data_7HEI
# 
_entry.id   7HEI 
# 
_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   7HEI         pdb_00007hei 10.2210/pdb7hei/pdb 
WWPDB D_1001407372 ?            ?                   
# 
_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                        7HEI 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                      18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                                          114.023   1   ? ? ? ? 
3 non-polymer syn '(2S)-3-(piperidin-1-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' 275.349   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                  35.453    1   ? ? ? ? 
5 water       nat water                                                                           18.015    426 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                          TFA   
3 '(2S)-3-(piperidin-1-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' A1A9V 
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 
A1A9V non-polymer         . '(2S)-3-(piperidin-1-yl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propan-1-ol' ? 'C14 H21 N5 O'   
275.349 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                                          ? 'C2 H F3 O2'     
114.023 
THR   'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
TYR   'L-peptide linking' y TYROSINE                                                                        ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A9V 1   202 201  A1A9V LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 105  HOH   HOH A . 
F 5 HOH   3   303 1289 HOH   HOH A . 
F 5 HOH   4   304 109  HOH   HOH A . 
F 5 HOH   5   305 625  HOH   HOH A . 
F 5 HOH   6   306 196  HOH   HOH A . 
F 5 HOH   7   307 153  HOH   HOH A . 
F 5 HOH   8   308 1301 HOH   HOH A . 
F 5 HOH   9   309 661  HOH   HOH A . 
F 5 HOH   10  310 18   HOH   HOH A . 
F 5 HOH   11  311 229  HOH   HOH A . 
F 5 HOH   12  312 209  HOH   HOH A . 
F 5 HOH   13  313 136  HOH   HOH A . 
F 5 HOH   14  314 192  HOH   HOH A . 
F 5 HOH   15  315 76   HOH   HOH A . 
F 5 HOH   16  316 1290 HOH   HOH A . 
F 5 HOH   17  317 281  HOH   HOH A . 
F 5 HOH   18  318 1283 HOH   HOH A . 
F 5 HOH   19  319 124  HOH   HOH A . 
F 5 HOH   20  320 18   HOH   HOH A . 
F 5 HOH   21  321 33   HOH   HOH A . 
F 5 HOH   22  322 11   HOH   HOH A . 
F 5 HOH   23  323 1295 HOH   HOH A . 
F 5 HOH   24  324 393  HOH   HOH A . 
F 5 HOH   25  325 86   HOH   HOH A . 
F 5 HOH   26  326 236  HOH   HOH A . 
F 5 HOH   27  327 39   HOH   HOH A . 
F 5 HOH   28  328 247  HOH   HOH A . 
F 5 HOH   29  329 57   HOH   HOH A . 
F 5 HOH   30  330 15   HOH   HOH A . 
F 5 HOH   31  331 1    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  334 630  HOH   HOH A . 
F 5 HOH   35  335 964  HOH   HOH A . 
F 5 HOH   36  336 469  HOH   HOH A . 
F 5 HOH   37  337 3    HOH   HOH A . 
F 5 HOH   38  338 1300 HOH   HOH A . 
F 5 HOH   39  339 17   HOH   HOH A . 
F 5 HOH   40  340 21   HOH   HOH A . 
F 5 HOH   41  341 164  HOH   HOH A . 
F 5 HOH   42  342 405  HOH   HOH A . 
F 5 HOH   43  343 320  HOH   HOH A . 
F 5 HOH   44  344 241  HOH   HOH A . 
F 5 HOH   45  345 7    HOH   HOH A . 
F 5 HOH   46  346 8    HOH   HOH A . 
F 5 HOH   47  347 493  HOH   HOH A . 
F 5 HOH   48  348 155  HOH   HOH A . 
F 5 HOH   49  349 102  HOH   HOH A . 
F 5 HOH   50  350 169  HOH   HOH A . 
F 5 HOH   51  351 165  HOH   HOH A . 
F 5 HOH   52  352 42   HOH   HOH A . 
F 5 HOH   53  353 225  HOH   HOH A . 
F 5 HOH   54  354 337  HOH   HOH A . 
F 5 HOH   55  355 92   HOH   HOH A . 
F 5 HOH   56  356 93   HOH   HOH A . 
F 5 HOH   57  357 195  HOH   HOH A . 
F 5 HOH   58  358 8    HOH   HOH A . 
F 5 HOH   59  359 26   HOH   HOH A . 
F 5 HOH   60  360 354  HOH   HOH A . 
F 5 HOH   61  361 85   HOH   HOH A . 
F 5 HOH   62  362 2    HOH   HOH A . 
F 5 HOH   63  363 162  HOH   HOH A . 
F 5 HOH   64  364 409  HOH   HOH A . 
F 5 HOH   65  365 49   HOH   HOH A . 
F 5 HOH   66  366 36   HOH   HOH A . 
F 5 HOH   67  367 66   HOH   HOH A . 
F 5 HOH   68  368 139  HOH   HOH A . 
F 5 HOH   69  369 396  HOH   HOH A . 
F 5 HOH   70  370 19   HOH   HOH A . 
F 5 HOH   71  371 45   HOH   HOH A . 
F 5 HOH   72  372 56   HOH   HOH A . 
F 5 HOH   73  373 5    HOH   HOH A . 
F 5 HOH   74  374 81   HOH   HOH A . 
F 5 HOH   75  375 939  HOH   HOH A . 
F 5 HOH   76  376 662  HOH   HOH A . 
F 5 HOH   77  377 34   HOH   HOH A . 
F 5 HOH   78  378 366  HOH   HOH A . 
F 5 HOH   79  379 159  HOH   HOH A . 
F 5 HOH   80  380 46   HOH   HOH A . 
F 5 HOH   81  381 62   HOH   HOH A . 
F 5 HOH   82  382 218  HOH   HOH A . 
F 5 HOH   83  383 14   HOH   HOH A . 
F 5 HOH   84  384 138  HOH   HOH A . 
F 5 HOH   85  385 13   HOH   HOH A . 
F 5 HOH   86  386 140  HOH   HOH A . 
F 5 HOH   87  387 74   HOH   HOH A . 
F 5 HOH   88  388 296  HOH   HOH A . 
F 5 HOH   89  389 199  HOH   HOH A . 
F 5 HOH   90  390 134  HOH   HOH A . 
F 5 HOH   91  391 186  HOH   HOH A . 
F 5 HOH   92  392 27   HOH   HOH A . 
F 5 HOH   93  393 70   HOH   HOH A . 
F 5 HOH   94  394 35   HOH   HOH A . 
F 5 HOH   95  395 461  HOH   HOH A . 
F 5 HOH   96  396 115  HOH   HOH A . 
F 5 HOH   97  397 1310 HOH   HOH A . 
F 5 HOH   98  398 333  HOH   HOH A . 
F 5 HOH   99  399 351  HOH   HOH A . 
F 5 HOH   100 400 116  HOH   HOH A . 
F 5 HOH   101 401 1275 HOH   HOH A . 
F 5 HOH   102 402 96   HOH   HOH A . 
F 5 HOH   103 403 15   HOH   HOH A . 
F 5 HOH   104 404 12   HOH   HOH A . 
F 5 HOH   105 405 1315 HOH   HOH A . 
F 5 HOH   106 406 148  HOH   HOH A . 
F 5 HOH   107 407 154  HOH   HOH A . 
F 5 HOH   108 408 83   HOH   HOH A . 
F 5 HOH   109 409 58   HOH   HOH A . 
F 5 HOH   110 410 25   HOH   HOH A . 
F 5 HOH   111 411 278  HOH   HOH A . 
F 5 HOH   112 412 121  HOH   HOH A . 
F 5 HOH   113 413 67   HOH   HOH A . 
F 5 HOH   114 414 68   HOH   HOH A . 
F 5 HOH   115 415 1313 HOH   HOH A . 
F 5 HOH   116 416 9    HOH   HOH A . 
F 5 HOH   117 417 123  HOH   HOH A . 
F 5 HOH   118 418 1308 HOH   HOH A . 
F 5 HOH   119 419 6    HOH   HOH A . 
F 5 HOH   120 420 125  HOH   HOH A . 
F 5 HOH   121 421 156  HOH   HOH A . 
F 5 HOH   122 422 3    HOH   HOH A . 
F 5 HOH   123 423 1068 HOH   HOH A . 
F 5 HOH   124 424 1279 HOH   HOH A . 
F 5 HOH   125 425 4    HOH   HOH A . 
F 5 HOH   126 426 303  HOH   HOH A . 
F 5 HOH   127 427 24   HOH   HOH A . 
F 5 HOH   128 428 53   HOH   HOH A . 
F 5 HOH   129 429 212  HOH   HOH A . 
F 5 HOH   130 430 95   HOH   HOH A . 
F 5 HOH   131 431 397  HOH   HOH A . 
F 5 HOH   132 432 1296 HOH   HOH A . 
F 5 HOH   133 433 51   HOH   HOH A . 
F 5 HOH   134 434 78   HOH   HOH A . 
F 5 HOH   135 435 381  HOH   HOH A . 
F 5 HOH   136 436 1309 HOH   HOH A . 
F 5 HOH   137 437 6    HOH   HOH A . 
F 5 HOH   138 438 122  HOH   HOH A . 
F 5 HOH   139 439 7    HOH   HOH A . 
F 5 HOH   140 440 1222 HOH   HOH A . 
F 5 HOH   141 441 582  HOH   HOH A . 
F 5 HOH   142 442 132  HOH   HOH A . 
F 5 HOH   143 443 71   HOH   HOH A . 
F 5 HOH   144 444 1286 HOH   HOH A . 
F 5 HOH   145 445 80   HOH   HOH A . 
F 5 HOH   146 446 1094 HOH   HOH A . 
F 5 HOH   147 447 944  HOH   HOH A . 
F 5 HOH   148 448 40   HOH   HOH A . 
F 5 HOH   149 449 16   HOH   HOH A . 
F 5 HOH   150 450 188  HOH   HOH A . 
F 5 HOH   151 451 952  HOH   HOH A . 
F 5 HOH   152 452 73   HOH   HOH A . 
F 5 HOH   153 453 94   HOH   HOH A . 
F 5 HOH   154 454 1238 HOH   HOH A . 
F 5 HOH   155 455 104  HOH   HOH A . 
F 5 HOH   156 456 10   HOH   HOH A . 
F 5 HOH   157 457 97   HOH   HOH A . 
F 5 HOH   158 458 79   HOH   HOH A . 
F 5 HOH   159 459 2    HOH   HOH A . 
F 5 HOH   160 460 576  HOH   HOH A . 
F 5 HOH   161 461 1119 HOH   HOH A . 
F 5 HOH   162 462 1189 HOH   HOH A . 
F 5 HOH   163 463 330  HOH   HOH A . 
F 5 HOH   164 464 5    HOH   HOH A . 
F 5 HOH   165 465 1134 HOH   HOH A . 
F 5 HOH   166 466 107  HOH   HOH A . 
F 5 HOH   167 467 509  HOH   HOH A . 
F 5 HOH   168 468 726  HOH   HOH A . 
F 5 HOH   169 469 163  HOH   HOH A . 
F 5 HOH   170 470 408  HOH   HOH A . 
F 5 HOH   171 471 756  HOH   HOH A . 
F 5 HOH   172 472 556  HOH   HOH A . 
F 5 HOH   173 473 1276 HOH   HOH A . 
F 5 HOH   174 474 126  HOH   HOH A . 
F 5 HOH   175 475 319  HOH   HOH A . 
F 5 HOH   176 476 801  HOH   HOH A . 
F 5 HOH   177 477 63   HOH   HOH A . 
F 5 HOH   178 478 361  HOH   HOH A . 
F 5 HOH   179 479 280  HOH   HOH A . 
F 5 HOH   180 480 1307 HOH   HOH A . 
F 5 HOH   181 481 250  HOH   HOH A . 
F 5 HOH   182 482 370  HOH   HOH A . 
F 5 HOH   183 483 342  HOH   HOH A . 
F 5 HOH   184 484 224  HOH   HOH A . 
F 5 HOH   185 485 1287 HOH   HOH A . 
F 5 HOH   186 486 135  HOH   HOH A . 
F 5 HOH   187 487 267  HOH   HOH A . 
F 5 HOH   188 488 1306 HOH   HOH A . 
F 5 HOH   189 489 202  HOH   HOH A . 
F 5 HOH   190 490 695  HOH   HOH A . 
F 5 HOH   191 491 674  HOH   HOH A . 
F 5 HOH   192 492 919  HOH   HOH A . 
F 5 HOH   193 493 315  HOH   HOH A . 
F 5 HOH   194 494 521  HOH   HOH A . 
F 5 HOH   195 495 309  HOH   HOH A . 
F 5 HOH   196 496 1299 HOH   HOH A . 
F 5 HOH   197 497 1314 HOH   HOH A . 
F 5 HOH   198 498 326  HOH   HOH A . 
F 5 HOH   199 499 331  HOH   HOH A . 
F 5 HOH   200 500 711  HOH   HOH A . 
F 5 HOH   201 501 318  HOH   HOH A . 
F 5 HOH   202 502 941  HOH   HOH A . 
F 5 HOH   203 503 805  HOH   HOH A . 
F 5 HOH   204 504 263  HOH   HOH A . 
F 5 HOH   205 505 208  HOH   HOH A . 
F 5 HOH   206 506 152  HOH   HOH A . 
F 5 HOH   207 507 1284 HOH   HOH A . 
F 5 HOH   208 508 356  HOH   HOH A . 
F 5 HOH   209 509 1071 HOH   HOH A . 
F 5 HOH   210 510 350  HOH   HOH A . 
F 5 HOH   211 511 180  HOH   HOH A . 
F 5 HOH   212 512 12   HOH   HOH A . 
F 5 HOH   213 513 363  HOH   HOH A . 
F 5 HOH   214 514 17   HOH   HOH A . 
F 5 HOH   215 515 313  HOH   HOH A . 
F 5 HOH   216 516 371  HOH   HOH A . 
F 5 HOH   217 517 185  HOH   HOH A . 
F 5 HOH   218 518 429  HOH   HOH A . 
F 5 HOH   219 519 70   HOH   HOH A . 
F 5 HOH   220 520 376  HOH   HOH A . 
F 5 HOH   221 521 772  HOH   HOH A . 
F 5 HOH   222 522 1074 HOH   HOH A . 
F 5 HOH   223 523 16   HOH   HOH A . 
F 5 HOH   224 524 346  HOH   HOH A . 
F 5 HOH   225 525 1292 HOH   HOH A . 
F 5 HOH   226 526 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 531  HOH   HOH B . 
G 5 HOH   4   204 1249 HOH   HOH B . 
G 5 HOH   5   205 240  HOH   HOH B . 
G 5 HOH   6   206 232  HOH   HOH B . 
G 5 HOH   7   207 364  HOH   HOH B . 
G 5 HOH   8   208 758  HOH   HOH B . 
G 5 HOH   9   209 358  HOH   HOH B . 
G 5 HOH   10  210 452  HOH   HOH B . 
G 5 HOH   11  211 120  HOH   HOH B . 
G 5 HOH   12  212 50   HOH   HOH B . 
G 5 HOH   13  213 343  HOH   HOH B . 
G 5 HOH   14  214 654  HOH   HOH B . 
G 5 HOH   15  215 743  HOH   HOH B . 
G 5 HOH   16  216 398  HOH   HOH B . 
G 5 HOH   17  217 444  HOH   HOH B . 
G 5 HOH   18  218 900  HOH   HOH B . 
G 5 HOH   19  219 264  HOH   HOH B . 
G 5 HOH   20  220 353  HOH   HOH B . 
G 5 HOH   21  221 332  HOH   HOH B . 
G 5 HOH   22  222 1140 HOH   HOH B . 
G 5 HOH   23  223 205  HOH   HOH B . 
G 5 HOH   24  224 1278 HOH   HOH B . 
G 5 HOH   25  225 131  HOH   HOH B . 
G 5 HOH   26  226 282  HOH   HOH B . 
G 5 HOH   27  227 82   HOH   HOH B . 
G 5 HOH   28  228 75   HOH   HOH B . 
G 5 HOH   29  229 172  HOH   HOH B . 
G 5 HOH   30  230 54   HOH   HOH B . 
G 5 HOH   31  231 60   HOH   HOH B . 
G 5 HOH   32  232 300  HOH   HOH B . 
G 5 HOH   33  233 128  HOH   HOH B . 
G 5 HOH   34  234 166  HOH   HOH B . 
G 5 HOH   35  235 272  HOH   HOH B . 
G 5 HOH   36  236 69   HOH   HOH B . 
G 5 HOH   37  237 127  HOH   HOH B . 
G 5 HOH   38  238 181  HOH   HOH B . 
G 5 HOH   39  239 1    HOH   HOH B . 
G 5 HOH   40  240 133  HOH   HOH B . 
G 5 HOH   41  241 276  HOH   HOH B . 
G 5 HOH   42  242 723  HOH   HOH B . 
G 5 HOH   43  243 1312 HOH   HOH B . 
G 5 HOH   44  244 14   HOH   HOH B . 
G 5 HOH   45  245 52   HOH   HOH B . 
G 5 HOH   46  246 9    HOH   HOH B . 
G 5 HOH   47  247 110  HOH   HOH B . 
G 5 HOH   48  248 72   HOH   HOH B . 
G 5 HOH   49  249 41   HOH   HOH B . 
G 5 HOH   50  250 325  HOH   HOH B . 
G 5 HOH   51  251 144  HOH   HOH B . 
G 5 HOH   52  252 129  HOH   HOH B . 
G 5 HOH   53  253 391  HOH   HOH B . 
G 5 HOH   54  254 143  HOH   HOH B . 
G 5 HOH   55  255 347  HOH   HOH B . 
G 5 HOH   56  256 231  HOH   HOH B . 
G 5 HOH   57  257 30   HOH   HOH B . 
G 5 HOH   58  258 47   HOH   HOH B . 
G 5 HOH   59  259 252  HOH   HOH B . 
G 5 HOH   60  260 31   HOH   HOH B . 
G 5 HOH   61  261 10   HOH   HOH B . 
G 5 HOH   62  262 242  HOH   HOH B . 
G 5 HOH   63  263 243  HOH   HOH B . 
G 5 HOH   64  264 59   HOH   HOH B . 
G 5 HOH   65  265 271  HOH   HOH B . 
G 5 HOH   66  266 11   HOH   HOH B . 
G 5 HOH   67  267 150  HOH   HOH B . 
G 5 HOH   68  268 77   HOH   HOH B . 
G 5 HOH   69  269 20   HOH   HOH B . 
G 5 HOH   70  270 61   HOH   HOH B . 
G 5 HOH   71  271 216  HOH   HOH B . 
G 5 HOH   72  272 103  HOH   HOH B . 
G 5 HOH   73  273 117  HOH   HOH B . 
G 5 HOH   74  274 287  HOH   HOH B . 
G 5 HOH   75  275 114  HOH   HOH B . 
G 5 HOH   76  276 43   HOH   HOH B . 
G 5 HOH   77  277 147  HOH   HOH B . 
G 5 HOH   78  278 1277 HOH   HOH B . 
G 5 HOH   79  279 84   HOH   HOH B . 
G 5 HOH   80  280 302  HOH   HOH B . 
G 5 HOH   81  281 221  HOH   HOH B . 
G 5 HOH   82  282 22   HOH   HOH B . 
G 5 HOH   83  283 175  HOH   HOH B . 
G 5 HOH   84  284 1305 HOH   HOH B . 
G 5 HOH   85  285 1285 HOH   HOH B . 
G 5 HOH   86  286 88   HOH   HOH B . 
G 5 HOH   87  287 89   HOH   HOH B . 
G 5 HOH   88  288 416  HOH   HOH B . 
G 5 HOH   89  289 220  HOH   HOH B . 
G 5 HOH   90  290 235  HOH   HOH B . 
G 5 HOH   91  291 1106 HOH   HOH B . 
G 5 HOH   92  292 106  HOH   HOH B . 
G 5 HOH   93  293 13   HOH   HOH B . 
G 5 HOH   94  294 137  HOH   HOH B . 
G 5 HOH   95  295 1066 HOH   HOH B . 
G 5 HOH   96  296 387  HOH   HOH B . 
G 5 HOH   97  297 99   HOH   HOH B . 
G 5 HOH   98  298 299  HOH   HOH B . 
G 5 HOH   99  299 38   HOH   HOH B . 
G 5 HOH   100 300 112  HOH   HOH B . 
G 5 HOH   101 301 160  HOH   HOH B . 
G 5 HOH   102 302 142  HOH   HOH B . 
G 5 HOH   103 303 311  HOH   HOH B . 
G 5 HOH   104 304 32   HOH   HOH B . 
G 5 HOH   105 305 297  HOH   HOH B . 
G 5 HOH   106 306 316  HOH   HOH B . 
G 5 HOH   107 307 215  HOH   HOH B . 
G 5 HOH   108 308 1274 HOH   HOH B . 
G 5 HOH   109 309 118  HOH   HOH B . 
G 5 HOH   110 310 101  HOH   HOH B . 
G 5 HOH   111 311 48   HOH   HOH B . 
G 5 HOH   112 312 141  HOH   HOH B . 
G 5 HOH   113 313 170  HOH   HOH B . 
G 5 HOH   114 314 37   HOH   HOH B . 
G 5 HOH   115 315 635  HOH   HOH B . 
G 5 HOH   116 316 197  HOH   HOH B . 
G 5 HOH   117 317 91   HOH   HOH B . 
G 5 HOH   118 318 341  HOH   HOH B . 
G 5 HOH   119 319 23   HOH   HOH B . 
G 5 HOH   120 320 177  HOH   HOH B . 
G 5 HOH   121 321 44   HOH   HOH B . 
G 5 HOH   122 322 28   HOH   HOH B . 
G 5 HOH   123 323 1294 HOH   HOH B . 
G 5 HOH   124 324 161  HOH   HOH B . 
G 5 HOH   125 325 100  HOH   HOH B . 
G 5 HOH   126 326 29   HOH   HOH B . 
G 5 HOH   127 327 1291 HOH   HOH B . 
G 5 HOH   128 328 704  HOH   HOH B . 
G 5 HOH   129 329 55   HOH   HOH B . 
G 5 HOH   130 330 98   HOH   HOH B . 
G 5 HOH   131 331 182  HOH   HOH B . 
G 5 HOH   132 332 1126 HOH   HOH B . 
G 5 HOH   133 333 445  HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 334  HOH   HOH B . 
G 5 HOH   136 336 234  HOH   HOH B . 
G 5 HOH   137 337 207  HOH   HOH B . 
G 5 HOH   138 338 65   HOH   HOH B . 
G 5 HOH   139 339 1293 HOH   HOH B . 
G 5 HOH   140 340 339  HOH   HOH B . 
G 5 HOH   141 341 619  HOH   HOH B . 
G 5 HOH   142 342 90   HOH   HOH B . 
G 5 HOH   143 343 960  HOH   HOH B . 
G 5 HOH   144 344 362  HOH   HOH B . 
G 5 HOH   145 345 178  HOH   HOH B . 
G 5 HOH   146 346 1304 HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 191  HOH   HOH B . 
G 5 HOH   149 349 1046 HOH   HOH B . 
G 5 HOH   150 350 623  HOH   HOH B . 
G 5 HOH   151 351 335  HOH   HOH B . 
G 5 HOH   152 352 87   HOH   HOH B . 
G 5 HOH   153 353 304  HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 290  HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 541  HOH   HOH B . 
G 5 HOH   158 358 479  HOH   HOH B . 
G 5 HOH   159 359 1077 HOH   HOH B . 
G 5 HOH   160 360 718  HOH   HOH B . 
G 5 HOH   161 361 389  HOH   HOH B . 
G 5 HOH   162 362 283  HOH   HOH B . 
G 5 HOH   163 363 1072 HOH   HOH B . 
G 5 HOH   164 364 1316 HOH   HOH B . 
G 5 HOH   165 365 898  HOH   HOH B . 
G 5 HOH   166 366 373  HOH   HOH B . 
G 5 HOH   167 367 615  HOH   HOH B . 
G 5 HOH   168 368 291  HOH   HOH B . 
G 5 HOH   169 369 1303 HOH   HOH B . 
G 5 HOH   170 370 340  HOH   HOH B . 
G 5 HOH   171 371 667  HOH   HOH B . 
G 5 HOH   172 372 190  HOH   HOH B . 
G 5 HOH   173 373 310  HOH   HOH B . 
G 5 HOH   174 374 431  HOH   HOH B . 
G 5 HOH   175 375 1173 HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 183  HOH   HOH B . 
G 5 HOH   178 378 1163 HOH   HOH B . 
G 5 HOH   179 379 418  HOH   HOH B . 
G 5 HOH   180 380 1000 HOH   HOH B . 
G 5 HOH   181 381 176  HOH   HOH B . 
G 5 HOH   182 382 1311 HOH   HOH B . 
G 5 HOH   183 383 981  HOH   HOH B . 
G 5 HOH   184 384 424  HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 1298 HOH   HOH B . 
G 5 HOH   187 387 265  HOH   HOH B . 
G 5 HOH   188 388 470  HOH   HOH B . 
G 5 HOH   189 389 248  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 410  HOH   HOH B . 
G 5 HOH   193 393 355  HOH   HOH B . 
G 5 HOH   194 394 566  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 321  HOH   HOH B . 
G 5 HOH   199 399 792  HOH   HOH B . 
G 5 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HEI 
_cell.length_a           88.754 
_cell.length_b           88.754 
_cell.length_c           39.448 
_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                         7HEI 
_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          7HEI 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.53 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_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                     7HEI 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164841 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.047 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.300 
_reflns.B_iso_Wilson_estimate        11.820 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.051 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1024717 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 32820 7419 ? 1.170 ? ? ? 4.400 ? 0.800  ? ? ? ? ? ? 90.600 1.325 0.606 0.581 
1 2 5.480 44.380 ? 7370  1093 ? 0.024 ? ? ? 6.700 ? 50.000 ? ? ? ? ? ? 99.900 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HEI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3800 
_refine.ls_number_reflns_obs                     164736 
_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                          0.1441 
_refine.ls_R_factor_R_work                       0.1435 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1550 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7951 
_refine.ls_number_reflns_R_work                  156785 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.4554 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1000 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                72.100 
_refine.B_iso_min                                8.280 
_refine.pdbx_overall_phase_error                 16.4900 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3018 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           12.05 
_refine_hist.pdbx_B_iso_mean_solvent          30.07 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 88.0000  4668 . 0.3781 0.3602 . 256 0.0000 4924 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 95.0000  4940 . 0.3121 0.3051 . 210 0.0000 5150 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5241 . 0.2744 0.2680 . 261 0.0000 5502 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5179 . 0.2471 0.2621 . 269 0.0000 5448 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5191 . 0.2261 0.2355 . 333 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5220 . 0.2208 0.2389 . 244 0.0000 5464 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5278 . 0.2057 0.2326 . 266 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5205 . 0.1798 0.2104 . 241 0.0000 5446 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5248 . 0.1713 0.1955 . 281 0.0000 5529 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5220 . 0.1537 0.1601 . 248 0.0000 5468 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5274 . 0.1413 0.1715 . 263 0.0000 5537 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5240 . 0.1320 0.1616 . 268 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5138 . 0.1267 0.1593 . 280 0.0000 5418 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5354 . 0.1221 0.1450 . 231 0.0000 5585 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5189 . 0.1232 0.1427 . 259 0.0000 5448 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5270 . 0.1246 0.1411 . 280 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5220 . 0.1257 0.1405 . 281 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5216 . 0.1330 0.1440 . 280 0.0000 5496 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5280 . 0.1316 0.1564 . 247 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5235 . 0.1253 0.1473 . 271 0.0000 5506 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5276 . 0.1188 0.1258 . 243 0.0000 5519 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5230 . 0.1159 0.1230 . 281 0.0000 5511 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5297 . 0.1171 0.1273 . 264 0.0000 5561 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5266 . 0.1240 0.1437 . 261 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5277 . 0.1322 0.1410 . 251 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5260 . 0.1321 0.1342 . 279 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5282 . 0.1384 0.1393 . 289 0.0000 5571 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5292 . 0.1367 0.1415 . 288 0.0000 5580 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5322 . 0.1477 0.1641 . 256 0.0000 5578 . 'X-RAY DIFFRACTION' 
3.1100 44.3800 30 100.0000 5477 . 0.1499 0.1627 . 270 0.0000 5747 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEI 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003677' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEI 
_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 7HEI A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEI 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 7HEI SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEI MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEI SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEI 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 TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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   -133.06 
2 1 SER A 128 ? B 68.23   -12.51  
3 1 SER A 167 ? B -102.70 66.19   
4 1 PHE A 168 ? B -121.25 -55.57  
5 1 HIS B 86  ? ? 57.27   -128.18 
# 
_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 524 ? 5.97 . 
2 1 O ? A HOH 525 ? 5.98 . 
3 1 O ? A HOH 526 ? 7.63 . 
4 1 O ? B HOH 400 ? 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 
A1A9V N2   N  Y N 1   
A1A9V C3   C  N N 2   
A1A9V C6   C  N N 3   
A1A9V C9   C  Y N 4   
A1A9V C12  C  Y N 5   
A1A9V C14  C  Y N 6   
A1A9V C1   C  N N 7   
A1A9V C10  C  Y N 8   
A1A9V C11  C  Y N 9   
A1A9V C13  C  Y N 10  
A1A9V C2   C  N S 11  
A1A9V C4   C  N N 12  
A1A9V C5   C  N N 13  
A1A9V C7   C  N N 14  
A1A9V C8   C  N N 15  
A1A9V N1   N  N N 16  
A1A9V N3   N  Y N 17  
A1A9V N4   N  Y N 18  
A1A9V N5   N  N N 19  
A1A9V O1   O  N N 20  
A1A9V H6   H  N N 21  
A1A9V H5   H  N N 22  
A1A9V H11  H  N N 23  
A1A9V H12  H  N N 24  
A1A9V H20  H  N N 25  
A1A9V H3   H  N N 26  
A1A9V H4   H  N N 27  
A1A9V H18  H  N N 28  
A1A9V H19  H  N N 29  
A1A9V H1   H  N N 30  
A1A9V H7   H  N N 31  
A1A9V H8   H  N N 32  
A1A9V H9   H  N N 33  
A1A9V H10  H  N N 34  
A1A9V H13  H  N N 35  
A1A9V H14  H  N N 36  
A1A9V H16  H  N N 37  
A1A9V H15  H  N N 38  
A1A9V H17  H  N N 39  
A1A9V H21  H  N N 40  
A1A9V H2   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CL    CL   CL N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
TFA   C1   C  N N 346 
TFA   C2   C  N N 347 
TFA   O    O  N N 348 
TFA   F1   F  N N 349 
TFA   F2   F  N N 350 
TFA   F3   F  N N 351 
TFA   OXT  O  N N 352 
TFA   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TYR   N    N  N N 371 
TYR   CA   C  N S 372 
TYR   C    C  N N 373 
TYR   O    O  N N 374 
TYR   CB   C  N N 375 
TYR   CG   C  Y N 376 
TYR   CD1  C  Y N 377 
TYR   CD2  C  Y N 378 
TYR   CE1  C  Y N 379 
TYR   CE2  C  Y N 380 
TYR   CZ   C  Y N 381 
TYR   OH   O  N N 382 
TYR   OXT  O  N N 383 
TYR   H    H  N N 384 
TYR   H2   H  N N 385 
TYR   HA   H  N N 386 
TYR   HB2  H  N N 387 
TYR   HB3  H  N N 388 
TYR   HD1  H  N N 389 
TYR   HD2  H  N N 390 
TYR   HE1  H  N N 391 
TYR   HE2  H  N N 392 
TYR   HH   H  N N 393 
TYR   HXT  H  N N 394 
VAL   N    N  N N 395 
VAL   CA   C  N S 396 
VAL   C    C  N N 397 
VAL   O    O  N N 398 
VAL   CB   C  N N 399 
VAL   CG1  C  N N 400 
VAL   CG2  C  N N 401 
VAL   OXT  O  N N 402 
VAL   H    H  N N 403 
VAL   H2   H  N N 404 
VAL   HA   H  N N 405 
VAL   HB   H  N N 406 
VAL   HG11 H  N N 407 
VAL   HG12 H  N N 408 
VAL   HG13 H  N N 409 
VAL   HG21 H  N N 410 
VAL   HG22 H  N N 411 
VAL   HG23 H  N N 412 
VAL   HXT  H  N N 413 
# 
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 
A1A9V C8  C7   sing N N 1   
A1A9V C8  N5   sing N N 2   
A1A9V C7  C6   sing N N 3   
A1A9V C6  C5   sing N N 4   
A1A9V C3  N5   sing N N 5   
A1A9V C3  C2   sing N N 6   
A1A9V N5  C4   sing N N 7   
A1A9V O1  C1   sing N N 8   
A1A9V C4  C5   sing N N 9   
A1A9V C1  C2   sing N N 10  
A1A9V C2  N1   sing N N 11  
A1A9V N1  C9   sing N N 12  
A1A9V C9  C12  doub Y N 13  
A1A9V C9  N2   sing Y N 14  
A1A9V C13 C12  sing Y N 15  
A1A9V C13 C14  doub Y N 16  
A1A9V C12 C11  sing Y N 17  
A1A9V N2  C10  doub Y N 18  
A1A9V C14 N4   sing Y N 19  
A1A9V C10 N3   sing Y N 20  
A1A9V C11 N4   sing Y N 21  
A1A9V C11 N3   doub Y N 22  
A1A9V C3  H6   sing N N 23  
A1A9V C3  H5   sing N N 24  
A1A9V C6  H11  sing N N 25  
A1A9V C6  H12  sing N N 26  
A1A9V C14 H20  sing N N 27  
A1A9V C1  H3   sing N N 28  
A1A9V C1  H4   sing N N 29  
A1A9V C10 H18  sing N N 30  
A1A9V C13 H19  sing N N 31  
A1A9V C2  H1   sing N N 32  
A1A9V C4  H7   sing N N 33  
A1A9V C4  H8   sing N N 34  
A1A9V C5  H9   sing N N 35  
A1A9V C5  H10  sing N N 36  
A1A9V C7  H13  sing N N 37  
A1A9V C7  H14  sing N N 38  
A1A9V C8  H16  sing N N 39  
A1A9V C8  H15  sing N N 40  
A1A9V N1  H17  sing N N 41  
A1A9V N4  H21  sing N N 42  
A1A9V O1  H2   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
TFA   C1  C2   sing N N 333 
TFA   C1  O    doub N N 334 
TFA   C1  OXT  sing N N 335 
TFA   C2  F1   sing N N 336 
TFA   C2  F2   sing N N 337 
TFA   C2  F3   sing N N 338 
TFA   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TYR   N   CA   sing N N 356 
TYR   N   H    sing N N 357 
TYR   N   H2   sing N N 358 
TYR   CA  C    sing N N 359 
TYR   CA  CB   sing N N 360 
TYR   CA  HA   sing N N 361 
TYR   C   O    doub N N 362 
TYR   C   OXT  sing N N 363 
TYR   CB  CG   sing N N 364 
TYR   CB  HB2  sing N N 365 
TYR   CB  HB3  sing N N 366 
TYR   CG  CD1  doub Y N 367 
TYR   CG  CD2  sing Y N 368 
TYR   CD1 CE1  sing Y N 369 
TYR   CD1 HD1  sing N N 370 
TYR   CD2 CE2  doub Y N 371 
TYR   CD2 HD2  sing N N 372 
TYR   CE1 CZ   doub Y N 373 
TYR   CE1 HE1  sing N N 374 
TYR   CE2 CZ   sing Y N 375 
TYR   CE2 HE2  sing N N 376 
TYR   CZ  OH   sing N N 377 
TYR   OH  HH   sing N N 378 
TYR   OXT HXT  sing N N 379 
VAL   N   CA   sing N N 380 
VAL   N   H    sing N N 381 
VAL   N   H2   sing N N 382 
VAL   CA  C    sing N N 383 
VAL   CA  CB   sing N N 384 
VAL   CA  HA   sing N N 385 
VAL   C   O    doub N N 386 
VAL   C   OXT  sing N N 387 
VAL   CB  CG1  sing N N 388 
VAL   CB  CG2  sing N N 389 
VAL   CB  HB   sing N N 390 
VAL   CG1 HG11 sing N N 391 
VAL   CG1 HG12 sing N N 392 
VAL   CG1 HG13 sing N N 393 
VAL   CG2 HG21 sing N N 394 
VAL   CG2 HG22 sing N N 395 
VAL   CG2 HG23 sing N N 396 
VAL   OXT HXT  sing N N 397 
# 
_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                    7HEI 
_atom_sites.fract_transf_matrix[1][1]   0.011267 
_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]   0.011267 
_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]   0.025350 
_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 
F  
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . VAL   A 1 3   ? 19.583 -16.057 22.242  1.00 58.21 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.627 -14.970 22.416  1.00 57.57 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.289 -13.632 22.104  1.00 54.64 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.404 -13.364 22.553  1.00 55.33 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.015 -14.985 23.833  1.00 59.21 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 16.987 -13.871 23.985  1.00 59.80 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.384 -16.340 24.125  1.00 59.74 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.901 -15.089 21.790  1.00 69.08 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.716 -14.835 24.487  1.00 71.05 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.499 -14.003 24.814  1.00 71.75 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.444 -13.016 24.006  1.00 71.75 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.373 -13.903 23.235  1.00 71.75 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.933 -16.301 24.983  1.00 71.69 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.746 -16.548 23.424  1.00 71.69 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.081 -17.014 24.148  1.00 71.69 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.602 -12.800 21.322  1.00 50.52 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.062 -11.453 21.007  1.00 45.92 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.938 -10.456 21.285  1.00 41.56 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.834 -10.829 21.697  1.00 41.74 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.607 -11.352 19.574  1.00 45.37 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.603 -11.787 18.532  1.00 44.70 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.471 -11.305 18.503  1.00 44.31 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 19.013 -12.709 17.667  1.00 44.49 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.850 -13.004 20.955  1.00 60.63 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.792 -11.237 21.599  1.00 55.10 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.850 -10.430 19.392  1.00 54.45 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.388 -11.921 19.495  1.00 54.45 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.483 -12.990 17.052  1.00 53.38 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.813 -13.025 17.721  1.00 53.38 ?  4   ASN   A HD22 1 
ATOM   30   N  N    A SER   A 1 5   ? 18.214 -9.175  21.047  0.58 38.97 ?  5   SER   A N    1 
ATOM   31   N  N    B SER   A 1 5   ? 18.238 -9.178  21.057  0.42 39.16 ?  5   SER   A N    1 
ATOM   32   C  CA   A SER   A 1 5   ? 17.305 -8.098  21.421  0.58 36.24 ?  5   SER   A CA   1 
ATOM   33   C  CA   B SER   A 1 5   ? 17.355 -8.079  21.420  0.42 36.61 ?  5   SER   A CA   1 
ATOM   34   C  C    A SER   A 1 5   ? 16.428 -7.615  20.269  0.58 32.57 ?  5   SER   A C    1 
ATOM   35   C  C    B SER   A 1 5   ? 16.471 -7.610  20.272  0.42 33.23 ?  5   SER   A C    1 
ATOM   36   O  O    A SER   A 1 5   ? 15.808 -6.552  20.385  0.58 32.93 ?  5   SER   A O    1 
ATOM   37   O  O    B SER   A 1 5   ? 15.688 -6.673  20.457  0.42 33.40 ?  5   SER   A O    1 
ATOM   38   C  CB   A SER   A 1 5   ? 18.086 -6.919  22.005  0.58 36.96 ?  5   SER   A CB   1 
ATOM   39   C  CB   B SER   A 1 5   ? 18.173 -6.902  21.966  0.42 37.24 ?  5   SER   A CB   1 
ATOM   40   O  OG   A SER   A 1 5   ? 19.089 -6.479  21.108  0.58 37.38 ?  5   SER   A OG   1 
ATOM   41   O  OG   B SER   A 1 5   ? 19.076 -6.411  20.990  0.42 37.58 ?  5   SER   A OG   1 
ATOM   42   H  H    A SER   A 1 5   ? 18.931 -8.903  20.660  0.58 46.77 ?  5   SER   A H    1 
ATOM   43   H  H    B SER   A 1 5   ? 18.968 -8.921  20.681  0.42 47.00 ?  5   SER   A H    1 
ATOM   44   H  HA   A SER   A 1 5   ? 16.721 -8.426  22.123  0.58 43.49 ?  5   SER   A HA   1 
ATOM   45   H  HA   B SER   A 1 5   ? 16.770 -8.375  22.131  0.42 43.93 ?  5   SER   A HA   1 
ATOM   46   H  HB2  A SER   A 1 5   ? 17.472 -6.185  22.172  0.58 44.35 ?  5   SER   A HB2  1 
ATOM   47   H  HB2  B SER   A 1 5   ? 17.569 -6.189  22.224  0.42 44.69 ?  5   SER   A HB2  1 
ATOM   48   H  HB3  A SER   A 1 5   ? 18.501 -7.196  22.837  0.58 44.35 ?  5   SER   A HB3  1 
ATOM   49   H  HB3  B SER   A 1 5   ? 18.678 -7.202  22.741  0.42 44.69 ?  5   SER   A HB3  1 
ATOM   50   H  HG   A SER   A 1 5   ? 19.511 -5.834  21.445  0.58 44.85 ?  5   SER   A HG   1 
ATOM   51   H  HG   B SER   A 1 5   ? 19.519 -5.769  21.305  0.42 45.09 ?  5   SER   A HG   1 
ATOM   52   N  N    A PHE   A 1 6   ? 16.362 -8.354  19.165  0.58 28.20 ?  6   PHE   A N    1 
ATOM   53   N  N    B PHE   A 1 6   ? 16.574 -8.225  19.096  0.42 29.46 ?  6   PHE   A N    1 
ATOM   54   C  CA   A PHE   A 1 6   ? 15.471 -7.983  18.073  0.58 24.01 ?  6   PHE   A CA   1 
ATOM   55   C  CA   B PHE   A 1 6   ? 15.629 -7.932  18.027  0.42 25.84 ?  6   PHE   A CA   1 
ATOM   56   C  C    A PHE   A 1 6   ? 14.032 -8.332  18.437  0.58 23.36 ?  6   PHE   A C    1 
ATOM   57   C  C    B PHE   A 1 6   ? 14.236 -8.359  18.464  0.42 25.31 ?  6   PHE   A C    1 
ATOM   58   O  O    A PHE   A 1 6   ? 13.763 -9.399  18.994  0.58 24.52 ?  6   PHE   A O    1 
ATOM   59   O  O    B PHE   A 1 6   ? 14.020 -9.513  18.842  0.42 25.82 ?  6   PHE   A O    1 
ATOM   60   C  CB   A PHE   A 1 6   ? 15.882 -8.704  16.791  0.58 21.05 ?  6   PHE   A CB   1 
ATOM   61   C  CB   B PHE   A 1 6   ? 16.020 -8.690  16.762  0.42 23.21 ?  6   PHE   A CB   1 
ATOM   62   C  CG   A PHE   A 1 6   ? 17.164 -8.187  16.188  0.58 18.86 ?  6   PHE   A CG   1 
ATOM   63   C  CG   B PHE   A 1 6   ? 17.283 -8.194  16.120  0.42 21.09 ?  6   PHE   A CG   1 
ATOM   64   C  CD1  A PHE   A 1 6   ? 17.178 -7.010  15.460  0.58 18.08 ?  6   PHE   A CD1  1 
ATOM   65   C  CD1  B PHE   A 1 6   ? 17.303 -6.986  15.445  0.42 20.22 ?  6   PHE   A CD1  1 
ATOM   66   C  CD2  A PHE   A 1 6   ? 18.347 -8.888  16.344  0.58 19.45 ?  6   PHE   A CD2  1 
ATOM   67   C  CD2  B PHE   A 1 6   ? 18.445 -8.944  16.178  0.42 20.90 ?  6   PHE   A CD2  1 
ATOM   68   C  CE1  A PHE   A 1 6   ? 18.351 -6.535  14.902  0.58 17.83 ?  6   PHE   A CE1  1 
ATOM   69   C  CE1  B PHE   A 1 6   ? 18.462 -6.529  14.848  0.42 19.88 ?  6   PHE   A CE1  1 
ATOM   70   C  CE2  A PHE   A 1 6   ? 19.521 -8.421  15.790  0.58 19.42 ?  6   PHE   A CE2  1 
ATOM   71   C  CE2  B PHE   A 1 6   ? 19.607 -8.494  15.582  0.42 20.63 ?  6   PHE   A CE2  1 
ATOM   72   C  CZ   A PHE   A 1 6   ? 19.525 -7.241  15.068  0.58 18.29 ?  6   PHE   A CZ   1 
ATOM   73   C  CZ   B PHE   A 1 6   ? 19.615 -7.284  14.917  0.42 19.98 ?  6   PHE   A CZ   1 
ATOM   74   H  H    A PHE   A 1 6   ? 16.820 -9.071  19.025  0.58 33.84 ?  6   PHE   A H    1 
ATOM   75   H  H    B PHE   A 1 6   ? 17.171 -8.811  18.896  0.42 35.35 ?  6   PHE   A H    1 
ATOM   76   H  HA   A PHE   A 1 6   ? 15.520 -7.032  17.926  0.58 28.81 ?  6   PHE   A HA   1 
ATOM   77   H  HA   B PHE   A 1 6   ? 15.624 -6.981  17.840  0.42 31.01 ?  6   PHE   A HA   1 
ATOM   78   H  HB2  A PHE   A 1 6   ? 16.003 -9.648  16.991  0.58 25.26 ?  6   PHE   A HB2  1 
ATOM   79   H  HB2  B PHE   A 1 6   ? 16.145 -9.626  16.988  0.42 27.85 ?  6   PHE   A HB2  1 
ATOM   80   H  HB3  A PHE   A 1 6   ? 15.176 -8.601  16.135  0.58 25.26 ?  6   PHE   A HB3  1 
ATOM   81   H  HB3  B PHE   A 1 6   ? 15.302 -8.603  16.115  0.42 27.85 ?  6   PHE   A HB3  1 
ATOM   82   H  HD1  A PHE   A 1 6   ? 16.385 -6.533  15.350  0.58 21.69 ?  6   PHE   A HD1  1 
ATOM   83   H  HD1  B PHE   A 1 6   ? 16.528 -6.474  15.399  0.42 24.26 ?  6   PHE   A HD1  1 
ATOM   84   H  HD2  A PHE   A 1 6   ? 18.349 -9.683  16.832  0.58 23.34 ?  6   PHE   A HD2  1 
ATOM   85   H  HD2  B PHE   A 1 6   ? 18.443 -9.760  16.627  0.42 25.08 ?  6   PHE   A HD2  1 
ATOM   86   H  HE1  A PHE   A 1 6   ? 18.346 -5.742  14.419  0.58 21.40 ?  6   PHE   A HE1  1 
ATOM   87   H  HE1  B PHE   A 1 6   ? 18.464 -5.714  14.401  0.42 23.85 ?  6   PHE   A HE1  1 
ATOM   88   H  HE2  A PHE   A 1 6   ? 20.311 -8.898  15.904  0.58 23.30 ?  6   PHE   A HE2  1 
ATOM   89   H  HE2  B PHE   A 1 6   ? 20.383 -9.005  15.631  0.42 24.75 ?  6   PHE   A HE2  1 
ATOM   90   H  HZ   A PHE   A 1 6   ? 20.313 -6.924  14.695  0.58 21.94 ?  6   PHE   A HZ   1 
ATOM   91   H  HZ   B PHE   A 1 6   ? 20.395 -6.978  14.516  0.42 23.97 ?  6   PHE   A HZ   1 
ATOM   92   N  N    A SER   A 1 7   ? 13.102 -7.426  18.123  0.58 21.51 ?  7   SER   A N    1 
ATOM   93   N  N    B SER   A 1 7   ? 13.285 -7.429  18.406  0.42 24.37 ?  7   SER   A N    1 
ATOM   94   C  CA   A SER   A 1 7   ? 11.726 -7.523  18.600  0.58 21.03 ?  7   SER   A CA   1 
ATOM   95   C  CA   B SER   A 1 7   ? 11.956 -7.663  18.949  0.42 24.00 ?  7   SER   A CA   1 
ATOM   96   C  C    A SER   A 1 7   ? 10.730 -7.319  17.465  0.58 18.89 ?  7   SER   A C    1 
ATOM   97   C  C    B SER   A 1 7   ? 10.902 -7.378  17.891  0.42 22.08 ?  7   SER   A C    1 
ATOM   98   O  O    A SER   A 1 7   ? 10.919 -6.453  16.608  0.58 18.80 ?  7   SER   A O    1 
ATOM   99   O  O    B SER   A 1 7   ? 11.043 -6.448  17.091  0.42 22.08 ?  7   SER   A O    1 
ATOM   100  C  CB   A SER   A 1 7   ? 11.474 -6.475  19.695  0.58 22.57 ?  7   SER   A CB   1 
ATOM   101  C  CB   B SER   A 1 7   ? 11.710 -6.786  20.182  0.42 25.30 ?  7   SER   A CB   1 
ATOM   102  O  OG   A SER   A 1 7   ? 10.123 -6.478  20.116  0.58 23.60 ?  7   SER   A OG   1 
ATOM   103  O  OG   B SER   A 1 7   ? 10.600 -7.255  20.925  0.42 26.21 ?  7   SER   A OG   1 
ATOM   104  H  H    A SER   A 1 7   ? 13.247 -6.741  17.626  0.58 25.81 ?  7   SER   A H    1 
ATOM   105  H  H    B SER   A 1 7   ? 13.386 -6.653  18.044  0.42 29.25 ?  7   SER   A H    1 
ATOM   106  H  HA   A SER   A 1 7   ? 11.574 -8.401  18.980  0.58 25.24 ?  7   SER   A HA   1 
ATOM   107  H  HA   B SER   A 1 7   ? 11.870 -8.590  19.214  0.42 28.80 ?  7   SER   A HA   1 
ATOM   108  H  HB2  A SER   A 1 7   ? 12.043 -6.676  20.455  0.58 27.08 ?  7   SER   A HB2  1 
ATOM   109  H  HB2  B SER   A 1 7   ? 12.504 -6.803  20.742  0.42 30.36 ?  7   SER   A HB2  1 
ATOM   110  H  HB3  A SER   A 1 7   ? 11.691 -5.598  19.345  0.58 27.08 ?  7   SER   A HB3  1 
ATOM   111  H  HB3  B SER   A 1 7   ? 11.527 -5.879  19.895  0.42 30.36 ?  7   SER   A HB3  1 
ATOM   112  H  HG   A SER   A 1 7   ? 10.009 -5.902  20.717  0.58 28.31 ?  7   SER   A HG   1 
ATOM   113  H  HG   B SER   A 1 7   ? 10.488 -6.776  21.606  0.42 31.45 ?  7   SER   A HG   1 
ATOM   114  N  N    A GLY   A 1 8   ? 9.664  -8.121  17.465  0.58 17.65 ?  8   GLY   A N    1 
ATOM   115  N  N    B GLY   A 1 8   ? 9.851  -8.194  17.886  0.42 20.26 ?  8   GLY   A N    1 
ATOM   116  C  CA   A GLY   A 1 8   ? 8.565  -7.916  16.540  0.58 16.36 ?  8   GLY   A CA   1 
ATOM   117  C  CA   B GLY   A 1 8   ? 8.731  -7.977  17.000  0.42 18.51 ?  8   GLY   A CA   1 
ATOM   118  C  C    A GLY   A 1 8   ? 8.784  -8.422  15.130  0.58 14.97 ?  8   GLY   A C    1 
ATOM   119  C  C    B GLY   A 1 8   ? 8.921  -8.453  15.582  0.42 16.87 ?  8   GLY   A C    1 
ATOM   120  O  O    A GLY   A 1 8   ? 8.055  -8.017  14.219  0.58 15.17 ?  8   GLY   A O    1 
ATOM   121  O  O    B GLY   A 1 8   ? 8.080  -8.146  14.730  0.42 17.07 ?  8   GLY   A O    1 
ATOM   122  H  H    A GLY   A 1 8   ? 9.560  -8.791  17.994  0.58 21.18 ?  8   GLY   A H    1 
ATOM   123  H  H    B GLY   A 1 8   ? 9.770  -8.887  18.389  0.42 24.32 ?  8   GLY   A H    1 
ATOM   124  H  HA2  A GLY   A 1 8   ? 7.772  -8.349  16.905  0.58 19.64 ?  8   GLY   A HA2  1 
ATOM   125  H  HA2  B GLY   A 1 8   ? 7.956  -8.437  17.351  0.42 22.22 ?  8   GLY   A HA2  1 
ATOM   126  H  HA3  A GLY   A 1 8   ? 8.378  -6.964  16.489  0.58 19.64 ?  8   GLY   A HA3  1 
ATOM   127  H  HA3  B GLY   A 1 8   ? 8.534  -7.031  16.966  0.42 22.22 ?  8   GLY   A HA3  1 
ATOM   128  N  N    A TYR   A 1 9   ? 9.762  -9.298  14.916  0.58 13.85 ?  9   TYR   A N    1 
ATOM   129  N  N    B TYR   A 1 9   ? 9.984  -9.197  15.295  0.42 15.55 ?  9   TYR   A N    1 
ATOM   130  C  CA   A TYR   A 1 9   ? 10.032 -9.851  13.597  0.58 12.74 ?  9   TYR   A CA   1 
ATOM   131  C  CA   B TYR   A 1 9   ? 10.210 -9.674  13.940  0.42 14.31 ?  9   TYR   A CA   1 
ATOM   132  C  C    A TYR   A 1 9   ? 9.179  -11.085 13.338  0.58 11.98 ?  9   TYR   A C    1 
ATOM   133  C  C    B TYR   A 1 9   ? 9.372  -10.912 13.657  0.42 13.43 ?  9   TYR   A C    1 
ATOM   134  O  O    A TYR   A 1 9   ? 8.876  -11.866 14.246  0.58 13.33 ?  9   TYR   A O    1 
ATOM   135  O  O    B TYR   A 1 9   ? 9.229  -11.798 14.506  0.42 14.48 ?  9   TYR   A O    1 
ATOM   136  C  CB   A TYR   A 1 9   ? 11.506 -10.250 13.463  0.58 13.14 ?  9   TYR   A CB   1 
ATOM   137  C  CB   B TYR   A 1 9   ? 11.691 -9.984  13.721  0.42 14.21 ?  9   TYR   A CB   1 
ATOM   138  C  CG   A TYR   A 1 9   ? 12.450 -9.085  13.318  0.58 13.37 ?  9   TYR   A CG   1 
ATOM   139  C  CG   B TYR   A 1 9   ? 12.520 -8.741  13.486  0.42 13.43 ?  9   TYR   A CG   1 
ATOM   140  C  CD1  A TYR   A 1 9   ? 12.819 -8.326  14.419  0.58 13.73 ?  9   TYR   A CD1  1 
ATOM   141  C  CD1  B TYR   A 1 9   ? 12.803 -7.867  14.526  0.42 13.66 ?  9   TYR   A CD1  1 
ATOM   142  C  CD2  A TYR   A 1 9   ? 12.967 -8.739  12.077  0.58 13.65 ?  9   TYR   A CD2  1 
ATOM   143  C  CD2  B TYR   A 1 9   ? 12.999 -8.431  12.220  0.42 12.93 ?  9   TYR   A CD2  1 
ATOM   144  C  CE1  A TYR   A 1 9   ? 13.671 -7.250  14.291  0.58 14.25 ?  9   TYR   A CE1  1 
ATOM   145  C  CE1  B TYR   A 1 9   ? 13.544 -6.723  14.314  0.42 13.50 ?  9   TYR   A CE1  1 
ATOM   146  C  CE2  A TYR   A 1 9   ? 13.816 -7.668  11.937  0.58 13.70 ?  9   TYR   A CE2  1 
ATOM   147  C  CE2  B TYR   A 1 9   ? 13.738 -7.291  11.999  0.42 12.51 ?  9   TYR   A CE2  1 
ATOM   148  C  CZ   A TYR   A 1 9   ? 14.164 -6.925  13.045  0.58 14.43 ?  9   TYR   A CZ   1 
ATOM   149  C  CZ   B TYR   A 1 9   ? 14.008 -6.446  13.047  0.42 12.75 ?  9   TYR   A CZ   1 
ATOM   150  O  OH   A TYR   A 1 9   ? 15.010 -5.857  12.905  0.58 15.59 ?  9   TYR   A OH   1 
ATOM   151  O  OH   B TYR   A 1 9   ? 14.740 -5.312  12.810  0.42 12.90 ?  9   TYR   A OH   1 
ATOM   152  H  H    A TYR   A 1 9   ? 10.278 -9.593  15.527  0.58 16.62 ?  9   TYR   A H    1 
ATOM   153  H  H    B TYR   A 1 9   ? 10.588 -9.445  15.863  0.42 18.66 ?  9   TYR   A H    1 
ATOM   154  H  HA   A TYR   A 1 9   ? 9.827  -9.189  12.915  0.58 15.29 ?  9   TYR   A HA   1 
ATOM   155  H  HA   B TYR   A 1 9   ? 9.956  -8.979  13.313  0.42 17.17 ?  9   TYR   A HA   1 
ATOM   156  H  HB2  A TYR   A 1 9   ? 11.767 -10.750 14.250  0.58 15.77 ?  9   TYR   A HB2  1 
ATOM   157  H  HB2  B TYR   A 1 9   ? 12.042 -10.451 14.497  0.42 17.05 ?  9   TYR   A HB2  1 
ATOM   158  H  HB3  A TYR   A 1 9   ? 11.597 -10.805 12.674  0.58 15.77 ?  9   TYR   A HB3  1 
ATOM   159  H  HB3  B TYR   A 1 9   ? 11.764 -10.547 12.935  0.42 17.05 ?  9   TYR   A HB3  1 
ATOM   160  H  HD1  A TYR   A 1 9   ? 12.473 -8.543  15.258  0.58 16.48 ?  9   TYR   A HD1  1 
ATOM   161  H  HD1  B TYR   A 1 9   ? 12.487 -8.059  15.380  0.42 16.39 ?  9   TYR   A HD1  1 
ATOM   162  H  HD2  A TYR   A 1 9   ? 12.731 -9.240  11.328  0.58 16.38 ?  9   TYR   A HD2  1 
ATOM   163  H  HD2  B TYR   A 1 9   ? 12.816 -9.002  11.509  0.42 15.52 ?  9   TYR   A HD2  1 
ATOM   164  H  HE1  A TYR   A 1 9   ? 13.909 -6.750  15.037  0.58 17.10 ?  9   TYR   A HE1  1 
ATOM   165  H  HE1  B TYR   A 1 9   ? 13.731 -6.148  15.020  0.42 16.20 ?  9   TYR   A HE1  1 
ATOM   166  H  HE2  A TYR   A 1 9   ? 14.163 -7.454  11.100  0.58 16.44 ?  9   TYR   A HE2  1 
ATOM   167  H  HE2  B TYR   A 1 9   ? 14.060 -7.094  11.146  0.42 15.01 ?  9   TYR   A HE2  1 
ATOM   168  H  HH   A TYR   A 1 9   ? 15.151 -5.507  13.655  0.58 18.71 ?  9   TYR   A HH   1 
ATOM   169  H  HH   B TYR   A 1 9   ? 14.847 -4.876  13.523  0.42 15.48 ?  9   TYR   A HH   1 
ATOM   170  N  N    A LEU   A 1 10  ? 8.806  -11.258 12.074  0.58 11.44 ?  10  LEU   A N    1 
ATOM   171  N  N    B LEU   A 1 10  ? 8.808  -10.961 12.453  0.42 12.29 ?  10  LEU   A N    1 
ATOM   172  C  CA   A LEU   A 1 10  ? 8.205  -12.490 11.588  0.58 11.15 ?  10  LEU   A CA   1 
ATOM   173  C  CA   B LEU   A 1 10  ? 8.144  -12.159 11.966  0.42 11.79 ?  10  LEU   A CA   1 
ATOM   174  C  C    A LEU   A 1 10  ? 9.322  -13.434 11.148  0.58 11.05 ?  10  LEU   A C    1 
ATOM   175  C  C    B LEU   A 1 10  ? 9.202  -13.133 11.467  0.42 11.34 ?  10  LEU   A C    1 
ATOM   176  O  O    A LEU   A 1 10  ? 10.262 -13.017 10.463  0.58 11.07 ?  10  LEU   A O    1 
ATOM   177  O  O    B LEU   A 1 10  ? 10.086 -12.760 10.690  0.42 11.48 ?  10  LEU   A O    1 
ATOM   178  C  CB   A LEU   A 1 10  ? 7.298  -12.171 10.401  0.58 12.40 ?  10  LEU   A CB   1 
ATOM   179  C  CB   B LEU   A 1 10  ? 7.198  -11.792 10.825  0.42 11.78 ?  10  LEU   A CB   1 
ATOM   180  C  CG   A LEU   A 1 10  ? 6.610  -13.348 9.719   0.58 14.02 ?  10  LEU   A CG   1 
ATOM   181  C  CG   B LEU   A 1 10  ? 6.479  -12.965 10.165  0.42 12.02 ?  10  LEU   A CG   1 
ATOM   182  C  CD1  A LEU   A 1 10  ? 5.602  -13.973 10.659  0.58 15.29 ?  10  LEU   A CD1  1 
ATOM   183  C  CD1  B LEU   A 1 10  ? 5.507  -13.610 11.140  0.42 13.11 ?  10  LEU   A CD1  1 
ATOM   184  C  CD2  A LEU   A 1 10  ? 5.947  -12.912 8.423   0.58 15.10 ?  10  LEU   A CD2  1 
ATOM   185  C  CD2  B LEU   A 1 10  ? 5.765  -12.471 8.926   0.42 13.20 ?  10  LEU   A CD2  1 
ATOM   186  H  H    A LEU   A 1 10  ? 8.896  -10.662 11.457  0.58 13.72 ?  10  LEU   A H    1 
ATOM   187  H  H    B LEU   A 1 10  ? 8.795  -10.303 11.895  0.42 14.74 ?  10  LEU   A H    1 
ATOM   188  H  HA   A LEU   A 1 10  ? 7.686  -12.913 12.294  0.58 13.38 ?  10  LEU   A HA   1 
ATOM   189  H  HA   B LEU   A 1 10  ? 7.630  -12.573 12.682  0.42 14.15 ?  10  LEU   A HA   1 
ATOM   190  H  HB2  A LEU   A 1 10  ? 6.598  -11.578 10.708  0.58 14.89 ?  10  LEU   A HB2  1 
ATOM   191  H  HB2  B LEU   A 1 10  ? 6.512  -11.190 11.166  0.42 14.13 ?  10  LEU   A HB2  1 
ATOM   192  H  HB3  A LEU   A 1 10  ? 7.829  -11.727 9.728   0.58 14.89 ?  10  LEU   A HB3  1 
ATOM   193  H  HB3  B LEU   A 1 10  ? 7.705  -11.341 10.134  0.42 14.13 ?  10  LEU   A HB3  1 
ATOM   194  H  HG   A LEU   A 1 10  ? 7.270  -14.028 9.501   0.58 16.83 ?  10  LEU   A HG   1 
ATOM   195  H  HG   B LEU   A 1 10  ? 7.127  -13.633 9.898   0.42 14.43 ?  10  LEU   A HG   1 
ATOM   196  H  HD11 A LEU   A 1 10  ? 5.243  -14.779 10.255  0.58 18.35 ?  10  LEU   A HD11 1 
ATOM   197  H  HD11 B LEU   A 1 10  ? 5.082  -14.370 10.709  0.42 15.73 ?  10  LEU   A HD11 1 
ATOM   198  H  HD12 A LEU   A 1 10  ? 6.036  -14.189 11.498  0.58 18.35 ?  10  LEU   A HD12 1 
ATOM   199  H  HD12 B LEU   A 1 10  ? 5.990  -13.909 11.927  0.42 15.73 ?  10  LEU   A HD12 1 
ATOM   200  H  HD13 A LEU   A 1 10  ? 4.884  -13.337 10.818  0.58 18.35 ?  10  LEU   A HD13 1 
ATOM   201  H  HD13 B LEU   A 1 10  ? 4.834  -12.960 11.397  0.42 15.73 ?  10  LEU   A HD13 1 
ATOM   202  H  HD21 A LEU   A 1 10  ? 5.517  -13.681 8.014   0.58 18.12 ?  10  LEU   A HD21 1 
ATOM   203  H  HD21 B LEU   A 1 10  ? 5.287  -13.212 8.524   0.42 15.84 ?  10  LEU   A HD21 1 
ATOM   204  H  HD22 A LEU   A 1 10  ? 5.286  -12.232 8.623   0.58 18.12 ?  10  LEU   A HD22 1 
ATOM   205  H  HD22 B LEU   A 1 10  ? 5.140  -11.773 9.181   0.42 15.84 ?  10  LEU   A HD22 1 
ATOM   206  H  HD23 A LEU   A 1 10  ? 6.623  -12.556 7.829   0.58 18.12 ?  10  LEU   A HD23 1 
ATOM   207  H  HD23 B LEU   A 1 10  ? 6.420  -12.120 8.307   0.42 15.84 ?  10  LEU   A HD23 1 
ATOM   208  N  N    A LYS   A 1 11  ? 9.217  -14.703 11.537  0.58 11.62 ?  11  LYS   A N    1 
ATOM   209  N  N    B LYS   A 1 11  ? 9.118  -14.377 11.918  0.42 11.52 ?  11  LYS   A N    1 
ATOM   210  C  CA   A LYS   A 1 11  ? 10.223 -15.705 11.206  0.58 11.34 ?  11  LYS   A CA   1 
ATOM   211  C  CA   B LYS   A 1 11  ? 10.071 -15.396 11.508  0.42 11.37 ?  11  LYS   A CA   1 
ATOM   212  C  C    A LYS   A 1 11  ? 9.876  -16.312 9.854   0.58 11.30 ?  11  LYS   A C    1 
ATOM   213  C  C    B LYS   A 1 11  ? 9.687  -15.913 10.127  0.42 10.66 ?  11  LYS   A C    1 
ATOM   214  O  O    A LYS   A 1 11  ? 8.800  -16.892 9.693   0.58 13.04 ?  11  LYS   A O    1 
ATOM   215  O  O    B LYS   A 1 11  ? 8.556  -16.368 9.925   0.42 10.84 ?  11  LYS   A O    1 
ATOM   216  C  CB   A LYS   A 1 11  ? 10.272 -16.771 12.302  0.58 11.72 ?  11  LYS   A CB   1 
ATOM   217  C  CB   B LYS   A 1 11  ? 10.064 -16.528 12.530  0.42 11.47 ?  11  LYS   A CB   1 
ATOM   218  C  CG   A LYS   A 1 11  ? 11.320 -17.866 12.124  0.58 12.37 ?  11  LYS   A CG   1 
ATOM   219  C  CG   B LYS   A 1 11  ? 11.031 -17.651 12.232  0.42 11.75 ?  11  LYS   A CG   1 
ATOM   220  C  CD   A LYS   A 1 11  ? 11.438 -18.682 13.416  0.58 12.32 ?  11  LYS   A CD   1 
ATOM   221  C  CD   B LYS   A 1 11  ? 11.029 -18.662 13.366  0.42 11.85 ?  11  LYS   A CD   1 
ATOM   222  C  CE   A LYS   A 1 11  ? 12.433 -19.831 13.307  0.58 12.35 ?  11  LYS   A CE   1 
ATOM   223  C  CE   B LYS   A 1 11  ? 12.030 -19.778 13.130  0.42 12.13 ?  11  LYS   A CE   1 
ATOM   224  N  NZ   A LYS   A 1 11  ? 13.808 -19.367 12.996  0.58 12.72 ?  11  LYS   A NZ   1 
ATOM   225  N  NZ   B LYS   A 1 11  ? 13.437 -19.282 13.071  0.42 12.62 ?  11  LYS   A NZ   1 
ATOM   226  H  H    A LYS   A 1 11  ? 8.550  -15.015 11.986  0.58 13.95 ?  11  LYS   A H    1 
ATOM   227  H  H    B LYS   A 1 11  ? 8.508  -14.660 12.456  0.42 13.82 ?  11  LYS   A H    1 
ATOM   228  H  HA   A LYS   A 1 11  ? 11.090 -15.283 11.141  0.58 13.61 ?  11  LYS   A HA   1 
ATOM   229  H  HA   B LYS   A 1 11  ? 10.960 -15.010 11.463  0.42 13.64 ?  11  LYS   A HA   1 
ATOM   230  H  HB2  A LYS   A 1 11  ? 10.462 -16.327 13.146  0.58 14.06 ?  11  LYS   A HB2  1 
ATOM   231  H  HB2  B LYS   A 1 11  ? 10.298 -16.158 13.397  0.42 13.76 ?  11  LYS   A HB2  1 
ATOM   232  H  HB3  A LYS   A 1 11  ? 9.408  -17.203 12.354  0.58 14.06 ?  11  LYS   A HB3  1 
ATOM   233  H  HB3  B LYS   A 1 11  ? 9.174  -16.905 12.565  0.42 13.76 ?  11  LYS   A HB3  1 
ATOM   234  H  HG2  A LYS   A 1 11  ? 11.052 -18.461 11.406  0.58 14.85 ?  11  LYS   A HG2  1 
ATOM   235  H  HG2  B LYS   A 1 11  ? 10.764 -18.103 11.417  0.42 14.10 ?  11  LYS   A HG2  1 
ATOM   236  H  HG3  A LYS   A 1 11  ? 12.184 -17.467 11.932  0.58 14.85 ?  11  LYS   A HG3  1 
ATOM   237  H  HG3  B LYS   A 1 11  ? 11.928 -17.290 12.142  0.42 14.10 ?  11  LYS   A HG3  1 
ATOM   238  H  HD2  A LYS   A 1 11  ? 11.734 -18.099 14.133  0.58 14.78 ?  11  LYS   A HD2  1 
ATOM   239  H  HD2  B LYS   A 1 11  ? 11.263 -18.212 14.193  0.42 14.22 ?  11  LYS   A HD2  1 
ATOM   240  H  HD3  A LYS   A 1 11  ? 10.569 -19.057 13.632  0.58 14.78 ?  11  LYS   A HD3  1 
ATOM   241  H  HD3  B LYS   A 1 11  ? 10.144 -19.054 13.438  0.42 14.22 ?  11  LYS   A HD3  1 
ATOM   242  H  HE2  A LYS   A 1 11  ? 12.460 -20.309 14.154  0.58 14.82 ?  11  LYS   A HE2  1 
ATOM   243  H  HE2  B LYS   A 1 11  ? 11.966 -20.420 13.855  0.42 14.55 ?  11  LYS   A HE2  1 
ATOM   244  H  HE3  A LYS   A 1 11  ? 12.148 -20.432 12.600  0.58 14.82 ?  11  LYS   A HE3  1 
ATOM   245  H  HE3  B LYS   A 1 11  ? 11.827 -20.212 12.285  0.42 14.55 ?  11  LYS   A HE3  1 
ATOM   246  H  HZ1  A LYS   A 1 11  ? 14.358 -20.066 12.941  0.58 15.26 ?  11  LYS   A HZ1  1 
ATOM   247  H  HZ1  B LYS   A 1 11  ? 13.987 -19.950 12.863  0.42 15.14 ?  11  LYS   A HZ1  1 
ATOM   248  H  HZ2  A LYS   A 1 11  ? 13.811 -18.934 12.220  0.58 15.26 ?  11  LYS   A HZ2  1 
ATOM   249  H  HZ2  B LYS   A 1 11  ? 13.510 -18.645 12.452  0.42 15.14 ?  11  LYS   A HZ2  1 
ATOM   250  H  HZ3  A LYS   A 1 11  ? 14.096 -18.822 13.636  0.58 15.26 ?  11  LYS   A HZ3  1 
ATOM   251  H  HZ3  B LYS   A 1 11  ? 13.674 -18.946 13.859  0.42 15.14 ?  11  LYS   A HZ3  1 
ATOM   252  N  N    A LEU   A 1 12  ? 10.770 -16.167 8.875   0.58 10.44 ?  12  LEU   A N    1 
ATOM   253  N  N    B LEU   A 1 12  ? 10.607 -15.817 9.168   0.42 10.99 ?  12  LEU   A N    1 
ATOM   254  C  CA   A LEU   A 1 12  ? 10.506 -16.756 7.565   0.58 10.78 ?  12  LEU   A CA   1 
ATOM   255  C  CA   B LEU   A 1 12  ? 10.377 -16.349 7.830   0.42 10.72 ?  12  LEU   A CA   1 
ATOM   256  C  C    A LEU   A 1 12  ? 11.104 -18.150 7.413   0.58 10.79 ?  12  LEU   A C    1 
ATOM   257  C  C    B LEU   A 1 12  ? 10.950 -17.744 7.640   0.42 10.58 ?  12  LEU   A C    1 
ATOM   258  O  O    A LEU   A 1 12  ? 10.467 -19.030 6.822   0.58 11.06 ?  12  LEU   A O    1 
ATOM   259  O  O    B LEU   A 1 12  ? 10.297 -18.601 7.033   0.42 11.02 ?  12  LEU   A O    1 
ATOM   260  C  CB   A LEU   A 1 12  ? 11.030 -15.850 6.445   0.58 11.01 ?  12  LEU   A CB   1 
ATOM   261  C  CB   B LEU   A 1 12  ? 10.970 -15.419 6.768   0.42 11.42 ?  12  LEU   A CB   1 
ATOM   262  C  CG   A LEU   A 1 12  ? 10.376 -14.480 6.272   0.58 12.06 ?  12  LEU   A CG   1 
ATOM   263  C  CG   B LEU   A 1 12  ? 10.280 -14.064 6.630   0.42 12.30 ?  12  LEU   A CG   1 
ATOM   264  C  CD1  A LEU   A 1 12  ? 11.119 -13.691 5.220   0.58 12.41 ?  12  LEU   A CD1  1 
ATOM   265  C  CD1  B LEU   A 1 12  ? 10.844 -13.309 5.443   0.42 12.85 ?  12  LEU   A CD1  1 
ATOM   266  C  CD2  A LEU   A 1 12  ? 8.902  -14.623 5.897   0.58 12.96 ?  12  LEU   A CD2  1 
ATOM   267  C  CD2  B LEU   A 1 12  ? 8.777  -14.255 6.494   0.42 12.63 ?  12  LEU   A CD2  1 
ATOM   268  H  H    A LEU   A 1 12  ? 11.517 -15.734 8.939   0.58 12.53 ?  12  LEU   A H    1 
ATOM   269  H  H    B LEU   A 1 12  ? 11.372 -15.427 9.263   0.42 13.19 ?  12  LEU   A H    1 
ATOM   270  H  HA   A LEU   A 1 12  ? 9.552  -16.839 7.455   0.58 12.93 ?  12  LEU   A HA   1 
ATOM   271  H  HA   B LEU   A 1 12  ? 9.423  -16.412 7.680   0.42 12.87 ?  12  LEU   A HA   1 
ATOM   272  H  HB2  A LEU   A 1 12  ? 11.972 -15.697 6.596   0.58 13.22 ?  12  LEU   A HB2  1 
ATOM   273  H  HB2  B LEU   A 1 12  ? 11.901 -15.249 6.990   0.42 13.70 ?  12  LEU   A HB2  1 
ATOM   274  H  HB3  A LEU   A 1 12  ? 10.915 -16.325 5.605   0.58 13.22 ?  12  LEU   A HB3  1 
ATOM   275  H  HB3  B LEU   A 1 12  ? 10.919 -15.860 5.906   0.42 13.70 ?  12  LEU   A HB3  1 
ATOM   276  H  HG   A LEU   A 1 12  ? 10.427 -13.995 7.110   0.58 14.47 ?  12  LEU   A HG   1 
ATOM   277  H  HG   B LEU   A 1 12  ? 10.447 -13.539 7.430   0.42 14.75 ?  12  LEU   A HG   1 
ATOM   278  H  HD11 A LEU   A 1 12  ? 10.692 -12.827 5.113   0.58 14.90 ?  12  LEU   A HD11 1 
ATOM   279  H  HD11 B LEU   A 1 12  ? 10.399 -12.450 5.375   0.42 15.42 ?  12  LEU   A HD11 1 
ATOM   280  H  HD12 A LEU   A 1 12  ? 12.038 -13.572 5.509   0.58 14.90 ?  12  LEU   A HD12 1 
ATOM   281  H  HD12 B LEU   A 1 12  ? 11.796 -13.179 5.575   0.42 15.42 ?  12  LEU   A HD12 1 
ATOM   282  H  HD13 A LEU   A 1 12  ? 11.096 -14.180 4.383   0.58 14.90 ?  12  LEU   A HD13 1 
ATOM   283  H  HD13 B LEU   A 1 12  ? 10.689 -13.827 4.638   0.42 15.42 ?  12  LEU   A HD13 1 
ATOM   284  H  HD21 A LEU   A 1 12  ? 8.531  -13.746 5.726   0.58 15.56 ?  12  LEU   A HD21 1 
ATOM   285  H  HD21 B LEU   A 1 12  ? 8.387  -13.451 6.125   0.42 15.15 ?  12  LEU   A HD21 1 
ATOM   286  H  HD22 A LEU   A 1 12  ? 8.831  -15.174 5.100   0.58 15.56 ?  12  LEU   A HD22 1 
ATOM   287  H  HD22 B LEU   A 1 12  ? 8.608  -15.010 5.908   0.42 15.15 ?  12  LEU   A HD22 1 
ATOM   288  H  HD23 A LEU   A 1 12  ? 8.427  -15.047 6.631   0.58 15.56 ?  12  LEU   A HD23 1 
ATOM   289  H  HD23 B LEU   A 1 12  ? 8.401  -14.434 7.374   0.42 15.15 ?  12  LEU   A HD23 1 
ATOM   290  N  N    A THR   A 1 13  ? 12.323 -18.352 7.910   0.58 11.16 ?  13  THR   A N    1 
ATOM   291  N  N    B THR   A 1 13  ? 12.166 -17.979 8.124   0.42 10.87 ?  13  THR   A N    1 
ATOM   292  C  CA   A THR   A 1 13  ? 13.024 -19.629 7.826   0.58 11.79 ?  13  THR   A CA   1 
ATOM   293  C  CA   B THR   A 1 13  ? 12.820 -19.273 8.020   0.42 11.09 ?  13  THR   A CA   1 
ATOM   294  C  C    A THR   A 1 13  ? 13.807 -19.824 9.120   0.58 11.67 ?  13  THR   A C    1 
ATOM   295  C  C    B THR   A 1 13  ? 13.578 -19.530 9.315   0.42 11.57 ?  13  THR   A C    1 
ATOM   296  O  O    A THR   A 1 13  ? 13.696 -19.037 10.065  0.58 12.11 ?  13  THR   A O    1 
ATOM   297  O  O    B THR   A 1 13  ? 13.491 -18.767 10.283  0.42 12.10 ?  13  THR   A O    1 
ATOM   298  C  CB   A THR   A 1 13  ? 13.988 -19.681 6.632   0.58 12.90 ?  13  THR   A CB   1 
ATOM   299  C  CB   B THR   A 1 13  ? 13.800 -19.321 6.841   0.42 11.23 ?  13  THR   A CB   1 
ATOM   300  O  OG1  A THR   A 1 13  ? 15.068 -18.773 6.867   0.58 13.22 ?  13  THR   A OG1  1 
ATOM   301  O  OG1  B THR   A 1 13  ? 14.870 -18.407 7.092   0.42 10.73 ?  13  THR   A OG1  1 
ATOM   302  C  CG2  A THR   A 1 13  ? 13.300 -19.314 5.325   0.58 13.81 ?  13  THR   A CG2  1 
ATOM   303  C  CG2  B THR   A 1 13  ? 13.119 -18.987 5.517   0.42 12.18 ?  13  THR   A CG2  1 
ATOM   304  H  H    A THR   A 1 13  ? 12.787 -17.743 8.303   0.58 13.40 ?  13  THR   A H    1 
ATOM   305  H  H    B THR   A 1 13  ? 12.646 -17.379 8.516   0.42 13.04 ?  13  THR   A H    1 
ATOM   306  H  HA   A THR   A 1 13  ? 12.380 -20.352 7.736   0.58 14.15 ?  13  THR   A HA   1 
ATOM   307  H  HA   B THR   A 1 13  ? 12.157 -19.967 7.902   0.42 13.31 ?  13  THR   A HA   1 
ATOM   308  H  HB   A THR   A 1 13  ? 14.342 -20.583 6.543   0.58 15.48 ?  13  THR   A HB   1 
ATOM   309  H  HB   B THR   A 1 13  ? 14.175 -20.209 6.771   0.42 13.48 ?  13  THR   A HB   1 
ATOM   310  H  HG1  A THR   A 1 13  ? 15.607 -18.794 6.221   0.58 15.87 ?  13  THR   A HG1  1 
ATOM   311  H  HG1  B THR   A 1 13  ? 15.410 -18.399 6.444   0.42 12.88 ?  13  THR   A HG1  1 
ATOM   312  H  HG21 A THR   A 1 13  ? 13.910 -19.455 4.581   0.58 16.57 ?  13  THR   A HG21 1 
ATOM   313  H  HG21 B THR   A 1 13  ? 13.756 -19.074 4.786   0.42 14.62 ?  13  THR   A HG21 1 
ATOM   314  H  HG22 A THR   A 1 13  ? 12.516 -19.865 5.196   0.58 16.57 ?  13  THR   A HG22 1 
ATOM   315  H  HG22 B THR   A 1 13  ? 12.384 -19.602 5.363   0.42 14.62 ?  13  THR   A HG22 1 
ATOM   316  H  HG23 A THR   A 1 13  ? 13.037 -18.382 5.341   0.58 16.57 ?  13  THR   A HG23 1 
ATOM   317  H  HG23 B THR   A 1 13  ? 12.779 -18.082 5.532   0.42 14.62 ?  13  THR   A HG23 1 
ATOM   318  N  N    A ASP   A 1 14  ? 14.641 -20.867 9.149   0.58 12.46 ?  14  ASP   A N    1 
ATOM   319  N  N    B ASP   A 1 14  ? 14.339 -20.621 9.309   0.42 12.08 ?  14  ASP   A N    1 
ATOM   320  C  CA   A ASP   A 1 14  ? 15.460 -21.118 10.329  0.58 13.52 ?  14  ASP   A CA   1 
ATOM   321  C  CA   B ASP   A 1 14  ? 15.231 -20.928 10.415  0.42 13.29 ?  14  ASP   A CA   1 
ATOM   322  C  C    A ASP   A 1 14  ? 16.281 -19.898 10.740  0.58 13.22 ?  14  ASP   A C    1 
ATOM   323  C  C    B ASP   A 1 14  ? 16.087 -19.723 10.785  0.42 12.76 ?  14  ASP   A C    1 
ATOM   324  O  O    A ASP   A 1 14  ? 16.573 -19.721 11.928  0.58 13.66 ?  14  ASP   A O    1 
ATOM   325  O  O    B ASP   A 1 14  ? 16.228 -19.395 11.968  0.42 12.57 ?  14  ASP   A O    1 
ATOM   326  C  CB   A ASP   A 1 14  ? 16.394 -22.302 10.079  0.58 16.39 ?  14  ASP   A CB   1 
ATOM   327  C  CB   B ASP   A 1 14  ? 16.124 -22.099 10.015  0.42 15.78 ?  14  ASP   A CB   1 
ATOM   328  C  CG   A ASP   A 1 14  ? 17.280 -22.591 11.268  0.58 20.32 ?  14  ASP   A CG   1 
ATOM   329  C  CG   B ASP   A 1 14  ? 17.126 -22.450 11.086  0.42 18.59 ?  14  ASP   A CG   1 
ATOM   330  O  OD1  A ASP   A 1 14  ? 16.755 -23.113 12.277  0.58 21.79 ?  14  ASP   A OD1  1 
ATOM   331  O  OD1  B ASP   A 1 14  ? 16.699 -22.737 12.224  0.42 19.33 ?  14  ASP   A OD1  1 
ATOM   332  O  OD2  A ASP   A 1 14  ? 18.489 -22.284 11.197  0.58 22.76 -1 14  ASP   A OD2  1 
ATOM   333  O  OD2  B ASP   A 1 14  ? 18.337 -22.431 10.791  0.42 20.29 -1 14  ASP   A OD2  1 
ATOM   334  H  H    A ASP   A 1 14  ? 14.750 -21.436 8.506   0.58 14.95 ?  14  ASP   A H    1 
ATOM   335  H  H    B ASP   A 1 14  ? 14.360 -21.185 8.673   0.42 14.50 ?  14  ASP   A H    1 
ATOM   336  H  HA   A ASP   A 1 14  ? 14.882 -21.356 11.068  0.58 16.23 ?  14  ASP   A HA   1 
ATOM   337  H  HA   B ASP   A 1 14  ? 14.707 -21.187 11.194  0.42 15.94 ?  14  ASP   A HA   1 
ATOM   338  H  HB2  A ASP   A 1 14  ? 15.863 -23.106 9.915   0.58 19.67 ?  14  ASP   A HB2  1 
ATOM   339  H  HB2  B ASP   A 1 14  ? 15.559 -22.873 9.836   0.42 18.93 ?  14  ASP   A HB2  1 
ATOM   340  H  HB3  A ASP   A 1 14  ? 16.956 -22.120 9.312   0.58 19.67 ?  14  ASP   A HB3  1 
ATOM   341  H  HB3  B ASP   A 1 14  ? 16.610 -21.859 9.209   0.42 18.93 ?  14  ASP   A HB3  1 
ATOM   342  N  N    . ASN   A 1 15  ? 16.656 -19.041 9.786   1.00 12.83 ?  15  ASN   A N    1 
ATOM   343  C  CA   . ASN   A 1 15  ? 17.635 -17.991 10.046  1.00 13.09 ?  15  ASN   A CA   1 
ATOM   344  C  C    . ASN   A 1 15  ? 17.266 -16.603 9.543   1.00 13.19 ?  15  ASN   A C    1 
ATOM   345  O  O    . ASN   A 1 15  ? 18.049 -15.678 9.764   1.00 14.78 ?  15  ASN   A O    1 
ATOM   346  C  CB   . ASN   A 1 15  ? 19.008 -18.391 9.469   1.00 12.75 ?  15  ASN   A CB   1 
ATOM   347  C  CG   . ASN   A 1 15  ? 19.001 -18.484 7.961   1.00 13.12 ?  15  ASN   A CG   1 
ATOM   348  O  OD1  . ASN   A 1 15  ? 18.285 -19.303 7.380   1.00 14.34 ?  15  ASN   A OD1  1 
ATOM   349  N  ND2  . ASN   A 1 15  ? 19.795 -17.633 7.310   1.00 13.38 ?  15  ASN   A ND2  1 
ATOM   350  H  H    A ASN   A 1 15  ? 16.347 -19.044 8.988   0.58 15.40 ?  15  ASN   A H    1 
ATOM   351  H  H    B ASN   A 1 15  ? 16.488 -19.172 8.957   0.42 15.40 ?  15  ASN   A H    1 
ATOM   352  H  HA   . ASN   A 1 15  ? 17.754 -17.917 11.006  1.00 15.70 ?  15  ASN   A HA   1 
ATOM   353  H  HB2  . ASN   A 1 15  ? 19.668 -17.722 9.734   1.00 15.30 ?  15  ASN   A HB2  1 
ATOM   354  H  HB3  . ASN   A 1 15  ? 19.266 -19.257 9.824   1.00 15.30 ?  15  ASN   A HB3  1 
ATOM   355  H  HD21 . ASN   A 1 15  ? 19.829 -17.641 6.450   1.00 16.05 ?  15  ASN   A HD21 1 
ATOM   356  H  HD22 . ASN   A 1 15  ? 20.283 -17.064 7.746   1.00 16.05 ?  15  ASN   A HD22 1 
ATOM   357  N  N    A VAL   A 1 16  ? 16.164 -16.458 8.807   0.58 12.47 ?  16  VAL   A N    1 
ATOM   358  N  N    B VAL   A 1 16  ? 16.073 -16.384 8.989   0.42 12.42 ?  16  VAL   A N    1 
ATOM   359  C  CA   A VAL   A 1 16  ? 15.760 -15.201 8.191   0.58 12.09 ?  16  VAL   A CA   1 
ATOM   360  C  CA   B VAL   A 1 16  ? 15.697 -15.076 8.456   0.42 11.57 ?  16  VAL   A CA   1 
ATOM   361  C  C    A VAL   A 1 16  ? 14.475 -14.716 8.850   0.58 11.49 ?  16  VAL   A C    1 
ATOM   362  C  C    B VAL   A 1 16  ? 14.440 -14.560 9.152   0.42 11.29 ?  16  VAL   A C    1 
ATOM   363  O  O    A VAL   A 1 16  ? 13.467 -15.433 8.886   0.58 10.70 ?  16  VAL   A O    1 
ATOM   364  O  O    B VAL   A 1 16  ? 13.472 -15.304 9.349   0.42 11.22 ?  16  VAL   A O    1 
ATOM   365  C  CB   A VAL   A 1 16  ? 15.587 -15.339 6.668   0.58 12.71 ?  16  VAL   A CB   1 
ATOM   366  C  CB   B VAL   A 1 16  ? 15.524 -15.109 6.923   0.42 11.42 ?  16  VAL   A CB   1 
ATOM   367  C  CG1  A VAL   A 1 16  ? 15.128 -14.013 6.060   0.58 13.43 ?  16  VAL   A CG1  1 
ATOM   368  C  CG1  B VAL   A 1 16  ? 15.149 -13.722 6.387   0.42 11.34 ?  16  VAL   A CG1  1 
ATOM   369  C  CG2  A VAL   A 1 16  ? 16.880 -15.807 6.013   0.58 13.31 ?  16  VAL   A CG2  1 
ATOM   370  C  CG2  B VAL   A 1 16  ? 16.791 -15.630 6.253   0.42 12.26 ?  16  VAL   A CG2  1 
ATOM   371  H  H    A VAL   A 1 16  ? 15.625 -17.113 8.645   0.58 14.96 ?  16  VAL   A H    1 
ATOM   372  H  H    B VAL   A 1 16  ? 15.453 -16.980 8.927   0.42 14.91 ?  16  VAL   A H    1 
ATOM   373  H  HA   A VAL   A 1 16  ? 16.456 -14.546 8.353   0.58 14.51 ?  16  VAL   A HA   1 
ATOM   374  H  HA   B VAL   A 1 16  ? 16.407 -14.448 8.654   0.42 13.88 ?  16  VAL   A HA   1 
ATOM   375  H  HB   A VAL   A 1 16  ? 14.906 -16.007 6.490   0.58 15.25 ?  16  VAL   A HB   1 
ATOM   376  H  HB   B VAL   A 1 16  ? 14.804 -15.717 6.707   0.42 13.71 ?  16  VAL   A HB   1 
ATOM   377  H  HG11 A VAL   A 1 16  ? 15.195 -14.073 5.094   0.58 16.12 ?  16  VAL   A HG11 1 
ATOM   378  H  HG11 B VAL   A 1 16  ? 15.214 -13.735 5.419   0.42 13.61 ?  16  VAL   A HG11 1 
ATOM   379  H  HG12 A VAL   A 1 16  ? 14.208 -13.849 6.317   0.58 16.12 ?  16  VAL   A HG12 1 
ATOM   380  H  HG12 B VAL   A 1 16  ? 14.237 -13.517 6.652   0.42 13.61 ?  16  VAL   A HG12 1 
ATOM   381  H  HG13 A VAL   A 1 16  ? 15.699 -13.302 6.388   0.58 16.12 ?  16  VAL   A HG13 1 
ATOM   382  H  HG13 B VAL   A 1 16  ? 15.758 -13.065 6.753   0.42 13.61 ?  16  VAL   A HG13 1 
ATOM   383  H  HG21 A VAL   A 1 16  ? 16.764 -15.800 5.051   0.58 15.97 ?  16  VAL   A HG21 1 
ATOM   384  H  HG21 B VAL   A 1 16  ? 16.739 -15.457 5.301   0.42 14.71 ?  16  VAL   A HG21 1 
ATOM   385  H  HG22 A VAL   A 1 16  ? 17.597 -15.206 6.265   0.58 15.97 ?  16  VAL   A HG22 1 
ATOM   386  H  HG22 B VAL   A 1 16  ? 17.560 -15.178 6.632   0.42 14.71 ?  16  VAL   A HG22 1 
ATOM   387  H  HG23 A VAL   A 1 16  ? 17.081 -16.707 6.315   0.58 15.97 ?  16  VAL   A HG23 1 
ATOM   388  H  HG23 B VAL   A 1 16  ? 16.862 -16.585 6.414   0.42 14.71 ?  16  VAL   A HG23 1 
ATOM   389  N  N    A TYR   A 1 17  ? 14.519 -13.479 9.333   0.58 11.47 ?  17  TYR   A N    1 
ATOM   390  N  N    B TYR   A 1 17  ? 14.462 -13.265 9.502   0.42 11.17 ?  17  TYR   A N    1 
ATOM   391  C  CA   A TYR   A 1 17  ? 13.430 -12.802 10.013  0.58 11.32 ?  17  TYR   A CA   1 
ATOM   392  C  CA   B TYR   A 1 17  ? 13.398 -12.580 10.225  0.42 10.97 ?  17  TYR   A CA   1 
ATOM   393  C  C    A TYR   A 1 17  ? 13.164 -11.491 9.284   0.58 11.62 ?  17  TYR   A C    1 
ATOM   394  C  C    B TYR   A 1 17  ? 13.128 -11.237 9.558   0.42 11.00 ?  17  TYR   A C    1 
ATOM   395  O  O    A TYR   A 1 17  ? 14.063 -10.945 8.642   0.58 11.43 ?  17  TYR   A O    1 
ATOM   396  O  O    B TYR   A 1 17  ? 14.044 -10.627 9.004   0.42 10.95 ?  17  TYR   A O    1 
ATOM   397  C  CB   A TYR   A 1 17  ? 13.846 -12.521 11.462  0.58 12.31 ?  17  TYR   A CB   1 
ATOM   398  C  CB   B TYR   A 1 17  ? 13.822 -12.344 11.677  0.42 11.67 ?  17  TYR   A CB   1 
ATOM   399  C  CG   A TYR   A 1 17  ? 14.098 -13.781 12.272  0.58 13.82 ?  17  TYR   A CG   1 
ATOM   400  C  CG   B TYR   A 1 17  ? 13.966 -13.625 12.458  0.42 12.31 ?  17  TYR   A CG   1 
ATOM   401  C  CD1  A TYR   A 1 17  ? 15.295 -14.488 12.161  0.58 14.77 ?  17  TYR   A CD1  1 
ATOM   402  C  CD1  B TYR   A 1 17  ? 15.121 -14.399 12.372  0.42 13.12 ?  17  TYR   A CD1  1 
ATOM   403  C  CD2  A TYR   A 1 17  ? 13.131 -14.271 13.142  0.58 14.52 ?  17  TYR   A CD2  1 
ATOM   404  C  CD2  B TYR   A 1 17  ? 12.938 -14.070 13.272  0.42 12.30 ?  17  TYR   A CD2  1 
ATOM   405  C  CE1  A TYR   A 1 17  ? 15.517 -15.650 12.895  0.58 15.40 ?  17  TYR   A CE1  1 
ATOM   406  C  CE1  B TYR   A 1 17  ? 15.243 -15.588 13.084  0.42 13.28 ?  17  TYR   A CE1  1 
ATOM   407  C  CE2  A TYR   A 1 17  ? 13.345 -15.433 13.881  0.58 15.29 ?  17  TYR   A CE2  1 
ATOM   408  C  CE2  B TYR   A 1 17  ? 13.046 -15.256 13.984  0.42 12.69 ?  17  TYR   A CE2  1 
ATOM   409  C  CZ   A TYR   A 1 17  ? 14.540 -16.117 13.752  0.58 15.53 ?  17  TYR   A CZ   1 
ATOM   410  C  CZ   B TYR   A 1 17  ? 14.199 -16.011 13.891  0.42 12.97 ?  17  TYR   A CZ   1 
ATOM   411  O  OH   A TYR   A 1 17  ? 14.754 -17.264 14.487  0.58 16.15 ?  17  TYR   A OH   1 
ATOM   412  O  OH   B TYR   A 1 17  ? 14.299 -17.186 14.607  0.42 13.18 ?  17  TYR   A OH   1 
ATOM   413  H  H    A TYR   A 1 17  ? 15.221 -12.989 9.262   0.58 13.76 ?  17  TYR   A H    1 
ATOM   414  H  H    B TYR   A 1 17  ? 15.124 -12.731 9.321   0.42 13.41 ?  17  TYR   A H    1 
ATOM   415  H  HA   A TYR   A 1 17  ? 12.635 -13.361 9.999   0.58 13.58 ?  17  TYR   A HA   1 
ATOM   416  H  HA   B TYR   A 1 17  ? 12.586 -13.101 10.210  0.42 13.16 ?  17  TYR   A HA   1 
ATOM   417  H  HB2  A TYR   A 1 17  ? 14.663 -12.000 11.457  0.58 14.77 ?  17  TYR   A HB2  1 
ATOM   418  H  HB2  B TYR   A 1 17  ? 14.675 -11.887 11.688  0.42 14.01 ?  17  TYR   A HB2  1 
ATOM   419  H  HB3  A TYR   A 1 17  ? 13.138 -12.026 11.893  0.58 14.77 ?  17  TYR   A HB3  1 
ATOM   420  H  HB3  B TYR   A 1 17  ? 13.152 -11.802 12.119  0.42 14.01 ?  17  TYR   A HB3  1 
ATOM   421  H  HD1  A TYR   A 1 17  ? 15.955 -14.184 11.585  0.58 17.73 ?  17  TYR   A HD1  1 
ATOM   422  H  HD1  B TYR   A 1 17  ? 15.822 -14.117 11.825  0.42 15.74 ?  17  TYR   A HD1  1 
ATOM   423  H  HD2  A TYR   A 1 17  ? 12.323 -13.817 13.232  0.58 17.43 ?  17  TYR   A HD2  1 
ATOM   424  H  HD2  B TYR   A 1 17  ? 12.157 -13.570 13.338  0.42 14.76 ?  17  TYR   A HD2  1 
ATOM   425  H  HE1  A TYR   A 1 17  ? 16.320 -16.114 12.813  0.58 18.48 ?  17  TYR   A HE1  1 
ATOM   426  H  HE1  B TYR   A 1 17  ? 16.023 -16.095 13.016  0.42 15.93 ?  17  TYR   A HE1  1 
ATOM   427  H  HE2  A TYR   A 1 17  ? 12.684 -15.745 14.461  0.58 18.35 ?  17  TYR   A HE2  1 
ATOM   428  H  HE2  B TYR   A 1 17  ? 12.349 -15.539 14.527  0.42 15.22 ?  17  TYR   A HE2  1 
ATOM   429  H  HH   A TYR   A 1 17  ? 15.513 -17.578 14.317  0.58 19.38 ?  17  TYR   A HH   1 
ATOM   430  H  HH   B TYR   A 1 17  ? 13.550 -17.387 14.927  0.42 15.82 ?  17  TYR   A HH   1 
ATOM   431  N  N    A ILE   A 1 18  ? 11.935 -10.976 9.376   0.58 11.86 ?  18  ILE   A N    1 
ATOM   432  N  N    B ILE   A 1 18  ? 11.877 -10.759 9.623   0.42 10.61 ?  18  ILE   A N    1 
ATOM   433  C  CA   A ILE   A 1 18  ? 11.556 -9.791  8.608   0.58 11.79 ?  18  ILE   A CA   1 
ATOM   434  C  CA   B ILE   A 1 18  ? 11.484 -9.569  8.873   0.42 10.35 ?  18  ILE   A CA   1 
ATOM   435  C  C    A ILE   A 1 18  ? 10.583 -8.936  9.414   0.58 12.46 ?  18  ILE   A C    1 
ATOM   436  C  C    B ILE   A 1 18  ? 10.563 -8.681  9.703   0.42 10.45 ?  18  ILE   A C    1 
ATOM   437  O  O    A ILE   A 1 18  ? 9.760  -9.451  10.175  0.58 12.78 ?  18  ILE   A O    1 
ATOM   438  O  O    B ILE   A 1 18  ? 9.761  -9.159  10.511  0.42 11.15 ?  18  ILE   A O    1 
ATOM   439  C  CB   A ILE   A 1 18  ? 10.997 -10.199 7.222   0.58 11.41 ?  18  ILE   A CB   1 
ATOM   440  C  CB   B ILE   A 1 18  ? 10.842 -9.958  7.522   0.42 10.35 ?  18  ILE   A CB   1 
ATOM   441  C  CG1  A ILE   A 1 18  ? 10.929 -8.995  6.284   0.58 11.58 ?  18  ILE   A CG1  1 
ATOM   442  C  CG1  B ILE   A 1 18  ? 10.761 -8.758  6.575   0.42 11.86 ?  18  ILE   A CG1  1 
ATOM   443  C  CG2  A ILE   A 1 18  ? 9.651  -10.919 7.360   0.58 11.40 ?  18  ILE   A CG2  1 
ATOM   444  C  CG2  B ILE   A 1 18  ? 9.473  -10.582 7.736   0.42 10.52 ?  18  ILE   A CG2  1 
ATOM   445  C  CD1  A ILE   A 1 18  ? 10.751 -9.378  4.844   0.58 12.87 ?  18  ILE   A CD1  1 
ATOM   446  C  CD1  B ILE   A 1 18  ? 10.406 -9.155  5.159   0.42 13.36 ?  18  ILE   A CD1  1 
ATOM   447  H  H    A ILE   A 1 18  ? 11.319 -11.296 9.878   0.58 14.24 ?  18  ILE   A H    1 
ATOM   448  H  H    B ILE   A 1 18  ? 11.240 -11.107 10.095  0.42 12.73 ?  18  ILE   A H    1 
ATOM   449  H  HA   A ILE   A 1 18  ? 12.354 -9.264  8.452   0.58 14.15 ?  18  ILE   A HA   1 
ATOM   450  H  HA   B ILE   A 1 18  ? 12.279 -9.052  8.681   0.42 12.42 ?  18  ILE   A HA   1 
ATOM   451  H  HB   A ILE   A 1 18  ? 11.623 -10.835 6.831   0.58 13.69 ?  18  ILE   A HB   1 
ATOM   452  H  HB   B ILE   A 1 18  ? 11.412 -10.621 7.112   0.42 12.42 ?  18  ILE   A HB   1 
ATOM   453  H  HG12 A ILE   A 1 18  ? 10.179 -8.440  6.543   0.58 13.89 ?  18  ILE   A HG12 1 
ATOM   454  H  HG12 B ILE   A 1 18  ? 10.081 -8.146  6.892   0.42 14.23 ?  18  ILE   A HG12 1 
ATOM   455  H  HG13 A ILE   A 1 18  ? 11.756 -8.493  6.358   0.58 13.89 ?  18  ILE   A HG13 1 
ATOM   456  H  HG13 B ILE   A 1 18  ? 11.624 -8.313  6.552   0.42 14.23 ?  18  ILE   A HG13 1 
ATOM   457  H  HG21 A ILE   A 1 18  ? 9.402  -11.293 6.496   0.58 13.68 ?  18  ILE   A HG21 1 
ATOM   458  H  HG21 B ILE   A 1 18  ? 9.186  -10.997 6.907   0.42 12.62 ?  18  ILE   A HG21 1 
ATOM   459  H  HG22 A ILE   A 1 18  ? 9.737  -11.634 8.010   0.58 13.68 ?  18  ILE   A HG22 1 
ATOM   460  H  HG22 B ILE   A 1 18  ? 9.537  -11.251 8.434   0.42 12.62 ?  18  ILE   A HG22 1 
ATOM   461  H  HG23 A ILE   A 1 18  ? 8.979  -10.285 7.649   0.58 13.68 ?  18  ILE   A HG23 1 
ATOM   462  H  HG23 B ILE   A 1 18  ? 8.844  -9.891  7.995   0.42 12.62 ?  18  ILE   A HG23 1 
ATOM   463  H  HD11 A ILE   A 1 18  ? 10.745 -8.569  4.304   0.58 15.45 ?  18  ILE   A HD11 1 
ATOM   464  H  HD11 B ILE   A 1 18  ? 10.457 -8.373  4.586   0.42 16.03 ?  18  ILE   A HD11 1 
ATOM   465  H  HD12 A ILE   A 1 18  ? 11.480 -9.951  4.575   0.58 15.45 ?  18  ILE   A HD12 1 
ATOM   466  H  HD12 B ILE   A 1 18  ? 11.036 -9.827  4.851   0.42 16.03 ?  18  ILE   A HD12 1 
ATOM   467  H  HD13 A ILE   A 1 18  ? 9.904  -9.843  4.744   0.58 15.45 ?  18  ILE   A HD13 1 
ATOM   468  H  HD13 B ILE   A 1 18  ? 9.507  -9.516  5.145   0.42 16.03 ?  18  ILE   A HD13 1 
ATOM   469  N  N    A LYS   A 1 19  ? 10.671 -7.615  9.222   0.58 13.07 ?  19  LYS   A N    1 
ATOM   470  N  N    B LYS   A 1 19  ? 10.672 -7.370  9.477   0.42 10.40 ?  19  LYS   A N    1 
ATOM   471  C  CA   A LYS   A 1 19  ? 9.847  -6.656  9.952   0.58 13.59 ?  19  LYS   A CA   1 
ATOM   472  C  CA   B LYS   A 1 19  ? 9.880  -6.390  10.205  0.42 11.46 ?  19  LYS   A CA   1 
ATOM   473  C  C    A LYS   A 1 19  ? 9.663  -5.402  9.104   0.58 13.25 ?  19  LYS   A C    1 
ATOM   474  C  C    B LYS   A 1 19  ? 9.693  -5.160  9.329   0.42 11.76 ?  19  LYS   A C    1 
ATOM   475  O  O    A LYS   A 1 19  ? 10.546 -5.037  8.324   0.58 13.03 ?  19  LYS   A O    1 
ATOM   476  O  O    B LYS   A 1 19  ? 10.609 -4.772  8.601   0.42 11.75 ?  19  LYS   A O    1 
ATOM   477  C  CB   A LYS   A 1 19  ? 10.546 -6.288  11.269  0.58 14.77 ?  19  LYS   A CB   1 
ATOM   478  C  CB   B LYS   A 1 19  ? 10.603 -5.996  11.498  0.42 12.45 ?  19  LYS   A CB   1 
ATOM   479  C  CG   A LYS   A 1 19  ? 9.845  -5.281  12.184  0.58 16.27 ?  19  LYS   A CG   1 
ATOM   480  C  CG   B LYS   A 1 19  ? 9.808  -5.117  12.428  0.42 13.92 ?  19  LYS   A CG   1 
ATOM   481  C  CD   A LYS   A 1 19  ? 10.726 -5.026  13.413  0.58 17.82 ?  19  LYS   A CD   1 
ATOM   482  C  CD   B LYS   A 1 19  ? 10.652 -4.745  13.626  0.42 15.66 ?  19  LYS   A CD   1 
ATOM   483  C  CE   A LYS   A 1 19  ? 10.110 -4.072  14.426  0.58 18.77 ?  19  LYS   A CE   1 
ATOM   484  C  CE   B LYS   A 1 19  ? 9.870  -3.919  14.619  0.42 16.91 ?  19  LYS   A CE   1 
ATOM   485  N  NZ   A LYS   A 1 19  ? 11.017 -3.883  15.601  0.58 18.91 ?  19  LYS   A NZ   1 
ATOM   486  N  NZ   B LYS   A 1 19  ? 10.743 -3.497  15.739  0.42 17.47 ?  19  LYS   A NZ   1 
ATOM   487  H  H    A LYS   A 1 19  ? 11.217 -7.249  8.664   0.58 15.68 ?  19  LYS   A H    1 
ATOM   488  H  H    B LYS   A 1 19  ? 11.202 -7.013  8.892   0.42 12.47 ?  19  LYS   A H    1 
ATOM   489  H  HA   A LYS   A 1 19  ? 8.979  -7.046  10.143  0.58 16.30 ?  19  LYS   A HA   1 
ATOM   490  H  HA   B LYS   A 1 19  ? 9.012  -6.758  10.431  0.42 13.75 ?  19  LYS   A HA   1 
ATOM   491  H  HB2  A LYS   A 1 19  ? 10.661 -7.102  11.780  0.58 17.72 ?  19  LYS   A HB2  1 
ATOM   492  H  HB2  B LYS   A 1 19  ? 10.825 -6.805  11.991  0.42 14.94 ?  19  LYS   A HB2  1 
ATOM   493  H  HB3  A LYS   A 1 19  ? 11.413 -5.918  11.052  0.58 17.72 ?  19  LYS   A HB3  1 
ATOM   494  H  HB3  B LYS   A 1 19  ? 11.417 -5.521  11.271  0.42 14.94 ?  19  LYS   A HB3  1 
ATOM   495  H  HG2  A LYS   A 1 19  ? 9.715  -4.441  11.717  0.58 19.52 ?  19  LYS   A HG2  1 
ATOM   496  H  HG2  B LYS   A 1 19  ? 9.551  -4.305  11.967  0.42 16.70 ?  19  LYS   A HG2  1 
ATOM   497  H  HG3  A LYS   A 1 19  ? 8.994  -5.641  12.483  0.58 19.52 ?  19  LYS   A HG3  1 
ATOM   498  H  HG3  B LYS   A 1 19  ? 9.024  -5.598  12.739  0.42 16.70 ?  19  LYS   A HG3  1 
ATOM   499  H  HD2  A LYS   A 1 19  ? 10.887 -5.869  13.866  0.58 21.38 ?  19  LYS   A HD2  1 
ATOM   500  H  HD2  B LYS   A 1 19  ? 10.950 -5.558  14.068  0.42 18.79 ?  19  LYS   A HD2  1 
ATOM   501  H  HD3  A LYS   A 1 19  ? 11.568 -4.643  13.124  0.58 21.38 ?  19  LYS   A HD3  1 
ATOM   502  H  HD3  B LYS   A 1 19  ? 11.416 -4.228  13.327  0.42 18.79 ?  19  LYS   A HD3  1 
ATOM   503  H  HE2  A LYS   A 1 19  ? 9.966  -3.205  14.013  0.58 22.52 ?  19  LYS   A HE2  1 
ATOM   504  H  HE2  B LYS   A 1 19  ? 9.527  -3.128  14.177  0.42 20.30 ?  19  LYS   A HE2  1 
ATOM   505  H  HE3  A LYS   A 1 19  ? 9.269  -4.434  14.748  0.58 22.52 ?  19  LYS   A HE3  1 
ATOM   506  H  HE3  B LYS   A 1 19  ? 9.142  -4.452  14.976  0.42 20.30 ?  19  LYS   A HE3  1 
ATOM   507  H  HZ1  A LYS   A 1 19  ? 10.660 -3.302  16.174  0.58 22.70 ?  19  LYS   A HZ1  1 
ATOM   508  H  HZ1  B LYS   A 1 19  ? 10.277 -3.013  16.319  0.42 20.97 ?  19  LYS   A HZ1  1 
ATOM   509  H  HZ2  A LYS   A 1 19  ? 11.139 -4.660  16.019  0.58 22.70 ?  19  LYS   A HZ2  1 
ATOM   510  H  HZ2  B LYS   A 1 19  ? 11.070 -4.214  16.154  0.42 20.97 ?  19  LYS   A HZ2  1 
ATOM   511  H  HZ3  A LYS   A 1 19  ? 11.805 -3.574  15.331  0.58 22.70 ?  19  LYS   A HZ3  1 
ATOM   512  H  HZ3  B LYS   A 1 19  ? 11.419 -3.010  15.428  0.42 20.97 ?  19  LYS   A HZ3  1 
ATOM   513  N  N    A ASN   A 1 20  ? 8.513  -4.739  9.263   0.58 14.51 ?  20  ASN   A N    1 
ATOM   514  N  N    B ASN   A 1 20  ? 8.508  -4.552  9.394   0.42 12.58 ?  20  ASN   A N    1 
ATOM   515  C  CA   A ASN   A 1 20  ? 8.308  -3.412  8.679   0.58 15.71 ?  20  ASN   A CA   1 
ATOM   516  C  CA   B ASN   A 1 20  ? 8.270  -3.260  8.745   0.42 13.65 ?  20  ASN   A CA   1 
ATOM   517  C  C    A ASN   A 1 20  ? 8.937  -2.401  9.630   0.58 15.55 ?  20  ASN   A C    1 
ATOM   518  C  C    B ASN   A 1 20  ? 8.854  -2.170  9.629   0.42 14.09 ?  20  ASN   A C    1 
ATOM   519  O  O    A ASN   A 1 20  ? 8.446  -2.197  10.746  0.58 15.73 ?  20  ASN   A O    1 
ATOM   520  O  O    B ASN   A 1 20  ? 8.210  -1.708  10.576  0.42 15.24 ?  20  ASN   A O    1 
ATOM   521  C  CB   A ASN   A 1 20  ? 6.818  -3.146  8.456   0.58 17.07 ?  20  ASN   A CB   1 
ATOM   522  C  CB   B ASN   A 1 20  ? 6.780  -3.034  8.513   0.42 14.60 ?  20  ASN   A CB   1 
ATOM   523  C  CG   A ASN   A 1 20  ? 6.519  -1.713  8.012   0.58 18.74 ?  20  ASN   A CG   1 
ATOM   524  C  CG   B ASN   A 1 20  ? 6.458  -1.620  8.041   0.42 16.10 ?  20  ASN   A CG   1 
ATOM   525  O  OD1  A ASN   A 1 20  ? 5.516  -1.139  8.426   0.58 21.08 ?  20  ASN   A OD1  1 
ATOM   526  O  OD1  B ASN   A 1 20  ? 5.440  -1.045  8.429   0.42 18.76 ?  20  ASN   A OD1  1 
ATOM   527  N  ND2  A ASN   A 1 20  ? 7.372  -1.143  7.167   0.58 19.23 ?  20  ASN   A ND2  1 
ATOM   528  N  ND2  B ASN   A 1 20  ? 7.321  -1.057  7.201   0.42 15.93 ?  20  ASN   A ND2  1 
ATOM   529  H  H    A ASN   A 1 20  ? 7.839  -5.031  9.715   0.58 17.41 ?  20  ASN   A H    1 
ATOM   530  H  H    B ASN   A 1 20  ? 7.825  -4.885  9.796   0.42 15.10 ?  20  ASN   A H    1 
ATOM   531  H  HA   A ASN   A 1 20  ? 8.757  -3.364  7.824   0.58 18.85 ?  20  ASN   A HA   1 
ATOM   532  H  HA   B ASN   A 1 20  ? 8.732  -3.246  7.894   0.42 16.38 ?  20  ASN   A HA   1 
ATOM   533  H  HB2  A ASN   A 1 20  ? 6.487  -3.743  7.764   0.58 20.48 ?  20  ASN   A HB2  1 
