  C  CD  B GLU   A 26  ? 0.2469 0.2843 0.2864 -0.0712 0.0732  -0.0054 26  GLU   A CD  
728  O  OE1 A GLU   A 26  ? 0.2495 0.2817 0.3102 -0.0463 0.0972  -0.0199 26  GLU   A OE1 
729  O  OE1 B GLU   A 26  ? 0.2537 0.3027 0.3000 -0.0569 0.0892  -0.0190 26  GLU   A OE1 
730  O  OE2 A GLU   A 26  ? 0.2692 0.2659 0.2977 -0.0638 0.0703  0.0367  26  GLU   A OE2 
731  O  OE2 B GLU   A 26  ? 0.2441 0.2759 0.2571 -0.0858 0.0794  -0.0056 26  GLU   A OE2 
744  N  N   A ALA   A 27  ? 0.1967 0.2280 0.1512 -0.0675 0.0461  -0.0057 27  ALA   A N   
745  N  N   B ALA   A 27  ? 0.2013 0.2438 0.1773 -0.0193 0.0561  0.0243  27  ALA   A N   
746  C  CA  A ALA   A 27  ? 0.2008 0.2291 0.1451 -0.0613 0.0476  -0.0102 27  ALA   A CA  
747  C  CA  B ALA   A 27  ? 0.2069 0.2452 0.1611 -0.0073 0.0422  0.0286  27  ALA   A CA  
748  C  C   A ALA   A 27  ? 0.2215 0.2411 0.1649 -0.0624 0.0535  -0.0244 27  ALA   A C   
749  C  C   B ALA   A 27  ? 0.2273 0.2597 0.1653 -0.0004 0.0388  0.0221  27  ALA   A C   
750  O  O   A ALA   A 27  ? 0.2279 0.2393 0.1721 -0.0691 0.0494  -0.0246 27  ALA   A O   
751  O  O   B ALA   A 27  ? 0.2253 0.2552 0.1660 0.0018  0.0311  0.0322  27  ALA   A O   
752  C  CB  A ALA   A 27  ? 0.1927 0.2179 0.1546 -0.0626 0.0349  -0.0027 27  ALA   A CB  
753  C  CB  B ALA   A 27  ? 0.1989 0.2357 0.1551 -0.0106 0.0299  0.0351  27  ALA   A CB  
764  N  N   A LYS   A 28  ? 0.2459 0.2632 0.1906 -0.0497 0.0561  -0.0427 28  LYS   A N   
765  N  N   B LYS   A 28  ? 0.2552 0.2801 0.1887 0.0075  0.0462  0.0021  28  LYS   A N   
766  C  CA  A LYS   A 28  ? 0.2749 0.2926 0.2247 -0.0400 0.0604  -0.0459 28  LYS   A CA  
767  C  CA  B LYS   A 28  ? 0.2869 0.3100 0.2209 0.0146  0.0524  -0.0134 28  LYS   A CA  
768  C  C   A LYS   A 28  ? 0.2921 0.3193 0.2264 -0.0398 0.0778  -0.0334 28  LYS   A C   
769  C  C   B LYS   A 28  ? 0.3132 0.3369 0.2192 0.0096  0.0617  -0.0068 28  LYS   A C   
770  O  O   A LYS   A 28  ? 0.2949 0.3226 0.2537 -0.0356 0.0616  -0.0324 28  LYS   A O   
771  O  O   B LYS   A 28  ? 0.3206 0.3426 0.2310 0.0151  0.0433  -0.0064 28  LYS   A O   
772  C  CB  A LYS   A 28  ? 0.2843 0.2979 0.2546 -0.0299 0.0565  -0.0527 28  LYS   A CB  
773  C  CB  B LYS   A 28  ? 0.2948 0.3157 0.2590 0.0231  0.0491  -0.0282 28  LYS   A CB  
774  C  CG  A LYS   A 28  ? 0.2926 0.3031 0.2792 -0.0219 0.0573  -0.0545 28  LYS   A CG  
775  C  CG  B LYS   A 28  ? 0.3028 0.3251 0.2917 0.0265  0.0524  -0.0333 28  LYS   A CG  
776  C  CD  A LYS   A 28  ? 0.2999 0.3141 0.3191 -0.0152 0.0568  -0.0439 28  LYS   A CD  
777  C  CD  B LYS   A 28  ? 0.3140 0.3380 0.3319 0.0281  0.0543  -0.0347 28  LYS   A CD  
778  C  CE  A LYS   A 28  ? 0.3067 0.3232 0.3473 -0.0111 0.0605  -0.0407 28  LYS   A CE  
779  C  CE  B LYS   A 28  ? 0.3248 0.3493 0.3617 0.0284  0.0541  -0.0364 28  LYS   A CE  
780  N  NZ  A LYS   A 28  ? 0.3121 0.3283 0.3615 -0.0060 0.0679  -0.0447 28  LYS   A NZ  
781  N  NZ  B LYS   A 28  ? 0.3320 0.3564 0.3766 0.0302  0.0516  -0.0407 28  LYS   A NZ  
808  N  N   A LYS   A 29  ? 0.3043 0.3433 0.2212 -0.0483 0.1067  -0.0135 29  LYS   A N   
809  N  N   B LYS   A 29  ? 0.3286 0.3583 0.2256 -0.0045 0.0914  0.0064  29  LYS   A N   
810  C  CA  A LYS   A 29  ? 0.3211 0.3685 0.2428 -0.0565 0.1163  0.0015  29  LYS   A CA  
811  C  CA  B LYS   A 29  ? 0.3465 0.3803 0.2508 -0.0190 0.1032  0.0140  29  LYS   A CA  
812  C  C   A LYS   A 29  ? 0.3196 0.3668 0.2216 -0.0699 0.1088  0.0063  29  LYS   A C   
813  C  C   B LYS   A 29  ? 0.3446 0.3764 0.2308 -0.0334 0.1017  0.0187  29  LYS   A C   
814  O  O   A LYS   A 29  ? 0.3225 0.3764 0.2221 -0.0677 0.1069  0.0067  29  LYS   A O   
815  O  O   B LYS   A 29  ? 0.3460 0.3849 0.2318 -0.0326 0.1111  0.0241  29  LYS   A O   
816  C  CB  A LYS   A 29  ? 0.3363 0.3935 0.2978 -0.0494 0.1284  0.0073  29  LYS   A CB  
817  C  CB  B LYS   A 29  ? 0.3640 0.4047 0.3003 -0.0172 0.1113  0.0120  29  LYS   A CB  
818  C  CG  A LYS   A 29  ? 0.3529 0.4155 0.3639 -0.0420 0.1255  0.0087  29  LYS   A CG  
819  C  CG  B LYS   A 29  ? 0.3826 0.4267 0.3616 -0.0145 0.1089  0.0074  29  LYS   A CG  
820  C  CD  A LYS   A 29  ? 0.3678 0.4344 0.4280 -0.0365 0.1205  0.0063  29  LYS   A CD  
821  C  CD  B LYS   A 29  ? 0.3976 0.4461 0.4199 -0.0126 0.1067  0.0020  29  LYS   A CD  
822  C  CE  A LYS   A 29  ? 0.3769 0.4470 0.4686 -0.0334 0.1195  0.0030  29  LYS   A CE  
823  C  CE  B LYS   A 29  ? 0.4074 0.4599 0.4572 -0.0121 0.1076  -0.0046 29  LYS   A CE  
824  N  NZ  A LYS   A 29  ? 0.3806 0.4537 0.4979 -0.0313 0.1170  0.0009  29  LYS   A NZ  
825  N  NZ  B LYS   A 29  ? 0.4121 0.4672 0.4832 -0.0114 0.1058  -0.0073 29  LYS   A NZ  
852  N  N   A VAL   A 30  ? 0.3145 0.3541 0.2020 -0.0842 0.1028  0.0124  30  VAL   A N   
853  N  N   B VAL   A 30  ? 0.3386 0.3617 0.2119 -0.0492 0.0928  0.0210  30  VAL   A N   
854  C  CA  A VAL   A 30  ? 0.3122 0.3415 0.1917 -0.0976 0.0813  0.0257  30  VAL   A CA  
855  C  CA  B VAL   A 30  ? 0.3349 0.3461 0.2009 -0.0648 0.0701  0.0321  30  VAL   A CA  
856  C  C   A VAL   A 30  ? 0.3231 0.3316 0.1575 -0.0938 0.0618  0.0310  30  VAL   A C   
857  C  C   B VAL   A 30  ? 0.3345 0.3342 0.1611 -0.0763 0.0562  0.0321  30  VAL   A C   
858  O  O   A VAL   A 30  ? 0.3301 0.3352 0.1617 -0.0938 0.0521  0.0333  30  VAL   A O   
859  O  O   B VAL   A 30  ? 0.3412 0.3376 0.1615 -0.0755 0.0479  0.0328  30  VAL   A O   
860  C  CB  A VAL   A 30  ? 0.3020 0.3379 0.2243 -0.1125 0.0674  0.0298  30  VAL   A CB  
861  C  CB  B VAL   A 30  ? 0.3328 0.3413 0.2351 -0.0677 0.0541  0.0385  30  VAL   A CB  
862  C  CG1 A VAL   A 30  ? 0.3013 0.3353 0.2356 -0.1141 0.0563  0.0319  30  VAL   A CG1 
863  C  CG1 B VAL   A 30  ? 0.3343 0.3392 0.2500 -0.0651 0.0416  0.0380  30  VAL   A CG1 
864  C  CG2 A VAL   A 30  ? 0.2988 0.3412 0.2456 -0.1192 0.0649  0.0290  30  VAL   A CG2 
865  C  CG2 B VAL   A 30  ? 0.3331 0.3424 0.2536 -0.0705 0.0513  0.0434  30  VAL   A CG2 
884  N  N   . LYS   A 31  ? 0.3256 0.3192 0.1468 -0.0860 0.0443  0.0265  31  LYS   A N   
885  C  CA  . LYS   A 31  ? 0.3349 0.3112 0.1536 -0.0748 0.0136  0.0223  31  LYS   A CA  
886  C  C   . LYS   A 31  ? 0.3068 0.2881 0.1286 -0.0610 0.0010  0.0569  31  LYS   A C   
887  O  O   . LYS   A 31  ? 0.3169 0.3046 0.1490 -0.0597 -0.0201 0.0611  31  LYS   A O   
888  C  CB  . LYS   A 31  ? 0.3760 0.3368 0.2755 -0.0708 -0.0103 -0.0059 31  LYS   A CB  
889  C  CG  . LYS   A 31  ? 0.4202 0.3662 0.4201 -0.0612 -0.0345 -0.0230 31  LYS   A CG  
890  C  CD  . LYS   A 31  ? 0.4566 0.3892 0.5297 -0.0544 -0.0562 -0.0379 31  LYS   A CD  
891  C  CE  . LYS   A 31  ? 0.4812 0.4067 0.5988 -0.0477 -0.0732 -0.0503 31  LYS   A CE  
892  N  NZ  . LYS   A 31  ? 0.4947 0.4157 0.6393 -0.0431 -0.0837 -0.0584 31  LYS   A NZ  
907  N  N   . PRO   A 32  ? 0.2633 0.2511 0.1148 -0.0577 0.0049  0.0407  32  PRO   A N   
908  C  CA  . PRO   A 32  ? 0.2540 0.2339 0.1420 -0.0538 -0.0017 0.0569  32  PRO   A CA  
909  C  C   . PRO   A 32  ? 0.2485 0.2333 0.1459 -0.0454 -0.0128 0.0513  32  PRO   A C   
910  O  O   . PRO   A 32  ? 0.2404 0.2274 0.1569 -0.0488 -0.0372 0.0540  32  PRO   A O   
911  C  CB  . PRO   A 32  ? 0.2435 0.2363 0.1531 -0.0521 -0.0065 0.0431  32  PRO   A CB  
912  C  CG  . PRO   A 32  ? 0.2372 0.2408 0.1099 -0.0478 -0.0120 0.0265  32  PRO   A CG  
913  C  CD  . PRO   A 32  ? 0.2429 0.2448 0.1096 -0.0540 -0.0068 0.0255  32  PRO   A CD  
921  N  N   . THR   A 33  ? 0.2517 0.2313 0.1279 -0.0395 -0.0098 0.0505  33  THR   A N   
922  C  CA  . THR   A 33  ? 0.2509 0.2324 0.1414 -0.0263 -0.0290 0.0454  33  THR   A CA  
923  C  C   . THR   A 33  ? 0.2216 0.2125 0.1258 -0.0261 -0.0259 0.0415  33  THR   A C   
924  O  O   . THR   A 33  ? 0.2166 0.2106 0.1516 -0.0307 -0.0355 0.0486  33  THR   A O   
925  C  CB  . THR   A 33  ? 0.2773 0.2543 0.1612 -0.0172 -0.0380 0.0650  33  THR   A CB  
926  O  OG1 . THR   A 33  ? 0.3018 0.2690 0.1880 -0.0026 -0.0253 0.0749  33  THR   A OG1 
927  C  CG2 . THR   A 33  ? 0.2783 0.2618 0.1886 -0.0137 -0.0516 0.0643  33  THR   A CG2 
935  N  N   . VAL   A 34  ? 0.1943 0.1961 0.1229 -0.0266 -0.0162 0.0427  34  VAL   A N   
936  C  CA  . VAL   A 34  ? 0.1740 0.1780 0.1100 -0.0259 -0.0113 0.0376  34  VAL   A CA  
937  C  C   . VAL   A 34  ? 0.1657 0.1658 0.1155 -0.0265 -0.0035 0.0286  34  VAL   A C   
938  O  O   . VAL   A 34  ? 0.1675 0.1691 0.1491 -0.0304 -0.0028 0.0356  34  VAL   A O   
939  C  CB  . VAL   A 34  ? 0.1762 0.1784 0.1343 -0.0237 -0.0056 0.0228  34  VAL   A CB  
940  C  CG1 . VAL   A 34  ? 0.1812 0.1739 0.1399 -0.0180 0.0001  0.0168  34  VAL   A CG1 
941  C  CG2 . VAL   A 34  ? 0.1761 0.1897 0.1778 -0.0174 -0.0238 0.0182  34  VAL   A CG2 
951  N  N   . VAL   A 35  ? 0.1495 0.1527 0.1272 -0.0273 -0.0087 0.0296  35  VAL   A N   
952  C  CA  . VAL   A 35  ? 0.1433 0.1491 0.1209 -0.0173 -0.0019 0.0236  35  VAL   A CA  
953  C  C   . VAL   A 35  ? 0.1378 0.1396 0.1122 -0.0134 0.0028  0.0220  35  VAL   A C   
954  O  O   . VAL   A 35  ? 0.1317 0.1507 0.1402 -0.0221 0.0109  0.0169  35  VAL   A O   
955  C  CB  . VAL   A 35  ? 0.1502 0.1520 0.1265 -0.0120 0.0093  0.0102  35  VAL   A CB  
956  C  CG1 . VAL   A 35  ? 0.1546 0.1589 0.1315 -0.0021 0.0062  0.0016  35  VAL   A CG1 
957  C  CG2 . VAL   A 35  ? 0.1526 0.1555 0.1561 -0.0074 0.0163  0.0060  35  VAL   A CG2 
967  N  N   . VAL   A 36  ? 0.1314 0.1386 0.1113 -0.0189 0.0041  0.0286  36  VAL   A N   
968  C  CA  . VAL   A 36  ? 0.1234 0.1300 0.1129 -0.0118 -0.0027 0.0182  36  VAL   A CA  
969  C  C   . VAL   A 36  ? 0.1208 0.1300 0.1191 -0.0118 0.0041  0.0219  36  VAL   A C   
970  O  O   . VAL   A 36  ? 0.1234 0.1305 0.1463 -0.0063 0.0183  0.0233  36  VAL   A O   
971  C  CB  . VAL   A 36  ? 0.1212 0.1224 0.1251 -0.0095 0.0058  0.0139  36  VAL   A CB  
972  C  CG1 . VAL   A 36  ? 0.1310 0.1254 0.1320 -0.0133 -0.0008 0.0048  36  VAL   A CG1 
973  C  CG2 . VAL   A 36  ? 0.1319 0.1260 0.1486 -0.0055 0.0058  0.0232  36  VAL   A CG2 
983  N  N   . ASN   A 37  ? 0.1142 0.1172 0.1211 -0.0004 0.0059  0.0211  37  ASN   A N   
984  C  CA  . ASN   A 37  ? 0.1128 0.1184 0.1176 0.0043  0.0075  0.0183  37  ASN   A CA  
985  C  C   . ASN   A 37  ? 0.1078 0.1166 0.1272 0.0011  0.0103  0.0276  37  ASN   A C   
986  O  O   . ASN   A 37  ? 0.1214 0.1283 0.1217 0.0065  0.0078  0.0181  37  ASN   A O   
987  C  CB  . ASN   A 37  ? 0.1161 0.1169 0.1266 0.0025  0.0088  0.0122  37  ASN   A CB  
988  C  CG  . ASN   A 37  ? 0.1213 0.1168 0.1403 0.0023  0.0105  0.0127  37  ASN   A CG  
989  O  OD1 . ASN   A 37  ? 0.1176 0.1194 0.1612 0.0009  0.0056  0.0235  37  ASN   A OD1 
990  N  ND2 . ASN   A 37  ? 0.1222 0.1177 0.1463 -0.0020 -0.0011 0.0310  37  ASN   A ND2 
997  N  N   A ALA   A 38  ? 0.1160 0.1220 0.1263 -0.0040 0.0144  0.0174  38  ALA   A N   
998  N  N   B ALA   A 38  ? 0.1126 0.1298 0.1381 0.0030  0.0095  0.0202  38  ALA   A N   
999  C  CA  A ALA   A 38  ? 0.1302 0.1193 0.1161 -0.0084 0.0091  0.0094  38  ALA   A CA  
1000 C  CA  B ALA   A 38  ? 0.1235 0.1381 0.1420 0.0026  -0.0014 0.0173  38  ALA   A CA  
1001 C  C   A ALA   A 38  ? 0.1276 0.1189 0.1102 -0.0024 -0.0008 0.0027  38  ALA   A C   
1002 C  C   B ALA   A 38  ? 0.1194 0.1347 0.1403 0.0103  -0.0121 0.0130  38  ALA   A C   
1003 O  O   A ALA   A 38  ? 0.1288 0.1096 0.0995 -0.0065 -0.0024 -0.0039 38  ALA   A O   
1004 O  O   B ALA   A 38  ? 0.1163 0.1327 0.1410 0.0081  -0.0195 0.0128  38  ALA   A O   
1005 C  CB  A ALA   A 38  ? 0.1352 0.1320 0.1187 -0.0173 0.0093  0.0119  38  ALA   A CB  
1006 C  CB  B ALA   A 38  ? 0.1256 0.1521 0.1585 -0.0037 -0.0081 0.0137  38  ALA   A CB  
1017 N  N   A ALA   A 39  ? 0.1226 0.1173 0.1119 0.0017  0.0065  0.0117  39  ALA   A N   
1018 N  N   B ALA   A 39  ? 0.1243 0.1350 0.1480 0.0076  -0.0071 0.0179  39  ALA   A N   
1019 C  CA  A ALA   A 39  ? 0.1155 0.1142 0.1130 0.0046  0.0106  0.0112  39  ALA   A CA  
1020 C  CA  B ALA   A 39  ? 0.1299 0.1317 0.1411 -0.0021 -0.0063 0.0109  39  ALA   A CA  
1021 C  C   A ALA   A 39  ? 0.1216 0.1187 0.1200 0.0029  0.0000  0.0075  39  ALA   A C   
1022 C  C   B ALA   A 39  ? 0.1279 0.1217 0.1477 -0.0045 -0.0069 0.0110  39  ALA   A C   
1023 O  O   A ALA   A 39  ? 0.1259 0.1269 0.1094 0.0001  0.0073  0.0127  39  ALA   A O   
1024 O  O   B ALA   A 39  ? 0.1440 0.1233 0.1519 -0.0097 -0.0001 0.0029  39  ALA   A O   
1025 C  CB  A ALA   A 39  ? 0.1181 0.1253 0.1397 0.0094  -0.0006 0.0102  39  ALA   A CB  
1026 C  CB  B ALA   A 39  ? 0.1436 0.1450 0.1520 -0.0015 -0.0157 0.0041  39  ALA   A CB  
1037 N  N   A ASN   A 40  ? 0.1257 0.1241 0.1184 -0.0041 0.0072  0.0011  40  ASN   A N   
1038 N  N   B ASN   A 40  ? 0.1298 0.1208 0.1455 -0.0097 0.0115  0.0121  40  ASN   A N   
1039 C  CA  A ASN   A 40  ? 0.1358 0.1248 0.1146 -0.0001 0.0042  -0.0087 40  ASN   A CA  
1040 C  CA  B ASN   A 40  ? 0.1416 0.1205 0.1351 -0.0066 0.0009  0.0170  40  ASN   A CA  
1041 C  C   A ASN   A 40  ? 0.1409 0.1204 0.1151 0.0040  0.0147  0.0032  40  ASN   A C   
1042 C  C   B ASN   A 40  ? 0.1466 0.1124 0.1113 -0.0106 0.0166  0.0279  40  ASN   A C   
1043 O  O   A ASN   A 40  ? 0.1424 0.1264 0.1260 0.0008  0.0153  0.0049  40  ASN   A O   
1044 O  O   B ASN   A 40  ? 0.1355 0.1107 0.1153 -0.0167 0.0136  0.0289  40  ASN   A O   
1045 C  CB  A ASN   A 40  ? 0.1455 0.1323 0.1354 0.0030  -0.0020 -0.0039 40  ASN   A CB  
1046 C  CB  B ASN   A 40  ? 0.1462 0.1237 0.1455 -0.0029 -0.0106 0.0202  40  ASN   A CB  
1047 C  CG  A ASN   A 40  ? 0.1551 0.1351 0.1776 0.0051  0.0004  0.0052  40  ASN   A CG  
1048 C  CG  B ASN   A 40  ? 0.1492 0.1286 0.1573 -0.0027 -0.0173 0.0153  40  ASN   A CG  
1049 O  OD1 A ASN   A 40  ? 0.1599 0.1319 0.1776 0.0089  -0.0089 0.0165  40  ASN   A OD1 
1050 O  OD1 B ASN   A 40  ? 0.1566 0.1349 0.1536 -0.0030 -0.0039 0.0083  40  ASN   A OD1 
1051 N  ND2 A ASN   A 40  ? 0.1541 0.1474 0.1946 0.0085  0.0088  -0.0042 40  ASN   A ND2 
1052 N  ND2 B ASN   A 40  ? 0.1456 0.1390 0.1773 -0.0088 -0.0119 -0.0039 40  ASN   A ND2 
1065 N  N   A VAL   A 41  ? 0.1475 0.1234 0.1176 0.0082  0.0103  0.0087  41  VAL   A N   
1066 N  N   B VAL   A 41  ? 0.1614 0.1156 0.1176 -0.0064 0.0166  0.0311  41  VAL   A N   
1067 C  CA  A VAL   A 41  ? 0.1493 0.1282 0.1321 0.0050  0.0234  0.0120  41  VAL   A CA  
1068 C  CA  B VAL   A 41  ? 0.1663 0.1261 0.1356 -0.0029 0.0306  0.0274  41  VAL   A CA  
1069 C  C   A VAL   A 41  ? 0.1495 0.1244 0.1452 0.0067  0.0287  0.0112  41  VAL   A C   
1070 C  C   B VAL   A 41  ? 0.1586 0.1216 0.1402 0.0054  0.0405  0.0206  41  VAL   A C   
1071 O  O   A VAL   A 41  ? 0.1570 0.1165 0.1719 0.0017  0.0203  -0.0051 41  VAL   A O   
1072 O  O   B VAL   A 41  ? 0.1645 0.1115 0.1420 0.0088  0.0424  0.0041  41  VAL   A O   
1073 C  CB  A VAL   A 41  ? 0.1501 0.1280 0.1308 0.0026  0.0358  0.0076  41  VAL   A CB  
1074 C  CB  B VAL   A 41  ? 0.1836 0.1375 0.1474 -0.0057 0.0396  0.0210  41  VAL   A CB  
1075 C  CG1 A VAL   A 41  ? 0.1605 0.1370 0.1384 0.0002  0.0306  -0.0004 41  VAL   A CG1 
1076 C  CG1 B VAL   A 41  ? 0.1999 0.1472 0.1671 -0.0067 0.0452  0.0068  41  VAL   A CG1 
1077 C  CG2 A VAL   A 41  ? 0.1455 0.1325 0.1103 -0.0004 0.0428  0.0090  41  VAL   A CG2 
1078 C  CG2 B VAL   A 41  ? 0.1870 0.1435 0.1373 -0.0082 0.0346  0.0201  41  VAL   A CG2 
1097 N  N   . TYR   A 42  ? 0.1445 0.1227 0.1631 0.0012  0.0367  0.0217  42  TYR   A N   
1098 C  CA  . TYR   A 42  ? 0.1451 0.1147 0.1658 -0.0053 0.0360  0.0266  42  TYR   A CA  
1099 C  C   . TYR   A 42  ? 0.1371 0.1158 0.1583 -0.0039 0.0290  0.0251  42  TYR   A C   
1100 O  O   . TYR   A 42  ? 0.1338 0.1183 0.1788 -0.0127 0.0267  0.0113  42  TYR   A O   
1101 C  CB  . TYR   A 42  ? 0.1683 0.1254 0.1613 -0.0068 0.0335  0.0286  42  TYR   A CB  
1102 C  CG  . TYR   A 42  ? 0.1827 0.1403 0.1623 -0.0049 0.0295  0.0316  42  TYR   A CG  
1103 C  CD1 . TYR   A 42  ? 0.1897 0.1520 0.1684 -0.0131 0.0307  0.0314  42  TYR   A CD1 
1104 C  CD2 . TYR   A 42  ? 0.1953 0.1631 0.1806 -0.0026 0.0209  0.0204  42  TYR   A CD2 
1105 C  CE1 . TYR   A 42  ? 0.2038 0.1591 0.1591 -0.0174 0.0347  0.0244  42  TYR   A CE1 
1106 C  CE2 . TYR   A 42  ? 0.2131 0.1772 0.1954 -0.0174 0.0253  0.0209  42  TYR   A CE2 
1107 C  CZ  . TYR   A 42  ? 0.2228 0.1751 0.1573 -0.0228 0.0362  0.0182  42  TYR   A CZ  
1108 O  OH  . TYR   A 42  ? 0.2440 0.2001 0.1878 -0.0380 0.0356  0.0095  42  TYR   A OH  
1119 N  N   A LEU   A 43  ? 0.1375 0.1118 0.1498 -0.0096 0.0181  0.0112  43  LEU   A N   
1120 N  N   B LEU   A 43  ? 0.1335 0.1195 0.1504 -0.0004 0.0150  0.0152  43  LEU   A N   
1121 C  CA  A LEU   A 43  ? 0.1298 0.1089 0.1472 -0.0155 0.0150  0.0100  43  LEU   A CA  
1122 C  CA  B LEU   A 43  ? 0.1225 0.1240 0.1506 0.0016  0.0110  0.0130  43  LEU   A CA  
1123 C  C   A LEU   A 43  ? 0.1299 0.1109 0.1438 -0.0186 0.0146  0.0016  43  LEU   A C   
1124 C  C   B LEU   A 43  ? 0.1215 0.1314 0.1411 0.0107  0.0090  0.0130  43  LEU   A C   
1125 O  O   A LEU   A 43  ? 0.1429 0.1122 0.1421 -0.0178 0.0069  0.0028  43  LEU   A O   
1126 O  O   B LEU   A 43  ? 0.1334 0.1370 0.1546 0.0168  -0.0010 0.0195  43  LEU   A O   
1127 C  CB  A LEU   A 43  ? 0.1336 0.1106 0.1593 -0.0090 0.0102  0.0057  43  LEU   A CB  
1128 C  CB  B LEU   A 43  ? 0.1162 0.1160 0.1608 -0.0013 0.0126  0.0110  43  LEU   A CB  
1129 C  CG  A LEU   A 43  ? 0.1361 0.1159 0.1586 -0.0087 0.0018  0.0069  43  LEU   A CG  
1130 C  CG  B LEU   A 43  ? 0.1203 0.1238 0.1648 -0.0030 0.0141  0.0133  43  LEU   A CG  
1131 C  CD1 A LEU   A 43  ? 0.1382 0.1223 0.1753 -0.0072 0.0007  0.0135  43  LEU   A CD1 
1132 C  CD1 B LEU   A 43  ? 0.1271 0.1305 0.1879 -0.0041 0.0138  0.0123  43  LEU   A CD1 
1133 C  CD2 A LEU   A 43  ? 0.1417 0.1170 0.1483 -0.0104 -0.0023 0.0061  43  LEU   A CD2 
1134 C  CD2 B LEU   A 43  ? 0.1320 0.1259 0.1708 -0.0053 0.0109  0.0315  43  LEU   A CD2 
1157 N  N   A LYS   A 44  ? 0.1353 0.1102 0.1512 -0.0149 0.0127  0.0041  44  LYS   A N   
1158 N  N   B LYS   A 44  ? 0.1267 0.1312 0.1335 0.0150  -0.0003 0.0184  44  LYS   A N   
1159 C  CA  A LYS   A 44  ? 0.1436 0.1192 0.1582 -0.0158 0.0211  0.0171  44  LYS   A CA  
1160 C  CA  B LYS   A 44  ? 0.1438 0.1339 0.1419 0.0142  0.0028  0.0198  44  LYS   A CA  
1161 C  C   A LYS   A 44  ? 0.1295 0.1218 0.1392 -0.0083 0.0104  0.0126  44  LYS   A C   
1162 C  C   B LYS   A 44  ? 0.1351 0.1306 0.1343 0.0080  -0.0040 0.0138  44  LYS   A C   
1163 O  O   A LYS   A 44  ? 0.1337 0.1365 0.1485 -0.0011 0.0061  0.0055  44  LYS   A O   
1164 O  O   B LYS   A 44  ? 0.1386 0.1391 0.1396 0.0036  -0.0019 0.0020  44  LYS   A O   
1165 C  CB  A LYS   A 44  ? 0.1691 0.1358 0.1943 -0.0204 0.0349  0.0308  44  LYS   A CB  
1166 C  CB  B LYS   A 44  ? 0.1709 0.1503 0.1865 0.0199  0.0172  0.0237  44  LYS   A CB  
1167 C  CG  A LYS   A 44  ? 0.1974 0.1586 0.2519 -0.0281 0.0528  0.0395  44  LYS   A CG  
1168 C  CG  B LYS   A 44  ? 0.1960 0.1800 0.2610 0.0244  0.0253  0.0237  44  LYS   A CG  
1169 C  CD  A LYS   A 44  ? 0.2332 0.1969 0.3501 -0.0340 0.0525  0.0350  44  LYS   A CD  
1170 C  CD  B LYS   A 44  ? 0.2308 0.2218 0.3612 0.0164  0.0181  0.0206  44  LYS   A CD  
1171 C  CE  A LYS   A 44  ? 0.2550 0.2290 0.4155 -0.0299 0.0497  0.0290  44  LYS   A CE  
1172 C  CE  B LYS   A 44  ? 0.2473 0.2477 0.4206 0.0091  0.0129  0.0198  44  LYS   A CE  
1173 N  NZ  A LYS   A 44  ? 0.2653 0.2483 0.4469 -0.0281 0.0444  0.0237  44  LYS   A NZ  
1174 N  NZ  B LYS   A 44  ? 0.2555 0.2589 0.4454 0.0013  0.0072  0.0187  44  LYS   A NZ  
1201 N  N   A HIS   A 45  ? 0.1200 0.1154 0.1296 -0.0058 0.0066  0.0183  45  HIS   A N   
1202 N  N   B HIS   A 45  ? 0.1325 0.1252 0.1449 0.0033  -0.0173 0.0157  45  HIS   A N   
1203 C  CA  A HIS   A 45  ? 0.1175 0.1143 0.1250 -0.0029 0.0127  0.0062  45  HIS   A CA  
1204 C  CA  B HIS   A 45  ? 0.1322 0.1259 0.1548 -0.0006 -0.0112 0.0051  45  HIS   A CA  
1205 C  C   A HIS   A 45  ? 0.1158 0.1219 0.1291 0.0032  0.0148  0.0143  45  HIS   A C   
1206 C  C   B HIS   A 45  ? 0.1397 0.1362 0.1657 0.0050  -0.0097 0.0166  45  HIS   A C   
1207 O  O   A HIS   A 45  ? 0.1251 0.1118 0.1572 0.0018  0.0070  -0.0018 45  HIS   A O   
1208 O  O   B HIS   A 45  ? 0.1502 0.1420 0.1955 0.0128  -0.0166 0.0106  45  HIS   A O   
1209 C  CB  A HIS   A 45  ? 0.1204 0.1121 0.1160 -0.0011 0.0143  0.0073  45  HIS   A CB  
1210 C  CB  B HIS   A 45  ? 0.1217 0.1185 0.1520 -0.0010 -0.0113 0.0018  45  HIS   A CB  
1211 C  CG  A HIS   A 45  ? 0.1270 0.1083 0.0986 -0.0040 0.0066  0.0058  45  HIS   A CG  
1212 C  CG  B HIS   A 45  ? 0.1169 0.1253 0.1386 -0.0057 0.0001  0.0027  45  HIS   A CG  
1213 N  ND1 A HIS   A 45  ? 0.1233 0.1134 0.1050 -0.0001 0.0044  0.0022  45  HIS   A ND1 
1214 N  ND1 B HIS   A 45  ? 0.1114 0.1328 0.1617 -0.0046 -0.0090 0.0149  45  HIS   A ND1 
1215 C  CD2 A HIS   A 45  ? 0.1348 0.1180 0.1294 -0.0078 0.0004  0.0182  45  HIS   A CD2 
1216 C  CD2 B HIS   A 45  ? 0.1116 0.1225 0.1328 -0.0038 -0.0020 0.0074  45  HIS   A CD2 
1217 C  CE1 A HIS   A 45  ? 0.1304 0.1205 0.1175 -0.0020 0.0064  0.0130  45  HIS   A CE1 
1218 C  CE1 B HIS   A 45  ? 0.1095 0.1250 0.1281 -0.0065 -0.0028 0.0072  45  HIS   A CE1 
1219 N  NE2 A HIS   A 45  ? 0.1369 0.1204 0.1411 0.0006  0.0067  0.0224  45  HIS   A NE2 
1220 N  NE2 B HIS   A 45  ? 0.1083 0.1233 0.1168 -0.0073 0.0028  0.0052  45  HIS   A NE2 
1235 N  N   A GLY   A 46  ? 0.1230 0.1383 0.1460 0.0139  0.0007  0.0210  46  GLY   A N   
1236 N  N   B GLY   A 46  ? 0.1463 0.1350 0.1687 -0.0003 -0.0145 0.0250  46  GLY   A N   
1237 C  CA  A GLY   A 46  ? 0.1249 0.1441 0.1705 0.0143  -0.0054 0.0282  46  GLY   A CA  
1238 C  CA  B GLY   A 46  ? 0.1438 0.1399 0.1732 0.0006  -0.0106 0.0284  46  GLY   A CA  
1239 C  C   A GLY   A 46  ? 0.1295 0.1422 0.1528 0.0182  -0.0045 0.0438  46  GLY   A C   
1240 C  C   B GLY   A 46  ? 0.1416 0.1414 0.1580 0.0035  -0.0005 0.0363  46  GLY   A C   
1241 O  O   A GLY   A 46  ? 0.1337 0.1436 0.1491 0.0237  -0.0162 0.0516  46  GLY   A O   
1242 O  O   B GLY   A 46  ? 0.1473 0.1494 0.1609 0.0018  -0.0018 0.0259  46  GLY   A O   
1249 N  N   A GLY   A 47  ? 0.1262 0.1404 0.1470 0.0169  -0.0083 0.0293  47  GLY   A N   
1250 N  N   B GLY   A 47  ? 0.1385 0.1443 0.1534 0.0063  0.0046  0.0257  47  GLY   A N   
1251 C  CA  A GLY   A 47  ? 0.1301 0.1460 0.1379 0.0205  -0.0047 0.0188  47  GLY   A CA  
1252 C  CA  B GLY   A 47  ? 0.1371 0.1489 0.1519 0.0030  -0.0046 0.0208  47  GLY   A CA  
1253 C  C   A GLY   A 47  ? 0.1300 0.1439 0.1332 0.0222  -0.0065 0.0186  47  GLY   A C   
1254 C  C   B GLY   A 47  ? 0.1298 0.1405 0.1207 0.0075  -0.0037 0.0123  47  GLY   A C   
1255 O  O   A GLY   A 47  ? 0.1304 0.1436 0.1494 0.0278  -0.0057 0.0214  47  GLY   A O   
1256 O  O   B GLY   A 47  ? 0.1242 0.1350 0.1278 0.0111  -0.0063 0.0205  47  GLY   A O   
1263 N  N   A GLY   A 48  ? 0.1293 0.1458 0.1205 0.0240  -0.0039 0.0118  48  GLY   A N   
1264 N  N   B GLY   A 48  ? 0.1266 0.1450 0.1308 0.0083  0.0015  0.0077  48  GLY   A N   
1265 C  CA  A GLY   A 48  ? 0.1288 0.1427 0.1313 0.0117  -0.0061 0.0010  48  GLY   A CA  
1266 C  CA  B GLY   A 48  ? 0.1273 0.1346 0.1216 0.0034  0.0078  -0.0001 48  GLY   A CA  
1267 C  C   A GLY   A 48  ? 0.1293 0.1367 0.1148 0.0015  -0.0027 -0.0027 48  GLY   A C   
1268 C  C   B GLY   A 48  ? 0.1259 0.1308 0.1259 0.0017  0.0134  0.0064  48  GLY   A C   
1269 O  O   A GLY   A 48  ? 0.1445 0.1380 0.1227 -0.0048 -0.0144 0.0017  48  GLY   A O   
1270 O  O   B GLY   A 48  ? 0.1417 0.1334 0.1256 0.0093  0.0206  0.0011  48  GLY   A O   
1277 N  N   A VAL   A 49  ? 0.1309 0.1321 0.1455 -0.0068 -0.0080 0.0110  49  VAL   A N   
1278 N  N   B VAL   A 49  ? 0.1150 0.1243 0.1315 -0.0026 0.0003  -0.0010 49  VAL   A N   
1279 C  CA  A VAL   A 49  ? 0.1464 0.1259 0.1568 -0.0109 0.0022  0.0080  49  VAL   A CA  
1280 C  CA  B VAL   A 49  ? 0.1156 0.1267 0.1342 -0.0014 0.0046  0.0057  49  VAL   A CA  
1281 C  C   A VAL   A 49  ? 0.1421 0.1214 0.1428 -0.0114 -0.0123 0.0243  49  VAL   A C   
1282 C  C   B VAL   A 49  ? 0.1204 0.1219 0.1116 0.0042  0.0152  -0.0082 49  VAL   A C   
1283 O  O   A VAL   A 49  ? 0.1479 0.1245 0.1450 -0.0224 -0.0212 0.0195  49  VAL   A O   
1284 O  O   B VAL   A 49  ? 0.1211 0.1267 0.1097 0.0053  0.0270  -0.0057 49  VAL   A O   
1285 C  CB  A VAL   A 49  ? 0.1645 0.1305 0.1757 -0.0150 0.0008  -0.0061 49  VAL   A CB  
1286 C  CB  B VAL   A 49  ? 0.1141 0.1260 0.1590 -0.0047 0.0063  0.0121  49  VAL   A CB  
1287 C  CG1 A VAL   A 49  ? 0.1719 0.1269 0.1858 -0.0127 0.0072  -0.0035 49  VAL   A CG1 
1288 C  CG1 B VAL   A 49  ? 0.1072 0.1142 0.1521 0.0030  -0.0037 0.0148  49  VAL   A CG1 
1289 C  CG2 A VAL   A 49  ? 0.1710 0.1372 0.2110 -0.0280 0.0053  -0.0162 49  VAL   A CG2 
1290 C  CG2 B VAL   A 49  ? 0.1183 0.1246 0.1840 -0.0041 0.0096  0.0184  49  VAL   A CG2 
1309 N  N   A ALA   A 50  ? 0.1277 0.1177 0.1464 -0.0114 -0.0236 0.0291  50  ALA   A N   
1310 N  N   B ALA   A 50  ? 0.1228 0.1194 0.1036 0.0043  0.0077  -0.0116 50  ALA   A N   
1311 C  CA  A ALA   A 50  ? 0.1205 0.1165 0.1536 -0.0184 -0.0086 0.0280  50  ALA   A CA  
1312 C  CA  B ALA   A 50  ? 0.1235 0.1176 0.1034 0.0002  0.0029  -0.0155 50  ALA   A CA  
1313 C  C   A ALA   A 50  ? 0.1087 0.1212 0.1535 -0.0159 -0.0021 0.0222  50  ALA   A C   
1314 C  C   B ALA   A 50  ? 0.1240 0.1189 0.1025 -0.0002 0.0015  -0.0071 50  ALA   A C   
1315 O  O   A ALA   A 50  ? 0.1116 0.1219 0.1645 -0.0072 -0.0064 0.0168  50  ALA   A O   
1316 O  O   B ALA   A 50  ? 0.1299 0.1194 0.1088 0.0032  0.0015  -0.0045 50  ALA   A O   
1317 C  CB  A ALA   A 50  ? 0.1196 0.1147 0.1550 -0.0212 -0.0119 0.0277  50  ALA   A CB  
1318 C  CB  B ALA   A 50  ? 0.1265 0.1164 0.0969 0.0016  0.0088  -0.0267 50  ALA   A CB  
1329 N  N   A GLY   A 51  ? 0.1157 0.1177 0.1467 -0.0028 -0.0074 0.0187  51  GLY   A N   
1330 N  N   B GLY   A 51  ? 0.1332 0.1121 0.1334 0.0067  -0.0119 -0.0116 51  GLY   A N   
1331 C  CA  A GLY   A 51  ? 0.1250 0.1163 0.1513 -0.0018 -0.0095 0.0176  51  GLY   A CA  
1332 C  CA  B GLY   A 51  ? 0.1434 0.1099 0.1255 0.0050  -0.0155 -0.0127 51  GLY   A CA  
1333 C  C   A GLY   A 51  ? 0.1135 0.1260 0.1480 0.0006  -0.0077 0.0152  51  GLY   A C   
1334 C  C   B GLY   A 51  ? 0.1337 0.1157 0.1231 0.0094  -0.0123 -0.0135 51  GLY   A C   
1335 O  O   A GLY   A 51  ? 0.1145 0.1373 0.1417 -0.0056 -0.0095 0.0096  51  GLY   A O   
1336 O  O   B GLY   A 51  ? 0.1412 0.1250 0.1235 0.0073  -0.0075 -0.0173 51  GLY   A O   
1343 N  N   A ALA   A 52  ? 0.1113 0.1356 0.1596 -0.0002 -0.0033 0.0084  52  ALA   A N   
1344 N  N   B ALA   A 52  ? 0.1302 0.1206 0.1269 0.0018  0.0003  -0.0262 52  ALA   A N   
1345 C  CA  A ALA   A 52  ? 0.1163 0.1465 0.1568 -0.0020 -0.0062 0.0131  52  ALA   A CA  
1346 C  CA  B ALA   A 52  ? 0.1294 0.1340 0.1299 -0.0035 0.0003  -0.0133 52  ALA   A CA  
1347 C  C   A ALA   A 52  ? 0.1137 0.1436 0.1364 -0.0063 -0.0071 0.0140  52  ALA   A C   
1348 C  C   B ALA   A 52  ? 0.1216 0.1320 0.1211 -0.0141 0.0137  -0.0109 52  ALA   A C   
1349 O  O   A ALA   A 52  ? 0.1226 0.1533 0.1476 -0.0008 -0.0126 0.0067  52  ALA   A O   
1350 O  O   B ALA   A 52  ? 0.1305 0.1322 0.1399 -0.0157 0.0127  -0.0111 52  ALA   A O   
1351 C  CB  A ALA   A 52  ? 0.1286 0.1680 0.1649 -0.0058 -0.0042 0.0150  52  ALA   A CB  
1352 C  CB  B ALA   A 52  ? 0.1383 0.1555 0.1402 -0.0051 -0.0051 -0.0139 52  ALA   A CB  
1363 N  N   A LEU   A 53  ? 0.1145 0.1398 0.1426 -0.0081 -0.0043 0.0115  53  LEU   A N   
1364 N  N   B LEU   A 53  ? 0.1158 0.1317 0.1179 -0.0021 0.0121  -0.0070 53  LEU   A N   
1365 C  CA  A LEU   A 53  ? 0.1251 0.1408 0.1446 -0.0128 -0.0027 0.0131  53  LEU   A CA  
1366 C  CA  B LEU   A 53  ? 0.1180 0.1351 0.1091 0.0004  0.0076  -0.0043 53  LEU   A CA  
1367 C  C   A LEU   A 53  ? 0.1317 0.1419 0.1311 -0.0086 0.0017  0.0078  53  LEU   A C   
1368 C  C   B LEU   A 53  ? 0.1262 0.1362 0.0886 0.0111  0.0047  -0.0031 53  LEU   A C   
1369 O  O   A LEU   A 53  ? 0.1409 0.1469 0.1418 -0.0232 0.0060  -0.0015 53  LEU   A O   
1370 O  O   B LEU   A 53  ? 0.1416 0.1379 0.1052 0.0029  0.0028  0.0056  53  LEU   A O   
1371 C  CB  A LEU   A 53  ? 0.1307 0.1446 0.1581 -0.0094 -0.0052 0.0184  53  LEU   A CB  
1372 C  CB  B LEU   A 53  ? 0.1133 0.1367 0.1044 -0.0025 0.0031  0.0029  53  LEU   A CB  
1373 C  CG  A LEU   A 53  ? 0.1304 0.1443 0.1566 -0.0055 -0.0025 0.0157  53  LEU   A CG  
1374 C  CG  B LEU   A 53  ? 0.1186 0.1384 0.1071 -0.0042 -0.0042 0.0020  53  LEU   A CG  
1375 C  CD1 A LEU   A 53  ? 0.1219 0.1541 0.1496 0.0017  -0.0036 0.0237  53  LEU   A CD1 
1376 C  CD1 B LEU   A 53  ? 0.1259 0.1479 0.1116 -0.0073 0.0008  -0.0067 53  LEU   A CD1 
1377 C  CD2 A LEU   A 53  ? 0.1419 0.1552 0.1717 -0.0102 -0.0036 0.0169  53  LEU   A CD2 
1378 C  CD2 B LEU   A 53  ? 0.1186 0.1393 0.1246 -0.0127 -0.0005 -0.0019 53  LEU   A CD2 
1401 N  N   A ASN   A 54  ? 0.1240 0.1325 0.1280 -0.0104 -0.0057 0.0139  54  ASN   A N   
1402 N  N   B ASN   A 54  ? 0.1206 0.1325 0.0987 0.0086  -0.0012 -0.0045 54  ASN   A N   
1403 C  CA  A ASN   A 54  ? 0.1199 0.1237 0.1408 -0.0127 -0.0068 0.0104  54  ASN   A CA  
1404 C  CA  B ASN   A 54  ? 0.1139 0.1311 0.1173 0.0038  -0.0036 -0.0053 54  ASN   A CA  
1405 C  C   A ASN   A 54  ? 0.1277 0.1311 0.1439 -0.0113 0.0039  0.0034  54  ASN   A C   
1406 C  C   B ASN   A 54  ? 0.1241 0.1336 0.1275 -0.0040 0.0045  -0.0051 54  ASN   A C   
1407 O  O   A ASN   A 54  ? 0.1327 0.1416 0.1443 -0.0079 -0.0021 -0.0068 54  ASN   A O   
1408 O  O   B ASN   A 54  ? 0.1276 0.1400 0.1183 -0.0032 -0.0026 -0.0134 54  ASN   A O   
1409 C  CB  A ASN   A 54  ? 0.1207 0.1178 0.1474 -0.0215 -0.0063 0.0143  54  ASN   A CB  
1410 C  CB  B ASN   A 54  ? 0.1176 0.1336 0.1188 0.0073  -0.0003 -0.0010 54  ASN   A CB  
1411 C  CG  A ASN   A 54  ? 0.1232 0.1183 0.1595 -0.0180 -0.0034 0.0123  54  ASN   A CG  
1412 C  CG  B ASN   A 54  ? 0.1176 0.1341 0.1127 0.0133  0.0046  -0.0046 54  ASN   A CG  
1413 O  OD1 A ASN   A 54  ? 0.1232 0.1171 0.1731 -0.0205 -0.0137 0.0206  54  ASN   A OD1 
1414 O  OD1 B ASN   A 54  ? 0.1177 0.1358 0.1022 0.0135  -0.0017 -0.0089 54  ASN   A OD1 
1415 N  ND2 A ASN   A 54  ? 0.1201 0.1204 0.1700 -0.0194 -0.0124 0.0041  54  ASN   A ND2 
1416 N  ND2 B ASN   A 54  ? 0.1195 0.1356 0.1286 0.0122  -0.0049 0.0092  54  ASN   A ND2 
1429 N  N   . LYS   A 55  ? 0.1229 0.1311 0.1487 -0.0012 0.0035  -0.0046 55  LYS   A N   
1430 C  CA  . LYS   A 55  ? 0.1348 0.1428 0.1448 0.0062  -0.0053 -0.0108 55  LYS   A CA  
1431 C  C   . LYS   A 55  ? 0.1323 0.1501 0.1459 -0.0017 -0.0062 -0.0181 55  LYS   A C   
1432 O  O   . LYS   A 55  ? 0.1412 0.1611 0.1540 0.0042  -0.0049 -0.0231 55  LYS   A O   
1433 C  CB  . LYS   A 55  ? 0.1452 0.1495 0.1601 0.0213  -0.0019 -0.0141 55  LYS   A CB  
1434 C  CG  . LYS   A 55  ? 0.1591 0.1794 0.1820 0.0259  -0.0198 -0.0231 55  LYS   A CG  
1435 C  CD  . LYS   A 55  ? 0.1703 0.2091 0.2000 0.0400  -0.0183 -0.0240 55  LYS   A CD  
1436 C  CE  . LYS   A 55  ? 0.1884 0.2455 0.2149 0.0530  -0.0291 -0.0214 55  LYS   A CE  
1437 N  NZ  . LYS   A 55  ? 0.1947 0.2684 0.2195 0.0576  -0.0330 -0.0218 55  LYS   A NZ  
1452 N  N   . ALA   A 56  ? 0.1360 0.1556 0.1417 -0.0046 0.0031  -0.0181 56  ALA   A N   
1453 C  CA  . ALA   A 56  ? 0.1523 0.1732 0.1341 -0.0059 0.0112  -0.0235 56  ALA   A CA  
1454 C  C   . ALA   A 56  ? 0.1544 0.1820 0.1230 -0.0084 0.0058  -0.0231 56  ALA   A C   
1455 O  O   . ALA   A 56  ? 0.1594 0.2178 0.1426 0.0028  0.0133  -0.0132 56  ALA   A O   
1456 C  CB  . ALA   A 56  ? 0.1512 0.1918 0.1534 -0.0103 0.0178  -0.0077 56  ALA   A CB  
1462 N  N   . THR   A 57  ? 0.1380 0.1645 0.1282 -0.0048 0.0119  -0.0180 57  THR   A N   
1463 C  CA  . THR   A 57  ? 0.1405 0.1614 0.1357 -0.0076 -0.0043 -0.0123 57  THR   A CA  
1464 C  C   . THR   A 57  ? 0.1417 0.1717 0.1382 -0.0006 -0.0060 -0.0165 57  THR   A C   
1465 O  O   . THR   A 57  ? 0.1401 0.1694 0.1595 -0.0034 -0.0146 -0.0246 57  THR   A O   
1466 C  CB  . THR   A 57  ? 0.1385 0.1595 0.1364 -0.0089 0.0043  -0.0097 57  THR   A CB  
1467 O  OG1 . THR   A 57  ? 0.1263 0.1549 0.1335 -0.0072 0.0008  -0.0043 57  THR   A OG1 
1468 C  CG2 . THR   A 57  ? 0.1482 0.1633 0.1294 -0.0068 0.0048  0.0011  57  THR   A CG2 
1476 N  N   . ASN   A 58  ? 0.1430 0.1644 0.1536 -0.0071 0.0083  -0.0243 58  ASN   A N   
1477 C  CA  . ASN   A 58  ? 0.1662 0.1580 0.1768 -0.0140 0.0107  -0.0389 58  ASN   A CA  
1478 C  C   . ASN   A 58  ? 0.1461 0.1444 0.1704 -0.0034 -0.0055 -0.0231 58  ASN   A C   
1479 O  O   . ASN   A 58  ? 0.1485 0.1548 0.1730 -0.0165 0.0016  -0.0246 58  ASN   A O   
1480 C  CB  . ASN   A 58  ? 0.2123 0.1760 0.2115 -0.0266 0.0394  -0.0475 58  ASN   A CB  
1481 C  CG  . ASN   A 58  ? 0.2592 0.2024 0.2791 -0.0192 0.0384  -0.0360 58  ASN   A CG  
1482 O  OD1 . ASN   A 58  ? 0.2859 0.1958 0.3239 0.0174  0.0699  -0.0262 58  ASN   A OD1 
1483 N  ND2 . ASN   A 58  ? 0.2740 0.2124 0.3012 -0.0229 0.0223  -0.0519 58  ASN   A ND2 
1490 N  N   . ASN   A 59  ? 0.1285 0.1359 0.1542 -0.0017 -0.0094 -0.0118 59  ASN   A N   
1491 C  CA  . ASN   A 59  ? 0.1289 0.1269 0.1518 -0.0042 -0.0053 -0.0057 59  ASN   A CA  
1492 C  C   . ASN   A 59  ? 0.1337 0.1304 0.1329 -0.0051 -0.0018 -0.0068 59  ASN   A C   
1493 O  O   . ASN   A 59  ? 0.1287 0.1355 0.1471 -0.0047 -0.0029 0.0019  59  ASN   A O   
1494 C  CB  . ASN   A 59  ? 0.1309 0.1266 0.1620 -0.0012 -0.0152 -0.0125 59  ASN   A CB  
1495 C  CG  . ASN   A 59  ? 0.1381 0.1328 0.1606 -0.0051 -0.0235 -0.0001 59  ASN   A CG  
1496 O  OD1 . ASN   A 59  ? 0.1496 0.1397 0.1500 -0.0105 -0.0247 0.0063  59  ASN   A OD1 
1497 N  ND2 . ASN   A 59  ? 0.1454 0.1369 0.1740 -0.0098 -0.0147 -0.0007 59  ASN   A ND2 
1504 N  N   . ALA   A 60  ? 0.1273 0.1386 0.1363 -0.0050 -0.0036 -0.0065 60  ALA   A N   
1505 C  CA  . ALA   A 60  ? 0.1283 0.1339 0.1471 -0.0012 -0.0072 -0.0016 60  ALA   A CA  
1506 C  C   . ALA   A 60  ? 0.1317 0.1307 0.1528 -0.0022 -0.0002 -0.0037 60  ALA   A C   
1507 O  O   . ALA   A 60  ? 0.1226 0.1317 0.1742 -0.0017 -0.0081 -0.0038 60  ALA   A O   
1508 C  CB  . ALA   A 60  ? 0.1388 0.1459 0.1562 -0.0003 -0.0091 -0.0188 60  ALA   A CB  
1514 N  N   . MET   A 61  ? 0.1224 0.1255 0.1458 -0.0076 -0.0002 -0.0062 61  MET   A N   
1515 C  CA  . MET   A 61  ? 0.1247 0.1257 0.1372 -0.0059 0.0026  0.0026  61  MET   A CA  
1516 C  C   . MET   A 61  ? 0.1203 0.1238 0.1416 -0.0047 -0.0080 -0.0006 61  MET   A C   
1517 O  O   . MET   A 61  ? 0.1244 0.1246 0.1540 -0.0026 0.0110  0.0061  61  MET   A O   
1518 C  CB  . MET   A 61  ? 0.1265 0.1282 0.1294 -0.0106 0.0052  -0.0030 61  MET   A CB  
1519 C  CG  . MET   A 61  ? 0.1252 0.1384 0.1513 -0.0112 0.0014  -0.0004 61  MET   A CG  
1520 S  SD  . MET   A 61  ? 0.1304 0.1351 0.1845 -0.0125 0.0011  -0.0140 61  MET   A SD  
1521 C  CE  . MET   A 61  ? 0.1446 0.1533 0.1978 -0.0190 0.0189  -0.0160 61  MET   A CE  
1531 N  N   . GLN   A 62  ? 0.1225 0.1228 0.1407 -0.0046 -0.0050 0.0033  62  GLN   A N   
1532 C  CA  . GLN   A 62  ? 0.1261 0.1219 0.1434 -0.0031 0.0021  0.0061  62  GLN   A CA  
1533 C  C   . GLN   A 62  ? 0.1244 0.1095 0.1625 -0.0019 0.0110  0.0009  62  GLN   A C   
1534 O  O   . GLN   A 62  ? 0.1277 0.1267 0.1561 -0.0020 0.0065  0.0027  62  GLN   A O   
1535 C  CB  . GLN   A 62  ? 0.1242 0.1198 0.1471 -0.0015 -0.0011 -0.0015 62  GLN   A CB  
1536 C  CG  . GLN   A 62  ? 0.1279 0.1175 0.1450 -0.0063 -0.0062 0.0124  62  GLN   A CG  
1537 C  CD  . GLN   A 62  ? 0.1336 0.1249 0.1457 -0.0050 0.0057  0.0125  62  GLN   A CD  
1538 O  OE1 . GLN   A 62  ? 0.1372 0.1350 0.1536 -0.0064 0.0014  0.0003  62  GLN   A OE1 
1539 N  NE2 . GLN   A 62  ? 0.1360 0.1314 0.1569 -0.0017 0.0032  -0.0045 62  GLN   A NE2 
1548 N  N   . VAL   A 63  ? 0.1179 0.1201 0.1745 -0.0045 0.0116  -0.0166 63  VAL   A N   
1549 C  CA  . VAL   A 63  ? 0.1211 0.1326 0.1979 -0.0113 0.0063  -0.0110 63  VAL   A CA  
1550 C  C   . VAL   A 63  ? 0.1157 0.1292 0.1840 -0.0088 -0.0050 -0.0179 63  VAL   A C   
1551 O  O   . VAL   A 63  ? 0.1174 0.1340 0.1980 -0.0135 -0.0004 -0.0101 63  VAL   A O   
1552 C  CB  . VAL   A 63  ? 0.1333 0.1483 0.2237 -0.0131 0.0004  -0.0382 63  VAL   A CB  
1553 C  CG1 . VAL   A 63  ? 0.1451 0.1664 0.2513 -0.0119 -0.0093 -0.0642 63  VAL   A CG1 
1554 C  CG2 . VAL   A 63  ? 0.1458 0.1437 0.2228 -0.0107 0.0153  -0.0330 63  VAL   A CG2 
1564 N  N   . GLU   A 64  ? 0.1201 0.1350 0.1694 -0.0041 -0.0009 -0.0095 64  GLU   A N   
1565 C  CA  . GLU   A 64  ? 0.1225 0.1339 0.1715 -0.0059 -0.0071 0.0016  64  GLU   A CA  
1566 C  C   . GLU   A 64  ? 0.1151 0.1303 0.1610 -0.0067 0.0047  0.0080  64  GLU   A C   
1567 O  O   . GLU   A 64  ? 0.1205 0.1374 0.1645 -0.0017 0.0020  0.0016  64  GLU   A O   
1568 C  CB  . GLU   A 64  ? 0.1308 0.1401 0.1783 -0.0088 0.0064  -0.0036 64  GLU   A CB  
1569 C  CG  . GLU   A 64  ? 0.1433 0.1454 0.1804 -0.0113 0.0033  -0.0000 64  GLU   A CG  
1570 C  CD  . GLU   A 64  ? 0.1527 0.1557 0.1788 -0.0146 0.0072  0.0023  64  GLU   A CD  
1571 O  OE1 . GLU   A 64  ? 0.1477 0.1691 0.2078 -0.0168 0.0151  -0.0007 64  GLU   A OE1 
1572 O  OE2 . GLU   A 64  ? 0.1731 0.1577 0.1699 -0.0202 -0.0016 0.0112  64  GLU   A OE2 
1579 N  N   . SER   A 65  ? 0.1114 0.1324 0.1541 -0.0014 -0.0003 0.0043  65  SER   A N   
1580 C  CA  . SER   A 65  ? 0.1210 0.1228 0.1487 -0.0041 -0.0031 0.0007  65  SER   A CA  
1581 C  C   . SER   A 65  ? 0.1233 0.1295 0.1516 -0.0064 0.0027  -0.0002 65  SER   A C   
1582 O  O   . SER   A 65  ? 0.1313 0.1361 0.1659 -0.0017 0.0150  -0.0020 65  SER   A O   
1583 C  CB  . SER   A 65  ? 0.1242 0.1203 0.1536 -0.0056 0.0055  0.0086  65  SER   A CB  
1584 O  OG  . SER   A 65  ? 0.1201 0.1350 0.1714 -0.0078 -0.0043 0.0161  65  SER   A OG  
1590 N  N   . ASP   A 66  ? 0.1260 0.1273 0.1590 -0.0087 0.0150  0.0060  66  ASP   A N   
1591 C  CA  . ASP   A 66  ? 0.1350 0.1355 0.1696 -0.0038 0.0088  0.0143  66  ASP   A CA  
1592 C  C   . ASP   A 66  ? 0.1313 0.1334 0.1719 -0.0068 0.0125  0.0131  66  ASP   A C   
1593 O  O   . ASP   A 66  ? 0.1341 0.1439 0.2004 -0.0030 0.0295  0.0243  66  ASP   A O   
1594 C  CB  . ASP   A 66  ? 0.1391 0.1469 0.1971 0.0049  0.0147  0.0325  66  ASP   A CB  
1595 C  CG  . ASP   A 66  ? 0.1615 0.1580 0.2267 0.0021  0.0119  0.0513  66  ASP   A CG  
1596 O  OD1 . ASP   A 66  ? 0.1640 0.1902 0.2128 -0.0072 -0.0002 0.0541  66  ASP   A OD1 
1597 O  OD2 . ASP   A 66  ? 0.1829 0.1689 0.3150 0.0193  -0.0101 0.0284  66  ASP   A OD2 
1602 N  N   . ASP   A 67  ? 0.1254 0.1372 0.1782 -0.0039 0.0180  0.0138  67  ASP   A N   
1603 C  CA  . ASP   A 67  ? 0.1270 0.1521 0.1903 -0.0014 0.0068  0.0238  67  ASP   A CA  
1604 C  C   . ASP   A 67  ? 0.1282 0.1541 0.1884 -0.0008 0.0077  0.0294  67  ASP   A C   
1605 O  O   . ASP   A 67  ? 0.1271 0.1629 0.2101 0.0030  0.0270  0.0304  67  ASP   A O   
1606 C  CB  . ASP   A 67  ? 0.1382 0.1617 0.2129 -0.0071 -0.0094 0.0261  67  ASP   A CB  