ATOM   534  H  HB2  B ASN   A 1 20  ? 6.475  -3.651  7.836   0.42 17.52 ?  20  ASN   A HB2  1 
ATOM   535  H  HB3  A ASN   A 1 20  ? 6.337  -3.306  9.282   0.58 20.48 ?  20  ASN   A HB3  1 
ATOM   536  H  HB3  B ASN   A 1 20  ? 6.310  -3.195  9.347   0.42 17.52 ?  20  ASN   A HB3  1 
ATOM   537  H  HD21 A ASN   A 1 20  ? 7.235  -0.339  6.894   0.58 23.08 ?  20  ASN   A HD21 1 
ATOM   538  H  HD21 B ASN   A 1 20  ? 7.183  -0.263  6.917   0.42 19.11 ?  20  ASN   A HD21 1 
ATOM   539  H  HD22 A ASN   A 1 20  ? 8.061  -1.579  6.893   0.58 23.08 ?  20  ASN   A HD22 1 
ATOM   540  H  HD22 B ASN   A 1 20  ? 8.022  -1.492  6.942   0.42 19.11 ?  20  ASN   A HD22 1 
ATOM   541  N  N    A ALA   A 1 21  ? 10.051 -1.802  9.216   0.58 15.66 ?  21  ALA   A N    1 
ATOM   542  N  N    B ALA   A 1 21  ? 10.079 -1.754  9.315   0.42 14.56 ?  21  ALA   A N    1 
ATOM   543  C  CA   A ALA   A 1 21  ? 10.761 -0.908  10.114  0.58 15.61 ?  21  ALA   A CA   1 
ATOM   544  C  CA   B ALA   A 1 21  ? 10.748 -0.730  10.099  0.42 14.78 ?  21  ALA   A CA   1 
ATOM   545  C  C    A ALA   A 1 21  ? 11.709 -0.022  9.327   0.58 14.97 ?  21  ALA   A C    1 
ATOM   546  C  C    B ALA   A 1 21  ? 11.815 -0.071  9.245   0.42 13.71 ?  21  ALA   A C    1 
ATOM   547  O  O    A ALA   A 1 21  ? 12.162 -0.381  8.236   0.58 15.04 ?  21  ALA   A O    1 
ATOM   548  O  O    B ALA   A 1 21  ? 12.340 -0.674  8.307   0.42 13.68 ?  21  ALA   A O    1 
ATOM   549  C  CB   A ALA   A 1 21  ? 11.539 -1.691  11.174  0.58 16.07 ?  21  ALA   A CB   1 
ATOM   550  C  CB   B ALA   A 1 21  ? 11.384 -1.311  11.366  0.42 15.78 ?  21  ALA   A CB   1 
ATOM   551  H  H    A ALA   A 1 21  ? 10.405 -1.901  8.440   0.58 18.79 ?  21  ALA   A H    1 
ATOM   552  H  H    B ALA   A 1 21  ? 10.541 -2.046  8.648   0.42 17.47 ?  21  ALA   A H    1 
ATOM   553  H  HA   A ALA   A 1 21  ? 10.117 -0.338  10.565  0.58 18.73 ?  21  ALA   A HA   1 
ATOM   554  H  HA   B ALA   A 1 21  ? 10.102 -0.058  10.361  0.42 17.73 ?  21  ALA   A HA   1 
ATOM   555  H  HB1  A ALA   A 1 21  ? 11.967 -1.061  11.770  0.58 19.28 ?  21  ALA   A HB1  1 
ATOM   556  H  HB1  B ALA   A 1 21  ? 11.810 -0.594  11.861  0.42 18.93 ?  21  ALA   A HB1  1 
ATOM   557  H  HB2  A ALA   A 1 21  ? 10.916 -2.247  11.671  0.58 19.28 ?  21  ALA   A HB2  1 
ATOM   558  H  HB2  B ALA   A 1 21  ? 10.691 -1.720  11.908  0.42 18.93 ?  21  ALA   A HB2  1 
ATOM   559  H  HB3  A ALA   A 1 21  ? 12.199 -2.244  10.734  0.58 19.28 ?  21  ALA   A HB3  1 
ATOM   560  H  HB3  B ALA   A 1 21  ? 12.043 -1.976  11.113  0.42 18.93 ?  21  ALA   A HB3  1 
ATOM   561  N  N    A ASP   A 1 22  ? 11.985 1.146   9.901   0.58 15.33 ?  22  ASP   A N    1 
ATOM   562  N  N    B ASP   A 1 22  ? 12.101 1.183   9.573   0.42 13.35 ?  22  ASP   A N    1 
ATOM   563  C  CA   A ASP   A 1 22  ? 13.032 2.038   9.424   0.58 15.68 ?  22  ASP   A CA   1 
ATOM   564  C  CA   B ASP   A 1 22  ? 13.261 1.880   9.037   0.42 13.01 ?  22  ASP   A CA   1 
ATOM   565  C  C    A ASP   A 1 22  ? 14.359 1.564   10.003  0.58 14.47 ?  22  ASP   A C    1 
ATOM   566  C  C    B ASP   A 1 22  ? 14.516 1.278   9.668   0.42 11.98 ?  22  ASP   A C    1 
ATOM   567  O  O    A ASP   A 1 22  ? 14.545 1.571   11.225  0.58 14.85 ?  22  ASP   A O    1 
ATOM   568  O  O    B ASP   A 1 22  ? 14.628 1.220   10.897  0.42 12.09 ?  22  ASP   A O    1 
ATOM   569  C  CB   A ASP   A 1 22  ? 12.714 3.457   9.894   0.58 17.67 ?  22  ASP   A CB   1 
ATOM   570  C  CB   B ASP   A 1 22  ? 13.128 3.358   9.409   0.42 14.00 ?  22  ASP   A CB   1 
ATOM   571  C  CG   A ASP   A 1 22  ? 13.757 4.481   9.459   0.58 19.60 ?  22  ASP   A CG   1 
ATOM   572  C  CG   B ASP   A 1 22  ? 14.177 4.241   8.761   0.42 14.19 ?  22  ASP   A CG   1 
ATOM   573  O  OD1  A ASP   A 1 22  ? 14.828 4.096   8.945   0.58 20.20 ?  22  ASP   A OD1  1 
ATOM   574  O  OD1  B ASP   A 1 22  ? 15.223 3.717   8.319   0.42 13.17 ?  22  ASP   A OD1  1 
ATOM   575  O  OD2  A ASP   A 1 22  ? 13.497 5.690   9.635   0.58 21.00 -1 22  ASP   A OD2  1 
ATOM   576  O  OD2  B ASP   A 1 22  ? 13.960 5.473   8.719   0.42 15.92 -1 22  ASP   A OD2  1 
ATOM   577  H  H    A ASP   A 1 22  ? 11.551 1.456   10.577  0.58 18.40 ?  22  ASP   A H    1 
ATOM   578  H  H    B ASP   A 1 22  ? 11.619 1.661   10.101  0.42 16.02 ?  22  ASP   A H    1 
ATOM   579  H  HA   A ASP   A 1 22  ? 13.076 2.022   8.454   0.58 18.81 ?  22  ASP   A HA   1 
ATOM   580  H  HA   B ASP   A 1 22  ? 13.298 1.787   8.067   0.42 15.62 ?  22  ASP   A HA   1 
ATOM   581  H  HB2  A ASP   A 1 22  ? 11.861 3.729   9.523   0.58 21.20 ?  22  ASP   A HB2  1 
ATOM   582  H  HB2  B ASP   A 1 22  ? 12.251 3.673   9.137   0.42 16.81 ?  22  ASP   A HB2  1 
ATOM   583  H  HB3  A ASP   A 1 22  ? 12.666 3.460   10.865  0.58 21.20 ?  22  ASP   A HB3  1 
ATOM   584  H  HB3  B ASP   A 1 22  ? 13.229 3.446   10.368  0.42 16.81 ?  22  ASP   A HB3  1 
ATOM   585  N  N    A ILE   A 1 23  ? 15.277 1.142   9.129   0.58 13.87 ?  23  ILE   A N    1 
ATOM   586  N  N    B ILE   A 1 23  ? 15.452 0.810   8.834   0.42 11.69 ?  23  ILE   A N    1 
ATOM   587  C  CA   A ILE   A 1 23  ? 16.527 0.535   9.586   0.58 13.33 ?  23  ILE   A CA   1 
ATOM   588  C  CA   B ILE   A 1 23  ? 16.674 0.194   9.356   0.42 11.19 ?  23  ILE   A CA   1 
ATOM   589  C  C    A ILE   A 1 23  ? 17.322 1.496   10.459  0.58 13.27 ?  23  ILE   A C    1 
ATOM   590  C  C    B ILE   A 1 23  ? 17.414 1.153   10.279  0.42 11.79 ?  23  ILE   A C    1 
ATOM   591  O  O    A ILE   A 1 23  ? 18.049 1.068   11.364  0.58 13.53 ?  23  ILE   A O    1 
ATOM   592  O  O    B ILE   A 1 23  ? 18.070 0.724   11.238  0.42 11.87 ?  23  ILE   A O    1 
ATOM   593  C  CB   A ILE   A 1 23  ? 17.344 0.016   8.384   0.58 13.12 ?  23  ILE   A CB   1 
ATOM   594  C  CB   B ILE   A 1 23  ? 17.580 -0.333  8.217   0.42 10.84 ?  23  ILE   A CB   1 
ATOM   595  C  CG1  A ILE   A 1 23  ? 18.483 -0.886  8.860   0.58 12.96 ?  23  ILE   A CG1  1 
ATOM   596  C  CG1  B ILE   A 1 23  ? 18.646 -1.279  8.788   0.42 10.76 ?  23  ILE   A CG1  1 
ATOM   597  C  CG2  A ILE   A 1 23  ? 17.859 1.178   7.535   0.58 13.32 ?  23  ILE   A CG2  1 
ATOM   598  C  CG2  B ILE   A 1 23  ? 18.238 0.817   7.450   0.42 10.54 ?  23  ILE   A CG2  1 
ATOM   599  C  CD1  A ILE   A 1 23  ? 19.184 -1.613  7.737   0.58 13.04 ?  23  ILE   A CD1  1 
ATOM   600  C  CD1  B ILE   A 1 23  ? 19.542 -1.931  7.738   0.42 10.80 ?  23  ILE   A CD1  1 
ATOM   601  H  H    A ILE   A 1 23  ? 15.195 1.194   8.277   0.58 16.64 ?  23  ILE   A H    1 
ATOM   602  H  H    B ILE   A 1 23  ? 15.402 0.834   7.983   0.42 14.03 ?  23  ILE   A H    1 
ATOM   603  H  HA   A ILE   A 1 23  ? 16.309 -0.232  10.133  0.58 16.00 ?  23  ILE   A HA   1 
ATOM   604  H  HA   B ILE   A 1 23  ? 16.417 -0.574  9.884   0.42 13.43 ?  23  ILE   A HA   1 
ATOM   605  H  HB   A ILE   A 1 23  ? 16.753 -0.516  7.830   0.58 15.74 ?  23  ILE   A HB   1 
ATOM   606  H  HB   B ILE   A 1 23  ? 17.033 -0.838  7.596   0.42 13.01 ?  23  ILE   A HB   1 
ATOM   607  H  HG12 A ILE   A 1 23  ? 19.143 -0.345  9.320   0.58 15.55 ?  23  ILE   A HG12 1 
ATOM   608  H  HG12 B ILE   A 1 23  ? 19.219 -0.781  9.390   0.42 12.91 ?  23  ILE   A HG12 1 
ATOM   609  H  HG13 A ILE   A 1 23  ? 18.122 -1.553  9.465   0.58 15.55 ?  23  ILE   A HG13 1 
ATOM   610  H  HG13 B ILE   A 1 23  ? 18.202 -1.992  9.275   0.42 12.91 ?  23  ILE   A HG13 1 
ATOM   611  H  HG21 A ILE   A 1 23  ? 18.214 0.830   6.702   0.58 15.98 ?  23  ILE   A HG21 1 
ATOM   612  H  HG21 B ILE   A 1 23  ? 18.632 0.466   6.632   0.42 12.65 ?  23  ILE   A HG21 1 
ATOM   613  H  HG22 A ILE   A 1 23  ? 17.121 1.784   7.348   0.58 15.98 ?  23  ILE   A HG22 1 
ATOM   614  H  HG22 B ILE   A 1 23  ? 17.565 1.476   7.234   0.42 12.65 ?  23  ILE   A HG22 1 
ATOM   615  H  HG23 A ILE   A 1 23  ? 18.553 1.647   8.021   0.58 15.98 ?  23  ILE   A HG23 1 
ATOM   616  H  HG23 B ILE   A 1 23  ? 18.930 1.212   8.002   0.42 12.65 ?  23  ILE   A HG23 1 
ATOM   617  H  HD11 A ILE   A 1 23  ? 19.846 -2.212  8.115   0.58 15.64 ?  23  ILE   A HD11 1 
ATOM   618  H  HD11 B ILE   A 1 23  ? 20.123 -2.577  8.175   0.42 12.96 ?  23  ILE   A HD11 1 
ATOM   619  H  HD12 A ILE   A 1 23  ? 18.528 -2.120  7.232   0.58 15.64 ?  23  ILE   A HD12 1 
ATOM   620  H  HD12 B ILE   A 1 23  ? 18.985 -2.382  7.083   0.42 12.96 ?  23  ILE   A HD12 1 
ATOM   621  H  HD13 A ILE   A 1 23  ? 19.615 -0.963  7.161   0.58 15.64 ?  23  ILE   A HD13 1 
ATOM   622  H  HD13 B ILE   A 1 23  ? 20.076 -1.248  7.306   0.42 12.96 ?  23  ILE   A HD13 1 
ATOM   623  N  N    A VAL   A 1 24  ? 17.196 2.802   10.213  0.58 13.70 ?  24  VAL   A N    1 
ATOM   624  N  N    B VAL   A 1 24  ? 17.321 2.457   10.012  0.42 12.59 ?  24  VAL   A N    1 
ATOM   625  C  CA   A VAL   A 1 24  ? 17.875 3.784   11.054  0.58 14.65 ?  24  VAL   A CA   1 
ATOM   626  C  CA   B VAL   A 1 24  ? 17.976 3.447   10.862  0.42 13.53 ?  24  VAL   A CA   1 
ATOM   627  C  C    A VAL   A 1 24  ? 17.363 3.699   12.484  0.58 15.18 ?  24  VAL   A C    1 
ATOM   628  C  C    B VAL   A 1 24  ? 17.365 3.442   12.257  0.42 14.22 ?  24  VAL   A C    1 
ATOM   629  O  O    A VAL   A 1 24  ? 18.141 3.618   13.443  0.58 15.57 ?  24  VAL   A O    1 
ATOM   630  O  O    B VAL   A 1 24  ? 18.080 3.493   13.266  0.42 15.22 ?  24  VAL   A O    1 
ATOM   631  C  CB   A VAL   A 1 24  ? 17.698 5.198   10.475  0.58 15.68 ?  24  VAL   A CB   1 
ATOM   632  C  CB   B VAL   A 1 24  ? 17.898 4.837   10.204  0.42 14.45 ?  24  VAL   A CB   1 
ATOM   633  C  CG1  A VAL   A 1 24  ? 18.197 6.245   11.465  0.58 16.52 ?  24  VAL   A CG1  1 
ATOM   634  C  CG1  B VAL   A 1 24  ? 18.534 5.884   11.098  0.42 15.90 ?  24  VAL   A CG1  1 
ATOM   635  C  CG2  A VAL   A 1 24  ? 18.415 5.319   9.139   0.58 16.09 ?  24  VAL   A CG2  1 
ATOM   636  C  CG2  B VAL   A 1 24  ? 18.557 4.809   8.830   0.42 14.38 ?  24  VAL   A CG2  1 
ATOM   637  H  H    A VAL   A 1 24  ? 16.726 3.139   9.575   0.58 16.44 ?  24  VAL   A H    1 
ATOM   638  H  H    B VAL   A 1 24  ? 16.883 2.790   9.352   0.42 15.10 ?  24  VAL   A H    1 
ATOM   639  H  HA   A VAL   A 1 24  ? 18.822 3.585   11.064  0.58 17.58 ?  24  VAL   A HA   1 
ATOM   640  H  HA   B VAL   A 1 24  ? 18.912 3.214   10.947  0.42 16.24 ?  24  VAL   A HA   1 
ATOM   641  H  HB   A VAL   A 1 24  ? 16.753 5.361   10.319  0.58 18.82 ?  24  VAL   A HB   1 
ATOM   642  H  HB   B VAL   A 1 24  ? 16.965 5.074   10.079  0.42 17.35 ?  24  VAL   A HB   1 
ATOM   643  H  HG11 A VAL   A 1 24  ? 18.342 7.078   10.992  0.58 19.82 ?  24  VAL   A HG11 1 
ATOM   644  H  HG11 B VAL   A 1 24  ? 18.669 6.694   10.583  0.42 19.07 ?  24  VAL   A HG11 1 
ATOM   645  H  HG12 A VAL   A 1 24  ? 17.529 6.369   12.157  0.58 19.82 ?  24  VAL   A HG12 1 
ATOM   646  H  HG12 B VAL   A 1 24  ? 17.941 6.063   11.845  0.42 19.07 ?  24  VAL   A HG12 1 
ATOM   647  H  HG13 A VAL   A 1 24  ? 19.029 5.935   11.854  0.58 19.82 ?  24  VAL   A HG13 1 
ATOM   648  H  HG13 B VAL   A 1 24  ? 19.384 5.549   11.418  0.42 19.07 ?  24  VAL   A HG13 1 
ATOM   649  H  HG21 A VAL   A 1 24  ? 18.167 6.159   8.724   0.58 19.31 ?  24  VAL   A HG21 1 
ATOM   650  H  HG21 B VAL   A 1 24  ? 18.576 5.709   8.471   0.42 17.26 ?  24  VAL   A HG21 1 
ATOM   651  H  HG22 A VAL   A 1 24  ? 19.372 5.297   9.292   0.58 19.31 ?  24  VAL   A HG22 1 
ATOM   652  H  HG22 B VAL   A 1 24  ? 19.462 4.471   8.923   0.42 17.26 ?  24  VAL   A HG22 1 
ATOM   653  H  HG23 A VAL   A 1 24  ? 18.152 4.579   8.568   0.58 19.31 ?  24  VAL   A HG23 1 
ATOM   654  H  HG23 B VAL   A 1 24  ? 18.047 4.228   8.244   0.42 17.26 ?  24  VAL   A HG23 1 
ATOM   655  N  N    A GLU   A 1 25  ? 16.038 3.731   12.646  0.58 15.61 ?  25  GLU   A N    1 
ATOM   656  N  N    B GLU   A 1 25  ? 16.033 3.376   12.338  0.42 14.44 ?  25  GLU   A N    1 
ATOM   657  C  CA   A GLU   A 1 25  ? 15.457 3.676   13.981  0.58 16.80 ?  25  GLU   A CA   1 
ATOM   658  C  CA   B GLU   A 1 25  ? 15.372 3.336   13.639  0.42 15.31 ?  25  GLU   A CA   1 
ATOM   659  C  C    A GLU   A 1 25  ? 15.686 2.319   14.630  0.58 15.48 ?  25  GLU   A C    1 
ATOM   660  C  C    B GLU   A 1 25  ? 15.632 2.012   14.351  0.42 15.01 ?  25  GLU   A C    1 
ATOM   661  O  O    A GLU   A 1 25  ? 15.898 2.238   15.846  0.58 15.87 ?  25  GLU   A O    1 
ATOM   662  O  O    B GLU   A 1 25  ? 15.836 1.989   15.570  0.42 15.56 ?  25  GLU   A O    1 
ATOM   663  C  CB   A GLU   A 1 25  ? 13.967 4.020   13.917  0.58 19.55 ?  25  GLU   A CB   1 
ATOM   664  C  CB   B GLU   A 1 25  ? 13.873 3.603   13.479  0.42 16.95 ?  25  GLU   A CB   1 
ATOM   665  C  CG   A GLU   A 1 25  ? 13.706 5.486   13.600  0.58 22.40 ?  25  GLU   A CG   1 
ATOM   666  C  CG   B GLU   A 1 25  ? 13.556 4.985   12.922  0.42 19.52 ?  25  GLU   A CG   1 
ATOM   667  C  CD   A GLU   A 1 25  ? 14.521 6.441   14.464  0.58 24.74 ?  25  GLU   A CD   1 
ATOM   668  C  CD   B GLU   A 1 25  ? 14.053 6.100   13.818  0.42 21.85 ?  25  GLU   A CD   1 
ATOM   669  O  OE1  A GLU   A 1 25  ? 14.618 6.211   15.689  0.58 25.26 ?  25  GLU   A OE1  1 
ATOM   670  O  OE1  B GLU   A 1 25  ? 14.030 5.921   15.055  0.42 22.90 ?  25  GLU   A OE1  1 
ATOM   671  O  OE2  A GLU   A 1 25  ? 15.082 7.410   13.912  0.58 26.04 -1 25  GLU   A OE2  1 
ATOM   672  O  OE2  B GLU   A 1 25  ? 14.468 7.152   13.288  0.42 22.76 -1 25  GLU   A OE2  1 
ATOM   673  H  H    A GLU   A 1 25  ? 15.464 3.798   12.006  0.58 18.74 ?  25  GLU   A H    1 
ATOM   674  H  H    B GLU   A 1 25  ? 15.501 3.355   11.663  0.42 17.33 ?  25  GLU   A H    1 
ATOM   675  H  HA   A GLU   A 1 25  ? 15.898 4.331   14.540  0.58 20.16 ?  25  GLU   A HA   1 
ATOM   676  H  HA   B GLU   A 1 25  ? 15.740 4.039   14.193  0.42 18.37 ?  25  GLU   A HA   1 
ATOM   677  H  HB2  A GLU   A 1 25  ? 13.545 3.486   13.220  0.58 23.46 ?  25  GLU   A HB2  1 
ATOM   678  H  HB2  B GLU   A 1 25  ? 13.499 2.948   12.871  0.42 20.34 ?  25  GLU   A HB2  1 
ATOM   679  H  HB3  A GLU   A 1 25  ? 13.555 3.822   14.773  0.58 23.46 ?  25  GLU   A HB3  1 
ATOM   680  H  HB3  B GLU   A 1 25  ? 13.447 3.530   14.347  0.42 20.34 ?  25  GLU   A HB3  1 
ATOM   681  H  HG2  A GLU   A 1 25  ? 13.950 5.654   12.679  0.58 26.88 ?  25  GLU   A HG2  1 
ATOM   682  H  HG2  B GLU   A 1 25  ? 13.977 5.083   12.052  0.42 23.43 ?  25  GLU   A HG2  1 
ATOM   683  H  HG3  A GLU   A 1 25  ? 12.764 5.673   13.739  0.58 26.88 ?  25  GLU   A HG3  1 
ATOM   684  H  HG3  B GLU   A 1 25  ? 12.596 5.085   12.839  0.42 23.43 ?  25  GLU   A HG3  1 
ATOM   685  N  N    A GLU   A 1 26  ? 15.659 1.245   13.839  0.58 15.02 ?  26  GLU   A N    1 
ATOM   686  N  N    B GLU   A 1 26  ? 15.632 0.900   13.612  0.42 14.76 ?  26  GLU   A N    1 
ATOM   687  C  CA   A GLU   A 1 26  ? 15.941 -0.078  14.385  0.58 14.87 ?  26  GLU   A CA   1 
ATOM   688  C  CA   B GLU   A 1 26  ? 16.011 -0.378  14.211  0.42 15.32 ?  26  GLU   A CA   1 
ATOM   689  C  C    A GLU   A 1 26  ? 17.359 -0.150  14.937  0.58 14.09 ?  26  GLU   A C    1 
ATOM   690  C  C    B GLU   A 1 26  ? 17.435 -0.331  14.745  0.42 14.68 ?  26  GLU   A C    1 
ATOM   691  O  O    A GLU   A 1 26  ? 17.576 -0.600  16.067  0.58 14.36 ?  26  GLU   A O    1 
ATOM   692  O  O    B GLU   A 1 26  ? 17.732 -0.906  15.798  0.42 14.88 ?  26  GLU   A O    1 
ATOM   693  C  CB   A GLU   A 1 26  ? 15.742 -1.145  13.308  0.58 15.72 ?  26  GLU   A CB   1 
ATOM   694  C  CB   B GLU   A 1 26  ? 15.874 -1.505  13.187  0.42 16.38 ?  26  GLU   A CB   1 
ATOM   695  C  CG   A GLU   A 1 26  ? 14.328 -1.659  13.169  0.58 19.10 ?  26  GLU   A CG   1 
ATOM   696  C  CG   B GLU   A 1 26  ? 14.452 -1.950  12.938  0.42 17.72 ?  26  GLU   A CG   1 
ATOM   697  C  CD   A GLU   A 1 26  ? 13.895 -2.507  14.354  0.58 21.16 ?  26  GLU   A CD   1 
ATOM   698  C  CD   B GLU   A 1 26  ? 13.776 -2.462  14.184  0.42 18.12 ?  26  GLU   A CD   1 
ATOM   699  O  OE1  A GLU   A 1 26  ? 14.313 -3.683  14.464  0.58 21.01 ?  26  GLU   A OE1  1 
ATOM   700  O  OE1  B GLU   A 1 26  ? 14.359 -3.332  14.864  0.42 18.40 ?  26  GLU   A OE1  1 
ATOM   701  O  OE2  A GLU   A 1 26  ? 13.143 -1.981  15.188  0.58 22.23 -1 26  GLU   A OE2  1 
ATOM   702  O  OE2  B GLU   A 1 26  ? 12.671 -1.971  14.487  0.42 16.90 -1 26  GLU   A OE2  1 
ATOM   703  H  H    A GLU   A 1 26  ? 15.491 1.262   12.995  0.58 18.03 ?  26  GLU   A H    1 
ATOM   704  H  H    B GLU   A 1 26  ? 15.420 0.856   12.781  0.42 17.71 ?  26  GLU   A H    1 
ATOM   705  H  HA   A GLU   A 1 26  ? 15.323 -0.255  15.108  0.58 17.84 ?  26  GLU   A HA   1 
ATOM   706  H  HA   B GLU   A 1 26  ? 15.420 -0.568  14.955  0.42 18.38 ?  26  GLU   A HA   1 
ATOM   707  H  HB2  A GLU   A 1 26  ? 16.004 -0.770  12.451  0.58 18.87 ?  26  GLU   A HB2  1 
ATOM   708  H  HB2  B GLU   A 1 26  ? 16.238 -1.203  12.338  0.42 19.66 ?  26  GLU   A HB2  1 
ATOM   709  H  HB3  A GLU   A 1 26  ? 16.310 -1.900  13.519  0.58 18.87 ?  26  GLU   A HB3  1 
ATOM   710  H  HB3  B GLU   A 1 26  ? 16.377 -2.276  13.499  0.42 19.66 ?  26  GLU   A HB3  1 
ATOM   711  H  HG2  A GLU   A 1 26  ? 13.729 -0.899  13.091  0.58 22.92 ?  26  GLU   A HG2  1 
ATOM   712  H  HG2  B GLU   A 1 26  ? 13.936 -1.198  12.619  0.42 21.26 ?  26  GLU   A HG2  1 
ATOM   713  H  HG3  A GLU   A 1 26  ? 14.269 -2.207  12.371  0.58 22.92 ?  26  GLU   A HG3  1 
ATOM   714  H  HG3  B GLU   A 1 26  ? 14.450 -2.665  12.286  0.42 21.26 ?  26  GLU   A HG3  1 
ATOM   715  N  N    A ALA   A 1 27  ? 18.342 0.284   14.145  0.58 13.95 ?  27  ALA   A N    1 
ATOM   716  N  N    B ALA   A 1 27  ? 18.335 0.335   14.023  0.42 13.98 ?  27  ALA   A N    1 
ATOM   717  C  CA   A ALA   A 1 27  ? 19.731 0.216   14.587  0.58 14.42 ?  27  ALA   A CA   1 
ATOM   718  C  CA   B ALA   A 1 27  ? 19.715 0.435   14.486  0.42 13.61 ?  27  ALA   A CA   1 
ATOM   719  C  C    A ALA   A 1 27  ? 19.946 1.025   15.862  0.58 15.56 ?  27  ALA   A C    1 
ATOM   720  C  C    B ALA   A 1 27  ? 19.803 1.281   15.751  0.42 13.84 ?  27  ALA   A C    1 
ATOM   721  O  O    A ALA   A 1 27  ? 20.644 0.577   16.781  0.58 15.98 ?  27  ALA   A O    1 
ATOM   722  O  O    B ALA   A 1 27  ? 20.433 0.882   16.738  0.42 13.74 ?  27  ALA   A O    1 
ATOM   723  C  CB   A ALA   A 1 27  ? 20.663 0.703   13.475  0.58 14.11 ?  27  ALA   A CB   1 
ATOM   724  C  CB   B ALA   A 1 27  ? 20.594 1.016   13.379  0.42 13.05 ?  27  ALA   A CB   1 
ATOM   725  H  H    A ALA   A 1 27  ? 18.231 0.615   13.358  0.58 16.74 ?  27  ALA   A H    1 
ATOM   726  H  H    B ALA   A 1 27  ? 18.172 0.728   13.276  0.42 16.77 ?  27  ALA   A H    1 
ATOM   727  H  HA   A ALA   A 1 27  ? 19.953 -0.707  14.776  0.58 17.30 ?  27  ALA   A HA   1 
ATOM   728  H  HA   B ALA   A 1 27  ? 20.041 -0.451  14.693  0.42 16.33 ?  27  ALA   A HA   1 
ATOM   729  H  HB1  A ALA   A 1 27  ? 21.582 0.649   13.786  0.58 16.93 ?  27  ALA   A HB1  1 
ATOM   730  H  HB1  B ALA   A 1 27  ? 21.508 1.061   13.694  0.42 15.66 ?  27  ALA   A HB1  1 
ATOM   731  H  HB2  A ALA   A 1 27  ? 20.548 0.136   12.694  0.58 16.93 ?  27  ALA   A HB2  1 
ATOM   732  H  HB2  B ALA   A 1 27  ? 20.540 0.442   12.598  0.42 15.66 ?  27  ALA   A HB2  1 
ATOM   733  H  HB3  A ALA   A 1 27  ? 20.443 1.620   13.252  0.58 16.93 ?  27  ALA   A HB3  1 
ATOM   734  H  HB3  B ALA   A 1 27  ? 20.276 1.906   13.154  0.42 15.66 ?  27  ALA   A HB3  1 
ATOM   735  N  N    A LYS   A 1 28  ? 19.352 2.217   15.943  0.58 16.92 ?  28  LYS   A N    1 
ATOM   736  N  N    B LYS   A 1 28  ? 19.159 2.450   15.747  0.42 14.87 ?  28  LYS   A N    1 
ATOM   737  C  CA   A LYS   A 1 28  ? 19.514 3.033   17.143  0.58 19.44 ?  28  LYS   A CA   1 
ATOM   738  C  CA   B LYS   A 1 28  ? 19.234 3.335   16.904  0.42 16.55 ?  28  LYS   A CA   1 
ATOM   739  C  C    A LYS   A 1 28  ? 18.976 2.320   18.378  0.58 20.21 ?  28  LYS   A C    1 
ATOM   740  C  C    B LYS   A 1 28  ? 18.680 2.676   18.160  0.42 17.02 ?  28  LYS   A C    1 
ATOM   741  O  O    A LYS   A 1 28  ? 19.558 2.428   19.464  0.58 21.23 ?  28  LYS   A O    1 
ATOM   742  O  O    B LYS   A 1 28  ? 19.196 2.911   19.259  0.42 17.52 ?  28  LYS   A O    1 
ATOM   743  C  CB   A LYS   A 1 28  ? 18.863 4.406   16.951  0.58 21.66 ?  28  LYS   A CB   1 
ATOM   744  C  CB   B LYS   A 1 28  ? 18.498 4.644   16.616  0.42 18.31 ?  28  LYS   A CB   1 
ATOM   745  C  CG   A LYS   A 1 28  ? 19.701 5.356   16.105  0.58 23.77 ?  28  LYS   A CG   1 
ATOM   746  C  CG   B LYS   A 1 28  ? 19.242 5.552   15.658  0.42 20.46 ?  28  LYS   A CG   1 
ATOM   747  C  CD   A LYS   A 1 28  ? 19.230 6.797   16.215  0.58 25.93 ?  28  LYS   A CD   1 
ATOM   748  C  CD   B LYS   A 1 28  ? 18.650 6.951   15.620  0.42 23.04 ?  28  LYS   A CD   1 
ATOM   749  C  CE   A LYS   A 1 28  ? 17.937 7.015   15.457  0.58 27.38 ?  28  LYS   A CE   1 
ATOM   750  C  CE   B LYS   A 1 28  ? 17.316 6.981   14.899  0.42 24.81 ?  28  LYS   A CE   1 
ATOM   751  N  NZ   A LYS   A 1 28  ? 17.590 8.462   15.387  0.58 28.40 ?  28  LYS   A NZ   1 
ATOM   752  N  NZ   B LYS   A 1 28  ? 16.741 8.355   14.877  0.42 25.50 ?  28  LYS   A NZ   1 
ATOM   753  H  H    A LYS   A 1 28  ? 18.868 2.569   15.331  0.58 20.30 ?  28  LYS   A H    1 
ATOM   754  H  H    B LYS   A 1 28  ? 18.679 2.748   15.099  0.42 17.85 ?  28  LYS   A H    1 
ATOM   755  H  HA   A LYS   A 1 28  ? 20.457 3.180   17.297  0.58 23.32 ?  28  LYS   A HA   1 
ATOM   756  H  HA   B LYS   A 1 28  ? 20.160 3.551   17.075  0.42 19.86 ?  28  LYS   A HA   1 
ATOM   757  H  HB2  A LYS   A 1 28  ? 18.010 4.297   16.508  0.58 25.99 ?  28  LYS   A HB2  1 
ATOM   758  H  HB2  B LYS   A 1 28  ? 17.634 4.442   16.221  0.42 21.98 ?  28  LYS   A HB2  1 
ATOM   759  H  HB3  A LYS   A 1 28  ? 18.736 4.823   17.818  0.58 25.99 ?  28  LYS   A HB3  1 
ATOM   760  H  HB3  B LYS   A 1 28  ? 18.374 5.128   17.448  0.42 21.98 ?  28  LYS   A HB3  1 
ATOM   761  H  HG2  A LYS   A 1 28  ? 20.623 5.321   16.403  0.58 28.52 ?  28  LYS   A HG2  1 
ATOM   762  H  HG2  B LYS   A 1 28  ? 20.167 5.622   15.941  0.42 24.55 ?  28  LYS   A HG2  1 
ATOM   763  H  HG3  A LYS   A 1 28  ? 19.641 5.092   15.174  0.58 28.52 ?  28  LYS   A HG3  1 
ATOM   764  H  HG3  B LYS   A 1 28  ? 19.193 5.180   14.764  0.42 24.55 ?  28  LYS   A HG3  1 
ATOM   765  H  HD2  A LYS   A 1 28  ? 19.075 7.015   17.148  0.58 31.12 ?  28  LYS   A HD2  1 
ATOM   766  H  HD2  B LYS   A 1 28  ? 18.511 7.264   16.529  0.42 27.65 ?  28  LYS   A HD2  1 
ATOM   767  H  HD3  A LYS   A 1 28  ? 19.904 7.386   15.840  0.58 31.12 ?  28  LYS   A HD3  1 
ATOM   768  H  HD3  B LYS   A 1 28  ? 19.261 7.544   15.153  0.42 27.65 ?  28  LYS   A HD3  1 
ATOM   769  H  HE2  A LYS   A 1 28  ? 18.036 6.681   14.552  0.58 32.86 ?  28  LYS   A HE2  1 
ATOM   770  H  HE2  B LYS   A 1 28  ? 17.442 6.687   13.983  0.42 29.78 ?  28  LYS   A HE2  1 
ATOM   771  H  HE3  A LYS   A 1 28  ? 17.217 6.550   15.911  0.58 32.86 ?  28  LYS   A HE3  1 
ATOM   772  H  HE3  B LYS   A 1 28  ? 16.692 6.396   15.356  0.42 29.78 ?  28  LYS   A HE3  1 
ATOM   773  H  HZ1  A LYS   A 1 28  ? 16.829 8.571   14.939  0.58 34.08 ?  28  LYS   A HZ1  1 
ATOM   774  H  HZ1  B LYS   A 1 28  ? 15.961 8.351   14.450  0.42 30.60 ?  28  LYS   A HZ1  1 
ATOM   775  H  HZ2  A LYS   A 1 28  ? 17.492 8.791   16.208  0.58 34.08 ?  28  LYS   A HZ2  1 
ATOM   776  H  HZ2  B LYS   A 1 28  ? 16.615 8.645   15.709  0.42 30.60 ?  28  LYS   A HZ2  1 
ATOM   777  H  HZ3  A LYS   A 1 28  ? 18.237 8.910   14.971  0.58 34.08 ?  28  LYS   A HZ3  1 
ATOM   778  H  HZ3  B LYS   A 1 28  ? 17.298 8.910   14.459  0.42 30.60 ?  28  LYS   A HZ3  1 
ATOM   779  N  N    A LYS   A 1 29  ? 17.887 1.562   18.229  0.58 20.83 ?  29  LYS   A N    1 
ATOM   780  N  N    B LYS   A 1 29  ? 17.639 1.854   18.021  0.42 17.55 ?  29  LYS   A N    1 
ATOM   781  C  CA   A LYS   A 1 29  ? 17.290 0.876   19.373  0.58 22.35 ?  29  LYS   A CA   1 
ATOM   782  C  CA   B LYS   A 1 29  ? 17.028 1.215   19.181  0.42 18.93 ?  29  LYS   A CA   1 
ATOM   783  C  C    A LYS   A 1 29  ? 18.093 -0.361  19.764  0.58 21.29 ?  29  LYS   A C    1 
ATOM   784  C  C    B LYS   A 1 29  ? 17.806 -0.022  19.611  0.42 18.32 ?  29  LYS   A C    1 
ATOM   785  O  O    A LYS   A 1 29  ? 18.365 -0.588  20.950  0.58 22.32 ?  29  LYS   A O    1 
ATOM   786  O  O    B LYS   A 1 29  ? 18.061 -0.216  20.805  0.42 18.99 ?  29  LYS   A O    1 
ATOM   787  C  CB   A LYS   A 1 29  ? 15.847 0.486   19.046  0.58 25.29 ?  29  LYS   A CB   1 
ATOM   788  C  CB   B LYS   A 1 29  ? 15.579 0.842   18.865  0.42 21.36 ?  29  LYS   A CB   1 
ATOM   789  C  CG   A LYS   A 1 29  ? 15.115 -0.226  20.178  0.58 28.19 ?  29  LYS   A CG   1 
ATOM   790  C  CG   B LYS   A 1 29  ? 14.842 0.160   20.010  0.42 24.03 ?  29  LYS   A CG   1 
ATOM   791  C  CD   A LYS   A 1 29  ? 14.784 0.726   21.318  0.58 30.71 ?  29  LYS   A CD   1 
ATOM   792  C  CD   B LYS   A 1 29  ? 14.583 1.122   21.156  0.42 26.38 ?  29  LYS   A CD   1 
ATOM   793  C  CE   A LYS   A 1 29  ? 13.912 0.053   22.368  0.58 32.48 ?  29  LYS   A CE   1 
ATOM   794  C  CE   B LYS   A 1 29  ? 13.693 0.494   22.215  0.42 28.15 ?  29  LYS   A CE   1 
ATOM   795  N  NZ   A LYS   A 1 29  ? 13.471 1.009   23.421  0.58 33.48 ?  29  LYS   A NZ   1 
ATOM   796  N  NZ   B LYS   A 1 29  ? 13.389 1.449   23.314  0.42 29.22 ?  29  LYS   A NZ   1 
ATOM   797  H  H    A LYS   A 1 29  ? 17.481 1.428   17.481  0.58 25.00 ?  29  LYS   A H    1 
ATOM   798  H  H    B LYS   A 1 29  ? 17.266 1.654   17.272  0.42 21.06 ?  29  LYS   A H    1 
ATOM   799  H  HA   A LYS   A 1 29  ? 17.271 1.481   20.131  0.58 26.82 ?  29  LYS   A HA   1 
ATOM   800  H  HA   B LYS   A 1 29  ? 17.025 1.833   19.925  0.42 22.72 ?  29  LYS   A HA   1 
ATOM   801  H  HB2  A LYS   A 1 29  ? 15.344 1.288   18.835  0.58 30.35 ?  29  LYS   A HB2  1 
ATOM   802  H  HB2  B LYS   A 1 29  ? 15.092 1.651   18.648  0.42 25.63 ?  29  LYS   A HB2  1 
ATOM   803  H  HB3  A LYS   A 1 29  ? 15.849 -0.109  18.281  0.58 30.35 ?  29  LYS   A HB3  1 
ATOM   804  H  HB3  B LYS   A 1 29  ? 15.569 0.237   18.109  0.42 25.63 ?  29  LYS   A HB3  1 
ATOM   805  H  HG2  A LYS   A 1 29  ? 14.282 -0.589  19.839  0.58 33.83 ?  29  LYS   A HG2  1 
ATOM   806  H  HG2  B LYS   A 1 29  ? 13.986 -0.162  19.688  0.42 28.83 ?  29  LYS   A HG2  1 
ATOM   807  H  HG3  A LYS   A 1 29  ? 15.668 -0.941  20.530  0.58 33.83 ?  29  LYS   A HG3  1 
ATOM   808  H  HG3  B LYS   A 1 29  ? 15.369 -0.583  20.347  0.42 28.83 ?  29  LYS   A HG3  1 
ATOM   809  H  HD2  A LYS   A 1 29  ? 15.606 1.014   21.745  0.58 36.86 ?  29  LYS   A HD2  1 
ATOM   810  H  HD2  B LYS   A 1 29  ? 15.427 1.361   21.570  0.42 31.65 ?  29  LYS   A HD2  1 
ATOM   811  H  HD3  A LYS   A 1 29  ? 14.302 1.491   20.966  0.58 36.86 ?  29  LYS   A HD3  1 
ATOM   812  H  HD3  B LYS   A 1 29  ? 14.140 1.913   20.814  0.42 31.65 ?  29  LYS   A HD3  1 
ATOM   813  H  HE2  A LYS   A 1 29  ? 13.121 -0.312  21.940  0.58 38.98 ?  29  LYS   A HE2  1 
ATOM   814  H  HE2  B LYS   A 1 29  ? 12.855 0.221   21.807  0.42 33.78 ?  29  LYS   A HE2  1 
ATOM   815  H  HE3  A LYS   A 1 29  ? 14.416 -0.657  22.796  0.58 38.98 ?  29  LYS   A HE3  1 
ATOM   816  H  HE3  B LYS   A 1 29  ? 14.145 -0.276  22.597  0.42 33.78 ?  29  LYS   A HE3  1 
ATOM   817  H  HZ1  A LYS   A 1 29  ? 12.963 0.589   24.020  0.58 40.17 ?  29  LYS   A HZ1  1 
ATOM   818  H  HZ1  B LYS   A 1 29  ? 12.867 1.059   23.920  0.42 35.07 ?  29  LYS   A HZ1  1 
ATOM   819  H  HZ2  A LYS   A 1 29  ? 14.179 1.355   23.834  0.58 40.17 ?  29  LYS   A HZ2  1 
ATOM   820  H  HZ2  B LYS   A 1 29  ? 14.144 1.711   23.706  0.42 35.07 ?  29  LYS   A HZ2  1 
ATOM   821  H  HZ3  A LYS   A 1 29  ? 12.999 1.669   23.054  0.58 40.17 ?  29  LYS   A HZ3  1 
ATOM   822  H  HZ3  B LYS   A 1 29  ? 12.970 2.163   22.987  0.42 35.07 ?  29  LYS   A HZ3  1 
ATOM   823  N  N    A VAL   A 1 30  ? 18.459 -1.184  18.781  0.58 20.37 ?  30  VAL   A N    1 
ATOM   824  N  N    B VAL   A 1 30  ? 18.177 -0.873  18.652  0.42 18.41 ?  30  VAL   A N    1 
ATOM   825  C  CA   A VAL   A 1 30  ? 19.102 -2.463  19.065  0.58 19.64 ?  30  VAL   A CA   1 
ATOM   826  C  CA   B VAL   A 1 30  ? 18.804 -2.147  18.993  0.42 18.50 ?  30  VAL   A CA   1 
ATOM   827  C  C    A VAL   A 1 30  ? 20.606 -2.315  19.282  0.58 18.05 ?  30  VAL   A C    1 
ATOM   828  C  C    B VAL   A 1 30  ? 20.297 -1.987  19.254  0.42 18.40 ?  30  VAL   A C    1 
ATOM   829  O  O    A VAL   A 1 30  ? 21.196 -3.063  20.072  0.58 18.53 ?  30  VAL   A O    1 
ATOM   830  O  O    B VAL   A 1 30  ? 20.857 -2.689  20.104  0.42 18.55 ?  30  VAL   A O    1 
ATOM   831  C  CB   A VAL   A 1 30  ? 18.790 -3.460  17.934  0.58 20.58 ?  30  VAL   A CB   1 
ATOM   832  C  CB   B VAL   A 1 30  ? 18.525 -3.187  17.891  0.42 18.84 ?  30  VAL   A CB   1 
ATOM   833  C  CG1  A VAL   A 1 30  ? 19.553 -4.766  18.131  0.58 21.39 ?  30  VAL   A CG1  1 
ATOM   834  C  CG1  B VAL   A 1 30  ? 19.257 -4.494  18.176  0.42 19.49 ?  30  VAL   A CG1  1 
ATOM   835  C  CG2  A VAL   A 1 30  ? 17.291 -3.716  17.850  0.58 21.20 ?  30  VAL   A CG2  1 
ATOM   836  C  CG2  B VAL   A 1 30  ? 17.028 -3.433  17.759  0.42 18.92 ?  30  VAL   A CG2  1 
ATOM   837  H  H    A VAL   A 1 30  ? 18.324 -1.033  17.944  0.58 24.44 ?  30  VAL   A H    1 
ATOM   838  H  H    B VAL   A 1 30  ? 18.069 -0.743  17.805  0.42 22.09 ?  30  VAL   A H    1 
ATOM   839  H  HA   A VAL   A 1 30  ? 18.721 -2.823  19.878  0.58 23.56 ?  30  VAL   A HA   1 
ATOM   840  H  HA   B VAL   A 1 30  ? 18.398 -2.479  19.804  0.42 22.20 ?  30  VAL   A HA   1 
ATOM   841  H  HB   A VAL   A 1 30  ? 19.073 -3.078  17.088  0.58 24.69 ?  30  VAL   A HB   1 
ATOM   842  H  HB   B VAL   A 1 30  ? 18.847 -2.849  17.041  0.42 22.61 ?  30  VAL   A HB   1 
ATOM   843  H  HG11 A VAL   A 1 30  ? 19.172 -5.444  17.549  0.58 25.67 ?  30  VAL   A HG11 1 
ATOM   844  H  HG11 B VAL   A 1 30  ? 18.898 -5.190  17.600  0.42 23.39 ?  30  VAL   A HG11 1 
ATOM   845  H  HG12 A VAL   A 1 30  ? 20.486 -4.628  17.909  0.58 25.67 ?  30  VAL   A HG12 1 
ATOM   846  H  HG12 B VAL   A 1 30  ? 20.203 -4.376  17.996  0.42 23.39 ?  30  VAL   A HG12 1 
ATOM   847  H  HG13 A VAL   A 1 30  ? 19.467 -5.044  19.057  0.58 25.67 ?  30  VAL   A HG13 1 
ATOM   848  H  HG13 B VAL   A 1 30  ? 19.121 -4.736  19.105  0.42 23.39 ?  30  VAL   A HG13 1 
ATOM   849  H  HG21 A VAL   A 1 30  ? 17.122 -4.382  17.165  0.58 25.44 ?  30  VAL   A HG21 1 
ATOM   850  H  HG21 B VAL   A 1 30  ? 16.877 -4.124  17.094  0.42 22.70 ?  30  VAL   A HG21 1 
ATOM   851  H  HG22 A VAL   A 1 30  ? 16.978 -4.040  18.709  0.58 25.44 ?  30  VAL   A HG22 1 
ATOM   852  H  HG22 B VAL   A 1 30  ? 16.679 -3.720  18.618  0.42 22.70 ?  30  VAL   A HG22 1 
ATOM   853  H  HG23 A VAL   A 1 30  ? 16.841 -2.888  17.625  0.58 25.44 ?  30  VAL   A HG23 1 
ATOM   854  H  HG23 B VAL   A 1 30  ? 16.597 -2.610  17.484  0.42 22.70 ?  30  VAL   A HG23 1 
ATOM   855  N  N    A LYS   A 1 31  ? 21.247 -1.373  18.598  0.58 16.90 ?  31  LYS   A N    1 
ATOM   856  N  N    B LYS   A 1 31  ? 20.956 -1.071  18.554  0.42 18.52 ?  31  LYS   A N    1 
ATOM   857  C  CA   A LYS   A 1 31  ? 22.702 -1.269  18.560  0.58 17.62 ?  31  LYS   A CA   1 
ATOM   858  C  CA   B LYS   A 1 31  ? 22.411 -0.984  18.530  0.42 18.78 ?  31  LYS   A CA   1 
ATOM   859  C  C    A LYS   A 1 31  ? 23.314 -2.629  18.213  0.58 15.49 ?  31  LYS   A C    1 
ATOM   860  C  C    B LYS   A 1 31  ? 23.015 -2.366  18.268  0.42 17.52 ?  31  LYS   A C    1 
ATOM   861  O  O    A LYS   A 1 31  ? 24.096 -3.185  18.992  0.58 16.60 ?  31  LYS   A O    1 
ATOM   862  O  O    B LYS   A 1 31  ? 23.730 -2.909  19.115  0.42 18.39 ?  31  LYS   A O    1 
ATOM   863  C  CB   A LYS   A 1 31  ? 23.271 -0.727  19.864  0.58 21.27 ?  31  LYS   A CB   1 
ATOM   864  C  CB   B LYS   A 1 31  ? 22.969 -0.381  19.811  0.42 21.31 ?  31  LYS   A CB   1 
ATOM   865  C  CG   A LYS   A 1 31  ? 22.586 0.536   20.362  0.58 26.15 ?  31  LYS   A CG   1 
ATOM   866  C  CG   B LYS   A 1 31  ? 22.326 0.927   20.211  0.42 24.83 ?  31  LYS   A CG   1 
ATOM   867  C  CD   A LYS   A 1 31  ? 23.594 1.587   20.809  0.58 29.89 ?  31  LYS   A CD   1 
ATOM   868  C  CD   B LYS   A 1 31  ? 23.309 1.801   20.965  0.42 27.74 ?  31  LYS   A CD   1 
ATOM   869  C  CE   A LYS   A 1 31  ? 22.950 2.632   21.711  0.58 32.24 ?  31  LYS   A CE   1 
ATOM   870  C  CE   B LYS   A 1 31  ? 22.591 2.837   21.803  0.42 29.86 ?  31  LYS   A CE   1 
ATOM   871  N  NZ   A LYS   A 1 31  ? 21.757 3.271   21.090  0.58 33.44 ?  31  LYS   A NZ   1 
ATOM   872  N  NZ   B LYS   A 1 31  ? 21.496 3.498   21.049  0.42 31.09 ?  31  LYS   A NZ   1 
ATOM   873  H  H    A LYS   A 1 31  ? 20.853 -0.768  18.132  0.58 20.28 ?  31  LYS   A H    1 
ATOM   874  H  H    B LYS   A 1 31  ? 20.569 -0.471  18.076  0.42 22.22 ?  31  LYS   A H    1 
ATOM   875  H  HA   A LYS   A 1 31  ? 22.944 -0.648  17.858  0.58 21.15 ?  31  LYS   A HA   1 
ATOM   876  H  HA   B LYS   A 1 31  ? 22.667 -0.400  17.802  0.42 22.53 ?  31  LYS   A HA   1 
ATOM   877  H  HB2  A LYS   A 1 31  ? 23.181 -1.407  20.546  0.58 25.53 ?  31  LYS   A HB2  1 
ATOM   878  H  HB2  B LYS   A 1 31  ? 22.837 -1.008  20.536  0.42 25.57 ?  31  LYS   A HB2  1 
ATOM   879  H  HB3  A LYS   A 1 31  ? 24.211 -0.521  19.728  0.58 25.53 ?  31  LYS   A HB3  1 
ATOM   880  H  HB3  B LYS   A 1 31  ? 23.918 -0.215  19.688  0.42 25.57 ?  31  LYS   A HB3  1 
ATOM   881  H  HG2  A LYS   A 1 31  ? 22.052 0.915   19.646  0.58 31.38 ?  31  LYS   A HG2  1 
ATOM   882  H  HG2  B LYS   A 1 31  ? 22.039 1.403   19.416  0.42 29.79 ?  31  LYS   A HG2  1 
ATOM   883  H  HG3  A LYS   A 1 31  ? 22.022 0.316   21.120  0.58 31.38 ?  31  LYS   A HG3  1 
ATOM   884  H  HG3  B LYS   A 1 31  ? 21.568 0.749   20.791  0.42 29.79 ?  31  LYS   A HG3  1 
ATOM   885  H  HD2  A LYS   A 1 31  ? 24.308 1.157   21.306  0.58 35.87 ?  31  LYS   A HD2  1 
ATOM   886  H  HD2  B LYS   A 1 31  ? 23.845 1.245   21.554  0.42 33.29 ?  31  LYS   A HD2  1 
ATOM   887  H  HD3  A LYS   A 1 31  ? 23.954 2.039   20.029  0.58 35.87 ?  31  LYS   A HD3  1 
ATOM   888  H  HD3  B LYS   A 1 31  ? 23.880 2.262   20.330  0.42 33.29 ?  31  LYS   A HD3  1 
ATOM   889  H  HE2  A LYS   A 1 31  ? 22.666 2.207   22.535  0.58 38.69 ?  31  LYS   A HE2  1 
ATOM   890  H  HE2  B LYS   A 1 31  ? 22.204 2.402   22.577  0.42 35.83 ?  31  LYS   A HE2  1 
ATOM   891  H  HE3  A LYS   A 1 31  ? 23.597 3.329   21.902  0.58 38.69 ?  31  LYS   A HE3  1 
ATOM   892  H  HE3  B LYS   A 1 31  ? 23.224 3.515   22.083  0.42 35.83 ?  31  LYS   A HE3  1 
ATOM   893  H  HZ1  A LYS   A 1 31  ? 21.422 3.889   21.638  0.58 40.13 ?  31  LYS   A HZ1  1 
ATOM   894  H  HZ1  B LYS   A 1 31  ? 21.165 4.172   21.525  0.42 37.31 ?  31  LYS   A HZ1  1 
ATOM   895  H  HZ2  A LYS   A 1 31  ? 21.984 3.660   20.322  0.58 40.13 ?  31  LYS   A HZ2  1 
ATOM   896  H  HZ2  B LYS   A 1 31  ? 21.807 3.813   20.277  0.42 37.31 ?  31  LYS   A HZ2  1 
ATOM   897  H  HZ3  A LYS   A 1 31  ? 21.131 2.659   20.930  0.58 40.13 ?  31  LYS   A HZ3  1 
ATOM   898  H  HZ3  B LYS   A 1 31  ? 20.845 2.914   20.881  0.42 37.31 ?  31  LYS   A HZ3  1 
ATOM   899  N  N    A PRO   A 1 32  ? 22.975 -3.185  17.054  0.58 14.21 ?  32  PRO   A N    1 
ATOM   900  N  N    B PRO   A 1 32  ? 22.744 -2.954  17.107  0.42 15.58 ?  32  PRO   A N    1 
ATOM   901  C  CA   A PRO   A 1 32  ? 23.446 -4.528  16.712  0.58 15.35 ?  32  PRO   A CA   1 
ATOM   902  C  CA   B PRO   A 1 32  ? 23.222 -4.310  16.833  0.42 15.24 ?  32  PRO   A CA   1 
ATOM   903  C  C    A PRO   A 1 32  ? 24.946 -4.554  16.489  0.58 15.14 ?  32  PRO   A C    1 
ATOM   904  C  C    B PRO   A 1 32  ? 24.729 -4.332  16.638  0.42 14.83 ?  32  PRO   A C    1 
ATOM   905  O  O    A PRO   A 1 32  ? 25.588 -3.535  16.219  0.58 14.73 ?  32  PRO   A O    1 
ATOM   906  O  O    B PRO   A 1 32  ? 25.397 -3.301  16.532  0.42 15.15 ?  32  PRO   A O    1 
ATOM   907  C  CB   A PRO   A 1 32  ? 22.709 -4.829  15.403  0.58 15.31 ?  32  PRO   A CB   1 
ATOM   908  C  CB   B PRO   A 1 32  ? 22.499 -4.666  15.533  0.42 15.32 ?  32  PRO   A CB   1 
ATOM   909  C  CG   A PRO   A 1 32  ? 22.539 -3.482  14.779  0.58 14.18 ?  32  PRO   A CG   1 
ATOM   910  C  CG   B PRO   A 1 32  ? 22.371 -3.355  14.833  0.42 14.89 ?  32  PRO   A CG   1 
ATOM   911  C  CD   A PRO   A 1 32  ? 22.257 -2.557  15.933  0.58 14.02 ?  32  PRO   A CD   1 
ATOM   912  C  CD   B PRO   A 1 32  ? 22.085 -2.360  15.930  0.42 15.05 ?  32  PRO   A CD   1 
ATOM   913  H  HA   A PRO   A 1 32  ? 23.196 -5.170  17.396  0.58 18.41 ?  32  PRO   A HA   1 
ATOM   914  H  HA   B PRO   A 1 32  ? 22.962 -4.922  17.539  0.42 18.29 ?  32  PRO   A HA   1 
ATOM   915  H  HB2  A PRO   A 1 32  ? 23.252 -5.410  14.843  0.58 18.37 ?  32  PRO   A HB2  1 
ATOM   916  H  HB2  B PRO   A 1 32  ? 23.035 -5.287  15.015  0.42 18.38 ?  32  PRO   A HB2  1 
ATOM   917  H  HB3  A PRO   A 1 32  ? 21.851 -5.241  15.595  0.58 18.37 ?  32  PRO   A HB3  1 
ATOM   918  H  HB3  B PRO   A 1 32  ? 21.625 -5.042  15.729  0.42 18.38 ?  32  PRO   A HB3  1 
ATOM   919  H  HG2  A PRO   A 1 32  ? 23.354 -3.233  14.320  0.58 17.01 ?  32  PRO   A HG2  1 
ATOM   920  H  HG2  B PRO   A 1 32  ? 23.203 -3.145  14.382  0.42 17.87 ?  32  PRO   A HG2  1 
ATOM   921  H  HG3  A PRO   A 1 32  ? 21.789 -3.507  14.161  0.58 17.01 ?  32  PRO   A HG3  1 
ATOM   922  H  HG3  B PRO   A 1 32  ? 21.637 -3.395  14.199  0.42 17.87 ?  32  PRO   A HG3  1 
ATOM   923  H  HD2  A PRO   A 1 32  ? 22.615 -1.677  15.740  0.58 16.82 ?  32  PRO   A HD2  1 
ATOM   924  H  HD2  B PRO   A 1 32  ? 22.480 -1.502  15.709  0.42 18.05 ?  32  PRO   A HD2  1 
ATOM   925  H  HD3  A PRO   A 1 32  ? 21.308 -2.529  16.112  0.58 16.82 ?  32  PRO   A HD3  1 
ATOM   926  H  HD3  B PRO   A 1 32  ? 21.129 -2.287  16.073  0.42 18.05 ?  32  PRO   A HD3  1 
ATOM   927  N  N    A THR   A 1 33  ? 25.500 -5.764  16.581  0.58 15.33 ?  33  THR   A N    1 
ATOM   928  N  N    B THR   A 1 33  ? 25.263 -5.551  16.581  0.42 14.81 ?  33  THR   A N    1 
ATOM   929  C  CA   A THR   A 1 33  ? 26.905 -5.946  16.248  0.58 15.73 ?  33  THR   A CA   1 
ATOM   930  C  CA   B THR   A 1 33  ? 26.685 -5.722  16.302  0.42 14.66 ?  33  THR   A CA   1 
ATOM   931  C  C    A THR   A 1 33  ? 27.187 -5.489  14.822  0.58 14.16 ?  33  THR   A C    1 
ATOM   932  C  C    B THR   A 1 33  ? 27.027 -5.275  14.884  0.42 13.80 ?  33  THR   A C    1 
ATOM   933  O  O    A THR   A 1 33  ? 28.243 -4.899  14.553  0.58 13.90 ?  33  THR   A O    1 
ATOM   934  O  O    B THR   A 1 33  ? 28.003 -4.545  14.672  0.42 13.86 ?  33  THR   A O    1 
ATOM   935  C  CB   A THR   A 1 33  ? 27.306 -7.410  16.453  0.58 17.54 ?  33  THR   A CB   1 
ATOM   936  C  CB   B THR   A 1 33  ? 27.081 -7.182  16.516  0.42 15.82 ?  33  THR   A CB   1 
ATOM   937  O  OG1  A THR   A 1 33  ? 27.050 -7.794  17.809  0.58 19.32 ?  33  THR   A OG1  1 
ATOM   938  O  OG1  B THR   A 1 33  ? 26.715 -7.581  17.841  0.42 16.84 ?  33  THR   A OG1  1 
ATOM   939  C  CG2  A THR   A 1 33  ? 28.783 -7.614  16.167  0.58 18.14 ?  33  THR   A CG2  1 
ATOM   940  C  CG2  B THR   A 1 33  ? 28.582 -7.360  16.319  0.42 16.59 ?  33  THR   A CG2  1 
ATOM   941  H  H    A THR   A 1 33  ? 25.089 -6.484  16.811  0.58 18.40 ?  33  THR   A H    1 
ATOM   942  H  H    B THR   A 1 33  ? 24.829 -6.284  16.710  0.42 17.77 ?  33  THR   A H    1 
ATOM   943  H  HA   A THR   A 1 33  ? 27.444 -5.404  16.844  0.58 18.87 ?  33  THR   A HA   1 
ATOM   944  H  HA   B THR   A 1 33  ? 27.195 -5.181  16.929  0.42 17.59 ?  33  THR   A HA   1 
ATOM   945  H  HB   A THR   A 1 33  ? 26.791 -7.975  15.855  0.58 21.04 ?  33  THR   A HB   1 
ATOM   946  H  HB   B THR   A 1 33  ? 26.619 -7.742  15.871  0.42 18.99 ?  33  THR   A HB   1 
ATOM   947  H  HG1  A THR   A 1 33  ? 27.475 -7.296  18.336  0.58 23.19 ?  33  THR   A HG1  1 
ATOM   948  H  HG1  B THR   A 1 33  ? 27.134 -7.119  18.407  0.42 20.21 ?  33  THR   A HG1  1 
ATOM   949  H  HG21 A THR   A 1 33  ? 29.054 -8.498  16.460  0.58 21.76 ?  33  THR   A HG21 1 
ATOM   950  H  HG21 B THR   A 1 33  ? 28.854 -8.241  16.614  0.42 19.91 ?  33  THR   A HG21 1 
ATOM   951  H  HG22 A THR   A 1 33  ? 28.953 -7.530  15.218  0.58 21.76 ?  33  THR   A HG22 1 
ATOM   952  H  HG22 B THR   A 1 33  ? 28.809 -7.260  15.379  0.42 19.91 ?  33  THR   A HG22 1 
ATOM   953  H  HG23 A THR   A 1 33  ? 29.305 -6.951  16.645  0.58 21.76 ?  33  THR   A HG23 1 
ATOM   954  H  HG23 B THR   A 1 33  ? 29.064 -6.692  16.831  0.42 19.91 ?  33  THR   A HG23 1 
ATOM   955  N  N    . VAL   A 1 34  ? 26.244 -5.719  13.902  1.00 13.22 ?  34  VAL   A N    1 
ATOM   956  C  CA   . VAL   A 1 34  ? 26.441 -5.393  12.493  1.00 11.95 ?  34  VAL   A CA   1 
ATOM   957  C  C    . VAL   A 1 34  ? 25.144 -4.837  11.920  1.00 11.35 ?  34  VAL   A C    1 
ATOM   958  O  O    . VAL   A 1 34  ? 24.106 -5.509  11.957  1.00 12.55 ?  34  VAL   A O    1 
ATOM   959  C  CB   . VAL   A 1 34  ? 26.879 -6.611  11.662  1.00 13.10 ?  34  VAL   A CB   1 
ATOM   960  C  CG1  . VAL   A 1 34  ? 27.048 -6.215  10.204  1.00 13.19 ?  34  VAL   A CG1  1 
ATOM   961  C  CG2  . VAL   A 1 34  ? 28.161 -7.223  12.210  1.00 14.35 ?  34  VAL   A CG2  1 
ATOM   962  H  H    A VAL   A 1 34  ? 25.475 -6.060  14.081  0.58 15.86 ?  34  VAL   A H    1 
ATOM   963  H  H    B VAL   A 1 34  ? 25.570 -6.236  14.037  0.42 15.86 ?  34  VAL   A H    1 
ATOM   964  H  HA   . VAL   A 1 34  ? 27.127 -4.709  12.413  1.00 14.34 ?  34  VAL   A HA   1 
ATOM   965  H  HB   . VAL   A 1 34  ? 26.183 -7.288  11.715  1.00 15.72 ?  34  VAL   A HB   1 
ATOM   966  H  HG11 . VAL   A 1 34  ? 27.557 -6.906  9.752   1.00 15.83 ?  34  VAL   A HG11 1 
ATOM   967  H  HG12 . VAL   A 1 34  ? 26.173 -6.130  9.796   1.00 15.83 ?  34  VAL   A HG12 1 
ATOM   968  H  HG13 . VAL   A 1 34  ? 27.522 -5.372  10.162  1.00 15.83 ?  34  VAL   A HG13 1 
ATOM   969  H  HG21 . VAL   A 1 34  ? 28.434 -7.952  11.628  1.00 17.22 ?  34  VAL   A HG21 1 
ATOM   970  H  HG22 . VAL   A 1 34  ? 28.850 -6.544  12.234  1.00 17.22 ?  34  VAL   A HG22 1 
ATOM   971  H  HG23 . VAL   A 1 34  ? 27.996 -7.563  13.104  1.00 17.22 ?  34  VAL   A HG23 1 
ATOM   972  N  N    . VAL   A 1 35  ? 25.216 -3.633  11.355  1.00 10.82 ?  35  VAL   A N    1 
ATOM   973  C  CA   . VAL   A 1 35  ? 24.187 -3.120  10.459  1.00 10.47 ?  35  VAL   A CA   1 
ATOM   974  C  C    . VAL   A 1 35  ? 24.744 -3.133  9.044   1.00 10.13 ?  35  VAL   A C    1 
ATOM   975  O  O    . VAL   A 1 35  ? 25.888 -2.729  8.813   1.00 10.75 ?  35  VAL   A O    1 
ATOM   976  C  CB   . VAL   A 1 35  ? 23.662 -1.724  10.859  1.00 11.43 ?  35  VAL   A CB   1 
ATOM   977  C  CG1  . VAL   A 1 35  ? 24.735 -0.631  10.736  1.00 12.18 ?  35  VAL   A CG1  1 
ATOM   978  C  CG2  . VAL   A 1 35  ? 22.438 -1.372  10.021  1.00 12.11 ?  35  VAL   A CG2  1 
ATOM   979  H  H    . VAL   A 1 35  ? 25.860 -3.078  11.481  1.00 12.98 ?  35  VAL   A H    1 
ATOM   980  H  HA   . VAL   A 1 35  ? 23.428 -3.730  10.480  1.00 12.56 ?  35  VAL   A HA   1 
ATOM   981  H  HB   . VAL   A 1 35  ? 23.372 -1.754  11.782  1.00 13.72 ?  35  VAL   A HB   1 
ATOM   982  H  HG11 . VAL   A 1 35  ? 24.380 0.203   11.089  1.00 14.62 ?  35  VAL   A HG11 1 
ATOM   983  H  HG12 . VAL   A 1 35  ? 25.515 -0.898  11.243  1.00 14.62 ?  35  VAL   A HG12 1 
ATOM   984  H  HG13 . VAL   A 1 35  ? 24.969 -0.516  9.801   1.00 14.62 ?  35  VAL   A HG13 1 
ATOM   985  H  HG21 . VAL   A 1 35  ? 22.071 -0.530  10.327  1.00 14.53 ?  35  VAL   A HG21 1 
ATOM   986  H  HG22 . VAL   A 1 35  ? 22.703 -1.294  9.086   1.00 14.53 ?  35  VAL   A HG22 1 
ATOM   987  H  HG23 . VAL   A 1 35  ? 21.774 -2.075  10.111  1.00 14.53 ?  35  VAL   A HG23 1 
ATOM   988  N  N    . VAL   A 1 36  ? 23.933 -3.601  8.096   1.00 9.45  ?  36  VAL   A N    1 
ATOM   989  C  CA   . VAL   A 1 36  ? 24.309 -3.620  6.691   1.00 9.12  ?  36  VAL   A CA   1 
ATOM   990  C  C    . VAL   A 1 36  ? 23.850 -2.332  6.018   1.00 9.52  ?  36  VAL   A C    1 
ATOM   991  O  O    . VAL   A 1 36  ? 22.683 -1.933  6.139   1.00 10.17 ?  36  VAL   A O    1 
ATOM   992  C  CB   . VAL   A 1 36  ? 23.709 -4.842  5.976   1.00 9.54  ?  36  VAL   A CB   1 
ATOM   993  C  CG1  . VAL   A 1 36  ? 23.977 -4.765  4.493   1.00 10.14 ?  36  VAL   A CG1  1 
ATOM   994  C  CG2  . VAL   A 1 36  ? 24.249 -6.132  6.572   1.00 10.47 ?  36  VAL   A CG2  1 
ATOM   995  H  H    . VAL   A 1 36  ? 23.145 -3.928  8.249   1.00 11.33 ?  36  VAL   A H    1 
ATOM   996  H  HA   . VAL   A 1 36  ? 25.275 -3.678  6.620   1.00 10.95 ?  36  VAL   A HA   1 
ATOM   997  H  HB   . VAL   A 1 36  ? 22.745 -4.832  6.102   1.00 11.45 ?  36  VAL   A HB   1 
ATOM   998  H  HG11 . VAL   A 1 36  ? 23.852 -5.644  4.106   1.00 12.17 ?  36  VAL   A HG11 1 
ATOM   999  H  HG12 . VAL   A 1 36  ? 23.356 -4.136  4.087   1.00 12.17 ?  36  VAL   A HG12 1 
ATOM   1000 H  HG13 . VAL   A 1 36  ? 24.888 -4.467  4.354   1.00 12.17 ?  36  VAL   A HG13 1 
ATOM   1001 H  HG21 . VAL   A 1 36  ? 23.868 -6.886  6.092   1.00 12.57 ?  36  VAL   A HG21 1 
ATOM   1002 H  HG22 . VAL   A 1 36  ? 25.215 -6.140  6.483   1.00 12.57 ?  36  VAL   A HG22 1 
ATOM   1003 H  HG23 . VAL   A 1 36  ? 24.002 -6.179  7.508   1.00 12.57 ?  36  VAL   A HG23 1 
ATOM   1004 N  N    . ASN   A 1 37  ? 24.774 -1.693  5.300   1.00 9.20  ?  37  ASN   A N    1 
ATOM   1005 C  CA   . ASN   A 1 37  ? 24.454 -0.580  4.423   1.00 8.91  ?  37  ASN   A CA   1 
ATOM   1006 C  C    . ASN   A 1 37  ? 24.326 -1.063  2.990   1.00 8.90  ?  37  ASN   A C    1 
ATOM   1007 O  O    . ASN   A 1 37  ? 25.114 -1.894  2.521   1.00 9.52  ?  37  ASN   A O    1 
ATOM   1008 C  CB   . ASN   A 1 37  ? 25.535 0.497   4.498   1.00 9.34  ?  37  ASN   A CB   1 
ATOM   1009 C  CG   . ASN   A 1 37  ? 25.216 1.688   3.636   1.00 9.53  ?  37  ASN   A CG   1 
ATOM   1010 O  OD1  . ASN   A 1 37  ? 24.047 2.023   3.438   1.00 10.15 ?  37  ASN   A OD1  1 
ATOM   1011 N  ND2  . ASN   A 1 37  ? 26.247 2.339   3.119   1.00 9.88  ?  37  ASN   A ND2  1 
ATOM   1012 H  H    . ASN   A 1 37  ? 25.612 -1.887  5.318   1.00 11.04 ?  37  ASN   A H    1 
ATOM   1013 H  HA   . ASN   A 1 37  ? 23.611 -0.184  4.701   1.00 10.70 ?  37  ASN   A HA   1 
ATOM   1014 H  HB2  . ASN   A 1 37  ? 25.623 0.801   5.416   1.00 11.21 ?  37  ASN   A HB2  1 
ATOM   1015 H  HB3  . ASN   A 1 37  ? 26.380 0.120   4.194   1.00 11.21 ?  37  ASN   A HB3  1 
ATOM   1016 H  HD21 . ASN   A 1 37  ? 26.112 3.028   2.618   1.00 11.85 ?  37  ASN   A HD21 1 
ATOM   1017 H  HD22 . ASN   A 1 37  ? 27.044 2.080   3.276   1.00 11.85 ?  37  ASN   A HD22 1 
ATOM   1018 N  N    A ALA   A 1 38  ? 23.305 -0.537  2.308   0.58 9.18  ?  38  ALA   A N    1 
ATOM   1019 N  N    B ALA   A 1 38  ? 23.318 -0.540  2.288   0.42 9.39  ?  38  ALA   A N    1 
ATOM   1020 C  CA   A ALA   A 1 38  ? 23.123 -0.687  0.866   0.58 9.43  ?  38  ALA   A CA   1 
ATOM   1021 C  CA   B ALA   A 1 38  ? 23.161 -0.782  0.853   0.42 9.92  ?  38  ALA   A CA   1 
ATOM   1022 C  C    A ALA   A 1 38  ? 24.032 0.324   0.169   0.58 9.81  ?  38  ALA   A C    1 
ATOM   1023 C  C    B ALA   A 1 38  ? 24.009 0.245   0.102   0.42 10.06 ?  38  ALA   A C    1 
ATOM   1024 O  O    A ALA   A 1 38  ? 23.625 1.423   -0.215  0.58 9.34  ?  38  ALA   A O    1 
ATOM   1025 O  O    B ALA   A 1 38  ? 23.533 1.274   -0.385  0.42 10.21 ?  38  ALA   A O    1 
ATOM   1026 C  CB   A ALA   A 1 38  ? 21.660 -0.467  0.497   0.58 10.14 ?  38  ALA   A CB   1 
ATOM   1027 C  CB   B ALA   A 1 38  ? 21.693 -0.727  0.453   0.42 11.08 ?  38  ALA   A CB   1 
ATOM   1028 H  H    A ALA   A 1 38  ? 22.690 -0.057  2.677   0.58 11.01 ?  38  ALA   A H    1 
ATOM   1029 H  H    B ALA   A 1 38  ? 22.708 -0.031  2.626   0.42 11.26 ?  38  ALA   A H    1 
ATOM   1030 H  HA   A ALA   A 1 38  ? 23.387 -1.576  0.596   0.58 11.31 ?  38  ALA   A HA   1 
ATOM   1031 H  HA   B ALA   A 1 38  ? 23.501 -1.669  0.646   0.42 11.91 ?  38  ALA   A HA   1 
ATOM   1032 H  HB1  A ALA   A 1 38  ? 21.557 -0.572  -0.461  0.58 12.17 ?  38  ALA   A HB1  1 
ATOM   1033 H  HB1  B ALA   A 1 38  ? 21.623 -0.887  -0.500  0.42 13.29 ?  38  ALA   A HB1  1 
ATOM   1034 H  HB2  A ALA   A 1 38  ? 21.116 -1.123  0.963   0.58 12.17 ?  38  ALA   A HB2  1 
ATOM   1035 H  HB2  B ALA   A 1 38  ? 21.206 -1.410  0.941   0.42 13.29 ?  38  ALA   A HB2  1 
ATOM   1036 H  HB3  A ALA   A 1 38  ? 21.396 0.428   0.763   0.58 12.17 ?  38  ALA   A HB3  1 
ATOM   1037 H  HB3  B ALA   A 1 38  ? 21.342 0.149   0.669   0.42 13.29 ?  38  ALA   A HB3  1 
ATOM   1038 N  N    . ALA   A 1 39  ? 25.300 -0.055  0.020   1.00 9.99  ?  39  ALA   A N    1 
ATOM   1039 C  CA   . ALA   A 1 39  ? 26.322 0.846   -0.486  1.00 9.88  ?  39  ALA   A CA   1 
ATOM   1040 C  C    . ALA   A 1 39  ? 26.452 0.782   -2.003  1.00 9.83  ?  39  ALA   A C    1 
ATOM   1041 O  O    . ALA   A 1 39  ? 25.977 -0.144  -2.661  1.00 10.38 ?  39  ALA   A O    1 
ATOM   1042 C  CB   . ALA   A 1 39  ? 27.666 0.480   0.148   1.00 11.22 ?  39  ALA   A CB   1 
ATOM   1043 H  H    A ALA   A 1 39  ? 25.592 -0.842  0.212   0.58 11.99 ?  39  ALA   A H    1 
ATOM   1044 H  H    B ALA   A 1 39  ? 25.621 -0.815  0.268   0.42 11.99 ?  39  ALA   A H    1 
ATOM   1045 H  HA   . ALA   A 1 39  ? 26.096 1.760   -0.231  1.00 11.86 ?  39  ALA   A HA   1 
ATOM   1046 H  HB1  . ALA   A 1 39  ? 28.343 1.091   -0.186  1.00 13.46 ?  39  ALA   A HB1  1 
ATOM   1047 H  HB2  . ALA   A 1 39  ? 27.593 0.574   1.115   1.00 13.46 ?  39  ALA   A HB2  1 
ATOM   1048 H  HB3  . ALA   A 1 39  ? 27.887 -0.427  -0.083  1.00 13.46 ?  39  ALA   A HB3  1 
ATOM   1049 N  N    A ASN   A 1 40  ? 27.182 1.763   -2.539  0.58 10.56 ?  40  ASN   A N    1 
ATOM   1050 N  N    B ASN   A 1 40  ? 27.059 1.817   -2.572  0.42 9.55  ?  40  ASN   A N    1 
ATOM   1051 C  CA   A ASN   A 1 40  ? 27.749 1.709   -3.880  0.58 10.64 ?  40  ASN   A CA   1 
ATOM   1052 C  CA   B ASN   A 1 40  ? 27.499 1.769   -3.959  0.42 9.44  ?  40  ASN   A CA   1 
ATOM   1053 C  C    A ASN   A 1 40  ? 29.270 1.601   -3.784  0.58 9.68  ?  40  ASN   A C    1 
ATOM   1054 C  C    B ASN   A 1 40  ? 29.021 1.658   -3.987  0.42 9.56  ?  40  ASN   A C    1 
ATOM   1055 O  O    A ASN   A 1 40  ? 29.851 1.693   -2.700  0.58 9.70  ?  40  ASN   A O    1 
ATOM   1056 O  O    B ASN   A 1 40  ? 29.686 1.769   -2.955  0.42 9.56  ?  40  ASN   A O    1 
ATOM   1057 C  CB   A ASN   A 1 40  ? 27.301 2.898   -4.750  0.58 11.04 ?  40  ASN   A CB   1 
ATOM   1058 C  CB   B ASN   A 1 40  ? 26.982 2.973   -4.765  0.42 9.89  ?  40  ASN   A CB   1 
ATOM   1059 C  CG   A ASN   A 1 40  ? 27.667 4.248   -4.160  0.58 11.90 ?  40  ASN   A CG   1 
ATOM   1060 C  CG   B ASN   A 1 40  ? 27.400 4.302   -4.175  0.42 10.99 ?  40  ASN   A CG   1 
ATOM   1061 O  OD1  A ASN   A 1 40  ? 28.822 4.494   -3.792  0.58 12.08 ?  40  ASN   A OD1  1 
ATOM   1062 O  OD1  B ASN   A 1 40  ? 28.588 4.622   -4.109  0.42 11.47 ?  40  ASN   A OD1  1 
ATOM   1063 N  ND2  A ASN   A 1 40  ? 26.673 5.137   -4.072  0.58 12.70 ?  40  ASN   A ND2  1 
ATOM   1064 N  ND2  B ASN   A 1 40  ? 26.417 5.094   -3.758  0.42 12.10 ?  40  ASN   A ND2  1 
ATOM   1065 H  H    A ASN   A 1 40  ? 27.380 2.484   -2.120  0.58 12.67 ?  40  ASN   A H    1 
ATOM   1066 H  H    B ASN   A 1 40  ? 27.223 2.562   -2.176  0.42 11.46 ?  40  ASN   A H    1 
ATOM   1067 H  HA   A ASN   A 1 40  ? 27.445 0.902   -4.311  0.58 12.76 ?  40  ASN   A HA   1 
ATOM   1068 H  HA   B ASN   A 1 40  ? 27.132 0.965   -4.373  0.42 11.33 ?  40  ASN   A HA   1 
ATOM   1069 H  HB2  A ASN   A 1 40  ? 27.724 2.825   -5.622  0.58 13.24 ?  40  ASN   A HB2  1 
ATOM   1070 H  HB2  B ASN   A 1 40  ? 27.329 2.919   -5.666  0.42 11.86 ?  40  ASN   A HB2  1 
ATOM   1071 H  HB3  A ASN   A 1 40  ? 26.338 2.863   -4.847  0.58 13.24 ?  40  ASN   A HB3  1 
ATOM   1072 H  HB3  B ASN   A 1 40  ? 26.007 2.943   -4.786  0.42 11.86 ?  40  ASN   A HB3  1 
ATOM   1073 H  HD21 A ASN   A 1 40  ? 26.820 5.923   -3.751  0.58 15.24 ?  40  ASN   A HD21 1 
ATOM   1074 H  HD21 B ASN   A 1 40  ? 26.602 5.859   -3.415  0.42 14.52 ?  40  ASN   A HD21 1 
ATOM   1075 H  HD22 A ASN   A 1 40  ? 25.879 4.924   -4.331  0.58 15.24 ?  40  ASN   A HD22 1 
ATOM   1076 H  HD22 B ASN   A 1 40  ? 25.597 4.841   -3.830  0.42 14.52 ?  40  ASN   A HD22 1 
ATOM   1077 N  N    A VAL   A 1 41  ? 29.910 1.370   -4.933  0.58 9.44  ?  41  VAL   A N    1 
ATOM   1078 N  N    B VAL   A 1 41  ? 29.580 1.416   -5.174  0.42 10.05 ?  41  VAL   A N    1 
ATOM   1079 C  CA   A VAL   A 1 41  ? 31.336 1.059   -4.944  0.58 9.77  ?  41  VAL   A CA   1 
ATOM   1080 C  CA   B VAL   A 1 41  ? 31.002 1.089   -5.251  0.42 10.39 ?  41  VAL   A CA   1 
ATOM   1081 C  C    A VAL   A 1 41  ? 32.188 2.221   -4.466  0.58 9.91  ?  41  VAL   A C    1 
ATOM   1082 C  C    B VAL   A 1 41  ? 31.884 2.219   -4.741  0.42 10.06 ?  41  VAL   A C    1 
ATOM   1083 O  O    A VAL   A 1 41  ? 33.319 2.000   -4.011  0.58 10.66 ?  41  VAL   A O    1 
ATOM   1084 O  O    B VAL   A 1 41  ? 33.033 1.976   -4.351  0.42 10.33 ?  41  VAL   A O    1 
ATOM   1085 C  CB   A VAL   A 1 41  ? 31.825 0.554   -6.317  0.58 9.66  ?  41  VAL   A CB   1 
ATOM   1086 C  CB   B VAL   A 1 41  ? 31.425 0.654   -6.671  0.42 11.26 ?  41  VAL   A CB   1 
ATOM   1087 C  CG1  A VAL   A 1 41  ? 31.114 -0.743  -6.708  0.58 10.47 ?  41  VAL   A CG1  1 
ATOM   1088 C  CG1  B VAL   A 1 41  ? 30.765 -0.671  -7.046  0.42 12.11 ?  41  VAL   A CG1  1 
ATOM   1089 C  CG2  A VAL   A 1 41  ? 31.681 1.621   -7.409  0.58 9.65  ?  41  VAL   A CG2  1 
ATOM   1090 C  CG2  B VAL   A 1 41  ? 31.118 1.740   -7.696  0.42 11.73 ?  41  VAL   A CG2  1 
ATOM   1091 H  H    A VAL   A 1 41  ? 29.548 1.379   -5.705  0.58 11.32 ?  41  VAL   A H    1 
ATOM   1092 H  H    B VAL   A 1 41  ? 29.163 1.438   -5.925  0.42 12.05 ?  41  VAL   A H    1 
ATOM   1093 H  HA   A VAL   A 1 41  ? 31.495 0.341   -4.317  0.58 11.73 ?  41  VAL   A HA   1 
ATOM   1094 H  HA   B VAL   A 1 41  ? 31.155 0.327   -4.670  0.42 12.47 ?  41  VAL   A HA   1 
ATOM   1095 H  HB   A VAL   A 1 41  ? 32.772 0.348   -6.249  0.58 11.60 ?  41  VAL   A HB   1 
ATOM   1096 H  HB   B VAL   A 1 41  ? 32.382 0.509   -6.673  0.42 13.51 ?  41  VAL   A HB   1 
ATOM   1097 H  HG11 A VAL   A 1 41  ? 31.452 -1.052  -7.563  0.58 12.56 ?  41  VAL   A HG11 1 
ATOM   1098 H  HG11 B VAL   A 1 41  ? 31.031 -0.912  -7.947  0.42 14.53 ?  41  VAL   A HG11 1 
ATOM   1099 H  HG12 A VAL   A 1 41  ? 31.275 -1.415  -6.027  0.58 12.56 ?  41  VAL   A HG12 1 
ATOM   1100 H  HG12 B VAL   A 1 41  ? 31.056 -1.357  -6.422  0.42 14.53 ?  41  VAL   A HG12 1 
ATOM   1101 H  HG13 A VAL   A 1 41  ? 30.157 -0.572  -6.777  0.58 12.56 ?  41  VAL   A HG13 1 
ATOM   1102 H  HG13 B VAL   A 1 41  ? 29.802 -0.573  -7.000  0.42 14.53 ?  41  VAL   A HG13 1 
ATOM   1103 H  HG21 A VAL   A 1 41  ? 31.913 1.225   -8.266  0.58 11.58 ?  41  VAL   A HG21 1 
ATOM   1104 H  HG21 B VAL   A 1 41  ? 31.423 1.442   -8.568  0.42 14.07 ?  41  VAL   A HG21 1 
ATOM   1105 H  HG22 A VAL   A 1 41  ? 30.764 1.928   -7.425  0.58 11.58 ?  41  VAL   A HG22 1 
ATOM   1106 H  HG22 B VAL   A 1 41  ? 30.160 1.894   -7.718  0.42 14.07 ?  41  VAL   A HG22 1 
ATOM   1107 H  HG23 A VAL   A 1 41  ? 32.279 2.356   -7.212  0.58 11.58 ?  41  VAL   A HG23 1 
ATOM   1108 H  HG23 B VAL   A 1 41  ? 31.580 2.552   -7.442  0.42 14.07 ?  41  VAL   A HG23 1 
ATOM   1109 N  N    A TYR   A 1 42  ? 31.687 3.452   -4.567  0.58 10.52 ?  42  TYR   A N    1 
ATOM   1110 N  N    B TYR   A 1 42  ? 31.384 3.456   -4.751  0.42 10.23 ?  42  TYR   A N    1 
ATOM   1111 C  CA   A TYR   A 1 42  ? 32.422 4.639   -4.146  0.58 10.19 ?  42  TYR   A CA   1 
ATOM   1112 C  CA   B TYR   A 1 42  ? 32.152 4.623   -4.325  0.42 10.77 ?  42  TYR   A CA   1 
ATOM   1113 C  C    A TYR   A 1 42  ? 32.132 5.017   -2.704  0.58 10.00 ?  42  TYR   A C    1 
ATOM   1114 C  C    B TYR   A 1 42  ? 31.927 4.992   -2.866  0.42 10.62 ?  42  TYR   A C    1 
ATOM   1115 O  O    A TYR   A 1 42  ? 32.694 6.002   -2.204  0.58 10.63 ?  42  TYR   A O    1 
ATOM   1116 O  O    B TYR   A 1 42  ? 32.519 5.969   -2.391  0.42 11.33 ?  42  TYR   A O    1 
ATOM   1117 C  CB   A TYR   A 1 42  ? 32.098 5.822   -5.077  0.58 10.77 ?  42  TYR   A CB   1 
ATOM   1118 C  CB   B TYR   A 1 42  ? 31.806 5.831   -5.205  0.42 11.48 ?  42  TYR   A CB   1 
ATOM   1119 C  CG   A TYR   A 1 42  ? 32.298 5.487   -6.541  0.58 11.19 ?  42  TYR   A CG   1 
ATOM   1120 C  CG   B TYR   A 1 42  ? 31.975 5.552   -6.676  0.42 11.89 ?  42  TYR   A CG   1 
ATOM   1121 C  CD1  A TYR   A 1 42  ? 33.570 5.278   -7.055  0.58 12.02 ?  42  TYR   A CD1  1 
ATOM   1122 C  CD1  B TYR   A 1 42  ? 33.233 5.334   -7.217  0.42 11.77 ?  42  TYR   A CD1  1 
ATOM   1123 C  CD2  A TYR   A 1 42  ? 31.217 5.343   -7.403  0.58 12.28 ?  42  TYR   A CD2  1 
ATOM   1124 C  CD2  B TYR   A 1 42  ? 30.877 5.489   -7.522  0.42 13.32 ?  42  TYR   A CD2  1 
ATOM   1125 C  CE1  A TYR   A 1 42  ? 33.761 4.948   -8.387  0.58 12.81 ?  42  TYR   A CE1  1 
ATOM   1126 C  CE1  B TYR   A 1 42  ? 33.394 5.063   -8.561  0.42 12.21 ?  42  TYR   A CE1  1 
ATOM   1127 C  CE2  A TYR   A 1 42  ? 31.401 5.022   -8.738  0.58 13.38 ?  42  TYR   A CE2  1 
ATOM   1128 C  CE2  B TYR   A 1 42  ? 31.028 5.229   -8.868  0.42 13.75 ?  42  TYR   A CE2  1 
ATOM   1129 C  CZ   A TYR   A 1 42  ? 32.678 4.828   -9.223  0.58 13.18 ?  42  TYR   A CZ   1 
ATOM   1130 C  CZ   B TYR   A 1 42  ? 32.289 5.016   -9.384  0.42 13.23 ?  42  TYR   A CZ   1 
ATOM   1131 O  OH   A TYR   A 1 42  ? 32.867 4.496   -10.545 0.58 14.31 ?  42  TYR   A OH   1 
ATOM   1132 O  OH   B TYR   A 1 42  ? 32.442 4.751   -10.725 0.42 14.09 ?  42  TYR   A OH   1 
ATOM   1133 H  H    A TYR   A 1 42  ? 30.905 3.626   -4.874  0.58 12.62 ?  42  TYR   A H    1 
ATOM   1134 H  H    B TYR   A 1 42  ? 30.589 3.647   -5.020  0.42 12.27 ?  42  TYR   A H    1 
ATOM   1135 H  HA   A TYR   A 1 42  ? 33.373 4.469   -4.220  0.58 12.23 ?  42  TYR   A HA   1 
ATOM   1136 H  HA   B TYR   A 1 42  ? 33.094 4.438   -4.447  0.42 12.93 ?  42  TYR   A HA   1 
ATOM   1137 H  HB2  A TYR   A 1 42  ? 31.170 6.080   -4.954  0.58 12.92 ?  42  TYR   A HB2  1 
ATOM   1138 H  HB2  B TYR   A 1 42  ? 30.880 6.082   -5.052  0.42 13.78 ?  42  TYR   A HB2  1 
ATOM   1139 H  HB3  A TYR   A 1 42  ? 32.679 6.570   -4.861  0.58 12.92 ?  42  TYR   A HB3  1 
ATOM   1140 H  HB3  B TYR   A 1 42  ? 32.390 6.572   -4.971  0.42 13.78 ?  42  TYR   A HB3  1 
ATOM   1141 H  HD1  A TYR   A 1 42  ? 34.310 5.360   -6.495  0.58 14.42 ?  42  TYR   A HD1  1 
ATOM   1142 H  HD1  B TYR   A 1 42  ? 33.981 5.366   -6.660  0.42 14.12 ?  42  TYR   A HD1  1 
ATOM   1143 H  HD2  A TYR   A 1 42  ? 30.353 5.481   -7.081  0.58 14.73 ?  42  TYR   A HD2  1 
ATOM   1144 H  HD2  B TYR   A 1 42  ? 30.025 5.637   -7.176  0.42 15.99 ?  42  TYR   A HD2  1 
ATOM   1145 H  HE1  A TYR   A 1 42  ? 34.622 4.821   -8.720  0.58 15.37 ?  42  TYR   A HE1  1 
ATOM   1146 H  HE1  B TYR   A 1 42  ? 34.246 4.920   -8.907  0.42 14.65 ?  42  TYR   A HE1  1 
ATOM   1147 H  HE2  A TYR   A 1 42  ? 30.664 4.942   -9.307  0.58 16.05 ?  42  TYR   A HE2  1 
ATOM   1148 H  HE2  B TYR   A 1 42  ? 30.285 5.193   -9.423  0.42 16.50 ?  42  TYR   A HE2  1 
ATOM   1149 H  HH   A TYR   A 1 42  ? 33.680 4.364   -10.698 0.58 17.18 ?  42  TYR   A HH   1 
ATOM   1150 H  HH   B TYR   A 1 42  ? 31.698 4.752   -11.103 0.42 16.91 ?  42  TYR   A HH   1 
ATOM   1151 N  N    A LEU   A 1 43  ? 31.275 4.256   -2.030  0.58 9.87  ?  43  LEU   A N    1 
ATOM   1152 N  N    B LEU   A 1 43  ? 31.084 4.247   -2.154  0.42 10.59 ?  43  LEU   A N    1 
ATOM   1153 C  CA   A LEU   A 1 43  ? 30.813 4.593   -0.690  0.58 9.65  ?  43  LEU   A CA   1 
ATOM   1154 C  CA   B LEU   A 1 43  ? 30.676 4.593   -0.793  0.42 10.42 ?  43  LEU   A CA   1 
ATOM   1155 C  C    A LEU   A 1 43  ? 30.342 6.044   -0.607  0.58 9.94  ?  43  LEU   A C    1 
ATOM   1156 C  C    B LEU   A 1 43  ? 30.188 6.037   -0.692  0.42 10.55 ?  43  LEU   A C    1 
ATOM   1157 O  O    A LEU   A 1 43  ? 30.637 6.764   0.350   0.58 11.09 ?  43  LEU   A O    1 
ATOM   1158 O  O    B LEU   A 1 43  ? 30.407 6.721   0.311   0.42 10.73 ?  43  LEU   A O    1 
ATOM   1159 C  CB   A LEU   A 1 43  ? 31.857 4.287   0.382   0.58 10.56 ?  43  LEU   A CB   1 
ATOM   1160 C  CB   B LEU   A 1 43  ? 31.761 4.298   0.243   0.42 10.67 ?  43  LEU   A CB   1 
ATOM   1161 C  CG   A LEU   A 1 43  ? 32.371 2.843   0.460   0.58 11.02 ?  43  LEU   A CG   1 
ATOM   1162 C  CG   B LEU   A 1 43  ? 32.201 2.837   0.388   0.42 10.87 ?  43  LEU   A CG   1 
ATOM   1163 C  CD1  A LEU   A 1 43  ? 33.443 2.745   1.537   0.58 11.52 ?  43  LEU   A CD1  1 
ATOM   1164 C  CD1  B LEU   A 1 43  ? 33.201 2.719   1.532   0.42 11.39 ?  43  LEU   A CD1  1 
ATOM   1165 C  CD2  A LEU   A 1 43  ? 31.258 1.839   0.721   0.58 11.20 ?  43  LEU   A CD2  1 
ATOM   1166 C  CD2  B LEU   A 1 43  ? 31.015 1.900   0.600   0.42 11.20 ?  43  LEU   A CD2  1 
ATOM   1167 H  H    A LEU   A 1 43  ? 30.938 3.524   -2.335  0.58 11.84 ?  43  LEU   A H    1 
ATOM   1168 H  H    B LEU   A 1 43  ? 30.729 3.519   -2.442  0.42 12.71 ?  43  LEU   A H    1 
ATOM   1169 H  HA   A LEU   A 1 43  ? 30.040 4.035   -0.495  0.58 11.58 ?  43  LEU   A HA   1 
ATOM   1170 H  HA   B LEU   A 1 43  ? 29.916 4.038   -0.569  0.42 12.50 ?  43  LEU   A HA   1 
ATOM   1171 H  HB2  A LEU   A 1 43  ? 32.622 4.860   0.231   0.58 12.67 ?  43  LEU   A HB2  1 
ATOM   1172 H  HB2  B LEU   A 1 43  ? 32.547 4.815   0.018   0.42 12.81 ?  43  LEU   A HB2  1 
ATOM   1173 H  HB3  A LEU   A 1 43  ? 31.464 4.495   1.246   0.58 12.67 ?  43  LEU   A HB3  1 
ATOM   1174 H  HB3  B LEU   A 1 43  ? 31.429 4.581   1.112   0.42 12.81 ?  43  LEU   A HB3  1 
ATOM   1175 H  HG   A LEU   A 1 43  ? 32.784 2.614   -0.387  0.58 13.23 ?  43  LEU   A HG   1 
ATOM   1176 H  HG   B LEU   A 1 43  ? 32.653 2.567   -0.425  0.42 13.05 ?  43  LEU   A HG   1 
ATOM   1177 H  HD11 A LEU   A 1 43  ? 33.764 1.832   1.579   0.58 13.82 ?  43  LEU   A HD11 1 
ATOM   1178 H  HD11 B LEU   A 1 43  ? 33.478 1.794   1.615   0.42 13.67 ?  43  LEU   A HD11 1 
ATOM   1179 H  HD12 A LEU   A 1 43  ? 34.172 3.344   1.310   0.58 13.82 ?  43  LEU   A HD12 1 
ATOM   1180 H  HD12 B LEU   A 1 43  ? 33.971 3.279   1.338   0.42 13.67 ?  43  LEU   A HD12 1 
ATOM   1181 H  HD13 A LEU   A 1 43  ? 33.057 3.002   2.389   0.58 13.82 ?  43  LEU   A HD13 1 
ATOM   1182 H  HD13 B LEU   A 1 43  ? 32.778 3.014   2.353   0.42 13.67 ?  43  LEU   A HD13 1 
ATOM   1183 H  HD21 A LEU   A 1 43  ? 31.647 0.955   0.817   0.58 13.44 ?  43  LEU   A HD21 1 
ATOM   1184 H  HD21 B LEU   A 1 43  ? 31.348 1.020   0.835   0.42 13.44 ?  43  LEU   A HD21 1 
ATOM   1185 H  HD22 A LEU   A 1 43  ? 30.794 2.086   1.536   0.58 13.44 ?  43  LEU   A HD22 1 
ATOM   1186 H  HD22 B LEU   A 1 43  ? 30.461 2.248   1.315   0.42 13.44 ?  43  LEU   A HD22 1 
ATOM   1187 H  HD23 A LEU   A 1 43  ? 30.642 1.849   -0.028  0.58 13.44 ?  43  LEU   A HD23 1 
ATOM   1188 H  HD23 B LEU   A 1 43  ? 30.504 1.851   -0.223  0.42 13.44 ?  43  LEU   A HD23 1 
ATOM   1189 N  N    A LYS   A 1 44  ? 29.591 6.474   -1.624  0.58 10.03 ?  44  LYS   A N    1 
ATOM   1190 N  N    B LYS   A 1 44  ? 29.491 6.495   -1.730  0.42 10.59 ?  44  LYS   A N    1 
ATOM   1191 C  CA   A LYS   A 1 44  ? 28.945 7.782   -1.632  0.58 10.56 ?  44  LYS   A CA   1 
ATOM   1192 C  CA   B LYS   A 1 44  ? 28.855 7.812   -1.723  0.42 10.88 ?  44  LYS   A CA   1 
ATOM   1193 C  C    A LYS   A 1 44  ? 27.513 7.582   -1.150  0.58 10.32 ?  44  LYS   A C    1 
ATOM   1194 C  C    B LYS   A 1 44  ? 27.443 7.648   -1.185  0.42 9.96  ?  44  LYS   A C    1 
ATOM   1195 O  O    A LYS   A 1 44  ? 26.673 7.028   -1.868  0.58 11.23 ?  44  LYS   A O    1 
ATOM   1196 O  O    B LYS   A 1 44  ? 26.534 7.217   -1.900  0.42 10.44 ?  44  LYS   A O    1 
ATOM   1197 C  CB   A LYS   A 1 44  ? 28.992 8.413   -3.019  0.58 12.57 ?  44  LYS   A CB   1 
ATOM   1198 C  CB   B LYS   A 1 44  ? 28.854 8.418   -3.122  0.42 13.39 ?  44  LYS   A CB   1 
ATOM   1199 C  CG   A LYS   A 1 44  ? 30.385 8.832   -3.461  0.58 15.61 ?  44  LYS   A CG   1 
ATOM   1200 C  CG   B LYS   A 1 44  ? 30.205 8.957   -3.561  0.42 16.58 ?  44  LYS   A CG   1 
ATOM   1201 C  CD   A LYS   A 1 44  ? 31.031 9.809   -2.481  0.58 20.36 ?  44  LYS   A CD   1 
ATOM   1202 C  CD   B LYS   A 1 44  ? 30.955 9.579   -2.392  0.42 20.12 ?  44  LYS   A CD   1 
ATOM   1203 C  CE   A LYS   A 1 44  ? 32.384 10.280  -2.981  0.58 23.25 ?  44  LYS   A CE   1 
ATOM   1204 C  CE   B LYS   A 1 44  ? 32.043 10.523  -2.849  0.42 21.91 ?  44  LYS   A CE   1 
ATOM   1205 N  NZ   A LYS   A 1 44  ? 33.175 10.935  -1.904  0.58 24.70 ?  44  LYS   A NZ   1 
ATOM   1206 N  NZ   B LYS   A 1 44  ? 32.974 10.855  -1.737  0.42 23.02 ?  44  LYS   A NZ   1 
ATOM   1207 H  H    A LYS   A 1 44  ? 29.440 6.016   -2.337  0.58 12.04 ?  44  LYS   A H    1 
ATOM   1208 H  H    B LYS   A 1 44  ? 29.378 6.062   -2.464  0.42 12.70 ?  44  LYS   A H    1 
ATOM   1209 H  HA   A LYS   A 1 44  ? 29.389 8.368   -0.999  0.58 12.67 ?  44  LYS   A HA   1 
ATOM   1210 H  HA   B LYS   A 1 44  ? 29.312 8.389   -1.094  0.42 13.06 ?  44  LYS   A HA   1 
ATOM   1211 H  HB2  A LYS   A 1 44  ? 28.657 7.775   -3.665  0.58 15.08 ?  44  LYS   A HB2  1 
ATOM   1212 H  HB2  B LYS   A 1 44  ? 28.586 7.735   -3.759  0.42 16.07 ?  44  LYS   A HB2  1 
ATOM   1213 H  HB3  A LYS   A 1 44  ? 28.432 9.208   -3.021  0.58 15.08 ?  44  LYS   A HB3  1 
ATOM   1214 H  HB3  B LYS   A 1 44  ? 28.220 9.153   -3.147  0.42 16.07 ?  44  LYS   A HB3  1 
ATOM   1215 H  HG2  A LYS   A 1 44  ? 30.952 8.048   -3.522  0.58 18.73 ?  44  LYS   A HG2  1 
ATOM   1216 H  HG2  B LYS   A 1 44  ? 30.739 8.231   -3.920  0.42 19.89 ?  44  LYS   A HG2  1 
ATOM   1217 H  HG3  A LYS   A 1 44  ? 30.329 9.272   -4.326  0.58 18.73 ?  44  LYS   A HG3  1 
ATOM   1218 H  HG3  B LYS   A 1 44  ? 30.073 9.643   -4.237  0.42 19.89 ?  44  LYS   A HG3  1 
ATOM   1219 H  HD2  A LYS   A 1 44  ? 30.451 10.577  -2.369  0.58 24.43 ?  44  LYS   A HD2  1 
ATOM   1220 H  HD2  B LYS   A 1 44  ? 30.329 10.086  -1.847  0.42 24.14 ?  44  LYS   A HD2  1 
ATOM   1221 H  HD3  A LYS   A 1 44  ? 31.167 9.362   -1.629  0.58 24.43 ?  44  LYS   A HD3  1 
ATOM   1222 H  HD3  B LYS   A 1 44  ? 31.361 8.870   -1.861  0.42 24.14 ?  44  LYS   A HD3  1 
ATOM   1223 H  HE2  A LYS   A 1 44  ? 32.887 9.518   -3.305  0.58 27.90 ?  44  LYS   A HE2  1 
ATOM   1224 H  HE2  B LYS   A 1 44  ? 32.551 10.103  -3.559  0.42 26.29 ?  44  LYS   A HE2  1 
ATOM   1225 H  HE3  A LYS   A 1 44  ? 32.250 10.923  -3.694  0.58 27.90 ?  44  LYS   A HE3  1 
ATOM   1226 H  HE3  B LYS   A 1 44  ? 31.636 11.345  -3.164  0.42 26.29 ?  44  LYS   A HE3  1 
ATOM   1227 H  HZ1  A LYS   A 1 44  ? 33.959 11.204  -2.223  0.58 29.64 ?  44  LYS   A HZ1  1 
ATOM   1228 H  HZ1  B LYS   A 1 44  ? 33.604 11.413  -2.027  0.42 27.63 ?  44  LYS   A HZ1  1 
ATOM   1229 H  HZ2  A LYS   A 1 44  ? 32.732 11.644  -1.591  0.58 29.64 ?  44  LYS   A HZ2  1 
ATOM   1230 H  HZ2  B LYS   A 1 44  ? 32.527 11.245  -1.072  0.42 27.63 ?  44  LYS   A HZ2  1 
ATOM   1231 H  HZ3  A LYS   A 1 44  ? 33.312 10.365  -1.236  0.58 29.64 ?  44  LYS   A HZ3  1 
ATOM   1232 H  HZ3  B LYS   A 1 44  ? 33.359 10.115  -1.431  0.42 27.63 ?  44  LYS   A HZ3  1 
ATOM   1233 N  N    . HIS   A 1 45  ? 27.258 7.990   0.088   1.00 9.94  ?  45  HIS   A N    1 
ATOM   1234 C  CA   . HIS   A 1 45  ? 26.022 7.660   0.787   1.00 9.98  ?  45  HIS   A CA   1 
ATOM   1235 C  C    . HIS   A 1 45  ? 25.001 8.786   0.620   1.00 10.93 ?  45  HIS   A C    1 
ATOM   1236 O  O    . HIS   A 1 45  ? 24.729 9.565   1.530   1.00 12.44 ?  45  HIS   A O    1 
ATOM   1237 C  CB   . HIS   A 1 45  ? 26.319 7.413   2.255   1.00 9.99  ?  45  HIS   A CB   1 
ATOM   1238 C  CG   . HIS   A 1 45  ? 27.429 6.443   2.488   1.00 9.73  ?  45  HIS   A CG   1 
ATOM   1239 N  ND1  . HIS   A 1 45  ? 27.425 5.157   1.985   1.00 10.13 ?  45  HIS   A ND1  1 
ATOM   1240 C  CD2  . HIS   A 1 45  ? 28.593 6.594   3.166   1.00 10.11 ?  45  HIS   A CD2  1 
ATOM   1241 C  CE1  . HIS   A 1 45  ? 28.547 4.560   2.361   1.00 9.98  ?  45  HIS   A CE1  1 
ATOM   1242 N  NE2  . HIS   A 1 45  ? 29.272 5.408   3.073   1.00 10.10 ?  45  HIS   A NE2  1 
ATOM   1243 H  H    A HIS   A 1 45  ? 27.796 8.469   0.560   0.58 11.92 ?  45  HIS   A H    1 
ATOM   1244 H  H    B HIS   A 1 45  ? 27.827 8.419   0.571   0.42 11.92 ?  45  HIS   A H    1 
ATOM   1245 H  HA   . HIS   A 1 45  ? 25.639 6.851   0.411   1.00 11.98 ?  45  HIS   A HA   1 
ATOM   1246 H  HB2  . HIS   A 1 45  ? 26.549 8.253   2.675   1.00 11.99 ?  45  HIS   A HB2  1 
ATOM   1247 H  HB3  . HIS   A 1 45  ? 25.512 7.052   2.678   1.00 11.99 ?  45  HIS   A HB3  1 
ATOM   1248 H  HD2  . HIS   A 1 45  ? 28.878 7.362   3.613   1.00 12.13 ?  45  HIS   A HD2  1 
ATOM   1249 H  HE1  . HIS   A 1 45  ? 28.783 3.685   2.161   1.00 11.98 ?  45  HIS   A HE1  1 
ATOM   1250 H  HE2  . HIS   A 1 45  ? 30.039 5.240   3.425   1.00 12.12 ?  45  HIS   A HE2  1 
ATOM   1251 N  N    A GLY   A 1 46  ? 24.436 8.857   -0.581  0.58 11.56 ?  46  GLY   A N    1 
ATOM   1252 N  N    B GLY   A 1 46  ? 24.386 8.840   -0.557  0.42 11.03 ?  46  GLY   A N    1 
ATOM   1253 C  CA   A GLY   A 1 46  ? 23.639 10.008  -0.960  0.58 12.08 ?  46  GLY   A CA   1 
ATOM   1254 C  CA   B GLY   A 1 46  ? 23.529 9.969   -0.878  0.42 10.98 ?  46  GLY   A CA   1 
ATOM   1255 C  C    A GLY   A 1 46  ? 22.149 9.875   -0.728  0.58 11.79 ?  46  GLY   A C    1 
ATOM   1256 C  C    B GLY   A 1 46  ? 22.079 9.852   -0.445  0.42 10.72 ?  46  GLY   A C    1 
ATOM   1257 O  O    A GLY   A 1 46  ? 21.468 10.866  -0.441  0.58 12.30 ?  46  GLY   A O    1 
ATOM   1258 O  O    B GLY   A 1 46  ? 21.487 10.828  0.028   0.42 11.26 ?  46  GLY   A O    1 
ATOM   1259 H  H    A GLY   A 1 46  ? 24.493 8.251   -1.185  0.58 13.87 ?  46  GLY   A H    1 
ATOM   1260 H  H    B GLY   A 1 46  ? 24.437 8.243   -1.172  0.42 13.24 ?  46  GLY   A H    1 
ATOM   1261 H  HA2  A GLY   A 1 46  ? 23.956 10.784  -0.469  0.58 14.49 ?  46  GLY   A HA2  1 
ATOM   1262 H  HA2  B GLY   A 1 46  ? 23.893 10.765  -0.455  0.42 13.18 ?  46  GLY   A HA2  1 
ATOM   1263 H  HA3  A GLY   A 1 46  ? 23.768 10.178  -1.904  0.58 14.49 ?  46  GLY   A HA3  1 
ATOM   1264 H  HA3  B GLY   A 1 46  ? 23.548 10.111  -1.836  0.42 13.18 ?  46  GLY   A HA3  1 
ATOM   1265 N  N    A GLY   A 1 47  ? 21.629 8.661   -0.866  0.58 11.37 ?  47  GLY   A N    1 
ATOM   1266 N  N    B GLY   A 1 47  ? 21.493 8.673   -0.606  0.42 10.81 ?  47  GLY   A N    1 
ATOM   1267 C  CA   A GLY   A 1 47  ? 20.198 8.443   -0.800  0.58 11.06 ?  47  GLY   A CA   1 
ATOM   1268 C  CA   B GLY   A 1 47  ? 20.077 8.503   -0.361  0.42 10.77 ?  47  GLY   A CA   1 
ATOM   1269 C  C    A GLY   A 1 47  ? 19.894 7.012   -0.411  0.58 10.67 ?  47  GLY   A C    1 
ATOM   1270 C  C    B GLY   A 1 47  ? 19.734 7.060   -0.061  0.42 10.09 ?  47  GLY   A C    1 
ATOM   1271 O  O    A GLY   A 1 47  ? 20.794 6.202   -0.185  0.58 10.95 ?  47  GLY   A O    1 
ATOM   1272 O  O    B GLY   A 1 47  ? 20.612 6.204   0.060   0.42 10.29 ?  47  GLY   A O    1 
ATOM   1273 H  H    A GLY   A 1 47  ? 22.086 7.944   -0.991  0.58 13.65 ?  47  GLY   A H    1 
ATOM   1274 H  H    B GLY   A 1 47  ? 21.901 7.960   -0.848  0.42 12.97 ?  47  GLY   A H    1 
ATOM   1275 H  HA2  A GLY   A 1 47  ? 19.799 9.041   -0.150  0.58 13.27 ?  47  GLY   A HA2  1 
ATOM   1276 H  HA2  B GLY   A 1 47  ? 19.806 9.048   0.394   0.42 12.92 ?  47  GLY   A HA2  1 
ATOM   1277 H  HA3  A GLY   A 1 47  ? 19.806 8.616   -1.670  0.58 13.27 ?  47  GLY   A HA3  1 
ATOM   1278 H  HA3  B GLY   A 1 47  ? 19.573 8.790   -1.142  0.42 12.92 ?  47  GLY   A HA3  1 
ATOM   1279 N  N    A GLY   A 1 48  ? 18.602 6.700   -0.349  0.58 10.75 ?  48  GLY   A N    1 
ATOM   1280 N  N    B GLY   A 1 48  ? 18.433 6.795   0.051   0.42 10.41 ?  48  GLY   A N    1 
ATOM   1281 C  CA   A GLY   A 1 48  ? 18.206 5.371   0.066   0.58 11.35 ?  48  GLY   A CA   1 
ATOM   1282 C  CA   B GLY   A 1 48  ? 17.995 5.463   0.432   0.42 10.09 ?  48  GLY   A CA   1 
ATOM   1283 C  C    A GLY   A 1 48  ? 18.664 5.079   1.481   0.58 10.89 ?  48  GLY   A C    1 
ATOM   1284 C  C    B GLY   A 1 48  ? 18.589 5.051   1.762   0.42 10.12 ?  48  GLY   A C    1 
ATOM   1285 O  O    A GLY   A 1 48  ? 18.871 5.980   2.305   0.58 10.87 ?  48  GLY   A O    1 
ATOM   1286 O  O    B GLY   A 1 48  ? 18.764 5.865   2.677   0.42 10.30 ?  48  GLY   A O    1 
ATOM   1287 H  H    A GLY   A 1 48  ? 17.952 7.228   -0.531  0.58 12.90 ?  48  GLY   A H    1 
ATOM   1288 H  H    B GLY   A 1 48  ? 17.792 7.353   -0.091  0.42 12.49 ?  48  GLY   A H    1 
ATOM   1289 H  HA2  A GLY   A 1 48  ? 17.243 5.281   0.023   0.58 13.62 ?  48  GLY   A HA2  1 
ATOM   1290 H  HA2  B GLY   A 1 48  ? 17.029 5.441   0.507   0.42 12.11 ?  48  GLY   A HA2  1 
ATOM   1291 H  HA3  A GLY   A 1 48  ? 18.609 4.709   -0.516  0.58 13.62 ?  48  GLY   A HA3  1 
ATOM   1292 H  HA3  B GLY   A 1 48  ? 18.269 4.821   -0.246  0.42 12.11 ?  48  GLY   A HA3  1 
ATOM   1293 N  N    A VAL   A 1 49  ? 18.845 3.786   1.765   0.58 10.90 ?  49  VAL   A N    1 
ATOM   1294 N  N    B VAL   A 1 49  ? 18.917 3.762   1.868   0.42 9.88  ?  49  VAL   A N    1 
ATOM   1295 C  CA   A VAL   A 1 49  ? 19.342 3.369   3.074   0.58 10.83 ?  49  VAL   A CA   1 
ATOM   1296 C  CA   B VAL   A 1 49  ? 19.532 3.238   3.085   0.42 9.59  ?  49  VAL   A CA   1 
ATOM   1297 C  C    A VAL   A 1 49  ? 20.649 4.072   3.412   0.58 10.19 ?  49  VAL   A C    1 
ATOM   1298 C  C    B VAL   A 1 49  ? 20.798 4.013   3.426   0.42 8.91  ?  49  VAL   A C    1 
ATOM   1299 O  O    A VAL   A 1 49  ? 20.857 4.506   4.550   0.58 10.62 ?  49  VAL   A O    1 
ATOM   1300 O  O    B VAL   A 1 49  ? 20.995 4.440   4.569   0.42 9.16  ?  49  VAL   A O    1 
ATOM   1301 C  CB   A VAL   A 1 49  ? 19.495 1.835   3.117   0.58 11.17 ?  49  VAL   A CB   1 
ATOM   1302 C  CB   B VAL   A 1 49  ? 19.824 1.733   2.931   0.42 9.47  ?  49  VAL   A CB   1 
ATOM   1303 C  CG1  A VAL   A 1 49  ? 20.286 1.403   4.350   0.58 10.98 ?  49  VAL   A CG1  1 
ATOM   1304 C  CG1  B VAL   A 1 49  ? 20.704 1.247   4.082   0.42 9.38  ?  49  VAL   A CG1  1 
ATOM   1305 C  CG2  A VAL   A 1 49  ? 18.130 1.164   3.095   0.58 13.04 ?  49  VAL   A CG2  1 
ATOM   1306 C  CG2  B VAL   A 1 49  ? 18.530 0.930   2.858   0.42 9.71  ?  49  VAL   A CG2  1 
ATOM   1307 H  H    A VAL   A 1 49  ? 18.690 3.134   1.225   0.58 13.08 ?  49  VAL   A H    1 
ATOM   1308 H  H    B VAL   A 1 49  ? 18.799 3.176   1.253   0.42 11.85 ?  49  VAL   A H    1 
ATOM   1309 H  HA   A VAL   A 1 49  ? 18.693 3.608   3.754   0.58 13.00 ?  49  VAL   A HA   1 
ATOM   1310 H  HA   B VAL   A 1 49  ? 18.913 3.340   3.825   0.42 11.51 ?  49  VAL   A HA   1 
ATOM   1311 H  HB   A VAL   A 1 49  ? 19.992 1.539   2.335   0.58 13.40 ?  49  VAL   A HB   1 
ATOM   1312 H  HB   B VAL   A 1 49  ? 20.309 1.586   2.103   0.42 11.36 ?  49  VAL   A HB   1 
ATOM   1313 H  HG11 A VAL   A 1 49  ? 20.135 0.458   4.506   0.58 13.18 ?  49  VAL   A HG11 1 
ATOM   1314 H  HG11 B VAL   A 1 49  ? 20.630 0.283   4.155   0.42 11.26 ?  49  VAL   A HG11 1 
ATOM   1315 H  HG12 A VAL   A 1 49  ? 21.230 1.564   4.198   0.58 13.18 ?  49  VAL   A HG12 1 
ATOM   1316 H  HG12 B VAL   A 1 49  ? 21.629 1.490   3.903   0.42 11.26 ?  49  VAL   A HG12 1 
ATOM   1317 H  HG13 A VAL   A 1 49  ? 19.978 1.916   5.114   0.58 13.18 ?  49  VAL   A HG13 1 
ATOM   1318 H  HG13 B VAL   A 1 49  ? 20.407 1.663   4.906   0.42 11.26 ?  49  VAL   A HG13 1 
ATOM   1319 H  HG21 A VAL   A 1 49  ? 18.249 0.201   3.119   0.58 15.64 ?  49  VAL   A HG21 1 
ATOM   1320 H  HG21 B VAL   A 1 49  ? 18.740 -0.011  2.748   0.42 11.65 ?  49  VAL   A HG21 1 
ATOM   1321 H  HG22 A VAL   A 1 49  ? 17.626 1.456   3.869   0.58 15.64 ?  49  VAL   A HG22 1 
ATOM   1322 H  HG22 B VAL   A 1 49  ? 18.029 1.060   3.682   0.42 11.65 ?  49  VAL   A HG22 1 
ATOM   1323 H  HG23 A VAL   A 1 49  ? 17.672 1.421   2.281   0.58 15.64 ?  49  VAL   A HG23 1 
ATOM   1324 H  HG23 B VAL   A 1 49  ? 18.005 1.242   2.103   0.42 11.65 ?  49  VAL   A HG23 1 
ATOM   1325 N  N    A ALA   A 1 50  ? 21.560 4.163   2.440   0.58 9.71  ?  50  ALA   A N    1 
ATOM   1326 N  N    B ALA   A 1 50  ? 21.692 4.170   2.447   0.42 8.88  ?  50  ALA   A N    1 
ATOM   1327 C  CA   A ALA   A 1 50  ? 22.885 4.717   2.709   0.58 9.51  ?  50  ALA   A CA   1 
ATOM   1328 C  CA   B ALA   A 1 50  ? 22.999 4.756   2.725   0.42 9.21  ?  50  ALA   A CA   1 
ATOM   1329 C  C    A ALA   A 1 50  ? 22.796 6.176   3.133   0.58 9.52  ?  50  ALA   A C    1 
ATOM   1330 C  C    B ALA   A 1 50  ? 22.871 6.211   3.153   0.42 9.33  ?  50  ALA   A C    1 
ATOM   1331 O  O    A ALA   A 1 50  ? 23.429 6.592   4.111   0.58 9.83  ?  50  ALA   A O    1 
ATOM   1332 O  O    B ALA   A 1 50  ? 23.495 6.639   4.130   0.42 9.59  ?  50  ALA   A O    1 
ATOM   1333 C  CB   A ALA   A 1 50  ? 23.758 4.581   1.466   0.58 9.69  ?  50  ALA   A CB   1 
ATOM   1334 C  CB   B ALA   A 1 50  ? 23.896 4.636   1.496   0.42 9.21  ?  50  ALA   A CB   1 
ATOM   1335 H  H    A ALA   A 1 50  ? 21.437 3.901   1.629   0.58 11.65 ?  50  ALA   A H    1 
ATOM   1336 H  H    B ALA   A 1 50  ? 21.565 3.938   1.627   0.42 10.66 ?  50  ALA   A H    1 
ATOM   1337 H  HA   A ALA   A 1 50  ? 23.299 4.220   3.431   0.58 11.41 ?  50  ALA   A HA   1 
ATOM   1338 H  HA   B ALA   A 1 50  ? 23.417 4.267   3.451   0.42 11.05 ?  50  ALA   A HA   1 
ATOM   1339 H  HB1  A ALA   A 1 50  ? 24.631 4.955   1.656   0.58 11.63 ?  50  ALA   A HB1  1 
ATOM   1340 H  HB1  B ALA   A 1 50  ? 24.757 5.034   1.696   0.42 11.06 ?  50  ALA   A HB1  1 
ATOM   1341 H  HB2  A ALA   A 1 50  ? 23.839 3.643   1.236   0.58 11.63 ?  50  ALA   A HB2  1 
ATOM   1342 H  HB2  B ALA   A 1 50  ? 24.008 3.698   1.273   0.42 11.06 ?  50  ALA   A HB2  1 
ATOM   1343 H  HB3  A ALA   A 1 50  ? 23.341 5.066   0.736   0.58 11.63 ?  50  ALA   A HB3  1 
ATOM   1344 H  HB3  B ALA   A 1 50  ? 23.480 5.104   0.755   0.42 11.06 ?  50  ALA   A HB3  1 
ATOM   1345 N  N    A GLY   A 1 51  ? 22.022 6.971   2.398   0.58 9.72  ?  51  GLY   A N    1 
ATOM   1346 N  N    B GLY   A 1 51  ? 22.075 6.989   2.424   0.42 9.44  ?  51  GLY   A N    1 
ATOM   1347 C  CA   A GLY   A 1 51  ? 21.866 8.363   2.774   0.58 10.14 ?  51  GLY   A CA   1 
ATOM   1348 C  CA   B GLY   A 1 51  ? 21.891 8.377   2.802   0.42 9.70  ?  51  GLY   A CA   1 
ATOM   1349 C  C    A GLY   A 1 51  ? 21.262 8.515   4.156   0.58 9.84  ?  51  GLY   A C    1 
ATOM   1350 C  C    B GLY   A 1 51  ? 21.266 8.518   4.175   0.42 9.71  ?  51  GLY   A C    1 
ATOM   1351 O  O    A GLY   A 1 51  ? 21.651 9.405   4.921   0.58 10.57 ?  51  GLY   A O    1 
ATOM   1352 O  O    B GLY   A 1 51  ? 21.640 9.402   4.951   0.42 10.34 ?  51  GLY   A O    1 
ATOM   1353 H  H    A GLY   A 1 51  ? 21.591 6.730   1.688   0.58 11.67 ?  51  GLY   A H    1 
ATOM   1354 H  H    B GLY   A 1 51  ? 21.644 6.737   1.721   0.42 11.33 ?  51  GLY   A H    1 
ATOM   1355 H  HA2  A GLY   A 1 51  ? 22.731 8.798   2.766   0.58 12.17 ?  51  GLY   A HA2  1 
ATOM   1356 H  HA2  B GLY   A 1 51  ? 22.750 8.824   2.806   0.42 11.64 ?  51  GLY   A HA2  1 
ATOM   1357 H  HA3  A GLY   A 1 51  ? 21.290 8.808   2.132   0.58 12.17 ?  51  GLY   A HA3  1 
ATOM   1358 H  HA3  B GLY   A 1 51  ? 21.317 8.813   2.154   0.42 11.64 ?  51  GLY   A HA3  1 
ATOM   1359 N  N    . ALA   A 1 52  ? 20.307 7.647   4.495   1.00 9.92  ?  52  ALA   A N    1 
ATOM   1360 C  CA   . ALA   A 1 52  ? 19.645 7.719   5.792   1.00 10.66 ?  52  ALA   A CA   1 
ATOM   1361 C  C    . ALA   A 1 52  ? 20.586 7.305   6.923   1.00 9.89  ?  52  ALA   A C    1 
ATOM   1362 O  O    . ALA   A 1 52  ? 20.659 7.974   7.959   1.00 10.85 ?  52  ALA   A O    1 
ATOM   1363 C  CB   . ALA   A 1 52  ? 18.378 6.861   5.769   1.00 11.89 ?  52  ALA   A CB   1 
ATOM   1364 H  H    A ALA   A 1 52  ? 20.033 7.001   3.991   0.58 11.91 ?  52  ALA   A H    1 
ATOM   1365 H  H    B ALA   A 1 52  ? 20.032 7.007   3.984   0.42 11.91 ?  52  ALA   A H    1 
ATOM   1366 H  HA   . ALA   A 1 52  ? 19.376 8.632   5.952   1.00 12.79 ?  52  ALA   A HA   1 
ATOM   1367 H  HB1  . ALA   A 1 52  ? 17.919 6.950   6.621   1.00 14.26 ?  52  ALA   A HB1  1 
ATOM   1368 H  HB2  . ALA   A 1 52  ? 17.800 7.170   5.053   1.00 14.26 ?  52  ALA   A HB2  1 
ATOM   1369 H  HB3  . ALA   A 1 52  ? 18.620 5.934   5.620   1.00 14.26 ?  52  ALA   A HB3  1 
ATOM   1370 N  N    A LEU   A 1 53  ? 21.314 6.199   6.749   0.58 10.02 ?  53  LEU   A N    1 
ATOM   1371 N  N    B LEU   A 1 53  ? 21.313 6.197   6.752   0.42 9.79  ?  53  LEU   A N    1 
ATOM   1372 C  CA   A LEU   A 1 53  ? 22.276 5.799   7.773   0.58 10.37 ?  53  LEU   A CA   1 
ATOM   1373 C  CA   B LEU   A 1 53  ? 22.301 5.815   7.759   0.42 9.81  ?  53  LEU   A CA   1 
ATOM   1374 C  C    A LEU   A 1 53  ? 23.345 6.863   7.957   0.58 10.02 ?  53  LEU   A C    1 
ATOM   1375 C  C    B LEU   A 1 53  ? 23.313 6.932   7.967   0.42 9.64  ?  53  LEU   A C    1 
ATOM   1376 O  O    A LEU   A 1 53  ? 23.728 7.186   9.086   0.58 10.77 ?  53  LEU   A O    1 
ATOM   1377 O  O    B LEU   A 1 53  ? 23.566 7.357   9.099   0.42 10.27 ?  53  LEU   A O    1 
ATOM   1378 C  CB   A LEU   A 1 53  ? 22.926 4.462   7.410   0.58 10.84 ?  53  LEU   A CB   1 
ATOM   1379 C  CB   B LEU   A 1 53  ? 23.020 4.524   7.353   0.42 9.97  ?  53  LEU   A CB   1 
ATOM   1380 C  CG   A LEU   A 1 53  ? 22.010 3.236   7.437   0.58 10.95 ?  53  LEU   A CG   1 
ATOM   1381 C  CG   B LEU   A 1 53  ? 22.300 3.175   7.473   0.42 9.89  ?  53  LEU   A CG   1 
ATOM   1382 C  CD1  A LEU   A 1 53  ? 22.751 2.019   6.913   0.58 11.06 ?  53  LEU   A CD1  1 
ATOM   1383 C  CD1  B LEU   A 1 53  ? 23.138 2.093   6.806   0.42 10.57 ?  53  LEU   A CD1  1 
ATOM   1384 C  CD2  A LEU   A 1 53  ? 21.483 2.980   8.842   0.58 11.44 ?  53  LEU   A CD2  1 
ATOM   1385 C  CD2  B LEU   A 1 53  ? 22.009 2.797   8.922   0.42 9.64  ?  53  LEU   A CD2  1 
ATOM   1386 H  H    A LEU   A 1 53  ? 21.267 5.673   6.068   0.58 12.03 ?  53  LEU   A H    1 
ATOM   1387 H  H    B LEU   A 1 53  ? 21.252 5.659   6.083   0.42 11.75 ?  53  LEU   A H    1 
ATOM   1388 H  HA   A LEU   A 1 53  ? 21.816 5.685   8.619   0.58 12.44 ?  53  LEU   A HA   1 
ATOM   1389 H  HA   B LEU   A 1 53  ? 21.850 5.654   8.603   0.42 11.78 ?  53  LEU   A HA   1 
ATOM   1390 H  HB2  A LEU   A 1 53  ? 23.287 4.530   6.510   0.58 13.01 ?  53  LEU   A HB2  1 
ATOM   1391 H  HB2  B LEU   A 1 53  ? 23.276 4.614   6.423   0.42 11.96 ?  53  LEU   A HB2  1 
ATOM   1392 H  HB3  A LEU   A 1 53  ? 23.650 4.290   8.033   0.58 13.01 ?  53  LEU   A HB3  1 
ATOM   1393 H  HB3  B LEU   A 1 53  ? 23.820 4.453   7.893   0.42 11.96 ?  53  LEU   A HB3  1 
ATOM   1394 H  HG   A LEU   A 1 53  ? 21.249 3.396   6.853   0.58 13.14 ?  53  LEU   A HG   1 
ATOM   1395 H  HG   B LEU   A 1 53  ? 21.454 3.220   7.001   0.42 11.87 ?  53  LEU   A HG   1 
ATOM   1396 H  HD11 A LEU   A 1 53  ? 22.158 1.253   6.935   0.58 13.27 ?  53  LEU   A HD11 1 
ATOM   1397 H  HD11 B LEU   A 1 53  ? 22.682 1.240   6.892   0.42 12.69 ?  53  LEU   A HD11 1 
ATOM   1398 H  HD12 A LEU   A 1 53  ? 23.036 2.190   6.001   0.58 13.27 ?  53  LEU   A HD12 1 
ATOM   1399 H  HD12 B LEU   A 1 53  ? 23.251 2.314   5.869   0.42 12.69 ?  53  LEU   A HD12 1 
ATOM   1400 H  HD13 A LEU   A 1 53  ? 23.525 1.856   7.475   0.58 13.27 ?  53  LEU   A HD13 1 
ATOM   1401 H  HD13 B LEU   A 1 53  ? 24.003 2.050   7.243   0.42 12.69 ?  53  LEU   A HD13 1 
ATOM   1402 H  HD21 A LEU   A 1 53  ? 20.971 2.159   8.842   0.58 13.73 ?  53  LEU   A HD21 1 
ATOM   1403 H  HD21 B LEU   A 1 53  ? 21.518 1.959   8.940   0.42 11.56 ?  53  LEU   A HD21 1 
ATOM   1404 H  HD22 A LEU   A 1 53  ? 22.235 2.904   9.448   0.58 13.73 ?  53  LEU   A HD22 1 
ATOM   1405 H  HD22 B LEU   A 1 53  ? 22.849 2.696   9.398   0.42 11.56 ?  53  LEU   A HD22 1 
ATOM   1406 H  HD23 A LEU   A 1 53  ? 20.918 3.723   9.108   0.58 13.73 ?  53  LEU   A HD23 1 
ATOM   1407 H  HD23 B LEU   A 1 53  ? 21.480 3.498   9.331   0.42 11.56 ?  53  LEU   A HD23 1 
ATOM   1408 N  N    A ASN   A 1 54  ? 23.847 7.414   6.857   0.58 9.94  ?  54  ASN   A N    1 
ATOM   1409 N  N    B ASN   A 1 54  ? 23.899 7.428   6.877   0.42 9.69  ?  54  ASN   A N    1 
ATOM   1410 C  CA   A ASN   A 1 54  ? 24.899 8.410   6.980   0.58 9.77  ?  54  ASN   A CA   1 
ATOM   1411 C  CA   B ASN   A 1 54  ? 24.936 8.441   7.015   0.42 9.60  ?  54  ASN   A CA   1 
ATOM   1412 C  C    A ASN   A 1 54  ? 24.396 9.657   7.705   0.58 9.83  ?  54  ASN   A C    1 
ATOM   1413 C  C    B ASN   A 1 54  ? 24.407 9.691   7.709   0.42 9.88  ?  54  ASN   A C    1 
ATOM   1414 O  O    A ASN   A 1 54  ? 25.085 10.193  8.582   0.58 10.48 ?  54  ASN   A O    1 
ATOM   1415 O  O    B ASN   A 1 54  ? 25.093 10.274  8.557   0.42 10.55 ?  54  ASN   A O    1 
ATOM   1416 C  CB   A ASN   A 1 54  ? 25.463 8.756   5.611   0.58 10.11 ?  54  ASN   A CB   1 
ATOM   1417 C  CB   B ASN   A 1 54  ? 25.532 8.796   5.661   0.42 9.80  ?  54  ASN   A CB   1 
ATOM   1418 C  CG   A ASN   A 1 54  ? 26.519 9.820   5.703   0.58 10.56 ?  54  ASN   A CG   1 
ATOM   1419 C  CG   B ASN   A 1 54  ? 26.495 9.950   5.766   0.42 9.48  ?  54  ASN   A CG   1 
ATOM   1420 O  OD1  A ASN   A 1 54  ? 27.526 9.643   6.397   0.58 10.57 ?  54  ASN   A OD1  1 
ATOM   1421 O  OD1  B ASN   A 1 54  ? 27.501 9.858   6.473   0.42 9.30  ?  54  ASN   A OD1  1 
ATOM   1422 N  ND2  A ASN   A 1 54  ? 26.295 10.941  5.037   0.58 11.53 ?  54  ASN   A ND2  1 
ATOM   1423 N  ND2  B ASN   A 1 54  ? 26.185 11.055  5.100   0.42 10.19 ?  54  ASN   A ND2  1 
ATOM   1424 H  H    A ASN   A 1 54  ? 23.598 7.230   6.053   0.58 11.93 ?  54  ASN   A H    1 
ATOM   1425 H  H    B ASN   A 1 54  ? 23.713 7.199   6.070   0.42 11.63 ?  54  ASN   A H    1 
ATOM   1426 H  HA   A ASN   A 1 54  ? 25.613 8.034   7.509   0.58 11.73 ?  54  ASN   A HA   1 
ATOM   1427 H  HA   B ASN   A 1 54  ? 25.642 8.082   7.567   0.42 11.52 ?  54  ASN   A HA   1 
ATOM   1428 H  HB2  A ASN   A 1 54  ? 25.866 7.959   5.227   0.58 12.14 ?  54  ASN   A HB2  1 
ATOM   1429 H  HB2  B ASN   A 1 54  ? 26.017 8.025   5.321   0.42 11.76 ?  54  ASN   A HB2  1 
ATOM   1430 H  HB3  A ASN   A 1 54  ? 24.750 9.079   5.043   0.58 12.14 ?  54  ASN   A HB3  1 
ATOM   1431 H  HB3  B ASN   A 1 54  ? 24.822 9.042   5.052   0.42 11.76 ?  54  ASN   A HB3  1 
ATOM   1432 H  HD21 A ASN   A 1 54  ? 26.867 11.580  5.070   0.58 13.83 ?  54  ASN   A HD21 1 
ATOM   1433 H  HD21 B ASN   A 1 54  ? 26.702 11.741  5.141   0.42 12.23 ?  54  ASN   A HD21 1 
ATOM   1434 H  HD22 A ASN   A 1 54  ? 25.578 11.026  4.569   0.58 13.83 ?  54  ASN   A HD22 1 
ATOM   1435 H  HD22 B ASN   A 1 54  ? 25.472 11.081  4.619   0.42 12.23 ?  54  ASN   A HD22 1 
ATOM   1436 N  N    . LYS   A 1 55  ? 23.189 10.121  7.364   1.00 10.14 ?  55  LYS   A N    1 
ATOM   1437 C  CA   . LYS   A 1 55  ? 22.606 11.278  8.033   1.00 10.90 ?  55  LYS   A CA   1 
ATOM   1438 C  C    . LYS   A 1 55  ? 22.515 11.049  9.536   1.00 10.86 ?  55  LYS   A C    1 
ATOM   1439 O  O    . LYS   A 1 55  ? 22.793 11.953  10.333  1.00 11.68 ?  55  LYS   A O    1 
ATOM   1440 C  CB   . LYS   A 1 55  ? 21.231 11.571  7.424   1.00 11.90 ?  55  LYS   A CB   1 
ATOM   1441 C  CG   . LYS   A 1 55  ? 20.481 12.730  8.061   1.00 13.30 ?  55  LYS   A CG   1 
ATOM   1442 C  CD   . LYS   A 1 55  ? 19.153 12.963  7.331   1.00 14.93 ?  55  LYS   A CD   1 
ATOM   1443 C  CE   . LYS   A 1 55  ? 18.302 14.036  8.000   1.00 17.25 ?  55  LYS   A CE   1 
ATOM   1444 N  NZ   . LYS   A 1 55  ? 16.956 14.155  7.364   1.00 18.16 ?  55  LYS   A NZ   1 
ATOM   1445 H  H    A LYS   A 1 55  ? 22.683 9.776   6.755   0.58 12.17 ?  55  LYS   A H    1 
ATOM   1446 H  H    B LYS   A 1 55  ? 22.682 9.758   6.767   0.42 12.17 ?  55  LYS   A H    1 
ATOM   1447 H  HA   . LYS   A 1 55  ? 23.170 12.049  7.881   1.00 13.08 ?  55  LYS   A HA   1 
ATOM   1448 H  HB2  . LYS   A 1 55  ? 21.347 11.785  6.485   1.00 14.28 ?  55  LYS   A HB2  1 
ATOM   1449 H  HB3  . LYS   A 1 55  ? 20.675 10.782  7.511   1.00 14.28 ?  55  LYS   A HB3  1 
ATOM   1450 H  HG2  . LYS   A 1 55  ? 20.279 12.521  8.988   1.00 15.96 ?  55  LYS   A HG2  1 
ATOM   1451 H  HG3  . LYS   A 1 55  ? 21.008 13.538  7.999   1.00 15.96 ?  55  LYS   A HG3  1 
ATOM   1452 H  HD2  . LYS   A 1 55  ? 19.341 13.247  6.421   1.00 17.92 ?  55  LYS   A HD2  1 
ATOM   1453 H  HD3  . LYS   A 1 55  ? 18.647 12.135  7.321   1.00 17.92 ?  55  LYS   A HD3  1 
ATOM   1454 H  HE2  . LYS   A 1 55  ? 18.178 13.807  8.934   1.00 20.70 ?  55  LYS   A HE2  1 
ATOM   1455 H  HE3  . LYS   A 1 55  ? 18.752 14.893  7.923   1.00 20.70 ?  55  LYS   A HE3  1 
ATOM   1456 H  HZ1  . LYS   A 1 55  ? 16.402 14.596  7.905   1.00 21.79 ?  55  LYS   A HZ1  1 
ATOM   1457 H  HZ2  . LYS   A 1 55  ? 17.018 14.600  6.595   1.00 21.79 ?  55  LYS   A HZ2  1 
ATOM   1458 H  HZ3  . LYS   A 1 55  ? 16.619 13.347  7.205   1.00 21.79 ?  55  LYS   A HZ3  1 
ATOM   1459 N  N    . ALA   A 1 56  ? 22.129 9.839   9.947   1.00 11.23 ?  56  ALA   A N    1 
ATOM   1460 C  CA   . ALA   A 1 56  ? 22.003 9.521   11.364  1.00 11.85 ?  56  ALA   A CA   1 
ATOM   1461 C  C    . ALA   A 1 56  ? 23.344 9.544   12.086  1.00 11.53 ?  56  ALA   A C    1 
ATOM   1462 O  O    . ALA   A 1 56  ? 23.367 9.719   13.307  1.00 13.14 ?  56  ALA   A O    1 
ATOM   1463 C  CB   . ALA   A 1 56  ? 21.310 8.168   11.551  1.00 13.09 ?  56  ALA   A CB   1 
ATOM   1464 H  H    . ALA   A 1 56  ? 21.938 9.189   9.422   1.00 13.48 ?  56  ALA   A H    1 
ATOM   1465 H  HA   . ALA   A 1 56  ? 21.447 10.187  11.783  1.00 14.22 ?  56  ALA   A HA   1 
ATOM   1466 H  HB1  . ALA   A 1 56  ? 21.248 7.973   12.504  1.00 15.70 ?  56  ALA   A HB1  1 
ATOM   1467 H  HB2  . ALA   A 1 56  ? 20.424 8.212   11.166  1.00 15.70 ?  56  ALA   A HB2  1 
ATOM   1468 H  HB3  . ALA   A 1 56  ? 21.831 7.477   11.112  1.00 15.70 ?  56  ALA   A HB3  1 
ATOM   1469 N  N    . THR   A 1 57  ? 24.453 9.359   11.368  1.00 11.10 ?  57  THR   A N    1 
ATOM   1470 C  CA   . THR   A 1 57  ? 25.796 9.483   11.943  1.00 11.41 ?  57  THR   A CA   1 
ATOM   1471 C  C    . THR   A 1 57  ? 26.354 10.900  11.859  1.00 11.48 ?  57  THR   A C    1 
ATOM   1472 O  O    . THR   A 1 57  ? 27.540 11.110  12.151  1.00 12.10 ?  57  THR   A O    1 
ATOM   1473 C  CB   . THR   A 1 57  ? 26.808 8.533   11.271  1.00 11.47 ?  57  THR   A CB   1 
ATOM   1474 O  OG1  . THR   A 1 57  ? 27.187 9.028   9.973   1.00 10.80 ?  57  THR   A OG1  1 
ATOM   1475 C  CG2  . THR   A 1 57  ? 26.272 7.113   11.176  1.00 11.43 ?  57  THR   A CG2  1 
ATOM   1476 H  H    . THR   A 1 57  ? 24.460 9.136   10.538  1.00 13.32 ?  57  THR   A H    1 
ATOM   1477 H  HA   . THR   A 1 57  ? 25.757 9.233   12.884  1.00 13.69 ?  57  THR   A HA   1 
ATOM   1478 H  HB   . THR   A 1 57  ? 27.606 8.496   11.826  1.00 13.76 ?  57  THR   A HB   1 
ATOM   1479 H  HG1  . THR   A 1 57  ? 26.507 9.096   9.486   1.00 12.96 ?  57  THR   A HG1  1 
ATOM   1480 H  HG21 . THR   A 1 57  ? 26.933 6.529   10.765  1.00 13.71 ?  57  THR   A HG21 1 
ATOM   1481 H  HG22 . THR   A 1 57  ? 26.063 6.770   12.061  1.00 13.71 ?  57  THR   A HG22 1 
ATOM   1482 H  HG23 . THR   A 1 57  ? 25.465 7.092   10.638  1.00 13.71 ?  57  THR   A HG23 1 
ATOM   1483 N  N    . ASN   A 1 58  ? 25.543 11.872  11.449  1.00 11.83 ?  58  ASN   A N    1 
ATOM   1484 C  CA   . ASN   A 1 58  ? 26.006 13.252  11.346  1.00 12.82 ?  58  ASN   A CA   1 
ATOM   1485 C  C    . ASN   A 1 58  ? 27.160 13.372  10.348  1.00 11.85 ?  58  ASN   A C    1 
ATOM   1486 O  O    . ASN   A 1 58  ? 28.057 14.200  10.511  1.00 12.50 ?  58  ASN   A O    1 
ATOM   1487 C  CB   . ASN   A 1 58  ? 26.368 13.797  12.738  1.00 15.81 ?  58  ASN   A CB   1 
ATOM   1488 C  CG   . ASN   A 1 58  ? 26.760 15.256  12.727  1.00 19.72 ?  58  ASN   A CG   1 
ATOM   1489 O  OD1  . ASN   A 1 58  ? 26.132 16.063  12.056  1.00 21.60 ?  58  ASN   A OD1  1 
ATOM   1490 N  ND2  . ASN   A 1 58  ? 27.799 15.603  13.483  1.00 21.54 ?  58  ASN   A ND2  1 
ATOM   1491 H  H    . ASN   A 1 58  ? 24.723 11.748  11.210  1.00 14.19 ?  58  ASN   A H    1 
ATOM   1492 H  HA   . ASN   A 1 58  ? 25.272 13.784  11.008  1.00 15.39 ?  58  ASN   A HA   1 
ATOM   1493 H  HB2  . ASN   A 1 58  ? 25.592 13.694  13.326  1.00 18.97 ?  58  ASN   A HB2  1 
ATOM   1494 H  HB3  . ASN   A 1 58  ? 27.112 13.299  13.096  1.00 18.97 ?  58  ASN   A HB3  1 
ATOM   1495 H  HD21 . ASN   A 1 58  ? 28.048 16.427  13.514  1.00 25.84 ?  58  ASN   A HD21 1 
ATOM   1496 H  HD22 . ASN   A 1 58  ? 28.208 15.008  13.939  1.00 25.84 ?  58  ASN   A HD22 1 
ATOM   1497 N  N    . ASN   A 1 59  ? 27.132 12.551  9.294   1.00 10.86 ?  59  ASN   A N    1 
ATOM   1498 C  CA   . ASN   A 1 59  ? 28.116 12.523  8.206   1.00 10.57 ?  59  ASN   A CA   1 
ATOM   1499 C  C    . ASN   A 1 59  ? 29.429 11.838  8.595   1.00 10.42 ?  59  ASN   A C    1 
ATOM   1500 O  O    . ASN   A 1 59  ? 30.346 11.787  7.768   1.00 10.97 ?  59  ASN   A O    1 
ATOM   1501 C  CB   . ASN   A 1 59  ? 28.409 13.910  7.601   1.00 11.06 ?  59  ASN   A CB   1 
ATOM   1502 C  CG   . ASN   A 1 59  ? 28.770 13.839  6.138   1.00 11.35 ?  59  ASN   A CG   1 
ATOM   1503 O  OD1  . ASN   A 1 59  ? 28.064 13.219  5.344   1.00 11.51 ?  59  ASN   A OD1  1 
ATOM   1504 N  ND2  . ASN   A 1 59  ? 29.861 14.487  5.763   1.00 11.94 ?  59  ASN   A ND2  1 
ATOM   1505 H  H    . ASN   A 1 59  ? 26.510 11.966  9.178   1.00 13.03 ?  59  ASN   A H    1 
ATOM   1506 H  HA   . ASN   A 1 59  ? 27.735 11.996  7.494   1.00 12.69 ?  59  ASN   A HA   1 
ATOM   1507 H  HB2  . ASN   A 1 59  ? 27.620 14.470  7.686   1.00 13.27 ?  59  ASN   A HB2  1 
ATOM   1508 H  HB3  . ASN   A 1 59  ? 29.154 14.315  8.069   1.00 13.27 ?  59  ASN   A HB3  1 
ATOM   1509 H  HD21 . ASN   A 1 59  ? 30.111 14.478  4.937   1.00 14.33 ?  59  ASN   A HD21 1 
ATOM   1510 H  HD22 . ASN   A 1 59  ? 30.335 14.912  6.344   1.00 14.33 ?  59  ASN   A HD22 1 
ATOM   1511 N  N    . ALA   A 1 60  ? 29.548 11.291  9.806   1.00 10.56 ?  60  ALA   A N    1 
ATOM   1512 C  CA   . ALA   A 1 60  ? 30.785 10.607  10.165  1.00 10.85 ?  60  ALA   A CA   1 
ATOM   1513 C  C    . ALA   A 1 60  ? 31.009 9.370   9.302   1.00 10.85 ?  60  ALA   A C    1 
ATOM   1514 O  O    . ALA   A 1 60  ? 32.153 9.037   8.973   1.00 11.21 ?  60  ALA   A O    1 
ATOM   1515 C  CB   . ALA   A 1 60  ? 30.782 10.252  11.648  1.00 11.78 ?  60  ALA   A CB   1 
ATOM   1516 H  H    . ALA   A 1 60  ? 28.948 11.300  10.422  1.00 12.67 ?  60  ALA   A H    1 
ATOM   1517 H  HA   . ALA   A 1 60  ? 31.531 11.210  10.012  1.00 13.02 ?  60  ALA   A HA   1 
ATOM   1518 H  HB1  . ALA   A 1 60  ? 31.612 9.802   11.870  1.00 14.14 ?  60  ALA   A HB1  1 
ATOM   1519 H  HB2  . ALA   A 1 60  ? 30.706 11.073  12.167  1.00 14.14 ?  60  ALA   A HB2  1 
ATOM   1520 H  HB3  . ALA   A 1 60  ? 30.028 9.675   11.834  1.00 14.14 ?  60  ALA   A HB3  1 
ATOM   1521 N  N    . MET   A 1 61  ? 29.939 8.682   8.918   1.00 10.24 ?  61  MET   A N    1 
ATOM   1522 C  CA   . MET   A 1 61  ? 30.076 7.539   8.019   1.00 10.24 ?  61  MET   A CA   1 
ATOM   1523 C  C    . MET   A 1 61  ? 30.710 7.965   6.696   1.00 10.10 ?  61  MET   A C    1 
ATOM   1524 O  O    . MET   A 1 61  ? 31.599 7.280   6.176   1.00 10.62 ?  61  MET   A O    1 
ATOM   1525 C  CB   . MET   A 1 61  ? 28.712 6.882   7.806   1.00 10.14 ?  61  MET   A CB   1 
ATOM   1526 C  CG   . MET   A 1 61  ? 28.719 5.712   6.833   1.00 10.97 ?  61  MET   A CG   1 
ATOM   1527 S  SD   . MET   A 1 61  ? 27.092 4.963   6.629   1.00 11.69 ?  61  MET   A SD   1 
ATOM   1528 C  CE   . MET   A 1 61  ? 26.977 4.079   8.187   1.00 13.59 ?  61  MET   A CE   1 
ATOM   1529 H  H    . MET   A 1 61  ? 29.134 8.852   9.161   1.00 12.29 ?  61  MET   A H    1 
ATOM   1530 H  HA   . MET   A 1 61  ? 30.655 6.883   8.441   1.00 12.28 ?  61  MET   A HA   1 
ATOM   1531 H  HB2  . MET   A 1 61  ? 28.391 6.556   8.659   1.00 12.17 ?  61  MET   A HB2  1 
ATOM   1532 H  HB3  . MET   A 1 61  ? 28.099 7.550   7.460   1.00 12.17 ?  61  MET   A HB3  1 
ATOM   1533 H  HG2  . MET   A 1 61  ? 29.004 6.019   5.960   1.00 13.16 ?  61  MET   A HG2  1 
ATOM   1534 H  HG3  . MET   A 1 61  ? 29.319 5.027   7.161   1.00 13.16 ?  61  MET   A HG3  1 
ATOM   1535 H  HE1  . MET   A 1 61  ? 26.139 3.591   8.211   1.00 16.31 ?  61  MET   A HE1  1 
ATOM   1536 H  HE2  . MET   A 1 61  ? 27.722 3.465   8.259   1.00 16.31 ?  61  MET   A HE2  1 
ATOM   1537 H  HE3  . MET   A 1 61  ? 27.005 4.719   8.920   1.00 16.31 ?  61  MET   A HE3  1 
ATOM   1538 N  N    . GLN   A 1 62  ? 30.264 9.092   6.136   1.00 10.02 ?  62  GLN   A N    1 
ATOM   1539 C  CA   . GLN   A 1 62  ? 30.831 9.564   4.875   1.00 10.28 ?  62  GLN   A CA   1 
ATOM   1540 C  C    . GLN   A 1 62  ? 32.304 9.934   5.024   1.00 10.34 ?  62  GLN   A C    1 
ATOM   1541 O  O    . GLN   A 1 62  ? 33.118 9.618   4.148   1.00 10.88 ?  62  GLN   A O    1 
ATOM   1542 C  CB   . GLN   A 1 62  ? 30.037 10.749  4.339   1.00 10.42 ?  62  GLN   A CB   1 
ATOM   1543 C  CG   . GLN   A 1 62  ? 30.420 11.100  2.917   1.00 10.46 ?  62  GLN   A CG   1 
ATOM   1544 C  CD   . GLN   A 1 62  ? 30.087 9.970   1.967   1.00 10.48 ?  62  GLN   A CD   1 
ATOM   1545 O  OE1  . GLN   A 1 62  ? 28.906 9.665   1.760   1.00 10.95 ?  62  GLN   A OE1  1 
ATOM   1546 N  NE2  . GLN   A 1 62  ? 31.108 9.291   1.446   1.00 11.04 ?  62  GLN   A NE2  1 
ATOM   1547 H  H    . GLN   A 1 62  ? 29.639 9.583   6.460   1.00 12.02 ?  62  GLN   A H    1 
ATOM   1548 H  HA   . GLN   A 1 62  ? 30.776 8.843   4.230   1.00 12.34 ?  62  GLN   A HA   1 
ATOM   1549 H  HB2  . GLN   A 1 62  ? 29.092 10.533  4.355   1.00 12.51 ?  62  GLN   A HB2  1 
ATOM   1550 H  HB3  . GLN   A 1 62  ? 30.210 11.525  4.898   1.00 12.51 ?  62  GLN   A HB3  1 
ATOM   1551 H  HG2  . GLN   A 1 62  ? 29.923 11.880  2.639   1.00 12.55 ?  62  GLN   A HG2  1 
ATOM   1552 H  HG3  . GLN   A 1 62  ? 31.372 11.267  2.873   1.00 12.55 ?  62  GLN   A HG3  1 
ATOM   1553 H  HE21 . GLN   A 1 62  ? 31.916 9.520   1.634   1.00 13.24 ?  62  GLN   A HE21 1 
ATOM   1554 H  HE22 . GLN   A 1 62  ? 30.960 8.634   0.913   1.00 13.24 ?  62  GLN   A HE22 1 
ATOM   1555 N  N    . VAL   A 1 63  ? 32.662 10.621  6.112   1.00 10.93 ?  63  VAL   A N    1 
ATOM   1556 C  CA   . VAL   A 1 63  ? 34.056 11.013  6.322   1.00 11.90 ?  63  VAL   A CA   1 
ATOM   1557 C  C    . VAL   A 1 63  ? 34.952 9.778   6.393   1.00 11.16 ?  63  VAL   A C    1 
ATOM   1558 O  O    . VAL   A 1 63  ? 36.005 9.706   5.742   1.00 11.79 ?  63  VAL   A O    1 
ATOM   1559 C  CB   . VAL   A 1 63  ? 34.168 11.896  7.577   1.00 13.38 ?  63  VAL   A CB   1 
ATOM   1560 C  CG1  . VAL   A 1 63  ? 35.616 12.126  7.937   1.00 15.32 ?  63  VAL   A CG1  1 
ATOM   1561 C  CG2  . VAL   A 1 63  ? 33.449 13.224  7.355   1.00 13.68 ?  63  VAL   A CG2  1 
ATOM   1562 H  H    . VAL   A 1 63  ? 32.119 10.872  6.736   1.00 13.12 ?  63  VAL   A H    1 
ATOM   1563 H  HA   . VAL   A 1 63  ? 34.341 11.544  5.564   1.00 14.28 ?  63  VAL   A HA   1 
ATOM   1564 H  HB   . VAL   A 1 63  ? 33.747 11.448  8.325   1.00 16.06 ?  63  VAL   A HB   1 
ATOM   1565 H  HG11 . VAL   A 1 63  ? 35.675 12.871  8.556   1.00 18.38 ?  63  VAL   A HG11 1 
ATOM   1566 H  HG12 . VAL   A 1 63  ? 35.976 11.326  8.348   1.00 18.38 ?  63  VAL   A HG12 1 
ATOM   1567 H  HG13 . VAL   A 1 63  ? 36.113 12.335  7.127   1.00 18.38 ?  63  VAL   A HG13 1 
ATOM   1568 H  HG21 . VAL   A 1 63  ? 33.546 13.776  8.148   1.00 16.42 ?  63  VAL   A HG21 1 
ATOM   1569 H  HG22 . VAL   A 1 63  ? 33.846 13.675  6.591   1.00 16.42 ?  63  VAL   A HG22 1 
ATOM   1570 H  HG23 . VAL   A 1 63  ? 32.511 13.050  7.184   1.00 16.42 ?  63  VAL   A HG23 1 
ATOM   1571 N  N    . GLU   A 1 64  ? 34.527 8.774   7.164   1.00 10.80 ?  64  GLU   A N    1 
ATOM   1572 C  CA   . GLU   A 1 64  ? 35.284 7.533   7.261   1.00 11.13 ?  64  GLU   A CA   1 
ATOM   1573 C  C    . GLU   A 1 64  ? 35.373 6.846   5.904   1.00 10.68 ?  64  GLU   A C    1 
ATOM   1574 O  O    . GLU   A 1 64  ? 36.418 6.295   5.530   1.00 11.42 ?  64  GLU   A O    1 
ATOM   1575 C  CB   . GLU   A 1 64  ? 34.591 6.625   8.276   1.00 11.26 ?  64  GLU   A CB   1 
ATOM   1576 C  CG   . GLU   A 1 64  ? 35.235 5.277   8.418   1.00 12.15 ?  64  GLU   A CG   1 
ATOM   1577 C  CD   . GLU   A 1 64  ? 34.360 4.285   9.153   1.00 13.01 ?  64  GLU   A CD   1 
ATOM   1578 O  OE1  . GLU   A 1 64  ? 33.121 4.362   9.002   1.00 13.55 ?  64  GLU   A OE1  1 
ATOM   1579 O  OE2  . GLU   A 1 64  ? 34.908 3.405   9.855   1.00 13.17 -1 64  GLU   A OE2  1 
ATOM   1580 H  H    . GLU   A 1 64  ? 33.798 8.787   7.628   1.00 12.96 ?  64  GLU   A H    1 
ATOM   1581 H  HA   . GLU   A 1 64  ? 36.181 7.730   7.579   1.00 13.35 ?  64  GLU   A HA   1 
ATOM   1582 H  HB2  . GLU   A 1 64  ? 34.616 7.059   9.152   1.00 13.52 ?  64  GLU   A HB2  1 
ATOM   1583 H  HB3  . GLU   A 1 64  ? 33.671 6.500   8.004   1.00 13.52 ?  64  GLU   A HB3  1 
ATOM   1584 H  HG2  . GLU   A 1 64  ? 35.420 4.911   7.536   1.00 14.58 ?  64  GLU   A HG2  1 
ATOM   1585 H  HG3  . GLU   A 1 64  ? 36.059 5.373   8.914   1.00 14.58 ?  64  GLU   A HG3  1 
ATOM   1586 N  N    . SER   A 1 65  ? 34.256 6.834   5.172   1.00 10.41 ?  65  SER   A N    1 
ATOM   1587 C  CA   . SER   A 1 65  ? 34.208 6.173   3.874   1.00 10.54 ?  65  SER   A CA   1 
ATOM   1588 C  C    . SER   A 1 65  ? 35.130 6.840   2.864   1.00 10.71 ?  65  SER   A C    1 
ATOM   1589 O  O    . SER   A 1 65  ? 35.764 6.159   2.052   1.00 11.67 ?  65  SER   A O    1 
ATOM   1590 C  CB   . SER   A 1 65  ? 32.774 6.182   3.346   1.00 10.50 ?  65  SER   A CB   1 
ATOM   1591 O  OG   . SER   A 1 65  ? 31.924 5.375   4.149   1.00 10.91 ?  65  SER   A OG   1 
ATOM   1592 H  H    . SER   A 1 65  ? 33.518 7.210   5.406   1.00 12.50 ?  65  SER   A H    1 
ATOM   1593 H  HA   . SER   A 1 65  ? 34.487 5.251   3.976   1.00 12.65 ?  65  SER   A HA   1 
ATOM   1594 H  HB2  . SER   A 1 65  ? 32.437 7.091   3.352   1.00 12.60 ?  65  SER   A HB2  1 
ATOM   1595 H  HB3  . SER   A 1 65  ? 32.770 5.834   2.441   1.00 12.60 ?  65  SER   A HB3  1 
ATOM   1596 H  HG   . SER   A 1 65  ? 31.924 5.667   4.943   1.00 13.09 ?  65  SER   A HG   1 
ATOM   1597 N  N    . ASP   A 1 66  ? 35.203 8.174   2.879   1.00 10.85 ?  66  ASP   A N    1 
ATOM   1598 C  CA   . ASP   A 1 66  ? 36.067 8.863   1.930   1.00 11.61 ?  66  ASP   A CA   1 
ATOM   1599 C  C    . ASP   A 1 66  ? 37.529 8.507   2.170   1.00 11.76 ?  66  ASP   A C    1 
ATOM   1600 O  O    . ASP   A 1 66  ? 38.297 8.324   1.219   1.00 12.89 ?  66  ASP   A O    1 
ATOM   1601 C  CB   . ASP   A 1 66  ? 35.855 10.372  2.025   1.00 12.81 ?  66  ASP   A CB   1 
ATOM   1602 C  CG   . ASP   A 1 66  ? 34.519 10.832  1.435   1.00 14.53 ?  66  ASP   A CG   1 
ATOM   1603 O  OD1  . ASP   A 1 66  ? 33.797 10.029  0.806   1.00 14.59 ?  66  ASP   A OD1  1 
ATOM   1604 O  OD2  . ASP   A 1 66  ? 34.230 12.037  1.571   1.00 17.37 -1 66  ASP   A OD2  1 
ATOM   1605 H  H    . ASP   A 1 66  ? 34.757 8.690   3.409   1.00 13.03 ?  66  ASP   A H    1 
ATOM   1606 H  HA   . ASP   A 1 66  ? 35.829 8.587   1.029   1.00 13.93 ?  66  ASP   A HA   1 
ATOM   1607 H  HB2  . ASP   A 1 66  ? 35.875 10.640  2.956   1.00 15.37 ?  66  ASP   A HB2  1 
ATOM   1608 H  HB3  . ASP   A 1 66  ? 36.567 10.822  1.538   1.00 15.37 ?  66  ASP   A HB3  1 
ATOM   1609 N  N    . ASP   A 1 67  ? 37.928 8.380   3.435   1.00 11.98 ?  67  ASP   A N    1 
ATOM   1610 C  CA   . ASP   A 1 67  ? 39.281 7.925   3.733   1.00 12.86 ?  67  ASP   A CA   1 
ATOM   1611 C  C    . ASP   A 1 67  ? 39.494 6.486   3.269   1.00 12.60 ?  67  ASP   A C    1 
ATOM   1612 O  O    . ASP   A 1 67  ? 40.549 6.156   2.714   1.00 13.16 ?  67  ASP   A O    1 
ATOM   1613 C  CB   . ASP   A 1 67  ? 39.554 8.065   5.228   1.00 14.16 ?  67  ASP   A CB   1 
ATOM   1614 C  CG   . ASP   A 1 67  ? 40.849 7.407   5.644   1.00 15.38 ?  67  ASP   A CG   1 
ATOM   1615 O  OD1  . ASP   A 1 67  ? 41.921 8.031   5.484   1.00 18.21 ?  67  ASP   A OD1  1 
ATOM   1616 O  OD2  . ASP   A 1 67  ? 40.795 6.249   6.120   1.00 15.16 -1 67  ASP   A OD2  1 
ATOM   1617 H  H    . ASP   A 1 67  ? 37.439 8.540   4.120   1.00 14.38 ?  67  ASP   A H    1 
ATOM   1618 H  HA   . ASP   A 1 67  ? 39.910 8.487   3.254   1.00 15.43 ?  67  ASP   A HA   1 
ATOM   1619 H  HB2  . ASP   A 1 67  ? 39.610 9.004   5.447   1.00 16.99 ?  67  ASP   A HB2  1 
ATOM   1620 H  HB3  . ASP   A 1 67  ? 38.830 7.645   5.717   1.00 16.99 ?  67  ASP   A HB3  1 
ATOM   1621 N  N    . TYR   A 1 68  ? 38.501 5.613   3.475   1.00 12.56 ?  68  TYR   A N    1 
ATOM   1622 C  CA   . TYR   A 1 68  ? 38.609 4.235   2.996   1.00 12.75 ?  68  TYR   A CA   1 
ATOM   1623 C  C    . TYR   A 1 68  ? 38.855 4.188   1.488   1.00 12.29 ?  68  TYR   A C    1 
ATOM   1624 O  O    . TYR   A 1 68  ? 39.731 3.454   1.013   1.00 12.78 ?  68  TYR   A O    1 
ATOM   1625 C  CB   . TYR   A 1 68  ? 37.354 3.418   3.374   1.00 12.63 ?  68  TYR   A CB   1 
ATOM   1626 C  CG   . TYR   A 1 68  ? 37.374 2.032   2.740   1.00 13.85 ?  68  TYR   A CG   1 
ATOM   1627 C  CD1  . TYR   A 1 68  ? 36.914 1.844   1.440   1.00 15.02 ?  68  TYR   A CD1  1 
ATOM   1628 C  CD2  . TYR   A 1 68  ? 37.909 0.940   3.405   1.00 15.35 ?  68  TYR   A CD2  1 
ATOM   1629 C  CE1  . TYR   A 1 68  ? 36.983 0.626   0.819   1.00 16.10 ?  68  TYR   A CE1  1 
ATOM   1630 C  CE2  . TYR   A 1 68  ? 37.972 -0.314  2.784   1.00 15.84 ?  68  TYR   A CE2  1 
ATOM   1631 C  CZ   . TYR   A 1 68  ? 37.515 -0.444  1.494   1.00 16.45 ?  68  TYR   A CZ   1 
ATOM   1632 O  OH   . TYR   A 1 68  ? 37.598 -1.661  0.872   1.00 17.66 ?  68  TYR   A OH   1 
ATOM   1633 H  H    . TYR   A 1 68  ? 37.764 5.792   3.885   1.00 15.07 ?  68  TYR   A H    1 
ATOM   1634 H  HA   . TYR   A 1 68  ? 39.367 3.816   3.429   1.00 15.30 ?  68  TYR   A HA   1 
ATOM   1635 H  HB2  . TYR   A 1 68  ? 37.320 3.309   4.336   1.00 15.15 ?  68  TYR   A HB2  1 
ATOM   1636 H  HB3  . TYR   A 1 68  ? 36.562 3.884   3.061   1.00 15.15 ?  68  TYR   A HB3  1 
ATOM   1637 H  HD1  . TYR   A 1 68  ? 36.566 2.573   0.972   1.00 18.02 ?  68  TYR   A HD1  1 
ATOM   1638 H  HD2  . TYR   A 1 68  ? 38.242 1.047   4.264   1.00 18.42 ?  68  TYR   A HD2  1 
ATOM   1639 H  HE1  . TYR   A 1 68  ? 36.656 0.525   -0.048  1.00 19.32 ?  68  TYR   A HE1  1 
ATOM   1640 H  HE2  . TYR   A 1 68  ? 38.335 -1.042  3.225   1.00 19.01 ?  68  TYR   A HE2  1 
ATOM   1641 H  HH   . TYR   A 1 68  ? 37.922 -2.231  1.402   1.00 21.19 ?  68  TYR   A HH   1 
ATOM   1642 N  N    . ILE   A 1 69  ? 38.069 4.946   0.715   1.00 11.72 ?  69  ILE   A N    1 
ATOM   1643 C  CA   . ILE   A 1 69  ? 38.212 4.934   -0.741  1.00 11.45 ?  69  ILE   A CA   1 
ATOM   1644 C  C    . ILE   A 1 69  ? 39.550 5.531   -1.165  1.00 11.56 ?  69  ILE   A C    1 
ATOM   1645 O  O    . ILE   A 1 69  ? 40.194 5.039   -2.099  1.00 12.19 ?  69  ILE   A O    1 
ATOM   1646 C  CB   . ILE   A 1 69  ? 37.023 5.651   -1.413  1.00 12.76 ?  69  ILE   A CB   1 
ATOM   1647 C  CG1  . ILE   A 1 69  ? 35.707 4.927   -1.133  1.00 12.86 ?  69  ILE   A CG1  1 
ATOM   1648 C  CG2  . ILE   A 1 69  ? 37.264 5.836   -2.920  1.00 13.90 ?  69  ILE   A CG2  1 
ATOM   1649 C  CD1  . ILE   A 1 69  ? 35.541 3.639   -1.896  1.00 13.34 ?  69  ILE   A CD1  1 
ATOM   1650 H  H    . ILE   A 1 69  ? 37.457 5.473   1.008   1.00 14.07 ?  69  ILE   A H    1 
ATOM   1651 H  HA   . ILE   A 1 69  ? 38.201 4.012   -1.039  1.00 13.74 ?  69  ILE   A HA   1 
ATOM   1652 H  HB   . ILE   A 1 69  ? 36.956 6.532   -1.020  1.00 15.32 ?  69  ILE   A HB   1 
ATOM   1653 H  HG12 . ILE   A 1 69  ? 35.664 4.718   -0.185  1.00 15.43 ?  69  ILE   A HG12 1 
ATOM   1654 H  HG13 . ILE   A 1 69  ? 34.974 5.513   -1.372  1.00 15.43 ?  69  ILE   A HG13 1 
ATOM   1655 H  HG21 . ILE   A 1 69  ? 36.423 6.057   -3.351  1.00 16.67 ?  69  ILE   A HG21 1 
ATOM   1656 H  HG22 . ILE   A 1 69  ? 37.897 6.567   -3.052  1.00 16.67 ?  69  ILE   A HG22 1 
ATOM   1657 H  HG23 . ILE   A 1 69  ? 37.623 5.019   -3.292  1.00 16.67 ?  69  ILE   A HG23 1 
ATOM   1658 H  HD11 . ILE   A 1 69  ? 34.740 3.194   -1.582  1.00 16.01 ?  69  ILE   A HD11 1 
ATOM   1659 H  HD12 . ILE   A 1 69  ? 35.456 3.842   -2.841  1.00 16.01 ?  69  ILE   A HD12 1 
ATOM   1660 H  HD13 . ILE   A 1 69  ? 36.314 3.077   -1.744  1.00 16.01 ?  69  ILE   A HD13 1 
ATOM   1661 N  N    . ALA   A 1 70  ? 39.971 6.616   -0.519  1.00 12.14 ?  70  ALA   A N    1 
ATOM   1662 C  CA   . ALA   A 1 70  ? 41.252 7.218   -0.867  1.00 13.03 ?  70  ALA   A CA   1 
ATOM   1663 C  C    . ALA   A 1 70  ? 42.396 6.231   -0.690  1.00 13.37 ?  70  ALA   A C    1 
ATOM   1664 O  O    . ALA   A 1 70  ? 43.367 6.265   -1.451  1.00 15.16 ?  70  ALA   A O    1 
ATOM   1665 C  CB   . ALA   A 1 70  ? 41.493 8.466   -0.018  1.00 13.91 ?  70  ALA   A CB   1 
ATOM   1666 H  H    . ALA   A 1 70  ? 39.537 7.013   0.105   1.00 14.57 ?  70  ALA   A H    1 
ATOM   1667 H  HA   . ALA   A 1 70  ? 41.226 7.495   -1.800  1.00 15.64 ?  70  ALA   A HA   1 
ATOM   1668 H  HB1  . ALA   A 1 70  ? 42.353 8.850   -0.264  1.00 16.69 ?  70  ALA   A HB1  1 
ATOM   1669 H  HB2  . ALA   A 1 70  ? 40.787 9.106   -0.180  1.00 16.69 ?  70  ALA   A HB2  1 
ATOM   1670 H  HB3  . ALA   A 1 70  ? 41.506 8.210   0.918   1.00 16.69 ?  70  ALA   A HB3  1 
ATOM   1671 N  N    . THR   A 1 71  ? 42.286 5.331   0.285   1.00 12.82 ?  71  THR   A N    1 
ATOM   1672 C  CA   . THR   A 1 71  ? 43.333 4.351   0.540   1.00 14.81 ?  71  THR   A CA   1 
ATOM   1673 C  C    . THR   A 1 71  ? 43.213 3.126   -0.355  1.00 14.77 ?  71  THR   A C    1 
ATOM   1674 O  O    . THR   A 1 71  ? 44.225 2.617   -0.854  1.00 16.94 ?  71  THR   A O    1 
ATOM   1675 C  CB   . THR   A 1 71  ? 43.258 3.906   1.996   1.00 16.65 ?  71  THR   A CB   1 
ATOM   1676 O  OG1  . THR   A 1 71  ? 43.506 5.033   2.842   1.00 17.81 ?  71  THR   A OG1  1 
ATOM   1677 C  CG2  . THR   A 1 71  ? 44.266 2.794   2.287   1.00 18.42 ?  71  THR   A CG2  1 
ATOM   1678 H  H    . THR   A 1 71  ? 41.608 5.266   0.805   1.00 15.39 ?  71  THR   A H    1 
ATOM   1679 H  HA   . THR   A 1 71  ? 44.198 4.753   0.377   1.00 17.77 ?  71  THR   A HA   1 
ATOM   1680 H  HB   . THR   A 1 71  ? 42.367 3.558   2.168   1.00 19.98 ?  71  THR   A HB   1 
ATOM   1681 H  HG1  . THR   A 1 71  ? 42.921 5.622   2.695   1.00 21.37 ?  71  THR   A HG1  1 
ATOM   1682 H  HG21 . THR   A 1 71  ? 44.393 2.713   3.243   1.00 22.10 ?  71  THR   A HG21 1 
ATOM   1683 H  HG22 . THR   A 1 71  ? 43.945 1.947   1.939   1.00 22.10 ?  71  THR   A HG22 1 
ATOM   1684 H  HG23 . THR   A 1 71  ? 45.119 3.003   1.873   1.00 22.10 ?  71  THR   A HG23 1 
ATOM   1685 N  N    . ASN   A 1 72  ? 41.990 2.621   -0.544  1.00 14.02 ?  72  ASN   A N    1 
ATOM   1686 C  CA   . ASN   A 1 72  ? 41.768 1.297   -1.112  1.00 14.29 ?  72  ASN   A CA   1 
ATOM   1687 C  C    . ASN   A 1 72  ? 41.143 1.288   -2.495  1.00 14.23 ?  72  ASN   A C    1 
ATOM   1688 O  O    . ASN   A 1 72  ? 41.153 0.235   -3.145  1.00 15.31 ?  72  ASN   A O    1 
ATOM   1689 C  CB   . ASN   A 1 72  ? 40.879 0.478   -0.169  1.00 14.86 ?  72  ASN   A CB   1 
ATOM   1690 C  CG   . ASN   A 1 72  ? 41.491 0.332   1.192   1.00 15.83 ?  72  ASN   A CG   1 
ATOM   1691 O  OD1  . ASN   A 1 72  ? 41.031 0.923   2.165   1.00 17.73 ?  72  ASN   A OD1  1 
ATOM   1692 N  ND2  . ASN   A 1 72  ? 42.550 -0.439  1.268   1.00 16.34 ?  72  ASN   A ND2  1 
ATOM   1693 H  H    . ASN   A 1 72  ? 41.258 3.035   -0.350  1.00 16.83 ?  72  ASN   A H    1 
ATOM   1694 H  HA   . ASN   A 1 72  ? 42.621 0.845   -1.180  1.00 17.14 ?  72  ASN   A HA   1 
ATOM   1695 H  HB2  . ASN   A 1 72  ? 40.023 0.918   -0.072  1.00 17.83 ?  72  ASN   A HB2  1 
ATOM   1696 H  HB3  . ASN   A 1 72  ? 40.758 -0.412  -0.542  1.00 17.83 ?  72  ASN   A HB3  1 
ATOM   1697 H  HD21 . ASN   A 1 72  ? 42.946 -0.555  2.023   1.00 19.61 ?  72  ASN   A HD21 1 
ATOM   1698 H  HD22 . ASN   A 1 72  ? 42.854 -0.829  0.562   1.00 19.61 ?  72  ASN   A HD22 1 
ATOM   1699 N  N    . GLY   A 1 73  ? 40.592 2.402   -2.956  1.00 13.50 ?  73  GLY   A N    1 
ATOM   1700 C  CA   . GLY   A 1 73  ? 39.857 2.416   -4.196  1.00 13.32 ?  73  GLY   A CA   1 
ATOM   1701 C  C    . GLY   A 1 73  ? 38.465 1.841   -4.028  1.00 12.80 ?  73  GLY   A C    1 
ATOM   1702 O  O    . GLY   A 1 73  ? 38.078 1.388   -2.944  1.00 13.31 ?  73  GLY   A O    1 
ATOM   1703 H  H    . GLY   A 1 73  ? 40.636 3.176   -2.569  1.00 16.20 ?  73  GLY   A H    1 
ATOM   1704 H  HA2  . GLY   A 1 73  ? 39.785 3.332   -4.519  1.00 15.98 ?  73  GLY   A HA2  1 
ATOM   1705 H  HA3  . GLY   A 1 73  ? 40.334 1.895   -4.863  1.00 15.98 ?  73  GLY   A HA3  1 
ATOM   1706 N  N    . PRO   A 1 74  ? 37.689 1.858   -5.109  1.00 13.30 ?  74  PRO   A N    1 
ATOM   1707 C  CA   . PRO   A 1 74  ? 36.291 1.432   -5.028  1.00 13.39 ?  74  PRO   A CA   1 
ATOM   1708 C  C    . PRO   A 1 74  ? 36.141 -0.047  -4.706  1.00 12.67 ?  74  PRO   A C    1 
ATOM   1709 O  O    . PRO   A 1 74  ? 37.008 -0.879  -4.994  1.00 13.45 ?  74  PRO   A O    1 
ATOM   1710 C  CB   . PRO   A 1 74  ? 35.746 1.734   -6.431  1.00 14.89 ?  74  PRO   A CB   1 
ATOM   1711 C  CG   . PRO   A 1 74  ? 36.689 2.718   -7.030  1.00 17.37 ?  74  PRO   A CG   1 
ATOM   1712 C  CD   . PRO   A 1 74  ? 38.028 2.390   -6.439  1.00 14.97 ?  74  PRO   A CD   1 
ATOM   1713 H  HA   . PRO   A 1 74  ? 35.809 1.961   -4.372  1.00 16.06 ?  74  PRO   A HA   1 
ATOM   1714 H  HB2  . PRO   A 1 74  ? 35.723 0.918   -6.954  1.00 17.87 ?  74  PRO   A HB2  1 
ATOM   1715 H  HB3  . PRO   A 1 74  ? 34.856 2.118   -6.359  1.00 17.87 ?  74  PRO   A HB3  1 
ATOM   1716 H  HG2  . PRO   A 1 74  ? 36.711 2.614   -7.995  1.00 20.84 ?  74  PRO   A HG2  1 
ATOM   1717 H  HG3  . PRO   A 1 74  ? 36.427 3.621   -6.790  1.00 20.84 ?  74  PRO   A HG3  1 
ATOM   1718 H  HD2  . PRO   A 1 74  ? 38.484 1.716   -6.972  1.00 17.96 ?  74  PRO   A HD2  1 
ATOM   1719 H  HD3  . PRO   A 1 74  ? 38.570 3.199   -6.367  1.00 17.96 ?  74  PRO   A HD3  1 
ATOM   1720 N  N    . LEU   A 1 75  ? 34.995 -0.365  -4.117  1.00 11.76 ?  75  LEU   A N    1 
ATOM   1721 C  CA   . LEU   A 1 75  ? 34.597 -1.753  -3.958  1.00 11.44 ?  75  LEU   A CA   1 
ATOM   1722 C  C    . LEU   A 1 75  ? 34.211 -2.335  -5.315  1.00 11.84 ?  75  LEU   A C    1 
ATOM   1723 O  O    . LEU   A 1 75  ? 34.069 -1.624  -6.314  1.00 13.52 ?  75  LEU   A O    1 
ATOM   1724 C  CB   . LEU   A 1 75  ? 33.405 -1.868  -3.007  1.00 11.24 ?  75  LEU   A CB   1 
ATOM   1725 C  CG   . LEU   A 1 75  ? 33.620 -1.456  -1.554  1.00 12.83 ?  75  LEU   A CG   1 
ATOM   1726 C  CD1  . LEU   A 1 75  ? 32.341 -1.652  -0.757  1.00 14.91 ?  75  LEU   A CD1  1 
ATOM   1727 C  CD2  . LEU   A 1 75  ? 34.759 -2.181  -0.902  1.00 16.36 ?  75  LEU   A CD2  1 
ATOM   1728 H  H    . LEU   A 1 75  ? 34.433 0.206   -3.805  1.00 14.11 ?  75  LEU   A H    1 
ATOM   1729 H  HA   . LEU   A 1 75  ? 35.338 -2.263  -3.602  1.00 13.73 ?  75  LEU   A HA   1 
ATOM   1730 H  HB2  . LEU   A 1 75  ? 32.686 -1.322  -3.355  1.00 13.49 ?  75  LEU   A HB2  1 
ATOM   1731 H  HB3  . LEU   A 1 75  ? 33.121 -2.798  -2.998  1.00 13.49 ?  75  LEU   A HB3  1 
ATOM   1732 H  HG   . LEU   A 1 75  ? 33.837 -0.510  -1.535  1.00 15.39 ?  75  LEU   A HG   1 
ATOM   1733 H  HD11 . LEU   A 1 75  ? 32.499 -1.377  0.160   1.00 17.89 ?  75  LEU   A HD11 1 
ATOM   1734 H  HD12 . LEU   A 1 75  ? 31.644 -1.103  -1.151  1.00 17.89 ?  75  LEU   A HD12 1 
ATOM   1735 H  HD13 . LEU   A 1 75  ? 32.091 -2.584  -0.789  1.00 17.89 ?  75  LEU   A HD13 1 
ATOM   1736 H  HD21 . LEU   A 1 75  ? 34.807 -1.928  0.033   1.00 19.63 ?  75  LEU   A HD21 1 
ATOM   1737 H  HD22 . LEU   A 1 75  ? 34.618 -3.136  -0.981  1.00 19.63 ?  75  LEU   A HD22 1 
ATOM   1738 H  HD23 . LEU   A 1 75  ? 35.592 -1.936  -1.347  1.00 19.63 ?  75  LEU   A HD23 1 
ATOM   1739 N  N    . LYS   A 1 76  ? 34.050 -3.658  -5.335  1.00 12.09 ?  76  LYS   A N    1 
ATOM   1740 C  CA   . LYS   A 1 76  ? 33.453 -4.383  -6.452  1.00 12.88 ?  76  LYS   A CA   1 
ATOM   1741 C  C    . LYS   A 1 76  ? 31.939 -4.464  -6.268  1.00 11.45 ?  76  LYS   A C    1 
ATOM   1742 O  O    . LYS   A 1 76  ? 31.450 -4.581  -5.148  1.00 11.42 ?  76  LYS   A O    1 
ATOM   1743 C  CB   . LYS   A 1 76  ? 33.992 -5.824  -6.494  1.00 14.10 ?  76  LYS   A CB   1 
ATOM   1744 C  CG   . LYS   A 1 76  ? 35.501 -5.936  -6.684  1.00 15.80 ?  76  LYS   A CG   1 
ATOM   1745 C  CD   . LYS   A 1 76  ? 36.014 -7.341  -6.464  1.00 17.08 ?  76  LYS   A CD   1 
ATOM   1746 C  CE   . LYS   A 1 76  ? 37.508 -7.411  -6.692  1.00 19.59 ?  76  LYS   A CE   1 
ATOM   1747 N  NZ   . LYS   A 1 76  ? 38.034 -8.761  -6.425  1.00 20.42 ?  76  LYS   A NZ   1 
ATOM   1748 H  H    . LYS   A 1 76  ? 34.288 -4.178  -4.687  1.00 14.51 ?  76  LYS   A H    1 
ATOM   1749 H  HA   . LYS   A 1 76  ? 33.657 -3.937  -7.291  1.00 15.46 ?  76  LYS   A HA   1 
ATOM   1750 H  HB2  . LYS   A 1 76  ? 33.768 -6.258  -5.659  1.00 16.92 ?  76  LYS   A HB2  1 
ATOM   1751 H  HB3  . LYS   A 1 76  ? 33.569 -6.287  -7.232  1.00 16.92 ?  76  LYS   A HB3  1 
ATOM   1752 H  HG2  . LYS   A 1 76  ? 35.726 -5.671  -7.590  1.00 18.97 ?  76  LYS   A HG2  1 
ATOM   1753 H  HG3  . LYS   A 1 76  ? 35.944 -5.352  -6.048  1.00 18.97 ?  76  LYS   A HG3  1 
ATOM   1754 H  HD2  . LYS   A 1 76  ? 35.826 -7.615  -5.551  1.00 20.49 ?  76  LYS   A HD2  1 
ATOM   1755 H  HD3  . LYS   A 1 76  ? 35.577 -7.945  -7.090  1.00 20.49 ?  76  LYS   A HD3  1 
ATOM   1756 H  HE2  . LYS   A 1 76  ? 37.699 -7.185  -7.614  1.00 23.51 ?  76  LYS   A HE2  1 
ATOM   1757 H  HE3  . LYS   A 1 76  ? 37.948 -6.791  -6.092  1.00 23.51 ?  76  LYS   A HE3  1 
ATOM   1758 H  HZ1  . LYS   A 1 76  ? 38.912 -8.785  -6.566  1.00 24.51 ?  76  LYS   A HZ1  1 
ATOM   1759 H  HZ2  . LYS   A 1 76  ? 37.870 -8.998  -5.582  1.00 24.51 ?  76  LYS   A HZ2  1 
ATOM   1760 H  HZ3  . LYS   A 1 76  ? 37.643 -9.357  -6.967  1.00 24.51 ?  76  LYS   A HZ3  1 
ATOM   1761 N  N    . VAL   A 1 77  ? 31.195 -4.442  -7.378  1.00 11.83 ?  77  VAL   A N    1 
ATOM   1762 C  CA   . VAL   A 1 77  ? 29.788 -4.828  -7.299  1.00 11.74 ?  77  VAL   A CA   1 
ATOM   1763 C  C    . VAL   A 1 77  ? 29.725 -6.279  -6.848  1.00 11.60 ?  77  VAL   A C    1 
ATOM   1764 O  O    . VAL   A 1 77  ? 30.390 -7.152  -7.417  1.00 11.82 ?  77  VAL   A O    1 
ATOM   1765 C  CB   . VAL   A 1 77  ? 29.075 -4.616  -8.642  1.00 12.60 ?  77  VAL   A CB   1 
ATOM   1766 C  CG1  . VAL   A 1 77  ? 27.615 -5.031  -8.530  1.00 13.33 ?  77  VAL   A CG1  1 
ATOM   1767 C  CG2  . VAL   A 1 77  ? 29.192 -3.163  -9.091  1.00 14.27 ?  77  VAL   A CG2  1 
ATOM   1768 H  H    . VAL   A 1 77  ? 31.477 -4.212  -8.157  1.00 14.20 ?  77  VAL   A H    1 
ATOM   1769 H  HA   . VAL   A 1 77  ? 29.350 -4.279  -6.630  1.00 14.08 ?  77  VAL   A HA   1 
ATOM   1770 H  HB   . VAL   A 1 77  ? 29.497 -5.170  -9.314  1.00 15.12 ?  77  VAL   A HB   1 
ATOM   1771 H  HG11 . VAL   A 1 77  ? 27.144 -4.732  -9.321  1.00 16.00 ?  77  VAL   A HG11 1 
ATOM   1772 H  HG12 . VAL   A 1 77  ? 27.565 -5.995  -8.456  1.00 16.00 ?  77  VAL   A HG12 1 
ATOM   1773 H  HG13 . VAL   A 1 77  ? 27.231 -4.616  -7.740  1.00 16.00 ?  77  VAL   A HG13 1 
ATOM   1774 H  HG21 . VAL   A 1 77  ? 28.677 -3.044  -9.902  1.00 17.13 ?  77  VAL   A HG21 1 
ATOM   1775 H  HG22 . VAL   A 1 77  ? 28.845 -2.589  -8.389  1.00 17.13 ?  77  VAL   A HG22 1 
ATOM   1776 H  HG23 . VAL   A 1 77  ? 30.125 -2.957  -9.255  1.00 17.13 ?  77  VAL   A HG23 1 
ATOM   1777 N  N    . GLY   A 1 78  ? 28.934 -6.539  -5.804  1.00 11.07 ?  78  GLY   A N    1 
ATOM   1778 C  CA   . GLY   A 1 78  ? 28.913 -7.823  -5.139  1.00 11.19 ?  78  GLY   A CA   1 
ATOM   1779 C  C    . GLY   A 1 78  ? 29.822 -7.910  -3.933  1.00 10.71 ?  78  GLY   A C    1 
ATOM   1780 O  O    . GLY   A 1 78  ? 29.755 -8.910  -3.197  1.00 11.37 ?  78  GLY   A O    1 
ATOM   1781 H  H    . GLY   A 1 78  ? 28.386 -5.960  -5.463  1.00 13.29 ?  78  GLY   A H    1 
ATOM   1782 H  HA2  . GLY   A 1 78  ? 28.008 -8.011  -4.851  1.00 13.43 ?  78  GLY   A HA2  1 
ATOM   1783 H  HA3  . GLY   A 1 78  ? 29.179 -8.505  -5.774  1.00 13.43 ?  78  GLY   A HA3  1 
ATOM   1784 N  N    . GLY   A 1 79  ? 30.677 -6.908  -3.715  1.00 10.81 ?  79  GLY   A N    1 
ATOM   1785 C  CA   . GLY   A 1 79  ? 31.638 -6.923  -2.635  1.00 11.14 ?  79  GLY   A CA   1 
ATOM   1786 C  C    . GLY   A 1 79  ? 31.191 -6.121  -1.426  1.00 10.67 ?  79  GLY   A C    1 
ATOM   1787 O  O    . GLY   A 1 79  ? 30.075 -5.602  -1.353  1.00 11.11 ?  79  GLY   A O    1 
ATOM   1788 H  H    . GLY   A 1 79  ? 30.722 -6.196  -4.201  1.00 12.97 ?  79  GLY   A H    1 
ATOM   1789 H  HA2  . GLY   A 1 79  ? 31.791 -7.844  -2.359  1.00 13.36 ?  79  GLY   A HA2  1 
ATOM   1790 H  HA3  . GLY   A 1 79  ? 32.484 -6.564  -2.953  1.00 13.36 ?  79  GLY   A HA3  1 
ATOM   1791 N  N    . SER   A 1 80  ? 32.097 -6.024  -0.454  1.00 11.40 ?  80  SER   A N    1 
ATOM   1792 C  CA   . SER   A 1 80  ? 31.775 -5.393  0.815   1.00 10.86 ?  80  SER   A CA   1 
ATOM   1793 C  C    . SER   A 1 80  ? 33.043 -4.943  1.519   1.00 10.97 ?  80  SER   A C    1 
ATOM   1794 O  O    . SER   A 1 80  ? 34.155 -5.378  1.194   1.00 12.50 ?  80  SER   A O    1 
ATOM   1795 C  CB   . SER   A 1 80  ? 31.010 -6.359  1.730   1.00 11.86 ?  80  SER   A CB   1 
ATOM   1796 O  OG   . SER   A 1 80  ? 31.840 -7.403  2.215   1.00 13.46 ?  80  SER   A OG   1 
ATOM   1797 H  H    . SER   A 1 80  ? 32.907 -6.303  -0.514  1.00 13.68 ?  80  SER   A H    1 
ATOM   1798 H  HA   . SER   A 1 80  ? 31.222 -4.609  0.636   1.00 13.03 ?  80  SER   A HA   1 
ATOM   1799 H  HB2  . SER   A 1 80  ? 30.662 -5.857  2.484   1.00 14.23 ?  80  SER   A HB2  1 
ATOM   1800 H  HB3  . SER   A 1 80  ? 30.274 -6.743  1.226   1.00 14.23 ?  80  SER   A HB3  1 
ATOM   1801 H  HG   . SER   A 1 80  ? 32.146 -7.841  1.561   1.00 16.15 ?  80  SER   A HG   1 
ATOM   1802 N  N    . CYS   A 1 81  ? 32.851 -4.084  2.515   1.00 10.47 ?  81  CYS   A N    1 
ATOM   1803 C  CA   . CYS   A 1 81  ? 33.903 -3.808  3.480   1.00 11.05 ?  81  CYS   A CA   1 
ATOM   1804 C  C    . CYS   A 1 81  ? 33.258 -3.567  4.835   1.00 10.66 ?  81  CYS   A C    1 
ATOM   1805 O  O    . CYS   A 1 81  ? 32.093 -3.165  4.919   1.00 11.94 ?  81  CYS   A O    1 
ATOM   1806 C  CB   . CYS   A 1 81  ? 34.774 -2.617  3.066   1.00 11.66 ?  81  CYS   A CB   1 
ATOM   1807 S  SG   . CYS   A 1 81  ? 33.879 -1.036  3.071   1.00 11.64 ?  81  CYS   A SG   1 
ATOM   1808 H  H    . CYS   A 1 81  ? 32.121 -3.647  2.652   1.00 12.57 ?  81  CYS   A H    1 
ATOM   1809 H  HA   . CYS   A 1 81  ? 34.478 -4.584  3.548   1.00 13.26 ?  81  CYS   A HA   1 
ATOM   1810 H  HB2  . CYS   A 1 81  ? 35.520 -2.542  3.687   1.00 13.99 ?  81  CYS   A HB2  1 
ATOM   1811 H  HB3  . CYS   A 1 81  ? 35.116 -2.769  2.168   1.00 13.99 ?  81  CYS   A HB3  1 
ATOM   1812 H  HG   . CYS   A 1 81  ? 34.628 -0.159  2.739   1.00 13.97 ?  81  CYS   A HG   1 
ATOM   1813 N  N    . VAL   A 1 82  ? 34.024 -3.822  5.893   1.00 10.92 ?  82  VAL   A N    1 
ATOM   1814 C  CA   . VAL   A 1 82  ? 33.592 -3.575  7.260   1.00 11.29 ?  82  VAL   A CA   1 
ATOM   1815 C  C    . VAL   A 1 82  ? 34.192 -2.262  7.730   1.00 11.58 ?  82  VAL   A C    1 
ATOM   1816 O  O    . VAL   A 1 82  ? 35.417 -2.093  7.717   1.00 12.36 ?  82  VAL   A O    1 
ATOM   1817 C  CB   . VAL   A 1 82  ? 34.015 -4.713  8.200   1.00 12.91 ?  82  VAL   A CB   1 
ATOM   1818 C  CG1  . VAL   A 1 82  ? 33.579 -4.414  9.626   1.00 14.30 ?  82  VAL   A CG1  1 
ATOM   1819 C  CG2  . VAL   A 1 82  ? 33.452 -6.038  7.734   1.00 13.75 ?  82  VAL   A CG2  1 
ATOM   1820 H  H    . VAL   A 1 82  ? 34.822 -4.153  5.837   1.00 13.11 ?  82  VAL   A H    1 
ATOM   1821 H  HA   . VAL   A 1 82  ? 32.626 -3.496  7.282   1.00 13.54 ?  82  VAL   A HA   1 
ATOM   1822 H  HB   . VAL   A 1 82  ? 34.981 -4.779  8.193   1.00 15.49 ?  82  VAL   A HB   1 
ATOM   1823 H  HG11 . VAL   A 1 82  ? 33.666 -5.222  10.157  1.00 17.16 ?  82  VAL   A HG11 1 
ATOM   1824 H  HG12 . VAL   A 1 82  ? 34.144 -3.717  9.996   1.00 17.16 ?  82  VAL   A HG12 1 
ATOM   1825 H  HG13 . VAL   A 1 82  ? 32.653 -4.123  9.622   1.00 17.16 ?  82  VAL   A HG13 1 
ATOM   1826 H  HG21 . VAL   A 1 82  ? 33.700 -6.727  8.370   1.00 16.50 ?  82  VAL   A HG21 1 
ATOM   1827 H  HG22 . VAL   A 1 82  ? 32.485 -5.970  7.681   1.00 16.50 ?  82  VAL   A HG22 1 
ATOM   1828 H  HG23 . VAL   A 1 82  ? 33.817 -6.247  6.860   1.00 16.50 ?  82  VAL   A HG23 1 
ATOM   1829 N  N    . LEU   A 1 83  ? 33.341 -1.337  8.151   1.00 10.90 ?  83  LEU   A N    1 
ATOM   1830 C  CA   . LEU   A 1 83  ? 33.753 -0.069  8.725   1.00 11.12 ?  83  LEU   A CA   1 
ATOM   1831 C  C    . LEU   A 1 83  ? 33.031 0.120   10.054  1.00 11.06 ?  83  LEU   A C    1 
ATOM   1832 O  O    . LEU   A 1 83  ? 32.312 -0.767  10.527  1.00 11.54 ?  83  LEU   A O    1 
ATOM   1833 C  CB   . LEU   A 1 83  ? 33.504 1.084   7.741   1.00 11.47 ?  83  LEU   A CB   1 
ATOM   1834 C  CG   . LEU   A 1 83  ? 34.409 1.081   6.504   1.00 12.12 ?  83  LEU   A CG   1 
ATOM   1835 C  CD1  . LEU   A 1 83  ? 33.967 2.122   5.490   1.00 13.04 ?  83  LEU   A CD1  1 
ATOM   1836 C  CD2  . LEU   A 1 83  ? 35.884 1.298   6.887   1.00 12.89 ?  83  LEU   A CD2  1 
ATOM   1837 H  H    . LEU   A 1 83  ? 32.488 -1.427  8.103   1.00 13.07 ?  83  LEU   A H    1 
ATOM   1838 H  HA   . LEU   A 1 83  ? 34.704 -0.096  8.906   1.00 13.34 ?  83  LEU   A HA   1 
ATOM   1839 H  HB2  . LEU   A 1 83  ? 32.587 1.034   7.426   1.00 13.76 ?  83  LEU   A HB2  1 
ATOM   1840 H  HB3  . LEU   A 1 83  ? 33.642 1.926   8.201   1.00 13.76 ?  83  LEU   A HB3  1 
ATOM   1841 H  HG   . LEU   A 1 83  ? 34.347 0.215   6.081   1.00 14.54 ?  83  LEU   A HG   1 
ATOM   1842 H  HD11 . LEU   A 1 83  ? 34.564 2.086   4.725   1.00 15.64 ?  83  LEU   A HD11 1 
ATOM   1843 H  HD12 . LEU   A 1 83  ? 33.061 1.921   5.212   1.00 15.64 ?  83  LEU   A HD12 1 
ATOM   1844 H  HD13 . LEU   A 1 83  ? 34.005 2.999   5.899   1.00 15.64 ?  83  LEU   A HD13 1 
ATOM   1845 H  HD21 . LEU   A 1 83  ? 36.408 1.442   6.079   1.00 15.47 ?  83  LEU   A HD21 1 
ATOM   1846 H  HD22 . LEU   A 1 83  ? 35.957 2.078   7.463   1.00 15.47 ?  83  LEU   A HD22 1 
ATOM   1847 H  HD23 . LEU   A 1 83  ? 36.216 0.515   7.355   1.00 15.47 ?  83  LEU   A HD23 1 
ATOM   1848 N  N    . SER   A 1 84  ? 33.251 1.269   10.683  1.00 11.77 ?  84  SER   A N    1 
ATOM   1849 C  CA   . SER   A 1 84  ? 32.605 1.528   11.959  1.00 11.97 ?  84  SER   A CA   1 
ATOM   1850 C  C    . SER   A 1 84  ? 31.086 1.612   11.808  1.00 11.83 ?  84  SER   A C    1 
ATOM   1851 O  O    . SER   A 1 84  ? 30.560 2.086   10.800  1.00 11.70 ?  84  SER   A O    1 
ATOM   1852 C  CB   . SER   A 1 84  ? 33.102 2.854   12.523  1.00 12.69 ?  84  SER   A CB   1 
ATOM   1853 O  OG   . SER   A 1 84  ? 32.476 3.131   13.758  1.00 13.74 ?  84  SER   A OG   1 
ATOM   1854 H  H    . SER   A 1 84  ? 33.757 1.907   10.392  1.00 14.13 ?  84  SER   A H    1 
ATOM   1855 H  HA   . SER   A 1 84  ? 32.829 0.822   12.581  1.00 14.36 ?  84  SER   A HA   1 
ATOM   1856 H  HB2  . SER   A 1 84  ? 34.064 2.806   12.654  1.00 15.23 ?  84  SER   A HB2  1 
ATOM   1857 H  HB3  . SER   A 1 84  ? 32.894 3.565   11.891  1.00 15.23 ?  84  SER   A HB3  1 
ATOM   1858 H  HG   . SER   A 1 84  ? 32.755 3.865   14.061  1.00 16.48 ?  84  SER   A HG   1 
ATOM   1859 N  N    . GLY   A 1 85  ? 30.378 1.205   12.857  1.00 12.65 ?  85  GLY   A N    1 
ATOM   1860 C  CA   . GLY   A 1 85  ? 28.955 1.449   12.940  1.00 12.94 ?  85  GLY   A CA   1 
ATOM   1861 C  C    . GLY   A 1 85  ? 28.591 2.765   13.587  1.00 12.48 ?  85  GLY   A C    1 
ATOM   1862 O  O    . GLY   A 1 85  ? 27.402 3.087   13.708  1.00 13.09 ?  85  GLY   A O    1 
ATOM   1863 H  H    . GLY   A 1 85  ? 30.709 0.781   13.535  1.00 15.18 ?  85  GLY   A H    1 
ATOM   1864 H  HA2  . GLY   A 1 85  ? 28.585 1.433   12.044  1.00 15.52 ?  85  GLY   A HA2  1 
ATOM   1865 H  HA3  . GLY   A 1 85  ? 28.544 0.737   13.448  1.00 15.52 ?  85  GLY   A HA3  1 
ATOM   1866 N  N    . HIS   A 1 86  ? 29.583 3.534   14.022  1.00 12.21 ?  86  HIS   A N    1 
ATOM   1867 C  CA   . HIS   A 1 86  ? 29.370 4.872   14.585  1.00 12.62 ?  86  HIS   A CA   1 
ATOM   1868 C  C    . HIS   A 1 86  ? 28.381 4.759   15.739  1.00 13.25 ?  86  HIS   A C    1 
ATOM   1869 O  O    . HIS   A 1 86  ? 28.555 3.885   16.603  1.00 14.56 ?  86  HIS   A O    1 
ATOM   1870 C  CB   . HIS   A 1 86  ? 28.993 5.844   13.475  1.00 13.00 ?  86  HIS   A CB   1 
ATOM   1871 C  CG   . HIS   A 1 86  ? 30.051 5.945   12.437  1.00 12.84 ?  86  HIS   A CG   1 
ATOM   1872 N  ND1  . HIS   A 1 86  ? 31.148 6.769   12.579  1.00 14.29 ?  86  HIS   A ND1  1 
ATOM   1873 C  CD2  . HIS   A 1 86  ? 30.232 5.257   11.287  1.00 12.39 ?  86  HIS   A CD2  1 
ATOM   1874 C  CE1  . HIS   A 1 86  ? 31.943 6.603   11.537  1.00 13.66 ?  86  HIS   A CE1  1 
ATOM   1875 N  NE2  . HIS   A 1 86  ? 31.416 5.686   10.746  1.00 12.99 ?  86  HIS   A NE2  1 
ATOM   1876 H  H    . HIS   A 1 86  ? 30.407 3.303   14.013  1.00 14.65 ?  86  HIS   A H    1 
ATOM   1877 H  HA   . HIS   A 1 86  ? 30.207 5.185   14.954  1.00 15.15 ?  86  HIS   A HA   1 
ATOM   1878 H  HB2  . HIS   A 1 86  ? 28.174 5.545   13.045  1.00 15.60 ?  86  HIS   A HB2  1 
ATOM   1879 H  HB3  . HIS   A 1 86  ? 28.860 6.732   13.850  1.00 15.60 ?  86  HIS   A HB3  1 
ATOM   1880 H  HD2  . HIS   A 1 86  ? 29.663 4.605   10.931  1.00 14.87 ?  86  HIS   A HD2  1 
ATOM   1881 H  HE1  . HIS   A 1 86  ? 32.736 7.057   11.373  1.00 16.39 ?  86  HIS   A HE1  1 
ATOM   1882 H  HE2  . HIS   A 1 86  ? 31.748 5.413   9.994   1.00 15.58 ?  86  HIS   A HE2  1 
ATOM   1883 N  N    . ASN   A 1 87  ? 27.375 5.617   15.804  1.00 14.37 ?  87  ASN   A N    1 
ATOM   1884 C  CA   . ASN   A 1 87  ? 26.399 5.619   16.875  1.00 15.63 ?  87  ASN   A CA   1 
ATOM   1885 C  C    . ASN   A 1 87  ? 25.267 4.635   16.643  1.00 16.46 ?  87  ASN   A C    1 
ATOM   1886 O  O    . ASN   A 1 87  ? 24.354 4.575   17.467  1.00 18.93 ?  87  ASN   A O    1 
ATOM   1887 C  CB   . ASN   A 1 87  ? 25.818 7.032   17.032  1.00 16.43 ?  87  ASN   A CB   1 
ATOM   1888 C  CG   . ASN   A 1 87  ? 25.309 7.611   15.715  1.00 17.06 ?  87  ASN   A CG   1 
ATOM   1889 O  OD1  . ASN   A 1 87  ? 25.955 7.490   14.676  1.00 17.74 ?  87  ASN   A OD1  1 
ATOM   1890 N  ND2  . ASN   A 1 87  ? 24.149 8.242   15.757  1.00 18.56 ?  87  ASN   A ND2  1 
ATOM   1891 H  H    . ASN   A 1 87  ? 27.227 6.225   15.219  1.00 17.24 ?  87  ASN   A H    1 
ATOM   1892 H  HA   . ASN   A 1 87  ? 26.826 5.374   17.712  1.00 18.76 ?  87  ASN   A HA   1 
ATOM   1893 H  HB2  . ASN   A 1 87  ? 25.071 7.002   17.660  1.00 19.71 ?  87  ASN   A HB2  1 
ATOM   1894 H  HB3  . ASN   A 1 87  ? 26.508 7.619   17.374  1.00 19.71 ?  87  ASN   A HB3  1 
ATOM   1895 H  HD21 . ASN   A 1 87  ? 23.823 8.581   15.040  1.00 22.27 ?  87  ASN   A HD21 1 
ATOM   1896 H  HD22 . ASN   A 1 87  ? 23.725 8.319   16.503  1.00 22.27 ?  87  ASN   A HD22 1 
ATOM   1897 N  N    A LEU   A 1 88  ? 25.310 3.863   15.559  0.58 15.17 ?  88  LEU   A N    1 
ATOM   1898 N  N    B LEU   A 1 88  ? 25.317 3.841   15.575  0.42 15.53 ?  88  LEU   A N    1 
ATOM   1899 C  CA   A LEU   A 1 88  ? 24.203 2.996   15.168  0.58 14.96 ?  88  LEU   A CA   1 
ATOM   1900 C  CA   B LEU   A 1 88  ? 24.196 2.998   15.187  0.42 15.26 ?  88  LEU   A CA   1 
ATOM   1901 C  C    A LEU   A 1 88  ? 24.418 1.529   15.506  0.58 14.61 ?  88  LEU   A C    1 
ATOM   1902 C  C    B LEU   A 1 88  ? 24.415 1.514   15.433  0.42 14.67 ?  88  LEU   A C    1 
ATOM   1903 O  O    A LEU   A 1 88  ? 23.443 0.817   15.768  0.58 15.40 ?  88  LEU   A O    1 
ATOM   1904 O  O    B LEU   A 1 88  ? 23.433 0.773   15.535  0.42 14.84 ?  88  LEU   A O    1 
ATOM   1905 C  CB   A LEU   A 1 88  ? 23.964 3.112   13.659  0.58 15.11 ?  88  LEU   A CB   1 
ATOM   1906 C  CB   B LEU   A 1 88  ? 23.897 3.187   13.695  0.42 15.48 ?  88  LEU   A CB   1 
ATOM   1907 C  CG   A LEU   A 1 88  ? 23.672 4.517   13.137  0.58 16.72 ?  88  LEU   A CG   1 
ATOM   1908 C  CG   B LEU   A 1 88  ? 23.588 4.622   13.260  0.42 16.16 ?  88  LEU   A CG   1 
ATOM   1909 C  CD1  A LEU   A 1 88  ? 23.556 4.485   11.625  0.58 16.96 ?  88  LEU   A CD1  1 
ATOM   1910 C  CD1  B LEU   A 1 88  ? 23.391 4.705   11.752  0.42 16.00 ?  88  LEU   A CD1  1 
ATOM   1911 C  CD2  A LEU   A 1 88  ? 22.404 5.081   13.767  0.58 18.27 ?  88  LEU   A CD2  1 
ATOM   1912 C  CD2  B LEU   A 1 88  ? 22.365 5.151   13.990  0.42 16.98 ?  88  LEU   A CD2  1 
ATOM   1913 H  H    A LEU   A 1 88  ? 25.985 3.823   15.030  0.58 18.20 ?  88  LEU   A H    1 
ATOM   1914 H  H    B LEU   A 1 88  ? 26.003 3.767   15.068  0.42 18.63 ?  88  LEU   A H    1 
ATOM   1915 H  HA   A LEU   A 1 88  ? 23.397 3.289   15.617  0.58 17.95 ?  88  LEU   A HA   1 
ATOM   1916 H  HA   B LEU   A 1 88  ? 23.408 3.271   15.684  0.42 18.32 ?  88  LEU   A HA   1 
ATOM   1917 H  HB2  A LEU   A 1 88  ? 24.751 2.795   13.191  0.58 18.13 ?  88  LEU   A HB2  1 
ATOM   1918 H  HB2  B LEU   A 1 88  ? 24.669 2.886   13.194  0.42 18.58 ?  88  LEU   A HB2  1 
ATOM   1919 H  HB3  A LEU   A 1 88  ? 23.202 2.558   13.421  0.58 18.13 ?  88  LEU   A HB3  1 
ATOM   1920 H  HB3  B LEU   A 1 88  ? 23.129 2.639   13.470  0.42 18.58 ?  88  LEU   A HB3  1 
ATOM   1921 H  HG   A LEU   A 1 88  ? 24.407 5.104   13.367  0.58 20.06 ?  88  LEU   A HG   1 
ATOM   1922 H  HG   B LEU   A 1 88  ? 24.339 5.188   13.490  0.42 19.40 ?  88  LEU   A HG   1 
ATOM   1923 H  HD11 A LEU   A 1 88  ? 23.410 5.386   11.297  0.58 20.35 ?  88  LEU   A HD11 1 
ATOM   1924 H  HD11 B LEU   A 1 88  ? 23.212 5.627   11.506  0.42 19.20 ?  88  LEU   A HD11 1 
ATOM   1925 H  HD12 A LEU   A 1 88  ? 24.377 4.125   11.254  0.58 20.35 ?  88  LEU   A HD12 1 
ATOM   1926 H  HD12 B LEU   A 1 88  ? 24.198 4.397   11.310  0.42 19.20 ?  88  LEU   A HD12 1 
ATOM   1927 H  HD13 A LEU   A 1 88  ? 22.807 3.918   11.380  0.58 20.35 ?  88  LEU   A HD13 1 
ATOM   1928 H  HD13 B LEU   A 1 88  ? 22.641 4.144   11.498  0.42 19.20 ?  88  LEU   A HD13 1 
ATOM   1929 H  HD21 A LEU   A 1 88  ? 22.186 5.925   13.339  0.58 21.93 ?  88  LEU   A HD21 1 
ATOM   1930 H  HD21 B LEU   A 1 88  ? 22.114 6.003   13.601  0.42 20.38 ?  88  LEU   A HD21 1 
ATOM   1931 H  HD22 A LEU   A 1 88  ? 21.680 4.449   13.640  0.58 21.93 ?  88  LEU   A HD22 1 
ATOM   1932 H  HD22 B LEU   A 1 88  ? 21.641 4.514   13.891  0.42 20.38 ?  88  LEU   A HD22 1 
ATOM   1933 H  HD23 A LEU   A 1 88  ? 22.558 5.222   14.714  0.58 21.93 ?  88  LEU   A HD23 1 
ATOM   1934 H  HD23 B LEU   A 1 88  ? 22.584 5.264   14.926  0.42 20.38 ?  88  LEU   A HD23 1 
ATOM   1935 N  N    . ALA   A 1 89  ? 25.663 1.063   15.500  1.00 13.88 ?  89  ALA   A N    1 
ATOM   1936 C  CA   . ALA   A 1 89  ? 25.984 -0.352  15.616  1.00 13.54 ?  89  ALA   A CA   1 
ATOM   1937 C  C    . ALA   A 1 89  ? 27.468 -0.434  15.935  1.00 14.08 ?  89  ALA   A C    1 
ATOM   1938 O  O    . ALA   A 1 89  ? 28.191 0.555   15.810  1.00 14.73 ?  89  ALA   A O    1 
ATOM   1939 C  CB   . ALA   A 1 89  ? 25.701 -1.066  14.296  1.00 13.16 ?  89  ALA   A CB   1 
ATOM   1940 H  H    A ALA   A 1 89  ? 26.357 1.567   15.430  0.58 16.65 ?  89  ALA   A H    1 
ATOM   1941 H  H    B ALA   A 1 89  ? 26.355 1.572   15.450  0.42 16.65 ?  89  ALA   A H    1 
ATOM   1942 H  HA   . ALA   A 1 89  ? 25.470 -0.759  16.333  1.00 16.25 ?  89  ALA   A HA   1 
ATOM   1943 H  HB1  . ALA   A 1 89  ? 25.941 -2.002  14.386  1.00 15.79 ?  89  ALA   A HB1  1 
ATOM   1944 H  HB2  . ALA   A 1 89  ? 24.754 -0.989  14.089  1.00 15.79 ?  89  ALA   A HB2  1 
ATOM   1945 H  HB3  . ALA   A 1 89  ? 26.227 -0.656  13.595  1.00 15.79 ?  89  ALA   A HB3  1 
ATOM   1946 N  N    . LYS   A 1 90  ? 27.935 -1.616  16.328  1.00 14.63 ?  90  LYS   A N    1 
ATOM   1947 C  CA   . LYS   A 1 90  ? 29.379 -1.775  16.478  1.00 15.31 ?  90  LYS   A CA   1 
ATOM   1948 C  C    . LYS   A 1 90  ? 30.083 -1.590  15.137  1.00 14.18 ?  90  LYS   A C    1 
ATOM   1949 O  O    . LYS   A 1 90  ? 31.027 -0.792  15.013  1.00 15.65 ?  90  LYS   A O    1 
ATOM   1950 C  CB   . LYS   A 1 90  ? 29.711 -3.136  17.093  1.00 17.97 ?  90  LYS   A CB   1 
ATOM   1951 C  CG   . LYS   A 1 90  ? 31.183 -3.293  17.436  1.00 23.24 ?  90  LYS   A CG   1 
ATOM   1952 C  CD   . LYS   A 1 90  ? 31.424 -4.561  18.239  1.00 28.07 ?  90  LYS   A CD   1 
ATOM   1953 C  CE   . LYS   A 1 90  ? 32.803 -4.571  18.881  1.00 31.88 ?  90  LYS   A CE   1 
ATOM   1954 N  NZ   . LYS   A 1 90  ? 33.892 -4.817  17.898  1.00 34.37 ?  90  LYS   A NZ   1 
ATOM   1955 H  H    . LYS   A 1 90  ? 27.457 -2.303  16.515  1.00 17.55 ?  90  LYS   A H    1 
ATOM   1956 H  HA   . LYS   A 1 90  ? 29.708 -1.091  17.078  1.00 18.37 ?  90  LYS   A HA   1 
ATOM   1957 H  HB2  . LYS   A 1 90  ? 29.199 -3.245  17.911  1.00 21.57 ?  90  LYS   A HB2  1 
ATOM   1958 H  HB3  . LYS   A 1 90  ? 29.475 -3.835  16.462  1.00 21.57 ?  90  LYS   A HB3  1 
ATOM   1959 H  HG2  . LYS   A 1 90  ? 31.701 -3.347  16.617  1.00 27.89 ?  90  LYS   A HG2  1 
ATOM   1960 H  HG3  . LYS   A 1 90  ? 31.472 -2.535  17.968  1.00 27.89 ?  90  LYS   A HG3  1 
ATOM   1961 H  HD2  . LYS   A 1 90  ? 30.760 -4.624  18.944  1.00 33.68 ?  90  LYS   A HD2  1 
ATOM   1962 H  HD3  . LYS   A 1 90  ? 31.358 -5.330  17.650  1.00 33.68 ?  90  LYS   A HD3  1 
ATOM   1963 H  HE2  . LYS   A 1 90  ? 32.964 -3.710  19.299  1.00 38.25 ?  90  LYS   A HE2  1 
ATOM   1964 H  HE3  . LYS   A 1 90  ? 32.836 -5.274  19.549  1.00 38.25 ?  90  LYS   A HE3  1 
ATOM   1965 H  HZ1  . LYS   A 1 90  ? 34.681 -4.816  18.312  1.00 41.24 ?  90  LYS   A HZ1  1 
ATOM   1966 H  HZ2  . LYS   A 1 90  ? 33.775 -5.608  17.506  1.00 41.24 ?  90  LYS   A HZ2  1 
ATOM   1967 H  HZ3  . LYS   A 1 90  ? 33.891 -4.182  17.277  1.00 41.24 ?  90  LYS   A HZ3  1 
ATOM   1968 N  N    . HIS   A 1 91  ? 29.610 -2.300  14.113  1.00 12.84 ?  91  HIS   A N    1 
ATOM   1969 C  CA   . HIS   A 1 91  ? 30.195 -2.296  12.786  1.00 12.31 ?  91  HIS   A CA   1 
ATOM   1970 C  C    . HIS   A 1 91  ? 29.115 -2.024  11.756  1.00 11.37 ?  91  HIS   A C    1 
ATOM   1971 O  O    . HIS   A 1 91  ? 27.952 -2.380  11.946  1.00 12.09 ?  91  HIS   A O    1 
ATOM   1972 C  CB   . HIS   A 1 91  ? 30.785 -3.669  12.437  1.00 14.96 ?  91  HIS   A CB   1 
ATOM   1973 C  CG   . HIS   A 1 91  ? 31.759 -4.187  13.443  1.00 19.38 ?  91  HIS   A CG   1 
ATOM   1974 N  ND1  . HIS   A 1 91  ? 33.045 -3.704  13.551  1.00 21.46 ?  91  HIS   A ND1  1 
ATOM   1975 C  CD2  . HIS   A 1 91  ? 31.642 -5.158  14.379  1.00 21.28 ?  91  HIS   A CD2  1 
ATOM   1976 C  CE1  . HIS   A 1 91  ? 33.678 -4.354  14.512  1.00 22.26 ?  91  HIS   A CE1  1 
ATOM   1977 N  NE2  . HIS   A 1 91  ? 32.849 -5.243  15.030  1.00 22.51 ?  91  HIS   A NE2  1 
ATOM   1978 H  H    . HIS   A 1 91  ? 28.915 -2.820  14.172  1.00 15.40 ?  91  HIS   A H    1 
ATOM   1979 H  HA   . HIS   A 1 91  ? 30.886 -1.624  12.721  1.00 14.77 ?  91  HIS   A HA   1 
ATOM   1980 H  HB2  . HIS   A 1 91  ? 30.062 -4.316  12.372  1.00 17.96 ?  91  HIS   A HB2  1 
ATOM   1981 H  HB3  . HIS   A 1 91  ? 31.243 -3.607  11.585  1.00 17.96 ?  91  HIS   A HB3  1 
ATOM   1982 H  HD1  . HIS   A 1 91  ? 33.386 -3.079  13.062  1.00 25.75 ?  91  HIS   A HD1  1 
ATOM   1983 H  HD2  . HIS   A 1 91  ? 30.892 -5.672  14.551  1.00 25.54 ?  91  HIS   A HD2  1 
ATOM   1984 H  HE1  . HIS   A 1 91  ? 34.562 -4.205  14.776  1.00 26.72 ?  91  HIS   A HE1  1 
ATOM   1985 N  N    . CYS   A 1 92  ? 29.525 -1.431  10.641  1.00 11.06 ?  92  CYS   A N    1 
ATOM   1986 C  CA   . CYS   A 1 92  ? 28.696 -1.353  9.448   1.00 10.89 ?  92  CYS   A CA   1 
ATOM   1987 C  C    . CYS   A 1 92  ? 29.346 -2.177  8.347   1.00 10.53 ?  92  CYS   A C    1 
ATOM   1988 O  O    . CYS   A 1 92  ? 30.505 -1.937  7.982   1.00 11.33 ?  92  CYS   A O    1 
ATOM   1989 C  CB   . CYS   A 1 92  ? 28.497 0.089   8.979   1.00 11.42 ?  92  CYS   A CB   1 
ATOM   1990 S  SG   . CYS   A 1 92  ? 27.478 0.190   7.473   1.00 10.66 ?  92  CYS   A SG   1 
ATOM   1991 H  H    . CYS   A 1 92  ? 30.298 -1.056  10.547  1.00 13.28 ?  92  CYS   A H    1 
ATOM   1992 H  HA   . CYS   A 1 92  ? 27.827 -1.730  9.635   1.00 13.07 ?  92  CYS   A HA   1 
ATOM   1993 H  HB2  . CYS   A 1 92  ? 28.048 0.593   9.679   1.00 13.71 ?  92  CYS   A HB2  1 
ATOM   1994 H  HB3  . CYS   A 1 92  ? 29.359 0.489   8.785   1.00 13.71 ?  92  CYS   A HB3  1 
ATOM   1995 H  HG   . CYS   A 1 92  ? 27.346 1.343   7.173   1.00 12.80 ?  92  CYS   A HG   1 
ATOM   1996 N  N    . LEU   A 1 93  ? 28.610 -3.161  7.840   1.00 10.03 ?  93  LEU   A N    1 
ATOM   1997 C  CA   . LEU   A 1 93  ? 29.023 -3.926  6.671   1.00 10.04 ?  93  LEU   A CA   1 
ATOM   1998 C  C    . LEU   A 1 93  ? 28.432 -3.239  5.446   1.00 9.52  ?  93  LEU   A C    1 
ATOM   1999 O  O    . LEU   A 1 93  ? 27.217 -3.295  5.217   1.00 9.72  ?  93  LEU   A O    1 
ATOM   2000 C  CB   . LEU   A 1 93  ? 28.533 -5.370  6.783   1.00 10.47 ?  93  LEU   A CB   1 
ATOM   2001 C  CG   . LEU   A 1 93  ? 28.923 -6.277  5.616   1.00 10.81 ?  93  LEU   A CG   1 
ATOM   2002 C  CD1  . LEU   A 1 93  ? 30.426 -6.544  5.593   1.00 11.76 ?  93  LEU   A CD1  1 
ATOM   2003 C  CD2  . LEU   A 1 93  ? 28.147 -7.595  5.667   1.00 11.50 ?  93  LEU   A CD2  1 
ATOM   2004 H  H    . LEU   A 1 93  ? 27.852 -3.407  8.170   1.00 12.04 ?  93  LEU   A H    1 
ATOM   2005 H  HA   . LEU   A 1 93  ? 29.987 -3.919  6.602   1.00 12.05 ?  93  LEU   A HA   1 
ATOM   2006 H  HB2  . LEU   A 1 93  ? 28.906 -5.752  7.597   1.00 12.57 ?  93  LEU   A HB2  1 
ATOM   2007 H  HB3  . LEU   A 1 93  ? 27.568 -5.363  6.842   1.00 12.57 ?  93  LEU   A HB3  1 
ATOM   2008 H  HG   . LEU   A 1 93  ? 28.699 -5.836  4.791   1.00 12.97 ?  93  LEU   A HG   1 
ATOM   2009 H  HD11 . LEU   A 1 93  ? 30.630 -7.159  4.871   1.00 14.11 ?  93  LEU   A HD11 1 
ATOM   2010 H  HD12 . LEU   A 1 93  ? 30.900 -5.711  5.464   1.00 14.11 ?  93  LEU   A HD12 1 
ATOM   2011 H  HD13 . LEU   A 1 93  ? 30.694 -6.945  6.444   1.00 14.11 ?  93  LEU   A HD13 1 
ATOM   2012 H  HD21 . LEU   A 1 93  ? 28.418 -8.150  4.919   1.00 13.80 ?  93  LEU   A HD21 1 
ATOM   2013 H  HD22 . LEU   A 1 93  ? 28.343 -8.050  6.503   1.00 13.80 ?  93  LEU   A HD22 1 
ATOM   2014 H  HD23 . LEU   A 1 93  ? 27.198 -7.404  5.611   1.00 13.80 ?  93  LEU   A HD23 1 
ATOM   2015 N  N    . HIS   A 1 94  ? 29.280 -2.551  4.686   1.00 9.28  ?  94  HIS   A N    1 
ATOM   2016 C  CA   . HIS   A 1 94  ? 28.865 -1.878  3.461   1.00 9.59  ?  94  HIS   A CA   1 
ATOM   2017 C  C    . HIS   A 1 94  ? 28.876 -2.910  2.351   1.00 9.30  ?  94  HIS   A C    1 
ATOM   2018 O  O    . HIS   A 1 94  ? 29.940 -3.433  2.014   1.00 10.93 ?  94  HIS   A O    1 
ATOM   2019 C  CB   . HIS   A 1 94  ? 29.824 -0.732  3.130   1.00 9.82  ?  94  HIS   A CB   1 
ATOM   2020 C  CG   . HIS   A 1 94  ? 29.812 0.360   4.143   1.00 9.40  ?  94  HIS   A CG   1 
ATOM   2021 N  ND1  . HIS   A 1 94  ? 28.942 1.424   4.081   1.00 9.79  ?  94  HIS   A ND1  1 
ATOM   2022 C  CD2  . HIS   A 1 94  ? 30.544 0.525   5.266   1.00 10.27 ?  94  HIS   A CD2  1 
ATOM   2023 C  CE1  . HIS   A 1 94  ? 29.155 2.209   5.121   1.00 9.81  ?  94  HIS   A CE1  1 
ATOM   2024 N  NE2  . HIS   A 1 94  ? 30.116 1.680   5.859   1.00 10.34 ?  94  HIS   A NE2  1 
ATOM   2025 H  H    . HIS   A 1 94  ? 30.119 -2.457  4.860   1.00 11.13 ?  94  HIS   A H    1 
ATOM   2026 H  HA   . HIS   A 1 94  ? 27.962 -1.525  3.564   1.00 11.51 ?  94  HIS   A HA   1 
ATOM   2027 H  HB2  . HIS   A 1 94  ? 30.718 -1.079  3.078   1.00 11.78 ?  94  HIS   A HB2  1 
ATOM   2028 H  HB3  . HIS   A 1 94  ? 29.559 -0.345  2.278   1.00 11.78 ?  94  HIS   A HB3  1 
ATOM   2029 H  HD2  . HIS   A 1 94  ? 31.210 -0.034  5.579   1.00 12.33 ?  94  HIS   A HD2  1 
ATOM   2030 H  HE1  . HIS   A 1 94  ? 28.690 2.998   5.307   1.00 11.77 ?  94  HIS   A HE1  1 
ATOM   2031 H  HE2  . HIS   A 1 94  ? 30.426 2.026   6.582   1.00 12.41 ?  94  HIS   A HE2  1 
ATOM   2032 N  N    . VAL   A 1 95  ? 27.705 -3.233  1.803   1.00 8.90  ?  95  VAL   A N    1 
ATOM   2033 C  CA   . VAL   A 1 95  ? 27.567 -4.270  0.781   1.00 9.65  ?  95  VAL   A CA   1 
ATOM   2034 C  C    . VAL   A 1 95  ? 27.020 -3.646  -0.491  1.00 9.14  ?  95  VAL   A C    1 
ATOM   2035 O  O    . VAL   A 1 95  ? 26.016 -2.927  -0.447  1.00 9.69  ?  95  VAL   A O    1 
ATOM   2036 C  CB   . VAL   A 1 95  ? 26.639 -5.410  1.241   1.00 10.19 ?  95  VAL   A CB   1 
ATOM   2037 C  CG1  . VAL   A 1 95  ? 26.543 -6.469  0.149   1.00 10.71 ?  95  VAL   A CG1  1 
ATOM   2038 C  CG2  . VAL   A 1 95  ? 27.136 -6.009  2.536   1.00 10.27 ?  95  VAL   A CG2  1 
ATOM   2039 H  H    . VAL   A 1 95  ? 26.954 -2.865  2.012   1.00 10.67 ?  95  VAL   A H    1 
ATOM   2040 H  HA   . VAL   A 1 95  ? 28.434 -4.649  0.582   1.00 11.58 ?  95  VAL   A HA   1 
ATOM   2041 H  HB   . VAL   A 1 95  ? 25.750 -5.064  1.394   1.00 12.22 ?  95  VAL   A HB   1 
ATOM   2042 H  HG11 . VAL   A 1 95  ? 26.156 -7.279  0.520   1.00 12.85 ?  95  VAL   A HG11 1 
ATOM   2043 H  HG12 . VAL   A 1 95  ? 25.981 -6.139  -0.571  1.00 12.85 ?  95  VAL   A HG12 1 
ATOM   2044 H  HG13 . VAL   A 1 95  ? 27.434 -6.661  -0.191  1.00 12.85 ?  95  VAL   A HG13 1 
ATOM   2045 H  HG21 . VAL   A 1 95  ? 26.588 -6.776  2.763   1.00 12.32 ?  95  VAL   A HG21 1 
ATOM   2046 H  HG22 . VAL   A 1 95  ? 28.060 -6.283  2.424   1.00 12.32 ?  95  VAL   A HG22 1 
ATOM   2047 H  HG23 . VAL   A 1 95  ? 27.072 -5.338  3.234   1.00 12.32 ?  95  VAL   A HG23 1 
ATOM   2048 N  N    . VAL   A 1 96  ? 27.657 -3.940  -1.623  1.00 9.27  ?  96  VAL   A N    1 
ATOM   2049 C  CA   . VAL   A 1 96  ? 27.240 -3.392  -2.908  1.00 9.74  ?  96  VAL   A CA   1 
ATOM   2050 C  C    . VAL   A 1 96  ? 26.444 -4.446  -3.671  1.00 10.19 ?  96  VAL   A C    1 
ATOM   2051 O  O    . VAL   A 1 96  ? 27.011 -5.395  -4.220  1.00 10.86 ?  96  VAL   A O    1 
ATOM   2052 C  CB   . VAL   A 1 96  ? 28.430 -2.918  -3.741  1.00 10.41 ?  96  VAL   A CB   1 
ATOM   2053 C  CG1  . VAL   A 1 96  ? 27.930 -2.285  -5.021  1.00 10.41 ?  96  VAL   A CG1  1 
ATOM   2054 C  CG2  . VAL   A 1 96  ? 29.291 -1.933  -2.959  1.00 10.91 ?  96  VAL   A CG2  1 
ATOM   2055 H  H    . VAL   A 1 96  ? 28.348 -4.453  -1.672  1.00 11.13 ?  96  VAL   A H    1 
ATOM   2056 H  HA   . VAL   A 1 96  ? 26.663 -2.628  -2.756  1.00 11.69 ?  96  VAL   A HA   1 
ATOM   2057 H  HB   . VAL   A 1 96  ? 28.983 -3.674  -3.976  1.00 12.49 ?  96  VAL   A HB   1 
ATOM   2058 H  HG11 . VAL   A 1 96  ? 28.666 -1.804  -5.440  1.00 12.49 ?  96  VAL   A HG11 1 
ATOM   2059 H  HG12 . VAL   A 1 96  ? 27.612 -2.978  -5.615  1.00 12.49 ?  96  VAL   A HG12 1 
ATOM   2060 H  HG13 . VAL   A 1 96  ? 27.215 -1.665  -4.811  1.00 12.49 ?  96  VAL   A HG13 1 
ATOM   2061 H  HG21 . VAL   A 1 96  ? 29.997 -1.597  -3.532  1.00 13.09 ?  96  VAL   A HG21 1 
ATOM   2062 H  HG22 . VAL   A 1 96  ? 28.735 -1.194  -2.656  1.00 13.09 ?  96  VAL   A HG22 1 
ATOM   2063 H  HG23 . VAL   A 1 96  ? 29.676 -2.387  -2.192  1.00 13.09 ?  96  VAL   A HG23 1 
ATOM   2064 N  N    A GLY   A 1 97  ? 25.124 -4.293  -3.691  0.58 10.60 ?  97  GLY   A N    1 
ATOM   2065 N  N    B GLY   A 1 97  ? 25.128 -4.275  -3.743  0.42 10.04 ?  97  GLY   A N    1 
ATOM   2066 C  CA   A GLY   A 1 97  ? 24.302 -5.043  -4.603  0.58 10.88 ?  97  GLY   A CA   1 
ATOM   2067 C  CA   B GLY   A 1 97  ? 24.328 -5.061  -4.649  0.42 9.86  ?  97  GLY   A CA   1 
ATOM   2068 C  C    A GLY   A 1 97  ? 24.269 -4.350  -5.949  0.58 10.83 ?  97  GLY   A C    1 
ATOM   2069 C  C    B GLY   A 1 97  ? 24.389 -4.486  -6.052  0.42 10.27 ?  97  GLY   A C    1 
ATOM   2070 O  O    A GLY   A 1 97  ? 24.523 -3.146  -6.056  0.58 11.35 ?  97  GLY   A O    1 
ATOM   2071 O  O    B GLY   A 1 97  ? 24.746 -3.321  -6.251  0.42 10.77 ?  97  GLY   A O    1 
ATOM   2072 H  H    A GLY   A 1 97  ? 24.688 -3.753  -3.180  0.58 12.72 ?  97  GLY   A H    1 
ATOM   2073 H  H    B GLY   A 1 97  ? 24.681 -3.707  -3.271  0.42 12.05 ?  97  GLY   A H    1 
ATOM   2074 H  HA2  A GLY   A 1 97  ? 24.666 -5.936  -4.703  0.58 13.06 ?  97  GLY   A HA2  1 
ATOM   2075 H  HA2  B GLY   A 1 97  ? 24.663 -5.973  -4.661  0.42 11.83 ?  97  GLY   A HA2  1 
ATOM   2076 H  HA3  A GLY   A 1 97  ? 23.398 -5.110  -4.252  0.58 13.06 ?  97  GLY   A HA3  1 
ATOM   2077 H  HA3  B GLY   A 1 97  ? 23.405 -5.075  -4.341  0.42 11.83 ?  97  GLY   A HA3  1 
ATOM   2078 N  N    A PRO   A 1 98  ? 23.961 -5.093  -7.007  0.58 10.50 ?  98  PRO   A N    1 
ATOM   2079 N  N    B PRO   A 1 98  ? 24.050 -5.292  -7.056  0.42 10.75 ?  98  PRO   A N    1 
ATOM   2080 C  CA   A PRO   A 1 98  ? 23.845 -4.465  -8.326  0.58 11.19 ?  98  PRO   A CA   1 
ATOM   2081 C  CA   B PRO   A 1 98  ? 24.021 -4.778  -8.430  0.42 11.98 ?  98  PRO   A CA   1 
ATOM   2082 C  C    A PRO   A 1 98  ? 22.732 -3.427  -8.351  0.58 10.79 ?  98  PRO   A C    1 
ATOM   2083 C  C    B PRO   A 1 98  ? 22.926 -3.738  -8.622  0.42 12.59 ?  98  PRO   A C    1 
ATOM   2084 O  O    A PRO   A 1 98  ? 21.665 -3.608  -7.759  0.58 11.05 ?  98  PRO   A O    1 
ATOM   2085 O  O    B PRO   A 1 98  ? 21.815 -3.864  -8.101  0.42 13.07 ?  98  PRO   A O    1 
ATOM   2086 C  CB   A PRO   A 1 98  ? 23.538 -5.644  -9.255  0.58 11.49 ?  98  PRO   A CB   1 
ATOM   2087 C  CB   B PRO   A 1 98  ? 23.745 -6.032  -9.268  0.42 11.94 ?  98  PRO   A CB   1 
ATOM   2088 C  CG   A PRO   A 1 98  ? 22.941 -6.691  -8.360  0.58 11.76 ?  98  PRO   A CG   1 
ATOM   2089 C  CG   B PRO   A 1 98  ? 23.040 -6.964  -8.326  0.42 11.77 ?  98  PRO   A CG   1 
ATOM   2090 C  CD   A PRO   A 1 98  ? 23.667 -6.536  -7.048  0.58 11.19 ?  98  PRO   A CD   1 
ATOM   2091 C  CD   B PRO   A 1 98  ? 23.696 -6.722  -6.991  0.42 10.98 ?  98  PRO   A CD   1 
ATOM   2092 H  HA   A PRO   A 1 98  ? 24.685 -4.055  -8.573  0.58 13.43 ?  98  PRO   A HA   1 
ATOM   2093 H  HA   B PRO   A 1 98  ? 24.884 -4.403  -8.673  0.42 14.38 ?  98  PRO   A HA   1 
ATOM   2094 H  HB2  A PRO   A 1 98  ? 22.901 -5.370  -9.930  0.58 13.79 ?  98  PRO   A HB2  1 
ATOM   2095 H  HB2  B PRO   A 1 98  ? 23.177 -5.801  -10.018 0.42 14.32 ?  98  PRO   A HB2  1 
ATOM   2096 H  HB3  A PRO   A 1 98  ? 24.358 -5.965  -9.657  0.58 13.79 ?  98  PRO   A HB3  1 
ATOM   2097 H  HB3  B PRO   A 1 98  ? 24.582 -6.417  -9.570  0.42 14.32 ?  98  PRO   A HB3  1 
ATOM   2098 H  HG2  A PRO   A 1 98  ? 21.992 -6.529  -8.248  0.58 14.11 ?  98  PRO   A HG2  1 
ATOM   2099 H  HG2  B PRO   A 1 98  ? 22.096 -6.739  -8.291  0.42 14.12 ?  98  PRO   A HG2  1 
ATOM   2100 H  HG3  A PRO   A 1 98  ? 23.098 -7.573  -8.736  0.58 14.11 ?  98  PRO   A HG3  1 
ATOM   2101 H  HG3  B PRO   A 1 98  ? 23.166 -7.879  -8.616  0.42 14.12 ?  98  PRO   A HG3  1 
ATOM   2102 H  HD2  A PRO   A 1 98  ? 23.094 -6.800  -6.307  0.58 13.42 ?  98  PRO   A HD2  1 
ATOM   2103 H  HD2  B PRO   A 1 98  ? 23.068 -6.886  -6.269  0.42 13.17 ?  98  PRO   A HD2  1 
ATOM   2104 H  HD3  A PRO   A 1 98  ? 24.495 -7.044  -7.051  0.58 13.42 ?  98  PRO   A HD3  1 
ATOM   2105 H  HD3  B PRO   A 1 98  ? 24.492 -7.274  -6.899  0.42 13.17 ?  98  PRO   A HD3  1 
ATOM   2106 N  N    A ASN   A 1 99  ? 23.003 -2.324  -9.041  0.58 12.03 ?  99  ASN   A N    1 
ATOM   2107 N  N    B ASN   A 1 99  ? 23.254 -2.703  -9.390  0.42 12.98 ?  99  ASN   A N    1 
ATOM   2108 C  CA   A ASN   A 1 99  ? 22.026 -1.265  -9.266  0.58 13.58 ?  99  ASN   A CA   1 
ATOM   2109 C  CA   B ASN   A 1 99  ? 22.315 -1.638  -9.728  0.42 13.95 ?  99  ASN   A CA   1 
ATOM   2110 C  C    A ASN   A 1 99  ? 21.481 -1.430  -10.679 0.58 14.84 ?  99  ASN   A C    1 
ATOM   2111 C  C    B ASN   A 1 99  ? 21.674 -1.976  -11.068 0.42 14.32 ?  99  ASN   A C    1 
ATOM   2112 O  O    A ASN   A 1 99  ? 22.172 -1.128  -11.660 0.58 15.82 ?  99  ASN   A O    1 
ATOM   2113 O  O    B ASN   A 1 99  ? 22.305 -1.839  -12.122 0.42 14.07 ?  99  ASN   A O    1 
ATOM   2114 C  CB   A ASN   A 1 99  ? 22.677 0.104   -9.091  0.58 13.83 ?  99  ASN   A CB   1 
ATOM   2115 C  CB   B ASN   A 1 99  ? 23.045 -0.302  -9.811  0.42 15.09 ?  99  ASN   A CB   1 
ATOM   2116 C  CG   A ASN   A 1 99  ? 21.663 1.242   -9.072  0.58 14.69 ?  99  ASN   A CG   1 
ATOM   2117 C  CG   B ASN   A 1 99  ? 22.119 0.855   -10.142 0.42 16.09 ?  99  ASN   A CG   1 
ATOM   2118 O  OD1  A ASN   A 1 99  ? 20.658 1.207   -9.780  0.58 14.71 ?  99  ASN   A OD1  1 
ATOM   2119 O  OD1  B ASN   A 1 99  ? 21.026 0.664   -10.669 0.42 15.78 ?  99  ASN   A OD1  1 
ATOM   2120 N  ND2  A ASN   A 1 99  ? 21.927 2.254   -8.256  0.58 15.30 ?  99  ASN   A ND2  1 
ATOM   2121 N  ND2  B ASN   A 1 99  ? 22.565 2.068   -9.846  0.42 18.12 ?  99  ASN   A ND2  1 
ATOM   2122 H  H    A ASN   A 1 99  ? 23.773 -2.158  -9.382  0.58 14.44 ?  99  ASN   A H    1 
ATOM   2123 H  H    B ASN   A 1 99  ? 24.037 -2.593  -9.722  0.42 15.58 ?  99  ASN   A H    1 
ATOM   2124 H  HA   A ASN   A 1 99  ? 21.295 -1.354  -8.627  0.58 16.30 ?  99  ASN   A HA   1 
ATOM   2125 H  HA   B ASN   A 1 99  ? 21.620 -1.583  -9.050  0.42 16.74 ?  99  ASN   A HA   1 
ATOM   2126 H  HB2  A ASN   A 1 99  ? 23.166 0.118   -8.256  0.58 16.59 ?  99  ASN   A HB2  1 
ATOM   2127 H  HB2  B ASN   A 1 99  ? 23.465 -0.119  -8.959  0.42 18.10 ?  99  ASN   A HB2  1 
ATOM   2128 H  HB3  A ASN   A 1 99  ? 23.283 0.253   -9.835  0.58 16.59 ?  99  ASN   A HB3  1 
ATOM   2129 H  HB3  B ASN   A 1 99  ? 23.717 -0.358  -10.509 0.42 18.10 ?  99  ASN   A HB3  1 
ATOM   2130 H  HD21 A ASN   A 1 99  ? 21.384 2.918   -8.207  0.58 18.36 ?  99  ASN   A HD21 1 
ATOM   2131 H  HD21 B ASN   A 1 99  ? 22.081 2.759   -10.016 0.42 21.74 ?  99  ASN   A HD21 1 
ATOM   2132 H  HD22 A ASN   A 1 99  ? 22.639 2.242   -7.774  0.58 18.36 ?  99  ASN   A HD22 1 
ATOM   2133 H  HD22 B ASN   A 1 99  ? 23.340 2.163   -9.487  0.42 21.74 ?  99  ASN   A HD22 1 
ATOM   2134 N  N    A VAL   A 1 100 ? 20.240 -1.917  -10.774 0.58 16.24 ?  100 VAL   A N    1 
ATOM   2135 N  N    B VAL   A 1 100 ? 20.413 -2.404  -11.018 0.42 16.07 ?  100 VAL   A N    1 
ATOM   2136 C  CA   A VAL   A 1 100 ? 19.629 -2.166  -12.076 0.58 18.00 ?  100 VAL   A CA   1 
ATOM   2137 C  CA   B VAL   A 1 100 ? 19.690 -2.801  -12.220 0.42 18.21 ?  100 VAL   A CA   1 
ATOM   2138 C  C    A VAL   A 1 100 ? 19.507 -0.870  -12.862 0.58 18.68 ?  100 VAL   A C    1 
ATOM   2139 C  C    B VAL   A 1 100 ? 19.571 -1.639  -13.194 0.42 17.80 ?  100 VAL   A C    1 
ATOM   2140 O  O    A VAL   A 1 100 ? 19.585 -0.872  -14.096 0.58 19.16 ?  100 VAL   A O    1 
ATOM   2141 O  O    B VAL   A 1 100 ? 19.571 -1.838  -14.415 0.42 17.95 ?  100 VAL   A O    1 
ATOM   2142 C  CB   A VAL   A 1 100 ? 18.273 -2.887  -11.906 0.58 19.27 ?  100 VAL   A CB   1 
ATOM   2143 C  CB   B VAL   A 1 100 ? 18.317 -3.383  -11.819 0.42 20.70 ?  100 VAL   A CB   1 
ATOM   2144 C  CG1  A VAL   A 1 100 ? 17.622 -3.154  -13.259 0.58 19.86 ?  100 VAL   A CG1  1 
ATOM   2145 C  CG1  B VAL   A 1 100 ? 17.175 -2.653  -12.522 0.42 21.44 ?  100 VAL   A CG1  1 
ATOM   2146 C  CG2  A VAL   A 1 100 ? 18.463 -4.199  -11.149 0.58 19.58 ?  100 VAL   A CG2  1 
ATOM   2147 C  CG2  B VAL   A 1 100 ? 18.277 -4.871  -12.104 0.42 21.91 ?  100 VAL   A CG2  1 
ATOM   2148 H  H    A VAL   A 1 100 ? 19.729 -2.111  -10.097 0.58 19.49 ?  100 VAL   A H    1 
ATOM   2149 H  H    B VAL   A 1 100 ? 19.956 -2.473  -10.292 0.42 19.28 ?  100 VAL   A H    1 
ATOM   2150 H  HA   A VAL   A 1 100 ? 20.204 -2.765  -12.574 0.58 21.60 ?  100 VAL   A HA   1 
ATOM   2151 H  HA   B VAL   A 1 100 ? 20.186 -3.504  -12.665 0.42 21.85 ?  100 VAL   A HA   1 
ATOM   2152 H  HB   A VAL   A 1 100 ? 17.671 -2.331  -11.387 0.58 23.13 ?  100 VAL   A HB   1 
ATOM   2153 H  HB   B VAL   A 1 100 ? 18.193 -3.265  -10.865 0.42 24.84 ?  100 VAL   A HB   1 
ATOM   2154 H  HG11 A VAL   A 1 100 ? 16.855 -3.738  -13.134 0.58 23.83 ?  100 VAL   A HG11 1 
ATOM   2155 H  HG11 B VAL   A 1 100 ? 16.340 -3.058  -12.245 0.42 25.73 ?  100 VAL   A HG11 1 
ATOM   2156 H  HG12 A VAL   A 1 100 ? 17.334 -2.313  -13.644 0.58 23.83 ?  100 VAL   A HG12 1 
ATOM   2157 H  HG12 B VAL   A 1 100 ? 17.179 -1.717  -12.262 0.42 25.73 ?  100 VAL   A HG12 1 
ATOM   2158 H  HG13 A VAL   A 1 100 ? 18.269 -3.584  -13.841 0.58 23.83 ?  100 VAL   A HG13 1 
ATOM   2159 H  HG13 B VAL   A 1 100 ? 17.275 -2.741  -13.482 0.42 25.73 ?  100 VAL   A HG13 1 
ATOM   2160 H  HG21 A VAL   A 1 100 ? 17.622 -4.685  -11.134 0.58 23.49 ?  100 VAL   A HG21 1 
ATOM   2161 H  HG21 B VAL   A 1 100 ? 17.447 -5.229  -11.759 0.42 26.29 ?  100 VAL   A HG21 1 
ATOM   2162 H  HG22 A VAL   A 1 100 ? 19.140 -4.728  -11.600 0.58 23.49 ?  100 VAL   A HG22 1 
ATOM   2163 H  HG22 B VAL   A 1 100 ? 18.330 -5.011  -13.061 0.42 26.29 ?  100 VAL   A HG22 1 
ATOM   2164 H  HG23 A VAL   A 1 100 ? 18.747 -4.005  -10.242 0.58 23.49 ?  100 VAL   A HG23 1 
ATOM   2165 H  HG23 B VAL   A 1 100 ? 19.030 -5.296  -11.662 0.42 26.29 ?  100 VAL   A HG23 1 
ATOM   2166 N  N    A ASN   A 1 101 ? 19.321 0.253   -12.173 0.58 19.46 ?  101 ASN   A N    1 
ATOM   2167 N  N    B ASN   A 1 101 ? 19.455 -0.412  -12.680 0.42 17.74 ?  101 ASN   A N    1 
ATOM   2168 C  CA   A ASN   A 1 101 ? 19.256 1.540   -12.853 0.58 20.83 ?  101 ASN   A CA   1 
ATOM   2169 C  CA   B ASN   A 1 101 ? 19.325 0.747   -13.555 0.42 18.24 ?  101 ASN   A CA   1 
ATOM   2170 C  C    A ASN   A 1 101 ? 20.608 1.988   -13.403 0.58 22.68 ?  101 ASN   A C    1 
ATOM   2171 C  C    B ASN   A 1 101 ? 20.605 1.028   -14.326 0.42 18.53 ?  101 ASN   A C    1 
ATOM   2172 O  O    A ASN   A 1 101 ? 20.672 3.039   -14.053 0.58 23.79 ?  101 ASN   A O    1 
ATOM   2173 O  O    B ASN   A 1 101 ? 20.554 1.714   -15.352 0.42 18.73 ?  101 ASN   A O    1 
ATOM   2174 C  CB   A ASN   A 1 101 ? 18.652 2.587   -11.916 0.58 19.86 ?  101 ASN   A CB   1 
ATOM   2175 C  CB   B ASN   A 1 101 ? 18.944 1.983   -12.741 0.42 18.44 ?  101 ASN   A CB   1 
ATOM   2176 C  CG   A ASN   A 1 101 ? 17.266 2.196   -11.429 0.58 19.29 ?  101 ASN   A CG   1 
ATOM   2177 C  CG   B ASN   A 1 101 ? 17.696 1.770   -11.907 0.42 19.42 ?  101 ASN   A CG   1 
ATOM   2178 O  OD1  A ASN   A 1 101 ? 16.432 1.731   -12.207 0.58 18.98 ?  101 ASN   A OD1  1 
ATOM   2179 O  OD1  B ASN   A 1 101 ? 16.734 1.141   -12.350 0.42 20.40 ?  101 ASN   A OD1  1 
ATOM   2180 N  ND2  A ASN   A 1 101 ? 17.021 2.362   -10.134 0.58 19.41 ?  101 ASN   A ND2  1 
ATOM   2181 N  ND2  B ASN   A 1 101 ? 17.711 2.283   -10.687 0.42 19.66 ?  101 ASN   A ND2  1 
ATOM   2182 H  H    A ASN   A 1 101 ? 19.217 0.289   -11.324 0.58 23.35 ?  101 ASN   A H    1 
ATOM   2183 H  H    B ASN   A 1 101 ? 19.450 -0.225  -11.840 0.42 21.29 ?  101 ASN   A H    1 
ATOM   2184 H  HA   A ASN   A 1 101 ? 18.657 1.448   -13.609 0.58 25.00 ?  101 ASN   A HA   1 
ATOM   2185 H  HA   B ASN   A 1 101 ? 18.620 0.580   -14.198 0.42 21.89 ?  101 ASN   A HA   1 
ATOM   2186 H  HB2  A ASN   A 1 101 ? 19.228 2.693   -11.146 0.58 23.83 ?  101 ASN   A HB2  1 
ATOM   2187 H  HB2  B ASN   A 1 101 ? 19.675 2.205   -12.142 0.42 22.12 ?  101 ASN   A HB2  1 
ATOM   2188 H  HB3  A ASN   A 1 101 ? 18.573 3.426   -12.396 0.58 23.83 ?  101 ASN   A HB3  1 
ATOM   2189 H  HB3  B ASN   A 1 101 ? 18.780 2.723   -13.350 0.42 22.12 ?  101 ASN   A HB3  1 
ATOM   2190 H  HD21 A ASN   A 1 101 ? 16.253 2.148   -9.809  0.58 23.29 ?  101 ASN   A HD21 1 
ATOM   2191 H  HD21 B ASN   A 1 101 ? 17.027 2.188   -10.178 0.42 23.59 ?  101 ASN   A HD21 1 
ATOM   2192 H  HD22 A ASN   A 1 101 ? 17.628 2.689   -9.620  0.58 23.29 ?  101 ASN   A HD22 1 