1607 C  CG  . ASP   A 67  ? 0.1324 0.1770 0.2617 -0.0088 -0.0247 0.0336  67  ASP   A CG  
1608 O  OD1 . ASP   A 67  ? 0.1371 0.1946 0.3541 -0.0094 -0.0373 0.0534  67  ASP   A OD1 
1609 O  OD2 . ASP   A 67  ? 0.1343 0.1799 0.2430 0.0003  -0.0156 0.0193  67  ASP   A OD2 
1614 N  N   . TYR   A 68  ? 0.1267 0.1400 0.1939 0.0004  0.0120  0.0288  68  TYR   A N   
1615 C  CA  . TYR   A 68  ? 0.1358 0.1375 0.1822 0.0030  0.0193  0.0232  68  TYR   A CA  
1616 C  C   . TYR   A 68  ? 0.1238 0.1393 0.1812 0.0009  0.0226  0.0206  68  TYR   A C   
1617 O  O   . TYR   A 68  ? 0.1327 0.1455 0.2000 0.0093  0.0260  0.0239  68  TYR   A O   
1618 C  CB  . TYR   A 68  ? 0.1443 0.1339 0.1875 0.0062  0.0411  0.0264  68  TYR   A CB  
1619 C  CG  . TYR   A 68  ? 0.1483 0.1516 0.2199 0.0041  0.0496  0.0307  68  TYR   A CG  
1620 C  CD1 . TYR   A 68  ? 0.1551 0.1607 0.2528 -0.0178 0.0405  -0.0037 68  TYR   A CD1 
1621 C  CD2 . TYR   A 68  ? 0.1695 0.1601 0.2622 0.0105  0.0505  0.0322  68  TYR   A CD2 
1622 C  CE1 . TYR   A 68  ? 0.1621 0.1703 0.2859 -0.0137 0.0427  -0.0101 68  TYR   A CE1 
1623 C  CE2 . TYR   A 68  ? 0.1635 0.1592 0.2747 0.0019  0.0607  0.0127  68  TYR   A CE2 
1624 C  CZ  . TYR   A 68  ? 0.1674 0.1630 0.2917 -0.0166 0.0471  -0.0102 68  TYR   A CZ  
1625 O  OH  . TYR   A 68  ? 0.1978 0.1631 0.3070 -0.0142 0.0277  -0.0199 68  TYR   A OH  
1635 N  N   . ILE   A 69  ? 0.1209 0.1317 0.1772 0.0015  0.0169  0.0206  69  ILE   A N   
1636 C  CA  . ILE   A 69  ? 0.1359 0.1328 0.1792 0.0025  0.0168  0.0079  69  ILE   A CA  
1637 C  C   . ILE   A 69  ? 0.1370 0.1357 0.1738 0.0087  0.0221  0.0205  69  ILE   A C   
1638 O  O   . ILE   A 69  ? 0.1446 0.1451 0.1787 0.0026  0.0267  0.0193  69  ILE   A O   
1639 C  CB  . ILE   A 69  ? 0.1429 0.1546 0.1797 0.0016  0.0131  -0.0000 69  ILE   A CB  
1640 C  CG1 . ILE   A 69  ? 0.1430 0.1648 0.1843 0.0032  0.0148  -0.0149 69  ILE   A CG1 
1641 C  CG2 . ILE   A 69  ? 0.1594 0.1791 0.1940 0.0091  0.0049  -0.0063 69  ILE   A CG2 
1642 C  CD1 . ILE   A 69  ? 0.1395 0.1740 0.2106 -0.0016 0.0154  -0.0203 69  ILE   A CD1 
1654 N  N   . ALA   A 70  ? 0.1426 0.1352 0.1792 -0.0033 0.0261  0.0160  70  ALA   A N   
1655 C  CA  . ALA   A 70  ? 0.1431 0.1515 0.1915 -0.0164 0.0330  0.0209  70  ALA   A CA  
1656 C  C   . ALA   A 70  ? 0.1392 0.1681 0.1922 -0.0100 0.0282  0.0229  70  ALA   A C   
1657 O  O   . ALA   A 70  ? 0.1579 0.2014 0.2141 0.0097  0.0517  0.0382  70  ALA   A O   
1658 C  CB  . ALA   A 70  ? 0.1496 0.1506 0.2144 -0.0201 0.0306  0.0205  70  ALA   A CB  
1664 N  N   . THR   A 71  ? 0.1396 0.1620 0.1789 -0.0031 0.0208  0.0232  71  THR   A N   
1665 C  CA  . THR   A 71  ? 0.1451 0.1807 0.2096 0.0067  0.0214  0.0254  71  THR   A CA  
1666 C  C   . THR   A 71  ? 0.1363 0.1725 0.2267 0.0135  0.0327  0.0191  71  THR   A C   
1667 O  O   . THR   A 71  ? 0.1422 0.1949 0.2789 0.0098  0.0461  -0.0031 71  THR   A O   
1668 C  CB  . THR   A 71  ? 0.1705 0.2052 0.2412 0.0189  -0.0101 0.0349  71  THR   A CB  
1669 O  OG1 . THR   A 71  ? 0.1980 0.2196 0.2476 0.0117  -0.0383 0.0242  71  THR   A OG1 
1670 C  CG2 . THR   A 71  ? 0.1879 0.2229 0.2656 0.0304  -0.0181 0.0494  71  THR   A CG2 
1678 N  N   . ASN   A 72  ? 0.1399 0.1578 0.2138 0.0096  0.0277  0.0254  72  ASN   A N   
1679 C  CA  . ASN   A 72  ? 0.1439 0.1561 0.2087 0.0153  0.0368  0.0236  72  ASN   A CA  
1680 C  C   . ASN   A 72  ? 0.1586 0.1566 0.2044 0.0143  0.0474  0.0125  72  ASN   A C   
1681 O  O   . ASN   A 72  ? 0.1748 0.1626 0.2402 0.0148  0.0476  0.0018  72  ASN   A O   
1682 C  CB  . ASN   A 72  ? 0.1662 0.1623 0.2316 0.0168  0.0375  0.0271  72  ASN   A CB  
1683 C  CG  . ASN   A 72  ? 0.1902 0.1749 0.2371 0.0260  0.0402  0.0364  72  ASN   A CG  
1684 O  OD1 . ASN   A 72  ? 0.2095 0.2042 0.2562 0.0269  0.0477  0.0328  72  ASN   A OD1 
1685 N  ND2 . ASN   A 72  ? 0.2049 0.1805 0.2301 0.0501  0.0246  0.0233  72  ASN   A ND2 
1692 N  N   . GLY   A 73  ? 0.1639 0.1584 0.1925 0.0105  0.0439  0.0110  73  GLY   A N   
1693 C  CA  . GLY   A 73  ? 0.1695 0.1530 0.1830 -0.0032 0.0411  0.0119  73  GLY   A CA  
1694 C  C   . GLY   A 73  ? 0.1627 0.1423 0.1759 0.0000  0.0525  0.0265  73  GLY   A C   
1695 O  O   . GLY   A 73  ? 0.1601 0.1475 0.1994 0.0104  0.0435  0.0301  73  GLY   A O   
1699 N  N   . PRO   A 74  ? 0.1743 0.1448 0.1777 -0.0117 0.0496  0.0125  74  PRO   A N   
1700 C  CA  . PRO   A 74  ? 0.1668 0.1422 0.1851 -0.0073 0.0470  0.0135  74  PRO   A CA  
1701 C  C   . PRO   A 74  ? 0.1625 0.1262 0.1807 0.0001  0.0303  0.0099  74  PRO   A C   
1702 O  O   . PRO   A 74  ? 0.1721 0.1326 0.2049 0.0039  0.0340  0.0026  74  PRO   A O   
1703 C  CB  . PRO   A 74  ? 0.1836 0.1707 0.2003 -0.0011 0.0391  0.0264  74  PRO   A CB  
1704 C  CG  . PRO   A 74  ? 0.2083 0.2026 0.2492 -0.0159 0.0315  0.0236  74  PRO   A CG  
1705 C  CD  . PRO   A 74  ? 0.1898 0.1810 0.1996 -0.0193 0.0389  0.0093  74  PRO   A CD  
1713 N  N   . LEU   A 75  ? 0.1589 0.1199 0.1607 -0.0000 0.0323  0.0071  75  LEU   A N   
1714 C  CA  . LEU   A 75  ? 0.1644 0.1261 0.1487 0.0003  0.0188  0.0103  75  LEU   A CA  
1715 C  C   . LEU   A 75  ? 0.1765 0.1297 0.1425 0.0041  0.0218  0.0158  75  LEU   A C   
1716 O  O   . LEU   A 75  ? 0.2110 0.1472 0.1518 0.0093  0.0132  0.0106  75  LEU   A O   
1717 C  CB  . LEU   A 75  ? 0.1691 0.1295 0.1358 -0.0067 0.0156  0.0209  75  LEU   A CB  
1718 C  CG  . LEU   A 75  ? 0.1832 0.1689 0.1464 -0.0361 0.0125  0.0113  75  LEU   A CG  
1719 C  CD1 . LEU   A 75  ? 0.1938 0.2196 0.1547 -0.0357 0.0138  -0.0060 75  LEU   A CD1 
1720 C  CD2 . LEU   A 75  ? 0.2054 0.2052 0.2077 -0.0125 0.0120  0.0076  75  LEU   A CD2 
1732 N  N   . LYS   A 76  ? 0.1804 0.1327 0.1630 -0.0040 0.0134  0.0048  76  LYS   A N   
1733 C  CA  . LYS   A 76  ? 0.1689 0.1485 0.1683 -0.0065 0.0097  -0.0086 76  LYS   A CA  
1734 C  C   . LYS   A 76  ? 0.1675 0.1382 0.1365 0.0004  0.0104  0.0103  76  LYS   A C   
1735 O  O   . LYS   A 76  ? 0.1699 0.1318 0.1421 -0.0021 0.0185  0.0141  76  LYS   A O   
1736 C  CB  . LYS   A 76  ? 0.1671 0.1724 0.2080 0.0049  0.0112  -0.0279 76  LYS   A CB  
1737 C  CG  . LYS   A 76  ? 0.1814 0.1649 0.2542 0.0102  0.0117  -0.0303 76  LYS   A CG  
1738 C  CD  . LYS   A 76  ? 0.1858 0.1686 0.3013 0.0182  0.0022  -0.0381 76  LYS   A CD  
1739 C  CE  . LYS   A 76  ? 0.2008 0.1896 0.3600 0.0066  0.0072  -0.0406 76  LYS   A CE  
1740 N  NZ  . LYS   A 76  ? 0.2031 0.1873 0.4070 -0.0061 0.0020  -0.0475 76  LYS   A NZ  
1754 N  N   . VAL   A 77  ? 0.1771 0.1400 0.1449 -0.0009 0.0258  0.0182  77  VAL   A N   
1755 C  CA  . VAL   A 77  ? 0.1736 0.1408 0.1379 0.0054  0.0185  0.0133  77  VAL   A CA  
1756 C  C   . VAL   A 77  ? 0.1629 0.1361 0.1358 0.0099  0.0134  0.0124  77  VAL   A C   
1757 O  O   . VAL   A 77  ? 0.1731 0.1387 0.1318 0.0157  0.0238  0.0015  77  VAL   A O   
1758 C  CB  . VAL   A 77  ? 0.1873 0.1574 0.1536 0.0024  0.0129  0.0224  77  VAL   A CB  
1759 C  CG1 . VAL   A 77  ? 0.1828 0.1756 0.1778 0.0164  0.0019  0.0133  77  VAL   A CG1 
1760 C  CG2 . VAL   A 77  ? 0.2110 0.1643 0.1713 -0.0021 -0.0014 0.0272  77  VAL   A CG2 
1770 N  N   . GLY   A 78  ? 0.1578 0.1325 0.1281 0.0056  0.0192  0.0140  78  GLY   A N   
1771 C  CA  . GLY   A 78  ? 0.1544 0.1276 0.1476 0.0031  0.0227  0.0123  78  GLY   A CA  
1772 C  C   . GLY   A 78  ? 0.1440 0.1209 0.1432 0.0022  0.0190  0.0102  78  GLY   A C   
1773 O  O   . GLY   A 78  ? 0.1424 0.1310 0.1605 -0.0012 0.0150  0.0222  78  GLY   A O   
1777 N  N   . GLY   A 79  ? 0.1520 0.1229 0.1415 0.0060  0.0139  0.0144  79  GLY   A N   
1778 C  CA  . GLY   A 79  ? 0.1488 0.1230 0.1538 0.0016  0.0119  0.0149  79  GLY   A CA  
1779 C  C   . GLY   A 79  ? 0.1299 0.1226 0.1417 -0.0002 0.0094  0.0099  79  GLY   A C   
1780 O  O   . GLY   A 79  ? 0.1335 0.1338 0.1574 0.0221  0.0100  0.0084  79  GLY   A O   
1784 N  N   . SER   A 80  ? 0.1274 0.1395 0.1650 -0.0002 0.0146  0.0032  80  SER   A N   
1785 C  CA  . SER   A 80  ? 0.1219 0.1307 0.1524 0.0018  0.0081  0.0103  80  SER   A CA  
1786 C  C   . SER   A 80  ? 0.1233 0.1365 0.1448 -0.0007 0.0089  0.0180  80  SER   A C   
1787 O  O   . SER   A 80  ? 0.1263 0.1493 0.1853 0.0068  0.0173  0.0041  80  SER   A O   
1788 C  CB  . SER   A 80  ? 0.1353 0.1312 0.1790 -0.0056 0.0015  0.0092  80  SER   A CB  
1789 O  OG  . SER   A 80  ? 0.1634 0.1347 0.2123 0.0062  -0.0091 0.0194  80  SER   A OG  
1795 N  N   . CYS   A 81  ? 0.1192 0.1298 0.1516 0.0042  -0.0021 0.0149  81  CYS   A N   
1796 C  CA  . CYS   A 81  ? 0.1183 0.1373 0.1495 -0.0041 -0.0083 0.0243  81  CYS   A CA  
1797 C  C   . CYS   A 81  ? 0.1219 0.1270 0.1459 -0.0063 -0.0040 0.0252  81  CYS   A C   
1798 O  O   . CYS   A 81  ? 0.1199 0.1569 0.1566 0.0045  0.0022  0.0336  81  CYS   A O   
1799 C  CB  . CYS   A 81  ? 0.1250 0.1409 0.1724 -0.0094 0.0001  0.0250  81  CYS   A CB  
1800 S  SG  . CYS   A 81  ? 0.1407 0.1339 0.1602 -0.0142 0.0019  0.0163  81  CYS   A SG  
1806 N  N   . VAL   A 82  ? 0.1255 0.1370 0.1467 0.0012  -0.0077 0.0231  82  VAL   A N   
1807 C  CA  . VAL   A 82  ? 0.1343 0.1458 0.1377 0.0033  -0.0099 0.0302  82  VAL   A CA  
1808 C  C   . VAL   A 82  ? 0.1306 0.1511 0.1490 0.0033  -0.0070 0.0343  82  VAL   A C   
1809 O  O   . VAL   A 82  ? 0.1254 0.1600 0.1733 0.0031  -0.0026 0.0001  82  VAL   A O   
1810 C  CB  . VAL   A 82  ? 0.1653 0.1573 0.1621 0.0015  -0.0081 0.0283  82  VAL   A CB  
1811 C  CG1 . VAL   A 82  ? 0.1894 0.1711 0.1803 0.0020  -0.0041 0.0206  82  VAL   A CG1 
1812 C  CG2 . VAL   A 82  ? 0.1728 0.1616 0.1787 0.0006  -0.0145 0.0294  82  VAL   A CG2 
1822 N  N   . LEU   A 83  ? 0.1237 0.1449 0.1491 -0.0066 -0.0087 0.0182  83  LEU   A N   
1823 C  CA  . LEU   A 83  ? 0.1281 0.1440 0.1397 -0.0114 -0.0121 0.0100  83  LEU   A CA  
1824 C  C   . LEU   A 83  ? 0.1364 0.1489 0.1418 -0.0087 -0.0135 0.0179  83  LEU   A C   
1825 O  O   . LEU   A 83  ? 0.1433 0.1496 0.1481 -0.0126 -0.0069 0.0192  83  LEU   A O   
1826 C  CB  . LEU   A 83  ? 0.1413 0.1521 0.1446 -0.0110 -0.0120 0.0150  83  LEU   A CB  
1827 C  CG  . LEU   A 83  ? 0.1518 0.1675 0.1489 -0.0172 0.0036  0.0113  83  LEU   A CG  
1828 C  CD1 . LEU   A 83  ? 0.1704 0.1645 0.1532 -0.0288 -0.0003 0.0299  83  LEU   A CD1 
1829 C  CD2 . LEU   A 83  ? 0.1483 0.1809 0.1673 -0.0153 0.0158  0.0203  83  LEU   A CD2 
1841 N  N   . SER   A 84  ? 0.1517 0.1531 0.1495 -0.0160 -0.0092 0.0224  84  SER   A N   
1842 C  CA  . SER   A 84  ? 0.1611 0.1580 0.1382 -0.0159 -0.0124 0.0179  84  SER   A CA  
1843 C  C   . SER   A 84  ? 0.1644 0.1537 0.1246 -0.0157 0.0021  0.0132  84  SER   A C   
1844 O  O   . SER   A 84  ? 0.1548 0.1650 0.1339 -0.0086 -0.0059 0.0093  84  SER   A O   
1845 C  CB  . SER   A 84  ? 0.1703 0.1800 0.1444 -0.0099 -0.0061 0.0096  84  SER   A CB  
1846 O  OG  . SER   A 84  ? 0.1716 0.2062 0.1505 -0.0084 -0.0137 -0.0036 84  SER   A OG  
1852 N  N   . GLY   A 85  ? 0.1819 0.1697 0.1327 -0.0173 0.0125  0.0103  85  GLY   A N   
1853 C  CA  . GLY   A 85  ? 0.1836 0.1764 0.1497 -0.0205 0.0187  -0.0003 85  GLY   A CA  
1854 C  C   . GLY   A 85  ? 0.1770 0.1818 0.1289 -0.0148 -0.0023 0.0021  85  GLY   A C   
1855 O  O   . GLY   A 85  ? 0.1752 0.1928 0.1378 -0.0224 0.0104  -0.0108 85  GLY   A O   
1859 N  N   . HIS   A 86  ? 0.1794 0.1742 0.1300 -0.0182 -0.0074 0.0026  86  HIS   A N   
1860 C  CA  . HIS   A 86  ? 0.1959 0.1801 0.1235 -0.0190 -0.0045 0.0018  86  HIS   A CA  
1861 C  C   . HIS   A 86  ? 0.2185 0.1919 0.1100 -0.0179 -0.0112 0.0098  86  HIS   A C   
1862 O  O   . HIS   A 86  ? 0.2247 0.2178 0.1290 -0.0108 0.0044  0.0059  86  HIS   A O   
1863 C  CB  . HIS   A 86  ? 0.1940 0.1706 0.1415 -0.0134 0.0039  0.0058  86  HIS   A CB  
1864 C  CG  . HIS   A 86  ? 0.1852 0.1680 0.1484 -0.0045 0.0098  0.0141  86  HIS   A CG  
1865 N  ND1 . HIS   A 86  ? 0.1932 0.1702 0.1752 -0.0150 0.0008  0.0112  86  HIS   A ND1 
1866 C  CD2 . HIS   A 86  ? 0.1850 0.1624 0.1439 0.0021  0.0116  0.0159  86  HIS   A CD2 
1867 C  CE1 . HIS   A 86  ? 0.1878 0.1684 0.1675 -0.0136 0.0171  0.0112  86  HIS   A CE1 
1868 N  NE2 . HIS   A 86  ? 0.1810 0.1612 0.1553 0.0040  0.0182  0.0231  86  HIS   A NE2 
1876 N  N   . ASN   A 87  ? 0.2341 0.1990 0.1296 -0.0144 0.0172  0.0018  87  ASN   A N   
1877 C  CA  . ASN   A 87  ? 0.2547 0.2128 0.1355 -0.0102 0.0405  -0.0173 87  ASN   A CA  
1878 C  C   . ASN   A 87  ? 0.2540 0.2274 0.1647 -0.0165 0.0625  -0.0109 87  ASN   A C   
1879 O  O   . ASN   A 87  ? 0.2813 0.2470 0.2059 -0.0276 0.0930  -0.0162 87  ASN   A O   
1880 C  CB  . ASN   A 87  ? 0.2696 0.2212 0.1526 0.0006  0.0384  -0.0081 87  ASN   A CB  
1881 C  CG  . ASN   A 87  ? 0.2801 0.2339 0.1602 0.0041  0.0519  0.0028  87  ASN   A CG  
1882 O  OD1 . ASN   A 87  ? 0.2962 0.2316 0.1773 0.0197  0.0505  0.0146  87  ASN   A OD1 
1883 N  ND2 . ASN   A 87  ? 0.2816 0.2608 0.1771 -0.0030 0.0548  0.0079  87  ASN   A ND2 
1890 N  N   . LEU   A 88  ? 0.2195 0.2130 0.1633 -0.0191 0.0376  0.0077  88  LEU   A N   
1891 C  CA  . LEU   A 88  ? 0.1969 0.2112 0.1800 -0.0231 0.0318  0.0250  88  LEU   A CA  
1892 C  C   . LEU   A 88  ? 0.1959 0.2140 0.1644 -0.0211 0.0298  0.0352  88  LEU   A C   
1893 O  O   . LEU   A 88  ? 0.2043 0.2207 0.2004 -0.0208 0.0378  0.0563  88  LEU   A O   
1894 C  CB  . LEU   A 88  ? 0.1991 0.2239 0.1887 -0.0296 -0.0032 0.0392  88  LEU   A CB  
1895 C  CG  . LEU   A 88  ? 0.2144 0.2388 0.2243 -0.0307 -0.0177 0.0404  88  LEU   A CG  
1896 C  CD1 . LEU   A 88  ? 0.2269 0.2516 0.2166 -0.0315 -0.0255 0.0216  88  LEU   A CD1 
1897 C  CD2 . LEU   A 88  ? 0.2289 0.2486 0.2715 -0.0215 -0.0173 0.0318  88  LEU   A CD2 
1909 N  N   . ALA   A 89  ? 0.1905 0.2081 0.1448 -0.0198 0.0214  0.0124  89  ALA   A N   
1910 C  CA  . ALA   A 89  ? 0.1957 0.2093 0.1330 -0.0163 0.0113  0.0216  89  ALA   A CA  
1911 C  C   . ALA   A 89  ? 0.1990 0.2109 0.1379 -0.0122 -0.0040 0.0177  89  ALA   A C   
1912 O  O   . ALA   A 89  ? 0.1927 0.2040 0.1781 -0.0201 -0.0081 -0.0071 89  ALA   A O   
1913 C  CB  . ALA   A 89  ? 0.1924 0.2118 0.1222 -0.0188 0.0100  0.0206  89  ALA   A CB  
1919 N  N   . LYS   A 90  ? 0.2114 0.2240 0.1379 -0.0175 -0.0178 0.0165  90  LYS   A N   
1920 C  CA  . LYS   A 90  ? 0.2211 0.2383 0.1314 -0.0155 -0.0302 0.0196  90  LYS   A CA  
1921 C  C   . LYS   A 90  ? 0.1969 0.2171 0.1391 -0.0222 -0.0204 0.0148  90  LYS   A C   
1922 O  O   . LYS   A 90  ? 0.2029 0.2296 0.1681 -0.0311 -0.0262 0.0107  90  LYS   A O   
1923 C  CB  . LYS   A 90  ? 0.2511 0.2775 0.1518 -0.0107 -0.0409 0.0469  90  LYS   A CB  
1924 C  CG  . LYS   A 90  ? 0.2963 0.3202 0.2585 -0.0064 -0.0378 0.0693  90  LYS   A CG  
1925 C  CD  . LYS   A 90  ? 0.3524 0.3683 0.3712 -0.0055 -0.0199 0.0783  90  LYS   A CD  
1926 C  CE  . LYS   A 90  ? 0.4019 0.4108 0.4592 -0.0060 -0.0090 0.0781  90  LYS   A CE  
1927 N  NZ  . LYS   A 90  ? 0.4338 0.4365 0.5159 -0.0070 -0.0038 0.0785  90  LYS   A NZ  
1941 N  N   . HIS   A 91  ? 0.1827 0.1914 0.1133 -0.0189 -0.0256 0.0166  91  HIS   A N   
1942 C  CA  . HIS   A 91  ? 0.1756 0.1765 0.1205 -0.0107 -0.0217 0.0181  91  HIS   A CA  
1943 C  C   . HIS   A 91  ? 0.1541 0.1626 0.1034 -0.0116 -0.0115 0.0215  91  HIS   A C   
1944 O  O   . HIS   A 91  ? 0.1459 0.1740 0.1374 -0.0190 0.0023  0.0228  91  HIS   A O   
1945 C  CB  . HIS   A 91  ? 0.1899 0.2027 0.1641 0.0098  -0.0400 0.0215  91  HIS   A CB  
1946 C  CG  . HIS   A 91  ? 0.2318 0.2542 0.2359 0.0238  -0.0686 0.0075  91  HIS   A CG  
1947 N  ND1 . HIS   A 91  ? 0.2403 0.2831 0.2792 0.0293  -0.0801 -0.0148 91  HIS   A ND1 
1948 C  CD2 . HIS   A 91  ? 0.2609 0.2774 0.2553 0.0303  -0.0846 0.0179  91  HIS   A CD2 
1949 C  CE1 . HIS   A 91  ? 0.2562 0.2946 0.2858 0.0321  -0.0794 -0.0031 91  HIS   A CE1 
1950 N  NE2 . HIS   A 91  ? 0.2714 0.2932 0.2817 0.0383  -0.0854 0.0104  91  HIS   A NE2 
1958 N  N   . CYS   A 92  ? 0.1396 0.1577 0.1171 -0.0132 -0.0134 0.0185  92  CYS   A N   
1959 C  CA  . CYS   A 92  ? 0.1354 0.1497 0.1340 -0.0144 0.0037  0.0195  92  CYS   A CA  
1960 C  C   . CYS   A 92  ? 0.1306 0.1444 0.1208 -0.0118 0.0012  0.0147  92  CYS   A C   
1961 O  O   . CYS   A 92  ? 0.1293 0.1498 0.1466 -0.0174 -0.0008 0.0106  92  CYS   A O   
1962 C  CB  . CYS   A 92  ? 0.1363 0.1505 0.1430 -0.0078 0.0039  0.0145  92  CYS   A CB  
1963 S  SG  . CYS   A 92  ? 0.1385 0.1382 0.1318 -0.0109 -0.0026 0.0129  92  CYS   A SG  
1969 N  N   . LEU   A 93  ? 0.1280 0.1349 0.1310 -0.0086 0.0043  0.0168  93  LEU   A N   
1970 C  CA  . LEU   A 93  ? 0.1173 0.1345 0.1322 -0.0042 0.0006  0.0126  93  LEU   A CA  
1971 C  C   . LEU   A 93  ? 0.1195 0.1199 0.1256 0.0020  0.0007  0.0141  93  LEU   A C   
1972 O  O   . LEU   A 93  ? 0.1149 0.1286 0.1327 0.0021  0.0028  0.0173  93  LEU   A O   
1973 C  CB  . LEU   A 93  ? 0.1248 0.1336 0.1325 -0.0013 -0.0008 0.0247  93  LEU   A CB  
1974 C  CG  . LEU   A 93  ? 0.1337 0.1344 0.1326 -0.0006 0.0034  0.0219  93  LEU   A CG  
1975 C  CD1 . LEU   A 93  ? 0.1394 0.1341 0.1721 0.0004  0.0102  0.0108  93  LEU   A CD1 
1976 C  CD2 . LEU   A 93  ? 0.1469 0.1330 0.1532 -0.0045 0.0081  0.0119  93  LEU   A CD2 
1988 N  N   . HIS   A 94  ? 0.1156 0.1172 0.1386 -0.0019 0.0046  0.0227  94  HIS   A N   
1989 C  CA  . HIS   A 94  ? 0.1154 0.1171 0.1286 -0.0029 -0.0002 0.0181  94  HIS   A CA  
1990 C  C   . HIS   A 94  ? 0.1101 0.1200 0.1413 -0.0068 -0.0010 0.0107  94  HIS   A C   
1991 O  O   . HIS   A 94  ? 0.1129 0.1371 0.1719 0.0013  -0.0012 -0.0015 94  HIS   A O   
1992 C  CB  . HIS   A 94  ? 0.1145 0.1196 0.1329 -0.0021 -0.0013 0.0209  94  HIS   A CB  
1993 C  CG  . HIS   A 94  ? 0.1227 0.1174 0.1295 -0.0083 -0.0054 0.0167  94  HIS   A CG  
1994 N  ND1 . HIS   A 94  ? 0.1182 0.1182 0.1355 -0.0074 -0.0025 0.0138  94  HIS   A ND1 
1995 C  CD2 . HIS   A 94  ? 0.1304 0.1302 0.1446 -0.0052 -0.0071 0.0079  94  HIS   A CD2 
1996 C  CE1 . HIS   A 94  ? 0.1215 0.1237 0.1394 -0.0112 -0.0140 0.0094  94  HIS   A CE1 
1997 N  NE2 . HIS   A 94  ? 0.1297 0.1258 0.1433 -0.0119 -0.0105 0.0035  94  HIS   A NE2 
2005 N  N   . VAL   A 95  ? 0.1076 0.1145 0.1224 -0.0019 0.0075  0.0089  95  VAL   A N   
2006 C  CA  . VAL   A 95  ? 0.1188 0.1196 0.1200 -0.0064 0.0088  0.0082  95  VAL   A CA  
2007 C  C   . VAL   A 95  ? 0.1188 0.1159 0.1094 -0.0131 0.0053  0.0028  95  VAL   A C   
2008 O  O   . VAL   A 95  ? 0.1231 0.1244 0.1321 0.0081  0.0077  0.0065  95  VAL   A O   
2009 C  CB  . VAL   A 95  ? 0.1219 0.1194 0.1392 -0.0068 0.0074  0.0070  95  VAL   A CB  
2010 C  CG1 . VAL   A 95  ? 0.1382 0.1211 0.1467 -0.0104 0.0066  0.0040  95  VAL   A CG1 
2011 C  CG2 . VAL   A 95  ? 0.1208 0.1231 0.1439 -0.0124 0.0053  0.0217  95  VAL   A CG2 
2021 N  N   . VAL   A 96  ? 0.1254 0.1165 0.1105 -0.0006 0.0043  0.0153  96  VAL   A N   
2022 C  CA  . VAL   A 96  ? 0.1349 0.1149 0.1262 0.0001  0.0107  0.0172  96  VAL   A CA  
2023 C  C   . VAL   A 96  ? 0.1377 0.1234 0.1290 0.0036  0.0071  0.0224  96  VAL   A C   
2024 O  O   . VAL   A 96  ? 0.1459 0.1293 0.1507 -0.0029 0.0122  0.0066  96  VAL   A O   
2025 C  CB  . VAL   A 96  ? 0.1379 0.1223 0.1376 -0.0013 0.0151  0.0189  96  VAL   A CB  
2026 C  CG1 . VAL   A 96  ? 0.1449 0.1311 0.1313 -0.0008 0.0092  0.0125  96  VAL   A CG1 
2027 C  CG2 . VAL   A 96  ? 0.1386 0.1333 0.1517 -0.0123 0.0143  0.0139  96  VAL   A CG2 
2037 N  N   A GLY   A 97  ? 0.1343 0.1235 0.1428 -0.0010 0.0075  0.0121  97  GLY   A N   
2038 N  N   B GLY   A 97  ? 0.1409 0.1300 0.1161 -0.0051 0.0050  0.0082  97  GLY   A N   
2039 C  CA  A GLY   A 97  ? 0.1456 0.1308 0.1500 0.0011  -0.0001 0.0151  97  GLY   A CA  
2040 C  CA  B GLY   A 97  ? 0.1556 0.1398 0.1040 -0.0043 -0.0027 0.0124  97  GLY   A CA  
2041 C  C   A GLY   A 97  ? 0.1441 0.1447 0.1411 0.0003  0.0005  0.0154  97  GLY   A C   
2042 C  C   B GLY   A 97  ? 0.1575 0.1508 0.0977 -0.0039 -0.0045 0.0126  97  GLY   A C   
2043 O  O   A GLY   A 97  ? 0.1520 0.1414 0.1530 -0.0006 0.0006  0.0154  97  GLY   A O   
2044 O  O   B GLY   A 97  ? 0.1636 0.1520 0.1166 -0.0052 0.0050  0.0177  97  GLY   A O   
2051 N  N   A PRO   A 98  ? 0.1512 0.1518 0.1199 0.0013  -0.0045 0.0153  98  PRO   A N   
2052 N  N   B PRO   A 98  ? 0.1696 0.1477 0.1138 -0.0034 -0.0121 0.0201  98  PRO   A N   
2053 C  CA  A PRO   A 98  ? 0.1585 0.1703 0.1086 0.0007  -0.0026 0.0082  98  PRO   A CA  
2054 C  CA  B PRO   A 98  ? 0.1871 0.1618 0.1370 -0.0038 -0.0156 0.0149  98  PRO   A CA  
2055 C  C   A PRO   A 98  ? 0.1536 0.1800 0.1013 -0.0041 -0.0062 0.0184  98  PRO   A C   
2056 C  C   B PRO   A 98  ? 0.2056 0.1624 0.1323 -0.0070 -0.0146 0.0314  98  PRO   A C   
2057 O  O   A PRO   A 98  ? 0.1435 0.1699 0.1155 -0.0017 -0.0040 0.0194  98  PRO   A O   
2058 O  O   B PRO   A 98  ? 0.2016 0.1564 0.1808 -0.0056 -0.0025 0.0249  98  PRO   A O   
2059 C  CB  A PRO   A 98  ? 0.1702 0.1760 0.1042 0.0043  -0.0022 -0.0054 98  PRO   A CB  
2060 C  CB  B PRO   A 98  ? 0.1930 0.1582 0.1377 -0.0001 -0.0175 0.0200  98  PRO   A CB  
2061 C  CG  A PRO   A 98  ? 0.1731 0.1708 0.1315 0.0019  -0.0001 -0.0053 98  PRO   A CG  
2062 C  CG  B PRO   A 98  ? 0.1893 0.1554 0.1338 -0.0068 -0.0088 0.0146  98  PRO   A CG  
2063 C  CD  A PRO   A 98  ? 0.1597 0.1548 0.1247 0.0027  -0.0052 0.0081  98  PRO   A CD  
2064 C  CD  B PRO   A 98  ? 0.1774 0.1448 0.1137 -0.0032 -0.0081 0.0243  98  PRO   A CD  
2079 N  N   A ASN   A 99  ? 0.1576 0.1964 0.1131 -0.0017 0.0044  0.0197  99  ASN   A N   
2080 N  N   B ASN   A 99  ? 0.2315 0.1648 0.1246 -0.0008 -0.0147 0.0430  99  ASN   A N   
2081 C  CA  A ASN   A 99  ? 0.1757 0.2095 0.1101 -0.0022 0.0010  0.0163  99  ASN   A CA  
2082 C  CA  B ASN   A 99  ? 0.2619 0.1770 0.1345 0.0038  -0.0204 0.0608  99  ASN   A CA  
2083 C  C   A ASN   A 99  ? 0.1948 0.2344 0.1142 -0.0143 0.0071  0.0174  99  ASN   A C   
2084 C  C   B ASN   A 99  ? 0.2797 0.1969 0.1361 0.0039  -0.0288 0.0681  99  ASN   A C   
2085 O  O   A ASN   A 99  ? 0.2028 0.2474 0.1324 -0.0051 -0.0003 0.0143  99  ASN   A O   
2086 O  O   B ASN   A 99  ? 0.2810 0.1828 0.1499 0.0108  -0.0318 0.0494  99  ASN   A O   
2087 C  CB  A ASN   A 99  ? 0.1727 0.2055 0.0959 -0.0009 -0.0077 0.0179  99  ASN   A CB  
2088 C  CB  B ASN   A 99  ? 0.2745 0.1783 0.1836 0.0067  -0.0256 0.0646  99  ASN   A CB  
2089 C  CG  A ASN   A 99  ? 0.1720 0.2008 0.1110 0.0073  -0.0069 0.0113  99  ASN   A CG  
2090 C  CG  B ASN   A 99  ? 0.2851 0.1888 0.2178 0.0088  -0.0278 0.0639  99  ASN   A CG  
2091 O  OD1 A ASN   A 99  ? 0.1766 0.2118 0.1287 0.0180  -0.0031 -0.0008 99  ASN   A OD1 
2092 O  OD1 B ASN   A 99  ? 0.2899 0.1946 0.2025 0.0127  -0.0334 0.0751  99  ASN   A OD1 
2093 N  ND2 A ASN   A 99  ? 0.1716 0.1923 0.1100 0.0017  -0.0173 0.0307  99  ASN   A ND2 
2094 N  ND2 B ASN   A 99  ? 0.2885 0.1936 0.2409 0.0143  -0.0290 0.0482  99  ASN   A ND2 
2107 N  N   A VAL   A 100 ? 0.2106 0.2464 0.1069 -0.0294 -0.0098 0.0128  100 VAL   A N   
2108 N  N   B VAL   A 100 ? 0.2970 0.2386 0.1525 -0.0006 -0.0410 0.0743  100 VAL   A N   
2109 C  CA  A VAL   A 100 ? 0.2363 0.2638 0.1120 -0.0342 -0.0155 0.0282  100 VAL   A CA  
2110 C  CA  B VAL   A 100 ? 0.3155 0.2799 0.1911 -0.0012 -0.0491 0.0733  100 VAL   A CA  
2111 C  C   A VAL   A 100 ? 0.2462 0.2791 0.1124 -0.0365 -0.0146 0.0552  100 VAL   A C   
2112 C  C   B VAL   A 100 ? 0.3255 0.3036 0.2069 0.0115  -0.0561 0.0817  100 VAL   A C   
2113 O  O   A VAL   A 100 ? 0.2519 0.2892 0.1191 -0.0343 0.0014  0.0572  100 VAL   A O   
2114 O  O   B VAL   A 100 ? 0.3301 0.3163 0.2272 0.0141  -0.0467 0.0649  100 VAL   A O   
2115 C  CB  A VAL   A 100 ? 0.2540 0.2648 0.1491 -0.0423 -0.0199 0.0197  100 VAL   A CB  
2116 C  CB  B VAL   A 100 ? 0.3246 0.2945 0.2364 -0.0098 -0.0453 0.0562  100 VAL   A CB  
2117 C  CG1 A VAL   A 100 ? 0.2559 0.2616 0.1552 -0.0445 -0.0193 0.0251  100 VAL   A CG1 
2118 C  CG1 B VAL   A 100 ? 0.3260 0.2956 0.2519 -0.0130 -0.0469 0.0520  100 VAL   A CG1 
2119 C  CG2 A VAL   A 100 ? 0.2625 0.2689 0.1606 -0.0465 -0.0210 0.0065  100 VAL   A CG2 
2120 C  CG2 B VAL   A 100 ? 0.3287 0.3009 0.2578 -0.0139 -0.0356 0.0489  100 VAL   A CG2 
2139 N  N   A ASN   A 101 ? 0.2533 0.2830 0.1460 -0.0392 -0.0146 0.0792  101 ASN   A N   
2140 N  N   B ASN   A 101 ? 0.3340 0.3126 0.2221 0.0183  -0.0613 0.0967  101 ASN   A N   
2141 C  CA  A ASN   A 101 ? 0.2724 0.2859 0.1588 -0.0374 -0.0197 0.0977  101 ASN   A CA  
2142 C  CA  B ASN   A 101 ? 0.3468 0.3232 0.2474 0.0225  -0.0518 0.1044  101 ASN   A CA  
2143 C  C   A ASN   A 101 ? 0.2977 0.3082 0.1782 -0.0409 0.0038  0.1188  101 ASN   A C   
2144 C  C   B ASN   A 101 ? 0.3634 0.3433 0.2620 0.0266  -0.0218 0.1157  101 ASN   A C   
2145 O  O   A ASN   A 101 ? 0.3114 0.3138 0.2261 -0.0408 0.0074  0.0955  101 ASN   A O   
2146 O  O   B ASN   A 101 ? 0.3714 0.3498 0.2652 0.0290  -0.0090 0.1211  101 ASN   A O   
2147 C  CB  A ASN   A 101 ? 0.2660 0.2654 0.1549 -0.0325 -0.0463 0.0853  101 ASN   A CB  
2148 C  CB  B ASN   A 101 ? 0.3435 0.3148 0.2599 0.0191  -0.0604 0.0907  101 ASN   A CB  
2149 C  CG  A ASN   A 101 ? 0.2573 0.2510 0.1565 -0.0266 -0.0653 0.0457  101 ASN   A CG  
2150 C  CG  B ASN   A 101 ? 0.3419 0.3125 0.2810 0.0135  -0.0671 0.0729  101 ASN   A CG  
2151 O  OD1 A ASN   A 101 ? 0.2499 0.2524 0.1676 -0.0125 -0.0641 0.0098  101 ASN   A OD1 
2152 O  OD1 B ASN   A 101 ? 0.3467 0.3174 0.3011 0.0066  -0.0585 0.0612  101 ASN   A OD1 
2153 N  ND2 A ASN   A 101 ? 0.2581 0.2423 0.1452 -0.0348 -0.0682 0.0361  101 ASN   A ND2 
2154 N  ND2 B ASN   A 101 ? 0.3393 0.3063 0.2896 0.0132  -0.0706 0.0636  101 ASN   A ND2 
2167 N  N   A LYS   A 102 ? 0.3061 0.3303 0.2073 -0.0439 0.0144  0.1262  102 LYS   A N   
2168 N  N   B LYS   A 102 ? 0.3709 0.3570 0.2932 0.0248  -0.0042 0.1031  102 LYS   A N   
2169 C  CA  A LYS   A 102 ? 0.3212 0.3532 0.2353 -0.0404 0.0057  0.1125  102 LYS   A CA  
2170 C  CA  B LYS   A 102 ? 0.3801 0.3703 0.3006 0.0190  0.0062  0.0919  102 LYS   A CA  
2171 C  C   A LYS   A 102 ? 0.3292 0.3717 0.2152 -0.0248 -0.0012 0.1042  102 LYS   A C   
2172 C  C   B LYS   A 102 ? 0.3808 0.3680 0.2882 0.0203  0.0005  0.1045  102 LYS   A C   
2173 O  O   A LYS   A 102 ? 0.3321 0.3834 0.2222 -0.0185 -0.0047 0.1009  102 LYS   A O   
2174 O  O   B LYS   A 102 ? 0.3833 0.3683 0.2853 0.0238  0.0057  0.1176  102 LYS   A O   
2175 C  CB  A LYS   A 102 ? 0.3311 0.3600 0.2871 -0.0506 -0.0051 0.0906  102 LYS   A CB  
2176 C  CB  B LYS   A 102 ? 0.3887 0.3861 0.3308 0.0155  0.0074  0.0664  102 LYS   A CB  
2177 C  CG  A LYS   A 102 ? 0.3395 0.3635 0.3253 -0.0607 -0.0192 0.0737  102 LYS   A CG  
2178 C  CG  B LYS   A 102 ? 0.3970 0.4012 0.3460 0.0118  0.0064  0.0452  102 LYS   A CG  
2179 C  CD  A LYS   A 102 ? 0.3484 0.3666 0.3601 -0.0663 -0.0275 0.0567  102 LYS   A CD  
2180 C  CD  B LYS   A 102 ? 0.4061 0.4162 0.3628 0.0106  0.0061  0.0260  102 LYS   A CD  
2181 C  CE  A LYS   A 102 ? 0.3544 0.3669 0.3873 -0.0703 -0.0340 0.0457  102 LYS   A CE  
2182 C  CE  B LYS   A 102 ? 0.4139 0.4276 0.3774 0.0112  0.0032  0.0133  102 LYS   A CE  
2183 N  NZ  A LYS   A 102 ? 0.3565 0.3657 0.4002 -0.0758 -0.0376 0.0378  102 LYS   A NZ  
2184 N  NZ  B LYS   A 102 ? 0.4190 0.4339 0.3853 0.0128  0.0017  0.0044  102 LYS   A NZ  
2211 N  N   A GLY   A 103 ? 0.3323 0.3805 0.2240 -0.0129 -0.0099 0.0777  103 GLY   A N   
2212 N  N   B GLY   A 103 ? 0.3760 0.3660 0.2726 0.0208  -0.0158 0.0963  103 GLY   A N   
2213 C  CA  A GLY   A 103 ? 0.3348 0.3854 0.2242 -0.0036 -0.0082 0.0572  103 GLY   A CA  
2214 C  CA  B GLY   A 103 ? 0.3683 0.3573 0.2549 0.0202  -0.0243 0.0963  103 GLY   A CA  
2215 C  C   A GLY   A 103 ? 0.3322 0.3890 0.2310 0.0022  0.0013  0.0408  103 GLY   A C   
2216 C  C   B GLY   A 103 ? 0.3549 0.3459 0.2257 0.0183  -0.0273 0.0880  103 GLY   A C   
2217 O  O   A GLY   A 103 ? 0.3411 0.3962 0.2559 0.0100  -0.0012 0.0278  103 GLY   A O   
2218 O  O   B GLY   A 103 ? 0.3633 0.3507 0.2329 0.0221  -0.0312 0.0892  103 GLY   A O   
2225 N  N   A GLU   A 104 ? 0.3174 0.3822 0.2070 -0.0049 0.0133  0.0337  104 GLU   A N   
2226 N  N   B GLU   A 104 ? 0.3296 0.3254 0.1908 0.0120  -0.0323 0.0799  104 GLU   A N   
2227 C  CA  A GLU   A 104 ? 0.2983 0.3727 0.1974 -0.0151 0.0160  0.0277  104 GLU   A CA  
2228 C  CA  B GLU   A 104 ? 0.3051 0.3057 0.1574 0.0037  -0.0347 0.0626  104 GLU   A CA  
2229 C  C   A GLU   A 104 ? 0.3064 0.3841 0.1969 -0.0132 0.0120  0.0035  104 GLU   A C   
2230 C  C   B GLU   A 104 ? 0.2892 0.3008 0.1539 0.0074  -0.0282 0.0343  104 GLU   A C   
2231 O  O   A GLU   A 104 ? 0.3057 0.3866 0.2078 -0.0155 0.0050  -0.0123 104 GLU   A O   
2232 O  O   B GLU   A 104 ? 0.2879 0.2966 0.1832 0.0082  -0.0342 0.0354  104 GLU   A O   
2233 C  CB  A GLU   A 104 ? 0.2672 0.3514 0.1927 -0.0296 0.0210  0.0539  104 GLU   A CB  
2234 C  CB  B GLU   A 104 ? 0.2975 0.2954 0.1516 -0.0089 -0.0292 0.0717  104 GLU   A CB  
2235 C  CG  A GLU   A 104 ? 0.2393 0.3312 0.2108 -0.0406 0.0161  0.0691  104 GLU   A CG  
2236 C  CG  B GLU   A 104 ? 0.2974 0.2966 0.1739 -0.0177 -0.0322 0.0737  104 GLU   A CG  
2237 C  CD  A GLU   A 104 ? 0.2107 0.3117 0.2109 -0.0507 0.0105  0.0808  104 GLU   A CD  
2238 C  CD  B GLU   A 104 ? 0.2976 0.3015 0.1777 -0.0201 -0.0388 0.0738  104 GLU   A CD  
2239 O  OE1 A GLU   A 104 ? 0.1907 0.2975 0.1720 -0.0464 -0.0020 0.0822  104 GLU   A OE1 
2240 O  OE1 B GLU   A 104 ? 0.2974 0.3022 0.1828 -0.0195 -0.0355 0.0631  104 GLU   A OE1 
2241 O  OE2 A GLU   A 104 ? 0.2144 0.3125 0.2415 -0.0595 0.0136  0.0839  104 GLU   A OE2 
2242 O  OE2 B GLU   A 104 ? 0.3034 0.3089 0.1732 -0.0239 -0.0462 0.0775  104 GLU   A OE2 
2255 N  N   A ASP   A 105 ? 0.3141 0.3915 0.2018 -0.0091 0.0133  -0.0078 105 ASP   A N   
2256 N  N   B ASP   A 105 ? 0.2823 0.3003 0.1683 0.0100  -0.0170 0.0127  105 ASP   A N   
2257 C  CA  A ASP   A 105 ? 0.3171 0.3986 0.2242 -0.0049 0.0109  -0.0261 105 ASP   A CA  
2258 C  CA  B ASP   A 105 ? 0.2726 0.2984 0.1946 0.0176  -0.0041 -0.0242 105 ASP   A CA  
2259 C  C   A ASP   A 105 ? 0.2939 0.3877 0.2071 -0.0161 -0.0002 -0.0417 105 ASP   A C   
2260 C  C   B ASP   A 105 ? 0.2562 0.2811 0.1691 0.0048  -0.0041 -0.0322 105 ASP   A C   
2261 O  O   A ASP   A 105 ? 0.2891 0.3915 0.1865 -0.0143 0.0011  -0.0498 105 ASP   A O   
2262 O  O   B ASP   A 105 ? 0.2368 0.2619 0.1075 0.0067  -0.0044 -0.0362 105 ASP   A O   
2263 C  CB  A ASP   A 105 ? 0.3383 0.4146 0.2723 0.0081  0.0161  -0.0278 105 ASP   A CB  
2264 C  CB  B ASP   A 105 ? 0.2776 0.3149 0.2481 0.0347  0.0033  -0.0472 105 ASP   A CB  
2265 C  CG  A ASP   A 105 ? 0.3549 0.4283 0.3120 0.0182  0.0139  -0.0313 105 ASP   A CG  
2266 C  CG  B ASP   A 105 ? 0.2792 0.3272 0.2897 0.0498  0.0049  -0.0734 105 ASP   A CG  
2267 O  OD1 A ASP   A 105 ? 0.3563 0.4328 0.3165 0.0230  0.0142  -0.0423 105 ASP   A OD1 
2268 O  OD1 B ASP   A 105 ? 0.2787 0.3318 0.2903 0.0481  -0.0047 -0.0828 105 ASP   A OD1 
2269 O  OD2 A ASP   A 105 ? 0.3668 0.4346 0.3443 0.0201  0.0100  -0.0235 105 ASP   A OD2 
2270 O  OD2 B ASP   A 105 ? 0.2842 0.3325 0.3250 0.0580  0.0035  -0.0741 105 ASP   A OD2 
2279 N  N   A ILE   A 106 ? 0.2723 0.3694 0.2100 -0.0294 -0.0217 -0.0497 106 ILE   A N   
2280 N  N   B ILE   A 106 ? 0.2560 0.2875 0.2001 -0.0043 -0.0164 -0.0273 106 ILE   A N   
2281 C  CA  A ILE   A 106 ? 0.2438 0.3451 0.2128 -0.0455 -0.0431 -0.0715 106 ILE   A CA  
2282 C  CA  B ILE   A 106 ? 0.2527 0.2896 0.2275 -0.0210 -0.0268 -0.0368 106 ILE   A CA  
2283 C  C   A ILE   A 106 ? 0.2232 0.3215 0.2206 -0.0620 -0.0414 -0.0812 106 ILE   A C   
2284 C  C   B ILE   A 106 ? 0.2491 0.2784 0.2343 -0.0321 -0.0199 -0.0278 106 ILE   A C   
2285 O  O   A ILE   A 106 ? 0.1981 0.3100 0.2237 -0.0652 -0.0346 -0.0831 106 ILE   A O   
2286 O  O   B ILE   A 106 ? 0.2395 0.2762 0.2362 -0.0337 -0.0091 -0.0212 106 ILE   A O   
2287 C  CB  A ILE   A 106 ? 0.2411 0.3448 0.2432 -0.0379 -0.0591 -0.0618 106 ILE   A CB  
2288 C  CB  B ILE   A 106 ? 0.2554 0.3055 0.2557 -0.0242 -0.0459 -0.0434 106 ILE   A CB  
2289 C  CG1 A ILE   A 106 ? 0.2320 0.3369 0.2616 -0.0311 -0.0688 -0.0504 106 ILE   A CG1 
2290 C  CG1 B ILE   A 106 ? 0.2475 0.3129 0.2568 -0.0192 -0.0560 -0.0445 106 ILE   A CG1 
2291 C  CG2 A ILE   A 106 ? 0.2458 0.3492 0.2571 -0.0324 -0.0624 -0.0613 106 ILE   A CG2 
2292 C  CG2 B ILE   A 106 ? 0.2623 0.3112 0.2633 -0.0258 -0.0511 -0.0456 106 ILE   A CG2 
2293 C  CD1 A ILE   A 106 ? 0.2262 0.3308 0.2710 -0.0238 -0.0689 -0.0366 106 ILE   A CD1 
2294 C  CD1 B ILE   A 106 ? 0.2408 0.3161 0.2592 -0.0165 -0.0616 -0.0419 106 ILE   A CD1 
2317 N  N   A GLN   A 107 ? 0.2401 0.3081 0.2501 -0.0633 -0.0247 -0.0887 107 GLN   A N   
2318 N  N   B GLN   A 107 ? 0.2602 0.2676 0.2517 -0.0334 -0.0150 -0.0288 107 GLN   A N   
2319 C  CA  A GLN   A 107 ? 0.2570 0.2934 0.3018 -0.0507 0.0035  -0.0824 107 GLN   A CA  
2320 C  CA  B GLN   A 107 ? 0.2722 0.2651 0.3056 -0.0341 -0.0041 -0.0266 107 GLN   A CA  
2321 C  C   A GLN   A 107 ? 0.2306 0.2506 0.2809 -0.0440 0.0277  -0.0564 107 GLN   A C   
2322 C  C   B GLN   A 107 ? 0.2433 0.2361 0.2858 -0.0379 0.0160  -0.0268 107 GLN   A C   
2323 O  O   A GLN   A 107 ? 0.2214 0.2421 0.3015 -0.0354 0.0573  -0.0578 107 GLN   A O   
2324 O  O   B GLN   A 107 ? 0.2469 0.2317 0.3239 -0.0415 0.0191  -0.0238 107 GLN   A O   
2325 C  CB  A GLN   A 107 ? 0.2955 0.3203 0.3827 -0.0507 0.0009  -0.0839 107 GLN   A CB  
2326 C  CB  B GLN   A 107 ? 0.3066 0.2932 0.3678 -0.0384 -0.0164 -0.0198 107 GLN   A CB  
2327 C  CG  A GLN   A 107 ? 0.3281 0.3447 0.4682 -0.0480 -0.0055 -0.0771 107 GLN   A CG  
2328 C  CG  B GLN   A 107 ? 0.3358 0.3182 0.4322 -0.0404 -0.0309 -0.0083 107 GLN   A CG  
2329 C  CD  A GLN   A 107 ? 0.3539 0.3634 0.5385 -0.0457 -0.0125 -0.0679 107 GLN   A CD  
2330 C  CD  B GLN   A 107 ? 0.3599 0.3406 0.4942 -0.0385 -0.0408 0.0040  107 GLN   A CD  
2331 O  OE1 A GLN   A 107 ? 0.3620 0.3733 0.5717 -0.0464 -0.0156 -0.0664 107 GLN   A OE1 
2332 O  OE1 B GLN   A 107 ? 0.3698 0.3454 0.5093 -0.0361 -0.0412 0.0132  107 GLN   A OE1 
2333 N  NE2 A GLN   A 107 ? 0.3617 0.3670 0.5615 -0.0449 -0.0157 -0.0672 107 GLN   A NE2 
2334 N  NE2 B GLN   A 107 ? 0.3671 0.3506 0.5125 -0.0379 -0.0477 0.0063  107 GLN   A NE2 
2351 N  N   . LEU   A 108 ? 0.2137 0.2151 0.2309 -0.0415 0.0267  -0.0400 108 LEU   A N   
2352 C  CA  . LEU   A 108 ? 0.1856 0.1803 0.2030 -0.0152 0.0213  -0.0145 108 LEU   A CA  
2353 C  C   . LEU   A 108 ? 0.1637 0.1468 0.1941 -0.0057 0.0210  0.0058  108 LEU   A C   
2354 O  O   . LEU   A 108 ? 0.1608 0.1541 0.2051 -0.0037 0.0288  0.0111  108 LEU   A O   
2355 C  CB  . LEU   A 108 ? 0.1933 0.1955 0.1705 -0.0187 0.0238  -0.0107 108 LEU   A CB  
2356 C  CG  . LEU   A 108 ? 0.2075 0.2210 0.2024 -0.0226 0.0336  -0.0119 108 LEU   A CG  
2357 C  CD1 . LEU   A 108 ? 0.2298 0.2273 0.1992 -0.0360 0.0503  -0.0111 108 LEU   A CD1 
2358 C  CD2 . LEU   A 108 ? 0.2072 0.2441 0.2550 -0.0140 0.0282  -0.0083 108 LEU   A CD2 
2371 N  N   . LEU   A 109 ? 0.1528 0.1493 0.1848 0.0021  0.0137  0.0158  109 LEU   A N   
2372 C  CA  . LEU   A 109 ? 0.1474 0.1426 0.1720 0.0007  -0.0013 0.0152  109 LEU   A CA  
2373 C  C   . LEU   A 109 ? 0.1365 0.1353 0.1676 -0.0090 0.0021  0.0159  109 LEU   A C   
2374 O  O   . LEU   A 109 ? 0.1455 0.1287 0.1852 -0.0063 -0.0044 0.0108  109 LEU   A O   
2375 C  CB  . LEU   A 109 ? 0.1569 0.1497 0.1938 0.0058  -0.0035 0.0328  109 LEU   A CB  
2376 C  CG  . LEU   A 109 ? 0.1446 0.1540 0.1995 0.0080  0.0002  0.0415  109 LEU   A CG  
2377 C  CD1 . LEU   A 109 ? 0.1525 0.1454 0.2187 -0.0006 0.0040  0.0235  109 LEU   A CD1 
2378 C  CD2 . LEU   A 109 ? 0.1456 0.1751 0.2166 0.0045  -0.0049 0.0332  109 LEU   A CD2 
2390 N  N   . LYS   A 110 ? 0.1397 0.1345 0.1667 -0.0084 -0.0058 0.0106  110 LYS   A N   
2391 C  CA  . LYS   A 110 ? 0.1391 0.1254 0.1664 -0.0094 -0.0031 0.0136  110 LYS   A CA  
2392 C  C   . LYS   A 110 ? 0.1417 0.1209 0.1445 -0.0103 0.0065  -0.0008 110 LYS   A C   
2393 O  O   . LYS   A 110 ? 0.1342 0.1253 0.1576 -0.0099 0.0053  0.0016  110 LYS   A O   
2394 C  CB  . LYS   A 110 ? 0.1468 0.1334 0.1888 -0.0117 -0.0068 0.0045  110 LYS   A CB  
2395 C  CG  . LYS   A 110 ? 0.1463 0.1300 0.2027 -0.0101 -0.0102 0.0010  110 LYS   A CG  
2396 C  CD  . LYS   A 110 ? 0.1465 0.1360 0.2293 -0.0121 -0.0172 -0.0042 110 LYS   A CD  
2397 C  CE  . LYS   A 110 ? 0.1556 0.1407 0.2506 -0.0113 0.0128  0.0024  110 LYS   A CE  
2398 N  NZ  . LYS   A 110 ? 0.1572 0.1459 0.2581 -0.0186 0.0145  0.0057  110 LYS   A NZ  
2412 N  N   . SER   A 111 ? 0.1412 0.1285 0.1513 0.0016  0.0017  0.0037  111 SER   A N   
2413 C  CA  . SER   A 111 ? 0.1339 0.1332 0.1550 0.0007  0.0022  0.0020  111 SER   A CA  
2414 C  C   . SER   A 111 ? 0.1245 0.1278 0.1525 -0.0068 0.0048  0.0078  111 SER   A C   
2415 O  O   . SER   A 111 ? 0.1375 0.1172 0.1746 -0.0064 0.0073  0.0074  111 SER   A O   
2416 C  CB  . SER   A 111 ? 0.1553 0.1529 0.1751 0.0008  0.0238  -0.0064 111 SER   A CB  
2417 O  OG  . SER   A 111 ? 0.1995 0.1687 0.1937 0.0021  0.0320  -0.0122 111 SER   A OG  
2423 N  N   . ALA   A 112 ? 0.1315 0.1229 0.1562 0.0016  0.0077  0.0118  112 ALA   A N   
2424 C  CA  . ALA   A 112 ? 0.1332 0.1166 0.1538 -0.0023 0.0128  0.0075  112 ALA   A CA  
2425 C  C   . ALA   A 112 ? 0.1239 0.1151 0.1566 0.0004  0.0048  0.0091  112 ALA   A C   
2426 O  O   . ALA   A 112 ? 0.1299 0.1149 0.1677 -0.0094 0.0117  0.0113  112 ALA   A O   
2427 C  CB  . ALA   A 112 ? 0.1447 0.1187 0.1558 -0.0043 0.0106  0.0106  112 ALA   A CB  
2433 N  N   . TYR   A 113 ? 0.1151 0.1179 0.1710 -0.0030 0.0055  0.0149  113 TYR   A N   
2434 C  CA  . TYR   A 113 ? 0.1148 0.1185 0.1669 -0.0030 0.0104  0.0144  113 TYR   A CA  
2435 C  C   . TYR   A 113 ? 0.1112 0.1204 0.1511 -0.0081 0.0068  0.0147  113 TYR   A C   
2436 O  O   . TYR   A 113 ? 0.1194 0.1213 0.1640 -0.0055 0.0102  0.0093  113 TYR   A O   
2437 C  CB  . TYR   A 113 ? 0.1172 0.1251 0.1703 -0.0021 0.0070  0.0165  113 TYR   A CB  
2438 C  CG  . TYR   A 113 ? 0.1233 0.1315 0.1605 -0.0090 0.0059  0.0215  113 TYR   A CG  
2439 C  CD1 . TYR   A 113 ? 0.1207 0.1398 0.1597 -0.0012 0.0071  0.0191  113 TYR   A CD1 
2440 C  CD2 . TYR   A 113 ? 0.1295 0.1364 0.1662 -0.0091 -0.0012 0.0262  113 TYR   A CD2 
2441 C  CE1 . TYR   A 113 ? 0.1308 0.1487 0.1648 -0.0029 0.0071  0.0280  113 TYR   A CE1 
2442 C  CE2 . TYR   A 113 ? 0.1311 0.1452 0.1731 -0.0073 -0.0032 0.0311  113 TYR   A CE2 
2443 C  CZ  . TYR   A 113 ? 0.1279 0.1472 0.1637 0.0048  0.0066  0.0356  113 TYR   A CZ  
2444 O  OH  . TYR   A 113 ? 0.1243 0.1590 0.1933 0.0143  0.0065  0.0315  113 TYR   A OH  
2454 N  N   . GLU   A 114 ? 0.1171 0.1174 0.1629 -0.0068 0.0084  0.0093  114 GLU   A N   
2455 C  CA  . GLU   A 114 ? 0.1199 0.1088 0.1701 0.0047  0.0033  0.0151  114 GLU   A CA  
2456 C  C   . GLU   A 114 ? 0.1184 0.1208 0.1652 0.0018  0.0111  0.0110  114 GLU   A C   
2457 O  O   . GLU   A 114 ? 0.1249 0.1224 0.1692 -0.0006 0.0017  0.0109  114 GLU   A O   
2458 C  CB  . GLU   A 114 ? 0.1217 0.1139 0.1774 0.0003  0.0037  0.0146  114 GLU   A CB  
2459 C  CG  . GLU   A 114 ? 0.1277 0.1176 0.1771 0.0031  0.0118  0.0008  114 GLU   A CG  
2460 C  CD  . GLU   A 114 ? 0.1388 0.1183 0.1860 -0.0041 0.0010  0.0075  114 GLU   A CD  
2461 O  OE1 . GLU   A 114 ? 0.1438 0.1223 0.1905 -0.0121 0.0146  -0.0009 114 GLU   A OE1 
2462 O  OE2 . GLU   A 114 ? 0.1601 0.1283 0.2111 -0.0134 0.0099  -0.0119 114 GLU   A OE2 
2469 N  N   . ASN   A 115 ? 0.1191 0.1178 0.1557 -0.0045 0.0121  0.0099  115 ASN   A N   
2470 C  CA  . ASN   A 115 ? 0.1199 0.1208 0.1619 -0.0117 0.0090  0.0135  115 ASN   A CA  
2471 C  C   . ASN   A 115 ? 0.1234 0.1176 0.1533 -0.0096 -0.0019 0.0080  115 ASN   A C   
2472 O  O   . ASN   A 115 ? 0.1240 0.1261 0.1614 -0.0084 0.0115  0.0168  115 ASN   A O   
2473 C  CB  . ASN   A 115 ? 0.1307 0.1303 0.1612 -0.0134 0.0082  0.0146  115 ASN   A CB  
2474 C  CG  . ASN   A 115 ? 0.1305 0.1474 0.1707 -0.0120 0.0139  0.0179  115 ASN   A CG  
2475 O  OD1 . ASN   A 115 ? 0.1309 0.2478 0.1954 -0.0084 0.0188  0.0333  115 ASN   A OD1 
2476 N  ND2 . ASN   A 115 ? 0.1290 0.1294 0.1721 -0.0115 0.0176  0.0175  115 ASN   A ND2 
2483 N  N   . PHE   A 116 ? 0.1171 0.1234 0.1547 0.0009  0.0071  0.0133  116 PHE   A N   
2484 C  CA  . PHE   A 116 ? 0.1205 0.1295 0.1483 0.0029  0.0107  0.0109  116 PHE   A CA  
2485 C  C   . PHE   A 116 ? 0.1221 0.1334 0.1541 -0.0040 0.0118  0.0137  116 PHE   A C   
2486 O  O   . PHE   A 116 ? 0.1254 0.1388 0.1696 0.0069  0.0144  0.0234  116 PHE   A O   
2487 C  CB  . PHE   A 116 ? 0.1193 0.1212 0.1692 0.0019  0.0159  0.0169  116 PHE   A CB  
2488 C  CG  . PHE   A 116 ? 0.1205 0.1227 0.1603 -0.0019 0.0068  0.0129  116 PHE   A CG  
2489 C  CD1 . PHE   A 116 ? 0.1278 0.1171 0.1719 -0.0016 0.0080  0.0191  116 PHE   A CD1 
2490 C  CD2 . PHE   A 116 ? 0.1310 0.1358 0.1659 -0.0012 0.0128  0.0191  116 PHE   A CD2 
2491 C  CE1 . PHE   A 116 ? 0.1273 0.1190 0.1820 -0.0083 0.0065  0.0139  116 PHE   A CE1 
2492 C  CE2 . PHE   A 116 ? 0.1269 0.1298 0.1809 -0.0024 0.0143  0.0086  116 PHE   A CE2 
2493 C  CZ  . PHE   A 116 ? 0.1299 0.1112 0.1728 0.0027  0.0058  0.0189  116 PHE   A CZ  
2503 N  N   . ASN   A 117 ? 0.1258 0.1281 0.1618 -0.0033 0.0103  0.0281  117 ASN   A N   
2504 C  CA  . ASN   A 117 ? 0.1267 0.1247 0.1636 -0.0022 0.0075  0.0251  117 ASN   A CA  
2505 C  C   . ASN   A 117 ? 0.1238 0.1324 0.1750 0.0025  0.0085  0.0305  117 ASN   A C   
2506 O  O   . ASN   A 117 ? 0.1336 0.1384 0.2065 -0.0035 -0.0056 0.0421  117 ASN   A O   
2507 C  CB  . ASN   A 117 ? 0.1239 0.1312 0.1739 0.0030  0.0077  0.0298  117 ASN   A CB  
2508 C  CG  . ASN   A 117 ? 0.1232 0.1284 0.1743 -0.0001 0.0098  0.0284  117 ASN   A CG  
2509 O  OD1 . ASN   A 117 ? 0.1247 0.1478 0.1907 -0.0086 0.0156  0.0197  117 ASN   A OD1 
2510 N  ND2 . ASN   A 117 ? 0.1202 0.1263 0.1839 -0.0019 0.0016  0.0279  117 ASN   A ND2 
2517 N  N   . GLN   A 118 ? 0.1201 0.1327 0.1840 -0.0048 0.0001  0.0355  118 GLN   A N   
2518 C  CA  . GLN   A 118 ? 0.1311 0.1417 0.1905 -0.0005 -0.0026 0.0234  118 GLN   A CA  
2519 C  C   . GLN   A 118 ? 0.1324 0.1512 0.1688 -0.0041 -0.0055 0.0272  118 GLN   A C   
2520 O  O   . GLN   A 118 ? 0.1303 0.1820 0.2017 0.0032  -0.0128 0.0075  118 GLN   A O   
2521 C  CB  . GLN   A 118 ? 0.1269 0.1413 0.2008 -0.0020 0.0098  0.0249  118 GLN   A CB  
2522 C  CG  . GLN   A 118 ? 0.1256 0.1509 0.2030 0.0051  0.0104  0.0296  118 GLN   A CG  
2523 C  CD  . GLN   A 118 ? 0.1193 0.1517 0.2110 0.0084  0.0099  0.0254  118 GLN   A CD  
2524 O  OE1 . GLN   A 118 ? 0.1236 0.1659 0.2192 0.0131  0.0007  0.0132  118 GLN   A OE1 
2525 N  NE2 . GLN   A 118 ? 0.1330 0.1545 0.2099 0.0068  -0.0000 0.0260  118 GLN   A NE2 
2534 N  N   . HIS   A 119 ? 0.1336 0.1504 0.1628 -0.0001 -0.0024 0.0290  119 HIS   A N   
2535 C  CA  . HIS   A 119 ? 0.1403 0.1560 0.1669 -0.0030 -0.0046 0.0311  119 HIS   A CA  
2536 C  C   . HIS   A 119 ? 0.1502 0.1650 0.1638 -0.0042 0.0108  0.0370  119 HIS   A C   
2537 O  O   . HIS   A 119 ? 0.1494 0.1722 0.1744 -0.0198 0.0036  0.0371  119 HIS   A O   
2538 C  CB  . HIS   A 119 ? 0.1472 0.1490 0.1785 -0.0005 0.0146  0.0382  119 HIS   A CB  
2539 C  CG  . HIS   A 119 ? 0.1548 0.1540 0.2294 0.0024  0.0122  0.0367  119 HIS   A CG  
2540 N  ND1 . HIS   A 119 ? 0.1676 0.1697 0.2893 -0.0110 0.0092  0.0253  119 HIS   A ND1 
2541 C  CD2 . HIS   A 119 ? 0.1568 0.1610 0.2567 0.0147  0.0343  0.0550  119 HIS   A CD2 
2542 C  CE1 . HIS   A 119 ? 0.1641 0.1667 0.3077 -0.0117 0.0292  0.0433  119 HIS   A CE1 
2543 N  NE2 . HIS   A 119 ? 0.1660 0.1631 0.2963 0.0054  0.0501  0.0593  119 HIS   A NE2 
2551 N  N   A GLU   A 120 ? 0.1526 0.1804 0.1703 0.0038  -0.0015 0.0509  120 GLU   A N   
2552 N  N   B GLU   A 120 ? 0.1551 0.1844 0.1724 0.0043  0.0051  0.0482  120 GLU   A N   
2553 C  CA  A GLU   A 120 ? 0.1683 0.1978 0.1860 0.0086  -0.0038 0.0806  120 GLU   A CA  
2554 C  CA  B GLU   A 120 ? 0.1723 0.2060 0.1918 0.0093  0.0063  0.0764  120 GLU   A CA  
2555 C  C   A GLU   A 120 ? 0.1624 0.1920 0.1642 -0.0040 0.0014  0.0779  120 GLU   A C   
2556 C  C   B GLU   A 120 ? 0.1654 0.1978 0.1682 -0.0010 0.0038  0.0728  120 GLU   A C   
2557 O  O   A GLU   A 120 ? 0.1616 0.1846 0.1811 -0.0107 0.0060  0.0813  120 GLU   A O   
2558 O  O   B GLU   A 120 ? 0.1664 0.1932 0.1882 -0.0030 0.0024  0.0701  120 GLU   A O   
2559 C  CB  A GLU   A 120 ? 0.1965 0.2330 0.2346 0.0162  0.0002  0.1055  120 GLU   A CB  
2560 C  CB  B GLU   A 120 ? 0.2019 0.2453 0.2440 0.0163  0.0188  0.1028  120 GLU   A CB  
2561 C  CG  A GLU   A 120 ? 0.2374 0.2632 0.3259 0.0229  0.0025  0.1050  120 GLU   A CG  
2562 C  CG  B GLU   A 120 ? 0.2433 0.2783 0.3316 0.0231  0.0254  0.1076  120 GLU   A CG  
2563 C  CD  A GLU   A 120 ? 0.2791 0.2916 0.4112 0.0285  0.0135  0.0892  120 GLU   A CD  
2564 C  CD  B GLU   A 120 ? 0.2834 0.3087 0.4100 0.0303  0.0378  0.0985  120 GLU   A CD  
2565 O  OE1 A GLU   A 120 ? 0.2954 0.3097 0.4401 0.0300  0.0159  0.0763  120 GLU   A OE1 
2566 O  OE1 B GLU   A 120 ? 0.2976 0.3261 0.4413 0.0332  0.0405  0.0863  120 GLU   A OE1 
2567 O  OE2 A GLU   A 120 ? 0.2907 0.2978 0.4366 0.0232  0.0168  0.0923  120 GLU   A OE2 
2568 O  OE2 B GLU   A 120 ? 0.2957 0.3149 0.4325 0.0271  0.0379  0.1006  120 GLU   A OE2 
2581 N  N   . VAL   A 121 ? 0.1610 0.1985 0.1502 -0.0053 0.0023  0.0601  121 VAL   A N   
2582 C  CA  . VAL   A 121 ? 0.1641 0.2041 0.1449 -0.0089 0.0162  0.0614  121 VAL   A CA  
2583 C  C   . VAL   A 121 ? 0.1534 0.1828 0.1363 -0.0191 0.0105  0.0474  121 VAL   A C   
2584 O  O   . VAL   A 121 ? 0.1589 0.1886 0.1577 -0.0246 -0.0076 0.0426  121 VAL   A O   
2585 C  CB  . VAL   A 121 ? 0.2025 0.2482 0.1781 0.0077  0.0256  0.0738  121 VAL   A CB  
2586 C  CG1 . VAL   A 121 ? 0.2041 0.2642 0.1841 0.0168  0.0348  0.0722  121 VAL   A CG1 
2587 C  CG2 . VAL   A 121 ? 0.2286 0.2706 0.2294 0.0006  0.0257  0.0618  121 VAL   A CG2 
2598 N  N   . LEU   A 122 ? 0.1430 0.1608 0.1480 -0.0173 0.0076  0.0377  122 LEU   A N   
2599 C  CA  . LEU   A 122 ? 0.1473 0.1475 0.1472 -0.0150 0.0204  0.0393  122 LEU   A CA  
2600 C  C   . LEU   A 122 ? 0.1447 0.1490 0.1488 -0.0185 0.0041  0.0344  122 LEU   A C   
2601 O  O   . LEU   A 122 ? 0.1458 0.1543 0.1766 -0.0223 0.0008  0.0351  122 LEU   A O   
2602 C  CB  . LEU   A 122 ? 0.1648 0.1537 0.1886 -0.0083 0.0118  0.0480  122 LEU   A CB  
2603 C  CG  . LEU   A 122 ? 0.1743 0.1626 0.1738 -0.0079 0.0191  0.0293  122 LEU   A CG  
2604 C  CD1 . LEU   A 122 ? 0.1889 0.1644 0.1847 -0.0163 0.0264  0.0318  122 LEU   A CD1 
2605 C  CD2 . LEU   A 122 ? 0.1660 0.1538 0.1608 -0.0047 0.0286  0.0268  122 LEU   A CD2 
2617 N  N   . LEU   A 123 ? 0.1347 0.1494 0.1453 -0.0222 0.0046  0.0324  123 LEU   A N   
2618 C  CA  . LEU   A 123 ? 0.1384 0.1511 0.1399 -0.0177 0.0074  0.0218  123 LEU   A CA  
2619 C  C   . LEU   A 123 ? 0.1366 0.1374 0.1246 -0.0114 0.0076  0.0282  123 LEU   A C   
2620 O  O   . LEU   A 123 ? 0.1359 0.1507 0.1448 -0.0212 0.0022  0.0316  123 LEU   A O   
2621 C  CB  . LEU   A 123 ? 0.1421 0.1565 0.1326 -0.0212 0.0144  0.0247  123 LEU   A CB  
2622 C  CG  . LEU   A 123 ? 0.1489 0.1668 0.1493 -0.0150 0.0167  0.0129  123 LEU   A CG  
2623 C  CD1 . LEU   A 123 ? 0.1550 0.1749 0.1724 -0.0039 0.0131  0.0092  123 LEU   A CD1 
2624 C  CD2 . LEU   A 123 ? 0.1664 0.1773 0.1760 -0.0107 0.0122  0.0077  123 LEU   A CD2 
2636 N  N   A ALA   A 124 ? 0.1333 0.1332 0.1168 -0.0079 0.0030  0.0266  124 ALA   A N   
2637 N  N   B ALA   A 124 ? 0.1361 0.1347 0.1375 -0.0169 0.0124  0.0202  124 ALA   A N   
2638 C  CA  A ALA   A 124 ? 0.1215 0.1313 0.1158 0.0022  -0.0015 0.0305  124 ALA   A CA  
2639 C  CA  B ALA   A 124 ? 0.1292 0.1333 0.1603 -0.0236 0.0144  0.0274  124 ALA   A CA  
2640 C  C   A ALA   A 124 ? 0.1187 0.1305 0.1247 -0.0053 0.0077  0.0286  124 ALA   A C   
2641 C  C   B ALA   A 124 ? 0.1225 0.1252 0.1585 -0.0178 0.0132  0.0273  124 ALA   A C   
2642 O  O   A ALA   A 124 ? 0.1207 0.1331 0.1341 -0.0054 0.0065  0.0332  124 ALA   A O   
2643 O  O   B ALA   A 124 ? 0.1252 0.1292 0.1600 -0.0074 0.0231  0.0236  124 ALA   A O   
2644 C  CB  A ALA   A 124 ? 0.1177 0.1273 0.1225 0.0163  -0.0067 0.0298  124 ALA   A CB  
2645 C  CB  B ALA   A 124 ? 0.1399 0.1351 0.1746 -0.0233 0.0130  0.0301  124 ALA   A CB  
2656 N  N   A PRO   A 125 ? 0.1201 0.1327 0.1383 -0.0030 0.0119  0.0284  125 PRO   A N   
2657 N  N   B PRO   A 125 ? 0.1108 0.1206 0.1489 -0.0055 0.0055  0.0306  125 PRO   A N   
2658 C  CA  A PRO   A 125 ? 0.1240 0.1353 0.1469 -0.0070 0.0061  0.0223  125 PRO   A CA  
2659 C  CA  B PRO   A 125 ? 0.1157 0.1271 0.1604 -0.0055 -0.0026 0.0270  125 PRO   A CA  
2660 C  C   A PRO   A 125 ? 0.1159 0.1279 0.1297 -0.0129 0.0074  0.0350  125 PRO   A C   
2661 C  C   B PRO   A 125 ? 0.1242 0.1440 0.1681 -0.0003 -0.0051 0.0276  125 PRO   A C   
2662 O  O   A PRO   A 125 ? 0.1300 0.1259 0.1552 -0.0022 0.0003  0.0298  125 PRO   A O   
2663 O  O   B PRO   A 125 ? 0.1329 0.1489 0.1753 0.0070  -0.0081 0.0247  125 PRO   A O   
2664 C  CB  A PRO   A 125 ? 0.1330 0.1430 0.1504 -0.0095 0.0146  0.0177  125 PRO   A CB  
2665 C  CB  B PRO   A 125 ? 0.1125 0.1202 0.1501 -0.0100 0.0060  0.0318  125 PRO   A CB  
2666 C  CG  A PRO   A 125 ? 0.1403 0.1422 0.1572 -0.0043 0.0057  0.0226  125 PRO   A CG  
2667 C  CG  B PRO   A 125 ? 0.1067 0.1080 0.1361 -0.0049 0.0061  0.0258  125 PRO   A CG  
2668 C  CD  A PRO   A 125 ? 0.1284 0.1384 0.1502 0.0005  0.0056  0.0183  125 PRO   A CD  
2669 C  CD  B PRO   A 125 ? 0.1042 0.1088 0.1246 -0.0096 0.0150  0.0303  125 PRO   A CD  
2684 N  N   A LEU   A 126 ? 0.1130 0.1294 0.1227 -0.0057 0.0020  0.0296  126 LEU   A N   
2685 N  N   B LEU   A 126 ? 0.1365 0.1557 0.1953 0.0080  -0.0075 0.0177  126 LEU   A N   
2686 C  CA  A LEU   A 126 ? 0.1108 0.1300 0.1265 -0.0097 0.0015  0.0234  126 LEU   A CA  
2687 C  CA  B LEU   A 126 ? 0.1463 0.1586 0.2098 0.0112  -0.0055 0.0133  126 LEU   A CA  
2688 C  C   A LEU   A 126 ? 0.1211 0.1333 0.1187 0.0011  -0.0009 0.0235  126 LEU   A C   
2689 C  C   B LEU   A 126 ? 0.1464 0.1568 0.1883 0.0162  -0.0024 0.0094  126 LEU   A C   
2690 O  O   A LEU   A 126 ? 0.1208 0.1304 0.1361 0.0031  0.0113  0.0254  126 LEU   A O   
2691 O  O   B LEU   A 126 ? 0.1464 0.1528 0.1959 0.0111  -0.0145 0.0143  126 LEU   A O   
2692 C  CB  A LEU   A 126 ? 0.1110 0.1314 0.1360 -0.0072 0.0003  0.0196  126 LEU   A CB  
2693 C  CB  B LEU   A 126 ? 0.1666 0.1761 0.2611 0.0064  -0.0143 0.0041  126 LEU   A CB  
2694 C  CG  A LEU   A 126 ? 0.1058 0.1539 0.1479 -0.0180 0.0077  0.0154  126 LEU   A CG  
2695 C  CG  B LEU   A 126 ? 0.1819 0.1911 0.3033 0.0027  -0.0243 0.0026  126 LEU   A CG  
2696 C  CD1 A LEU   A 126 ? 0.1126 0.1662 0.1674 -0.0213 0.0034  0.0154  126 LEU   A CD1 
2697 C  CD1 B LEU   A 126 ? 0.1844 0.1910 0.3119 -0.0049 -0.0249 -0.0035 126 LEU   A CD1 
2698 C  CD2 A LEU   A 126 ? 0.1247 0.1519 0.1633 -0.0259 -0.0014 0.0304  126 LEU   A CD2 
2699 C  CD2 B LEU   A 126 ? 0.1879 0.1997 0.3164 0.0059  -0.0289 0.0083  126 LEU   A CD2 
2722 N  N   A LEU   A 127 ? 0.1419 0.1378 0.1350 0.0002  0.0091  0.0241  127 LEU   A N   
2723 N  N   B LEU   A 127 ? 0.1480 0.1569 0.1821 0.0192  0.0049  0.0136  127 LEU   A N   
2724 C  CA  A LEU   A 127 ? 0.1474 0.1383 0.1346 0.0000  0.0126  0.0164  127 LEU   A CA  
2725 C  CA  B LEU   A 127 ? 0.1444 0.1554 0.1639 0.0191  -0.0035 0.0198  127 LEU   A CA  
2726 C  C   A LEU   A 127 ? 0.1466 0.1321 0.1426 -0.0059 0.0173  0.0053  127 LEU   A C   
2727 C  C   B LEU   A 127 ? 0.1388 0.1443 0.1585 0.0183  -0.0098 0.0096  127 LEU   A C   
2728 O  O   A LEU   A 127 ? 0.1524 0.1328 0.1441 -0.0185 0.0252  0.0120  127 LEU   A O   
2729 O  O   B LEU   A 127 ? 0.1507 0.1470 0.1724 0.0144  -0.0107 0.0136  127 LEU   A O   
2730 C  CB  A LEU   A 127 ? 0.1492 0.1375 0.1388 0.0089  0.0093  0.0086  127 LEU   A CB  
2731 C  CB  B LEU   A 127 ? 0.1434 0.1648 0.1600 0.0187  -0.0058 0.0103  127 LEU   A CB  
2732 C  CG  A LEU   A 127 ? 0.1503 0.1308 0.1392 0.0115  -0.0034 0.0075  127 LEU   A CG  
2733 C  CG  B LEU   A 127 ? 0.1438 0.1713 0.1503 0.0168  -0.0052 0.0184  127 LEU   A CG  
2734 C  CD1 A LEU   A 127 ? 0.1537 0.1180 0.1572 0.0102  -0.0147 -0.0048 127 LEU   A CD1 
2735 C  CD1 B LEU   A 127 ? 0.1436 0.1762 0.1604 0.0195  -0.0025 0.0191  127 LEU   A CD1 
2736 C  CD2 A LEU   A 127 ? 0.1643 0.1216 0.1697 0.0144  -0.0063 0.0115  127 LEU   A CD2 
2737 C  CD2 B LEU   A 127 ? 0.1616 0.1824 0.1662 0.0132  -0.0140 0.0162  127 LEU   A CD2 
2760 N  N   A SER   A 128 ? 0.1495 0.1358 0.1471 -0.0044 0.0112  0.0101  128 SER   A N   
2761 N  N   B SER   A 128 ? 0.1390 0.1426 0.1465 0.0089  -0.0151 0.0148  128 SER   A N   
2762 C  CA  A SER   A 128 ? 0.1551 0.1433 0.1548 -0.0003 0.0072  0.0110  128 SER   A CA  
2763 C  CA  B SER   A 128 ? 0.1490 0.1395 0.1462 0.0064  -0.0154 0.0185  128 SER   A CA  
2764 C  C   A SER   A 128 ? 0.1619 0.1455 0.1661 0.0113  0.0079  0.0166  128 SER   A C   
2765 C  C   B SER   A 128 ? 0.1529 0.1376 0.1552 0.0072  -0.0285 0.0219  128 SER   A C   
2766 O  O   A SER   A 128 ? 0.1743 0.1677 0.2016 0.0169  0.0036  0.0094  128 SER   A O   
2767 O  O   B SER   A 128 ? 0.1595 0.1479 0.1700 0.0048  -0.0307 0.0172  128 SER   A O   
2768 C  CB  A SER   A 128 ? 0.1492 0.1501 0.1517 -0.0064 -0.0007 0.0106  128 SER   A CB  
2769 C  CB  B SER   A 128 ? 0.1496 0.1457 0.1402 0.0034  -0.0114 0.0200  128 SER   A CB  
2770 O  OG  A SER   A 128 ? 0.1455 0.1528 0.1550 -0.0058 0.0020  0.0032  128 SER   A OG  
2771 O  OG  B SER   A 128 ? 0.1528 0.1515 0.1386 0.0058  -0.0001 0.0203  128 SER   A OG  
2782 N  N   A ALA   A 129 ? 0.1534 0.1451 0.1741 0.0060  0.0075  0.0255  129 ALA   A N   
2783 N  N   B ALA   A 129 ? 0.1448 0.1448 0.1818 0.0036  -0.0330 0.0265  129 ALA   A N   
2784 C  CA  A ALA   A 129 ? 0.1456 0.1462 0.1807 0.0092  -0.0020 0.0182  129 ALA   A CA  
2785 C  CA  B ALA   A 129 ? 0.1483 0.1529 0.1971 0.0002  -0.0270 0.0159  129 ALA   A CA  
2786 C  C   A ALA   A 129 ? 0.1460 0.1362 0.1628 0.0067  -0.0128 -0.0011 129 ALA   A C   
2787 C  C   B ALA   A 129 ? 0.1593 0.1577 0.1922 0.0004  -0.0338 0.0011  129 ALA   A C   
2788 O  O   A ALA   A 129 ? 0.1463 0.1356 0.1676 -0.0001 -0.0056 0.0137  129 ALA   A O   
2789 O  O   B ALA   A 129 ? 0.1671 0.1665 0.1955 -0.0048 -0.0265 0.0196  129 ALA   A O   
2790 C  CB  A ALA   A 129 ? 0.1458 0.1596 0.2130 0.0148  0.0009  0.0178  129 ALA   A CB  
2791 C  CB  B ALA   A 129 ? 0.1493 0.1625 0.2042 -0.0038 -0.0259 0.0111  129 ALA   A CB  
2802 N  N   A GLY   A 130 ? 0.1438 0.1295 0.1653 0.0089  -0.0243 -0.0145 130 GLY   A N   
2803 N  N   B GLY   A 130 ? 0.1623 0.1561 0.1944 -0.0016 -0.0489 -0.0068 130 GLY   A N   
2804 C  CA  A GLY   A 130 ? 0.1566 0.1262 0.1711 0.0070  -0.0300 -0.0172 130 GLY   A CA  
2805 C  CA  B GLY   A 130 ? 0.1740 0.1648 0.2073 0.0016  -0.0523 -0.0110 130 GLY   A CA  
2806 C  C   A GLY   A 130 ? 0.1640 0.1233 0.1803 0.0082  -0.0311 0.0005  130 GLY   A C   
2807 C  C   B GLY   A 130 ? 0.1865 0.1713 0.2132 0.0078  -0.0500 -0.0051 130 GLY   A C   
2808 O  O   A GLY   A 130 ? 0.1699 0.1193 0.1808 0.0060  -0.0281 -0.0022 130 GLY   A O   
2809 O  O   B GLY   A 130 ? 0.1917 0.1767 0.2233 0.0116  -0.0526 0.0053  130 GLY   A O   
2816 N  N   A ILE   A 131 ? 0.1661 0.1283 0.1945 0.0015  -0.0332 0.0155  131 ILE   A N   
2817 N  N   B ILE   A 131 ? 0.1917 0.1684 0.2215 0.0075  -0.0360 -0.0033 131 ILE   A N   
2818 C  CA  A ILE   A 131 ? 0.1830 0.1326 0.1750 -0.0028 -0.0424 0.0239  131 ILE   A CA  
2819 C  CA  B ILE   A 131 ? 0.2057 0.1638 0.1930 0.0089  -0.0419 -0.0064 131 ILE   A CA  
2820 C  C   A ILE   A 131 ? 0.1835 0.1400 0.1643 -0.0016 -0.0342 0.0328  131 ILE   A C   
2821 C  C   B ILE   A 131 ? 0.2067 0.1647 0.1774 0.0171  -0.0365 -0.0117 131 ILE   A C   
2822 O  O   A ILE   A 131 ? 0.1974 0.1536 0.1707 -0.0045 -0.0292 0.0374  131 ILE   A O   
2823 O  O   B ILE   A 131 ? 0.2130 0.1648 0.1979 0.0191  -0.0337 -0.0102 131 ILE   A O   
2824 C  CB  A ILE   A 131 ? 0.2044 0.1444 0.1862 -0.0089 -0.0520 0.0175  131 ILE   A CB  
2825 C  CB  B ILE   A 131 ? 0.2178 0.1683 0.1979 0.0010  -0.0472 -0.0046 131 ILE   A CB  
2826 C  CG1 A ILE   A 131 ? 0.2141 0.1603 0.1778 -0.0228 -0.0510 0.0215  131 ILE   A CG1 
2827 C  CG1 B ILE   A 131 ? 0.2288 0.1878 0.2083 -0.0057 -0.0537 -0.0040 131 ILE   A CG1 
2828 C  CG2 A ILE   A 131 ? 0.2132 0.1335 0.1961 -0.0020 -0.0477 0.0094  131 ILE   A CG2 
2829 C  CG2 B ILE   A 131 ? 0.2218 0.1544 0.2104 -0.0008 -0.0378 -0.0085 131 ILE   A CG2 
2830 C  CD1 A ILE   A 131 ? 0.2229 0.1655 0.1952 -0.0264 -0.0504 0.0226  131 ILE   A CD1 
2831 C  CD1 B ILE   A 131 ? 0.2377 0.2000 0.2207 -0.0147 -0.0517 0.0013  131 ILE   A CD1 
2854 N  N   A PHE   A 132 ? 0.1758 0.1365 0.1583 0.0036  -0.0337 0.0298  132 PHE   A N   
2855 N  N   B PHE   A 132 ? 0.2034 0.1696 0.1649 0.0229  -0.0282 -0.0093 132 PHE   A N   
2856 C  CA  A PHE   A 132 ? 0.1764 0.1384 0.1640 0.0003  -0.0304 0.0194  132 PHE   A CA  
2857 C  CA  B PHE   A 132 ? 0.2055 0.1811 0.1613 0.0238  -0.0201 -0.0114 132 PHE   A CA  
2858 C  C   A PHE   A 132 ? 0.1833 0.1479 0.1714 0.0023  -0.0304 0.0199  132 PHE   A C   
2859 C  C   B PHE   A 132 ? 0.2132 0.1961 0.1660 0.0209  -0.0293 -0.0050 132 PHE   A C   
2860 O  O   A PHE   A 132 ? 0.1976 0.1480 0.1777 -0.0005 -0.0265 0.0181  132 PHE   A O   
2861 O  O   B PHE   A 132 ? 0.2252 0.1996 0.1686 0.0190  -0.0280 -0.0079 132 PHE   A O   
2862 C  CB  A PHE   A 132 ? 0.1663 0.1340 0.1514 -0.0032 -0.0272 0.0297  132 PHE   A CB  
2863 C  CB  B PHE   A 132 ? 0.1964 0.1760 0.1537 0.0281  -0.0096 -0.0105 132 PHE   A CB  
2864 C  CG  A PHE   A 132 ? 0.1654 0.1376 0.1387 -0.0041 -0.0274 0.0227  132 PHE   A CG  
2865 C  CG  B PHE   A 132 ? 0.1882 0.1767 0.1347 0.0271  -0.0058 -0.0013 132 PHE   A CG  
2866 C  CD1 A PHE   A 132 ? 0.1662 0.1482 0.1571 0.0034  -0.0199 0.0043  132 PHE   A CD1 
2867 C  CD1 B PHE   A 132 ? 0.1850 0.1813 0.1436 0.0275  -0.0041 -0.0012 132 PHE   A CD1 
2868 C  CD2 A PHE   A 132 ? 0.1688 0.1529 0.1659 -0.0041 -0.0307 0.0075  132 PHE   A CD2 
2869 C  CD2 B PHE   A 132 ? 0.1865 0.1801 0.1342 0.0249  -0.0009 -0.0077 132 PHE   A CD2 
2870 C  CE1 A PHE   A 132 ? 0.1631 0.1562 0.1454 0.0035  -0.0175 -0.0106 132 PHE   A CE1 
2871 C  CE1 B PHE   A 132 ? 0.1809 0.1838 0.1378 0.0290  -0.0007 0.0002  132 PHE   A CE1 
2872 C  CE2 A PHE   A 132 ? 0.1655 0.1631 0.1777 0.0024  -0.0303 -0.0004 132 PHE   A CE2 
2873 C  CE2 B PHE   A 132 ? 0.1795 0.1819 0.1263 0.0314  0.0054  0.0059  132 PHE   A CE2 
2874 C  CZ  A PHE   A 132 ? 0.1617 0.1626 0.1634 -0.0014 -0.0298 -0.0064 132 PHE   A CZ  
2875 C  CZ  B PHE   A 132 ? 0.1771 0.1832 0.1195 0.0301  0.0052  0.0054  132 PHE   A CZ  
2894 N  N   A GLY   A 133 ? 0.1806 0.1537 0.1765 0.0041  -0.0404 0.0140  133 GLY   A N   
2895 N  N   B GLY   A 133 ? 0.2111 0.2057 0.1649 0.0149  -0.0440 0.0010  133 GLY   A N   
2896 C  CA  A GLY   A 133 ? 0.1849 0.1650 0.1812 0.0081  -0.0442 0.0003  133 GLY   A CA  
2897 C  CA  B GLY   A 133 ? 0.2130 0.2187 0.1615 0.0067  -0.0489 0.0003  133 GLY   A CA  
2898 C  C   A GLY   A 133 ? 0.1815 0.1723 0.1779 0.0045  -0.0389 -0.0132 133 GLY   A C   
2899 C  C   B GLY   A 133 ? 0.2099 0.2305 0.1423 -0.0053 -0.0543 -0.0016 133 GLY   A C   
2900 O  O   A GLY   A 133 ? 0.1911 0.1921 0.1882 -0.0002 -0.0299 -0.0238 133 GLY   A O   
2901 O  O   B GLY   A 133 ? 0.2127 0.2352 0.1320 -0.0139 -0.0421 -0.0149 133 GLY   A O   
2908 N  N   A ALA   A 134 ? 0.1704 0.1590 0.1781 0.0024  -0.0247 -0.0117 134 ALA   A N   
2909 N  N   B ALA   A 134 ? 0.2099 0.2390 0.1476 -0.0076 -0.0520 0.0083  134 ALA   A N   
2910 C  CA  A ALA   A 134 ? 0.1622 0.1566 0.1925 0.0002  -0.0134 -0.0096 134 ALA   A CA  
2911 C  CA  B ALA   A 134 ? 0.2122 0.2510 0.1681 -0.0092 -0.0479 0.0155  134 ALA   A CA  
2912 C  C   A ALA   A 134 ? 0.1661 0.1655 0.1822 0.0046  -0.0160 -0.0001 134 ALA   A C   
2913 C  C   B ALA   A 134 ? 0.2163 0.2648 0.1772 -0.0102 -0.0575 0.0302  134 ALA   A C   
2914 O  O   A ALA   A 134 ? 0.1768 0.1707 0.1826 0.0087  0.0032  -0.0044 134 ALA   A O   
2915 O  O   B ALA   A 134 ? 0.2289 0.2687 0.1834 -0.0084 -0.0568 0.0268  134 ALA   A O   
2916 C  CB  A ALA   A 134 ? 0.1603 0.1484 0.2176 -0.0070 -0.0138 -0.0091 134 ALA   A CB  
2917 C  CB  B ALA   A 134 ? 0.2162 0.2486 0.1816 -0.0098 -0.0352 0.0148  134 ALA   A CB  
2928 N  N   A ASP   A 135 ? 0.1672 0.1743 0.1770 -0.0059 -0.0179 0.0159  135 ASP   A N   
2929 N  N   B ASP   A 135 ? 0.2141 0.2763 0.2046 -0.0120 -0.0538 0.0428  135 ASP   A N   
2930 C  CA  A ASP   A 135 ? 0.1637 0.1858 0.1903 -0.0168 -0.0322 0.0266  135 ASP   A CA  
2931 C  CA  B ASP   A 135 ? 0.2151 0.2895 0.2289 -0.0172 -0.0641 0.0561  135 ASP   A CA  
2932 C  C   A ASP   A 135 ? 0.1542 0.1751 0.1817 -0.0127 -0.0289 0.0359  135 ASP   A C   
2933 C  C   B ASP   A 135 ? 0.2035 0.2756 0.2071 -0.0120 -0.0499 0.0531  135 ASP   A C   
2934 O  O   A ASP   A 135 ? 0.1599 0.1613 0.1900 -0.0167 -0.0296 0.0408  135 ASP   A O   
2935 O  O   B ASP   A 135 ? 0.2021 0.2665 0.2025 -0.0120 -0.0424 0.0585  135 ASP   A O   
2936 C  CB  A ASP   A 135 ? 0.1780 0.2127 0.2091 -0.0361 -0.0554 0.0265  135 ASP   A CB  
2937 C  CB  B ASP   A 135 ? 0.2306 0.3169 0.2799 -0.0298 -0.0835 0.0696  135 ASP   A CB  
2938 C  CG  A ASP   A 135 ? 0.1908 0.2391 0.2424 -0.0503 -0.0587 0.0423  135 ASP   A CG  
2939 C  CG  B ASP   A 135 ? 0.2419 0.3383 0.3274 -0.0413 -0.1055 0.0839  135 ASP   A CG  
2940 O  OD1 A ASP   A 135 ? 0.1841 0.2508 0.2605 -0.0569 -0.0657 0.0558  135 ASP   A OD1 
2941 O  OD1 B ASP   A 135 ? 0.2343 0.3454 0.3371 -0.0463 -0.1246 0.0987  135 ASP   A OD1 
2942 O  OD2 A ASP   A 135 ? 0.2202 0.2572 0.2787 -0.0472 -0.0491 0.0501  135 ASP   A OD2 
2943 O  OD2 B ASP   A 135 ? 0.2586 0.3494 0.3577 -0.0420 -0.1059 0.0829  135 ASP   A OD2 
2952 N  N   A PRO   A 136 ? 0.1437 0.1729 0.1743 0.0038  -0.0260 0.0376  136 PRO   A N   
2953 N  N   B PRO   A 136 ? 0.1937 0.2673 0.1971 -0.0043 -0.0381 0.0447  136 PRO   A N   
2954 C  CA  A PRO   A 136 ? 0.1376 0.1757 0.1818 -0.0013 -0.0164 0.0281  136 PRO   A CA  
2955 C  CA  B PRO   A 136 ? 0.1849 0.2629 0.1974 -0.0063 -0.0280 0.0399  136 PRO   A CA  
2956 C  C   A PRO   A 136 ? 0.1194 0.1742 0.1837 -0.0014 -0.0119 0.0272  136 PRO   A C   
2957 C  C   B PRO   A 136 ? 0.1712 0.2567 0.2119 -0.0034 -0.0263 0.0408  136 PRO   A C   
2958 O  O   A PRO   A 136 ? 0.1143 0.1578 0.1630 -0.0034 0.0058  0.0294  136 PRO   A O   
2959 O  O   B PRO   A 136 ? 0.1665 0.2553 0.2072 0.0006  -0.0271 0.0453  136 PRO   A O   
2960 C  CB  A PRO   A 136 ? 0.1560 0.1752 0.1900 0.0056  -0.0156 0.0259  136 PRO   A CB  
2961 C  CB  B PRO   A 136 ? 0.1958 0.2646 0.1949 -0.0033 -0.0258 0.0374  136 PRO   A CB  
2962 C  CG  A PRO   A 136 ? 0.1666 0.1807 0.2060 0.0105  -0.0132 0.0218  136 PRO   A CG  
2963 C  CG  B PRO   A 136 ? 0.2012 0.2663 0.1978 0.0007  -0.0374 0.0314  136 PRO   A CG  
2964 C  CD  A PRO   A 136 ? 0.1531 0.1740 0.1875 0.0107  -0.0177 0.0443  136 PRO   A CD  
2965 C  CD  B PRO   A 136 ? 0.1990 0.2659 0.2033 0.0009  -0.0376 0.0354  136 PRO   A CD  
2980 N  N   A ILE   A 137 ? 0.1193 0.1831 0.2053 -0.0028 -0.0314 0.0305  137 ILE   A N   
2981 N  N   B ILE   A 137 ? 0.1720 0.2547 0.2284 -0.0090 -0.0357 0.0403  137 ILE   A N   
2982 C  CA  A ILE   A 137 ? 0.1267 0.1984 0.2143 -0.0117 -0.0321 0.0340  137 ILE   A CA  
2983 C  CA  B ILE   A 137 ? 0.1796 0.2562 0.2497 -0.0165 -0.0426 0.0392  137 ILE   A CA  
2984 C  C   A ILE   A 137 ? 0.1342 0.1925 0.2101 -0.0155 -0.0243 0.0435  137 ILE   A C   
2985 C  C   B ILE   A 137 ? 0.1732 0.2499 0.2477 -0.0171 -0.0436 0.0402  137 ILE   A C   
2986 O  O   A ILE   A 137 ? 0.1376 0.1860 0.2064 -0.0263 -0.0285 0.0393  137 ILE   A O   
2987 O  O   B ILE   A 137 ? 0.1727 0.2408 0.2444 -0.0278 -0.0412 0.0289  137 ILE   A O   
2988 C  CB  A ILE   A 137 ? 0.1304 0.2233 0.2157 -0.0171 -0.0408 0.0386  137 ILE   A CB  
2989 C  CB  B ILE   A 137 ? 0.1975 0.2666 0.2739 -0.0186 -0.0439 0.0345  137 ILE   A CB  
2990 C  CG1 A ILE   A 137 ? 0.1377 0.2463 0.2098 -0.0144 -0.0365 0.0514  137 ILE   A CG1 
2991 C  CG1 B ILE   A 137 ? 0.2177 0.2797 0.2722 -0.0022 -0.0503 0.0330  137 ILE   A CG1 
2992 C  CG2 A ILE   A 137 ? 0.1380 0.2299 0.2448 -0.0206 -0.0470 0.0367  137 ILE   A CG2 
2993 C  CG2 B ILE   A 137 ? 0.2022 0.2667 0.2939 -0.0319 -0.0362 0.0345  137 ILE   A CG2 
2994 C  CD1 A ILE   A 137 ? 0.1495 0.2635 0.2219 -0.0071 -0.0253 0.0531  137 ILE   A CD1 
2995 C  CD1 B ILE   A 137 ? 0.2308 0.2863 0.2735 0.0063  -0.0472 0.0325  137 ILE   A CD1 
3018 N  N   A HIS   A 138 ? 0.1359 0.2012 0.2127 -0.0175 0.0038  0.0417  138 HIS   A N   
3019 N  N   B HIS   A 138 ? 0.1673 0.2534 0.2506 -0.0105 -0.0359 0.0424  138 HIS   A N   
3020 C  CA  A HIS   A 138 ? 0.1423 0.2018 0.2129 -0.0133 -0.0046 0.0357  138 HIS   A CA  
3021 C  CA  B HIS   A 138 ? 0.1623 0.2500 0.2372 -0.0104 -0.0372 0.0451  138 HIS   A CA  
3022 C  C   A HIS   A 138 ? 0.1377 0.2025 0.2139 -0.0155 -0.0090 0.0516  138 HIS   A C   
3023 C  C   B HIS   A 138 ? 0.1433 0.2290 0.2241 -0.0095 -0.0359 0.0540  138 HIS   A C   
3024 O  O   A HIS   A 138 ? 0.1441 0.2020 0.2238 -0.0207 -0.0022 0.0430  138 HIS   A O   
3025 O  O   B HIS   A 138 ? 0.1449 0.2294 0.2201 -0.0102 -0.0324 0.0516  138 HIS   A O   
3026 C  CB  A HIS   A 138 ? 0.1524 0.2014 0.1980 -0.0126 -0.0104 0.0174  138 HIS   A CB  
3027 C  CB  B HIS   A 138 ? 0.1906 0.2643 0.2327 -0.0158 -0.0434 0.0395  138 HIS   A CB  
3028 C  CG  A HIS   A 138 ? 0.1695 0.1953 0.2054 -0.0161 -0.0165 0.0025  138 HIS   A CG  
3029 C  CG  B HIS   A 138 ? 0.2147 0.2701 0.2484 -0.0192 -0.0406 0.0290  138 HIS   A CG  
3030 N  ND1 A HIS   A 138 ? 0.1823 0.1984 0.2287 -0.0216 -0.0206 -0.0105 138 HIS   A ND1 
3031 N  ND1 B HIS   A 138 ? 0.2273 0.2748 0.2676 -0.0224 -0.0386 0.0242  138 HIS   A ND1 
3032 C  CD2 A HIS   A 138 ? 0.1684 0.1843 0.1913 -0.0114 -0.0167 0.0012  138 HIS   A CD2 
3033 C  CD2 B HIS   A 138 ? 0.2223 0.2741 0.2527 -0.0171 -0.0418 0.0271  138 HIS   A CD2 
3034 C  CE1 A HIS   A 138 ? 0.1844 0.1943 0.2173 -0.0169 -0.0230 -0.0139 138 HIS   A CE1 
3035 C  CE1 B HIS   A 138 ? 0.2329 0.2749 0.2703 -0.0211 -0.0427 0.0201  138 HIS   A CE1 
3036 N  NE2 A HIS   A 138 ? 0.1780 0.1869 0.1895 -0.0120 -0.0159 -0.0085 138 HIS   A NE2 
3037 N  NE2 B HIS   A 138 ? 0.2281 0.2742 0.2531 -0.0158 -0.0426 0.0209  138 HIS   A NE2 
3052 N  N   . SER   A 139 ? 0.1331 0.2045 0.2261 -0.0123 -0.0145 0.0631  139 SER   A N   
3053 C  CA  . SER   A 139 ? 0.1284 0.1950 0.2222 -0.0111 -0.0083 0.0590  139 SER   A CA  
3054 C  C   . SER   A 139 ? 0.1240 0.1783 0.2181 -0.0101 -0.0054 0.0536  139 SER   A C   
3055 O  O   . SER   A 139 ? 0.1206 0.1752 0.2253 -0.0091 -0.0017 0.0568  139 SER   A O   
3056 C  CB  . SER   A 139 ? 0.1260 0.1893 0.2290 -0.0102 -0.0091 0.0610  139 SER   A CB  
3057 O  OG  . SER   A 139 ? 0.1367 0.1874 0.2281 -0.0153 -0.0214 0.0694  139 SER   A OG  
3064 N  N   . LEU   A 140 ? 0.1298 0.1818 0.2119 -0.0064 -0.0150 0.0589  140 LEU   A N   
3065 C  CA  . LEU   A 140 ? 0.1259 0.1693 0.2126 -0.0076 -0.0025 0.0558  140 LEU   A CA  
3066 C  C   . LEU   A 140 ? 0.1182 0.1805 0.2117 -0.0120 -0.0067 0.0498  140 LEU   A C   
3067 O  O   . LEU   A 140 ? 0.1285 0.1755 0.2190 -0.0024 -0.0049 0.0468  140 LEU   A O   
3068 C  CB  . LEU   A 140 ? 0.1279 0.1764 0.2140 -0.0091 -0.0080 0.0449  140 LEU   A CB  
3069 C  CG  . LEU   A 140 ? 0.1269 0.1828 0.2185 -0.0202 0.0007  0.0563  140 LEU   A CG  
3070 C  CD1 . LEU   A 140 ? 0.1277 0.1801 0.2209 -0.0172 -0.0070 0.0483  140 LEU   A CD1 
3071 C  CD2 . LEU   A 140 ? 0.1413 0.1993 0.2262 -0.0194 0.0097  0.0565  140 LEU   A CD2 
3083 N  N   . ARG   A 141 ? 0.1291 0.1935 0.2215 -0.0144 -0.0074 0.0457  141 ARG   A N   
3084 C  CA  . ARG   A 141 ? 0.1421 0.2104 0.2283 -0.0271 -0.0240 0.0259  141 ARG   A CA  
3085 C  C   . ARG   A 141 ? 0.1418 0.1837 0.2114 -0.0214 -0.0220 0.0250  141 ARG   A C   
3086 O  O   . ARG   A 141 ? 0.1430 0.1763 0.2170 -0.0230 -0.0019 0.0151  141 ARG   A O   
3087 C  CB  . ARG   A 141 ? 0.1622 0.2444 0.2698 -0.0414 -0.0319 0.0080  141 ARG   A CB  
3088 C  CG  . ARG   A 141 ? 0.1974 0.2839 0.3058 -0.0419 -0.0170 0.0043  141 ARG   A CG  
3089 C  CD  . ARG   A 141 ? 0.2245 0.3150 0.3387 -0.0498 -0.0097 -0.0045 141 ARG   A CD  
3090 N  NE  . ARG   A 141 ? 0.2198 0.3407 0.3505 -0.0577 -0.0219 -0.0042 141 ARG   A NE  
3091 C  CZ  . ARG   A 141 ? 0.2197 0.3564 0.3582 -0.0758 -0.0156 -0.0025 141 ARG   A CZ  
3092 N  NH1 . ARG   A 141 ? 0.2065 0.3581 0.3572 -0.0882 0.0097  -0.0166 141 ARG   A NH1 
3093 N  NH2 . ARG   A 141 ? 0.2249 0.3658 0.3707 -0.0736 -0.0288 0.0055  141 ARG   A NH2 
3107 N  N   . VAL   A 142 ? 0.1338 0.1736 0.2087 -0.0142 -0.0121 0.0217  142 VAL   A N   
3108 C  CA  . VAL   A 142 ? 0.1350 0.1692 0.2064 -0.0126 0.0045  0.0277  142 VAL   A CA  
3109 C  C   . VAL   A 142 ? 0.1181 0.1630 0.2006 -0.0154 0.0042  0.0251  142 VAL   A C   
3110 O  O   . VAL   A 142 ? 0.1237 0.1640 0.2002 -0.0038 0.0059  0.0259  142 VAL   A O   
3111 C  CB  . VAL   A 142 ? 0.1470 0.1777 0.1850 -0.0145 0.0075  0.0285  142 VAL   A CB  
3112 C  CG1 . VAL   A 142 ? 0.1381 0.1674 0.1932 -0.0180 0.0058  0.0184  142 VAL   A CG1 
3113 C  CG2 . VAL   A 142 ? 0.1634 0.1967 0.2024 -0.0113 0.0017  0.0299  142 VAL   A CG2 
3123 N  N   . CYS   A 143 ? 0.1271 0.1569 0.1993 -0.0130 -0.0015 0.0260  143 CYS   A N   
3124 C  CA  . CYS   A 143 ? 0.1269 0.1525 0.2008 -0.0147 0.0039  0.0289  143 CYS   A CA  
3125 C  C   . CYS   A 143 ? 0.1224 0.1488 0.2060 -0.0132 0.0030  0.0325  143 CYS   A C   
3126 O  O   . CYS   A 143 ? 0.1216 0.1493 0.2000 -0.0052 0.0016  0.0368  143 CYS   A O   
3127 C  CB  . CYS   A 143 ? 0.1392 0.1503 0.2046 -0.0053 0.0110  0.0392  143 CYS   A CB  
3128 S  SG  . CYS   A 143 ? 0.1496 0.1578 0.1969 0.0060  0.0119  0.0256  143 CYS   A SG  
3134 N  N   . VAL   A 144 ? 0.1228 0.1586 0.2181 -0.0110 0.0061  0.0408  144 VAL   A N   
3135 C  CA  . VAL   A 144 ? 0.1275 0.1660 0.2545 -0.0162 0.0147  0.0304  144 VAL   A CA  
3136 C  C   . VAL   A 144 ? 0.1331 0.1552 0.2321 -0.0201 -0.0090 0.0284  144 VAL   A C   
3137 O  O   . VAL   A 144 ? 0.1507 0.1511 0.2413 -0.0097 -0.0052 0.0313  144 VAL   A O   
3138 C  CB  . VAL   A 144 ? 0.1532 0.1852 0.3121 -0.0062 0.0360  0.0366  144 VAL   A CB  
3139 C  CG1 . VAL   A 144 ? 0.1672 0.2071 0.3434 -0.0176 0.0257  0.0356  144 VAL   A CG1 
3140 C  CG2 . VAL   A 144 ? 0.1370 0.1870 0.3271 -0.0075 0.0481  0.0546  144 VAL   A CG2 
3150 N  N   . ASP   A 145 ? 0.1357 0.1526 0.2380 -0.0200 -0.0051 0.0269  145 ASP   A N   
3151 C  CA  . ASP   A 145 ? 0.1502 0.1550 0.2471 -0.0229 -0.0067 0.0140  145 ASP   A CA  
3152 C  C   . ASP   A 145 ? 0.1524 0.1432 0.2499 -0.0154 -0.0040 0.0024  145 ASP   A C   
3153 O  O   . ASP   A 145 ? 0.1670 0.1507 0.3109 -0.0213 -0.0003 -0.0304 145 ASP   A O   
3154 C  CB  . ASP   A 145 ? 0.1607 0.1921 0.2717 -0.0313 -0.0213 0.0108  145 ASP   A CB  
3155 C  CG  . ASP   A 145 ? 0.1802 0.2319 0.3082 -0.0552 -0.0316 0.0203  145 ASP   A CG  
3156 O  OD1 . ASP   A 145 ? 0.1728 0.2442 0.3261 -0.0652 -0.0214 0.0226  145 ASP   A OD1 
3157 O  OD2 . ASP   A 145 ? 0.2010 0.2584 0.3194 -0.0662 -0.0562 0.0228  145 ASP   A OD2 
3162 N  N   . THR   A 146 ? 0.1365 0.1331 0.2025 -0.0134 0.0035  0.0184  146 THR   A N   
3163 C  CA  . THR   A 146 ? 0.1291 0.1354 0.1929 -0.0087 -0.0013 0.0139  146 THR   A CA  
3164 C  C   . THR   A 146 ? 0.1268 0.1324 0.1928 -0.0043 0.0090  0.0185  146 THR   A C   
3165 O  O   . THR   A 146 ? 0.1340 0.1414 0.2136 0.0052  -0.0001 0.0157  146 THR   A O   
3166 C  CB  . THR   A 146 ? 0.1292 0.1384 0.1890 -0.0039 0.0028  0.0226  146 THR   A CB  
3167 O  OG1 . THR   A 146 ? 0.1305 0.1550 0.1994 -0.0026 -0.0005 0.0105  146 THR   A OG1 
3168 C  CG2 . THR   A 146 ? 0.1253 0.1359 0.2201 -0.0070 0.0002  0.0229  146 THR   A CG2 
3176 N  N   . VAL   A 147 ? 0.1222 0.1384 0.1806 -0.0022 0.0150  0.0213  147 VAL   A N   
3177 C  CA  . VAL   A 147 ? 0.1209 0.1416 0.1824 -0.0101 0.0218  0.0239  147 VAL   A CA  
3178 C  C   . VAL   A 147 ? 0.1274 0.1365 0.2071 -0.0145 0.0158  0.0275  147 VAL   A C   
3179 O  O   . VAL   A 147 ? 0.1316 0.1399 0.2243 -0.0142 0.0080  0.0288  147 VAL   A O   
3180 C  CB  . VAL   A 147 ? 0.1348 0.1384 0.1815 -0.0074 0.0160  0.0262  147 VAL   A CB  
3181 C  CG1 . VAL   A 147 ? 0.1698 0.1484 0.1757 -0.0077 0.0156  0.0328  147 VAL   A CG1 
3182 C  CG2 . VAL   A 147 ? 0.1389 0.1402 0.1783 -0.0151 0.0100  0.0173  147 VAL   A CG2 
3192 N  N   . ARG   A 148 ? 0.1248 0.1342 0.2144 -0.0159 0.0151  0.0424  148 ARG   A N   
3193 C  CA  . ARG   A 148 ? 0.1332 0.1363 0.2069 -0.0144 0.0040  0.0434  148 ARG   A CA  
3194 C  C   . ARG   A 148 ? 0.1398 0.1341 0.2139 -0.0171 0.0057  0.0606  148 ARG   A C   
3195 O  O   . ARG   A 148 ? 0.1722 0.1498 0.2272 -0.0218 0.0189  0.0489  148 ARG   A O   
3196 C  CB  . ARG   A 148 ? 0.1393 0.1393 0.2220 -0.0065 0.0155  0.0398  148 ARG   A CB  
3197 C  CG  . ARG   A 148 ? 0.1532 0.1381 0.2625 -0.0067 0.0304  0.0302  148 ARG   A CG  
3198 C  CD  . ARG   A 148 ? 0.1697 0.1334 0.2770 -0.0094 0.0437  0.0468  148 ARG   A CD  
3199 N  NE  . ARG   A 148 ? 0.1634 0.1408 0.2676 0.0042  0.0448  0.0461  148 ARG   A NE  
3200 C  CZ  . ARG   A 148 ? 0.1627 0.1346 0.2488 0.0031  0.0431  0.0423  148 ARG   A CZ  
3201 N  NH1 . ARG   A 148 ? 0.1701 0.1363 0.2529 -0.0102 0.0415  0.0240  148 ARG   A NH1 
3202 N  NH2 . ARG   A 148 ? 0.1591 0.1533 0.2601 0.0072  0.0360  0.0462  148 ARG   A NH2 
3216 N  N   . THR   A 149 ? 0.1401 0.1480 0.2064 -0.0150 -0.0024 0.0517  149 THR   A N   
3217 C  CA  . THR   A 149 ? 0.1415 0.1532 0.1998 -0.0120 0.0028  0.0502  149 THR   A CA  
3218 C  C   . THR   A 149 ? 0.1371 0.1514 0.1784 -0.0197 0.0089  0.0563  149 THR   A C   
3219 O  O   . THR   A 149 ? 0.1382 0.1595 0.2023 -0.0175 0.0085  0.0499  149 THR   A O   
3220 C  CB  . THR   A 149 ? 0.1433 0.1649 0.1958 -0.0138 0.0038  0.0425  149 THR   A CB  
3221 O  OG1 . THR   A 149 ? 0.1433 0.1576 0.2055 -0.0232 0.0041  0.0386  149 THR   A OG1 
3222 C  CG2 . THR   A 149 ? 0.1401 0.1796 0.1986 -0.0042 -0.0009 0.0492  149 THR   A CG2 
3230 N  N   . ASN   A 150 ? 0.1401 0.1583 0.1927 -0.0076 0.0042  0.0564  150 ASN   A N   
3231 C  CA  . ASN   A 150 ? 0.1497 0.1658 0.1905 -0.0076 0.0184  0.0514  150 ASN   A CA  
3232 C  C   . ASN   A 150 ? 0.1337 0.1527 0.1885 -0.0106 0.0064  0.0521  150 ASN   A C   
3233 O  O   . ASN   A 150 ? 0.1450 0.1629 0.2222 -0.0117 -0.0097 0.0416  150 ASN   A O   
3234 C  CB  . ASN   A 150 ? 0.1984 0.1938 0.2231 -0.0100 0.0382  0.0780  150 ASN   A CB  
3235 C  CG  . ASN   A 150 ? 0.2545 0.2307 0.2968 -0.0056 0.0170  0.0832  150 ASN   A CG  
3236 O  OD1 . ASN   A 150 ? 0.2745 0.2347 0.3108 -0.0103 0.0194  0.0989  150 ASN   A OD1 
3237 N  ND2 . ASN   A 150 ? 0.2833 0.2567 0.3263 -0.0030 0.0035  0.0866  150 ASN   A ND2 
3244 N  N   . VAL   A 151 ? 0.1346 0.1451 0.1949 -0.0129 0.0042  0.0476  151 VAL   A N   
3245 C  CA  . VAL   A 151 ? 0.1444 0.1463 0.1861 -0.0178 0.0020  0.0443  151 VAL   A CA  
3246 C  C   . VAL   A 151 ? 0.1366 0.1398 0.1875 -0.0280 0.0099  0.0542  151 VAL   A C   
3247 O  O   . VAL   A 151 ? 0.1407 0.1481 0.2379 -0.0171 0.0099  0.0422  151 VAL   A O   
3248 C  CB  . VAL   A 151 ? 0.1689 0.1591 0.1900 -0.0052 0.0077  0.0412  151 VAL   A CB  
3249 C  CG1 . VAL   A 151 ? 0.1663 0.1772 0.2172 -0.0081 0.0079  0.0422  151 VAL   A CG1 
3250 C  CG2 . VAL   A 151 ? 0.1778 0.1551 0.1910 -0.0038 0.0225  0.0324  151 VAL   A CG2 
3260 N  N   A TYR   A 152 ? 0.1286 0.1420 0.1937 -0.0255 0.0094  0.0490  152 TYR   A N   
3261 N  N   B TYR   A 152 ? 0.1317 0.1433 0.1815 -0.0227 -0.0008 0.0458  152 TYR   A N   
3262 C  CA  A TYR   A 152 ? 0.1325 0.1469 0.1857 -0.0217 0.0210  0.0523  152 TYR   A CA  
3263 C  CA  B TYR   A 152 ? 0.1358 0.1480 0.1608 -0.0171 -0.0015 0.0431  152 TYR   A CA  
3264 C  C   A TYR   A 152 ? 0.1275 0.1358 0.1786 -0.0168 0.0284  0.0440  152 TYR   A C   
3265 C  C   B TYR   A 152 ? 0.1341 0.1474 0.1477 -0.0133 -0.0009 0.0428  152 TYR   A C   
3266 O  O   A TYR   A 152 ? 0.1353 0.1308 0.1738 -0.0236 0.0252  0.0327  152 TYR   A O   
3267 O  O   B TYR   A 152 ? 0.1390 0.1453 0.1650 -0.0161 -0.0005 0.0422  152 TYR   A O   
3268 C  CB  A TYR   A 152 ? 0.1503 0.1606 0.1935 -0.0162 0.0236  0.0594  152 TYR   A CB  
3269 C  CB  B TYR   A 152 ? 0.1506 0.1534 0.1718 -0.0063 0.0057  0.0428  152 TYR   A CB  
3270 C  CG  A TYR   A 152 ? 0.1590 0.1800 0.1927 -0.0227 0.0273  0.0529  152 TYR   A CG  
3271 C  CG  B TYR   A 152 ? 0.1645 0.1643 0.1742 -0.0126 0.0283  0.0370  152 TYR   A CG  
3272 C  CD1 A TYR   A 152 ? 0.1639 0.1928 0.1992 -0.0211 0.0200  0.0468  152 TYR   A CD1 
3273 C  CD1 B TYR   A 152 ? 0.1723 0.1687 0.1862 -0.0116 0.0373  0.0406  152 TYR   A CD1 
3274 C  CD2 A TYR   A 152 ? 0.1642 0.1940 0.1908 -0.0267 0.0272  0.0486  152 TYR   A CD2 
3275 C  CD2 B TYR   A 152 ? 0.1691 0.1723 0.1604 -0.0233 0.0301  0.0348  152 TYR   A CD2 
3276 C  CE1 A TYR   A 152 ? 0.1756 0.2084 0.2118 -0.0204 0.0145  0.0596  152 TYR   A CE1 
3277 C  CE1 B TYR   A 152 ? 0.1907 0.1728 0.1847 -0.0167 0.0219  0.0425  152 TYR   A CE1 
3278 C  CE2 A TYR   A 152 ? 0.1799 0.2119 0.2005 -0.0245 0.0305  0.0574  152 TYR   A CE2 
3279 C  CE2 B TYR   A 152 ? 0.1878 0.1852 0.1710 -0.0260 0.0324  0.0403  152 TYR   A CE2 
3280 C  CZ  A TYR   A 152 ? 0.1882 0.2200 0.2087 -0.0184 0.0181  0.0738  152 TYR   A CZ  
3281 C  CZ  B TYR   A 152 ? 0.2003 0.1837 0.1684 -0.0274 0.0208  0.0494  152 TYR   A CZ  
3282 O  OH  A TYR   A 152 ? 0.2028 0.2405 0.2494 -0.0104 0.0135  0.0906  152 TYR   A OH  
3283 O  OH  B TYR   A 152 ? 0.2188 0.2016 0.1883 -0.0336 0.0186  0.0557  152 TYR   A OH  
3302 N  N   A LEU   A 153 ? 0.1181 0.1315 0.1872 -0.0138 0.0264  0.0374  153 LEU   A N   