ATOM   2193 H  HD22 B ASN   A 1 101 ? 18.400 2.717   -10.412 0.42 23.59 ?  101 ASN   A HD22 1 
ATOM   2194 N  N    A LYS   A 1 102 ? 21.674 1.215   -13.171 0.58 23.78 ?  102 LYS   A N    1 
ATOM   2195 N  N    B LYS   A 1 102 ? 21.745 0.530   -13.846 0.42 19.66 ?  102 LYS   A N    1 
ATOM   2196 C  CA   A LYS   A 1 102 ? 22.963 1.411   -13.822 0.58 24.96 ?  102 LYS   A CA   1 
ATOM   2197 C  CA   B LYS   A 1 102 ? 23.029 0.670   -14.521 0.42 20.42 ?  102 LYS   A CA   1 
ATOM   2198 C  C    A LYS   A 1 102 ? 23.280 0.321   -14.836 0.58 25.35 ?  102 LYS   A C    1 
ATOM   2199 C  C    B LYS   A 1 102 ? 23.382 -0.545  -15.374 0.42 19.66 ?  102 LYS   A C    1 
ATOM   2200 O  O    A LYS   A 1 102 ? 24.347 0.367   -15.455 0.58 25.77 ?  102 LYS   A O    1 
ATOM   2201 O  O    B LYS   A 1 102 ? 24.516 -0.643  -15.853 0.42 19.90 ?  102 LYS   A O    1 
ATOM   2202 C  CB   A LYS   A 1 102 ? 24.089 1.462   -12.781 0.58 25.93 ?  102 LYS   A CB   1 
ATOM   2203 C  CB   B LYS   A 1 102 ? 24.144 0.913   -13.497 0.42 22.75 ?  102 LYS   A CB   1 
ATOM   2204 C  CG   A LYS   A 1 102 ? 23.981 2.601   -11.789 0.58 26.82 ?  102 LYS   A CG   1 
ATOM   2205 C  CG   B LYS   A 1 102 ? 24.137 2.290   -12.851 0.42 24.87 ?  102 LYS   A CG   1 
ATOM   2206 C  CD   A LYS   A 1 102 ? 25.111 2.535   -10.773 0.58 27.81 ?  102 LYS   A CD   1 
ATOM   2207 C  CD   B LYS   A 1 102 ? 25.330 2.453   -11.917 0.42 26.67 ?  102 LYS   A CD   1 
ATOM   2208 C  CE   A LYS   A 1 102 ? 25.067 3.706   -9.809  0.58 28.70 ?  102 LYS   A CE   1 
ATOM   2209 C  CE   B LYS   A 1 102 ? 25.506 3.896   -11.468 0.42 28.09 ?  102 LYS   A CE   1 
ATOM   2210 N  NZ   A LYS   A 1 102 ? 26.105 3.581   -8.745  0.58 29.18 ?  102 LYS   A NZ   1 
ATOM   2211 N  NZ   B LYS   A 1 102 ? 26.708 4.069   -10.600 0.42 28.87 ?  102 LYS   A NZ   1 
ATOM   2212 H  H    A LYS   A 1 102 ? 21.673 0.545   -12.626 0.58 28.54 ?  102 LYS   A H    1 
ATOM   2213 H  H    B LYS   A 1 102 ? 21.800 0.107   -13.098 0.42 23.60 ?  102 LYS   A H    1 
ATOM   2214 H  HA   A LYS   A 1 102 ? 22.955 2.250   -14.295 0.58 29.95 ?  102 LYS   A HA   1 
ATOM   2215 H  HA   B LYS   A 1 102 ? 22.995 1.444   -15.100 0.42 24.51 ?  102 LYS   A HA   1 
ATOM   2216 H  HB2  A LYS   A 1 102 ? 24.088 0.632   -12.279 0.58 31.12 ?  102 LYS   A HB2  1 
ATOM   2217 H  HB2  B LYS   A 1 102 ? 24.062 0.260   -12.785 0.42 27.30 ?  102 LYS   A HB2  1 
ATOM   2218 H  HB3  A LYS   A 1 102 ? 24.936 1.557   -13.247 0.58 31.12 ?  102 LYS   A HB3  1 
ATOM   2219 H  HB3  B LYS   A 1 102 ? 25.001 0.808   -13.939 0.42 27.30 ?  102 LYS   A HB3  1 
ATOM   2220 H  HG2  A LYS   A 1 102 ? 24.040 3.446   -12.262 0.58 32.18 ?  102 LYS   A HG2  1 
ATOM   2221 H  HG2  B LYS   A 1 102 ? 24.193 2.972   -13.540 0.42 29.84 ?  102 LYS   A HG2  1 
ATOM   2222 H  HG3  A LYS   A 1 102 ? 23.136 2.535   -11.317 0.58 32.18 ?  102 LYS   A HG3  1 
ATOM   2223 H  HG3  B LYS   A 1 102 ? 23.324 2.402   -12.332 0.42 29.84 ?  102 LYS   A HG3  1 
ATOM   2224 H  HD2  A LYS   A 1 102 ? 25.030 1.716   -10.259 0.58 33.37 ?  102 LYS   A HD2  1 
ATOM   2225 H  HD2  B LYS   A 1 102 ? 25.195 1.905   -11.127 0.42 32.00 ?  102 LYS   A HD2  1 
ATOM   2226 H  HD3  A LYS   A 1 102 ? 25.961 2.555   -11.240 0.58 33.37 ?  102 LYS   A HD3  1 
ATOM   2227 H  HD3  B LYS   A 1 102 ? 26.138 2.179   -12.379 0.42 32.00 ?  102 LYS   A HD3  1 
ATOM   2228 H  HE2  A LYS   A 1 102 ? 25.232 4.528   -10.300 0.58 34.43 ?  102 LYS   A HE2  1 
ATOM   2229 H  HE2  B LYS   A 1 102 ? 25.614 4.461   -12.249 0.42 33.70 ?  102 LYS   A HE2  1 
ATOM   2230 H  HE3  A LYS   A 1 102 ? 24.196 3.739   -9.385  0.58 34.43 ?  102 LYS   A HE3  1 
ATOM   2231 H  HE3  B LYS   A 1 102 ? 24.726 4.170   -10.962 0.42 33.70 ?  102 LYS   A HE3  1 
ATOM   2232 H  HZ1  A LYS   A 1 102 ? 26.061 4.277   -8.194  0.58 35.02 ?  102 LYS   A HZ1  1 
ATOM   2233 H  HZ1  B LYS   A 1 102 ? 26.786 4.921   -10.354 0.42 34.64 ?  102 LYS   A HZ1  1 
ATOM   2234 H  HZ2  A LYS   A 1 102 ? 25.973 2.833   -8.280  0.58 35.02 ?  102 LYS   A HZ2  1 
ATOM   2235 H  HZ2  B LYS   A 1 102 ? 26.633 3.563   -9.872  0.42 34.64 ?  102 LYS   A HZ2  1 
ATOM   2236 H  HZ3  A LYS   A 1 102 ? 26.915 3.552   -9.113  0.58 35.02 ?  102 LYS   A HZ3  1 
ATOM   2237 H  HZ3  B LYS   A 1 102 ? 27.442 3.829   -11.044 0.42 34.64 ?  102 LYS   A HZ3  1 
ATOM   2238 N  N    A GLY   A 1 103 ? 22.395 -0.658  -15.016 0.58 25.87 ?  103 GLY   A N    1 
ATOM   2239 N  N    B GLY   A 1 103 ? 22.452 -1.478  -15.561 0.42 19.29 ?  103 GLY   A N    1 
ATOM   2240 C  CA   A GLY   A 1 103 ? 22.644 -1.742  -15.946 0.58 26.07 ?  103 GLY   A CA   1 
ATOM   2241 C  CA   B GLY   A 1 103 ? 22.730 -2.672  -16.335 0.42 18.97 ?  103 GLY   A CA   1 
ATOM   2242 C  C    A GLY   A 1 103 ? 23.518 -2.850  -15.410 0.58 26.13 ?  103 GLY   A C    1 
ATOM   2243 C  C    B GLY   A 1 103 ? 23.576 -3.714  -15.636 0.42 17.91 ?  103 GLY   A C    1 
ATOM   2244 O  O    A GLY   A 1 103 ? 24.134 -3.571  -16.200 0.58 26.85 ?  103 GLY   A O    1 
ATOM   2245 O  O    B GLY   A 1 103 ? 24.034 -4.657  -16.292 0.42 18.16 ?  103 GLY   A O    1 
ATOM   2246 H  H    A GLY   A 1 103 ? 21.645 -0.723  -14.605 0.58 31.05 ?  103 GLY   A H    1 
ATOM   2247 H  H    B GLY   A 1 103 ? 21.649 -1.432  -15.250 0.42 23.15 ?  103 GLY   A H    1 
ATOM   2248 H  HA2  A GLY   A 1 103 ? 21.792 -2.119  -16.235 0.58 31.28 ?  103 GLY   A HA2  1 
ATOM   2249 H  HA2  B GLY   A 1 103 ? 21.890 -3.087  -16.576 0.42 22.76 ?  103 GLY   A HA2  1 
ATOM   2250 H  HA3  A GLY   A 1 103 ? 23.094 -1.394  -16.727 0.58 31.28 ?  103 GLY   A HA3  1 
ATOM   2251 H  HA3  B GLY   A 1 103 ? 23.182 -2.409  -17.153 0.42 22.76 ?  103 GLY   A HA3  1 
ATOM   2252 N  N    A GLU   A 1 104 ? 23.604 -3.006  -14.092 0.58 24.98 ?  104 GLU   A N    1 
ATOM   2253 N  N    B GLU   A 1 104 ? 23.792 -3.585  -14.330 0.42 16.65 ?  104 GLU   A N    1 
ATOM   2254 C  CA   A GLU   A 1 104 ? 24.470 -4.009  -13.491 0.58 23.60 ?  104 GLU   A CA   1 
ATOM   2255 C  CA   B GLU   A 1 104 ? 24.644 -4.522  -13.612 0.42 15.47 ?  104 GLU   A CA   1 
ATOM   2256 C  C    A GLU   A 1 104 ? 23.773 -5.363  -13.399 0.58 23.87 ?  104 GLU   A C    1 
ATOM   2257 C  C    B GLU   A 1 104 ? 23.929 -5.858  -13.420 0.42 15.02 ?  104 GLU   A C    1 
ATOM   2258 O  O    A GLU   A 1 104 ? 22.546 -5.451  -13.287 0.58 24.07 ?  104 GLU   A O    1 
ATOM   2259 O  O    B GLU   A 1 104 ? 22.709 -5.920  -13.237 0.42 15.68 ?  104 GLU   A O    1 
ATOM   2260 C  CB   A GLU   A 1 104 ? 24.959 -3.527  -12.122 0.58 21.85 ?  104 GLU   A CB   1 
ATOM   2261 C  CB   B GLU   A 1 104 ? 25.089 -3.911  -12.280 0.42 15.36 ?  104 GLU   A CB   1 
ATOM   2262 C  CG   A GLU   A 1 104 ? 25.927 -2.347  -12.274 0.58 20.87 ?  104 GLU   A CG   1 
ATOM   2263 C  CG   B GLU   A 1 104 ? 25.911 -2.633  -12.477 0.42 16.37 ?  104 GLU   A CG   1 
ATOM   2264 C  CD   A GLU   A 1 104 ? 26.272 -1.606  -10.988 0.58 19.84 ?  104 GLU   A CD   1 
ATOM   2265 C  CD   B GLU   A 1 104 ? 26.203 -1.864  -11.197 0.42 16.96 ?  104 GLU   A CD   1 
ATOM   2266 O  OE1  A GLU   A 1 104 ? 25.653 -1.862  -9.937  0.58 18.22 ?  104 GLU   A OE1  1 
ATOM   2267 O  OE1  B GLU   A 1 104 ? 25.792 -2.299  -10.105 0.42 17.35 ?  104 GLU   A OE1  1 
ATOM   2268 O  OE2  A GLU   A 1 104 ? 27.181 -0.744  -11.049 0.58 20.56 -1 104 GLU   A OE2  1 
ATOM   2269 O  OE2  B GLU   A 1 104 ? 26.842 -0.793  -11.299 0.42 17.44 -1 104 GLU   A OE2  1 
ATOM   2270 H  H    A GLU   A 1 104 ? 23.174 -2.529  -13.519 0.58 29.97 ?  104 GLU   A H    1 
ATOM   2271 H  H    B GLU   A 1 104 ? 23.447 -2.972  -13.837 0.42 19.98 ?  104 GLU   A H    1 
ATOM   2272 H  HA   A GLU   A 1 104 ? 25.243 -4.122  -14.060 0.58 28.32 ?  104 GLU   A HA   1 
ATOM   2273 H  HA   B GLU   A 1 104 ? 25.439 -4.689  -14.140 0.42 18.57 ?  104 GLU   A HA   1 
ATOM   2274 H  HB2  A GLU   A 1 104 ? 24.194 -3.242  -11.596 0.58 26.22 ?  104 GLU   A HB2  1 
ATOM   2275 H  HB2  B GLU   A 1 104 ? 24.308 -3.690  -11.753 0.42 18.43 ?  104 GLU   A HB2  1 
ATOM   2276 H  HB3  A GLU   A 1 104 ? 25.421 -4.255  -11.678 0.58 26.22 ?  104 GLU   A HB3  1 
ATOM   2277 H  HB3  B GLU   A 1 104 ? 25.643 -4.553  -11.806 0.42 18.43 ?  104 GLU   A HB3  1 
ATOM   2278 H  HG2  A GLU   A 1 104 ? 26.757 -2.685  -12.632 0.58 25.05 ?  104 GLU   A HG2  1 
ATOM   2279 H  HG2  B GLU   A 1 104 ? 26.759 -2.866  -12.886 0.42 19.65 ?  104 GLU   A HG2  1 
ATOM   2280 H  HG3  A GLU   A 1 104 ? 25.532 -1.715  -12.896 0.58 25.05 ?  104 GLU   A HG3  1 
ATOM   2281 H  HG3  B GLU   A 1 104 ? 25.420 -2.034  -13.063 0.42 19.65 ?  104 GLU   A HG3  1 
ATOM   2282 N  N    A ASP   A 1 105 ? 24.581 -6.423  -13.448 0.58 24.47 ?  105 ASP   A N    1 
ATOM   2283 N  N    B ASP   A 1 105 ? 24.714 -6.935  -13.469 0.42 14.93 ?  105 ASP   A N    1 
ATOM   2284 C  CA   A ASP   A 1 105 ? 24.079 -7.787  -13.571 0.58 25.19 ?  105 ASP   A CA   1 
ATOM   2285 C  CA   B ASP   A 1 105 ? 24.193 -8.299  -13.537 0.42 15.33 ?  105 ASP   A CA   1 
ATOM   2286 C  C    A ASP   A 1 105 ? 23.398 -8.213  -12.274 0.58 23.64 ?  105 ASP   A C    1 
ATOM   2287 C  C    B ASP   A 1 105 ? 23.460 -8.666  -12.250 0.42 13.81 ?  105 ASP   A C    1 
ATOM   2288 O  O    A ASP   A 1 105 ? 24.015 -8.184  -11.206 0.58 22.96 ?  105 ASP   A O    1 
ATOM   2289 O  O    B ASP   A 1 105 ? 24.058 -8.688  -11.172 0.42 11.74 ?  105 ASP   A O    1 
ATOM   2290 C  CB   A ASP   A 1 105 ? 25.249 -8.716  -13.893 0.58 27.58 ?  105 ASP   A CB   1 
ATOM   2291 C  CB   B ASP   A 1 105 ? 25.371 -9.245  -13.777 0.42 17.50 ?  105 ASP   A CB   1 
ATOM   2292 C  CG   A ASP   A 1 105 ? 24.808 -10.128 -14.197 0.58 29.67 ?  105 ASP   A CG   1 
ATOM   2293 C  CG   B ASP   A 1 105 ? 24.979 -10.709 -13.781 0.42 19.25 ?  105 ASP   A CG   1 
ATOM   2294 O  OD1  A ASP   A 1 105 ? 23.587 -10.359 -14.302 0.58 30.29 ?  105 ASP   A OD1  1 
ATOM   2295 O  OD1  B ASP   A 1 105 ? 23.774 -11.023 -13.852 0.42 19.36 ?  105 ASP   A OD1  1 
ATOM   2296 O  OD2  A ASP   A 1 105 ? 25.689 -11.004 -14.340 0.58 30.71 -1 105 ASP   A OD2  1 
ATOM   2297 O  OD2  B ASP   A 1 105 ? 25.904 -11.552 -13.710 0.42 21.16 -1 105 ASP   A OD2  1 
ATOM   2298 H  H    A ASP   A 1 105 ? 25.438 -6.381  -13.399 0.58 29.36 ?  105 ASP   A H    1 
ATOM   2299 H  H    B ASP   A 1 105 ? 25.575 -6.902  -13.463 0.42 17.92 ?  105 ASP   A H    1 
ATOM   2300 H  HA   A ASP   A 1 105 ? 23.436 -7.848  -14.294 0.58 30.22 ?  105 ASP   A HA   1 
ATOM   2301 H  HA   B ASP   A 1 105 ? 23.572 -8.374  -14.276 0.42 18.39 ?  105 ASP   A HA   1 
ATOM   2302 H  HB2  A ASP   A 1 105 ? 25.714 -8.387  -14.679 0.58 33.10 ?  105 ASP   A HB2  1 
ATOM   2303 H  HB2  B ASP   A 1 105 ? 25.771 -9.033  -14.636 0.42 21.00 ?  105 ASP   A HB2  1 
ATOM   2304 H  HB3  A ASP   A 1 105 ? 25.858 -8.743  -13.137 0.58 33.10 ?  105 ASP   A HB3  1 
ATOM   2305 H  HB3  B ASP   A 1 105 ? 26.021 -9.129  -13.070 0.42 21.00 ?  105 ASP   A HB3  1 
ATOM   2306 N  N    A ILE   A 1 106 ? 22.129 -8.622  -12.370 0.58 22.80 ?  106 ILE   A N    1 
ATOM   2307 N  N    B ILE   A 1 106 ? 22.167 -8.980  -12.365 0.42 15.13 ?  106 ILE   A N    1 
ATOM   2308 C  CA   A ILE   A 1 106 ? 21.365 -9.001  -11.185 0.58 21.87 ?  106 ILE   A CA   1 
ATOM   2309 C  CA   B ILE   A 1 106 ? 21.386 -9.344  -11.189 0.42 16.11 ?  106 ILE   A CA   1 
ATOM   2310 C  C    A ILE   A 1 106 ? 21.887 -10.286 -10.556 0.58 20.50 ?  106 ILE   A C    1 
ATOM   2311 C  C    B ILE   A 1 106 ? 21.943 -10.591 -10.523 0.42 16.48 ?  106 ILE   A C    1 
ATOM   2312 O  O    A ILE   A 1 106 ? 21.650 -10.523 -9.367  0.58 19.62 ?  106 ILE   A O    1 
ATOM   2313 O  O    B ILE   A 1 106 ? 21.747 -10.787 -9.319  0.42 16.64 ?  106 ILE   A O    1 
ATOM   2314 C  CB   A ILE   A 1 106 ? 19.858 -9.082  -11.512 0.58 23.06 ?  106 ILE   A CB   1 
ATOM   2315 C  CB   B ILE   A 1 106 ? 19.889 -9.489  -11.544 0.42 17.64 ?  106 ILE   A CB   1 
ATOM   2316 C  CG1  A ILE   A 1 106 ? 19.019 -9.116  -10.229 0.58 23.60 ?  106 ILE   A CG1  1 
ATOM   2317 C  CG1  B ILE   A 1 106 ? 19.031 -9.576  -10.277 0.42 18.39 ?  106 ILE   A CG1  1 
ATOM   2318 C  CG2  A ILE   A 1 106 ? 19.556 -10.307 -12.365 0.58 23.50 ?  106 ILE   A CG2  1 
ATOM   2319 C  CG2  B ILE   A 1 106 ? 19.664 -10.718 -12.391 0.42 18.10 ?  106 ILE   A CG2  1 
ATOM   2320 C  CD1  A ILE   A 1 106 ? 19.194 -7.897  -9.346  0.58 24.18 ?  106 ILE   A CD1  1 
ATOM   2321 C  CD1  B ILE   A 1 106 ? 19.036 -8.320  -9.436  0.42 18.75 ?  106 ILE   A CD1  1 
ATOM   2322 H  H    A ILE   A 1 106 ? 21.693 -8.687  -13.105 0.58 27.36 ?  106 ILE   A H    1 
ATOM   2323 H  H    B ILE   A 1 106 ? 21.734 -8.998  -13.106 0.42 18.16 ?  106 ILE   A H    1 
ATOM   2324 H  HA   A ILE   A 1 106 ? 21.487 -8.306  -10.527 0.58 26.24 ?  106 ILE   A HA   1 
ATOM   2325 H  HA   B ILE   A 1 106 ? 21.466 -8.626  -10.549 0.42 19.33 ?  106 ILE   A HA   1 
ATOM   2326 H  HB   A ILE   A 1 106 ? 19.611 -8.294  -12.016 0.58 27.67 ?  106 ILE   A HB   1 
ATOM   2327 H  HB   B ILE   A 1 106 ? 19.616 -8.705  -12.048 0.42 21.17 ?  106 ILE   A HB   1 
ATOM   2328 H  HG12 A ILE   A 1 106 ? 18.080 -9.172  -10.472 0.58 28.31 ?  106 ILE   A HG12 1 
ATOM   2329 H  HG12 B ILE   A 1 106 ? 18.113 -9.750  -10.535 0.42 22.07 ?  106 ILE   A HG12 1 
ATOM   2330 H  HG13 A ILE   A 1 106 ? 19.268 -9.897  -9.711  0.58 28.31 ?  106 ILE   A HG13 1 
ATOM   2331 H  HG13 B ILE   A 1 106 ? 19.358 -10.302 -9.723  0.42 22.07 ?  106 ILE   A HG13 1 
ATOM   2332 H  HG21 A ILE   A 1 106 ? 18.658 -10.227 -12.724 0.58 28.20 ?  106 ILE   A HG21 1 
ATOM   2333 H  HG21 B ILE   A 1 106 ? 18.773 -10.677 -12.767 0.42 21.72 ?  106 ILE   A HG21 1 
ATOM   2334 H  HG22 A ILE   A 1 106 ? 20.199 -10.351 -13.089 0.58 28.20 ?  106 ILE   A HG22 1 
ATOM   2335 H  HG22 B ILE   A 1 106 ? 20.326 -10.735 -13.096 0.42 21.72 ?  106 ILE   A HG22 1 
ATOM   2336 H  HG23 A ILE   A 1 106 ? 19.621 -11.103 -11.815 0.58 28.20 ?  106 ILE   A HG23 1 
ATOM   2337 H  HG23 B ILE   A 1 106 ? 19.754 -11.504 -11.830 0.42 21.72 ?  106 ILE   A HG23 1 
ATOM   2338 H  HD11 A ILE   A 1 106 ? 18.458 -7.857  -8.718  0.58 29.02 ?  106 ILE   A HD11 1 
ATOM   2339 H  HD11 B ILE   A 1 106 ? 18.335 -8.384  -8.769  0.42 22.50 ?  106 ILE   A HD11 1 
ATOM   2340 H  HD12 A ILE   A 1 106 ? 20.035 -7.972  -8.868  0.58 29.02 ?  106 ILE   A HD12 1 
ATOM   2341 H  HD12 B ILE   A 1 106 ? 19.899 -8.235  -8.998  0.42 22.50 ?  106 ILE   A HD12 1 
ATOM   2342 H  HD13 A ILE   A 1 106 ? 19.197 -7.103  -9.904  0.58 29.02 ?  106 ILE   A HD13 1 
ATOM   2343 H  HD13 B ILE   A 1 106 ? 18.879 -7.555  -10.010 0.42 22.50 ?  106 ILE   A HD13 1 
ATOM   2344 N  N    A GLN   A 1 107 ? 22.609 -11.115 -11.322 0.58 20.95 ?  107 GLN   A N    1 
ATOM   2345 N  N    B GLN   A 1 107 ? 22.651 -11.438 -11.278 0.42 17.43 ?  107 GLN   A N    1 
ATOM   2346 C  CA   A GLN   A 1 107 ? 23.181 -12.345 -10.774 0.58 22.50 ?  107 GLN   A CA   1 
ATOM   2347 C  CA   B GLN   A 1 107 ? 23.331 -12.576 -10.675 0.42 19.70 ?  107 GLN   A CA   1 
ATOM   2348 C  C    A GLN   A 1 107 ? 24.145 -12.053 -9.629  0.58 19.75 ?  107 GLN   A C    1 
ATOM   2349 C  C    B GLN   A 1 107 ? 24.339 -12.140 -9.623  0.42 18.28 ?  107 GLN   A C    1 
ATOM   2350 O  O    A GLN   A 1 107 ? 24.304 -12.875 -8.718  0.58 20.52 ?  107 GLN   A O    1 
ATOM   2351 O  O    B GLN   A 1 107 ? 24.713 -12.948 -8.764  0.42 19.16 ?  107 GLN   A O    1 
ATOM   2352 C  CB   A GLN   A 1 107 ? 23.887 -13.122 -11.890 0.58 26.56 ?  107 GLN   A CB   1 
ATOM   2353 C  CB   B GLN   A 1 107 ? 24.014 -13.420 -11.756 0.42 23.04 ?  107 GLN   A CB   1 
ATOM   2354 C  CG   A GLN   A 1 107 ? 23.044 -13.311 -13.150 0.58 30.73 ?  107 GLN   A CG   1 
ATOM   2355 C  CG   B GLN   A 1 107 ? 23.052 -13.963 -12.806 0.42 26.23 ?  107 GLN   A CG   1 
ATOM   2356 C  CD   A GLN   A 1 107 ? 21.755 -14.065 -12.883 0.58 33.98 ?  107 GLN   A CD   1 
ATOM   2357 C  CD   B GLN   A 1 107 ? 21.946 -14.807 -12.203 0.42 28.99 ?  107 GLN   A CD   1 
ATOM   2358 O  OE1  A GLN   A 1 107 ? 21.763 -15.136 -12.276 0.58 35.35 ?  107 GLN   A OE1  1 
ATOM   2359 O  OE1  B GLN   A 1 107 ? 22.200 -15.691 -11.383 0.42 30.04 ?  107 GLN   A OE1  1 
ATOM   2360 N  NE2  A GLN   A 1 107 ? 20.637 -13.505 -13.331 0.58 35.08 ?  107 GLN   A NE2  1 
ATOM   2361 N  NE2  B GLN   A 1 107 ? 20.706 -14.534 -12.602 0.42 29.90 ?  107 GLN   A NE2  1 
ATOM   2362 H  H    A GLN   A 1 107 ? 22.788 -10.979 -12.150 0.58 25.14 ?  107 GLN   A H    1 
ATOM   2363 H  H    B GLN   A 1 107 ? 22.752 -11.373 -12.130 0.42 20.92 ?  107 GLN   A H    1 
ATOM   2364 H  HA   A GLN   A 1 107 ? 22.471 -12.902 -10.429 0.58 27.00 ?  107 GLN   A HA   1 
ATOM   2365 H  HA   B GLN   A 1 107 ? 22.676 -13.136 -10.240 0.42 23.64 ?  107 GLN   A HA   1 
ATOM   2366 H  HB2  A GLN   A 1 107 ? 24.694 -12.648 -12.148 0.58 31.88 ?  107 GLN   A HB2  1 
ATOM   2367 H  HB2  B GLN   A 1 107 ? 24.676 -12.877 -12.212 0.42 27.65 ?  107 GLN   A HB2  1 
ATOM   2368 H  HB3  A GLN   A 1 107 ? 24.119 -14.006 -11.563 0.58 31.88 ?  107 GLN   A HB3  1 
ATOM   2369 H  HB3  B GLN   A 1 107 ? 24.448 -14.179 -11.335 0.42 27.65 ?  107 GLN   A HB3  1 
ATOM   2370 H  HG2  A GLN   A 1 107 ? 22.812 -12.444 -13.518 0.58 36.88 ?  107 GLN   A HG2  1 
ATOM   2371 H  HG2  B GLN   A 1 107 ? 22.642 -13.219 -13.275 0.42 31.47 ?  107 GLN   A HG2  1 
ATOM   2372 H  HG3  A GLN   A 1 107 ? 23.558 -13.815 -13.801 0.58 36.88 ?  107 GLN   A HG3  1 
ATOM   2373 H  HG3  B GLN   A 1 107 ? 23.545 -14.518 -13.432 0.42 31.47 ?  107 GLN   A HG3  1 
ATOM   2374 H  HE21 A GLN   A 1 107 ? 20.669 -12.756 -13.750 0.58 42.09 ?  107 GLN   A HE21 1 
ATOM   2375 H  HE21 B GLN   A 1 107 ? 20.567 -13.907 -13.175 0.42 35.88 ?  107 GLN   A HE21 1 
ATOM   2376 H  HE22 A GLN   A 1 107 ? 19.882 -13.896 -13.204 0.58 42.09 ?  107 GLN   A HE22 1 
ATOM   2377 H  HE22 B GLN   A 1 107 ? 20.042 -14.983 -12.289 0.42 35.88 ?  107 GLN   A HE22 1 
ATOM   2378 N  N    . LEU   A 1 108 ? 24.777 -10.878 -9.650  1.00 16.60 ?  108 LEU   A N    1 
ATOM   2379 C  CA   . LEU   A 1 108 ? 25.687 -10.427 -8.608  1.00 14.73 ?  108 LEU   A CA   1 
ATOM   2380 C  C    . LEU   A 1 108 ? 24.981 -10.228 -7.277  1.00 12.92 ?  108 LEU   A C    1 
ATOM   2381 O  O    . LEU   A 1 108 ? 25.661 -10.052 -6.264  1.00 13.49 ?  108 LEU   A O    1 
ATOM   2382 C  CB   . LEU   A 1 108 ? 26.402 -9.140  -9.042  1.00 14.69 ?  108 LEU   A CB   1 
ATOM   2383 C  CG   . LEU   A 1 108 ? 27.397 -9.351  -10.184 1.00 16.32 ?  108 LEU   A CG   1 
ATOM   2384 C  CD1  . LEU   A 1 108 ? 27.864 -8.022  -10.766 1.00 17.18 ?  108 LEU   A CD1  1 
ATOM   2385 C  CD2  . LEU   A 1 108 ? 28.590 -10.162 -9.707  1.00 18.14 ?  108 LEU   A CD2  1 
ATOM   2386 H  H    A LEU   A 1 108 ? 24.688 -10.310 -10.281 0.58 19.92 ?  108 LEU   A H    1 
ATOM   2387 H  H    B LEU   A 1 108 ? 24.579 -10.297 -10.243 0.42 19.92 ?  108 LEU   A H    1 
ATOM   2388 H  HA   . LEU   A 1 108 ? 26.362 -11.103 -8.467  1.00 17.68 ?  108 LEU   A HA   1 
ATOM   2389 H  HB2  . LEU   A 1 108 ? 25.739 -8.499  -9.342  1.00 17.63 ?  108 LEU   A HB2  1 
ATOM   2390 H  HB3  . LEU   A 1 108 ? 26.889 -8.781  -8.286  1.00 17.63 ?  108 LEU   A HB3  1 
ATOM   2391 H  HG   . LEU   A 1 108 ? 26.963 -9.853  -10.893 1.00 19.59 ?  108 LEU   A HG   1 
ATOM   2392 H  HD11 . LEU   A 1 108 ? 28.477 -8.197  -11.503 1.00 20.61 ?  108 LEU   A HD11 1 
ATOM   2393 H  HD12 . LEU   A 1 108 ? 27.096 -7.529  -11.090 1.00 20.61 ?  108 LEU   A HD12 1 
ATOM   2394 H  HD13 . LEU   A 1 108 ? 28.319 -7.515  -10.076 1.00 20.61 ?  108 LEU   A HD13 1 
ATOM   2395 H  HD21 . LEU   A 1 108 ? 29.281 -10.131 -10.384 1.00 21.76 ?  108 LEU   A HD21 1 
ATOM   2396 H  HD22 . LEU   A 1 108 ? 28.917 -9.778  -8.879  1.00 21.76 ?  108 LEU   A HD22 1 
ATOM   2397 H  HD23 . LEU   A 1 108 ? 28.309 -11.078 -9.559  1.00 21.76 ?  108 LEU   A HD23 1 
ATOM   2398 N  N    . LEU   A 1 109 ? 23.645 -10.267 -7.246  1.00 12.33 ?  109 LEU   A N    1 
ATOM   2399 C  CA   . LEU   A 1 109 ? 22.944 -10.139 -5.975  1.00 11.86 ?  109 LEU   A CA   1 
ATOM   2400 C  C    . LEU   A 1 109 ? 23.274 -11.298 -5.043  1.00 11.00 ?  109 LEU   A C    1 
ATOM   2401 O  O    . LEU   A 1 109 ? 23.397 -11.110 -3.828  1.00 11.48 ?  109 LEU   A O    1 
ATOM   2402 C  CB   . LEU   A 1 109 ? 21.440 -10.040 -6.228  1.00 12.80 ?  109 LEU   A CB   1 
ATOM   2403 C  CG   . LEU   A 1 109 ? 20.551 -9.752  -5.020  1.00 12.92 ?  109 LEU   A CG   1 
ATOM   2404 C  CD1  . LEU   A 1 109 ? 21.017 -8.496  -4.305  1.00 13.05 ?  109 LEU   A CD1  1 
ATOM   2405 C  CD2  . LEU   A 1 109 ? 19.098 -9.595  -5.457  1.00 14.13 ?  109 LEU   A CD2  1 
ATOM   2406 H  H    . LEU   A 1 109 ? 23.133 -10.360 -7.930  1.00 14.80 ?  109 LEU   A H    1 
ATOM   2407 H  HA   . LEU   A 1 109 ? 23.230 -9.314  -5.544  1.00 14.23 ?  109 LEU   A HA   1 
ATOM   2408 H  HB2  . LEU   A 1 109 ? 21.287 -9.327  -6.870  1.00 15.36 ?  109 LEU   A HB2  1 
ATOM   2409 H  HB3  . LEU   A 1 109 ? 21.142 -10.879 -6.605  1.00 15.36 ?  109 LEU   A HB3  1 
ATOM   2410 H  HG   . LEU   A 1 109 ? 20.607 -10.489 -4.397  1.00 15.51 ?  109 LEU   A HG   1 
ATOM   2411 H  HD11 . LEU   A 1 109 ? 20.328 -8.200  -3.694  1.00 15.66 ?  109 LEU   A HD11 1 
ATOM   2412 H  HD12 . LEU   A 1 109 ? 21.835 -8.686  -3.818  1.00 15.66 ?  109 LEU   A HD12 1 
ATOM   2413 H  HD13 . LEU   A 1 109 ? 21.187 -7.797  -4.966  1.00 15.66 ?  109 LEU   A HD13 1 
ATOM   2414 H  HD21 . LEU   A 1 109 ? 18.565 -9.322  -4.692  1.00 16.96 ?  109 LEU   A HD21 1 
ATOM   2415 H  HD22 . LEU   A 1 109 ? 19.045 -8.921  -6.152  1.00 16.96 ?  109 LEU   A HD22 1 
ATOM   2416 H  HD23 . LEU   A 1 109 ? 18.777 -10.446 -5.796  1.00 16.96 ?  109 LEU   A HD23 1 
ATOM   2417 N  N    . LYS   A 1 110 ? 23.424 -12.508 -5.586  1.00 11.25 ?  110 LYS   A N    1 
ATOM   2418 C  CA   . LYS   A 1 110 ? 23.798 -13.627 -4.732  1.00 11.23 ?  110 LYS   A CA   1 
ATOM   2419 C  C    . LYS   A 1 110 ? 25.179 -13.411 -4.124  1.00 10.79 ?  110 LYS   A C    1 
ATOM   2420 O  O    . LYS   A 1 110 ? 25.372 -13.611 -2.921  1.00 11.09 ?  110 LYS   A O    1 
ATOM   2421 C  CB   . LYS   A 1 110 ? 23.716 -14.951 -5.493  1.00 12.03 ?  110 LYS   A CB   1 
ATOM   2422 C  CG   . LYS   A 1 110 ? 23.925 -16.161 -4.584  1.00 12.20 ?  110 LYS   A CG   1 
ATOM   2423 C  CD   . LYS   A 1 110 ? 23.683 -17.485 -5.297  1.00 12.99 ?  110 LYS   A CD   1 
ATOM   2424 C  CE   . LYS   A 1 110 ? 23.786 -18.667 -4.347  1.00 14.07 ?  110 LYS   A CE   1 
ATOM   2425 N  NZ   . LYS   A 1 110 ? 22.612 -18.794 -3.452  1.00 14.28 ?  110 LYS   A NZ   1 
ATOM   2426 H  H    . LYS   A 1 110 ? 23.322 -12.695 -6.415  1.00 13.50 ?  110 LYS   A H    1 
ATOM   2427 H  HA   . LYS   A 1 110 ? 23.162 -13.676 -3.997  1.00 13.48 ?  110 LYS   A HA   1 
ATOM   2428 H  HB2  . LYS   A 1 110 ? 22.840 -15.031 -5.899  1.00 14.44 ?  110 LYS   A HB2  1 
ATOM   2429 H  HB3  . LYS   A 1 110 ? 24.405 -14.969 -6.173  1.00 14.44 ?  110 LYS   A HB3  1 
ATOM   2430 H  HG2  . LYS   A 1 110 ? 24.837 -16.158 -4.251  1.00 14.63 ?  110 LYS   A HG2  1 
ATOM   2431 H  HG3  . LYS   A 1 110 ? 23.304 -16.107 -3.836  1.00 14.63 ?  110 LYS   A HG3  1 
ATOM   2432 H  HD2  . LYS   A 1 110 ? 22.798 -17.484 -5.682  1.00 15.59 ?  110 LYS   A HD2  1 
ATOM   2433 H  HD3  . LYS   A 1 110 ? 24.355 -17.597 -5.989  1.00 15.59 ?  110 LYS   A HD3  1 
ATOM   2434 H  HE2  . LYS   A 1 110 ? 23.859 -19.486 -4.863  1.00 16.89 ?  110 LYS   A HE2  1 
ATOM   2435 H  HE3  . LYS   A 1 110 ? 24.574 -18.562 -3.787  1.00 16.89 ?  110 LYS   A HE3  1 
ATOM   2436 H  HZ1  . LYS   A 1 110 ? 22.704 -19.495 -2.915  1.00 17.14 ?  110 LYS   A HZ1  1 
ATOM   2437 H  HZ2  . LYS   A 1 110 ? 22.522 -18.058 -2.958  1.00 17.14 ?  110 LYS   A HZ2  1 
ATOM   2438 H  HZ3  . LYS   A 1 110 ? 21.869 -18.901 -3.939  1.00 17.14 ?  110 LYS   A HZ3  1 
ATOM   2439 N  N    . SER   A 1 111 ? 26.140 -12.966 -4.936  1.00 11.00 ?  111 SER   A N    1 
ATOM   2440 C  CA   . SER   A 1 111 ? 27.469 -12.661 -4.420  1.00 11.05 ?  111 SER   A CA   1 
ATOM   2441 C  C    . SER   A 1 111 ? 27.405 -11.616 -3.316  1.00 10.63 ?  111 SER   A C    1 
ATOM   2442 O  O    . SER   A 1 111 ? 28.098 -11.724 -2.298  1.00 11.43 ?  111 SER   A O    1 
ATOM   2443 C  CB   . SER   A 1 111 ? 28.349 -12.166 -5.564  1.00 12.35 ?  111 SER   A CB   1 
ATOM   2444 O  OG   . SER   A 1 111 ? 28.432 -13.147 -6.586  1.00 14.16 ?  111 SER   A OG   1 
ATOM   2445 H  H    . SER   A 1 111 ? 26.038 -12.835 -5.778  1.00 13.20 ?  111 SER   A H    1 
ATOM   2446 H  HA   . SER   A 1 111 ? 27.865 -13.469 -4.059  1.00 13.26 ?  111 SER   A HA   1 
ATOM   2447 H  HB2  . SER   A 1 111 ? 27.957 -11.361 -5.941  1.00 14.82 ?  111 SER   A HB2  1 
ATOM   2448 H  HB3  . SER   A 1 111 ? 29.235 -11.978 -5.226  1.00 14.82 ?  111 SER   A HB3  1 
ATOM   2449 H  HG   . SER   A 1 111 ? 28.928 -12.868 -7.214  1.00 16.99 ?  111 SER   A HG   1 
ATOM   2450 N  N    . ALA   A 1 112 ? 26.560 -10.604 -3.496  1.00 10.67 ?  112 ALA   A N    1 
ATOM   2451 C  CA   . ALA   A 1 112 ? 26.417 -9.568  -2.478  1.00 10.77 ?  112 ALA   A CA   1 
ATOM   2452 C  C    . ALA   A 1 112 ? 25.930 -10.163 -1.158  1.00 10.43 ?  112 ALA   A C    1 
ATOM   2453 O  O    . ALA   A 1 112 ? 26.478 -9.872  -0.089  1.00 10.81 ?  112 ALA   A O    1 
ATOM   2454 C  CB   . ALA   A 1 112 ? 25.458 -8.486  -2.971  1.00 11.31 ?  112 ALA   A CB   1 
ATOM   2455 H  H    . ALA   A 1 112 ? 26.061 -10.492 -4.187  1.00 12.81 ?  112 ALA   A H    1 
ATOM   2456 H  HA   . ALA   A 1 112 ? 27.279 -9.152  -2.320  1.00 12.92 ?  112 ALA   A HA   1 
ATOM   2457 H  HB1  . ALA   A 1 112 ? 25.381 -7.793  -2.289  1.00 13.58 ?  112 ALA   A HB1  1 
ATOM   2458 H  HB2  . ALA   A 1 112 ? 25.809 -8.097  -3.788  1.00 13.58 ?  112 ALA   A HB2  1 
ATOM   2459 H  HB3  . ALA   A 1 112 ? 24.589 -8.879  -3.136  1.00 13.58 ?  112 ALA   A HB3  1 
ATOM   2460 N  N    . TYR   A 1 113 ? 24.889 -10.998 -1.209  1.00 10.52 ?  113 TYR   A N    1 
ATOM   2461 C  CA   . TYR   A 1 113 ? 24.376 -11.599 0.017   1.00 10.36 ?  113 TYR   A CA   1 
ATOM   2462 C  C    . TYR   A 1 113 ? 25.377 -12.553 0.665   1.00 9.91  ?  113 TYR   A C    1 
ATOM   2463 O  O    . TYR   A 1 113 ? 25.331 -12.744 1.884   1.00 10.57 ?  113 TYR   A O    1 
ATOM   2464 C  CB   . TYR   A 1 113 ? 23.048 -12.313 -0.253  1.00 10.73 ?  113 TYR   A CB   1 
ATOM   2465 C  CG   . TYR   A 1 113 ? 21.842 -11.401 -0.183  1.00 10.48 ?  113 TYR   A CG   1 
ATOM   2466 C  CD1  . TYR   A 1 113 ? 21.484 -10.789 1.009   1.00 10.90 ?  113 TYR   A CD1  1 
ATOM   2467 C  CD2  . TYR   A 1 113 ? 21.041 -11.174 -1.301  1.00 10.72 ?  113 TYR   A CD2  1 
ATOM   2468 C  CE1  . TYR   A 1 113 ? 20.365 -9.976  1.090   1.00 11.41 ?  113 TYR   A CE1  1 
ATOM   2469 C  CE2  . TYR   A 1 113 ? 19.903 -10.356 -1.227  1.00 11.20 ?  113 TYR   A CE2  1 
ATOM   2470 C  CZ   . TYR   A 1 113 ? 19.579 -9.761  -0.026  1.00 11.18 ?  113 TYR   A CZ   1 
ATOM   2471 O  OH   . TYR   A 1 113 ? 18.467 -8.954  0.101   1.00 11.76 ?  113 TYR   A OH   1 
ATOM   2472 H  H    . TYR   A 1 113 ? 24.477 -11.225 -1.929  1.00 12.63 ?  113 TYR   A H    1 
ATOM   2473 H  HA   . TYR   A 1 113 ? 24.205 -10.892 0.653   1.00 12.44 ?  113 TYR   A HA   1 
ATOM   2474 H  HB2  . TYR   A 1 113 ? 23.074 -12.698 -1.144  1.00 12.87 ?  113 TYR   A HB2  1 
ATOM   2475 H  HB3  . TYR   A 1 113 ? 22.930 -13.014 0.404   1.00 12.87 ?  113 TYR   A HB3  1 
ATOM   2476 H  HD1  . TYR   A 1 113 ? 22.003 -10.936 1.767   1.00 13.08 ?  113 TYR   A HD1  1 
ATOM   2477 H  HD2  . TYR   A 1 113 ? 21.251 -11.581 -2.109  1.00 12.86 ?  113 TYR   A HD2  1 
ATOM   2478 H  HE1  . TYR   A 1 113 ? 20.146 -9.577  1.899   1.00 13.69 ?  113 TYR   A HE1  1 
ATOM   2479 H  HE2  . TYR   A 1 113 ? 19.371 -10.208 -1.979  1.00 13.44 ?  113 TYR   A HE2  1 
ATOM   2480 H  HH   . TYR   A 1 113 ? 18.075 -8.897  -0.646  1.00 14.11 ?  113 TYR   A HH   1 
ATOM   2481 N  N    . GLU   A 1 114 ? 26.271 -13.177 -0.120  1.00 10.63 ?  114 GLU   A N    1 
ATOM   2482 C  CA   . GLU   A 1 114 ? 27.269 -14.068 0.473   1.00 10.58 ?  114 GLU   A CA   1 
ATOM   2483 C  C    . GLU   A 1 114 ? 28.123 -13.362 1.519   1.00 10.92 ?  114 GLU   A C    1 
ATOM   2484 O  O    . GLU   A 1 114 ? 28.588 -13.997 2.475   1.00 11.08 ?  114 GLU   A O    1 
ATOM   2485 C  CB   . GLU   A 1 114 ? 28.136 -14.720 -0.614  1.00 10.90 ?  114 GLU   A CB   1 
ATOM   2486 C  CG   . GLU   A 1 114 ? 27.375 -15.774 -1.395  1.00 11.00 ?  114 GLU   A CG   1 
ATOM   2487 C  CD   . GLU   A 1 114 ? 28.091 -16.300 -2.630  1.00 11.62 ?  114 GLU   A CD   1 
ATOM   2488 O  OE1  . GLU   A 1 114 ? 29.038 -15.669 -3.135  1.00 11.96 ?  114 GLU   A OE1  1 
ATOM   2489 O  OE2  . GLU   A 1 114 ? 27.638 -17.360 -3.122  1.00 12.86 -1 114 GLU   A OE2  1 
ATOM   2490 H  H    . GLU   A 1 114 ? 26.321 -13.097 -0.982  1.00 12.76 ?  114 GLU   A H    1 
ATOM   2491 H  HA   . GLU   A 1 114 ? 26.801 -14.782 0.921   1.00 12.70 ?  114 GLU   A HA   1 
ATOM   2492 H  HB2  . GLU   A 1 114 ? 28.431 -14.042 -1.244  1.00 13.08 ?  114 GLU   A HB2  1 
ATOM   2493 H  HB3  . GLU   A 1 114 ? 28.900 -15.149 -0.203  1.00 13.08 ?  114 GLU   A HB3  1 
ATOM   2494 H  HG2  . GLU   A 1 114 ? 27.209 -16.534 -0.813  1.00 13.20 ?  114 GLU   A HG2  1 
ATOM   2495 H  HG3  . GLU   A 1 114 ? 26.526 -15.399 -1.683  1.00 13.20 ?  114 GLU   A HG3  1 
ATOM   2496 N  N    . ASN   A 1 115 ? 28.310 -12.045 1.387   1.00 10.58 ?  115 ASN   A N    1 
ATOM   2497 C  CA   . ASN   A 1 115 ? 29.077 -11.322 2.394   1.00 10.71 ?  115 ASN   A CA   1 
ATOM   2498 C  C    . ASN   A 1 115 ? 28.458 -11.453 3.778   1.00 10.31 ?  115 ASN   A C    1 
ATOM   2499 O  O    . ASN   A 1 115 ? 29.171 -11.380 4.787   1.00 10.95 ?  115 ASN   A O    1 
ATOM   2500 C  CB   . ASN   A 1 115 ? 29.198 -9.847  2.018   1.00 11.40 ?  115 ASN   A CB   1 
ATOM   2501 C  CG   . ASN   A 1 115 ? 29.988 -9.638  0.755   1.00 12.15 ?  115 ASN   A CG   1 
ATOM   2502 O  OD1  . ASN   A 1 115 ? 31.201 -9.760  0.763   1.00 15.35 ?  115 ASN   A OD1  1 
ATOM   2503 N  ND2  . ASN   A 1 115 ? 29.311 -9.327  -0.334  1.00 11.58 ?  115 ASN   A ND2  1 
ATOM   2504 H  H    . ASN   A 1 115 ? 28.012 -11.558 0.740   1.00 12.70 ?  115 ASN   A H    1 
ATOM   2505 H  HA   . ASN   A 1 115 ? 29.968 -11.690 2.437   1.00 12.85 ?  115 ASN   A HA   1 
ATOM   2506 H  HB2  . ASN   A 1 115 ? 28.307 -9.475  1.892   1.00 13.68 ?  115 ASN   A HB2  1 
ATOM   2507 H  HB3  . ASN   A 1 115 ? 29.646 -9.372  2.742   1.00 13.68 ?  115 ASN   A HB3  1 
ATOM   2508 H  HD21 . ASN   A 1 115 ? 29.724 -9.200  -1.077  1.00 13.89 ?  115 ASN   A HD21 1 
ATOM   2509 H  HD22 . ASN   A 1 115 ? 28.451 -9.273  -0.306  1.00 13.89 ?  115 ASN   A HD22 1 
ATOM   2510 N  N    . PHE   A 1 116 ? 27.130 -11.617 3.855   1.00 10.53 ?  116 PHE   A N    1 
ATOM   2511 C  CA   . PHE   A 1 116 ? 26.480 -11.711 5.159   1.00 10.71 ?  116 PHE   A CA   1 
ATOM   2512 C  C    . PHE   A 1 116 ? 26.951 -12.939 5.932   1.00 10.94 ?  116 PHE   A C    1 
ATOM   2513 O  O    . PHE   A 1 116 ? 26.885 -12.954 7.162   1.00 11.35 ?  116 PHE   A O    1 
ATOM   2514 C  CB   . PHE   A 1 116 ? 24.950 -11.836 5.027   1.00 10.64 ?  116 PHE   A CB   1 
ATOM   2515 C  CG   . PHE   A 1 116 ? 24.199 -10.591 4.555   1.00 10.62 ?  116 PHE   A CG   1 
ATOM   2516 C  CD1  . PHE   A 1 116 ? 24.776 -9.578  3.797   1.00 10.34 ?  116 PHE   A CD1  1 
ATOM   2517 C  CD2  . PHE   A 1 116 ? 22.841 -10.479 4.875   1.00 11.11 ?  116 PHE   A CD2  1 
ATOM   2518 C  CE1  . PHE   A 1 116 ? 24.014 -8.504  3.369   1.00 10.77 ?  116 PHE   A CE1  1 
ATOM   2519 C  CE2  . PHE   A 1 116 ? 22.085 -9.406  4.457   1.00 11.06 ?  116 PHE   A CE2  1 
ATOM   2520 C  CZ   . PHE   A 1 116 ? 22.664 -8.417  3.705   1.00 10.47 ?  116 PHE   A CZ   1 
ATOM   2521 H  H    . PHE   A 1 116 ? 26.593 -11.666 3.179   1.00 12.63 ?  116 PHE   A H    1 
ATOM   2522 H  HA   . PHE   A 1 116 ? 26.676 -10.919 5.681   1.00 12.85 ?  116 PHE   A HA   1 
ATOM   2523 H  HB2  . PHE   A 1 116 ? 24.758 -12.549 4.394   1.00 12.77 ?  116 PHE   A HB2  1 
ATOM   2524 H  HB3  . PHE   A 1 116 ? 24.590 -12.079 5.896   1.00 12.77 ?  116 PHE   A HB3  1 
ATOM   2525 H  HD1  . PHE   A 1 116 ? 25.671 -9.641  3.562   1.00 12.41 ?  116 PHE   A HD1  1 
ATOM   2526 H  HD2  . PHE   A 1 116 ? 22.433 -11.158 5.374   1.00 13.33 ?  116 PHE   A HD2  1 
ATOM   2527 H  HE1  . PHE   A 1 116 ? 24.413 -7.828  2.870   1.00 12.92 ?  116 PHE   A HE1  1 
ATOM   2528 H  HE2  . PHE   A 1 116 ? 21.185 -9.357  4.686   1.00 13.27 ?  116 PHE   A HE2  1 
ATOM   2529 H  HZ   . PHE   A 1 116 ? 22.160 -7.686  3.434   1.00 12.56 ?  116 PHE   A HZ   1 
ATOM   2530 N  N    . ASN   A 1 117 ? 27.398 -13.987 5.231   1.00 11.16 ?  117 ASN   A N    1 
ATOM   2531 C  CA   . ASN   A 1 117 ? 27.761 -15.231 5.908   1.00 11.54 ?  117 ASN   A CA   1 
ATOM   2532 C  C    . ASN   A 1 117 ? 29.019 -15.110 6.746   1.00 11.72 ?  117 ASN   A C    1 
ATOM   2533 O  O    . ASN   A 1 117 ? 29.315 -16.024 7.524   1.00 12.81 ?  117 ASN   A O    1 
ATOM   2534 C  CB   . ASN   A 1 117 ? 27.874 -16.362 4.896   1.00 11.56 ?  117 ASN   A CB   1 
ATOM   2535 C  CG   . ASN   A 1 117 ? 26.527 -16.735 4.350   1.00 11.52 ?  117 ASN   A CG   1 
ATOM   2536 O  OD1  . ASN   A 1 117 ? 25.549 -16.763 5.094   1.00 12.50 ?  117 ASN   A OD1  1 
ATOM   2537 N  ND2  . ASN   A 1 117 ? 26.449 -16.995 3.058   1.00 11.44 ?  117 ASN   A ND2  1 
ATOM   2538 H  H    . ASN   A 1 117 ? 27.476 -14.008 4.371   1.00 13.39 ?  117 ASN   A H    1 
ATOM   2539 H  HA   . ASN   A 1 117 ? 27.037 -15.463 6.511   1.00 13.85 ?  117 ASN   A HA   1 
ATOM   2540 H  HB2  . ASN   A 1 117 ? 28.435 -16.080 4.157   1.00 13.87 ?  117 ASN   A HB2  1 
ATOM   2541 H  HB3  . ASN   A 1 117 ? 28.252 -17.143 5.329   1.00 13.87 ?  117 ASN   A HB3  1 
ATOM   2542 H  HD21 . ASN   A 1 117 ? 25.694 -17.209 2.712   1.00 13.73 ?  117 ASN   A HD21 1 
ATOM   2543 H  HD22 . ASN   A 1 117 ? 27.156 -16.959 2.573   1.00 13.73 ?  117 ASN   A HD22 1 
ATOM   2544 N  N    . GLN   A 1 118 ? 29.743 -13.999 6.626   1.00 11.79 ?  118 GLN   A N    1 
ATOM   2545 C  CA   . GLN   A 1 118 ? 30.920 -13.760 7.447   1.00 12.65 ?  118 GLN   A CA   1 
ATOM   2546 C  C    . GLN   A 1 118 ? 30.575 -13.180 8.814   1.00 12.60 ?  118 GLN   A C    1 
ATOM   2547 O  O    . GLN   A 1 118 ? 31.492 -12.886 9.592   1.00 13.82 ?  118 GLN   A O    1 
ATOM   2548 C  CB   . GLN   A 1 118 ? 31.916 -12.861 6.704   1.00 12.56 ?  118 GLN   A CB   1 
ATOM   2549 C  CG   . GLN   A 1 118 ? 32.391 -13.447 5.384   1.00 12.80 ?  118 GLN   A CG   1 
ATOM   2550 C  CD   . GLN   A 1 118 ? 33.222 -14.703 5.569   1.00 13.06 ?  118 GLN   A CD   1 
ATOM   2551 O  OE1  . GLN   A 1 118 ? 34.080 -14.773 6.459   1.00 13.71 ?  118 GLN   A OE1  1 
ATOM   2552 N  NE2  . GLN   A 1 118 ? 32.975 -15.702 4.721   1.00 13.16 ?  118 GLN   A NE2  1 
ATOM   2553 H  H    . GLN   A 1 118 ? 29.563 -13.358 6.075   1.00 14.15 ?  118 GLN   A H    1 
ATOM   2554 H  HA   . GLN   A 1 118 ? 31.351 -14.617 7.600   1.00 15.18 ?  118 GLN   A HA   1 
ATOM   2555 H  HB2  . GLN   A 1 118 ? 31.494 -12.011 6.523   1.00 15.07 ?  118 GLN   A HB2  1 
ATOM   2556 H  HB3  . GLN   A 1 118 ? 32.695 -12.733 7.270   1.00 15.07 ?  118 GLN   A HB3  1 
ATOM   2557 H  HG2  . GLN   A 1 118 ? 31.619 -13.669 4.836   1.00 15.36 ?  118 GLN   A HG2  1 
ATOM   2558 H  HG3  . GLN   A 1 118 ? 32.940 -12.789 4.925   1.00 15.36 ?  118 GLN   A HG3  1 
ATOM   2559 H  HE21 . GLN   A 1 118 ? 32.365 -15.612 4.109   1.00 15.79 ?  118 GLN   A HE21 1 
ATOM   2560 H  HE22 . GLN   A 1 118 ? 33.414 -16.437 4.772   1.00 15.79 ?  118 GLN   A HE22 1 
ATOM   2561 N  N    . HIS   A 1 119 ? 29.285 -13.020 9.122   1.00 12.43 ?  119 HIS   A N    1 
ATOM   2562 C  CA   . HIS   A 1 119 ? 28.831 -12.407 10.363  1.00 12.50 ?  119 HIS   A CA   1 
ATOM   2563 C  C    . HIS   A 1 119 ? 27.691 -13.229 10.937  1.00 12.66 ?  119 HIS   A C    1 
ATOM   2564 O  O    . HIS   A 1 119 ? 26.750 -13.572 10.221  1.00 13.04 ?  119 HIS   A O    1 
ATOM   2565 C  CB   . HIS   A 1 119 ? 28.378 -10.974 10.080  1.00 12.83 ?  119 HIS   A CB   1 
ATOM   2566 C  CG   . HIS   A 1 119 ? 29.463 -10.163 9.471   1.00 14.15 ?  119 HIS   A CG   1 
ATOM   2567 N  ND1  . HIS   A 1 119 ? 30.434 -9.551  10.229  1.00 16.53 ?  119 HIS   A ND1  1 
ATOM   2568 C  CD2  . HIS   A 1 119 ? 29.808 -9.968  8.178   1.00 15.11 ?  119 HIS   A CD2  1 
ATOM   2569 C  CE1  . HIS   A 1 119 ? 31.302 -8.962  9.427   1.00 17.08 ?  119 HIS   A CE1  1 
ATOM   2570 N  NE2  . HIS   A 1 119 ? 30.956 -9.213  8.177   1.00 17.03 ?  119 HIS   A NE2  1 
ATOM   2571 H  H    . HIS   A 1 119 ? 28.633 -13.282 8.618   1.00 14.92 ?  119 HIS   A H    1 
ATOM   2572 H  HA   . HIS   A 1 119 ? 29.559 -12.392 11.004  1.00 15.00 ?  119 HIS   A HA   1 
ATOM   2573 H  HB2  . HIS   A 1 119 ? 27.628 -10.998 9.466   1.00 15.39 ?  119 HIS   A HB2  1 
ATOM   2574 H  HB3  . HIS   A 1 119 ? 28.116 -10.560 10.916  1.00 15.39 ?  119 HIS   A HB3  1 
ATOM   2575 H  HD1  . HIS   A 1 119 ? 30.460 -9.536  11.087  1.00 19.84 ?  119 HIS   A HD1  1 
ATOM   2576 H  HD2  . HIS   A 1 119 ? 29.352 -10.282 7.430   1.00 18.13 ?  119 HIS   A HD2  1 
ATOM   2577 H  HE1  . HIS   A 1 119 ? 32.038 -8.461  9.695   1.00 20.49 ?  119 HIS   A HE1  1 
ATOM   2578 N  N    . GLU   A 1 120 ? 27.765 -13.522 12.235  1.00 13.41 ?  120 GLU   A N    1 
ATOM   2579 C  CA   . GLU   A 1 120 ? 26.808 -14.449 12.833  1.00 15.68 ?  120 GLU   A CA   1 
ATOM   2580 C  C    . GLU   A 1 120 ? 25.393 -13.885 12.886  1.00 14.18 ?  120 GLU   A C    1 
ATOM   2581 O  O    . GLU   A 1 120 ? 24.424 -14.650 12.769  1.00 14.27 ?  120 GLU   A O    1 
ATOM   2582 C  CB   . GLU   A 1 120 ? 27.275 -14.845 14.235  1.00 20.76 ?  120 GLU   A CB   1 
ATOM   2583 C  CG   . GLU   A 1 120 ? 28.495 -15.749 14.242  1.00 27.74 ?  120 GLU   A CG   1 
ATOM   2584 C  CD   . GLU   A 1 120 ? 28.665 -16.485 15.551  1.00 34.43 ?  120 GLU   A CD   1 
ATOM   2585 O  OE1  . GLU   A 1 120 ? 28.271 -15.930 16.599  1.00 36.52 ?  120 GLU   A OE1  1 
ATOM   2586 O  OE2  . GLU   A 1 120 ? 29.189 -17.619 15.532  1.00 39.35 -1 120 GLU   A OE2  1 
ATOM   2587 H  H    . GLU   A 1 120 ? 28.353 -13.202 12.784  1.00 16.09 ?  120 GLU   A H    1 
ATOM   2588 H  HA   . GLU   A 1 120 ? 26.788 -15.255 12.303  1.00 18.82 ?  120 GLU   A HA   1 
ATOM   2589 H  HB2  . GLU   A 1 120 ? 27.506 -14.050 14.740  1.00 24.91 ?  120 GLU   A HB2  1 
ATOM   2590 H  HB3  . GLU   A 1 120 ? 26.560 -15.323 14.688  1.00 24.91 ?  120 GLU   A HB3  1 
ATOM   2591 H  HG2  . GLU   A 1 120 ? 28.417 -16.403 13.530  1.00 33.29 ?  120 GLU   A HG2  1 
ATOM   2592 H  HG3  . GLU   A 1 120 ? 29.295 -15.217 14.123  1.00 33.29 ?  120 GLU   A HG3  1 
ATOM   2593 N  N    . VAL   A 1 121 ? 25.260 -12.574 13.098  1.00 13.65 ?  121 VAL   A N    1 
ATOM   2594 C  CA   . VAL   A 1 121 ? 23.965 -11.906 13.213  1.00 13.67 ?  121 VAL   A CA   1 
ATOM   2595 C  C    . VAL   A 1 121 ? 24.074 -10.531 12.566  1.00 12.15 ?  121 VAL   A C    1 
ATOM   2596 O  O    . VAL   A 1 121 ? 25.038 -9.800  12.811  1.00 12.76 ?  121 VAL   A O    1 
ATOM   2597 C  CB   . VAL   A 1 121 ? 23.522 -11.748 14.685  1.00 16.69 ?  121 VAL   A CB   1 
ATOM   2598 C  CG1  . VAL   A 1 121 ? 22.126 -11.138 14.754  1.00 17.09 ?  121 VAL   A CG1  1 
ATOM   2599 C  CG2  . VAL   A 1 121 ? 23.558 -13.069 15.435  1.00 19.05 ?  121 VAL   A CG2  1 
ATOM   2600 H  H    . VAL   A 1 121 ? 25.927 -12.033 13.186  1.00 16.37 ?  121 VAL   A H    1 
ATOM   2601 H  HA   . VAL   A 1 121 ? 23.295 -12.424 12.744  1.00 16.40 ?  121 VAL   A HA   1 
ATOM   2602 H  HB   . VAL   A 1 121 ? 24.128 -11.138 15.132  1.00 20.02 ?  121 VAL   A HB   1 
ATOM   2603 H  HG11 . VAL   A 1 121 ? 21.802 -11.191 15.669  1.00 20.51 ?  121 VAL   A HG11 1 
ATOM   2604 H  HG12 . VAL   A 1 121 ? 22.165 -10.212 14.473  1.00 20.51 ?  121 VAL   A HG12 1 
ATOM   2605 H  HG13 . VAL   A 1 121 ? 21.533 -11.638 14.169  1.00 20.51 ?  121 VAL   A HG13 1 
ATOM   2606 H  HG21 . VAL   A 1 121 ? 23.205 -12.934 16.333  1.00 22.86 ?  121 VAL   A HG21 1 
ATOM   2607 H  HG22 . VAL   A 1 121 ? 23.008 -13.716 14.964  1.00 22.86 ?  121 VAL   A HG22 1 
ATOM   2608 H  HG23 . VAL   A 1 121 ? 24.471 -13.382 15.484  1.00 22.86 ?  121 VAL   A HG23 1 
ATOM   2609 N  N    . LEU   A 1 122 ? 23.068 -10.156 11.773  1.00 11.59 ?  122 LEU   A N    1 
ATOM   2610 C  CA   . LEU   A 1 122 ? 23.066 -8.866  11.089  1.00 11.09 ?  122 LEU   A CA   1 
ATOM   2611 C  C    . LEU   A 1 122 ? 21.665 -8.277  11.055  1.00 10.76 ?  122 LEU   A C    1 
ATOM   2612 O  O    . LEU   A 1 122 ? 20.678 -8.999  10.907  1.00 12.15 ?  122 LEU   A O    1 
ATOM   2613 C  CB   . LEU   A 1 122 ? 23.496 -8.974  9.619   1.00 12.73 ?  122 LEU   A CB   1 
ATOM   2614 C  CG   . LEU   A 1 122 ? 24.721 -9.812  9.281   1.00 12.74 ?  122 LEU   A CG   1 
ATOM   2615 C  CD1  . LEU   A 1 122 ? 24.338 -11.271 9.063   1.00 13.61 ?  122 LEU   A CD1  1 
ATOM   2616 C  CD2  . LEU   A 1 122 ? 25.418 -9.249  8.056   1.00 12.48 ?  122 LEU   A CD2  1 
ATOM   2617 H  H    . LEU   A 1 122 ? 22.368 -10.631 11.613  1.00 13.90 ?  122 LEU   A H    1 
ATOM   2618 H  HA   . LEU   A 1 122 ? 23.661 -8.246  11.543  1.00 13.31 ?  122 LEU   A HA   1 
ATOM   2619 H  HB2  . LEU   A 1 122 ? 22.763 -9.357  9.120   1.00 15.28 ?  122 LEU   A HB2  1 
ATOM   2620 H  HB3  . LEU   A 1 122 ? 23.680 -8.084  9.292   1.00 15.28 ?  122 LEU   A HB3  1 
ATOM   2621 H  HG   . LEU   A 1 122 ? 25.357 -9.782  10.016  1.00 15.29 ?  122 LEU   A HG   1 
ATOM   2622 H  HD11 . LEU   A 1 122 ? 25.127 -11.782 8.813   1.00 16.34 ?  122 LEU   A HD11 1 
ATOM   2623 H  HD12 . LEU   A 1 122 ? 23.966 -11.628 9.885   1.00 16.34 ?  122 LEU   A HD12 1 
ATOM   2624 H  HD13 . LEU   A 1 122 ? 23.678 -11.324 8.353   1.00 16.34 ?  122 LEU   A HD13 1 
ATOM   2625 H  HD21 . LEU   A 1 122 ? 26.176 -9.812  7.822   1.00 14.97 ?  122 LEU   A HD21 1 
ATOM   2626 H  HD22 . LEU   A 1 122 ? 24.791 -9.220  7.318   1.00 14.97 ?  122 LEU   A HD22 1 
ATOM   2627 H  HD23 . LEU   A 1 122 ? 25.733 -8.349  8.256   1.00 14.97 ?  122 LEU   A HD23 1 
ATOM   2628 N  N    . LEU   A 1 123 ? 21.601 -6.946  11.150  1.00 11.03 ?  123 LEU   A N    1 
ATOM   2629 C  CA   . LEU   A 1 123 ? 20.433 -6.150  10.775  1.00 10.68 ?  123 LEU   A CA   1 
ATOM   2630 C  C    . LEU   A 1 123 ? 20.679 -5.638  9.362   1.00 10.39 ?  123 LEU   A C    1 
ATOM   2631 O  O    . LEU   A 1 123 ? 21.732 -5.048  9.111   1.00 10.75 ?  123 LEU   A O    1 
ATOM   2632 C  CB   . LEU   A 1 123 ? 20.313 -4.959  11.727  1.00 11.21 ?  123 LEU   A CB   1 
ATOM   2633 C  CG   . LEU   A 1 123 ? 19.263 -3.900  11.387  1.00 12.05 ?  123 LEU   A CG   1 
ATOM   2634 C  CD1  . LEU   A 1 123 ? 17.853 -4.483  11.374  1.00 12.65 ?  123 LEU   A CD1  1 
ATOM   2635 C  CD2  . LEU   A 1 123 ? 19.367 -2.731  12.364  1.00 12.80 ?  123 LEU   A CD2  1 
ATOM   2636 H  H    . LEU   A 1 123 ? 22.252 -6.463  11.443  1.00 13.23 ?  123 LEU   A H    1 
ATOM   2637 H  HA   . LEU   A 1 123 ? 19.624 -6.685  10.804  1.00 12.82 ?  123 LEU   A HA   1 
ATOM   2638 H  HB2  . LEU   A 1 123 ? 20.096 -5.294  12.612  1.00 13.45 ?  123 LEU   A HB2  1 
ATOM   2639 H  HB3  . LEU   A 1 123 ? 21.169 -4.505  11.760  1.00 13.45 ?  123 LEU   A HB3  1 
ATOM   2640 H  HG   . LEU   A 1 123 ? 19.441 -3.548  10.499  1.00 14.46 ?  123 LEU   A HG   1 
ATOM   2641 H  HD11 . LEU   A 1 123 ? 17.214 -3.781  11.186  1.00 15.18 ?  123 LEU   A HD11 1 
ATOM   2642 H  HD12 . LEU   A 1 123 ? 17.800 -5.172  10.691  1.00 15.18 ?  123 LEU   A HD12 1 
ATOM   2643 H  HD13 . LEU   A 1 123 ? 17.665 -4.875  12.246  1.00 15.18 ?  123 LEU   A HD13 1 
ATOM   2644 H  HD21 . LEU   A 1 123 ? 18.695 -2.069  12.142  1.00 15.36 ?  123 LEU   A HD21 1 
ATOM   2645 H  HD22 . LEU   A 1 123 ? 19.213 -3.066  13.267  1.00 15.36 ?  123 LEU   A HD22 1 
ATOM   2646 H  HD23 . LEU   A 1 123 ? 20.252 -2.346  12.304  1.00 15.36 ?  123 LEU   A HD23 1 
ATOM   2647 N  N    A ALA   A 1 124 ? 19.709 -5.802  8.460   0.58 9.66  ?  124 ALA   A N    1 
ATOM   2648 N  N    B ALA   A 1 124 ? 19.746 -5.891  8.443   0.42 10.38 ?  124 ALA   A N    1 
ATOM   2649 C  CA   A ALA   A 1 124 ? 20.000 -5.515  7.062   0.58 9.51  ?  124 ALA   A CA   1 
ATOM   2650 C  CA   B ALA   A 1 124 ? 20.023 -5.651  7.033   0.42 10.43 ?  124 ALA   A CA   1 
ATOM   2651 C  C    A ALA   A 1 124 ? 18.753 -5.066  6.315   0.58 9.68  ?  124 ALA   A C    1 
ATOM   2652 C  C    B ALA   A 1 124 ? 18.790 -5.164  6.284   0.42 9.88  ?  124 ALA   A C    1 
ATOM   2653 O  O    A ALA   A 1 124 ? 17.627 -5.403  6.702   0.58 10.50 ?  124 ALA   A O    1 
ATOM   2654 O  O    B ALA   A 1 124 ? 17.654 -5.487  6.655   0.42 10.43 ?  124 ALA   A O    1 
ATOM   2655 C  CB   A ALA   A 1 124 ? 20.595 -6.736  6.356   0.58 9.60  ?  124 ALA   A CB   1 
ATOM   2656 C  CB   B ALA   A 1 124 ? 20.546 -6.917  6.336   0.42 10.61 ?  124 ALA   A CB   1 
ATOM   2657 H  H    A ALA   A 1 124 ? 18.904 -6.076  8.628   0.58 11.59 ?  124 ALA   A H    1 
ATOM   2658 H  H    B ALA   A 1 124 ? 18.956 -6.202  8.603   0.42 12.45 ?  124 ALA   A H    1 
ATOM   2659 H  HA   A ALA   A 1 124 ? 20.647 -4.801  7.032   0.58 11.41 ?  124 ALA   A HA   1 
ATOM   2660 H  HA   B ALA   A 1 124 ? 20.717 -4.980  6.968   0.42 12.52 ?  124 ALA   A HA   1 
ATOM   2661 H  HB1  A ALA   A 1 124 ? 20.780 -6.508  5.431   0.58 11.52 ?  124 ALA   A HB1  1 
ATOM   2662 H  HB1  B ALA   A 1 124 ? 20.729 -6.721  5.400   0.42 12.73 ?  124 ALA   A HB1  1 
ATOM   2663 H  HB2  A ALA   A 1 124 ? 21.425 -6.983  6.803   0.58 11.52 ?  124 ALA   A HB2  1 
ATOM   2664 H  HB2  B ALA   A 1 124 ? 21.369 -7.208  6.770   0.42 12.73 ?  124 ALA   A HB2  1 
ATOM   2665 H  HB3  A ALA   A 1 124 ? 19.968 -7.471  6.399   0.58 11.52 ?  124 ALA   A HB3  1 
ATOM   2666 H  HB3  B ALA   A 1 124 ? 19.880 -7.619  6.398   0.42 12.73 ?  124 ALA   A HB3  1 
ATOM   2667 N  N    A PRO   A 1 125 ? 18.932 -4.330  5.220   0.58 10.01 ?  125 PRO   A N    1 
ATOM   2668 N  N    B PRO   A 1 125 ? 18.996 -4.407  5.200   0.42 8.94  ?  125 PRO   A N    1 
ATOM   2669 C  CA   A PRO   A 1 125 ? 17.876 -4.115  4.232   0.58 10.25 ?  125 PRO   A CA   1 
ATOM   2670 C  CA   B PRO   A 1 125 ? 17.893 -4.032  4.314   0.42 9.31  ?  125 PRO   A CA   1 
ATOM   2671 C  C    A PRO   A 1 125 ? 17.938 -5.188  3.150   0.58 9.73  ?  125 PRO   A C    1 
ATOM   2672 C  C    B PRO   A 1 125 ? 17.819 -5.024  3.170   0.42 9.61  ?  125 PRO   A C    1 
ATOM   2673 O  O    A PRO   A 1 125 ? 18.903 -5.952  3.046   0.58 9.81  ?  125 PRO   A O    1 
ATOM   2674 O  O    B PRO   A 1 125 ? 18.703 -5.879  3.051   0.42 10.44 ?  125 PRO   A O    1 
ATOM   2675 C  CB   A PRO   A 1 125 ? 18.299 -2.772  3.624   0.58 10.57 ?  125 PRO   A CB   1 
ATOM   2676 C  CB   B PRO   A 1 125 ? 18.354 -2.671  3.792   0.42 9.16  ?  125 PRO   A CB   1 
ATOM   2677 C  CG   A PRO   A 1 125 ? 19.813 -2.911  3.558   0.58 11.15 ?  125 PRO   A CG   1 
ATOM   2678 C  CG   B PRO   A 1 125 ? 19.861 -2.886  3.613   0.42 9.00  ?  125 PRO   A CG   1 
ATOM   2679 C  CD   A PRO   A 1 125 ? 20.168 -3.605  4.861   0.58 10.86 ?  125 PRO   A CD   1 
ATOM   2680 C  CD   B PRO   A 1 125 ? 20.280 -3.872  4.704   0.42 8.28  ?  125 PRO   A CD   1 
ATOM   2681 H  HA   A PRO   A 1 125 ? 16.994 -4.065  4.629   0.58 12.30 ?  125 PRO   A HA   1 
ATOM   2682 H  HA   B PRO   A 1 125 ? 17.049 -3.965  4.792   0.42 11.18 ?  125 PRO   A HA   1 
ATOM   2683 H  HB2  A PRO   A 1 125 ? 17.912 -2.664  2.740   0.58 12.69 ?  125 PRO   A HB2  1 
ATOM   2684 H  HB2  B PRO   A 1 125 ? 17.919 -2.473  2.945   0.42 10.99 ?  125 PRO   A HB2  1 
ATOM   2685 H  HB3  A PRO   A 1 125 ? 18.037 -2.042  4.211   0.58 12.69 ?  125 PRO   A HB3  1 
ATOM   2686 H  HB3  B PRO   A 1 125 ? 18.168 -1.981  4.450   0.42 10.99 ?  125 PRO   A HB3  1 
ATOM   2687 H  HG2  A PRO   A 1 125 ? 20.064 -3.460  2.795   0.58 13.38 ?  125 PRO   A HG2  1 
ATOM   2688 H  HG2  B PRO   A 1 125 ? 20.031 -3.258  2.733   0.42 10.80 ?  125 PRO   A HG2  1 
ATOM   2689 H  HG3  A PRO   A 1 125 ? 20.228 -2.036  3.502   0.58 13.38 ?  125 PRO   A HG3  1 
ATOM   2690 H  HG3  B PRO   A 1 125 ? 20.323 -2.040  3.719   0.42 10.80 ?  125 PRO   A HG3  1 
ATOM   2691 H  HD2  A PRO   A 1 125 ? 20.901 -4.222  4.732   0.58 13.03 ?  125 PRO   A HD2  1 
ATOM   2692 H  HD2  B PRO   A 1 125 ? 20.830 -4.577  4.323   0.42 9.94  ?  125 PRO   A HD2  1 
ATOM   2693 H  HD3  A PRO   A 1 125 ? 20.376 -2.944  5.546   0.58 13.03 ?  125 PRO   A HD3  1 
ATOM   2694 H  HD3  B PRO   A 1 125 ? 20.749 -3.401  5.411   0.42 9.94  ?  125 PRO   A HD3  1 
ATOM   2695 N  N    A LEU   A 1 126 ? 16.900 -5.203  2.316   0.58 9.81  ?  126 LEU   A N    1 
ATOM   2696 N  N    B LEU   A 1 126 ? 16.817 -4.915  2.303   0.42 9.78  ?  126 LEU   A N    1 
ATOM   2697 C  CA   A LEU   A 1 126 ? 16.906 -6.030  1.118   0.58 10.37 ?  126 LEU   A CA   1 
ATOM   2698 C  CA   B LEU   A 1 126 ? 16.801 -5.721  1.088   0.42 9.79  ?  126 LEU   A CA   1 
ATOM   2699 C  C    A LEU   A 1 126 ? 17.819 -5.414  0.066   0.58 10.57 ?  126 LEU   A C    1 
ATOM   2700 C  C    B LEU   A 1 126 ? 17.758 -5.108  0.070   0.42 9.75  ?  126 LEU   A C    1 
ATOM   2701 O  O    A LEU   A 1 126 ? 17.587 -4.297  -0.403  0.58 11.63 ?  126 LEU   A O    1 
ATOM   2702 O  O    B LEU   A 1 126 ? 17.526 -4.005  -0.437  0.42 10.83 ?  126 LEU   A O    1 
ATOM   2703 C  CB   A LEU   A 1 126 ? 15.489 -6.186  0.579   0.58 10.47 ?  126 LEU   A CB   1 
ATOM   2704 C  CB   B LEU   A 1 126 ? 15.389 -5.828  0.526   0.42 10.68 ?  126 LEU   A CB   1 
ATOM   2705 C  CG   A LEU   A 1 126 ? 14.624 -7.168  1.364   0.58 11.42 ?  126 LEU   A CG   1 
ATOM   2706 C  CG   B LEU   A 1 126 ? 14.444 -6.754  1.294   0.42 11.04 ?  126 LEU   A CG   1 
ATOM   2707 C  CD1  A LEU   A 1 126 ? 13.183 -7.045  0.937   0.58 12.93 ?  126 LEU   A CD1  1 
ATOM   2708 C  CD1  B LEU   A 1 126 ? 13.080 -6.733  0.634   0.42 11.79 ?  126 LEU   A CD1  1 
ATOM   2709 C  CD2  A LEU   A 1 126 ? 15.131 -8.600  1.170   0.58 11.50 ?  126 LEU   A CD2  1 
ATOM   2710 C  CD2  B LEU   A 1 126 ? 14.974 -8.185  1.387   0.42 11.34 ?  126 LEU   A CD2  1 
ATOM   2711 H  H    A LEU   A 1 126 ? 16.189 -4.733  2.413   0.58 11.77 ?  126 LEU   A H    1 
ATOM   2712 H  H    B LEU   A 1 126 ? 16.141 -4.382  2.394   0.42 11.73 ?  126 LEU   A H    1 
ATOM   2713 H  HA   A LEU   A 1 126 ? 17.255 -6.905  1.328   0.58 12.44 ?  126 LEU   A HA   1 
ATOM   2714 H  HA   B LEU   A 1 126 ? 17.117 -6.612  1.301   0.42 11.75 ?  126 LEU   A HA   1 
ATOM   2715 H  HB2  A LEU   A 1 126 ? 15.045 -5.323  0.610   0.58 12.56 ?  126 LEU   A HB2  1 
ATOM   2716 H  HB2  B LEU   A 1 126 ? 14.992 -4.941  0.526   0.42 12.82 ?  126 LEU   A HB2  1 
ATOM   2717 H  HB3  A LEU   A 1 126 ? 15.530 -6.499  -0.338  0.58 12.56 ?  126 LEU   A HB3  1 
ATOM   2718 H  HB3  B LEU   A 1 126 ? 15.448 -6.156  -0.383  0.42 12.82 ?  126 LEU   A HB3  1 
ATOM   2719 H  HG   A LEU   A 1 126 ? 14.679 -6.961  2.308   0.58 13.71 ?  126 LEU   A HG   1 
ATOM   2720 H  HG   B LEU   A 1 126 ? 14.339 -6.417  2.196   0.42 13.24 ?  126 LEU   A HG   1 
ATOM   2721 H  HD11 A LEU   A 1 126 ? 12.649 -7.682  1.438   0.58 15.52 ?  126 LEU   A HD11 1 
ATOM   2722 H  HD11 B LEU   A 1 126 ? 12.483 -7.319  1.127   0.42 14.15 ?  126 LEU   A HD11 1 
ATOM   2723 H  HD12 A LEU   A 1 126 ? 12.880 -6.143  1.115   0.58 15.52 ?  126 LEU   A HD12 1 
ATOM   2724 H  HD12 B LEU   A 1 126 ? 12.738 -5.828  0.641   0.42 14.15 ?  126 LEU   A HD12 1 
ATOM   2725 H  HD13 A LEU   A 1 126 ? 13.118 -7.237  -0.013  0.58 15.52 ?  126 LEU   A HD13 1 
ATOM   2726 H  HD13 B LEU   A 1 126 ? 13.168 -7.049  -0.281  0.42 14.15 ?  126 LEU   A HD13 1 
ATOM   2727 H  HD21 A LEU   A 1 126 ? 14.476 -9.219  1.522   0.58 13.80 ?  126 LEU   A HD21 1 
ATOM   2728 H  HD21 B LEU   A 1 126 ? 14.262 -8.766  1.693   0.42 13.61 ?  126 LEU   A HD21 1 
ATOM   2729 H  HD22 A LEU   A 1 126 ? 15.263 -8.761  0.220   0.58 13.80 ?  126 LEU   A HD22 1 
ATOM   2730 H  HD22 B LEU   A 1 126 ? 15.278 -8.466  0.510   0.42 13.61 ?  126 LEU   A HD22 1 
ATOM   2731 H  HD23 A LEU   A 1 126 ? 15.974 -8.705  1.640   0.58 13.80 ?  126 LEU   A HD23 1 
ATOM   2732 H  HD23 B LEU   A 1 126 ? 15.713 -8.207  2.015   0.42 13.61 ?  126 LEU   A HD23 1 
ATOM   2733 N  N    A LEU   A 1 127 ? 18.854 -6.152  -0.311  0.58 10.89 ?  127 LEU   A N    1 
ATOM   2734 N  N    B LEU   A 1 127 ? 18.841 -5.818  -0.229  0.42 9.09  ?  127 LEU   A N    1 
ATOM   2735 C  CA   A LEU   A 1 127 ? 19.847 -5.635  -1.237  0.58 10.64 ?  127 LEU   A CA   1 
ATOM   2736 C  CA   B LEU   A 1 127 ? 19.831 -5.297  -1.157  0.42 9.56  ?  127 LEU   A CA   1 
ATOM   2737 C  C    A LEU   A 1 127 ? 19.242 -5.456  -2.619  0.58 9.77  ?  127 LEU   A C    1 
ATOM   2738 C  C    B LEU   A 1 127 ? 19.276 -5.252  -2.578  0.42 9.97  ?  127 LEU   A C    1 
ATOM   2739 O  O    A LEU   A 1 127 ? 18.424 -6.259  -3.076  0.58 10.45 ?  127 LEU   A O    1 
ATOM   2740 O  O    B LEU   A 1 127 ? 18.446 -6.070  -2.980  0.42 10.43 ?  127 LEU   A O    1 
ATOM   2741 C  CB   A LEU   A 1 127 ? 21.039 -6.586  -1.320  0.58 10.91 ?  127 LEU   A CB   1 
ATOM   2742 C  CB   B LEU   A 1 127 ? 21.097 -6.154  -1.129  0.42 10.33 ?  127 LEU   A CB   1 
ATOM   2743 C  CG   A LEU   A 1 127 ? 21.817 -6.809  -0.024  0.58 11.28 ?  127 LEU   A CG   1 
ATOM   2744 C  CG   B LEU   A 1 127 ? 21.887 -6.147  0.182   0.42 11.04 ?  127 LEU   A CG   1 
ATOM   2745 C  CD1  A LEU   A 1 127 ? 22.917 -7.814  -0.282  0.58 11.52 ?  127 LEU   A CD1  1 
ATOM   2746 C  CD1  B LEU   A 1 127 ? 23.037 -7.137  0.116   0.42 11.84 ?  127 LEU   A CD1  1 
ATOM   2747 C  CD2  A LEU   A 1 127 ? 22.399 -5.512  0.512   0.58 11.92 ?  127 LEU   A CD2  1 
ATOM   2748 C  CD2  B LEU   A 1 127 ? 22.401 -4.742  0.492   0.42 11.29 ?  127 LEU   A CD2  1 
ATOM   2749 H  H    A LEU   A 1 127 ? 18.998 -6.954  -0.047  0.58 13.06 ?  127 LEU   A H    1 
ATOM   2750 H  H    B LEU   A 1 127 ? 19.029 -6.598  0.102   0.42 10.91 ?  127 LEU   A H    1 
ATOM   2751 H  HA   A LEU   A 1 127 ? 20.158 -4.777  -0.928  0.58 12.77 ?  127 LEU   A HA   1 
ATOM   2752 H  HA   B LEU   A 1 127 ? 20.069 -4.394  -0.884  0.42 11.47 ?  127 LEU   A HA   1 
ATOM   2753 H  HB2  A LEU   A 1 127 ? 20.721 -7.453  -1.616  0.58 13.09 ?  127 LEU   A HB2  1 
ATOM   2754 H  HB2  B LEU   A 1 127 ? 20.846 -7.072  -1.313  0.42 12.40 ?  127 LEU   A HB2  1 
ATOM   2755 H  HB3  A LEU   A 1 127 ? 21.664 -6.233  -1.974  0.58 13.09 ?  127 LEU   A HB3  1 
ATOM   2756 H  HB3  B LEU   A 1 127 ? 21.690 -5.835  -1.827  0.42 12.40 ?  127 LEU   A HB3  1 
ATOM   2757 H  HG   A LEU   A 1 127 ? 21.221 -7.176  0.649   0.58 13.54 ?  127 LEU   A HG   1 
ATOM   2758 H  HG   B LEU   A 1 127 ? 21.301 -6.418  0.905   0.42 13.25 ?  127 LEU   A HG   1 
ATOM   2759 H  HD11 A LEU   A 1 127 ? 23.397 -7.979  0.547   0.58 13.83 ?  127 LEU   A HD11 1 
ATOM   2760 H  HD11 B LEU   A 1 127 ? 23.540 -7.092  0.945   0.42 14.21 ?  127 LEU   A HD11 1 
ATOM   2761 H  HD12 A LEU   A 1 127 ? 22.524 -8.640  -0.604  0.58 13.83 ?  127 LEU   A HD12 1 
ATOM   2762 H  HD12 B LEU   A 1 127 ? 22.678 -8.031  -0.004  0.42 14.21 ?  127 LEU   A HD12 1 
ATOM   2763 H  HD13 A LEU   A 1 127 ? 23.524 -7.454  -0.947  0.58 13.83 ?  127 LEU   A HD13 1 
ATOM   2764 H  HD13 B LEU   A 1 127 ? 23.610 -6.907  -0.631  0.42 14.21 ?  127 LEU   A HD13 1 
ATOM   2765 H  HD21 A LEU   A 1 127 ? 22.965 -5.713  1.273   0.58 14.30 ?  127 LEU   A HD21 1 
ATOM   2766 H  HD21 B LEU   A 1 127 ? 23.016 -4.788  1.240   0.42 13.55 ?  127 LEU   A HD21 1 
ATOM   2767 H  HD22 A LEU   A 1 127 ? 22.924 -5.093  -0.190  0.58 14.30 ?  127 LEU   A HD22 1 
ATOM   2768 H  HD22 B LEU   A 1 127 ? 22.857 -4.392  -0.290  0.42 13.55 ?  127 LEU   A HD22 1 
ATOM   2769 H  HD23 A LEU   A 1 127 ? 21.675 -4.928  0.779   0.58 14.30 ?  127 LEU   A HD23 1 
ATOM   2770 H  HD23 B LEU   A 1 127 ? 21.649 -4.172  0.718   0.42 13.55 ?  127 LEU   A HD23 1 
ATOM   2771 N  N    A SER   A 1 128 ? 19.681 -4.400  -3.290  0.58 9.93  ?  128 SER   A N    1 
ATOM   2772 N  N    B SER   A 1 128 ? 19.764 -4.272  -3.335  0.42 10.54 ?  128 SER   A N    1 
ATOM   2773 C  CA   A SER   A 1 128 ? 19.269 -4.032  -4.634  0.58 10.46 ?  128 SER   A CA   1 
ATOM   2774 C  CA   B SER   A 1 128 ? 19.421 -4.035  -4.736  0.42 10.40 ?  128 SER   A CA   1 
ATOM   2775 C  C    A SER   A 1 128 ? 17.808 -3.599  -4.724  0.58 11.24 ?  128 SER   A C    1 
ATOM   2776 C  C    B SER   A 1 128 ? 17.986 -3.570  -4.983  0.42 10.47 ?  128 SER   A C    1 
ATOM   2777 O  O    A SER   A 1 128 ? 17.325 -3.330  -5.830  0.58 12.11 ?  128 SER   A O    1 
ATOM   2778 O  O    B SER   A 1 128 ? 17.674 -3.127  -6.092  0.42 10.71 ?  128 SER   A O    1 
ATOM   2779 C  CB   A SER   A 1 128 ? 19.616 -5.111  -5.665  0.58 11.07 ?  128 SER   A CB   1 
ATOM   2780 C  CB   B SER   A 1 128 ? 19.773 -5.233  -5.619  0.42 11.01 ?  128 SER   A CB   1 
ATOM   2781 O  OG   A SER   A 1 128 ? 21.025 -5.274  -5.762  0.58 11.47 ?  128 SER   A OG   1 
ATOM   2782 O  OG   B SER   A 1 128 ? 21.180 -5.390  -5.719  0.42 11.10 ?  128 SER   A OG   1 
ATOM   2783 H  H    A SER   A 1 128 ? 20.270 -3.855  -2.964  0.58 11.91 ?  128 SER   A H    1 
ATOM   2784 H  H    B SER   A 1 128 ? 20.347 -3.712  -3.041  0.42 12.65 ?  128 SER   A H    1 
ATOM   2785 H  HA   A SER   A 1 128 ? 19.782 -3.256  -4.878  0.58 12.55 ?  128 SER   A HA   1 
ATOM   2786 H  HA   B SER   A 1 128 ? 19.980 -3.308  -5.034  0.42 12.48 ?  128 SER   A HA   1 
ATOM   2787 H  HB2  A SER   A 1 128 ? 19.217 -5.952  -5.386  0.58 13.28 ?  128 SER   A HB2  1 
ATOM   2788 H  HB2  B SER   A 1 128 ? 19.391 -6.033  -5.236  0.42 13.22 ?  128 SER   A HB2  1 
ATOM   2789 H  HB3  A SER   A 1 128 ? 19.275 -4.843  -6.524  0.58 13.28 ?  128 SER   A HB3  1 
ATOM   2790 H  HB3  B SER   A 1 128 ? 19.408 -5.078  -6.506  0.42 13.22 ?  128 SER   A HB3  1 
ATOM   2791 H  HG   A SER   A 1 128 ? 21.380 -4.537  -5.965  0.58 13.76 ?  128 SER   A HG   1 
ATOM   2792 H  HG   B SER   A 1 128 ? 21.519 -4.693  -6.051  0.42 13.32 ?  128 SER   A HG   1 
ATOM   2793 N  N    A ALA   A 1 129 ? 17.101 -3.496  -3.595  0.58 11.60 ?  129 ALA   A N    1 
ATOM   2794 N  N    B ALA   A 1 129 ? 17.108 -3.660  -3.984  0.42 11.03 ?  129 ALA   A N    1 
ATOM   2795 C  CA   A ALA   A 1 129 ? 15.728 -3.012  -3.573  0.58 11.46 ?  129 ALA   A CA   1 
ATOM   2796 C  CA   B ALA   A 1 129 ? 15.758 -3.124  -4.107  0.42 11.44 ?  129 ALA   A CA   1 
ATOM   2797 C  C    A ALA   A 1 129 ? 15.716 -1.483  -3.526  0.58 10.94 ?  129 ALA   A C    1 
ATOM   2798 C  C    B ALA   A 1 129 ? 15.805 -1.610  -3.898  0.42 11.73 ?  129 ALA   A C    1 
ATOM   2799 O  O    A ALA   A 1 129 ? 16.757 -0.822  -3.589  0.58 11.15 ?  129 ALA   A O    1 
ATOM   2800 O  O    B ALA   A 1 129 ? 16.877 -1.004  -3.815  0.42 12.10 ?  129 ALA   A O    1 
ATOM   2801 C  CB   A ALA   A 1 129 ? 14.961 -3.624  -2.397  0.58 12.43 ?  129 ALA   A CB   1 
ATOM   2802 C  CB   B ALA   A 1 129 ? 14.807 -3.840  -3.148  0.42 11.94 ?  129 ALA   A CB   1 
ATOM   2803 H  H    A ALA   A 1 129 ? 17.410 -3.703  -2.815  0.58 13.92 ?  129 ALA   A H    1 
ATOM   2804 H  H    B ALA   A 1 129 ? 17.266 -4.033  -3.224  0.42 13.24 ?  129 ALA   A H    1 
ATOM   2805 H  HA   A ALA   A 1 129 ? 15.286 -3.288  -4.384  0.58 13.75 ?  129 ALA   A HA   1 
ATOM   2806 H  HA   B ALA   A 1 129 ? 15.441 -3.280  -5.009  0.42 13.72 ?  129 ALA   A HA   1 
ATOM   2807 H  HB1  A ALA   A 1 129 ? 14.044 -3.295  -2.407  0.58 14.92 ?  129 ALA   A HB1  1 
ATOM   2808 H  HB1  B ALA   A 1 129 ? 13.915 -3.470  -3.256  0.42 14.33 ?  129 ALA   A HB1  1 
ATOM   2809 H  HB2  A ALA   A 1 129 ? 14.962 -4.590  -2.482  0.58 14.92 ?  129 ALA   A HB2  1 
ATOM   2810 H  HB2  B ALA   A 1 129 ? 14.800 -4.785  -3.357  0.42 14.33 ?  129 ALA   A HB2  1 
ATOM   2811 H  HB3  A ALA   A 1 129 ? 15.389 -3.367  -1.562  0.58 14.92 ?  129 ALA   A HB3  1 
ATOM   2812 H  HB3  B ALA   A 1 129 ? 15.113 -3.701  -2.238  0.42 14.33 ?  129 ALA   A HB3  1 
ATOM   2813 N  N    A GLY   A 1 130 ? 14.521 -0.914  -3.416  0.58 11.48 ?  130 GLY   A N    1 
ATOM   2814 N  N    B GLY   A 1 130 ? 14.635 -0.985  -3.816  0.42 11.80 ?  130 GLY   A N    1 
ATOM   2815 C  CA   A GLY   A 1 130 ? 14.418 0.534   -3.374  0.58 12.16 ?  130 GLY   A CA   1 
ATOM   2816 C  CA   B GLY   A 1 130 ? 14.603 0.459   -3.670  0.42 12.27 ?  130 GLY   A CA   1 
ATOM   2817 C  C    A GLY   A 1 130 ? 15.015 1.155   -4.620  0.58 11.78 ?  130 GLY   A C    1 
ATOM   2818 C  C    B GLY   A 1 130 ? 15.278 1.145   -4.840  0.42 12.38 ?  130 GLY   A C    1 
ATOM   2819 O  O    A GLY   A 1 130 ? 14.769 0.702   -5.745  0.58 11.86 ?  130 GLY   A O    1 
ATOM   2820 O  O    B GLY   A 1 130 ? 15.125 0.744   -6.000  0.42 12.83 ?  130 GLY   A O    1 
ATOM   2821 H  H    A GLY   A 1 130 ? 13.766 -1.332  -3.366  0.58 13.78 ?  130 GLY   A H    1 
ATOM   2822 H  H    B GLY   A 1 130 ? 13.861 -1.370  -3.840  0.42 14.16 ?  130 GLY   A H    1 
ATOM   2823 H  HA2  A GLY   A 1 130 ? 13.482 0.797   -3.307  0.58 14.59 ?  130 GLY   A HA2  1 
ATOM   2824 H  HA2  B GLY   A 1 130 ? 13.680 0.764   -3.621  0.42 14.73 ?  130 GLY   A HA2  1 
ATOM   2825 H  HA3  A GLY   A 1 130 ? 14.890 0.875   -2.602  0.58 14.59 ?  130 GLY   A HA3  1 
ATOM   2826 H  HA3  B GLY   A 1 130 ? 15.060 0.717   -2.857  0.42 14.73 ?  130 GLY   A HA3  1 
ATOM   2827 N  N    A ILE   A 1 131 ? 15.824 2.203   -4.419  0.58 12.37 ?  131 ILE   A N    1 
ATOM   2828 N  N    B ILE   A 1 131 ? 16.055 2.187   -4.533  0.42 12.47 ?  131 ILE   A N    1 
ATOM   2829 C  CA   A ILE   A 1 131 ? 16.368 2.976   -5.533  0.58 12.19 ?  131 ILE   A CA   1 
ATOM   2830 C  CA   B ILE   A 1 131 ? 16.673 3.010   -5.564  0.42 12.31 ?  131 ILE   A CA   1 
ATOM   2831 C  C    A ILE   A 1 131 ? 17.396 2.213   -6.356  0.58 12.41 ?  131 ILE   A C    1 
ATOM   2832 C  C    B ILE   A 1 131 ? 17.668 2.247   -6.429  0.42 12.07 ?  131 ILE   A C    1 
ATOM   2833 O  O    A ILE   A 1 131 ? 17.795 2.707   -7.416  0.58 12.90 ?  131 ILE   A O    1 
ATOM   2834 O  O    B ILE   A 1 131 ? 18.086 2.767   -7.469  0.42 12.69 ?  131 ILE   A O    1 
ATOM   2835 C  CB   A ILE   A 1 131 ? 16.910 4.349   -5.077  0.58 12.93 ?  131 ILE   A CB   1 
ATOM   2836 C  CB   B ILE   A 1 131 ? 17.314 4.288   -4.970  0.42 13.04 ?  131 ILE   A CB   1 
ATOM   2837 C  CG1  A ILE   A 1 131 ? 18.157 4.198   -4.193  0.58 14.00 ?  131 ILE   A CG1  1 
ATOM   2838 C  CG1  B ILE   A 1 131 ? 18.519 3.952   -4.083  0.42 13.55 ?  131 ILE   A CG1  1 
ATOM   2839 C  CG2  A ILE   A 1 131 ? 15.816 5.136   -4.366  0.58 13.13 ?  131 ILE   A CG2  1 
ATOM   2840 C  CG2  B ILE   A 1 131 ? 16.280 5.094   -4.194  0.42 13.43 ?  131 ILE   A CG2  1 
ATOM   2841 C  CD1  A ILE   A 1 131 ? 18.798 5.533   -3.802  0.58 14.89 ?  131 ILE   A CD1  1 
ATOM   2842 C  CD1  B ILE   A 1 131 ? 19.172 5.184   -3.440  0.42 13.87 ?  131 ILE   A CD1  1 
ATOM   2843 H  H    A ILE   A 1 131 ? 16.065 2.488   -3.645  0.58 14.84 ?  131 ILE   A H    1 
ATOM   2844 H  H    B ILE   A 1 131 ? 16.223 2.442   -3.729  0.42 14.96 ?  131 ILE   A H    1 
ATOM   2845 H  HA   A ILE   A 1 131 ? 15.639 3.163   -6.140  0.58 14.63 ?  131 ILE   A HA   1 
ATOM   2846 H  HA   B ILE   A 1 131 ? 15.971 3.303   -6.157  0.42 14.77 ?  131 ILE   A HA   1 
ATOM   2847 H  HB   A ILE   A 1 131 ? 17.167 4.845   -5.868  0.58 15.51 ?  131 ILE   A HB   1 
ATOM   2848 H  HB   B ILE   A 1 131 ? 17.624 4.831   -5.708  0.42 15.65 ?  131 ILE   A HB   1 
ATOM   2849 H  HG12 A ILE   A 1 131 ? 17.910 3.735   -3.377  0.58 16.80 ?  131 ILE   A HG12 1 
ATOM   2850 H  HG12 B ILE   A 1 131 ? 18.231 3.363   -3.371  0.42 16.26 ?  131 ILE   A HG12 1 
ATOM   2851 H  HG13 A ILE   A 1 131 ? 18.826 3.681   -4.672  0.58 16.80 ?  131 ILE   A HG13 1 
ATOM   2852 H  HG13 B ILE   A 1 131 ? 19.194 3.514   -4.623  0.42 16.26 ?  131 ILE   A HG13 1 
ATOM   2853 H  HG21 A ILE   A 1 131 ? 16.119 6.044   -4.225  0.58 15.75 ?  131 ILE   A HG21 1 
ATOM   2854 H  HG21 B ILE   A 1 131 ? 16.634 5.979   -4.021  0.42 16.12 ?  131 ILE   A HG21 1 
ATOM   2855 H  HG22 A ILE   A 1 131 ? 15.019 5.132   -4.919  0.58 15.75 ?  131 ILE   A HG22 1 
ATOM   2856 H  HG22 B ILE   A 1 131 ? 15.470 5.159   -4.724  0.42 16.12 ?  131 ILE   A HG22 1 
ATOM   2857 H  HG23 A ILE   A 1 131 ? 15.626 4.711   -3.514  0.58 15.75 ?  131 ILE   A HG23 1 
ATOM   2858 H  HG23 B ILE   A 1 131 ? 16.090 4.641   -3.357  0.42 16.12 ?  131 ILE   A HG23 1 
ATOM   2859 H  HD11 A ILE   A 1 131 ? 19.633 5.360   -3.338  0.58 17.87 ?  131 ILE   A HD11 1 
ATOM   2860 H  HD11 B ILE   A 1 131 ? 19.995 4.915   -3.002  0.42 16.64 ?  131 ILE   A HD11 1 
ATOM   2861 H  HD12 A ILE   A 1 131 ? 18.969 6.050   -4.606  0.58 17.87 ?  131 ILE   A HD12 1 
ATOM   2862 H  HD12 B ILE   A 1 131 ? 19.364 5.840   -4.129  0.42 16.64 ?  131 ILE   A HD12 1 
ATOM   2863 H  HD13 A ILE   A 1 131 ? 18.192 6.018   -3.221  0.58 17.87 ?  131 ILE   A HD13 1 
ATOM   2864 H  HD13 B ILE   A 1 131 ? 18.562 5.565   -2.786  0.42 16.64 ?  131 ILE   A HD13 1 
ATOM   2865 N  N    A PHE   A 1 132 ? 17.832 1.027   -5.909  0.58 12.28 ?  132 PHE   A N    1 
ATOM   2866 N  N    B PHE   A 1 132 ? 18.061 1.031   -6.031  0.42 11.93 ?  132 PHE   A N    1 
ATOM   2867 C  CA   A PHE   A 1 132 ? 18.698 0.185   -6.731  0.58 12.06 ?  132 PHE   A CA   1 
ATOM   2868 C  CA   B PHE   A 1 132 ? 18.963 0.228   -6.851  0.42 12.26 ?  132 PHE   A CA   1 
ATOM   2869 C  C    A PHE   A 1 132 ? 17.930 -0.575  -7.813  0.58 12.69 ?  132 PHE   A C    1 
ATOM   2870 C  C    B PHE   A 1 132 ? 18.257 -0.502  -7.994  0.42 13.20 ?  132 PHE   A C    1 
ATOM   2871 O  O    A PHE   A 1 132 ? 18.554 -1.215  -8.665  0.58 12.99 ?  132 PHE   A O    1 
ATOM   2872 O  O    B PHE   A 1 132 ? 18.939 -1.052  -8.867  0.42 14.12 ?  132 PHE   A O    1 
ATOM   2873 C  CB   A PHE   A 1 132 ? 19.489 -0.802  -5.859  0.58 11.98 ?  132 PHE   A CB   1 
ATOM   2874 C  CB   B PHE   A 1 132 ? 19.762 -0.758  -5.986  0.42 11.50 ?  132 PHE   A CB   1 
ATOM   2875 C  CG   A PHE   A 1 132 ? 20.734 -0.218  -5.215  0.58 12.18 ?  132 PHE   A CG   1 
ATOM   2876 C  CG   B PHE   A 1 132 ? 20.922 -0.131  -5.239  0.42 11.10 ?  132 PHE   A CG   1 
ATOM   2877 C  CD1  A PHE   A 1 132 ? 20.649 0.831   -4.310  0.58 13.11 ?  132 PHE   A CD1  1 
ATOM   2878 C  CD1  B PHE   A 1 132 ? 20.705 0.758   -4.196  0.42 11.91 ?  132 PHE   A CD1  1 
ATOM   2879 C  CD2  A PHE   A 1 132 ? 21.985 -0.766  -5.478  0.58 12.57 ?  132 PHE   A CD2  1 
ATOM   2880 C  CD2  B PHE   A 1 132 ? 22.228 -0.459  -5.566  0.42 11.57 ?  132 PHE   A CD2  1 
ATOM   2881 C  CE1  A PHE   A 1 132 ? 21.791 1.347   -3.708  0.58 13.35 ?  132 PHE   A CE1  1 
ATOM   2882 C  CE1  B PHE   A 1 132 ? 21.770 1.320   -3.507  0.42 12.33 ?  132 PHE   A CE1  1 
ATOM   2883 C  CE2  A PHE   A 1 132 ? 23.128 -0.261  -4.874  0.58 12.84 ?  132 PHE   A CE2  1 
ATOM   2884 C  CE2  B PHE   A 1 132 ? 23.297 0.095   -4.880  0.42 11.92 ?  132 PHE   A CE2  1 
ATOM   2885 C  CZ   A PHE   A 1 132 ? 23.027 0.798   -3.987  0.58 13.16 ?  132 PHE   A CZ   1 
ATOM   2886 C  CZ   B PHE   A 1 132 ? 23.065 0.986   -3.847  0.42 12.33 ?  132 PHE   A CZ   1 
ATOM   2887 H  H    A PHE   A 1 132 ? 17.643 0.689   -5.138  0.58 14.73 ?  132 PHE   A H    1 
ATOM   2888 H  H    B PHE   A 1 132 ? 17.830 0.656   -5.288  0.42 14.32 ?  132 PHE   A H    1 
ATOM   2889 H  HA   A PHE   A 1 132 ? 19.344 0.752   -7.174  0.58 14.47 ?  132 PHE   A HA   1 
ATOM   2890 H  HA   B PHE   A 1 132 ? 19.607 0.828   -7.253  0.42 14.71 ?  132 PHE   A HA   1 
ATOM   2891 H  HB2  A PHE   A 1 132 ? 18.917 -1.120  -5.145  0.58 14.37 ?  132 PHE   A HB2  1 
ATOM   2892 H  HB2  B PHE   A 1 132 ? 19.172 -1.150  -5.327  0.42 13.80 ?  132 PHE   A HB2  1 
ATOM   2893 H  HB3  A PHE   A 1 132 ? 19.772 -1.551  -6.409  0.58 14.37 ?  132 PHE   A HB3  1 
ATOM   2894 H  HB3  B PHE   A 1 132 ? 20.125 -1.455  -6.559  0.42 13.80 ?  132 PHE   A HB3  1 
ATOM   2895 H  HD1  A PHE   A 1 132 ? 19.821 1.201   -4.113  0.58 15.73 ?  132 PHE   A HD1  1 
ATOM   2896 H  HD1  B PHE   A 1 132 ? 19.836 0.984   -3.960  0.42 14.29 ?  132 PHE   A HD1  1 
ATOM   2897 H  HD2  A PHE   A 1 132 ? 22.063 -1.478  -6.072  0.58 15.09 ?  132 PHE   A HD2  1 
ATOM   2898 H  HD2  B PHE   A 1 132 ? 22.396 -1.058  -6.259  0.42 13.88 ?  132 PHE   A HD2  1 
ATOM   2899 H  HE1  A PHE   A 1 132 ? 21.721 2.054   -3.107  0.58 16.01 ?  132 PHE   A HE1  1 
ATOM   2900 H  HE1  B PHE   A 1 132 ? 21.611 1.917   -2.811  0.42 14.79 ?  132 PHE   A HE1  1 
ATOM   2901 H  HE2  A PHE   A 1 132 ? 23.961 -0.627  -5.067  0.58 15.41 ?  132 PHE   A HE2  1 
ATOM   2902 H  HE2  B PHE   A 1 132 ? 24.171 -0.127  -5.113  0.42 14.31 ?  132 PHE   A HE2  1 
ATOM   2903 H  HZ   A PHE   A 1 132 ? 23.791 1.144   -3.582  0.58 15.79 ?  132 PHE   A HZ   1 
ATOM   2904 H  HZ   B PHE   A 1 132 ? 23.780 1.364   -3.386  0.42 14.80 ?  132 PHE   A HZ   1 
ATOM   2905 N  N    A GLY   A 1 133 ? 16.599 -0.545  -7.792  0.58 12.42 ?  133 GLY   A N    1 
ATOM   2906 N  N    B GLY   A 1 133 ? 16.918 -0.531  -8.015  0.42 13.16 ?  133 GLY   A N    1 
ATOM   2907 C  CA   A GLY   A 1 133 ? 15.807 -0.924  -8.947  0.58 13.11 ?  133 GLY   A CA   1 
ATOM   2908 C  CA   B GLY   A 1 133 ? 16.172 -0.880  -9.206  0.42 13.44 ?  133 GLY   A CA   1 
ATOM   2909 C  C    A GLY   A 1 133 ? 15.537 -2.399  -9.167  0.58 13.67 ?  133 GLY   A C    1 
ATOM   2910 C  C    B GLY   A 1 133 ? 15.570 -2.274  -9.245  0.42 13.79 ?  133 GLY   A C    1 
ATOM   2911 O  O    A GLY   A 1 133 ? 14.965 -2.741  -10.208 0.58 14.98 ?  133 GLY   A O    1 
ATOM   2912 O  O    B GLY   A 1 133 ? 14.686 -2.517  -10.077 0.42 14.24 ?  133 GLY   A O    1 
ATOM   2913 H  H    A GLY   A 1 133 ? 16.133 -0.307  -7.113  0.58 14.91 ?  133 GLY   A H    1 
ATOM   2914 H  H    B GLY   A 1 133 ? 16.422 -0.340  -7.335  0.42 15.79 ?  133 GLY   A H    1 
ATOM   2915 H  HA2  A GLY   A 1 133 ? 14.946 -0.480  -8.881  0.58 15.73 ?  133 GLY   A HA2  1 
ATOM   2916 H  HA2  B GLY   A 1 133 ? 15.436 -0.260  -9.303  0.42 16.12 ?  133 GLY   A HA2  1 
ATOM   2917 H  HA3  A GLY   A 1 133 ? 16.246 -0.597  -9.745  0.58 15.73 ?  133 GLY   A HA3  1 
ATOM   2918 H  HA3  B GLY   A 1 133 ? 16.754 -0.770  -9.977  0.42 16.12 ?  133 GLY   A HA3  1 
ATOM   2919 N  N    A ALA   A 1 134 ? 15.923 -3.287  -8.252  0.58 13.33 ?  134 ALA   A N    1 
ATOM   2920 N  N    B ALA   A 1 134 ? 16.003 -3.191  -8.383  0.42 13.81 ?  134 ALA   A N    1 
ATOM   2921 C  CA   A ALA   A 1 134 ? 15.611 -4.698  -8.429  0.58 13.94 ?  134 ALA   A CA   1 
ATOM   2922 C  CA   B ALA   A 1 134 ? 15.581 -4.579  -8.501  0.42 13.99 ?  134 ALA   A CA   1 
ATOM   2923 C  C    A ALA   A 1 134 ? 14.248 -5.034  -7.822  0.58 13.88 ?  134 ALA   A C    1 
ATOM   2924 C  C    B ALA   A 1 134 ? 14.275 -4.835  -7.744  0.42 13.75 ?  134 ALA   A C    1 
ATOM   2925 O  O    A ALA   A 1 134 ? 13.656 -4.253  -7.075  0.58 15.04 ?  134 ALA   A O    1 
ATOM   2926 O  O    B ALA   A 1 134 ? 13.824 -4.029  -6.926  0.42 13.96 ?  134 ALA   A O    1 
ATOM   2927 C  CB   A ALA   A 1 134 ? 16.697 -5.588  -7.823  0.58 14.75 ?  134 ALA   A CB   1 
ATOM   2928 C  CB   B ALA   A 1 134 ? 16.681 -5.522  -8.012  0.42 14.74 ?  134 ALA   A CB   1 
ATOM   2929 H  H    A ALA   A 1 134 ? 16.371 -3.099  -7.537  0.58 16.00 ?  134 ALA   A H    1 
ATOM   2930 H  H    B ALA   A 1 134 ? 16.530 -3.028  -7.722  0.42 16.57 ?  134 ALA   A H    1 
ATOM   2931 H  HA   A ALA   A 1 134 ? 15.571 -4.889  -9.379  0.58 16.73 ?  134 ALA   A HA   1 
ATOM   2932 H  HA   B ALA   A 1 134 ? 15.426 -4.772  -9.439  0.42 16.79 ?  134 ALA   A HA   1 
ATOM   2933 H  HB1  A ALA   A 1 134 ? 16.475 -6.515  -7.996  0.58 17.70 ?  134 ALA   A HB1  1 
ATOM   2934 H  HB1  B ALA   A 1 134 ? 16.373 -6.435  -8.107  0.42 17.68 ?  134 ALA   A HB1  1 
ATOM   2935 H  HB2  A ALA   A 1 134 ? 17.550 -5.370  -8.236  0.58 17.70 ?  134 ALA   A HB2  1 
ATOM   2936 H  HB2  B ALA   A 1 134 ? 17.476 -5.382  -8.551  0.42 17.68 ?  134 ALA   A HB2  1 
ATOM   2937 H  HB3  A ALA   A 1 134 ? 16.741 -5.428  -6.869  0.58 17.70 ?  134 ALA   A HB3  1 
ATOM   2938 H  HB3  B ALA   A 1 134 ? 16.871 -5.327  -7.083  0.42 17.68 ?  134 ALA   A HB3  1 
ATOM   2939 N  N    A ASP   A 1 135 ? 13.750 -6.218  -8.167  0.58 14.06 ?  135 ASP   A N    1 
ATOM   2940 N  N    B ASP   A 1 135 ? 13.671 -5.989  -8.035  0.42 14.28 ?  135 ASP   A N    1 
ATOM   2941 C  CA   A ASP   A 1 135 ? 12.488 -6.709  -7.620  0.58 14.41 ?  135 ASP   A CA   1 
ATOM   2942 C  CA   B ASP   A 1 135 ? 12.400 -6.379  -7.430  0.42 14.87 ?  135 ASP   A CA   1 
ATOM   2943 C  C    A ASP   A 1 135 ? 12.701 -7.140  -6.175  0.58 13.97 ?  135 ASP   A C    1 
ATOM   2944 C  C    B ASP   A 1 135 ? 12.640 -6.849  -6.000  0.42 13.97 ?  135 ASP   A C    1 
ATOM   2945 O  O    A ASP   A 1 135 ? 13.494 -8.057  -5.925  0.58 14.01 ?  135 ASP   A O    1 
ATOM   2946 O  O    B ASP   A 1 135 ? 13.397 -7.804  -5.793  0.42 13.21 ?  135 ASP   A O    1 
ATOM   2947 C  CB   A ASP   A 1 135 ? 12.018 -7.898  -8.451  0.58 16.29 ?  135 ASP   A CB   1 
ATOM   2948 C  CB   B ASP   A 1 135 ? 11.778 -7.514  -8.235  0.42 16.23 ?  135 ASP   A CB   1 
ATOM   2949 C  CG   A ASP   A 1 135 ? 10.733 -8.528  -7.932  0.58 18.34 ?  135 ASP   A CG   1 
ATOM   2950 C  CG   B ASP   A 1 135 ? 10.349 -7.839  -7.806  0.42 18.02 ?  135 ASP   A CG   1 
ATOM   2951 O  OD1  A ASP   A 1 135 ? 10.166 -8.059  -6.926  0.58 18.63 ?  135 ASP   A OD1  1 
ATOM   2952 O  OD1  B ASP   A 1 135 ? 9.954  -7.474  -6.676  0.42 18.74 ?  135 ASP   A OD1  1 
ATOM   2953 O  OD2  A ASP   A 1 135 ? 10.287 -9.516  -8.548  0.58 20.34 -1 135 ASP   A OD2  1 
ATOM   2954 O  OD2  B ASP   A 1 135 ? 9.622  -8.474  -8.600  0.42 19.32 -1 135 ASP   A OD2  1 
ATOM   2955 H  H    A ASP   A 1 135 ? 14.124 -6.755  -8.725  0.58 16.87 ?  135 ASP   A H    1 
ATOM   2956 H  H    B ASP   A 1 135 ? 13.981 -6.569  -8.586  0.42 17.13 ?  135 ASP   A H    1 
ATOM   2957 H  HA   A ASP   A 1 135 ? 11.822 -6.006  -7.665  0.58 17.29 ?  135 ASP   A HA   1 
ATOM   2958 H  HA   B ASP   A 1 135 ? 11.791 -5.623  -7.440  0.42 17.84 ?  135 ASP   A HA   1 
ATOM   2959 H  HB2  A ASP   A 1 135 ? 11.854 -7.603  -9.356  0.58 19.54 ?  135 ASP   A HB2  1 
ATOM   2960 H  HB2  B ASP   A 1 135 ? 11.784 -7.269  -9.175  0.42 19.47 ?  135 ASP   A HB2  1 
ATOM   2961 H  HB3  A ASP   A 1 135 ? 12.703 -8.581  -8.437  0.58 19.54 ?  135 ASP   A HB3  1 
ATOM   2962 H  HB3  B ASP   A 1 135 ? 12.301 -8.317  -8.099  0.42 19.47 ?  135 ASP   A HB3  1 
ATOM   2963 N  N    A PRO   A 1 136 ? 12.028 -6.526  -5.202  0.58 13.56 ?  136 PRO   A N    1 
ATOM   2964 N  N    B PRO   A 1 136 ? 12.027 -6.220  -4.995  0.42 13.64 ?  136 PRO   A N    1 
ATOM   2965 C  CA   A PRO   A 1 136 ? 12.264 -6.915  -3.800  0.58 13.40 ?  136 PRO   A CA   1 
ATOM   2966 C  CA   B PRO   A 1 136 ? 12.265 -6.656  -3.608  0.42 13.63 ?  136 PRO   A CA   1 
ATOM   2967 C  C    A PRO   A 1 136 ? 11.856 -8.341  -3.477  0.58 12.66 ?  136 PRO   A C    1 
ATOM   2968 C  C    B PRO   A 1 136 ? 11.845 -8.087  -3.320  0.42 13.08 ?  136 PRO   A C    1 
ATOM   2969 O  O    A PRO   A 1 136 ? 12.474 -8.966  -2.608  0.58 12.62 ?  136 PRO   A O    1 
ATOM   2970 O  O    B PRO   A 1 136 ? 12.421 -8.715  -2.423  0.42 12.43 ?  136 PRO   A O    1 
ATOM   2971 C  CB   A PRO   A 1 136 ? 11.449 -5.887  -3.003  0.58 14.51 ?  136 PRO   A CB   1 
ATOM   2972 C  CB   B PRO   A 1 136 ? 11.472 -5.636  -2.777  0.42 14.35 ?  136 PRO   A CB   1 
ATOM   2973 C  CG   A PRO   A 1 136 ? 10.411 -5.396  -3.967  0.58 15.29 ?  136 PRO   A CG   1 
ATOM   2974 C  CG   B PRO   A 1 136 ? 10.491 -5.042  -3.738  0.42 14.85 ?  136 PRO   A CG   1 
ATOM   2975 C  CD   A PRO   A 1 136 ? 11.039 -5.442  -5.326  0.58 14.50 ?  136 PRO   A CD   1 
ATOM   2976 C  CD   B PRO   A 1 136 ? 11.173 -5.025  -5.056  0.42 14.25 ?  136 PRO   A CD   1 
ATOM   2977 H  HA   A PRO   A 1 136 ? 13.204 -6.806  -3.578  0.58 16.08 ?  136 PRO   A HA   1 
ATOM   2978 H  HA   B PRO   A 1 136 ? 13.203 -6.567  -3.389  0.42 16.36 ?  136 PRO   A HA   1 
ATOM   2979 H  HB2  A PRO   A 1 136 ? 11.035 -6.320  -2.238  0.58 17.41 ?  136 PRO   A HB2  1 
ATOM   2980 H  HB2  B PRO   A 1 136 ? 11.011 -6.086  -2.051  0.42 17.21 ?  136 PRO   A HB2  1 
ATOM   2981 H  HB3  A PRO   A 1 136 ? 12.029 -5.164  -2.715  0.58 17.41 ?  136 PRO   A HB3  1 
ATOM   2982 H  HB3  B PRO   A 1 136 ? 12.071 -4.954  -2.434  0.42 17.21 ?  136 PRO   A HB3  1 
ATOM   2983 H  HG2  A PRO   A 1 136 ? 9.637  -5.975  -3.933  0.58 18.35 ?  136 PRO   A HG2  1 
ATOM   2984 H  HG2  B PRO   A 1 136 ? 9.699  -5.602  -3.782  0.42 17.82 ?  136 PRO   A HG2  1 
ATOM   2985 H  HG3  A PRO   A 1 136 ? 10.167 -4.485  -3.741  0.58 18.35 ?  136 PRO   A HG3  1 
ATOM   2986 H  HG3  B PRO   A 1 136 ? 10.262 -4.144  -3.462  0.42 17.82 ?  136 PRO   A HG3  1 
ATOM   2987 H  HD2  A PRO   A 1 136 ? 10.375 -5.671  -5.997  0.58 17.40 ?  136 PRO   A HD2  1 
ATOM   2988 H  HD2  B PRO   A 1 136 ? 10.522 -5.108  -5.772  0.42 17.10 ?  136 PRO   A HD2  1 
ATOM   2989 H  HD3  A PRO   A 1 136 ? 11.477 -4.601  -5.531  0.58 17.40 ?  136 PRO   A HD3  1 
ATOM   2990 H  HD3  B PRO   A 1 136 ? 11.713 -4.225  -5.154  0.42 17.10 ?  136 PRO   A HD3  1 
ATOM   2991 N  N    A ILE   A 1 137 ? 10.819 -8.871  -4.127  0.58 13.04 ?  137 ILE   A N    1 
ATOM   2992 N  N    B ILE   A 1 137 ? 10.850 -8.621  -4.033  0.42 13.85 ?  137 ILE   A N    1 
ATOM   2993 C  CA   A ILE   A 1 137 ? 10.459 -10.272 -3.924  0.58 13.12 ?  137 ILE   A CA   1 
ATOM   2994 C  CA   B ILE   A 1 137 ? 10.456 -10.013 -3.822  0.42 14.15 ?  137 ILE   A CA   1 
ATOM   2995 C  C    A ILE   A 1 137 ? 11.626 -11.164 -4.315  0.58 12.37 ?  137 ILE   A C    1 
ATOM   2996 C  C    B ILE   A 1 137 ? 11.602 -10.939 -4.198  0.42 13.27 ?  137 ILE   A C    1 
ATOM   2997 O  O    A ILE   A 1 137 ? 11.952 -12.133 -3.618  0.58 12.46 ?  137 ILE   A O    1 
ATOM   2998 O  O    B ILE   A 1 137 ? 11.918 -11.894 -3.477  0.42 13.33 ?  137 ILE   A O    1 
ATOM   2999 C  CB   A ILE   A 1 137 ? 9.175  -10.611 -4.706  0.58 14.54 ?  137 ILE   A CB   1 
ATOM   3000 C  CB   B ILE   A 1 137 ? 9.186  -10.342 -4.628  0.42 15.38 ?  137 ILE   A CB   1 
ATOM   3001 C  CG1  A ILE   A 1 137 ? 7.973  -9.855  -4.120  0.58 15.87 ?  137 ILE   A CG1  1 
ATOM   3002 C  CG1  B ILE   A 1 137 ? 8.091  -9.298  -4.389  0.42 16.83 ?  137 ILE   A CG1  1 
ATOM   3003 C  CG2  A ILE   A 1 137 ? 8.938  -12.118 -4.712  0.58 14.93 ?  137 ILE   A CG2  1 
ATOM   3004 C  CG2  B ILE   A 1 137 ? 8.688  -11.746 -4.284  0.42 15.52 ?  137 ILE   A CG2  1 
ATOM   3005 C  CD1  A ILE   A 1 137 ? 6.722  -9.903  -4.982  0.58 16.65 ?  137 ILE   A CD1  1 
ATOM   3006 C  CD1  B ILE   A 1 137 ? 7.134  -9.176  -5.546  0.42 17.95 ?  137 ILE   A CD1  1 
ATOM   3007 H  H    A ILE   A 1 137 ? 10.317 -8.450  -4.682  0.58 15.65 ?  137 ILE   A H    1 
ATOM   3008 H  H    B ILE   A 1 137 ? 10.398 -8.206  -4.640  0.42 16.62 ?  137 ILE   A H    1 
ATOM   3009 H  HA   A ILE   A 1 137 ? 10.284 -10.423 -2.985  0.58 15.75 ?  137 ILE   A HA   1 
ATOM   3010 H  HA   B ILE   A 1 137 ? 10.255 -10.150 -2.885  0.42 16.97 ?  137 ILE   A HA   1 
ATOM   3011 H  HB   A ILE   A 1 137 ? 9.293  -10.326 -5.623  0.58 17.45 ?  137 ILE   A HB   1 
ATOM   3012 H  HB   B ILE   A 1 137 ? 9.413  -10.334 -5.568  0.42 18.46 ?  137 ILE   A HB   1 
ATOM   3013 H  HG12 A ILE   A 1 137 ? 7.759  -10.240 -3.257  0.58 19.05 ?  137 ILE   A HG12 1 
ATOM   3014 H  HG12 B ILE   A 1 137 ? 7.581  -9.556  -3.608  0.42 20.20 ?  137 ILE   A HG12 1 
ATOM   3015 H  HG13 A ILE   A 1 137 ? 8.225  -8.924  -4.010  0.58 19.05 ?  137 ILE   A HG13 1 
ATOM   3016 H  HG13 B ILE   A 1 137 ? 8.486  -8.423  -4.243  0.42 20.20 ?  137 ILE   A HG13 1 
ATOM   3017 H  HG21 A ILE   A 1 137 ? 8.011  -12.299 -4.936  0.58 17.92 ?  137 ILE   A HG21 1 
ATOM   3018 H  HG21 B ILE   A 1 137 ? 7.826  -11.891 -4.707  0.42 18.63 ?  137 ILE   A HG21 1 
ATOM   3019 H  HG22 A ILE   A 1 137 ? 9.518  -12.527 -5.375  0.58 17.92 ?  137 ILE   A HG22 1 
ATOM   3020 H  HG22 B ILE   A 1 137 ? 9.328  -12.399 -4.611  0.42 18.63 ?  137 ILE   A HG22 1 
ATOM   3021 H  HG23 A ILE   A 1 137 ? 9.137  -12.473 -3.833  0.58 17.92 ?  137 ILE   A HG23 1 
ATOM   3022 H  HG23 B ILE   A 1 137 ? 8.599  -11.824 -3.321  0.42 18.63 ?  137 ILE   A HG23 1 
ATOM   3023 H  HD11 A ILE   A 1 137 ? 5.956  -10.047 -4.408  0.58 19.98 ?  137 ILE   A HD11 1 
ATOM   3024 H  HD11 B ILE   A 1 137 ? 6.922  -8.240  -5.680  0.42 21.54 ?  137 ILE   A HD11 1 
ATOM   3025 H  HD12 A ILE   A 1 137 ? 6.636  -9.060  -5.450  0.58 19.98 ?  137 ILE   A HD12 1 
ATOM   3026 H  HD12 B ILE   A 1 137 ? 7.553  -9.533  -6.345  0.42 21.54 ?  137 ILE   A HD12 1 
ATOM   3027 H  HD13 A ILE   A 1 137 ? 6.801  -10.629 -5.620  0.58 19.98 ?  137 ILE   A HD13 1 
ATOM   3028 H  HD13 B ILE   A 1 137 ? 6.333  -9.676  -5.341  0.42 21.54 ?  137 ILE   A HD13 1 
ATOM   3029 N  N    A HIS   A 1 138 ? 12.282 -10.840 -5.429  0.58 12.62 ?  138 HIS   A N    1 
ATOM   3030 N  N    B HIS   A 1 138 ? 12.239 -10.668 -5.338  0.42 13.44 ?  138 HIS   A N    1 
ATOM   3031 C  CA   A HIS   A 1 138 ? 13.488 -11.561 -5.817  0.58 12.88 ?  138 HIS   A CA   1 
ATOM   3032 C  CA   B HIS   A 1 138 ? 13.378 -11.470 -5.774  0.42 13.26 ?  138 HIS   A CA   1 
ATOM   3033 C  C    A HIS   A 1 138 ? 14.603 -11.375 -4.792  0.58 12.40 ?  138 HIS   A C    1 
ATOM   3034 C  C    B HIS   A 1 138 ? 14.538 -11.358 -4.790  0.42 12.76 ?  138 HIS   A C    1 
ATOM   3035 O  O    A HIS   A 1 138 ? 15.284 -12.338 -4.423  0.58 12.54 ?  138 HIS   A O    1 
ATOM   3036 O  O    B HIS   A 1 138 ? 15.181 -12.358 -4.454  0.42 13.04 ?  138 HIS   A O    1 
ATOM   3037 C  CB   A HIS   A 1 138 ? 13.937 -11.122 -7.209  0.58 14.10 ?  138 HIS   A CB   1 
ATOM   3038 C  CB   B HIS   A 1 138 ? 13.797 -11.019 -7.173  0.42 13.52 ?  138 HIS   A CB   1 
ATOM   3039 C  CG   A HIS   A 1 138 ? 15.181 -11.810 -7.674  0.58 15.10 ?  138 HIS   A CG   1 
ATOM   3040 C  CG   B HIS   A 1 138 ? 15.083 -11.623 -7.642  0.42 14.05 ?  138 HIS   A CG   1 
ATOM   3041 N  ND1  A HIS   A 1 138 ? 15.240 -13.170 -7.891  0.58 16.62 ?  138 HIS   A ND1  1 
ATOM   3042 N  ND1  B HIS   A 1 138 ? 15.213 -12.963 -7.937  0.42 15.17 ?  138 HIS   A ND1  1 
ATOM   3043 C  CD2  A HIS   A 1 138 ? 16.420 -11.332 -7.933  0.58 15.57 ?  138 HIS   A CD2  1 
ATOM   3044 C  CD2  B HIS   A 1 138 ? 16.298 -11.069 -7.862  0.42 14.20 ?  138 HIS   A CD2  1 
ATOM   3045 C  CE1  A HIS   A 1 138 ? 16.459 -13.497 -8.280  0.58 16.98 ?  138 HIS   A CE1  1 
ATOM   3046 C  CE1  B HIS   A 1 138 ? 16.454 -13.207 -8.321  0.42 15.20 ?  138 HIS   A CE1  1 
ATOM   3047 N  NE2  A HIS   A 1 138 ? 17.195 -12.400 -8.314  0.58 16.19 ?  138 HIS   A NE2  1 
ATOM   3048 N  NE2  B HIS   A 1 138 ? 17.133 -12.074 -8.285  0.42 14.63 ?  138 HIS   A NE2  1 
ATOM   3049 H  H    A HIS   A 1 138 ? 12.050 -10.213 -5.975  0.58 15.15 ?  138 HIS   A H    1 
ATOM   3050 H  H    B HIS   A 1 138 ? 12.034 -10.022 -5.872  0.42 16.13 ?  138 HIS   A H    1 
ATOM   3051 H  HA   A HIS   A 1 138 ? 13.280 -12.506 -5.867  0.58 15.46 ?  138 HIS   A HA   1 
ATOM   3052 H  HA   B HIS   A 1 138 ? 13.110 -12.398 -5.825  0.42 15.91 ?  138 HIS   A HA   1 
ATOM   3053 H  HB2  A HIS   A 1 138 ? 13.230 -11.322 -7.849  0.58 16.91 ?  138 HIS   A HB2  1 
ATOM   3054 H  HB2  B HIS   A 1 138 ? 13.104 -11.273 -7.807  0.42 16.22 ?  138 HIS   A HB2  1 
ATOM   3055 H  HB3  A HIS   A 1 138 ? 14.109 -10.168 -7.201  0.58 16.91 ?  138 HIS   A HB3  1 
ATOM   3056 H  HB3  B HIS   A 1 138 ? 13.906 -10.056 -7.178  0.42 16.22 ?  138 HIS   A HB3  1 
ATOM   3057 H  HD1  A HIS   A 1 138 ? 14.583 -13.717 -7.798  0.58 19.94 ?  138 HIS   A HD1  1 
ATOM   3058 H  HD1  B HIS   A 1 138 ? 14.584 -13.550 -7.882  0.42 18.20 ?  138 HIS   A HD1  1 
ATOM   3059 H  HD2  A HIS   A 1 138 ? 16.690 -10.443 -7.871  0.58 18.69 ?  138 HIS   A HD2  1 
ATOM   3060 H  HD2  B HIS   A 1 138 ? 16.525 -10.176 -7.750  0.42 17.04 ?  138 HIS   A HD2  1 
ATOM   3061 H  HE1  A HIS   A 1 138 ? 16.750 -14.352 -8.492  0.58 20.37 ?  138 HIS   A HE1  1 
ATOM   3062 H  HE1  B HIS   A 1 138 ? 16.790 -14.039 -8.574  0.42 18.24 ?  138 HIS   A HE1  1 
ATOM   3063 N  N    . SER   A 1 139 ? 14.815 -10.144 -4.321  1.00 12.31 ?  139 SER   A N    1 
ATOM   3064 C  CA   . SER   A 1 139 ? 15.880 -9.935  -3.349  1.00 11.96 ?  139 SER   A CA   1 
ATOM   3065 C  C    . SER   A 1 139 ? 15.665 -10.769 -2.091  1.00 11.51 ?  139 SER   A C    1 
ATOM   3066 O  O    . SER   A 1 139 ? 16.613 -11.356 -1.558  1.00 11.61 ?  139 SER   A O    1 
ATOM   3067 C  CB   . SER   A 1 139 ? 15.999 -8.453  -3.008  1.00 12.18 ?  139 SER   A CB   1 
ATOM   3068 O  OG   . SER   A 1 139 ? 17.083 -8.261  -2.115  1.00 12.44 ?  139 SER   A OG   1 
ATOM   3069 H  H    A SER   A 1 139 ? 14.373 -9.439  -4.541  0.58 14.77 ?  139 SER   A H    1 
ATOM   3070 H  H    B SER   A 1 139 ? 14.397 -9.427  -4.547  0.42 14.77 ?  139 SER   A H    1 
ATOM   3071 H  HA   . SER   A 1 139 ? 16.722 -10.213 -3.746  1.00 14.35 ?  139 SER   A HA   1 
ATOM   3072 H  HB2  . SER   A 1 139 ? 16.165 -7.948  -3.819  1.00 14.61 ?  139 SER   A HB2  1 
ATOM   3073 H  HB3  . SER   A 1 139 ? 15.179 -8.154  -2.586  1.00 14.61 ?  139 SER   A HB3  1 
ATOM   3074 H  HG   . SER   A 1 139 ? 17.156 -7.444  -1.915  1.00 14.93 ?  139 SER   A HG   1 
ATOM   3075 N  N    A LEU   A 1 140 ? 14.417 -10.878 -1.628  0.58 11.58 ?  140 LEU   A N    1 
ATOM   3076 N  N    B LEU   A 1 140 ? 14.432 -10.781 -1.572  0.42 11.15 ?  140 LEU   A N    1 
ATOM   3077 C  CA   A LEU   A 1 140 ? 14.146 -11.728 -0.473  0.58 11.40 ?  140 LEU   A CA   1 
ATOM   3078 C  CA   B LEU   A 1 140 ? 14.146 -11.545 -0.361  0.42 10.48 ?  140 LEU   A CA   1 
ATOM   3079 C  C    A LEU   A 1 140 ? 14.438 -13.190 -0.789  0.58 11.26 ?  140 LEU   A C    1 
ATOM   3080 C  C    B LEU   A 1 140 ? 14.397 -13.032 -0.580  0.42 10.45 ?  140 LEU   A C    1 
ATOM   3081 O  O    A LEU   A 1 140 ? 15.036 -13.903 0.025   0.58 11.75 ?  140 LEU   A O    1 
ATOM   3082 O  O    B LEU   A 1 140 ? 14.913 -13.720 0.309   0.42 10.89 ?  140 LEU   A O    1 
ATOM   3083 C  CB   A LEU   A 1 140 ? 12.699 -11.550 -0.011  0.58 11.97 ?  140 LEU   A CB   1 
ATOM   3084 C  CB   B LEU   A 1 140 ? 12.705 -11.291 0.089   0.42 10.20 ?  140 LEU   A CB   1 
ATOM   3085 C  CG   A LEU   A 1 140 ? 12.269 -12.464 1.139   0.58 11.91 ?  140 LEU   A CG   1 
ATOM   3086 C  CG   B LEU   A 1 140 ? 12.204 -12.089 1.297   0.42 10.41 ?  140 LEU   A CG   1 
ATOM   3087 C  CD1  A LEU   A 1 140 ? 13.166 -12.286 2.357   0.58 11.99 ?  140 LEU   A CD1  1 
ATOM   3088 C  CD1  B LEU   A 1 140 ? 13.064 -11.842 2.526   0.42 10.32 ?  140 LEU   A CD1  1 
ATOM   3089 C  CD2  A LEU   A 1 140 ? 10.803 -12.217 1.499   0.58 12.55 ?  140 LEU   A CD2  1 
ATOM   3090 C  CD2  B LEU   A 1 140 ? 10.744 -11.754 1.588   0.42 10.70 ?  140 LEU   A CD2  1 
ATOM   3091 H  H    A LEU   A 1 140 ? 13.730 -10.480 -1.958  0.58 13.89 ?  140 LEU   A H    1 
ATOM   3092 H  H    B LEU   A 1 140 ? 13.760 -10.350 -1.894  0.42 13.38 ?  140 LEU   A H    1 
ATOM   3093 H  HA   A LEU   A 1 140 ? 14.724 -11.462 0.254   0.58 13.68 ?  140 LEU   A HA   1 
ATOM   3094 H  HA   B LEU   A 1 140 ? 14.735 -11.239 0.347   0.42 12.58 ?  140 LEU   A HA   1 
ATOM   3095 H  HB2  A LEU   A 1 140 ? 12.581 -10.633 0.284   0.58 14.36 ?  140 LEU   A HB2  1 
ATOM   3096 H  HB2  B LEU   A 1 140 ? 12.618 -10.351 0.313   0.42 12.23 ?  140 LEU   A HB2  1 
ATOM   3097 H  HB3  A LEU   A 1 140 ? 12.110 -11.728 -0.761  0.58 14.36 ?  140 LEU   A HB3  1 
ATOM   3098 H  HB3  B LEU   A 1 140 ? 12.116 -11.498 -0.651  0.42 12.23 ?  140 LEU   A HB3  1 
ATOM   3099 H  HG   A LEU   A 1 140 ? 12.343 -13.386 0.852   0.58 14.29 ?  140 LEU   A HG   1 
ATOM   3100 H  HG   B LEU   A 1 140 ? 12.251 -13.033 1.091   0.42 12.50 ?  140 LEU   A HG   1 
ATOM   3101 H  HD11 A LEU   A 1 140 ? 12.796 -12.789 3.097   0.58 14.39 ?  140 LEU   A HD11 1 
ATOM   3102 H  HD11 B LEU   A 1 140 ? 12.679 -12.315 3.279   0.42 12.39 ?  140 LEU   A HD11 1 
ATOM   3103 H  HD12 A LEU   A 1 140 ? 14.055 -12.616 2.146   0.58 14.39 ?  140 LEU   A HD12 1 
ATOM   3104 H  HD12 B LEU   A 1 140 ? 13.961 -12.169 2.352   0.42 12.39 ?  140 LEU   A HD12 1 
ATOM   3105 H  HD13 A LEU   A 1 140 ? 13.209 -11.344 2.583   0.58 14.39 ?  140 LEU   A HD13 1 
ATOM   3106 H  HD13 B LEU   A 1 140 ? 13.088 -10.890 2.709   0.42 12.39 ?  140 LEU   A HD13 1 
ATOM   3107 H  HD21 A LEU   A 1 140 ? 10.554 -12.806 2.230   0.58 15.06 ?  140 LEU   A HD21 1 
ATOM   3108 H  HD21 B LEU   A 1 140 ? 10.430 -12.319 2.314   0.42 12.84 ?  140 LEU   A HD21 1 
ATOM   3109 H  HD22 A LEU   A 1 140 ? 10.696 -11.291 1.772   0.58 15.06 ?  140 LEU   A HD22 1 
ATOM   3110 H  HD22 B LEU   A 1 140 ? 10.677 -10.822 1.843   0.42 12.84 ?  140 LEU   A HD22 1 
ATOM   3111 H  HD23 A LEU   A 1 140 ? 10.250 -12.399 0.724   0.58 15.06 ?  140 LEU   A HD23 1 
ATOM   3112 H  HD23 B LEU   A 1 140 ? 10.217 -11.921 0.791   0.42 12.84 ?  140 LEU   A HD23 1 
ATOM   3113 N  N    A ARG   A 1 141 ? 14.023 -13.652 -1.971  0.58 12.01 ?  141 ARG   A N    1 
ATOM   3114 N  N    B ARG   A 1 141 ? 14.046 -13.545 -1.763  0.42 11.21 ?  141 ARG   A N    1 
ATOM   3115 C  CA   A ARG   A 1 141 ? 14.280 -15.032 -2.366  0.58 13.07 ?  141 ARG   A CA   1 
ATOM   3116 C  CA   B ARG   A 1 141 ? 14.283 -14.958 -2.047  0.42 11.42 ?  141 ARG   A CA   1 
ATOM   3117 C  C    A ARG   A 1 141 ? 15.774 -15.338 -2.342  0.58 12.82 ?  141 ARG   A C    1 
ATOM   3118 C  C    B ARG   A 1 141 ? 15.775 -15.251 -2.143  0.42 11.33 ?  141 ARG   A C    1 
ATOM   3119 O  O    A ARG   A 1 141 ? 16.202 -16.369 -1.810  0.58 12.88 ?  141 ARG   A O    1 
ATOM   3120 O  O    B ARG   A 1 141 ? 16.263 -16.232 -1.569  0.42 11.59 ?  141 ARG   A O    1 
ATOM   3121 C  CB   A ARG   A 1 141 ? 13.703 -15.267 -3.763  0.58 14.53 ?  141 ARG   A CB   1 
ATOM   3122 C  CB   B ARG   A 1 141 ? 13.550 -15.377 -3.326  0.42 12.19 ?  141 ARG   A CB   1 
ATOM   3123 C  CG   A ARG   A 1 141 ? 13.630 -16.722 -4.191  0.58 16.84 ?  141 ARG   A CG   1 
ATOM   3124 C  CG   B ARG   A 1 141 ? 13.740 -16.853 -3.706  0.42 13.69 ?  141 ARG   A CG   1 
ATOM   3125 C  CD   A ARG   A 1 141 ? 12.609 -17.473 -3.368  0.58 17.92 ?  141 ARG   A CD   1 
ATOM   3126 C  CD   B ARG   A 1 141 ? 13.128 -17.793 -2.678  0.42 14.45 ?  141 ARG   A CD   1 
ATOM   3127 N  NE   A ARG   A 1 141 ? 13.231 -18.292 -2.337  0.58 18.89 ?  141 ARG   A NE   1 
ATOM   3128 N  NE   B ARG   A 1 141 ? 11.703 -17.540 -2.501  0.42 15.37 ?  141 ARG   A NE   1 
ATOM   3129 C  CZ   A ARG   A 1 141 ? 12.571 -18.845 -1.328  0.58 19.57 ?  141 ARG   A CZ   1 
ATOM   3130 C  CZ   B ARG   A 1 141 ? 10.950 -18.108 -1.569  0.42 15.71 ?  141 ARG   A CZ   1 
ATOM   3131 N  NH1  A ARG   A 1 141 ? 11.284 -18.607 -1.129  0.58 20.03 ?  141 ARG   A NH1  1 
ATOM   3132 N  NH1  B ARG   A 1 141 ? 11.452 -18.981 -0.711  0.42 15.99 ?  141 ARG   A NH1  1 
ATOM   3133 N  NH2  A ARG   A 1 141 ? 13.217 -19.658 -0.499  0.58 19.97 ?  141 ARG   A NH2  1 
ATOM   3134 N  NH2  B ARG   A 1 141 ? 9.660  -17.791 -1.496  0.42 16.31 ?  141 ARG   A NH2  1 
ATOM   3135 H  H    A ARG   A 1 141 ? 13.592 -13.192 -2.555  0.58 14.41 ?  141 ARG   A H    1 
ATOM   3136 H  H    B ARG   A 1 141 ? 13.673 -13.105 -2.402  0.42 13.45 ?  141 ARG   A H    1 
ATOM   3137 H  HA   A ARG   A 1 141 ? 13.841 -15.634 -1.745  0.58 15.68 ?  141 ARG   A HA   1 
ATOM   3138 H  HA   B ARG   A 1 141 ? 13.930 -15.486 -1.318  0.42 13.71 ?  141 ARG   A HA   1 
ATOM   3139 H  HB2  A ARG   A 1 141 ? 12.803 -14.909 -3.787  0.58 17.44 ?  141 ARG   A HB2  1 
ATOM   3140 H  HB2  B ARG   A 1 141 ? 12.595 -15.227 -3.202  0.42 14.63 ?  141 ARG   A HB2  1 
ATOM   3141 H  HB3  A ARG   A 1 141 ? 14.257 -14.804 -4.406  0.58 17.44 ?  141 ARG   A HB3  1 
ATOM   3142 H  HB3  B ARG   A 1 141 ? 13.868 -14.839 -4.064  0.42 14.63 ?  141 ARG   A HB3  1 
ATOM   3143 H  HG2  A ARG   A 1 141 ? 13.368 -16.773 -5.123  0.58 20.21 ?  141 ARG   A HG2  1 
ATOM   3144 H  HG2  B ARG   A 1 141 ? 13.308 -17.020 -4.560  0.42 16.42 ?  141 ARG   A HG2  1 
ATOM   3145 H  HG3  A ARG   A 1 141 ? 14.495 -17.144 -4.060  0.58 20.21 ?  141 ARG   A HG3  1 
ATOM   3146 H  HG3  B ARG   A 1 141 ? 14.688 -17.054 -3.773  0.42 16.42 ?  141 ARG   A HG3  1 
ATOM   3147 H  HD2  A ARG   A 1 141 ? 12.023 -16.840 -2.928  0.58 21.50 ?  141 ARG   A HD2  1 
ATOM   3148 H  HD2  B ARG   A 1 141 ? 13.235 -18.708 -2.978  0.42 17.34 ?  141 ARG   A HD2  1 
ATOM   3149 H  HD3  A ARG   A 1 141 ? 12.091 -18.053 -3.952  0.58 21.50 ?  141 ARG   A HD3  1 
ATOM   3150 H  HD3  B ARG   A 1 141 ? 13.567 -17.665 -1.824  0.42 17.34 ?  141 ARG   A HD3  1 
ATOM   3151 H  HE   A ARG   A 1 141 ? 14.057 -18.511 -2.443  0.58 22.67 ?  141 ARG   A HE   1 
ATOM   3152 H  HE   B ARG   A 1 141 ? 11.316 -17.010 -3.058  0.42 18.44 ?  141 ARG   A HE   1 
ATOM   3153 H  HH11 A ARG   A 1 141 ? 10.851 -18.094 -1.664  0.58 24.04 ?  141 ARG   A HH11 1 
ATOM   3154 H  HH11 B ARG   A 1 141 ? 12.283 -19.195 -0.751  0.42 19.19 ?  141 ARG   A HH11 1 
ATOM   3155 H  HH12 A ARG   A 1 141 ? 10.878 -18.977 -0.466  0.58 24.04 ?  141 ARG   A HH12 1 
ATOM   3156 H  HH12 B ARG   A 1 141 ? 10.943 -19.340 -0.118  0.42 19.19 ?  141 ARG   A HH12 1 
ATOM   3157 H  HH21 A ARG   A 1 141 ? 14.056 -19.819 -0.619  0.58 23.96 ?  141 ARG   A HH21 1 
ATOM   3158 H  HH21 B ARG   A 1 141 ? 9.323  -17.226 -2.049  0.42 19.57 ?  141 ARG   A HH21 1 
ATOM   3159 H  HH22 A ARG   A 1 141 ? 12.804 -20.015 0.165   0.58 23.96 ?  141 ARG   A HH22 1 
ATOM   3160 H  HH22 B ARG   A 1 141 ? 9.161  -18.156 -0.898  0.42 19.57 ?  141 ARG   A HH22 1 
ATOM   3161 N  N    A VAL   A 1 142 ? 16.586 -14.456 -2.926  0.58 12.48 ?  142 VAL   A N    1 
ATOM   3162 N  N    B VAL   A 1 142 ? 16.522 -14.407 -2.862  0.42 11.47 ?  142 VAL   A N    1 
ATOM   3163 C  CA   A VAL   A 1 142 ? 18.029 -14.678 -2.923  0.58 11.96 ?  142 VAL   A CA   1 
ATOM   3164 C  CA   B VAL   A 1 142 ? 17.969 -14.592 -2.939  0.42 11.55 ?  142 VAL   A CA   1 
ATOM   3165 C  C    A VAL   A 1 142 ? 18.577 -14.632 -1.502  0.58 11.55 ?  142 VAL   A C    1 
ATOM   3166 C  C    B VAL   A 1 142 ? 18.573 -14.595 -1.541  0.42 11.42 ?  142 VAL   A C    1 
ATOM   3167 O  O    A VAL   A 1 142 ? 19.424 -15.449 -1.127  0.58 12.02 ?  142 VAL   A O    1 
ATOM   3168 O  O    B VAL   A 1 142 ? 19.454 -15.402 -1.227  0.42 11.91 ?  142 VAL   A O    1 
ATOM   3169 C  CB   A VAL   A 1 142 ? 18.748 -13.696 -3.867  0.58 12.13 ?  142 VAL   A CB   1 
ATOM   3170 C  CB   B VAL   A 1 142 ? 18.608 -13.518 -3.841  0.42 12.17 ?  142 VAL   A CB   1 
ATOM   3171 C  CG1  A VAL   A 1 142 ? 20.256 -13.944 -3.841  0.58 11.08 ?  142 VAL   A CG1  1 
ATOM   3172 C  CG1  B VAL   A 1 142 ? 20.125 -13.623 -3.795  0.42 12.21 ?  142 VAL   A CG1  1 
ATOM   3173 C  CG2  A VAL   A 1 142 ? 18.227 -13.833 -5.289  0.58 13.38 ?  142 VAL   A CG2  1 
ATOM   3174 C  CG2  B VAL   A 1 142 ? 18.125 -13.657 -5.274  0.42 12.94 ?  142 VAL   A CG2  1 
ATOM   3175 H  H    A VAL   A 1 142 ? 16.334 -13.736 -3.326  0.58 14.97 ?  142 VAL   A H    1 
ATOM   3176 H  H    B VAL   A 1 142 ? 16.224 -13.724 -3.301  0.42 13.76 ?  142 VAL   A H    1 
ATOM   3177 H  HA   A VAL   A 1 142 ? 18.201 -15.567 -3.266  0.58 14.35 ?  142 VAL   A HA   1 
ATOM   3178 H  HA   B VAL   A 1 142 ? 18.153 -15.451 -3.347  0.42 13.86 ?  142 VAL   A HA   1 
ATOM   3179 H  HB   A VAL   A 1 142 ? 18.591 -12.784 -3.574  0.58 14.56 ?  142 VAL   A HB   1 
ATOM   3180 H  HB   B VAL   A 1 142 ? 18.359 -12.633 -3.524  0.42 14.60 ?  142 VAL   A HB   1 
ATOM   3181 H  HG11 A VAL   A 1 142 ? 20.675 -13.462 -4.573  0.58 13.29 ?  142 VAL   A HG11 1 
ATOM   3182 H  HG11 B VAL   A 1 142 ? 20.503 -13.055 -4.488  0.42 14.65 ?  142 VAL   A HG11 1 
ATOM   3183 H  HG12 A VAL   A 1 142 ? 20.619 -13.632 -2.996  0.58 13.29 ?  142 VAL   A HG12 1 
ATOM   3184 H  HG12 B VAL   A 1 142 ? 20.441 -13.328 -2.926  0.42 14.65 ?  142 VAL   A HG12 1 
ATOM   3185 H  HG13 A VAL   A 1 142 ? 20.424 -14.896 -3.940  0.58 13.29 ?  142 VAL   A HG13 1 
ATOM   3186 H  HG13 B VAL   A 1 142 ? 20.381 -14.543 -3.948  0.42 14.65 ?  142 VAL   A HG13 1 
ATOM   3187 H  HG21 A VAL   A 1 142 ? 18.729 -13.236 -5.869  0.58 16.06 ?  142 VAL   A HG21 1 
ATOM   3188 H  HG21 B VAL   A 1 142 ? 18.531 -12.959 -5.814  0.42 15.53 ?  142 VAL   A HG21 1 
ATOM   3189 H  HG22 A VAL   A 1 142 ? 18.345 -14.750 -5.578  0.58 16.06 ?  142 VAL   A HG22 1 
ATOM   3190 H  HG22 B VAL   A 1 142 ? 18.392 -14.528 -5.608  0.42 15.53 ?  142 VAL   A HG22 1 
ATOM   3191 H  HG23 A VAL   A 1 142 ? 17.289 -13.596 -5.302  0.58 16.06 ?  142 VAL   A HG23 1 
ATOM   3192 H  HG23 B VAL   A 1 142 ? 17.163 -13.574 -5.290  0.42 15.53 ?  142 VAL   A HG23 1 
ATOM   3193 N  N    . CYS   A 1 143 ? 18.109 -13.686 -0.684  1.00 11.35 ?  143 CYS   A N    1 
ATOM   3194 C  CA   . CYS   A 1 143 ? 18.569 -13.638 0.701   1.00 11.78 ?  143 CYS   A CA   1 
ATOM   3195 C  C    . CYS   A 1 143 ? 18.333 -14.975 1.397   1.00 11.68 ?  143 CYS   A C    1 
ATOM   3196 O  O    . CYS   A 1 143 ? 19.247 -15.563 1.983   1.00 11.84 ?  143 CYS   A O    1 
ATOM   3197 C  CB   . CYS   A 1 143 ? 17.852 -12.513 1.444   1.00 12.31 ?  143 CYS   A CB   1 
ATOM   3198 S  SG   . CYS   A 1 143 ? 18.346 -12.334 3.169   1.00 12.51 ?  143 CYS   A SG   1 
ATOM   3199 H  H    A CYS   A 1 143 ? 17.538 -13.082 -0.901  0.58 13.63 ?  143 CYS   A H    1 
ATOM   3200 H  H    B CYS   A 1 143 ? 17.529 -13.085 -0.884  0.42 13.63 ?  143 CYS   A H    1 
ATOM   3201 H  HA   . CYS   A 1 143 ? 19.521 -13.457 0.715   1.00 14.14 ?  143 CYS   A HA   1 
ATOM   3202 H  HB2  . CYS   A 1 143 ? 18.035 -11.675 0.992   1.00 14.77 ?  143 CYS   A HB2  1 
ATOM   3203 H  HB3  . CYS   A 1 143 ? 16.901 -12.689 1.428   1.00 14.77 ?  143 CYS   A HB3  1 
ATOM   3204 H  HG   . CYS   A 1 143 ? 17.766 -11.398 3.635   1.00 15.01 ?  143 CYS   A HG   1 
ATOM   3205 N  N    . VAL   A 1 144 ? 17.103 -15.475 1.334   1.00 12.02 ?  144 VAL   A N    1 
ATOM   3206 C  CA   . VAL   A 1 144 ? 16.756 -16.707 2.032   1.00 13.23 ?  144 VAL   A CA   1 
ATOM   3207 C  C    . VAL   A 1 144 ? 17.573 -17.881 1.513   1.00 13.00 ?  144 VAL   A C    1 
ATOM   3208 O  O    . VAL   A 1 144 ? 17.943 -18.784 2.276   1.00 13.73 ?  144 VAL   A O    1 
ATOM   3209 C  CB   . VAL   A 1 144 ? 15.240 -16.942 1.894   1.00 15.73 ?  144 VAL   A CB   1 
ATOM   3210 C  CG1  . VAL   A 1 144 ? 14.867 -18.379 2.193   1.00 17.30 ?  144 VAL   A CG1  1 
ATOM   3211 C  CG2  . VAL   A 1 144 ? 14.486 -15.961 2.793   1.00 15.76 ?  144 VAL   A CG2  1 
ATOM   3212 H  H    . VAL   A 1 144 ? 16.450 -15.117 0.893   1.00 14.42 ?  144 VAL   A H    1 
ATOM   3213 H  HA   . VAL   A 1 144 ? 16.949 -16.603 2.969   1.00 15.87 ?  144 VAL   A HA   1 
ATOM   3214 H  HB   . VAL   A 1 144 ? 14.970 -16.752 0.976   1.00 18.87 ?  144 VAL   A HB   1 
ATOM   3215 H  HG11 . VAL   A 1 144 ? 13.913 -18.429 2.369   1.00 20.76 ?  144 VAL   A HG11 1 
ATOM   3216 H  HG12 . VAL   A 1 144 ? 15.087 -18.931 1.426   1.00 20.76 ?  144 VAL   A HG12 1 
ATOM   3217 H  HG13 . VAL   A 1 144 ? 15.360 -18.675 2.972   1.00 20.76 ?  144 VAL   A HG13 1 
ATOM   3218 H  HG21 . VAL   A 1 144 ? 13.530 -16.117 2.712   1.00 18.91 ?  144 VAL   A HG21 1 
ATOM   3219 H  HG22 . VAL   A 1 144 ? 14.764 -16.094 3.712   1.00 18.91 ?  144 VAL   A HG22 1 
ATOM   3220 H  HG23 . VAL   A 1 144 ? 14.691 -15.050 2.516   1.00 18.91 ?  144 VAL   A HG23 1 
ATOM   3221 N  N    . ASP   A 1 145 ? 17.849 -17.901 0.211   1.00 13.04 ?  145 ASP   A N    1 
ATOM   3222 C  CA   . ASP   A 1 145 ? 18.561 -19.008 -0.415  1.00 13.52 ?  145 ASP   A CA   1 
ATOM   3223 C  C    . ASP   A 1 145 ? 20.080 -18.865 -0.362  1.00 13.41 ?  145 ASP   A C    1 
ATOM   3224 O  O    . ASP   A 1 145 ? 20.783 -19.763 -0.834  1.00 15.58 ?  145 ASP   A O    1 
ATOM   3225 C  CB   . ASP   A 1 145 ? 18.115 -19.149 -1.874  1.00 14.77 ?  145 ASP   A CB   1 
ATOM   3226 C  CG   . ASP   A 1 145 ? 16.668 -19.596 -2.006  1.00 17.29 ?  145 ASP   A CG   1 
ATOM   3227 O  OD1  . ASP   A 1 145 ? 16.102 -20.142 -1.032  1.00 18.08 ?  145 ASP   A OD1  1 
ATOM   3228 O  OD2  . ASP   A 1 145 ? 16.098 -19.397 -3.096  1.00 18.88 -1 145 ASP   A OD2  1 
ATOM   3229 H  H    . ASP   A 1 145 ? 17.619 -17.281 -0.344  1.00 15.65 ?  145 ASP   A H    1 
ATOM   3230 H  HA   . ASP   A 1 145 ? 18.325 -19.829 0.042   1.00 16.22 ?  145 ASP   A HA   1 
ATOM   3231 H  HB2  . ASP   A 1 145 ? 18.213 -18.293 -2.320  1.00 17.72 ?  145 ASP   A HB2  1 
ATOM   3232 H  HB3  . ASP   A 1 145 ? 18.672 -19.815 -2.311  1.00 17.72 ?  145 ASP   A HB3  1 
ATOM   3233 N  N    . THR   A 1 146 ? 20.599 -17.771 0.182   1.00 11.92 ?  146 THR   A N    1 
ATOM   3234 C  CA   . THR   A 1 146 ? 22.039 -17.527 0.204   1.00 11.54 ?  146 THR   A CA   1 
ATOM   3235 C  C    . THR   A 1 146 ? 22.594 -17.340 1.603   1.00 11.86 ?  146 THR   A C    1 
ATOM   3236 O  O    . THR   A 1 146 ? 23.670 -17.870 1.909   1.00 13.05 ?  146 THR   A O    1 
ATOM   3237 C  CB   . THR   A 1 146 ? 22.369 -16.281 -0.637  1.00 11.63 ?  146 THR   A CB   1 
ATOM   3238 O  OG1  . THR   A 1 146 ? 21.846 -16.449 -1.954  1.00 12.06 ?  146 THR   A OG1  1 
ATOM   3239 C  CG2  . THR   A 1 146 ? 23.863 -16.057 -0.733  1.00 12.34 ?  146 THR   A CG2  1 
ATOM   3240 H  H    . THR   A 1 146 ? 20.134 -17.140 0.542   1.00 14.31 ?  146 THR   A H    1 
ATOM   3241 H  HA   . THR   A 1 146 ? 22.495 -18.280 -0.194  1.00 13.84 ?  146 THR   A HA   1 
ATOM   3242 H  HB   . THR   A 1 146 ? 21.975 -15.495 -0.230  1.00 13.95 ?  146 THR   A HB   1 
ATOM   3243 H  HG1  . THR   A 1 146 ? 21.010 -16.519 -1.920  1.00 14.47 ?  146 THR   A HG1  1 
ATOM   3244 H  HG21 . THR   A 1 146 ? 24.053 -15.390 -1.411  1.00 14.81 ?  146 THR   A HG21 1 
ATOM   3245 H  HG22 . THR   A 1 146 ? 24.208 -15.748 0.118   1.00 14.81 ?  146 THR   A HG22 1 
ATOM   3246 H  HG23 . THR   A 1 146 ? 24.305 -16.885 -0.974  1.00 14.81 ?  146 THR   A HG23 1 
ATOM   3247 N  N    . VAL   A 1 147 ? 21.918 -16.560 2.437   1.00 11.48 ?  147 VAL   A N    1 
ATOM   3248 C  CA   . VAL   A 1 147 ? 22.408 -16.263 3.775   1.00 11.80 ?  147 VAL   A CA   1 
ATOM   3249 C  C    . VAL   A 1 147 ? 22.081 -17.428 4.693   1.00 11.90 ?  147 VAL   A C    1 
ATOM   3250 O  O    . VAL   A 1 147 ? 20.938 -17.902 4.737   1.00 12.95 ?  147 VAL   A O    1 
ATOM   3251 C  CB   . VAL   A 1 147 ? 21.790 -14.955 4.294   1.00 11.98 ?  147 VAL   A CB   1 
ATOM   3252 C  CG1  . VAL   A 1 147 ? 22.314 -14.639 5.672   1.00 12.89 ?  147 VAL   A CG1  1 
ATOM   3253 C  CG2  . VAL   A 1 147 ? 22.051 -13.809 3.328   1.00 12.29 ?  147 VAL   A CG2  1 
ATOM   3254 H  H    . VAL   A 1 147 ? 21.162 -16.188 2.252   1.00 13.77 ?  147 VAL   A H    1 
ATOM   3255 H  HA   . VAL   A 1 147 ? 23.371 -16.154 3.745   1.00 14.15 ?  147 VAL   A HA   1 
ATOM   3256 H  HB   . VAL   A 1 147 ? 20.832 -15.068 4.365   1.00 14.38 ?  147 VAL   A HB   1 
ATOM   3257 H  HG11 . VAL   A 1 147 ? 22.065 -13.734 5.906   1.00 15.47 ?  147 VAL   A HG11 1 
ATOM   3258 H  HG12 . VAL   A 1 147 ? 21.925 -15.263 6.309   1.00 15.47 ?  147 VAL   A HG12 1 
ATOM   3259 H  HG13 . VAL   A 1 147 ? 23.280 -14.729 5.673   1.00 15.47 ?  147 VAL   A HG13 1 
ATOM   3260 H  HG21 . VAL   A 1 147 ? 21.724 -12.983 3.720   1.00 14.75 ?  147 VAL   A HG21 1 
ATOM   3261 H  HG22 . VAL   A 1 147 ? 23.004 -13.742 3.163   1.00 14.75 ?  147 VAL   A HG22 1 
ATOM   3262 H  HG23 . VAL   A 1 147 ? 21.583 -13.986 2.496   1.00 14.75 ?  147 VAL   A HG23 1 
ATOM   3263 N  N    . ARG   A 1 148 ? 23.100 -17.904 5.410   1.00 12.33 ?  148 ARG   A N    1 
ATOM   3264 C  CA   . ARG   A 1 148 ? 22.964 -18.977 6.380   1.00 12.84 ?  148 ARG   A CA   1 
ATOM   3265 C  C    . ARG   A 1 148 ? 23.084 -18.497 7.814   1.00 12.91 ?  148 ARG   A C    1 
ATOM   3266 O  O    . ARG   A 1 148 ? 22.671 -19.217 8.729   1.00 14.40 ?  148 ARG   A O    1 
ATOM   3267 C  CB   . ARG   A 1 148 ? 24.007 -20.069 6.109   1.00 13.57 ?  148 ARG   A CB   1 
ATOM   3268 C  CG   . ARG   A 1 148 ? 23.837 -20.718 4.751   1.00 14.82 ?  148 ARG   A CG   1 
ATOM   3269 C  CD   . ARG   A 1 148 ? 24.927 -21.741 4.458   1.00 15.61 ?  148 ARG   A CD   1 
ATOM   3270 N  NE   . ARG   A 1 148 ? 26.265 -21.163 4.483   1.00 15.67 ?  148 ARG   A NE   1 
ATOM   3271 C  CZ   . ARG   A 1 148 ? 26.782 -20.437 3.500   1.00 15.00 ?  148 ARG   A CZ   1 
ATOM   3272 N  NH1  . ARG   A 1 148 ? 26.109 -20.205 2.385   1.00 15.21 ?  148 ARG   A NH1  1 
ATOM   3273 N  NH2  . ARG   A 1 148 ? 28.001 -19.918 3.645   1.00 15.19 ?  148 ARG   A NH2  1 
ATOM   3274 H  H    . ARG   A 1 148 ? 23.907 -17.606 5.337   1.00 14.80 ?  148 ARG   A H    1 
ATOM   3275 H  HA   . ARG   A 1 148 ? 22.092 -19.376 6.277   1.00 15.41 ?  148 ARG   A HA   1 
ATOM   3276 H  HB2  . ARG   A 1 148 ? 24.895 -19.687 6.144   1.00 16.28 ?  148 ARG   A HB2  1 
ATOM   3277 H  HB3  . ARG   A 1 148 ? 23.917 -20.768 6.777   1.00 16.28 ?  148 ARG   A HB3  1 
ATOM   3278 H  HG2  . ARG   A 1 148 ? 22.978 -21.167 4.718   1.00 17.79 ?  148 ARG   A HG2  1 
ATOM   3279 H  HG3  . ARG   A 1 148 ? 23.878 -20.029 4.066   1.00 17.79 ?  148 ARG   A HG3  1 
ATOM   3280 H  HD2  . ARG   A 1 148 ? 24.889 -22.440 5.129   1.00 18.73 ?  148 ARG   A HD2  1 
ATOM   3281 H  HD3  . ARG   A 1 148 ? 24.776 -22.121 3.576   1.00 18.73 ?  148 ARG   A HD3  1 
ATOM   3282 H  HE   . ARG   A 1 148 ? 26.745 -21.294 5.180   1.00 18.81 ?  148 ARG   A HE   1 
ATOM   3283 H  HH11 . ARG   A 1 148 ? 25.320 -20.525 2.277   1.00 18.25 ?  148 ARG   A HH11 1 
ATOM   3284 H  HH12 . ARG   A 1 148 ? 26.464 -19.726 1.760   1.00 18.25 ?  148 ARG   A HH12 1 
ATOM   3285 H  HH21 . ARG   A 1 148 ? 28.443 -20.054 4.369   1.00 18.23 ?  148 ARG   A HH21 1 
ATOM   3286 H  HH22 . ARG   A 1 148 ? 28.346 -19.440 3.016   1.00 18.23 ?  148 ARG   A HH22 1 
ATOM   3287 N  N    . THR   A 1 149 ? 23.629 -17.304 8.027   1.00 12.85 ?  149 THR   A N    1 
ATOM   3288 C  CA   . THR   A 1 149 ? 23.705 -16.707 9.347   1.00 13.02 ?  149 THR   A CA   1 
ATOM   3289 C  C    . THR   A 1 149 ? 22.380 -16.009 9.649   1.00 12.63 ?  149 THR   A C    1 
ATOM   3290 O  O    . THR   A 1 149 ? 21.450 -16.009 8.834   1.00 13.41 ?  149 THR   A O    1 
ATOM   3291 C  CB   . THR   A 1 149 ? 24.903 -15.771 9.404   1.00 13.51 ?  149 THR   A CB   1 
ATOM   3292 O  OG1  . THR   A 1 149 ? 24.778 -14.842 8.324   1.00 13.50 ?  149 THR   A OG1  1 
ATOM   3293 C  CG2  . THR   A 1 149 ? 26.221 -16.562 9.288   1.00 14.20 ?  149 THR   A CG2  1 
ATOM   3294 H  H    . THR   A 1 149 ? 23.975 -16.812 7.408   1.00 15.42 ?  149 THR   A H    1 
ATOM   3295 H  HA   . THR   A 1 149 ? 23.833 -17.408 10.003  1.00 15.62 ?  149 THR   A HA   1 
ATOM   3296 H  HB   . THR   A 1 149 ? 24.894 -15.291 10.243  1.00 16.21 ?  149 THR   A HB   1 
ATOM   3297 H  HG1  . THR   A 1 149 ? 25.429 -14.310 8.321   1.00 16.21 ?  149 THR   A HG1  1 
ATOM   3298 H  HG21 . THR   A 1 149 ? 26.979 -15.958 9.336   1.00 17.05 ?  149 THR   A HG21 1 
ATOM   3299 H  HG22 . THR   A 1 149 ? 26.290 -17.208 10.011  1.00 17.05 ?  149 THR   A HG22 1 
ATOM   3300 H  HG23 . THR   A 1 149 ? 26.257 -17.040 8.441   1.00 17.05 ?  149 THR   A HG23 1 
ATOM   3301 N  N    . ASN   A 1 150 ? 22.252 -15.467 10.854  1.00 13.04 ?  150 ASN   A N    1 
ATOM   3302 C  CA   . ASN   A 1 150 ? 20.969 -14.943 11.321  1.00 13.30 ?  150 ASN   A CA   1 
ATOM   3303 C  C    . ASN   A 1 150 ? 20.792 -13.507 10.855  1.00 12.53 ?  150 ASN   A C    1 
ATOM   3304 O  O    . ASN   A 1 150 ? 21.550 -12.617 11.257  1.00 13.65 ?  150 ASN   A O    1 
ATOM   3305 C  CB   . ASN   A 1 150 ? 20.893 -15.042 12.840  1.00 16.01 ?  150 ASN   A CB   1 
ATOM   3306 C  CG   . ASN   A 1 150 ? 20.806 -16.474 13.308  1.00 20.18 ?  150 ASN   A CG   1 
ATOM   3307 O  OD1  . ASN   A 1 150 ? 20.218 -17.315 12.629  1.00 21.28 ?  150 ASN   A OD1  1 
ATOM   3308 N  ND2  . ASN   A 1 150 ? 21.404 -16.769 14.460  1.00 22.46 ?  150 ASN   A ND2  1 
ATOM   3309 H  H    . ASN   A 1 150 ? 22.890 -15.392 11.425  1.00 15.65 ?  150 ASN   A H    1 
ATOM   3310 H  HA   . ASN   A 1 150 ? 20.247 -15.477 10.951  1.00 15.96 ?  150 ASN   A HA   1 
ATOM   3311 H  HB2  . ASN   A 1 150 ? 21.686 -14.648 13.231  1.00 19.21 ?  150 ASN   A HB2  1 
ATOM   3312 H  HB3  . ASN   A 1 150 ? 20.099 -14.582 13.156  1.00 19.21 ?  150 ASN   A HB3  1 
ATOM   3313 H  HD21 . ASN   A 1 150 ? 21.387 -17.575 14.771  1.00 26.95 ?  150 ASN   A HD21 1 
ATOM   3314 H  HD22 . ASN   A 1 150 ? 21.806 -16.152 14.908  1.00 26.95 ?  150 ASN   A HD22 1 
ATOM   3315 N  N    . VAL   A 1 151 ? 19.795 -13.280 10.011  1.00 11.94 ?  151 VAL   A N    1 
ATOM   3316 C  CA   . VAL   A 1 151 ? 19.586 -11.978 9.396   1.00 11.93 ?  151 VAL   A CA   1 
ATOM   3317 C  C    . VAL   A 1 151 ? 18.197 -11.466 9.751   1.00 11.77 ?  151 VAL   A C    1 
ATOM   3318 O  O    . VAL   A 1 151 ? 17.189 -12.175 9.597   1.00 13.36 ?  151 VAL   A O    1 
ATOM   3319 C  CB   . VAL   A 1 151 ? 19.878 -11.994 7.881   1.00 13.34 ?  151 VAL   A CB   1 
ATOM   3320 C  CG1  . VAL   A 1 151 ? 19.049 -13.026 7.154   1.00 14.65 ?  151 VAL   A CG1  1 
ATOM   3321 C  CG2  . VAL   A 1 151 ? 19.698 -10.596 7.282   1.00 13.54 ?  151 VAL   A CG2  1 
ATOM   3322 H  H    . VAL   A 1 151 ? 19.217 -13.871 9.777   1.00 14.33 ?  151 VAL   A H    1 
ATOM   3323 H  HA   . VAL   A 1 151 ? 20.226 -11.358 9.785   1.00 14.31 ?  151 VAL   A HA   1 
ATOM   3324 H  HB   . VAL   A 1 151 ? 20.812 -12.238 7.753   1.00 16.00 ?  151 VAL   A HB   1 
ATOM   3325 H  HG11 . VAL   A 1 151 ? 19.242 -12.987 6.204   1.00 17.58 ?  151 VAL   A HG11 1 
ATOM   3326 H  HG12 . VAL   A 1 151 ? 19.274 -13.912 7.494   1.00 17.58 ?  151 VAL   A HG12 1 
ATOM   3327 H  HG13 . VAL   A 1 151 ? 18.108 -12.848 7.308   1.00 17.58 ?  151 VAL   A HG13 1 
ATOM   3328 H  HG21 . VAL   A 1 151 ? 20.016 -10.606 6.361   1.00 16.25 ?  151 VAL   A HG21 1 
ATOM   3329 H  HG22 . VAL   A 1 151 ? 18.758 -10.363 7.300   1.00 16.25 ?  151 VAL   A HG22 1 
ATOM   3330 H  HG23 . VAL   A 1 151 ? 20.213 -9.961  7.799   1.00 16.25 ?  151 VAL   A HG23 1 
ATOM   3331 N  N    . TYR   A 1 152 ? 18.177 -10.218 10.227  1.00 11.81 ?  152 TYR   A N    1 
ATOM   3332 C  CA   . TYR   A 1 152 ? 16.983 -9.481  10.605  1.00 11.54 ?  152 TYR   A CA   1 
ATOM   3333 C  C    . TYR   A 1 152 ? 16.790 -8.388  9.563   1.00 11.09 ?  152 TYR   A C    1 
ATOM   3334 O  O    . TYR   A 1 152 ? 17.574 -7.433  9.502   1.00 11.49 ?  152 TYR   A O    1 
ATOM   3335 C  CB   . TYR   A 1 152 ? 17.161 -8.927  12.016  1.00 12.49 ?  152 TYR   A CB   1 
ATOM   3336 C  CG   . TYR   A 1 152 ? 17.114 -10.048 13.019  1.00 13.40 ?  152 TYR   A CG   1 
ATOM   3337 C  CD1  . TYR   A 1 152 ? 18.235 -10.824 13.285  1.00 14.84 ?  152 TYR   A CD1  1 
ATOM   3338 C  CD2  . TYR   A 1 152 ? 15.932 -10.373 13.662  1.00 13.87 ?  152 TYR   A CD2  1 
ATOM   3339 C  CE1  . TYR   A 1 152 ? 18.183 -11.879 14.176  1.00 16.43 ?  152 TYR   A CE1  1 
ATOM   3340 C  CE2  . TYR   A 1 152 ? 15.866 -11.437 14.555  1.00 15.69 ?  152 TYR   A CE2  1 
ATOM   3341 C  CZ   . TYR   A 1 152 ? 16.999 -12.182 14.809  1.00 16.31 ?  152 TYR   A CZ   1 
ATOM   3342 O  OH   . TYR   A 1 152 ? 16.948 -13.242 15.693  1.00 19.03 ?  152 TYR   A OH   1 
ATOM   3343 H  H    . TYR   A 1 152 ? 18.899 -9.747  10.335  1.00 14.17 ?  152 TYR   A H    1 
ATOM   3344 H  HA   . TYR   A 1 152 ? 16.218 -10.073 10.591  1.00 13.85 ?  152 TYR   A HA   1 
ATOM   3345 H  HB2  . TYR   A 1 152 ? 18.028 -8.496  12.085  1.00 14.99 ?  152 TYR   A HB2  1 
ATOM   3346 H  HB3  . TYR   A 1 152 ? 16.453 -8.303  12.213  1.00 14.99 ?  152 TYR   A HB3  1 
ATOM   3347 H  HD1  . TYR   A 1 152 ? 19.035 -10.629 12.852  1.00 17.81 ?  152 TYR   A HD1  1 
ATOM   3348 H  HD2  . TYR   A 1 152 ? 15.161 -9.873  13.484  1.00 16.65 ?  152 TYR   A HD2  1 
ATOM   3349 H  HE1  . TYR   A 1 152 ? 18.942 -12.384 14.346  1.00 19.72 ?  152 TYR   A HE1  1 
ATOM   3350 H  HE2  . TYR   A 1 152 ? 15.064 -11.635 14.985  1.00 18.83 ?  152 TYR   A HE2  1 
ATOM   3351 H  HH   . TYR   A 1 152 ? 16.173 -13.304 16.019  1.00 22.84 ?  152 TYR   A HH   1 
ATOM   3352 N  N    A LEU   A 1 153 ? 15.803 -8.597  8.688   0.58 10.96 ?  153 LEU   A N    1 
ATOM   3353 N  N    B LEU   A 1 153 ? 15.724 -8.496  8.778   0.42 11.01 ?  153 LEU   A N    1 
ATOM   3354 C  CA   A LEU   A 1 153 ? 15.537 -7.731  7.546   0.58 10.92 ?  153 LEU   A CA   1 
ATOM   3355 C  CA   B LEU   A 1 153 ? 15.470 -7.569  7.685   0.42 10.70 ?  153 LEU   A CA   1 
ATOM   3356 C  C    A LEU   A 1 153 ? 14.535 -6.655  7.934   0.58 10.92 ?  153 LEU   A C    1 
ATOM   3357 C  C    B LEU   A 1 153 ? 14.486 -6.490  8.115   0.42 11.09 ?  153 LEU   A C    1 
ATOM   3358 O  O    A LEU   A 1 153 ? 13.418 -6.961  8.370   0.58 11.85 ?  153 LEU   A O    1 
ATOM   3359 O  O    B LEU   A 1 153 ? 13.399 -6.790  8.622   0.42 11.75 ?  153 LEU   A O    1 
ATOM   3360 C  CB   A LEU   A 1 153 ? 14.964 -8.547  6.387   0.58 11.04 ?  153 LEU   A CB   1 
ATOM   3361 C  CB   B LEU   A 1 153 ? 14.924 -8.313  6.469   0.42 10.68 ?  153 LEU   A CB   1 
ATOM   3362 C  CG   A LEU   A 1 153 ? 15.908 -9.522  5.688   0.58 11.44 ?  153 LEU   A CG   1 
ATOM   3363 C  CG   B LEU   A 1 153 ? 15.866 -9.356  5.869   0.42 10.92 ?  153 LEU   A CG   1 
ATOM   3364 C  CD1  A LEU   A 1 153 ? 15.128 -10.431 4.751   0.58 11.70 ?  153 LEU   A CD1  1 
ATOM   3365 C  CD1  B LEU   A 1 153 ? 15.116 -10.196 4.854   0.42 11.50 ?  153 LEU   A CD1  1 
ATOM   3366 C  CD2  A LEU   A 1 153 ? 16.974 -8.763  4.923   0.58 11.49 ?  153 LEU   A CD2  1 
ATOM   3367 C  CD2  B LEU   A 1 153 ? 17.084 -8.700  5.233   0.42 11.49 ?  153 LEU   A CD2  1 
ATOM   3368 H  H    A LEU   A 1 153 ? 15.256 -9.264  8.742   0.58 13.16 ?  153 LEU   A H    1 
ATOM   3369 H  H    B LEU   A 1 153 ? 15.113 -9.100  8.870   0.42 13.22 ?  153 LEU   A H    1 
ATOM   3370 H  HA   A LEU   A 1 153 ? 16.358 -7.313  7.261   0.58 13.10 ?  153 LEU   A HA   1 
ATOM   3371 H  HA   B LEU   A 1 153 ? 16.299 -7.143  7.439   0.42 12.84 ?  153 LEU   A HA   1 
ATOM   3372 H  HB2  A LEU   A 1 153 ? 14.215 -9.069  6.720   0.58 13.25 ?  153 LEU   A HB2  1 
ATOM   3373 H  HB2  B LEU   A 1 153 ? 14.111 -8.770  6.731   0.42 12.82 ?  153 LEU   A HB2  1 
ATOM   3374 H  HB3  A LEU   A 1 153 ? 14.645 -7.931  5.711   0.58 13.25 ?  153 LEU   A HB3  1 
ATOM   3375 H  HB3  B LEU   A 1 153 ? 14.727 -7.664  5.779   0.42 12.82 ?  153 LEU   A HB3  1 
ATOM   3376 H  HG   A LEU   A 1 153 ? 16.347 -10.079 6.353   0.58 13.73 ?  153 LEU   A HG   1 
ATOM   3377 H  HG   B LEU   A 1 153 ? 16.179 -9.945  6.574   0.42 13.11 ?  153 LEU   A HG   1 
ATOM   3378 H  HD11 A LEU   A 1 153 ? 15.715 -11.126 4.418   0.58 14.04 ?  153 LEU   A HD11 1 
ATOM   3379 H  HD11 B LEU   A 1 153 ? 15.713 -10.872 4.500   0.42 13.80 ?  153 LEU   A HD11 1 
ATOM   3380 H  HD12 A LEU   A 1 153 ? 14.389 -10.826 5.236   0.58 14.04 ?  153 LEU   A HD12 1 
ATOM   3381 H  HD12 B LEU   A 1 153 ? 14.359 -10.615 5.291   0.42 13.80 ?  153 LEU   A HD12 1 
ATOM   3382 H  HD13 A LEU   A 1 153 ? 14.790 -9.901  4.010   0.58 14.04 ?  153 LEU   A HD13 1 
ATOM   3383 H  HD13 B LEU   A 1 153 ? 14.806 -9.618  4.137   0.42 13.80 ?  153 LEU   A HD13 1 
ATOM   3384 H  HD21 A LEU   A 1 153 ? 17.556 -9.396  4.482   0.58 13.79 ?  153 LEU   A HD21 1 
ATOM   3385 H  HD21 B LEU   A 1 153 ? 17.623 -9.384  4.807   0.42 13.79 ?  153 LEU   A HD21 1 
ATOM   3386 H  HD22 A LEU   A 1 153 ? 16.539 -8.196  4.269   0.58 13.79 ?  153 LEU   A HD22 1 
ATOM   3387 H  HD22 B LEU   A 1 153 ? 16.785 -8.054  4.574   0.42 13.79 ?  153 LEU   A HD22 1 
ATOM   3388 H  HD23 A LEU   A 1 153 ? 17.481 -8.224  5.548   0.58 13.79 ?  153 LEU   A HD23 1 
ATOM   3389 H  HD23 B LEU   A 1 153 ? 17.600 -8.254  5.924   0.42 13.79 ?  153 LEU   A HD23 1 
ATOM   3390 N  N    A ALA   A 1 154 ? 14.927 -5.403  7.740   0.58 10.99 ?  154 ALA   A N    1 
ATOM   3391 N  N    B ALA   A 1 154 ? 14.874 -5.236  7.897   0.42 10.84 ?  154 ALA   A N    1 
ATOM   3392 C  CA   A ALA   A 1 154 ? 14.065 -4.254  7.968   0.58 11.54 ?  154 ALA   A CA   1 
ATOM   3393 C  CA   B ALA   A 1 154 ? 14.020 -4.079  8.134   0.42 11.41 ?  154 ALA   A CA   1 
ATOM   3394 C  C    A ALA   A 1 154 ? 13.569 -3.750  6.622   0.58 11.35 ?  154 ALA   A C    1 
ATOM   3395 C  C    B ALA   A 1 154 ? 13.537 -3.581  6.776   0.42 11.03 ?  154 ALA   A C    1 
ATOM   3396 O  O    A ALA   A 1 154 ? 14.374 -3.421  5.746   0.58 11.49 ?  154 ALA   A O    1 
ATOM   3397 O  O    B ALA   A 1 154 ? 14.334 -3.099  5.966   0.42 11.04 ?  154 ALA   A O    1 
ATOM   3398 C  CB   A ALA   A 1 154 ? 14.833 -3.147  8.687   0.58 12.30 ?  154 ALA   A CB   1 
ATOM   3399 C  CB   B ALA   A 1 154 ? 14.798 -2.992  8.873   0.42 12.18 ?  154 ALA   A CB   1 
ATOM   3400 H  H    A ALA   A 1 154 ? 15.712 -5.193  7.452   0.58 13.19 ?  154 ALA   A H    1 
ATOM   3401 H  H    B ALA   A 1 154 ? 15.652 -5.021  7.592   0.42 13.01 ?  154 ALA   A H    1 
ATOM   3402 H  HA   A ALA   A 1 154 ? 13.304 -4.514  8.506   0.58 13.84 ?  154 ALA   A HA   1 
ATOM   3403 H  HA   B ALA   A 1 154 ? 13.252 -4.333  8.669   0.42 13.69 ?  154 ALA   A HA   1 
ATOM   3404 H  HB1  A ALA   A 1 154 ? 14.238 -2.394  8.827   0.58 14.76 ?  154 ALA   A HB1  1 
ATOM   3405 H  HB1  B ALA   A 1 154 ? 14.215 -2.231  9.026   0.42 14.62 ?  154 ALA   A HB1  1 
ATOM   3406 H  HB2  A ALA   A 1 154 ? 15.147 -3.485  9.538   0.58 14.76 ?  154 ALA   A HB2  1 
ATOM   3407 H  HB2  B ALA   A 1 154 ? 15.108 -3.347  9.722   0.42 14.62 ?  154 ALA   A HB2  1 
ATOM   3408 H  HB3  A ALA   A 1 154 ? 15.585 -2.876  8.137   0.58 14.76 ?  154 ALA   A HB3  1 
ATOM   3409 H  HB3  B ALA   A 1 154 ? 15.557 -2.723  8.332   0.42 14.62 ?  154 ALA   A HB3  1 
ATOM   3410 N  N    A VAL   A 1 155 ? 12.249 -3.689  6.466   0.28 10.57 ?  155 VAL   A N    1 
ATOM   3411 N  N    B VAL   A 1 155 ? 12.237 -3.712  6.530   0.42 9.93  ?  155 VAL   A N    1 
ATOM   3412 C  CA   A VAL   A 1 155 ? 11.601 -3.218  5.247   0.28 11.94 ?  155 VAL   A CA   1 
ATOM   3413 C  CA   B VAL   A 1 155 ? 11.597 -3.267  5.298   0.42 11.42 ?  155 VAL   A CA   1 
ATOM   3414 C  CA   T VAL   A 1 155 ? 11.592 -3.270  5.234   0.30 14.39 ?  155 VAL   A CA   1 
ATOM   3415 C  C    A VAL   A 1 155 ? 10.864 -1.930  5.587   0.28 12.92 ?  155 VAL   A C    1 
ATOM   3416 C  C    B VAL   A 1 155 ? 10.947 -1.917  5.580   0.42 12.44 ?  155 VAL   A C    1 
ATOM   3417 C  C    T VAL   A 1 155 ? 10.926 -1.925  5.529   0.30 14.40 ?  155 VAL   A C    1 
ATOM   3418 O  O    A VAL   A 1 155 ? 9.859  -1.955  6.309   0.28 13.01 ?  155 VAL   A O    1 
ATOM   3419 O  O    B VAL   A 1 155 ? 10.100 -1.808  6.476   0.42 12.64 ?  155 VAL   A O    1 
ATOM   3420 O  O    T VAL   A 1 155 ? 10.016 -1.840  6.354   0.30 14.66 ?  155 VAL   A O    1 
ATOM   3421 C  CB   A VAL   A 1 155 ? 10.643 -4.273  4.680   0.28 12.09 ?  155 VAL   A CB   1 
ATOM   3422 C  CB   B VAL   A 1 155 ? 10.566 -4.301  4.812   0.42 11.53 ?  155 VAL   A CB   1 
ATOM   3423 C  CB   T VAL   A 1 155 ? 10.593 -4.324  4.719   0.30 14.21 ?  155 VAL   A CB   1 
ATOM   3424 C  CG1  A VAL   A 1 155 ? 9.942  -3.738  3.447   0.28 12.65 ?  155 VAL   A CG1  1 
ATOM   3425 C  CG1  B VAL   A 1 155 ? 9.845  -3.809  3.568   0.42 12.33 ?  155 VAL   A CG1  1 
ATOM   3426 C  CG1  T VAL   A 1 155 ? 9.850  -3.803  3.503   0.30 14.52 ?  155 VAL   A CG1  1 
ATOM   3427 C  CG2  A VAL   A 1 155 ? 11.399 -5.553  4.363   0.28 12.53 ?  155 VAL   A CG2  1 
ATOM   3428 C  CG2  B VAL   A 1 155 ? 11.242 -5.641  4.545   0.42 12.14 ?  155 VAL   A CG2  1 
ATOM   3429 C  CG2  T VAL   A 1 155 ? 11.314 -5.626  4.387   0.30 14.53 ?  155 VAL   A CG2  1 
ATOM   3430 H  H    A VAL   A 1 155 ? 11.690 -3.932  7.074   0.28 12.69 ?  155 VAL   A H    1 
ATOM   3431 H  H    B VAL   A 1 155 ? 11.683 -4.067  7.084   0.42 11.91 ?  155 VAL   A H    1 
ATOM   3432 H  HA   A VAL   A 1 155 ? 12.272 -3.018  4.579   0.28 14.33 ?  155 VAL   A HA   1 
ATOM   3433 H  HA   B VAL   A 1 155 ? 12.264 -3.151  4.604   0.42 13.70 ?  155 VAL   A HA   1 
ATOM   3434 H  HB   A VAL   A 1 155 ? 9.966  -4.476  5.348   0.28 14.50 ?  155 VAL   A HB   1 
ATOM   3435 H  HB   B VAL   A 1 155 ? 9.903  -4.440  5.510   0.42 13.83 ?  155 VAL   A HB   1 
ATOM   3436 H  HB   T VAL   A 1 155 ? 9.946  -4.508  5.417   0.30 17.06 ?  155 VAL   A HB   1 
ATOM   3437 H  HG11 A VAL   A 1 155 ? 9.488  -4.471  3.005   0.28 15.18 ?  155 VAL   A HG11 1 
ATOM   3438 H  HG11 B VAL   A 1 155 ? 9.333  -4.542  3.189   0.42 14.79 ?  155 VAL   A HG11 1 
ATOM   3439 H  HG11 T VAL   A 1 155 ? 9.353  -4.533  3.103   0.30 17.42 ?  155 VAL   A HG11 1 
ATOM   3440 H  HG12 A VAL   A 1 155 ? 9.298  -3.063  3.714   0.28 15.18 ?  155 VAL   A HG12 1 
ATOM   3441 H  HG12 B VAL   A 1 155 ? 9.248  -3.085  3.813   0.42 14.79 ?  155 VAL   A HG12 1 
ATOM   3442 H  HG12 T VAL   A 1 155 ? 9.242  -3.101  3.781   0.30 17.42 ?  155 VAL   A HG12 1 
ATOM   3443 H  HG13 A VAL   A 1 155 ? 10.603 -3.351  2.854   0.28 15.18 ?  155 VAL   A HG13 1 
ATOM   3444 H  HG13 B VAL   A 1 155 ? 10.501 -3.498  2.927   0.42 14.79 ?  155 VAL   A HG13 1 
ATOM   3445 H  HG13 T VAL   A 1 155 ? 10.494 -3.453  2.867   0.30 17.42 ?  155 VAL   A HG13 1 
ATOM   3446 H  HG21 A VAL   A 1 155 ? 10.788 -6.186  3.958   0.28 15.04 ?  155 VAL   A HG21 1 
ATOM   3447 H  HG21 B VAL   A 1 155 ? 10.619 -6.222  4.082   0.42 14.57 ?  155 VAL   A HG21 1 
ATOM   3448 H  HG21 T VAL   A 1 155 ? 10.664 -6.275  4.072   0.30 17.43 ?  155 VAL   A HG21 1 
ATOM   3449 H  HG22 A VAL   A 1 155 ? 12.120 -5.347  3.749   0.28 15.04 ?  155 VAL   A HG22 1 
ATOM   3450 H  HG22 B VAL   A 1 155 ? 12.026 -5.491  3.992   0.42 14.57 ?  155 VAL   A HG22 1 
ATOM   3451 H  HG22 T VAL   A 1 155 ? 11.972 -5.455  3.694   0.30 17.43 ?  155 VAL   A HG22 1 
ATOM   3452 H  HG23 A VAL   A 1 155 ? 11.760 -5.920  5.186   0.28 15.04 ?  155 VAL   A HG23 1 
ATOM   3453 H  HG23 B VAL   A 1 155 ? 11.506 -6.039  5.389   0.42 14.57 ?  155 VAL   A HG23 1 
ATOM   3454 H  HG23 T VAL   A 1 155 ? 11.753 -5.959  5.185   0.30 17.43 ?  155 VAL   A HG23 1 
ATOM   3455 N  N    A PHE   A 1 156 ? 11.352 -0.803  5.053   0.28 13.78 ?  156 PHE   A N    1 
ATOM   3456 N  N    B PHE   A 1 156 ? 11.352 -0.887  4.827   0.42 13.25 ?  156 PHE   A N    1 
ATOM   3457 N  N    T PHE   A 1 156 ? 11.396 -0.881  4.837   0.30 14.34 ?  156 PHE   A N    1 
ATOM   3458 C  CA   A PHE   A 1 156 ? 10.794 0.502   5.410   0.28 14.93 ?  156 PHE   A CA   1 
ATOM   3459 C  CA   B PHE   A 1 156 ? 10.897 0.479   5.104   0.42 14.28 ?  156 PHE   A CA   1 
ATOM   3460 C  CA   T PHE   A 1 156 ? 10.949 0.485   5.112   0.30 14.60 ?  156 PHE   A CA   1 
ATOM   3461 C  C    A PHE   A 1 156 ? 9.333  0.631   4.989   0.28 15.22 ?  156 PHE   A C    1 
ATOM   3462 C  C    B PHE   A 1 156 ? 9.412  0.659   4.798   0.42 15.27 ?  156 PHE   A C    1 
ATOM   3463 C  C    T PHE   A 1 156 ? 9.492  0.694   4.715   0.30 15.12 ?  156 PHE   A C    1 
ATOM   3464 O  O    A PHE   A 1 156 ? 8.499  1.120   5.763   0.28 15.34 ?  156 PHE   A O    1 
ATOM   3465 O  O    B PHE   A 1 156 ? 8.681  1.271   5.588   0.42 15.99 ?  156 PHE   A O    1 
ATOM   3466 O  O    T PHE   A 1 156 ? 8.726  1.329   5.450   0.30 15.84 ?  156 PHE   A O    1 
ATOM   3467 C  CB   A PHE   A 1 156 ? 11.641 1.617   4.787   0.28 15.64 ?  156 PHE   A CB   1 
ATOM   3468 C  CB   B PHE   A 1 156 ? 11.742 1.469   4.291   0.42 13.96 ?  156 PHE   A CB   1 
ATOM   3469 C  CB   T PHE   A 1 156 ? 11.859 1.460   4.359   0.30 14.06 ?  156 PHE   A CB   1 
ATOM   3470 C  CG   A PHE   A 1 156 ? 11.146 3.007   5.100   0.28 16.61 ?  156 PHE   A CG   1 
ATOM   3471 C  CG   B PHE   A 1 156 ? 11.462 2.933   4.593   0.42 14.41 ?  156 PHE   A CG   1 
ATOM   3472 C  CG   T PHE   A 1 156 ? 11.509 2.920   4.548   0.30 13.94 ?  156 PHE   A CG   1 
ATOM   3473 C  CD1  A PHE   A 1 156 ? 11.076 3.449   6.410   0.28 17.07 ?  156 PHE   A CD1  1 
ATOM   3474 C  CD1  B PHE   A 1 156 ? 10.462 3.623   3.922   0.42 15.53 ?  156 PHE   A CD1  1 
ATOM   3475 C  CD1  T PHE   A 1 156 ? 11.893 3.597   5.697   0.30 14.47 ?  156 PHE   A CD1  1 
ATOM   3476 C  CD2  A PHE   A 1 156 ? 10.764 3.874   4.085   0.28 17.19 ?  156 PHE   A CD2  1 
ATOM   3477 C  CD2  B PHE   A 1 156 ? 12.227 3.621   5.529   0.42 14.96 ?  156 PHE   A CD2  1 
ATOM   3478 C  CD2  T PHE   A 1 156 ? 10.837 3.620   3.557   0.30 14.29 ?  156 PHE   A CD2  1 
ATOM   3479 C  CE1  A PHE   A 1 156 ? 10.625 4.723   6.705   0.28 17.42 ?  156 PHE   A CE1  1 
ATOM   3480 C  CE1  B PHE   A 1 156 ? 10.214 4.965   4.195   0.42 16.30 ?  156 PHE   A CE1  1 
ATOM   3481 C  CE1  T PHE   A 1 156 ? 11.589 4.937   5.866   0.30 15.12 ?  156 PHE   A CE1  1 
ATOM   3482 C  CE2  A PHE   A 1 156 ? 10.311 5.152   4.375   0.28 17.72 ?  156 PHE   A CE2  1 
ATOM   3483 C  CE2  B PHE   A 1 156 ? 11.988 4.964   5.803   0.42 15.46 ?  156 PHE   A CE2  1 
ATOM   3484 C  CE2  T PHE   A 1 156 ? 10.532 4.962   3.719   0.30 14.80 ?  156 PHE   A CE2  1 
ATOM   3485 C  CZ   A PHE   A 1 156 ? 10.245 5.577   5.686   0.28 17.73 ?  156 PHE   A CZ   1 
ATOM   3486 C  CZ   B PHE   A 1 156 ? 10.985 5.635   5.135   0.42 15.97 ?  156 PHE   A CZ   1 
ATOM   3487 C  CZ   T PHE   A 1 156 ? 10.908 5.620   4.877   0.30 15.14 ?  156 PHE   A CZ   1 
ATOM   3488 H  H    A PHE   A 1 156 ? 12.001 -0.770  4.488   0.28 16.54 ?  156 PHE   A H    1 
ATOM   3489 H  H    B PHE   A 1 156 ? 11.890 -0.957  4.159   0.42 15.89 ?  156 PHE   A H    1 
ATOM   3490 H  H    T PHE   A 1 156 ? 11.975 -0.942  4.205   0.30 17.21 ?  156 PHE   A H    1 
ATOM   3491 H  HA   A PHE   A 1 156 ? 10.835 0.611   6.370   0.28 17.91 ?  156 PHE   A HA   1 
ATOM   3492 H  HA   B PHE   A 1 156 ? 11.041 0.668   6.043   0.42 17.13 ?  156 PHE   A HA   1 
ATOM   3493 H  HA   T PHE   A 1 156 ? 11.033 0.663   6.061   0.30 17.52 ?  156 PHE   A HA   1 
ATOM   3494 H  HB2  A PHE   A 1 156 ? 12.552 1.548   5.123   0.28 18.77 ?  156 PHE   A HB2  1 
ATOM   3495 H  HB2  B PHE   A 1 156 ? 12.682 1.304   4.478   0.42 16.75 ?  156 PHE   A HB2  1 
ATOM   3496 H  HB2  T PHE   A 1 156 ? 12.771 1.330   4.667   0.30 16.87 ?  156 PHE   A HB2  1 
ATOM   3497 H  HB3  A PHE   A 1 156 ? 11.642 1.516   3.823   0.28 18.77 ?  156 PHE   A HB3  1 
ATOM   3498 H  HB3  B PHE   A 1 156 ? 11.572 1.322   3.347   0.42 16.75 ?  156 PHE   A HB3  1 
ATOM   3499 H  HB3  T PHE   A 1 156 ? 11.805 1.263   3.411   0.30 16.87 ?  156 PHE   A HB3  1 
ATOM   3500 H  HD1  A PHE   A 1 156 ? 11.332 2.882   7.100   0.28 20.48 ?  156 PHE   A HD1  1 
ATOM   3501 H  HD1  B PHE   A 1 156 ? 9.947  3.179   3.288   0.42 18.64 ?  156 PHE   A HD1  1 
ATOM   3502 H  HD1  T PHE   A 1 156 ? 12.351 3.138   6.369   0.30 17.36 ?  156 PHE   A HD1  1 
ATOM   3503 H  HD2  A PHE   A 1 156 ? 10.811 3.593   3.200   0.28 20.62 ?  156 PHE   A HD2  1 
ATOM   3504 H  HD2  B PHE   A 1 156 ? 12.906 3.170   5.984   0.42 17.95 ?  156 PHE   A HD2  1 
ATOM   3505 H  HD2  T PHE   A 1 156 ? 10.581 3.178   2.782   0.30 17.15 ?  156 PHE   A HD2  1 
ATOM   3506 H  HE1  A PHE   A 1 156 ? 10.581 5.008   7.592   0.28 20.91 ?  156 PHE   A HE1  1 
ATOM   3507 H  HE1  B PHE   A 1 156 ? 9.542  5.415   3.741   0.42 19.56 ?  156 PHE   A HE1  1 
ATOM   3508 H  HE1  T PHE   A 1 156 ? 11.844 5.376   6.646   0.30 18.14 ?  156 PHE   A HE1  1 
ATOM   3509 H  HE2  A PHE   A 1 156 ? 10.058 5.723   3.686   0.28 21.26 ?  156 PHE   A HE2  1 
ATOM   3510 H  HE2  B PHE   A 1 156 ? 12.504 5.406   6.439   0.42 18.55 ?  156 PHE   A HE2  1 
ATOM   3511 H  HE2  T PHE   A 1 156 ? 10.071 5.415   3.056   0.30 17.76 ?  156 PHE   A HE2  1 
ATOM   3512 H  HZ   A PHE   A 1 156 ? 9.941  6.435   5.886   0.28 21.27 ?  156 PHE   A HZ   1 
ATOM   3513 H  HZ   B PHE   A 1 156 ? 10.821 6.532   5.319   0.42 19.16 ?  156 PHE   A HZ   1 
ATOM   3514 H  HZ   T PHE   A 1 156 ? 10.702 6.517   4.991   0.30 18.16 ?  156 PHE   A HZ   1 
ATOM   3515 N  N    A ASP   A 1 157 ? 9.004  0.204   3.773   0.28 15.80 ?  157 ASP   A N    1 
ATOM   3516 N  N    B ASP   A 1 157 ? 8.950  0.141   3.664   0.42 16.20 ?  157 ASP   A N    1 
ATOM   3517 N  N    T ASP   A 1 157 ? 9.095  0.180   3.556   0.30 15.22 ?  157 ASP   A N    1 
ATOM   3518 C  CA   A ASP   A 1 157 ? 7.680  0.442   3.208   0.28 16.65 ?  157 ASP   A CA   1 
ATOM   3519 C  CA   B ASP   A 1 157 ? 7.614  0.437   3.160   0.42 17.23 ?  157 ASP   A CA   1 
ATOM   3520 C  CA   T ASP   A 1 157 ? 7.781  0.448   2.987   0.30 15.93 ?  157 ASP   A CA   1 
ATOM   3521 C  C    A ASP   A 1 157 ? 6.690  -0.595  3.732   0.28 17.45 ?  157 ASP   A C    1 
ATOM   3522 C  C    B ASP   A 1 157 ? 6.616  -0.633  3.590   0.42 17.22 ?  157 ASP   A C    1 
ATOM   3523 C  C    T ASP   A 1 157 ? 6.758  -0.527  3.561   0.30 16.56 ?  157 ASP   A C    1 
ATOM   3524 O  O    A ASP   A 1 157 ? 6.842  -1.793  3.470   0.28 17.29 ?  157 ASP   A O    1 
ATOM   3525 O  O    B ASP   A 1 157 ? 6.881  -1.832  3.462   0.42 16.86 ?  157 ASP   A O    1 
ATOM   3526 O  O    T ASP   A 1 157 ? 6.849  -1.736  3.324   0.30 16.14 ?  157 ASP   A O    1 
ATOM   3527 C  CB   A ASP   A 1 157 ? 7.763  0.380   1.685   0.28 16.95 ?  157 ASP   A CB   1 
ATOM   3528 C  CB   B ASP   A 1 157 ? 7.638  0.556   1.637   0.42 18.57 ?  157 ASP   A CB   1 
ATOM   3529 C  CB   T ASP   A 1 157 ? 7.862  0.298   1.471   0.30 16.12 ?  157 ASP   A CB   1 
ATOM   3530 C  CG   A ASP   A 1 157 ? 6.525  0.921   1.010   0.28 17.79 ?  157 ASP   A CG   1 
ATOM   3531 C  CG   B ASP   A 1 157 ? 6.270  0.855   1.055   0.42 20.51 ?  157 ASP   A CG   1 
ATOM   3532 C  CG   T ASP   A 1 157 ? 6.682  0.914   0.764   0.30 16.51 ?  157 ASP   A CG   1 
ATOM   3533 O  OD1  A ASP   A 1 157 ? 6.262  2.135   1.134   0.28 18.65 ?  157 ASP   A OD1  1 
ATOM   3534 O  OD1  B ASP   A 1 157 ? 5.476  -0.090  0.869   0.42 21.03 ?  157 ASP   A OD1  1 
ATOM   3535 O  OD1  T ASP   A 1 157 ? 5.586  0.316   0.804   0.30 16.93 ?  157 ASP   A OD1  1 
ATOM   3536 O  OD2  A ASP   A 1 157 ? 5.815  0.131   0.351   0.28 17.58 -1 157 ASP   A OD2  1 
ATOM   3537 O  OD2  B ASP   A 1 157 ? 5.976  2.039   0.801   0.42 21.47 -1 157 ASP   A OD2  1 
ATOM   3538 O  OD2  T ASP   A 1 157 ? 6.843  2.005   0.182   0.30 16.20 -1 157 ASP   A OD2  1 
ATOM   3539 H  H    A ASP   A 1 157 ? 9.534  -0.233  3.252   0.28 18.96 ?  157 ASP   A H    1 
ATOM   3540 H  H    B ASP   A 1 157 ? 9.397  -0.400  3.170   0.42 19.43 ?  157 ASP   A H    1 
ATOM   3541 H  H    T ASP   A 1 157 ? 9.583  -0.336  3.064   0.30 18.27 ?  157 ASP   A H    1 
ATOM   3542 H  HA   A ASP   A 1 157 ? 7.371  1.324   3.464   0.28 19.98 ?  157 ASP   A HA   1 
ATOM   3543 H  HA   B ASP   A 1 157 ? 7.320  1.283   3.527   0.42 20.68 ?  157 ASP   A HA   1 
ATOM   3544 H  HA   T ASP   A 1 157 ? 7.510  1.357   3.199   0.30 19.11 ?  157 ASP   A HA   1 
ATOM   3545 H  HB2  A ASP   A 1 157 ? 8.525  0.899   1.388   0.28 20.34 ?  157 ASP   A HB2  1 
ATOM   3546 H  HB2  B ASP   A 1 157 ? 8.250  1.269   1.388   0.42 22.28 ?  157 ASP   A HB2  1 
ATOM   3547 H  HB2  T ASP   A 1 157 ? 8.678  0.715   1.156   0.30 19.34 ?  157 ASP   A HB2  1 
ATOM   3548 H  HB3  A ASP   A 1 157 ? 7.866  -0.542  1.410   0.28 20.34 ?  157 ASP   A HB3  1 
ATOM   3549 H  HB3  B ASP   A 1 157 ? 7.930  -0.283  1.256   0.42 22.28 ?  157 ASP   A HB3  1 
ATOM   3550 H  HB3  T ASP   A 1 157 ? 7.876  -0.647  1.253   0.30 19.34 ?  157 ASP   A HB3  1 
ATOM   3551 N  N    A LYS   A 1 158 ? 5.665  -0.135  4.459   0.28 18.69 ?  158 LYS   A N    1 
ATOM   3552 N  N    B LYS   A 1 158 ? 5.453  -0.186  4.071   0.42 18.43 ?  158 LYS   A N    1 
ATOM   3553 N  N    T LYS   A 1 158 ? 5.772  -0.001  4.296   0.30 18.26 ?  158 LYS   A N    1 
ATOM   3554 C  CA   A LYS   A 1 158 ? 4.688  -1.061  5.030   0.28 19.77 ?  158 LYS   A CA   1 
ATOM   3555 C  CA   B LYS   A 1 158 ? 4.479  -1.096  4.671   0.42 19.40 ?  158 LYS   A CA   1 
ATOM   3556 C  CA   T LYS   A 1 158 ? 4.781  -0.873  4.923   0.30 19.69 ?  158 LYS   A CA   1 
ATOM   3557 C  C    A LYS   A 1 158 ? 3.934  -1.813  3.940   0.28 19.63 ?  158 LYS   A C    1 
ATOM   3558 C  C    B LYS   A 1 158 ? 3.803  -1.967  3.615   0.42 18.74 ?  158 LYS   A C    1 
ATOM   3559 C  C    T LYS   A 1 158 ? 4.002  -1.666  3.881   0.30 19.51 ?  158 LYS   A C    1 
ATOM   3560 O  O    A LYS   A 1 158 ? 3.698  -3.021  4.059   0.28 19.81 ?  158 LYS   A O    1 
ATOM   3561 O  O    B LYS   A 1 158 ? 3.674  -3.184  3.789   0.42 18.24 ?  158 LYS   A O    1 
ATOM   3562 O  O    T LYS   A 1 158 ? 3.729  -2.856  4.073   0.30 19.57 ?  158 LYS   A O    1 
ATOM   3563 C  CB   A LYS   A 1 158 ? 3.714  -0.313  5.944   0.28 20.90 ?  158 LYS   A CB   1 
ATOM   3564 C  CB   B LYS   A 1 158 ? 3.451  -0.284  5.464   0.42 21.52 ?  158 LYS   A CB   1 
ATOM   3565 C  CB   T LYS   A 1 158 ? 3.829  -0.065  5.807   0.30 21.52 ?  158 LYS   A CB   1 
ATOM   3566 C  CG   A LYS   A 1 158 ? 2.484  -1.121  6.376   0.28 22.06 ?  158 LYS   A CG   1 
ATOM   3567 C  CG   B LYS   A 1 158 ? 2.234  -1.063  5.949   0.42 23.79 ?  158 LYS   A CG   1 
ATOM   3568 C  CG   T LYS   A 1 158 ? 2.606  -0.848  6.289   0.30 23.23 ?  158 LYS   A CG   1 
ATOM   3569 C  CD   A LYS   A 1 158 ? 2.847  -2.382  7.158   0.28 22.97 ?  158 LYS   A CD   1 
ATOM   3570 C  CD   B LYS   A 1 158 ? 2.589  -2.103  7.003   0.42 25.66 ?  158 LYS   A CD   1 
ATOM   3571 C  CD   T LYS   A 1 158 ? 2.993  -2.066  7.125   0.30 24.73 ?  158 LYS   A CD   1 
ATOM   3572 C  CE   A LYS   A 1 158 ? 1.598  -3.067  7.704   0.28 23.34 ?  158 LYS   A CE   1 
ATOM   3573 C  CE   B LYS   A 1 158 ? 1.345  -2.852  7.468   0.42 26.66 ?  158 LYS   A CE   1 
ATOM   3574 C  CE   T LYS   A 1 158 ? 1.762  -2.872  7.529   0.30 25.66 ?  158 LYS   A CE   1 
ATOM   3575 N  NZ   A LYS   A 1 158 ? 1.883  -4.397  8.315   0.28 23.39 ?  158 LYS   A NZ   1 
ATOM   3576 N  NZ   B LYS   A 1 158 ? 1.657  -3.950  8.424   0.42 26.98 ?  158 LYS   A NZ   1 
ATOM   3577 N  NZ   T LYS   A 1 158 ? 2.104  -4.092  8.317   0.30 26.10 ?  158 LYS   A NZ   1 
ATOM   3578 H  H    A LYS   A 1 158 ? 5.518  0.695   4.629   0.28 22.43 ?  158 LYS   A H    1 
ATOM   3579 H  H    B LYS   A 1 158 ? 5.205  0.635   4.059   0.42 22.11 ?  158 LYS   A H    1 
ATOM   3580 H  H    T LYS   A 1 158 ? 5.655  0.840   4.441   0.30 21.91 ?  158 LYS   A H    1 
ATOM   3581 H  HA   A LYS   A 1 158 ? 5.156  -1.714  5.570   0.28 23.72 ?  158 LYS   A HA   1 
ATOM   3582 H  HA   B LYS   A 1 158 ? 4.935  -1.683  5.295   0.42 23.28 ?  158 LYS   A HA   1 
ATOM   3583 H  HA   T LYS   A 1 158 ? 5.243  -1.506  5.494   0.30 23.63 ?  158 LYS   A HA   1 
ATOM   3584 H  HB2  A LYS   A 1 158 ? 4.184  -0.045  6.749   0.28 25.08 ?  158 LYS   A HB2  1 
ATOM   3585 H  HB2  B LYS   A 1 158 ? 3.890  0.085   6.251   0.42 25.82 ?  158 LYS   A HB2  1 
ATOM   3586 H  HB2  T LYS   A 1 158 ? 4.311  0.236   6.595   0.30 25.82 ?  158 LYS   A HB2  1 
ATOM   3587 H  HB3  A LYS   A 1 158 ? 3.395  0.475   5.478   0.28 25.08 ?  158 LYS   A HB3  1 
ATOM   3588 H  HB3  B LYS   A 1 158 ? 3.130  0.440   4.906   0.42 25.82 ?  158 LYS   A HB3  1 
ATOM   3589 H  HB3  T LYS   A 1 158 ? 3.508  0.701   5.308   0.30 25.82 ?  158 LYS   A HB3  1 
ATOM   3590 H  HG2  A LYS   A 1 158 ? 1.933  -0.566  6.949   0.28 26.47 ?  158 LYS   A HG2  1 
ATOM   3591 H  HG2  B LYS   A 1 158 ? 1.607  -0.441  6.349   0.42 28.55 ?  158 LYS   A HG2  1 
ATOM   3592 H  HG2  T LYS   A 1 158 ? 2.062  -0.270  6.844   0.30 27.87 ?  158 LYS   A HG2  1 
ATOM   3593 H  HG3  A LYS   A 1 158 ? 1.974  -1.385  5.592   0.28 26.47 ?  158 LYS   A HG3  1 
ATOM   3594 H  HG3  B LYS   A 1 158 ? 1.813  -1.517  5.204   0.42 28.55 ?  158 LYS   A HG3  1 
ATOM   3595 H  HG3  T LYS   A 1 158 ? 2.085  -1.153  5.528   0.30 27.87 ?  158 LYS   A HG3  1 
ATOM   3596 H  HD2  A LYS   A 1 158 ? 3.305  -3.004  6.573   0.28 27.57 ?  158 LYS   A HD2  1 
ATOM   3597 H  HD2  B LYS   A 1 158 ? 3.212  -2.744  6.626   0.42 30.80 ?  158 LYS   A HD2  1 
ATOM   3598 H  HD2  T LYS   A 1 158 ? 3.574  -2.644  6.608   0.30 29.67 ?  158 LYS   A HD2  1 
ATOM   3599 H  HD3  A LYS   A 1 158 ? 3.414  -2.142  7.907   0.28 27.57 ?  158 LYS   A HD3  1 
ATOM   3600 H  HD3  B LYS   A 1 158 ? 2.986  -1.659  7.771   0.42 30.80 ?  158 LYS   A HD3  1 
ATOM   3601 H  HD3  T LYS   A 1 158 ? 3.441  -1.771  7.933   0.30 29.67 ?  158 LYS   A HD3  1 
ATOM   3602 H  HE2  A LYS   A 1 158 ? 1.197  -2.501  8.384   0.28 28.01 ?  158 LYS   A HE2  1 
ATOM   3603 H  HE2  B LYS   A 1 158 ? 0.749  -2.227  7.910   0.42 31.99 ?  158 LYS   A HE2  1 
ATOM   3604 H  HE2  T LYS   A 1 158 ? 1.179  -2.317  8.071   0.30 30.80 ?  158 LYS   A HE2  1 
ATOM   3605 H  HE3  A LYS   A 1 158 ? 0.971  -3.200  6.978   0.28 28.01 ?  158 LYS   A HE3  1 
ATOM   3606 H  HE3  B LYS   A 1 158 ? 0.906  -3.240  6.695   0.42 31.99 ?  158 LYS   A HE3  1 
ATOM   3607 H  HE3  T LYS   A 1 158 ? 1.294  -3.157  6.728   0.30 30.80 ?  158 LYS   A HE3  1 
ATOM   3608 H  HZ1  A LYS   A 1 158 ? 1.130  -4.759  8.621   0.28 28.07 ?  158 LYS   A HZ1  1 
ATOM   3609 H  HZ1  B LYS   A 1 158 ? 0.908  -4.361  8.670   0.42 32.38 ?  158 LYS   A HZ1  1 
ATOM   3610 H  HZ1  T LYS   A 1 158 ? 1.361  -4.533  8.533   0.30 31.32 ?  158 LYS   A HZ1  1 
ATOM   3611 H  HZ2  A LYS   A 1 158 ? 2.238  -4.940  7.706   0.28 28.07 ?  158 LYS   A HZ2  1 
ATOM   3612 H  HZ2  B LYS   A 1 158 ? 2.200  -4.542  8.040   0.42 32.38 ?  158 LYS   A HZ2  1 
ATOM   3613 H  HZ2  T LYS   A 1 158 ? 2.628  -4.626  7.836   0.30 31.32 ?  158 LYS   A HZ2  1 
ATOM   3614 H  HZ3  A LYS   A 1 158 ? 2.455  -4.306  8.991   0.28 28.07 ?  158 LYS   A HZ3  1 
ATOM   3615 H  HZ3  B LYS   A 1 158 ? 2.057  -3.619  9.147   0.42 32.38 ?  158 LYS   A HZ3  1 
ATOM   3616 H  HZ3  T LYS   A 1 158 ? 2.530  -3.862  9.063   0.30 31.32 ?  158 LYS   A HZ3  1 
ATOM   3617 N  N    A ASN   A 1 159 ? 3.534  -1.116  2.876   0.28 19.23 ?  159 ASN   A N    1 
ATOM   3618 N  N    B ASN   A 1 159 ? 3.351  -1.362  2.516   0.42 19.15 ?  159 ASN   A N    1 
ATOM   3619 N  N    T ASN   A 1 159 ? 3.618  -1.025  2.784   0.30 19.35 ?  159 ASN   A N    1 
ATOM   3620 C  CA   A ASN   A 1 159 ? 2.842  -1.794  1.785   0.28 18.70 ?  159 ASN   A CA   1 
ATOM   3621 C  CA   B ASN   A 1 159 ? 2.725  -2.146  1.457   0.42 19.69 ?  159 ASN   A CA   1 
ATOM   3622 C  CA   T ASN   A 1 159 ? 2.883  -1.720  1.735   0.30 19.13 ?  159 ASN   A CA   1 
ATOM   3623 C  C    A ASN   A 1 159 ? 3.726  -2.864  1.157   0.28 17.94 ?  159 ASN   A C    1 
ATOM   3624 C  C    B ASN   A 1 159 ? 3.681  -3.215  0.941   0.42 18.21 ?  159 ASN   A C    1 
ATOM   3625 C  C    T ASN   A 1 159 ? 3.719  -2.830  1.106   0.30 19.07 ?  159 ASN   A C    1 
ATOM   3626 O  O    A ASN   A 1 159 ? 3.263  -3.974  0.876   0.28 17.89 ?  159 ASN   A O    1 
ATOM   3627 O  O    B ASN   A 1 159 ? 3.280  -4.360  0.698   0.42 18.14 ?  159 ASN   A O    1 
ATOM   3628 O  O    T ASN   A 1 159 ? 3.193  -3.889  0.771   0.30 19.07 ?  159 ASN   A O    1 
ATOM   3629 C  CB   A ASN   A 1 159 ? 2.374  -0.778  0.742   0.28 19.22 ?  159 ASN   A CB   1 
ATOM   3630 C  CB   B ASN   A 1 159 ? 2.262  -1.214  0.334   0.42 22.00 ?  159 ASN   A CB   1 
ATOM   3631 C  CB   T ASN   A 1 159 ? 2.393  -0.739  0.668   0.30 19.40 ?  159 ASN   A CB   1 
ATOM   3632 C  CG   A ASN   A 1 159 ? 1.153  -0.003  1.194   0.28 20.01 ?  159 ASN   A CG   1 
ATOM   3633 C  CG   B ASN   A 1 159 ? 1.089  -0.344  0.748   0.42 24.48 ?  159 ASN   A CG   1 
ATOM   3634 C  CG   T ASN   A 1 159 ? 1.177  0.048   1.118   0.30 19.99 ?  159 ASN   A CG   1 
ATOM   3635 O  OD1  A ASN   A 1 159 ? 0.305  -0.531  1.910   0.28 20.30 ?  159 ASN   A OD1  1 
ATOM   3636 O  OD1  B ASN   A 1 159 ? 1.263  0.674   1.417   0.42 25.35 ?  159 ASN   A OD1  1 
ATOM   3637 O  OD1  T ASN   A 1 159 ? 0.362  -0.446  1.894   0.30 20.17 ?  159 ASN   A OD1  1 
ATOM   3638 N  ND2  A ASN   A 1 159 ? 1.057  1.254   0.778   0.28 20.03 ?  159 ASN   A ND2  1 
ATOM   3639 N  ND2  B ASN   A 1 159 ? -0.112 -0.741  0.349   0.42 25.48 ?  159 ASN   A ND2  1 
ATOM   3640 N  ND2  T ASN   A 1 159 ? 1.048  1.276   0.632   0.30 19.97 ?  159 ASN   A ND2  1 
ATOM   3641 H  H    A ASN   A 1 159 ? 3.645  -0.273  2.765   0.28 23.08 ?  159 ASN   A H    1 
ATOM   3642 H  H    B ASN   A 1 159 ? 3.404  -0.521  2.362   0.42 22.97 ?  159 ASN   A H    1 
ATOM   3643 H  H    T ASN   A 1 159 ? 3.757  -0.192  2.632   0.30 23.21 ?  159 ASN   A H    1 
ATOM   3644 H  HA   A ASN   A 1 159 ? 2.055  -2.237  2.140   0.28 22.44 ?  159 ASN   A HA   1 
ATOM   3645 H  HA   B ASN   A 1 159 ? 1.939  -2.591  1.810   0.42 23.62 ?  159 ASN   A HA   1 
ATOM   3646 H  HA   T ASN   A 1 159 ? 2.105  -2.139  2.131   0.30 22.96 ?  159 ASN   A HA   1 
ATOM   3647 H  HB2  A ASN   A 1 159 ? 3.084  -0.144  0.574   0.28 23.06 ?  159 ASN   A HB2  1 
ATOM   3648 H  HB2  B ASN   A 1 159 ? 2.992  -0.623  0.086   0.42 26.40 ?  159 ASN   A HB2  1 
ATOM   3649 H  HB2  T ASN   A 1 159 ? 3.099  -0.110  0.468   0.30 23.28 ?  159 ASN   A HB2  1 
ATOM   3650 H  HB3  A ASN   A 1 159 ? 2.144  -1.249  -0.076  0.28 23.06 ?  159 ASN   A HB3  1 
ATOM   3651 H  HB3  B ASN   A 1 159 ? 1.983  -1.739  -0.428  0.42 26.40 ?  159 ASN   A HB3  1 
ATOM   3652 H  HB3  T ASN   A 1 159 ? 2.152  -1.238  -0.130  0.30 23.28 ?  159 ASN   A HB3  1 
ATOM   3653 H  HD21 A ASN   A 1 159 ? 0.381  1.732   1.009   0.28 24.03 ?  159 ASN   A HD21 1 
ATOM   3654 H  HD21 B ASN   A 1 159 ? -0.812 -0.282  0.557   0.42 30.58 ?  159 ASN   A HD21 1 
ATOM   3655 H  HD21 T ASN   A 1 159 ? 0.373  1.758   0.858   0.30 23.97 ?  159 ASN   A HD21 1 
ATOM   3656 H  HD22 A ASN   A 1 159 ? 1.670  1.588   0.280   0.28 24.03 ?  159 ASN   A HD22 1 
ATOM   3657 H  HD22 B ASN   A 1 159 ? -0.193 -1.457  -0.118  0.42 30.58 ?  159 ASN   A HD22 1 
ATOM   3658 H  HD22 T ASN   A 1 159 ? 1.639  1.585   0.093   0.30 23.97 ?  159 ASN   A HD22 1 
ATOM   3659 N  N    A LEU   A 1 160 ? 5.007  -2.558  0.946   0.28 17.10 ?  160 LEU   A N    1 
ATOM   3660 N  N    B LEU   A 1 160 ? 4.959  -2.870  0.808   0.42 16.95 ?  160 LEU   A N    1 
ATOM   3661 N  N    T LEU   A 1 160 ? 5.018  -2.601  0.955   0.30 18.91 ?  160 LEU   A N    1 
ATOM   3662 C  CA   A LEU   A 1 160 ? 5.911  -3.566  0.403   0.28 16.34 ?  160 LEU   A CA   1 
ATOM   3663 C  CA   B LEU   A 1 160 ? 5.946  -3.845  0.366   0.42 16.14 ?  160 LEU   A CA   1 
ATOM   3664 C  CA   T LEU   A 1 160 ? 5.890  -3.628  0.398   0.30 18.77 ?  160 LEU   A CA   1 
ATOM   3665 C  C    A LEU   A 1 160 ? 6.080  -4.730  1.370   0.28 15.25 ?  160 LEU   A C    1 
ATOM   3666 C  C    B LEU   A 1 160 ? 6.110  -4.955  1.397   0.42 14.72 ?  160 LEU   A C    1 
ATOM   3667 O  O    A LEU   A 1 160 ? 6.123  -5.892  0.951   0.28 14.77 ?  160 LEU   A O    1 
ATOM   3668 O  O    B LEU   A 1 160 ? 6.119  -6.142  1.052   0.42 14.46 ?  160 LEU   A O    1 
ATOM   3669 C  CB   A LEU   A 1 160 ? 7.265  -2.944  0.074   0.28 16.33 ?  160 LEU   A CB   1 
ATOM   3670 C  CB   B LEU   A 1 160 ? 7.274  -3.140  0.112   0.42 16.36 ?  160 LEU   A CB   1 
ATOM   3671 C  CB   T LEU   A 1 160 ? 7.257  -3.050  0.042   0.30 18.45 ?  160 LEU   A CB   1 
ATOM   3672 C  CG   A LEU   A 1 160 ? 8.337  -3.952  -0.340  0.28 16.75 ?  160 LEU   A CG   1 
ATOM   3673 C  CG   B LEU   A 1 160 ? 8.402  -4.059  -0.333  0.42 17.22 ?  160 LEU   A CG   1 
ATOM   3674 C  CG   T LEU   A 1 160 ? 8.295  -4.084  -0.389  0.30 18.52 ?  160 LEU   A CG   1 
ATOM   3675 C  CD1  A LEU   A 1 160 ? 7.888  -4.748  -1.555  0.28 17.24 ?  160 LEU   A CD1  1 
ATOM   3676 C  CD1  B LEU   A 1 160 ? 7.924  -4.919  -1.483  0.42 17.88 ?  160 LEU   A CD1  1 
ATOM   3677 C  CD1  T LEU   A 1 160 ? 7.841  -4.822  -1.636  0.30 18.88 ?  160 LEU   A CD1  1 
ATOM   3678 C  CD2  A LEU   A 1 160 ? 9.653  -3.249  -0.610  0.28 16.76 ?  160 LEU   A CD2  1 
ATOM   3679 C  CD2  B LEU   A 1 160 ? 9.607  -3.233  -0.735  0.42 17.43 ?  160 LEU   A CD2  1 
ATOM   3680 C  CD2  T LEU   A 1 160 ? 9.636  -3.416  -0.619  0.30 18.36 ?  160 LEU   A CD2  1 
ATOM   3681 H  H    A LEU   A 1 160 ? 5.366  -1.791  1.105   0.28 20.52 ?  160 LEU   A H    1 
ATOM   3682 H  H    B LEU   A 1 160 ? 5.274  -2.090  0.977   0.42 20.34 ?  160 LEU   A H    1 
ATOM   3683 H  H    T LEU   A 1 160 ? 5.417  -1.866  1.169   0.30 22.69 ?  160 LEU   A H    1 
ATOM   3684 H  HA   A LEU   A 1 160 ? 5.535  -3.913  -0.415  0.28 19.61 ?  160 LEU   A HA   1 
ATOM   3685 H  HA   B LEU   A 1 160 ? 5.638  -4.237  -0.466  0.42 19.37 ?  160 LEU   A HA   1 
ATOM   3686 H  HB2  A LEU   A 1 160 ? 7.155  -2.304  -0.651  0.28 19.59 ?  160 LEU   A HB2  1 
ATOM   3687 H  HB2  B LEU   A 1 160 ? 7.149  -2.474  -0.583  0.42 19.63 ?  160 LEU   A HB2  1 
ATOM   3688 H  HB2  T LEU   A 1 160 ? 7.147  -2.408  -0.680  0.30 22.14 ?  160 LEU   A HB2  1 
ATOM   3689 H  HB3  A LEU   A 1 160 ? 7.593  -2.494  0.864   0.28 19.59 ?  160 LEU   A HB3  1 
ATOM   3690 H  HB3  B LEU   A 1 160 ? 7.558  -2.703  0.932   0.42 19.63 ?  160 LEU   A HB3  1 
ATOM   3691 H  HB3  T LEU   A 1 160 ? 7.616  -2.609  0.825   0.30 22.14 ?  160 LEU   A HB3  1 
ATOM   3692 H  HG   A LEU   A 1 160 ? 8.487  -4.575  0.388   0.28 20.10 ?  160 LEU   A HG   1 
ATOM   3693 H  HG   B LEU   A 1 160 ? 8.661  -4.640  0.402   0.42 20.66 ?  160 LEU   A HG   1 
ATOM   3694 H  HG   T LEU   A 1 160 ? 8.406  -4.734  0.323   0.30 22.23 ?  160 LEU   A HG   1 
ATOM   3695 H  HD11 A LEU   A 1 160 ? 8.626  -5.300  -1.857  0.28 20.69 ?  160 LEU   A HD11 1 
ATOM   3696 H  HD11 B LEU   A 1 160 ? 8.678  -5.394  -1.848  0.42 21.45 ?  160 LEU   A HD11 1 
ATOM   3697 H  HD11 T LEU   A 1 160 ? 8.550  -5.417  -1.925  0.30 22.65 ?  160 LEU   A HD11 1 
ATOM   3698 H  HD12 A LEU   A 1 160 ? 7.137  -5.310  -1.306  0.28 20.69 ?  160 LEU   A HD12 1 
ATOM   3699 H  HD12 B LEU   A 1 160 ? 7.266  -5.552  -1.156  0.42 21.45 ?  160 LEU   A HD12 1 
ATOM   3700 H  HD12 T LEU   A 1 160 ? 7.044  -5.334  -1.426  0.30 22.65 ?  160 LEU   A HD12 1 
ATOM   3701 H  HD13 A LEU   A 1 160 ? 7.625  -4.132  -2.256  0.28 20.69 ?  160 LEU   A HD13 1 
ATOM   3702 H  HD13 B LEU   A 1 160 ? 7.527  -4.344  -2.159  0.42 21.45 ?  160 LEU   A HD13 1 
ATOM   3703 H  HD13 T LEU   A 1 160 ? 7.647  -4.175  -2.331  0.30 22.65 ?  160 LEU   A HD13 1 
ATOM   3704 H  HD21 A LEU   A 1 160 ? 10.315 -3.910  -0.866  0.28 20.11 ?  160 LEU   A HD21 1 
ATOM   3705 H  HD21 B LEU   A 1 160 ? 10.332 -3.828  -0.982  0.42 20.91 ?  160 LEU   A HD21 1 
ATOM   3706 H  HD21 T LEU   A 1 160 ? 10.280 -4.088  -0.890  0.30 22.03 ?  160 LEU   A HD21 1 
ATOM   3707 H  HD22 A LEU   A 1 160 ? 9.528  -2.609  -1.327  0.28 20.11 ?  160 LEU   A HD22 1 
ATOM   3708 H  HD22 B LEU   A 1 160 ? 9.367  -2.672  -1.490  0.42 20.91 ?  160 LEU   A HD22 1 
ATOM   3709 H  HD22 T LEU   A 1 160 ? 9.540  -2.749  -1.316  0.30 22.03 ?  160 LEU   A HD22 1 
ATOM   3710 H  HD23 A LEU   A 1 160 ? 9.938  -2.792  0.197   0.28 20.11 ?  160 LEU   A HD23 1 
ATOM   3711 H  HD23 B LEU   A 1 160 ? 9.877  -2.679  0.015   0.42 20.91 ?  160 LEU   A HD23 1 
ATOM   3712 H  HD23 T LEU   A 1 160 ? 9.925  -2.994  0.205   0.30 22.03 ?  160 LEU   A HD23 1 
ATOM   3713 N  N    A TYR   A 1 161 ? 6.189  -4.438  2.667   0.58 15.73 ?  161 TYR   A N    1 
ATOM   3714 N  N    B TYR   A 1 161 ? 6.254  -4.584  2.671   0.42 15.26 ?  161 TYR   A N    1 
ATOM   3715 C  CA   A TYR   A 1 161 ? 6.330  -5.498  3.660   0.58 15.50 ?  161 TYR   A CA   1 
ATOM   3716 C  CA   B TYR   A 1 161 ? 6.320  -5.577  3.741   0.42 15.24 ?  161 TYR   A CA   1 
ATOM   3717 C  C    A TYR   A 1 161 ? 5.184  -6.497  3.568   0.58 16.37 ?  161 TYR   A C    1 
ATOM   3718 C  C    B TYR   A 1 161 ? 5.138  -6.537  3.669   0.42 16.13 ?  161 TYR   A C    1 
ATOM   3719 O  O    A TYR   A 1 161 ? 5.405  -7.713  3.507   0.58 15.70 ?  161 TYR   A O    1 
ATOM   3720 O  O    B TYR   A 1 161 ? 5.302  -7.756  3.789   0.42 15.80 ?  161 TYR   A O    1 
ATOM   3721 C  CB   A TYR   A 1 161 ? 6.394  -4.896  5.061   0.58 15.28 ?  161 TYR   A CB   1 
ATOM   3722 C  CB   B TYR   A 1 161 ? 6.366  -4.873  5.102   0.42 14.98 ?  161 TYR   A CB   1 
ATOM   3723 C  CG   A TYR   A 1 161 ? 6.303  -5.936  6.146   0.58 14.37 ?  161 TYR   A CG   1 
ATOM   3724 C  CG   B TYR   A 1 161 ? 6.269  -5.807  6.296   0.42 14.33 ?  161 TYR   A CG   1 
ATOM   3725 C  CD1  A TYR   A 1 161 ? 7.426  -6.638  6.551   0.58 14.11 ?  161 TYR   A CD1  1 
ATOM   3726 C  CD1  B TYR   A 1 161 ? 7.382  -6.497  6.763   0.42 14.57 ?  161 TYR   A CD1  1 
ATOM   3727 C  CD2  A TYR   A 1 161 ? 5.090  -6.223  6.763   0.58 14.26 ?  161 TYR   A CD2  1 
ATOM   3728 C  CD2  B TYR   A 1 161 ? 5.064  -5.984  6.967   0.42 13.88 ?  161 TYR   A CD2  1 
ATOM   3729 C  CE1  A TYR   A 1 161 ? 7.349  -7.592  7.535   0.58 13.59 ?  161 TYR   A CE1  1 
ATOM   3730 C  CE1  B TYR   A 1 161 ? 7.292  -7.350  7.855   0.42 14.62 ?  161 TYR   A CE1  1 
ATOM   3731 C  CE2  A TYR   A 1 161 ? 5.002  -7.179  7.750   0.58 13.98 ?  161 TYR   A CE2  1 
ATOM   3732 C  CE2  B TYR   A 1 161 ? 4.963  -6.833  8.061   0.42 14.01 ?  161 TYR   A CE2  1 
ATOM   3733 C  CZ   A TYR   A 1 161 ? 6.137  -7.859  8.132   0.58 13.46 ?  161 TYR   A CZ   1 
ATOM   3734 C  CZ   B TYR   A 1 161 ? 6.079  -7.513  8.500   0.42 14.74 ?  161 TYR   A CZ   1 
ATOM   3735 O  OH   A TYR   A 1 161 ? 6.072  -8.810  9.119   0.58 13.69 ?  161 TYR   A OH   1 
ATOM   3736 O  OH   B TYR   A 1 161 ? 5.986  -8.362  9.588   0.42 15.81 ?  161 TYR   A OH   1 
ATOM   3737 H  H    A TYR   A 1 161 ? 6.184  -3.645  2.996   0.58 18.88 ?  161 TYR   A H    1 
ATOM   3738 H  H    B TYR   A 1 161 ? 6.318  -3.772  2.933   0.42 18.31 ?  161 TYR   A H    1 
ATOM   3739 H  HA   A TYR   A 1 161 ? 7.152  -5.982  3.505   0.58 18.60 ?  161 TYR   A HA   1 
ATOM   3740 H  HA   B TYR   A 1 161 ? 7.132  -6.094  3.643   0.42 18.29 ?  161 TYR   A HA   1 
ATOM   3741 H  HB2  A TYR   A 1 161 ? 7.239  -4.432  5.168   0.58 18.34 ?  161 TYR   A HB2  1 
ATOM   3742 H  HB2  B TYR   A 1 161 ? 7.205  -4.391  5.173   0.42 17.98 ?  161 TYR   A HB2  1 
ATOM   3743 H  HB3  A TYR   A 1 161 ? 5.657  -4.278  5.179   0.58 18.34 ?  161 TYR   A HB3  1 
ATOM   3744 H  HB3  B TYR   A 1 161 ? 5.626  -4.248  5.155   0.42 17.98 ?  161 TYR   A HB3  1 
ATOM   3745 H  HD1  A TYR   A 1 161 ? 8.244  -6.464  6.153   0.58 16.94 ?  161 TYR   A HD1  1 
ATOM   3746 H  HD1  B TYR   A 1 161 ? 8.199  -6.391  6.336   0.42 17.48 ?  161 TYR   A HD1  1 
ATOM   3747 H  HD2  A TYR   A 1 161 ? 4.319  -5.771  6.506   0.58 17.12 ?  161 TYR   A HD2  1 
ATOM   3748 H  HD2  B TYR   A 1 161 ? 4.305  -5.531  6.677   0.42 16.66 ?  161 TYR   A HD2  1 
ATOM   3749 H  HE1  A TYR   A 1 161 ? 8.109  -8.061  7.798   0.58 16.30 ?  161 TYR   A HE1  1 
ATOM   3750 H  HE1  B TYR   A 1 161 ? 8.044  -7.809  8.158   0.42 17.55 ?  161 TYR   A HE1  1 
ATOM   3751 H  HE2  A TYR   A 1 161 ? 4.179  -7.370  8.155   0.58 16.78 ?  161 TYR   A HE2  1 
ATOM   3752 H  HE2  B TYR   A 1 161 ? 4.144  -6.944  8.497   0.42 16.82 ?  161 TYR   A HE2  1 
ATOM   3753 H  HH   A TYR   A 1 161 ? 5.277  -8.893  9.396   0.58 16.42 ?  161 TYR   A HH   1 
ATOM   3754 H  HH   B TYR   A 1 161 ? 5.193  -8.368  9.885   0.42 18.97 ?  161 TYR   A HH   1 
ATOM   3755 N  N    A ASP   A 1 162 ? 3.943  -6.000  3.573   0.58 17.66 ?  162 ASP   A N    1 
ATOM   3756 N  N    B ASP   A 1 162 ? 3.932  -5.998  3.467   0.42 17.25 ?  162 ASP   A N    1 
ATOM   3757 C  CA   A ASP   A 1 162 ? 2.793  -6.898  3.501   0.58 18.55 ?  162 ASP   A CA   1 
ATOM   3758 C  CA   B ASP   A 1 162 ? 2.745  -6.844  3.371   0.42 18.20 ?  162 ASP   A CA   1 
ATOM   3759 C  C    A ASP   A 1 162 ? 2.835  -7.733  2.230   0.58 18.70 ?  162 ASP   A C    1 
ATOM   3760 C  C    B ASP   A 1 162 ? 2.848  -7.815  2.197   0.42 18.01 ?  162 ASP   A C    1 
ATOM   3761 O  O    A ASP   A 1 162 ? 2.522  -8.930  2.250   0.58 19.00 ?  162 ASP   A O    1 
ATOM   3762 O  O    B ASP   A 1 162 ? 2.463  -8.985  2.313   0.42 18.24 ?  162 ASP   A O    1 
ATOM   3763 C  CB   A ASP   A 1 162 ? 1.489  -6.102  3.574   0.58 19.02 ?  162 ASP   A CB   1 
ATOM   3764 C  CB   B ASP   A 1 162 ? 1.482  -5.980  3.248   0.42 19.32 ?  162 ASP   A CB   1 
ATOM   3765 C  CG   A ASP   A 1 162 ? 1.184  -5.595  4.968   0.58 19.74 ?  162 ASP   A CG   1 
ATOM   3766 C  CG   B ASP   A 1 162 ? 1.200  -5.144  4.494   0.42 19.96 ?  162 ASP   A CG   1 
ATOM   3767 O  OD1  A ASP   A 1 162 ? 1.829  -6.052  5.936   0.58 20.06 ?  162 ASP   A OD1  1 
ATOM   3768 O  OD1  B ASP   A 1 162 ? 1.711  -5.479  5.582   0.42 20.48 ?  162 ASP   A OD1  1 
ATOM   3769 O  OD2  A ASP   A 1 162 ? 0.282  -4.737  5.088   0.58 20.19 -1 162 ASP   A OD2  1 
ATOM   3770 O  OD2  B ASP   A 1 162 ? 0.433  -4.158  4.388   0.42 20.45 -1 162 ASP   A OD2  1 
ATOM   3771 H  H    A ASP   A 1 162 ? 3.742  -5.162  3.609   0.58 21.19 ?  162 ASP   A H    1 
ATOM   3772 H  H    B ASP   A 1 162 ? 3.776  -5.157  3.393   0.42 20.70 ?  162 ASP   A H    1 
ATOM   3773 H  HA   A ASP   A 1 162 ? 2.813  -7.504  4.255   0.58 22.26 ?  162 ASP   A HA   1 
ATOM   3774 H  HA   B ASP   A 1 162 ? 2.665  -7.372  4.178   0.42 21.84 ?  162 ASP   A HA   1 
ATOM   3775 H  HB2  A ASP   A 1 162 ? 1.546  -5.336  2.982   0.58 22.82 ?  162 ASP   A HB2  1 
ATOM   3776 H  HB2  B ASP   A 1 162 ? 1.582  -5.374  2.500   0.42 23.18 ?  162 ASP   A HB2  1 
ATOM   3777 H  HB3  A ASP   A 1 162 ? 0.749  -6.671  3.314   0.58 22.82 ?  162 ASP   A HB3  1 
ATOM   3778 H  HB3  B ASP   A 1 162 ? 0.715  -6.555  3.115   0.42 23.18 ?  162 ASP   A HB3  1 
ATOM   3779 N  N    A LYS   A 1 163 ? 3.220  -7.119  1.110   0.58 19.32 ?  163 LYS   A N    1 
ATOM   3780 N  N    B LYS   A 1 163 ? 3.369  -7.349  1.057   0.42 18.31 ?  163 LYS   A N    1 
ATOM   3781 C  CA   A LYS   A 1 163 ? 3.343  -7.878  -0.127  0.58 20.19 ?  163 LYS   A CA   1 
ATOM   3782 C  CA   B LYS   A 1 163 ? 3.449  -8.201  -0.127  0.42 18.70 ?  163 LYS   A CA   1 
ATOM   3783 C  C    A LYS   A 1 163 ? 4.448  -8.921  -0.026  0.58 18.96 ?  163 LYS   A C    1 
ATOM   3784 C  C    B LYS   A 1 163 ? 4.521  -9.279  0.022   0.42 17.25 ?  163 LYS   A C    1 
ATOM   3785 O  O    A LYS   A 1 163 ? 4.314  -10.029 -0.558  0.58 19.45 ?  163 LYS   A O    1 
ATOM   3786 O  O    B LYS   A 1 163 ? 4.329  -10.420 -0.417  0.42 17.94 ?  163 LYS   A O    1 
ATOM   3787 C  CB   A LYS   A 1 163 ? 3.606  -6.940  -1.302  0.58 22.45 ?  163 LYS   A CB   1 
ATOM   3788 C  CB   B LYS   A 1 163 ? 3.700  -7.337  -1.367  0.42 21.10 ?  163 LYS   A CB   1 
ATOM   3789 C  CG   A LYS   A 1 163 ? 3.661  -7.663  -2.636  0.58 24.92 ?  163 LYS   A CG   1 
ATOM   3790 C  CG   B LYS   A 1 163 ? 3.864  -8.131  -2.651  0.42 23.68 ?  163 LYS   A CG   1 
ATOM   3791 C  CD   A LYS   A 1 163 ? 4.081  -6.739  -3.757  0.58 27.29 ?  163 LYS   A CD   1 
ATOM   3792 C  CD   B LYS   A 1 163 ? 3.588  -7.288  -3.892  0.42 26.05 ?  163 LYS   A CD   1 
ATOM   3793 C  CE   A LYS   A 1 163 ? 4.036  -7.453  -5.098  0.58 29.09 ?  163 LYS   A CE   1 
ATOM   3794 C  CE   B LYS   A 1 163 ? 4.855  -6.668  -4.460  0.42 27.77 ?  163 LYS   A CE   1 
ATOM   3795 N  NZ   A LYS   A 1 163 ? 4.664  -6.646  -6.176  0.58 30.27 ?  163 LYS   A NZ   1 
ATOM   3796 N  NZ   B LYS   A 1 163 ? 4.780  -6.535  -5.943  0.42 28.82 ?  163 LYS   A NZ   1 
ATOM   3797 H  H    A LYS   A 1 163 ? 3.407  -6.278  1.045   0.58 23.19 ?  163 LYS   A H    1 
ATOM   3798 H  H    B LYS   A 1 163 ? 3.673  -6.549  0.944   0.42 21.97 ?  163 LYS   A H    1 
ATOM   3799 H  HA   A LYS   A 1 163 ? 2.507  -8.339  -0.293  0.58 24.23 ?  163 LYS   A HA   1 
ATOM   3800 H  HA   B LYS   A 1 163 ? 2.595  -8.642  -0.253  0.42 22.44 ?  163 LYS   A HA   1 
ATOM   3801 H  HB2  A LYS   A 1 163 ? 2.892  -6.283  -1.348  0.58 26.94 ?  163 LYS   A HB2  1 
ATOM   3802 H  HB2  B LYS   A 1 163 ? 2.946  -6.734  -1.485  0.42 25.32 ?  163 LYS   A HB2  1 
ATOM   3803 H  HB3  A LYS   A 1 163 ? 4.456  -6.496  -1.166  0.58 26.94 ?  163 LYS   A HB3  1 
ATOM   3804 H  HB3  B LYS   A 1 163 ? 4.510  -6.821  -1.234  0.42 25.32 ?  163 LYS   A HB3  1 
ATOM   3805 H  HG2  A LYS   A 1 163 ? 4.306  -8.387  -2.586  0.58 29.90 ?  163 LYS   A HG2  1 
ATOM   3806 H  HG2  B LYS   A 1 163 ? 4.774  -8.466  -2.704  0.42 28.41 ?  163 LYS   A HG2  1 
ATOM   3807 H  HG3  A LYS   A 1 163 ? 2.780  -8.016  -2.843  0.58 29.90 ?  163 LYS   A HG3  1 
ATOM   3808 H  HG3  B LYS   A 1 163 ? 3.239  -8.869  -2.650  0.42 28.41 ?  163 LYS   A HG3  1 
ATOM   3809 H  HD2  A LYS   A 1 163 ? 3.475  -5.983  -3.791  0.58 32.75 ?  163 LYS   A HD2  1 
ATOM   3810 H  HD2  B LYS   A 1 163 ? 3.196  -7.849  -4.577  0.42 31.26 ?  163 LYS   A HD2  1 
ATOM   3811 H  HD3  A LYS   A 1 163 ? 4.989  -6.438  -3.600  0.58 32.75 ?  163 LYS   A HD3  1 
ATOM   3812 H  HD3  B LYS   A 1 163 ? 2.978  -6.566  -3.664  0.42 31.26 ?  163 LYS   A HD3  1 
ATOM   3813 H  HE2  A LYS   A 1 163 ? 4.513  -8.294  -5.027  0.58 34.91 ?  163 LYS   A HE2  1 
ATOM   3814 H  HE2  B LYS   A 1 163 ? 4.973  -5.782  -4.084  0.42 33.32 ?  163 LYS   A HE2  1 
ATOM   3815 H  HE3  A LYS   A 1 163 ? 3.110  -7.615  -5.340  0.58 34.91 ?  163 LYS   A HE3  1 
ATOM   3816 H  HE3  B LYS   A 1 163 ? 5.617  -7.226  -4.243  0.42 33.32 ?  163 LYS   A HE3  1 
ATOM   3817 H  HZ1  A LYS   A 1 163 ? 4.624  -7.087  -6.947  0.58 36.32 ?  163 LYS   A HZ1  1 
ATOM   3818 H  HZ1  B LYS   A 1 163 ? 5.530  -6.173  -6.256  0.42 34.58 ?  163 LYS   A HZ1  1 
ATOM   3819 H  HZ2  A LYS   A 1 163 ? 4.237  -5.870  -6.262  0.58 36.32 ?  163 LYS   A HZ2  1 
ATOM   3820 H  HZ2  B LYS   A 1 163 ? 4.669  -7.337  -6.315  0.42 34.58 ?  163 LYS   A HZ2  1 
ATOM   3821 H  HZ3  A LYS   A 1 163 ? 5.517  -6.486  -5.977  0.58 36.32 ?  163 LYS   A HZ3  1 
ATOM   3822 H  HZ3  B LYS   A 1 163 ? 4.092  -6.017  -6.168  0.42 34.58 ?  163 LYS   A HZ3  1 
ATOM   3823 N  N    A LEU   A 1 164 ? 5.556  -8.582  0.635   0.58 17.20 ?  164 LEU   A N    1 
ATOM   3824 N  N    B LEU   A 1 164 ? 5.654  -8.940  0.644   0.42 15.24 ?  164 LEU   A N    1 
ATOM   3825 C  CA   A LEU   A 1 164 ? 6.638  -9.548  0.799   0.58 16.45 ?  164 LEU   A CA   1 
ATOM   3826 C  CA   B LEU   A 1 164 ? 6.742  -9.903  0.804   0.42 14.23 ?  164 LEU   A CA   1 
ATOM   3827 C  C    A LEU   A 1 164 ? 6.200  -10.717 1.670   0.58 16.27 ?  164 LEU   A C    1 
ATOM   3828 C  C    B LEU   A 1 164 ? 6.310  -11.085 1.661   0.42 14.11 ?  164 LEU   A C    1 
ATOM   3829 O  O    A LEU   A 1 164 ? 6.462  -11.880 1.343   0.58 16.60 ?  164 LEU   A O    1 
ATOM   3830 O  O    B LEU   A 1 164 ? 6.687  -12.231 1.391   0.42 14.06 ?  164 LEU   A O    1 
ATOM   3831 C  CB   A LEU   A 1 164 ? 7.859  -8.864  1.404   0.58 15.93 ?  164 LEU   A CB   1 
ATOM   3832 C  CB   B LEU   A 1 164 ? 7.945  -9.221  1.451   0.42 13.58 ?  164 LEU   A CB   1 
ATOM   3833 C  CG   A LEU   A 1 164 ? 8.625  -7.945  0.458   0.58 16.04 ?  164 LEU   A CG   1 
ATOM   3834 C  CG   B LEU   A 1 164 ? 8.685  -8.173  0.624   0.42 13.55 ?  164 LEU   A CG   1 
ATOM   3835 C  CD1  A LEU   A 1 164 ? 9.585  -7.097  1.260   0.58 15.17 ?  164 LEU   A CD1  1 
ATOM   3836 C  CD1  B LEU   A 1 164 ? 9.520  -7.276  1.526   0.42 13.73 ?  164 LEU   A CD1  1 
ATOM   3837 C  CD2  A LEU   A 1 164 ? 9.371  -8.740  -0.607  0.58 16.77 ?  164 LEU   A CD2  1 
ATOM   3838 C  CD2  B LEU   A 1 164 ? 9.567  -8.849  -0.410  0.42 13.74 ?  164 LEU   A CD2  1 
ATOM   3839 H  H    A LEU   A 1 164 ? 5.707  -7.805  0.987   0.58 20.64 ?  164 LEU   A H    1 
ATOM   3840 H  H    B LEU   A 1 164 ? 5.810  -8.170  0.985   0.42 18.29 ?  164 LEU   A H    1 
ATOM   3841 H  HA   A LEU   A 1 164 ? 6.883  -9.894  -0.072  0.58 19.74 ?  164 LEU   A HA   1 
ATOM   3842 H  HA   B LEU   A 1 164 ? 7.003  -10.243 -0.067  0.42 17.07 ?  164 LEU   A HA   1 
ATOM   3843 H  HB2  A LEU   A 1 164 ? 7.571  -8.330  2.159   0.58 19.12 ?  164 LEU   A HB2  1 
ATOM   3844 H  HB2  B LEU   A 1 164 ? 7.641  -8.789  2.261   0.42 16.29 ?  164 LEU   A HB2  1 
ATOM   3845 H  HB3  A LEU   A 1 164 ? 8.475  -9.550  1.705   0.58 19.12 ?  164 LEU   A HB3  1 
ATOM   3846 H  HB3  B LEU   A 1 164 ? 8.588  -9.912  1.679   0.42 16.29 ?  164 LEU   A HB3  1 
ATOM   3847 H  HG   A LEU   A 1 164 ? 7.998  -7.354  0.011   0.58 19.25 ?  164 LEU   A HG   1 
ATOM   3848 H  HG   B LEU   A 1 164 ? 8.039  -7.620  0.160   0.42 16.26 ?  164 LEU   A HG   1 
ATOM   3849 H  HD11 A LEU   A 1 164 ? 10.082 -6.527  0.658   0.58 18.21 ?  164 LEU   A HD11 1 
ATOM   3850 H  HD11 B LEU   A 1 164 ? 9.987  -6.627  0.979   0.42 16.47 ?  164 LEU   A HD11 1 
ATOM   3851 H  HD12 A LEU   A 1 164 ? 9.077  -6.558  1.888   0.58 18.21 ?  164 LEU   A HD12 1 