3303 N  N   B LEU   A 153 ? 0.1320 0.1470 0.1535 -0.0159 0.0018  0.0360  153 LEU   A N   
3304 C  CA  A LEU   A 153 ? 0.1187 0.1262 0.1937 -0.0098 0.0169  0.0349  153 LEU   A CA  
3305 C  CA  B LEU   A 153 ? 0.1304 0.1392 0.1555 -0.0069 0.0091  0.0274  153 LEU   A CA  
3306 C  C   A LEU   A 153 ? 0.1204 0.1240 0.1859 -0.0043 0.0163  0.0317  153 LEU   A C   
3307 C  C   B LEU   A 153 ? 0.1347 0.1454 0.1586 -0.0053 0.0225  0.0269  153 LEU   A C   
3308 O  O   A LEU   A 153 ? 0.1278 0.1302 0.2242 -0.0065 0.0310  0.0230  153 LEU   A O   
3309 O  O   B LEU   A 153 ? 0.1368 0.1546 0.1705 -0.0081 0.0354  0.0247  153 LEU   A O   
3310 C  CB  A LEU   A 153 ? 0.1132 0.1230 0.2084 -0.0186 0.0076  0.0253  153 LEU   A CB  
3311 C  CB  B LEU   A 153 ? 0.1284 0.1385 0.1547 -0.0004 0.0010  0.0274  153 LEU   A CB  
3312 C  CG  A LEU   A 153 ? 0.1209 0.1291 0.2070 -0.0175 0.0119  0.0154  153 LEU   A CG  
3313 C  CG  B LEU   A 153 ? 0.1347 0.1490 0.1479 0.0045  0.0085  0.0279  153 LEU   A CG  
3314 C  CD1 A LEU   A 153 ? 0.1321 0.1236 0.2130 -0.0162 0.0003  0.0089  153 LEU   A CD1 
3315 C  CD1 B LEU   A 153 ? 0.1418 0.1446 0.1579 0.0124  0.0037  0.0295  153 LEU   A CD1 
3316 C  CD2 A LEU   A 153 ? 0.1260 0.1360 0.1878 -0.0226 0.0195  0.0066  153 LEU   A CD2 
3317 C  CD2 B LEU   A 153 ? 0.1393 0.1627 0.1563 -0.0017 0.0054  0.0186  153 LEU   A CD2 
3340 N  N   A ALA   A 154 ? 0.1180 0.1178 0.1795 -0.0001 0.0086  0.0335  154 ALA   A N   
3341 N  N   B ALA   A 154 ? 0.1358 0.1380 0.1563 -0.0052 0.0294  0.0236  154 ALA   A N   
3342 C  CA  A ALA   A 154 ? 0.1347 0.1269 0.1977 0.0108  0.0164  0.0291  154 ALA   A CA  
3343 C  CA  B ALA   A 154 ? 0.1448 0.1417 0.1936 -0.0009 0.0325  0.0209  154 ALA   A CA  
3344 C  C   A ALA   A 154 ? 0.1429 0.1291 0.2203 0.0144  0.0074  0.0392  154 ALA   A C   
3345 C  C   B ALA   A 154 ? 0.1448 0.1467 0.2019 -0.0090 0.0219  0.0354  154 ALA   A C   
3346 O  O   A ALA   A 154 ? 0.1494 0.1327 0.2273 0.0081  0.0092  0.0292  154 ALA   A O   
3347 O  O   B ALA   A 154 ? 0.1472 0.1443 0.1868 -0.0213 0.0213  0.0381  154 ALA   A O   
3348 C  CB  A ALA   A 154 ? 0.1445 0.1246 0.1966 0.0261  0.0240  0.0224  154 ALA   A CB  
3349 C  CB  B ALA   A 154 ? 0.1485 0.1403 0.2038 0.0034  0.0400  0.0063  154 ALA   A CB  
3360 N  N   A VAL   A 155 ? 0.1569 0.1488 0.2400 0.0143  0.0019  0.0668  155 VAL   A N   
3361 N  N   B VAL   A 155 ? 0.1483 0.1557 0.2315 -0.0126 0.0253  0.0538  155 VAL   A N   
3362 C  CA  A VAL   A 155 ? 0.1678 0.1589 0.2620 0.0203  -0.0134 0.0755  155 VAL   A CA  
3363 C  CA  B VAL   A 155 ? 0.1497 0.1567 0.2619 -0.0121 0.0156  0.0572  155 VAL   A CA  
3364 C  C   A VAL   A 155 ? 0.1752 0.1674 0.2881 0.0257  -0.0174 0.0689  155 VAL   A C   
3365 C  C   B VAL   A 155 ? 0.1491 0.1625 0.2733 -0.0074 0.0277  0.0634  155 VAL   A C   
3366 O  O   A VAL   A 155 ? 0.1733 0.1733 0.3065 0.0355  -0.0117 0.0631  155 VAL   A O   
3367 O  O   B VAL   A 155 ? 0.1532 0.1693 0.2918 0.0060  0.0405  0.0637  155 VAL   A O   
3368 C  CB  A VAL   A 155 ? 0.1735 0.1672 0.2609 0.0234  -0.0249 0.0759  155 VAL   A CB  
3369 C  CB  B VAL   A 155 ? 0.1505 0.1551 0.2758 -0.0017 -0.0044 0.0482  155 VAL   A CB  
3370 C  CG1 A VAL   A 155 ? 0.1758 0.1757 0.2682 0.0307  -0.0306 0.0723  155 VAL   A CG1 
3371 C  CG1 B VAL   A 155 ? 0.1535 0.1608 0.2863 0.0103  -0.0110 0.0385  155 VAL   A CG1 
3372 C  CG2 A VAL   A 155 ? 0.1841 0.1735 0.2653 0.0321  -0.0411 0.0766  155 VAL   A CG2 
3373 C  CG2 B VAL   A 155 ? 0.1654 0.1600 0.2846 0.0074  -0.0152 0.0415  155 VAL   A CG2 
3392 N  N   A PHE   A 156 ? 0.1883 0.1666 0.2759 0.0208  -0.0194 0.0660  156 PHE   A N   
3393 N  N   B PHE   A 156 ? 0.1555 0.1638 0.2758 -0.0129 0.0279  0.0667  156 PHE   A N   
3394 C  CA  A PHE   A 156 ? 0.2057 0.1683 0.2780 0.0255  -0.0201 0.0621  156 PHE   A CA  
3395 C  CA  B PHE   A 156 ? 0.1686 0.1681 0.2772 -0.0065 0.0168  0.0607  156 PHE   A CA  
3396 C  C   A PHE   A 156 ? 0.2022 0.1669 0.2721 0.0338  -0.0184 0.0654  156 PHE   A C   
3397 C  C   B PHE   A 156 ? 0.1724 0.1767 0.2750 -0.0034 0.0285  0.0588  156 PHE   A C   
3398 O  O   A PHE   A 156 ? 0.2082 0.1779 0.2819 0.0361  -0.0130 0.0446  156 PHE   A O   
3399 O  O   B PHE   A 156 ? 0.1821 0.1973 0.2863 0.0051  0.0353  0.0545  156 PHE   A O   
3400 C  CB  A PHE   A 156 ? 0.2274 0.1794 0.2852 0.0243  -0.0234 0.0659  156 PHE   A CB  
3401 C  CB  B PHE   A 156 ? 0.1728 0.1605 0.2668 -0.0091 0.0106  0.0699  156 PHE   A CB  
3402 C  CG  A PHE   A 156 ? 0.2499 0.1904 0.3089 0.0310  -0.0248 0.0559  156 PHE   A CG  
3403 C  CG  B PHE   A 156 ? 0.1795 0.1599 0.2645 -0.0047 0.0027  0.0729  156 PHE   A CG  
3404 C  CD1 A PHE   A 156 ? 0.2623 0.1984 0.3213 0.0339  -0.0208 0.0518  156 PHE   A CD1 
3405 C  CD1 B PHE   A 156 ? 0.1788 0.1684 0.2780 0.0016  0.0051  0.0695  156 PHE   A CD1 
3406 C  CD2 A PHE   A 156 ? 0.2618 0.2012 0.3208 0.0410  -0.0315 0.0479  156 PHE   A CD2 
3407 C  CD2 B PHE   A 156 ? 0.1887 0.1638 0.2814 -0.0044 -0.0013 0.0691  156 PHE   A CD2 
3408 C  CE1 A PHE   A 156 ? 0.2737 0.2046 0.3351 0.0361  -0.0172 0.0447  156 PHE   A CE1 
3409 C  CE1 B PHE   A 156 ? 0.1821 0.1738 0.2914 -0.0006 0.0089  0.0527  156 PHE   A CE1 
3410 C  CE2 A PHE   A 156 ? 0.2745 0.2084 0.3316 0.0437  -0.0282 0.0367  156 PHE   A CE2 
3411 C  CE2 B PHE   A 156 ? 0.1960 0.1702 0.3000 -0.0082 -0.0046 0.0556  156 PHE   A CE2 
3412 C  CZ  A PHE   A 156 ? 0.2787 0.2073 0.3353 0.0440  -0.0200 0.0382  156 PHE   A CZ  
3413 C  CZ  B PHE   A 156 ? 0.1874 0.1681 0.3011 -0.0115 0.0057  0.0553  156 PHE   A CZ  
3432 N  N   A ASP   A 157 ? 0.1956 0.1657 0.2654 0.0329  -0.0205 0.0650  157 ASP   A N   
3433 N  N   B ASP   A 157 ? 0.1766 0.1766 0.2849 -0.0170 0.0136  0.0650  157 ASP   A N   
3434 C  CA  A ASP   A 157 ? 0.2000 0.1891 0.2653 0.0306  -0.0292 0.0660  157 ASP   A CA  
3435 C  CA  B ASP   A 157 ? 0.1936 0.1876 0.2899 -0.0220 -0.0054 0.0545  157 ASP   A CA  
3436 C  C   A ASP   A 157 ? 0.1905 0.2029 0.2602 0.0377  -0.0232 0.0748  157 ASP   A C   
3437 C  C   B ASP   A 157 ? 0.1954 0.1952 0.2839 -0.0267 0.0012  0.0640  157 ASP   A C   
3438 O  O   A ASP   A 157 ? 0.1853 0.1947 0.2502 0.0356  -0.0149 0.0815  157 ASP   A O   
3439 O  O   B ASP   A 157 ? 0.1935 0.1920 0.2848 -0.0266 0.0111  0.0707  157 ASP   A O   
3440 C  CB  A ASP   A 157 ? 0.2171 0.1926 0.2772 0.0265  -0.0421 0.0675  157 ASP   A CB  
3441 C  CB  B ASP   A 157 ? 0.2151 0.1871 0.3032 -0.0198 -0.0184 0.0441  157 ASP   A CB  
3442 C  CG  A ASP   A 157 ? 0.2400 0.1982 0.3084 0.0283  -0.0542 0.0668  157 ASP   A CG  
3443 C  CG  B ASP   A 157 ? 0.2371 0.1801 0.3128 -0.0182 -0.0387 0.0331  157 ASP   A CG  
3444 O  OD1 A ASP   A 157 ? 0.2625 0.2100 0.3304 0.0283  -0.0699 0.0561  157 ASP   A OD1 
3445 O  OD1 B ASP   A 157 ? 0.2596 0.1748 0.3266 -0.0203 -0.0596 0.0266  157 ASP   A OD1 
3446 O  OD2 A ASP   A 157 ? 0.2357 0.1890 0.3306 0.0247  -0.0483 0.0660  157 ASP   A OD2 
3447 O  OD2 B ASP   A 157 ? 0.2311 0.1845 0.3111 -0.0184 -0.0369 0.0225  157 ASP   A OD2 
3456 N  N   A LYS   A 158 ? 0.1887 0.2216 0.2692 0.0455  -0.0175 0.0743  158 LYS   A N   
3457 N  N   B LYS   A 158 ? 0.2016 0.2095 0.2876 -0.0321 -0.0025 0.0684  158 LYS   A N   
3458 C  CA  A LYS   A 158 ? 0.1840 0.2400 0.2869 0.0520  -0.0010 0.0618  158 LYS   A CA  
3459 C  CA  B LYS   A 158 ? 0.2143 0.2349 0.3137 -0.0314 0.0016  0.0591  158 LYS   A CA  
3460 C  C   A LYS   A 158 ? 0.1772 0.2465 0.2839 0.0494  0.0013  0.0622  158 LYS   A C   
3461 C  C   B LYS   A 158 ? 0.1912 0.2269 0.3098 -0.0296 -0.0076 0.0577  158 LYS   A C   
3462 O  O   A LYS   A 158 ? 0.1720 0.2557 0.2934 0.0458  0.0188  0.0594  158 LYS   A O   
3463 O  O   B LYS   A 158 ? 0.1813 0.2289 0.3149 -0.0302 0.0007  0.0688  158 LYS   A O   
3464 C  CB  A LYS   A 158 ? 0.1917 0.2442 0.3020 0.0537  0.0251  0.0554  158 LYS   A CB  
3465 C  CB  B LYS   A 158 ? 0.2479 0.2693 0.3491 -0.0309 0.0208  0.0562  158 LYS   A CB  
3466 C  CG  A LYS   A 158 ? 0.2007 0.2492 0.3153 0.0508  0.0423  0.0525  158 LYS   A CG  
3467 C  CG  B LYS   A 158 ? 0.2808 0.2994 0.3970 -0.0266 0.0287  0.0558  158 LYS   A CG  
3468 C  CD  A LYS   A 158 ? 0.2026 0.2508 0.3196 0.0439  0.0644  0.0590  158 LYS   A CD  
3469 C  CD  B LYS   A 158 ? 0.3049 0.3234 0.4300 -0.0237 0.0411  0.0557  158 LYS   A CD  
3470 C  CE  A LYS   A 158 ? 0.1996 0.2508 0.3282 0.0353  0.0829  0.0724  158 LYS   A CE  
3471 C  CE  B LYS   A 158 ? 0.3196 0.3411 0.4536 -0.0219 0.0526  0.0576  158 LYS   A CE  
3472 N  NZ  A LYS   A 158 ? 0.1981 0.2474 0.3316 0.0258  0.0917  0.0876  158 LYS   A NZ  
3473 N  NZ  B LYS   A 158 ? 0.3272 0.3513 0.4694 -0.0208 0.0574  0.0591  158 LYS   A NZ  
3500 N  N   A ASN   A 159 ? 0.1739 0.2432 0.2902 0.0522  -0.0245 0.0629  159 ASN   A N   
3501 N  N   B ASN   A 159 ? 0.1907 0.2282 0.3184 -0.0153 -0.0234 0.0412  159 ASN   A N   
3502 C  CA  A ASN   A 159 ? 0.1800 0.2454 0.3044 0.0477  -0.0346 0.0708  159 ASN   A CA  
3503 C  CA  B ASN   A 159 ? 0.1912 0.2288 0.3252 0.0006  -0.0406 0.0375  159 ASN   A CA  
3504 C  C   A ASN   A 159 ? 0.1726 0.2395 0.2925 0.0424  -0.0109 0.0671  159 ASN   A C   
3505 C  C   B ASN   A 159 ? 0.1712 0.2100 0.3108 -0.0015 -0.0377 0.0427  159 ASN   A C   
3506 O  O   A ASN   A 159 ? 0.1634 0.2418 0.2722 0.0410  -0.0040 0.0445  159 ASN   A O   
3507 O  O   B ASN   A 159 ? 0.1663 0.2174 0.3149 -0.0049 -0.0521 0.0267  159 ASN   A O   
3508 C  CB  A ASN   A 159 ? 0.1939 0.2552 0.3268 0.0436  -0.0397 0.0864  159 ASN   A CB  
3509 C  CB  B ASN   A 159 ? 0.2172 0.2528 0.3488 0.0140  -0.0453 0.0298  159 ASN   A CB  
3510 C  CG  A ASN   A 159 ? 0.2161 0.2729 0.3733 0.0355  -0.0198 0.0819  159 ASN   A CG  
3511 C  CG  B ASN   A 159 ? 0.2427 0.2831 0.3774 0.0170  -0.0429 0.0178  159 ASN   A CG  
3512 O  OD1 A ASN   A 159 ? 0.2248 0.2886 0.3995 0.0337  0.0090  0.0730  159 ASN   A OD1 
3513 O  OD1 B ASN   A 159 ? 0.2514 0.3030 0.4021 0.0166  -0.0339 0.0193  159 ASN   A OD1 
3514 N  ND2 A ASN   A 159 ? 0.2210 0.2759 0.3870 0.0324  -0.0256 0.0776  159 ASN   A ND2 
3515 N  ND2 B ASN   A 159 ? 0.2550 0.2937 0.3919 0.0212  -0.0494 0.0115  159 ASN   A ND2 
3528 N  N   A LEU   A 160 ? 0.1690 0.2274 0.2982 0.0387  -0.0117 0.0833  160 LEU   A N   
3529 N  N   B LEU   A 160 ? 0.1562 0.1925 0.3162 -0.0040 -0.0283 0.0642  160 LEU   A N   
3530 C  CA  A LEU   A 160 ? 0.1704 0.2207 0.2981 0.0267  -0.0076 0.1056  160 LEU   A CA  
3531 C  CA  B LEU   A 160 ? 0.1542 0.1879 0.3208 -0.0071 -0.0154 0.0858  160 LEU   A CA  
3532 C  C   A LEU   A 160 ? 0.1554 0.2232 0.2993 0.0182  -0.0086 0.1273  160 LEU   A C   
3533 C  C   B LEU   A 160 ? 0.1470 0.1952 0.3244 -0.0041 -0.0007 0.0980  160 LEU   A C   
3534 O  O   A LEU   A 160 ? 0.1496 0.2281 0.3212 0.0163  -0.0209 0.1299  160 LEU   A O   
3535 O  O   B LEU   A 160 ? 0.1463 0.1860 0.3444 -0.0098 -0.0094 0.1172  160 LEU   A O   
3536 C  CB  A LEU   A 160 ? 0.1803 0.2159 0.2868 0.0187  0.0051  0.0992  160 LEU   A CB  
3537 C  CB  B LEU   A 160 ? 0.1671 0.1839 0.3124 -0.0196 -0.0142 0.0869  160 LEU   A CB  
3538 C  CG  A LEU   A 160 ? 0.1845 0.2153 0.2816 0.0080  0.0141  0.0756  160 LEU   A CG  
3539 C  CG  B LEU   A 160 ? 0.1716 0.1910 0.3119 -0.0261 -0.0179 0.0806  160 LEU   A CG  
3540 C  CD1 A LEU   A 160 ? 0.1948 0.2233 0.2883 0.0048  0.0150  0.0522  160 LEU   A CD1 
3541 C  CD1 B LEU   A 160 ? 0.1760 0.1969 0.3198 -0.0177 -0.0173 0.0735  160 LEU   A CD1 
3542 C  CD2 A LEU   A 160 ? 0.1832 0.2110 0.2762 0.0115  0.0193  0.0684  160 LEU   A CD2 
3543 C  CD2 B LEU   A 160 ? 0.1818 0.1902 0.3141 -0.0328 -0.0179 0.0777  160 LEU   A CD2 
3566 N  N   A TYR   A 161 ? 0.1530 0.2222 0.3094 0.0095  -0.0007 0.1160  161 TYR   A N   
3567 N  N   B TYR   A 161 ? 0.1428 0.2094 0.3204 -0.0039 0.0108  0.0993  161 TYR   A N   
3568 C  CA  A TYR   A 161 ? 0.1540 0.2179 0.3132 -0.0049 0.0037  0.1148  161 TYR   A CA  
3569 C  CA  B TYR   A 161 ? 0.1417 0.2115 0.3123 -0.0035 0.0237  0.1025  161 TYR   A CA  
3570 C  C   A TYR   A 161 ? 0.1440 0.2279 0.3293 -0.0108 0.0009  0.1169  161 TYR   A C   
3571 C  C   B TYR   A 161 ? 0.1425 0.2379 0.3275 -0.0036 0.0224  0.0994  161 TYR   A C   
3572 O  O   A TYR   A 161 ? 0.1363 0.2321 0.3257 -0.0164 0.0045  0.1202  161 TYR   A O   
3573 O  O   B TYR   A 161 ? 0.1347 0.2428 0.3241 -0.0060 0.0303  0.0919  161 TYR   A O   
3574 C  CB  A TYR   A 161 ? 0.1673 0.2076 0.3298 -0.0089 -0.0016 0.0972  161 TYR   A CB  
3575 C  CB  B TYR   A 161 ? 0.1435 0.1902 0.3222 0.0023  0.0261  0.0883  161 TYR   A CB  
3576 C  CG  A TYR   A 161 ? 0.1720 0.1978 0.3312 -0.0134 -0.0181 0.0777  161 TYR   A CG  
3577 C  CG  B TYR   A 161 ? 0.1380 0.1709 0.3120 0.0048  0.0285  0.0680  161 TYR   A CG  
3578 C  CD1 A TYR   A 161 ? 0.1742 0.1923 0.3304 -0.0159 -0.0227 0.0670  161 TYR   A CD1 
3579 C  CD1 B TYR   A 161 ? 0.1347 0.1643 0.3041 0.0029  0.0326  0.0465  161 TYR   A CD1 
3580 C  CD2 A TYR   A 161 ? 0.1725 0.1961 0.3302 -0.0129 -0.0301 0.0677  161 TYR   A CD2 
3581 C  CD2 B TYR   A 161 ? 0.1374 0.1645 0.3030 0.0098  0.0287  0.0651  161 TYR   A CD2 
3582 C  CE1 A TYR   A 161 ? 0.1772 0.1792 0.3291 -0.0192 -0.0298 0.0673  161 TYR   A CE1 
3583 C  CE1 B TYR   A 161 ? 0.1403 0.1608 0.3036 0.0049  0.0291  0.0403  161 TYR   A CE1 
3584 C  CE2 A TYR   A 161 ? 0.1772 0.1843 0.3264 -0.0138 -0.0362 0.0666  161 TYR   A CE2 
3585 C  CE2 B TYR   A 161 ? 0.1426 0.1605 0.3012 0.0023  0.0325  0.0638  161 TYR   A CE2 
3586 C  CZ  A TYR   A 161 ? 0.1831 0.1708 0.3306 -0.0221 -0.0359 0.0718  161 TYR   A CZ  
3587 C  CZ  B TYR   A 161 ? 0.1548 0.1561 0.3057 -0.0007 0.0291  0.0492  161 TYR   A CZ  
3588 O  OH  A TYR   A 161 ? 0.1933 0.1496 0.3414 -0.0272 -0.0394 0.0838  161 TYR   A OH  
3589 O  OH  B TYR   A 161 ? 0.1774 0.1520 0.3166 -0.0058 0.0110  0.0444  161 TYR   A OH  
3608 N  N   A ASP   A 162 ? 0.1399 0.2351 0.3527 -0.0095 0.0010  0.1174  162 ASP   A N   
3609 N  N   B ASP   A 162 ? 0.1481 0.2595 0.3523 -0.0019 0.0192  0.1021  162 ASP   A N   
3610 C  CA  A ASP   A 162 ? 0.1337 0.2487 0.3549 -0.0136 0.0008  0.1141  162 ASP   A CA  
3611 C  CA  B ASP   A 162 ? 0.1574 0.2843 0.3672 -0.0019 0.0196  0.0979  162 ASP   A CA  
3612 C  C   A ASP   A 162 ? 0.1271 0.2697 0.3456 -0.0224 -0.0031 0.1114  162 ASP   A C   
3613 C  C   B ASP   A 162 ? 0.1652 0.3007 0.3523 -0.0034 0.0195  0.0965  162 ASP   A C   
3614 O  O   A ASP   A 162 ? 0.1243 0.2678 0.3574 -0.0313 -0.0006 0.1072  162 ASP   A O   
3615 O  O   B ASP   A 162 ? 0.1695 0.3039 0.3591 -0.0015 0.0239  0.0916  162 ASP   A O   
3616 C  CB  A ASP   A 162 ? 0.1452 0.2448 0.3672 -0.0097 0.0068  0.1094  162 ASP   A CB  
3617 C  CB  B ASP   A 162 ? 0.1649 0.2918 0.4012 -0.0025 0.0226  0.0947  162 ASP   A CB  
3618 C  CG  A ASP   A 162 ? 0.1619 0.2426 0.3778 -0.0015 0.0158  0.1049  162 ASP   A CG  
3619 C  CG  B ASP   A 162 ? 0.1773 0.3002 0.4303 -0.0008 0.0227  0.0987  162 ASP   A CG  
3620 O  OD1 A ASP   A 162 ? 0.1784 0.2460 0.3918 -0.0019 0.0213  0.0993  162 ASP   A OD1 
3621 O  OD1 B ASP   A 162 ? 0.1853 0.3008 0.4431 0.0055  0.0177  0.1020  162 ASP   A OD1 
3622 O  OD2 A ASP   A 162 ? 0.1706 0.2415 0.3837 0.0032  0.0326  0.1035  162 ASP   A OD2 
3623 O  OD2 B ASP   A 162 ? 0.1902 0.3046 0.4394 0.0044  0.0227  0.1016  162 ASP   A OD2 
3632 N  N   A LYS   A 163 ? 0.1314 0.2925 0.3408 -0.0233 -0.0277 0.1097  163 LYS   A N   
3633 N  N   B LYS   A 163 ? 0.1779 0.3132 0.3526 -0.0077 -0.0021 0.0993  163 LYS   A N   
3634 C  CA  A LYS   A 163 ? 0.1460 0.3119 0.3222 -0.0249 -0.0285 0.1123  163 LYS   A CA  
3635 C  CA  B LYS   A 163 ? 0.1929 0.3222 0.3386 -0.0163 -0.0096 0.1019  163 LYS   A CA  
3636 C  C   A LYS   A 163 ? 0.1368 0.3078 0.2999 -0.0272 -0.0081 0.1171  163 LYS   A C   
3637 C  C   B LYS   A 163 ? 0.1843 0.3080 0.3238 -0.0279 -0.0002 0.1005  163 LYS   A C   
3638 O  O   A LYS   A 163 ? 0.1306 0.3242 0.2958 -0.0338 -0.0006 0.1195  163 LYS   A O   
3639 O  O   B LYS   A 163 ? 0.1890 0.3162 0.3271 -0.0341 0.0050  0.0952  163 LYS   A O   
3640 C  CB  A LYS   A 163 ? 0.1855 0.3334 0.3525 -0.0184 -0.0421 0.1040  163 LYS   A CB  
3641 C  CB  B LYS   A 163 ? 0.2266 0.3444 0.3679 -0.0109 -0.0149 0.1000  163 LYS   A CB  
3642 C  CG  A LYS   A 163 ? 0.2228 0.3511 0.3833 -0.0181 -0.0343 0.0988  163 LYS   A CG  
3643 C  CG  B LYS   A 163 ? 0.2576 0.3636 0.3974 -0.0093 -0.0086 0.1006  163 LYS   A CG  
3644 C  CD  A LYS   A 163 ? 0.2497 0.3657 0.4233 -0.0205 -0.0311 0.0873  163 LYS   A CD  
3645 C  CD  B LYS   A 163 ? 0.2824 0.3801 0.4350 -0.0090 -0.0037 0.0990  163 LYS   A CD  
3646 C  CE  A LYS   A 163 ? 0.2810 0.3763 0.4500 -0.0215 -0.0281 0.0814  163 LYS   A CE  
3647 C  CE  B LYS   A 163 ? 0.3015 0.3925 0.4632 -0.0084 -0.0011 0.0973  163 LYS   A CE  
3648 N  NZ  A LYS   A 163 ? 0.2942 0.3823 0.4710 -0.0224 -0.0295 0.0803  163 LYS   A NZ  
3649 N  NZ  B LYS   A 163 ? 0.3121 0.3996 0.4838 -0.0080 -0.0013 0.0946  163 LYS   A NZ  
3676 N  N   A LEU   A 164 ? 0.1277 0.2843 0.2879 -0.0317 -0.0101 0.1071  164 LEU   A N   
3677 N  N   B LEU   A 164 ? 0.1684 0.2856 0.3096 -0.0344 -0.0053 0.0994  164 LEU   A N   
3678 C  CA  A LEU   A 164 ? 0.1321 0.2627 0.2760 -0.0320 0.0085  0.0954  164 LEU   A CA  
3679 C  CA  B LEU   A 164 ? 0.1624 0.2656 0.2965 -0.0375 0.0088  0.1000  164 LEU   A CA  
3680 C  C   A LEU   A 164 ? 0.1482 0.2584 0.2718 -0.0328 0.0111  0.0856  164 LEU   A C   
3681 C  C   B LEU   A 164 ? 0.1638 0.2630 0.2928 -0.0315 0.0147  0.0936  164 LEU   A C   
3682 O  O   A LEU   A 164 ? 0.1537 0.2698 0.2627 -0.0365 0.0261  0.0714  164 LEU   A O   
3683 O  O   B LEU   A 164 ? 0.1649 0.2711 0.2905 -0.0290 0.0334  0.0856  164 LEU   A O   
3684 C  CB  A LEU   A 164 ? 0.1304 0.2498 0.2727 -0.0270 0.0105  0.0864  164 LEU   A CB  
3685 C  CB  B LEU   A 164 ? 0.1641 0.2565 0.2916 -0.0429 0.0130  0.0995  164 LEU   A CB  
3686 C  CG  A LEU   A 164 ? 0.1351 0.2410 0.2709 -0.0170 0.0040  0.0671  164 LEU   A CG  
3687 C  CG  B LEU   A 164 ? 0.1718 0.2544 0.2861 -0.0411 0.0183  0.0867  164 LEU   A CG  
3688 C  CD1 A LEU   A 164 ? 0.1181 0.2334 0.2623 -0.0062 -0.0148 0.0667  164 LEU   A CD1 
3689 C  CD1 B LEU   A 164 ? 0.1718 0.2568 0.2870 -0.0438 0.0129  0.0772  164 LEU   A CD1 
3690 C  CD2 A LEU   A 164 ? 0.1487 0.2378 0.2658 -0.0224 0.0142  0.0578  164 LEU   A CD2 
3691 C  CD2 B LEU   A 164 ? 0.1812 0.2562 0.2783 -0.0373 0.0208  0.0830  164 LEU   A CD2 
3714 N  N   A VAL   A 165 ? 0.1490 0.2428 0.2737 -0.0328 0.0138  0.0872  165 VAL   A N   
3715 N  N   B VAL   A 165 ? 0.1550 0.2561 0.2943 -0.0291 0.0108  0.0862  165 VAL   A N   
3716 C  CA  A VAL   A 165 ? 0.1588 0.2324 0.2673 -0.0311 0.0221  0.0834  165 VAL   A CA  
3717 C  CA  B VAL   A 165 ? 0.1535 0.2514 0.2884 -0.0266 0.0216  0.0814  165 VAL   A CA  
3718 C  C   A VAL   A 165 ? 0.1577 0.2434 0.2519 -0.0237 0.0223  0.0865  165 VAL   A C   
3719 C  C   B VAL   A 165 ? 0.1393 0.2582 0.2764 -0.0269 0.0179  0.0791  165 VAL   A C   
3720 O  O   A VAL   A 165 ? 0.1561 0.2442 0.2305 -0.0264 0.0277  0.0893  165 VAL   A O   
3721 O  O   B VAL   A 165 ? 0.1421 0.2600 0.2634 -0.0269 0.0161  0.0779  165 VAL   A O   
3722 C  CB  A VAL   A 165 ? 0.1684 0.2202 0.2804 -0.0287 0.0295  0.0670  165 VAL   A CB  
3723 C  CB  B VAL   A 165 ? 0.1652 0.2461 0.2928 -0.0169 0.0326  0.0736  165 VAL   A CB  
3724 C  CG1 A VAL   A 165 ? 0.1723 0.2192 0.2842 -0.0263 0.0434  0.0546  165 VAL   A CG1 
3725 C  CG1 B VAL   A 165 ? 0.1744 0.2486 0.3002 -0.0190 0.0381  0.0632  165 VAL   A CG1 
3726 C  CG2 A VAL   A 165 ? 0.1761 0.2153 0.2816 -0.0279 0.0258  0.0670  165 VAL   A CG2 
3727 C  CG2 B VAL   A 165 ? 0.1667 0.2418 0.2845 -0.0019 0.0313  0.0793  165 VAL   A CG2 
3746 N  N   A SER   A 166 ? 0.1673 0.2567 0.2790 -0.0138 0.0165  0.0797  166 SER   A N   
3747 N  N   B SER   A 166 ? 0.1233 0.2644 0.2894 -0.0277 0.0218  0.0757  166 SER   A N   
3748 C  CA  A SER   A 166 ? 0.1820 0.2747 0.2909 -0.0123 0.0116  0.0732  166 SER   A CA  
3749 C  CA  B SER   A 166 ? 0.1216 0.2747 0.2984 -0.0314 0.0153  0.0656  166 SER   A CA  
3750 C  C   A SER   A 166 ? 0.1844 0.2862 0.2765 -0.0057 -0.0092 0.0755  166 SER   A C   
3751 C  C   B SER   A 166 ? 0.1310 0.2905 0.2937 -0.0321 0.0087  0.0662  166 SER   A C   
3752 O  O   A SER   A 166 ? 0.1936 0.2921 0.2743 -0.0110 -0.0178 0.0763  166 SER   A O   
3753 O  O   B SER   A 166 ? 0.1411 0.2951 0.3048 -0.0332 0.0040  0.0624  166 SER   A O   
3754 C  CB  A SER   A 166 ? 0.2028 0.2820 0.3166 -0.0091 0.0171  0.0659  166 SER   A CB  
3755 C  CB  B SER   A 166 ? 0.1331 0.2732 0.3214 -0.0204 0.0005  0.0516  166 SER   A CB  
3756 O  OG  A SER   A 166 ? 0.2174 0.2879 0.3370 -0.0102 0.0248  0.0673  166 SER   A OG  
3757 O  OG  B SER   A 166 ? 0.1410 0.2696 0.3396 -0.0147 -0.0191 0.0482  166 SER   A OG  
3768 N  N   A SER   A 167 ? 0.1822 0.2897 0.2628 0.0085  -0.0182 0.0770  167 SER   A N   
3769 N  N   B SER   A 167 ? 0.1464 0.2995 0.2896 -0.0274 0.0090  0.0672  167 SER   A N   
3770 C  CA  A SER   A 167 ? 0.1885 0.2894 0.2573 0.0085  -0.0139 0.0688  167 SER   A CA  
3771 C  CA  B SER   A 167 ? 0.1783 0.3088 0.2818 -0.0223 0.0099  0.0662  167 SER   A CA  
3772 C  C   A SER   A 167 ? 0.1834 0.2935 0.2489 0.0082  -0.0011 0.0642  167 SER   A C   
3773 C  C   B SER   A 167 ? 0.1954 0.3222 0.2720 -0.0162 0.0131  0.0664  167 SER   A C   
3774 O  O   A SER   A 167 ? 0.1981 0.2925 0.2522 0.0089  -0.0087 0.0722  167 SER   A O   
3775 O  O   B SER   A 167 ? 0.2050 0.3224 0.2815 -0.0185 0.0071  0.0616  167 SER   A O   
3776 C  CB  A SER   A 167 ? 0.1936 0.2833 0.2608 0.0147  -0.0050 0.0722  167 SER   A CB  
3777 C  CB  B SER   A 167 ? 0.1895 0.3100 0.2958 -0.0158 0.0191  0.0573  167 SER   A CB  
3778 O  OG  A SER   A 167 ? 0.1949 0.2782 0.2568 0.0191  0.0046  0.0801  167 SER   A OG  
3779 O  OG  B SER   A 167 ? 0.1929 0.3098 0.2988 -0.0116 0.0314  0.0548  167 SER   A OG  
3790 N  N   A PHE   A 168 ? 0.1629 0.2978 0.2400 0.0074  0.0183  0.0530  168 PHE   A N   
3791 N  N   B PHE   A 168 ? 0.2121 0.3400 0.2691 -0.0032 0.0112  0.0664  168 PHE   A N   
3792 C  CA  A PHE   A 168 ? 0.1510 0.3044 0.2521 0.0004  0.0337  0.0315  168 PHE   A CA  
3793 C  CA  B PHE   A 168 ? 0.2408 0.3592 0.2819 0.0083  0.0156  0.0685  168 PHE   A CA  
3794 C  C   A PHE   A 168 ? 0.1590 0.3312 0.2821 -0.0063 0.0719  0.0038  168 PHE   A C   
3795 C  C   B PHE   A 168 ? 0.3036 0.3930 0.3363 0.0119  0.0073  0.0547  168 PHE   A C   
3796 O  O   A PHE   A 168 ? 0.1644 0.3421 0.3101 -0.0137 0.0803  0.0154  168 PHE   A O   
3797 O  O   B PHE   A 168 ? 0.2994 0.3928 0.3183 0.0095  0.0047  0.0656  168 PHE   A O   
3798 C  CB  A PHE   A 168 ? 0.1468 0.2858 0.2314 -0.0078 0.0118  0.0359  168 PHE   A CB  
3799 C  CB  B PHE   A 168 ? 0.2183 0.3479 0.2619 0.0094  0.0241  0.0831  168 PHE   A CB  
3800 C  CG  A PHE   A 168 ? 0.1435 0.2705 0.2104 -0.0209 -0.0048 0.0369  168 PHE   A CG  
3801 C  CG  B PHE   A 168 ? 0.2049 0.3382 0.2488 0.0105  0.0242  0.0984  168 PHE   A CG  
3802 C  CD1 A PHE   A 168 ? 0.1437 0.2708 0.2038 -0.0287 -0.0138 0.0376  168 PHE   A CD1 
3803 C  CD1 B PHE   A 168 ? 0.2019 0.3385 0.2488 0.0098  0.0314  0.1042  168 PHE   A CD1 
3804 C  CD2 A PHE   A 168 ? 0.1421 0.2614 0.2083 -0.0273 -0.0027 0.0290  168 PHE   A CD2 
3805 C  CD2 B PHE   A 168 ? 0.2001 0.3312 0.2524 0.0127  0.0157  0.1009  168 PHE   A CD2 
3806 C  CE1 A PHE   A 168 ? 0.1352 0.2660 0.1930 -0.0333 -0.0176 0.0317  168 PHE   A CE1 
3807 C  CE1 B PHE   A 168 ? 0.1999 0.3361 0.2545 0.0114  0.0252  0.1055  168 PHE   A CE1 
3808 C  CE2 A PHE   A 168 ? 0.1496 0.2573 0.2129 -0.0300 0.0021  0.0321  168 PHE   A CE2 
3809 C  CE2 B PHE   A 168 ? 0.1999 0.3297 0.2507 0.0126  0.0155  0.1040  168 PHE   A CE2 
3810 C  CZ  A PHE   A 168 ? 0.1452 0.2614 0.2012 -0.0312 -0.0098 0.0322  168 PHE   A CZ  
3811 C  CZ  B PHE   A 168 ? 0.2011 0.3324 0.2513 0.0111  0.0211  0.1041  168 PHE   A CZ  
3830 N  N   A LEU   A 169 ? 0.1880 0.3459 0.3177 -0.0213 0.0666  -0.0267 169 LEU   A N   
3831 N  N   B LEU   A 169 ? 0.3744 0.4287 0.4201 0.0129  -0.0022 0.0340  169 LEU   A N   
3832 C  CA  A LEU   A 169 ? 0.2509 0.3642 0.3845 -0.0268 0.0247  -0.0399 169 LEU   A CA  
3833 C  CA  B LEU   A 169 ? 0.4353 0.4625 0.4987 0.0149  -0.0148 0.0168  169 LEU   A CA  
3834 C  C   A LEU   A 169 ? 0.2780 0.3677 0.4075 -0.0257 0.0135  -0.0361 169 LEU   A C   
3835 C  C   B LEU   A 169 ? 0.4594 0.4767 0.5414 0.0150  -0.0159 0.0247  169 LEU   A C   
3836 O  O   A LEU   A 169 ? 0.2960 0.3739 0.4160 -0.0209 0.0141  -0.0412 169 LEU   A O   
3837 O  O   B LEU   A 169 ? 0.4668 0.4827 0.5562 0.0138  -0.0131 0.0296  169 LEU   A O   
3838 C  CB  A LEU   A 169 ? 0.2854 0.3782 0.4124 -0.0341 0.0021  -0.0559 169 LEU   A CB  
3839 C  CB  B LEU   A 169 ? 0.4640 0.4801 0.5231 0.0146  -0.0250 -0.0096 169 LEU   A CB  
3840 C  CG  A LEU   A 169 ? 0.3136 0.3901 0.4385 -0.0407 -0.0143 -0.0745 169 LEU   A CG  
3841 C  CG  B LEU   A 169 ? 0.4843 0.4943 0.5437 0.0125  -0.0306 -0.0330 169 LEU   A CG  
3842 C  CD1 A LEU   A 169 ? 0.3216 0.3935 0.4497 -0.0429 -0.0199 -0.0802 169 LEU   A CD1 
3843 C  CD1 B LEU   A 169 ? 0.4888 0.4983 0.5513 0.0116  -0.0337 -0.0407 169 LEU   A CD1 
3844 C  CD2 A LEU   A 169 ? 0.3230 0.3950 0.4443 -0.0429 -0.0181 -0.0808 169 LEU   A CD2 
3845 C  CD2 B LEU   A 169 ? 0.4931 0.4998 0.5486 0.0114  -0.0318 -0.0417 169 LEU   A CD2 
3846 O  OXT A LEU   A 169 ? 0.2666 0.3650 0.4095 -0.0281 0.0126  -0.0341 169 LEU   A OXT 
3847 O  OXT B LEU   A 169 ? 0.4707 0.4824 0.5583 0.0156  -0.0180 0.0244  169 LEU   A OXT 
3870 N  N   A SER   B 1   ? 0.3985 0.3621 0.3889 -0.0985 -0.0777 0.0399  1   SER   B N   
3871 N  N   B SER   B 1   ? 0.3594 0.3455 0.3604 -0.1095 -0.0578 0.0435  1   SER   B N   
3872 C  CA  A SER   B 1   ? 0.3924 0.3632 0.3936 -0.1002 -0.0785 0.0388  1   SER   B CA  
3873 C  CA  B SER   B 1   ? 0.3512 0.3490 0.3629 -0.1114 -0.0585 0.0416  1   SER   B CA  
3874 C  C   A SER   B 1   ? 0.3715 0.3590 0.3756 -0.1001 -0.0832 0.0528  1   SER   B C   
3875 C  C   B SER   B 1   ? 0.3244 0.3483 0.3360 -0.1126 -0.0691 0.0580  1   SER   B C   
3876 O  O   A SER   B 1   ? 0.3793 0.3618 0.3647 -0.0960 -0.0804 0.0504  1   SER   B O   
3877 O  O   B SER   B 1   ? 0.3302 0.3498 0.3173 -0.1090 -0.0683 0.0544  1   SER   B O   
3878 C  CB  A SER   B 1   ? 0.4039 0.3647 0.3990 -0.1009 -0.0735 0.0273  1   SER   B CB  
3879 C  CB  B SER   B 1   ? 0.3652 0.3489 0.3750 -0.1103 -0.0487 0.0259  1   SER   B CB  
3880 O  OG  A SER   B 1   ? 0.4142 0.3713 0.4319 -0.0989 -0.0697 0.0248  1   SER   B OG  
3881 O  OG  B SER   B 1   ? 0.3769 0.3550 0.4106 -0.1072 -0.0453 0.0187  1   SER   B OG  
3896 N  N   A MET   B 2   ? 0.3445 0.3497 0.3586 -0.1011 -0.0848 0.0799  2   MET   B N   
3897 N  N   B MET   B 2   ? 0.2969 0.3444 0.3163 -0.1115 -0.0732 0.0928  2   MET   B N   
3898 C  CA  A MET   B 2   ? 0.3222 0.3425 0.3646 -0.0894 -0.0808 0.0966  2   MET   B CA  
3899 C  CA  B MET   B 2   ? 0.2776 0.3442 0.3172 -0.0925 -0.0711 0.1127  2   MET   B CA  
3900 C  C   A MET   B 2   ? 0.2801 0.3147 0.3185 -0.0825 -0.0914 0.1161  2   MET   B C   
3901 C  C   B MET   B 2   ? 0.2472 0.3268 0.2864 -0.0737 -0.0697 0.1229  2   MET   B C   
3902 O  O   A MET   B 2   ? 0.2747 0.3220 0.3078 -0.0781 -0.1028 0.1216  2   MET   B O   
3903 O  O   B MET   B 2   ? 0.2428 0.3399 0.2912 -0.0642 -0.0685 0.1166  2   MET   B O   
3904 C  CB  A MET   B 2   ? 0.3483 0.3681 0.4351 -0.0732 -0.0629 0.0771  2   MET   B CB  
3905 C  CB  B MET   B 2   ? 0.2989 0.3682 0.3670 -0.0778 -0.0675 0.1041  2   MET   B CB  
3906 C  CG  A MET   B 2   ? 0.3728 0.3913 0.4994 -0.0552 -0.0452 0.0648  2   MET   B CG  
3907 C  CG  B MET   B 2   ? 0.3171 0.3906 0.4037 -0.0613 -0.0611 0.1116  2   MET   B CG  
3908 S  SD  A MET   B 2   ? 0.3959 0.4113 0.5688 -0.0404 -0.0323 0.0581  2   MET   B SD  
3909 S  SD  B MET   B 2   ? 0.3355 0.4136 0.4378 -0.0469 -0.0591 0.1205  2   MET   B SD  
3910 C  CE  A MET   B 2   ? 0.4012 0.4179 0.5694 -0.0377 -0.0279 0.0596  2   MET   B CE  
3911 C  CE  B MET   B 2   ? 0.3369 0.4183 0.4495 -0.0470 -0.0595 0.1090  2   MET   B CE  
3930 N  N   A VAL   B 3   ? 0.2433 0.2731 0.2926 -0.0893 -0.0846 0.1207  3   VAL   B N   
3931 N  N   B VAL   B 3   ? 0.2223 0.2921 0.2672 -0.0741 -0.0612 0.1265  3   VAL   B N   
3932 C  CA  A VAL   B 3   ? 0.2233 0.2405 0.2794 -0.0798 -0.0738 0.1129  3   VAL   B CA  
3933 C  CA  B VAL   B 3   ? 0.2138 0.2617 0.2599 -0.0630 -0.0501 0.1060  3   VAL   B CA  
3934 C  C   A VAL   B 3   ? 0.1978 0.2258 0.2412 -0.0665 -0.0659 0.1032  3   VAL   B C   
3935 C  C   B VAL   B 3   ? 0.1966 0.2458 0.2302 -0.0517 -0.0448 0.0958  3   VAL   B C   
3936 O  O   A VAL   B 3   ? 0.1903 0.2174 0.2392 -0.0617 -0.0685 0.1101  3   VAL   B O   
3937 O  O   B VAL   B 3   ? 0.1959 0.2554 0.2350 -0.0339 -0.0471 0.0916  3   VAL   B O   
3938 C  CB  A VAL   B 3   ? 0.2373 0.2349 0.3198 -0.0789 -0.0619 0.1035  3   VAL   B CB  
3939 C  CB  B VAL   B 3   ? 0.2311 0.2501 0.2922 -0.0613 -0.0400 0.0978  3   VAL   B CB  
3940 C  CG1 A VAL   B 3   ? 0.2478 0.2315 0.3394 -0.0792 -0.0585 0.1015  3   VAL   B CG1 
3941 C  CG1 B VAL   B 3   ? 0.2409 0.2442 0.3087 -0.0619 -0.0364 0.0950  3   VAL   B CG1 
3942 C  CG2 A VAL   B 3   ? 0.2415 0.2407 0.3403 -0.0729 -0.0480 0.1017  3   VAL   B CG2 
3943 C  CG2 B VAL   B 3   ? 0.2362 0.2514 0.3045 -0.0578 -0.0313 0.0989  3   VAL   B CG2 
3962 N  N   . ASN   B 4   ? 0.1866 0.2209 0.2155 -0.0573 -0.0500 0.0846  4   ASN   B N   
3963 C  CA  . ASN   B 4   ? 0.1888 0.2170 0.1784 -0.0540 -0.0448 0.0488  4   ASN   B CA  
3964 C  C   . ASN   B 4   ? 0.1924 0.2327 0.1643 -0.0530 -0.0367 0.0349  4   ASN   B C   
3965 O  O   . ASN   B 4   ? 0.1937 0.2373 0.1883 -0.0498 -0.0297 0.0076  4   ASN   B O   
3966 C  CB  . ASN   B 4   ? 0.1891 0.2111 0.1703 -0.0446 -0.0548 0.0372  4   ASN   B CB  
3967 C  CG  . ASN   B 4   ? 0.1869 0.1981 0.1611 -0.0471 -0.0457 0.0309  4   ASN   B CG  
3968 O  OD1 . ASN   B 4   ? 0.1882 0.1799 0.1672 -0.0483 -0.0454 0.0293  4   ASN   B OD1 
3969 N  ND2 . ASN   B 4   ? 0.2064 0.2069 0.1773 -0.0270 -0.0306 0.0237  4   ASN   B ND2 
3977 N  N   . SER   B 5   ? 0.2013 0.2553 0.1809 -0.0557 -0.0273 0.0331  5   SER   B N   
3978 C  CA  . SER   B 5   ? 0.2312 0.2916 0.2055 -0.0481 -0.0079 0.0365  5   SER   B CA  
3979 C  C   . SER   B 5   ? 0.2485 0.2951 0.2488 -0.0647 0.0213  0.0324  5   SER   B C   
3980 O  O   . SER   B 5   ? 0.2666 0.2920 0.3380 -0.0641 0.0649  0.0299  5   SER   B O   
3981 C  CB  . SER   B 5   ? 0.2458 0.3142 0.2216 -0.0398 -0.0077 0.0420  5   SER   B CB  
3982 O  OG  . SER   B 5   ? 0.2718 0.3403 0.2799 -0.0290 -0.0056 0.0405  5   SER   B OG  
3988 N  N   . PHE   B 6   ? 0.2639 0.3115 0.2217 -0.0690 0.0283  0.0393  6   PHE   B N   
3989 C  CA  . PHE   B 6   ? 0.2750 0.3129 0.1803 -0.0906 0.0302  0.0166  6   PHE   B CA  
3990 C  C   . PHE   B 6   ? 0.3294 0.3450 0.2180 -0.1001 0.0572  -0.0089 6   PHE   B C   
3991 O  O   . PHE   B 6   ? 0.3446 0.3766 0.2727 -0.0932 0.0429  -0.0262 6   PHE   B O   
3992 C  CB  . PHE   B 6   ? 0.2448 0.2895 0.1583 -0.0812 0.0114  0.0122  6   PHE   B CB  
3993 C  CG  . PHE   B 6   ? 0.2163 0.2554 0.1540 -0.0752 -0.0028 0.0082  6   PHE   B CG  
3994 C  CD1 . PHE   B 6   ? 0.2189 0.2266 0.1378 -0.0636 -0.0122 0.0047  6   PHE   B CD1 
3995 C  CD2 . PHE   B 6   ? 0.1945 0.2505 0.1628 -0.0642 0.0025  0.0356  6   PHE   B CD2 
3996 C  CE1 . PHE   B 6   ? 0.2134 0.1982 0.1572 -0.0535 -0.0155 0.0064  6   PHE   B CE1 
3997 C  CE2 . PHE   B 6   ? 0.1963 0.2334 0.2000 -0.0505 -0.0007 0.0331  6   PHE   B CE2 
3998 C  CZ  . PHE   B 6   ? 0.2020 0.2034 0.1780 -0.0474 -0.0080 0.0095  6   PHE   B CZ  
4008 N  N   . SER   B 7   ? 0.3671 0.3313 0.2437 -0.1195 0.0937  -0.0327 7   SER   B N   
4009 C  CA  . SER   B 7   ? 0.4001 0.3412 0.2987 -0.1174 0.1147  -0.0488 7   SER   B CA  
4010 C  C   . SER   B 7   ? 0.3979 0.3248 0.2870 -0.1186 0.1348  -0.0650 7   SER   B C   
4011 O  O   . SER   B 7   ? 0.4010 0.3242 0.3270 -0.1233 0.1356  -0.0627 7   SER   B O   
4012 C  CB  . SER   B 7   ? 0.4227 0.3650 0.3621 -0.1138 0.1243  -0.0498 7   SER   B CB  
4013 O  OG  . SER   B 7   ? 0.4367 0.3808 0.4128 -0.1116 0.1252  -0.0434 7   SER   B OG  
4019 N  N   . GLY   B 8   ? 0.3961 0.3175 0.3018 -0.1020 0.1451  -0.0748 8   GLY   B N   
4020 C  CA  . GLY   B 8   ? 0.3790 0.3027 0.3026 -0.0934 0.1516  -0.0785 8   GLY   B CA  
4021 C  C   . GLY   B 8   ? 0.3514 0.2762 0.2916 -0.0909 0.1537  -0.0746 8   GLY   B C   
4022 O  O   . GLY   B 8   ? 0.3598 0.2825 0.3360 -0.0835 0.1511  -0.0827 8   GLY   B O   
4026 N  N   . TYR   B 9   ? 0.3291 0.2494 0.2659 -0.0806 0.1206  -0.0823 9   TYR   B N   
4027 C  CA  . TYR   B 9   ? 0.3058 0.2198 0.2277 -0.0696 0.0878  -0.0620 9   TYR   B CA  
4028 C  C   . TYR   B 9   ? 0.3051 0.2180 0.2148 -0.0645 0.0562  -0.0472 9   TYR   B C   
4029 O  O   . TYR   B 9   ? 0.3211 0.2421 0.2669 -0.0672 0.0542  -0.0265 9   TYR   B O   
4030 C  CB  . TYR   B 9   ? 0.2947 0.1936 0.2299 -0.0598 0.0775  -0.0568 9   TYR   B CB  
4031 C  CG  . TYR   B 9   ? 0.2844 0.1736 0.2294 -0.0656 0.0682  -0.0515 9   TYR   B CG  
4032 C  CD1 . TYR   B 9   ? 0.2933 0.1754 0.2462 -0.0775 0.0670  -0.0355 9   TYR   B CD1 
4033 C  CD2 . TYR   B 9   ? 0.2711 0.1717 0.2212 -0.0565 0.0612  -0.0589 9   TYR   B CD2 
4034 C  CE1 . TYR   B 9   ? 0.2879 0.1881 0.2522 -0.0832 0.0701  -0.0485 9   TYR   B CE1 
4035 C  CE2 . TYR   B 9   ? 0.2737 0.1769 0.2317 -0.0579 0.0578  -0.0533 9   TYR   B CE2 
4036 C  CZ  . TYR   B 9   ? 0.2795 0.1911 0.2472 -0.0748 0.0624  -0.0638 9   TYR   B CZ  
4037 O  OH  . TYR   B 9   ? 0.2761 0.2096 0.2594 -0.0876 0.0645  -0.0770 9   TYR   B OH  
4047 N  N   . LEU   B 10  ? 0.2868 0.1924 0.1966 -0.0629 0.0326  -0.0491 10  LEU   B N   
4048 C  CA  . LEU   B 10  ? 0.2829 0.1923 0.1920 -0.0693 0.0019  -0.0421 10  LEU   B CA  
4049 C  C   . LEU   B 10  ? 0.2642 0.1939 0.2022 -0.0672 -0.0209 -0.0327 10  LEU   B C   
4050 O  O   . LEU   B 10  ? 0.2504 0.1937 0.2003 -0.0500 -0.0085 -0.0213 10  LEU   B O   
4051 C  CB  . LEU   B 10  ? 0.3001 0.1919 0.2178 -0.0764 -0.0139 -0.0201 10  LEU   B CB  
4052 C  CG  . LEU   B 10  ? 0.3264 0.2038 0.2583 -0.0731 -0.0437 -0.0046 10  LEU   B CG  
4053 C  CD1 . LEU   B 10  ? 0.3454 0.2185 0.2822 -0.0671 -0.0429 -0.0045 10  LEU   B CD1 
4054 C  CD2 . LEU   B 10  ? 0.3357 0.2067 0.2853 -0.0726 -0.0427 0.0109  10  LEU   B CD2 
4066 N  N   . LYS   B 11  ? 0.2767 0.2181 0.2027 -0.0655 -0.0341 -0.0255 11  LYS   B N   
4067 C  CA  . LYS   B 11  ? 0.2993 0.2453 0.2354 -0.0514 -0.0432 -0.0348 11  LYS   B CA  
4068 C  C   . LYS   B 11  ? 0.2840 0.2244 0.2420 -0.0705 -0.0365 -0.0427 11  LYS   B C   
4069 O  O   . LYS   B 11  ? 0.2989 0.2429 0.2807 -0.0891 -0.0343 -0.0731 11  LYS   B O   
4070 C  CB  . LYS   B 11  ? 0.3340 0.2969 0.3018 -0.0221 -0.0485 -0.0359 11  LYS   B CB  
4071 C  CG  . LYS   B 11  ? 0.3664 0.3312 0.3758 -0.0042 -0.0467 -0.0377 11  LYS   B CG  
4072 C  CD  . LYS   B 11  ? 0.3923 0.3526 0.4453 0.0052  -0.0430 -0.0408 11  LYS   B CD  
4073 C  CE  . LYS   B 11  ? 0.4112 0.3671 0.4971 0.0057  -0.0442 -0.0448 11  LYS   B CE  
4074 N  NZ  . LYS   B 11  ? 0.4221 0.3762 0.5272 0.0037  -0.0474 -0.0458 11  LYS   B NZ  
4088 N  N   . LEU   B 12  ? 0.2504 0.1940 0.2430 -0.0591 -0.0339 -0.0426 12  LEU   B N   
4089 C  CA  . LEU   B 12  ? 0.2298 0.1775 0.2614 -0.0496 -0.0241 -0.0389 12  LEU   B CA  
4090 C  C   . LEU   B 12  ? 0.2117 0.1786 0.2719 -0.0524 -0.0375 -0.0354 12  LEU   B C   
4091 O  O   . LEU   B 12  ? 0.2133 0.1769 0.2914 -0.0619 -0.0490 -0.0277 12  LEU   B O   
4092 C  CB  . LEU   B 12  ? 0.2316 0.1601 0.2592 -0.0392 -0.0185 -0.0389 12  LEU   B CB  
4093 C  CG  . LEU   B 12  ? 0.2301 0.1556 0.2617 -0.0414 -0.0153 -0.0261 12  LEU   B CG  
4094 C  CD1 . LEU   B 12  ? 0.2386 0.1570 0.2464 -0.0333 -0.0163 -0.0111 12  LEU   B CD1 
4095 C  CD2 . LEU   B 12  ? 0.2364 0.1567 0.2804 -0.0395 -0.0135 -0.0378 12  LEU   B CD2 
4107 N  N   . THR   B 13  ? 0.2022 0.1850 0.2701 -0.0534 -0.0397 -0.0401 13  THR   B N   
4108 C  CA  . THR   B 13  ? 0.2023 0.1910 0.2543 -0.0619 -0.0531 -0.0238 13  THR   B CA  
4109 C  C   . THR   B 13  ? 0.2443 0.2076 0.2728 -0.0689 -0.0668 -0.0137 13  THR   B C   
4110 O  O   . THR   B 13  ? 0.2623 0.2081 0.2813 -0.0665 -0.0324 -0.0098 13  THR   B O   
4111 C  CB  . THR   B 13  ? 0.1899 0.1899 0.2589 -0.0525 -0.0440 -0.0114 13  THR   B CB  
4112 O  OG1 . THR   B 13  ? 0.1801 0.1804 0.2595 -0.0469 -0.0332 -0.0133 13  THR   B OG1 
4113 C  CG2 . THR   B 13  ? 0.1938 0.1940 0.2649 -0.0451 -0.0316 -0.0108 13  THR   B CG2 
4121 N  N   A ASP   B 14  ? 0.2548 0.2190 0.2846 -0.0749 -0.0952 -0.0086 14  ASP   B N   
4122 N  N   B ASP   B 14  ? 0.2563 0.2204 0.2802 -0.0705 -0.0916 -0.0035 14  ASP   B N   
4123 C  CA  A ASP   B 14  ? 0.2662 0.2329 0.3146 -0.0743 -0.1001 0.0082  14  ASP   B CA  
4124 C  CA  B ASP   B 14  ? 0.2690 0.2357 0.3042 -0.0663 -0.0953 0.0144  14  ASP   B CA  
4125 C  C   A ASP   B 14  ? 0.2547 0.2155 0.2741 -0.0739 -0.0877 0.0180  14  ASP   B C   
4126 C  C   B ASP   B 14  ? 0.2549 0.2180 0.2705 -0.0674 -0.0874 0.0183  14  ASP   B C   
4127 O  O   A ASP   B 14  ? 0.2725 0.2248 0.2699 -0.0771 -0.0894 0.0269  14  ASP   B O   
4128 O  O   B ASP   B 14  ? 0.2700 0.2265 0.2674 -0.0676 -0.0951 0.0219  14  ASP   B O   
4129 C  CB  A ASP   B 14  ? 0.2882 0.2635 0.3947 -0.0733 -0.1093 0.0045  14  ASP   B CB  
4130 C  CB  B ASP   B 14  ? 0.2947 0.2680 0.3738 -0.0599 -0.0990 0.0171  14  ASP   B CB  
4131 C  CG  A ASP   B 14  ? 0.3114 0.2873 0.4607 -0.0708 -0.1036 -0.0080 14  ASP   B CG  
4132 C  CG  B ASP   B 14  ? 0.3207 0.2945 0.4319 -0.0524 -0.0913 0.0091  14  ASP   B CG  
4133 O  OD1 A ASP   B 14  ? 0.3253 0.2937 0.4766 -0.0737 -0.1035 -0.0198 14  ASP   B OD1 
4134 O  OD1 B ASP   B 14  ? 0.3325 0.3058 0.4417 -0.0511 -0.0888 -0.0008 14  ASP   B OD1 
4135 O  OD2 A ASP   B 14  ? 0.3144 0.2974 0.4919 -0.0706 -0.0974 -0.0069 14  ASP   B OD2 
4136 O  OD2 B ASP   B 14  ? 0.3286 0.3039 0.4590 -0.0523 -0.0864 0.0116  14  ASP   B OD2 
4145 N  N   . ASN   B 15  ? 0.2243 0.1932 0.2441 -0.0615 -0.0773 0.0186  15  ASN   B N   
4146 C  CA  . ASN   B 15  ? 0.1812 0.1651 0.2216 -0.0401 -0.0560 0.0034  15  ASN   B CA  
4147 C  C   . ASN   B 15  ? 0.1656 0.1542 0.2071 -0.0289 -0.0389 -0.0015 15  ASN   B C   
4148 O  O   . ASN   B 15  ? 0.1631 0.1500 0.2170 -0.0239 -0.0423 -0.0132 15  ASN   B O   
4149 C  CB  . ASN   B 15  ? 0.1764 0.1621 0.2459 -0.0194 -0.0573 0.0072  15  ASN   B CB  
4150 C  CG  . ASN   B 15  ? 0.1643 0.1576 0.2341 -0.0273 -0.0215 0.0061  15  ASN   B CG  
4151 O  OD1 . ASN   B 15  ? 0.1713 0.1821 0.2758 -0.0432 -0.0271 0.0121  15  ASN   B OD1 
4152 N  ND2 . ASN   B 15  ? 0.1654 0.1415 0.2269 -0.0196 0.0028  -0.0067 15  ASN   B ND2 
4160 N  N   . VAL   B 16  ? 0.1667 0.1474 0.2216 -0.0319 -0.0448 -0.0021 16  VAL   B N   