ATOM   3852 H  HD12 B LEU   A 1 164 ? 8.933  -6.823  2.152   0.42 16.47 ?  164 LEU   A HD12 1 
ATOM   3853 H  HD13 A LEU   A 1 164 ? 10.191 -7.682  1.743   0.58 18.21 ?  164 LEU   A HD13 1 
ATOM   3854 H  HD13 B LEU   A 1 164 ? 10.159 -7.823  2.010   0.42 16.47 ?  164 LEU   A HD13 1 
ATOM   3855 H  HD21 A LEU   A 1 164 ? 9.913  -8.130  -1.133  0.58 20.12 ?  164 LEU   A HD21 1 
ATOM   3856 H  HD21 B LEU   A 1 164 ? 10.015 -8.166  -0.933  0.42 16.48 ?  164 LEU   A HD21 1 
ATOM   3857 H  HD22 A LEU   A 1 164 ? 9.940  -9.395  -0.172  0.58 20.12 ?  164 LEU   A HD22 1 
ATOM   3858 H  HD22 B LEU   A 1 164 ? 10.221 -9.400  0.046   0.42 16.48 ?  164 LEU   A HD22 1 
ATOM   3859 H  HD23 A LEU   A 1 164 ? 8.729  -9.188  -1.179  0.58 20.12 ?  164 LEU   A HD23 1 
ATOM   3860 H  HD23 B LEU   A 1 164 ? 9.012  -9.397  -0.986  0.42 16.48 ?  164 LEU   A HD23 1 
ATOM   3861 N  N    A VAL   A 1 165 ? 5.539  -10.426 2.791   0.58 15.55 ?  165 VAL   A N    1 
ATOM   3862 N  N    B VAL   A 1 165 ? 5.539  -10.819 2.714   0.42 13.97 ?  165 VAL   A N    1 
ATOM   3863 C  CA   A VAL   A 1 165 ? 5.060  -11.492 3.664   0.58 15.46 ?  165 VAL   A CA   1 
ATOM   3864 C  CA   B VAL   A 1 165 ? 5.076  -11.887 3.593   0.42 13.72 ?  165 VAL   A CA   1 
ATOM   3865 C  C    A VAL   A 1 165 ? 4.023  -12.342 2.941   0.58 15.44 ?  165 VAL   A C    1 
ATOM   3866 C  C    B VAL   A 1 165 ? 4.078  -12.780 2.866   0.42 13.90 ?  165 VAL   A C    1 
ATOM   3867 O  O    A VAL   A 1 165 ? 4.121  -13.574 2.900   0.58 15.76 ?  165 VAL   A O    1 
ATOM   3868 O  O    B VAL   A 1 165 ? 4.208  -14.009 2.864   0.42 13.89 ?  165 VAL   A O    1 
ATOM   3869 C  CB   A VAL   A 1 165 ? 4.518  -10.906 4.981   0.58 15.77 ?  165 VAL   A CB   1 
ATOM   3870 C  CB   B VAL   A 1 165 ? 4.478  -11.285 4.879   0.42 14.24 ?  165 VAL   A CB   1 
ATOM   3871 C  CG1  A VAL   A 1 165 ? 3.715  -11.951 5.746   0.58 15.83 ?  165 VAL   A CG1  1 
ATOM   3872 C  CG1  B VAL   A 1 165 ? 3.896  -12.376 5.766   0.42 14.49 ?  165 VAL   A CG1  1 
ATOM   3873 C  CG2  A VAL   A 1 165 ? 5.664  -10.372 5.830   0.58 16.09 ?  165 VAL   A CG2  1 
ATOM   3874 C  CG2  B VAL   A 1 165 ? 5.526  -10.472 5.628   0.42 14.75 ?  165 VAL   A CG2  1 
ATOM   3875 H  H    A VAL   A 1 165 ? 5.360  -9.630  3.065   0.58 18.66 ?  165 VAL   A H    1 
ATOM   3876 H  H    B VAL   A 1 165 ? 5.275  -10.039 2.943   0.42 16.76 ?  165 VAL   A H    1 
ATOM   3877 H  HA   A VAL   A 1 165 ? 5.804  -12.068 3.890   0.58 18.56 ?  165 VAL   A HA   1 
ATOM   3878 H  HA   B VAL   A 1 165 ? 5.833  -12.439 3.851   0.42 16.47 ?  165 VAL   A HA   1 
ATOM   3879 H  HB   A VAL   A 1 165 ? 3.926  -10.162 4.781   0.58 18.92 ?  165 VAL   A HB   1 
ATOM   3880 H  HB   B VAL   A 1 165 ? 3.755  -10.688 4.635   0.42 17.09 ?  165 VAL   A HB   1 
ATOM   3881 H  HG11 A VAL   A 1 165 ? 3.625  -11.666 6.670   0.58 19.00 ?  165 VAL   A HG11 1 
ATOM   3882 H  HG11 B VAL   A 1 165 ? 3.731  -12.007 6.648   0.42 17.39 ?  165 VAL   A HG11 1 
ATOM   3883 H  HG12 A VAL   A 1 165 ? 2.837  -12.038 5.343   0.58 19.00 ?  165 VAL   A HG12 1 
ATOM   3884 H  HG12 B VAL   A 1 165 ? 3.062  -12.689 5.380   0.42 17.39 ?  165 VAL   A HG12 1 
ATOM   3885 H  HG13 A VAL   A 1 165 ? 4.186  -12.798 5.709   0.58 19.00 ?  165 VAL   A HG13 1 
ATOM   3886 H  HG13 B VAL   A 1 165 ? 4.530  -13.105 5.827   0.42 17.39 ?  165 VAL   A HG13 1 
ATOM   3887 H  HG21 A VAL   A 1 165 ? 5.314  -10.083 6.687   0.58 19.31 ?  165 VAL   A HG21 1 
ATOM   3888 H  HG21 B VAL   A 1 165 ? 5.123  -10.100 6.429   0.42 17.69 ?  165 VAL   A HG21 1 
ATOM   3889 H  HG22 A VAL   A 1 165 ? 6.314  -11.080 5.960   0.58 19.31 ?  165 VAL   A HG22 1 
ATOM   3890 H  HG22 B VAL   A 1 165 ? 6.265  -11.050 5.867   0.42 17.69 ?  165 VAL   A HG22 1 
ATOM   3891 H  HG23 A VAL   A 1 165 ? 6.076  -9.624  5.370   0.58 19.31 ?  165 VAL   A HG23 1 
ATOM   3892 H  HG23 B VAL   A 1 165 ? 5.838  -9.754  5.055   0.42 17.69 ?  165 VAL   A HG23 1 
ATOM   3893 N  N    A SER   A 1 166 ? 3.022  -11.693 2.343   0.58 15.55 ?  166 SER   A N    1 
ATOM   3894 N  N    B SER   A 1 166 ? 3.077  -12.172 2.226   0.42 14.40 ?  166 SER   A N    1 
ATOM   3895 C  CA   A SER   A 1 166 ? 1.918  -12.439 1.748   0.58 16.61 ?  166 SER   A CA   1 
ATOM   3896 C  CA   B SER   A 1 166 ? 1.992  -12.948 1.632   0.42 15.51 ?  166 SER   A CA   1 
ATOM   3897 C  C    A SER   A 1 166 ? 2.332  -13.251 0.526   0.58 16.76 ?  166 SER   A C    1 
ATOM   3898 C  C    B SER   A 1 166 ? 2.513  -13.909 0.575   0.42 16.25 ?  166 SER   A C    1 
ATOM   3899 O  O    A SER   A 1 166 ? 1.612  -14.187 0.155   0.58 17.80 ?  166 SER   A O    1 
ATOM   3900 O  O    B SER   A 1 166 ? 2.019  -15.038 0.454   0.42 16.62 ?  166 SER   A O    1 
ATOM   3901 C  CB   A SER   A 1 166 ? 0.773  -11.496 1.369   0.58 18.26 ?  166 SER   A CB   1 
ATOM   3902 C  CB   B SER   A 1 166 ? 0.952  -12.007 1.024   0.42 16.07 ?  166 SER   A CB   1 
ATOM   3903 O  OG   A SER   A 1 166 ? 0.126  -10.977 2.522   0.58 19.53 ?  166 SER   A OG   1 
ATOM   3904 O  OG   B SER   A 1 166 ? 0.434  -11.133 2.010   0.42 17.50 ?  166 SER   A OG   1 
ATOM   3905 H  H    A SER   A 1 166 ? 2.952  -10.833 2.285   0.58 18.66 ?  166 SER   A H    1 
ATOM   3906 H  H    B SER   A 1 166 ? 3.006  -11.330 2.121   0.42 17.28 ?  166 SER   A H    1 
ATOM   3907 H  HA   A SER   A 1 166 ? 1.570  -13.056 2.409   0.58 19.93 ?  166 SER   A HA   1 
ATOM   3908 H  HA   B SER   A 1 166 ? 1.551  -13.475 2.316   0.42 18.61 ?  166 SER   A HA   1 
ATOM   3909 H  HB2  A SER   A 1 166 ? 1.121  -10.767 0.833   0.58 21.91 ?  166 SER   A HB2  1 
ATOM   3910 H  HB2  B SER   A 1 166 ? 1.368  -11.491 0.313   0.42 19.29 ?  166 SER   A HB2  1 
ATOM   3911 H  HB3  A SER   A 1 166 ? 0.108  -11.990 0.863   0.58 21.91 ?  166 SER   A HB3  1 
ATOM   3912 H  HB3  B SER   A 1 166 ? 0.219  -12.530 0.659   0.42 19.29 ?  166 SER   A HB3  1 
ATOM   3913 H  HG   A SER   A 1 166 ? -0.478 -10.438 2.301   0.58 23.43 ?  166 SER   A HG   1 
ATOM   3914 H  HG   B SER   A 1 166 ? 1.053  -10.643 2.311   0.42 21.00 ?  166 SER   A HG   1 
ATOM   3915 N  N    A SER   A 1 167 ? 3.450  -12.914 -0.119  0.58 16.64 ?  167 SER   A N    1 
ATOM   3916 N  N    B SER   A 1 167 ? 3.503  -13.473 -0.200  0.42 17.21 ?  167 SER   A N    1 
ATOM   3917 C  CA   A SER   A 1 167 ? 3.903  -13.642 -1.299  0.58 16.96 ?  167 SER   A CA   1 
ATOM   3918 C  CA   B SER   A 1 167 ? 4.101  -14.296 -1.246  0.42 18.68 ?  167 SER   A CA   1 
ATOM   3919 C  C    A SER   A 1 167 ? 5.038  -14.624 -1.007  0.58 16.89 ?  167 SER   A C    1 
ATOM   3920 C  C    B SER   A 1 167 ? 5.442  -14.835 -0.761  0.42 19.91 ?  167 SER   A C    1 
ATOM   3921 O  O    A SER   A 1 167 ? 5.544  -15.266 -1.937  0.58 17.22 ?  167 SER   A O    1 
ATOM   3922 O  O    B SER   A 1 167 ? 6.507  -14.495 -1.278  0.42 21.91 ?  167 SER   A O    1 
ATOM   3923 C  CB   A SER   A 1 167 ? 4.339  -12.661 -2.399  0.58 17.40 ?  167 SER   A CB   1 
ATOM   3924 C  CB   B SER   A 1 167 ? 4.279  -13.476 -2.518  0.42 18.87 ?  167 SER   A CB   1 
ATOM   3925 O  OG   A SER   A 1 167 ? 5.375  -11.801 -1.944  0.58 17.64 ?  167 SER   A OG   1 
ATOM   3926 O  OG   B SER   A 1 167 ? 5.366  -12.574 -2.384  0.42 18.58 ?  167 SER   A OG   1 
ATOM   3927 H  H    A SER   A 1 167 ? 3.960  -12.250 0.109   0.58 19.96 ?  167 SER   A H    1 
ATOM   3928 H  H    B SER   A 1 167 ? 3.845  -12.686 -0.143  0.42 20.65 ?  167 SER   A H    1 
ATOM   3929 H  HA   A SER   A 1 167 ? 3.150  -14.142 -1.645  0.58 20.35 ?  167 SER   A HA   1 
ATOM   3930 H  HA   B SER   A 1 167 ? 3.538  -15.054 -1.436  0.42 22.42 ?  167 SER   A HA   1 
ATOM   3931 H  HB2  A SER   A 1 167 ? 4.663  -13.172 -3.158  0.58 20.88 ?  167 SER   A HB2  1 
ATOM   3932 H  HB2  B SER   A 1 167 ? 4.460  -14.078 -3.257  0.42 22.64 ?  167 SER   A HB2  1 
ATOM   3933 H  HB3  A SER   A 1 167 ? 3.570  -12.128 -2.671  0.58 20.88 ?  167 SER   A HB3  1 
ATOM   3934 H  HB3  B SER   A 1 167 ? 3.469  -12.973 -2.685  0.42 22.64 ?  167 SER   A HB3  1 
ATOM   3935 H  HG   A SER   A 1 167 ? 5.096  -11.354 -1.287  0.58 21.17 ?  167 SER   A HG   1 
ATOM   3936 H  HG   B SER   A 1 167 ? 6.095  -12.995 -2.392  0.42 22.29 ?  167 SER   A HG   1 
ATOM   3937 N  N    A PHE   A 1 168 ? 5.458  -14.759 0.248   0.58 16.24 ?  168 PHE   A N    1 
ATOM   3938 N  N    B PHE   A 1 168 ? 5.381  -15.695 0.254   0.42 18.68 ?  168 PHE   A N    1 
ATOM   3939 C  CA   A PHE   A 1 168 ? 6.647  -15.549 0.532   0.58 16.67 ?  168 PHE   A CA   1 
ATOM   3940 C  CA   B PHE   A 1 168 ? 6.603  -16.331 0.733   0.42 17.94 ?  168 PHE   A CA   1 
ATOM   3941 C  C    A PHE   A 1 168 ? 6.353  -17.036 0.405   0.58 18.43 ?  168 PHE   A C    1 
ATOM   3942 C  C    B PHE   A 1 168 ? 6.559  -17.851 0.660   0.42 18.52 ?  168 PHE   A C    1 
ATOM   3943 O  O    A PHE   A 1 168 ? 5.360  -17.534 0.943   0.58 20.25 ?  168 PHE   A O    1 
ATOM   3944 O  O    B PHE   A 1 168 ? 7.460  -18.444 0.062   0.42 17.73 ?  168 PHE   A O    1 
ATOM   3945 C  CB   A PHE   A 1 168 ? 7.179  -15.259 1.930   0.58 15.80 ?  168 PHE   A CB   1 
ATOM   3946 C  CB   B PHE   A 1 168 ? 7.026  -15.870 2.132   0.42 17.75 ?  168 PHE   A CB   1 
ATOM   3947 C  CG   A PHE   A 1 168 ? 8.445  -16.000 2.236   0.58 15.19 ?  168 PHE   A CG   1 
ATOM   3948 C  CG   B PHE   A 1 168 ? 8.363  -16.412 2.540   0.42 17.47 ?  168 PHE   A CG   1 
ATOM   3949 C  CD1  A PHE   A 1 168 ? 9.625  -15.638 1.612   0.58 15.38 ?  168 PHE   A CD1  1 
ATOM   3950 C  CD1  B PHE   A 1 168 ? 9.519  -15.948 1.935   0.42 17.71 ?  168 PHE   A CD1  1 
ATOM   3951 C  CD2  A PHE   A 1 168 ? 8.460  -17.075 3.110   0.58 14.79 ?  168 PHE   A CD2  1 
ATOM   3952 C  CD2  B PHE   A 1 168 ? 8.467  -17.413 3.489   0.42 17.28 ?  168 PHE   A CD2  1 
ATOM   3953 C  CE1  A PHE   A 1 168 ? 10.794 -16.318 1.865   0.58 14.88 ?  168 PHE   A CE1  1 
ATOM   3954 C  CE1  B PHE   A 1 168 ? 10.754 -16.454 2.285   0.42 17.84 ?  168 PHE   A CE1  1 
ATOM   3955 C  CE2  A PHE   A 1 168 ? 9.636  -17.757 3.369   0.58 14.74 ?  168 PHE   A CE2  1 
ATOM   3956 C  CE2  B PHE   A 1 168 ? 9.703  -17.922 3.846   0.42 17.59 ?  168 PHE   A CE2  1 
ATOM   3957 C  CZ   A PHE   A 1 168 ? 10.800 -17.377 2.745   0.58 14.86 ?  168 PHE   A CZ   1 
ATOM   3958 C  CZ   B PHE   A 1 168 ? 10.847 -17.442 3.242   0.42 17.85 ?  168 PHE   A CZ   1 
ATOM   3959 H  H    A PHE   A 1 168 ? 5.079  -14.407 0.935   0.58 19.49 ?  168 PHE   A H    1 
ATOM   3960 H  H    B PHE   A 1 168 ? 4.661  -15.928 0.668   0.42 22.41 ?  168 PHE   A H    1 
ATOM   3961 H  HA   A PHE   A 1 168 ? 7.333  -15.318 -0.112  0.58 20.01 ?  168 PHE   A HA   1 
ATOM   3962 H  HA   B PHE   A 1 168 ? 7.320  -16.067 0.135   0.42 21.53 ?  168 PHE   A HA   1 
ATOM   3963 H  HB2  A PHE   A 1 168 ? 7.355  -14.309 2.005   0.58 18.95 ?  168 PHE   A HB2  1 
ATOM   3964 H  HB2  B PHE   A 1 168 ? 7.082  -14.902 2.141   0.42 21.31 ?  168 PHE   A HB2  1 
ATOM   3965 H  HB3  A PHE   A 1 168 ? 6.509  -15.525 2.580   0.58 18.95 ?  168 PHE   A HB3  1 
ATOM   3966 H  HB3  B PHE   A 1 168 ? 6.372  -16.173 2.777   0.42 21.31 ?  168 PHE   A HB3  1 
ATOM   3967 H  HD1  A PHE   A 1 168 ? 9.630  -14.921 1.015   0.58 18.46 ?  168 PHE   A HD1  1 
ATOM   3968 H  HD1  B PHE   A 1 168 ? 9.463  -15.281 1.288   0.42 21.25 ?  168 PHE   A HD1  1 
ATOM   3969 H  HD2  A PHE   A 1 168 ? 7.673  -17.335 3.531   0.58 17.74 ?  168 PHE   A HD2  1 
ATOM   3970 H  HD2  B PHE   A 1 168 ? 7.698  -17.739 3.897   0.42 20.73 ?  168 PHE   A HD2  1 
ATOM   3971 H  HE1  A PHE   A 1 168 ? 11.585 -16.058 1.444   0.58 17.85 ?  168 PHE   A HE1  1 
ATOM   3972 H  HE1  B PHE   A 1 168 ? 11.525 -16.128 1.877   0.42 21.41 ?  168 PHE   A HE1  1 
ATOM   3973 H  HE2  A PHE   A 1 168 ? 9.635  -18.474 3.960   0.58 17.68 ?  168 PHE   A HE2  1 
ATOM   3974 H  HE2  B PHE   A 1 168 ? 9.763  -18.590 4.490   0.42 21.11 ?  168 PHE   A HE2  1 
ATOM   3975 H  HZ   A PHE   A 1 168 ? 11.593 -17.834 2.916   0.58 17.83 ?  168 PHE   A HZ   1 
ATOM   3976 H  HZ   B PHE   A 1 168 ? 11.682 -17.783 3.480   0.42 21.42 ?  168 PHE   A HZ   1 
ATOM   3977 N  N    A LEU   A 1 169 ? 7.242  -17.750 -0.279  0.58 19.46 ?  169 LEU   A N    1 
ATOM   3978 N  N    B LEU   A 1 169 ? 5.572  -18.506 1.264   0.42 19.66 ?  169 LEU   A N    1 
ATOM   3979 C  CA   A LEU   A 1 169 ? 7.077  -19.187 -0.442  0.58 21.72 ?  169 LEU   A CA   1 
ATOM   3980 C  CA   B LEU   A 1 169 ? 5.573  -19.970 1.315   0.42 21.26 ?  169 LEU   A CA   1 
ATOM   3981 C  C    A LEU   A 1 169 ? 7.924  -19.936 0.581   0.58 21.89 ?  169 LEU   A C    1 
ATOM   3982 C  C    B LEU   A 1 169 ? 5.057  -20.569 0.009   0.42 21.85 ?  169 LEU   A C    1 
ATOM   3983 O  O    A LEU   A 1 169 ? 7.371  -20.469 1.545   0.58 22.50 ?  169 LEU   A O    1 
ATOM   3984 O  O    B LEU   A 1 169 ? 5.584  -21.572 -0.475  0.42 22.62 ?  169 LEU   A O    1 
ATOM   3985 C  CB   A LEU   A 1 169 ? 7.415  -19.620 -1.874  0.58 23.01 ?  169 LEU   A CB   1 
ATOM   3986 C  CB   B LEU   A 1 169 ? 4.729  -20.480 2.488   0.42 22.05 ?  169 LEU   A CB   1 
ATOM   3987 C  CG   A LEU   A 1 169 ? 7.072  -21.070 -2.235  0.58 24.05 ?  169 LEU   A CG   1 
ATOM   3988 C  CG   B LEU   A 1 169 ? 5.044  -21.865 3.076   0.42 22.96 ?  169 LEU   A CG   1 
ATOM   3989 C  CD1  A LEU   A 1 169 ? 5.639  -21.405 -1.849  0.58 24.42 ?  169 LEU   A CD1  1 
ATOM   3990 C  CD1  B LEU   A 1 169 ? 4.330  -22.037 4.410   0.42 23.45 ?  169 LEU   A CD1  1 
ATOM   3991 C  CD2  A LEU   A 1 169 ? 7.291  -21.324 -3.721  0.58 24.24 ?  169 LEU   A CD2  1 
ATOM   3992 C  CD2  B LEU   A 1 169 ? 4.681  -23.012 2.143   0.42 23.63 ?  169 LEU   A CD2  1 
ATOM   3993 O  OXT  A LEU   A 1 169 ? 9.154  -20.019 0.495   0.58 21.33 -1 169 LEU   A OXT  1 
ATOM   3994 O  OXT  B LEU   A 1 169 ? 4.107  -20.065 -0.590  0.42 21.72 -1 169 LEU   A OXT  1 
ATOM   3995 H  H    A LEU   A 1 169 ? 7.950  -17.427 -0.655  0.58 23.36 ?  169 LEU   A H    1 
ATOM   3996 H  H    B LEU   A 1 169 ? 4.900  -18.129 1.646   0.42 23.59 ?  169 LEU   A H    1 
ATOM   3997 H  HA   A LEU   A 1 169 ? 6.156  -19.415 -0.269  0.58 26.06 ?  169 LEU   A HA   1 
ATOM   3998 H  HA   B LEU   A 1 169 ? 6.485  -20.271 1.450   0.42 25.51 ?  169 LEU   A HA   1 
ATOM   3999 H  HB2  A LEU   A 1 169 ? 6.926  -19.051 -2.489  0.58 27.61 ?  169 LEU   A HB2  1 
ATOM   4000 H  HB2  B LEU   A 1 169 ? 4.817  -19.843 3.209   0.42 26.46 ?  169 LEU   A HB2  1 
ATOM   4001 H  HB3  A LEU   A 1 169 ? 8.366  -19.509 -2.018  0.58 27.61 ?  169 LEU   A HB3  1 
ATOM   4002 H  HB3  B LEU   A 1 169 ? 3.808  -20.506 2.193   0.42 26.46 ?  169 LEU   A HB3  1 
ATOM   4003 H  HG   A LEU   A 1 169 ? 7.659  -21.667 -1.746  0.58 28.86 ?  169 LEU   A HG   1 
ATOM   4004 H  HG   B LEU   A 1 169 ? 5.995  -21.922 3.246   0.42 27.56 ?  169 LEU   A HG   1 
ATOM   4005 H  HD11 A LEU   A 1 169 ? 5.377  -22.231 -2.285  0.58 29.31 ?  169 LEU   A HD11 1 
ATOM   4006 H  HD11 B LEU   A 1 169 ? 4.425  -22.957 4.703   0.42 28.14 ?  169 LEU   A HD11 1 
ATOM   4007 H  HD12 A LEU   A 1 169 ? 5.587  -21.511 -0.886  0.58 29.31 ?  169 LEU   A HD12 1 
ATOM   4008 H  HD12 B LEU   A 1 169 ? 4.732  -21.442 5.062   0.42 28.14 ?  169 LEU   A HD12 1 
ATOM   4009 H  HD13 A LEU   A 1 169 ? 5.057  -20.683 -2.136  0.58 29.31 ?  169 LEU   A HD13 1 
ATOM   4010 H  HD13 B LEU   A 1 169 ? 3.392  -21.821 4.297   0.42 28.14 ?  169 LEU   A HD13 1 
ATOM   4011 H  HD21 A LEU   A 1 169 ? 7.076  -22.249 -3.922  0.58 29.09 ?  169 LEU   A HD21 1 
ATOM   4012 H  HD21 B LEU   A 1 169 ? 4.822  -23.854 2.610   0.42 28.35 ?  169 LEU   A HD21 1 
ATOM   4013 H  HD22 A LEU   A 1 169 ? 6.712  -20.734 -4.231  0.58 29.09 ?  169 LEU   A HD22 1 
ATOM   4014 H  HD22 B LEU   A 1 169 ? 3.750  -22.930 1.891   0.42 28.35 ?  169 LEU   A HD22 1 
ATOM   4015 H  HD23 A LEU   A 1 169 ? 8.219  -21.146 -3.939  0.58 29.09 ?  169 LEU   A HD23 1 
ATOM   4016 H  HD23 B LEU   A 1 169 ? 5.246  -22.975 1.358   0.42 28.35 ?  169 LEU   A HD23 1 
ATOM   4017 N  N    A SER   B 1 1   ? 50.784 -9.251  -23.705 0.58 27.92 ?  1   SER   B N    1 
ATOM   4018 N  N    B SER   B 1 1   ? 50.727 -9.219  -23.699 0.42 25.47 ?  1   SER   B N    1 
ATOM   4019 C  CA   A SER   B 1 1   ? 51.291 -10.303 -22.801 0.58 27.83 ?  1   SER   B CA   1 
ATOM   4020 C  CA   B SER   B 1 1   ? 51.207 -10.219 -22.724 0.42 25.08 ?  1   SER   B CA   1 
ATOM   4021 C  C    A SER   B 1 1   ? 50.220 -11.355 -22.545 0.58 27.32 ?  1   SER   B C    1 
ATOM   4022 C  C    B SER   B 1 1   ? 50.134 -11.265 -22.466 0.42 23.81 ?  1   SER   B C    1 
ATOM   4023 O  O    A SER   B 1 1   ? 49.028 -11.139 -22.792 0.58 27.31 ?  1   SER   B O    1 
ATOM   4024 O  O    B SER   B 1 1   ? 48.956 -11.090 -22.810 0.42 23.63 ?  1   SER   B O    1 
ATOM   4025 C  CB   A SER   B 1 1   ? 51.755 -9.702  -21.476 0.58 28.32 ?  1   SER   B CB   1 
ATOM   4026 C  CB   B SER   B 1 1   ? 51.603 -9.549  -21.412 0.42 25.93 ?  1   SER   B CB   1 
ATOM   4027 O  OG   A SER   B 1 1   ? 50.651 -9.416  -20.638 0.58 29.76 ?  1   SER   B OG   1 
ATOM   4028 O  OG   B SER   B 1 1   ? 50.461 -9.320  -20.605 0.42 27.29 ?  1   SER   B OG   1 
ATOM   4029 H  H1   A SER   B 1 1   ? 50.697 -9.588  -24.522 0.58 33.50 ?  1   SER   B H1   1 
ATOM   4030 H  H1   B SER   B 1 1   ? 50.635 -9.611  -24.490 0.42 30.56 ?  1   SER   B H1   1 
ATOM   4031 H  H2   A SER   B 1 1   ? 49.998 -8.968  -23.409 0.58 33.50 ?  1   SER   B H2   1 
ATOM   4032 H  H2   B SER   B 1 1   ? 49.947 -8.901  -23.424 0.42 30.56 ?  1   SER   B H2   1 
ATOM   4033 H  H3   A SER   B 1 1   ? 51.364 -8.578  -23.717 0.58 33.50 ?  1   SER   B H3   1 
ATOM   4034 H  H3   B SER   B 1 1   ? 51.322 -8.563  -23.753 0.42 30.56 ?  1   SER   B H3   1 
ATOM   4035 H  HA   A SER   B 1 1   ? 52.047 -10.728 -23.227 0.58 33.39 ?  1   SER   B HA   1 
ATOM   4036 H  HA   B SER   B 1 1   ? 51.986 -10.657 -23.093 0.42 30.09 ?  1   SER   B HA   1 
ATOM   4037 H  HB2  A SER   B 1 1   ? 52.328 -10.344 -21.032 0.58 33.99 ?  1   SER   B HB2  1 
ATOM   4038 H  HB2  B SER   B 1 1   ? 52.223 -10.130 -20.943 0.42 31.12 ?  1   SER   B HB2  1 
ATOM   4039 H  HB3  A SER   B 1 1   ? 52.244 -8.883  -21.653 0.58 33.99 ?  1   SER   B HB3  1 
ATOM   4040 H  HB3  B SER   B 1 1   ? 52.027 -8.698  -21.604 0.42 31.12 ?  1   SER   B HB3  1 
ATOM   4041 H  HG   A SER   B 1 1   ? 50.898 -8.921  -20.005 0.58 35.71 ?  1   SER   B HG   1 
ATOM   4042 H  HG   B SER   B 1 1   ? 50.623 -8.705  -20.056 0.42 32.75 ?  1   SER   B HG   1 
ATOM   4043 N  N    A MET   B 1 2   ? 50.668 -12.493 -22.034 0.58 26.82 ?  2   MET   B N    1 
ATOM   4044 N  N    B MET   B 1 2   ? 50.560 -12.355 -21.844 0.42 22.73 ?  2   MET   B N    1 
ATOM   4045 C  CA   A MET   B 1 2   ? 49.840 -13.680 -21.870 0.58 26.75 ?  2   MET   B CA   1 
ATOM   4046 C  CA   B MET   B 1 2   ? 49.737 -13.539 -21.650 0.42 22.28 ?  2   MET   B CA   1 
ATOM   4047 C  C    A MET   B 1 2   ? 49.595 -13.904 -20.386 0.58 24.28 ?  2   MET   B C    1 
ATOM   4048 C  C    B MET   B 1 2   ? 49.476 -13.687 -20.158 0.42 20.35 ?  2   MET   B C    1 
ATOM   4049 O  O    A MET   B 1 2   ? 50.528 -14.202 -19.634 0.58 24.39 ?  2   MET   B O    1 
ATOM   4050 O  O    B MET   B 1 2   ? 50.399 -13.960 -19.384 0.42 20.20 ?  2   MET   B O    1 
ATOM   4051 C  CB   A MET   B 1 2   ? 50.548 -14.878 -22.486 0.58 29.94 ?  2   MET   B CB   1 
ATOM   4052 C  CB   B MET   B 1 2   ? 50.485 -14.746 -22.201 0.42 24.63 ?  2   MET   B CB   1 
ATOM   4053 C  CG   A MET   B 1 2   ? 49.698 -16.132 -22.581 0.58 32.95 ?  2   MET   B CG   1 
ATOM   4054 C  CG   B MET   B 1 2   ? 49.611 -15.892 -22.691 0.42 26.49 ?  2   MET   B CG   1 
ATOM   4055 S  SD   A MET   B 1 2   ? 50.520 -17.410 -23.549 0.58 35.65 ?  2   MET   B SD   1 
ATOM   4056 S  SD   B MET   B 1 2   ? 50.525 -16.994 -23.779 0.42 28.21 ?  2   MET   B SD   1 
ATOM   4057 C  CE   A MET   B 1 2   ? 51.071 -16.415 -24.933 0.58 35.81 ?  2   MET   B CE   1 
ATOM   4058 C  CE   B MET   B 1 2   ? 51.513 -15.819 -24.675 0.42 28.38 ?  2   MET   B CE   1 
ATOM   4059 H  H    A MET   B 1 2   ? 51.478 -12.607 -21.770 0.58 32.18 ?  2   MET   B H    1 
ATOM   4060 H  H    B MET   B 1 2   ? 51.355 -12.447 -21.518 0.42 27.27 ?  2   MET   B H    1 
ATOM   4061 H  HA   A MET   B 1 2   ? 48.996 -13.556 -22.330 0.58 32.10 ?  2   MET   B HA   1 
ATOM   4062 H  HA   B MET   B 1 2   ? 48.905 -13.455 -22.141 0.42 26.74 ?  2   MET   B HA   1 
ATOM   4063 H  HB2  A MET   B 1 2   ? 50.821 -14.607 -23.371 0.58 35.93 ?  2   MET   B HB2  1 
ATOM   4064 H  HB2  B MET   B 1 2   ? 51.019 -14.401 -22.926 0.42 29.56 ?  2   MET   B HB2  1 
ATOM   4065 H  HB3  A MET   B 1 2   ? 51.328 -15.099 -21.956 0.58 35.93 ?  2   MET   B HB3  1 
ATOM   4066 H  HB3  B MET   B 1 2   ? 51.066 -15.120 -21.528 0.42 29.56 ?  2   MET   B HB3  1 
ATOM   4067 H  HG2  A MET   B 1 2   ? 49.537 -16.476 -21.686 0.58 39.54 ?  2   MET   B HG2  1 
ATOM   4068 H  HG2  B MET   B 1 2   ? 49.292 -16.406 -21.926 0.42 31.78 ?  2   MET   B HG2  1 
ATOM   4069 H  HG3  A MET   B 1 2   ? 48.858 -15.921 -23.018 0.58 39.54 ?  2   MET   B HG3  1 
ATOM   4070 H  HG3  B MET   B 1 2   ? 48.862 -15.554 -23.196 0.42 31.78 ?  2   MET   B HG3  1 
ATOM   4071 H  HE1  A MET   B 1 2   ? 51.240 -16.995 -25.679 0.58 42.97 ?  2   MET   B HE1  1 
ATOM   4072 H  HE1  B MET   B 1 2   ? 51.819 -16.252 -25.461 0.42 34.06 ?  2   MET   B HE1  1 
ATOM   4073 H  HE2  A MET   B 1 2   ? 50.367 -15.779 -25.154 0.58 42.97 ?  2   MET   B HE2  1 
ATOM   4074 H  HE2  B MET   B 1 2   ? 50.955 -15.055 -24.903 0.42 34.06 ?  2   MET   B HE2  1 
ATOM   4075 H  HE3  A MET   B 1 2   ? 51.883 -15.932 -24.692 0.58 42.97 ?  2   MET   B HE3  1 
ATOM   4076 H  HE3  B MET   B 1 2   ? 52.271 -15.535 -24.129 0.42 34.06 ?  2   MET   B HE3  1 
ATOM   4077 N  N    A VAL   B 1 3   ? 48.340 -13.761 -19.968 0.58 21.82 ?  3   VAL   B N    1 
ATOM   4078 N  N    B VAL   B 1 3   ? 48.228 -13.475 -19.755 0.42 18.88 ?  3   VAL   B N    1 
ATOM   4079 C  CA   A VAL   B 1 3   ? 47.936 -13.995 -18.591 0.58 20.27 ?  3   VAL   B CA   1 
ATOM   4080 C  CA   B VAL   B 1 3   ? 47.787 -13.742 -18.393 0.42 18.55 ?  3   VAL   B CA   1 
ATOM   4081 C  C    A VAL   B 1 3   ? 46.694 -14.876 -18.602 0.58 18.05 ?  3   VAL   B C    1 
ATOM   4082 C  C    B VAL   B 1 3   ? 46.536 -14.606 -18.439 0.42 17.46 ?  3   VAL   B C    1 
ATOM   4083 O  O    A VAL   B 1 3   ? 46.004 -15.005 -19.616 0.58 17.74 ?  3   VAL   B O    1 
ATOM   4084 O  O    B VAL   B 1 3   ? 45.707 -14.489 -19.346 0.42 17.50 ?  3   VAL   B O    1 
ATOM   4085 C  CB   A VAL   B 1 3   ? 47.659 -12.680 -17.832 0.58 21.73 ?  3   VAL   B CB   1 
ATOM   4086 C  CB   B VAL   B 1 3   ? 47.533 -12.451 -17.581 0.42 19.78 ?  3   VAL   B CB   1 
ATOM   4087 C  CG1  A VAL   B 1 3   ? 48.929 -11.837 -17.737 0.58 22.25 ?  3   VAL   B CG1  1 
ATOM   4088 C  CG1  B VAL   B 1 3   ? 48.819 -11.644 -17.444 0.42 20.15 ?  3   VAL   B CG1  1 
ATOM   4089 C  CG2  A VAL   B 1 3   ? 46.542 -11.904 -18.512 0.58 22.32 ?  3   VAL   B CG2  1 
ATOM   4090 C  CG2  B VAL   B 1 3   ? 46.432 -11.622 -18.219 0.42 20.24 ?  3   VAL   B CG2  1 
ATOM   4091 H  H    A VAL   B 1 3   ? 47.690 -13.529 -20.484 0.58 26.19 ?  3   VAL   B H    1 
ATOM   4092 H  H    B VAL   B 1 3   ? 47.611 -13.162 -20.268 0.42 22.66 ?  3   VAL   B H    1 
ATOM   4093 H  HA   A VAL   B 1 3   ? 48.646 -14.471 -18.129 0.58 24.33 ?  3   VAL   B HA   1 
ATOM   4094 H  HA   B VAL   B 1 3   ? 48.472 -14.247 -17.938 0.42 22.26 ?  3   VAL   B HA   1 
ATOM   4095 H  HB   A VAL   B 1 3   ? 47.372 -12.896 -16.931 0.58 26.08 ?  3   VAL   B HB   1 
ATOM   4096 H  HB   B VAL   B 1 3   ? 47.242 -12.698 -16.691 0.42 23.73 ?  3   VAL   B HB   1 
ATOM   4097 H  HG11 A VAL   B 1 3   ? 48.729 -11.026 -17.244 0.58 26.70 ?  3   VAL   B HG11 1 
ATOM   4098 H  HG11 B VAL   B 1 3   ? 48.636 -10.849 -16.921 0.42 24.18 ?  3   VAL   B HG11 1 
ATOM   4099 H  HG12 A VAL   B 1 3   ? 49.612 -12.347 -17.273 0.58 26.70 ?  3   VAL   B HG12 1 
ATOM   4100 H  HG12 B VAL   B 1 3   ? 49.485 -12.189 -16.998 0.42 24.18 ?  3   VAL   B HG12 1 
ATOM   4101 H  HG13 A VAL   B 1 3   ? 49.229 -11.617 -18.631 0.58 26.70 ?  3   VAL   B HG13 1 
ATOM   4102 H  HG13 B VAL   B 1 3   ? 49.131 -11.396 -18.328 0.42 24.18 ?  3   VAL   B HG13 1 
ATOM   4103 H  HG21 A VAL   B 1 3   ? 46.470 -11.032 -18.096 0.58 26.78 ?  3   VAL   B HG21 1 
ATOM   4104 H  HG21 B VAL   B 1 3   ? 46.393 -10.760 -17.779 0.42 24.29 ?  3   VAL   B HG21 1 
ATOM   4105 H  HG22 A VAL   B 1 3   ? 46.752 -11.805 -19.454 0.58 26.78 ?  3   VAL   B HG22 1 
ATOM   4106 H  HG22 B VAL   B 1 3   ? 46.630 -11.506 -19.161 0.42 24.29 ?  3   VAL   B HG22 1 
ATOM   4107 H  HG23 A VAL   B 1 3   ? 45.708 -12.389 -18.408 0.58 26.78 ?  3   VAL   B HG23 1 
ATOM   4108 H  HG23 B VAL   B 1 3   ? 45.586 -12.086 -18.114 0.42 24.29 ?  3   VAL   B HG23 1 
ATOM   4109 N  N    . ASN   B 1 4   ? 46.412 -15.485 -17.448 1.00 16.46 ?  4   ASN   B N    1 
ATOM   4110 C  CA   . ASN   B 1 4   ? 45.272 -16.392 -17.325 1.00 15.42 ?  4   ASN   B CA   1 
ATOM   4111 C  C    . ASN   B 1 4   ? 45.214 -17.361 -18.503 1.00 15.74 ?  4   ASN   B C    1 
ATOM   4112 O  O    . ASN   B 1 4   ? 44.154 -17.619 -19.067 1.00 16.88 ?  4   ASN   B O    1 
ATOM   4113 C  CB   . ASN   B 1 4   ? 43.952 -15.630 -17.158 1.00 15.06 ?  4   ASN   B CB   1 
ATOM   4114 C  CG   . ASN   B 1 4   ? 43.911 -14.816 -15.877 1.00 14.58 ?  4   ASN   B CG   1 
ATOM   4115 O  OD1  . ASN   B 1 4   ? 44.193 -15.330 -14.796 1.00 14.56 ?  4   ASN   B OD1  1 
ATOM   4116 N  ND2  . ASN   B 1 4   ? 43.562 -13.540 -15.993 1.00 15.46 ?  4   ASN   B ND2  1 
ATOM   4117 H  H    A ASN   B 1 4   ? 46.864 -15.387 -16.726 0.58 19.75 ?  4   ASN   B H    1 
ATOM   4118 H  H    B ASN   B 1 4   ? 46.998 -15.586 -16.829 0.42 19.75 ?  4   ASN   B H    1 
ATOM   4119 H  HA   . ASN   B 1 4   ? 45.398 -16.922 -16.522 1.00 18.50 ?  4   ASN   B HA   1 
ATOM   4120 H  HB2  . ASN   B 1 4   ? 43.832 -15.023 -17.902 1.00 18.07 ?  4   ASN   B HB2  1 
ATOM   4121 H  HB3  . ASN   B 1 4   ? 43.220 -16.269 -17.130 1.00 18.07 ?  4   ASN   B HB3  1 
ATOM   4122 H  HD21 . ASN   B 1 4   ? 43.529 -13.037 -15.293 1.00 18.55 ?  4   ASN   B HD21 1 
ATOM   4123 H  HD22 . ASN   B 1 4   ? 43.377 -13.210 -16.765 1.00 18.55 ?  4   ASN   B HD22 1 
ATOM   4124 N  N    . SER   B 1 5   ? 46.372 -17.901 -18.886 1.00 16.88 ?  5   SER   B N    1 
ATOM   4125 C  CA   . SER   B 1 5   ? 46.470 -18.814 -20.025 1.00 19.50 ?  5   SER   B CA   1 
ATOM   4126 C  C    . SER   B 1 5   ? 46.449 -20.236 -19.477 1.00 20.88 ?  5   SER   B C    1 
ATOM   4127 O  O    . SER   B 1 5   ? 47.470 -20.912 -19.375 1.00 22.92 ?  5   SER   B O    1 
ATOM   4128 C  CB   . SER   B 1 5   ? 47.730 -18.528 -20.839 1.00 21.17 ?  5   SER   B CB   1 
ATOM   4129 O  OG   . SER   B 1 5   ? 48.892 -18.692 -20.044 1.00 24.02 ?  5   SER   B OG   1 
ATOM   4130 H  H    . SER   B 1 5   ? 47.126 -17.753 -18.497 1.00 20.26 ?  5   SER   B H    1 
ATOM   4131 H  HA   . SER   B 1 5   ? 45.699 -18.696 -20.600 1.00 23.40 ?  5   SER   B HA   1 
ATOM   4132 H  HB2  . SER   B 1 5   ? 47.760 -19.139 -21.595 1.00 25.40 ?  5   SER   B HB2  1 
ATOM   4133 H  HB3  . SER   B 1 5   ? 47.683 -17.614 -21.159 1.00 25.40 ?  5   SER   B HB3  1 
ATOM   4134 H  HG   . SER   B 1 5   ? 48.952 -19.490 -19.791 1.00 28.82 ?  5   SER   B HG   1 
ATOM   4135 N  N    . PHE   B 1 6   ? 45.255 -20.676 -19.096 1.00 21.43 ?  6   PHE   B N    1 
ATOM   4136 C  CA   . PHE   B 1 6   ? 45.067 -22.016 -18.558 1.00 20.86 ?  6   PHE   B CA   1 
ATOM   4137 C  C    . PHE   B 1 6   ? 44.989 -23.005 -19.711 1.00 24.53 ?  6   PHE   B C    1 
ATOM   4138 O  O    . PHE   B 1 6   ? 44.317 -22.744 -20.713 1.00 26.49 ?  6   PHE   B O    1 
ATOM   4139 C  CB   . PHE   B 1 6   ? 43.781 -22.070 -17.733 1.00 19.12 ?  6   PHE   B CB   1 
ATOM   4140 C  CG   . PHE   B 1 6   ? 43.810 -21.208 -16.499 1.00 16.91 ?  6   PHE   B CG   1 
ATOM   4141 C  CD1  . PHE   B 1 6   ? 44.319 -21.695 -15.313 1.00 15.70 ?  6   PHE   B CD1  1 
ATOM   4142 C  CD2  . PHE   B 1 6   ? 43.330 -19.907 -16.530 1.00 16.18 ?  6   PHE   B CD2  1 
ATOM   4143 C  CE1  . PHE   B 1 6   ? 44.332 -20.909 -14.171 1.00 15.36 ?  6   PHE   B CE1  1 
ATOM   4144 C  CE2  . PHE   B 1 6   ? 43.351 -19.110 -15.398 1.00 17.00 ?  6   PHE   B CE2  1 
ATOM   4145 C  CZ   . PHE   B 1 6   ? 43.853 -19.605 -14.221 1.00 15.91 ?  6   PHE   B CZ   1 
ATOM   4146 H  H    . PHE   B 1 6   ? 44.528 -20.220 -19.149 1.00 25.72 ?  6   PHE   B H    1 
ATOM   4147 H  HA   . PHE   B 1 6   ? 45.814 -22.257 -17.993 1.00 25.03 ?  6   PHE   B HA   1 
ATOM   4148 H  HB2  . PHE   B 1 6   ? 43.041 -21.771 -18.285 1.00 22.94 ?  6   PHE   B HB2  1 
ATOM   4149 H  HB3  . PHE   B 1 6   ? 43.627 -22.986 -17.450 1.00 22.94 ?  6   PHE   B HB3  1 
ATOM   4150 H  HD1  . PHE   B 1 6   ? 44.645 -22.567 -15.274 1.00 18.84 ?  6   PHE   B HD1  1 
ATOM   4151 H  HD2  . PHE   B 1 6   ? 42.985 -19.570 -17.322 1.00 19.41 ?  6   PHE   B HD2  1 
ATOM   4152 H  HE1  . PHE   B 1 6   ? 44.685 -21.241 -13.374 1.00 18.43 ?  6   PHE   B HE1  1 
ATOM   4153 H  HE2  . PHE   B 1 6   ? 43.022 -18.242 -15.436 1.00 20.40 ?  6   PHE   B HE2  1 
ATOM   4154 H  HZ   . PHE   B 1 6   ? 43.870 -19.072 -13.458 1.00 19.09 ?  6   PHE   B HZ   1 
ATOM   4155 N  N    . SER   B 1 7   ? 45.696 -24.128 -19.580 1.00 25.67 ?  7   SER   B N    1 
ATOM   4156 C  CA   . SER   B 1 7   ? 45.771 -25.121 -20.642 1.00 28.82 ?  7   SER   B CA   1 
ATOM   4157 C  C    . SER   B 1 7   ? 45.716 -26.524 -20.057 1.00 27.94 ?  7   SER   B C    1 
ATOM   4158 O  O    . SER   B 1 7   ? 46.320 -26.799 -19.017 1.00 28.65 ?  7   SER   B O    1 
ATOM   4159 C  CB   . SER   B 1 7   ? 47.062 -24.955 -21.455 1.00 32.00 ?  7   SER   B CB   1 
ATOM   4160 O  OG   . SER   B 1 7   ? 47.049 -25.781 -22.606 1.00 34.16 ?  7   SER   B OG   1 
ATOM   4161 H  H    . SER   B 1 7   ? 46.155 -24.332 -18.878 1.00 30.81 ?  7   SER   B H    1 
ATOM   4162 H  HA   . SER   B 1 7   ? 45.019 -25.014 -21.239 1.00 34.58 ?  7   SER   B HA   1 
ATOM   4163 H  HB2  . SER   B 1 7   ? 47.142 -24.029 -21.734 1.00 38.40 ?  7   SER   B HB2  1 
ATOM   4164 H  HB3  . SER   B 1 7   ? 47.820 -25.199 -20.900 1.00 38.40 ?  7   SER   B HB3  1 
ATOM   4165 H  HG   . SER   B 1 7   ? 47.761 -25.680 -23.040 1.00 40.99 ?  7   SER   B HG   1 
ATOM   4166 N  N    . GLY   B 1 8   ? 44.999 -27.410 -20.745 1.00 27.33 ?  8   GLY   B N    1 
ATOM   4167 C  CA   . GLY   B 1 8   ? 44.957 -28.803 -20.360 1.00 26.35 ?  8   GLY   B CA   1 
ATOM   4168 C  C    . GLY   B 1 8   ? 44.018 -29.128 -19.229 1.00 24.73 ?  8   GLY   B C    1 
ATOM   4169 O  O    . GLY   B 1 8   ? 44.159 -30.192 -18.614 1.00 26.15 ?  8   GLY   B O    1 
ATOM   4170 H  H    . GLY   B 1 8   ? 44.535 -27.221 -21.441 1.00 32.80 ?  8   GLY   B H    1 
ATOM   4171 H  HA2  . GLY   B 1 8   ? 44.692 -29.332 -21.126 1.00 31.62 ?  8   GLY   B HA2  1 
ATOM   4172 H  HA3  . GLY   B 1 8   ? 45.843 -29.084 -20.090 1.00 31.62 ?  8   GLY   B HA3  1 
ATOM   4173 N  N    . TYR   B 1 9   ? 43.050 -28.261 -18.937 1.00 22.77 ?  9   TYR   B N    1 
ATOM   4174 C  CA   . TYR   B 1 9   ? 42.096 -28.536 -17.876 1.00 20.66 ?  9   TYR   B CA   1 
ATOM   4175 C  C    . TYR   B 1 9   ? 40.919 -29.340 -18.396 1.00 20.14 ?  9   TYR   B C    1 
ATOM   4176 O  O    . TYR   B 1 9   ? 40.511 -29.217 -19.556 1.00 21.81 ?  9   TYR   B O    1 
ATOM   4177 C  CB   . TYR   B 1 9   ? 41.581 -27.249 -17.238 1.00 19.89 ?  9   TYR   B CB   1 
ATOM   4178 C  CG   . TYR   B 1 9   ? 42.603 -26.614 -16.331 1.00 19.21 ?  9   TYR   B CG   1 
ATOM   4179 C  CD1  . TYR   B 1 9   ? 43.686 -25.928 -16.856 1.00 19.65 ?  9   TYR   B CD1  1 
ATOM   4180 C  CD2  . TYR   B 1 9   ? 42.507 -26.734 -14.953 1.00 18.56 ?  9   TYR   B CD2  1 
ATOM   4181 C  CE1  . TYR   B 1 9   ? 44.638 -25.364 -16.038 1.00 19.96 ?  9   TYR   B CE1  1 
ATOM   4182 C  CE2  . TYR   B 1 9   ? 43.455 -26.168 -14.122 1.00 18.64 ?  9   TYR   B CE2  1 
ATOM   4183 C  CZ   . TYR   B 1 9   ? 44.519 -25.483 -14.674 1.00 19.49 ?  9   TYR   B CZ   1 
ATOM   4184 O  OH   . TYR   B 1 9   ? 45.472 -24.927 -13.861 1.00 20.11 ?  9   TYR   B OH   1 
ATOM   4185 H  H    . TYR   B 1 9   ? 42.912 -27.519 -19.352 1.00 27.32 ?  9   TYR   B H    1 
ATOM   4186 H  HA   . TYR   B 1 9   ? 42.526 -29.057 -17.188 1.00 24.79 ?  9   TYR   B HA   1 
ATOM   4187 H  HB2  . TYR   B 1 9   ? 41.348 -26.608 -17.930 1.00 23.87 ?  9   TYR   B HB2  1 
ATOM   4188 H  HB3  . TYR   B 1 9   ? 40.805 -27.465 -16.705 1.00 23.87 ?  9   TYR   B HB3  1 
ATOM   4189 H  HD1  . TYR   B 1 9   ? 43.768 -25.848 -17.778 1.00 23.58 ?  9   TYR   B HD1  1 
ATOM   4190 H  HD2  . TYR   B 1 9   ? 41.787 -27.200 -14.581 1.00 22.27 ?  9   TYR   B HD2  1 
ATOM   4191 H  HE1  . TYR   B 1 9   ? 45.352 -24.906 -16.405 1.00 23.96 ?  9   TYR   B HE1  1 
ATOM   4192 H  HE2  . TYR   B 1 9   ? 43.372 -26.256 -13.197 1.00 22.37 ?  9   TYR   B HE2  1 
ATOM   4193 H  HH   . TYR   B 1 9   ? 46.054 -24.543 -14.325 1.00 24.13 ?  9   TYR   B HH   1 
ATOM   4194 N  N    . LEU   B 1 10  ? 40.389 -30.181 -17.518 1.00 18.28 ?  10  LEU   B N    1 
ATOM   4195 C  CA   . LEU   B 1 10  ? 39.181 -30.939 -17.785 1.00 18.12 ?  10  LEU   B CA   1 
ATOM   4196 C  C    . LEU   B 1 10  ? 37.997 -30.167 -17.221 1.00 17.56 ?  10  LEU   B C    1 
ATOM   4197 O  O    . LEU   B 1 10  ? 38.017 -29.748 -16.059 1.00 17.29 ?  10  LEU   B O    1 
ATOM   4198 C  CB   . LEU   B 1 10  ? 39.282 -32.304 -17.108 1.00 19.07 ?  10  LEU   B CB   1 
ATOM   4199 C  CG   . LEU   B 1 10  ? 38.141 -33.265 -17.418 1.00 21.06 ?  10  LEU   B CG   1 
ATOM   4200 C  CD1  . LEU   B 1 10  ? 38.236 -33.757 -18.856 1.00 22.31 ?  10  LEU   B CD1  1 
ATOM   4201 C  CD2  . LEU   B 1 10  ? 38.140 -34.431 -16.445 1.00 22.13 ?  10  LEU   B CD2  1 
ATOM   4202 H  H    . LEU   B 1 10  ? 40.716 -30.331 -16.731 1.00 21.93 ?  10  LEU   B H    1 
ATOM   4203 H  HA   . LEU   B 1 10  ? 39.062 -31.062 -18.737 1.00 21.75 ?  10  LEU   B HA   1 
ATOM   4204 H  HB2  . LEU   B 1 10  ? 40.106 -32.732 -17.393 1.00 22.89 ?  10  LEU   B HB2  1 
ATOM   4205 H  HB3  . LEU   B 1 10  ? 39.300 -32.176 -16.146 1.00 22.89 ?  10  LEU   B HB3  1 
ATOM   4206 H  HG   . LEU   B 1 10  ? 37.296 -32.798 -17.320 1.00 25.27 ?  10  LEU   B HG   1 
ATOM   4207 H  HD11 . LEU   B 1 10  ? 37.544 -34.418 -19.009 1.00 26.77 ?  10  LEU   B HD11 1 
ATOM   4208 H  HD12 . LEU   B 1 10  ? 38.113 -33.004 -19.455 1.00 26.77 ?  10  LEU   B HD12 1 
ATOM   4209 H  HD13 . LEU   B 1 10  ? 39.110 -34.152 -18.995 1.00 26.77 ?  10  LEU   B HD13 1 
ATOM   4210 H  HD21 . LEU   B 1 10  ? 37.407 -35.025 -16.668 1.00 26.56 ?  10  LEU   B HD21 1 
ATOM   4211 H  HD22 . LEU   B 1 10  ? 38.984 -34.899 -16.517 1.00 26.56 ?  10  LEU   B HD22 1 
ATOM   4212 H  HD23 . LEU   B 1 10  ? 38.026 -34.086 -15.546 1.00 26.56 ?  10  LEU   B HD23 1 
ATOM   4213 N  N    . LYS   B 1 11  ? 36.973 -29.983 -18.045 1.00 18.90 ?  11  LYS   B N    1 
ATOM   4214 C  CA   . LYS   B 1 11  ? 35.777 -29.267 -17.631 1.00 20.66 ?  11  LYS   B CA   1 
ATOM   4215 C  C    . LYS   B 1 11  ? 34.903 -30.194 -16.793 1.00 19.58 ?  11  LYS   B C    1 
ATOM   4216 O  O    . LYS   B 1 11  ? 34.526 -31.280 -17.249 1.00 21.43 ?  11  LYS   B O    1 
ATOM   4217 C  CB   . LYS   B 1 11  ? 35.026 -28.799 -18.876 1.00 24.66 ?  11  LYS   B CB   1 
ATOM   4218 C  CG   . LYS   B 1 11  ? 33.867 -27.857 -18.620 1.00 28.28 ?  11  LYS   B CG   1 
ATOM   4219 C  CD   . LYS   B 1 11  ? 33.120 -27.577 -19.919 1.00 31.20 ?  11  LYS   B CD   1 
ATOM   4220 C  CE   . LYS   B 1 11  ? 32.118 -26.449 -19.764 1.00 33.32 ?  11  LYS   B CE   1 
ATOM   4221 N  NZ   . LYS   B 1 11  ? 32.791 -25.131 -19.612 1.00 34.57 ?  11  LYS   B NZ   1 
ATOM   4222 H  H    . LYS   B 1 11  ? 36.946 -30.266 -18.858 1.00 22.68 ?  11  LYS   B H    1 
ATOM   4223 H  HA   . LYS   B 1 11  ? 36.022 -28.493 -17.099 1.00 24.79 ?  11  LYS   B HA   1 
ATOM   4224 H  HB2  . LYS   B 1 11  ? 35.652 -28.336 -19.456 1.00 29.59 ?  11  LYS   B HB2  1 
ATOM   4225 H  HB3  . LYS   B 1 11  ? 34.673 -29.576 -19.334 1.00 29.59 ?  11  LYS   B HB3  1 
ATOM   4226 H  HG2  . LYS   B 1 11  ? 33.250 -28.265 -17.993 1.00 33.93 ?  11  LYS   B HG2  1 
ATOM   4227 H  HG3  . LYS   B 1 11  ? 34.202 -27.017 -18.270 1.00 33.93 ?  11  LYS   B HG3  1 
ATOM   4228 H  HD2  . LYS   B 1 11  ? 33.760 -27.324 -20.604 1.00 37.44 ?  11  LYS   B HD2  1 
ATOM   4229 H  HD3  . LYS   B 1 11  ? 32.641 -28.376 -20.189 1.00 37.44 ?  11  LYS   B HD3  1 
ATOM   4230 H  HE2  . LYS   B 1 11  ? 31.553 -26.413 -20.552 1.00 39.99 ?  11  LYS   B HE2  1 
ATOM   4231 H  HE3  . LYS   B 1 11  ? 31.579 -26.614 -18.975 1.00 39.99 ?  11  LYS   B HE3  1 
ATOM   4232 H  HZ1  . LYS   B 1 11  ? 32.183 -24.486 -19.534 1.00 41.48 ?  11  LYS   B HZ1  1 
ATOM   4233 H  HZ2  . LYS   B 1 11  ? 33.305 -25.134 -18.887 1.00 41.48 ?  11  LYS   B HZ2  1 
ATOM   4234 H  HZ3  . LYS   B 1 11  ? 33.298 -24.965 -20.326 1.00 41.48 ?  11  LYS   B HZ3  1 
ATOM   4235 N  N    . LEU   B 1 12  ? 34.577 -29.770 -15.571 1.00 18.06 ?  12  LEU   B N    1 
ATOM   4236 C  CA   . LEU   B 1 12  ? 33.623 -30.486 -14.731 1.00 17.59 ?  12  LEU   B CA   1 
ATOM   4237 C  C    . LEU   B 1 12  ? 32.233 -29.879 -14.816 1.00 17.73 ?  12  LEU   B C    1 
ATOM   4238 O  O    . LEU   B 1 12  ? 31.248 -30.596 -14.985 1.00 18.53 ?  12  LEU   B O    1 
ATOM   4239 C  CB   . LEU   B 1 12  ? 34.086 -30.510 -13.270 1.00 17.15 ?  12  LEU   B CB   1 
ATOM   4240 C  CG   . LEU   B 1 12  ? 35.435 -31.178 -13.009 1.00 17.05 ?  12  LEU   B CG   1 
ATOM   4241 C  CD1  . LEU   B 1 12  ? 35.784 -31.126 -11.535 1.00 17.32 ?  12  LEU   B CD1  1 
ATOM   4242 C  CD2  . LEU   B 1 12  ? 35.434 -32.616 -13.508 1.00 17.89 ?  12  LEU   B CD2  1 
ATOM   4243 H  H    . LEU   B 1 12  ? 34.895 -29.056 -15.204 1.00 21.68 ?  12  LEU   B H    1 
ATOM   4244 H  HA   . LEU   B 1 12  ? 33.556 -31.399 -15.041 1.00 21.11 ?  12  LEU   B HA   1 
ATOM   4245 H  HB2  . LEU   B 1 12  ? 34.143 -29.598 -12.952 1.00 20.58 ?  12  LEU   B HB2  1 
ATOM   4246 H  HB3  . LEU   B 1 12  ? 33.419 -30.991 -12.750 1.00 20.58 ?  12  LEU   B HB3  1 
ATOM   4247 H  HG   . LEU   B 1 12  ? 36.120 -30.694 -13.495 1.00 20.45 ?  12  LEU   B HG   1 
ATOM   4248 H  HD11 . LEU   B 1 12  ? 36.648 -31.553 -11.400 1.00 20.78 ?  12  LEU   B HD11 1 
ATOM   4249 H  HD12 . LEU   B 1 12  ? 35.828 -30.200 -11.250 1.00 20.78 ?  12  LEU   B HD12 1 
ATOM   4250 H  HD13 . LEU   B 1 12  ? 35.104 -31.597 -11.029 1.00 20.78 ?  12  LEU   B HD13 1 
ATOM   4251 H  HD21 . LEU   B 1 12  ? 36.242 -33.057 -13.205 1.00 21.46 ?  12  LEU   B HD21 1 
ATOM   4252 H  HD22 . LEU   B 1 12  ? 34.654 -33.073 -13.156 1.00 21.46 ?  12  LEU   B HD22 1 
ATOM   4253 H  HD23 . LEU   B 1 12  ? 35.403 -32.615 -14.479 1.00 21.46 ?  12  LEU   B HD23 1 
ATOM   4254 N  N    . THR   B 1 13  ? 32.148 -28.560 -14.704 1.00 17.42 ?  13  THR   B N    1 
ATOM   4255 C  CA   . THR   B 1 13  ? 30.924 -27.807 -14.909 1.00 17.56 ?  13  THR   B CA   1 
ATOM   4256 C  C    . THR   B 1 13  ? 31.259 -26.613 -15.794 1.00 19.30 ?  13  THR   B C    1 
ATOM   4257 O  O    . THR   B 1 13  ? 32.403 -26.426 -16.219 1.00 19.90 ?  13  THR   B O    1 
ATOM   4258 C  CB   . THR   B 1 13  ? 30.323 -27.337 -13.579 1.00 17.08 ?  13  THR   B CB   1 
ATOM   4259 O  OG1  . THR   B 1 13  ? 31.161 -26.318 -13.026 1.00 16.89 ?  13  THR   B OG1  1 
ATOM   4260 C  CG2  . THR   B 1 13  ? 30.202 -28.496 -12.588 1.00 17.41 ?  13  THR   B CG2  1 
ATOM   4261 H  H    . THR   B 1 13  ? 32.817 -28.058 -14.502 1.00 20.90 ?  13  THR   B H    1 
ATOM   4262 H  HA   . THR   B 1 13  ? 30.270 -28.360 -15.360 1.00 21.08 ?  13  THR   B HA   1 
ATOM   4263 H  HB   . THR   B 1 13  ? 29.434 -26.973 -13.734 1.00 20.49 ?  13  THR   B HB   1 
ATOM   4264 H  HG1  . THR   B 1 13  ? 30.867 -25.552 -13.238 1.00 20.26 ?  13  THR   B HG1  1 
ATOM   4265 H  HG21 . THR   B 1 13  ? 29.717 -28.212 -11.797 1.00 20.89 ?  13  THR   B HG21 1 
ATOM   4266 H  HG22 . THR   B 1 13  ? 29.723 -29.234 -13.000 1.00 20.89 ?  13  THR   B HG22 1 
ATOM   4267 H  HG23 . THR   B 1 13  ? 31.083 -28.803 -12.324 1.00 20.89 ?  13  THR   B HG23 1 
ATOM   4268 N  N    A ASP   B 1 14  ? 30.248 -25.789 -16.063 0.58 20.36 ?  14  ASP   B N    1 
ATOM   4269 N  N    B ASP   B 1 14  ? 30.252 -25.779 -16.059 0.42 20.23 ?  14  ASP   B N    1 
ATOM   4270 C  CA   A ASP   B 1 14  ? 30.465 -24.632 -16.922 0.58 21.51 ?  14  ASP   B CA   1 
ATOM   4271 C  CA   B ASP   B 1 14  ? 30.453 -24.623 -16.926 0.42 21.12 ?  14  ASP   B CA   1 
ATOM   4272 C  C    A ASP   B 1 14  ? 31.569 -23.728 -16.386 0.58 19.44 ?  14  ASP   B C    1 
ATOM   4273 C  C    B ASP   B 1 14  ? 31.427 -23.605 -16.352 0.42 19.20 ?  14  ASP   B C    1 
ATOM   4274 O  O    A ASP   B 1 14  ? 32.265 -23.075 -17.172 0.58 20.24 ?  14  ASP   B O    1 
ATOM   4275 O  O    B ASP   B 1 14  ? 31.841 -22.701 -17.086 0.42 19.62 ?  14  ASP   B O    1 
ATOM   4276 C  CB   A ASP   B 1 14  ? 29.159 -23.855 -17.100 0.58 24.82 ?  14  ASP   B CB   1 
ATOM   4277 C  CB   B ASP   B 1 14  ? 29.128 -23.916 -17.202 0.42 23.94 ?  14  ASP   B CB   1 
ATOM   4278 C  CG   A ASP   B 1 14  ? 28.182 -24.549 -18.026 0.58 27.87 ?  14  ASP   B CG   1 
ATOM   4279 C  CG   B ASP   B 1 14  ? 28.279 -24.652 -18.220 0.42 26.45 ?  14  ASP   B CG   1 
ATOM   4280 O  OD1  A ASP   B 1 14  ? 28.524 -25.602 -18.611 0.58 28.85 ?  14  ASP   B OD1  1 
ATOM   4281 O  OD1  B ASP   B 1 14  ? 28.859 -25.319 -19.104 0.42 27.31 ?  14  ASP   B OD1  1 
ATOM   4282 O  OD2  A ASP   B 1 14  ? 27.053 -24.034 -18.160 0.58 29.12 -1 14  ASP   B OD2  1 
ATOM   4283 O  OD2  B ASP   B 1 14  ? 27.035 -24.571 -18.138 0.42 27.42 -1 14  ASP   B OD2  1 
ATOM   4284 H  H    A ASP   B 1 14  ? 29.451 -25.866 -15.755 0.58 24.43 ?  14  ASP   B H    1 
ATOM   4285 H  H    B ASP   B 1 14  ? 29.456 -25.854 -15.746 0.42 24.28 ?  14  ASP   B H    1 
ATOM   4286 H  HA   A ASP   B 1 14  ? 30.750 -24.931 -17.793 0.58 25.81 ?  14  ASP   B HA   1 
ATOM   4287 H  HA   B ASP   B 1 14  ? 30.805 -24.933 -17.775 0.42 25.35 ?  14  ASP   B HA   1 
ATOM   4288 H  HB2  A ASP   B 1 14  ? 28.710 -23.771 -16.248 0.58 29.78 ?  14  ASP   B HB2  1 
ATOM   4289 H  HB2  B ASP   B 1 14  ? 28.628 -23.851 -16.373 0.42 28.73 ?  14  ASP   B HB2  1 
ATOM   4290 H  HB3  A ASP   B 1 14  ? 29.347 -22.980 -17.471 0.58 29.78 ?  14  ASP   B HB3  1 
ATOM   4291 H  HB3  B ASP   B 1 14  ? 29.316 -23.021 -17.541 0.42 28.73 ?  14  ASP   B HB3  1 
ATOM   4292 N  N    . ASN   B 1 15  ? 31.768 -23.698 -15.064 1.00 17.36 ?  15  ASN   B N    1 
ATOM   4293 C  CA   . ASN   B 1 15  ? 32.726 -22.780 -14.458 1.00 15.05 ?  15  ASN   B CA   1 
ATOM   4294 C  C    . ASN   B 1 15  ? 33.818 -23.439 -13.622 1.00 14.19 ?  15  ASN   B C    1 
ATOM   4295 O  O    . ASN   B 1 15  ? 34.663 -22.714 -13.085 1.00 14.21 ?  15  ASN   B O    1 
ATOM   4296 C  CB   . ASN   B 1 15  ? 32.008 -21.730 -13.594 1.00 15.25 ?  15  ASN   B CB   1 
ATOM   4297 C  CG   . ASN   B 1 15  ? 31.396 -22.332 -12.349 1.00 15.05 ?  15  ASN   B CG   1 
ATOM   4298 O  OD1  . ASN   B 1 15  ? 30.458 -23.128 -12.432 1.00 16.72 ?  15  ASN   B OD1  1 
ATOM   4299 N  ND2  . ASN   B 1 15  ? 31.925 -21.982 -11.194 1.00 14.02 ?  15  ASN   B ND2  1 
ATOM   4300 H  H    A ASN   B 1 15  ? 31.367 -24.213 -14.501 0.58 20.83 ?  15  ASN   B H    1 
ATOM   4301 H  H    B ASN   B 1 15  ? 31.422 -24.262 -14.512 0.42 20.83 ?  15  ASN   B H    1 
ATOM   4302 H  HA   . ASN   B 1 15  ? 33.174 -22.295 -15.159 1.00 18.06 ?  15  ASN   B HA   1 
ATOM   4303 H  HB2  . ASN   B 1 15  ? 32.653 -21.049 -13.318 1.00 18.30 ?  15  ASN   B HB2  1 
ATOM   4304 H  HB3  . ASN   B 1 15  ? 31.300 -21.312 -14.112 1.00 18.30 ?  15  ASN   B HB3  1 
ATOM   4305 H  HD21 . ASN   B 1 15  ? 31.607 -22.294 -10.455 1.00 16.82 ?  15  ASN   B HD21 1 
ATOM   4306 H  HD22 . ASN   B 1 15  ? 32.589 -21.428 -11.164 1.00 16.82 ?  15  ASN   B HD22 1 
ATOM   4307 N  N    . VAL   B 1 16  ? 33.838 -24.766 -13.486 1.00 14.04 ?  16  VAL   B N    1 
ATOM   4308 C  CA   . VAL   B 1 16  ? 34.834 -25.459 -12.672 1.00 13.87 ?  16  VAL   B CA   1 
ATOM   4309 C  C    . VAL   B 1 16  ? 35.629 -26.394 -13.566 1.00 14.14 ?  16  VAL   B C    1 
ATOM   4310 O  O    . VAL   B 1 16  ? 35.058 -27.281 -14.220 1.00 14.82 ?  16  VAL   B O    1 
ATOM   4311 C  CB   . VAL   B 1 16  ? 34.204 -26.228 -11.502 1.00 14.28 ?  16  VAL   B CB   1 
ATOM   4312 C  CG1  . VAL   B 1 16  ? 35.288 -26.963 -10.711 1.00 14.10 ?  16  VAL   B CG1  1 
ATOM   4313 C  CG2  . VAL   B 1 16  ? 33.407 -25.287 -10.607 1.00 15.16 ?  16  VAL   B CG2  1 
ATOM   4314 H  H    . VAL   B 1 16  ? 33.266 -25.296 -13.864 1.00 16.85 ?  16  VAL   B H    1 
ATOM   4315 H  HA   . VAL   B 1 16  ? 35.443 -24.805 -12.299 1.00 16.64 ?  16  VAL   B HA   1 
ATOM   4316 H  HB   . VAL   B 1 16  ? 33.592 -26.896 -11.857 1.00 17.14 ?  16  VAL   B HB   1 
ATOM   4317 H  HG11 . VAL   B 1 16  ? 34.913 -27.256 -9.865  1.00 16.92 ?  16  VAL   B HG11 1 
ATOM   4318 H  HG12 . VAL   B 1 16  ? 35.592 -27.729 -11.220 1.00 16.92 ?  16  VAL   B HG12 1 
ATOM   4319 H  HG13 . VAL   B 1 16  ? 36.025 -26.354 -10.551 1.00 16.92 ?  16  VAL   B HG13 1 
ATOM   4320 H  HG21 . VAL   B 1 16  ? 33.062 -25.789 -9.851  1.00 18.20 ?  16  VAL   B HG21 1 
ATOM   4321 H  HG22 . VAL   B 1 16  ? 33.989 -24.579 -10.298 1.00 18.20 ?  16  VAL   B HG22 1 
ATOM   4322 H  HG23 . VAL   B 1 16  ? 32.672 -24.914 -11.119 1.00 18.20 ?  16  VAL   B HG23 1 
ATOM   4323 N  N    . TYR   B 1 17  ? 36.950 -26.223 -13.543 1.00 14.17 ?  17  TYR   B N    1 
ATOM   4324 C  CA   . TYR   B 1 17  ? 37.899 -26.968 -14.352 1.00 14.55 ?  17  TYR   B CA   1 
ATOM   4325 C  C    . TYR   B 1 17  ? 38.948 -27.578 -13.432 1.00 13.83 ?  17  TYR   B C    1 
ATOM   4326 O  O    . TYR   B 1 17  ? 39.220 -27.053 -12.350 1.00 14.14 ?  17  TYR   B O    1 
ATOM   4327 C  CB   . TYR   B 1 17  ? 38.607 -26.044 -15.348 1.00 16.99 ?  17  TYR   B CB   1 
ATOM   4328 C  CG   . TYR   B 1 17  ? 37.681 -25.277 -16.260 1.00 20.00 ?  17  TYR   B CG   1 
ATOM   4329 C  CD1  . TYR   B 1 17  ? 37.077 -24.097 -15.845 1.00 21.32 ?  17  TYR   B CD1  1 
ATOM   4330 C  CD2  . TYR   B 1 17  ? 37.406 -25.739 -17.540 1.00 21.91 ?  17  TYR   B CD2  1 
ATOM   4331 C  CE1  . TYR   B 1 17  ? 36.227 -23.394 -16.682 1.00 22.84 ?  17  TYR   B CE1  1 
ATOM   4332 C  CE2  . TYR   B 1 17  ? 36.564 -25.044 -18.385 1.00 23.36 ?  17  TYR   B CE2  1 
ATOM   4333 C  CZ   . TYR   B 1 17  ? 35.974 -23.874 -17.950 1.00 23.88 ?  17  TYR   B CZ   1 
ATOM   4334 O  OH   . TYR   B 1 17  ? 35.134 -23.183 -18.790 1.00 25.39 ?  17  TYR   B OH   1 
ATOM   4335 H  H    . TYR   B 1 17  ? 37.343 -25.645 -13.034 1.00 17.00 ?  17  TYR   B H    1 
ATOM   4336 H  HA   . TYR   B 1 17  ? 37.441 -27.677 -14.838 1.00 17.46 ?  17  TYR   B HA   1 
ATOM   4337 H  HB2  . TYR   B 1 17  ? 39.143 -25.404 -14.856 1.00 20.38 ?  17  TYR   B HB2  1 
ATOM   4338 H  HB3  . TYR   B 1 17  ? 39.177 -26.585 -15.911 1.00 20.38 ?  17  TYR   B HB3  1 
ATOM   4339 H  HD1  . TYR   B 1 17  ? 37.247 -23.771 -14.992 1.00 25.58 ?  17  TYR   B HD1  1 
ATOM   4340 H  HD2  . TYR   B 1 17  ? 37.800 -26.525 -17.838 1.00 26.29 ?  17  TYR   B HD2  1 
ATOM   4341 H  HE1  . TYR   B 1 17  ? 35.829 -22.603 -16.394 1.00 27.41 ?  17  TYR   B HE1  1 
ATOM   4342 H  HE2  . TYR   B 1 17  ? 36.386 -25.365 -19.241 1.00 28.03 ?  17  TYR   B HE2  1 
ATOM   4343 H  HH   . TYR   B 1 17  ? 35.062 -23.580 -19.528 1.00 30.47 ?  17  TYR   B HH   1 
ATOM   4344 N  N    . ILE   B 1 18  ? 39.563 -28.678 -13.866 1.00 13.87 ?  18  ILE   B N    1 
ATOM   4345 C  CA   . ILE   B 1 18  ? 40.486 -29.410 -13.004 1.00 13.97 ?  18  ILE   B CA   1 
ATOM   4346 C  C    . ILE   B 1 18  ? 41.643 -29.965 -13.823 1.00 14.51 ?  18  ILE   B C    1 
ATOM   4347 O  O    . ILE   B 1 18  ? 41.484 -30.352 -14.985 1.00 15.91 ?  18  ILE   B O    1 
ATOM   4348 C  CB   . ILE   B 1 18  ? 39.741 -30.514 -12.206 1.00 14.50 ?  18  ILE   B CB   1 
ATOM   4349 C  CG1  . ILE   B 1 18  ? 40.606 -31.051 -11.060 1.00 14.75 ?  18  ILE   B CG1  1 
ATOM   4350 C  CG2  . ILE   B 1 18  ? 39.245 -31.639 -13.133 1.00 14.82 ?  18  ILE   B CG2  1 
ATOM   4351 C  CD1  . ILE   B 1 18  ? 39.807 -31.852 -10.038 1.00 16.23 ?  18  ILE   B CD1  1 
ATOM   4352 H  H    . ILE   B 1 18  ? 39.457 -29.026 -14.645 1.00 16.64 ?  18  ILE   B H    1 
ATOM   4353 H  HA   . ILE   B 1 18  ? 40.851 -28.796 -12.352 1.00 16.77 ?  18  ILE   B HA   1 
ATOM   4354 H  HB   . ILE   B 1 18  ? 38.956 -30.114 -11.801 1.00 17.40 ?  18  ILE   B HB   1 
ATOM   4355 H  HG12 . ILE   B 1 18  ? 41.292 -31.631 -11.421 1.00 17.70 ?  18  ILE   B HG12 1 
ATOM   4356 H  HG13 . ILE   B 1 18  ? 41.012 -30.302 -10.595 1.00 17.70 ?  18  ILE   B HG13 1 
ATOM   4357 H  HG21 . ILE   B 1 18  ? 38.660 -32.230 -12.630 1.00 17.78 ?  18  ILE   B HG21 1 
ATOM   4358 H  HG22 . ILE   B 1 18  ? 38.753 -31.239 -13.867 1.00 17.78 ?  18  ILE   B HG22 1 
ATOM   4359 H  HG23 . ILE   B 1 18  ? 40.005 -32.132 -13.470 1.00 17.78 ?  18  ILE   B HG23 1 
ATOM   4360 H  HD11 . ILE   B 1 18  ? 40.400 -32.131 -9.321  1.00 19.48 ?  18  ILE   B HD11 1 
ATOM   4361 H  HD12 . ILE   B 1 18  ? 39.098 -31.294 -9.682  1.00 19.48 ?  18  ILE   B HD12 1 
ATOM   4362 H  HD13 . ILE   B 1 18  ? 39.428 -32.631 -10.474 1.00 19.48 ?  18  ILE   B HD13 1 
ATOM   4363 N  N    . LYS   B 1 19  ? 42.822 -29.997 -13.201 1.00 14.72 ?  19  LYS   B N    1 
ATOM   4364 C  CA   . LYS   B 1 19  ? 44.033 -30.465 -13.856 1.00 15.71 ?  19  LYS   B CA   1 
ATOM   4365 C  C    . LYS   B 1 19  ? 44.932 -31.143 -12.834 1.00 15.64 ?  19  LYS   B C    1 
ATOM   4366 O  O    . LYS   B 1 19  ? 45.019 -30.706 -11.684 1.00 15.06 ?  19  LYS   B O    1 
ATOM   4367 C  CB   . LYS   B 1 19  ? 44.799 -29.295 -14.486 1.00 17.00 ?  19  LYS   B CB   1 
ATOM   4368 C  CG   . LYS   B 1 19  ? 46.006 -29.699 -15.307 1.00 18.63 ?  19  LYS   B CG   1 
ATOM   4369 C  CD   . LYS   B 1 19  ? 46.720 -28.470 -15.846 1.00 20.47 ?  19  LYS   B CD   1 
ATOM   4370 C  CE   . LYS   B 1 19  ? 47.892 -28.846 -16.729 1.00 22.55 ?  19  LYS   B CE   1 
ATOM   4371 N  NZ   . LYS   B 1 19  ? 48.592 -27.648 -17.255 1.00 23.72 ?  19  LYS   B NZ   1 
ATOM   4372 H  H    . LYS   B 1 19  ? 42.936 -29.750 -12.382 1.00 17.66 ?  19  LYS   B H    1 
ATOM   4373 H  HA   . LYS   B 1 19  ? 43.800 -31.104 -14.548 1.00 18.85 ?  19  LYS   B HA   1 
ATOM   4374 H  HB2  . LYS   B 1 19  ? 44.193 -28.815 -15.069 1.00 20.40 ?  19  LYS   B HB2  1 
ATOM   4375 H  HB3  . LYS   B 1 19  ? 45.101 -28.708 -13.772 1.00 20.40 ?  19  LYS   B HB3  1 
ATOM   4376 H  HG2  . LYS   B 1 19  ? 46.621 -30.199 -14.749 1.00 22.35 ?  19  LYS   B HG2  1 
ATOM   4377 H  HG3  . LYS   B 1 19  ? 45.711 -30.243 -16.056 1.00 22.35 ?  19  LYS   B HG3  1 
ATOM   4378 H  HD2  . LYS   B 1 19  ? 46.096 -27.943 -16.370 1.00 24.57 ?  19  LYS   B HD2  1 
ATOM   4379 H  HD3  . LYS   B 1 19  ? 47.054 -27.945 -15.100 1.00 24.57 ?  19  LYS   B HD3  1 
ATOM   4380 H  HE2  . LYS   B 1 19  ? 48.525 -29.367 -16.211 1.00 27.05 ?  19  LYS   B HE2  1 
ATOM   4381 H  HE3  . LYS   B 1 19  ? 47.567 -29.365 -17.482 1.00 27.05 ?  19  LYS   B HE3  1 
ATOM   4382 H  HZ1  . LYS   B 1 19  ? 49.256 -27.896 -17.795 1.00 28.47 ?  19  LYS   B HZ1  1 
ATOM   4383 H  HZ2  . LYS   B 1 19  ? 48.024 -27.138 -17.714 1.00 28.47 ?  19  LYS   B HZ2  1 
ATOM   4384 H  HZ3  . LYS   B 1 19  ? 48.929 -27.171 -16.583 1.00 28.47 ?  19  LYS   B HZ3  1 
ATOM   4385 N  N    . ASN   B 1 20  ? 45.619 -32.194 -13.270 1.00 16.70 ?  20  ASN   B N    1 
ATOM   4386 C  CA   . ASN   B 1 20  ? 46.647 -32.829 -12.453 1.00 17.72 ?  20  ASN   B CA   1 
ATOM   4387 C  C    . ASN   B 1 20  ? 47.916 -32.006 -12.642 1.00 18.19 ?  20  ASN   B C    1 
ATOM   4388 O  O    . ASN   B 1 20  ? 48.555 -32.066 -13.696 1.00 20.03 ?  20  ASN   B O    1 
ATOM   4389 C  CB   . ASN   B 1 20  ? 46.816 -34.281 -12.894 1.00 19.49 ?  20  ASN   B CB   1 
ATOM   4390 C  CG   . ASN   B 1 20  ? 47.974 -34.987 -12.212 1.00 20.95 ?  20  ASN   B CG   1 
ATOM   4391 O  OD1  . ASN   B 1 20  ? 48.628 -35.839 -12.819 1.00 23.56 ?  20  ASN   B OD1  1 
ATOM   4392 N  ND2  . ASN   B 1 20  ? 48.223 -34.662 -10.953 1.00 20.66 ?  20  ASN   B ND2  1 
ATOM   4393 H  H    . ASN   B 1 20  ? 45.506 -32.560 -14.040 1.00 20.04 ?  20  ASN   B H    1 
ATOM   4394 H  HA   . ASN   B 1 20  ? 46.371 -32.812 -11.520 1.00 21.27 ?  20  ASN   B HA   1 
ATOM   4395 H  HB2  . ASN   B 1 20  ? 46.002 -34.771 -12.683 1.00 23.38 ?  20  ASN   B HB2  1 
ATOM   4396 H  HB3  . ASN   B 1 20  ? 46.971 -34.299 -13.849 1.00 23.38 ?  20  ASN   B HB3  1 
ATOM   4397 H  HD21 . ASN   B 1 20  ? 48.874 -35.034 -10.535 1.00 24.79 ?  20  ASN   B HD21 1 
ATOM   4398 H  HD22 . ASN   B 1 20  ? 47.747 -34.063 -10.554 1.00 24.79 ?  20  ASN   B HD22 1 
ATOM   4399 N  N    . ALA   B 1 21  ? 48.270 -31.207 -11.633 1.00 17.68 ?  21  ALA   B N    1 
ATOM   4400 C  CA   . ALA   B 1 21  ? 49.371 -30.272 -11.791 1.00 18.44 ?  21  ALA   B CA   1 
ATOM   4401 C  C    . ALA   B 1 21  ? 49.839 -29.778 -10.431 1.00 17.32 ?  21  ALA   B C    1 
ATOM   4402 O  O    . ALA   B 1 21  ? 49.100 -29.810 -9.440  1.00 16.94 ?  21  ALA   B O    1 
ATOM   4403 C  CB   . ALA   B 1 21  ? 48.962 -29.089 -12.669 1.00 19.52 ?  21  ALA   B CB   1 
ATOM   4404 H  H    . ALA   B 1 21  ? 47.886 -31.193 -10.853 1.00 21.22 ?  21  ALA   B H    1 
ATOM   4405 H  HA   . ALA   B 1 21  ? 50.109 -30.733 -12.214 1.00 22.13 ?  21  ALA   B HA   1 
ATOM   4406 H  HB1  . ALA   B 1 21  ? 49.744 -28.547 -12.828 1.00 23.42 ?  21  ALA   B HB1  1 
ATOM   4407 H  HB2  . ALA   B 1 21  ? 48.615 -29.434 -13.505 1.00 23.42 ?  21  ALA   B HB2  1 
ATOM   4408 H  HB3  . ALA   B 1 21  ? 48.278 -28.579 -12.210 1.00 23.42 ?  21  ALA   B HB3  1 
ATOM   4409 N  N    . ASP   B 1 22  ? 51.099 -29.340 -10.414 1.00 16.58 ?  22  ASP   B N    1 
ATOM   4410 C  CA   . ASP   B 1 22  ? 51.714 -28.644 -9.290  1.00 15.63 ?  22  ASP   B CA   1 
ATOM   4411 C  C    . ASP   B 1 22  ? 51.308 -27.173 -9.371  1.00 14.20 ?  22  ASP   B C    1 
ATOM   4412 O  O    . ASP   B 1 22  ? 51.616 -26.499 -10.357 1.00 14.52 ?  22  ASP   B O    1 
ATOM   4413 C  CB   . ASP   B 1 22  ? 53.232 -28.814 -9.445  1.00 17.32 ?  22  ASP   B CB   1 
ATOM   4414 C  CG   . ASP   B 1 22  ? 54.055 -28.057 -8.409  1.00 18.86 ?  22  ASP   B CG   1 
ATOM   4415 O  OD1  . ASP   B 1 22  ? 53.675 -26.950 -7.988  1.00 19.04 ?  22  ASP   B OD1  1 
ATOM   4416 O  OD2  . ASP   B 1 22  ? 55.136 -28.568 -8.040  1.00 21.23 -1 22  ASP   B OD2  1 
ATOM   4417 H  H    . ASP   B 1 22  ? 51.640 -29.440 -11.079 1.00 19.89 ?  22  ASP   B H    1 
ATOM   4418 H  HA   . ASP   B 1 22  ? 51.425 -29.024 -8.447  1.00 18.76 ?  22  ASP   B HA   1 
ATOM   4419 H  HB2  . ASP   B 1 22  ? 53.456 -29.750 -9.367  1.00 20.79 ?  22  ASP   B HB2  1 
ATOM   4420 H  HB3  . ASP   B 1 22  ? 53.497 -28.480 -10.317 1.00 20.79 ?  22  ASP   B HB3  1 
ATOM   4421 N  N    . ILE   B 1 23  ? 50.599 -26.683 -8.348  1.00 13.54 ?  23  ILE   B N    1 
ATOM   4422 C  CA   . ILE   B 1 23  ? 50.011 -25.342 -8.415  1.00 12.66 ?  23  ILE   B CA   1 
ATOM   4423 C  C    . ILE   B 1 23  ? 51.066 -24.252 -8.554  1.00 12.70 ?  23  ILE   B C    1 
ATOM   4424 O  O    . ILE   B 1 23  ? 50.799 -23.208 -9.159  1.00 12.27 ?  23  ILE   B O    1 
ATOM   4425 C  CB   . ILE   B 1 23  ? 49.069 -25.099 -7.218  1.00 13.35 ?  23  ILE   B CB   1 
ATOM   4426 C  CG1  . ILE   B 1 23  ? 48.237 -23.835 -7.426  1.00 13.93 ?  23  ILE   B CG1  1 
ATOM   4427 C  CG2  . ILE   B 1 23  ? 49.833 -25.048 -5.907  1.00 14.15 ?  23  ILE   B CG2  1 
ATOM   4428 C  CD1  . ILE   B 1 23  ? 47.129 -23.666 -6.396  1.00 14.34 ?  23  ILE   B CD1  1 
ATOM   4429 H  H    . ILE   B 1 23  ? 50.442 -27.106 -7.617  1.00 16.25 ?  23  ILE   B H    1 
ATOM   4430 H  HA   . ILE   B 1 23  ? 49.462 -25.299 -9.212  1.00 15.19 ?  23  ILE   B HA   1 
ATOM   4431 H  HB   . ILE   B 1 23  ? 48.454 -25.847 -7.172  1.00 16.02 ?  23  ILE   B HB   1 
ATOM   4432 H  HG12 . ILE   B 1 23  ? 48.821 -23.059 -7.367  1.00 16.72 ?  23  ILE   B HG12 1 
ATOM   4433 H  HG13 . ILE   B 1 23  ? 47.827 -23.866 -8.307  1.00 16.72 ?  23  ILE   B HG13 1 
ATOM   4434 H  HG21 . ILE   B 1 23  ? 49.201 -25.059 -5.172  1.00 16.98 ?  23  ILE   B HG21 1 
ATOM   4435 H  HG22 . ILE   B 1 23  ? 50.419 -25.817 -5.854  1.00 16.98 ?  23  ILE   B HG22 1 
ATOM   4436 H  HG23 . ILE   B 1 23  ? 50.358 -24.231 -5.880  1.00 16.98 ?  23  ILE   B HG23 1 
ATOM   4437 H  HD11 . ILE   B 1 23  ? 46.583 -22.904 -6.643  1.00 17.21 ?  23  ILE   B HD11 1 
ATOM   4438 H  HD12 . ILE   B 1 23  ? 46.589 -24.472 -6.386  1.00 17.21 ?  23  ILE   B HD12 1 
ATOM   4439 H  HD13 . ILE   B 1 23  ? 47.528 -23.523 -5.525  1.00 17.21 ?  23  ILE   B HD13 1 
ATOM   4440 N  N    . VAL   B 1 24  ? 52.261 -24.455 -7.991  1.00 12.75 ?  24  VAL   B N    1 
ATOM   4441 C  CA   . VAL   B 1 24  ? 53.340 -23.482 -8.163  1.00 13.57 ?  24  VAL   B CA   1 
ATOM   4442 C  C    . VAL   B 1 24  ? 53.788 -23.438 -9.616  1.00 13.86 ?  24  VAL   B C    1 
ATOM   4443 O  O    . VAL   B 1 24  ? 53.936 -22.362 -10.209 1.00 14.33 ?  24  VAL   B O    1 
ATOM   4444 C  CB   . VAL   B 1 24  ? 54.517 -23.803 -7.221  1.00 14.67 ?  24  VAL   B CB   1 
ATOM   4445 C  CG1  . VAL   B 1 24  ? 55.724 -22.930 -7.552  1.00 15.54 ?  24  VAL   B CG1  1 
ATOM   4446 C  CG2  . VAL   B 1 24  ? 54.105 -23.608 -5.779  1.00 15.39 ?  24  VAL   B CG2  1 
ATOM   4447 H  H    . VAL   B 1 24  ? 52.470 -25.138 -7.511  1.00 15.30 ?  24  VAL   B H    1 
ATOM   4448 H  HA   . VAL   B 1 24  ? 53.012 -22.605 -7.927  1.00 16.28 ?  24  VAL   B HA   1 
ATOM   4449 H  HB   . VAL   B 1 24  ? 54.778 -24.735 -7.333  1.00 17.60 ?  24  VAL   B HB   1 
ATOM   4450 H  HG11 . VAL   B 1 24  ? 56.325 -22.923 -6.790  1.00 18.65 ?  24  VAL   B HG11 1 
ATOM   4451 H  HG12 . VAL   B 1 24  ? 56.177 -23.299 -8.325  1.00 18.65 ?  24  VAL   B HG12 1 
ATOM   4452 H  HG13 . VAL   B 1 24  ? 55.416 -22.031 -7.739  1.00 18.65 ?  24  VAL   B HG13 1 
ATOM   4453 H  HG21 . VAL   B 1 24  ? 54.838 -23.868 -5.199  1.00 18.47 ?  24  VAL   B HG21 1 
ATOM   4454 H  HG22 . VAL   B 1 24  ? 53.889 -22.673 -5.639  1.00 18.47 ?  24  VAL   B HG22 1 
ATOM   4455 H  HG23 . VAL   B 1 24  ? 53.327 -24.158 -5.594  1.00 18.47 ?  24  VAL   B HG23 1 
ATOM   4456 N  N    . GLU   B 1 25  ? 54.045 -24.608 -10.208 1.00 14.97 ?  25  GLU   B N    1 
ATOM   4457 C  CA   . GLU   B 1 25  ? 54.446 -24.636 -11.610 1.00 16.46 ?  25  GLU   B CA   1 
ATOM   4458 C  C    . GLU   B 1 25  ? 53.339 -24.093 -12.499 1.00 14.84 ?  25  GLU   B C    1 
ATOM   4459 O  O    . GLU   B 1 25  ? 53.604 -23.371 -13.468 1.00 15.64 ?  25  GLU   B O    1 
ATOM   4460 C  CB   . GLU   B 1 25  ? 54.846 -26.052 -12.018 1.00 20.61 ?  25  GLU   B CB   1 
ATOM   4461 C  CG   . GLU   B 1 25  ? 56.136 -26.508 -11.353 1.00 25.97 ?  25  GLU   B CG   1 
ATOM   4462 C  CD   . GLU   B 1 25  ? 57.260 -25.486 -11.455 1.00 31.06 ?  25  GLU   B CD   1 
ATOM   4463 O  OE1  . GLU   B 1 25  ? 57.647 -25.132 -12.589 1.00 32.56 ?  25  GLU   B OE1  1 
ATOM   4464 O  OE2  . GLU   B 1 25  ? 57.747 -25.020 -10.398 1.00 32.40 -1 25  GLU   B OE2  1 
ATOM   4465 H  H    . GLU   B 1 25  ? 53.998 -25.380 -9.828  1.00 17.97 ?  25  GLU   B H    1 
ATOM   4466 H  HA   . GLU   B 1 25  ? 55.204 -24.048 -11.729 1.00 19.75 ?  25  GLU   B HA   1 
ATOM   4467 H  HB2  . GLU   B 1 25  ? 54.141 -26.670 -11.758 1.00 24.73 ?  25  GLU   B HB2  1 
ATOM   4468 H  HB3  . GLU   B 1 25  ? 54.972 -26.082 -12.980 1.00 24.73 ?  25  GLU   B HB3  1 
ATOM   4469 H  HG2  . GLU   B 1 25  ? 55.970 -26.659 -10.415 1.00 31.16 ?  25  GLU   B HG2  1 
ATOM   4470 H  HG3  . GLU   B 1 25  ? 56.439 -27.321 -11.783 1.00 31.16 ?  25  GLU   B HG3  1 
ATOM   4471 N  N    . GLU   B 1 26  ? 52.088 -24.423 -12.173 1.00 14.04 ?  26  GLU   B N    1 
ATOM   4472 C  CA   . GLU   B 1 26  ? 50.956 -23.894 -12.925 1.00 14.64 ?  26  GLU   B CA   1 
ATOM   4473 C  C    . GLU   B 1 26  ? 50.911 -22.377 -12.848 1.00 13.51 ?  26  GLU   B C    1 
ATOM   4474 O  O    . GLU   B 1 26  ? 50.705 -21.702 -13.862 1.00 14.84 ?  26  GLU   B O    1 
ATOM   4475 C  CB   . GLU   B 1 26  ? 49.646 -24.464 -12.383 1.00 16.79 ?  26  GLU   B CB   1 
ATOM   4476 C  CG   . GLU   B 1 26  ? 49.155 -25.723 -13.072 1.00 20.51 ?  26  GLU   B CG   1 
ATOM   4477 C  CD   . GLU   B 1 26  ? 48.930 -25.562 -14.577 1.00 22.01 ?  26  GLU   B CD   1 
ATOM   4478 O  OE1  . GLU   B 1 26  ? 47.950 -24.919 -15.016 1.00 22.60 ?  26  GLU   B OE1  1 
ATOM   4479 O  OE2  . GLU   B 1 26  ? 49.740 -26.121 -15.325 1.00 23.99 -1 26  GLU   B OE2  1 
ATOM   4480 H  H    . GLU   B 1 26  ? 51.867 -24.951 -11.527 1.00 16.85 ?  26  GLU   B H    1 
ATOM   4481 H  HA   . GLU   B 1 26  ? 51.042 -24.145 -13.854 1.00 17.56 ?  26  GLU   B HA   1 
ATOM   4482 H  HB2  . GLU   B 1 26  ? 49.763 -24.673 -11.441 1.00 20.14 ?  26  GLU   B HB2  1 
ATOM   4483 H  HB3  . GLU   B 1 26  ? 48.951 -23.790 -12.476 1.00 20.14 ?  26  GLU   B HB3  1 
ATOM   4484 H  HG2  . GLU   B 1 26  ? 49.825 -26.406 -12.955 1.00 24.61 ?  26  GLU   B HG2  1 
ATOM   4485 H  HG3  . GLU   B 1 26  ? 48.318 -25.993 -12.666 1.00 24.61 ?  26  GLU   B HG3  1 
ATOM   4486 N  N    . ALA   B 1 27  ? 51.055 -21.825 -11.641 1.00 12.85 ?  27  ALA   B N    1 
ATOM   4487 C  CA   . ALA   B 1 27  ? 51.008 -20.374 -11.499 1.00 13.18 ?  27  ALA   B CA   1 
ATOM   4488 C  C    . ALA   B 1 27  ? 52.082 -19.708 -12.351 1.00 14.03 ?  27  ALA   B C    1 
ATOM   4489 O  O    . ALA   B 1 27  ? 51.820 -18.706 -13.034 1.00 14.76 ?  27  ALA   B O    1 
ATOM   4490 C  CB   . ALA   B 1 27  ? 51.143 -19.981 -10.025 1.00 13.47 ?  27  ALA   B CB   1 
ATOM   4491 H  H    . ALA   B 1 27  ? 51.177 -22.258 -10.904 1.00 15.42 ?  27  ALA   B H    1 
ATOM   4492 H  HA   . ALA   B 1 27  ? 50.150 -20.057 -11.807 1.00 15.81 ?  27  ALA   B HA   1 
ATOM   4493 H  HB1  . ALA   B 1 27  ? 51.099 -19.012 -9.950  1.00 16.17 ?  27  ALA   B HB1  1 
ATOM   4494 H  HB2  . ALA   B 1 27  ? 50.411 -20.378 -9.523  1.00 16.17 ?  27  ALA   B HB2  1 
ATOM   4495 H  HB3  . ALA   B 1 27  ? 51.989 -20.300 -9.682  1.00 16.17 ?  27  ALA   B HB3  1 
ATOM   4496 N  N    . LYS   B 1 28  ? 53.298 -20.260 -12.341 1.00 15.57 ?  28  LYS   B N    1 
ATOM   4497 C  CA   . LYS   B 1 28  ? 54.373 -19.645 -13.111 1.00 18.09 ?  28  LYS   B CA   1 
ATOM   4498 C  C    . LYS   B 1 28  ? 54.115 -19.732 -14.609 1.00 18.88 ?  28  LYS   B C    1 
ATOM   4499 O  O    . LYS   B 1 28  ? 54.526 -18.838 -15.356 1.00 20.13 ?  28  LYS   B O    1 
ATOM   4500 C  CB   . LYS   B 1 28  ? 55.728 -20.244 -12.722 1.00 21.61 ?  28  LYS   B CB   1 
ATOM   4501 C  CG   . LYS   B 1 28  ? 56.126 -19.907 -11.289 1.00 25.40 ?  28  LYS   B CG   1 
ATOM   4502 C  CD   . LYS   B 1 28  ? 57.553 -20.314 -10.948 1.00 29.91 ?  28  LYS   B CD   1 
ATOM   4503 C  CE   . LYS   B 1 28  ? 57.670 -21.794 -10.667 1.00 33.54 ?  28  LYS   B CE   1 
ATOM   4504 N  NZ   . LYS   B 1 28  ? 59.019 -22.136 -10.130 1.00 36.65 ?  28  LYS   B NZ   1 
ATOM   4505 H  H    . LYS   B 1 28  ? 53.523 -20.968 -11.906 1.00 18.68 ?  28  LYS   B H    1 
ATOM   4506 H  HA   . LYS   B 1 28  ? 54.407 -18.703 -12.890 1.00 21.71 ?  28  LYS   B HA   1 
ATOM   4507 H  HB2  . LYS   B 1 28  ? 55.686 -21.207 -12.801 1.00 25.93 ?  28  LYS   B HB2  1 
ATOM   4508 H  HB3  . LYS   B 1 28  ? 56.413 -19.889 -13.313 1.00 25.93 ?  28  LYS   B HB3  1 
ATOM   4509 H  HG2  . LYS   B 1 28  ? 56.051 -18.947 -11.161 1.00 30.48 ?  28  LYS   B HG2  1 
ATOM   4510 H  HG3  . LYS   B 1 28  ? 55.529 -20.368 -10.683 1.00 30.48 ?  28  LYS   B HG3  1 
ATOM   4511 H  HD2  . LYS   B 1 28  ? 58.132 -20.100 -11.697 1.00 35.89 ?  28  LYS   B HD2  1 
ATOM   4512 H  HD3  . LYS   B 1 28  ? 57.839 -19.830 -10.157 1.00 35.89 ?  28  LYS   B HD3  1 
ATOM   4513 H  HE2  . LYS   B 1 28  ? 57.005 -22.048 -10.008 1.00 40.25 ?  28  LYS   B HE2  1 
ATOM   4514 H  HE3  . LYS   B 1 28  ? 57.534 -22.289 -11.490 1.00 40.25 ?  28  LYS   B HE3  1 
ATOM   4515 H  HZ1  . LYS   B 1 28  ? 59.071 -23.009 -9.970  1.00 43.98 ?  28  LYS   B HZ1  1 
ATOM   4516 H  HZ2  . LYS   B 1 28  ? 59.646 -21.912 -10.720 1.00 43.98 ?  28  LYS   B HZ2  1 
ATOM   4517 H  HZ3  . LYS   B 1 28  ? 59.165 -21.693 -9.372  1.00 43.98 ?  28  LYS   B HZ3  1 
ATOM   4518 N  N    . LYS   B 1 29  ? 53.405 -20.764 -15.063 1.00 19.96 ?  29  LYS   B N    1 
ATOM   4519 C  CA   . LYS   B 1 29  ? 53.123 -20.907 -16.488 1.00 22.76 ?  29  LYS   B CA   1 
ATOM   4520 C  C    . LYS   B 1 29  ? 51.873 -20.150 -16.928 1.00 21.59 ?  29  LYS   B C    1 
ATOM   4521 O  O    . LYS   B 1 29  ? 51.866 -19.543 -18.004 1.00 22.91 ?  29  LYS   B O    1 
ATOM   4522 C  CB   . LYS   B 1 29  ? 52.988 -22.388 -16.850 1.00 27.65 ?  29  LYS   B CB   1 
ATOM   4523 C  CG   . LYS   B 1 29  ? 52.875 -22.654 -18.341 1.00 32.49 ?  29  LYS   B CG   1 
ATOM   4524 C  CD   . LYS   B 1 29  ? 53.082 -24.130 -18.658 1.00 36.34 ?  29  LYS   B CD   1 
ATOM   4525 C  CE   . LYS   B 1 29  ? 51.924 -24.985 -18.166 1.00 38.76 ?  29  LYS   B CE   1 
ATOM   4526 N  NZ   . LYS   B 1 29  ? 52.140 -26.431 -18.464 1.00 40.01 ?  29  LYS   B NZ   1 
ATOM   4527 H  H    . LYS   B 1 29  ? 53.074 -21.392 -14.566 1.00 23.95 ?  29  LYS   B H    1 
ATOM   4528 H  HA   . LYS   B 1 29  ? 53.868 -20.550 -16.985 1.00 27.31 ?  29  LYS   B HA   1 
ATOM   4529 H  HB2  . LYS   B 1 29  ? 53.775 -22.855 -16.528 1.00 33.18 ?  29  LYS   B HB2  1 
ATOM   4530 H  HB3  . LYS   B 1 29  ? 52.196 -22.744 -16.426 1.00 33.18 ?  29  LYS   B HB3  1 
ATOM   4531 H  HG2  . LYS   B 1 29  ? 51.990 -22.396 -18.645 1.00 38.99 ?  29  LYS   B HG2  1 
ATOM   4532 H  HG3  . LYS   B 1 29  ? 53.553 -22.142 -18.811 1.00 38.99 ?  29  LYS   B HG3  1 
ATOM   4533 H  HD2  . LYS   B 1 29  ? 53.155 -24.243 -19.618 1.00 43.61 ?  29  LYS   B HD2  1 
ATOM   4534 H  HD3  . LYS   B 1 29  ? 53.892 -24.439 -18.222 1.00 43.61 ?  29  LYS   B HD3  1 
ATOM   4535 H  HE2  . LYS   B 1 29  ? 51.835 -24.885 -17.205 1.00 46.52 ?  29  LYS   B HE2  1 
ATOM   4536 H  HE3  . LYS   B 1 29  ? 51.108 -24.703 -18.609 1.00 46.52 ?  29  LYS   B HE3  1 
ATOM   4537 H  HZ1  . LYS   B 1 29  ? 51.450 -26.909 -18.168 1.00 48.02 ?  29  LYS   B HZ1  1 
ATOM   4538 H  HZ2  . LYS   B 1 29  ? 52.220 -26.552 -19.342 1.00 48.02 ?  29  LYS   B HZ2  1 
ATOM   4539 H  HZ3  . LYS   B 1 29  ? 52.882 -26.716 -18.064 1.00 48.02 ?  29  LYS   B HZ3  1 
ATOM   4540 N  N    . VAL   B 1 30  ? 50.814 -20.189 -16.115 1.00 19.69 ?  30  VAL   B N    1 
ATOM   4541 C  CA   . VAL   B 1 30  ? 49.523 -19.597 -16.477 1.00 19.78 ?  30  VAL   B CA   1 
ATOM   4542 C  C    . VAL   B 1 30  ? 49.533 -18.085 -16.329 1.00 18.82 ?  30  VAL   B C    1 
ATOM   4543 O  O    . VAL   B 1 30  ? 48.800 -17.375 -17.037 1.00 19.89 ?  30  VAL   B O    1 
ATOM   4544 C  CB   . VAL   B 1 30  ? 48.432 -20.209 -15.575 1.00 20.59 ?  30  VAL   B CB   1 
ATOM   4545 C  CG1  . VAL   B 1 30  ? 47.138 -19.406 -15.641 1.00 20.97 ?  30  VAL   B CG1  1 
ATOM   4546 C  CG2  . VAL   B 1 30  ? 48.190 -21.666 -15.942 1.00 21.80 ?  30  VAL   B CG2  1 
ATOM   4547 H  H    . VAL   B 1 30  ? 50.805 -20.582 -15.337 1.00 23.63 ?  30  VAL   B H    1 
ATOM   4548 H  HA   . VAL   B 1 30  ? 49.314 -19.829 -17.394 1.00 23.74 ?  30  VAL   B HA   1 
ATOM   4549 H  HB   . VAL   B 1 30  ? 48.737 -20.197 -14.654 1.00 24.71 ?  30  VAL   B HB   1 
ATOM   4550 H  HG11 . VAL   B 1 30  ? 46.402 -19.990 -15.397 1.00 25.16 ?  30  VAL   B HG11 1 
ATOM   4551 H  HG12 . VAL   B 1 30  ? 47.190 -18.669 -15.016 1.00 25.16 ?  30  VAL   B HG12 1 
ATOM   4552 H  HG13 . VAL   B 1 30  ? 47.009 -19.085 -16.541 1.00 25.16 ?  30  VAL   B HG13 1 
ATOM   4553 H  HG21 . VAL   B 1 30  ? 47.509 -22.035 -15.352 1.00 26.16 ?  30  VAL   B HG21 1 
ATOM   4554 H  HG22 . VAL   B 1 30  ? 47.884 -21.714 -16.862 1.00 26.16 ?  30  VAL   B HG22 1 
ATOM   4555 H  HG23 . VAL   B 1 30  ? 49.015 -22.161 -15.839 1.00 26.16 ?  30  VAL   B HG23 1 
ATOM   4556 N  N    . LYS   B 1 31  ? 50.307 -17.585 -15.384 1.00 18.73 ?  31  LYS   B N    1 
ATOM   4557 C  CA   . LYS   B 1 31  ? 50.338 -16.174 -15.033 1.00 19.09 ?  31  LYS   B CA   1 
ATOM   4558 C  C    . LYS   B 1 31  ? 48.942 -15.689 -14.647 1.00 16.83 ?  31  LYS   B C    1 
ATOM   4559 O  O    . LYS   B 1 31  ? 48.404 -14.765 -15.272 1.00 17.92 ?  31  LYS   B O    1 
ATOM   4560 C  CB   . LYS   B 1 31  ? 50.971 -15.370 -16.172 1.00 22.46 ?  31  LYS   B CB   1 
ATOM   4561 C  CG   . LYS   B 1 31  ? 52.396 -15.835 -16.490 1.00 26.17 ?  31  LYS   B CG   1 
ATOM   4562 C  CD   . LYS   B 1 31  ? 52.977 -15.120 -17.693 1.00 29.43 ?  31  LYS   B CD   1 
ATOM   4563 C  CE   . LYS   B 1 31  ? 54.458 -15.395 -17.839 1.00 31.78 ?  31  LYS   B CE   1 
ATOM   4564 N  NZ   . LYS   B 1 31  ? 55.197 -14.961 -16.624 1.00 32.82 ?  31  LYS   B NZ   1 
ATOM   4565 H  H    . LYS   B 1 31  ? 50.846 -18.074 -14.926 1.00 22.48 ?  31  LYS   B H    1 
ATOM   4566 H  HA   . LYS   B 1 31  ? 50.899 -16.088 -14.261 1.00 22.91 ?  31  LYS   B HA   1 
ATOM   4567 H  HB2  . LYS   B 1 31  ? 50.436 -15.470 -16.976 1.00 26.96 ?  31  LYS   B HB2  1 
ATOM   4568 H  HB3  . LYS   B 1 31  ? 51.010 -14.442 -15.906 1.00 26.96 ?  31  LYS   B HB3  1 
ATOM   4569 H  HG2  . LYS   B 1 31  ? 52.958 -15.661 -15.720 1.00 31.41 ?  31  LYS   B HG2  1 
ATOM   4570 H  HG3  . LYS   B 1 31  ? 52.384 -16.789 -16.681 1.00 31.41 ?  31  LYS   B HG3  1 
ATOM   4571 H  HD2  . LYS   B 1 31  ? 52.528 -15.433 -18.491 1.00 35.32 ?  31  LYS   B HD2  1 
ATOM   4572 H  HD3  . LYS   B 1 31  ? 52.852 -14.169 -17.582 1.00 35.32 ?  31  LYS   B HD3  1 
ATOM   4573 H  HE2  . LYS   B 1 31  ? 54.604 -16.347 -17.962 1.00 38.13 ?  31  LYS   B HE2  1 
ATOM   4574 H  HE3  . LYS   B 1 31  ? 54.803 -14.901 -18.600 1.00 38.13 ?  31  LYS   B HE3  1 
ATOM   4575 H  HZ1  . LYS   B 1 31  ? 56.072 -14.975 -16.778 1.00 39.38 ?  31  LYS   B HZ1  1 
ATOM   4576 H  HZ2  . LYS   B 1 31  ? 54.954 -14.134 -16.403 1.00 39.38 ?  31  LYS   B HZ2  1 
ATOM   4577 H  HZ3  . LYS   B 1 31  ? 55.014 -15.507 -15.945 1.00 39.38 ?  31  LYS   B HZ3  1 
ATOM   4578 N  N    . PRO   B 1 32  ? 48.331 -16.283 -13.615 1.00 14.50 ?  32  PRO   B N    1 
ATOM   4579 C  CA   . PRO   B 1 32  ? 46.955 -15.924 -13.260 1.00 13.55 ?  32  PRO   B CA   1 
ATOM   4580 C  C    . PRO   B 1 32  ? 46.875 -14.578 -12.555 1.00 13.77 ?  32  PRO   B C    1 
ATOM   4581 O  O    . PRO   B 1 32  ? 47.796 -14.156 -11.848 1.00 15.09 ?  32  PRO   B O    1 
ATOM   4582 C  CB   . PRO   B 1 32  ? 46.554 -17.040 -12.288 1.00 13.53 ?  32  PRO   B CB   1 
ATOM   4583 C  CG   . PRO   B 1 32  ? 47.856 -17.386 -11.600 1.00 13.96 ?  32  PRO   B CG   1 
ATOM   4584 C  CD   . PRO   B 1 32  ? 48.901 -17.272 -12.676 1.00 14.52 ?  32  PRO   B CD   1 
ATOM   4585 H  HA   . PRO   B 1 32  ? 46.376 -15.937 -14.042 1.00 16.26 ?  32  PRO   B HA   1 
ATOM   4586 H  HB2  . PRO   B 1 32  ? 45.899 -16.707 -11.651 1.00 16.24 ?  32  PRO   B HB2  1 
ATOM   4587 H  HB3  . PRO   B 1 32  ? 46.206 -17.802 -12.777 1.00 16.24 ?  32  PRO   B HB3  1 
ATOM   4588 H  HG2  . PRO   B 1 32  ? 48.029 -16.750 -10.883 1.00 16.75 ?  32  PRO   B HG2  1 
ATOM   4589 H  HG3  . PRO   B 1 32  ? 47.819 -18.290 -11.253 1.00 16.75 ?  32  PRO   B HG3  1 
ATOM   4590 H  HD2  . PRO   B 1 32  ? 49.731 -16.940 -12.306 1.00 17.42 ?  32  PRO   B HD2  1 
ATOM   4591 H  HD3  . PRO   B 1 32  ? 49.016 -18.121 -13.120 1.00 17.42 ?  32  PRO   B HD3  1 
ATOM   4592 N  N    . THR   B 1 33  ? 45.724 -13.922 -12.724 1.00 13.23 ?  33  THR   B N    1 
ATOM   4593 C  CA   . THR   B 1 33  ? 45.429 -12.747 -11.913 1.00 13.12 ?  33  THR   B CA   1 
ATOM   4594 C  C    . THR   B 1 33  ? 45.385 -13.099 -10.430 1.00 12.90 ?  33  THR   B C    1 
ATOM   4595 O  O    . THR   B 1 33  ? 45.860 -12.320 -9.589  1.00 13.92 ?  33  THR   B O    1 
ATOM   4596 C  CB   . THR   B 1 33  ? 44.110 -12.114 -12.364 1.00 13.95 ?  33  THR   B CB   1 
ATOM   4597 O  OG1  . THR   B 1 33  ? 44.158 -11.858 -13.770 1.00 14.01 ?  33  THR   B OG1  1 
ATOM   4598 C  CG2  . THR   B 1 33  ? 43.841 -10.821 -11.613 1.00 15.18 ?  33  THR   B CG2  1 
ATOM   4599 H  H    . THR   B 1 33  ? 45.107 -14.131 -13.293 1.00 15.88 ?  33  THR   B H    1 
ATOM   4600 H  HA   . THR   B 1 33  ? 46.126 -12.090 -12.041 1.00 15.74 ?  33  THR   B HA   1 
ATOM   4601 H  HB   . THR   B 1 33  ? 43.377 -12.729 -12.183 1.00 16.74 ?  33  THR   B HB   1 
ATOM   4602 H  HG1  . THR   B 1 33  ? 43.441 -11.485 -14.021 1.00 16.81 ?  33  THR   B HG1  1 
ATOM   4603 H  HG21 . THR   B 1 33  ? 43.087 -10.360 -12.004 1.00 18.21 ?  33  THR   B HG21 1 
ATOM   4604 H  HG22 . THR   B 1 33  ? 43.645 -11.013 -10.681 1.00 18.21 ?  33  THR   B HG22 1 
ATOM   4605 H  HG23 . THR   B 1 33  ? 44.623 -10.248 -11.658 1.00 18.21 ?  33  THR   B HG23 1 
ATOM   4606 N  N    . VAL   B 1 34  ? 44.837 -14.271 -10.091 1.00 12.08 ?  34  VAL   B N    1 
ATOM   4607 C  CA   . VAL   B 1 34  ? 44.641 -14.675 -8.702  1.00 11.73 ?  34  VAL   B CA   1 
ATOM   4608 C  C    . VAL   B 1 34  ? 45.066 -16.125 -8.541  1.00 10.93 ?  34  VAL   B C    1 
ATOM   4609 O  O    . VAL   B 1 34  ? 44.543 -17.013 -9.227  1.00 11.58 ?  34  VAL   B O    1 
ATOM   4610 C  CB   . VAL   B 1 34  ? 43.169 -14.535 -8.257  1.00 12.62 ?  34  VAL   B CB   1 
ATOM   4611 C  CG1  . VAL   B 1 34  ? 43.001 -14.994 -6.814  1.00 13.07 ?  34  VAL   B CG1  1 
ATOM   4612 C  CG2  . VAL   B 1 34  ? 42.679 -13.104 -8.438  1.00 13.63 ?  34  VAL   B CG2  1 
ATOM   4613 H  H    . VAL   B 1 34  ? 44.568 -14.862 -10.660 1.00 14.50 ?  34  VAL   B H    1 
ATOM   4614 H  HA   . VAL   B 1 34  ? 45.194 -14.123 -8.124  1.00 14.07 ?  34  VAL   B HA   1 
ATOM   4615 H  HB   . VAL   B 1 34  ? 42.621 -15.105 -8.814  1.00 15.15 ?  34  VAL   B HB   1 
ATOM   4616 H  HG11 . VAL   B 1 34  ? 42.144 -14.681 -6.479  1.00 15.69 ?  34  VAL   B HG11 1 
ATOM   4617 H  HG12 . VAL   B 1 34  ? 43.028 -15.965 -6.781  1.00 15.69 ?  34  VAL   B HG12 1 
ATOM   4618 H  HG13 . VAL   B 1 34  ? 43.718 -14.625 -6.274  1.00 15.69 ?  34  VAL   B HG13 1 
ATOM   4619 H  HG21 . VAL   B 1 34  ? 41.763 -13.040 -8.122  1.00 16.35 ?  34  VAL   B HG21 1 
ATOM   4620 H  HG22 . VAL   B 1 34  ? 43.246 -12.504 -7.930  1.00 16.35 ?  34  VAL   B HG22 1 
ATOM   4621 H  HG23 . VAL   B 1 34  ? 42.716 -12.873 -9.382  1.00 16.35 ?  34  VAL   B HG23 1 
ATOM   4622 N  N    . VAL   B 1 35  ? 45.977 -16.370 -7.604  1.00 10.43 ?  35  VAL   B N    1 
ATOM   4623 C  CA   . VAL   B 1 35  ? 46.209 -17.711 -7.083  1.00 10.12 ?  35  VAL   B CA   1 
ATOM   4624 C  C    . VAL   B 1 35  ? 45.674 -17.764 -5.662  1.00 9.71  ?  35  VAL   B C    1 
ATOM   4625 O  O    . VAL   B 1 35  ? 45.895 -16.842 -4.872  1.00 10.33 ?  35  VAL   B O    1 
ATOM   4626 C  CB   . VAL   B 1 35  ? 47.691 -18.140 -7.170  1.00 10.70 ?  35  VAL   B CB   1 
ATOM   4627 C  CG1  . VAL   B 1 35  ? 48.588 -17.293 -6.266  1.00 11.47 ?  35  VAL   B CG1  1 
ATOM   4628 C  CG2  . VAL   B 1 35  ? 47.836 -19.631 -6.847  1.00 11.07 ?  35  VAL   B CG2  1 
ATOM   4629 H  H    . VAL   B 1 35  ? 46.478 -15.766 -7.241  1.00 12.52 ?  35  VAL   B H    1 
ATOM   4630 H  HA   . VAL   B 1 35  ? 45.693 -18.340 -7.608  1.00 12.14 ?  35  VAL   B HA   1 
ATOM   4631 H  HB   . VAL   B 1 35  ? 47.994 -18.014 -8.083  1.00 12.84 ?  35  VAL   B HB   1 
ATOM   4632 H  HG11 . VAL   B 1 35  ? 49.512 -17.519 -6.443  1.00 13.76 ?  35  VAL   B HG11 1 
ATOM   4633 H  HG12 . VAL   B 1 35  ? 48.425 -16.360 -6.450  1.00 13.76 ?  35  VAL   B HG12 1 
ATOM   4634 H  HG13 . VAL   B 1 35  ? 48.371 -17.494 -5.338  1.00 13.76 ?  35  VAL   B HG13 1 
ATOM   4635 H  HG21 . VAL   B 1 35  ? 48.760 -19.896 -6.956  1.00 13.29 ?  35  VAL   B HG21 1 
ATOM   4636 H  HG22 . VAL   B 1 35  ? 47.552 -19.789 -5.930  1.00 13.29 ?  35  VAL   B HG22 1 
ATOM   4637 H  HG23 . VAL   B 1 35  ? 47.272 -20.146 -7.453  1.00 13.29 ?  35  VAL   B HG23 1 
ATOM   4638 N  N    . VAL   B 1 36  ? 44.950 -18.840 -5.344  1.00 9.85  ?  36  VAL   B N    1 
ATOM   4639 C  CA   . VAL   B 1 36  ? 44.407 -19.044 -4.012  1.00 9.57  ?  36  VAL   B CA   1 
ATOM   4640 C  C    . VAL   B 1 36  ? 45.416 -19.804 -3.163  1.00 9.43  ?  36  VAL   B C    1 
ATOM   4641 O  O    . VAL   B 1 36  ? 45.957 -20.835 -3.588  1.00 10.39 ?  36  VAL   B O    1 
ATOM   4642 C  CB   . VAL   B 1 36  ? 43.068 -19.799 -4.083  1.00 10.21 ?  36  VAL   B CB   1 
ATOM   4643 C  CG1  . VAL   B 1 36  ? 42.562 -20.153 -2.699  1.00 10.71 ?  36  VAL   B CG1  1 
ATOM   4644 C  CG2  . VAL   B 1 36  ? 42.035 -18.967 -4.823  1.00 10.84 ?  36  VAL   B CG2  1 
ATOM   4645 H  H    . VAL   B 1 36  ? 44.765 -19.477 -5.893  1.00 11.82 ?  36  VAL   B H    1 
ATOM   4646 H  HA   . VAL   B 1 36  ? 44.243 -18.183 -3.597  1.00 11.49 ?  36  VAL   B HA   1 
ATOM   4647 H  HB   . VAL   B 1 36  ? 43.191 -20.624 -4.577  1.00 12.25 ?  36  VAL   B HB   1 
ATOM   4648 H  HG11 . VAL   B 1 36  ? 41.620 -20.390 -2.756  1.00 12.85 ?  36  VAL   B HG11 1 
ATOM   4649 H  HG12 . VAL   B 1 36  ? 43.069 -20.898 -2.352  1.00 12.85 ?  36  VAL   B HG12 1 
ATOM   4650 H  HG13 . VAL   B 1 36  ? 42.664 -19.378 -2.119  1.00 12.85 ?  36  VAL   B HG13 1 
ATOM   4651 H  HG21 . VAL   B 1 36  ? 41.193 -19.449 -4.847  1.00 13.01 ?  36  VAL   B HG21 1 
ATOM   4652 H  HG22 . VAL   B 1 36  ? 41.917 -18.122 -4.360  1.00 13.01 ?  36  VAL   B HG22 1 
ATOM   4653 H  HG23 . VAL   B 1 36  ? 42.346 -18.804 -5.729  1.00 13.01 ?  36  VAL   B HG23 1 
ATOM   4654 N  N    . ASN   B 1 37  ? 45.640 -19.309 -1.950  1.00 9.73  ?  37  ASN   B N    1 
ATOM   4655 C  CA   . ASN   B 1 37  ? 46.393 -20.031 -0.940  1.00 9.85  ?  37  ASN   B CA   1 
ATOM   4656 C  C    . ASN   B 1 37  ? 45.444 -20.709 0.038   1.00 10.21 ?  37  ASN   B C    1 
ATOM   4657 O  O    . ASN   B 1 37  ? 44.428 -20.135 0.443   1.00 10.41 ?  37  ASN   B O    1 
ATOM   4658 C  CB   . ASN   B 1 37  ? 47.316 -19.085 -0.173  1.00 10.19 ?  37  ASN   B CB   1 
ATOM   4659 C  CG   . ASN   B 1 37  ? 48.170 -19.802 0.832   1.00 10.47 ?  37  ASN   B CG   1 
ATOM   4660 O  OD1  . ASN   B 1 37  ? 48.517 -20.972 0.649   1.00 11.11 ?  37  ASN   B OD1  1 
ATOM   4661 N  ND2  . ASN   B 1 37  ? 48.522 -19.105 1.908   1.00 10.46 ?  37  ASN   B ND2  1 
ATOM   4662 H  H    . ASN   B 1 37  ? 45.353 -18.538 -1.683  1.00 11.68 ?  37  ASN   B H    1 
ATOM   4663 H  HA   . ASN   B 1 37  ? 46.930 -20.715 -1.363  1.00 11.82 ?  37  ASN   B HA   1 
ATOM   4664 H  HB2  . ASN   B 1 37  ? 47.902 -18.642 -0.802  1.00 12.22 ?  37  ASN   B HB2  1 
ATOM   4665 H  HB3  . ASN   B 1 37  ? 46.779 -18.431 0.303   1.00 12.22 ?  37  ASN   B HB3  1 
ATOM   4666 H  HD21 . ASN   B 1 37  ? 49.019 -19.465 2.513   1.00 12.55 ?  37  ASN   B HD21 1 
ATOM   4667 H  HD22 . ASN   B 1 37  ? 48.267 -18.292 2.001   1.00 12.55 ?  37  ASN   B HD22 1 
ATOM   4668 N  N    . ALA   B 1 38  ? 45.799 -21.941 0.416   1.00 10.35 ?  38  ALA   B N    1 
ATOM   4669 C  CA   . ALA   B 1 38  ? 45.141 -22.684 1.495   1.00 10.66 ?  38  ALA   B CA   1 
ATOM   4670 C  C    . ALA   B 1 38  ? 45.722 -22.191 2.818   1.00 10.39 ?  38  ALA   B C    1 
ATOM   4671 O  O    . ALA   B 1 38  ? 46.627 -22.796 3.404   1.00 11.31 ?  38  ALA   B O    1 
ATOM   4672 C  CB   . ALA   B 1 38  ? 45.371 -24.178 1.312   1.00 11.90 ?  38  ALA   B CB   1 
ATOM   4673 H  H    . ALA   B 1 38  ? 46.450 -22.377 0.061   1.00 12.42 ?  38  ALA   B H    1 
ATOM   4674 H  HA   . ALA   B 1 38  ? 44.189 -22.506 1.485   1.00 12.79 ?  38  ALA   B HA   1 
ATOM   4675 H  HB1  . ALA   B 1 38  ? 44.922 -24.656 2.034   1.00 14.27 ?  38  ALA   B HB1  1 
ATOM   4676 H  HB2  . ALA   B 1 38  ? 44.994 -24.451 0.460   1.00 14.27 ?  38  ALA   B HB2  1 
ATOM   4677 H  HB3  . ALA   B 1 38  ? 46.318 -24.361 1.334   1.00 14.27 ?  38  ALA   B HB3  1 
ATOM   4678 N  N    . ALA   B 1 39  ? 45.200 -21.055 3.277   1.00 10.41 ?  39  ALA   B N    1 
ATOM   4679 C  CA   . ALA   B 1 39  ? 45.749 -20.319 4.405   1.00 10.79 ?  39  ALA   B CA   1 
ATOM   4680 C  C    . ALA   B 1 39  ? 45.135 -20.764 5.730   1.00 10.24 ?  39  ALA   B C    1 
ATOM   4681 O  O    . ALA   B 1 39  ? 44.105 -21.437 5.783   1.00 11.84 ?  39  ALA   B O    1 