4161 C  CA  . VAL   B 16  ? 0.1648 0.1471 0.2069 -0.0276 -0.0265 -0.0192 16  VAL   B CA  
4162 C  C   . VAL   B 16  ? 0.1630 0.1585 0.2005 -0.0359 -0.0293 -0.0162 16  VAL   B C   
4163 O  O   . VAL   B 16  ? 0.1676 0.1730 0.2251 -0.0359 -0.0210 -0.0334 16  VAL   B O   
4164 C  CB  . VAL   B 16  ? 0.1746 0.1457 0.2107 -0.0169 -0.0210 -0.0172 16  VAL   B CB  
4165 C  CG1 . VAL   B 16  ? 0.1861 0.1388 0.2187 -0.0111 -0.0181 -0.0149 16  VAL   B CG1 
4166 C  CG2 . VAL   B 16  ? 0.1765 0.1532 0.2260 -0.0095 -0.0206 -0.0172 16  VAL   B CG2 
4176 N  N   . TYR   B 17  ? 0.1712 0.1676 0.1999 -0.0322 -0.0255 -0.0191 17  TYR   B N   
4177 C  CA  . TYR   B 17  ? 0.1777 0.1755 0.2035 -0.0354 -0.0239 -0.0020 17  TYR   B CA  
4178 C  C   . TYR   B 17  ? 0.1732 0.1498 0.2040 -0.0397 -0.0148 -0.0136 17  TYR   B C   
4179 O  O   . TYR   B 17  ? 0.1743 0.1563 0.2045 -0.0292 -0.0232 -0.0362 17  TYR   B O   
4180 C  CB  . TYR   B 17  ? 0.2098 0.2218 0.2291 -0.0182 -0.0232 0.0321  17  TYR   B CB  
4181 C  CG  . TYR   B 17  ? 0.2380 0.2724 0.2603 -0.0098 -0.0383 0.0425  17  TYR   B CG  
4182 C  CD1 . TYR   B 17  ? 0.2540 0.2897 0.2769 -0.0080 -0.0504 0.0495  17  TYR   B CD1 
4183 C  CD2 . TYR   B 17  ? 0.2600 0.3030 0.2848 -0.0027 -0.0467 0.0413  17  TYR   B CD2 
4184 C  CE1 . TYR   B 17  ? 0.2720 0.3131 0.2915 -0.0001 -0.0642 0.0433  17  TYR   B CE1 
4185 C  CE2 . TYR   B 17  ? 0.2767 0.3215 0.2977 0.0080  -0.0653 0.0466  17  TYR   B CE2 
4186 C  CZ  . TYR   B 17  ? 0.2866 0.3315 0.3034 0.0095  -0.0707 0.0466  17  TYR   B CZ  
4187 O  OH  . TYR   B 17  ? 0.3032 0.3503 0.3224 0.0168  -0.0764 0.0478  17  TYR   B OH  
4197 N  N   . ILE   B 18  ? 0.1816 0.1518 0.1854 -0.0337 -0.0066 -0.0224 18  ILE   B N   
4198 C  CA  . ILE   B 18  ? 0.1883 0.1464 0.1882 -0.0391 -0.0028 -0.0252 18  ILE   B CA  
4199 C  C   . ILE   B 18  ? 0.1980 0.1554 0.1877 -0.0463 -0.0012 -0.0344 18  ILE   B C   
4200 O  O   . ILE   B 18  ? 0.2173 0.1732 0.1904 -0.0350 0.0114  -0.0368 18  ILE   B O   
4201 C  CB  . ILE   B 18  ? 0.1948 0.1511 0.1927 -0.0414 -0.0040 -0.0245 18  ILE   B CB  
4202 C  CG1 . ILE   B 18  ? 0.1952 0.1562 0.2040 -0.0409 0.0018  -0.0113 18  ILE   B CG1 
4203 C  CG2 . ILE   B 18  ? 0.1948 0.1610 0.1932 -0.0472 -0.0081 -0.0131 18  ILE   B CG2 
4204 C  CD1 . ILE   B 18  ? 0.2018 0.1797 0.2262 -0.0413 -0.0153 0.0198  18  ILE   B CD1 
4216 N  N   . LYS   B 19  ? 0.1946 0.1561 0.2002 -0.0273 0.0246  -0.0371 19  LYS   B N   
4217 C  CA  . LYS   B 19  ? 0.2051 0.1615 0.2219 -0.0286 0.0231  -0.0483 19  LYS   B CA  
4218 C  C   . LYS   B 19  ? 0.1881 0.1602 0.2355 -0.0222 0.0322  -0.0540 19  LYS   B C   
4219 O  O   . LYS   B 19  ? 0.1848 0.1600 0.2128 -0.0162 0.0245  -0.0436 19  LYS   B O   
4220 C  CB  . LYS   B 19  ? 0.2286 0.1819 0.2277 -0.0327 0.0349  -0.0311 19  LYS   B CB  
4221 C  CG  . LYS   B 19  ? 0.2522 0.2050 0.2529 -0.0431 0.0460  -0.0387 19  LYS   B CG  
4222 C  CD  . LYS   B 19  ? 0.2813 0.2396 0.2650 -0.0491 0.0576  -0.0393 19  LYS   B CD  
4223 C  CE  . LYS   B 19  ? 0.3062 0.2658 0.2845 -0.0534 0.0603  -0.0417 19  LYS   B CE  
4224 N  NZ  . LYS   B 19  ? 0.3215 0.2808 0.2803 -0.0564 0.0636  -0.0454 19  LYS   B NZ  
4238 N  N   . ASN   B 20  ? 0.1902 0.1707 0.2800 -0.0199 0.0386  -0.0601 20  ASN   B N   
4239 C  CA  . ASN   B 20  ? 0.1894 0.1785 0.2954 -0.0177 0.0458  -0.0784 20  ASN   B CA  
4240 C  C   . ASN   B 20  ? 0.1908 0.1975 0.2934 -0.0255 0.0561  -0.0888 20  ASN   B C   
4241 O  O   . ASN   B 20  ? 0.2116 0.2321 0.3049 -0.0401 0.0531  -0.0900 20  ASN   B O   
4242 C  CB  . ASN   B 20  ? 0.2198 0.1885 0.3265 0.0042  0.0325  -0.0775 20  ASN   B CB  
4243 C  CG  . ASN   B 20  ? 0.2475 0.1946 0.3493 0.0389  0.0293  -0.0842 20  ASN   B CG  
4244 O  OD1 . ASN   B 20  ? 0.2796 0.2251 0.3747 0.0558  0.0326  -0.0878 20  ASN   B OD1 
4245 N  ND2 . ASN   B 20  ? 0.2365 0.1959 0.3393 0.0423  0.0192  -0.0761 20  ASN   B ND2 
4252 N  N   . ALA   B 21  ? 0.1869 0.1824 0.2859 -0.0313 0.0598  -0.0701 21  ALA   B N   
4253 C  CA  . ALA   B 21  ? 0.1996 0.1896 0.2963 -0.0316 0.0437  -0.0569 21  ALA   B CA  
4254 C  C   . ALA   B 21  ? 0.2003 0.1645 0.2830 -0.0232 0.0432  -0.0436 21  ALA   B C   
4255 O  O   . ALA   B 21  ? 0.2027 0.1555 0.2794 -0.0318 0.0422  -0.0385 21  ALA   B O   
4256 C  CB  . ALA   B 21  ? 0.2178 0.2169 0.2984 -0.0415 0.0449  -0.0462 21  ALA   B CB  
4262 N  N   . ASP   B 22  ? 0.1927 0.1566 0.2653 -0.0223 0.0405  -0.0359 22  ASP   B N   
4263 C  CA  . ASP   B 22  ? 0.1857 0.1509 0.2587 -0.0096 0.0247  -0.0271 22  ASP   B CA  
4264 C  C   . ASP   B 22  ? 0.1755 0.1471 0.2154 -0.0100 0.0182  -0.0136 22  ASP   B C   
4265 O  O   . ASP   B 22  ? 0.1787 0.1565 0.2158 -0.0084 0.0103  -0.0132 22  ASP   B O   
4266 C  CB  . ASP   B 22  ? 0.1964 0.1575 0.2952 -0.0049 0.0304  -0.0115 22  ASP   B CB  
4267 C  CG  . ASP   B 22  ? 0.1959 0.1759 0.3410 -0.0020 0.0073  -0.0112 22  ASP   B CG  
4268 O  OD1 . ASP   B 22  ? 0.2046 0.1686 0.3399 -0.0004 -0.0180 -0.0083 22  ASP   B OD1 
4269 O  OD2 . ASP   B 22  ? 0.2044 0.2077 0.3951 0.0086  -0.0033 -0.0263 22  ASP   B OD2 
4274 N  N   . ILE   B 23  ? 0.1768 0.1413 0.1898 -0.0084 0.0056  0.0126  23  ILE   B N   
4275 C  CA  . ILE   B 23  ? 0.1683 0.1419 0.1701 -0.0068 0.0003  0.0063  23  ILE   B CA  
4276 C  C   . ILE   B 23  ? 0.1586 0.1414 0.1790 -0.0054 -0.0055 0.0017  23  ILE   B C   
4277 O  O   . ILE   B 23  ? 0.1557 0.1469 0.1582 -0.0103 -0.0029 0.0045  23  ILE   B O   
4278 C  CB  . ILE   B 23  ? 0.1659 0.1458 0.1845 -0.0143 0.0033  0.0095  23  ILE   B CB  
4279 C  CG1 . ILE   B 23  ? 0.1670 0.1531 0.2004 -0.0099 0.0043  0.0204  23  ILE   B CG1 
4280 C  CG2 . ILE   B 23  ? 0.1708 0.1679 0.1846 -0.0129 0.0002  0.0059  23  ILE   B CG2 
4281 C  CD1 . ILE   B 23  ? 0.1745 0.1627 0.2131 -0.0047 0.0009  0.0198  23  ILE   B CD1 
4293 N  N   . VAL   B 24  ? 0.1594 0.1375 0.1900 -0.0096 -0.0080 0.0006  24  VAL   B N   
4294 C  CA  . VAL   B 24  ? 0.1559 0.1447 0.2071 -0.0051 -0.0165 -0.0006 24  VAL   B CA  
4295 C  C   . VAL   B 24  ? 0.1559 0.1487 0.2097 -0.0135 -0.0085 0.0005  24  VAL   B C   
4296 O  O   . VAL   B 24  ? 0.1561 0.1573 0.2186 -0.0154 -0.0057 0.0088  24  VAL   B O   
4297 C  CB  . VAL   B 24  ? 0.1678 0.1630 0.2235 0.0040  -0.0178 -0.0016 24  VAL   B CB  
4298 C  CG1 . VAL   B 24  ? 0.1728 0.1706 0.2458 -0.0087 -0.0210 -0.0003 24  VAL   B CG1 
4299 C  CG2 . VAL   B 24  ? 0.1756 0.1919 0.2198 0.0144  -0.0191 -0.0123 24  VAL   B CG2 
4309 N  N   . GLU   B 25  ? 0.1795 0.1637 0.2123 -0.0127 0.0074  -0.0031 25  GLU   B N   
4310 C  CA  . GLU   B 25  ? 0.1850 0.1888 0.2397 -0.0001 0.0222  -0.0075 25  GLU   B CA  
4311 C  C   . GLU   B 25  ? 0.1835 0.1779 0.2070 -0.0115 0.0161  0.0012  25  GLU   B C   
4312 O  O   . GLU   B 25  ? 0.1884 0.1927 0.2115 -0.0122 0.0198  0.0085  25  GLU   B O   
4313 C  CB  . GLU   B 25  ? 0.2178 0.2310 0.2987 0.0214  0.0424  -0.0052 25  GLU   B CB  
4314 C  CG  . GLU   B 25  ? 0.2591 0.2869 0.4120 0.0279  0.0430  -0.0108 25  GLU   B CG  
4315 C  CD  . GLU   B 25  ? 0.2959 0.3494 0.5146 0.0226  0.0350  -0.0130 25  GLU   B CD  
4316 O  OE1 . GLU   B 25  ? 0.3172 0.3708 0.5436 0.0264  0.0379  -0.0104 25  GLU   B OE1 
4317 O  OE2 . GLU   B 25  ? 0.3175 0.3665 0.5487 0.0205  0.0267  -0.0205 25  GLU   B OE2 
4324 N  N   A GLU   B 26  ? 0.1854 0.1716 0.1813 -0.0279 0.0095  -0.0065 26  GLU   B N   
4325 N  N   B GLU   B 26  ? 0.1837 0.1773 0.1965 -0.0216 0.0126  0.0021  26  GLU   B N   
4326 C  CA  A GLU   B 26  ? 0.1850 0.1772 0.1823 -0.0373 -0.0050 -0.0070 26  GLU   B CA  
4327 C  CA  B GLU   B 26  ? 0.1806 0.1873 0.2135 -0.0254 0.0020  0.0081  26  GLU   B CA  
4328 C  C   A GLU   B 26  ? 0.1675 0.1804 0.1811 -0.0288 0.0071  0.0098  26  GLU   B C   
4329 C  C   B GLU   B 26  ? 0.1648 0.1851 0.1939 -0.0224 0.0108  0.0177  26  GLU   B C   
4330 O  O   A GLU   B 26  ? 0.1803 0.2017 0.1924 -0.0259 0.0019  0.0178  26  GLU   B O   
4331 O  O   B GLU   B 26  ? 0.1767 0.2053 0.2006 -0.0193 0.0055  0.0252  26  GLU   B O   
4332 C  CB  A GLU   B 26  ? 0.2104 0.1865 0.1930 -0.0438 -0.0075 0.0018  26  GLU   B CB  
4333 C  CB  B GLU   B 26  ? 0.1984 0.2033 0.2534 -0.0242 0.0019  0.0235  26  GLU   B CB  
4334 C  CG  A GLU   B 26  ? 0.2419 0.1995 0.2230 -0.0451 -0.0020 -0.0110 26  GLU   B CG  
4335 C  CG  B GLU   B 26  ? 0.2190 0.2226 0.3106 -0.0170 0.0124  0.0204  26  GLU   B CG  
4336 C  CD  A GLU   B 26  ? 0.2596 0.2029 0.2163 -0.0537 0.0141  -0.0281 26  GLU   B CD  
4337 C  CD  B GLU   B 26  ? 0.2209 0.2250 0.3298 -0.0148 0.0319  0.0170  26  GLU   B CD  
4338 O  OE1 A GLU   B 26  ? 0.2665 0.1874 0.1931 -0.0475 0.0458  -0.0446 26  GLU   B OE1 
4339 O  OE1 B GLU   B 26  ? 0.2194 0.2239 0.3560 -0.0175 0.0677  0.0095  26  GLU   B OE1 
4340 O  OE2 A GLU   B 26  ? 0.2679 0.2228 0.2463 -0.0609 0.0164  -0.0062 26  GLU   B OE2 
4341 O  OE2 B GLU   B 26  ? 0.2178 0.2258 0.3270 -0.0064 0.0274  0.0065  26  GLU   B OE2 
4354 N  N   . ALA   B 27  ? 0.1535 0.1666 0.1823 -0.0225 0.0154  0.0161  27  ALA   B N   
4355 C  CA  . ALA   B 27  ? 0.1550 0.1627 0.1857 -0.0146 0.0087  0.0291  27  ALA   B CA  
4356 C  C   . ALA   B 27  ? 0.1603 0.1739 0.2086 -0.0136 0.0140  0.0413  27  ALA   B C   
4357 O  O   . ALA   B 27  ? 0.1688 0.1840 0.2212 -0.0062 0.0090  0.0482  27  ALA   B O   
4358 C  CB  . ALA   B 27  ? 0.1684 0.1513 0.1857 -0.0137 0.0074  0.0217  27  ALA   B CB  
4365 N  N   . LYS   B 28  ? 0.1534 0.1874 0.2545 -0.0202 0.0227  0.0603  28  LYS   B N   
4366 C  CA  . LYS   B 28  ? 0.1705 0.2294 0.2793 -0.0076 0.0461  0.0951  28  LYS   B CA  
4367 C  C   . LYS   B 28  ? 0.1913 0.2537 0.2578 -0.0011 0.0604  0.0825  28  LYS   B C   
4368 O  O   . LYS   B 28  ? 0.2148 0.2662 0.2729 -0.0031 0.0637  0.0764  28  LYS   B O   
4369 C  CB  . LYS   B 28  ? 0.1859 0.2639 0.3372 0.0081  0.0671  0.1179  28  LYS   B CB  
4370 C  CG  . LYS   B 28  ? 0.2115 0.3128 0.3784 0.0204  0.0678  0.1257  28  LYS   B CG  
4371 C  CD  . LYS   B 28  ? 0.2598 0.3742 0.4374 0.0323  0.0838  0.1225  28  LYS   B CD  
4372 C  CE  . LYS   B 28  ? 0.3114 0.4211 0.4856 0.0447  0.0864  0.1263  28  LYS   B CE  
4373 N  NZ  . LYS   B 28  ? 0.3355 0.4452 0.5018 0.0516  0.0848  0.1339  28  LYS   B NZ  
4387 N  N   . LYS   B 29  ? 0.2115 0.2795 0.2525 0.0209  0.0671  0.0713  29  LYS   B N   
4388 C  CA  . LYS   B 29  ? 0.2578 0.3153 0.2737 0.0221  0.0652  0.0732  29  LYS   B CA  
4389 C  C   . LYS   B 29  ? 0.2513 0.3197 0.2289 0.0184  0.0488  0.0833  29  LYS   B C   
4390 O  O   . LYS   B 29  ? 0.2711 0.3438 0.2364 0.0237  0.0447  0.0852  29  LYS   B O   
4391 C  CB  . LYS   B 29  ? 0.3167 0.3529 0.3650 0.0213  0.0716  0.0568  29  LYS   B CB  
4392 C  CG  . LYS   B 29  ? 0.3721 0.3866 0.4683 0.0190  0.0754  0.0507  29  LYS   B CG  
4393 C  CD  . LYS   B 29  ? 0.4184 0.4099 0.5436 0.0141  0.0865  0.0465  29  LYS   B CD  
4394 C  CE  . LYS   B 29  ? 0.4557 0.4272 0.5933 0.0105  0.0958  0.0412  29  LYS   B CE  
4395 N  NZ  . LYS   B 29  ? 0.4771 0.4347 0.6297 0.0090  0.0964  0.0369  29  LYS   B NZ  
4409 N  N   . VAL   B 30  ? 0.2201 0.2987 0.2088 0.0038  0.0425  0.0853  30  VAL   B N   
4410 C  CA  . VAL   B 30  ? 0.2059 0.2879 0.2607 -0.0120 0.0040  0.0838  30  VAL   B CA  
4411 C  C   . VAL   B 30  ? 0.1838 0.2811 0.2544 -0.0120 0.0119  0.1005  30  VAL   B C   
4412 O  O   . VAL   B 30  ? 0.1985 0.2975 0.2588 -0.0027 0.0070  0.1133  30  VAL   B O   
4413 C  CB  . VAL   B 30  ? 0.2110 0.2800 0.3203 -0.0286 -0.0302 0.0761  30  VAL   B CB  
4414 C  CG1 . VAL   B 30  ? 0.2189 0.2861 0.3309 -0.0297 -0.0177 0.0684  30  VAL   B CG1 
4415 C  CG2 . VAL   B 30  ? 0.2259 0.2801 0.3431 -0.0334 -0.0501 0.0608  30  VAL   B CG2 
4425 N  N   . LYS   B 31  ? 0.1692 0.2419 0.2916 -0.0296 0.0123  0.1011  31  LYS   B N   
4426 C  CA  . LYS   B 31  ? 0.1602 0.2319 0.3321 -0.0386 0.0014  0.1047  31  LYS   B CA  
4427 C  C   . LYS   B 31  ? 0.1580 0.1932 0.2895 -0.0329 -0.0199 0.0914  31  LYS   B C   
4428 O  O   . LYS   B 31  ? 0.1625 0.2070 0.3054 -0.0257 -0.0226 0.1053  31  LYS   B O   
4429 C  CB  . LYS   B 31  ? 0.1794 0.2787 0.3907 -0.0354 0.0265  0.1215  31  LYS   B CB  
4430 C  CG  . LYS   B 31  ? 0.2148 0.3265 0.4307 -0.0307 0.0431  0.1204  31  LYS   B CG  
4431 C  CD  . LYS   B 31  ? 0.2591 0.3801 0.4787 -0.0266 0.0438  0.1091  31  LYS   B CD  
4432 C  CE  . LYS   B 31  ? 0.2865 0.4193 0.5255 -0.0238 0.0360  0.0973  31  LYS   B CE  
4433 N  NZ  . LYS   B 31  ? 0.3196 0.4472 0.5405 -0.0163 0.0238  0.0886  31  LYS   B NZ  
4447 N  N   . PRO   B 32  ? 0.1715 0.1578 0.2138 -0.0328 -0.0425 0.0521  32  PRO   B N   
4448 C  CA  . PRO   B 32  ? 0.1803 0.1545 0.1730 -0.0360 -0.0453 0.0284  32  PRO   B CA  
4449 C  C   . PRO   B 32  ? 0.1840 0.1462 0.1789 -0.0426 -0.0489 0.0397  32  PRO   B C   
4450 O  O   . PRO   B 32  ? 0.1942 0.1496 0.2120 -0.0424 -0.0667 0.0374  32  PRO   B O   
4451 C  CB  . PRO   B 32  ? 0.1939 0.1473 0.1759 -0.0404 -0.0381 0.0188  32  PRO   B CB  
4452 C  CG  . PRO   B 32  ? 0.2071 0.1392 0.1793 -0.0380 -0.0496 0.0221  32  PRO   B CG  
4453 C  CD  . PRO   B 32  ? 0.1914 0.1456 0.2012 -0.0268 -0.0555 0.0260  32  PRO   B CD  
4461 N  N   . THR   B 33  ? 0.1856 0.1371 0.1693 -0.0357 -0.0477 0.0175  33  THR   B N   
4462 C  CA  . THR   B 33  ? 0.1946 0.1455 0.1654 -0.0368 -0.0399 0.0208  33  THR   B CA  
4463 C  C   . THR   B 33  ? 0.1959 0.1337 0.1552 -0.0380 -0.0425 0.0156  33  THR   B C   
4464 O  O   . THR   B 33  ? 0.2242 0.1339 0.1683 -0.0464 -0.0567 0.0210  33  THR   B O   
4465 C  CB  . THR   B 33  ? 0.2007 0.1529 0.1635 -0.0180 -0.0493 0.0255  33  THR   B CB  
4466 O  OG1 . THR   B 33  ? 0.1938 0.1604 0.1750 -0.0230 -0.0430 0.0287  33  THR   B OG1 
4467 C  CG2 . THR   B 33  ? 0.2239 0.1579 0.1876 -0.0117 -0.0467 0.0236  33  THR   B CG2 
4475 N  N   . VAL   B 34  ? 0.1795 0.1322 0.1432 -0.0384 -0.0364 0.0080  34  VAL   B N   
4476 C  CA  . VAL   B 34  ? 0.1652 0.1310 0.1324 -0.0256 -0.0264 0.0053  34  VAL   B CA  
4477 C  C   . VAL   B 34  ? 0.1478 0.1233 0.1252 -0.0281 -0.0174 0.0093  34  VAL   B C   
4478 O  O   . VAL   B 34  ? 0.1711 0.1271 0.1407 -0.0258 -0.0320 0.0087  34  VAL   B O   
4479 C  CB  . VAL   B 34  ? 0.1692 0.1407 0.1689 -0.0079 -0.0272 0.0011  34  VAL   B CB  
4480 C  CG1 . VAL   B 34  ? 0.1626 0.1560 0.1666 -0.0093 -0.0112 0.0000  34  VAL   B CG1 
4481 C  CG2 . VAL   B 34  ? 0.1730 0.1431 0.1939 -0.0023 -0.0217 0.0028  34  VAL   B CG2 
4491 N  N   . VAL   B 35  ? 0.1426 0.1226 0.1280 -0.0245 -0.0119 0.0080  35  VAL   B N   
4492 C  CA  . VAL   B 35  ? 0.1392 0.1202 0.1281 -0.0208 -0.0090 0.0027  35  VAL   B CA  
4493 C  C   . VAL   B 35  ? 0.1282 0.1120 0.1283 -0.0178 -0.0139 0.0041  35  VAL   B C   
4494 O  O   . VAL   B 35  ? 0.1346 0.1222 0.1373 -0.0224 -0.0016 -0.0015 35  VAL   B O   
4495 C  CB  . VAL   B 35  ? 0.1359 0.1421 0.1311 -0.0191 0.0052  0.0058  35  VAL   B CB  
4496 C  CG1 . VAL   B 35  ? 0.1316 0.1507 0.1527 -0.0210 0.0036  0.0062  35  VAL   B CG1 
4497 C  CG2 . VAL   B 35  ? 0.1374 0.1427 0.1491 -0.0136 -0.0008 -0.0083 35  VAL   B CG2 
4507 N  N   . VAL   B 36  ? 0.1320 0.1179 0.1269 -0.0158 -0.0154 0.0069  36  VAL   B N   
4508 C  CA  . VAL   B 36  ? 0.1255 0.1168 0.1260 -0.0141 -0.0065 0.0042  36  VAL   B CA  
4509 C  C   . VAL   B 36  ? 0.1215 0.1177 0.1170 -0.0110 -0.0024 0.0026  36  VAL   B C   
4510 O  O   . VAL   B 36  ? 0.1317 0.1271 0.1429 -0.0099 -0.0012 -0.0060 36  VAL   B O   
4511 C  CB  . VAL   B 36  ? 0.1267 0.1203 0.1311 -0.0153 -0.0088 0.0067  36  VAL   B CB  
4512 C  CG1 . VAL   B 36  ? 0.1259 0.1316 0.1386 -0.0177 -0.0068 0.0106  36  VAL   B CG1 
4513 C  CG2 . VAL   B 36  ? 0.1391 0.1267 0.1406 -0.0185 -0.0131 0.0069  36  VAL   B CG2 
4523 N  N   . ASN   B 37  ? 0.1259 0.1223 0.1171 0.0015  -0.0059 0.0041  37  ASN   B N   
4524 C  CA  . ASN   B 37  ? 0.1269 0.1189 0.1306 0.0045  -0.0094 0.0050  37  ASN   B CA  
4525 C  C   . ASN   B 37  ? 0.1243 0.1224 0.1215 0.0001  -0.0111 0.0047  37  ASN   B C   
4526 O  O   . ASN   B 37  ? 0.1293 0.1248 0.1419 0.0029  -0.0008 0.0081  37  ASN   B O   
4527 C  CB  . ASN   B 37  ? 0.1306 0.1229 0.1284 0.0007  -0.0130 0.0046  37  ASN   B CB  
4528 C  CG  . ASN   B 37  ? 0.1303 0.1290 0.1352 0.0008  -0.0091 0.0008  37  ASN   B CG  
4529 O  OD1 . ASN   B 37  ? 0.1353 0.1332 0.1541 0.0093  -0.0095 0.0004  37  ASN   B OD1 
4530 N  ND2 . ASN   B 37  ? 0.1325 0.1235 0.1450 -0.0019 -0.0127 0.0041  37  ASN   B ND2 
4537 N  N   . ALA   B 38  ? 0.1353 0.1228 0.1262 0.0086  -0.0012 0.0051  38  ALA   B N   
4538 C  CA  . ALA   B 38  ? 0.1484 0.1278 0.1314 0.0029  0.0038  0.0136  38  ALA   B CA  
4539 C  C   . ALA   B 38  ? 0.1408 0.1265 0.1289 0.0007  0.0056  0.0116  38  ALA   B C   
4540 O  O   . ALA   B 38  ? 0.1472 0.1350 0.1418 0.0072  -0.0014 0.0060  38  ALA   B O   
4541 C  CB  . ALA   B 38  ? 0.1683 0.1350 0.1522 -0.0078 0.0138  0.0128  38  ALA   B CB  
4547 N  N   . ALA   B 39  ? 0.1355 0.1274 0.1282 0.0065  -0.0002 0.0093  39  ALA   B N   
4548 C  CA  . ALA   B 39  ? 0.1479 0.1293 0.1214 0.0072  -0.0098 0.0016  39  ALA   B CA  
4549 C  C   . ALA   B 39  ? 0.1511 0.1409 0.1139 0.0132  -0.0077 0.0047  39  ALA   B C   
4550 O  O   . ALA   B 39  ? 0.1506 0.1479 0.1410 0.0012  0.0021  0.0107  39  ALA   B O   
4551 C  CB  . ALA   B 39  ? 0.1518 0.1367 0.1354 -0.0023 -0.0026 0.0015  39  ALA   B CB  
4557 N  N   . ASN   B 40  ? 0.1527 0.1612 0.1205 0.0029  0.0003  -0.0023 40  ASN   B N   
4558 C  CA  . ASN   B 40  ? 0.1564 0.1649 0.1355 0.0055  -0.0049 -0.0056 40  ASN   B CA  
4559 C  C   . ASN   B 40  ? 0.1635 0.1638 0.1167 0.0061  -0.0062 0.0013  40  ASN   B C   
4560 O  O   . ASN   B 40  ? 0.1555 0.1519 0.1280 0.0077  -0.0134 0.0031  40  ASN   B O   
4561 C  CB  . ASN   B 40  ? 0.1709 0.1619 0.1668 0.0120  -0.0177 0.0082  40  ASN   B CB  
4562 C  CG  . ASN   B 40  ? 0.1760 0.1701 0.1950 0.0103  -0.0282 0.0190  40  ASN   B CG  
4563 O  OD1 . ASN   B 40  ? 0.1744 0.1634 0.2781 0.0038  -0.0326 0.0214  40  ASN   B OD1 
4564 N  ND2 . ASN   B 40  ? 0.1792 0.1720 0.1837 0.0036  -0.0248 0.0185  40  ASN   B ND2 
4571 N  N   . VAL   B 41  ? 0.1730 0.1691 0.1225 0.0124  0.0006  0.0013  41  VAL   B N   
4572 C  CA  . VAL   B 41  ? 0.1802 0.1800 0.1277 0.0115  0.0012  -0.0125 41  VAL   B CA  
4573 C  C   . VAL   B 41  ? 0.1773 0.1783 0.1136 0.0197  -0.0061 -0.0129 41  VAL   B C   
4574 O  O   . VAL   B 41  ? 0.1762 0.1727 0.1430 0.0168  -0.0141 -0.0136 41  VAL   B O   
4575 C  CB  . VAL   B 41  ? 0.1984 0.2009 0.1476 -0.0020 0.0194  -0.0216 41  VAL   B CB  
4576 C  CG1 . VAL   B 41  ? 0.1919 0.2061 0.1592 -0.0069 0.0345  -0.0225 41  VAL   B CG1 
4577 C  CG2 . VAL   B 41  ? 0.2121 0.2227 0.1534 -0.0082 0.0279  -0.0165 41  VAL   B CG2 
4587 N  N   . TYR   B 42  ? 0.1856 0.1793 0.1257 0.0182  -0.0126 -0.0019 42  TYR   B N   
4588 C  CA  . TYR   B 42  ? 0.1928 0.1867 0.1334 0.0174  -0.0260 -0.0152 42  TYR   B CA  
4589 C  C   . TYR   B 42  ? 0.1711 0.1675 0.1486 0.0204  -0.0161 -0.0109 42  TYR   B C   
4590 O  O   . TYR   B 42  ? 0.1716 0.1743 0.1780 0.0152  -0.0231 -0.0199 42  TYR   B O   
4591 C  CB  . TYR   B 42  ? 0.2160 0.2165 0.1453 0.0092  -0.0341 -0.0002 42  TYR   B CB  
4592 C  CG  . TYR   B 42  ? 0.2142 0.2359 0.1433 -0.0053 -0.0341 0.0049  42  TYR   B CG  
4593 C  CD1 . TYR   B 42  ? 0.2089 0.2401 0.1115 -0.0072 -0.0169 -0.0036 42  TYR   B CD1 
4594 C  CD2 . TYR   B 42  ? 0.2297 0.2481 0.1880 -0.0042 -0.0140 0.0213  42  TYR   B CD2 
4595 C  CE1 . TYR   B 42  ? 0.2291 0.2610 0.1196 0.0031  -0.0095 0.0023  42  TYR   B CE1 
4596 C  CE2 . TYR   B 42  ? 0.2347 0.2643 0.1856 0.0004  0.0124  0.0321  42  TYR   B CE2 
4597 C  CZ  . TYR   B 42  ? 0.2461 0.2855 0.1598 0.0190  0.0129  0.0174  42  TYR   B CZ  
4598 O  OH  . TYR   B 42  ? 0.2796 0.3176 0.2131 0.0416  0.0189  0.0261  42  TYR   B OH  
4608 N  N   . LEU   B 43  ? 0.1588 0.1490 0.1381 0.0111  -0.0155 -0.0091 43  LEU   B N   
4609 C  CA  . LEU   B 43  ? 0.1613 0.1520 0.1363 0.0028  -0.0167 0.0015  43  LEU   B CA  
4610 C  C   . LEU   B 43  ? 0.1705 0.1506 0.1377 0.0022  -0.0146 0.0032  43  LEU   B C   
4611 O  O   . LEU   B 43  ? 0.1654 0.1553 0.1656 0.0072  -0.0259 0.0083  43  LEU   B O   
4612 C  CB  . LEU   B 43  ? 0.1554 0.1469 0.1434 -0.0001 -0.0231 -0.0040 43  LEU   B CB  
4613 C  CG  . LEU   B 43  ? 0.1602 0.1444 0.1527 0.0012  -0.0246 -0.0036 43  LEU   B CG  
4614 C  CD1 . LEU   B 43  ? 0.1703 0.1517 0.1819 -0.0055 -0.0446 -0.0012 43  LEU   B CD1 
4615 C  CD2 . LEU   B 43  ? 0.1581 0.1451 0.1599 -0.0080 -0.0272 -0.0060 43  LEU   B CD2 
4627 N  N   . LYS   B 44  ? 0.1625 0.1504 0.1448 0.0061  -0.0075 -0.0069 44  LYS   B N   
4628 C  CA  . LYS   B 44  ? 0.1748 0.1656 0.1387 0.0121  -0.0124 -0.0002 44  LYS   B CA  
4629 C  C   . LYS   B 44  ? 0.1576 0.1545 0.1356 0.0135  -0.0131 0.0052  44  LYS   B C   
4630 O  O   . LYS   B 44  ? 0.1807 0.1508 0.1676 0.0089  -0.0052 0.0045  44  LYS   B O   
4631 C  CB  . LYS   B 44  ? 0.2091 0.1860 0.1488 0.0162  -0.0290 0.0036  44  LYS   B CB  
4632 C  CG  . LYS   B 44  ? 0.2489 0.2096 0.1812 0.0119  -0.0620 0.0087  44  LYS   B CG  
4633 C  CD  . LYS   B 44  ? 0.2864 0.2256 0.2477 -0.0018 -0.0686 0.0003  44  LYS   B CD  
4634 C  CE  . LYS   B 44  ? 0.3204 0.2501 0.2888 -0.0094 -0.0768 0.0103  44  LYS   B CE  
4635 N  NZ  . LYS   B 44  ? 0.3325 0.2624 0.3219 -0.0072 -0.0857 0.0333  44  LYS   B NZ  
4649 N  N   . HIS   B 45  ? 0.1508 0.1648 0.1414 0.0065  -0.0109 0.0094  45  HIS   B N   
4650 C  CA  . HIS   B 45  ? 0.1555 0.1578 0.1415 0.0098  -0.0086 0.0024  45  HIS   B CA  
4651 C  C   . HIS   B 45  ? 0.1806 0.1727 0.1883 0.0175  -0.0183 -0.0042 45  HIS   B C   
4652 O  O   . HIS   B 45  ? 0.1865 0.2029 0.2333 0.0421  -0.0011 -0.0008 45  HIS   B O   
4653 C  CB  . HIS   B 45  ? 0.1502 0.1610 0.1427 0.0033  -0.0086 -0.0048 45  HIS   B CB  
4654 C  CG  . HIS   B 45  ? 0.1511 0.1544 0.1368 -0.0038 -0.0042 -0.0050 45  HIS   B CG  
4655 N  ND1 . HIS   B 45  ? 0.1587 0.1476 0.1513 0.0026  -0.0141 -0.0073 45  HIS   B ND1 
4656 C  CD2 . HIS   B 45  ? 0.1598 0.1560 0.1597 -0.0099 -0.0135 -0.0011 45  HIS   B CD2 
4657 C  CE1 . HIS   B 45  ? 0.1707 0.1402 0.1274 0.0026  -0.0228 -0.0053 45  HIS   B CE1 
4658 N  NE2 . HIS   B 45  ? 0.1728 0.1460 0.1386 -0.0035 -0.0130 -0.0064 45  HIS   B NE2 
4666 N  N   A GLY   B 46  ? 0.1912 0.1664 0.2173 0.0194  -0.0327 0.0046  46  GLY   B N   
4667 N  N   B GLY   B 46  ? 0.1934 0.1707 0.2089 0.0184  -0.0304 0.0105  46  GLY   B N   
4668 C  CA  A GLY   B 46  ? 0.2034 0.1777 0.2600 0.0163  -0.0410 0.0051  46  GLY   B CA  
4669 C  CA  B GLY   B 46  ? 0.2084 0.1858 0.2406 0.0145  -0.0397 0.0153  46  GLY   B CA  
4670 C  C   A GLY   B 46  ? 0.2049 0.1929 0.3025 0.0207  -0.0356 0.0053  46  GLY   B C   
4671 C  C   B GLY   B 46  ? 0.2142 0.2049 0.2781 0.0177  -0.0354 0.0210  46  GLY   B C   
4672 O  O   A GLY   B 46  ? 0.2054 0.1990 0.3785 0.0317  -0.0227 -0.0136 46  GLY   B O   
4673 O  O   B GLY   B 46  ? 0.2249 0.2221 0.3149 0.0239  -0.0301 0.0274  46  GLY   B O   
4680 N  N   . GLY   B 47  ? 0.2081 0.2049 0.2757 0.0073  -0.0235 0.0041  47  GLY   B N   
4681 C  CA  . GLY   B 47  ? 0.1914 0.1796 0.2369 0.0055  -0.0171 0.0077  47  GLY   B CA  
4682 C  C   . GLY   B 47  ? 0.1700 0.1567 0.1879 0.0055  -0.0016 0.0114  47  GLY   B C   
4683 O  O   . GLY   B 47  ? 0.1828 0.1421 0.2004 0.0054  -0.0064 0.0109  47  GLY   B O   
4688 N  N   . GLY   B 48  ? 0.1516 0.1506 0.1851 0.0051  -0.0095 0.0199  48  GLY   B N   
4689 C  CA  . GLY   B 48  ? 0.1511 0.1478 0.1862 0.0010  0.0046  0.0055  48  GLY   B CA  
4690 C  C   . GLY   B 48  ? 0.1476 0.1395 0.1826 -0.0022 0.0094  0.0082  48  GLY   B C   
4691 O  O   . GLY   B 48  ? 0.1435 0.1400 0.2050 0.0034  -0.0063 0.0046  48  GLY   B O   
4695 N  N   . VAL   B 49  ? 0.1489 0.1422 0.1711 0.0125  0.0063  0.0071  49  VAL   B N   
4696 C  CA  . VAL   B 49  ? 0.1514 0.1556 0.1550 0.0113  -0.0078 -0.0025 49  VAL   B CA  
4697 C  C   . VAL   B 49  ? 0.1404 0.1447 0.1325 0.0097  -0.0079 0.0100  49  VAL   B C   
4698 O  O   . VAL   B 49  ? 0.1496 0.1466 0.1534 0.0059  -0.0047 0.0062  49  VAL   B O   
4699 C  CB  . VAL   B 49  ? 0.1528 0.1721 0.1877 0.0039  -0.0196 0.0032  49  VAL   B CB  
4700 C  CG1 . VAL   B 49  ? 0.1499 0.1793 0.1800 0.0056  -0.0318 0.0019  49  VAL   B CG1 
4701 C  CG2 . VAL   B 49  ? 0.1688 0.1830 0.2102 -0.0084 -0.0360 -0.0068 49  VAL   B CG2 
4711 N  N   . ALA   B 50  ? 0.1375 0.1416 0.1371 0.0025  0.0016  0.0083  50  ALA   B N   
4712 C  CA  . ALA   B 50  ? 0.1393 0.1321 0.1391 0.0084  -0.0027 0.0078  50  ALA   B CA  
4713 C  C   . ALA   B 50  ? 0.1434 0.1384 0.1472 0.0091  -0.0038 0.0086  50  ALA   B C   
4714 O  O   . ALA   B 50  ? 0.1445 0.1368 0.1404 0.0081  -0.0028 0.0025  50  ALA   B O   
4715 C  CB  . ALA   B 50  ? 0.1473 0.1365 0.1449 -0.0001 -0.0036 0.0085  50  ALA   B CB  
4721 N  N   . GLY   B 51  ? 0.1372 0.1501 0.1535 0.0160  -0.0162 0.0075  51  GLY   B N   
4722 C  CA  . GLY   B 51  ? 0.1427 0.1551 0.1723 0.0231  -0.0157 0.0115  51  GLY   B CA  
4723 C  C   . GLY   B 51  ? 0.1441 0.1518 0.1673 0.0214  -0.0113 0.0053  51  GLY   B C   
4724 O  O   . GLY   B 51  ? 0.1460 0.1607 0.1922 0.0089  -0.0072 -0.0002 51  GLY   B O   
4728 N  N   . ALA   B 52  ? 0.1462 0.1428 0.1614 0.0177  -0.0056 0.0109  52  ALA   B N   
4729 C  CA  . ALA   B 52  ? 0.1499 0.1504 0.1660 0.0137  0.0038  -0.0010 52  ALA   B CA  
4730 C  C   . ALA   B 52  ? 0.1408 0.1483 0.1470 0.0059  0.0019  0.0014  52  ALA   B C   
4731 O  O   . ALA   B 52  ? 0.1408 0.1524 0.1768 0.0108  0.0020  0.0066  52  ALA   B O   
4732 C  CB  . ALA   B 52  ? 0.1637 0.1503 0.1695 0.0088  0.0142  -0.0003 52  ALA   B CB  
4738 N  N   . LEU   B 53  ? 0.1313 0.1492 0.1489 0.0144  -0.0001 0.0065  53  LEU   B N   
4739 C  CA  . LEU   B 53  ? 0.1381 0.1565 0.1440 0.0120  -0.0067 0.0050  53  LEU   B CA  
4740 C  C   . LEU   B 53  ? 0.1384 0.1440 0.1518 0.0105  -0.0037 0.0033  53  LEU   B C   
4741 O  O   . LEU   B 53  ? 0.1446 0.1551 0.1626 0.0010  0.0029  0.0186  53  LEU   B O   
4742 C  CB  . LEU   B 53  ? 0.1332 0.1642 0.1547 0.0140  -0.0043 0.0126  53  LEU   B CB  
4743 C  CG  . LEU   B 53  ? 0.1334 0.1716 0.1602 0.0038  -0.0067 0.0224  53  LEU   B CG  
4744 C  CD1 . LEU   B 53  ? 0.1453 0.1927 0.1815 0.0105  -0.0115 0.0071  53  LEU   B CD1 
4745 C  CD2 . LEU   B 53  ? 0.1541 0.1956 0.1875 -0.0055 -0.0163 -0.0077 53  LEU   B CD2 
4757 N  N   . ASN   B 54  ? 0.1372 0.1334 0.1461 0.0069  -0.0005 0.0096  54  ASN   B N   
4758 C  CA  . ASN   B 54  ? 0.1447 0.1478 0.1519 0.0062  -0.0083 -0.0019 54  ASN   B CA  
4759 C  C   . ASN   B 54  ? 0.1434 0.1502 0.1807 0.0055  0.0015  -0.0026 54  ASN   B C   
4760 O  O   . ASN   B 54  ? 0.1371 0.1514 0.1939 -0.0014 0.0053  -0.0045 54  ASN   B O   
4761 C  CB  . ASN   B 54  ? 0.1478 0.1615 0.1623 0.0085  -0.0012 -0.0005 54  ASN   B CB  
4762 C  CG  . ASN   B 54  ? 0.1417 0.1675 0.1638 0.0056  -0.0046 -0.0033 54  ASN   B CG  
4763 O  OD1 . ASN   B 54  ? 0.1413 0.1668 0.1755 0.0029  -0.0163 -0.0161 54  ASN   B OD1 
4764 N  ND2 . ASN   B 54  ? 0.1538 0.1878 0.2003 -0.0001 -0.0253 0.0135  54  ASN   B ND2 
4771 N  N   . LYS   B 55  ? 0.1369 0.1582 0.1914 0.0105  0.0036  0.0059  55  LYS   B N   
4772 C  CA  . LYS   B 55  ? 0.1445 0.1760 0.2069 0.0219  0.0015  0.0048  55  LYS   B CA  
4773 C  C   . LYS   B 55  ? 0.1405 0.1714 0.2087 0.0180  0.0066  -0.0046 55  LYS   B C   
4774 O  O   . LYS   B 55  ? 0.1332 0.1832 0.2219 0.0136  0.0047  -0.0023 55  LYS   B O   
4775 C  CB  . LYS   B 55  ? 0.1536 0.1878 0.2462 0.0330  0.0134  0.0113  55  LYS   B CB  
4776 C  CG  . LYS   B 55  ? 0.2013 0.2191 0.3275 0.0381  0.0274  0.0251  55  LYS   B CG  
4777 C  CD  . LYS   B 55  ? 0.2421 0.2442 0.3946 0.0494  0.0383  0.0333  55  LYS   B CD  
4778 C  CE  . LYS   B 55  ? 0.2713 0.2680 0.4652 0.0475  0.0526  0.0363  55  LYS   B CE  
4779 N  NZ  . LYS   B 55  ? 0.2792 0.2849 0.4971 0.0452  0.0391  0.0462  55  LYS   B NZ  
4793 N  N   . ALA   B 56  ? 0.1398 0.1702 0.1874 0.0114  0.0020  -0.0066 56  ALA   B N   
4794 C  CA  . ALA   B 56  ? 0.1553 0.1874 0.1845 0.0076  0.0056  -0.0001 56  ALA   B CA  
4795 C  C   . ALA   B 56  ? 0.1578 0.1860 0.1779 0.0041  0.0126  0.0037  56  ALA   B C   
4796 O  O   . ALA   B 56  ? 0.1705 0.1954 0.2002 0.0036  0.0361  0.0050  56  ALA   B O   
4797 C  CB  . ALA   B 56  ? 0.1644 0.2027 0.1810 -0.0111 0.0019  -0.0042 56  ALA   B CB  
4803 N  N   . THR   B 57  ? 0.1537 0.1787 0.1830 0.0028  0.0153  0.0029  57  THR   B N   
4804 C  CA  . THR   B 57  ? 0.1519 0.1768 0.1795 -0.0030 0.0213  0.0095  57  THR   B CA  
4805 C  C   . THR   B 57  ? 0.1488 0.1850 0.1903 -0.0016 0.0199  0.0032  57  THR   B C   
4806 O  O   . THR   B 57  ? 0.1568 0.1854 0.2065 -0.0147 0.0142  0.0042  57  THR   B O   
4807 C  CB  . THR   B 57  ? 0.1603 0.1624 0.1617 -0.0013 0.0153  0.0060  57  THR   B CB  
4808 O  OG1 . THR   B 57  ? 0.1561 0.1530 0.1813 -0.0037 0.0153  0.0027  57  THR   B OG1 
4809 C  CG2 . THR   B 57  ? 0.1531 0.1697 0.1706 -0.0014 0.0109  0.0043  57  THR   B CG2 
4817 N  N   . ASN   B 58  ? 0.1394 0.2022 0.2187 -0.0073 0.0074  -0.0086 58  ASN   B N   
4818 C  CA  . ASN   B 58  ? 0.1570 0.2351 0.2581 -0.0206 0.0311  -0.0065 58  ASN   B CA  
4819 C  C   . ASN   B 58  ? 0.1424 0.2192 0.2218 -0.0146 0.0015  -0.0109 58  ASN   B C   
4820 O  O   . ASN   B 58  ? 0.1514 0.2294 0.2326 -0.0188 0.0011  -0.0185 58  ASN   B O   
4821 C  CB  . ASN   B 58  ? 0.2410 0.3008 0.3759 -0.0332 0.0740  0.0026  58  ASN   B CB  
4822 C  CG  . ASN   B 58  ? 0.3574 0.3841 0.5252 -0.0368 0.0955  0.0243  58  ASN   B CG  
4823 O  OD1 . ASN   B 58  ? 0.3939 0.4049 0.5793 -0.0390 0.1010  0.0303  58  ASN   B OD1 
4824 N  ND2 . ASN   B 58  ? 0.3947 0.4058 0.5740 -0.0381 0.1056  0.0299  58  ASN   B ND2 
4831 N  N   . ASN   B 59  ? 0.1439 0.2056 0.1949 -0.0042 -0.0032 0.0000  59  ASN   B N   
4832 C  CA  . ASN   B 59  ? 0.1466 0.2050 0.1936 -0.0044 -0.0141 0.0123  59  ASN   B CA  
4833 C  C   . ASN   B 59  ? 0.1380 0.1932 0.1915 -0.0126 -0.0134 0.0015  59  ASN   B C   
4834 O  O   . ASN   B 59  ? 0.1466 0.1927 0.1958 -0.0100 -0.0110 0.0022  59  ASN   B O   
4835 C  CB  . ASN   B 59  ? 0.1585 0.2218 0.2117 0.0016  -0.0299 0.0100  59  ASN   B CB  
4836 C  CG  . ASN   B 59  ? 0.1699 0.2382 0.2226 0.0046  -0.0380 0.0080  59  ASN   B CG  
4837 O  OD1 . ASN   B 59  ? 0.1748 0.2445 0.2167 0.0051  -0.0188 0.0204  59  ASN   B OD1 
4838 N  ND2 . ASN   B 59  ? 0.1774 0.2489 0.2308 -0.0038 -0.0393 -0.0012 59  ASN   B ND2 
4845 N  N   . ALA   B 60  ? 0.1426 0.1829 0.1926 -0.0101 -0.0001 -0.0016 60  ALA   B N   
4846 C  CA  . ALA   B 60  ? 0.1518 0.1693 0.1896 -0.0127 -0.0035 0.0066  60  ALA   B CA  
4847 C  C   . ALA   B 60  ? 0.1508 0.1584 0.1764 -0.0056 -0.0045 0.0062  60  ALA   B C   
4848 O  O   . ALA   B 60  ? 0.1539 0.1609 0.1934 -0.0100 0.0005  -0.0058 60  ALA   B O   
4849 C  CB  . ALA   B 60  ? 0.1659 0.1689 0.2192 -0.0115 0.0018  0.0099  60  ALA   B CB  
4855 N  N   . MET   B 61  ? 0.1407 0.1498 0.1780 -0.0081 -0.0003 0.0067  61  MET   B N   
4856 C  CA  . MET   B 61  ? 0.1402 0.1471 0.1635 -0.0092 -0.0156 0.0046  61  MET   B CA  
4857 C  C   . MET   B 61  ? 0.1422 0.1465 0.1647 -0.0132 -0.0142 0.0074  61  MET   B C   
4858 O  O   . MET   B 61  ? 0.1479 0.1463 0.1579 -0.0006 -0.0101 -0.0066 61  MET   B O   
4859 C  CB  . MET   B 61  ? 0.1366 0.1492 0.1559 0.0013  -0.0109 -0.0032 61  MET   B CB  
4860 C  CG  . MET   B 61  ? 0.1354 0.1477 0.1449 0.0012  -0.0080 0.0023  61  MET   B CG  
4861 S  SD  . MET   B 61  ? 0.1394 0.1496 0.1786 -0.0023 -0.0041 -0.0076 61  MET   B SD  
4862 C  CE  . MET   B 61  ? 0.1469 0.1678 0.1947 -0.0011 0.0028  -0.0167 61  MET   B CE  
4872 N  N   . GLN   B 62  ? 0.1461 0.1510 0.1481 -0.0046 -0.0185 -0.0005 62  GLN   B N   
4873 C  CA  . GLN   B 62  ? 0.1462 0.1573 0.1558 0.0016  -0.0243 -0.0029 62  GLN   B CA  
4874 C  C   . GLN   B 62  ? 0.1448 0.1619 0.1603 0.0037  -0.0237 -0.0045 62  GLN   B C   
4875 O  O   . GLN   B 62  ? 0.1577 0.1594 0.1720 -0.0015 -0.0294 -0.0171 62  GLN   B O   
4876 C  CB  . GLN   B 62  ? 0.1500 0.1625 0.1608 0.0003  -0.0144 0.0020  62  GLN   B CB  
4877 C  CG  . GLN   B 62  ? 0.1539 0.1679 0.1641 0.0016  -0.0212 -0.0040 62  GLN   B CG  
4878 C  CD  . GLN   B 62  ? 0.1488 0.1623 0.1638 0.0040  -0.0196 0.0111  62  GLN   B CD  
4879 O  OE1 . GLN   B 62  ? 0.1536 0.1580 0.1784 0.0010  -0.0232 -0.0019 62  GLN   B OE1 
4880 N  NE2 . GLN   B 62  ? 0.1501 0.1649 0.1702 0.0023  -0.0223 -0.0052 62  GLN   B NE2 
4889 N  N   . VAL   B 63  ? 0.1456 0.1648 0.1849 -0.0053 -0.0225 -0.0061 63  VAL   B N   
4890 C  CA  . VAL   B 63  ? 0.1576 0.1682 0.2007 -0.0129 -0.0294 -0.0071 63  VAL   B CA  
4891 C  C   . VAL   B 63  ? 0.1578 0.1592 0.1781 -0.0208 -0.0325 -0.0123 63  VAL   B C   
4892 O  O   . VAL   B 63  ? 0.1699 0.1552 0.1996 -0.0124 -0.0417 -0.0093 63  VAL   B O   
4893 C  CB  . VAL   B 63  ? 0.1584 0.1820 0.2369 -0.0170 -0.0261 -0.0099 63  VAL   B CB  
4894 C  CG1 . VAL   B 63  ? 0.1658 0.1843 0.2548 -0.0272 -0.0194 -0.0110 63  VAL   B CG1 
4895 C  CG2 . VAL   B 63  ? 0.1531 0.2001 0.2441 -0.0149 -0.0321 -0.0121 63  VAL   B CG2 
4905 N  N   . GLU   B 64  ? 0.1564 0.1515 0.1728 -0.0098 -0.0274 -0.0110 64  GLU   B N   
4906 C  CA  . GLU   B 64  ? 0.1546 0.1423 0.1745 -0.0101 -0.0299 -0.0036 64  GLU   B CA  
4907 C  C   . GLU   B 64  ? 0.1499 0.1427 0.1678 -0.0042 -0.0325 -0.0113 64  GLU   B C   
4908 O  O   . GLU   B 64  ? 0.1639 0.1521 0.1635 -0.0115 -0.0278 -0.0137 64  GLU   B O   
4909 C  CB  . GLU   B 64  ? 0.1546 0.1486 0.1654 -0.0164 -0.0240 0.0036  64  GLU   B CB  
4910 C  CG  . GLU   B 64  ? 0.1614 0.1571 0.1708 -0.0213 -0.0293 -0.0026 64  GLU   B CG  
4911 C  CD  . GLU   B 64  ? 0.1665 0.1737 0.1722 -0.0270 -0.0274 -0.0047 64  GLU   B CD  
4912 O  OE1 . GLU   B 64  ? 0.1689 0.1890 0.1849 -0.0280 -0.0162 -0.0284 64  GLU   B OE1 
4913 O  OE2 . GLU   B 64  ? 0.1845 0.1820 0.1743 -0.0309 -0.0346 -0.0118 64  GLU   B OE2 
4920 N  N   . SER   B 65  ? 0.1545 0.1387 0.1595 -0.0109 -0.0228 -0.0158 65  SER   B N   
4921 C  CA  . SER   B 65  ? 0.1528 0.1409 0.1537 -0.0043 -0.0187 -0.0102 65  SER   B CA  
4922 C  C   . SER   B 65  ? 0.1541 0.1415 0.1597 -0.0025 -0.0249 -0.0119 65  SER   B C   
4923 O  O   . SER   B 65  ? 0.1609 0.1562 0.1579 0.0020  -0.0236 -0.0203 65  SER   B O   
4924 C  CB  . SER   B 65  ? 0.1531 0.1480 0.1547 -0.0118 -0.0183 -0.0132 65  SER   B CB  
4925 O  OG  . SER   B 65  ? 0.1549 0.1461 0.1652 -0.0105 -0.0158 -0.0186 65  SER   B OG  
4931 N  N   . ASP   B 66  ? 0.1664 0.1523 0.1606 -0.0022 -0.0275 -0.0127 66  ASP   B N   
4932 C  CA  . ASP   B 66  ? 0.1742 0.1619 0.1513 0.0033  -0.0314 -0.0148 66  ASP   B CA  
4933 C  C   . ASP   B 66  ? 0.1788 0.1676 0.1489 -0.0015 -0.0283 -0.0168 66  ASP   B C   
4934 O  O   . ASP   B 66  ? 0.1787 0.1715 0.1610 0.0062  -0.0344 -0.0219 66  ASP   B O   
4935 C  CB  . ASP   B 66  ? 0.1842 0.1758 0.1751 0.0115  -0.0461 -0.0183 66  ASP   B CB  
4936 C  CG  . ASP   B 66  ? 0.2093 0.1907 0.2001 0.0167  -0.0585 -0.0030 66  ASP   B CG  
4937 O  OD1 . ASP   B 66  ? 0.2279 0.1833 0.2079 0.0154  -0.0470 0.0028  66  ASP   B OD1 
4938 O  OD2 . ASP   B 66  ? 0.2259 0.2095 0.2716 0.0333  -0.0598 -0.0027 66  ASP   B OD2 
4943 N  N   . ASP   B 67  ? 0.1738 0.1583 0.1493 -0.0054 -0.0254 -0.0171 67  ASP   B N   
4944 C  CA  . ASP   B 67  ? 0.1872 0.1535 0.1614 -0.0054 -0.0288 -0.0078 67  ASP   B CA  
4945 C  C   . ASP   B 67  ? 0.1806 0.1538 0.1808 0.0044  -0.0253 -0.0186 67  ASP   B C   
4946 O  O   . ASP   B 67  ? 0.1844 0.1573 0.1852 0.0004  -0.0191 -0.0283 67  ASP   B O   
4947 C  CB  . ASP   B 67  ? 0.2146 0.1677 0.1836 -0.0117 -0.0357 -0.0074 67  ASP   B CB  
4948 C  CG  . ASP   B 67  ? 0.2501 0.1700 0.1920 -0.0112 -0.0658 -0.0144 67  ASP   B CG  
4949 O  OD1 . ASP   B 67  ? 0.2684 0.1785 0.2119 -0.0182 -0.0703 -0.0089 67  ASP   B OD1 
4950 O  OD2 . ASP   B 67  ? 0.2700 0.1737 0.2143 0.0023  -0.0737 -0.0164 67  ASP   B OD2 
4955 N  N   . TYR   B 68  ? 0.1794 0.1529 0.1615 0.0053  -0.0345 -0.0234 68  TYR   B N   
4956 C  CA  . TYR   B 68  ? 0.1748 0.1676 0.1770 0.0076  -0.0375 -0.0322 68  TYR   B CA  
4957 C  C   . TYR   B 68  ? 0.1646 0.1686 0.1740 0.0070  -0.0364 -0.0351 68  TYR   B C   
4958 O  O   . TYR   B 68  ? 0.1701 0.1734 0.1851 0.0114  -0.0316 -0.0468 68  TYR   B O   
4959 C  CB  . TYR   B 68  ? 0.1728 0.1831 0.1827 0.0146  -0.0412 -0.0359 68  TYR   B CB  
4960 C  CG  . TYR   B 68  ? 0.1805 0.1999 0.1910 0.0193  -0.0339 -0.0560 68  TYR   B CG  
4961 C  CD1 . TYR   B 68  ? 0.1880 0.2028 0.2192 0.0019  -0.0292 -0.0605 68  TYR   B CD1 
4962 C  CD2 . TYR   B 68  ? 0.1904 0.2181 0.2117 0.0233  -0.0438 -0.0450 68  TYR   B CD2 
4963 C  CE1 . TYR   B 68  ? 0.1934 0.2139 0.2403 0.0041  -0.0282 -0.0535 68  TYR   B CE1 
4964 C  CE2 . TYR   B 68  ? 0.1924 0.2228 0.2194 0.0214  -0.0398 -0.0540 68  TYR   B CE2 
4965 C  CZ  . TYR   B 68  ? 0.1911 0.2191 0.2365 0.0120  -0.0322 -0.0577 68  TYR   B CZ  
4966 O  OH  . TYR   B 68  ? 0.1845 0.2366 0.2578 0.0093  -0.0240 -0.0397 68  TYR   B OH  
4976 N  N   . ILE   B 69  ? 0.1652 0.1587 0.1716 0.0102  -0.0347 -0.0346 69  ILE   B N   
4977 C  CA  . ILE   B 69  ? 0.1729 0.1658 0.1784 0.0023  -0.0193 -0.0363 69  ILE   B CA  
4978 C  C   . ILE   B 69  ? 0.1705 0.1629 0.1712 0.0058  -0.0329 -0.0315 69  ILE   B C   
4979 O  O   . ILE   B 69  ? 0.1755 0.1727 0.1688 0.0011  -0.0209 -0.0358 69  ILE   B O   
4980 C  CB  . ILE   B 69  ? 0.1805 0.1710 0.1998 -0.0000 0.0017  -0.0284 69  ILE   B CB  
4981 C  CG1 . ILE   B 69  ? 0.1799 0.1797 0.2059 -0.0072 0.0046  -0.0270 69  ILE   B CG1 
4982 C  CG2 . ILE   B 69  ? 0.1923 0.1772 0.2107 -0.0012 0.0013  -0.0207 69  ILE   B CG2 
4983 C  CD1 . ILE   B 69  ? 0.1714 0.1835 0.2098 -0.0141 0.0051  -0.0342 69  ILE   B CD1 
4995 N  N   . ALA   B 70  ? 0.1699 0.1632 0.1747 0.0059  -0.0396 -0.0247 70  ALA   B N   
4996 C  CA  . ALA   B 70  ? 0.1764 0.1663 0.1599 0.0005  -0.0396 -0.0215 70  ALA   B CA  
4997 C  C   . ALA   B 70  ? 0.1810 0.1630 0.1634 -0.0007 -0.0428 -0.0348 70  ALA   B C   
4998 O  O   . ALA   B 70  ? 0.1875 0.1705 0.1737 0.0040  -0.0416 -0.0380 70  ALA   B O   
4999 C  CB  . ALA   B 70  ? 0.1781 0.1803 0.1766 -0.0012 -0.0334 -0.0267 70  ALA   B CB  
5005 N  N   . THR   B 71  ? 0.1881 0.1627 0.1723 0.0022  -0.0449 -0.0314 71  THR   B N   
5006 C  CA  . THR   B 71  ? 0.2016 0.1683 0.2089 0.0090  -0.0587 -0.0319 71  THR   B CA  
5007 C  C   . THR   B 71  ? 0.1941 0.1724 0.2269 0.0255  -0.0586 -0.0489 71  THR   B C   
5008 O  O   . THR   B 71  ? 0.2031 0.1797 0.2645 0.0314  -0.0551 -0.0640 71  THR   B O   
5009 C  CB  . THR   B 71  ? 0.2234 0.1927 0.2334 0.0013  -0.0704 -0.0103 71  THR   B CB  
5010 O  OG1 . THR   B 71  ? 0.2382 0.2188 0.2646 -0.0174 -0.0635 0.0083  71  THR   B OG1 