ATOM   4682 C  CB   . ALA   B 1 39  ? 45.509 -18.814 4.213   1.00 11.34 ?  39  ALA   B CB   1 
ATOM   4683 H  H    . ALA   B 1 39  ? 44.512 -20.677 2.927   1.00 12.49 ?  39  ALA   B H    1 
ATOM   4684 H  HA   . ALA   B 1 39  ? 46.702 -20.464 4.449   1.00 12.94 ?  39  ALA   B HA   1 
ATOM   4685 H  HB1  . ALA   B 1 39  ? 45.876 -18.335 4.973   1.00 13.61 ?  39  ALA   B HB1  1 
ATOM   4686 H  HB2  . ALA   B 1 39  ? 45.948 -18.523 3.397   1.00 13.61 ?  39  ALA   B HB2  1 
ATOM   4687 H  HB3  . ALA   B 1 39  ? 44.554 -18.648 4.148   1.00 13.61 ?  39  ALA   B HB3  1 
ATOM   4688 N  N    . ASN   B 1 40  ? 45.778 -20.341 6.812   1.00 11.31 ?  40  ASN   B N    1 
ATOM   4689 C  CA   . ASN   B 1 40  ? 45.220 -20.386 8.154   1.00 12.08 ?  40  ASN   B CA   1 
ATOM   4690 C  C    . ASN   B 1 40  ? 45.042 -18.956 8.673   1.00 11.76 ?  40  ASN   B C    1 
ATOM   4691 O  O    . ASN   B 1 40  ? 45.453 -17.979 8.036   1.00 11.62 ?  40  ASN   B O    1 
ATOM   4692 C  CB   . ASN   B 1 40  ? 46.074 -21.254 9.094   1.00 13.04 ?  40  ASN   B CB   1 
ATOM   4693 C  CG   . ASN   B 1 40  ? 47.533 -20.851 9.107   1.00 14.03 ?  40  ASN   B CG   1 
ATOM   4694 O  OD1  . ASN   B 1 40  ? 47.854 -19.669 9.159   1.00 16.15 ?  40  ASN   B OD1  1 
ATOM   4695 N  ND2  . ASN   B 1 40  ? 48.423 -21.828 9.065   1.00 14.25 ?  40  ASN   B ND2  1 
ATOM   4696 H  H    . ASN   B 1 40  ? 46.572 -20.015 6.788   1.00 13.57 ?  40  ASN   B H    1 
ATOM   4697 H  HA   . ASN   B 1 40  ? 44.336 -20.782 8.110   1.00 14.50 ?  40  ASN   B HA   1 
ATOM   4698 H  HB2  . ASN   B 1 40  ? 45.729 -21.168 9.995   1.00 15.65 ?  40  ASN   B HB2  1 
ATOM   4699 H  HB3  . ASN   B 1 40  ? 46.017 -22.173 8.799   1.00 15.65 ?  40  ASN   B HB3  1 
ATOM   4700 H  HD21 . ASN   B 1 40  ? 49.265 -21.646 9.075   1.00 17.10 ?  40  ASN   B HD21 1 
ATOM   4701 H  HD22 . ASN   B 1 40  ? 48.161 -22.645 9.030   1.00 17.10 ?  40  ASN   B HD22 1 
ATOM   4702 N  N    . VAL   B 1 41  ? 44.394 -18.829 9.834   1.00 12.27 ?  41  VAL   B N    1 
ATOM   4703 C  CA   . VAL   B 1 41  ? 43.935 -17.510 10.278  1.00 12.85 ?  41  VAL   B CA   1 
ATOM   4704 C  C    . VAL   B 1 41  ? 45.085 -16.554 10.570  1.00 12.70 ?  41  VAL   B C    1 
ATOM   4705 O  O    . VAL   B 1 41  ? 44.905 -15.334 10.483  1.00 13.01 ?  41  VAL   B O    1 
ATOM   4706 C  CB   . VAL   B 1 41  ? 42.964 -17.591 11.473  1.00 14.54 ?  41  VAL   B CB   1 
ATOM   4707 C  CG1  . VAL   B 1 41  ? 41.667 -18.275 11.067  1.00 14.83 ?  41  VAL   B CG1  1 
ATOM   4708 C  CG2  . VAL   B 1 41  ? 43.622 -18.279 12.659  1.00 15.48 ?  41  VAL   B CG2  1 
ATOM   4709 H  H    . VAL   B 1 41  ? 44.210 -19.472 10.366  1.00 14.72 ?  41  VAL   B H    1 
ATOM   4710 H  HA   . VAL   B 1 41  ? 43.435 -17.112 9.551   1.00 15.42 ?  41  VAL   B HA   1 
ATOM   4711 H  HB   . VAL   B 1 41  ? 42.737 -16.692 11.753  1.00 17.45 ?  41  VAL   B HB   1 
ATOM   4712 H  HG11 . VAL   B 1 41  ? 41.061 -18.287 11.827  1.00 17.79 ?  41  VAL   B HG11 1 
ATOM   4713 H  HG12 . VAL   B 1 41  ? 41.265 -17.784 10.334  1.00 17.79 ?  41  VAL   B HG12 1 
ATOM   4714 H  HG13 . VAL   B 1 41  ? 41.860 -19.185 10.790  1.00 17.79 ?  41  VAL   B HG13 1 
ATOM   4715 H  HG21 . VAL   B 1 41  ? 42.994 -18.309 13.394  1.00 18.57 ?  41  VAL   B HG21 1 
ATOM   4716 H  HG22 . VAL   B 1 41  ? 43.872 -19.182 12.401  1.00 18.57 ?  41  VAL   B HG22 1 
ATOM   4717 H  HG23 . VAL   B 1 41  ? 44.411 -17.778 12.914  1.00 18.57 ?  41  VAL   B HG23 1 
ATOM   4718 N  N    . TYR   B 1 42  ? 46.254 -17.066 10.953  1.00 12.98 ?  42  TYR   B N    1 
ATOM   4719 C  CA   . TYR   B 1 42  ? 47.409 -16.219 11.219  1.00 13.37 ?  42  TYR   B CA   1 
ATOM   4720 C  C    . TYR   B 1 42  ? 48.373 -16.152 10.038  1.00 12.90 ?  42  TYR   B C    1 
ATOM   4721 O  O    . TYR   B 1 42  ? 49.467 -15.591 10.169  1.00 14.00 ?  42  TYR   B O    1 
ATOM   4722 C  CB   . TYR   B 1 42  ? 48.103 -16.630 12.523  1.00 15.31 ?  42  TYR   B CB   1 
ATOM   4723 C  CG   . TYR   B 1 42  ? 47.496 -15.951 13.748  1.00 15.42 ?  42  TYR   B CG   1 
ATOM   4724 C  CD1  . TYR   B 1 42  ? 47.704 -14.596 13.981  1.00 14.78 ?  42  TYR   B CD1  1 
ATOM   4725 C  CD2  . TYR   B 1 42  ? 46.715 -16.653 14.653  1.00 17.37 ?  42  TYR   B CD2  1 
ATOM   4726 C  CE1  . TYR   B 1 42  ? 47.157 -13.960 15.075  1.00 15.79 ?  42  TYR   B CE1  1 
ATOM   4727 C  CE2  . TYR   B 1 42  ? 46.166 -16.024 15.759  1.00 17.65 ?  42  TYR   B CE2  1 
ATOM   4728 C  CZ   . TYR   B 1 42  ? 46.388 -14.673 15.966  1.00 17.46 ?  42  TYR   B CZ   1 
ATOM   4729 O  OH   . TYR   B 1 42  ? 45.849 -14.035 17.066  1.00 20.60 ?  42  TYR   B OH   1 
ATOM   4730 H  H    . TYR   B 1 42  ? 46.400 -17.912 11.058  1.00 15.58 ?  42  TYR   B H    1 
ATOM   4731 H  HA   . TYR   B 1 42  ? 47.085 -15.322 11.351  1.00 16.04 ?  42  TYR   B HA   1 
ATOM   4732 H  HB2  . TYR   B 1 42  ? 48.023 -17.588 12.640  1.00 18.37 ?  42  TYR   B HB2  1 
ATOM   4733 H  HB3  . TYR   B 1 42  ? 49.040 -16.379 12.473  1.00 18.37 ?  42  TYR   B HB3  1 
ATOM   4734 H  HD1  . TYR   B 1 42  ? 48.225 -14.106 13.376  1.00 17.74 ?  42  TYR   B HD1  1 
ATOM   4735 H  HD2  . TYR   B 1 42  ? 46.562 -17.561 14.513  1.00 20.84 ?  42  TYR   B HD2  1 
ATOM   4736 H  HE1  . TYR   B 1 42  ? 47.311 -13.052 15.211  1.00 18.95 ?  42  TYR   B HE1  1 
ATOM   4737 H  HE2  . TYR   B 1 42  ? 45.643 -16.509 16.355  1.00 21.18 ?  42  TYR   B HE2  1 
ATOM   4738 H  HH   . TYR   B 1 42  ? 46.065 -13.228 17.054  1.00 24.71 ?  42  TYR   B HH   1 
ATOM   4739 N  N    . LEU   B 1 43  ? 47.971 -16.672 8.880   1.00 11.86 ?  43  LEU   B N    1 
ATOM   4740 C  CA   . LEU   B 1 43  ? 48.783 -16.600 7.669   1.00 11.52 ?  43  LEU   B CA   1 
ATOM   4741 C  C    . LEU   B 1 43  ? 50.196 -17.111 7.924   1.00 11.70 ?  43  LEU   B C    1 
ATOM   4742 O  O    . LEU   B 1 43  ? 51.176 -16.523 7.471   1.00 12.49 ?  43  LEU   B O    1 
ATOM   4743 C  CB   . LEU   B 1 43  ? 48.803 -15.194 7.067   1.00 11.82 ?  43  LEU   B CB   1 
ATOM   4744 C  CG   . LEU   B 1 43  ? 47.446 -14.581 6.692   1.00 11.94 ?  43  LEU   B CG   1 
ATOM   4745 C  CD1  . LEU   B 1 43  ? 47.656 -13.190 6.104   1.00 13.63 ?  43  LEU   B CD1  1 
ATOM   4746 C  CD2  . LEU   B 1 43  ? 46.677 -15.476 5.732   1.00 12.03 ?  43  LEU   B CD2  1 
ATOM   4747 H  H    . LEU   B 1 43  ? 47.228 -17.089 8.766   1.00 14.23 ?  43  LEU   B H    1 
ATOM   4748 H  HA   . LEU   B 1 43  ? 48.385 -17.187 7.001   1.00 13.82 ?  43  LEU   B HA   1 
ATOM   4749 H  HB2  . LEU   B 1 43  ? 49.224 -14.601 7.708   1.00 14.19 ?  43  LEU   B HB2  1 
ATOM   4750 H  HB3  . LEU   B 1 43  ? 49.338 -15.222 6.258   1.00 14.19 ?  43  LEU   B HB3  1 
ATOM   4751 H  HG   . LEU   B 1 43  ? 46.918 -14.483 7.498   1.00 14.33 ?  43  LEU   B HG   1 
ATOM   4752 H  HD11 . LEU   B 1 43  ? 46.792 -12.813 5.873   1.00 16.36 ?  43  LEU   B HD11 1 
ATOM   4753 H  HD12 . LEU   B 1 43  ? 48.095 -12.630 6.764   1.00 16.36 ?  43  LEU   B HD12 1 
ATOM   4754 H  HD13 . LEU   B 1 43  ? 48.209 -13.262 5.310   1.00 16.36 ?  43  LEU   B HD13 1 
ATOM   4755 H  HD21 . LEU   B 1 43  ? 45.881 -15.008 5.434   1.00 14.44 ?  43  LEU   B HD21 1 
ATOM   4756 H  HD22 . LEU   B 1 43  ? 47.242 -15.684 4.972   1.00 14.44 ?  43  LEU   B HD22 1 
ATOM   4757 H  HD23 . LEU   B 1 43  ? 46.428 -16.292 6.193   1.00 14.44 ?  43  LEU   B HD23 1 
ATOM   4758 N  N    . LYS   B 1 44  ? 50.295 -18.231 8.645   1.00 11.80 ?  44  LYS   B N    1 
ATOM   4759 C  CA   . LYS   B 1 44  ? 51.560 -18.916 8.884   1.00 12.64 ?  44  LYS   B CA   1 
ATOM   4760 C  C    . LYS   B 1 44  ? 51.679 -20.037 7.860   1.00 12.23 ?  44  LYS   B C    1 
ATOM   4761 O  O    . LYS   B 1 44  ? 50.978 -21.050 7.947   1.00 13.53 ?  44  LYS   B O    1 
ATOM   4762 C  CB   . LYS   B 1 44  ? 51.612 -19.428 10.322  1.00 14.14 ?  44  LYS   B CB   1 
ATOM   4763 C  CG   . LYS   B 1 44  ? 51.793 -18.310 11.341  1.00 16.97 ?  44  LYS   B CG   1 
ATOM   4764 C  CD   . LYS   B 1 44  ? 52.994 -17.445 10.945  1.00 20.53 ?  44  LYS   B CD   1 
ATOM   4765 C  CE   . LYS   B 1 44  ? 53.495 -16.556 12.052  1.00 23.48 ?  44  LYS   B CE   1 
ATOM   4766 N  NZ   . LYS   B 1 44  ? 54.703 -15.789 11.654  1.00 24.99 ?  44  LYS   B NZ   1 
ATOM   4767 H  H    . LYS   B 1 44  ? 49.620 -18.616 9.017   1.00 14.16 ?  44  LYS   B H    1 
ATOM   4768 H  HA   . LYS   B 1 44  ? 52.294 -18.307 8.721   1.00 15.17 ?  44  LYS   B HA   1 
ATOM   4769 H  HB2  . LYS   B 1 44  ? 50.775 -19.879 10.527  1.00 16.97 ?  44  LYS   B HB2  1 
ATOM   4770 H  HB3  . LYS   B 1 44  ? 52.352 -20.040 10.417  1.00 16.97 ?  44  LYS   B HB3  1 
ATOM   4771 H  HG2  . LYS   B 1 44  ? 51.000 -17.756 11.365  1.00 20.36 ?  44  LYS   B HG2  1 
ATOM   4772 H  HG3  . LYS   B 1 44  ? 51.966 -18.698 12.217  1.00 20.36 ?  44  LYS   B HG3  1 
ATOM   4773 H  HD2  . LYS   B 1 44  ? 53.718 -18.032 10.659  1.00 24.63 ?  44  LYS   B HD2  1 
ATOM   4774 H  HD3  . LYS   B 1 44  ? 52.729 -16.871 10.208  1.00 24.63 ?  44  LYS   B HD3  1 
ATOM   4775 H  HE2  . LYS   B 1 44  ? 52.805 -15.913 12.252  1.00 28.18 ?  44  LYS   B HE2  1 
ATOM   4776 H  HE3  . LYS   B 1 44  ? 53.707 -17.095 12.831  1.00 28.18 ?  44  LYS   B HE3  1 
ATOM   4777 H  HZ1  . LYS   B 1 44  ? 54.969 -15.272 12.327  1.00 29.98 ?  44  LYS   B HZ1  1 
ATOM   4778 H  HZ2  . LYS   B 1 44  ? 55.362 -16.344 11.435  1.00 29.98 ?  44  LYS   B HZ2  1 
ATOM   4779 H  HZ3  . LYS   B 1 44  ? 54.515 -15.272 10.951  1.00 29.98 ?  44  LYS   B HZ3  1 
ATOM   4780 N  N    . HIS   B 1 45  ? 52.528 -19.819 6.858   1.00 11.99 ?  45  HIS   B N    1 
ATOM   4781 C  CA   . HIS   B 1 45  ? 52.553 -20.649 5.652   1.00 12.05 ?  45  HIS   B CA   1 
ATOM   4782 C  C    . HIS   B 1 45  ? 53.571 -21.774 5.815   1.00 14.23 ?  45  HIS   B C    1 
ATOM   4783 O  O    . HIS   B 1 45  ? 54.635 -21.795 5.200   1.00 16.51 ?  45  HIS   B O    1 
ATOM   4784 C  CB   . HIS   B 1 45  ? 52.868 -19.794 4.436   1.00 12.24 ?  45  HIS   B CB   1 
ATOM   4785 C  CG   . HIS   B 1 45  ? 51.997 -18.591 4.325   1.00 11.99 ?  45  HIS   B CG   1 
ATOM   4786 N  ND1  . HIS   B 1 45  ? 50.620 -18.669 4.294   1.00 11.72 ?  45  HIS   B ND1  1 
ATOM   4787 C  CD2  . HIS   B 1 45  ? 52.315 -17.279 4.249   1.00 12.88 ?  45  HIS   B CD2  1 
ATOM   4788 C  CE1  . HIS   B 1 45  ? 50.133 -17.445 4.193   1.00 11.77 ?  45  HIS   B CE1  1 
ATOM   4789 N  NE2  . HIS   B 1 45  ? 51.137 -16.586 4.160   1.00 12.18 ?  45  HIS   B NE2  1 
ATOM   4790 H  H    . HIS   B 1 45  ? 53.093 -19.175 6.842   1.00 14.39 ?  45  HIS   B H    1 
ATOM   4791 H  HA   . HIS   B 1 45  ? 51.670 -21.045 5.517   1.00 14.46 ?  45  HIS   B HA   1 
ATOM   4792 H  HB2  . HIS   B 1 45  ? 53.788 -19.496 4.492   1.00 14.68 ?  45  HIS   B HB2  1 
ATOM   4793 H  HB3  . HIS   B 1 45  ? 52.745 -20.331 3.632   1.00 14.68 ?  45  HIS   B HB3  1 
ATOM   4794 H  HD2  . HIS   B 1 45  ? 53.171 -16.913 4.256   1.00 15.45 ?  45  HIS   B HD2  1 
ATOM   4795 H  HE1  . HIS   B 1 45  ? 49.231 -17.227 4.141   1.00 14.12 ?  45  HIS   B HE1  1 
ATOM   4796 H  HE2  . HIS   B 1 45  ? 51.060 -15.729 4.109   1.00 14.61 ?  45  HIS   B HE2  1 
ATOM   4797 N  N    A GLY   B 1 46  ? 53.195 -22.749 6.639   0.58 15.17 ?  46  GLY   B N    1 
ATOM   4798 N  N    B GLY   B 1 46  ? 53.211 -22.730 6.662   0.42 15.22 ?  46  GLY   B N    1 
ATOM   4799 C  CA   A GLY   B 1 46  ? 54.123 -23.789 7.045   0.58 16.93 ?  46  GLY   B CA   1 
ATOM   4800 C  CA   B GLY   B 1 46  ? 54.135 -23.788 7.009   0.42 16.59 ?  46  GLY   B CA   1 
ATOM   4801 C  C    A GLY   B 1 46  ? 54.189 -25.027 6.175   0.58 18.39 ?  46  GLY   B C    1 
ATOM   4802 C  C    B GLY   B 1 46  ? 54.172 -24.927 6.011   0.42 17.80 ?  46  GLY   B C    1 
ATOM   4803 O  O    A GLY   B 1 46  ? 55.281 -25.495 5.838   0.58 20.78 ?  46  GLY   B O    1 
ATOM   4804 O  O    B GLY   B 1 46  ? 55.205 -25.192 5.387   0.42 19.01 ?  46  GLY   B O    1 
ATOM   4805 H  H    A GLY   B 1 46  ? 52.408 -22.815 6.991   0.58 18.20 ?  46  GLY   B H    1 
ATOM   4806 H  H    B GLY   B 1 46  ? 52.441 -22.777 7.052   0.42 18.26 ?  46  GLY   B H    1 
ATOM   4807 H  HA2  A GLY   B 1 46  ? 55.012 -23.405 7.087   0.58 20.32 ?  46  GLY   B HA2  1 
ATOM   4808 H  HA2  B GLY   B 1 46  ? 55.026 -23.414 7.076   0.42 19.91 ?  46  GLY   B HA2  1 
ATOM   4809 H  HA3  A GLY   B 1 46  ? 53.883 -24.083 7.936   0.58 20.32 ?  46  GLY   B HA3  1 
ATOM   4810 H  HA3  B GLY   B 1 46  ? 53.891 -24.141 7.880   0.42 19.91 ?  46  GLY   B HA3  1 
ATOM   4811 N  N    . GLY   B 1 47  ? 53.037 -25.598 5.829   1.00 17.94 ?  47  GLY   B N    1 
ATOM   4812 C  CA   . GLY   B 1 47  ? 52.990 -26.865 5.131   1.00 15.76 ?  47  GLY   B CA   1 
ATOM   4813 C  C    . GLY   B 1 47  ? 52.067 -26.843 3.928   1.00 13.68 ?  47  GLY   B C    1 
ATOM   4814 O  O    . GLY   B 1 47  ? 51.413 -25.842 3.634   1.00 13.85 ?  47  GLY   B O    1 
ATOM   4815 H  H    A GLY   B 1 47  ? 52.260 -25.276 6.017   0.58 21.52 ?  47  GLY   B H    1 
ATOM   4816 H  H    B GLY   B 1 47  ? 52.267 -25.326 6.104   0.42 21.52 ?  47  GLY   B H    1 
ATOM   4817 H  HA2  . GLY   B 1 47  ? 53.879 -27.107 4.828   1.00 18.92 ?  47  GLY   B HA2  1 
ATOM   4818 H  HA3  . GLY   B 1 47  ? 52.683 -27.556 5.743   1.00 18.92 ?  47  GLY   B HA3  1 
ATOM   4819 N  N    . GLY   B 1 48  ? 52.016 -27.984 3.245   1.00 12.77 ?  48  GLY   B N    1 
ATOM   4820 C  CA   . GLY   B 1 48  ? 51.096 -28.136 2.137   1.00 12.90 ?  48  GLY   B CA   1 
ATOM   4821 C  C    . GLY   B 1 48  ? 51.222 -27.026 1.120   1.00 11.90 ?  48  GLY   B C    1 
ATOM   4822 O  O    . GLY   B 1 48  ? 52.318 -26.558 0.803   1.00 12.52 ?  48  GLY   B O    1 
ATOM   4823 H  H    . GLY   B 1 48  ? 52.508 -28.668 3.400   1.00 15.32 ?  48  GLY   B H    1 
ATOM   4824 H  HA2  . GLY   B 1 48  ? 51.266 -28.985 1.692   1.00 15.48 ?  48  GLY   B HA2  1 
ATOM   4825 H  HA3  . GLY   B 1 48  ? 50.186 -28.144 2.469   1.00 15.48 ?  48  GLY   B HA3  1 
ATOM   4826 N  N    . VAL   B 1 49  ? 50.075 -26.596 0.595   1.00 12.06 ?  49  VAL   B N    1 
ATOM   4827 C  CA   . VAL   B 1 49  ? 50.052 -25.570 -0.446  1.00 12.06 ?  49  VAL   B CA   1 
ATOM   4828 C  C    . VAL   B 1 49  ? 50.710 -24.282 0.037   1.00 11.17 ?  49  VAL   B C    1 
ATOM   4829 O  O    . VAL   B 1 49  ? 51.493 -23.662 -0.690  1.00 11.91 ?  49  VAL   B O    1 
ATOM   4830 C  CB   . VAL   B 1 49  ? 48.605 -25.321 -0.915  1.00 13.28 ?  49  VAL   B CB   1 
ATOM   4831 C  CG1  . VAL   B 1 49  ? 48.531 -24.081 -1.796  1.00 13.11 ?  49  VAL   B CG1  1 
ATOM   4832 C  CG2  . VAL   B 1 49  ? 48.059 -26.536 -1.655  1.00 14.71 ?  49  VAL   B CG2  1 
ATOM   4833 H  H    . VAL   B 1 49  ? 49.293 -26.881 0.823   1.00 14.48 ?  49  VAL   B H    1 
ATOM   4834 H  HA   . VAL   B 1 49  ? 50.551 -25.890 -1.212  1.00 14.47 ?  49  VAL   B HA   1 
ATOM   4835 H  HB   . VAL   B 1 49  ? 48.041 -25.169 -0.141  1.00 15.93 ?  49  VAL   B HB   1 
ATOM   4836 H  HG11 . VAL   B 1 49  ? 47.698 -24.096 -2.297  1.00 15.74 ?  49  VAL   B HG11 1 
ATOM   4837 H  HG12 . VAL   B 1 49  ? 48.555 -23.287 -1.234  1.00 15.74 ?  49  VAL   B HG12 1 
ATOM   4838 H  HG13 . VAL   B 1 49  ? 49.281 -24.078 -2.407  1.00 15.74 ?  49  VAL   B HG13 1 
ATOM   4839 H  HG21 . VAL   B 1 49  ? 47.147 -26.354 -1.937  1.00 17.65 ?  49  VAL   B HG21 1 
ATOM   4840 H  HG22 . VAL   B 1 49  ? 48.615 -26.709 -2.431  1.00 17.65 ?  49  VAL   B HG22 1 
ATOM   4841 H  HG23 . VAL   B 1 49  ? 48.074 -27.300 -1.059  1.00 17.65 ?  49  VAL   B HG23 1 
ATOM   4842 N  N    . ALA   B 1 50  ? 50.367 -23.832 1.244   1.00 11.09 ?  50  ALA   B N    1 
ATOM   4843 C  CA   . ALA   B 1 50  ? 50.889 -22.555 1.722   1.00 11.03 ?  50  ALA   B CA   1 
ATOM   4844 C  C    . ALA   B 1 50  ? 52.408 -22.586 1.825   1.00 11.07 ?  50  ALA   B C    1 
ATOM   4845 O  O    . ALA   B 1 50  ? 53.089 -21.622 1.454   1.00 11.14 ?  50  ALA   B O    1 
ATOM   4846 C  CB   . ALA   B 1 50  ? 50.265 -22.205 3.069   1.00 11.53 ?  50  ALA   B CB   1 
ATOM   4847 H  H    . ALA   B 1 50  ? 49.846 -24.237 1.793   1.00 13.30 ?  50  ALA   B H    1 
ATOM   4848 H  HA   . ALA   B 1 50  ? 50.653 -21.860 1.094   1.00 13.23 ?  50  ALA   B HA   1 
ATOM   4849 H  HB1  . ALA   B 1 50  ? 50.620 -21.354 3.373   1.00 13.84 ?  50  ALA   B HB1  1 
ATOM   4850 H  HB2  . ALA   B 1 50  ? 49.301 -22.140 2.963   1.00 13.84 ?  50  ALA   B HB2  1 
ATOM   4851 H  HB3  . ALA   B 1 50  ? 50.479 -22.900 3.711   1.00 13.84 ?  50  ALA   B HB3  1 
ATOM   4852 N  N    . GLY   B 1 51  ? 52.958 -23.678 2.343   1.00 11.51 ?  51  GLY   B N    1 
ATOM   4853 C  CA   . GLY   B 1 51  ? 54.402 -23.784 2.412   1.00 12.35 ?  51  GLY   B CA   1 
ATOM   4854 C  C    . GLY   B 1 51  ? 55.049 -23.734 1.044   1.00 12.20 ?  51  GLY   B C    1 
ATOM   4855 O  O    . GLY   B 1 51  ? 56.096 -23.106 0.867   1.00 13.19 ?  51  GLY   B O    1 
ATOM   4856 H  H    . GLY   B 1 51  ? 52.528 -24.357 2.651   1.00 13.81 ?  51  GLY   B H    1 
ATOM   4857 H  HA2  . GLY   B 1 51  ? 54.758 -23.056 2.942   1.00 14.82 ?  51  GLY   B HA2  1 
ATOM   4858 H  HA3  . GLY   B 1 51  ? 54.647 -24.623 2.836   1.00 14.82 ?  51  GLY   B HA3  1 
ATOM   4859 N  N    . ALA   B 1 52  ? 54.444 -24.404 0.062   1.00 11.81 ?  52  ALA   B N    1 
ATOM   4860 C  CA   . ALA   B 1 52  ? 55.005 -24.413 -1.281  1.00 12.08 ?  52  ALA   B CA   1 
ATOM   4861 C  C    . ALA   B 1 52  ? 54.925 -23.037 -1.930  1.00 11.46 ?  52  ALA   B C    1 
ATOM   4862 O  O    . ALA   B 1 52  ? 55.893 -22.586 -2.563  1.00 12.28 ?  52  ALA   B O    1 
ATOM   4863 C  CB   . ALA   B 1 52  ? 54.289 -25.453 -2.138  1.00 13.05 ?  52  ALA   B CB   1 
ATOM   4864 H  H    . ALA   B 1 52  ? 53.709 -24.850 0.148   1.00 14.17 ?  52  ALA   B H    1 
ATOM   4865 H  HA   . ALA   B 1 52  ? 55.937 -24.660 -1.228  1.00 14.50 ?  52  ALA   B HA   1 
ATOM   4866 H  HB1  . ALA   B 1 52  ? 54.677 -25.450 -3.030  1.00 15.66 ?  52  ALA   B HB1  1 
ATOM   4867 H  HB2  . ALA   B 1 52  ? 54.409 -26.330 -1.735  1.00 15.66 ?  52  ALA   B HB2  1 
ATOM   4868 H  HB3  . ALA   B 1 52  ? 53.347 -25.238 -2.186  1.00 15.66 ?  52  ALA   B HB3  1 
ATOM   4869 N  N    . LEU   B 1 53  ? 53.780 -22.357 -1.804  1.00 11.32 ?  53  LEU   B N    1 
ATOM   4870 C  CA   . LEU   B 1 53  ? 53.665 -21.016 -2.373  1.00 11.50 ?  53  LEU   B CA   1 
ATOM   4871 C  C    . LEU   B 1 53  ? 54.668 -20.069 -1.729  1.00 11.59 ?  53  LEU   B C    1 
ATOM   4872 O  O    . LEU   B 1 53  ? 55.378 -19.326 -2.420  1.00 12.34 ?  53  LEU   B O    1 
ATOM   4873 C  CB   . LEU   B 1 53  ? 52.241 -20.473 -2.205  1.00 11.94 ?  53  LEU   B CB   1 
ATOM   4874 C  CG   . LEU   B 1 53  ? 51.109 -21.203 -2.937  1.00 12.25 ?  53  LEU   B CG   1 
ATOM   4875 C  CD1  . LEU   B 1 53  ? 49.764 -20.605 -2.577  1.00 13.52 ?  53  LEU   B CD1  1 
ATOM   4876 C  CD2  . LEU   B 1 53  ? 51.303 -21.184 -4.450  1.00 14.04 ?  53  LEU   B CD2  1 
ATOM   4877 H  H    . LEU   B 1 53  ? 53.071 -22.642 -1.408  1.00 13.59 ?  53  LEU   B H    1 
ATOM   4878 H  HA   . LEU   B 1 53  ? 53.864 -21.058 -3.324  1.00 13.80 ?  53  LEU   B HA   1 
ATOM   4879 H  HB2  . LEU   B 1 53  ? 52.026 -20.490 -1.263  1.00 14.33 ?  53  LEU   B HB2  1 
ATOM   4880 H  HB3  . LEU   B 1 53  ? 52.235 -19.554 -2.518  1.00 14.33 ?  53  LEU   B HB3  1 
ATOM   4881 H  HG   . LEU   B 1 53  ? 51.101 -22.127 -2.656  1.00 14.70 ?  53  LEU   B HG   1 
ATOM   4882 H  HD11 . LEU   B 1 53  ? 49.065 -21.089 -3.051  1.00 16.23 ?  53  LEU   B HD11 1 
ATOM   4883 H  HD12 . LEU   B 1 53  ? 49.626 -20.691 -1.619  1.00 16.23 ?  53  LEU   B HD12 1 
ATOM   4884 H  HD13 . LEU   B 1 53  ? 49.748 -19.671 -2.831  1.00 16.23 ?  53  LEU   B HD13 1 
ATOM   4885 H  HD21 . LEU   B 1 53  ? 50.614 -21.728 -4.865  1.00 16.85 ?  53  LEU   B HD21 1 
ATOM   4886 H  HD22 . LEU   B 1 53  ? 51.232 -20.270 -4.769  1.00 16.85 ?  53  LEU   B HD22 1 
ATOM   4887 H  HD23 . LEU   B 1 53  ? 52.177 -21.543 -4.665  1.00 16.85 ?  53  LEU   B HD23 1 
ATOM   4888 N  N    . ASN   B 1 54  ? 54.764 -20.100 -0.402  1.00 11.23 ?  54  ASN   B N    1 
ATOM   4889 C  CA   . ASN   B 1 54  ? 55.681 -19.193 0.268   1.00 12.02 ?  54  ASN   B CA   1 
ATOM   4890 C  C    . ASN   B 1 54  ? 57.123 -19.478 -0.135  1.00 12.30 ?  54  ASN   B C    1 
ATOM   4891 O  O    . ASN   B 1 54  ? 57.904 -18.544 -0.367  1.00 12.68 ?  54  ASN   B O    1 
ATOM   4892 C  CB   . ASN   B 1 54  ? 55.523 -19.272 1.779   1.00 12.74 ?  54  ASN   B CB   1 
ATOM   4893 C  CG   . ASN   B 1 54  ? 56.503 -18.365 2.483   1.00 12.99 ?  54  ASN   B CG   1 
ATOM   4894 O  OD1  . ASN   B 1 54  ? 56.523 -17.156 2.240   1.00 12.91 ?  54  ASN   B OD1  1 
ATOM   4895 N  ND2  . ASN   B 1 54  ? 57.346 -18.939 3.330   1.00 14.17 ?  54  ASN   B ND2  1 
ATOM   4896 H  H    . ASN   B 1 54  ? 54.322 -20.627 0.118   1.00 13.48 ?  54  ASN   B H    1 
ATOM   4897 H  HA   . ASN   B 1 54  ? 55.470 -18.288 -0.005  1.00 14.42 ?  54  ASN   B HA   1 
ATOM   4898 H  HB2  . ASN   B 1 54  ? 54.627 -18.994 2.024   1.00 15.29 ?  54  ASN   B HB2  1 
ATOM   4899 H  HB3  . ASN   B 1 54  ? 55.688 -20.180 2.073   1.00 15.29 ?  54  ASN   B HB3  1 
ATOM   4900 H  HD21 . ASN   B 1 54  ? 57.933 -18.464 3.749   1.00 17.00 ?  54  ASN   B HD21 1 
ATOM   4901 H  HD22 . ASN   B 1 54  ? 57.313 -19.788 3.464   1.00 17.00 ?  54  ASN   B HD22 1 
ATOM   4902 N  N    . LYS   B 1 55  ? 57.501 -20.758 -0.207  1.00 12.73 ?  55  LYS   B N    1 
ATOM   4903 C  CA   . LYS   B 1 55  ? 58.858 -21.105 -0.620  1.00 13.88 ?  55  LYS   B CA   1 
ATOM   4904 C  C    . LYS   B 1 55  ? 59.159 -20.565 -2.012  1.00 13.51 ?  55  LYS   B C    1 
ATOM   4905 O  O    . LYS   B 1 55  ? 60.259 -20.056 -2.263  1.00 13.90 ?  55  LYS   B O    1 
ATOM   4906 C  CB   . LYS   B 1 55  ? 59.051 -22.621 -0.570  1.00 15.37 ?  55  LYS   B CB   1 
ATOM   4907 C  CG   . LYS   B 1 55  ? 60.428 -23.090 -1.011  1.00 19.31 ?  55  LYS   B CG   1 
ATOM   4908 C  CD   . LYS   B 1 55  ? 60.603 -24.581 -0.790  1.00 22.63 ?  55  LYS   B CD   1 
ATOM   4909 C  CE   . LYS   B 1 55  ? 60.735 -24.928 0.693   1.00 25.72 ?  55  LYS   B CE   1 
ATOM   4910 N  NZ   . LYS   B 1 55  ? 61.074 -26.356 0.909   1.00 27.34 ?  55  LYS   B NZ   1 
ATOM   4911 H  H    . LYS   B 1 55  ? 56.993 -21.430 -0.028  1.00 15.28 ?  55  LYS   B H    1 
ATOM   4912 H  HA   . LYS   B 1 55  ? 59.484 -20.701 -0.005  1.00 16.65 ?  55  LYS   B HA   1 
ATOM   4913 H  HB2  . LYS   B 1 55  ? 58.915 -22.917 0.344   1.00 18.44 ?  55  LYS   B HB2  1 
ATOM   4914 H  HB3  . LYS   B 1 55  ? 58.398 -23.041 -1.150  1.00 18.44 ?  55  LYS   B HB3  1 
ATOM   4915 H  HG2  . LYS   B 1 55  ? 60.541 -22.909 -1.957  1.00 23.17 ?  55  LYS   B HG2  1 
ATOM   4916 H  HG3  . LYS   B 1 55  ? 61.105 -22.623 -0.497  1.00 23.17 ?  55  LYS   B HG3  1 
ATOM   4917 H  HD2  . LYS   B 1 55  ? 59.832 -25.055 -1.140  1.00 27.16 ?  55  LYS   B HD2  1 
ATOM   4918 H  HD3  . LYS   B 1 55  ? 61.411 -24.883 -1.239  1.00 27.16 ?  55  LYS   B HD3  1 
ATOM   4919 H  HE2  . LYS   B 1 55  ? 61.439 -24.381 1.081   1.00 30.86 ?  55  LYS   B HE2  1 
ATOM   4920 H  HE3  . LYS   B 1 55  ? 59.891 -24.742 1.136   1.00 30.86 ?  55  LYS   B HE3  1 
ATOM   4921 H  HZ1  . LYS   B 1 55  ? 61.107 -26.528 1.782   1.00 32.81 ?  55  LYS   B HZ1  1 
ATOM   4922 H  HZ2  . LYS   B 1 55  ? 60.453 -26.871 0.535   1.00 32.81 ?  55  LYS   B HZ2  1 
ATOM   4923 H  HZ3  . LYS   B 1 55  ? 61.863 -26.538 0.545   1.00 32.81 ?  55  LYS   B HZ3  1 
ATOM   4924 N  N    . ALA   B 1 56  ? 58.184 -20.643 -2.926  1.00 12.91 ?  56  ALA   B N    1 
ATOM   4925 C  CA   . ALA   B 1 56  ? 58.407 -20.146 -4.278  1.00 13.78 ?  56  ALA   B CA   1 
ATOM   4926 C  C    . ALA   B 1 56  ? 58.690 -18.650 -4.275  1.00 13.44 ?  56  ALA   B C    1 
ATOM   4927 O  O    . ALA   B 1 56  ? 59.409 -18.151 -5.151  1.00 14.56 ?  56  ALA   B O    1 
ATOM   4928 C  CB   . ALA   B 1 56  ? 57.203 -20.467 -5.166  1.00 14.92 ?  56  ALA   B CB   1 
ATOM   4929 H  H    . ALA   B 1 56  ? 57.394 -20.961 -2.788  1.00 15.50 ?  56  ALA   B H    1 
ATOM   4930 H  HA   . ALA   B 1 56  ? 59.181 -20.590 -4.652  1.00 16.54 ?  56  ALA   B HA   1 
ATOM   4931 H  HB1  . ALA   B 1 56  ? 57.376 -20.136 -6.065  1.00 17.90 ?  56  ALA   B HB1  1 
ATOM   4932 H  HB2  . ALA   B 1 56  ? 57.078 -21.428 -5.191  1.00 17.90 ?  56  ALA   B HB2  1 
ATOM   4933 H  HB3  . ALA   B 1 56  ? 56.415 -20.038 -4.804  1.00 17.90 ?  56  ALA   B HB3  1 
ATOM   4934 N  N    . THR   B 1 57  ? 58.129 -17.919 -3.309  1.00 13.28 ?  57  THR   B N    1 
ATOM   4935 C  CA   . THR   B 1 57  ? 58.365 -16.483 -3.187  1.00 13.52 ?  57  THR   B CA   1 
ATOM   4936 C  C    . THR   B 1 57  ? 59.610 -16.154 -2.374  1.00 14.19 ?  57  THR   B C    1 
ATOM   4937 O  O    . THR   B 1 57  ? 59.851 -14.977 -2.071  1.00 14.54 ?  57  THR   B O    1 
ATOM   4938 C  CB   . THR   B 1 57  ? 57.161 -15.755 -2.557  1.00 12.63 ?  57  THR   B CB   1 
ATOM   4939 O  OG1  . THR   B 1 57  ? 57.135 -15.960 -1.136  1.00 13.15 ?  57  THR   B OG1  1 
ATOM   4940 C  CG2  . THR   B 1 57  ? 55.848 -16.186 -3.198  1.00 12.89 ?  57  THR   B CG2  1 
ATOM   4941 H  H    . THR   B 1 57  ? 57.590 -18.235 -2.716  1.00 15.93 ?  57  THR   B H    1 
ATOM   4942 H  HA   . THR   B 1 57  ? 58.487 -16.120 -4.078  1.00 16.22 ?  57  THR   B HA   1 
ATOM   4943 H  HB   . THR   B 1 57  ? 57.260 -14.806 -2.732  1.00 15.15 ?  57  THR   B HB   1 
ATOM   4944 H  HG1  . THR   B 1 57  ? 57.057 -16.782 -0.973  1.00 15.78 ?  57  THR   B HG1  1 
ATOM   4945 H  HG21 . THR   B 1 57  ? 55.120 -15.641 -2.868  1.00 15.46 ?  57  THR   B HG21 1 
ATOM   4946 H  HG22 . THR   B 1 57  ? 55.899 -16.096 -4.164  1.00 15.46 ?  57  THR   B HG22 1 
ATOM   4947 H  HG23 . THR   B 1 57  ? 55.664 -17.116 -2.985  1.00 15.46 ?  57  THR   B HG23 1 
ATOM   4948 N  N    . ASN   B 1 58  ? 60.407 -17.157 -2.017  1.00 14.97 ?  58  ASN   B N    1 
ATOM   4949 C  CA   . ASN   B 1 58  ? 61.605 -16.938 -1.213  1.00 18.28 ?  58  ASN   B CA   1 
ATOM   4950 C  C    . ASN   B 1 58  ? 61.266 -16.231 0.100   1.00 15.71 ?  58  ASN   B C    1 
ATOM   4951 O  O    . ASN   B 1 58  ? 62.003 -15.361 0.570   1.00 16.41 ?  58  ASN   B O    1 
ATOM   4952 C  CB   . ASN   B 1 58  ? 62.684 -16.183 -1.996  1.00 26.23 ?  58  ASN   B CB   1 
ATOM   4953 C  CG   . ASN   B 1 58  ? 64.058 -16.318 -1.370  1.00 35.26 ?  58  ASN   B CG   1 
ATOM   4954 O  OD1  . ASN   B 1 58  ? 64.366 -17.325 -0.732  1.00 37.45 ?  58  ASN   B OD1  1 
ATOM   4955 N  ND2  . ASN   B 1 58  ? 64.893 -15.301 -1.548  1.00 41.62 ?  58  ASN   B ND2  1 
ATOM   4956 H  H    . ASN   B 1 58  ? 60.275 -17.986 -2.228  1.00 17.97 ?  58  ASN   B H    1 
ATOM   4957 H  HA   . ASN   B 1 58  ? 61.975 -17.805 -0.992  1.00 21.94 ?  58  ASN   B HA   1 
ATOM   4958 H  HB2  . ASN   B 1 58  ? 62.730 -16.537 -2.902  1.00 31.48 ?  58  ASN   B HB2  1 
ATOM   4959 H  HB3  . ASN   B 1 58  ? 62.459 -15.240 -2.023  1.00 31.48 ?  58  ASN   B HB3  1 
ATOM   4960 H  HD21 . ASN   B 1 58  ? 65.685 -15.331 -1.214  1.00 49.94 ?  58  ASN   B HD21 1 
ATOM   4961 H  HD22 . ASN   B 1 58  ? 64.642 -14.612 -1.998  1.00 49.94 ?  58  ASN   B HD22 1 
ATOM   4962 N  N    . ASN   B 1 59  ? 60.140 -16.614 0.701   1.00 14.53 ?  59  ASN   B N    1 
ATOM   4963 C  CA   . ASN   B 1 59  ? 59.665 -16.134 2.000   1.00 14.31 ?  59  ASN   B CA   1 
ATOM   4964 C  C    . ASN   B 1 59  ? 59.074 -14.727 1.943   1.00 13.74 ?  59  ASN   B C    1 
ATOM   4965 O  O    . ASN   B 1 59  ? 58.645 -14.221 2.986   1.00 14.13 ?  59  ASN   B O    1 
ATOM   4966 C  CB   . ASN   B 1 59  ? 60.739 -16.183 3.101   1.00 15.57 ?  59  ASN   B CB   1 
ATOM   4967 C  CG   . ASN   B 1 59  ? 60.156 -16.370 4.481   1.00 16.45 ?  59  ASN   B CG   1 
ATOM   4968 O  OD1  . ASN   B 1 59  ? 59.341 -17.265 4.704   1.00 16.78 ?  59  ASN   B OD1  1 
ATOM   4969 N  ND2  . ASN   B 1 59  ? 60.576 -15.533 5.422   1.00 17.19 ?  59  ASN   B ND2  1 
ATOM   4970 H  H    . ASN   B 1 59  ? 59.601 -17.199 0.357   1.00 17.43 ?  59  ASN   B H    1 
ATOM   4971 H  HA   . ASN   B 1 59  ? 58.957 -16.728 2.287   1.00 17.17 ?  59  ASN   B HA   1 
ATOM   4972 H  HB2  . ASN   B 1 59  ? 61.339 -16.929 2.936   1.00 18.69 ?  59  ASN   B HB2  1 
ATOM   4973 H  HB3  . ASN   B 1 59  ? 61.235 -15.352 3.104   1.00 18.69 ?  59  ASN   B HB3  1 
ATOM   4974 H  HD21 . ASN   B 1 59  ? 60.269 -15.596 6.225   1.00 20.62 ?  59  ASN   B HD21 1 
ATOM   4975 H  HD22 . ASN   B 1 59  ? 61.144 -14.918 5.228   1.00 20.62 ?  59  ASN   B HD22 1 
ATOM   4976 N  N    . ALA   B 1 60  ? 59.016 -14.086 0.774   1.00 13.44 ?  60  ALA   B N    1 
ATOM   4977 C  CA   . ALA   B 1 60  ? 58.419 -12.756 0.701   1.00 13.72 ?  60  ALA   B CA   1 
ATOM   4978 C  C    . ALA   B 1 60  ? 56.952 -12.781 1.102   1.00 12.62 ?  60  ALA   B C    1 
ATOM   4979 O  O    . ALA   B 1 60  ? 56.451 -11.830 1.714   1.00 13.27 ?  60  ALA   B O    1 
ATOM   4980 C  CB   . ALA   B 1 60  ? 58.581 -12.173 -0.702  1.00 14.50 ?  60  ALA   B CB   1 
ATOM   4981 H  H    . ALA   B 1 60  ? 59.310 -14.396 0.028   1.00 16.13 ?  60  ALA   B H    1 
ATOM   4982 H  HA   . ALA   B 1 60  ? 58.882 -12.176 1.322   1.00 16.46 ?  60  ALA   B HA   1 
ATOM   4983 H  HB1  . ALA   B 1 60  ? 58.180 -11.293 -0.722  1.00 17.40 ?  60  ALA   B HB1  1 
ATOM   4984 H  HB2  . ALA   B 1 60  ? 59.528 -12.112 -0.907  1.00 17.40 ?  60  ALA   B HB2  1 
ATOM   4985 H  HB3  . ALA   B 1 60  ? 58.142 -12.757 -1.338  1.00 17.40 ?  60  ALA   B HB3  1 
ATOM   4986 N  N    . MET   B 1 61  ? 56.245 -13.857 0.758   1.00 12.32 ?  61  MET   B N    1 
ATOM   4987 C  CA   . MET   B 1 61  ? 54.847 -13.978 1.149   1.00 11.89 ?  61  MET   B CA   1 
ATOM   4988 C  C    . MET   B 1 61  ? 54.705 -13.987 2.670   1.00 11.84 ?  61  MET   B C    1 
ATOM   4989 O  O    . MET   B 1 61  ? 53.810 -13.337 3.222   1.00 11.63 ?  61  MET   B O    1 
ATOM   4990 C  CB   . MET   B 1 61  ? 54.269 -15.248 0.519   1.00 11.75 ?  61  MET   B CB   1 
ATOM   4991 C  CG   . MET   B 1 61  ? 52.826 -15.531 0.917   1.00 11.30 ?  61  MET   B CG   1 
ATOM   4992 S  SD   . MET   B 1 61  ? 52.178 -17.038 0.168   1.00 12.16 ?  61  MET   B SD   1 
ATOM   4993 C  CE   . MET   B 1 61  ? 51.908 -16.456 -1.501  1.00 13.40 ?  61  MET   B CE   1 
ATOM   4994 H  H    . MET   B 1 61  ? 56.549 -14.528 0.303   1.00 14.78 ?  61  MET   B H    1 
ATOM   4995 H  HA   . MET   B 1 61  ? 54.355 -13.225 0.790   1.00 14.27 ?  61  MET   B HA   1 
ATOM   4996 H  HB2  . MET   B 1 61  ? 54.294 -15.160 -0.448  1.00 14.10 ?  61  MET   B HB2  1 
ATOM   4997 H  HB3  . MET   B 1 61  ? 54.804 -16.008 0.793   1.00 14.10 ?  61  MET   B HB3  1 
ATOM   4998 H  HG2  . MET   B 1 61  ? 52.773 -15.633 1.882   1.00 13.56 ?  61  MET   B HG2  1 
ATOM   4999 H  HG3  . MET   B 1 61  ? 52.267 -14.786 0.635   1.00 13.56 ?  61  MET   B HG3  1 
ATOM   5000 H  HE1  . MET   B 1 61  ? 51.529 -17.177 -2.030  1.00 16.08 ?  61  MET   B HE1  1 
ATOM   5001 H  HE2  . MET   B 1 61  ? 51.290 -15.705 -1.482  1.00 16.08 ?  61  MET   B HE2  1 
ATOM   5002 H  HE3  . MET   B 1 61  ? 52.753 -16.175 -1.881  1.00 16.08 ?  61  MET   B HE3  1 
ATOM   5003 N  N    . GLN   B 1 62  ? 55.583 -14.708 3.368   1.00 11.95 ?  62  GLN   B N    1 
ATOM   5004 C  CA   . GLN   B 1 62  ? 55.482 -14.767 4.823   1.00 12.32 ?  62  GLN   B CA   1 
ATOM   5005 C  C    . GLN   B 1 62  ? 55.770 -13.410 5.456   1.00 12.43 ?  62  GLN   B C    1 
ATOM   5006 O  O    . GLN   B 1 62  ? 55.088 -13.008 6.404   1.00 13.00 ?  62  GLN   B O    1 
ATOM   5007 C  CB   . GLN   B 1 62  ? 56.433 -15.826 5.383   1.00 12.60 ?  62  GLN   B CB   1 
ATOM   5008 C  CG   . GLN   B 1 62  ? 56.220 -16.093 6.863   1.00 12.86 ?  62  GLN   B CG   1 
ATOM   5009 C  CD   . GLN   B 1 62  ? 54.845 -16.670 7.116   1.00 12.50 ?  62  GLN   B CD   1 
ATOM   5010 O  OE1  . GLN   B 1 62  ? 54.577 -17.820 6.760   1.00 12.88 ?  62  GLN   B OE1  1 
ATOM   5011 N  NE2  . GLN   B 1 62  ? 53.943 -15.863 7.668   1.00 12.66 ?  62  GLN   B NE2  1 
ATOM   5012 H  H    . GLN   B 1 62  ? 56.232 -15.164 3.026   1.00 14.34 ?  62  GLN   B H    1 
ATOM   5013 H  HA   . GLN   B 1 62  ? 54.576 -15.024 5.057   1.00 14.79 ?  62  GLN   B HA   1 
ATOM   5014 H  HB2  . GLN   B 1 62  ? 56.297 -16.662 4.907   1.00 15.12 ?  62  GLN   B HB2  1 
ATOM   5015 H  HB3  . GLN   B 1 62  ? 57.348 -15.525 5.261   1.00 15.12 ?  62  GLN   B HB3  1 
ATOM   5016 H  HG2  . GLN   B 1 62  ? 56.882 -16.735 7.168   1.00 15.43 ?  62  GLN   B HG2  1 
ATOM   5017 H  HG3  . GLN   B 1 62  ? 56.306 -15.263 7.355   1.00 15.43 ?  62  GLN   B HG3  1 
ATOM   5018 H  HE21 . GLN   B 1 62  ? 54.162 -15.059 7.885   1.00 15.19 ?  62  GLN   B HE21 1 
ATOM   5019 H  HE22 . GLN   B 1 62  ? 53.147 -16.147 7.819   1.00 15.19 ?  62  GLN   B HE22 1 
ATOM   5020 N  N    . VAL   B 1 63  ? 56.784 -12.697 4.964   1.00 13.03 ?  63  VAL   B N    1 
ATOM   5021 C  CA   . VAL   B 1 63  ? 57.091 -11.379 5.516   1.00 14.17 ?  63  VAL   B CA   1 
ATOM   5022 C  C    . VAL   B 1 63  ? 55.899 -10.446 5.338   1.00 13.18 ?  63  VAL   B C    1 
ATOM   5023 O  O    . VAL   B 1 63  ? 55.485 -9.741  6.271   1.00 13.96 ?  63  VAL   B O    1 
ATOM   5024 C  CB   . VAL   B 1 63  ? 58.378 -10.820 4.884   1.00 15.49 ?  63  VAL   B CB   1 
ATOM   5025 C  CG1  . VAL   B 1 63  ? 58.612 -9.379  5.329   1.00 16.21 ?  63  VAL   B CG1  1 
ATOM   5026 C  CG2  . VAL   B 1 63  ? 59.569 -11.695 5.266   1.00 16.16 ?  63  VAL   B CG2  1 
ATOM   5027 H  H    . VAL   B 1 63  ? 57.290 -12.946 4.313   1.00 15.63 ?  63  VAL   B H    1 
ATOM   5028 H  HA   . VAL   B 1 63  ? 57.250 -11.474 6.465   1.00 17.00 ?  63  VAL   B HA   1 
ATOM   5029 H  HB   . VAL   B 1 63  ? 58.296 -10.833 3.918   1.00 18.58 ?  63  VAL   B HB   1 
ATOM   5030 H  HG11 . VAL   B 1 63  ? 59.527 -9.135  5.130   1.00 19.46 ?  63  VAL   B HG11 1 
ATOM   5031 H  HG12 . VAL   B 1 63  ? 58.000 -8.800  4.850   1.00 19.46 ?  63  VAL   B HG12 1 
ATOM   5032 H  HG13 . VAL   B 1 63  ? 58.451 -9.319  6.284   1.00 19.46 ?  63  VAL   B HG13 1 
ATOM   5033 H  HG21 . VAL   B 1 63  ? 60.375 -11.320 4.878   1.00 19.40 ?  63  VAL   B HG21 1 
ATOM   5034 H  HG22 . VAL   B 1 63  ? 59.648 -11.714 6.235   1.00 19.40 ?  63  VAL   B HG22 1 
ATOM   5035 H  HG23 . VAL   B 1 63  ? 59.426 -12.593 4.930   1.00 19.40 ?  63  VAL   B HG23 1 
ATOM   5036 N  N    . GLU   B 1 64  ? 55.330 -10.427 4.132   1.00 12.69 ?  64  GLU   B N    1 
ATOM   5037 C  CA   . GLU   B 1 64  ? 54.164 -9.590  3.861   1.00 12.29 ?  64  GLU   B CA   1 
ATOM   5038 C  C    . GLU   B 1 64  ? 52.980 -9.997  4.733   1.00 12.07 ?  64  GLU   B C    1 
ATOM   5039 O  O    . GLU   B 1 64  ? 52.229 -9.142  5.231   1.00 12.59 ?  64  GLU   B O    1 
ATOM   5040 C  CB   . GLU   B 1 64  ? 53.807 -9.735  2.382   1.00 12.40 ?  64  GLU   B CB   1 
ATOM   5041 C  CG   . GLU   B 1 64  ? 52.533 -9.017  1.949   1.00 12.78 ?  64  GLU   B CG   1 
ATOM   5042 C  CD   . GLU   B 1 64  ? 52.002 -9.516  0.619   1.00 13.49 ?  64  GLU   B CD   1 
ATOM   5043 O  OE1  . GLU   B 1 64  ? 52.184 -10.721 0.301   1.00 14.35 ?  64  GLU   B OE1  1 
ATOM   5044 O  OE2  . GLU   B 1 64  ? 51.385 -8.705  -0.107  1.00 14.28 -1 64  GLU   B OE2  1 
ATOM   5045 H  H    . GLU   B 1 64  ? 55.604 -10.886 3.453   1.00 15.22 ?  64  GLU   B H    1 
ATOM   5046 H  HA   . GLU   B 1 64  ? 54.379 -8.661  4.037   1.00 14.75 ?  64  GLU   B HA   1 
ATOM   5047 H  HB2  . GLU   B 1 64  ? 54.530 -9.366  1.845   1.00 14.87 ?  64  GLU   B HB2  1 
ATOM   5048 H  HB3  . GLU   B 1 64  ? 53.693 -10.671 2.176   1.00 14.87 ?  64  GLU   B HB3  1 
ATOM   5049 H  HG2  . GLU   B 1 64  ? 51.834 -9.156  2.614   1.00 15.34 ?  64  GLU   B HG2  1 
ATOM   5050 H  HG3  . GLU   B 1 64  ? 52.714 -8.066  1.868   1.00 15.34 ?  64  GLU   B HG3  1 
ATOM   5051 N  N    . SER   B 1 65  ? 52.795 -11.302 4.916   1.00 11.89 ?  65  SER   B N    1 
ATOM   5052 C  CA   . SER   B 1 65  ? 51.689 -11.808 5.717   1.00 11.97 ?  65  SER   B CA   1 
ATOM   5053 C  C    . SER   B 1 65  ? 51.824 -11.405 7.179   1.00 12.12 ?  65  SER   B C    1 
ATOM   5054 O  O    . SER   B 1 65  ? 50.829 -11.037 7.819   1.00 12.31 ?  65  SER   B O    1 
ATOM   5055 C  CB   . SER   B 1 65  ? 51.619 -13.329 5.589   1.00 12.18 ?  65  SER   B CB   1 
ATOM   5056 O  OG   . SER   B 1 65  ? 51.257 -13.728 4.278   1.00 12.11 ?  65  SER   B OG   1 
ATOM   5057 H  H    . SER   B 1 65  ? 53.297 -11.922 4.586   1.00 14.26 ?  65  SER   B H    1 
ATOM   5058 H  HA   . SER   B 1 65  ? 50.854 -11.441 5.376   1.00 14.36 ?  65  SER   B HA   1 
ATOM   5059 H  HB2  . SER   B 1 65  ? 52.484 -13.702 5.802   1.00 14.61 ?  65  SER   B HB2  1 
ATOM   5060 H  HB3  . SER   B 1 65  ? 50.952 -13.664 6.215   1.00 14.61 ?  65  SER   B HB3  1 
ATOM   5061 H  HG   . SER   B 1 65  ? 51.818 -13.443 3.721   1.00 14.53 ?  65  SER   B HG   1 
ATOM   5062 N  N    . ASP   B 1 66  ? 53.033 -11.501 7.742   1.00 12.41 ?  66  ASP   B N    1 
ATOM   5063 C  CA   . ASP   B 1 66  ? 53.218 -11.111 9.136   1.00 12.58 ?  66  ASP   B CA   1 
ATOM   5064 C  C    . ASP   B 1 66  ? 52.904 -9.632  9.333   1.00 12.98 ?  66  ASP   B C    1 
ATOM   5065 O  O    . ASP   B 1 66  ? 52.331 -9.241  10.355  1.00 13.62 ?  66  ASP   B O    1 
ATOM   5066 C  CB   . ASP   B 1 66  ? 54.647 -11.422 9.587   1.00 13.84 ?  66  ASP   B CB   1 
ATOM   5067 C  CG   . ASP   B 1 66  ? 54.920 -12.915 9.737   1.00 15.71 ?  66  ASP   B CG   1 
ATOM   5068 O  OD1  . ASP   B 1 66  ? 53.972 -13.727 9.669   1.00 16.48 ?  66  ASP   B OD1  1 
ATOM   5069 O  OD2  . ASP   B 1 66  ? 56.101 -13.276 9.942   1.00 18.46 -1 66  ASP   B OD2  1 
ATOM   5070 H  H    . ASP   B 1 66  ? 53.736 -11.787 7.347   1.00 14.89 ?  66  ASP   B H    1 
ATOM   5071 H  HA   . ASP   B 1 66  ? 52.608 -11.614 9.696   1.00 15.10 ?  66  ASP   B HA   1 
ATOM   5072 H  HB2  . ASP   B 1 66  ? 55.269 -11.076 8.931   1.00 16.61 ?  66  ASP   B HB2  1 
ATOM   5073 H  HB3  . ASP   B 1 66  ? 54.805 -10.999 10.449  1.00 16.61 ?  66  ASP   B HB3  1 
ATOM   5074 N  N    . ASP   B 1 67  ? 53.276 -8.792  8.366   1.00 12.47 ?  67  ASP   B N    1 
ATOM   5075 C  CA   . ASP   B 1 67  ? 52.935 -7.380  8.449   1.00 13.01 ?  67  ASP   B CA   1 
ATOM   5076 C  C    . ASP   B 1 67  ? 51.424 -7.173  8.366   1.00 13.25 ?  67  ASP   B C    1 
ATOM   5077 O  O    . ASP   B 1 67  ? 50.862 -6.371  9.118   1.00 13.83 ?  67  ASP   B O    1 
ATOM   5078 C  CB   . ASP   B 1 67  ? 53.649 -6.614  7.343   1.00 14.56 ?  67  ASP   B CB   1 
ATOM   5079 C  CG   . ASP   B 1 67  ? 53.218 -5.170  7.290   1.00 16.30 ?  67  ASP   B CG   1 
ATOM   5080 O  OD1  . ASP   B 1 67  ? 53.710 -4.351  8.103   1.00 17.42 ?  67  ASP   B OD1  1 
ATOM   5081 O  OD2  . ASP   B 1 67  ? 52.354 -4.869  6.450   1.00 17.15 -1 67  ASP   B OD2  1 
ATOM   5082 H  H    . ASP   B 1 67  ? 53.730 -9.015  7.668   1.00 14.96 ?  67  ASP   B H    1 
ATOM   5083 H  HA   . ASP   B 1 67  ? 53.241 -7.029  9.298   1.00 15.61 ?  67  ASP   B HA   1 
ATOM   5084 H  HB2  . ASP   B 1 67  ? 54.606 -6.640  7.502   1.00 17.47 ?  67  ASP   B HB2  1 
ATOM   5085 H  HB3  . ASP   B 1 67  ? 53.447 -7.030  6.486   1.00 17.47 ?  67  ASP   B HB3  1 
ATOM   5086 N  N    . TYR   B 1 68  ? 50.744 -7.905  7.475   1.00 13.03 ?  68  TYR   B N    1 
ATOM   5087 C  CA   . TYR   B 1 68  ? 49.286 -7.831  7.409   1.00 13.76 ?  68  TYR   B CA   1 
ATOM   5088 C  C    . TYR   B 1 68  ? 48.654 -8.175  8.755   1.00 13.30 ?  68  TYR   B C    1 
ATOM   5089 O  O    . TYR   B 1 68  ? 47.727 -7.493  9.208   1.00 14.05 ?  68  TYR   B O    1 
ATOM   5090 C  CB   . TYR   B 1 68  ? 48.749 -8.761  6.313   1.00 14.34 ?  68  TYR   B CB   1 
ATOM   5091 C  CG   . TYR   B 1 68  ? 47.242 -8.911  6.369   1.00 15.20 ?  68  TYR   B CG   1 
ATOM   5092 C  CD1  . TYR   B 1 68  ? 46.652 -9.871  7.188   1.00 16.24 ?  68  TYR   B CD1  1 
ATOM   5093 C  CD2  . TYR   B 1 68  ? 46.411 -8.068  5.649   1.00 16.32 ?  68  TYR   B CD2  1 
ATOM   5094 C  CE1  . TYR   B 1 68  ? 45.288 -9.991  7.281   1.00 17.10 ?  68  TYR   B CE1  1 
ATOM   5095 C  CE2  . TYR   B 1 68  ? 45.029 -8.192  5.727   1.00 16.71 ?  68  TYR   B CE2  1 
ATOM   5096 C  CZ   . TYR   B 1 68  ? 44.488 -9.150  6.551   1.00 16.90 ?  68  TYR   B CZ   1 
ATOM   5097 O  OH   . TYR   B 1 68  ? 43.121 -9.267  6.648   1.00 18.06 ?  68  TYR   B OH   1 
ATOM   5098 H  H    . TYR   B 1 68  ? 51.102 -8.458  6.915   1.00 15.63 ?  68  TYR   B H    1 
ATOM   5099 H  HA   . TYR   B 1 68  ? 49.035 -6.924  7.185   1.00 16.51 ?  68  TYR   B HA   1 
ATOM   5100 H  HB2  . TYR   B 1 68  ? 48.975 -8.394  5.447   1.00 17.21 ?  68  TYR   B HB2  1 
ATOM   5101 H  HB3  . TYR   B 1 68  ? 49.138 -9.640  6.420   1.00 17.21 ?  68  TYR   B HB3  1 
ATOM   5102 H  HD1  . TYR   B 1 68  ? 47.192 -10.442 7.687   1.00 19.49 ?  68  TYR   B HD1  1 
ATOM   5103 H  HD2  . TYR   B 1 68  ? 46.780 -7.411  5.110   1.00 19.59 ?  68  TYR   B HD2  1 
ATOM   5104 H  HE1  . TYR   B 1 68  ? 44.905 -10.651 7.822   1.00 20.52 ?  68  TYR   B HE1  1 
ATOM   5105 H  HE2  . TYR   B 1 68  ? 44.471 -7.622  5.245   1.00 20.05 ?  68  TYR   B HE2  1 
ATOM   5106 H  HH   . TYR   B 1 68  ? 42.732 -8.712  6.142   1.00 21.68 ?  68  TYR   B HH   1 
ATOM   5107 N  N    . ILE   B 1 69  ? 49.138 -9.239  9.404   1.00 12.99 ?  69  ILE   B N    1 
ATOM   5108 C  CA   . ILE   B 1 69  ? 48.581 -9.659  10.687  1.00 13.43 ?  69  ILE   B CA   1 
ATOM   5109 C  C    . ILE   B 1 69  ? 48.837 -8.610  11.761  1.00 13.26 ?  69  ILE   B C    1 
ATOM   5110 O  O    . ILE   B 1 69  ? 47.968 -8.328  12.593  1.00 13.57 ?  69  ILE   B O    1 
ATOM   5111 C  CB   . ILE   B 1 69  ? 49.151 -11.034 11.085  1.00 14.08 ?  69  ILE   B CB   1 
ATOM   5112 C  CG1  . ILE   B 1 69  ? 48.613 -12.139 10.169  1.00 14.91 ?  69  ILE   B CG1  1 
ATOM   5113 C  CG2  . ILE   B 1 69  ? 48.861 -11.345 12.550  1.00 14.97 ?  69  ILE   B CG2  1 
ATOM   5114 C  CD1  . ILE   B 1 69  ? 47.130 -12.413 10.310  1.00 15.26 ?  69  ILE   B CD1  1 
ATOM   5115 H  H    . ILE   B 1 69  ? 49.786 -9.726  9.127   1.00 15.59 ?  69  ILE   B H    1 
ATOM   5116 H  HA   . ILE   B 1 69  ? 47.623 -9.752  10.595  1.00 16.12 ?  69  ILE   B HA   1 
ATOM   5117 H  HB   . ILE   B 1 69  ? 50.116 -10.999 10.979  1.00 16.89 ?  69  ILE   B HB   1 
ATOM   5118 H  HG12 . ILE   B 1 69  ? 48.782 -11.883 9.249   1.00 17.89 ?  69  ILE   B HG12 1 
ATOM   5119 H  HG13 . ILE   B 1 69  ? 49.085 -12.963 10.370  1.00 17.89 ?  69  ILE   B HG13 1 
ATOM   5120 H  HG21 . ILE   B 1 69  ? 48.996 -12.295 12.700  1.00 17.96 ?  69  ILE   B HG21 1 
ATOM   5121 H  HG22 . ILE   B 1 69  ? 49.467 -10.837 13.113  1.00 17.96 ?  69  ILE   B HG22 1 
ATOM   5122 H  HG23 . ILE   B 1 69  ? 47.943 -11.107 12.748  1.00 17.96 ?  69  ILE   B HG23 1 
ATOM   5123 H  HD11 . ILE   B 1 69  ? 46.894 -13.153 9.736   1.00 18.31 ?  69  ILE   B HD11 1 
ATOM   5124 H  HD12 . ILE   B 1 69  ? 46.932 -12.632 11.234  1.00 18.31 ?  69  ILE   B HD12 1 
ATOM   5125 H  HD13 . ILE   B 1 69  ? 46.635 -11.619 10.046  1.00 18.31 ?  69  ILE   B HD13 1 
ATOM   5126 N  N    . ALA   B 1 70  ? 50.031 -8.026  11.783  1.00 13.34 ?  70  ALA   B N    1 
ATOM   5127 C  CA   . ALA   B 1 70  ? 50.306 -6.993  12.775  1.00 13.43 ?  70  ALA   B CA   1 
ATOM   5128 C  C    . ALA   B 1 70  ? 49.312 -5.849  12.657  1.00 14.05 ?  70  ALA   B C    1 
ATOM   5129 O  O    . ALA   B 1 70  ? 48.866 -5.297  13.667  1.00 14.37 ?  70  ALA   B O    1 
ATOM   5130 C  CB   . ALA   B 1 70  ? 51.735 -6.487  12.613  1.00 13.85 ?  70  ALA   B CB   1 
ATOM   5131 H  H    . ALA   B 1 70  ? 50.672 -8.201  11.250  1.00 16.00 ?  70  ALA   B H    1 
ATOM   5132 H  HA   . ALA   B 1 70  ? 50.220 -7.371  13.664  1.00 16.11 ?  70  ALA   B HA   1 
ATOM   5133 H  HB1  . ALA   B 1 70  ? 51.916 -5.823  13.299  1.00 16.62 ?  70  ALA   B HB1  1 
ATOM   5134 H  HB2  . ALA   B 1 70  ? 52.347 -7.234  12.709  1.00 16.62 ?  70  ALA   B HB2  1 
ATOM   5135 H  HB3  . ALA   B 1 70  ? 51.834 -6.090  11.734  1.00 16.62 ?  70  ALA   B HB3  1 
ATOM   5136 N  N    . THR   B 1 71  ? 48.946 -5.484  11.430  1.00 14.45 ?  71  THR   B N    1 
ATOM   5137 C  CA   . THR   B 1 71  ? 48.051 -4.352  11.212  1.00 15.19 ?  71  THR   B CA   1 
ATOM   5138 C  C    . THR   B 1 71  ? 46.584 -4.717  11.418  1.00 15.93 ?  71  THR   B C    1 
ATOM   5139 O  O    . THR   B 1 71  ? 45.803 -3.897  11.924  1.00 17.38 ?  71  THR   B O    1 
ATOM   5140 C  CB   . THR   B 1 71  ? 48.269 -3.786  9.806   1.00 16.98 ?  71  THR   B CB   1 
ATOM   5141 O  OG1  . THR   B 1 71  ? 49.600 -3.263  9.705   1.00 18.96 ?  71  THR   B OG1  1 
ATOM   5142 C  CG2  . THR   B 1 71  ? 47.265 -2.683  9.493   1.00 18.56 ?  71  THR   B CG2  1 
ATOM   5143 H  H    . THR   B 1 71  ? 49.204 -5.874  10.710  1.00 17.33 ?  71  THR   B H    1 
ATOM   5144 H  HA   . THR   B 1 71  ? 48.272 -3.652  11.845  1.00 18.22 ?  71  THR   B HA   1 
ATOM   5145 H  HB   . THR   B 1 71  ? 48.162 -4.488  9.148   1.00 20.38 ?  71  THR   B HB   1 
ATOM   5146 H  HG1  . THR   B 1 71  ? 49.728 -2.931  8.937   1.00 22.76 ?  71  THR   B HG1  1 
ATOM   5147 H  HG21 . THR   B 1 71  ? 47.565 -2.165  8.726   1.00 22.28 ?  71  THR   B HG21 1 
ATOM   5148 H  HG22 . THR   B 1 71  ? 46.399 -3.067  9.290   1.00 22.28 ?  71  THR   B HG22 1 
ATOM   5149 H  HG23 . THR   B 1 71  ? 47.178 -2.086  10.254  1.00 22.28 ?  71  THR   B HG23 1 
ATOM   5150 N  N    . ASN   B 1 72  ? 46.188 -5.931  11.032  1.00 15.64 ?  72  ASN   B N    1 
ATOM   5151 C  CA   . ASN   B 1 72  ? 44.784 -6.287  10.902  1.00 16.12 ?  72  ASN   B CA   1 
ATOM   5152 C  C    . ASN   B 1 72  ? 44.311 -7.386  11.843  1.00 16.38 ?  72  ASN   B C    1 
ATOM   5153 O  O    . ASN   B 1 72  ? 43.095 -7.542  12.013  1.00 17.94 ?  72  ASN   B O    1 
ATOM   5154 C  CB   . ASN   B 1 72  ? 44.479 -6.710  9.456   1.00 17.05 ?  72  ASN   B CB   1 
ATOM   5155 C  CG   . ASN   B 1 72  ? 44.762 -5.610  8.463   1.00 17.82 ?  72  ASN   B CG   1 
ATOM   5156 O  OD1  . ASN   B 1 72  ? 45.778 -5.624  7.759   1.00 18.77 ?  72  ASN   B OD1  1 
ATOM   5157 N  ND2  . ASN   B 1 72  ? 43.880 -4.632  8.417   1.00 19.50 ?  72  ASN   B ND2  1 
ATOM   5158 H  H    . ASN   B 1 72  ? 46.726 -6.581  10.836  1.00 18.77 ?  72  ASN   B H    1 
ATOM   5159 H  HA   . ASN   B 1 72  ? 44.252 -5.497  11.088  1.00 19.35 ?  72  ASN   B HA   1 
ATOM   5160 H  HB2  . ASN   B 1 72  ? 45.032 -7.471  9.223   1.00 20.46 ?  72  ASN   B HB2  1 
ATOM   5161 H  HB3  . ASN   B 1 72  ? 43.541 -6.944  9.384   1.00 20.46 ?  72  ASN   B HB3  1 
ATOM   5162 H  HD21 . ASN   B 1 72  ? 43.986 -3.975  7.870   1.00 23.40 ?  72  ASN   B HD21 1 
ATOM   5163 H  HD22 . ASN   B 1 72  ? 43.181 -4.654  8.923   1.00 23.40 ?  72  ASN   B HD22 1 
ATOM   5164 N  N    . GLY   B 1 73  ? 45.214 -8.141  12.459  1.00 15.73 ?  73  GLY   B N    1 
ATOM   5165 C  CA   . GLY   B 1 73  ? 44.822 -9.280  13.252  1.00 15.05 ?  73  GLY   B CA   1 
ATOM   5166 C  C    . GLY   B 1 73  ? 44.452 -10.466 12.390  1.00 13.98 ?  73  GLY   B C    1 
ATOM   5167 O  O    . GLY   B 1 73  ? 44.439 -10.389 11.159  1.00 13.86 ?  73  GLY   B O    1 
ATOM   5168 H  H    . GLY   B 1 73  ? 46.066 -8.006  12.432  1.00 18.88 ?  73  GLY   B H    1 
ATOM   5169 H  HA2  . GLY   B 1 73  ? 45.554 -9.535  13.836  1.00 18.06 ?  73  GLY   B HA2  1 
ATOM   5170 H  HA3  . GLY   B 1 73  ? 44.058 -9.044  13.802  1.00 18.06 ?  73  GLY   B HA3  1 
ATOM   5171 N  N    . PRO   B 1 74  ? 44.145 -11.587 13.036  1.00 14.39 ?  74  PRO   B N    1 
ATOM   5172 C  CA   . PRO   B 1 74  ? 43.889 -12.822 12.293  1.00 13.88 ?  74  PRO   B CA   1 
ATOM   5173 C  C    . PRO   B 1 74  ? 42.592 -12.764 11.506  1.00 13.03 ?  74  PRO   B C    1 
ATOM   5174 O  O    . PRO   B 1 74  ? 41.654 -12.030 11.836  1.00 14.36 ?  74  PRO   B O    1 
ATOM   5175 C  CB   . PRO   B 1 74  ? 43.812 -13.879 13.400  1.00 14.58 ?  74  PRO   B CB   1 
ATOM   5176 C  CG   . PRO   B 1 74  ? 43.371 -13.125 14.608  1.00 16.29 ?  74  PRO   B CG   1 
ATOM   5177 C  CD   . PRO   B 1 74  ? 44.043 -11.786 14.491  1.00 15.82 ?  74  PRO   B CD   1 
ATOM   5178 H  HA   . PRO   B 1 74  ? 44.630 -13.018 11.696  1.00 16.65 ?  74  PRO   B HA   1 
ATOM   5179 H  HB2  . PRO   B 1 74  ? 43.162 -14.557 13.157  1.00 17.50 ?  74  PRO   B HB2  1 
ATOM   5180 H  HB3  . PRO   B 1 74  ? 44.687 -14.272 13.539  1.00 17.50 ?  74  PRO   B HB3  1 
ATOM   5181 H  HG2  . PRO   B 1 74  ? 42.404 -13.028 14.596  1.00 19.55 ?  74  PRO   B HG2  1 
ATOM   5182 H  HG3  . PRO   B 1 74  ? 43.661 -13.587 15.407  1.00 19.55 ?  74  PRO   B HG3  1 
ATOM   5183 H  HD2  . PRO   B 1 74  ? 43.489 -11.093 14.894  1.00 18.98 ?  74  PRO   B HD2  1 
ATOM   5184 H  HD3  . PRO   B 1 74  ? 44.924 -11.810 14.890  1.00 18.98 ?  74  PRO   B HD3  1 
ATOM   5185 N  N    . LEU   B 1 75  ? 42.555 -13.572 10.451  1.00 12.55 ?  75  LEU   B N    1 
ATOM   5186 C  CA   . LEU   B 1 75  ? 41.343 -13.779 9.683   1.00 12.63 ?  75  LEU   B CA   1 
ATOM   5187 C  C    . LEU   B 1 75  ? 40.370 -14.642 10.483  1.00 13.09 ?  75  LEU   B C    1 
ATOM   5188 O  O    . LEU   B 1 75  ? 40.713 -15.212 11.519  1.00 14.02 ?  75  LEU   B O    1 
ATOM   5189 C  CB   . LEU   B 1 75  ? 41.665 -14.490 8.367   1.00 12.55 ?  75  LEU   B CB   1 
ATOM   5190 C  CG   . LEU   B 1 75  ? 42.520 -13.742 7.339   1.00 14.28 ?  75  LEU   B CG   1 
ATOM   5191 C  CD1  . LEU   B 1 75  ? 42.733 -14.578 6.081   1.00 15.68 ?  75  LEU   B CD1  1 
ATOM   5192 C  CD2  . LEU   B 1 75  ? 41.915 -12.410 6.982   1.00 17.56 ?  75  LEU   B CD2  1 
ATOM   5193 H  H    . LEU   B 1 75  ? 43.230 -14.024 10.160  1.00 15.06 ?  75  LEU   B H    1 
ATOM   5194 H  HA   . LEU   B 1 75  ? 40.924 -12.927 9.488   1.00 15.15 ?  75  LEU   B HA   1 
ATOM   5195 H  HB2  . LEU   B 1 75  ? 42.132 -15.313 8.577   1.00 15.06 ?  75  LEU   B HB2  1 
ATOM   5196 H  HB3  . LEU   B 1 75  ? 40.826 -14.706 7.929   1.00 15.06 ?  75  LEU   B HB3  1 
ATOM   5197 H  HG   . LEU   B 1 75  ? 43.394 -13.574 7.726   1.00 17.13 ?  75  LEU   B HG   1 
ATOM   5198 H  HD11 . LEU   B 1 75  ? 43.282 -14.075 5.454   1.00 18.81 ?  75  LEU   B HD11 1 
ATOM   5199 H  HD12 . LEU   B 1 75  ? 43.182 -15.404 6.319   1.00 18.81 ?  75  LEU   B HD12 1 
ATOM   5200 H  HD13 . LEU   B 1 75  ? 41.873 -14.773 5.678   1.00 18.81 ?  75  LEU   B HD13 1 
ATOM   5201 H  HD21 . LEU   B 1 75  ? 42.434 -12.006 6.270   1.00 21.07 ?  75  LEU   B HD21 1 
ATOM   5202 H  HD22 . LEU   B 1 75  ? 41.001 -12.547 6.690   1.00 21.07 ?  75  LEU   B HD22 1 
ATOM   5203 H  HD23 . LEU   B 1 75  ? 41.929 -11.837 7.766   1.00 21.07 ?  75  LEU   B HD23 1 
ATOM   5204 N  N    . LYS   B 1 76  ? 39.137 -14.730 9.984   1.00 14.26 ?  76  LYS   B N    1 
ATOM   5205 C  CA   . LYS   B 1 76  ? 38.155 -15.691 10.468  1.00 15.76 ?  76  LYS   B CA   1 
ATOM   5206 C  C    . LYS   B 1 76  ? 38.247 -16.966 9.634   1.00 14.41 ?  76  LYS   B C    1 
ATOM   5207 O  O    . LYS   B 1 76  ? 38.530 -16.911 8.439   1.00 13.96 ?  76  LYS   B O    1 
ATOM   5208 C  CB   . LYS   B 1 76  ? 36.736 -15.123 10.292  1.00 17.59 ?  76  LYS   B CB   1 
ATOM   5209 C  CG   . LYS   B 1 76  ? 36.455 -13.740 10.910  1.00 19.22 ?  76  LYS   B CG   1 
ATOM   5210 C  CD   . LYS   B 1 76  ? 35.046 -13.228 10.553  1.00 20.44 ?  76  LYS   B CD   1 
ATOM   5211 C  CE   . LYS   B 1 76  ? 34.766 -11.862 11.166  1.00 22.51 ?  76  LYS   B CE   1 
ATOM   5212 N  NZ   . LYS   B 1 76  ? 33.476 -11.270 10.713  1.00 23.30 ?  76  LYS   B NZ   1 
ATOM   5213 H  H    . LYS   B 1 76  ? 38.842 -14.236 9.341   1.00 17.11 ?  76  LYS   B H    1 
ATOM   5214 H  HA   . LYS   B 1 76  ? 38.311 -15.904 11.401  1.00 18.91 ?  76  LYS   B HA   1 
ATOM   5215 H  HB2  . LYS   B 1 76  ? 36.553 -15.053 9.343   1.00 21.10 ?  76  LYS   B HB2  1 
ATOM   5216 H  HB3  . LYS   B 1 76  ? 36.109 -15.746 10.694  1.00 21.10 ?  76  LYS   B HB3  1 
ATOM   5217 H  HG2  . LYS   B 1 76  ? 36.523 -13.804 11.876  1.00 23.06 ?  76  LYS   B HG2  1 
ATOM   5218 H  HG3  . LYS   B 1 76  ? 37.107 -13.104 10.571  1.00 23.06 ?  76  LYS   B HG3  1 
ATOM   5219 H  HD2  . LYS   B 1 76  ? 34.972 -13.151 9.588   1.00 24.53 ?  76  LYS   B HD2  1 
ATOM   5220 H  HD3  . LYS   B 1 76  ? 34.387 -13.855 10.890  1.00 24.53 ?  76  LYS   B HD3  1 
ATOM   5221 H  HE2  . LYS   B 1 76  ? 34.735 -11.953 12.130  1.00 27.01 ?  76  LYS   B HE2  1 
ATOM   5222 H  HE3  . LYS   B 1 76  ? 35.481 -11.255 10.914  1.00 27.01 ?  76  LYS   B HE3  1 
ATOM   5223 H  HZ1  . LYS   B 1 76  ? 33.355 -10.474 11.095  1.00 27.96 ?  76  LYS   B HZ1  1 
ATOM   5224 H  HZ2  . LYS   B 1 76  ? 33.481 -11.166 9.828   1.00 27.96 ?  76  LYS   B HZ2  1 
ATOM   5225 H  HZ3  . LYS   B 1 76  ? 32.800 -11.803 10.937  1.00 27.96 ?  76  LYS   B HZ3  1 
ATOM   5226 N  N    . VAL   B 1 77  ? 37.999 -18.122 10.262  1.00 14.98 ?  77  VAL   B N    1 
ATOM   5227 C  CA   . VAL   B 1 77  ? 37.792 -19.336 9.478   1.00 14.68 ?  77  VAL   B CA   1 
ATOM   5228 C  C    . VAL   B 1 77  ? 36.600 -19.102 8.561   1.00 13.79 ?  77  VAL   B C    1 
ATOM   5229 O  O    . VAL   B 1 77  ? 35.536 -18.656 9.007   1.00 13.77 ?  77  VAL   B O    1 
ATOM   5230 C  CB   . VAL   B 1 77  ? 37.594 -20.557 10.389  1.00 16.48 ?  77  VAL   B CB   1 
ATOM   5231 C  CG1  . VAL   B 1 77  ? 37.330 -21.798 9.546   1.00 17.05 ?  77  VAL   B CG1  1 
ATOM   5232 C  CG2  . VAL   B 1 77  ? 38.815 -20.763 11.291  1.00 17.82 ?  77  VAL   B CG2  1 
ATOM   5233 H  H    . VAL   B 1 77  ? 37.945 -18.226 11.108  1.00 17.97 ?  77  VAL   B H    1 
ATOM   5234 H  HA   . VAL   B 1 77  ? 38.565 -19.495 8.918   1.00 17.62 ?  77  VAL   B HA   1 
ATOM   5235 H  HB   . VAL   B 1 77  ? 36.814 -20.409 10.950  1.00 19.78 ?  77  VAL   B HB   1 
ATOM   5236 H  HG11 . VAL   B 1 77  ? 37.374 -22.579 10.119  1.00 20.46 ?  77  VAL   B HG11 1 
ATOM   5237 H  HG12 . VAL   B 1 77  ? 36.445 -21.735 9.147   1.00 20.46 ?  77  VAL   B HG12 1 
ATOM   5238 H  HG13 . VAL   B 1 77  ? 38.002 -21.857 8.852   1.00 20.46 ?  77  VAL   B HG13 1 
ATOM   5239 H  HG21 . VAL   B 1 77  ? 38.682 -21.567 11.813  1.00 21.38 ?  77  VAL   B HG21 1 
ATOM   5240 H  HG22 . VAL   B 1 77  ? 39.600 -20.849 10.734  1.00 21.38 ?  77  VAL   B HG22 1 
ATOM   5241 H  HG23 . VAL   B 1 77  ? 38.900 -19.994 11.875  1.00 21.38 ?  77  VAL   B HG23 1 
ATOM   5242 N  N    . GLY   B 1 78  ? 36.780 -19.377 7.269   1.00 13.13 ?  78  GLY   B N    1 
ATOM   5243 C  CA   . GLY   B 1 78  ? 35.797 -19.060 6.257   1.00 12.71 ?  78  GLY   B CA   1 
ATOM   5244 C  C    . GLY   B 1 78  ? 36.038 -17.741 5.559   1.00 12.04 ?  78  GLY   B C    1 
ATOM   5245 O  O    . GLY   B 1 78  ? 35.357 -17.452 4.571   1.00 12.60 ?  78  GLY   B O    1 
ATOM   5246 H  H    . GLY   B 1 78  ? 37.484 -19.758 6.947   1.00 15.75 ?  78  GLY   B H    1 
ATOM   5247 H  HA2  . GLY   B 1 78  ? 35.791 -19.759 5.583   1.00 15.25 ?  78  GLY   B HA2  1 
ATOM   5248 H  HA3  . GLY   B 1 78  ? 34.918 -19.025 6.663   1.00 15.25 ?  78  GLY   B HA3  1 
ATOM   5249 N  N    . GLY   B 1 79  ? 36.986 -16.937 6.044   1.00 12.18 ?  79  GLY   B N    1 
ATOM   5250 C  CA   . GLY   B 1 79  ? 37.282 -15.644 5.464   1.00 12.13 ?  79  GLY   B CA   1 
ATOM   5251 C  C    . GLY   B 1 79  ? 38.527 -15.660 4.585   1.00 11.46 ?  79  GLY   B C    1 
ATOM   5252 O  O    . GLY   B 1 79  ? 39.148 -16.690 4.341   1.00 11.99 ?  79  GLY   B O    1 
ATOM   5253 H  H    . GLY   B 1 79  ? 37.487 -17.131 6.709   1.00 14.61 ?  79  GLY   B H    1 
ATOM   5254 H  HA2  . GLY   B 1 79  ? 36.530 -15.349 4.921   1.00 14.56 ?  79  GLY   B HA2  1 
ATOM   5255 H  HA3  . GLY   B 1 79  ? 37.423 -14.998 6.168   1.00 14.56 ?  79  GLY   B HA3  1 
ATOM   5256 N  N    . SER   B 1 80  ? 38.890 -14.468 4.104   1.00 11.70 ?  80  SER   B N    1 
ATOM   5257 C  CA   . SER   B 1 80  ? 40.004 -14.334 3.173   1.00 11.36 ?  80  SER   B CA   1 
ATOM   5258 C  C    . SER   B 1 80  ? 40.586 -12.926 3.231   1.00 11.20 ?  80  SER   B C    1 
ATOM   5259 O  O    . SER   B 1 80  ? 39.972 -11.990 3.747   1.00 12.14 ?  80  SER   B O    1 
ATOM   5260 C  CB   . SER   B 1 80  ? 39.572 -14.623 1.732   1.00 11.58 ?  80  SER   B CB   1 
ATOM   5261 O  OG   . SER   B 1 80  ? 38.720 -13.608 1.234   1.00 12.49 ?  80  SER   B OG   1 
ATOM   5262 H  H    . SER   B 1 80  ? 38.509 -13.722 4.302   1.00 14.04 ?  80  SER   B H    1 
ATOM   5263 H  HA   . SER   B 1 80  ? 40.693 -14.965 3.422   1.00 13.64 ?  80  SER   B HA   1 
ATOM   5264 H  HB2  . SER   B 1 80  ? 40.360 -14.662 1.167   1.00 13.90 ?  80  SER   B HB2  1 
ATOM   5265 H  HB3  . SER   B 1 80  ? 39.102 -15.469 1.704   1.00 13.90 ?  80  SER   B HB3  1 
ATOM   5266 H  HG   . SER   B 1 80  ? 38.019 -13.557 1.712   1.00 14.98 ?  80  SER   B HG   1 
ATOM   5267 N  N    . CYS   B 1 81  ? 41.773 -12.787 2.647   1.00 10.86 ?  81  CYS   B N    1 
ATOM   5268 C  CA   . CYS   B 1 81  ? 42.326 -11.480 2.332   1.00 11.13 ?  81  CYS   B CA   1 
ATOM   5269 C  C    . CYS   B 1 81  ? 43.095 -11.569 1.021   1.00 10.63 ?  81  CYS   B C    1 
ATOM   5270 O  O    . CYS   B 1 81  ? 43.604 -12.633 0.646   1.00 11.35 ?  81  CYS   B O    1 
ATOM   5271 C  CB   . CYS   B 1 81  ? 43.212 -10.928 3.455   1.00 12.10 ?  81  CYS   B CB   1 
ATOM   5272 S  SG   . CYS   B 1 81  ? 44.734 -11.865 3.691   1.00 12.46 ?  81  CYS   B SG   1 
ATOM   5273 H  H    . CYS   B 1 81  ? 42.289 -13.445 2.422   1.00 13.04 ?  81  CYS   B H    1 
ATOM   5274 H  HA   . CYS   B 1 81  ? 41.591 -10.856 2.202   1.00 13.36 ?  81  CYS   B HA   1 
ATOM   5275 H  HB2  . CYS   B 1 81  ? 43.457 -10.012 3.246   1.00 14.52 ?  81  CYS   B HB2  1 
ATOM   5276 H  HB3  . CYS   B 1 81  ? 42.711 -10.946 4.291   1.00 14.52 ?  81  CYS   B HB3  1 
ATOM   5277 H  HG   . CYS   B 1 81  ? 45.360 -11.375 4.592   1.00 14.96 ?  81  CYS   B HG   1 
ATOM   5278 N  N    . VAL   B 1 82  ? 43.200 -10.426 0.346   1.00 10.89 ?  82  VAL   B N    1 
ATOM   5279 C  CA   . VAL   B 1 82  ? 43.967 -10.299 -0.890  1.00 11.23 ?  82  VAL   B CA   1 
ATOM   5280 C  C    . VAL   B 1 82  ? 45.309 -9.662  -0.567  1.00 11.71 ?  82  VAL   B C    1 
ATOM   5281 O  O    . VAL   B 1 82  ? 45.364 -8.542  -0.039  1.00 12.63 ?  82  VAL   B O    1 
ATOM   5282 C  CB   . VAL   B 1 82  ? 43.220 -9.458  -1.937  1.00 12.19 ?  82  VAL   B CB   1 
ATOM   5283 C  CG1  . VAL   B 1 82  ? 44.068 -9.304  -3.193  1.00 13.41 ?  82  VAL   B CG1  1 
ATOM   5284 C  CG2  . VAL   B 1 82  ? 41.868 -10.066 -2.257  1.00 13.04 ?  82  VAL   B CG2  1 
ATOM   5285 H  H    . VAL   B 1 82  ? 42.826 -9.686  0.587   1.00 13.07 ?  82  VAL   B H    1 
ATOM   5286 H  HA   . VAL   B 1 82  ? 44.129 -11.177 -1.263  1.00 13.47 ?  82  VAL   B HA   1 
ATOM   5287 H  HB   . VAL   B 1 82  ? 43.065 -8.573  -1.578  1.00 14.63 ?  82  VAL   B HB   1 
ATOM   5288 H  HG11 . VAL   B 1 82  ? 43.508 -8.991  -3.920  1.00 16.09 ?  82  VAL   B HG11 1 
ATOM   5289 H  HG12 . VAL   B 1 82  ? 44.774 -8.654  -3.023  1.00 16.09 ?  82  VAL   B HG12 1 
ATOM   5290 H  HG13 . VAL   B 1 82  ? 44.459 -10.161 -3.422  1.00 16.09 ?  82  VAL   B HG13 1 
ATOM   5291 H  HG21 . VAL   B 1 82  ? 41.434 -9.541  -2.948  1.00 15.65 ?  82  VAL   B HG21 1 
ATOM   5292 H  HG22 . VAL   B 1 82  ? 41.995 -10.979 -2.570  1.00 15.65 ?  82  VAL   B HG22 1 
ATOM   5293 H  HG23 . VAL   B 1 82  ? 41.322 -10.070 -1.454  1.00 15.65 ?  82  VAL   B HG23 1 
ATOM   5294 N  N    . LEU   B 1 83  ? 46.385 -10.352 -0.931  1.00 10.89 ?  83  LEU   B N    1 
ATOM   5295 C  CA   . LEU   B 1 83  ? 47.743 -9.835  -0.811  1.00 10.96 ?  83  LEU   B CA   1 
ATOM   5296 C  C    . LEU   B 1 83  ? 48.444 -9.973  -2.165  1.00 10.83 ?  83  LEU   B C    1 
ATOM   5297 O  O    . LEU   B 1 83  ? 47.840 -10.389 -3.158  1.00 10.85 ?  83  LEU   B O    1 
ATOM   5298 C  CB   . LEU   B 1 83  ? 48.495 -10.519 0.338   1.00 11.29 ?  83  LEU   B CB   1 
ATOM   5299 C  CG   . LEU   B 1 83  ? 47.979 -10.153 1.736   1.00 12.58 ?  83  LEU   B CG   1 
ATOM   5300 C  CD1  . LEU   B 1 83  ? 48.607 -11.024 2.799   1.00 13.04 ?  83  LEU   B CD1  1 
ATOM   5301 C  CD2  . LEU   B 1 83  ? 48.191 -8.669  2.061   1.00 13.52 ?  83  LEU   B CD2  1 
ATOM   5302 H  H    . LEU   B 1 83  ? 46.351 -11.151 -1.259  1.00 13.07 ?  83  LEU   B H    1 
ATOM   5303 H  HA   . LEU   B 1 83  ? 47.692 -8.890  -0.613  1.00 13.15 ?  83  LEU   B HA   1 
ATOM   5304 H  HB2  . LEU   B 1 83  ? 48.417 -11.476 0.233   1.00 13.55 ?  83  LEU   B HB2  1 
ATOM   5305 H  HB3  . LEU   B 1 83  ? 49.428 -10.256 0.289   1.00 13.55 ?  83  LEU   B HB3  1 
ATOM   5306 H  HG   . LEU   B 1 83  ? 47.024 -10.316 1.757   1.00 15.09 ?  83  LEU   B HG   1 
ATOM   5307 H  HD11 . LEU   B 1 83  ? 48.250 -10.771 3.666   1.00 15.64 ?  83  LEU   B HD11 1 
ATOM   5308 H  HD12 . LEU   B 1 83  ? 48.389 -11.953 2.613   1.00 15.64 ?  83  LEU   B HD12 1 
ATOM   5309 H  HD13 . LEU   B 1 83  ? 49.567 -10.901 2.786   1.00 15.64 ?  83  LEU   B HD13 1 
ATOM   5310 H  HD21 . LEU   B 1 83  ? 47.987 -8.519  2.996   1.00 16.22 ?  83  LEU   B HD21 1 
ATOM   5311 H  HD22 . LEU   B 1 83  ? 49.111 -8.434  1.877   1.00 16.22 ?  83  LEU   B HD22 1 
ATOM   5312 H  HD23 . LEU   B 1 83  ? 47.596 -8.137  1.505   1.00 16.22 ?  83  LEU   B HD23 1 
ATOM   5313 N  N    . SER   B 1 84  ? 49.719 -9.605  -2.223  1.00 11.87 ?  84  SER   B N    1 
ATOM   5314 C  CA   . SER   B 1 84  ? 50.452 -9.729  -3.474  1.00 12.20 ?  84  SER   B CA   1 
ATOM   5315 C  C    . SER   B 1 84  ? 50.600 -11.189 -3.886  1.00 11.59 ?  84  SER   B C    1 
ATOM   5316 O  O    . SER   B 1 84  ? 50.718 -12.086 -3.053  1.00 11.43 ?  84  SER   B O    1 
ATOM   5317 C  CB   . SER   B 1 84  ? 51.851 -9.136  -3.329  1.00 14.07 ?  84  SER   B CB   1 
ATOM   5318 O  OG   . SER   B 1 84  ? 52.587 -9.337  -4.522  1.00 15.58 ?  84  SER   B OG   1 
ATOM   5319 H  H    . SER   B 1 84  ? 50.169 -9.273  -1.569  1.00 14.25 ?  84  SER   B H    1 
ATOM   5320 H  HA   . SER   B 1 84  ? 49.985 -9.254  -4.179  1.00 14.64 ?  84  SER   B HA   1 
ATOM   5321 H  HB2  . SER   B 1 84  ? 51.778 -8.182  -3.150  1.00 16.88 ?  84  SER   B HB2  1 
ATOM   5322 H  HB3  . SER   B 1 84  ? 52.313 -9.575  -2.600  1.00 16.88 ?  84  SER   B HB3  1 
ATOM   5323 H  HG   . SER   B 1 84  ? 53.361 -8.994  -4.450  1.00 18.69 ?  84  SER   B HG   1 
ATOM   5324 N  N    . GLY   B 1 85  ? 50.659 -11.408 -5.193  1.00 12.70 ?  85  GLY   B N    1 
ATOM   5325 C  CA   . GLY   B 1 85  ? 51.013 -12.698 -5.730  1.00 13.20 ?  85  GLY   B CA   1 
ATOM   5326 C  C    . GLY   B 1 85  ? 52.480 -12.885 -6.036  1.00 12.39 ?  85  GLY   B C    1 
ATOM   5327 O  O    . GLY   B 1 85  ? 52.856 -13.961 -6.502  1.00 12.58 ?  85  GLY   B O    1 
ATOM   5328 H  H    . GLY   B 1 85  ? 50.510 -10.815 -5.793  1.00 15.24 ?  85  GLY   B H    1 
ATOM   5329 H  HA2  . GLY   B 1 85  ? 50.756 -13.388 -5.095  1.00 15.83 ?  85  GLY   B HA2  1 
ATOM   5330 H  HA3  . GLY   B 1 85  ? 50.519 -12.848 -6.547  1.00 15.83 ?  85  GLY   B HA3  1 
ATOM   5331 N  N    . HIS   B 1 86  ? 53.328 -11.887 -5.808  1.00 12.38 ?  86  HIS   B N    1 
ATOM   5332 C  CA   . HIS   B 1 86  ? 54.790 -12.055 -5.893  1.00 12.19 ?  86  HIS   B CA   1 
ATOM   5333 C  C    . HIS   B 1 86  ? 55.161 -12.565 -7.283  1.00 12.38 ?  86  HIS   B C    1 
ATOM   5334 O  O    . HIS   B 1 86  ? 54.776 -11.947 -8.286  1.00 13.24 ?  86  HIS   B O    1 
ATOM   5335 C  CB   . HIS   B 1 86  ? 55.280 -12.903 -4.722  1.00 13.09 ?  86  HIS   B CB   1 
ATOM   5336 C  CG   . HIS   B 1 86  ? 54.972 -12.299 -3.395  1.00 13.06 ?  86  HIS   B CG   1 
ATOM   5337 N  ND1  . HIS   B 1 86  ? 55.808 -11.395 -2.774  1.00 14.18 ?  86  HIS   B ND1  1 
ATOM   5338 C  CD2  . HIS   B 1 86  ? 53.894 -12.439 -2.587  1.00 12.88 ?  86  HIS   B CD2  1 
ATOM   5339 C  CE1  . HIS   B 1 86  ? 55.250 -11.003 -1.642  1.00 13.88 ?  86  HIS   B CE1  1 
ATOM   5340 N  NE2  . HIS   B 1 86  ? 54.089 -11.619 -1.506  1.00 13.28 ?  86  HIS   B NE2  1 
ATOM   5341 H  H    . HIS   B 1 86  ? 53.088 -11.092 -5.601  1.00 14.85 ?  86  HIS   B H    1 
ATOM   5342 H  HA   . HIS   B 1 86  ? 55.202 -11.183 -5.797  1.00 14.62 ?  86  HIS   B HA   1 
ATOM   5343 H  HB2  . HIS   B 1 86  ? 54.859 -13.774 -4.763  1.00 15.70 ?  86  HIS   B HB2  1 
ATOM   5344 H  HB3  . HIS   B 1 86  ? 56.246 -13.001 -4.783  1.00 15.70 ?  86  HIS   B HB3  1 
ATOM   5345 H  HD2  . HIS   B 1 86  ? 53.145 -12.976 -2.750  1.00 15.46 ?  86  HIS   B HD2  1 
ATOM   5346 H  HE1  . HIS   B 1 86  ? 55.619 -10.412 -1.031  1.00 16.65 ?  86  HIS   B HE1  1 
ATOM   5347 H  HE2  . HIS   B 1 86  ? 53.547 -11.537 -0.840  1.00 15.94 ?  86  HIS   B HE2  1 
ATOM   5348 N  N    . ASN   B 1 87  ? 55.932 -13.647 -7.394  1.00 13.15 ?  87  ASN   B N    1 
ATOM   5349 C  CA   . ASN   B 1 87  ? 56.328 -14.219 -8.672  1.00 13.85 ?  87  ASN   B CA   1 
ATOM   5350 C  C    . ASN   B 1 87  ? 55.348 -15.265 -9.177  1.00 13.46 ?  87  ASN   B C    1 
ATOM   5351 O  O    . ASN   B 1 87  ? 55.666 -15.975 -10.138 1.00 15.23 ?  87  ASN   B O    1 
ATOM   5352 C  CB   . ASN   B 1 87  ? 57.723 -14.848 -8.556  1.00 15.68 ?  87  ASN   B CB   1 
ATOM   5353 C  CG   . ASN   B 1 87  ? 57.780 -15.963 -7.515  1.00 16.62 ?  87  ASN   B CG   1 
ATOM   5354 O  OD1  . ASN   B 1 87  ? 57.134 -15.889 -6.465  1.00 15.64 ?  87  ASN   B OD1  1 
ATOM   5355 N  ND2  . ASN   B 1 87  ? 58.534 -17.021 -7.820  1.00 18.98 ?  87  ASN   B ND2  1 
ATOM   5356 H  H    . ASN   B 1 87  ? 56.241 -14.084 -6.723  1.00 15.78 ?  87  ASN   B H    1 
ATOM   5357 H  HA   . ASN   B 1 87  ? 56.374 -13.510 -9.334  1.00 16.62 ?  87  ASN   B HA   1 
ATOM   5358 H  HB2  . ASN   B 1 87  ? 57.972 -15.225 -9.417  1.00 18.82 ?  87  ASN   B HB2  1 
ATOM   5359 H  HB3  . ASN   B 1 87  ? 58.356 -14.161 -8.301  1.00 18.82 ?  87  ASN   B HB3  1 
ATOM   5360 H  HD21 . ASN   B 1 87  ? 58.600 -17.674 -7.268  1.00 22.77 ?  87  ASN   B HD21 1 
ATOM   5361 H  HD22 . ASN   B 1 87  ? 58.964 -17.044 -8.568  1.00 22.77 ?  87  ASN   B HD22 1 
ATOM   5362 N  N    . LEU   B 1 88  ? 54.169 -15.370 -8.557  1.00 12.52 ?  88  LEU   B N    1 
ATOM   5363 C  CA   . LEU   B 1 88  ? 53.189 -16.399 -8.885  1.00 12.56 ?  88  LEU   B CA   1 
ATOM   5364 C  C    . LEU   B 1 88  ? 51.961 -15.879 -9.610  1.00 12.27 ?  88  LEU   B C    1 
ATOM   5365 O  O    . LEU   B 1 88  ? 51.359 -16.630 -10.387 1.00 13.99 ?  88  LEU   B O    1 
ATOM   5366 C  CB   . LEU   B 1 88  ? 52.715 -17.087 -7.601  1.00 13.78 ?  88  LEU   B CB   1 
ATOM   5367 C  CG   . LEU   B 1 88  ? 53.834 -17.738 -6.800  1.00 15.80 ?  88  LEU   B CG   1 
ATOM   5368 C  CD1  . LEU   B 1 88  ? 53.329 -18.142 -5.426  1.00 17.27 ?  88  LEU   B CD1  1 
ATOM   5369 C  CD2  . LEU   B 1 88  ? 54.375 -18.934 -7.558  1.00 18.98 ?  88  LEU   B CD2  1 
ATOM   5370 H  H    . LEU   B 1 88  ? 53.911 -14.843 -7.920  1.00 15.03 ?  88  LEU   B H    1 
ATOM   5371 H  HA   . LEU   B 1 88  ? 53.605 -17.063 -9.447  1.00 15.07 ?  88  LEU   B HA   1 
ATOM   5372 H  HB2  . LEU   B 1 88  ? 52.286 -16.433 -7.029  1.00 16.54 ?  88  LEU   B HB2  1 
ATOM   5373 H  HB3  . LEU   B 1 88  ? 52.079 -17.783 -7.836  1.00 16.54 ?  88  LEU   B HB3  1 
ATOM   5374 H  HG   . LEU   B 1 88  ? 54.554 -17.101 -6.681  1.00 18.96 ?  88  LEU   B HG   1 
ATOM   5375 H  HD11 . LEU   B 1 88  ? 54.013 -18.664 -4.979  1.00 20.73 ?  88  LEU   B HD11 1 
ATOM   5376 H  HD12 . LEU   B 1 88  ? 53.131 -17.343 -4.913  1.00 20.73 ?  88  LEU   B HD12 1 
ATOM   5377 H  HD13 . LEU   B 1 88  ? 52.525 -18.674 -5.532  1.00 20.73 ?  88  LEU   B HD13 1 
ATOM   5378 H  HD21 . LEU   B 1 88  ? 55.000 -19.408 -6.989  1.00 22.78 ?  88  LEU   B HD21 1 
ATOM   5379 H  HD22 . LEU   B 1 88  ? 53.636 -19.516 -7.796  1.00 22.78 ?  88  LEU   B HD22 1 
ATOM   5380 H  HD23 . LEU   B 1 88  ? 54.824 -18.623 -8.358  1.00 22.78 ?  88  LEU   B HD23 1 
ATOM   5381 N  N    . ALA   B 1 89  ? 51.555 -14.646 -9.340  1.00 11.77 ?  89  ALA   B N    1 
ATOM   5382 C  CA   . ALA   B 1 89  ? 50.255 -14.155 -9.773  1.00 11.23 ?  89  ALA   B CA   1 
ATOM   5383 C  C    . ALA   B 1 89  ? 50.229 -12.663 -9.497  1.00 11.64 ?  89  ALA   B C    1 
ATOM   5384 O  O    . ALA   B 1 89  ? 51.069 -12.141 -8.763  1.00 12.63 ?  89  ALA   B O    1 
ATOM   5385 C  CB   . ALA   B 1 89  ? 49.133 -14.826 -8.993  1.00 11.41 ?  89  ALA   B CB   1 
ATOM   5386 H  H    . ALA   B 1 89  ? 52.011 -14.063 -8.898  1.00 14.12 ?  89  ALA   B H    1 
ATOM   5387 H  HA   . ALA   B 1 89  ? 50.129 -14.310 -10.723 1.00 13.47 ?  89  ALA   B HA   1 
ATOM   5388 H  HB1  . ALA   B 1 89  ? 48.281 -14.491 -9.316  1.00 13.69 ?  89  ALA   B HB1  1 
ATOM   5389 H  HB2  . ALA   B 1 89  ? 49.185 -15.785 -9.135  1.00 13.69 ?  89  ALA   B HB2  1 
ATOM   5390 H  HB3  . ALA   B 1 89  ? 49.237 -14.622 -8.054  1.00 13.69 ?  89  ALA   B HB3  1 
ATOM   5391 N  N    . LYS   B 1 90  ? 49.236 -11.974 -10.058 1.00 12.68 ?  90  LYS   B N    1 
ATOM   5392 C  CA   . LYS   B 1 90  ? 49.048 -10.586 -9.653  1.00 12.51 ?  90  LYS   B CA   1 
ATOM   5393 C  C    . LYS   B 1 90  ? 48.736 -10.511 -8.162  1.00 12.43 ?  90  LYS   B C    1 
ATOM   5394 O  O    . LYS   B 1 90  ? 49.378 -9.759  -7.414  1.00 13.59 ?  90  LYS   B O    1 
ATOM   5395 C  CB   . LYS   B 1 90  ? 47.966 -9.923  -10.504 1.00 14.20 ?  90  LYS   B CB   1 
ATOM   5396 C  CG   . LYS   B 1 90  ? 47.686 -8.477  -10.129 1.00 14.80 ?  90  LYS   B CG   1 
ATOM   5397 C  CD   . LYS   B 1 90  ? 48.908 -7.592  -10.198 1.00 17.97 ?  90  LYS   B CD   1 
ATOM   5398 C  CE   . LYS   B 1 90  ? 48.482 -6.164  -9.948  1.00 20.34 ?  90  LYS   B CE   1 
ATOM   5399 N  NZ   . LYS   B 1 90  ? 49.642 -5.251  -9.812  1.00 20.06 ?  90  LYS   B NZ   1 
ATOM   5400 H  H    . LYS   B 1 90  ? 48.678 -12.280 -10.639 1.00 15.22 ?  90  LYS   B H    1 
ATOM   5401 H  HA   . LYS   B 1 90  ? 49.872 -10.111 -9.805  1.00 15.02 ?  90  LYS   B HA   1 
ATOM   5402 H  HB2  . LYS   B 1 90  ? 48.250 -9.933  -11.435 1.00 17.04 ?  90  LYS   B HB2  1 
ATOM   5403 H  HB3  . LYS   B 1 90  ? 47.138 -10.418 -10.413 1.00 17.04 ?  90  LYS   B HB3  1 
ATOM   5404 H  HG2  . LYS   B 1 90  ? 47.023 -8.116  -10.740 1.00 17.76 ?  90  LYS   B HG2  1 
ATOM   5405 H  HG3  . LYS   B 1 90  ? 47.343 -8.447  -9.221  1.00 17.76 ?  90  LYS   B HG3  1 
ATOM   5406 H  HD2  . LYS   B 1 90  ? 49.544 -7.853  -9.510  1.00 21.56 ?  90  LYS   B HD2  1 
ATOM   5407 H  HD3  . LYS   B 1 90  ? 49.311 -7.653  -11.078 1.00 21.56 ?  90  LYS   B HD3  1 
ATOM   5408 H  HE2  . LYS   B 1 90  ? 47.947 -5.851  -10.696 1.00 24.41 ?  90  LYS   B HE2  1 
ATOM   5409 H  HE3  . LYS   B 1 90  ? 47.970 -6.115  -9.128  1.00 24.41 ?  90  LYS   B HE3  1 
ATOM   5410 H  HZ1  . LYS   B 1 90  ? 49.365 -4.416  -9.669  1.00 24.08 ?  90  LYS   B HZ1  1 
ATOM   5411 H  HZ2  . LYS   B 1 90  ? 50.154 -5.504  -9.129  1.00 24.08 ?  90  LYS   B HZ2  1 
ATOM   5412 H  HZ3  . LYS   B 1 90  ? 50.133 -5.264  -10.558 1.00 24.08 ?  90  LYS   B HZ3  1 
ATOM   5413 N  N    . HIS   B 1 91  ? 47.775 -11.319 -7.711  1.00 11.01 ?  91  HIS   B N    1 
ATOM   5414 C  CA   . HIS   B 1 91  ? 47.314 -11.344 -6.337  1.00 11.19 ?  91  HIS   B CA   1 
ATOM   5415 C  C    . HIS   B 1 91  ? 47.306 -12.773 -5.820  1.00 10.52 ?  91  HIS   B C    1 
ATOM   5416 O  O    . HIS   B 1 91  ? 47.080 -13.728 -6.574  1.00 11.01 ?  91  HIS   B O    1 
ATOM   5417 C  CB   . HIS   B 1 91  ? 45.862 -10.863 -6.222  1.00 12.91 ?  91  HIS   B CB   1 
ATOM   5418 C  CG   . HIS   B 1 91  ? 45.647 -9.457  -6.666  1.00 16.11 ?  91  HIS   B CG   1 
ATOM   5419 N  ND1  . HIS   B 1 91  ? 46.232 -8.377  -6.042  1.00 18.76 ?  91  HIS   B ND1  1 
ATOM   5420 C  CD2  . HIS   B 1 91  ? 44.876 -8.949  -7.653  1.00 18.33 ?  91  HIS   B CD2  1 
ATOM   5421 C  CE1  . HIS   B 1 91  ? 45.850 -7.263  -6.641  1.00 20.09 ?  91  HIS   B CE1  1 
ATOM   5422 N  NE2  . HIS   B 1 91  ? 45.022 -7.583  -7.619  1.00 20.06 ?  91  HIS   B NE2  1 
ATOM   5423 H  H    . HIS   B 1 91  ? 47.358 -11.886 -8.208  1.00 13.21 ?  91  HIS   B H    1 
ATOM   5424 H  HA   . HIS   B 1 91  ? 47.884 -10.788 -5.773  1.00 13.42 ?  91  HIS   B HA   1 
ATOM   5425 H  HB2  . HIS   B 1 91  ? 45.300 -11.434 -6.769  1.00 15.49 ?  91  HIS   B HB2  1 
ATOM   5426 H  HB3  . HIS   B 1 91  ? 45.582 -10.926 -5.293  1.00 15.49 ?  91  HIS   B HB3  1 
ATOM   5427 H  HD1  . HIS   B 1 91  ? 46.768 -8.422  -5.370  1.00 22.51 ?  91  HIS   B HD1  1 
ATOM   5428 H  HD2  . HIS   B 1 91  ? 44.354 -9.427  -8.254  1.00 21.99 ?  91  HIS   B HD2  1 
ATOM   5429 H  HE1  . HIS   B 1 91  ? 46.113 -6.400  -6.406  1.00 24.11 ?  91  HIS   B HE1  1 
ATOM   5430 N  N    . CYS   B 1 92  ? 47.497 -12.905 -4.513  1.00 10.38 ?  92  CYS   B N    1 
ATOM   5431 C  CA   . CYS   B 1 92  ? 47.204 -14.145 -3.807  1.00 10.36 ?  92  CYS   B CA   1 
ATOM   5432 C  C    . CYS   B 1 92  ? 45.986 -13.910 -2.925  1.00 9.94  ?  92  CYS   B C    1 
ATOM   5433 O  O    . CYS   B 1 92  ? 45.986 -13.005 -2.080  1.00 10.83 ?  92  CYS   B O    1 
ATOM   5434 C  CB   . CYS   B 1 92  ? 48.384 -14.603 -2.954  1.00 10.52 ?  92  CYS   B CB   1 
ATOM   5435 S  SG   . CYS   B 1 92  ? 48.025 -16.135 -2.062  1.00 10.73 ?  92  CYS   B SG   1 
ATOM   5436 H  H    . CYS   B 1 92  ? 47.813 -12.281 -4.003  1.00 12.46 ?  92  CYS   B H    1 
ATOM   5437 H  HA   . CYS   B 1 92  ? 47.000 -14.838 -4.454  1.00 12.44 ?  92  CYS   B HA   1 
ATOM   5438 H  HB2  . CYS   B 1 92  ? 49.147 -14.753 -3.525  1.00 12.62 ?  92  CYS   B HB2  1 
ATOM   5439 H  HB3  . CYS   B 1 92  ? 48.580 -13.912 -2.301  1.00 12.62 ?  92  CYS   B HB3  1 
ATOM   5440 H  HG   . CYS   B 1 92  ? 48.995 -16.447 -1.429  1.00 12.87 ?  92  CYS   B HG   1 
ATOM   5441 N  N    . LEU   B 1 93  ? 44.950 -14.713 -3.136  1.00 9.97  ?  93  LEU   B N    1 
ATOM   5442 C  CA   . LEU   B 1 93  ? 43.771 -14.721 -2.278  1.00 10.10 ?  93  LEU   B CA   1 
ATOM   5443 C  C    . LEU   B 1 93  ? 43.991 -15.786 -1.212  1.00 9.80  ?  93  LEU   B C    1 
ATOM   5444 O  O    . LEU   B 1 93  ? 43.941 -16.987 -1.505  1.00 10.06 ?  93  LEU   B O    1 
ATOM   5445 C  CB   . LEU   B 1 93  ? 42.512 -15.018 -3.087  1.00 10.21 ?  93  LEU   B CB   1 
ATOM   5446 C  CG   . LEU   B 1 93  ? 41.214 -15.021 -2.272  1.00 11.14 ?  93  LEU   B CG   1 
ATOM   5447 C  CD1  . LEU   B 1 93  ? 40.860 -13.635 -1.782  1.00 11.34 ?  93  LEU   B CD1  1 
ATOM   5448 C  CD2  . LEU   B 1 93  ? 40.088 -15.614 -3.098  1.00 11.37 ?  93  LEU   B CD2  1 
ATOM   5449 H  H    . LEU   B 1 93  ? 44.904 -15.285 -3.787  1.00 11.96 ?  93  LEU   B H    1 
ATOM   5450 H  HA   . LEU   B 1 93  ? 43.676 -13.858 -1.849  1.00 12.12 ?  93  LEU   B HA   1 
ATOM   5451 H  HB2  . LEU   B 1 93  ? 42.422 -14.337 -3.774  1.00 12.25 ?  93  LEU   B HB2  1 
ATOM   5452 H  HB3  . LEU   B 1 93  ? 42.606 -15.887 -3.497  1.00 12.25 ?  93  LEU   B HB3  1 
ATOM   5453 H  HG   . LEU   B 1 93  ? 41.335 -15.587 -1.497  1.00 13.37 ?  93  LEU   B HG   1 
ATOM   5454 H  HD11 . LEU   B 1 93  ? 40.005 -13.670 -1.330  1.00 13.61 ?  93  LEU   B HD11 1 
ATOM   5455 H  HD12 . LEU   B 1 93  ? 41.549 -13.329 -1.174  1.00 13.61 ?  93  LEU   B HD12 1 
ATOM   5456 H  HD13 . LEU   B 1 93  ? 40.805 -13.036 -2.548  1.00 13.61 ?  93  LEU   B HD13 1 
ATOM   5457 H  HD21 . LEU   B 1 93  ? 39.274 -15.602 -2.574  1.00 13.65 ?  93  LEU   B HD21 1 
ATOM   5458 H  HD22 . LEU   B 1 93  ? 39.973 -15.084 -3.903  1.00 13.65 ?  93  LEU   B HD22 1 
ATOM   5459 H  HD23 . LEU   B 1 93  ? 40.317 -16.528 -3.336  1.00 13.65 ?  93  LEU   B HD23 1 
ATOM   5460 N  N    . HIS   B 1 94  ? 44.267 -15.349 0.009   1.00 9.59  ?  94  HIS   B N    1 
ATOM   5461 C  CA   . HIS   B 1 94  ? 44.491 -16.252 1.130   1.00 9.95  ?  94  HIS   B CA   1 
ATOM   5462 C  C    . HIS   B 1 94  ? 43.131 -16.601 1.712   1.00 9.96  ?  94  HIS   B C    1 
ATOM   5463 O  O    . HIS   B 1 94  ? 42.467 -15.728 2.274   1.00 11.37 ?  94  HIS   B O    1 
ATOM   5464 C  CB   . HIS   B 1 94  ? 45.354 -15.564 2.181   1.00 10.35 ?  94  HIS   B CB   1 
ATOM   5465 C  CG   . HIS   B 1 94  ? 46.739 -15.269 1.716   1.00 10.11 ?  94  HIS   B CG   1 
ATOM   5466 N  ND1  . HIS   B 1 94  ? 47.764 -16.184 1.812   1.00 10.53 ?  94  HIS   B ND1  1 
ATOM   5467 C  CD2  . HIS   B 1 94  ? 47.251 -14.171 1.110   1.00 10.52 ?  94  HIS   B CD2  1 
ATOM   5468 C  CE1  . HIS   B 1 94  ? 48.856 -15.644 1.301   1.00 10.45 ?  94  HIS   B CE1  1 
ATOM   5469 N  NE2  . HIS   B 1 94  ? 48.575 -14.425 0.869   1.00 10.79 ?  94  HIS   B NE2  1 
ATOM   5470 H  H    . HIS   B 1 94  ? 44.335 -14.514 0.215   1.00 11.50 ?  94  HIS   B H    1 
ATOM   5471 H  HA   . HIS   B 1 94  ? 44.927 -17.061 0.824   1.00 11.94 ?  94  HIS   B HA   1 
ATOM   5472 H  HB2  . HIS   B 1 94  ? 44.937 -14.728 2.428   1.00 12.42 ?  94  HIS   B HB2  1 
ATOM   5473 H  HB3  . HIS   B 1 94  ? 45.418 -16.147 2.953   1.00 12.42 ?  94  HIS   B HB3  1 
ATOM   5474 H  HD2  . HIS   B 1 94  ? 46.796 -13.389 0.904   1.00 12.63 ?  94  HIS   B HD2  1 
ATOM   5475 H  HE1  . HIS   B 1 94  ? 49.685 -16.063 1.253   1.00 12.54 ?  94  HIS   B HE1  1 
ATOM   5476 H  HE2  . HIS   B 1 94  ? 49.134 -13.890 0.500   1.00 12.95 ?  94  HIS   B HE2  1 
ATOM   5477 N  N    . VAL   B 1 95  ? 42.695 -17.852 1.562   1.00 9.92  ?  95  VAL   B N    1 
ATOM   5478 C  CA   . VAL   B 1 95  ? 41.367 -18.294 1.996   1.00 10.15 ?  95  VAL   B CA   1 
ATOM   5479 C  C    . VAL   B 1 95  ? 41.534 -19.332 3.090   1.00 10.38 ?  95  VAL   B C    1 
ATOM   5480 O  O    . VAL   B 1 95  ? 42.307 -20.283 2.929   1.00 10.82 ?  95  VAL   B O    1 
ATOM   5481 C  CB   . VAL   B 1 95  ? 40.550 -18.902 0.840   1.00 10.49 ?  95  VAL   B CB   1 
ATOM   5482 C  CG1  . VAL   B 1 95  ? 39.171 -19.341 1.324   1.00 11.44 ?  95  VAL   B CG1  1 
ATOM   5483 C  CG2  . VAL   B 1 95  ? 40.423 -17.918 -0.299  1.00 10.89 ?  95  VAL   B CG2  1 
ATOM   5484 H  H    . VAL   B 1 95  ? 43.154 -18.481 1.199   1.00 11.90 ?  95  VAL   B H    1 
ATOM   5485 H  HA   . VAL   B 1 95  ? 40.870 -17.539 2.358   1.00 12.18 ?  95  VAL   B HA   1 
ATOM   5486 H  HB   . VAL   B 1 95  ? 41.010 -19.681 0.504   1.00 12.59 ?  95  VAL   B HB   1 
ATOM   5487 H  HG11 . VAL   B 1 95  ? 38.608 -19.532 0.551   1.00 13.73 ?  95  VAL   B HG11 1 
ATOM   5488 H  HG12 . VAL   B 1 95  ? 39.261 -20.140 1.864   1.00 13.73 ?  95  VAL   B HG12 1 
ATOM   5489 H  HG13 . VAL   B 1 95  ? 38.771 -18.628 1.847   1.00 13.73 ?  95  VAL   B HG13 1 
ATOM   5490 H  HG21 . VAL   B 1 95  ? 39.851 -18.303 -0.983  1.00 13.07 ?  95  VAL   B HG21 1 
ATOM   5491 H  HG22 . VAL   B 1 95  ? 40.031 -17.097 0.036   1.00 13.07 ?  95  VAL   B HG22 1 
ATOM   5492 H  HG23 . VAL   B 1 95  ? 41.303 -17.745 -0.662  1.00 13.07 ?  95  VAL   B HG23 1 
ATOM   5493 N  N    . VAL   B 1 96  ? 40.801 -19.158 4.187   1.00 10.79 ?  96  VAL   B N    1 
ATOM   5494 C  CA   . VAL   B 1 96  ? 40.881 -20.065 5.328   1.00 11.50 ?  96  VAL   B CA   1 
ATOM   5495 C  C    . VAL   B 1 96  ? 39.695 -21.025 5.282   1.00 11.80 ?  96  VAL   B C    1 
ATOM   5496 O  O    . VAL   B 1 96  ? 38.576 -20.672 5.666   1.00 12.59 ?  96  VAL   B O    1 
ATOM   5497 C  CB   . VAL   B 1 96  ? 40.939 -19.318 6.665   1.00 12.01 ?  96  VAL   B CB   1 
ATOM   5498 C  CG1  . VAL   B 1 96  ? 41.113 -20.322 7.805   1.00 12.91 ?  96  VAL   B CG1  1 
ATOM   5499 C  CG2  . VAL   B 1 96  ? 42.058 -18.283 6.678   1.00 12.53 ?  96  VAL   B CG2  1 
ATOM   5500 H  H    . VAL   B 1 96  ? 40.240 -18.518 4.298   1.00 12.94 ?  96  VAL   B H    1 
ATOM   5501 H  HA   . VAL   B 1 96  ? 41.694 -20.596 5.254   1.00 13.79 ?  96  VAL   B HA   1 
ATOM   5502 H  HB   . VAL   B 1 96  ? 40.097 -18.858 6.804   1.00 14.41 ?  96  VAL   B HB   1 
ATOM   5503 H  HG11 . VAL   B 1 96  ? 41.310 -19.838 8.624   1.00 15.49 ?  96  VAL   B HG11 1 
ATOM   5504 H  HG12 . VAL   B 1 96  ? 40.293 -20.830 7.916   1.00 15.49 ?  96  VAL   B HG12 1 
ATOM   5505 H  HG13 . VAL   B 1 96  ? 41.847 -20.920 7.594   1.00 15.49 ?  96  VAL   B HG13 1 
ATOM   5506 H  HG21 . VAL   B 1 96  ? 42.096 -17.870 7.558   1.00 15.03 ?  96  VAL   B HG21 1 
ATOM   5507 H  HG22 . VAL   B 1 96  ? 42.899 -18.721 6.483   1.00 15.03 ?  96  VAL   B HG22 1 
ATOM   5508 H  HG23 . VAL   B 1 96  ? 41.870 -17.608 6.007   1.00 15.03 ?  96  VAL   B HG23 1 
ATOM   5509 N  N    . GLY   B 1 97  ? 39.935 -22.255 4.835   1.00 11.76 ?  97  GLY   B N    1 
ATOM   5510 C  CA   . GLY   B 1 97  ? 38.968 -23.316 4.998   1.00 12.33 ?  97  GLY   B CA   1 