5011 C  CG2 . THR   B 71  ? 0.2408 0.1912 0.2647 0.0036  -0.0581 -0.0028 71  THR   B CG2 
5019 N  N   . ASN   B 72  ? 0.1794 0.1751 0.2194 0.0173  -0.0593 -0.0633 72  ASN   B N   
5020 C  CA  . ASN   B 72  ? 0.1841 0.1864 0.2273 0.0183  -0.0483 -0.0730 72  ASN   B CA  
5021 C  C   . ASN   B 72  ? 0.1860 0.2001 0.2363 0.0027  -0.0313 -0.0678 72  ASN   B C   
5022 O  O   . ASN   B 72  ? 0.1862 0.2199 0.2650 0.0073  -0.0167 -0.0735 72  ASN   B O   
5023 C  CB  . ASN   B 72  ? 0.1900 0.2050 0.2323 0.0151  -0.0566 -0.0620 72  ASN   B CB  
5024 C  CG  . ASN   B 72  ? 0.2064 0.2189 0.2433 0.0332  -0.0618 -0.0410 72  ASN   B CG  
5025 O  OD1 . ASN   B 72  ? 0.2309 0.2384 0.2580 0.0198  -0.0547 -0.0437 72  ASN   B OD1 
5026 N  ND2 . ASN   B 72  ? 0.2168 0.2262 0.2859 0.0514  -0.0504 -0.0070 72  ASN   B ND2 
5033 N  N   . GLY   B 73  ? 0.1902 0.2000 0.2102 -0.0005 -0.0334 -0.0646 73  GLY   B N   
5034 C  CA  . GLY   B 73  ? 0.1853 0.2058 0.2013 -0.0010 -0.0248 -0.0530 73  GLY   B CA  
5035 C  C   . GLY   B 73  ? 0.1780 0.2037 0.1538 0.0045  -0.0267 -0.0473 73  GLY   B C   
5036 O  O   . GLY   B 73  ? 0.1716 0.1897 0.1630 0.0067  -0.0191 -0.0317 73  GLY   B O   
5040 N  N   . PRO   B 74  ? 0.1802 0.2112 0.1477 0.0058  -0.0245 -0.0349 74  PRO   B N   
5041 C  CA  . PRO   B 74  ? 0.1694 0.2130 0.1329 0.0097  -0.0208 -0.0228 74  PRO   B CA  
5042 C  C   . PRO   B 74  ? 0.1557 0.2006 0.1354 0.0095  -0.0153 -0.0189 74  PRO   B C   
5043 O  O   . PRO   B 74  ? 0.1559 0.2033 0.1912 0.0078  -0.0123 -0.0334 74  PRO   B O   
5044 C  CB  . PRO   B 74  ? 0.1861 0.2339 0.1399 0.0030  -0.0237 -0.0146 74  PRO   B CB  
5045 C  CG  . PRO   B 74  ? 0.2077 0.2433 0.1601 0.0014  -0.0179 -0.0122 74  PRO   B CG  
5046 C  CD  . PRO   B 74  ? 0.2024 0.2297 0.1483 0.0041  -0.0113 -0.0250 74  PRO   B CD  
5054 N  N   . LEU   B 75  ? 0.1564 0.1868 0.1227 0.0129  -0.0162 -0.0211 75  LEU   B N   
5055 C  CA  . LEU   B 75  ? 0.1584 0.1895 0.1296 0.0054  -0.0137 -0.0036 75  LEU   B CA  
5056 C  C   . LEU   B 75  ? 0.1652 0.1968 0.1349 0.0100  -0.0035 -0.0066 75  LEU   B C   
5057 O  O   . LEU   B 75  ? 0.1784 0.2044 0.1434 0.0029  -0.0082 -0.0052 75  LEU   B O   
5058 C  CB  . LEU   B 75  ? 0.1695 0.1918 0.1157 -0.0011 -0.0245 0.0058  75  LEU   B CB  
5059 C  CG  . LEU   B 75  ? 0.2046 0.2062 0.1382 -0.0289 -0.0150 0.0016  75  LEU   B CG  
5060 C  CD1 . LEU   B 75  ? 0.2369 0.2191 0.1449 -0.0426 0.0102  -0.0003 75  LEU   B CD1 
5061 C  CD2 . LEU   B 75  ? 0.2412 0.2210 0.2196 -0.0221 0.0064  0.0034  75  LEU   B CD2 
5073 N  N   . LYS   B 76  ? 0.1598 0.2128 0.1582 0.0083  -0.0015 0.0040  76  LYS   B N   
5074 C  CA  . LYS   B 76  ? 0.1749 0.2186 0.1797 -0.0002 0.0195  0.0030  76  LYS   B CA  
5075 C  C   . LYS   B 76  ? 0.1667 0.2057 0.1467 0.0072  0.0049  0.0224  76  LYS   B C   
5076 O  O   . LYS   B 76  ? 0.1692 0.1869 0.1520 0.0071  0.0031  0.0212  76  LYS   B O   
5077 C  CB  . LYS   B 76  ? 0.1948 0.2298 0.2587 -0.0054 0.0394  -0.0314 76  LYS   B CB  
5078 C  CG  . LYS   B 76  ? 0.2033 0.2486 0.3038 0.0042  0.0268  -0.0403 76  LYS   B CG  
5079 C  CD  . LYS   B 76  ? 0.2004 0.2575 0.3398 0.0097  0.0128  -0.0564 76  LYS   B CD  
5080 C  CE  . LYS   B 76  ? 0.2041 0.2754 0.3931 0.0113  -0.0001 -0.0755 76  LYS   B CE  
5081 N  NZ  . LYS   B 76  ? 0.2022 0.2849 0.4133 0.0053  -0.0216 -0.0981 76  LYS   B NZ  
5095 N  N   . VAL   B 77  ? 0.1743 0.2181 0.1509 0.0172  0.0102  0.0252  77  VAL   B N   
5096 C  CA  . VAL   B 77  ? 0.1742 0.2071 0.1726 0.0210  0.0145  0.0466  77  VAL   B CA  
5097 C  C   . VAL   B 77  ? 0.1590 0.1830 0.1755 0.0226  0.0206  0.0358  77  VAL   B C   
5098 O  O   . VAL   B 77  ? 0.1655 0.1786 0.1764 0.0304  0.0300  0.0297  77  VAL   B O   
5099 C  CB  . VAL   B 77  ? 0.1858 0.2161 0.2050 0.0194  0.0267  0.0643  77  VAL   B CB  
5100 C  CG1 . VAL   B 77  ? 0.1902 0.2086 0.2457 0.0106  0.0365  0.0823  77  VAL   B CG1 
5101 C  CG2 . VAL   B 77  ? 0.2004 0.2341 0.2150 0.0152  0.0084  0.0643  77  VAL   B CG2 
5111 N  N   . GLY   B 78  ? 0.1510 0.1719 0.1719 0.0124  0.0186  0.0269  78  GLY   B N   
5112 C  CA  . GLY   B 78  ? 0.1546 0.1691 0.1607 0.0109  0.0232  0.0170  78  GLY   B CA  
5113 C  C   . GLY   B 78  ? 0.1491 0.1590 0.1506 0.0119  0.0162  0.0156  78  GLY   B C   
5114 O  O   . GLY   B 78  ? 0.1522 0.1577 0.1598 0.0188  0.0133  0.0185  78  GLY   B O   
5118 N  N   . GLY   B 79  ? 0.1461 0.1606 0.1554 0.0112  0.0148  0.0077  79  GLY   B N   
5119 C  CA  . GLY   B 79  ? 0.1468 0.1517 0.1556 0.0136  0.0086  0.0046  79  GLY   B CA  
5120 C  C   . GLY   B 79  ? 0.1382 0.1490 0.1486 0.0171  0.0094  0.0102  79  GLY   B C   
5121 O  O   . GLY   B 79  ? 0.1441 0.1474 0.1603 0.0160  0.0166  0.0175  79  GLY   B O   
5125 N  N   . SER   B 80  ? 0.1394 0.1406 0.1463 0.0103  0.0152  0.0092  80  SER   B N   
5126 C  CA  . SER   B 80  ? 0.1342 0.1381 0.1500 0.0062  0.0060  0.0113  80  SER   B CA  
5127 C  C   . SER   B 80  ? 0.1406 0.1366 0.1496 0.0132  -0.0052 0.0010  80  SER   B C   
5128 O  O   . SER   B 80  ? 0.1538 0.1380 0.1784 0.0130  0.0043  -0.0011 80  SER   B O   
5129 C  CB  . SER   B 80  ? 0.1392 0.1391 0.1558 -0.0006 -0.0010 0.0085  80  SER   B CB  
5130 O  OG  . SER   B 80  ? 0.1461 0.1582 0.1825 -0.0041 -0.0161 0.0083  80  SER   B OG  
5136 N  N   . CYS   B 81  ? 0.1361 0.1233 0.1569 0.0002  -0.0057 -0.0052 81  CYS   B N   
5137 C  CA  . CYS   B 81  ? 0.1478 0.1248 0.1548 0.0030  -0.0181 -0.0018 81  CYS   B CA  
5138 C  C   . CYS   B 81  ? 0.1428 0.1219 0.1304 0.0014  -0.0149 -0.0007 81  CYS   B C   
5139 O  O   . CYS   B 81  ? 0.1626 0.1259 0.1507 0.0087  -0.0016 -0.0033 81  CYS   B O   
5140 C  CB  . CYS   B 81  ? 0.1608 0.1351 0.1593 -0.0027 -0.0194 -0.0010 81  CYS   B CB  
5141 S  SG  . CYS   B 81  ? 0.1566 0.1540 0.1507 -0.0027 -0.0243 -0.0085 81  CYS   B SG  
5147 N  N   . VAL   B 82  ? 0.1414 0.1236 0.1515 -0.0001 -0.0175 -0.0039 82  VAL   B N   
5148 C  CA  . VAL   B 82  ? 0.1510 0.1271 0.1343 -0.0066 -0.0128 0.0071  82  VAL   B CA  
5149 C  C   . VAL   B 82  ? 0.1572 0.1185 0.1527 -0.0075 -0.0155 0.0021  82  VAL   B C   
5150 O  O   . VAL   B 82  ? 0.1652 0.1191 0.1943 -0.0078 -0.0126 -0.0091 82  VAL   B O   
5151 C  CB  . VAL   B 82  ? 0.1602 0.1480 0.1548 -0.0037 -0.0177 0.0089  82  VAL   B CB  
5152 C  CG1 . VAL   B 82  ? 0.1833 0.1713 0.1612 -0.0005 -0.0140 0.0179  82  VAL   B CG1 
5153 C  CG2 . VAL   B 82  ? 0.1640 0.1593 0.1829 -0.0049 -0.0326 0.0165  82  VAL   B CG2 
5163 N  N   . LEU   B 83  ? 0.1435 0.1191 0.1506 -0.0151 -0.0191 -0.0068 83  LEU   B N   
5164 C  CA  . LEU   B 83  ? 0.1465 0.1195 0.1469 -0.0127 -0.0212 -0.0061 83  LEU   B CA  
5165 C  C   . LEU   B 83  ? 0.1483 0.1219 0.1460 -0.0186 -0.0204 -0.0060 83  LEU   B C   
5166 O  O   . LEU   B 83  ? 0.1466 0.1324 0.1380 -0.0179 -0.0164 0.0068  83  LEU   B O   
5167 C  CB  . LEU   B 83  ? 0.1567 0.1326 0.1553 -0.0112 -0.0202 -0.0097 83  LEU   B CB  
5168 C  CG  . LEU   B 83  ? 0.1730 0.1573 0.1581 -0.0170 -0.0107 -0.0094 83  LEU   B CG  
5169 C  CD1 . LEU   B 83  ? 0.1827 0.1690 0.1626 -0.0154 -0.0186 0.0037  83  LEU   B CD1 
5170 C  CD2 . LEU   B 83  ? 0.1918 0.1603 0.1705 -0.0054 -0.0146 -0.0244 83  LEU   B CD2 
5182 N  N   . SER   B 84  ? 0.1544 0.1386 0.1635 -0.0259 -0.0197 0.0030  84  SER   B N   
5183 C  CA  . SER   B 84  ? 0.1542 0.1537 0.1573 -0.0276 -0.0182 0.0086  84  SER   B CA  
5184 C  C   . SER   B 84  ? 0.1470 0.1716 0.1206 -0.0225 -0.0186 0.0173  84  SER   B C   
5185 O  O   . SER   B 84  ? 0.1547 0.1563 0.1299 -0.0209 -0.0114 -0.0005 84  SER   B O   
5186 C  CB  . SER   B 84  ? 0.1732 0.1575 0.2050 -0.0277 0.0085  0.0098  84  SER   B CB  
5187 O  OG  . SER   B 84  ? 0.1725 0.1662 0.2551 -0.0325 0.0053  0.0182  84  SER   B OG  
5193 N  N   . GLY   B 85  ? 0.1483 0.1884 0.1388 -0.0235 -0.0141 0.0202  85  GLY   B N   
5194 C  CA  . GLY   B 85  ? 0.1443 0.1946 0.1536 -0.0348 -0.0055 -0.0023 85  GLY   B CA  
5195 C  C   . GLY   B 85  ? 0.1447 0.1785 0.1392 -0.0370 0.0004  0.0051  85  GLY   B C   
5196 O  O   . GLY   B 85  ? 0.1608 0.1782 0.1474 -0.0507 0.0103  -0.0091 85  GLY   B O   
5200 N  N   . HIS   B 86  ? 0.1461 0.1631 0.1606 -0.0289 -0.0124 0.0161  86  HIS   B N   
5201 C  CA  . HIS   B 86  ? 0.1516 0.1636 0.1569 -0.0280 -0.0153 0.0212  86  HIS   B CA  
5202 C  C   . HIS   B 86  ? 0.1530 0.1736 0.1575 -0.0466 -0.0074 0.0325  86  HIS   B C   
5203 O  O   . HIS   B 86  ? 0.1627 0.1921 0.1567 -0.0353 0.0044  0.0244  86  HIS   B O   
5204 C  CB  . HIS   B 86  ? 0.1598 0.1714 0.1524 -0.0199 -0.0205 0.0086  86  HIS   B CB  
5205 C  CG  . HIS   B 86  ? 0.1563 0.1744 0.1503 -0.0114 -0.0126 0.0119  86  HIS   B CG  
5206 N  ND1 . HIS   B 86  ? 0.1635 0.1977 0.1781 -0.0201 -0.0174 -0.0086 86  HIS   B ND1 
5207 C  CD2 . HIS   B 86  ? 0.1606 0.1807 0.1569 -0.0041 -0.0175 0.0100  86  HIS   B CD2 
5208 C  CE1 . HIS   B 86  ? 0.1707 0.1981 0.1651 -0.0126 -0.0101 -0.0225 86  HIS   B CE1 
5209 N  NE2 . HIS   B 86  ? 0.1692 0.1891 0.1519 0.0002  -0.0110 -0.0032 86  HIS   B NE2 
5217 N  N   . ASN   B 87  ? 0.1555 0.1786 0.1594 -0.0357 0.0017  0.0194  87  ASN   B N   
5218 C  CA  . ASN   B 87  ? 0.1598 0.1940 0.1619 -0.0348 0.0188  0.0136  87  ASN   B CA  
5219 C  C   . ASN   B 87  ? 0.1743 0.1802 0.1447 -0.0266 0.0277  0.0161  87  ASN   B C   
5220 O  O   . ASN   B 87  ? 0.1986 0.1927 0.1813 -0.0228 0.0487  0.0146  87  ASN   B O   
5221 C  CB  . ASN   B 87  ? 0.1598 0.2309 0.2007 -0.0275 0.0222  0.0125  87  ASN   B CB  
5222 C  CG  . ASN   B 87  ? 0.1704 0.2538 0.2076 0.0103  0.0297  0.0287  87  ASN   B CG  
5223 O  OD1 . ASN   B 87  ? 0.1665 0.2361 0.1941 0.0162  0.0440  0.0450  87  ASN   B OD1 
5224 N  ND2 . ASN   B 87  ? 0.2038 0.2691 0.2432 0.0173  0.0393  0.0282  87  ASN   B ND2 
5231 N  N   . LEU   B 88  ? 0.1622 0.1686 0.1350 -0.0321 0.0101  0.0128  88  LEU   B N   
5232 C  CA  . LEU   B 88  ? 0.1733 0.1660 0.1565 -0.0326 0.0042  -0.0002 88  LEU   B CA  
5233 C  C   . LEU   B 88  ? 0.1752 0.1518 0.1456 -0.0371 0.0037  0.0023  88  LEU   B C   
5234 O  O   . LEU   B 88  ? 0.2014 0.1612 0.1723 -0.0267 -0.0230 -0.0088 88  LEU   B O   
5235 C  CB  . LEU   B 88  ? 0.1868 0.1675 0.1631 -0.0423 -0.0058 0.0201  88  LEU   B CB  
5236 C  CG  . LEU   B 88  ? 0.2226 0.2020 0.1828 -0.0310 -0.0228 0.0363  88  LEU   B CG  
5237 C  CD1 . LEU   B 88  ? 0.2312 0.2312 0.1996 -0.0437 -0.0259 0.0452  88  LEU   B CD1 
5238 C  CD2 . LEU   B 88  ? 0.2567 0.2265 0.2370 0.0094  -0.0500 0.0197  88  LEU   B CD2 
5250 N  N   . ALA   B 89  ? 0.1590 0.1526 0.1348 -0.0353 0.0207  0.0053  89  ALA   B N   
5251 C  CA  . ALA   B 89  ? 0.1576 0.1479 0.1184 -0.0344 0.0023  0.0090  89  ALA   B CA  
5252 C  C   . ALA   B 89  ? 0.1659 0.1501 0.1360 -0.0384 0.0133  0.0021  89  ALA   B C   
5253 O  O   . ALA   B 89  ? 0.1494 0.1623 0.1711 -0.0371 0.0120  -0.0264 89  ALA   B O   
5254 C  CB  . ALA   B 89  ? 0.1524 0.1469 0.1386 -0.0388 -0.0004 0.0169  89  ALA   B CB  
5260 N  N   . LYS   B 90  ? 0.1958 0.1371 0.1433 -0.0478 -0.0075 0.0105  90  LYS   B N   
5261 C  CA  . LYS   B 90  ? 0.2142 0.1399 0.1354 -0.0432 -0.0128 0.0105  90  LYS   B CA  
5262 C  C   . LYS   B 90  ? 0.1976 0.1288 0.1452 -0.0472 -0.0136 0.0013  90  LYS   B C   
5263 O  O   . LYS   B 90  ? 0.2085 0.1462 0.1636 -0.0613 0.0040  0.0085  90  LYS   B O   
5264 C  CB  . LYS   B 90  ? 0.2313 0.1468 0.1573 -0.0380 -0.0030 0.0169  90  LYS   B CB  
5265 C  CG  . LYS   B 90  ? 0.2321 0.1645 0.1623 -0.0214 0.0216  0.0067  90  LYS   B CG  
5266 C  CD  . LYS   B 90  ? 0.2637 0.1919 0.2248 -0.0152 0.0437  -0.0086 90  LYS   B CD  
5267 C  CE  . LYS   B 90  ? 0.2673 0.2071 0.2823 -0.0247 0.0599  -0.0178 90  LYS   B CE  
5268 N  NZ  . LYS   B 90  ? 0.2790 0.2010 0.2856 -0.0346 0.0810  -0.0154 90  LYS   B NZ  
5282 N  N   . HIS   B 91  ? 0.1723 0.1194 0.1277 -0.0315 -0.0211 0.0070  91  HIS   B N   
5283 C  CA  . HIS   B 91  ? 0.1617 0.1249 0.1368 -0.0253 -0.0182 0.0016  91  HIS   B CA  
5284 C  C   . HIS   B 91  ? 0.1454 0.1277 0.1229 -0.0303 -0.0079 0.0015  91  HIS   B C   
5285 O  O   . HIS   B 91  ? 0.1617 0.1280 0.1216 -0.0285 -0.0216 0.0059  91  HIS   B O   
5286 C  CB  . HIS   B 91  ? 0.1785 0.1290 0.1861 -0.0089 -0.0061 0.0140  91  HIS   B CB  
5287 C  CG  . HIS   B 91  ? 0.2183 0.1454 0.2484 0.0026  0.0257  0.0235  91  HIS   B CG  
5288 N  ND1 . HIS   B 91  ? 0.2507 0.1509 0.3061 -0.0020 0.0314  0.0132  91  HIS   B ND1 
5289 C  CD2 . HIS   B 91  ? 0.2289 0.1744 0.2969 0.0191  0.0215  0.0506  91  HIS   B CD2 
5290 C  CE1 . HIS   B 91  ? 0.2535 0.1686 0.3190 0.0140  0.0290  0.0209  91  HIS   B CE1 
5291 N  NE2 . HIS   B 91  ? 0.2433 0.1806 0.3209 0.0292  0.0331  0.0558  91  HIS   B NE2 
5299 N  N   . CYS   B 92  ? 0.1407 0.1266 0.1259 -0.0255 -0.0117 -0.0003 92  CYS   B N   
5300 C  CA  . CYS   B 92  ? 0.1415 0.1255 0.1213 -0.0193 -0.0038 -0.0018 92  CYS   B CA  
5301 C  C   . CYS   B 92  ? 0.1392 0.1199 0.1184 -0.0119 -0.0085 0.0024  92  CYS   B C   
5302 O  O   . CYS   B 92  ? 0.1464 0.1272 0.1369 -0.0172 -0.0045 -0.0003 92  CYS   B O   
5303 C  CB  . CYS   B 92  ? 0.1412 0.1323 0.1358 -0.0138 -0.0066 -0.0007 92  CYS   B CB  
5304 S  SG  . CYS   B 92  ? 0.1409 0.1334 0.1309 -0.0126 -0.0112 0.0031  92  CYS   B SG  
5310 N  N   . LEU   B 93  ? 0.1288 0.1220 0.1187 -0.0092 -0.0043 -0.0054 93  LEU   B N   
5311 C  CA  . LEU   B 93  ? 0.1308 0.1277 0.1266 0.0030  -0.0089 0.0034  93  LEU   B CA  
5312 C  C   . LEU   B 93  ? 0.1222 0.1223 0.1119 -0.0042 -0.0047 0.0075  93  LEU   B C   
5313 O  O   . LEU   B 93  ? 0.1306 0.1193 0.1344 -0.0097 -0.0083 0.0033  93  LEU   B O   
5314 C  CB  . LEU   B 93  ? 0.1370 0.1238 0.1315 0.0008  -0.0124 0.0100  93  LEU   B CB  
5315 C  CG  . LEU   B 93  ? 0.1287 0.1350 0.1480 -0.0016 -0.0053 0.0178  93  LEU   B CG  
5316 C  CD1 . LEU   B 93  ? 0.1340 0.1428 0.1452 0.0071  -0.0016 0.0019  93  LEU   B CD1 
5317 C  CD2 . LEU   B 93  ? 0.1289 0.1376 0.1649 -0.0024 -0.0090 -0.0016 93  LEU   B CD2 
5329 N  N   . HIS   B 94  ? 0.1285 0.1167 0.1129 -0.0057 -0.0165 0.0076  94  HIS   B N   
5330 C  CA  . HIS   B 94  ? 0.1297 0.1189 0.1213 -0.0009 -0.0065 0.0070  94  HIS   B CA  
5331 C  C   . HIS   B 94  ? 0.1256 0.1224 0.1338 0.0006  -0.0002 0.0101  94  HIS   B C   
5332 O  O   . HIS   B 94  ? 0.1260 0.1322 0.1759 -0.0027 0.0161  -0.0036 94  HIS   B O   
5333 C  CB  . HIS   B 94  ? 0.1282 0.1266 0.1314 -0.0013 -0.0061 0.0034  94  HIS   B CB  
5334 C  CG  . HIS   B 94  ? 0.1327 0.1238 0.1351 -0.0057 -0.0197 0.0048  94  HIS   B CG  
5335 N  ND1 . HIS   B 94  ? 0.1382 0.1269 0.1304 -0.0055 -0.0204 0.0011  94  HIS   B ND1 
5336 C  CD2 . HIS   B 94  ? 0.1390 0.1226 0.1366 -0.0012 -0.0159 0.0050  94  HIS   B CD2 
5337 C  CE1 . HIS   B 94  ? 0.1422 0.1241 0.1325 -0.0139 -0.0192 0.0026  94  HIS   B CE1 
5338 N  NE2 . HIS   B 94  ? 0.1348 0.1301 0.1447 -0.0123 -0.0128 0.0034  94  HIS   B NE2 
5346 N  N   . VAL   B 95  ? 0.1197 0.1173 0.1375 -0.0026 -0.0001 0.0061  95  VAL   B N   
5347 C  CA  . VAL   B 95  ? 0.1300 0.1292 0.1325 -0.0001 0.0049  0.0128  95  VAL   B CA  
5348 C  C   . VAL   B 95  ? 0.1300 0.1281 0.1245 0.0015  0.0075  0.0046  95  VAL   B C   
5349 O  O   . VAL   B 95  ? 0.1331 0.1269 0.1552 0.0057  0.0056  0.0133  95  VAL   B O   
5350 C  CB  . VAL   B 95  ? 0.1313 0.1232 0.1351 -0.0034 -0.0061 0.0040  95  VAL   B CB  
5351 C  CG1 . VAL   B 95  ? 0.1393 0.1426 0.1449 -0.0093 -0.0009 0.0157  95  VAL   B CG1 
5352 C  CG2 . VAL   B 95  ? 0.1377 0.1253 0.1431 0.0050  -0.0091 -0.0015 95  VAL   B CG2 
5362 N  N   . VAL   B 96  ? 0.1429 0.1293 0.1356 0.0149  0.0129  0.0138  96  VAL   B N   
5363 C  CA  . VAL   B 96  ? 0.1457 0.1422 0.1279 0.0123  0.0039  0.0217  96  VAL   B CA  
5364 C  C   . VAL   B 96  ? 0.1492 0.1452 0.1364 0.0136  0.0085  0.0167  96  VAL   B C   
5365 O  O   . VAL   B 96  ? 0.1519 0.1499 0.1526 0.0099  0.0158  0.0040  96  VAL   B O   
5366 C  CB  . VAL   B 96  ? 0.1517 0.1626 0.1310 0.0127  0.0049  0.0112  96  VAL   B CB  
5367 C  CG1 . VAL   B 96  ? 0.1490 0.1795 0.1555 0.0186  0.0140  0.0163  96  VAL   B CG1 
5368 C  CG2 . VAL   B 96  ? 0.1568 0.1633 0.1467 0.0052  0.0088  0.0022  96  VAL   B CG2 
5378 N  N   . GLY   B 97  ? 0.1510 0.1469 0.1347 0.0096  0.0019  0.0187  97  GLY   B N   
5379 C  CA  . GLY   B 97  ? 0.1683 0.1478 0.1381 0.0078  0.0055  0.0190  97  GLY   B CA  
5380 C  C   . GLY   B 97  ? 0.1843 0.1593 0.1582 0.0166  0.0114  0.0210  97  GLY   B C   
5381 O  O   . GLY   B 97  ? 0.1948 0.1637 0.1627 0.0108  0.0037  0.0158  97  GLY   B O   
5385 N  N   . PRO   B 98  ? 0.1958 0.1659 0.1693 0.0139  0.0335  0.0334  98  PRO   B N   
5386 C  CA  . PRO   B 98  ? 0.2090 0.1800 0.1810 0.0226  0.0429  0.0336  98  PRO   B CA  
5387 C  C   . PRO   B 98  ? 0.2181 0.1798 0.1535 0.0349  0.0450  0.0513  98  PRO   B C   
5388 O  O   . PRO   B 98  ? 0.2032 0.1760 0.1760 0.0270  0.0476  0.0520  98  PRO   B O   
5389 C  CB  . PRO   B 98  ? 0.2007 0.1830 0.2027 0.0198  0.0508  0.0308  98  PRO   B CB  
5390 C  CG  . PRO   B 98  ? 0.1927 0.1759 0.1935 0.0159  0.0468  0.0462  98  PRO   B CG  
5391 C  CD  . PRO   B 98  ? 0.1823 0.1699 0.1939 0.0154  0.0432  0.0396  98  PRO   B CD  
5399 N  N   . ASN   B 99  ? 0.2307 0.1970 0.1625 0.0472  0.0400  0.0338  99  ASN   B N   
5400 C  CA  . ASN   B 99  ? 0.2519 0.2087 0.1687 0.0601  0.0393  0.0518  99  ASN   B CA  
5401 C  C   . ASN   B 99  ? 0.2830 0.2419 0.2005 0.0650  0.0648  0.0803  99  ASN   B C   
5402 O  O   . ASN   B 99  ? 0.3035 0.2513 0.2062 0.0676  0.0592  0.0794  99  ASN   B O   
5403 C  CB  . ASN   B 99  ? 0.2603 0.2044 0.1674 0.0588  0.0308  0.0470  99  ASN   B CB  
5404 C  CG  . ASN   B 99  ? 0.2642 0.2092 0.1908 0.0524  0.0205  0.0356  99  ASN   B CG  
5405 O  OD1 . ASN   B 99  ? 0.2611 0.2090 0.2265 0.0593  0.0176  0.0453  99  ASN   B OD1 
5406 N  ND2 . ASN   B 99  ? 0.2684 0.2095 0.2021 0.0514  -0.0069 0.0258  99  ASN   B ND2 
5413 N  N   A VAL   B 100 ? 0.3003 0.2539 0.2458 0.0560  0.0678  0.0974  100 VAL   B N   
5414 N  N   B VAL   B 100 ? 0.2994 0.2532 0.2467 0.0548  0.0677  0.0979  100 VAL   B N   
5415 C  CA  A VAL   B 100 ? 0.3268 0.2708 0.2951 0.0454  0.0666  0.1098  100 VAL   B CA  
5416 C  CA  B VAL   B 100 ? 0.3253 0.2693 0.2961 0.0431  0.0665  0.1107  100 VAL   B CA  
5417 C  C   A VAL   B 100 ? 0.3477 0.2750 0.2866 0.0524  0.0609  0.1268  100 VAL   B C   
5418 C  C   B VAL   B 100 ? 0.3468 0.2737 0.2861 0.0509  0.0598  0.1262  100 VAL   B C   
5419 O  O   A VAL   B 100 ? 0.3575 0.2857 0.2948 0.0485  0.0679  0.1224  100 VAL   B O   
5420 O  O   B VAL   B 100 ? 0.3564 0.2832 0.2920 0.0465  0.0655  0.1202  100 VAL   B O   
5421 C  CB  A VAL   B 100 ? 0.3368 0.2861 0.3555 0.0244  0.0641  0.1113  100 VAL   B CB  
5422 C  CB  B VAL   B 100 ? 0.3339 0.2834 0.3553 0.0205  0.0660  0.1147  100 VAL   B CB  
5423 C  CG1 A VAL   B 100 ? 0.3415 0.2922 0.3784 0.0214  0.0631  0.1108  100 VAL   B CG1 
5424 C  CG1 B VAL   B 100 ? 0.3381 0.2890 0.3777 0.0175  0.0657  0.1157  100 VAL   B CG1 
5425 C  CG2 A VAL   B 100 ? 0.3377 0.2909 0.3733 0.0141  0.0658  0.1137  100 VAL   B CG2 
5426 C  CG2 B VAL   B 100 ? 0.3345 0.2876 0.3723 0.0091  0.0686  0.1184  100 VAL   B CG2 
5445 N  N   . ASN   B 101 ? 0.3615 0.2757 0.2940 0.0627  0.0457  0.1312  101 ASN   B N   
5446 C  CA  . ASN   B 101 ? 0.4025 0.2902 0.3040 0.0700  0.0166  0.1375  101 ASN   B CA  
5447 C  C   . ASN   B 101 ? 0.4492 0.3260 0.2968 0.0721  0.0041  0.1513  101 ASN   B C   
5448 O  O   . ASN   B 101 ? 0.4564 0.3409 0.3279 0.0769  0.0089  0.1155  101 ASN   B O   
5449 C  CB  . ASN   B 101 ? 0.4008 0.2748 0.3206 0.0623  0.0175  0.1207  101 ASN   B CB  
5450 C  CG  . ASN   B 101 ? 0.3999 0.2558 0.3137 0.0564  0.0204  0.1262  101 ASN   B CG  
5451 O  OD1 . ASN   B 101 ? 0.4039 0.2583 0.3421 0.0436  0.0428  0.1157  101 ASN   B OD1 
5452 N  ND2 . ASN   B 101 ? 0.3983 0.2546 0.3043 0.0538  0.0152  0.1078  101 ASN   B ND2 
5460 N  N   . LYS   B 102 ? 0.4853 0.3570 0.3140 0.0609  0.0090  0.1546  102 LYS   B N   
5461 C  CA  . LYS   B 102 ? 0.5196 0.4003 0.3416 0.0415  0.0179  0.1214  102 LYS   B CA  
5462 C  C   . LYS   B 102 ? 0.5157 0.4033 0.3139 0.0401  0.0296  0.1239  102 LYS   B C   
5463 O  O   . LYS   B 102 ? 0.5281 0.4100 0.3330 0.0430  0.0121  0.1127  102 LYS   B O   
5464 C  CB  . LYS   B 102 ? 0.5534 0.4383 0.4130 0.0247  0.0274  0.0724  102 LYS   B CB  
5465 C  CG  . LYS   B 102 ? 0.5821 0.4720 0.4801 0.0114  0.0372  0.0279  102 LYS   B CG  
5466 C  CD  . LYS   B 102 ? 0.6052 0.4995 0.5518 0.0019  0.0491  -0.0060 102 LYS   B CD  
5467 C  CE  . LYS   B 102 ? 0.6220 0.5189 0.6051 -0.0048 0.0558  -0.0315 102 LYS   B CE  
5468 N  NZ  . LYS   B 102 ? 0.6305 0.5300 0.6355 -0.0073 0.0561  -0.0452 102 LYS   B NZ  
5482 N  N   . GLY   B 103 ? 0.4943 0.3955 0.3060 0.0342  0.0588  0.1252  103 GLY   B N   
5483 C  CA  . GLY   B 103 ? 0.4711 0.3872 0.3142 0.0343  0.0793  0.0995  103 GLY   B CA  
5484 C  C   . GLY   B 103 ? 0.4445 0.3741 0.3148 0.0327  0.0946  0.0772  103 GLY   B C   
5485 O  O   . GLY   B 103 ? 0.4515 0.3839 0.3245 0.0305  0.0989  0.0809  103 GLY   B O   
5489 N  N   A GLU   B 104 ? 0.4273 0.3638 0.3074 0.0368  0.1004  0.0608  104 GLU   B N   
5490 N  N   B GLU   B 104 ? 0.4248 0.3571 0.3029 0.0277  0.0975  0.0639  104 GLU   B N   
5491 C  CA  A GLU   B 104 ? 0.4085 0.3540 0.2937 0.0440  0.1025  0.0460  104 GLU   B CA  
5492 C  CA  B GLU   B 104 ? 0.4038 0.3409 0.2836 0.0255  0.0960  0.0526  104 GLU   B CA  
5493 C  C   A GLU   B 104 ? 0.4098 0.3577 0.3129 0.0296  0.1294  0.0452  104 GLU   B C   
5494 C  C   B GLU   B 104 ? 0.4013 0.3404 0.3003 0.0160  0.1204  0.0530  104 GLU   B C   
5495 O  O   A GLU   B 104 ? 0.4134 0.3636 0.3311 0.0253  0.1239  0.0406  104 GLU   B O   
5496 O  O   B GLU   B 104 ? 0.4051 0.3439 0.3206 0.0131  0.1139  0.0450  104 GLU   B O   
5497 C  CB  A GLU   B 104 ? 0.3925 0.3394 0.2838 0.0662  0.0690  0.0217  104 GLU   B CB  
5498 C  CB  B GLU   B 104 ? 0.3895 0.3237 0.2711 0.0327  0.0610  0.0305  104 GLU   B CB  
5499 C  CG  A GLU   B 104 ? 0.3783 0.3280 0.2699 0.0867  0.0318  -0.0056 104 GLU   B CG  
5500 C  CG  B GLU   B 104 ? 0.3775 0.3095 0.2534 0.0389  0.0223  0.0046  104 GLU   B CG  
5501 C  CD  A GLU   B 104 ? 0.3669 0.3182 0.2545 0.1034  -0.0015 -0.0187 104 GLU   B CD  
5502 C  CD  B GLU   B 104 ? 0.3688 0.2963 0.2313 0.0400  -0.0091 -0.0055 104 GLU   B CD  
5503 O  OE1 A GLU   B 104 ? 0.3519 0.3058 0.2185 0.1182  0.0037  -0.0206 104 GLU   B OE1 
5504 O  OE1 B GLU   B 104 ? 0.3571 0.2846 0.2012 0.0420  -0.0066 -0.0051 104 GLU   B OE1 
5505 O  OE2 A GLU   B 104 ? 0.3694 0.3233 0.2615 0.1032  -0.0274 -0.0297 104 GLU   B OE2 
5506 O  OE2 B GLU   B 104 ? 0.3710 0.2980 0.2258 0.0369  -0.0349 -0.0140 104 GLU   B OE2 
5519 N  N   A ASP   B 105 ? 0.4048 0.3564 0.3129 0.0185  0.1547  0.0490  105 ASP   B N   
5520 N  N   B ASP   B 105 ? 0.3925 0.3375 0.2887 0.0072  0.1455  0.0609  105 ASP   B N   
5521 C  CA  A ASP   B 105 ? 0.4033 0.3560 0.3390 0.0084  0.1677  0.0390  105 ASP   B CA  
5522 C  CA  B ASP   B 105 ? 0.3872 0.3349 0.3053 -0.0006 0.1601  0.0538  105 ASP   B CA  
5523 C  C   A ASP   B 105 ? 0.3898 0.3330 0.3121 -0.0009 0.1691  0.0388  105 ASP   B C   
5524 C  C   B ASP   B 105 ? 0.3762 0.3155 0.2868 -0.0095 0.1603  0.0475  105 ASP   B C   
5525 O  O   A ASP   B 105 ? 0.3850 0.3304 0.3056 0.0010  0.1726  0.0415  105 ASP   B O   
5526 O  O   B ASP   B 105 ? 0.3693 0.3105 0.2814 -0.0106 0.1640  0.0526  105 ASP   B O   
5527 C  CB  A ASP   B 105 ? 0.4141 0.3750 0.4020 0.0113  0.1732  0.0235  105 ASP   B CB  
5528 C  CB  B ASP   B 105 ? 0.3927 0.3492 0.3518 0.0033  0.1663  0.0478  105 ASP   B CB  
5529 C  CG  A ASP   B 105 ? 0.4225 0.3903 0.4631 0.0116  0.1826  0.0121  105 ASP   B CG  
5530 C  CG  B ASP   B 105 ? 0.3968 0.3592 0.3957 0.0022  0.1784  0.0476  105 ASP   B CG  
5531 O  OD1 A ASP   B 105 ? 0.4230 0.3942 0.4723 0.0073  0.1934  0.0139  105 ASP   B OD1 
5532 O  OD1 B ASP   B 105 ? 0.3952 0.3636 0.3990 -0.0044 0.1880  0.0532  105 ASP   B OD1 
5533 O  OD2 A ASP   B 105 ? 0.4269 0.3976 0.4938 0.0150  0.1792  0.0029  105 ASP   B OD2 
5534 O  OD2 B ASP   B 105 ? 0.3970 0.3622 0.4055 0.0028  0.1867  0.0481  105 ASP   B OD2 
5543 N  N   A ILE   B 106 ? 0.3781 0.3100 0.3125 -0.0092 0.1585  0.0398  106 ILE   B N   
5544 N  N   B ILE   B 106 ? 0.3689 0.2997 0.2893 -0.0133 0.1474  0.0378  106 ILE   B N   
5545 C  CA  A ILE   B 106 ? 0.3573 0.2838 0.3191 -0.0223 0.1572  0.0401  106 ILE   B CA  
5546 C  CA  B ILE   B 106 ? 0.3529 0.2824 0.3028 -0.0223 0.1436  0.0286  106 ILE   B CA  
5547 C  C   A ILE   B 106 ? 0.3283 0.2747 0.3192 -0.0185 0.1547  0.0259  106 ILE   B C   
5548 C  C   B ILE   B 106 ? 0.3263 0.2775 0.3071 -0.0194 0.1400  0.0107  106 ILE   B C   
5549 O  O   A ILE   B 106 ? 0.3216 0.2551 0.3194 -0.0222 0.1541  0.0259  106 ILE   B O   
5550 O  O   B ILE   B 106 ? 0.3198 0.2601 0.3054 -0.0257 0.1342  0.0054  106 ILE   B O   
5551 C  CB  A ILE   B 106 ? 0.3692 0.2727 0.3348 -0.0351 0.1455  0.0469  106 ILE   B CB  
5552 C  CB  B ILE   B 106 ? 0.3669 0.2770 0.3208 -0.0313 0.1316  0.0302  106 ILE   B CB  
5553 C  CG1 A ILE   B 106 ? 0.3738 0.2701 0.3378 -0.0312 0.1378  0.0425  106 ILE   B CG1 
5554 C  CG1 B ILE   B 106 ? 0.3737 0.2774 0.3320 -0.0249 0.1199  0.0263  106 ILE   B CG1 
5555 C  CG2 A ILE   B 106 ? 0.3729 0.2731 0.3530 -0.0434 0.1422  0.0494  106 ILE   B CG2 
5556 C  CG2 B ILE   B 106 ? 0.3706 0.2792 0.3366 -0.0389 0.1300  0.0284  106 ILE   B CG2 
5557 C  CD1 A ILE   B 106 ? 0.3765 0.2703 0.3295 -0.0255 0.1339  0.0441  106 ILE   B CD1 
5558 C  CD1 B ILE   B 106 ? 0.3774 0.2790 0.3292 -0.0182 0.1143  0.0271  106 ILE   B CD1 
5581 N  N   A GLN   B 107 ? 0.3098 0.2863 0.3311 -0.0165 0.1474  0.0230  107 GLN   B N   
5582 N  N   B GLN   B 107 ? 0.3103 0.2907 0.3248 -0.0158 0.1357  0.0082  107 GLN   B N   
5583 C  CA  A GLN   B 107 ? 0.2931 0.2990 0.3500 -0.0126 0.1281  0.0195  107 GLN   B CA  
5584 C  CA  B GLN   B 107 ? 0.2953 0.3038 0.3450 -0.0121 0.1226  0.0108  107 GLN   B CA  
5585 C  C   A GLN   B 107 ? 0.2594 0.2761 0.3164 -0.0049 0.1056  0.0141  107 GLN   B C   
5586 C  C   B GLN   B 107 ? 0.2621 0.2812 0.3130 -0.0063 0.1040  0.0096  107 GLN   B C   
5587 O  O   A GLN   B 107 ? 0.2486 0.2729 0.3451 0.0017  0.0797  -0.0029 107 GLN   B O   
5588 O  O   B GLN   B 107 ? 0.2548 0.2833 0.3421 -0.0037 0.0785  -0.0073 107 GLN   B O   
5589 C  CB  A GLN   B 107 ? 0.3210 0.3361 0.4162 -0.0108 0.1088  0.0182  107 GLN   B CB  
5590 C  CB  B GLN   B 107 ? 0.3236 0.3407 0.4108 -0.0091 0.1068  0.0117  107 GLN   B CB  
5591 C  CG  A GLN   B 107 ? 0.3476 0.3684 0.4810 -0.0064 0.0836  0.0145  107 GLN   B CG  
5592 C  CG  B GLN   B 107 ? 0.3509 0.3731 0.4759 -0.0036 0.0845  0.0095  107 GLN   B CG  
5593 C  CD  A GLN   B 107 ? 0.3660 0.3934 0.5361 -0.0057 0.0657  0.0146  107 GLN   B CD  
5594 C  CD  B GLN   B 107 ? 0.3704 0.3982 0.5321 -0.0020 0.0676  0.0101  107 GLN   B CD  
5595 O  OE1 A GLN   B 107 ? 0.3728 0.4031 0.5547 -0.0076 0.0638  0.0120  107 GLN   B OE1 
5596 O  OE1 B GLN   B 107 ? 0.3782 0.4081 0.5498 -0.0043 0.0662  0.0094  107 GLN   B OE1 
5597 N  NE2 A GLN   B 107 ? 0.3724 0.4011 0.5534 -0.0013 0.0571  0.0184  107 GLN   B NE2 
5598 N  NE2 B GLN   B 107 ? 0.3766 0.4060 0.5505 0.0024  0.0601  0.0126  107 GLN   B NE2 
5615 N  N   . LEU   B 108 ? 0.2388 0.2592 0.2795 0.0108  0.0942  0.0148  108 LEU   B N   
5616 C  CA  . LEU   B 108 ? 0.2203 0.2334 0.2287 0.0291  0.0671  0.0231  108 LEU   B CA  
5617 C  C   . LEU   B 108 ? 0.1899 0.1913 0.2193 0.0275  0.0374  0.0274  108 LEU   B C   
5618 O  O   . LEU   B 108 ? 0.1872 0.1783 0.2079 0.0281  0.0289  0.0253  108 LEU   B O   
5619 C  CB  . LEU   B 108 ? 0.2352 0.2556 0.2190 0.0291  0.0703  0.0342  108 LEU   B CB  
5620 C  CG  . LEU   B 108 ? 0.2506 0.2874 0.2263 0.0323  0.0575  0.0111  108 LEU   B CG  
5621 C  CD1 . LEU   B 108 ? 0.2596 0.3013 0.2062 0.0227  0.0652  0.0108  108 LEU   B CD1 
5622 C  CD2 . LEU   B 108 ? 0.2657 0.3018 0.2490 0.0402  0.0413  -0.0019 108 LEU   B CD2 
5635 N  N   . LEU   B 109 ? 0.1795 0.1678 0.2073 0.0191  0.0325  0.0214  109 LEU   B N   
5636 C  CA  . LEU   B 109 ? 0.1597 0.1431 0.2246 0.0081  0.0304  0.0278  109 LEU   B CA  
5637 C  C   . LEU   B 109 ? 0.1476 0.1310 0.2191 0.0082  0.0313  0.0255  109 LEU   B C   
5638 O  O   . LEU   B 109 ? 0.1431 0.1322 0.2149 0.0069  0.0297  0.0373  109 LEU   B O   
5639 C  CB  . LEU   B 109 ? 0.1666 0.1412 0.2249 0.0046  0.0220  0.0387  109 LEU   B CB  
5640 C  CG  . LEU   B 109 ? 0.1635 0.1336 0.2343 0.0046  0.0203  0.0226  109 LEU   B CG  
5641 C  CD1 . LEU   B 109 ? 0.1646 0.1448 0.2171 0.0097  0.0203  0.0233  109 LEU   B CD1 
5642 C  CD2 . LEU   B 109 ? 0.1716 0.1412 0.2553 0.0082  0.0150  0.0227  109 LEU   B CD2 
5654 N  N   . LYS   B 110 ? 0.1417 0.1354 0.2141 -0.0003 0.0279  0.0204  110 LYS   B N   
5655 C  CA  . LYS   B 110 ? 0.1389 0.1306 0.2125 -0.0012 0.0260  0.0206  110 LYS   B CA  
5656 C  C   . LYS   B 110 ? 0.1344 0.1354 0.2018 0.0034  0.0255  0.0156  110 LYS   B C   
5657 O  O   . LYS   B 110 ? 0.1317 0.1353 0.2016 -0.0019 0.0175  0.0037  110 LYS   B O   
5658 C  CB  . LYS   B 110 ? 0.1424 0.1274 0.2374 -0.0014 0.0249  0.0187  110 LYS   B CB  
5659 C  CG  . LYS   B 110 ? 0.1430 0.1276 0.2531 -0.0094 0.0116  0.0149  110 LYS   B CG  
5660 C  CD  . LYS   B 110 ? 0.1485 0.1325 0.2528 -0.0066 0.0104  0.0130  110 LYS   B CD  
5661 C  CE  . LYS   B 110 ? 0.1428 0.1483 0.2762 -0.0019 0.0069  0.0072  110 LYS   B CE  
5662 N  NZ  . LYS   B 110 ? 0.1422 0.1618 0.2685 -0.0006 -0.0082 -0.0010 110 LYS   B NZ  
5676 N  N   . SER   B 111 ? 0.1447 0.1330 0.2035 -0.0022 0.0252  0.0180  111 SER   B N   
5677 C  CA  . SER   B 111 ? 0.1504 0.1363 0.1935 0.0020  0.0187  0.0148  111 SER   B CA  
5678 C  C   . SER   B 111 ? 0.1382 0.1290 0.1826 0.0020  0.0157  0.0093  111 SER   B C   
5679 O  O   . SER   B 111 ? 0.1342 0.1328 0.1946 -0.0009 0.0080  0.0144  111 SER   B O   
5680 C  CB  . SER   B 111 ? 0.1610 0.1580 0.2015 0.0060  0.0310  0.0262  111 SER   B CB  
5681 O  OG  . SER   B 111 ? 0.1809 0.1936 0.1993 0.0114  0.0397  0.0274  111 SER   B OG  
5687 N  N   . ALA   B 112 ? 0.1337 0.1332 0.1917 0.0085  0.0210  0.0196  112 ALA   B N   
5688 C  CA  . ALA   B 112 ? 0.1333 0.1374 0.1785 0.0056  0.0077  0.0057  112 ALA   B CA  
5689 C  C   . ALA   B 112 ? 0.1230 0.1265 0.1750 0.0021  0.0065  0.0084  112 ALA   B C   
5690 O  O   . ALA   B 112 ? 0.1258 0.1263 0.1962 -0.0014 0.0090  0.0054  112 ALA   B O   
5691 C  CB  . ALA   B 112 ? 0.1306 0.1440 0.1954 0.0078  0.0063  0.0150  112 ALA   B CB  
5697 N  N   . TYR   B 113 ? 0.1261 0.1188 0.1946 -0.0014 0.0159  0.0133  113 TYR   B N   
5698 C  CA  . TYR   B 113 ? 0.1201 0.1197 0.1817 0.0009  0.0176  0.0040  113 TYR   B CA  
5699 C  C   . TYR   B 113 ? 0.1156 0.1137 0.1777 -0.0067 0.0079  0.0087  113 TYR   B C   
5700 O  O   . TYR   B 113 ? 0.1255 0.1157 0.1742 -0.0051 0.0033  0.0043  113 TYR   B O   
5701 C  CB  . TYR   B 113 ? 0.1296 0.1182 0.1874 -0.0014 0.0148  0.0144  113 TYR   B CB  
5702 C  CG  . TYR   B 113 ? 0.1277 0.1169 0.1990 -0.0062 0.0121  0.0143  113 TYR   B CG  
5703 C  CD1 . TYR   B 113 ? 0.1369 0.1223 0.2126 -0.0075 0.0131  0.0164  113 TYR   B CD1 
5704 C  CD2 . TYR   B 113 ? 0.1371 0.1196 0.2051 -0.0068 0.0065  0.0093  113 TYR   B CD2 
5705 C  CE1 . TYR   B 113 ? 0.1377 0.1282 0.2024 -0.0027 0.0183  0.0127  113 TYR   B CE1 
5706 C  CE2 . TYR   B 113 ? 0.1414 0.1155 0.2117 0.0027  0.0105  0.0128  113 TYR   B CE2 
5707 C  CZ  . TYR   B 113 ? 0.1346 0.1232 0.2107 0.0028  0.0106  0.0119  113 TYR   B CZ  
5708 O  OH  . TYR   B 113 ? 0.1383 0.1204 0.2427 0.0122  0.0216  0.0071  113 TYR   B OH  
5718 N  N   . GLU   B 114 ? 0.1168 0.1152 0.1884 -0.0016 0.0101  0.0075  114 GLU   B N   
5719 C  CA  . GLU   B 114 ? 0.1157 0.1088 0.1820 0.0057  0.0014  0.0030  114 GLU   B CA  
5720 C  C   . GLU   B 114 ? 0.1198 0.1187 0.1695 0.0032  0.0056  0.0047  114 GLU   B C   
5721 O  O   . GLU   B 114 ? 0.1247 0.1151 0.1919 0.0018  -0.0042 0.0127  114 GLU   B O   
5722 C  CB  . GLU   B 114 ? 0.1203 0.1170 0.1973 -0.0011 0.0033  0.0106  114 GLU   B CB  
5723 C  CG  . GLU   B 114 ? 0.1263 0.1196 0.2002 0.0001  0.0062  0.0070  114 GLU   B CG  
5724 C  CD  . GLU   B 114 ? 0.1243 0.1234 0.2158 -0.0055 0.0067  0.0083  114 GLU   B CD  
5725 O  OE1 . GLU   B 114 ? 0.1218 0.1386 0.2054 -0.0070 0.0197  0.0115  114 GLU   B OE1 
5726 O  OE2 . GLU   B 114 ? 0.1232 0.1391 0.2293 -0.0149 0.0107  0.0058  114 GLU   B OE2 
5733 N  N   . ASN   B 115 ? 0.1263 0.1135 0.1623 0.0008  0.0002  0.0088  115 ASN   B N   
5734 C  CA  . ASN   B 115 ? 0.1261 0.1222 0.1579 -0.0086 -0.0032 0.0103  115 ASN   B CA  
5735 C  C   . ASN   B 115 ? 0.1187 0.1152 0.1688 -0.0119 -0.0072 -0.0025 115 ASN   B C   
5736 O  O   . ASN   B 115 ? 0.1317 0.1148 0.1725 -0.0141 -0.0002 0.0033  115 ASN   B O   
5737 C  CB  . ASN   B 115 ? 0.1362 0.1304 0.1643 -0.0070 0.0040  0.0030  115 ASN   B CB  
5738 C  CG  . ASN   B 115 ? 0.1422 0.1341 0.1647 0.0020  -0.0005 0.0033  115 ASN   B CG  
5739 O  OD1 . ASN   B 115 ? 0.1830 0.1453 0.1789 -0.0000 0.0036  -0.0126 115 ASN   B OD1 
5740 N  ND2 . ASN   B 115 ? 0.1386 0.1418 0.1644 -0.0018 0.0052  0.0029  115 ASN   B ND2 
5747 N  N   . PHE   B 116 ? 0.1227 0.1166 0.1606 -0.0088 -0.0024 0.0032  116 PHE   B N   
5748 C  CA  . PHE   B 116 ? 0.1265 0.1181 0.1535 -0.0096 -0.0026 0.0049  116 PHE   B CA  
5749 C  C   . PHE   B 116 ? 0.1269 0.1078 0.1581 -0.0076 -0.0060 0.0070  116 PHE   B C   
5750 O  O   . PHE   B 116 ? 0.1337 0.1164 0.1672 -0.0047 -0.0075 0.0066  116 PHE   B O   
5751 C  CB  . PHE   B 116 ? 0.1240 0.1177 0.1534 -0.0065 -0.0064 0.0098  116 PHE   B CB  
5752 C  CG  . PHE   B 116 ? 0.1199 0.1167 0.1598 -0.0079 -0.0029 0.0041  116 PHE   B CG  
5753 C  CD1 . PHE   B 116 ? 0.1252 0.1233 0.1809 -0.0061 -0.0016 0.0098  116 PHE   B CD1 
5754 C  CD2 . PHE   B 116 ? 0.1280 0.1236 0.1557 -0.0067 0.0015  -0.0003 116 PHE   B CD2 
5755 C  CE1 . PHE   B 116 ? 0.1297 0.1285 0.1803 -0.0062 -0.0030 0.0077  116 PHE   B CE1 
5756 C  CE2 . PHE   B 116 ? 0.1290 0.1281 0.1684 -0.0048 0.0056  0.0059  116 PHE   B CE2 
5757 C  CZ  . PHE   B 116 ? 0.1214 0.1295 0.1794 -0.0052 -0.0043 0.0091  116 PHE   B CZ  
5767 N  N   . ASN   B 117 ? 0.1219 0.1165 0.1734 -0.0033 -0.0117 0.0090  117 ASN   B N   
5768 C  CA  . ASN   B 117 ? 0.1316 0.1195 0.1675 -0.0009 -0.0107 0.0037  117 ASN   B CA  
5769 C  C   . ASN   B 117 ? 0.1348 0.1153 0.1809 -0.0025 -0.0078 0.0043  117 ASN   B C   
5770 O  O   . ASN   B 117 ? 0.1452 0.1245 0.2063 -0.0071 -0.0311 0.0075  117 ASN   B O   
5771 C  CB  . ASN   B 117 ? 0.1313 0.1217 0.1804 -0.0003 -0.0013 -0.0008 117 ASN   B CB  
5772 C  CG  . ASN   B 117 ? 0.1276 0.1232 0.1956 -0.0004 -0.0063 -0.0033 117 ASN   B CG  
5773 O  OD1 . ASN   B 117 ? 0.1551 0.1227 0.2029 -0.0137 0.0033  -0.0026 117 ASN   B OD1 
5774 N  ND2 . ASN   B 117 ? 0.1305 0.1248 0.1861 -0.0040 -0.0005 -0.0019 117 ASN   B ND2 
5781 N  N   . GLN   B 118 ? 0.1378 0.1086 0.1792 -0.0104 -0.0131 0.0028  118 GLN   B N   
5782 C  CA  . GLN   B 118 ? 0.1412 0.1185 0.1801 0.0013  -0.0065 -0.0002 118 GLN   B CA  
5783 C  C   . GLN   B 118 ? 0.1417 0.1192 0.1883 -0.0003 -0.0074 -0.0022 118 GLN   B C   
5784 O  O   . GLN   B 118 ? 0.1571 0.1147 0.2272 -0.0082 0.0035  0.0078  118 GLN   B O   
5785 C  CB  . GLN   B 118 ? 0.1471 0.1211 0.1871 0.0001  -0.0130 -0.0059 118 GLN   B CB  
5786 C  CG  . GLN   B 118 ? 0.1538 0.1264 0.1891 0.0073  -0.0079 -0.0127 118 GLN   B CG  
5787 C  CD  . GLN   B 118 ? 0.1533 0.1181 0.1834 -0.0007 -0.0083 -0.0127 118 GLN   B CD  
5788 O  OE1 . GLN   B 118 ? 0.1652 0.1215 0.2051 -0.0000 0.0004  0.0038  118 GLN   B OE1 
5789 N  NE2 . GLN   B 118 ? 0.1628 0.1205 0.1946 0.0023  -0.0118 0.0020  118 GLN   B NE2 
5798 N  N   . HIS   B 119 ? 0.1410 0.1231 0.1713 -0.0041 -0.0152 0.0077  119 HIS   B N   
5799 C  CA  . HIS   B 119 ? 0.1482 0.1330 0.1625 -0.0007 -0.0145 0.0065  119 HIS   B CA  
5800 C  C   . HIS   B 119 ? 0.1502 0.1331 0.1611 -0.0067 -0.0234 0.0072  119 HIS   B C   
5801 O  O   . HIS   B 119 ? 0.1627 0.1328 0.1784 -0.0271 -0.0186 0.0077  119 HIS   B O   
5802 C  CB  . HIS   B 119 ? 0.1506 0.1448 0.1665 -0.0033 -0.0151 0.0021  119 HIS   B CB  
5803 C  CG  . HIS   B 119 ? 0.1581 0.1635 0.1869 0.0073  -0.0396 -0.0074 119 HIS   B CG  
5804 N  ND1 . HIS   B 119 ? 0.1708 0.1752 0.2170 0.0031  -0.0427 -0.0322 119 HIS   B ND1 
5805 C  CD2 . HIS   B 119 ? 0.1688 0.1819 0.1909 0.0407  -0.0521 -0.0175 119 HIS   B CD2 
5806 C  CE1 . HIS   B 119 ? 0.1898 0.1912 0.2307 0.0170  -0.0486 -0.0447 119 HIS   B CE1 
5807 N  NE2 . HIS   B 119 ? 0.1896 0.2032 0.2153 0.0330  -0.0478 -0.0339 119 HIS   B NE2 
5815 N  N   . GLU   B 120 ? 0.1715 0.1359 0.1572 -0.0117 -0.0329 0.0147  120 GLU   B N   
5816 C  CA  . GLU   B 120 ? 0.1953 0.1493 0.1614 -0.0067 -0.0389 0.0204  120 GLU   B CA  
5817 C  C   . GLU   B 120 ? 0.1779 0.1363 0.1499 -0.0124 -0.0284 0.0222  120 GLU   B C   
5818 O  O   . GLU   B 120 ? 0.1703 0.1509 0.1651 -0.0150 -0.0249 0.0122  120 GLU   B O   
5819 C  CB  . GLU   B 120 ? 0.2627 0.1824 0.2344 0.0121  -0.0749 0.0410  120 GLU   B CB  
5820 C  CG  . GLU   B 120 ? 0.3218 0.2588 0.3402 0.0243  -0.1032 0.0653  120 GLU   B CG  
5821 C  CD  . GLU   B 120 ? 0.3722 0.3385 0.4521 0.0225  -0.1106 0.0883  120 GLU   B CD  
5822 O  OE1 . GLU   B 120 ? 0.3927 0.3612 0.4951 0.0136  -0.1020 0.1021  120 GLU   B OE1 
5823 O  OE2 . GLU   B 120 ? 0.4004 0.3830 0.5068 0.0236  -0.1140 0.0859  120 GLU   B OE2 
5830 N  N   . VAL   B 121 ? 0.1673 0.1326 0.1544 -0.0146 -0.0146 0.0117  121 VAL   B N   
5831 C  CA  . VAL   B 121 ? 0.1657 0.1475 0.1391 -0.0159 -0.0224 0.0133  121 VAL   B CA  
5832 C  C   . VAL   B 121 ? 0.1598 0.1411 0.1354 -0.0247 -0.0137 0.0112  121 VAL   B C   
5833 O  O   . VAL   B 121 ? 0.1652 0.1362 0.1627 -0.0303 -0.0217 0.0027  121 VAL   B O   
5834 C  CB  . VAL   B 121 ? 0.1877 0.1826 0.1469 -0.0033 -0.0195 0.0126  121 VAL   B CB  
5835 C  CG1 . VAL   B 121 ? 0.1910 0.1911 0.1761 -0.0136 -0.0057 0.0115  121 VAL   B CG1 
5836 C  CG2 . VAL   B 121 ? 0.2119 0.2093 0.1445 0.0013  -0.0210 -0.0016 121 VAL   B CG2 
5846 N  N   . LEU   B 122 ? 0.1454 0.1307 0.1412 -0.0201 -0.0145 0.0059  122 LEU   B N   
5847 C  CA  . LEU   B 122 ? 0.1412 0.1407 0.1217 -0.0152 -0.0188 0.0125  122 LEU   B CA  
5848 C  C   . LEU   B 122 ? 0.1416 0.1261 0.1322 -0.0215 -0.0129 0.0037  122 LEU   B C   
5849 O  O   . LEU   B 122 ? 0.1491 0.1306 0.1693 -0.0240 -0.0194 -0.0005 122 LEU   B O   
5850 C  CB  . LEU   B 122 ? 0.1643 0.1520 0.1628 -0.0009 -0.0193 0.0093  122 LEU   B CB  
5851 C  CG  . LEU   B 122 ? 0.1531 0.1557 0.1684 -0.0133 -0.0060 0.0089  122 LEU   B CG  
5852 C  CD1 . LEU   B 122 ? 0.1564 0.1762 0.1708 -0.0174 -0.0107 0.0094  122 LEU   B CD1 
5853 C  CD2 . LEU   B 122 ? 0.1546 0.1570 0.1406 -0.0135 -0.0013 0.0011  122 LEU   B CD2 
5865 N  N   . LEU   B 123 ? 0.1424 0.1214 0.1321 -0.0193 -0.0087 0.0067  123 LEU   B N   
5866 C  CA  . LEU   B 123 ? 0.1443 0.1231 0.1385 -0.0209 -0.0133 -0.0026 123 LEU   B CA  
5867 C  C   . LEU   B 123 ? 0.1364 0.1172 0.1370 -0.0262 -0.0114 -0.0013 123 LEU   B C   
5868 O  O   . LEU   B 123 ? 0.1491 0.1215 0.1421 -0.0330 -0.0118 0.0016  123 LEU   B O   
5869 C  CB  . LEU   B 123 ? 0.1479 0.1290 0.1417 -0.0245 -0.0087 -0.0066 123 LEU   B CB  
5870 C  CG  . LEU   B 123 ? 0.1480 0.1365 0.1543 -0.0180 -0.0090 0.0102  123 LEU   B CG  
5871 C  CD1 . LEU   B 123 ? 0.1608 0.1384 0.1510 -0.0174 -0.0025 -0.0095 123 LEU   B CD1 
5872 C  CD2 . LEU   B 123 ? 0.1557 0.1399 0.1789 -0.0142 -0.0025 0.0191  123 LEU   B CD2 
5884 N  N   . ALA   B 124 ? 0.1367 0.1195 0.1329 -0.0205 -0.0002 -0.0063 124 ALA   B N   
5885 C  CA  . ALA   B 124 ? 0.1323 0.1183 0.1468 -0.0131 -0.0081 -0.0076 124 ALA   B CA  
5886 C  C   . ALA   B 124 ? 0.1280 0.1184 0.1439 -0.0186 -0.0121 -0.0021 124 ALA   B C   
5887 O  O   . ALA   B 124 ? 0.1357 0.1216 0.1602 -0.0146 -0.0081 0.0024  124 ALA   B O   
5888 C  CB  . ALA   B 124 ? 0.1378 0.1240 0.1620 -0.0009 0.0001  -0.0022 124 ALA   B CB  
5894 N  N   . PRO   B 125 ? 0.1320 0.1226 0.1447 -0.0150 -0.0105 0.0094  125 PRO   B N   
5895 C  CA  . PRO   B 125 ? 0.1442 0.1236 0.1522 -0.0162 -0.0107 0.0185  125 PRO   B CA  
5896 C  C   . PRO   B 125 ? 0.1378 0.1191 0.1671 -0.0137 -0.0080 0.0078  125 PRO   B C   
5897 O  O   . PRO   B 125 ? 0.1367 0.1199 0.1890 -0.0095 0.0060  0.0143  125 PRO   B O   
5898 C  CB  . PRO   B 125 ? 0.1480 0.1474 0.1626 -0.0216 -0.0225 0.0329  125 PRO   B CB  
5899 C  CG  . PRO   B 125 ? 0.1537 0.1522 0.1543 -0.0300 -0.0185 0.0119  125 PRO   B CG  
5900 C  CD  . PRO   B 125 ? 0.1466 0.1372 0.1458 -0.0308 -0.0067 0.0085  125 PRO   B CD  
5908 N  N   . LEU   B 126 ? 0.1439 0.1108 0.1894 -0.0134 0.0108  0.0109  126 LEU   B N   
5909 C  CA  . LEU   B 126 ? 0.1478 0.1239 0.1995 -0.0123 0.0242  0.0094  126 LEU   B CA  
5910 C  C   . LEU   B 126 ? 0.1449 0.1309 0.2051 0.0042  0.0240  0.0179  126 LEU   B C   
5911 O  O   . LEU   B 126 ? 0.1617 0.1615 0.2124 0.0170  0.0022  -0.0025 126 LEU   B O   
5912 C  CB  . LEU   B 126 ? 0.1726 0.1240 0.2337 -0.0197 0.0261  0.0098  126 LEU   B CB  
5913 C  CG  . LEU   B 126 ? 0.1836 0.1297 0.2424 -0.0263 0.0233  -0.0122 126 LEU   B CG  
5914 C  CD1 . LEU   B 126 ? 0.1979 0.1423 0.2823 -0.0247 0.0149  -0.0178 126 LEU   B CD1 
5915 C  CD2 . LEU   B 126 ? 0.1807 0.1489 0.2343 -0.0286 0.0150  -0.0140 126 LEU   B CD2 
5927 N  N   . LEU   B 127 ? 0.1417 0.1246 0.2013 0.0044  0.0206  0.0129  127 LEU   B N   
5928 C  CA  . LEU   B 127 ? 0.1423 0.1333 0.2107 -0.0042 0.0252  0.0276  127 LEU   B CA  
5929 C  C   . LEU   B 127 ? 0.1381 0.1281 0.2123 0.0017  0.0207  0.0268  127 LEU   B C   
5930 O  O   . LEU   B 127 ? 0.1456 0.1304 0.2105 -0.0106 0.0132  0.0248  127 LEU   B O   
5931 C  CB  . LEU   B 127 ? 0.1524 0.1327 0.2136 -0.0027 0.0190  0.0246  127 LEU   B CB  
5932 C  CG  . LEU   B 127 ? 0.1657 0.1309 0.2290 0.0016  0.0242  0.0225  127 LEU   B CG  
5933 C  CD1 . LEU   B 127 ? 0.1694 0.1279 0.2343 0.0105  0.0174  0.0170  127 LEU   B CD1 
5934 C  CD2 . LEU   B 127 ? 0.1688 0.1399 0.2484 -0.0050 0.0247  0.0320  127 LEU   B CD2 
5946 N  N   . SER   B 128 ? 0.1411 0.1285 0.2036 0.0044  0.0092  0.0199  128 SER   B N   
5947 C  CA  . SER   B 128 ? 0.1537 0.1396 0.1969 0.0135  -0.0006 0.0207  128 SER   B CA  
5948 C  C   . SER   B 128 ? 0.1632 0.1405 0.2251 0.0091  -0.0129 0.0208  128 SER   B C   
5949 O  O   . SER   B 128 ? 0.1763 0.1423 0.2561 0.0030  -0.0151 0.0314  128 SER   B O   
5950 C  CB  . SER   B 128 ? 0.1648 0.1394 0.1966 0.0070  0.0056  0.0299  128 SER   B CB  
5951 O  OG  . SER   B 128 ? 0.1757 0.1551 0.2085 0.0129  0.0125  0.0345  128 SER   B OG  
5957 N  N   . ALA   B 129 ? 0.1785 0.1424 0.2528 0.0270  -0.0095 -0.0027 129 ALA   B N   
5958 C  CA  . ALA   B 129 ? 0.2001 0.1524 0.2622 0.0358  -0.0086 -0.0111 129 ALA   B CA  
5959 C  C   . ALA   B 129 ? 0.1851 0.1479 0.2551 0.0250  0.0111  0.0012  129 ALA   B C   
5960 O  O   . ALA   B 129 ? 0.1671 0.1476 0.2565 0.0178  0.0041  0.0125  129 ALA   B O   
5961 C  CB  . ALA   B 129 ? 0.2282 0.1791 0.2882 0.0381  -0.0031 -0.0208 129 ALA   B CB  
5967 N  N   . GLY   B 130 ? 0.1796 0.1439 0.2586 0.0300  0.0143  -0.0011 130 GLY   B N   
5968 C  CA  . GLY   B 130 ? 0.1802 0.1536 0.2667 0.0247  0.0285  0.0004  130 GLY   B CA  
5969 C  C   . GLY   B 130 ? 0.1825 0.1536 0.2579 0.0183  0.0204  0.0111  130 GLY   B C   
5970 O  O   . GLY   B 130 ? 0.1972 0.1674 0.2681 0.0175  0.0190  0.0199  130 GLY   B O   
5974 N  N   . ILE   B 131 ? 0.1784 0.1680 0.2670 0.0345  0.0224  0.0093  131 ILE   B N   
5975 C  CA  . ILE   B 131 ? 0.1971 0.1837 0.2574 0.0320  0.0102  0.0241  131 ILE   B CA  
5976 C  C   . ILE   B 131 ? 0.2085 0.1771 0.2307 0.0249  0.0126  0.0229  131 ILE   B C   
5977 O  O   . ILE   B 131 ? 0.2374 0.1883 0.2414 0.0267  -0.0047 0.0202  131 ILE   B O   
5978 C  CB  . ILE   B 131 ? 0.1974 0.2214 0.2974 0.0281  -0.0062 0.0273  131 ILE   B CB  
5979 C  CG1 . ILE   B 131 ? 0.2021 0.2469 0.3030 -0.0021 -0.0041 0.0324  131 ILE   B CG1 
5980 C  CG2 . ILE   B 131 ? 0.1994 0.2369 0.3245 0.0352  -0.0024 0.0189  131 ILE   B CG2 
5981 C  CD1 . ILE   B 131 ? 0.2090 0.2672 0.3082 -0.0230 -0.0083 0.0413  131 ILE   B CD1 
5993 N  N   . PHE   B 132 ? 0.1915 0.1586 0.2279 0.0168  0.0216  0.0191  132 PHE   B N   
5994 C  CA  . PHE   B 132 ? 0.2047 0.1596 0.2213 0.0120  0.0351  0.0109  132 PHE   B CA  
5995 C  C   . PHE   B 132 ? 0.2267 0.1714 0.2321 0.0151  0.0428  0.0112  132 PHE   B C   
5996 O  O   . PHE   B 132 ? 0.2461 0.1957 0.2583 0.0077  0.0580  0.0212  132 PHE   B O   
5997 C  CB  . PHE   B 132 ? 0.1880 0.1591 0.2020 0.0134  0.0341  0.0188  132 PHE   B CB  
5998 C  CG  . PHE   B 132 ? 0.1830 0.1609 0.1898 0.0183  0.0253  0.0135  132 PHE   B CG  
5999 C  CD1 . PHE   B 132 ? 0.1921 0.1634 0.2305 0.0166  0.0257  0.0136  132 PHE   B CD1 
6000 C  CD2 . PHE   B 132 ? 0.1829 0.1659 0.1655 0.0258  0.0219  0.0224  132 PHE   B CD2 
6001 C  CE1 . PHE   B 132 ? 0.1940 0.1645 0.2446 0.0104  0.0175  0.0174  132 PHE   B CE1 
6002 C  CE2 . PHE   B 132 ? 0.1917 0.1718 0.1791 0.0226  0.0195  0.0138  132 PHE   B CE2 
6003 C  CZ  . PHE   B 132 ? 0.1965 0.1686 0.2237 0.0145  0.0032  0.0251  132 PHE   B CZ  
6013 N  N   . GLY   B 133 ? 0.2238 0.1622 0.2237 0.0104  0.0294  0.0334  133 GLY   B N   
6014 C  CA  . GLY   B 133 ? 0.2317 0.1767 0.2429 -0.0101 0.0266  0.0528  133 GLY   B CA  
6015 C  C   . GLY   B 133 ? 0.2372 0.1869 0.2417 -0.0259 0.0285  0.0588  133 GLY   B C   
6016 O  O   . GLY   B 133 ? 0.2572 0.1999 0.2809 -0.0424 0.0244  0.0695  133 GLY   B O   
6020 N  N   . ALA   B 134 ? 0.2144 0.1792 0.2261 -0.0222 0.0334  0.0354  134 ALA   B N   
6021 C  CA  . ALA   B 134 ? 0.2076 0.1761 0.2473 -0.0143 0.0390  0.0146  134 ALA   B CA  
6022 C  C   . ALA   B 134 ? 0.2160 0.1683 0.2582 -0.0072 0.0389  0.0251  134 ALA   B C   
6023 O  O   . ALA   B 134 ? 0.2184 0.1859 0.2806 0.0033  0.0380  0.0186  134 ALA   B O   
6024 C  CB  . ALA   B 134 ? 0.2046 0.1755 0.2706 -0.0067 0.0260  0.0154  134 ALA   B CB  
6030 N  N   . ASP   B 135 ? 0.2302 0.1648 0.2542 -0.0134 0.0206  0.0354  135 ASP   B N   
6031 C  CA  . ASP   B 135 ? 0.2487 0.1568 0.2776 -0.0134 0.0045  0.0359  135 ASP   B CA  
6032 C  C   . ASP   B 135 ? 0.2272 0.1449 0.2607 -0.0007 0.0082  0.0290  135 ASP   B C   
6033 O  O   . ASP   B 135 ? 0.2192 0.1405 0.2695 0.0012  0.0067  0.0298  135 ASP   B O   
6034 C  CB  . ASP   B 135 ? 0.2833 0.1664 0.2989 -0.0388 0.0039  0.0412  135 ASP   B CB  
6035 C  CG  . ASP   B 135 ? 0.3143 0.1706 0.3463 -0.0598 0.0020  0.0296  135 ASP   B CG  
6036 O  OD1 . ASP   B 135 ? 0.3183 0.1556 0.3379 -0.0395 -0.0019 0.0264  135 ASP   B OD1 
6037 O  OD2 . ASP   B 135 ? 0.3410 0.2087 0.3983 -0.0758 -0.0026 0.0066  135 ASP   B OD2 
6042 N  N   . PRO   B 136 ? 0.2180 0.1501 0.2770 0.0211  -0.0017 0.0252  136 PRO   B N   
6043 C  CA  . PRO   B 136 ? 0.1993 0.1459 0.2717 0.0184  0.0001  0.0111  136 PRO   B CA  
6044 C  C   . PRO   B 136 ? 0.1766 0.1298 0.2796 0.0147  0.0004  0.0080  136 PRO   B C   
6045 O  O   . PRO   B 136 ? 0.1579 0.1281 0.2728 0.0077  -0.0010 0.0165  136 PRO   B O   
6046 C  CB  . PRO   B 136 ? 0.2062 0.1695 0.2816 0.0337  -0.0032 0.0059  136 PRO   B CB  
6047 C  CG  . PRO   B 136 ? 0.2265 0.1754 0.3037 0.0360  0.0003  0.0046  136 PRO   B CG  
6048 C  CD  . PRO   B 136 ? 0.2274 0.1644 0.2910 0.0387  0.0018  0.0183  136 PRO   B CD  
6056 N  N   . ILE   B 137 ? 0.1880 0.1239 0.2901 0.0141  -0.0089 0.0103  137 ILE   B N   
6057 C  CA  . ILE   B 137 ? 0.1950 0.1258 0.2948 -0.0041 0.0006  0.0107  137 ILE   B CA  
6058 C  C   . ILE   B 137 ? 0.1807 0.1279 0.2761 -0.0076 0.0126  0.0180  137 ILE   B C   
6059 O  O   . ILE   B 137 ? 0.1740 0.1325 0.2757 -0.0117 0.0059  0.0127  137 ILE   B O   
6060 C  CB  . ILE   B 137 ? 0.2221 0.1352 0.3498 -0.0106 -0.0029 0.0183  137 ILE   B CB  
6061 C  CG1 . ILE   B 137 ? 0.2532 0.1496 0.4078 -0.0023 0.0037  -0.0012 137 ILE   B CG1 
6062 C  CG2 . ILE   B 137 ? 0.2284 0.1356 0.3594 -0.0304 -0.0060 0.0206  137 ILE   B CG2 
6063 C  CD1 . ILE   B 137 ? 0.2758 0.1758 0.4505 0.0103  0.0016  0.0024  137 ILE   B CD1 
6075 N  N   . HIS   B 138 ? 0.1826 0.1303 0.2788 -0.0065 0.0196  0.0170  138 HIS   B N   
6076 C  CA  . HIS   B 138 ? 0.1945 0.1404 0.2802 -0.0060 0.0330  0.0136  138 HIS   B CA  
6077 C  C   . HIS   B 138 ? 0.1795 0.1353 0.2684 -0.0055 0.0282  0.0258  138 HIS   B C   
6078 O  O   . HIS   B 138 ? 0.1699 0.1420 0.2948 0.0007  0.0368  0.0435  138 HIS   B O   
6079 C  CB  . HIS   B 138 ? 0.2221 0.1477 0.2953 -0.0100 0.0538  0.0095  138 HIS   B CB  
6080 C  CG  . HIS   B 138 ? 0.2527 0.1655 0.2936 -0.0107 0.0674  0.0356  138 HIS   B CG  
6081 N  ND1 . HIS   B 138 ? 0.2653 0.1827 0.3169 -0.0036 0.0768  0.0255  138 HIS   B ND1 
6082 C  CD2 . HIS   B 138 ? 0.2734 0.1774 0.2795 -0.0110 0.0825  0.0280  138 HIS   B CD2 
6083 C  CE1 . HIS   B 138 ? 0.2748 0.1846 0.3069 -0.0066 0.0900  0.0257  138 HIS   B CE1 
6084 N  NE2 . HIS   B 138 ? 0.2821 0.1736 0.2843 -0.0027 0.0881  0.0211  138 HIS   B NE2 
6092 N  N   . SER   B 139 ? 0.1767 0.1264 0.2619 0.0034  0.0194  0.0207  139 SER   B N   
6093 C  CA  . SER   B 139 ? 0.1707 0.1205 0.2542 -0.0044 0.0185  0.0066  139 SER   B CA  
6094 C  C   . SER   B 139 ? 0.1509 0.1157 0.2413 -0.0030 0.0095  0.0059  139 SER   B C   
6095 O  O   . SER   B 139 ? 0.1526 0.1154 0.2438 -0.0024 0.0022  0.0112  139 SER   B O   
6096 C  CB  . SER   B 139 ? 0.1742 0.1243 0.2629 0.0004  0.0086  0.0054  139 SER   B CB  
6097 O  OG  . SER   B 139 ? 0.1740 0.1212 0.2567 -0.0020 -0.0081 0.0188  139 SER   B OG  
6103 N  N   . LEU   B 140 ? 0.1517 0.1101 0.2445 -0.0098 0.0149  0.0023  140 LEU   B N   
6104 C  CA  . LEU   B 140 ? 0.1444 0.1108 0.2453 -0.0006 0.0133  0.0047  140 LEU   B CA  
6105 C  C   . LEU   B 140 ? 0.1486 0.1109 0.2564 -0.0025 0.0023  -0.0029 140 LEU   B C   
6106 O  O   . LEU   B 140 ? 0.1436 0.1222 0.2406 -0.0014 0.0010  0.0026  140 LEU   B O   
6107 C  CB  . LEU   B 140 ? 0.1465 0.1119 0.2451 -0.0096 0.0154  -0.0034 140 LEU   B CB  
6108 C  CG  . LEU   B 140 ? 0.1504 0.1212 0.2396 -0.0078 0.0105  -0.0004 140 LEU   B CG  
6109 C  CD1 . LEU   B 140 ? 0.1644 0.1265 0.2635 -0.0146 0.0143  -0.0013 140 LEU   B CD1 
6110 C  CD2 . LEU   B 140 ? 0.1672 0.1388 0.2575 -0.0096 0.0102  -0.0118 140 LEU   B CD2 
6122 N  N   . ARG   B 141 ? 0.1429 0.1156 0.2585 -0.0080 0.0107  -0.0033 141 ARG   B N   
6123 C  CA  . ARG   B 141 ? 0.1429 0.1158 0.2996 -0.0119 0.0266  0.0002  141 ARG   B CA  
6124 C  C   . ARG   B 141 ? 0.1358 0.1154 0.2856 -0.0137 0.0190  -0.0051 141 ARG   B C   
6125 O  O   . ARG   B 141 ? 0.1447 0.1205 0.2752 -0.0117 0.0089  -0.0090 141 ARG   B O   
6126 C  CB  . ARG   B 141 ? 0.1592 0.1260 0.3241 -0.0188 0.0328  0.0013  141 ARG   B CB  
6127 C  CG  . ARG   B 141 ? 0.1902 0.1514 0.3377 -0.0256 0.0317  0.0033  141 ARG   B CG  
6128 C  CD  . ARG   B 141 ? 0.2336 0.1780 0.3422 -0.0241 0.0166  -0.0108 141 ARG   B CD  
6129 N  NE  . ARG   B 141 ? 0.2574 0.1749 0.3389 -0.0362 0.0306  -0.0194 141 ARG   B NE  
6130 C  CZ  . ARG   B 141 ? 0.2728 0.1609 0.3303 -0.0238 0.0381  -0.0307 141 ARG   B CZ  
6131 N  NH1 . ARG   B 141 ? 0.2811 0.1528 0.3197 -0.0245 0.0370  -0.0291 141 ARG   B NH1 
6132 N  NH2 . ARG   B 141 ? 0.2893 0.1673 0.3457 -0.0107 0.0263  -0.0269 141 ARG   B NH2 
6146 N  N   . VAL   B 142 ? 0.1413 0.1164 0.2638 -0.0082 0.0123  -0.0034 142 VAL   B N   
6147 C  CA  . VAL   B 142 ? 0.1365 0.1184 0.2632 -0.0007 0.0200  0.0012  142 VAL   B CA  
6148 C  C   . VAL   B 142 ? 0.1368 0.1189 0.2609 -0.0017 0.0139  -0.0044 142 VAL   B C   
6149 O  O   . VAL   B 142 ? 0.1403 0.1181 0.2712 0.0001  0.0139  -0.0022 142 VAL   B O   
6150 C  CB  . VAL   B 142 ? 0.1489 0.1262 0.2692 0.0002  0.0239  0.0050  142 VAL   B CB  
6151 C  CG1 . VAL   B 142 ? 0.1476 0.1263 0.2785 0.0061  0.0225  0.0019  142 VAL   B CG1 
6152 C  CG2 . VAL   B 142 ? 0.1715 0.1282 0.2735 -0.0049 0.0124  0.0087  142 VAL   B CG2 
6162 N  N   . CYS   B 143 ? 0.1336 0.1208 0.2388 -0.0003 0.0084  0.0088  143 CYS   B N   
6163 C  CA  . CYS   B 143 ? 0.1310 0.1175 0.2344 -0.0103 0.0078  0.0036  143 CYS   B CA  
6164 C  C   . CYS   B 143 ? 0.1267 0.1214 0.2354 -0.0080 0.0076  -0.0029 143 CYS   B C   
6165 O  O   . CYS   B 143 ? 0.1336 0.1216 0.2414 -0.0090 -0.0018 -0.0008 143 CYS   B O   
6166 C  CB  . CYS   B 143 ? 0.1382 0.1241 0.2374 -0.0116 0.0030  -0.0033 143 CYS   B CB  
6167 S  SG  . CYS   B 143 ? 0.1405 0.1398 0.2311 -0.0042 0.0061  0.0037  143 CYS   B SG  
6173 N  N   . VAL   B 144 ? 0.1300 0.1232 0.2471 -0.0097 0.0028  -0.0107 144 VAL   B N   
6174 C  CA  . VAL   B 144 ? 0.1410 0.1314 0.2688 -0.0141 -0.0068 -0.0175 144 VAL   B CA  
6175 C  C   . VAL   B 144 ? 0.1339 0.1348 0.2725 -0.0140 -0.0105 -0.0010 144 VAL   B C   
6176 O  O   . VAL   B 144 ? 0.1465 0.1530 0.2929 -0.0007 -0.0105 0.0154  144 VAL   B O   
6177 C  CB  . VAL   B 144 ? 0.1636 0.1507 0.3267 -0.0176 -0.0167 -0.0306 144 VAL   B CB  
6178 C  CG1 . VAL   B 144 ? 0.1880 0.1855 0.3637 -0.0130 -0.0143 -0.0302 144 VAL   B CG1 
6179 C  CG2 . VAL   B 144 ? 0.1771 0.1501 0.3220 -0.0066 -0.0319 -0.0401 144 VAL   B CG2 
6189 N  N   . ASP   B 145 ? 0.1355 0.1255 0.2835 -0.0080 0.0020  -0.0086 145 ASP   B N   
6190 C  CA  . ASP   B 145 ? 0.1346 0.1313 0.3125 -0.0060 0.0107  -0.0056 145 ASP   B CA  
6191 C  C   . ASP   B 145 ? 0.1340 0.1278 0.2921 -0.0080 0.0132  -0.0075 145 ASP   B C   
6192 O  O   . ASP   B 145 ? 0.1389 0.1459 0.3498 -0.0110 0.0099  -0.0199 145 ASP   B O   
6193 C  CB  . ASP   B 145 ? 0.1464 0.1428 0.3595 -0.0189 0.0213  -0.0045 145 ASP   B CB  
6194 C  CG  . ASP   B 145 ? 0.1625 0.1404 0.4021 -0.0293 0.0367  -0.0027 145 ASP   B CG  
6195 O  OD1 . ASP   B 145 ? 0.1650 0.1454 0.4048 -0.0271 0.0030  -0.0150 145 ASP   B OD1 
6196 O  OD2 . ASP   B 145 ? 0.1935 0.1431 0.4437 -0.0299 0.0586  0.0046  145 ASP   B OD2 
6201 N  N   . THR   B 146 ? 0.1264 0.1217 0.2377 -0.0093 0.0048  0.0051  146 THR   B N   
6202 C  CA  . THR   B 146 ? 0.1336 0.1190 0.2217 -0.0072 0.0072  0.0006  146 THR   B CA  
6203 C  C   . THR   B 146 ? 0.1354 0.1191 0.2174 -0.0027 0.0001  -0.0017 146 THR   B C   
6204 O  O   . THR   B 146 ? 0.1407 0.1219 0.2238 -0.0030 -0.0009 -0.0018 146 THR   B O   
6205 C  CB  . THR   B 146 ? 0.1387 0.1171 0.2389 -0.0036 0.0164  0.0082  146 THR   B CB  
6206 O  OG1 . THR   B 146 ? 0.1409 0.1200 0.2453 -0.0044 0.0193  0.0126  146 THR   B OG1 
6207 C  CG2 . THR   B 146 ? 0.1508 0.1257 0.2197 -0.0067 0.0144  0.0015  146 THR   B CG2 
6215 N  N   . VAL   B 147 ? 0.1436 0.1189 0.2067 -0.0053 0.0101  -0.0002 147 VAL   B N   
6216 C  CA  . VAL   B 147 ? 0.1403 0.1182 0.2031 -0.0113 -0.0023 -0.0041 147 VAL   B CA  
6217 C  C   . VAL   B 147 ? 0.1378 0.1178 0.2083 -0.0175 -0.0102 -0.0010 147 VAL   B C   
6218 O  O   . VAL   B 147 ? 0.1459 0.1320 0.2279 -0.0218 -0.0224 -0.0029 147 VAL   B O   
6219 C  CB  . VAL   B 147 ? 0.1399 0.1320 0.1916 -0.0092 -0.0088 0.0003  147 VAL   B CB  
6220 C  CG1 . VAL   B 147 ? 0.1397 0.1444 0.1935 -0.0113 -0.0064 0.0024  147 VAL   B CG1 
6221 C  CG2 . VAL   B 147 ? 0.1439 0.1248 0.2001 -0.0109 -0.0032 0.0014  147 VAL   B CG2 
6231 N  N   . ARG   B 148 ? 0.1403 0.1205 0.1980 -0.0131 -0.0138 -0.0098 148 ARG   B N   
6232 C  CA  . ARG   B 148 ? 0.1467 0.1309 0.1934 -0.0135 -0.0218 -0.0038 148 ARG   B CA  
6233 C  C   . ARG   B 148 ? 0.1534 0.1402 0.1841 -0.0140 -0.0251 -0.0029 148 ARG   B C   
6234 O  O   . ARG   B 148 ? 0.1666 0.1738 0.1857 -0.0270 -0.0337 0.0068  148 ARG   B O   
6235 C  CB  . ARG   B 148 ? 0.1499 0.1391 0.1988 -0.0063 -0.0303 -0.0076 148 ARG   B CB  
6236 C  CG  . ARG   B 148 ? 0.1433 0.1576 0.2173 -0.0109 -0.0288 -0.0191 148 ARG   B CG  
6237 C  CD  . ARG   B 148 ? 0.1514 0.1690 0.2276 0.0060  -0.0273 -0.0246 148 ARG   B CD  
6238 N  NE  . ARG   B 148 ? 0.1574 0.1668 0.2144 0.0216  -0.0266 -0.0195 148 ARG   B NE  
6239 C  CZ  . ARG   B 148 ? 0.1489 0.1577 0.1970 0.0139  -0.0199 -0.0214 148 ARG   B CZ  
6240 N  NH1 . ARG   B 148 ? 0.1406 0.1590 0.2124 -0.0059 -0.0031 -0.0131 148 ARG   B NH1 
6241 N  NH2 . ARG   B 148 ? 0.1680 0.1432 0.2042 0.0129  -0.0220 -0.0073 148 ARG   B NH2 
6255 N  N   . THR   B 149 ? 0.1536 0.1308 0.1919 -0.0151 -0.0251 0.0015  149 THR   B N   
6256 C  CA  . THR   B 149 ? 0.1569 0.1377 0.1863 -0.0166 -0.0174 0.0051  149 THR   B CA  
6257 C  C   . THR   B 149 ? 0.1569 0.1369 0.1684 -0.0190 -0.0245 0.0048  149 THR   B C   
6258 O  O   . THR   B 149 ? 0.1613 0.1357 0.1955 -0.0227 -0.0103 -0.0006 149 THR   B O   
6259 C  CB  . THR   B 149 ? 0.1573 0.1357 0.1870 -0.0168 -0.0203 -0.0003 149 THR   B CB  
6260 O  OG1 . THR   B 149 ? 0.1550 0.1408 0.1781 -0.0215 -0.0267 0.0021  149 THR   B OG1 
6261 C  CG2 . THR   B 149 ? 0.1605 0.1398 0.1959 -0.0115 -0.0142 0.0064  149 THR   B CG2 
6269 N  N   . ASN   B 150 ? 0.1594 0.1331 0.1693 -0.0147 -0.0256 -0.0027 150 ASN   B N   
6270 C  CA  . ASN   B 150 ? 0.1644 0.1512 0.1706 -0.0199 -0.0237 -0.0047 150 ASN   B CA  
6271 C  C   . ASN   B 150 ? 0.1535 0.1450 0.1692 -0.0181 -0.0183 -0.0059 150 ASN   B C   
6272 O  O   . ASN   B 150 ? 0.1638 0.1424 0.1858 -0.0269 -0.0402 -0.0005 150 ASN   B O   
6273 C  CB  . ASN   B 150 ? 0.1896 0.1838 0.1735 -0.0167 -0.0351 0.0063  150 ASN   B CB  
6274 C  CG  . ASN   B 150 ? 0.2156 0.2251 0.2110 -0.0194 -0.0371 0.0193  150 ASN   B CG  
6275 O  OD1 . ASN   B 150 ? 0.2237 0.2436 0.2291 -0.0309 -0.0532 0.0119  150 ASN   B OD1 
6276 N  ND2 . ASN   B 150 ? 0.2270 0.2433 0.2519 -0.0071 -0.0480 0.0542  150 ASN   B ND2 
6283 N  N   . VAL   B 151 ? 0.1397 0.1436 0.1692 -0.0203 -0.0208 0.0016  151 VAL   B N   
6284 C  CA  . VAL   B 151 ? 0.1476 0.1465 0.1655 -0.0179 -0.0181 0.0019  151 VAL   B CA  
6285 C  C   . VAL   B 151 ? 0.1508 0.1368 0.1668 -0.0273 -0.0234 -0.0036 151 VAL   B C   
6286 O  O   . VAL   B 151 ? 0.1603 0.1432 0.1955 -0.0247 -0.0164 -0.0126 151 VAL   B O   
6287 C  CB  . VAL   B 151 ? 0.1668 0.1560 0.1708 -0.0087 -0.0133 0.0018  151 VAL   B CB  
6288 C  CG1 . VAL   B 151 ? 0.1746 0.1590 0.1981 -0.0119 -0.0037 -0.0008 151 VAL   B CG1 
6289 C  CG2 . VAL   B 151 ? 0.1772 0.1718 0.1655 0.0011  -0.0104 0.0119  151 VAL   B CG2 
6299 N  N   . TYR   B 152 ? 0.1488 0.1290 0.1654 -0.0231 -0.0151 -0.0058 152 TYR   B N   
6300 C  CA  . TYR   B 152 ? 0.1546 0.1428 0.1534 -0.0299 -0.0047 -0.0069 152 TYR   B CA  
6301 C  C   . TYR   B 152 ? 0.1508 0.1244 0.1431 -0.0265 -0.0040 -0.0146 152 TYR   B C   
6302 O  O   . TYR   B 152 ? 0.1590 0.1310 0.1601 -0.0280 -0.0063 -0.0022 152 TYR   B O   
6303 C  CB  . TYR   B 152 ? 0.1707 0.1556 0.1604 -0.0276 -0.0073 0.0043  152 TYR   B CB  
6304 C  CG  . TYR   B 152 ? 0.1821 0.1669 0.1562 -0.0380 -0.0128 0.0042  152 TYR   B CG  
6305 C  CD1 . TYR   B 152 ? 0.1868 0.1796 0.1558 -0.0317 -0.0258 0.0045  152 TYR   B CD1 
6306 C  CD2 . TYR   B 152 ? 0.2047 0.1868 0.1697 -0.0391 -0.0105 -0.0053 152 TYR   B CD2 
6307 C  CE1 . TYR   B 152 ? 0.2072 0.1986 0.1641 -0.0255 -0.0285 0.0163  152 TYR   B CE1 
6308 C  CE2 . TYR   B 152 ? 0.2123 0.2070 0.1602 -0.0397 -0.0154 -0.0130 152 TYR   B CE2 
6309 C  CZ  . TYR   B 152 ? 0.2183 0.2206 0.1534 -0.0344 -0.0416 0.0098  152 TYR   B CZ  
6310 O  OH  . TYR   B 152 ? 0.2430 0.2556 0.1923 -0.0241 -0.0477 0.0135  152 TYR   B OH  
6320 N  N   . LEU   B 153 ? 0.1488 0.1270 0.1633 -0.0279 -0.0079 -0.0125 153 LEU   B N   
6321 C  CA  . LEU   B 153 ? 0.1549 0.1216 0.1521 -0.0208 -0.0013 -0.0096 153 LEU   B CA  
6322 C  C   . LEU   B 153 ? 0.1573 0.1190 0.1575 -0.0223 -0.0032 -0.0118 153 LEU   B C   
6323 O  O   . LEU   B 153 ? 0.1608 0.1429 0.1807 -0.0128 -0.0061 -0.0339 153 LEU   B O   
6324 C  CB  . LEU   B 153 ? 0.1611 0.1170 0.1645 -0.0206 -0.0013 -0.0050 153 LEU   B CB  
6325 C  CG  . LEU   B 153 ? 0.1528 0.1323 0.2022 -0.0209 -0.0032 -0.0014 153 LEU   B CG  
6326 C  CD1 . LEU   B 153 ? 0.1583 0.1457 0.2152 -0.0256 0.0028  0.0096  153 LEU   B CD1 
6327 C  CD2 . LEU   B 153 ? 0.1535 0.1470 0.1996 -0.0239 0.0086  -0.0022 153 LEU   B CD2 
6339 N  N   . ALA   B 154 ? 0.1509 0.1238 0.1747 -0.0063 -0.0137 -0.0101 154 ALA   B N   
6340 C  CA  . ALA   B 154 ? 0.1588 0.1355 0.1923 -0.0034 -0.0127 -0.0197 154 ALA   B CA  
6341 C  C   . ALA   B 154 ? 0.1690 0.1383 0.2049 -0.0029 -0.0224 -0.0225 154 ALA   B C   
6342 O  O   . ALA   B 154 ? 0.2028 0.1395 0.2113 0.0035  -0.0086 -0.0092 154 ALA   B O   
6343 C  CB  . ALA   B 154 ? 0.1548 0.1522 0.2173 -0.0034 -0.0088 -0.0306 154 ALA   B CB  
6349 N  N   . VAL   B 155 ? 0.1402 0.1275 0.2267 -0.0057 0.0003  -0.0109 155 VAL   B N   
6350 C  CA  . VAL   B 155 ? 0.1362 0.1296 0.2369 -0.0045 -0.0045 -0.0111 155 VAL   B CA  
6351 C  C   . VAL   B 155 ? 0.1383 0.1304 0.2409 -0.0047 -0.0088 -0.0191 155 VAL   B C   
6352 O  O   . VAL   B 155 ? 0.1539 0.1540 0.2744 0.0049  -0.0108 -0.0449 155 VAL   B O   
6353 C  CB  . VAL   B 155 ? 0.1415 0.1455 0.2686 -0.0074 -0.0107 -0.0050 155 VAL   B CB  
6354 C  CG1 . VAL   B 155 ? 0.1444 0.1399 0.2581 -0.0130 -0.0052 -0.0008 155 VAL   B CG1 
6355 C  CG2 . VAL   B 155 ? 0.1380 0.1570 0.3098 -0.0087 -0.0198 0.0246  155 VAL   B CG2 
6365 N  N   . PHE   B 156 ? 0.1282 0.1434 0.2534 0.0037  -0.0052 -0.0152 156 PHE   B N   
6366 C  CA  . PHE   B 156 ? 0.1350 0.1476 0.2758 0.0097  -0.0055 -0.0180 156 PHE   B CA  
6367 C  C   . PHE   B 156 ? 0.1317 0.1528 0.3163 0.0093  -0.0108 -0.0403 156 PHE   B C   
6368 O  O   . PHE   B 156 ? 0.1558 0.1772 0.3409 0.0243  0.0003  -0.0476 156 PHE   B O   
6369 C  CB  . PHE   B 156 ? 0.1448 0.1450 0.2719 0.0023  -0.0098 -0.0118 156 PHE   B CB  
6370 C  CG  . PHE   B 156 ? 0.1421 0.1572 0.2812 0.0052  -0.0099 0.0106  156 PHE   B CG  
6371 C  CD1 . PHE   B 156 ? 0.1450 0.1808 0.3139 0.0092  0.0003  0.0419  156 PHE   B CD1 
6372 C  CD2 . PHE   B 156 ? 0.1541 0.1661 0.2838 0.0107  -0.0167 0.0075  156 PHE   B CD2 
6373 C  CE1 . PHE   B 156 ? 0.1532 0.1974 0.3316 0.0087  -0.0007 0.0384  156 PHE   B CE1 
6374 C  CE2 . PHE   B 156 ? 0.1584 0.1873 0.2963 0.0152  -0.0117 0.0148  156 PHE   B CE2 
6375 C  CZ  . PHE   B 156 ? 0.1481 0.1966 0.3241 0.0180  -0.0170 0.0230  156 PHE   B CZ  
6385 N  N   . ASP   B 157 ? 0.1378 0.1421 0.3343 0.0115  -0.0217 -0.0213 157 ASP   B N   
6386 C  CA  . ASP   B 157 ? 0.1477 0.1515 0.3557 0.0075  -0.0245 -0.0275 157 ASP   B CA  
6387 C  C   . ASP   B 157 ? 0.1517 0.1523 0.3522 0.0075  -0.0160 -0.0470 157 ASP   B C   
6388 O  O   . ASP   B 157 ? 0.1405 0.1534 0.3324 0.0045  -0.0176 -0.0393 157 ASP   B O   
6389 C  CB  . ASP   B 157 ? 0.1656 0.1730 0.3700 0.0077  -0.0455 -0.0146 157 ASP   B CB  
6390 C  CG  . ASP   B 157 ? 0.2054 0.1902 0.3990 0.0039  -0.0332 -0.0181 157 ASP   B CG  
6391 O  OD1 . ASP   B 157 ? 0.2167 0.1772 0.4239 0.0106  -0.0235 -0.0161 157 ASP   B OD1 
6392 O  OD2 . ASP   B 157 ? 0.2328 0.2116 0.4255 0.0034  -0.0215 -0.0162 157 ASP   B OD2 
6397 N  N   A LYS   B 158 ? 0.1531 0.1656 0.3634 0.0062  -0.0073 -0.0687 158 LYS   B N   
6398 N  N   B LYS   B 158 ? 0.1595 0.1732 0.3598 0.0102  -0.0066 -0.0645 158 LYS   B N   
6399 C  CA  A LYS   B 158 ? 0.1660 0.1820 0.3650 0.0021  -0.0022 -0.0818 158 LYS   B CA  
6400 C  CA  B LYS   B 158 ? 0.1794 0.1979 0.3592 0.0104  -0.0002 -0.0755 158 LYS   B CA  
6401 C  C   A LYS   B 158 ? 0.1666 0.1710 0.3744 -0.0009 -0.0158 -0.0766 158 LYS   B C   
6402 C  C   B LYS   B 158 ? 0.1850 0.1935 0.3643 0.0093  -0.0086 -0.0678 158 LYS   B C   
6403 O  O   A LYS   B 158 ? 0.1661 0.1687 0.3724 -0.0133 -0.0149 -0.0914 158 LYS   B O   
6404 O  O   B LYS   B 158 ? 0.1887 0.1974 0.3599 0.0021  -0.0048 -0.0751 158 LYS   B O   
6405 C  CB  A LYS   B 158 ? 0.1887 0.2163 0.3657 0.0026  0.0091  -0.0900 158 LYS   B CB  
6406 C  CB  B LYS   B 158 ? 0.2015 0.2306 0.3610 0.0132  0.0085  -0.0876 158 LYS   B CB  
6407 C  CG  A LYS   B 158 ? 0.2181 0.2501 0.3711 0.0031  0.0130  -0.0930 158 LYS   B CG  
6408 C  CG  B LYS   B 158 ? 0.2281 0.2619 0.3661 0.0147  0.0127  -0.0937 158 LYS   B CG  
6409 C  CD  A LYS   B 158 ? 0.2375 0.2828 0.3786 0.0014  0.0116  -0.0895 158 LYS   B CD  
6410 C  CD  B LYS   B 158 ? 0.2476 0.2950 0.3738 0.0136  0.0113  -0.0921 158 LYS   B CD  
6411 C  CE  A LYS   B 158 ? 0.2518 0.3068 0.3911 0.0015  0.0053  -0.0845 158 LYS   B CE  
6412 C  CE  B LYS   B 158 ? 0.2623 0.3185 0.3869 0.0143  0.0058  -0.0871 158 LYS   B CE  
6413 N  NZ  A LYS   B 158 ? 0.2518 0.3165 0.3909 -0.0030 0.0018  -0.0849 158 LYS   B NZ  
6414 N  NZ  B LYS   B 158 ? 0.2644 0.3285 0.3883 0.0121  0.0044  -0.0862 158 LYS   B NZ  
6441 N  N   A ASN   B 159 ? 0.1680 0.1569 0.3882 0.0023  -0.0338 -0.0562 159 ASN   B N   
6442 N  N   B ASN   B 159 ? 0.1861 0.1820 0.3747 0.0095  -0.0231 -0.0520 159 ASN   B N   
6443 C  CA  A ASN   B 159 ? 0.1778 0.1531 0.4018 0.0111  -0.0475 -0.0438 159 ASN   B CA  
6444 C  CA  B ASN   B 159 ? 0.1928 0.1749 0.3866 0.0150  -0.0335 -0.0420 159 ASN   B CA  
6445 C  C   A ASN   B 159 ? 0.1676 0.1456 0.3985 0.0089  -0.0512 -0.0411 159 ASN   B C   
6446 C  C   B ASN   B 159 ? 0.1759 0.1562 0.3899 0.0140  -0.0421 -0.0419 159 ASN   B C   
6447 O  O   A ASN   B 159 ? 0.1711 0.1400 0.4164 -0.0050 -0.0530 -0.0306 159 ASN   B O   
6448 O  O   B ASN   B 159 ? 0.1786 0.1495 0.4032 0.0087  -0.0438 -0.0321 159 ASN   B O   
6449 C  CB  A ASN   B 159 ? 0.1996 0.1643 0.4223 0.0183  -0.0460 -0.0397 159 ASN   B CB  
6450 C  CB  B ASN   B 159 ? 0.2143 0.1893 0.3957 0.0195  -0.0309 -0.0362 159 ASN   B CB  
6451 C  CG  A ASN   B 159 ? 0.2229 0.1802 0.4447 0.0203  -0.0461 -0.0557 159 ASN   B CG  
6452 C  CG  B ASN   B 159 ? 0.2344 0.2078 0.4107 0.0225  -0.0346 -0.0410 159 ASN   B CG  
6453 O  OD1 A ASN   B 159 ? 0.2335 0.1793 0.4543 0.0225  -0.0379 -0.0707 159 ASN   B OD1 
6454 O  OD1 B ASN   B 159 ? 0.2445 0.2156 0.4138 0.0278  -0.0308 -0.0438 159 ASN   B OD1 
6455 N  ND2 A ASN   B 159 ? 0.2266 0.1903 0.4553 0.0239  -0.0514 -0.0501 159 ASN   B ND2 
6456 N  ND2 B ASN   B 159 ? 0.2372 0.2147 0.4204 0.0260  -0.0394 -0.0358 159 ASN   B ND2 
6469 N  N   . LEU   B 160 ? 0.1613 0.1499 0.3868 0.0083  -0.0444 -0.0376 160 LEU   B N   
6470 C  CA  . LEU   B 160 ? 0.1525 0.1484 0.3570 0.0107  -0.0382 -0.0231 160 LEU   B CA  
6471 C  C   . LEU   B 160 ? 0.1443 0.1393 0.3471 0.0025  -0.0261 -0.0316 160 LEU   B C   
6472 O  O   . LEU   B 160 ? 0.1337 0.1436 0.3390 -0.0009 -0.0209 -0.0186 160 LEU   B O   
6473 C  CB  . LEU   B 160 ? 0.1489 0.1539 0.3348 0.0009  -0.0369 -0.0098 160 LEU   B CB  
6474 C  CG  . LEU   B 160 ? 0.1538 0.1662 0.3159 0.0053  -0.0309 -0.0042 160 LEU   B CG  
6475 C  CD1 . LEU   B 160 ? 0.1669 0.1813 0.3078 -0.0008 -0.0180 -0.0065 160 LEU   B CD1 
6476 C  CD2 . LEU   B 160 ? 0.1568 0.1737 0.3219 0.0176  -0.0251 -0.0153 160 LEU   B CD2 
6489 N  N   . TYR   B 161 ? 0.1413 0.1421 0.3546 -0.0019 -0.0047 -0.0434 161 TYR   B N   
6490 C  CA  . TYR   B 161 ? 0.1524 0.1399 0.3362 -0.0117 0.0135  -0.0475 161 TYR   B CA  
6491 C  C   . TYR   B 161 ? 0.1604 0.1401 0.3250 -0.0045 0.0168  -0.0412 161 TYR   B C   
6492 O  O   . TYR   B 161 ? 0.1630 0.1392 0.3152 -0.0143 0.0122  -0.0428 161 TYR   B O   
6493 C  CB  . TYR   B 161 ? 0.1690 0.1467 0.3348 -0.0246 0.0296  -0.0533 161 TYR   B CB  
6494 C  CG  . TYR   B 161 ? 0.1922 0.1525 0.3259 -0.0307 0.0361  -0.0580 161 TYR   B CG  
6495 C  CD1 . TYR   B 161 ? 0.1993 0.1515 0.3221 -0.0404 0.0375  -0.0565 161 TYR   B CD1 
6496 C  CD2 . TYR   B 161 ? 0.2132 0.1632 0.3152 -0.0318 0.0250  -0.0665 161 TYR   B CD2 
6497 C  CE1 . TYR   B 161 ? 0.2186 0.1736 0.3217 -0.0423 0.0426  -0.0553 161 TYR   B CE1 
6498 C  CE2 . TYR   B 161 ? 0.2340 0.1817 0.3218 -0.0348 0.0330  -0.0602 161 TYR   B CE2 
6499 C  CZ  . TYR   B 161 ? 0.2351 0.1878 0.3223 -0.0469 0.0291  -0.0496 161 TYR   B CZ  
6500 O  OH  . TYR   B 161 ? 0.2605 0.2134 0.3430 -0.0517 0.0204  -0.0453 161 TYR   B OH  
6510 N  N   . ASP   B 162 ? 0.1636 0.1392 0.3465 -0.0087 -0.0026 -0.0558 162 ASP   B N   
6511 C  CA  . ASP   B 162 ? 0.1688 0.1505 0.3403 -0.0017 -0.0030 -0.0509 162 ASP   B CA  
6512 C  C   . ASP   B 162 ? 0.1642 0.1380 0.3322 -0.0090 -0.0090 -0.0455 162 ASP   B C   
6513 O  O   . ASP   B 162 ? 0.1755 0.1434 0.3436 -0.0093 -0.0231 -0.0353 162 ASP   B O   
6514 C  CB  . ASP   B 162 ? 0.1892 0.1694 0.3535 0.0039  -0.0086 -0.0687 162 ASP   B CB  
6515 C  CG  . ASP   B 162 ? 0.1962 0.1966 0.3761 0.0133  -0.0073 -0.0781 162 ASP   B CG  
6516 O  OD1 . ASP   B 162 ? 0.1941 0.2167 0.3549 0.0061  0.0149  -0.0752 162 ASP   B OD1 
6517 O  OD2 . ASP   B 162 ? 0.2135 0.2127 0.4103 0.0304  -0.0127 -0.0855 162 ASP   B OD2 
6522 N  N   . LYS   B 163 ? 0.1630 0.1336 0.3237 -0.0114 -0.0258 -0.0352 163 LYS   B N   
6523 C  CA  . LYS   B 163 ? 0.1776 0.1451 0.3330 -0.0233 -0.0164 -0.0133 163 LYS   B CA  
6524 C  C   . LYS   B 163 ? 0.1460 0.1369 0.3192 -0.0132 -0.0203 -0.0007 163 LYS   B C   
6525 O  O   . LYS   B 163 ? 0.1452 0.1465 0.3407 -0.0169 -0.0207 -0.0007 163 LYS   B O   
6526 C  CB  . LYS   B 163 ? 0.2269 0.1800 0.3777 -0.0274 -0.0174 0.0073  163 LYS   B CB  
6527 C  CG  . LYS   B 163 ? 0.3070 0.2635 0.4436 -0.0353 -0.0125 0.0183  163 LYS   B CG  
6528 C  CD  . LYS   B 163 ? 0.3912 0.3503 0.5135 -0.0480 -0.0168 0.0223  163 LYS   B CD  
6529 C  CE  . LYS   B 163 ? 0.4563 0.4306 0.5564 -0.0549 -0.0150 0.0276  163 LYS   B CE  
6530 N  NZ  . LYS   B 163 ? 0.4992 0.4746 0.5900 -0.0572 -0.0133 0.0252  163 LYS   B NZ  
6544 N  N   . LEU   B 164 ? 0.1381 0.1297 0.2941 -0.0148 -0.0148 -0.0036 164 LEU   B N   
6545 C  CA  . LEU   B 164 ? 0.1413 0.1327 0.2702 -0.0109 -0.0217 -0.0029 164 LEU   B CA  
6546 C  C   . LEU   B 164 ? 0.1474 0.1315 0.2723 -0.0134 -0.0237 0.0009  164 LEU   B C   
6547 O  O   . LEU   B 164 ? 0.1497 0.1550 0.2837 -0.0131 -0.0257 -0.0020 164 LEU   B O   
6548 C  CB  . LEU   B 164 ? 0.1395 0.1305 0.2585 -0.0133 -0.0168 -0.0057 164 LEU   B CB  
6549 C  CG  . LEU   B 164 ? 0.1520 0.1455 0.2524 -0.0113 -0.0052 0.0009  164 LEU   B CG  
6550 C  CD1 . LEU   B 164 ? 0.1572 0.1443 0.2549 -0.0168 -0.0156 -0.0119 164 LEU   B CD1 
6551 C  CD2 . LEU   B 164 ? 0.1660 0.1836 0.2651 -0.0090 0.0084  -0.0124 164 LEU   B CD2 
6563 N  N   . VAL   B 165 ? 0.1777 0.1399 0.2938 -0.0192 -0.0267 -0.0148 165 VAL   B N   
6564 C  CA  . VAL   B 165 ? 0.2111 0.1529 0.2963 -0.0317 -0.0442 -0.0055 165 VAL   B CA  
6565 C  C   . VAL   B 165 ? 0.2384 0.1638 0.3194 -0.0368 -0.0688 -0.0034 165 VAL   B C   
6566 O  O   . VAL   B 165 ? 0.2570 0.1745 0.3264 -0.0424 -0.0692 0.0069  165 VAL   B O   
6567 C  CB  . VAL   B 165 ? 0.2309 0.1673 0.2954 -0.0210 -0.0191 -0.0228 165 VAL   B CB  
6568 C  CG1 . VAL   B 165 ? 0.2483 0.1781 0.3185 -0.0227 -0.0107 -0.0175 165 VAL   B CG1 
6569 C  CG2 . VAL   B 165 ? 0.2231 0.1766 0.2795 -0.0197 -0.0036 -0.0127 165 VAL   B CG2 
6579 N  N   . SER   B 166 ? 0.2447 0.1505 0.3542 -0.0370 -0.0746 -0.0222 166 SER   B N   
6580 C  CA  . SER   B 166 ? 0.2398 0.1507 0.4089 -0.0413 -0.0660 -0.0341 166 SER   B CA  
6581 C  C   . SER   B 166 ? 0.2234 0.1616 0.4235 -0.0440 -0.0684 -0.0101 166 SER   B C   
6582 O  O   . SER   B 166 ? 0.2266 0.1855 0.4579 -0.0533 -0.0769 -0.0382 166 SER   B O   
6583 C  CB  . SER   B 166 ? 0.2399 0.1624 0.4389 -0.0273 -0.0571 -0.0390 166 SER   B CB  
6584 O  OG  . SER   B 166 ? 0.2227 0.1582 0.4508 -0.0233 -0.0644 -0.0180 166 SER   B OG  
6590 N  N   . SER   B 167 ? 0.2038 0.1538 0.4000 -0.0404 -0.0767 0.0323  167 SER   B N   
6591 C  CA  . SER   B 167 ? 0.1970 0.1637 0.3849 -0.0395 -0.0523 0.0300  167 SER   B CA  
6592 C  C   . SER   B 167 ? 0.1907 0.1727 0.3689 -0.0507 -0.0457 0.0409  167 SER   B C   
6593 O  O   . SER   B 167 ? 0.1921 0.1833 0.3568 -0.0540 -0.0406 0.0393  167 SER   B O   
6594 C  CB  . SER   B 167 ? 0.1873 0.1720 0.3781 -0.0350 -0.0172 0.0210  167 SER   B CB  
6595 O  OG  . SER   B 167 ? 0.1798 0.1798 0.3576 -0.0164 -0.0012 0.0223  167 SER   B OG  
6601 N  N   . PHE   B 168 ? 0.1906 0.1712 0.3580 -0.0441 -0.0364 0.0514  168 PHE   B N   
6602 C  CA  . PHE   B 168 ? 0.1983 0.1668 0.3285 -0.0461 -0.0322 0.0322  168 PHE   B CA  
6603 C  C   . PHE   B 168 ? 0.1693 0.1534 0.2927 -0.0287 -0.0175 0.0256  168 PHE   B C   
6604 O  O   . PHE   B 168 ? 0.1966 0.1490 0.3003 -0.0041 -0.0182 0.0131  168 PHE   B O   
6605 C  CB  . PHE   B 168 ? 0.2132 0.1698 0.3282 -0.0544 -0.0468 0.0425  168 PHE   B CB  
6606 C  CG  . PHE   B 168 ? 0.2375 0.1546 0.3081 -0.0539 -0.0452 0.0217  168 PHE   B CG  
6607 C  CD1 . PHE   B 168 ? 0.2691 0.1602 0.3114 -0.0552 -0.0517 0.0200  168 PHE   B CD1 
6608 C  CD2 . PHE   B 168 ? 0.2260 0.1499 0.3008 -0.0435 -0.0421 0.0192  168 PHE   B CD2 
6609 C  CE1 . PHE   B 168 ? 0.2826 0.1724 0.3046 -0.0411 -0.0500 0.0229  168 PHE   B CE1 
6610 C  CE2 . PHE   B 168 ? 0.2542 0.1583 0.3103 -0.0327 -0.0494 0.0144  168 PHE   B CE2 
6611 C  CZ  . PHE   B 168 ? 0.2698 0.1618 0.3028 -0.0282 -0.0566 0.0297  168 PHE   B CZ  
6621 N  N   . LEU   B 169 ? 0.1686 0.1683 0.2842 -0.0096 0.0040  0.0043  169 LEU   B N   
6622 C  CA  . LEU   B 169 ? 0.1961 0.1983 0.3098 -0.0126 0.0103  -0.0263 169 LEU   B CA  
6623 C  C   . LEU   B 169 ? 0.2235 0.2226 0.3612 0.0006  0.0081  -0.0575 169 LEU   B C   
6624 O  O   . LEU   B 169 ? 0.2470 0.2463 0.4164 -0.0006 0.0056  -0.0791 169 LEU   B O   
6625 C  CB  . LEU   B 169 ? 0.2217 0.2378 0.3171 -0.0214 -0.0029 -0.0017 169 LEU   B CB  
6626 C  CG  . LEU   B 169 ? 0.2662 0.2783 0.3569 -0.0110 -0.0070 0.0066  169 LEU   B CG  
6627 C  CD1 . LEU   B 169 ? 0.2804 0.2996 0.3627 -0.0058 -0.0162 0.0244  169 LEU   B CD1 
6628 C  CD2 . LEU   B 169 ? 0.2663 0.2870 0.3642 -0.0020 0.0043  -0.0076 169 LEU   B CD2 
6629 O  OXT . LEU   B 169 ? 0.2416 0.2402 0.3575 0.0287  0.0155  -0.0568 169 LEU   B OXT 
6641 N  N2  B A1A9Z C .   ? 0.1476 0.1512 0.1725 -0.0066 0.0081  0.0058  201 A1A9Z A N2  
6642 C  C3  B A1A9Z C .   ? 0.1854 0.1727 0.2225 -0.0123 -0.0038 0.0113  201 A1A9Z A C3  
6643 C  C6  B A1A9Z C .   ? 0.1676 0.1568 0.1931 -0.0100 0.0175  0.0077  201 A1A9Z A C6  
6644 C  C9  B A1A9Z C .   ? 0.1392 0.1459 0.1603 -0.0086 0.0133  0.0173  201 A1A9Z A C9  
6645 C  C12 B A1A9Z C .   ? 0.1330 0.1488 0.1715 -0.0060 0.0117  0.0324  201 A1A9Z A C12 
6646 C  C14 B A1A9Z C .   ? 0.1275 0.1525 0.1996 -0.0093 0.0009  0.0462  201 A1A9Z A C14 
6647 C  C1  B A1A9Z C .   ? 0.1820 0.1819 0.2423 0.0015  -0.0122 0.0302  201 A1A9Z A C1  
6648 C  C10 B A1A9Z C .   ? 0.1406 0.1532 0.1730 -0.0012 0.0137  0.0241  201 A1A9Z A C10 
6649 C  C11 B A1A9Z C .   ? 0.1347 0.1470 0.1742 -0.0051 0.0145  0.0400  201 A1A9Z A C11 
6650 C  C13 B A1A9Z C .   ? 0.1312 0.1543 0.1909 -0.0061 0.0095  0.0417  201 A1A9Z A C13 
6651 C  C15 B A1A9Z C .   ? 0.1829 0.1712 0.2291 -0.0055 0.0129  0.0053  201 A1A9Z A C15 
6652 C  C16 B A1A9Z C .   ? 0.1891 0.1768 0.2438 -0.0057 -0.0015 0.0079  201 A1A9Z A C16 
6653 C  C2  B A1A9Z C .   ? 0.1843 0.1767 0.2345 -0.0060 -0.0058 0.0175  201 A1A9Z A C2  
6654 C  C4  B A1A9Z C .   ? 0.1843 0.1672 0.2199 -0.0119 -0.0004 0.0058  201 A1A9Z A C4  
6655 C  C5  B A1A9Z C .   ? 0.1762 0.1636 0.2137 -0.0085 0.0171  0.0089  201 A1A9Z A C5  
6656 C  C7  B A1A9Z C .   ? 0.1585 0.1444 0.1724 -0.0108 0.0227  0.0162  201 A1A9Z A C7  
6657 C  C8  B A1A9Z C .   ? 0.1744 0.1658 0.2162 -0.0051 0.0216  0.0090  201 A1A9Z A C8  
6658 N  N1  B A1A9Z C .   ? 0.1466 0.1368 0.1617 -0.0092 0.0166  0.0137  201 A1A9Z A N1  
6659 N  N3  B A1A9Z C .   ? 0.1386 0.1509 0.1680 -0.0062 0.0177  0.0408  201 A1A9Z A N3  
6660 N  N4  B A1A9Z C .   ? 0.1379 0.1492 0.1888 0.0011  -0.0007 0.0462  201 A1A9Z A N4  
6661 O  O1  B A1A9Z C .   ? 0.1865 0.1763 0.2520 -0.0105 0.0263  0.0126  201 A1A9Z A O1  
6680 O  O1  C A1A9Y D .   ? 0.1940 0.1976 0.2789 -0.0002 -0.0049 0.0154  202 A1A9Y A O1  
6681 C  C1  C A1A9Y D .   ? 0.1812 0.1846 0.2457 -0.0050 -0.0312 0.0517  202 A1A9Y A C1  
6682 C  C2  C A1A9Y D .   ? 0.1857 0.1821 0.2488 -0.0098 -0.0299 0.0415  202 A1A9Y A C2  
6683 C  C3  C A1A9Y D .   ? 0.1888 0.1809 0.2445 -0.0135 -0.0270 0.0321  202 A1A9Y A C3  
6684 C  C4  C A1A9Y D .   ? 0.1925 0.1795 0.2482 -0.0120 -0.0290 0.0245  202 A1A9Y A C4  
6685 C  C5  C A1A9Y D .   ? 0.1921 0.1793 0.2587 -0.0082 -0.0287 0.0222  202 A1A9Y A C5  
6686 C  C6  C A1A9Y D .   ? 0.1877 0.1724 0.2550 -0.0069 -0.0260 0.0201  202 A1A9Y A C6  
6687 C  C7  C A1A9Y D .   ? 0.1768 0.1642 0.2317 0.0002  -0.0245 0.0195  202 A1A9Y A C7  
6688 C  C8  C A1A9Y D .   ? 0.1866 0.1853 0.2569 0.0052  -0.0171 0.0138  202 A1A9Y A C8  
6689 C  C10 C A1A9Y D .   ? 0.1532 0.1369 0.1839 0.0023  -0.0101 0.0111  202 A1A9Y A C10 
6690 C  C11 C A1A9Y D .   ? 0.1457 0.1293 0.1748 0.0032  -0.0019 0.0144  202 A1A9Y A C11 
6691 C  C12 C A1A9Y D .   ? 0.1453 0.1344 0.1821 0.0018  -0.0084 0.0194  202 A1A9Y A C12 
6692 C  C13 C A1A9Y D .   ? 0.1429 0.1372 0.1885 0.0040  -0.0036 0.0208  202 A1A9Y A C13 
6693 C  C14 C A1A9Y D .   ? 0.1404 0.1363 0.1899 0.0032  -0.0077 0.0180  202 A1A9Y A C14 
6694 C  C15 C A1A9Y D .   ? 0.1920 0.1827 0.2601 -0.0090 -0.0283 0.0288  202 A1A9Y A C15 
6695 C  C16 C A1A9Y D .   ? 0.1911 0.1824 0.2539 -0.0107 -0.0303 0.0401  202 A1A9Y A C16 
6696 C  C9  C A1A9Y D .   ? 0.1536 0.1413 0.1925 -0.0012 -0.0145 0.0158  202 A1A9Y A C9  
6697 N  N1  C A1A9Y D .   ? 0.1625 0.1447 0.2056 0.0008  -0.0224 0.0222  202 A1A9Y A N1  
6698 N  N2  C A1A9Y D .   ? 0.1615 0.1431 0.2047 -0.0028 -0.0133 0.0075  202 A1A9Y A N2  
6699 N  N3  C A1A9Y D .   ? 0.1483 0.1305 0.1669 -0.0002 -0.0055 0.0123  202 A1A9Y A N3  
6700 N  N4  C A1A9Y D .   ? 0.1481 0.1311 0.1795 0.0093  -0.0088 0.0166  202 A1A9Y A N4  
6719 CL CL  B CL    E .   ? 0.1839 0.2017 0.3000 -0.0110 0.0116  -0.0335 203 CL    A CL  
6720 O  O   . HOH   F .   ? 0.4109 0.8274 0.4591 -0.1076 0.0741  0.0512  301 HOH   A O   
6721 O  O   . HOH   F .   ? 0.3097 0.3620 0.3398 0.0028  -0.0117 0.0750  302 HOH   A O   
6722 O  O   . HOH   F .   ? 0.3121 0.3338 0.1863 -0.0382 0.0614  0.0487  303 HOH   A O   
6723 O  O   . HOH   F .   ? 0.5553 0.4886 0.3353 0.1947  -0.1131 0.0677  304 HOH   A O   
6724 O  O   . HOH   F .   ? 0.3005 0.2562 0.5192 -0.0265 -0.1445 0.1233  305 HOH   A O   
6725 O  O   . HOH   F .   ? 0.3348 0.3085 0.3035 -0.0964 0.0388  0.0687  306 HOH   A O   
6726 O  O   . HOH   F .   ? 0.7580 0.5840 0.3814 -0.1489 -0.0500 0.1840  307 HOH   A O   
6727 O  O   . HOH   F .   ? 0.5647 0.7628 0.5838 0.1701  -0.0427 0.0925  308 HOH   A O   
6728 O  O   . HOH   F .   ? 0.5381 0.3355 0.4917 0.1288  -0.0667 -0.0050 309 HOH   A O   
6729 O  O   . HOH   F .   ? 0.2778 0.2108 0.4203 -0.0265 -0.0696 0.0418  310 HOH   A O   
6730 O  O   . HOH   F .   ? 0.4950 0.3529 0.6358 -0.0385 0.2006  -0.0725 311 HOH   A O   
6731 O  O   . HOH   F .   ? 0.1521 0.4285 0.3005 -0.0101 0.0108  0.1053  312 HOH   A O   
6732 O  O   . HOH   F .   ? 0.6323 0.3811 0.5359 -0.0457 0.2094  0.1028  313 HOH   A O   
6733 O  O   A HOH   F .   ? 0.2716 0.3992 0.5715 -0.0247 0.1083  0.1805  314 HOH   A O   
6734 O  O   . HOH   F .   ? 0.4935 0.2074 0.5016 0.0725  0.0012  -0.0085 315 HOH   A O   
6735 O  O   A HOH   F .   ? 0.3194 0.1530 0.1736 0.0275  0.0335  0.0174  316 HOH   A O   
6736 O  O   A HOH   F .   ? 0.1724 0.1841 0.2545 -0.0080 0.0528  0.0687  317 HOH   A O   
6737 O  O   . HOH   F .   ? 0.5964 0.6636 0.4104 0.2544  -0.0743 -0.0950 318 HOH   A O   
6738 O  O   . HOH   F .   ? 0.1713 0.3607 0.2920 0.0373  -0.0308 0.0125  319 HOH   A O   
6739 O  O   . HOH   F .   ? 0.2118 0.1893 0.3707 -0.0498 -0.0017 -0.0156 320 HOH   A O   
6740 O  O   . HOH   F .   ? 0.4005 0.3357 0.3820 -0.1322 -0.0356 0.0082  321 HOH   A O   
6741 O  O   . HOH   F .   ? 0.5288 0.3987 0.4086 -0.0271 -0.0706 0.0241  322 HOH   A O   
6742 O  O   . HOH   F .   ? 0.2416 0.2124 0.2628 -0.0304 0.0340  0.0041  323 HOH   A O   
6743 O  O   . HOH   F .   ? 0.2060 0.1648 0.2392 0.0188  -0.0349 0.0017  324 HOH   A O   
6744 O  O   . HOH   F .   ? 0.7046 0.6205 0.3577 -0.0835 -0.0478 0.1295  325 HOH   A O   
6745 O  O   . HOH   F .   ? 0.4822 0.5606 0.6056 0.2164  0.1160  -0.0421 326 HOH   A O   
6746 O  O   . HOH   F .   ? 0.2515 0.5690 0.4226 -0.0403 -0.0841 0.0919  327 HOH   A O   
6747 O  O   . HOH   F .   ? 0.3017 0.4220 0.2748 -0.0071 0.0482  0.0588  328 HOH   A O   
6748 O  O   . HOH   F .   ? 0.3511 0.2792 0.3745 0.0056  -0.0998 -0.0575 329 HOH   A O   
6749 O  O   . HOH   F .   ? 0.3604 0.3656 0.3881 -0.0745 0.1499  0.0306  330 HOH   A O   
6750 O  O   . HOH   F .   ? 0.4527 0.1877 0.4963 0.0140  -0.1309 0.0757  331 HOH   A O   
6751 O  O   . HOH   F .   ? 0.2162 0.3594 0.4597 -0.0454 0.0395  -0.1004 332 HOH   A O   
6752 O  O   . HOH   F .   ? 0.2393 0.2285 0.2554 0.0460  0.0229  0.0415  333 HOH   A O   
6753 O  O   . HOH   F .   ? 0.5951 0.5163 0.4497 -0.0475 -0.0777 -0.0140 334 HOH   A O   
6754 O  O   . HOH   F .   ? 0.1706 0.1638 0.2114 0.0166  -0.0168 0.0294  335 HOH   A O   
6755 O  O   . HOH   F .   ? 0.1477 0.1987 0.2782 0.0132  -0.0330 -0.0604 336 HOH   A O   
6756 O  O   A HOH   F .   ? 0.1485 0.2525 0.2133 0.0591  0.0480  0.0887  337 HOH   A O   
6757 O  O   . HOH   F .   ? 0.2893 0.4275 0.3325 -0.1103 -0.0760 -0.0162 338 HOH   A O   
6758 O  O   . HOH   F .   ? 0.2049 0.4302 0.3500 -0.0092 -0.0343 0.1358  339 HOH   A O   
6759 O  O   . HOH   F .   ? 0.1527 0.2083 0.2303 0.0040  -0.0072 0.0535  340 HOH   A O   
6760 O  O   . HOH   F .   ? 0.1638 0.1710 0.2358 -0.0237 0.0091  0.0385  341 HOH   A O   
6761 O  O   . HOH   F .   ? 0.2980 0.3558 0.2304 -0.0645 -0.0290 -0.0715 342 HOH   A O   
6762 O  O   B HOH   F .   ? 0.1663 0.2009 0.2862 0.0371  -0.0203 0.0011  343 HOH   A O   
6763 O  O   . HOH   F .   ? 0.6662 0.5265 0.5536 0.0743  0.2695  -0.1086 344 HOH   A O   
6764 O  O   B HOH   F .   ? 0.2654 0.3187 0.2613 0.1520  0.0629  0.1171  345 HOH   A O   
6765 O  O   . HOH   F .   ? 0.1907 0.2112 0.2158 -0.0157 -0.0080 0.0736  346 HOH   A O   
6766 O  O   B HOH   F .   ? 0.1926 0.2962 0.4088 -0.0087 -0.0977 0.0204  347 HOH   A O   
6767 O  O   . HOH   F .   ? 0.5819 0.6469 0.6277 -0.0887 0.0669  0.0703  348 HOH   A O   
6768 O  O   . HOH   F .   ? 0.5302 0.5052 0.2825 -0.1128 0.1519  0.0617  349 HOH   A O   
6769 O  O   . HOH   F .   ? 0.2446 0.3954 0.3604 0.0936  -0.0722 -0.0237 350 HOH   A O   
6770 O  O   . HOH   F .   ? 0.2023 0.2036 0.3013 0.0053  -0.0519 -0.0213 351 HOH   A O   
6771 O  O   A HOH   F .   ? 0.2205 0.2393 0.2433 0.0133  0.0782  0.0167  352 HOH   A O   
6772 O  O   . HOH   F .   ? 0.4363 0.3720 0.4414 -0.1802 -0.1018 0.1880  353 HOH   A O   
6773 O  O   . HOH   F .   ? 0.2846 0.4604 0.3414 -0.0731 0.0506  -0.0198 354 HOH   A O   
6774 O  O   . HOH   F .   ? 0.1986 0.1946 0.3869 0.0191  0.0950  -0.0149 355 HOH   A O   
6775 O  O   . HOH   F .   ? 0.1292 0.1261 0.1536 -0.0025 0.0083  0.0147  356 HOH   A O   
6776 O  O   . HOH   F .   ? 0.1856 0.1914 0.2389 -0.0296 0.0059  0.0366  357 HOH   A O   
6777 O  O   . HOH   F .   ? 0.3539 0.4074 0.3927 0.1726  0.0626  0.0475  358 HOH   A O   
6778 O  O   . HOH   F .   ? 0.1430 0.1885 0.2510 0.0109  -0.0048 0.0085  359 HOH   A O   
6779 O  O   . HOH   F .   ? 0.5032 0.2764 0.4284 -0.1712 0.1849  -0.0780 360 HOH   A O   
6780 O  O   . HOH   F .   ? 0.5813 0.3659 0.2882 0.0598  0.0819  0.1110  361 HOH   A O   
6781 O  O   . HOH   F .   ? 0.3032 0.3623 0.5192 -0.0807 -0.0940 -0.0981 362 HOH   A O   
6782 O  O   B HOH   F .   ? 0.2922 0.2898 0.4842 0.0044  -0.0118 0.0670  363 HOH   A O   
6783 O  O   . HOH   F .   ? 0.7720 0.5063 0.6698 -0.0297 -0.1338 0.0469  364 HOH   A O   
6784 O  O   . HOH   F .   ? 0.7226 0.5504 0.4926 -0.0221 -0.0868 0.0368  365 HOH   A O   
6785 O  O   . HOH   F .   ? 0.1504 0.1292 0.2193 -0.0060 0.0180  -0.0122 366 HOH   A O   
6786 O  O   . HOH   F .   ? 0.1898 0.1837 0.1909 0.0026  0.0156  0.0180  367 HOH   A O   
6787 O  O   . HOH   F .   ? 0.5493 0.5757 0.7085 -0.1056 -0.0467 0.1869  368 HOH   A O   
6788 O  O   . HOH   F .   ? 0.2897 0.4359 0.3093 0.0504  0.0822  0.1881  369 HOH   A O   
6789 O  O   . HOH   F .   ? 0.1949 0.2564 0.3505 0.0315  0.0792  -0.0419 370 HOH   A O   
6790 O  O   . HOH   F .   ? 0.3624 0.7749 0.4834 -0.0724 -0.1210 0.0300  371 HOH   A O   
6791 O  O   . HOH   F .   ? 0.2088 0.3720 0.3890 -0.0298 0.0096  0.0513  372 HOH   A O   
6792 O  O   . HOH   F .   ? 0.3961 0.2271 0.4702 -0.1112 0.0549  0.0634  373 HOH   A O   
6793 O  O   . HOH   F .   ? 0.1460 0.1440 0.1548 -0.0039 -0.0079 -0.0058 374 HOH   A O   
6794 O  O   . HOH   F .   ? 0.4608 0.3067 0.3155 -0.0691 0.0849  0.0095  375 HOH   A O   
6795 O  O   . HOH   F .   ? 0.3997 0.2073 0.2306 0.1235  0.0401  0.0225  376 HOH   A O   
6796 O  O   . HOH   F .   ? 0.3076 0.2357 0.5469 -0.0650 -0.0593 0.0568  377 HOH   A O   
6797 O  O   . HOH   F .   ? 0.2992 0.2670 0.2252 0.0323  0.0678  0.0171  378 HOH   A O   
6798 O  O   . HOH   F .   ? 0.1974 0.2110 0.2227 -0.0233 -0.0374 0.0345  379 HOH   A O   
6799 O  O   . HOH   F .   ? 0.1790 0.1412 0.1612 -0.0248 0.0167  0.0058  380 HOH   A O   
6800 O  O   . HOH   F .   ? 0.3449 0.7145 0.5676 -0.0856 -0.0981 0.2060  381 HOH   A O   
6801 O  O   . HOH   F .   ? 0.5016 0.6927 0.6465 0.1904  -0.0415 0.1440  382 HOH   A O   
6802 O  O   B HOH   F .   ? 0.2523 0.1963 0.2939 -0.0140 -0.1269 0.0024  383 HOH   A O   
6803 O  O   . HOH   F .   ? 0.2168 0.1669 0.1532 -0.0078 0.0138  0.0146  384 HOH   A O   
6804 O  O   . HOH   F .   ? 0.1371 0.1399 0.1825 0.0010  -0.0157 0.0060  385 HOH   A O   
6805 O  O   . HOH   F .   ? 0.3206 0.6863 0.4055 0.1321  0.0964  -0.1310 386 HOH   A O   
6806 O  O   B HOH   F .   ? 0.2472 0.4345 0.4610 0.0612  -0.1025 -0.1240 387 HOH   A O   
6807 O  O   . HOH   F .   ? 0.3357 0.2544 0.3205 0.0019  -0.0358 0.0884  388 HOH   A O   
6808 O  O   . HOH   F .   ? 0.3218 0.3471 0.6347 -0.0348 0.1191  -0.0755 389 HOH   A O   
6809 O  O   . HOH   F .   ? 0.1918 0.2016 0.2528 -0.0100 -0.0080 0.0778  390 HOH   A O   
6810 O  O   B HOH   F .   ? 0.2523 0.4003 0.2108 -0.0016 0.0372  0.0411  391 HOH   A O   
6811 O  O   . HOH   F .   ? 0.3575 0.2530 0.6403 0.0744  0.0830  0.0359  392 HOH   A O   
6812 O  O   . HOH   F .   ? 0.2451 0.1993 0.1832 -0.0471 0.0193  0.0267  393 HOH   A O   
6813 O  O   . HOH   F .   ? 0.2649 0.2417 0.3187 0.0209  -0.0208 0.0822  394 HOH   A O   
6814 O  O   . HOH   F .   ? 0.4140 0.6688 0.4129 -0.0376 0.0192  0.1813  395 HOH   A O   
6815 O  O   . HOH   F .   ? 0.2256 0.2518 0.3541 0.0121  -0.0252 -0.0125 396 HOH   A O   
6816 O  O   . HOH   F .   ? 0.3978 0.3790 0.5208 0.0823  0.1289  -0.1044 397 HOH   A O   
6817 O  O   . HOH   F .   ? 0.1932 0.2591 0.3746 -0.0069 -0.0155 0.0257  398 HOH   A O   
6818 O  O   . HOH   F .   ? 0.2936 0.3053 0.4073 -0.0942 0.1239  -0.0208 399 HOH   A O   
6819 O  O   . HOH   F .   ? 0.1822 0.1902 0.3906 0.0345  0.1071  0.1035  400 HOH   A O   
6820 O  O   . HOH   F .   ? 0.3526 0.5151 0.2458 -0.0674 -0.0929 -0.0044 401 HOH   A O   
6821 O  O   . HOH   F .   ? 0.2559 0.4007 0.3294 -0.0346 0.1010  -0.0678 402 HOH   A O   
6822 O  O   A HOH   F .   ? 0.1814 0.3483 0.2124 0.0520  0.0149  0.0218  403 HOH   A O   
6823 O  O   . HOH   F .   ? 0.2979 0.5584 0.5913 0.0308  -0.0183 0.1885  404 HOH   A O   
6824 O  O   . HOH   F .   ? 0.2522 0.2098 0.2446 -0.0578 0.0000  0.0487  405 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2122 0.1690 0.3049 -0.0012 -0.0266 0.0061  406 HOH   A O   
6826 O  O   A HOH   F .   ? 0.2650 0.4436 0.4683 0.0455  0.0381  0.0961  407 HOH   A O   
6827 O  O   . HOH   F .   ? 0.3016 0.2595 0.2210 -0.0740 -0.0854 0.0333  408 HOH   A O   
6828 O  O   . HOH   F .   ? 0.4831 0.4825 0.2071 0.0059  0.0954  0.1029  409 HOH   A O   
6829 O  O   A HOH   F .   ? 0.1203 0.1244 0.1212 0.0081  -0.0250 0.0009  410 HOH   A O   
6830 O  O   . HOH   F .   ? 0.5741 0.6836 0.6372 -0.0082 -0.1244 -0.1055 411 HOH   A O   
6831 O  O   A HOH   F .   ? 0.1050 0.1363 0.1059 0.0124  0.0011  -0.0070 412 HOH   A O   
6832 O  O   . HOH   F .   ? 0.1747 0.2308 0.3937 -0.0046 0.0712  0.0747  413 HOH   A O   
6833 O  O   . HOH   F .   ? 0.2466 0.1842 0.2590 -0.0072 0.0178  0.0337  414 HOH   A O   
6834 O  O   . HOH   F .   ? 0.6831 0.3921 0.4708 0.1894  -0.0630 0.1391  415 HOH   A O   
6835 O  O   A HOH   F .   ? 0.4894 0.3353 0.3610 -0.0440 0.1586  0.0950  416 HOH   A O   
6836 O  O   A HOH   F .   ? 0.2726 0.2266 0.3816 -0.0409 0.0901  -0.0196 417 HOH   A O   
6837 O  O   . HOH   F .   ? 0.1680 0.2383 0.3086 -0.0257 -0.0196 0.0640  418 HOH   A O   
6838 O  O   . HOH   F .   ? 0.5032 0.2844 0.3039 -0.1381 0.0482  0.0353  419 HOH   A O   
6839 O  O   . HOH   F .   ? 0.1491 0.1686 0.2955 0.0025  0.0006  0.0291  420 HOH   A O   
6840 O  O   . HOH   F .   ? 0.2942 0.6131 0.1707 -0.0278 0.0441  0.0083  421 HOH   A O   
6841 O  O   B HOH   F .   ? 0.3351 0.1912 0.2427 0.0543  -0.0444 0.0440  422 HOH   A O   
6842 O  O   A HOH   F .   ? 0.1636 0.1588 0.2179 0.0171  -0.0422 0.0150  423 HOH   A O   
6843 O  O   . HOH   F .   ? 0.2162 0.2630 0.2582 -0.0009 -0.0603 0.0489  424 HOH   A O   
6844 O  O   . HOH   F .   ? 0.3463 0.1312 0.1968 0.0002  -0.0325 0.0088  425 HOH   A O   
6845 O  O   . HOH   F .   ? 0.4068 0.5284 0.3455 0.1571  -0.0838 -0.1438 426 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2322 0.4192 0.2385 0.1600  0.0009  0.0207  427 HOH   A O   
6847 O  O   . HOH   F .   ? 0.4488 0.6030 0.3214 -0.0963 -0.0274 0.1146  428 HOH   A O   
6848 O  O   . HOH   F .   ? 0.3943 0.2213 0.5563 -0.0748 -0.2156 0.1141  429 HOH   A O   
6849 O  O   . HOH   F .   ? 0.2031 0.1941 0.3277 0.0186  -0.0393 0.0503  430 HOH   A O   
6850 O  O   . HOH   F .   ? 0.6516 0.6699 0.6625 -0.1395 0.0003  -0.1319 431 HOH   A O   
6851 O  O   . HOH   F .   ? 0.3289 0.3586 0.7533 -0.0118 0.1064  -0.0498 432 HOH   A O   
6852 O  O   B HOH   F .   ? 0.2886 0.3292 0.4360 0.1078  -0.0513 -0.0341 433 HOH   A O   
6853 O  O   A HOH   F .   ? 0.1608 0.1015 0.0920 -0.0023 -0.0116 0.0010  434 HOH   A O   
6854 O  O   . HOH   F .   ? 0.5827 0.7382 0.4343 0.0642  0.2797  -0.0802 435 HOH   A O   
6855 O  O   . HOH   F .   ? 0.2807 0.3353 0.4934 0.0262  0.0803  -0.1140 436 HOH   A O   
6856 O  O   . HOH   F .   ? 0.9871 1.0512 0.7948 -0.0446 -0.0510 -0.0053 437 HOH   A O   
6857 O  O   . HOH   F .   ? 0.6641 0.7825 0.4424 0.1850  -0.1041 0.1831  438 HOH   A O   
6858 O  O   . HOH   F .   ? 0.4894 0.4669 0.3951 -0.0249 -0.1547 0.0144  439 HOH   A O   
6859 O  O   A HOH   F .   ? 0.4913 0.3699 0.3581 -0.0777 0.0881  0.0522  440 HOH   A O   
6860 O  O   . HOH   F .   ? 0.5542 0.5951 0.5654 -0.1109 0.0940  0.2647  441 HOH   A O   
6861 O  O   . HOH   F .   ? 0.3600 0.2535 0.1955 -0.0633 0.0334  0.0434  442 HOH   A O   
6862 O  O   . HOH   F .   ? 0.4136 0.4591 0.5404 -0.0636 -0.1072 -0.1235 443 HOH   A O   
6863 O  O   . HOH   F .   ? 0.2527 0.1650 0.2679 -0.0032 0.0030  0.0112  444 HOH   A O   
6864 O  O   . HOH   F .   ? 0.3746 0.3556 0.3033 0.2060  -0.0357 -0.0366 445 HOH   A O   
6865 O  O   A HOH   F .   ? 0.2006 0.1268 0.2624 0.0358  -0.0970 -0.0487 446 HOH   A O   
6866 O  O   . HOH   F .   ? 0.6248 0.6557 0.6886 0.1155  0.0289  -0.1249 447 HOH   A O   
6867 O  O   . HOH   F .   ? 0.1906 0.2186 0.4733 -0.0301 -0.0835 0.0510  448 HOH   A O   
6868 O  O   B HOH   F .   ? 0.3254 0.1785 0.4646 -0.0923 -0.0631 0.0533  449 HOH   A O   
6869 O  O   . HOH   F .   ? 0.2373 0.2131 0.2630 0.0158  0.0265  0.0287  450 HOH   A O   
6870 O  O   . HOH   F .   ? 0.2112 0.2500 0.2422 0.0104  -0.0224 -0.0371 451 HOH   A O   
6871 O  O   . HOH   F .   ? 0.7564 0.7298 0.7119 0.1047  -0.1313 0.0165  452 HOH   A O   
6872 O  O   . HOH   F .   ? 0.7028 0.5879 0.5439 -0.1320 -0.1321 -0.0753 453 HOH   A O   
6873 O  O   . HOH   F .   ? 0.7246 0.6553 0.7897 0.0772  -0.1207 0.2587  454 HOH   A O   
6874 O  O   . HOH   F .   ? 0.4457 0.3297 0.3829 0.0747  0.0797  0.1037  455 HOH   A O   
6875 O  O   A HOH   F .   ? 0.3259 0.1623 0.2714 -0.0146 0.0855  0.0619  456 HOH   A O   
6876 O  O   B HOH   F .   ? 0.1781 0.2668 0.2758 -0.0031 -0.0576 0.0589  457 HOH   A O   
6877 O  O   . HOH   F .   ? 0.4530 0.4161 0.4881 0.0671  -0.0315 0.1296  458 HOH   A O   
6878 O  O   . HOH   F .   ? 0.6621 0.5796 0.5021 -0.0483 0.1508  0.0951  459 HOH   A O   
6879 O  O   B HOH   F .   ? 0.1781 0.3484 0.3848 0.0168  -0.0230 -0.0733 460 HOH   A O   
6880 O  O   . HOH   F .   ? 0.2655 0.2817 0.3677 0.0551  -0.0283 0.0197  461 HOH   A O   
6881 O  O   . HOH   F .   ? 0.4417 0.3413 0.4137 0.0474  0.0348  -0.0036 462 HOH   A O   
6882 O  O   . HOH   F .   ? 0.3051 0.3158 0.3354 -0.0830 0.0157  -0.0777 463 HOH   A O   
6883 O  O   . HOH   F .   ? 0.2985 0.5001 0.5425 -0.1388 0.0723  -0.1427 464 HOH   A O   
6884 O  O   . HOH   F .   ? 0.7428 0.7550 0.4910 0.0311  -0.1212 0.0082  465 HOH   A O   
6885 O  O   . HOH   F .   ? 0.2741 0.4148 0.5879 0.0637  -0.0043 -0.1962 466 HOH   A O   
6886 O  O   . HOH   F .   ? 0.3554 0.4662 0.5249 0.1083  -0.0220 0.1195  467 HOH   A O   
6887 O  O   . HOH   F .   ? 0.2745 0.2736 0.6343 0.0573  -0.1225 -0.0332 468 HOH   A O   
6888 O  O   . HOH   F .   ? 0.6368 0.5732 0.6684 0.1376  0.2276  0.2132  469 HOH   A O   
6889 O  O   . HOH   F .   ? 0.5336 0.5771 0.4655 0.0859  -0.1297 -0.1130 470 HOH   A O   
6890 O  O   . HOH   F .   ? 0.3529 0.4126 0.4184 -0.1156 0.0004  -0.0104 471 HOH   A O   
6891 O  O   . HOH   F .   ? 0.2367 0.2581 0.3515 -0.0659 0.0385  -0.0085 472 HOH   A O   
6892 O  O   . HOH   F .   ? 0.6533 0.3274 0.7910 0.0219  0.0178  0.2379  473 HOH   A O   
6893 O  O   . HOH   F .   ? 0.2672 0.1776 0.2543 0.0322  -0.0841 -0.0247 474 HOH   A O   
6894 O  O   . HOH   F .   ? 0.4469 0.5674 0.3647 0.0263  -0.0736 -0.0683 475 HOH   A O   
6895 O  O   . HOH   F .   ? 0.3822 0.6076 0.4319 -0.0771 -0.0998 0.2437  476 HOH   A O   
6896 O  O   . HOH   F .   ? 0.3189 0.2404 0.3967 0.0122  0.0942  0.0243  477 HOH   A O   
6897 O  O   . HOH   F .   ? 0.5570 0.5329 0.4545 0.0159  0.1489  0.0529  478 HOH   A O   
6898 O  O   . HOH   F .   ? 0.2444 0.2367 0.2510 0.0180  -0.0018 0.0086  479 HOH   A O   
6899 O  O   . HOH   F .   ? 0.4591 0.5676 0.5712 -0.1491 -0.1052 0.0902  480 HOH   A O   
6900 O  O   . HOH   F .   ? 0.4382 0.5170 0.2949 -0.0265 -0.0300 0.0079  481 HOH   A O   
6901 O  O   . HOH   F .   ? 0.4422 0.4331 0.5487 -0.2058 -0.0587 0.0142  482 HOH   A O   
6902 O  O   . HOH   F .   ? 0.4861 0.2541 0.3566 -0.0590 -0.1218 0.0524  483 HOH   A O   
6903 O  O   . HOH   F .   ? 0.7985 0.5131 0.5961 -0.0853 -0.1285 -0.1037 484 HOH   A O   
6904 O  O   . HOH   F .   ? 0.6306 0.3904 0.4563 0.0768  -0.0255 -0.1335 485 HOH   A O   
6905 O  O   . HOH   F .   ? 0.4761 0.4757 0.3823 -0.0593 -0.0819 0.0064  486 HOH   A O   
6906 O  O   . HOH   F .   ? 0.7807 0.3824 0.3072 -0.0513 -0.1276 -0.0020 487 HOH   A O   
6907 O  O   . HOH   F .   ? 0.7562 0.5683 0.7011 -0.1199 0.0542  -0.0892 488 HOH   A O   
6908 O  O   . HOH   F .   ? 0.4280 0.3406 0.2534 -0.0821 0.1251  -0.0471 489 HOH   A O   
6909 O  O   B HOH   F .   ? 0.5156 0.3832 0.4275 0.0365  -0.1441 -0.0154 490 HOH   A O   
6910 O  O   . HOH   F .   ? 0.7519 0.6840 0.4604 -0.1006 0.1331  0.1226  491 HOH   A O   
6911 O  O   . HOH   F .   ? 0.2713 0.4324 0.4852 0.0081  0.1329  0.1213  492 HOH   A O   
6912 O  O   . HOH   F .   ? 0.2810 0.5756 0.4131 0.1503  0.1130  0.2721  493 HOH   A O   
6913 O  O   . HOH   F .   ? 0.6264 0.4207 0.4524 -0.0374 0.1056  -0.0032 494 HOH   A O   
6914 O  O   . HOH   F .   ? 0.6029 0.5575 0.7291 0.1205  0.1884  -0.1129 495 HOH   A O   
6915 O  O   . HOH   F .   ? 0.2635 0.2277 0.7354 -0.0008 -0.1083 0.0174  496 HOH   A O   
6916 O  O   . HOH   F .   ? 0.5069 0.5154 0.5212 -0.0202 -0.1164 0.0511  497 HOH   A O   
6917 O  O   . HOH   F .   ? 0.3490 0.4940 0.3399 -0.0600 -0.0119 -0.0764 498 HOH   A O   
6918 O  O   . HOH   F .   ? 0.2869 0.2121 0.6451 0.0085  0.0875  0.0888  499 HOH   A O   
6919 O  O   . HOH   F .   ? 0.4722 0.3361 0.4114 -0.0326 0.1887  0.0245  500 HOH   A O   
6920 O  O   . HOH   F .   ? 0.7102 0.7944 0.5946 0.2718  -0.1371 0.0473  501 HOH   A O   
6921 O  O   . HOH   F .   ? 0.5417 0.4923 0.4337 -0.0024 -0.0919 -0.0385 502 HOH   A O   
6922 O  O   . HOH   F .   ? 0.4370 0.3111 0.4721 -0.1180 0.0456  0.0947  503 HOH   A O   
6923 O  O   . HOH   F .   ? 0.2490 0.2831 0.5038 0.0064  0.0893  -0.0506 504 HOH   A O   
6924 O  O   . HOH   F .   ? 0.3978 0.8700 0.5623 -0.1212 -0.0617 0.2429  505 HOH   A O   
6925 O  O   B HOH   F .   ? 0.2556 0.5439 0.3838 -0.0169 0.0493  -0.0259 506 HOH   A O   
6926 O  O   . HOH   F .   ? 0.4731 0.2445 0.3962 -0.1401 0.0016  0.0291  507 HOH   A O   
6927 O  O   . HOH   F .   ? 0.2526 0.3197 0.3364 0.0695  -0.0478 0.0375  508 HOH   A O   
6928 O  O   . HOH   F .   ? 0.6601 0.2650 0.4609 -0.0591 0.0843  0.0631  509 HOH   A O   
6929 O  O   . HOH   F .   ? 0.3125 0.4191 0.4027 0.0850  -0.0095 0.0222  510 HOH   A O   
6930 O  O   . HOH   F .   ? 0.7796 0.5116 0.5689 -0.0523 -0.0397 -0.0157 511 HOH   A O   
6931 O  O   B HOH   F .   ? 0.4026 0.4897 0.3657 -0.0045 -0.0341 -0.0224 512 HOH   A O   
6932 O  O   . HOH   F .   ? 0.4932 0.7413 0.5187 0.1087  -0.0175 0.1259  513 HOH   A O   
6933 O  O   . HOH   F .   ? 0.2698 0.2194 0.4412 0.0081  0.0369  0.0273  514 HOH   A O   
6934 O  O   . HOH   F .   ? 0.5135 0.7473 0.4775 0.3339  -0.0267 0.0861  515 HOH   A O   
6935 O  O   . HOH   F .   ? 0.5099 0.6067 0.4577 0.0394  -0.0951 -0.1094 516 HOH   A O   
6936 O  O   B HOH   F .   ? 0.2929 0.5066 0.4101 0.0962  0.0484  0.1652  517 HOH   A O   
6937 O  O   A HOH   F .   ? 0.3609 0.5011 0.1657 0.1236  0.0109  0.0789  518 HOH   A O   
6938 O  O   . HOH   F .   ? 0.2992 0.6908 0.4041 0.0674  0.0460  0.0048  519 HOH   A O   
6939 O  O   . HOH   F .   ? 0.4434 0.5078 0.4402 0.1206  -0.0386 0.1307  520 HOH   A O   
6940 O  O   B HOH   F .   ? 0.2652 0.3015 0.3774 -0.0224 0.0745  0.1133  521 HOH   A O   
6941 O  O   . HOH   F .   ? 0.5064 0.6799 0.6091 -0.0594 -0.0494 0.0655  522 HOH   A O   
6942 O  O   . HOH   F .   ? 0.3072 0.4447 0.5588 -0.0512 -0.0985 0.2732  523 HOH   A O   
6943 O  O   . HOH   G .   ? 0.2304 0.2063 0.3033 0.0218  0.0686  0.0403  201 HOH   B O   
6944 O  O   . HOH   G .   ? 0.3841 0.3856 0.5670 -0.1288 0.0687  -0.1334 202 HOH   B O   
6945 O  O   . HOH   G .   ? 0.4438 0.3592 0.4096 -0.0452 0.0137  -0.1523 203 HOH   B O   
6946 O  O   . HOH   G .   ? 0.3168 0.4409 0.7300 -0.0372 0.0314  -0.1080 204 HOH   B O   
6947 O  O   . HOH   G .   ? 0.2942 0.7102 0.4678 0.0944  0.0348  0.2763  205 HOH   B O   
6948 O  O   . HOH   G .   ? 0.4789 0.6403 0.2547 0.0982  -0.0419 -0.1485 206 HOH   B O   
6949 O  O   . HOH   G .   ? 0.4601 0.6184 0.3460 0.2990  -0.0834 -0.0402 207 HOH   B O   
6950 O  O   . HOH   G .   ? 0.2839 0.2048 0.5253 0.0174  0.1727  0.0946  208 HOH   B O   
6951 O  O   . HOH   G .   ? 0.3060 0.5672 0.5298 -0.0111 0.1706  -0.1882 209 HOH   B O   
6952 O  O   . HOH   G .   ? 0.2018 0.2189 0.2823 -0.0007 0.0222  -0.0230 210 HOH   B O   
6953 O  O   . HOH   G .   ? 0.6412 0.3635 0.5335 0.0523  0.1717  0.0106  211 HOH   B O   
6954 O  O   . HOH   G .   ? 0.6890 0.6269 0.5420 0.1963  0.0678  0.0568  212 HOH   B O   
6955 O  O   . HOH   G .   ? 0.2744 0.2964 0.6716 0.0717  -0.1139 0.0459  213 HOH   B O   
6956 O  O   . HOH   G .   ? 0.4520 0.3963 0.3594 -0.0290 -0.1318 0.0901  214 HOH   B O   
6957 O  O   . HOH   G .   ? 0.6066 0.3025 0.4390 -0.2046 0.0535  0.0088  215 HOH   B O   
6958 O  O   . HOH   G .   ? 0.5140 0.4134 0.6264 0.0626  -0.1087 0.2554  216 HOH   B O   
6959 O  O   . HOH   G .   ? 0.3580 0.5639 0.5061 0.2420  0.0198  -0.0782 217 HOH   B O   
6960 O  O   . HOH   G .   ? 0.1507 0.1482 0.2250 -0.0199 0.0044  0.0101  218 HOH   B O   
6961 O  O   . HOH   G .   ? 0.1561 0.1925 0.2729 -0.0179 -0.0132 0.0093  219 HOH   B O   
6962 O  O   . HOH   G .   ? 0.4046 0.4963 0.4649 0.2229  -0.0235 0.0583  220 HOH   B O   
6963 O  O   . HOH   G .   ? 0.4218 0.4514 0.4142 0.0181  0.0627  -0.1677 221 HOH   B O   
6964 O  O   . HOH   G .   ? 0.4206 0.4791 0.7105 0.0103  -0.1543 -0.1276 222 HOH   B O   
6965 O  O   . HOH   G .   ? 0.4561 0.2047 0.2945 -0.0195 -0.0869 0.0047  223 HOH   B O   
6966 O  O   . HOH   G .   ? 0.3478 0.3840 0.4017 0.0134  -0.1362 -0.0259 224 HOH   B O   
6967 O  O   . HOH   G .   ? 0.3520 0.2816 0.4051 0.0862  -0.0299 -0.0430 225 HOH   B O   
6968 O  O   . HOH   G .   ? 0.2469 0.1781 0.2892 -0.0266 0.1043  0.0022  226 HOH   B O   
6969 O  O   . HOH   G .   ? 0.8253 0.4319 0.4933 0.2343  -0.0051 -0.1035 227 HOH   B O   
6970 O  O   . HOH   G .   ? 0.3994 0.3724 0.5787 -0.1508 0.0041  0.1013  228 HOH   B O   
6971 O  O   . HOH   G .   ? 0.1715 0.2040 0.3201 -0.0174 0.0116  -0.0205 229 HOH   B O   
6972 O  O   . HOH   G .   ? 0.3539 0.3251 0.1989 0.0418  0.0661  0.0517  230 HOH   B O   
6973 O  O   . HOH   G .   ? 0.2837 0.2678 0.6464 -0.0116 0.0753  0.0066  231 HOH   B O   
6974 O  O   . HOH   G .   ? 0.2516 0.2461 0.3150 0.0170  0.0207  -0.0778 232 HOH   B O   
6975 O  O   . HOH   G .   ? 0.3601 0.1769 0.2147 0.0150  -0.0742 -0.0152 233 HOH   B O   
6976 O  O   . HOH   G .   ? 0.3016 0.2067 0.4976 0.0006  0.1585  0.0236  234 HOH   B O   
6977 O  O   . HOH   G .   ? 0.2208 0.2174 0.3897 -0.0407 -0.0013 -0.0637 235 HOH   B O   
6978 O  O   . HOH   G .   ? 0.1966 0.3936 0.2482 -0.0355 -0.0073 0.0518  236 HOH   B O   
6979 O  O   . HOH   G .   ? 0.2039 0.2258 0.3359 -0.0358 0.0054  -0.0342 237 HOH   B O   
6980 O  O   . HOH   G .   ? 0.5093 0.6616 0.3273 0.2905  0.0375  0.0486  238 HOH   B O   
6981 O  O   . HOH   G .   ? 0.2882 0.3395 0.3066 -0.0894 0.0450  -0.0176 239 HOH   B O   
6982 O  O   . HOH   G .   ? 0.2111 0.1291 0.3608 0.0118  -0.0660 -0.0144 240 HOH   B O   
6983 O  O   . HOH   G .   ? 0.5242 0.3268 0.3793 -0.2339 0.0330  -0.0049 241 HOH   B O   
6984 O  O   . HOH   G .   ? 0.1550 0.1444 0.2575 -0.0043 0.0057  -0.0093 242 HOH   B O   
6985 O  O   . HOH   G .   ? 0.2293 0.3517 0.3190 -0.0433 -0.0668 -0.0610 243 HOH   B O   
6986 O  O   . HOH   G .   ? 0.3655 0.2988 0.4091 0.0658  -0.0715 -0.1469 244 HOH   B O   
6987 O  O   . HOH   G .   ? 0.3190 0.2499 0.3382 -0.0499 0.0298  -0.0672 245 HOH   B O   
6988 O  O   . HOH   G .   ? 0.1433 0.1437 0.1557 -0.0126 -0.0055 -0.0056 246 HOH   B O   
6989 O  O   . HOH   G .   ? 0.1378 0.1308 0.1659 0.0003  -0.0041 0.0080  247 HOH   B O   
6990 O  O   . HOH   G .   ? 0.3183 0.1828 0.6082 -0.0228 -0.1390 -0.0426 248 HOH   B O   
6991 O  O   . HOH   G .   ? 0.6064 0.3503 0.2689 -0.0522 0.1067  -0.0530 249 HOH   B O   
6992 O  O   . HOH   G .   ? 0.2788 0.4294 0.3189 -0.0908 -0.0457 -0.0808 250 HOH   B O   
6993 O  O   . HOH   G .   ? 0.2152 0.2083 0.2134 -0.0348 -0.0532 0.0152  251 HOH   B O   
6994 O  O   . HOH   G .   ? 0.3423 0.3811 0.2062 0.0448  0.0818  0.0055  252 HOH   B O   
6995 O  O   . HOH   G .   ? 0.6361 0.5520 0.3198 0.0828  0.0295  0.0122  253 HOH   B O   
6996 O  O   . HOH   G .   ? 0.2528 0.2156 0.1875 0.0240  -0.0184 0.0013  254 HOH   B O   
6997 O  O   . HOH   G .   ? 0.2219 0.2166 0.2590 0.0646  -0.0742 -0.0626 255 HOH   B O   
6998 O  O   . HOH   G .   ? 0.2828 0.2397 0.2890 0.0933  0.0967  0.0106  256 HOH   B O   
6999 O  O   . HOH   G .   ? 0.4638 0.3423 0.4429 0.0222  0.0855  -0.0196 257 HOH   B O   
7000 O  O   . HOH   G .   ? 0.2160 0.1525 0.2008 -0.0323 -0.0329 0.0277  258 HOH   B O   
7001 O  O   . HOH   G .   ? 0.1650 0.1642 0.2882 -0.0233 -0.0273 0.0117  259 HOH   B O   
7002 O  O   . HOH   G .   ? 0.2234 0.2907 0.2254 -0.0422 0.0209  0.0473  260 HOH   B O   
7003 O  O   . HOH   G .   ? 0.1367 0.1597 0.2069 -0.0039 0.0035  0.0140  261 HOH   B O   
7004 O  O   . HOH   G .   ? 0.3230 0.4810 0.3625 -0.0423 -0.1064 0.1343  262 HOH   B O   
7005 O  O   . HOH   G .   ? 0.4180 0.3561 0.4484 -0.0313 -0.1185 -0.0882 263 HOH   B O   
7006 O  O   . HOH   G .   ? 0.1784 0.2667 0.2702 0.0550  0.0498  0.0916  264 HOH   B O   
7007 O  O   . HOH   G .   ? 0.2425 0.4690 0.5305 0.0049  0.0429  -0.1338 265 HOH   B O   
7008 O  O   . HOH   G .   ? 0.2262 0.2119 0.1948 0.0158  0.0002  0.0019  266 HOH   B O   
7009 O  O   . HOH   G .   ? 0.5588 0.6751 0.2805 0.0054  -0.1404 0.0507  267 HOH   B O   
7010 O  O   . HOH   G .   ? 0.2566 0.5314 0.4983 0.1653  -0.0439 -0.0599 268 HOH   B O   
7011 O  O   . HOH   G .   ? 0.2489 0.2706 0.2338 -0.0316 -0.0691 0.0102  269 HOH   B O   
7012 O  O   . HOH   G .   ? 0.2070 0.1492 0.2286 -0.0283 -0.0195 0.0120  270 HOH   B O   
7013 O  O   . HOH   G .   ? 0.2135 0.3963 0.4878 -0.0385 -0.0122 -0.1819 271 HOH   B O   
7014 O  O   . HOH   G .   ? 0.1943 0.1695 0.1661 -0.0444 -0.0480 0.0148  272 HOH   B O   
7015 O  O   . HOH   G .   ? 0.2492 0.2597 0.2363 -0.0559 -0.0697 -0.0270 273 HOH   B O   
7016 O  O   . HOH   G .   ? 0.2507 0.2040 0.2915 -0.0560 0.0165  -0.0093 274 HOH   B O   
7017 O  O   . HOH   G .   ? 0.2331 0.1830 0.3721 -0.0036 -0.0647 -0.0295 275 HOH   B O   
7018 O  O   . HOH   G .   ? 0.2547 0.3993 0.3396 0.0085  0.1075  0.0115  276 HOH   B O   
7019 O  O   . HOH   G .   ? 0.1762 0.1413 0.3738 -0.0074 -0.0315 -0.0066 277 HOH   B O   
7020 O  O   . HOH   G .   ? 0.2299 0.2821 0.2396 0.0830  -0.0224 -0.0245 278 HOH   B O   
7021 O  O   . HOH   G .   ? 0.2271 0.4104 0.3147 -0.0456 0.0524  -0.1576 279 HOH   B O   
7022 O  O   . HOH   G .   ? 0.3413 0.3809 0.4708 0.1420  -0.0601 -0.0990 280 HOH   B O   
7023 O  O   . HOH   G .   ? 0.2758 0.6888 0.7423 0.1399  -0.0705 -0.0561 281 HOH   B O   
7024 O  O   . HOH   G .   ? 0.1623 0.1545 0.1859 0.0003  0.0065  0.0015  282 HOH   B O   
7025 O  O   . HOH   G .   ? 0.1618 0.1492 0.3403 -0.0148 0.0144  -0.0075 283 HOH   B O   
7026 O  O   . HOH   G .   ? 0.2589 0.2191 0.4905 0.0161  0.0445  0.0739  284 HOH   B O   
7027 O  O   . HOH   G .   ? 0.3536 0.7157 0.3487 0.1993  -0.0515 0.0999  285 HOH   B O   
7028 O  O   . HOH   G .   ? 0.1572 0.1991 0.1599 -0.0131 -0.0191 0.0076  286 HOH   B O   
7029 O  O   . HOH   G .   ? 0.1650 0.1980 0.3088 0.0227  -0.0103 0.0048  287 HOH   B O   
7030 O  O   . HOH   G .   ? 0.2496 0.2697 0.2810 0.0295  -0.0746 0.0201  288 HOH   B O   
7031 O  O   . HOH   G .   ? 0.4719 0.3649 0.2898 0.0369  -0.0015 -0.1030 289 HOH   B O   
7032 O  O   . HOH   G .   ? 0.4304 0.4580 0.4921 0.0099  -0.1492 0.0138  290 HOH   B O   
7033 O  O   . HOH   G .   ? 0.1722 0.3235 0.4721 0.0282  -0.0026 -0.1237 291 HOH   B O   
7034 O  O   . HOH   G .   ? 0.4315 0.3063 0.5111 -0.0845 0.0471  0.1351  292 HOH   B O   
7035 O  O   . HOH   G .   ? 0.4154 0.3881 0.4107 -0.1064 0.1007  -0.1329 293 HOH   B O   
7036 O  O   . HOH   G .   ? 0.3569 0.2350 0.4018 -0.1090 -0.1940 0.0843  294 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2763 0.4567 0.5053 -0.1020 -0.1191 0.1093  295 HOH   B O   
7038 O  O   . HOH   G .   ? 0.3622 0.2793 0.2176 0.0334  -0.1012 -0.0066 296 HOH   B O   
7039 O  O   . HOH   G .   ? 0.1694 0.1611 0.2389 0.0121  0.0062  0.0131  297 HOH   B O   
7040 O  O   . HOH   G .   ? 0.2034 0.2971 0.6403 0.0506  -0.0549 -0.1593 298 HOH   B O   
7041 O  O   . HOH   G .   ? 0.4398 0.4698 0.1992 -0.0377 0.0711  0.0179  299 HOH   B O   
7042 O  O   . HOH   G .   ? 0.4410 0.3877 0.2245 0.1253  -0.0708 0.0550  300 HOH   B O   
7043 O  O   . HOH   G .   ? 0.2476 0.6956 0.2445 0.0565  -0.0414 -0.0367 301 HOH   B O   
7044 O  O   . HOH   G .   ? 0.2142 0.1617 0.2616 -0.0238 -0.0272 -0.0031 302 HOH   B O   
7045 O  O   . HOH   G .   ? 0.3039 0.3627 0.4191 -0.1143 0.0898  -0.0351 303 HOH   B O   
7046 O  O   . HOH   G .   ? 0.3095 0.2926 0.5241 -0.0307 -0.0926 0.1188  304 HOH   B O   
7047 O  O   . HOH   G .   ? 0.3059 0.2965 0.2942 -0.0320 0.0170  -0.1252 305 HOH   B O   
7048 O  O   . HOH   G .   ? 0.5632 0.3720 0.3202 0.2551  0.1110  0.0790  306 HOH   B O   
7049 O  O   . HOH   G .   ? 0.1559 0.1501 0.3024 0.0098  0.0088  0.0063  307 HOH   B O   
7050 O  O   . HOH   G .   ? 0.3199 0.3487 0.7605 -0.0090 -0.0810 0.1410  308 HOH   B O   
7051 O  O   . HOH   G .   ? 0.2295 0.3001 0.5190 -0.0026 -0.0698 -0.0353 309 HOH   B O   
7052 O  O   . HOH   G .   ? 0.2089 0.1564 0.3428 0.0313  -0.0988 -0.0031 310 HOH   B O   
7053 O  O   . HOH   G .   ? 0.3372 0.1871 0.3640 0.0775  0.1250  0.0467  311 HOH   B O   
7054 O  O   . HOH   G .   ? 0.3918 0.2247 0.2672 0.1426  0.0992  0.0408  312 HOH   B O   
7055 O  O   . HOH   G .   ? 0.5271 0.2967 0.2386 -0.1824 0.0722  -0.0375 313 HOH   B O   
7056 O  O   . HOH   G .   ? 0.5808 0.5340 0.5235 -0.1035 0.0084  0.1159  314 HOH   B O   
7057 O  O   . HOH   G .   ? 0.2392 0.1497 0.2540 -0.0185 -0.0175 0.0298  315 HOH   B O   
7058 O  O   . HOH   G .   ? 0.1548 0.1859 0.2969 -0.0240 -0.0150 0.0097  316 HOH   B O   
7059 O  O   . HOH   G .   ? 0.2638 0.3348 0.4783 -0.0589 -0.1420 0.1269  317 HOH   B O   
7060 O  O   . HOH   G .   ? 0.2800 0.2866 0.3571 -0.0409 0.0926  -0.0831 318 HOH   B O   
7061 O  O   . HOH   G .   ? 0.6212 0.6029 0.4784 0.2780  -0.0319 -0.0150 319 HOH   B O   
7062 O  O   . HOH   G .   ? 0.2145 0.1939 0.1885 -0.0014 0.0128  0.0198  320 HOH   B O   
7063 O  O   . HOH   G .   ? 0.1641 0.2855 0.2329 -0.0078 -0.0151 0.0680  321 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2151 0.6539 0.5660 -0.0729 0.0017  -0.0238 322 HOH   B O   
7065 O  O   . HOH   G .   ? 0.4708 0.4301 0.2651 0.0180  -0.0398 -0.0754 323 HOH   B O   
7066 O  O   . HOH   G .   ? 0.6622 0.4723 0.5367 0.1407  0.1730  -0.0218 324 HOH   B O   
7067 O  O   . HOH   G .   ? 0.4170 0.4030 0.6406 0.0386  -0.0002 0.0645  325 HOH   B O   
7068 O  O   . HOH   G .   ? 0.1542 0.1625 0.2847 -0.0100 -0.0191 -0.0102 326 HOH   B O   
7069 O  O   . HOH   G .   ? 0.2873 0.2294 0.2406 0.0225  -0.0264 0.0320  327 HOH   B O   
7070 O  O   . HOH   G .   ? 0.1949 0.1938 0.2978 0.0314  0.0468  0.0239  328 HOH   B O   
7071 O  O   . HOH   G .   ? 0.4306 0.4490 0.2189 0.1129  -0.0746 -0.0075 329 HOH   B O   
7072 O  O   . HOH   G .   ? 0.7752 0.1994 0.3383 0.0159  -0.0873 0.0084  330 HOH   B O   
7073 O  O   . HOH   G .   ? 0.1873 0.2906 0.3186 0.0375  -0.0037 -0.0717 331 HOH   B O   
7074 O  O   . HOH   G .   ? 0.4273 0.3236 0.5328 0.1065  0.2179  0.1592  332 HOH   B O   
7075 O  O   . HOH   G .   ? 0.4550 0.2647 0.3035 0.0405  0.0763  0.0932  333 HOH   B O   
7076 O  O   . HOH   G .   ? 0.5850 0.3507 0.4251 -0.0003 0.1190  -0.1684 334 HOH   B O   
7077 O  O   . HOH   G .   ? 0.2627 0.2030 0.5125 -0.0090 0.0161  0.0295  335 HOH   B O   
7078 O  O   . HOH   G .   ? 0.6240 0.3575 0.3724 -0.0033 0.1183  0.1142  336 HOH   B O   
7079 O  O   . HOH   G .   ? 0.5416 0.4974 0.6839 0.0360  -0.1292 0.2321  337 HOH   B O   
7080 O  O   . HOH   G .   ? 0.2364 0.2388 0.5523 -0.0531 0.0166  0.1374  338 HOH   B O   
7081 O  O   . HOH   G .   ? 0.5302 0.4744 0.6295 -0.0766 -0.0592 -0.1224 339 HOH   B O   
7082 O  O   . HOH   G .   ? 0.1689 0.1467 0.2346 0.0095  -0.0194 0.0139  340 HOH   B O   
7083 O  O   . HOH   G .   ? 0.4793 0.5717 0.3342 0.0099  -0.1017 0.0424  341 HOH   B O   
7084 O  O   . HOH   G .   ? 0.4139 0.7201 0.3428 -0.0679 -0.0645 0.1855  342 HOH   B O   
7085 O  O   . HOH   G .   ? 0.5103 0.3496 0.3250 0.0714  -0.1357 -0.0770 343 HOH   B O   
7086 O  O   . HOH   G .   ? 0.2304 0.5812 0.6415 0.0235  -0.0196 0.0447  344 HOH   B O   
7087 O  O   . HOH   G .   ? 0.6145 0.6863 0.2859 -0.0125 -0.0484 0.1664  345 HOH   B O   
7088 O  O   . HOH   G .   ? 0.3734 0.6308 0.4188 -0.1229 -0.0880 -0.0871 346 HOH   B O   
7089 O  O   . HOH   G .   ? 0.2053 0.1928 0.2853 -0.0034 0.0488  -0.0075 347 HOH   B O   
7090 O  O   . HOH   G .   ? 0.4249 0.5265 0.5593 -0.0004 -0.1091 0.0633  348 HOH   B O   
7091 O  O   . HOH   G .   ? 0.4925 0.5397 0.5036 -0.1193 0.0627  0.0653  349 HOH   B O   
7092 O  O   . HOH   G .   ? 0.2234 0.3660 0.5123 0.0414  0.0456  0.0518  350 HOH   B O   
7093 O  O   . HOH   G .   ? 0.2689 0.2184 0.5397 -0.0304 -0.0721 -0.0575 351 HOH   B O   
7094 O  O   . HOH   G .   ? 0.2349 0.6104 0.3646 0.1477  -0.0577 -0.1539 352 HOH   B O   
7095 O  O   . HOH   G .   ? 0.4609 0.6568 0.7595 0.0723  0.0079  -0.0397 353 HOH   B O   
7096 O  O   . HOH   G .   ? 0.3409 0.4328 0.4921 -0.1442 0.0369  -0.0305 354 HOH   B O   
7097 O  O   . HOH   G .   ? 0.3994 0.2231 0.3239 -0.0724 0.0073  -0.0827 355 HOH   B O   
7098 O  O   . HOH   G .   ? 0.3070 0.1969 0.3989 0.0412  -0.1287 -0.0582 356 HOH   B O   
7099 O  O   . HOH   G .   ? 0.4791 0.2647 0.5111 -0.0843 0.1329  0.0162  357 HOH   B O   
7100 O  O   . HOH   G .   ? 0.5393 0.3521 0.4557 0.0532  0.1524  -0.0587 358 HOH   B O   
7101 O  O   . HOH   G .   ? 0.3643 0.2944 0.4144 -0.1101 0.0020  -0.0642 359 HOH   B O   
7102 O  O   . HOH   G .   ? 0.4354 0.4610 0.4946 -0.0232 -0.0283 -0.0172 360 HOH   B O   
7103 O  O   . HOH   G .   ? 0.4699 0.5281 0.5059 0.2013  -0.1263 0.1369  361 HOH   B O   
7104 O  O   . HOH   G .   ? 0.5098 0.3527 0.4656 -0.0080 -0.1632 -0.0320 362 HOH   B O   
7105 O  O   . HOH   G .   ? 0.4409 0.7258 0.2851 0.2481  -0.0057 0.0546  363 HOH   B O   
7106 O  O   . HOH   G .   ? 0.4597 0.3800 0.6432 0.0727  0.0784  0.0963  364 HOH   B O   
7107 O  O   . HOH   G .   ? 0.2148 0.3712 0.6850 -0.0715 -0.0494 -0.0760 365 HOH   B O   
7108 O  O   . HOH   G .   ? 0.6410 0.4664 0.4201 0.1163  0.0691  0.0651  366 HOH   B O   
7109 O  O   . HOH   G .   ? 0.5272 0.3092 0.5092 -0.1139 -0.0812 0.0149  367 HOH   B O   
7110 O  O   . HOH   G .   ? 0.5282 0.5890 0.3188 0.1058  -0.1762 0.0451  368 HOH   B O   
7111 O  O   . HOH   G .   ? 0.5499 0.5252 0.4542 -0.0646 -0.0746 -0.1091 369 HOH   B O   
7112 O  O   . HOH   G .   ? 0.6332 0.2072 0.3622 -0.0170 0.0391  0.0451  370 HOH   B O   
7113 O  O   . HOH   G .   ? 0.4585 0.3883 0.5393 0.0916  -0.1597 0.0229  371 HOH   B O   
7114 O  O   . HOH   G .   ? 0.7563 0.7987 0.4910 0.3428  -0.1208 0.1151  372 HOH   B O   
7115 O  O   . HOH   G .   ? 0.6926 0.4225 0.3100 -0.0850 -0.1109 -0.0997 373 HOH   B O   
7116 O  O   . HOH   G .   ? 0.4315 0.5799 0.5368 0.2584  0.0830  0.0976  374 HOH   B O   
7117 O  O   . HOH   G .   ? 0.4217 0.3080 0.3619 0.0838  -0.1571 -0.0445 375 HOH   B O   
7118 O  O   . HOH   G .   ? 0.2506 0.4052 0.4273 0.0710  -0.0608 -0.0545 376 HOH   B O   
7119 O  O   . HOH   G .   ? 0.4513 0.4642 0.4831 -0.0670 -0.0698 0.0201  377 HOH   B O   
7120 O  O   . HOH   G .   ? 0.4943 0.7047 0.6713 0.1767  0.0845  0.3091  378 HOH   B O   
7121 O  O   . HOH   G .   ? 0.7703 0.4026 0.5204 -0.0960 -0.0935 -0.0430 379 HOH   B O   
7122 O  O   . HOH   G .   ? 0.2846 0.4182 0.2350 0.0743  0.0048  -0.0005 380 HOH   B O   
7123 O  O   . HOH   G .   ? 0.3263 0.4914 0.5980 0.0938  -0.0175 0.0415  381 HOH   B O   
7124 O  O   . HOH   G .   ? 0.5203 0.7218 0.3766 -0.1372 0.0235  -0.1488 382 HOH   B O   
7125 O  O   . HOH   G .   ? 0.2875 0.2657 0.3469 0.0045  0.0387  0.0320  383 HOH   B O   
7126 O  O   . HOH   G .   ? 0.5786 0.6971 0.5901 0.0444  0.2765  0.1649  384 HOH   B O   
7127 O  O   . HOH   G .   ? 0.4698 0.8640 0.5703 0.0883  0.2200  0.1201  385 HOH   B O   
7128 O  O   . HOH   G .   ? 0.7228 0.5774 0.3756 0.2543  0.0861  0.0034  386 HOH   B O   
7129 O  O   . HOH   G .   ? 0.6812 0.3945 0.4618 0.0948  0.0537  -0.0611 387 HOH   B O   
7130 O  O   . HOH   G .   ? 0.4484 0.3822 0.3261 0.0001  0.0399  -0.0070 388 HOH   B O   
7131 O  O   . HOH   G .   ? 0.5516 0.4696 0.5438 -0.0557 0.0824  -0.0007 389 HOH   B O   
7132 O  O   . HOH   G .   ? 0.2538 0.4027 0.3710 -0.0579 -0.0926 -0.0286 390 HOH   B O   
7133 O  O   . HOH   G .   ? 0.3611 0.2216 0.3353 0.0607  -0.0509 0.0095  391 HOH   B O   
7134 O  O   . HOH   G .   ? 0.5426 0.4319 0.3921 0.0561  0.0182  0.0410  392 HOH   B O   
7135 O  O   . HOH   G .   ? 0.4105 0.2346 0.4948 -0.0499 0.0384  0.0634  393 HOH   B O   
7136 O  O   . HOH   G .   ? 0.2576 0.3927 0.6836 -0.1305 -0.0607 0.0078  394 HOH   B O   
7137 O  O   . HOH   G .   ? 0.4384 0.4222 0.4179 0.0060  0.0784  0.0902  395 HOH   B O   
7138 O  O   . HOH   G .   ? 0.4725 0.5810 0.3761 0.1778  -0.0434 -0.0902 396 HOH   B O   
7139 O  O   . HOH   G .   ? 0.3194 0.3720 0.3521 0.0458  0.0296  -0.0520 397 HOH   B O   
7140 O  O   . HOH   G .   ? 0.2306 0.2666 0.5722 -0.0550 -0.0998 0.0052  398 HOH   B O   
7141 O  O   . HOH   G .   ? 0.5521 0.7035 0.6886 0.1609  -0.1063 0.2246  399 HOH   B O   
7142 O  O   . HOH   G .   ? 0.5081 0.4273 0.3050 -0.2100 -0.0502 0.1105  400 HOH   B O   
7143 O  O   . HOH   G .   ? 0.6681 0.6536 0.4006 0.1689  -0.0153 -0.0324 401 HOH   B O   
# 