ATOM   5511 C  C    . GLY   B 1 97  ? 39.097 -23.932 6.376   1.00 13.40 ?  97  GLY   B C    1 
ATOM   5512 O  O    . GLY   B 1 97  ? 40.141 -23.814 7.032   1.00 13.86 ?  97  GLY   B O    1 
ATOM   5513 H  H    . GLY   B 1 97  ? 40.655 -22.494 4.428   1.00 14.12 ?  97  GLY   B H    1 
ATOM   5514 H  HA2  . GLY   B 1 97  ? 38.070 -22.955 4.882   1.00 14.79 ?  97  GLY   B HA2  1 
ATOM   5515 H  HA3  . GLY   B 1 97  ? 39.111 -24.000 4.323   1.00 14.79 ?  97  GLY   B HA3  1 
ATOM   5516 N  N    . PRO   B 1 98  ? 38.045 -24.607 6.845   1.00 14.43 ?  98  PRO   B N    1 
ATOM   5517 C  CA   . PRO   B 1 98  ? 38.135 -25.305 8.129   1.00 15.44 ?  98  PRO   B CA   1 
ATOM   5518 C  C    . PRO   B 1 98  ? 39.164 -26.423 8.082   1.00 15.26 ?  98  PRO   B C    1 
ATOM   5519 O  O    . PRO   B 1 98  ? 39.264 -27.167 7.107   1.00 15.73 ?  98  PRO   B O    1 
ATOM   5520 C  CB   . PRO   B 1 98  ? 36.717 -25.853 8.331   1.00 15.84 ?  98  PRO   B CB   1 
ATOM   5521 C  CG   . PRO   B 1 98  ? 36.160 -25.979 6.960   1.00 15.39 ?  98  PRO   B CG   1 
ATOM   5522 C  CD   . PRO   B 1 98  ? 36.728 -24.797 6.211   1.00 14.52 ?  98  PRO   B CD   1 
ATOM   5523 H  HA   . PRO   B 1 98  ? 38.354 -24.683 8.834   1.00 18.52 ?  98  PRO   B HA   1 
ATOM   5524 H  HB2  . PRO   B 1 98  ? 36.762 -26.719 8.765   1.00 19.00 ?  98  PRO   B HB2  1 
ATOM   5525 H  HB3  . PRO   B 1 98  ? 36.197 -25.228 8.854   1.00 19.00 ?  98  PRO   B HB3  1 
ATOM   5526 H  HG2  . PRO   B 1 98  ? 36.454 -26.819 6.563   1.00 18.47 ?  98  PRO   B HG2  1 
ATOM   5527 H  HG3  . PRO   B 1 98  ? 35.192 -25.940 6.994   1.00 18.47 ?  98  PRO   B HG3  1 
ATOM   5528 H  HD2  . PRO   B 1 98  ? 36.823 -25.011 5.264   1.00 17.42 ?  98  PRO   B HD2  1 
ATOM   5529 H  HD3  . PRO   B 1 98  ? 36.174 -24.014 6.341   1.00 17.42 ?  98  PRO   B HD3  1 
ATOM   5530 N  N    . ASN   B 1 99  ? 39.924 -26.545 9.161   1.00 16.29 ?  99  ASN   B N    1 
ATOM   5531 C  CA   . ASN   B 1 99  ? 40.903 -27.616 9.320   1.00 17.43 ?  99  ASN   B CA   1 
ATOM   5532 C  C    . ASN   B 1 99  ? 40.277 -28.697 10.202  1.00 19.98 ?  99  ASN   B C    1 
ATOM   5533 O  O    . ASN   B 1 99  ? 40.206 -28.550 11.423  1.00 20.62 ?  99  ASN   B O    1 
ATOM   5534 C  CB   . ASN   B 1 99  ? 42.177 -27.053 9.934   1.00 17.65 ?  99  ASN   B CB   1 
ATOM   5535 C  CG   . ASN   B 1 99  ? 43.307 -28.055 9.950   1.00 18.64 ?  99  ASN   B CG   1 
ATOM   5536 O  OD1  . ASN   B 1 99  ? 43.082 -29.243 10.133  1.00 19.43 ?  99  ASN   B OD1  1 
ATOM   5537 N  ND2  . ASN   B 1 99  ? 44.526 -27.583 9.752   1.00 18.64 ?  99  ASN   B ND2  1 
ATOM   5538 H  H    . ASN   B 1 99  ? 39.891 -26.004 9.826   1.00 19.54 ?  99  ASN   B H    1 
ATOM   5539 H  HA   . ASN   B 1 99  ? 41.109 -28.005 8.457   1.00 20.91 ?  99  ASN   B HA   1 
ATOM   5540 H  HB2  . ASN   B 1 99  ? 42.457 -26.286 9.424   1.00 21.18 ?  99  ASN   B HB2  1 
ATOM   5541 H  HB3  . ASN   B 1 99  ? 41.990 -26.797 10.854  1.00 21.18 ?  99  ASN   B HB3  1 
ATOM   5542 H  HD21 . ASN   B 1 99  ? 45.199 -28.117 9.747   1.00 22.37 ?  99  ASN   B HD21 1 
ATOM   5543 H  HD22 . ASN   B 1 99  ? 44.639 -26.742 9.627   1.00 22.37 ?  99  ASN   B HD22 1 
ATOM   5544 N  N    A VAL   B 1 100 ? 39.801 -29.775 9.572   0.58 22.17 ?  100 VAL   B N    1 
ATOM   5545 N  N    B VAL   B 1 100 ? 39.822 -29.782 9.567   0.42 22.13 ?  100 VAL   B N    1 
ATOM   5546 C  CA   A VAL   B 1 100 ? 39.189 -30.867 10.328  0.58 24.67 ?  100 VAL   B CA   1 
ATOM   5547 C  CA   B VAL   B 1 100 ? 39.197 -30.884 10.296  0.42 24.42 ?  100 VAL   B CA   1 
ATOM   5548 C  C    A VAL   B 1 100 ? 40.205 -31.530 11.251  0.58 25.23 ?  100 VAL   B C    1 
ATOM   5549 C  C    B VAL   B 1 100 ? 40.198 -31.562 11.223  0.42 25.05 ?  100 VAL   B C    1 
ATOM   5550 O  O    A VAL   B 1 100 ? 39.845 -32.029 12.325  0.58 25.80 ?  100 VAL   B O    1 
ATOM   5551 O  O    B VAL   B 1 100 ? 39.820 -32.102 12.271  0.42 25.34 ?  100 VAL   B O    1 
ATOM   5552 C  CB   A VAL   B 1 100 ? 38.523 -31.878 9.372   0.58 26.78 ?  100 VAL   B CB   1 
ATOM   5553 C  CB   B VAL   B 1 100 ? 38.557 -31.875 9.302   0.42 26.11 ?  100 VAL   B CB   1 
ATOM   5554 C  CG1  A VAL   B 1 100 ? 38.023 -33.093 10.139  0.58 27.50 ?  100 VAL   B CG1  1 
ATOM   5555 C  CG1  B VAL   B 1 100 ? 38.043 -33.111 10.025  0.42 26.67 ?  100 VAL   B CG1  1 
ATOM   5556 C  CG2  A VAL   B 1 100 ? 37.376 -31.218 8.620   0.58 27.27 ?  100 VAL   B CG2  1 
ATOM   5557 C  CG2  B VAL   B 1 100 ? 37.429 -31.198 8.538   0.42 26.52 ?  100 VAL   B CG2  1 
ATOM   5558 H  H    A VAL   B 1 100 ? 39.807 -29.888 8.716   0.58 26.60 ?  100 VAL   B H    1 
ATOM   5559 H  H    B VAL   B 1 100 ? 39.859 -29.899 8.713   0.42 26.55 ?  100 VAL   B H    1 
ATOM   5560 H  HA   A VAL   B 1 100 ? 38.484 -30.496 10.882  0.58 29.60 ?  100 VAL   B HA   1 
ATOM   5561 H  HA   B VAL   B 1 100 ? 38.483 -30.524 10.843  0.42 29.31 ?  100 VAL   B HA   1 
ATOM   5562 H  HB   A VAL   B 1 100 ? 39.175 -32.183 8.723   0.58 32.13 ?  100 VAL   B HB   1 
ATOM   5563 H  HB   B VAL   B 1 100 ? 39.226 -32.161 8.660   0.42 31.33 ?  100 VAL   B HB   1 
ATOM   5564 H  HG11 A VAL   B 1 100 ? 37.426 -33.602 9.567   0.58 33.00 ?  100 VAL   B HG11 1 
ATOM   5565 H  HG11 B VAL   B 1 100 ? 37.465 -33.610 9.425   0.42 32.00 ?  100 VAL   B HG11 1 
ATOM   5566 H  HG12 A VAL   B 1 100 ? 38.779 -33.643 10.396  0.58 33.00 ?  100 VAL   B HG12 1 
ATOM   5567 H  HG12 B VAL   B 1 100 ? 38.795 -33.664 10.289  0.42 32.00 ?  100 VAL   B HG12 1 
ATOM   5568 H  HG13 A VAL   B 1 100 ? 37.545 -32.794 10.928  0.58 33.00 ?  100 VAL   B HG13 1 
ATOM   5569 H  HG13 B VAL   B 1 100 ? 37.542 -32.835 10.808  0.42 32.00 ?  100 VAL   B HG13 1 
ATOM   5570 H  HG21 A VAL   B 1 100 ? 36.968 -31.871 8.030   0.58 32.73 ?  100 VAL   B HG21 1 
ATOM   5571 H  HG21 B VAL   B 1 100 ? 37.024 -31.843 7.937   0.42 31.83 ?  100 VAL   B HG21 1 
ATOM   5572 H  HG22 A VAL   B 1 100 ? 36.721 -30.899 9.262   0.58 32.73 ?  100 VAL   B HG22 1 
ATOM   5573 H  HG22 B VAL   B 1 100 ? 36.768 -30.877 9.172   0.42 31.83 ?  100 VAL   B HG22 1 
ATOM   5574 H  HG23 A VAL   B 1 100 ? 37.723 -30.476 8.104   0.58 32.73 ?  100 VAL   B HG23 1 
ATOM   5575 H  HG23 B VAL   B 1 100 ? 37.792 -30.455 8.033   0.42 31.83 ?  100 VAL   B HG23 1 
ATOM   5576 N  N    . ASN   B 1 101 ? 41.480 -31.563 10.853  1.00 25.49 ?  101 ASN   B N    1 
ATOM   5577 C  CA   . ASN   B 1 101 ? 42.517 -32.107 11.728  1.00 27.29 ?  101 ASN   B CA   1 
ATOM   5578 C  C    . ASN   B 1 101 ? 42.712 -31.274 12.990  1.00 28.91 ?  101 ASN   B C    1 
ATOM   5579 O  O    . ASN   B 1 101 ? 43.324 -31.761 13.951  1.00 30.07 ?  101 ASN   B O    1 
ATOM   5580 C  CB   . ASN   B 1 101 ? 43.839 -32.239 10.970  1.00 27.02 ?  101 ASN   B CB   1 
ATOM   5581 C  CG   . ASN   B 1 101 ? 43.829 -33.390 9.983   1.00 26.43 ?  101 ASN   B CG   1 
ATOM   5582 O  OD1  . ASN   B 1 101 ? 43.146 -34.385 10.191  1.00 27.33 ?  101 ASN   B OD1  1 
ATOM   5583 N  ND2  . ASN   B 1 101 ? 44.579 -33.252 8.897   1.00 25.75 ?  101 ASN   B ND2  1 
ATOM   5584 H  H    A ASN   B 1 101 ? 41.760 -31.293 10.084  0.58 30.59 ?  101 ASN   B H    1 
ATOM   5585 H  H    B ASN   B 1 101 ? 41.768 -31.265 10.098  0.42 30.59 ?  101 ASN   B H    1 
ATOM   5586 H  HA   . ASN   B 1 101 ? 42.247 -32.990 12.008  1.00 32.74 ?  101 ASN   B HA   1 
ATOM   5587 H  HB2  . ASN   B 1 101 ? 44.011 -31.425 10.474  1.00 32.42 ?  101 ASN   B HB2  1 
ATOM   5588 H  HB3  . ASN   B 1 101 ? 44.553 -32.395 11.609  1.00 32.42 ?  101 ASN   B HB3  1 
ATOM   5589 H  HD21 . ASN   B 1 101 ? 44.606 -33.881 8.311   1.00 30.90 ?  101 ASN   B HD21 1 
ATOM   5590 H  HD22 . ASN   B 1 101 ? 45.037 -32.535 8.781   1.00 30.90 ?  101 ASN   B HD22 1 
ATOM   5591 N  N    . LYS   B 1 102 ? 42.218 -30.034 13.002  1.00 31.20 ?  102 LYS   B N    1 
ATOM   5592 C  CA   . LYS   B 1 102 ? 42.193 -29.195 14.194  1.00 33.98 ?  102 LYS   B CA   1 
ATOM   5593 C  C    . LYS   B 1 102 ? 40.812 -29.141 14.837  1.00 33.12 ?  102 LYS   B C    1 
ATOM   5594 O  O    . LYS   B 1 102 ? 40.594 -28.333 15.744  1.00 33.70 ?  102 LYS   B O    1 
ATOM   5595 C  CB   . LYS   B 1 102 ? 42.640 -27.770 13.859  1.00 37.51 ?  102 LYS   B CB   1 
ATOM   5596 C  CG   . LYS   B 1 102 ? 44.108 -27.613 13.503  1.00 40.88 ?  102 LYS   B CG   1 
ATOM   5597 C  CD   . LYS   B 1 102 ? 44.365 -26.198 13.005  1.00 43.74 ?  102 LYS   B CD   1 
ATOM   5598 C  CE   . LYS   B 1 102 ? 45.843 -25.898 12.849  1.00 45.95 ?  102 LYS   B CE   1 
ATOM   5599 N  NZ   . LYS   B 1 102 ? 46.054 -24.498 12.378  1.00 47.20 ?  102 LYS   B NZ   1 
ATOM   5600 H  H    . LYS   B 1 102 ? 41.878 -29.643 12.309  1.00 37.44 ?  102 LYS   B H    1 
ATOM   5601 H  HA   . LYS   B 1 102 ? 42.816 -29.554 14.842  1.00 40.78 ?  102 LYS   B HA   1 
ATOM   5602 H  HB2  . LYS   B 1 102 ? 42.123 -27.451 13.104  1.00 45.01 ?  102 LYS   B HB2  1 
ATOM   5603 H  HB3  . LYS   B 1 102 ? 42.469 -27.204 14.630  1.00 45.01 ?  102 LYS   B HB3  1 
ATOM   5604 H  HG2  . LYS   B 1 102 ? 44.655 -27.767 14.290  1.00 49.06 ?  102 LYS   B HG2  1 
ATOM   5605 H  HG3  . LYS   B 1 102 ? 44.342 -28.236 12.798  1.00 49.06 ?  102 LYS   B HG3  1 
ATOM   5606 H  HD2  . LYS   B 1 102 ? 43.942 -26.085 12.139  1.00 52.49 ?  102 LYS   B HD2  1 
ATOM   5607 H  HD3  . LYS   B 1 102 ? 43.995 -25.566 13.641  1.00 52.49 ?  102 LYS   B HD3  1 
ATOM   5608 H  HE2  . LYS   B 1 102 ? 46.286 -26.002 13.706  1.00 55.13 ?  102 LYS   B HE2  1 
ATOM   5609 H  HE3  . LYS   B 1 102 ? 46.228 -26.502 12.194  1.00 55.13 ?  102 LYS   B HE3  1 
ATOM   5610 H  HZ1  . LYS   B 1 102 ? 46.923 -24.334 12.290  1.00 56.64 ?  102 LYS   B HZ1  1 
ATOM   5611 H  HZ2  . LYS   B 1 102 ? 45.655 -24.380 11.591  1.00 56.64 ?  102 LYS   B HZ2  1 
ATOM   5612 H  HZ3  . LYS   B 1 102 ? 45.708 -23.925 12.965  1.00 56.64 ?  102 LYS   B HZ3  1 
ATOM   5613 N  N    . GLY   B 1 103 ? 39.871 -29.960 14.373  1.00 32.23 ?  103 GLY   B N    1 
ATOM   5614 C  CA   . GLY   B 1 103 ? 38.548 -30.011 14.960  1.00 31.65 ?  103 GLY   B CA   1 
ATOM   5615 C  C    . GLY   B 1 103 ? 37.590 -28.938 14.495  1.00 30.61 ?  103 GLY   B C    1 
ATOM   5616 O  O    . GLY   B 1 103 ? 36.497 -28.819 15.063  1.00 31.02 ?  103 GLY   B O    1 
ATOM   5617 H  H    . GLY   B 1 103 ? 39.979 -30.495 13.711  1.00 38.68 ?  103 GLY   B H    1 
ATOM   5618 H  HA2  . GLY   B 1 103 ? 38.150 -30.871 14.760  1.00 37.97 ?  103 GLY   B HA2  1 
ATOM   5619 H  HA3  . GLY   B 1 103 ? 38.630 -29.937 15.925  1.00 37.97 ?  103 GLY   B HA3  1 
ATOM   5620 N  N    A GLU   B 1 104 ? 37.964 -28.146 13.494  0.58 29.40 ?  104 GLU   B N    1 
ATOM   5621 N  N    B GLU   B 1 104 ? 37.946 -28.166 13.473  0.42 29.64 ?  104 GLU   B N    1 
ATOM   5622 C  CA   A GLU   B 1 104 ? 37.120 -27.051 13.044  0.58 28.27 ?  104 GLU   B CA   1 
ATOM   5623 C  CA   B GLU   B 1 104 ? 37.081 -27.095 13.006  0.42 28.65 ?  104 GLU   B CA   1 
ATOM   5624 C  C    A GLU   B 1 104 ? 35.932 -27.580 12.239  0.58 28.51 ?  104 GLU   B C    1 
ATOM   5625 C  C    B GLU   B 1 104 ? 35.919 -27.653 12.185  0.42 28.63 ?  104 GLU   B C    1 
ATOM   5626 O  O    A GLU   B 1 104 ? 35.965 -28.673 11.667  0.58 29.20 ?  104 GLU   B O    1 
ATOM   5627 O  O    B GLU   B 1 104 ? 35.991 -28.743 11.610  0.42 29.08 ?  104 GLU   B O    1 
ATOM   5628 C  CB   A GLU   B 1 104 ? 37.949 -26.049 12.236  0.58 27.25 ?  104 GLU   B CB   1 
ATOM   5629 C  CB   B GLU   B 1 104 ? 37.894 -26.075 12.208  0.42 27.81 ?  104 GLU   B CB   1 
ATOM   5630 C  CG   A GLU   B 1 104 ? 39.047 -25.400 13.073  0.58 26.12 ?  104 GLU   B CG   1 
ATOM   5631 C  CG   B GLU   B 1 104 ? 38.973 -25.414 13.058  0.42 26.94 ?  104 GLU   B CG   1 
ATOM   5632 C  CD   A GLU   B 1 104 ? 39.983 -24.515 12.279  0.58 24.74 ?  104 GLU   B CD   1 
ATOM   5633 C  CD   B GLU   B 1 104 ? 39.940 -24.565 12.262  0.42 26.02 ?  104 GLU   B CD   1 
ATOM   5634 O  OE1  A GLU   B 1 104 ? 39.989 -24.587 11.032  0.58 22.75 ?  104 GLU   B OE1  1 
ATOM   5635 O  OE1  B GLU   B 1 104 ? 39.897 -24.596 11.015  0.42 25.06 ?  104 GLU   B OE1  1 
ATOM   5636 O  OE2  A GLU   B 1 104 ? 40.723 -23.741 12.918  0.58 25.04 -1 104 GLU   B OE2  1 
ATOM   5637 O  OE2  B GLU   B 1 104 ? 40.755 -23.863 12.897  0.42 26.00 -1 104 GLU   B OE2  1 
ATOM   5638 H  H    A GLU   B 1 104 ? 38.708 -28.218 13.068  0.58 35.27 ?  104 GLU   B H    1 
ATOM   5639 H  H    B GLU   B 1 104 ? 38.685 -28.239 13.038  0.42 35.57 ?  104 GLU   B H    1 
ATOM   5640 H  HA   A GLU   B 1 104 ? 36.774 -26.584 13.821  0.58 33.92 ?  104 GLU   B HA   1 
ATOM   5641 H  HA   B GLU   B 1 104 ? 36.709 -26.637 13.775  0.42 34.38 ?  104 GLU   B HA   1 
ATOM   5642 H  HB2  A GLU   B 1 104 ? 38.369 -26.508 11.493  0.58 32.69 ?  104 GLU   B HB2  1 
ATOM   5643 H  HB2  B GLU   B 1 104 ? 38.327 -26.522 11.465  0.42 33.37 ?  104 GLU   B HB2  1 
ATOM   5644 H  HB3  A GLU   B 1 104 ? 37.366 -25.346 11.908  0.58 32.69 ?  104 GLU   B HB3  1 
ATOM   5645 H  HB3  B GLU   B 1 104 ? 37.300 -25.380 11.881  0.42 33.37 ?  104 GLU   B HB3  1 
ATOM   5646 H  HG2  A GLU   B 1 104 ? 38.640 -24.849 13.760  0.58 31.34 ?  104 GLU   B HG2  1 
ATOM   5647 H  HG2  B GLU   B 1 104 ? 38.547 -24.843 13.717  0.42 32.33 ?  104 GLU   B HG2  1 
ATOM   5648 H  HG3  A GLU   B 1 104 ? 39.586 -26.092 13.485  0.58 31.34 ?  104 GLU   B HG3  1 
ATOM   5649 H  HG3  B GLU   B 1 104 ? 39.488 -26.103 13.506  0.42 32.33 ?  104 GLU   B HG3  1 
ATOM   5650 N  N    A ASP   B 1 105 ? 34.868 -26.778 12.207  0.58 28.38 ?  105 ASP   B N    1 
ATOM   5651 N  N    B ASP   B 1 105 ? 34.833 -26.882 12.140  0.42 28.31 ?  105 ASP   B N    1 
ATOM   5652 C  CA   A ASP   B 1 105 ? 33.587 -27.223 11.671  0.58 28.83 ?  105 ASP   B CA   1 
ATOM   5653 C  CA   B ASP   B 1 105 ? 33.567 -27.355 11.590  0.42 28.34 ?  105 ASP   B CA   1 
ATOM   5654 C  C    A ASP   B 1 105 ? 33.635 -27.278 10.148  0.58 26.81 ?  105 ASP   B C    1 
ATOM   5655 C  C    B ASP   B 1 105 ? 33.628 -27.367 10.066  0.42 27.10 ?  105 ASP   B C    1 
ATOM   5656 O  O    A ASP   B 1 105 ? 33.794 -26.248 9.485   0.58 26.14 ?  105 ASP   B O    1 
ATOM   5657 O  O    B ASP   B 1 105 ? 33.803 -26.319 9.435   0.42 26.66 ?  105 ASP   B O    1 
ATOM   5658 C  CB   A ASP   B 1 105 ? 32.483 -26.273 12.130  0.58 31.68 ?  105 ASP   B CB   1 
ATOM   5659 C  CB   B ASP   B 1 105 ? 32.425 -26.462 12.073  0.42 29.73 ?  105 ASP   B CB   1 
ATOM   5660 C  CG   A ASP   B 1 105 ? 31.102 -26.734 11.709  0.58 33.87 ?  105 ASP   B CG   1 
ATOM   5661 C  CG   B ASP   B 1 105 ? 31.057 -27.046 11.762  0.42 30.69 ?  105 ASP   B CG   1 
ATOM   5662 O  OD1  A ASP   B 1 105 ? 30.982 -27.847 11.154  0.58 34.13 ?  105 ASP   B OD1  1 
ATOM   5663 O  OD1  B ASP   B 1 105 ? 30.989 -28.043 11.012  0.42 30.82 ?  105 ASP   B OD1  1 
ATOM   5664 O  OD2  A ASP   B 1 105 ? 30.132 -25.977 11.930  0.58 35.10 -1 105 ASP   B OD2  1 
ATOM   5665 O  OD2  B ASP   B 1 105 ? 30.049 -26.517 12.277  0.42 30.97 -1 105 ASP   B OD2  1 
ATOM   5666 H  H    A ASP   B 1 105 ? 34.867 -25.968 12.491  0.58 34.05 ?  105 ASP   B H    1 
ATOM   5667 H  H    B ASP   B 1 105 ? 34.806 -26.071 12.423  0.42 33.97 ?  105 ASP   B H    1 
ATOM   5668 H  HA   A ASP   B 1 105 ? 33.386 -28.111 12.005  0.58 34.59 ?  105 ASP   B HA   1 
ATOM   5669 H  HA   B ASP   B 1 105 ? 33.395 -28.259 11.895  0.42 34.01 ?  105 ASP   B HA   1 
ATOM   5670 H  HB2  A ASP   B 1 105 ? 32.509 -26.201 13.099  0.58 38.02 ?  105 ASP   B HB2  1 
ATOM   5671 H  HB2  B ASP   B 1 105 ? 32.490 -26.356 13.036  0.42 35.68 ?  105 ASP   B HB2  1 
ATOM   5672 H  HB3  A ASP   B 1 105 ? 32.627 -25.402 11.731  0.58 38.02 ?  105 ASP   B HB3  1 
ATOM   5673 H  HB3  B ASP   B 1 105 ? 32.496 -25.593 11.642  0.42 35.68 ?  105 ASP   B HB3  1 
ATOM   5674 N  N    A ILE   B 1 106 ? 33.464 -28.483 9.595   0.58 26.10 ?  106 ILE   B N    1 
ATOM   5675 N  N    B ILE   B 1 106 ? 33.463 -28.556 9.479   0.42 26.48 ?  106 ILE   B N    1 
ATOM   5676 C  CA   A ILE   B 1 106 ? 33.463 -28.670 8.149   0.58 25.28 ?  106 ILE   B CA   1 
ATOM   5677 C  CA   B ILE   B 1 106 ? 33.466 -28.703 8.028   0.42 25.92 ?  106 ILE   B CA   1 
ATOM   5678 C  C    A ILE   B 1 106 ? 32.363 -27.861 7.474   0.58 24.00 ?  106 ILE   B C    1 
ATOM   5679 C  C    B ILE   B 1 106 ? 32.360 -27.885 7.375   0.42 25.06 ?  106 ILE   B C    1 
ATOM   5680 O  O    A ILE   B 1 106 ? 32.465 -27.552 6.282   0.58 23.08 ?  106 ILE   B O    1 
ATOM   5681 O  O    B ILE   B 1 106 ? 32.441 -27.577 6.181   0.42 24.50 ?  106 ILE   B O    1 
ATOM   5682 C  CB   A ILE   B 1 106 ? 33.364 -30.178 7.824   0.58 26.20 ?  106 ILE   B CB   1 
ATOM   5683 C  CB   B ILE   B 1 106 ? 33.377 -30.203 7.661   0.42 26.50 ?  106 ILE   B CB   1 
ATOM   5684 C  CG1  A ILE   B 1 106 ? 33.626 -30.438 6.339   0.58 26.56 ?  106 ILE   B CG1  1 
ATOM   5685 C  CG1  B ILE   B 1 106 ? 33.651 -30.424 6.172   0.42 26.85 ?  106 ILE   B CG1  1 
ATOM   5686 C  CG2  A ILE   B 1 106 ? 32.001 -30.727 8.230   0.58 26.81 ?  106 ILE   B CG2  1 
ATOM   5687 C  CG2  B ILE   B 1 106 ? 32.014 -30.769 8.038   0.42 26.91 ?  106 ILE   B CG2  1 
ATOM   5688 C  CD1  A ILE   B 1 106 ? 34.986 -29.974 5.875   0.58 26.66 ?  106 ILE   B CD1  1 
ATOM   5689 C  CD1  B ILE   B 1 106 ? 35.008 -29.937 5.728   0.42 27.07 ?  106 ILE   B CD1  1 
ATOM   5690 H  H    A ILE   B 1 106 ? 33.348 -29.205 10.042  0.58 31.32 ?  106 ILE   B H    1 
ATOM   5691 H  H    B ILE   B 1 106 ? 33.354 -29.292 9.904   0.42 31.77 ?  106 ILE   B H    1 
ATOM   5692 H  HA   A ILE   B 1 106 ? 34.307 -28.348 7.806   0.58 30.33 ?  106 ILE   B HA   1 
ATOM   5693 H  HA   B ILE   B 1 106 ? 34.306 -28.365 7.693   0.42 31.11 ?  106 ILE   B HA   1 
ATOM   5694 H  HB   A ILE   B 1 106 ? 34.041 -30.645 8.337   0.58 31.44 ?  106 ILE   B HB   1 
ATOM   5695 H  HB   B ILE   B 1 106 ? 34.051 -30.680 8.168   0.42 31.80 ?  106 ILE   B HB   1 
ATOM   5696 H  HG12 A ILE   B 1 106 ? 33.571 -31.394 6.175   0.58 31.87 ?  106 ILE   B HG12 1 
ATOM   5697 H  HG12 B ILE   B 1 106 ? 33.605 -31.376 5.984   0.42 32.21 ?  106 ILE   B HG12 1 
ATOM   5698 H  HG13 A ILE   B 1 106 ? 32.958 -29.976 5.813   0.58 31.87 ?  106 ILE   B HG13 1 
ATOM   5699 H  HG13 B ILE   B 1 106 ? 32.981 -29.956 5.653   0.42 32.21 ?  106 ILE   B HG13 1 
ATOM   5700 H  HG21 A ILE   B 1 106 ? 32.016 -31.694 8.158   0.58 32.18 ?  106 ILE   B HG21 1 
ATOM   5701 H  HG21 B ILE   B 1 106 ? 32.039 -31.735 7.952   0.42 32.29 ?  106 ILE   B HG21 1 
ATOM   5702 H  HG22 A ILE   B 1 106 ? 31.818 -30.468 9.148   0.58 32.18 ?  106 ILE   B HG22 1 
ATOM   5703 H  HG22 B ILE   B 1 106 ? 31.814 -30.524 8.955   0.42 32.29 ?  106 ILE   B HG22 1 
ATOM   5704 H  HG23 A ILE   B 1 106 ? 31.322 -30.362 7.642   0.58 32.18 ?  106 ILE   B HG23 1 
ATOM   5705 H  HG23 B ILE   B 1 106 ? 31.341 -30.402 7.443   0.42 32.29 ?  106 ILE   B HG23 1 
ATOM   5706 H  HD11 A ILE   B 1 106 ? 35.188 -30.389 5.023   0.58 31.99 ?  106 ILE   B HD11 1 
ATOM   5707 H  HD11 B ILE   B 1 106 ? 35.218 -30.332 4.869   0.42 32.49 ?  106 ILE   B HD11 1 
ATOM   5708 H  HD12 A ILE   B 1 106 ? 34.975 -29.008 5.777   0.58 31.99 ?  106 ILE   B HD12 1 
ATOM   5709 H  HD12 B ILE   B 1 106 ? 34.986 -28.970 5.650   0.42 32.49 ?  106 ILE   B HD12 1 
ATOM   5710 H  HD13 A ILE   B 1 106 ? 35.651 -30.233 6.534   0.58 31.99 ?  106 ILE   B HD13 1 
ATOM   5711 H  HD13 B ILE   B 1 106 ? 35.669 -30.203 6.386   0.42 32.49 ?  106 ILE   B HD13 1 
ATOM   5712 N  N    A GLN   B 1 107 ? 31.313 -27.490 8.212   0.58 24.28 ?  107 GLN   B N    1 
ATOM   5713 N  N    B GLN   B 1 107 ? 31.323 -27.518 8.131   0.42 25.21 ?  107 GLN   B N    1 
ATOM   5714 C  CA   A GLN   B 1 107 ? 30.233 -26.702 7.626   0.58 24.79 ?  107 GLN   B CA   1 
ATOM   5715 C  CA   B GLN   B 1 107 ? 30.238 -26.713 7.578   0.42 25.48 ?  107 GLN   B CA   1 
ATOM   5716 C  C    A GLN   B 1 107 ? 30.720 -25.357 7.106   0.58 22.99 ?  107 GLN   B C    1 
ATOM   5717 C  C    B GLN   B 1 107 ? 30.712 -25.343 7.107   0.42 23.40 ?  107 GLN   B C    1 
ATOM   5718 O  O    A GLN   B 1 107 ? 30.083 -24.784 6.218   0.58 23.37 ?  107 GLN   B O    1 
ATOM   5719 O  O    B GLN   B 1 107 ? 30.054 -24.735 6.258   0.42 23.71 ?  107 GLN   B O    1 
ATOM   5720 C  CB   A GLN   B 1 107 ? 29.121 -26.493 8.658   0.58 28.11 ?  107 GLN   B CB   1 
ATOM   5721 C  CB   B GLN   B 1 107 ? 29.123 -26.563 8.618   0.42 28.20 ?  107 GLN   B CB   1 
ATOM   5722 C  CG   A GLN   B 1 107 ? 27.799 -25.974 8.087   0.58 31.39 ?  107 GLN   B CG   1 
ATOM   5723 C  CG   B GLN   B 1 107 ? 27.795 -26.054 8.062   0.42 30.84 ?  107 GLN   B CG   1 
ATOM   5724 C  CD   A GLN   B 1 107 ? 27.754 -24.460 7.965   0.58 33.85 ?  107 GLN   B CD   1 
ATOM   5725 C  CD   B GLN   B 1 107 ? 27.696 -24.539 8.056   0.42 32.87 ?  107 GLN   B CD   1 
ATOM   5726 O  OE1  A GLN   B 1 107 ? 28.594 -23.753 8.525   0.58 34.74 ?  107 GLN   B OE1  1 
ATOM   5727 O  OE1  B GLN   B 1 107 ? 28.524 -23.847 8.650   0.42 33.53 ?  107 GLN   B OE1  1 
ATOM   5728 N  NE2  A GLN   B 1 107 ? 26.765 -23.955 7.231   0.58 34.77 ?  107 GLN   B NE2  1 
ATOM   5729 N  NE2  B GLN   B 1 107 ? 26.674 -24.016 7.386   0.42 33.65 ?  107 GLN   B NE2  1 
ATOM   5730 H  H    A GLN   B 1 107 ? 31.211 -27.664 9.043   0.58 29.14 ?  107 GLN   B H    1 
ATOM   5731 H  H    B GLN   B 1 107 ? 31.222 -27.723 8.958   0.42 30.25 ?  107 GLN   B H    1 
ATOM   5732 H  HA   A GLN   B 1 107 ? 29.856 -27.192 6.878   0.58 29.75 ?  107 GLN   B HA   1 
ATOM   5733 H  HA   B GLN   B 1 107 ? 29.864 -27.177 6.813   0.42 30.57 ?  107 GLN   B HA   1 
ATOM   5734 H  HB2  A GLN   B 1 107 ? 28.938 -27.341 9.085   0.58 33.73 ?  107 GLN   B HB2  1 
ATOM   5735 H  HB2  B GLN   B 1 107 ? 28.955 -27.428 9.017   0.42 33.84 ?  107 GLN   B HB2  1 
ATOM   5736 H  HB3  A GLN   B 1 107 ? 29.427 -25.852 9.318   0.58 33.73 ?  107 GLN   B HB3  1 
ATOM   5737 H  HB3  B GLN   B 1 107 ? 29.415 -25.940 9.301   0.42 33.84 ?  107 GLN   B HB3  1 
ATOM   5738 H  HG2  A GLN   B 1 107 ? 27.666 -26.346 7.202   0.58 37.67 ?  107 GLN   B HG2  1 
ATOM   5739 H  HG2  B GLN   B 1 107 ? 27.694 -26.362 7.148   0.42 37.01 ?  107 GLN   B HG2  1 
ATOM   5740 H  HG3  A GLN   B 1 107 ? 27.073 -26.251 8.672   0.58 37.67 ?  107 GLN   B HG3  1 
ATOM   5741 H  HG3  B GLN   B 1 107 ? 27.070 -26.402 8.609   0.42 37.01 ?  107 GLN   B HG3  1 
ATOM   5742 H  HE21 A GLN   B 1 107 ? 26.196 -24.480 6.853   0.58 41.72 ?  107 GLN   B HE21 1 
ATOM   5743 H  HE21 B GLN   B 1 107 ? 26.114 -24.530 6.981   0.42 40.38 ?  107 GLN   B HE21 1 
ATOM   5744 H  HE22 A GLN   B 1 107 ? 26.690 -23.103 7.133   0.58 41.72 ?  107 GLN   B HE22 1 
ATOM   5745 H  HE22 B GLN   B 1 107 ? 26.571 -23.163 7.355   0.42 40.38 ?  107 GLN   B HE22 1 
ATOM   5746 N  N    . LEU   B 1 108 ? 31.838 -24.845 7.628   1.00 21.09 ?  108 LEU   B N    1 
ATOM   5747 C  CA   . LEU   B 1 108 ? 32.372 -23.546 7.210   1.00 18.74 ?  108 LEU   B CA   1 
ATOM   5748 C  C    . LEU   B 1 108 ? 33.026 -23.573 5.839   1.00 16.25 ?  108 LEU   B C    1 
ATOM   5749 O  O    . LEU   B 1 108 ? 33.460 -22.514 5.353   1.00 15.27 ?  108 LEU   B O    1 
ATOM   5750 C  CB   . LEU   B 1 108 ? 33.373 -23.030 8.242   1.00 19.04 ?  108 LEU   B CB   1 
ATOM   5751 C  CG   . LEU   B 1 108 ? 32.770 -22.512 9.547   1.00 20.55 ?  108 LEU   B CG   1 
ATOM   5752 C  CD1  . LEU   B 1 108 ? 33.777 -22.587 10.680  1.00 21.02 ?  108 LEU   B CD1  1 
ATOM   5753 C  CD2  . LEU   B 1 108 ? 32.297 -21.079 9.358   1.00 21.65 ?  108 LEU   B CD2  1 
ATOM   5754 H  H    A LEU   B 1 108 ? 32.295 -25.228 8.242   0.58 25.31 ?  108 LEU   B H    1 
ATOM   5755 H  H    B LEU   B 1 108 ? 32.300 -25.236 8.233   0.42 25.31 ?  108 LEU   B H    1 
ATOM   5756 H  HA   . LEU   B 1 108 ? 31.637 -22.912 7.171   1.00 22.49 ?  108 LEU   B HA   1 
ATOM   5757 H  HB2  . LEU   B 1 108 ? 33.974 -23.753 8.472   1.00 22.85 ?  108 LEU   B HB2  1 
ATOM   5758 H  HB3  . LEU   B 1 108 ? 33.871 -22.302 7.846   1.00 22.85 ?  108 LEU   B HB3  1 
ATOM   5759 H  HG   . LEU   B 1 108 ? 32.000 -23.054 9.786   1.00 24.66 ?  108 LEU   B HG   1 
ATOM   5760 H  HD11 . LEU   B 1 108 ? 33.363 -22.254 11.494  1.00 25.22 ?  108 LEU   B HD11 1 
ATOM   5761 H  HD12 . LEU   B 1 108 ? 34.047 -23.510 10.801  1.00 25.22 ?  108 LEU   B HD12 1 
ATOM   5762 H  HD13 . LEU   B 1 108 ? 34.546 -22.041 10.455  1.00 25.22 ?  108 LEU   B HD13 1 
ATOM   5763 H  HD21 . LEU   B 1 108 ? 31.899 -20.765 10.186  1.00 25.98 ?  108 LEU   B HD21 1 
ATOM   5764 H  HD22 . LEU   B 1 108 ? 33.057 -20.525 9.125   1.00 25.98 ?  108 LEU   B HD22 1 
ATOM   5765 H  HD23 . LEU   B 1 108 ? 31.638 -21.055 8.646   1.00 25.98 ?  108 LEU   B HD23 1 
ATOM   5766 N  N    . LEU   B 1 109 ? 33.096 -24.742 5.208   1.00 15.16 ?  109 LEU   B N    1 
ATOM   5767 C  CA   . LEU   B 1 109 ? 33.728 -24.847 3.901   1.00 14.30 ?  109 LEU   B CA   1 
ATOM   5768 C  C    . LEU   B 1 109 ? 32.964 -24.063 2.841   1.00 13.69 ?  109 LEU   B C    1 
ATOM   5769 O  O    . LEU   B 1 109 ? 33.579 -23.471 1.947   1.00 13.44 ?  109 LEU   B O    1 
ATOM   5770 C  CB   . LEU   B 1 109 ? 33.841 -26.321 3.521   1.00 14.40 ?  109 LEU   B CB   1 
ATOM   5771 C  CG   . LEU   B 1 109 ? 34.634 -26.648 2.260   1.00 14.05 ?  109 LEU   B CG   1 
ATOM   5772 C  CD1  . LEU   B 1 109 ? 36.017 -25.999 2.281   1.00 13.92 ?  109 LEU   B CD1  1 
ATOM   5773 C  CD2  . LEU   B 1 109 ? 34.757 -28.164 2.105   1.00 15.13 ?  109 LEU   B CD2  1 
ATOM   5774 H  H    . LEU   B 1 109 ? 32.793 -25.487 5.511   1.00 18.19 ?  109 LEU   B H    1 
ATOM   5775 H  HA   . LEU   B 1 109 ? 34.623 -24.483 3.952   1.00 17.16 ?  109 LEU   B HA   1 
ATOM   5776 H  HB2  . LEU   B 1 109 ? 34.267 -26.795 4.252   1.00 17.28 ?  109 LEU   B HB2  1 
ATOM   5777 H  HB3  . LEU   B 1 109 ? 32.945 -26.676 3.393   1.00 17.28 ?  109 LEU   B HB3  1 
ATOM   5778 H  HG   . LEU   B 1 109 ? 34.153 -26.318 1.483   1.00 16.86 ?  109 LEU   B HG   1 
ATOM   5779 H  HD11 . LEU   B 1 109 ? 36.552 -26.364 1.558   1.00 16.70 ?  109 LEU   B HD11 1 
ATOM   5780 H  HD12 . LEU   B 1 109 ? 35.915 -25.042 2.166   1.00 16.70 ?  109 LEU   B HD12 1 
ATOM   5781 H  HD13 . LEU   B 1 109 ? 36.440 -26.190 3.133   1.00 16.70 ?  109 LEU   B HD13 1 
ATOM   5782 H  HD21 . LEU   B 1 109 ? 35.339 -28.362 1.350   1.00 18.16 ?  109 LEU   B HD21 1 
ATOM   5783 H  HD22 . LEU   B 1 109 ? 35.134 -28.538 2.915   1.00 18.16 ?  109 LEU   B HD22 1 
ATOM   5784 H  HD23 . LEU   B 1 109 ? 33.876 -28.544 1.944   1.00 18.16 ?  109 LEU   B HD23 1 
ATOM   5785 N  N    . LYS   B 1 110 ? 31.632 -24.021 2.929   1.00 13.43 ?  110 LYS   B N    1 
ATOM   5786 C  CA   . LYS   B 1 110 ? 30.872 -23.259 1.942   1.00 13.15 ?  110 LYS   B CA   1 
ATOM   5787 C  C    . LYS   B 1 110 ? 31.211 -21.771 2.024   1.00 12.65 ?  110 LYS   B C    1 
ATOM   5788 O  O    . LYS   B 1 110 ? 31.468 -21.126 1.003   1.00 12.41 ?  110 LYS   B O    1 
ATOM   5789 C  CB   . LYS   B 1 110 ? 29.366 -23.496 2.095   1.00 13.67 ?  110 LYS   B CB   1 
ATOM   5790 C  CG   . LYS   B 1 110 ? 28.559 -22.895 0.941   1.00 14.03 ?  110 LYS   B CG   1 
ATOM   5791 C  CD   . LYS   B 1 110 ? 27.090 -23.303 0.972   1.00 14.34 ?  110 LYS   B CD   1 
ATOM   5792 C  CE   . LYS   B 1 110 ? 26.330 -22.770 -0.245  1.00 15.06 ?  110 LYS   B CE   1 
ATOM   5793 N  NZ   . LYS   B 1 110 ? 26.663 -23.501 -1.497  1.00 15.51 ?  110 LYS   B NZ   1 
ATOM   5794 H  H    . LYS   B 1 110 ? 31.158 -24.412 3.530   1.00 16.11 ?  110 LYS   B H    1 
ATOM   5795 H  HA   . LYS   B 1 110 ? 31.126 -23.562 1.055   1.00 15.78 ?  110 LYS   B HA   1 
ATOM   5796 H  HB2  . LYS   B 1 110 ? 29.199 -24.454 2.112   1.00 16.40 ?  110 LYS   B HB2  1 
ATOM   5797 H  HB3  . LYS   B 1 110 ? 29.062 -23.092 2.919   1.00 16.40 ?  110 LYS   B HB3  1 
ATOM   5798 H  HG2  . LYS   B 1 110 ? 28.597 -21.929 0.994   1.00 16.84 ?  110 LYS   B HG2  1 
ATOM   5799 H  HG3  . LYS   B 1 110 ? 28.931 -23.199 0.098   1.00 16.84 ?  110 LYS   B HG3  1 
ATOM   5800 H  HD2  . LYS   B 1 110 ? 27.023 -24.275 0.968   1.00 17.21 ?  110 LYS   B HD2  1 
ATOM   5801 H  HD3  . LYS   B 1 110 ? 26.671 -22.947 1.772   1.00 17.21 ?  110 LYS   B HD3  1 
ATOM   5802 H  HE2  . LYS   B 1 110 ? 25.378 -22.859 -0.090  1.00 18.07 ?  110 LYS   B HE2  1 
ATOM   5803 H  HE3  . LYS   B 1 110 ? 26.561 -21.836 -0.373  1.00 18.07 ?  110 LYS   B HE3  1 
ATOM   5804 H  HZ1  . LYS   B 1 110 ? 26.205 -23.158 -2.178  1.00 18.61 ?  110 LYS   B HZ1  1 
ATOM   5805 H  HZ2  . LYS   B 1 110 ? 27.533 -23.429 -1.668  1.00 18.61 ?  110 LYS   B HZ2  1 
ATOM   5806 H  HZ3  . LYS   B 1 110 ? 26.455 -24.361 -1.410  1.00 18.61 ?  110 LYS   B HZ3  1 
ATOM   5807 N  N    . SER   B 1 111 ? 31.229 -21.215 3.240   1.00 13.18 ?  111 SER   B N    1 
ATOM   5808 C  CA   . SER   B 1 111 ? 31.627 -19.819 3.413   1.00 12.83 ?  111 SER   B CA   1 
ATOM   5809 C  C    . SER   B 1 111 ? 33.008 -19.568 2.821   1.00 12.72 ?  111 SER   B C    1 
ATOM   5810 O  O    . SER   B 1 111 ? 33.238 -18.539 2.166   1.00 12.75 ?  111 SER   B O    1 
ATOM   5811 C  CB   . SER   B 1 111 ? 31.627 -19.458 4.898   1.00 13.93 ?  111 SER   B CB   1 
ATOM   5812 O  OG   . SER   B 1 111 ? 30.319 -19.465 5.431   1.00 15.57 ?  111 SER   B OG   1 
ATOM   5813 H  H    . SER   B 1 111 ? 31.022 -21.625 3.967   1.00 15.81 ?  111 SER   B H    1 
ATOM   5814 H  HA   . SER   B 1 111 ? 30.996 -19.248 2.959   1.00 15.40 ?  111 SER   B HA   1 
ATOM   5815 H  HB2  . SER   B 1 111 ? 32.155 -20.112 5.384   1.00 16.71 ?  111 SER   B HB2  1 
ATOM   5816 H  HB3  . SER   B 1 111 ? 32.013 -18.576 5.007   1.00 16.71 ?  111 SER   B HB3  1 
ATOM   5817 H  HG   . SER   B 1 111 ? 30.336 -19.247 6.249   1.00 18.68 ?  111 SER   B HG   1 
ATOM   5818 N  N    . ALA   B 1 112 ? 33.948 -20.486 3.056   1.00 12.65 ?  112 ALA   B N    1 
ATOM   5819 C  CA   . ALA   B 1 112 ? 35.293 -20.327 2.513   1.00 12.23 ?  112 ALA   B CA   1 
ATOM   5820 C  C    . ALA   B 1 112 ? 35.261 -20.236 0.990   1.00 11.57 ?  112 ALA   B C    1 
ATOM   5821 O  O    . ALA   B 1 112 ? 35.881 -19.345 0.399   1.00 11.80 ?  112 ALA   B O    1 
ATOM   5822 C  CB   . ALA   B 1 112 ? 36.185 -21.473 2.995   1.00 12.49 ?  112 ALA   B CB   1 
ATOM   5823 H  H    . ALA   B 1 112 ? 33.834 -21.205 3.525   1.00 15.18 ?  112 ALA   B H    1 
ATOM   5824 H  HA   . ALA   B 1 112 ? 35.667 -19.500 2.856   1.00 14.67 ?  112 ALA   B HA   1 
ATOM   5825 H  HB1  . ALA   B 1 112 ? 37.079 -21.348 2.635   1.00 14.99 ?  112 ALA   B HB1  1 
ATOM   5826 H  HB2  . ALA   B 1 112 ? 36.223 -21.459 3.968   1.00 14.99 ?  112 ALA   B HB2  1 
ATOM   5827 H  HB3  . ALA   B 1 112 ? 35.819 -22.313 2.691   1.00 14.99 ?  112 ALA   B HB3  1 
ATOM   5828 N  N    . TYR   B 1 113 ? 34.527 -21.137 0.333   1.00 11.54 ?  113 TYR   B N    1 
ATOM   5829 C  CA   . TYR   B 1 113 ? 34.448 -21.091 -1.123  1.00 11.34 ?  113 TYR   B CA   1 
ATOM   5830 C  C    . TYR   B 1 113 ? 33.739 -19.842 -1.638  1.00 11.12 ?  113 TYR   B C    1 
ATOM   5831 O  O    . TYR   B 1 113 ? 34.015 -19.406 -2.762  1.00 11.11 ?  113 TYR   B O    1 
ATOM   5832 C  CB   . TYR   B 1 113 ? 33.780 -22.351 -1.676  1.00 11.53 ?  113 TYR   B CB   1 
ATOM   5833 C  CG   . TYR   B 1 113 ? 34.739 -23.495 -1.931  1.00 12.17 ?  113 TYR   B CG   1 
ATOM   5834 C  CD1  . TYR   B 1 113 ? 35.727 -23.399 -2.901  1.00 12.66 ?  113 TYR   B CD1  1 
ATOM   5835 C  CD2  . TYR   B 1 113 ? 34.638 -24.682 -1.222  1.00 12.36 ?  113 TYR   B CD2  1 
ATOM   5836 C  CE1  . TYR   B 1 113 ? 36.603 -24.431 -3.144  1.00 12.72 ?  113 TYR   B CE1  1 
ATOM   5837 C  CE2  . TYR   B 1 113 ? 35.508 -25.732 -1.462  1.00 12.54 ?  113 TYR   B CE2  1 
ATOM   5838 C  CZ   . TYR   B 1 113 ? 36.485 -25.604 -2.427  1.00 12.54 ?  113 TYR   B CZ   1 
ATOM   5839 O  OH   . TYR   B 1 113 ? 37.362 -26.622 -2.699  1.00 13.58 ?  113 TYR   B OH   1 
ATOM   5840 H  H    . TYR   B 1 113 ? 34.067 -21.768 0.707   1.00 13.85 ?  113 TYR   B H    1 
ATOM   5841 H  HA   . TYR   B 1 113 ? 35.351 -21.071 -1.461  1.00 13.61 ?  113 TYR   B HA   1 
ATOM   5842 H  HB2  . TYR   B 1 113 ? 33.116 -22.664 -1.036  1.00 13.84 ?  113 TYR   B HB2  1 
ATOM   5843 H  HB3  . TYR   B 1 113 ? 33.347 -22.133 -2.513  1.00 13.84 ?  113 TYR   B HB3  1 
ATOM   5844 H  HD1  . TYR   B 1 113 ? 35.812 -22.606 -3.386  1.00 15.20 ?  113 TYR   B HD1  1 
ATOM   5845 H  HD2  . TYR   B 1 113 ? 33.975 -24.777 -0.578  1.00 14.83 ?  113 TYR   B HD2  1 
ATOM   5846 H  HE1  . TYR   B 1 113 ? 37.262 -24.342 -3.800  1.00 15.27 ?  113 TYR   B HE1  1 
ATOM   5847 H  HE2  . TYR   B 1 113 ? 35.427 -26.530 -0.987  1.00 15.05 ?  113 TYR   B HE2  1 
ATOM   5848 H  HH   . TYR   B 1 113 ? 37.194 -27.288 -2.218  1.00 16.29 ?  113 TYR   B HH   1 
ATOM   5849 N  N    . GLU   B 1 114 ? 32.822 -19.258 -0.858  1.00 11.27 ?  114 GLU   B N    1 
ATOM   5850 C  CA   . GLU   B 1 114 ? 32.141 -18.054 -1.322  1.00 11.27 ?  114 GLU   B CA   1 
ATOM   5851 C  C    . GLU   B 1 114 ? 33.126 -16.934 -1.618  1.00 10.73 ?  114 GLU   B C    1 
ATOM   5852 O  O    . GLU   B 1 114 ? 32.847 -16.072 -2.456  1.00 11.21 ?  114 GLU   B O    1 
ATOM   5853 C  CB   . GLU   B 1 114 ? 31.077 -17.616 -0.311  1.00 11.55 ?  114 GLU   B CB   1 
ATOM   5854 C  CG   . GLU   B 1 114 ? 29.861 -18.535 -0.372  1.00 11.80 ?  114 GLU   B CG   1 
ATOM   5855 C  CD   . GLU   B 1 114 ? 28.836 -18.343 0.743   1.00 12.10 ?  114 GLU   B CD   1 
ATOM   5856 O  OE1  . GLU   B 1 114 ? 29.125 -17.722 1.786   1.00 12.37 ?  114 GLU   B OE1  1 
ATOM   5857 O  OE2  . GLU   B 1 114 ? 27.715 -18.876 0.577   1.00 12.77 -1 114 GLU   B OE2  1 
ATOM   5858 H  H    . GLU   B 1 114 ? 32.578 -19.539 -0.076  1.00 13.52 ?  114 GLU   B H    1 
ATOM   5859 H  HA   . GLU   B 1 114 ? 31.688 -18.260 -2.147  1.00 13.52 ?  114 GLU   B HA   1 
ATOM   5860 H  HB2  . GLU   B 1 114 ? 31.446 -17.656 0.588   1.00 13.87 ?  114 GLU   B HB2  1 
ATOM   5861 H  HB3  . GLU   B 1 114 ? 30.790 -16.713 -0.515  1.00 13.87 ?  114 GLU   B HB3  1 
ATOM   5862 H  HG2  . GLU   B 1 114 ? 29.407 -18.385 -1.214  1.00 14.16 ?  114 GLU   B HG2  1 
ATOM   5863 H  HG3  . GLU   B 1 114 ? 30.171 -19.455 -0.329  1.00 14.16 ?  114 GLU   B HG3  1 
ATOM   5864 N  N    . ASN   B 1 115 ? 34.289 -16.930 -0.965  1.00 10.73 ?  115 ASN   B N    1 
ATOM   5865 C  CA   . ASN   B 1 115 ? 35.275 -15.896 -1.266  1.00 10.73 ?  115 ASN   B CA   1 
ATOM   5866 C  C    . ASN   B 1 115 ? 35.686 -15.924 -2.733  1.00 10.35 ?  115 ASN   B C    1 
ATOM   5867 O  O    . ASN   B 1 115 ? 36.081 -14.888 -3.292  1.00 11.28 ?  115 ASN   B O    1 
ATOM   5868 C  CB   . ASN   B 1 115 ? 36.517 -16.071 -0.383  1.00 11.47 ?  115 ASN   B CB   1 
ATOM   5869 C  CG   . ASN   B 1 115 ? 36.248 -15.809 1.073   1.00 12.02 ?  115 ASN   B CG   1 
ATOM   5870 O  OD1  . ASN   B 1 115 ? 36.246 -14.659 1.514   1.00 13.93 ?  115 ASN   B OD1  1 
ATOM   5871 N  ND2  . ASN   B 1 115 ? 36.078 -16.876 1.851   1.00 12.03 ?  115 ASN   B ND2  1 
ATOM   5872 H  H    . ASN   B 1 115 ? 34.529 -17.494 -0.356  1.00 12.88 ?  115 ASN   B H    1 
ATOM   5873 H  HA   . ASN   B 1 115 ? 34.899 -15.025 -1.078  1.00 12.88 ?  115 ASN   B HA   1 
ATOM   5874 H  HB2  . ASN   B 1 115 ? 36.846 -16.980 -0.471  1.00 13.76 ?  115 ASN   B HB2  1 
ATOM   5875 H  HB3  . ASN   B 1 115 ? 37.204 -15.445 -0.672  1.00 13.76 ?  115 ASN   B HB3  1 
ATOM   5876 H  HD21 . ASN   B 1 115 ? 35.928 -16.777 2.694   1.00 14.43 ?  115 ASN   B HD21 1 
ATOM   5877 H  HD22 . ASN   B 1 115 ? 36.098 -17.667 1.511   1.00 14.43 ?  115 ASN   B HD22 1 
ATOM   5878 N  N    . PHE   B 1 116 ? 35.656 -17.103 -3.363  1.00 10.35 ?  116 PHE   B N    1 
ATOM   5879 C  CA   . PHE   B 1 116 ? 36.091 -17.195 -4.752  1.00 10.83 ?  116 PHE   B CA   1 
ATOM   5880 C  C    . PHE   B 1 116 ? 35.192 -16.373 -5.670  1.00 10.44 ?  116 PHE   B C    1 
ATOM   5881 O  O    . PHE   B 1 116 ? 35.628 -15.943 -6.744  1.00 11.12 ?  116 PHE   B O    1 
ATOM   5882 C  CB   . PHE   B 1 116 ? 36.058 -18.640 -5.267  1.00 10.52 ?  116 PHE   B CB   1 
ATOM   5883 C  CG   . PHE   B 1 116 ? 37.127 -19.592 -4.719  1.00 10.49 ?  116 PHE   B CG   1 
ATOM   5884 C  CD1  . PHE   B 1 116 ? 37.776 -19.409 -3.511  1.00 11.35 ?  116 PHE   B CD1  1 
ATOM   5885 C  CD2  . PHE   B 1 116 ? 37.432 -20.729 -5.454  1.00 11.08 ?  116 PHE   B CD2  1 
ATOM   5886 C  CE1  . PHE   B 1 116 ? 38.709 -20.336 -3.060  1.00 11.31 ?  116 PHE   B CE1  1 
ATOM   5887 C  CE2  . PHE   B 1 116 ? 38.360 -21.658 -5.005  1.00 10.88 ?  116 PHE   B CE2  1 
ATOM   5888 C  CZ   . PHE   B 1 116 ? 38.996 -21.466 -3.814  1.00 11.05 ?  116 PHE   B CZ   1 
ATOM   5889 H  H    . PHE   B 1 116 ? 35.395 -17.851 -3.012  1.00 12.41 ?  116 PHE   B H    1 
ATOM   5890 H  HA   . PHE   B 1 116 ? 36.999 -16.867 -4.830  1.00 12.99 ?  116 PHE   B HA   1 
ATOM   5891 H  HB2  . PHE   B 1 116 ? 35.187 -19.020 -5.042  1.00 12.62 ?  116 PHE   B HB2  1 
ATOM   5892 H  HB3  . PHE   B 1 116 ? 36.150 -18.620 -6.232  1.00 12.62 ?  116 PHE   B HB3  1 
ATOM   5893 H  HD1  . PHE   B 1 116 ? 37.577 -18.660 -2.993  1.00 13.62 ?  116 PHE   B HD1  1 
ATOM   5894 H  HD2  . PHE   B 1 116 ? 36.995 -20.878 -6.262  1.00 13.29 ?  116 PHE   B HD2  1 
ATOM   5895 H  HE1  . PHE   B 1 116 ? 39.142 -20.199 -2.249  1.00 13.57 ?  116 PHE   B HE1  1 
ATOM   5896 H  HE2  . PHE   B 1 116 ? 38.554 -22.409 -5.518  1.00 13.06 ?  116 PHE   B HE2  1 
ATOM   5897 H  HZ   . PHE   B 1 116 ? 39.630 -22.077 -3.516  1.00 13.26 ?  116 PHE   B HZ   1 
ATOM   5898 N  N    . ASN   B 1 117 ? 33.925 -16.165 -5.283  1.00 10.92 ?  117 ASN   B N    1 
ATOM   5899 C  CA   . ASN   B 1 117 ? 32.976 -15.465 -6.145  1.00 11.36 ?  117 ASN   B CA   1 
ATOM   5900 C  C    . ASN   B 1 117 ? 33.290 -13.984 -6.295  1.00 11.75 ?  117 ASN   B C    1 
ATOM   5901 O  O    . ASN   B 1 117 ? 32.697 -13.327 -7.151  1.00 12.64 ?  117 ASN   B O    1 
ATOM   5902 C  CB   . ASN   B 1 117 ? 31.554 -15.688 -5.647  1.00 11.41 ?  117 ASN   B CB   1 
ATOM   5903 C  CG   . ASN   B 1 117 ? 31.098 -17.096 -5.903  1.00 11.56 ?  117 ASN   B CG   1 
ATOM   5904 O  OD1  . ASN   B 1 117 ? 31.457 -17.690 -6.919  1.00 12.28 ?  117 ASN   B OD1  1 
ATOM   5905 N  ND2  . ASN   B 1 117 ? 30.355 -17.667 -4.970  1.00 11.63 ?  117 ASN   B ND2  1 
ATOM   5906 H  H    . ASN   B 1 117 ? 33.602 -16.417 -4.521  1.00 13.10 ?  117 ASN   B H    1 
ATOM   5907 H  HA   . ASN   B 1 117 ? 33.036 -15.859 -7.023  1.00 13.64 ?  117 ASN   B HA   1 
ATOM   5908 H  HB2  . ASN   B 1 117 ? 31.520 -15.525 -4.688  1.00 13.69 ?  117 ASN   B HB2  1 
ATOM   5909 H  HB3  . ASN   B 1 117 ? 30.958 -15.077 -6.108  1.00 13.69 ?  117 ASN   B HB3  1 
ATOM   5910 H  HD21 . ASN   B 1 117 ? 30.068 -18.470 -5.079  1.00 13.96 ?  117 ASN   B HD21 1 
ATOM   5911 H  HD22 . ASN   B 1 117 ? 30.130 -17.224 -4.266  1.00 13.96 ?  117 ASN   B HD22 1 
ATOM   5912 N  N    . GLN   B 1 118 ? 34.222 -13.458 -5.517  1.00 11.29 ?  118 GLN   B N    1 
ATOM   5913 C  CA   . GLN   B 1 118 ? 34.651 -12.073 -5.658  1.00 11.84 ?  118 GLN   B CA   1 
ATOM   5914 C  C    . GLN   B 1 118 ? 35.717 -11.881 -6.733  1.00 11.90 ?  118 GLN   B C    1 
ATOM   5915 O  O    . GLN   B 1 118 ? 36.197 -10.756 -6.914  1.00 13.32 ?  118 GLN   B O    1 
ATOM   5916 C  CB   . GLN   B 1 118 ? 35.134 -11.545 -4.303  1.00 12.31 ?  118 GLN   B CB   1 
ATOM   5917 C  CG   . GLN   B 1 118 ? 34.052 -11.576 -3.230  1.00 12.34 ?  118 GLN   B CG   1 
ATOM   5918 C  CD   . GLN   B 1 118 ? 32.881 -10.672 -3.562  1.00 12.22 ?  118 GLN   B CD   1 
ATOM   5919 O  OE1  . GLN   B 1 118 ? 33.067 -9.533  -3.999  1.00 13.20 ?  118 GLN   B OE1  1 
ATOM   5920 N  NE2  . GLN   B 1 118 ? 31.670 -11.167 -3.361  1.00 12.57 ?  118 GLN   B NE2  1 
ATOM   5921 H  H    . GLN   B 1 118 ? 34.643 -13.885 -4.894  1.00 13.54 ?  118 GLN   B H    1 
ATOM   5922 H  HA   . GLN   B 1 118 ? 33.886 -11.542 -5.923  1.00 14.21 ?  118 GLN   B HA   1 
ATOM   5923 H  HB2  . GLN   B 1 118 ? 35.877 -12.083 -3.998  1.00 14.77 ?  118 GLN   B HB2  1 
ATOM   5924 H  HB3  . GLN   B 1 118 ? 35.418 -10.619 -4.408  1.00 14.77 ?  118 GLN   B HB3  1 
ATOM   5925 H  HG2  . GLN   B 1 118 ? 33.721 -12.484 -3.143  1.00 14.81 ?  118 GLN   B HG2  1 
ATOM   5926 H  HG3  . GLN   B 1 118 ? 34.437 -11.283 -2.386  1.00 14.81 ?  118 GLN   B HG3  1 
ATOM   5927 H  HE21 . GLN   B 1 118 ? 31.579 -11.967 -3.049  1.00 15.09 ?  118 GLN   B HE21 1 
ATOM   5928 H  HE22 . GLN   B 1 118 ? 30.980 -10.690 -3.529  1.00 15.09 ?  118 GLN   B HE22 1 
ATOM   5929 N  N    . HIS   B 1 119 ? 36.078 -12.940 -7.460  1.00 11.23 ?  119 HIS   B N    1 
ATOM   5930 C  CA   . HIS   B 1 119 ? 37.115 -12.892 -8.482  1.00 11.55 ?  119 HIS   B CA   1 
ATOM   5931 C  C    . HIS   B 1 119 ? 36.634 -13.628 -9.716  1.00 11.64 ?  119 HIS   B C    1 
ATOM   5932 O  O    . HIS   B 1 119 ? 36.118 -14.739 -9.608  1.00 12.19 ?  119 HIS   B O    1 
ATOM   5933 C  CB   . HIS   B 1 119 ? 38.395 -13.529 -7.943  1.00 12.17 ?  119 HIS   B CB   1 
ATOM   5934 C  CG   . HIS   B 1 119 ? 38.881 -12.839 -6.717  1.00 13.39 ?  119 HIS   B CG   1 
ATOM   5935 N  ND1  . HIS   B 1 119 ? 39.670 -11.709 -6.769  1.00 15.15 ?  119 HIS   B ND1  1 
ATOM   5936 C  CD2  . HIS   B 1 119 ? 38.593 -13.042 -5.410  1.00 14.31 ?  119 HIS   B CD2  1 
ATOM   5937 C  CE1  . HIS   B 1 119 ? 39.885 -11.278 -5.540  1.00 16.11 ?  119 HIS   B CE1  1 
ATOM   5938 N  NE2  . HIS   B 1 119 ? 39.231 -12.057 -4.699  1.00 15.87 ?  119 HIS   B NE2  1 
ATOM   5939 H  H    . HIS   B 1 119 ? 35.717 -13.724 -7.384  1.00 13.47 ?  119 HIS   B H    1 
ATOM   5940 H  HA   . HIS   B 1 119 ? 37.296 -11.971 -8.725  1.00 13.86 ?  119 HIS   B HA   1 
ATOM   5941 H  HB2  . HIS   B 1 119 ? 38.228 -14.456 -7.730  1.00 14.61 ?  119 HIS   B HB2  1 
ATOM   5942 H  HB3  . HIS   B 1 119 ? 39.092 -13.463 -8.623  1.00 14.61 ?  119 HIS   B HB3  1 
ATOM   5943 H  HD2  . HIS   B 1 119 ? 38.064 -13.725 -5.062  1.00 17.17 ?  119 HIS   B HD2  1 
ATOM   5944 H  HE1  . HIS   B 1 119 ? 40.409 -10.548 -5.300  1.00 19.33 ?  119 HIS   B HE1  1 
ATOM   5945 H  HE2  . HIS   B 1 119 ? 39.239 -11.990 -3.838  1.00 19.04 ?  119 HIS   B HE2  1 
ATOM   5946 N  N    . GLU   B 1 120 ? 36.785 -13.013 -10.889 1.00 12.29 ?  120 GLU   B N    1 
ATOM   5947 C  CA   . GLU   B 1 120 ? 36.188 -13.600 -12.084 1.00 13.55 ?  120 GLU   B CA   1 
ATOM   5948 C  C    . GLU   B 1 120 ? 36.868 -14.897 -12.501 1.00 12.25 ?  120 GLU   B C    1 
ATOM   5949 O  O    . GLU   B 1 120 ? 36.211 -15.766 -13.085 1.00 12.74 ?  120 GLU   B O    1 
ATOM   5950 C  CB   . GLU   B 1 120 ? 36.182 -12.598 -13.238 1.00 18.25 ?  120 GLU   B CB   1 
ATOM   5951 C  CG   . GLU   B 1 120 ? 35.215 -11.447 -13.021 1.00 24.21 ?  120 GLU   B CG   1 
ATOM   5952 C  CD   . GLU   B 1 120 ? 35.072 -10.546 -14.233 1.00 30.00 ?  120 GLU   B CD   1 
ATOM   5953 O  OE1  . GLU   B 1 120 ? 36.062 -10.384 -14.979 1.00 31.58 ?  120 GLU   B OE1  1 
ATOM   5954 O  OE2  . GLU   B 1 120 ? 33.967 -10.001 -14.435 1.00 32.74 -1 120 GLU   B OE2  1 
ATOM   5955 H  H    . GLU   B 1 120 ? 37.213 -12.276 -11.022 1.00 14.75 ?  120 GLU   B H    1 
ATOM   5956 H  HA   . GLU   B 1 120 ? 35.268 -13.815 -11.889 1.00 16.26 ?  120 GLU   B HA   1 
ATOM   5957 H  HB2  . GLU   B 1 120 ? 37.069 -12.224 -13.342 1.00 21.90 ?  120 GLU   B HB2  1 
ATOM   5958 H  HB3  . GLU   B 1 120 ? 35.918 -13.056 -14.054 1.00 21.90 ?  120 GLU   B HB3  1 
ATOM   5959 H  HG2  . GLU   B 1 120 ? 34.335 -11.804 -12.817 1.00 29.05 ?  120 GLU   B HG2  1 
ATOM   5960 H  HG3  . GLU   B 1 120 ? 35.530 -10.901 -12.287 1.00 29.05 ?  120 GLU   B HG3  1 
ATOM   5961 N  N    . VAL   B 1 121 ? 38.167 -15.038 -12.237 1.00 12.07 ?  121 VAL   B N    1 
ATOM   5962 C  CA   . VAL   B 1 121 ? 38.915 -16.244 -12.591 1.00 11.92 ?  121 VAL   B CA   1 
ATOM   5963 C  C    . VAL   B 1 121 ? 40.025 -16.448 -11.570 1.00 11.81 ?  121 VAL   B C    1 
ATOM   5964 O  O    . VAL   B 1 121 ? 40.705 -15.494 -11.177 1.00 12.26 ?  121 VAL   B O    1 
ATOM   5965 C  CB   . VAL   B 1 121 ? 39.433 -16.192 -14.048 1.00 13.96 ?  121 VAL   B CB   1 
ATOM   5966 C  CG1  . VAL   B 1 121 ? 40.291 -14.952 -14.303 1.00 15.22 ?  121 VAL   B CG1  1 
ATOM   5967 C  CG2  . VAL   B 1 121 ? 40.182 -17.474 -14.400 1.00 15.33 ?  121 VAL   B CG2  1 
ATOM   5968 H  H    . VAL   B 1 121 ? 38.650 -14.436 -11.854 1.00 14.48 ?  121 VAL   B H    1 
ATOM   5969 H  HA   . VAL   B 1 121 ? 38.309 -16.998 -12.527 1.00 14.31 ?  121 VAL   B HA   1 
ATOM   5970 H  HB   . VAL   B 1 121 ? 38.664 -16.139 -14.642 1.00 16.75 ?  121 VAL   B HB   1 
ATOM   5971 H  HG11 . VAL   B 1 121 ? 40.603 -14.967 -15.221 1.00 18.26 ?  121 VAL   B HG11 1 
ATOM   5972 H  HG12 . VAL   B 1 121 ? 39.753 -14.159 -14.150 1.00 18.26 ?  121 VAL   B HG12 1 
ATOM   5973 H  HG13 . VAL   B 1 121 ? 41.046 -14.962 -13.696 1.00 18.26 ?  121 VAL   B HG13 1 
ATOM   5974 H  HG21 . VAL   B 1 121 ? 40.381 -17.471 -15.351 1.00 18.40 ?  121 VAL   B HG21 1 
ATOM   5975 H  HG22 . VAL   B 1 121 ? 41.008 -17.508 -13.893 1.00 18.40 ?  121 VAL   B HG22 1 
ATOM   5976 H  HG23 . VAL   B 1 121 ? 39.626 -18.238 -14.184 1.00 18.40 ?  121 VAL   B HG23 1 
ATOM   5977 N  N    . LEU   B 1 122 ? 40.214 -17.702 -11.143 1.00 11.16 ?  122 LEU   B N    1 
ATOM   5978 C  CA   . LEU   B 1 122 ? 41.201 -18.046 -10.122 1.00 10.82 ?  122 LEU   B CA   1 
ATOM   5979 C  C    . LEU   B 1 122 ? 41.852 -19.381 -10.438 1.00 10.94 ?  122 LEU   B C    1 
ATOM   5980 O  O    . LEU   B 1 122 ? 41.190 -20.302 -10.932 1.00 11.88 ?  122 LEU   B O    1 
ATOM   5981 C  CB   . LEU   B 1 122 ? 40.554 -18.268 -8.743  1.00 12.63 ?  122 LEU   B CB   1 
ATOM   5982 C  CG   . LEU   B 1 122 ? 39.513 -17.256 -8.254  1.00 12.28 ?  122 LEU   B CG   1 
ATOM   5983 C  CD1  . LEU   B 1 122 ? 38.117 -17.617 -8.730  1.00 13.18 ?  122 LEU   B CD1  1 
ATOM   5984 C  CD2  . LEU   B 1 122 ? 39.546 -17.139 -6.739  1.00 12.21 ?  122 LEU   B CD2  1 
ATOM   5985 H  H    . LEU   B 1 122 ? 39.778 -18.385 -11.439 1.00 13.39 ?  122 LEU   B H    1 
ATOM   5986 H  HA   . LEU   B 1 122 ? 41.882 -17.357 -10.055 1.00 12.98 ?  122 LEU   B HA   1 
ATOM   5987 H  HB2  . LEU   B 1 122 ? 40.121 -19.131 -8.754  1.00 15.16 ?  122 LEU   B HB2  1 
ATOM   5988 H  HB3  . LEU   B 1 122 ? 41.262 -18.275 -8.082  1.00 15.16 ?  122 LEU   B HB3  1 
ATOM   5989 H  HG   . LEU   B 1 122 ? 39.728 -16.385 -8.617  1.00 14.74 ?  122 LEU   B HG   1 
ATOM   5990 H  HD11 . LEU   B 1 122 ? 37.482 -16.981 -8.360  1.00 15.82 ?  122 LEU   B HD11 1 
ATOM   5991 H  HD12 . LEU   B 1 122 ? 38.092 -17.572 -9.701  1.00 15.82 ?  122 LEU   B HD12 1 
ATOM   5992 H  HD13 . LEU   B 1 122 ? 37.899 -18.511 -8.435  1.00 15.82 ?  122 LEU   B HD13 1 
ATOM   5993 H  HD21 . LEU   B 1 122 ? 38.860 -16.514 -6.452  1.00 14.65 ?  122 LEU   B HD21 1 
ATOM   5994 H  HD22 . LEU   B 1 122 ? 39.380 -18.011 -6.347  1.00 14.65 ?  122 LEU   B HD22 1 
ATOM   5995 H  HD23 . LEU   B 1 122 ? 40.420 -16.815 -6.466  1.00 14.65 ?  122 LEU   B HD23 1 
ATOM   5996 N  N    . LEU   B 1 123 ? 43.141 -19.489 -10.093 1.00 10.50 ?  123 LEU   B N    1 
ATOM   5997 C  CA   . LEU   B 1 123 ? 43.847 -20.759 -9.964  1.00 10.89 ?  123 LEU   B CA   1 
ATOM   5998 C  C    . LEU   B 1 123 ? 43.820 -21.143 -8.490  1.00 10.36 ?  123 LEU   B C    1 
ATOM   5999 O  O    . LEU   B 1 123 ? 44.175 -20.320 -7.639  1.00 10.76 ?  123 LEU   B O    1 
ATOM   6000 C  CB   . LEU   B 1 123 ? 45.297 -20.582 -10.428 1.00 11.25 ?  123 LEU   B CB   1 
ATOM   6001 C  CG   . LEU   B 1 123 ? 46.239 -21.759 -10.179 1.00 11.66 ?  123 LEU   B CG   1 
ATOM   6002 C  CD1  . LEU   B 1 123 ? 45.815 -23.000 -10.957 1.00 11.97 ?  123 LEU   B CD1  1 
ATOM   6003 C  CD2  . LEU   B 1 123 ? 47.652 -21.361 -10.555 1.00 12.68 ?  123 LEU   B CD2  1 
ATOM   6004 H  H    . LEU   B 1 123 ? 43.648 -18.809 -9.919  1.00 12.60 ?  123 LEU   B H    1 
ATOM   6005 H  HA   . LEU   B 1 123 ? 43.413 -21.449 -10.491 1.00 13.06 ?  123 LEU   B HA   1 
ATOM   6006 H  HB2  . LEU   B 1 123 ? 45.287 -20.419 -11.385 1.00 13.51 ?  123 LEU   B HB2  1 
ATOM   6007 H  HB3  . LEU   B 1 123 ? 45.668 -19.813 -9.974  1.00 13.51 ?  123 LEU   B HB3  1 
ATOM   6008 H  HG   . LEU   B 1 123 ? 46.237 -21.981 -9.235  1.00 13.99 ?  123 LEU   B HG   1 
ATOM   6009 H  HD11 . LEU   B 1 123 ? 46.454 -23.708 -10.786 1.00 14.37 ?  123 LEU   B HD11 1 
ATOM   6010 H  HD12 . LEU   B 1 123 ? 44.933 -23.266 -10.661 1.00 14.37 ?  123 LEU   B HD12 1 
ATOM   6011 H  HD13 . LEU   B 1 123 ? 45.801 -22.784 -11.901 1.00 14.37 ?  123 LEU   B HD13 1 
ATOM   6012 H  HD21 . LEU   B 1 123 ? 48.244 -22.112 -10.397 1.00 15.21 ?  123 LEU   B HD21 1 
ATOM   6013 H  HD22 . LEU   B 1 123 ? 47.670 -21.117 -11.495 1.00 15.21 ?  123 LEU   B HD22 1 
ATOM   6014 H  HD23 . LEU   B 1 123 ? 47.921 -20.605 -10.012 1.00 15.21 ?  123 LEU   B HD23 1 
ATOM   6015 N  N    . ALA   B 1 124 ? 43.389 -22.374 -8.176  1.00 10.40 ?  124 ALA   B N    1 
ATOM   6016 C  CA   . ALA   B 1 124 ? 43.133 -22.690 -6.779  1.00 10.42 ?  124 ALA   B CA   1 
ATOM   6017 C  C    . ALA   B 1 124 ? 43.401 -24.150 -6.450  1.00 10.28 ?  124 ALA   B C    1 
ATOM   6018 O  O    . ALA   B 1 124 ? 43.265 -25.025 -7.319  1.00 11.06 ?  124 ALA   B O    1 
ATOM   6019 C  CB   . ALA   B 1 124 ? 41.673 -22.375 -6.419  1.00 10.99 ?  124 ALA   B CB   1 
ATOM   6020 H  H    . ALA   B 1 124 ? 43.236 -23.016 -8.734  1.00 12.48 ?  124 ALA   B H    1 
ATOM   6021 H  HA   . ALA   B 1 124 ? 43.701 -22.134 -6.229  1.00 12.50 ?  124 ALA   B HA   1 
ATOM   6022 H  HB1  . ALA   B 1 124 ? 41.514 -22.585 -5.487  1.00 13.19 ?  124 ALA   B HB1  1 
ATOM   6023 H  HB2  . ALA   B 1 124 ? 41.503 -21.427 -6.575  1.00 13.19 ?  124 ALA   B HB2  1 
ATOM   6024 H  HB3  . ALA   B 1 124 ? 41.082 -22.904 -6.982  1.00 13.19 ?  124 ALA   B HB3  1 
ATOM   6025 N  N    . PRO   B 1 125 ? 43.700 -24.444 -5.188  1.00 10.51 ?  125 PRO   B N    1 
ATOM   6026 C  CA   . PRO   B 1 125 ? 43.636 -25.809 -4.668  1.00 11.10 ?  125 PRO   B CA   1 
ATOM   6027 C  C    . PRO   B 1 125 ? 42.237 -26.081 -4.121  1.00 11.20 ?  125 PRO   B C    1 
ATOM   6028 O  O    . PRO   B 1 125 ? 41.440 -25.167 -3.915  1.00 11.90 ?  125 PRO   B O    1 
ATOM   6029 C  CB   . PRO   B 1 125 ? 44.628 -25.739 -3.502  1.00 12.12 ?  125 PRO   B CB   1 
ATOM   6030 C  CG   . PRO   B 1 125 ? 44.379 -24.357 -2.924  1.00 12.11 ?  125 PRO   B CG   1 
ATOM   6031 C  CD   . PRO   B 1 125 ? 44.017 -23.478 -4.119  1.00 11.08 ?  125 PRO   B CD   1 
ATOM   6032 H  HA   . PRO   B 1 125 ? 43.906 -26.475 -5.322  1.00 13.32 ?  125 PRO   B HA   1 
ATOM   6033 H  HB2  . PRO   B 1 125 ? 44.427 -26.429 -2.847  1.00 14.54 ?  125 PRO   B HB2  1 
ATOM   6034 H  HB3  . PRO   B 1 125 ? 45.537 -25.821 -3.827  1.00 14.54 ?  125 PRO   B HB3  1 
ATOM   6035 H  HG2  . PRO   B 1 125 ? 43.643 -24.389 -2.290  1.00 14.53 ?  125 PRO   B HG2  1 
ATOM   6036 H  HG3  . PRO   B 1 125 ? 45.186 -24.031 -2.487  1.00 14.53 ?  125 PRO   B HG3  1 
ATOM   6037 H  HD2  . PRO   B 1 125 ? 43.248 -22.925 -3.917  1.00 13.29 ?  125 PRO   B HD2  1 
ATOM   6038 H  HD3  . PRO   B 1 125 ? 44.785 -22.930 -4.376  1.00 13.29 ?  125 PRO   B HD3  1 
ATOM   6039 N  N    . LEU   B 1 126 ? 41.969 -27.362 -3.840  1.00 12.14 ?  126 LEU   B N    1 
ATOM   6040 C  CA   . LEU   B 1 126 ? 40.750 -27.727 -3.125  1.00 12.77 ?  126 LEU   B CA   1 
ATOM   6041 C  C    . LEU   B 1 126 ? 40.870 -27.318 -1.666  1.00 12.81 ?  126 LEU   B C    1 
ATOM   6042 O  O    . LEU   B 1 126 ? 41.761 -27.781 -0.949  1.00 14.34 ?  126 LEU   B O    1 
ATOM   6043 C  CB   . LEU   B 1 126 ? 40.497 -29.226 -3.225  1.00 14.33 ?  126 LEU   B CB   1 
ATOM   6044 C  CG   . LEU   B 1 126 ? 39.969 -29.706 -4.577  1.00 15.36 ?  126 LEU   B CG   1 
ATOM   6045 C  CD1  . LEU   B 1 126 ? 40.016 -31.218 -4.667  1.00 17.24 ?  126 LEU   B CD1  1 
ATOM   6046 C  CD2  . LEU   B 1 126 ? 38.552 -29.212 -4.830  1.00 15.53 ?  126 LEU   B CD2  1 
ATOM   6047 H  H    . LEU   B 1 126 ? 42.475 -28.026 -4.041  1.00 14.57 ?  126 LEU   B H    1 
ATOM   6048 H  HA   . LEU   B 1 126 ? 39.996 -27.254 -3.512  1.00 15.32 ?  126 LEU   B HA   1 
ATOM   6049 H  HB2  . LEU   B 1 126 ? 41.331 -29.686 -3.054  1.00 17.20 ?  126 LEU   B HB2  1 
ATOM   6050 H  HB3  . LEU   B 1 126 ? 39.844 -29.471 -2.552  1.00 17.20 ?  126 LEU   B HB3  1 
ATOM   6051 H  HG   . LEU   B 1 126 ? 40.539 -29.350 -5.277  1.00 18.43 ?  126 LEU   B HG   1 
ATOM   6052 H  HD11 . LEU   B 1 126 ? 39.678 -31.494 -5.534  1.00 20.69 ?  126 LEU   B HD11 1 
ATOM   6053 H  HD12 . LEU   B 1 126 ? 40.931 -31.516 -4.557  1.00 20.69 ?  126 LEU   B HD12 1 
ATOM   6054 H  HD13 . LEU   B 1 126 ? 39.459 -31.593 -3.963  1.00 20.69 ?  126 LEU   B HD13 1 
ATOM   6055 H  HD21 . LEU   B 1 126 ? 38.210 -29.631 -5.635  1.00 18.64 ?  126 LEU   B HD21 1 
ATOM   6056 H  HD22 . LEU   B 1 126 ? 37.995 -29.443 -4.072  1.00 18.64 ?  126 LEU   B HD22 1 
ATOM   6057 H  HD23 . LEU   B 1 126 ? 38.568 -28.246 -4.945  1.00 18.64 ?  126 LEU   B HD23 1 
ATOM   6058 N  N    . LEU   B 1 127 ? 39.940 -26.492 -1.210  1.00 12.74 ?  127 LEU   B N    1 
ATOM   6059 C  CA   . LEU   B 1 127 ? 39.995 -25.995 0.153   1.00 13.19 ?  127 LEU   B CA   1 
ATOM   6060 C  C    . LEU   B 1 127 ? 39.725 -27.114 1.150   1.00 12.65 ?  127 LEU   B C    1 
ATOM   6061 O  O    . LEU   B 1 127 ? 38.909 -28.014 0.919   1.00 13.26 ?  127 LEU   B O    1 
ATOM   6062 C  CB   . LEU   B 1 127 ? 38.971 -24.880 0.361   1.00 13.29 ?  127 LEU   B CB   1 
ATOM   6063 C  CG   . LEU   B 1 127 ? 39.148 -23.613 -0.478  1.00 13.63 ?  127 LEU   B CG   1 
ATOM   6064 C  CD1  . LEU   B 1 127 ? 38.041 -22.648 -0.136  1.00 13.86 ?  127 LEU   B CD1  1 
ATOM   6065 C  CD2  . LEU   B 1 127 ? 40.513 -22.969 -0.261  1.00 14.40 ?  127 LEU   B CD2  1 
ATOM   6066 H  H    . LEU   B 1 127 ? 39.270 -26.196 -1.670  1.00 15.28 ?  127 LEU   B H    1 
ATOM   6067 H  HA   . LEU   B 1 127 ? 40.878 -25.632 0.326   1.00 15.83 ?  127 LEU   B HA   1 
ATOM   6068 H  HB2  . LEU   B 1 127 ? 38.090 -25.231 0.160   1.00 15.95 ?  127 LEU   B HB2  1 
ATOM   6069 H  HB3  . LEU   B 1 127 ? 39.000 -24.607 1.292   1.00 15.95 ?  127 LEU   B HB3  1 
ATOM   6070 H  HG   . LEU   B 1 127 ? 39.060 -23.834 -1.416  1.00 16.36 ?  127 LEU   B HG   1 
ATOM   6071 H  HD11 . LEU   B 1 127 ? 38.151 -21.835 -0.662  1.00 16.63 ?  127 LEU   B HD11 1 
ATOM   6072 H  HD12 . LEU   B 1 127 ? 37.184 -23.053 -0.335  1.00 16.63 ?  127 LEU   B HD12 1 
ATOM   6073 H  HD13 . LEU   B 1 127 ? 38.090 -22.428 0.811   1.00 16.63 ?  127 LEU   B HD13 1 
ATOM   6074 H  HD21 . LEU   B 1 127 ? 40.544 -22.120 -0.728  1.00 17.28 ?  127 LEU   B HD21 1 
ATOM   6075 H  HD22 . LEU   B 1 127 ? 40.650 -22.829 0.690   1.00 17.28 ?  127 LEU   B HD22 1 
ATOM   6076 H  HD23 . LEU   B 1 127 ? 41.197 -23.563 -0.608  1.00 17.28 ?  127 LEU   B HD23 1 
ATOM   6077 N  N    . SER   B 1 128 ? 40.412 -27.030 2.280   1.00 12.73 ?  128 SER   B N    1 
ATOM   6078 C  CA   . SER   B 1 128 ? 40.302 -27.947 3.403   1.00 13.64 ?  128 SER   B CA   1 
ATOM   6079 C  C    . SER   B 1 128 ? 40.791 -29.356 3.079   1.00 14.49 ?  128 SER   B C    1 
ATOM   6080 O  O    . SER   B 1 128 ? 40.685 -30.241 3.928   1.00 15.86 ?  128 SER   B O    1 
ATOM   6081 C  CB   . SER   B 1 128 ? 38.898 -27.949 4.026   1.00 13.86 ?  128 SER   B CB   1 
ATOM   6082 O  OG   . SER   B 1 128 ? 38.583 -26.671 4.570   1.00 14.08 ?  128 SER   B OG   1 
ATOM   6083 H  H    . SER   B 1 128 ? 40.977 -26.396 2.426   1.00 15.28 ?  128 SER   B H    1 
ATOM   6084 H  HA   . SER   B 1 128 ? 40.891 -27.611 4.087   1.00 16.36 ?  128 SER   B HA   1 
ATOM   6085 H  HB2  . SER   B 1 128 ? 38.243 -28.184 3.348   1.00 16.63 ?  128 SER   B HB2  1 
ATOM   6086 H  HB3  . SER   B 1 128 ? 38.874 -28.614 4.743   1.00 16.63 ?  128 SER   B HB3  1 
ATOM   6087 H  HG   . SER   B 1 128 ? 39.149 -26.466 5.153   1.00 16.89 ?  128 SER   B HG   1 
ATOM   6088 N  N    . ALA   B 1 129 ? 41.373 -29.574 1.898   1.00 15.79 ?  129 ALA   B N    1 
ATOM   6089 C  CA   . ALA   B 1 129 ? 41.903 -30.879 1.538   1.00 16.52 ?  129 ALA   B CA   1 
ATOM   6090 C  C    . ALA   B 1 129 ? 43.298 -31.064 2.124   1.00 15.34 ?  129 ALA   B C    1 
ATOM   6091 O  O    . ALA   B 1 129 ? 43.864 -30.165 2.761   1.00 15.15 ?  129 ALA   B O    1 
ATOM   6092 C  CB   . ALA   B 1 129 ? 41.941 -31.031 0.020   1.00 18.50 ?  129 ALA   B CB   1 
ATOM   6093 H  H    . ALA   B 1 129 ? 41.474 -28.974 1.282   1.00 18.95 ?  129 ALA   B H    1 
ATOM   6094 H  HA   . ALA   B 1 129 ? 41.324 -31.566 1.899   1.00 19.83 ?  129 ALA   B HA   1 
ATOM   6095 H  HB1  . ALA   B 1 129 ? 42.287 -31.913 -0.199  1.00 22.20 ?  129 ALA   B HB1  1 
ATOM   6096 H  HB2  . ALA   B 1 129 ? 41.044 -30.933 -0.331  1.00 22.20 ?  129 ALA   B HB2  1 
ATOM   6097 H  HB3  . ALA   B 1 129 ? 42.521 -30.349 -0.352  1.00 22.20 ?  129 ALA   B HB3  1 
ATOM   6098 N  N    . GLY   B 1 130 ? 43.858 -32.247 1.891   1.00 15.18 ?  130 GLY   B N    1 
ATOM   6099 C  CA   . GLY   B 1 130 ? 45.247 -32.479 2.239   1.00 16.04 ?  130 GLY   B CA   1 
ATOM   6100 C  C    . GLY   B 1 130 ? 45.467 -32.380 3.730   1.00 16.09 ?  130 GLY   B C    1 
ATOM   6101 O  O    . GLY   B 1 130 ? 44.770 -33.019 4.530   1.00 17.12 ?  130 GLY   B O    1 
ATOM   6102 H  H    . GLY   B 1 130 ? 43.459 -32.918 1.530   1.00 18.22 ?  130 GLY   B H    1 
ATOM   6103 H  HA2  . GLY   B 1 130 ? 45.510 -33.368 1.946   1.00 19.24 ?  130 GLY   B HA2  1 
ATOM   6104 H  HA3  . GLY   B 1 130 ? 45.809 -31.828 1.797   1.00 19.24 ?  130 GLY   B HA3  1 
ATOM   6105 N  N    . ILE   B 1 131 ? 46.445 -31.554 4.114   1.00 16.69 ?  131 ILE   B N    1 
ATOM   6106 C  CA   . ILE   B 1 131 ? 46.800 -31.422 5.521   1.00 17.50 ?  131 ILE   B CA   1 
ATOM   6107 C  C    . ILE   B 1 131 ? 45.685 -30.820 6.357   1.00 16.68 ?  131 ILE   B C    1 
ATOM   6108 O  O    . ILE   B 1 131 ? 45.760 -30.885 7.588   1.00 17.99 ?  131 ILE   B O    1 
ATOM   6109 C  CB   . ILE   B 1 131 ? 48.119 -30.644 5.728   1.00 19.26 ?  131 ILE   B CB   1 
ATOM   6110 C  CG1  . ILE   B 1 131 ? 47.956 -29.161 5.363   1.00 20.22 ?  131 ILE   B CG1  1 
ATOM   6111 C  CG2  . ILE   B 1 131 ? 49.240 -31.270 4.914   1.00 20.31 ?  131 ILE   B CG2  1 
ATOM   6112 C  CD1  . ILE   B 1 131 ? 49.178 -28.311 5.679   1.00 21.24 ?  131 ILE   B CD1  1 
ATOM   6113 H  H    . ILE   B 1 131 ? 46.910 -31.062 3.581   1.00 20.02 ?  131 ILE   B H    1 
ATOM   6114 H  HA   . ILE   B 1 131 ? 46.948 -32.312 5.867   1.00 21.01 ?  131 ILE   B HA   1 
ATOM   6115 H  HB   . ILE   B 1 131 ? 48.353 -30.697 6.667   1.00 23.11 ?  131 ILE   B HB   1 
ATOM   6116 H  HG12 . ILE   B 1 131 ? 47.781 -29.094 4.412   1.00 24.26 ?  131 ILE   B HG12 1 
ATOM   6117 H  HG13 . ILE   B 1 131 ? 47.207 -28.789 5.859   1.00 24.26 ?  131 ILE   B HG13 1 
ATOM   6118 H  HG21 . ILE   B 1 131 ? 50.081 -30.875 5.185   1.00 24.37 ?  131 ILE   B HG21 1 
ATOM   6119 H  HG22 . ILE   B 1 131 ? 49.248 -32.222 5.077   1.00 24.37 ?  131 ILE   B HG22 1 
ATOM   6120 H  HG23 . ILE   B 1 131 ? 49.077 -31.093 3.973   1.00 24.37 ?  131 ILE   B HG23 1 
ATOM   6121 H  HD11 . ILE   B 1 131 ? 48.959 -27.379 5.528   1.00 25.49 ?  131 ILE   B HD11 1 
ATOM   6122 H  HD12 . ILE   B 1 131 ? 49.422 -28.447 6.608   1.00 25.49 ?  131 ILE   B HD12 1 
ATOM   6123 H  HD13 . ILE   B 1 131 ? 49.907 -28.580 5.101   1.00 25.49 ?  131 ILE   B HD13 1 
ATOM   6124 N  N    . PHE   B 1 132 ? 44.656 -30.242 5.729   1.00 15.43 ?  132 PHE   B N    1 
ATOM   6125 C  CA   . PHE   B 1 132 ? 43.498 -29.734 6.457   1.00 15.64 ?  132 PHE   B CA   1 
ATOM   6126 C  C    . PHE   B 1 132 ? 42.476 -30.824 6.789   1.00 17.03 ?  132 PHE   B C    1 
ATOM   6127 O  O    . PHE   B 1 132 ? 41.575 -30.574 7.599   1.00 18.71 ?  132 PHE   B O    1 
ATOM   6128 C  CB   . PHE   B 1 132 ? 42.821 -28.601 5.674   1.00 14.47 ?  132 PHE   B CB   1 
ATOM   6129 C  CG   . PHE   B 1 132 ? 43.515 -27.257 5.783   1.00 14.39 ?  132 PHE   B CG   1 
ATOM   6130 C  CD1  . PHE   B 1 132 ? 44.806 -27.078 5.307   1.00 15.14 ?  132 PHE   B CD1  1 
ATOM   6131 C  CD2  . PHE   B 1 132 ? 42.848 -26.161 6.315   1.00 13.84 ?  132 PHE   B CD2  1 
ATOM   6132 C  CE1  . PHE   B 1 132 ? 45.431 -25.840 5.398   1.00 15.80 ?  132 PHE   B CE1  1 
ATOM   6133 C  CE2  . PHE   B 1 132 ? 43.458 -24.920 6.392   1.00 14.40 ?  132 PHE   B CE2  1 
ATOM   6134 C  CZ   . PHE   B 1 132 ? 44.751 -24.759 5.937   1.00 15.35 ?  132 PHE   B CZ   1 
ATOM   6135 H  H    . PHE   B 1 132 ? 44.605 -30.134 4.874   1.00 18.52 ?  132 PHE   B H    1 
ATOM   6136 H  HA   . PHE   B 1 132 ? 43.807 -29.365 7.295   1.00 18.77 ?  132 PHE   B HA   1 
ATOM   6137 H  HB2  . PHE   B 1 132 ? 42.805 -28.844 4.740   1.00 17.36 ?  132 PHE   B HB2  1 
ATOM   6138 H  HB3  . PHE   B 1 132 ? 41.916 -28.495 6.007   1.00 17.36 ?  132 PHE   B HB3  1 
ATOM   6139 H  HD1  . PHE   B 1 132 ? 45.267 -27.807 4.950   1.00 18.17 ?  132 PHE   B HD1  1 
ATOM   6140 H  HD2  . PHE   B 1 132 ? 41.978 -26.265 6.626   1.00 16.61 ?  132 PHE   B HD2  1 
ATOM   6141 H  HE1  . PHE   B 1 132 ? 46.301 -25.736 5.086   1.00 18.96 ?  132 PHE   B HE1  1 
ATOM   6142 H  HE2  . PHE   B 1 132 ? 43.004 -24.197 6.764   1.00 17.28 ?  132 PHE   B HE2  1 
ATOM   6143 H  HZ   . PHE   B 1 132 ? 45.166 -23.924 5.999   1.00 18.42 ?  132 PHE   B HZ   1 
ATOM   6144 N  N    . GLY   B 1 133 ? 42.574 -32.014 6.181   1.00 16.70 ?  133 GLY   B N    1 
ATOM   6145 C  CA   . GLY   B 1 133 ? 41.863 -33.182 6.669   1.00 17.73 ?  133 GLY   B CA   1 
ATOM   6146 C  C    . GLY   B 1 133 ? 40.466 -33.443 6.135   1.00 18.03 ?  133 GLY   B C    1 
ATOM   6147 O  O    . GLY   B 1 133 ? 39.882 -34.468 6.495   1.00 19.75 ?  133 GLY   B O    1 
ATOM   6148 H  H    . GLY   B 1 133 ? 43.056 -32.161 5.480   1.00 20.03 ?  133 GLY   B H    1 
ATOM   6149 H  HA2  . GLY   B 1 133 ? 42.402 -33.964 6.473   1.00 21.27 ?  133 GLY   B HA2  1 
ATOM   6150 H  HA3  . GLY   B 1 133 ? 41.791 -33.109 7.631   1.00 21.27 ?  133 GLY   B HA3  1 
ATOM   6151 N  N    . ALA   B 1 134 ? 39.899 -32.572 5.310   1.00 17.09 ?  134 ALA   B N    1 
ATOM   6152 C  CA   . ALA   B 1 134 ? 38.574 -32.859 4.781   1.00 17.42 ?  134 ALA   B CA   1 
ATOM   6153 C  C    . ALA   B 1 134 ? 38.658 -33.855 3.630   1.00 17.27 ?  134 ALA   B C    1 
ATOM   6154 O  O    . ALA   B 1 134 ? 39.711 -34.053 3.017   1.00 18.13 ?  134 ALA   B O    1 
ATOM   6155 C  CB   . ALA   B 1 134 ? 37.895 -31.580 4.298   1.00 17.99 ?  134 ALA   B CB   1 
ATOM   6156 H  H    . ALA   B 1 134 ? 40.246 -31.825 5.054   1.00 20.51 ?  134 ALA   B H    1 
ATOM   6157 H  HA   . ALA   B 1 134 ? 38.027 -33.245 5.486   1.00 20.90 ?  134 ALA   B HA   1 
ATOM   6158 H  HB1  . ALA   B 1 134 ? 37.008 -31.801 3.970   1.00 21.59 ?  134 ALA   B HB1  1 
ATOM   6159 H  HB2  . ALA   B 1 134 ? 37.828 -30.958 5.038   1.00 21.59 ?  134 ALA   B HB2  1 
ATOM   6160 H  HB3  . ALA   B 1 134 ? 38.424 -31.193 3.585   1.00 21.59 ?  134 ALA   B HB3  1 
ATOM   6161 N  N    . ASP   B 1 135 ? 37.524 -34.482 3.342   1.00 17.72 ?  135 ASP   B N    1 
ATOM   6162 C  CA   . ASP   B 1 135 ? 37.427 -35.380 2.201   1.00 18.41 ?  135 ASP   B CA   1 
ATOM   6163 C  C    . ASP   B 1 135 ? 37.530 -34.543 0.933   1.00 17.15 ?  135 ASP   B C    1 
ATOM   6164 O  O    . ASP   B 1 135 ? 36.677 -33.670 0.710   1.00 16.85 ?  135 ASP   B O    1 
ATOM   6165 C  CB   . ASP   B 1 135 ? 36.087 -36.110 2.249   1.00 20.22 ?  135 ASP   B CB   1 
ATOM   6166 C  CG   . ASP   B 1 135 ? 35.916 -37.109 1.123   1.00 22.10 ?  135 ASP   B CG   1 
ATOM   6167 O  OD1  . ASP   B 1 135 ? 36.784 -37.159 0.224   1.00 21.62 ?  135 ASP   B OD1  1 
ATOM   6168 O  OD2  . ASP   B 1 135 ? 34.914 -37.861 1.150   1.00 24.98 -1 135 ASP   B OD2  1 
ATOM   6169 H  H    . ASP   B 1 135 ? 36.795 -34.409 3.793   1.00 21.26 ?  135 ASP   B H    1 
ATOM   6170 H  HA   . ASP   B 1 135 ? 38.146 -36.034 2.232   1.00 22.10 ?  135 ASP   B HA   1 
ATOM   6171 H  HB2  . ASP   B 1 135 ? 36.023 -36.590 3.087   1.00 24.26 ?  135 ASP   B HB2  1 
ATOM   6172 H  HB3  . ASP   B 1 135 ? 35.376 -35.461 2.175   1.00 24.26 ?  135 ASP   B HB3  1 
ATOM   6173 N  N    . PRO   B 1 136 ? 38.539 -34.751 0.086   1.00 17.26 ?  136 PRO   B N    1 
ATOM   6174 C  CA   . PRO   B 1 136 ? 38.634 -33.929 -1.129  1.00 16.58 ?  136 PRO   B CA   1 
ATOM   6175 C  C    . PRO   B 1 136 ? 37.443 -34.090 -2.052  1.00 15.88 ?  136 PRO   B C    1 
ATOM   6176 O  O    . PRO   B 1 136 ? 37.116 -33.141 -2.776  1.00 15.32 ?  136 PRO   B O    1 
ATOM   6177 C  CB   . PRO   B 1 136 ? 39.951 -34.391 -1.773  1.00 17.51 ?  136 PRO   B CB   1 
ATOM   6178 C  CG   . PRO   B 1 136 ? 40.172 -35.774 -1.224  1.00 18.64 ?  136 PRO   B CG   1 
ATOM   6179 C  CD   . PRO   B 1 136 ? 39.635 -35.732 0.176   1.00 18.35 ?  136 PRO   B CD   1 
ATOM   6180 H  HA   . PRO   B 1 136 ? 38.714 -32.994 -0.892  1.00 19.90 ?  136 PRO   B HA   1 
ATOM   6181 H  HB2  . PRO   B 1 136 ? 39.859 -34.413 -2.740  1.00 21.01 ?  136 PRO   B HB2  1 
ATOM   6182 H  HB3  . PRO   B 1 136 ? 40.670 -33.795 -1.511  1.00 21.01 ?  136 PRO   B HB3  1 
ATOM   6183 H  HG2  . PRO   B 1 136 ? 39.685 -36.425 -1.756  1.00 22.37 ?  136 PRO   B HG2  1 
ATOM   6184 H  HG3  . PRO   B 1 136 ? 41.122 -35.981 -1.218  1.00 22.37 ?  136 PRO   B HG3  1 
ATOM   6185 H  HD2  . PRO   B 1 136 ? 39.294 -36.601 0.436   1.00 22.02 ?  136 PRO   B HD2  1 
ATOM   6186 H  HD3  . PRO   B 1 136 ? 40.315 -35.416 0.794   1.00 22.02 ?  136 PRO   B HD3  1 
ATOM   6187 N  N    . ILE   B 1 137 ? 36.779 -35.252 -2.046  1.00 16.04 ?  137 ILE   B N    1 
ATOM   6188 C  CA   . ILE   B 1 137 ? 35.562 -35.418 -2.836  1.00 16.51 ?  137 ILE   B CA   1 
ATOM   6189 C  C    . ILE   B 1 137 ? 34.491 -34.442 -2.363  1.00 16.00 ?  137 ILE   B C    1 
ATOM   6190 O  O    . ILE   B 1 137 ? 33.781 -33.823 -3.169  1.00 15.55 ?  137 ILE   B O    1 
ATOM   6191 C  CB   . ILE   B 1 137 ? 35.082 -36.882 -2.773  1.00 18.74 ?  137 ILE   B CB   1 
ATOM   6192 C  CG1  . ILE   B 1 137 ? 36.092 -37.795 -3.474  1.00 21.15 ?  137 ILE   B CG1  1 
ATOM   6193 C  CG2  . ILE   B 1 137 ? 33.686 -37.019 -3.380  1.00 19.29 ?  137 ILE   B CG2  1 
ATOM   6194 C  CD1  . ILE   B 1 137 ? 35.796 -39.274 -3.319  1.00 23.32 ?  137 ILE   B CD1  1 
ATOM   6195 H  H    . ILE   B 1 137 ? 37.010 -35.948 -1.600  1.00 19.25 ?  137 ILE   B H    1 
ATOM   6196 H  HA   . ILE   B 1 137 ? 35.757 -35.214 -3.765  1.00 19.81 ?  137 ILE   B HA   1 
ATOM   6197 H  HB   . ILE   B 1 137 ? 35.026 -37.145 -1.846  1.00 22.49 ?  137 ILE   B HB   1 
ATOM   6198 H  HG12 . ILE   B 1 137 ? 36.094 -37.598 -4.424  1.00 25.38 ?  137 ILE   B HG12 1 
ATOM   6199 H  HG13 . ILE   B 1 137 ? 36.970 -37.634 -3.101  1.00 25.38 ?  137 ILE   B HG13 1 
ATOM   6200 H  HG21 . ILE   B 1 137 ? 33.460 -37.957 -3.475  1.00 23.14 ?  137 ILE   B HG21 1 
ATOM   6201 H  HG22 . ILE   B 1 137 ? 33.037 -36.593 -2.796  1.00 23.14 ?  137 ILE   B HG22 1 
ATOM   6202 H  HG23 . ILE   B 1 137 ? 33.673 -36.591 -4.252  1.00 23.14 ?  137 ILE   B HG23 1 
ATOM   6203 H  HD11 . ILE   B 1 137 ? 36.504 -39.776 -3.751  1.00 27.99 ?  137 ILE   B HD11 1 
ATOM   6204 H  HD12 . ILE   B 1 137 ? 35.762 -39.497 -2.375  1.00 27.99 ?  137 ILE   B HD12 1 
ATOM   6205 H  HD13 . ILE   B 1 137 ? 34.948 -39.485 -3.740  1.00 27.99 ?  137 ILE   B HD13 1 
ATOM   6206 N  N    . HIS   B 1 138 ? 34.358 -34.289 -1.049  1.00 16.42 ?  138 HIS   B N    1 
ATOM   6207 C  CA   . HIS   B 1 138 ? 33.411 -33.320 -0.516  1.00 16.89 ?  138 HIS   B CA   1 
ATOM   6208 C  C    . HIS   B 1 138 ? 33.830 -31.894 -0.842  1.00 15.94 ?  138 HIS   B C    1 
ATOM   6209 O  O    . HIS   B 1 138 ? 32.985 -31.051 -1.159  1.00 16.23 ?  138 HIS   B O    1 
ATOM   6210 C  CB   . HIS   B 1 138 ? 33.297 -33.489 0.991   1.00 18.20 ?  138 HIS   B CB   1 
ATOM   6211 C  CG   . HIS   B 1 138 ? 32.361 -32.511 1.623   1.00 19.32 ?  138 HIS   B CG   1 
ATOM   6212 N  ND1  . HIS   B 1 138 ? 31.024 -32.445 1.296   1.00 20.80 ?  138 HIS   B ND1  1 
ATOM   6213 C  CD2  . HIS   B 1 138 ? 32.574 -31.537 2.538   1.00 19.82 ?  138 HIS   B CD2  1 
ATOM   6214 C  CE1  . HIS   B 1 138 ? 30.448 -31.485 1.997   1.00 20.71 ?  138 HIS   B CE1  1 
ATOM   6215 N  NE2  . HIS   B 1 138 ? 31.367 -30.917 2.758   1.00 20.12 ?  138 HIS   B NE2  1 
ATOM   6216 H  H    . HIS   B 1 138 ? 34.792 -34.732 -0.458  1.00 19.71 ?  138 HIS   B H    1 
ATOM   6217 H  HA   . HIS   B 1 138 ? 32.534 -33.482 -0.907  1.00 20.27 ?  138 HIS   B HA   1 
ATOM   6218 H  HB2  . HIS   B 1 138 ? 32.969 -34.380 1.184   1.00 21.83 ?  138 HIS   B HB2  1 
ATOM   6219 H  HB3  . HIS   B 1 138 ? 34.170 -33.361 1.386   1.00 21.83 ?  138 HIS   B HB3  1 
ATOM   6220 H  HD1  . HIS   B 1 138 ? 30.623 -32.958 0.729   1.00 24.96 ?  138 HIS   B HD1  1 
ATOM   6221 H  HD2  . HIS   B 1 138 ? 33.375 -31.332 2.953   1.00 23.78 ?  138 HIS   B HD2  1 
ATOM   6222 H  HE1  . HIS   B 1 138 ? 29.543 -31.256 1.960   1.00 24.85 ?  138 HIS   B HE1  1 
ATOM   6223 N  N    . SER   B 1 139 ? 35.124 -31.591 -0.751  1.00 15.18 ?  139 SER   B N    1 
ATOM   6224 C  CA   . SER   B 1 139 ? 35.567 -30.245 -1.080  1.00 14.54 ?  139 SER   B CA   1 
ATOM   6225 C  C    . SER   B 1 139 ? 35.228 -29.899 -2.519  1.00 13.80 ?  139 SER   B C    1 
ATOM   6226 O  O    . SER   B 1 139 ? 34.778 -28.787 -2.800  1.00 13.73 ?  139 SER   B O    1 
ATOM   6227 C  CB   . SER   B 1 139 ? 37.065 -30.109 -0.823  1.00 14.83 ?  139 SER   B CB   1 
ATOM   6228 O  OG   . SER   B 1 139 ? 37.472 -28.774 -1.076  1.00 14.90 ?  139 SER   B OG   1 
ATOM   6229 H  H    . SER   B 1 139 ? 35.737 -32.133 -0.513  1.00 18.21 ?  139 SER   B H    1 
ATOM   6230 H  HA   . SER   B 1 139 ? 35.101 -29.615 -0.514  1.00 17.45 ?  139 SER   B HA   1 
ATOM   6231 H  HB2  . SER   B 1 139 ? 37.247 -30.329 0.103   1.00 17.80 ?  139 SER   B HB2  1 
ATOM   6232 H  HB3  . SER   B 1 139 ? 37.548 -30.706 -1.412  1.00 17.80 ?  139 SER   B HB3  1 
ATOM   6233 H  HG   . SER   B 1 139 ? 38.301 -28.694 -0.928  1.00 17.89 ?  139 SER   B HG   1 
ATOM   6234 N  N    . LEU   B 1 140 ? 35.423 -30.840 -3.445  1.00 13.46 ?  140 LEU   B N    1 
ATOM   6235 C  CA   . LEU   B 1 140 ? 35.057 -30.593 -4.832  1.00 13.74 ?  140 LEU   B CA   1 
ATOM   6236 C  C    . LEU   B 1 140 ? 33.557 -30.364 -4.962  1.00 14.03 ?  140 LEU   B C    1 
ATOM   6237 O  O    . LEU   B 1 140 ? 33.121 -29.479 -5.699  1.00 14.02 ?  140 LEU   B O    1 
ATOM   6238 C  CB   . LEU   B 1 140 ? 35.523 -31.756 -5.708  1.00 13.85 ?  140 LEU   B CB   1 
ATOM   6239 C  CG   . LEU   B 1 140 ? 35.163 -31.656 -7.182  1.00 14.14 ?  140 LEU   B CG   1 
ATOM   6240 C  CD1  . LEU   B 1 140 ? 35.745 -30.380 -7.777  1.00 14.98 ?  140 LEU   B CD1  1 
ATOM   6241 C  CD2  . LEU   B 1 140 ? 35.644 -32.890 -7.923  1.00 15.39 ?  140 LEU   B CD2  1 
ATOM   6242 H  H    . LEU   B 1 140 ? 35.754 -31.616 -3.300  1.00 16.15 ?  140 LEU   B H    1 
ATOM   6243 H  HA   . LEU   B 1 140 ? 35.508 -29.792 -5.143  1.00 16.48 ?  140 LEU   B HA   1 
ATOM   6244 H  HB2  . LEU   B 1 140 ? 36.489 -31.821 -5.654  1.00 16.61 ?  140 LEU   B HB2  1 
ATOM   6245 H  HB3  . LEU   B 1 140 ? 35.124 -32.576 -5.376  1.00 16.61 ?  140 LEU   B HB3  1 
ATOM   6246 H  HG   . LEU   B 1 140 ? 34.200 -31.607 -7.271  1.00 16.97 ?  140 LEU   B HG   1 
ATOM   6247 H  HD11 . LEU   B 1 140 ? 35.642 -30.409 -8.741  1.00 17.97 ?  140 LEU   B HD11 1 
ATOM   6248 H  HD12 . LEU   B 1 140 ? 35.269 -29.615 -7.418  1.00 17.97 ?  140 LEU   B HD12 1 
ATOM   6249 H  HD13 . LEU   B 1 140 ? 36.686 -30.325 -7.547  1.00 17.97 ?  140 LEU   B HD13 1 
ATOM   6250 H  HD21 . LEU   B 1 140 ? 35.402 -32.802 -8.860  1.00 18.47 ?  140 LEU   B HD21 1 
ATOM   6251 H  HD22 . LEU   B 1 140 ? 36.602 -32.959 -7.830  1.00 18.47 ?  140 LEU   B HD22 1 
ATOM   6252 H  HD23 . LEU   B 1 140 ? 35.209 -33.667 -7.541  1.00 18.47 ?  140 LEU   B HD23 1 
ATOM   6253 N  N    . ARG   B 1 141 ? 32.757 -31.153 -4.244  1.00 14.08 ?  141 ARG   B N    1 
ATOM   6254 C  CA   . ARG   B 1 141 ? 31.307 -30.979 -4.227  1.00 15.01 ?  141 ARG   B CA   1 
ATOM   6255 C  C    . ARG   B 1 141 ? 30.926 -29.570 -3.801  1.00 14.35 ?  141 ARG   B C    1 
ATOM   6256 O  O    . ARG   B 1 141 ? 30.118 -28.898 -4.459  1.00 14.65 ?  141 ARG   B O    1 
ATOM   6257 C  CB   . ARG   B 1 141 ? 30.721 -31.999 -3.245  1.00 16.37 ?  141 ARG   B CB   1 
ATOM   6258 C  CG   . ARG   B 1 141 ? 29.254 -31.872 -2.917  1.00 18.02 ?  141 ARG   B CG   1 
ATOM   6259 C  CD   . ARG   B 1 141 ? 28.451 -32.514 -3.973  1.00 19.33 ?  141 ARG   B CD   1 
ATOM   6260 N  NE   . ARG   B 1 141 ? 28.202 -31.616 -5.090  1.00 19.72 ?  141 ARG   B NE   1 
ATOM   6261 C  CZ   . ARG   B 1 141 ? 28.201 -31.981 -6.364  1.00 19.31 ?  141 ARG   B CZ   1 
ATOM   6262 N  NH1  . ARG   B 1 141 ? 28.619 -33.179 -6.743  1.00 19.08 ?  141 ARG   B NH1  1 
ATOM   6263 N  NH2  . ARG   B 1 141 ? 27.767 -31.123 -7.282  1.00 19.99 ?  141 ARG   B NH2  1 
ATOM   6264 H  H    . ARG   B 1 141 ? 33.036 -31.801 -3.756  1.00 16.90 ?  141 ARG   B H    1 
ATOM   6265 H  HA   . ARG   B 1 141 ? 30.941 -31.145 -5.107  1.00 18.02 ?  141 ARG   B HA   1 
ATOM   6266 H  HB2  . ARG   B 1 141 ? 30.865 -32.887 -3.610  1.00 19.65 ?  141 ARG   B HB2  1 
ATOM   6267 H  HB3  . ARG   B 1 141 ? 31.204 -31.926 -2.408  1.00 19.65 ?  141 ARG   B HB3  1 
ATOM   6268 H  HG2  . ARG   B 1 141 ? 29.080 -32.311 -2.073  1.00 21.63 ?  141 ARG   B HG2  1 
ATOM   6269 H  HG3  . ARG   B 1 141 ? 29.004 -30.930 -2.858  1.00 21.63 ?  141 ARG   B HG3  1 
ATOM   6270 H  HD2  . ARG   B 1 141 ? 28.922 -33.301 -4.297  1.00 23.19 ?  141 ARG   B HD2  1 
ATOM   6271 H  HD3  . ARG   B 1 141 ? 27.603 -32.777 -3.597  1.00 23.19 ?  141 ARG   B HD3  1 
ATOM   6272 H  HE   . ARG   B 1 141 ? 28.035 -30.792 -4.909  1.00 23.66 ?  141 ARG   B HE   1 
ATOM   6273 H  HH11 . ARG   B 1 141 ? 28.889 -33.754 -6.162  1.00 22.90 ?  141 ARG   B HH11 1 
ATOM   6274 H  HH12 . ARG   B 1 141 ? 28.614 -33.391 -7.575  1.00 22.90 ?  141 ARG   B HH12 1 
ATOM   6275 H  HH21 . ARG   B 1 141 ? 27.504 -30.338 -7.049  1.00 23.99 ?  141 ARG   B HH21 1 
ATOM   6276 H  HH22 . ARG   B 1 141 ? 27.781 -31.341 -8.115  1.00 23.99 ?  141 ARG   B HH22 1 
ATOM   6277 N  N    . VAL   B 1 142 ? 31.470 -29.122 -2.672  1.00 14.01 ?  142 VAL   B N    1 
ATOM   6278 C  CA   . VAL   B 1 142 ? 31.133 -27.790 -2.188  1.00 13.90 ?  142 VAL   B CA   1 
ATOM   6279 C  C    . VAL   B 1 142 ? 31.608 -26.732 -3.176  1.00 13.90 ?  142 VAL   B C    1 
ATOM   6280 O  O    . VAL   B 1 142 ? 30.910 -25.746 -3.433  1.00 14.12 ?  142 VAL   B O    1 
ATOM   6281 C  CB   . VAL   B 1 142 ? 31.680 -27.560 -0.767  1.00 14.91 ?  142 VAL   B CB   1 
ATOM   6282 C  CG1  . VAL   B 1 142 ? 31.361 -26.134 -0.296  1.00 15.08 ?  142 VAL   B CG1  1 
ATOM   6283 C  CG2  . VAL   B 1 142 ? 31.096 -28.582 0.194   1.00 15.53 ?  142 VAL   B CG2  1 
ATOM   6284 H  H    . VAL   B 1 142 ? 32.029 -29.555 -2.180  1.00 16.81 ?  142 VAL   B H    1 
ATOM   6285 H  HA   . VAL   B 1 142 ? 30.171 -27.718 -2.138  1.00 16.68 ?  142 VAL   B HA   1 
ATOM   6286 H  HB   . VAL   B 1 142 ? 32.645 -27.664 -0.774  1.00 17.89 ?  142 VAL   B HB   1 
ATOM   6287 H  HG11 . VAL   B 1 142 ? 31.548 -26.066 0.652   1.00 18.10 ?  142 VAL   B HG11 1 
ATOM   6288 H  HG12 . VAL   B 1 142 ? 31.918 -25.504 -0.786  1.00 18.10 ?  142 VAL   B HG12 1 
ATOM   6289 H  HG13 . VAL   B 1 142 ? 30.426 -25.947 -0.465  1.00 18.10 ?  142 VAL   B HG13 1 
ATOM   6290 H  HG21 . VAL   B 1 142 ? 31.413 -28.389 1.090   1.00 18.63 ?  142 VAL   B HG21 1 
ATOM   6291 H  HG22 . VAL   B 1 142 ? 30.129 -28.524 0.164   1.00 18.63 ?  142 VAL   B HG22 1 
ATOM   6292 H  HG23 . VAL   B 1 142 ? 31.385 -29.467 -0.077  1.00 18.63 ?  142 VAL   B HG23 1 
ATOM   6293 N  N    . CYS   B 1 143 ? 32.792 -26.931 -3.758  1.00 13.24 ?  143 CYS   B N    1 
ATOM   6294 C  CA   . CYS   B 1 143 ? 33.290 -25.992 -4.760  1.00 13.27 ?  143 CYS   B CA   1 
ATOM   6295 C  C    . CYS   B 1 143 ? 32.290 -25.846 -5.903  1.00 13.28 ?  143 CYS   B C    1 
ATOM   6296 O  O    . CYS   B 1 143 ? 31.875 -24.737 -6.255  1.00 13.35 ?  143 CYS   B O    1 
ATOM   6297 C  CB   . CYS   B 1 143 ? 34.649 -26.477 -5.285  1.00 13.65 ?  143 CYS   B CB   1 
ATOM   6298 S  SG   . CYS   B 1 143 ? 35.395 -25.381 -6.509  1.00 13.61 ?  143 CYS   B SG   1 
ATOM   6299 H  H    . CYS   B 1 143 ? 33.325 -27.582 -3.586  1.00 15.89 ?  143 CYS   B H    1 
ATOM   6300 H  HA   . CYS   B 1 143 ? 33.425 -25.120 -4.357  1.00 15.92 ?  143 CYS   B HA   1 
ATOM   6301 H  HB2  . CYS   B 1 143 ? 35.272 -26.559 -4.544  1.00 16.39 ?  143 CYS   B HB2  1 
ATOM   6302 H  HB3  . CYS   B 1 143 ? 34.533 -27.345 -5.702  1.00 16.39 ?  143 CYS   B HB3  1 
ATOM   6303 H  HG   . CYS   B 1 143 ? 36.468 -25.815 -6.833  1.00 16.34 ?  143 CYS   B HG   1 
ATOM   6304 N  N    . VAL   B 1 144 ? 31.885 -26.966 -6.492  1.00 13.75 ?  144 VAL   B N    1 
ATOM   6305 C  CA   . VAL   B 1 144 ? 30.975 -26.916 -7.629  1.00 14.57 ?  144 VAL   B CA   1 
ATOM   6306 C  C    . VAL   B 1 144 ? 29.641 -26.290 -7.246  1.00 14.56 ?  144 VAL   B C    1 
ATOM   6307 O  O    . VAL   B 1 144 ? 29.018 -25.588 -8.051  1.00 15.82 ?  144 VAL   B O    1 
ATOM   6308 C  CB   . VAL   B 1 144 ? 30.805 -28.338 -8.180  1.00 17.00 ?  144 VAL   B CB   1 
ATOM   6309 C  CG1  . VAL   B 1 144 ? 29.527 -28.475 -9.002  1.00 19.50 ?  144 VAL   B CG1  1 
ATOM   6310 C  CG2  . VAL   B 1 144 ? 32.045 -28.748 -8.968  1.00 17.19 ?  144 VAL   B CG2  1 
ATOM   6311 H  H    . VAL   B 1 144 ? 32.124 -27.761 -6.263  1.00 16.49 ?  144 VAL   B H    1 
ATOM   6312 H  HA   . VAL   B 1 144 ? 31.363 -26.371 -8.332  1.00 17.48 ?  144 VAL   B HA   1 
ATOM   6313 H  HB   . VAL   B 1 144 ? 30.729 -28.950 -7.429  1.00 20.41 ?  144 VAL   B HB   1 
ATOM   6314 H  HG11 . VAL   B 1 144 ? 29.593 -29.274 -9.553  1.00 23.40 ?  144 VAL   B HG11 1 
ATOM   6315 H  HG12 . VAL   B 1 144 ? 28.770 -28.556 -8.402  1.00 23.40 ?  144 VAL   B HG12 1 
ATOM   6316 H  HG13 . VAL   B 1 144 ? 29.428 -27.696 -9.568  1.00 23.40 ?  144 VAL   B HG13 1 
ATOM   6317 H  HG21 . VAL   B 1 144 ? 31.924 -29.653 -9.304  1.00 20.63 ?  144 VAL   B HG21 1 
ATOM   6318 H  HG22 . VAL   B 1 144 ? 32.163 -28.136 -9.712  1.00 20.63 ?  144 VAL   B HG22 1 
ATOM   6319 H  HG23 . VAL   B 1 144 ? 32.817 -28.714 -8.384  1.00 20.63 ?  144 VAL   B HG23 1 
ATOM   6320 N  N    . ASP   B 1 145 ? 29.172 -26.542 -6.027  1.00 14.79 ?  145 ASP   B N    1 
ATOM   6321 C  CA   . ASP   B 1 145 ? 27.860 -26.076 -5.601  1.00 15.63 ?  145 ASP   B CA   1 
ATOM   6322 C  C    . ASP   B 1 145 ? 27.889 -24.650 -5.067  1.00 14.99 ?  145 ASP   B C    1 
ATOM   6323 O  O    . ASP   B 1 145 ? 26.827 -24.101 -4.749  1.00 16.76 ?  145 ASP   B O    1 
ATOM   6324 C  CB   . ASP   B 1 145 ? 27.279 -26.996 -4.520  1.00 17.16 ?  145 ASP   B CB   1 
ATOM   6325 C  CG   . ASP   B 1 145 ? 26.917 -28.368 -5.032  1.00 18.79 ?  145 ASP   B CG   1 
ATOM   6326 O  OD1  . ASP   B 1 145 ? 26.817 -28.566 -6.259  1.00 19.20 ?  145 ASP   B OD1  1 
ATOM   6327 O  OD2  . ASP   B 1 145 ? 26.720 -29.245 -4.176  1.00 20.44 -1 145 ASP   B OD2  1 
ATOM   6328 H  H    . ASP   B 1 145 ? 29.603 -26.973 -5.424  1.00 17.75 ?  145 ASP   B H    1 
ATOM   6329 H  HA   . ASP   B 1 145 ? 27.263 -26.074 -6.363  1.00 18.75 ?  145 ASP   B HA   1 
ATOM   6330 H  HB2  . ASP   B 1 145 ? 27.930 -27.108 -3.820  1.00 20.59 ?  145 ASP   B HB2  1 
ATOM   6331 H  HB3  . ASP   B 1 145 ? 26.470 -26.589 -4.169  1.00 20.59 ?  145 ASP   B HB3  1 
ATOM   6332 N  N    . THR   B 1 146 ? 29.066 -24.041 -4.951  1.00 13.54 ?  146 THR   B N    1 
ATOM   6333 C  CA   . THR   B 1 146 ? 29.200 -22.717 -4.350  1.00 13.14 ?  146 THR   B CA   1 
ATOM   6334 C  C    . THR   B 1 146 ? 29.833 -21.688 -5.271  1.00 12.85 ?  146 THR   B C    1 
ATOM   6335 O  O    . THR   B 1 146 ? 29.375 -20.530 -5.321  1.00 12.91 ?  146 THR   B O    1 
ATOM   6336 C  CB   . THR   B 1 146 ? 30.032 -22.816 -3.065  1.00 13.42 ?  146 THR   B CB   1 
ATOM   6337 O  OG1  . THR   B 1 146 ? 29.457 -23.799 -2.202  1.00 13.84 ?  146 THR   B OG1  1 
ATOM   6338 C  CG2  . THR   B 1 146 ? 30.101 -21.471 -2.345  1.00 13.82 ?  146 THR   B CG2  1 
ATOM   6339 H  H    . THR   B 1 146 ? 29.820 -24.363 -5.222  1.00 16.25 ?  146 THR   B H    1 
ATOM   6340 H  HA   . THR   B 1 146 ? 28.328 -22.381 -4.106  1.00 15.77 ?  146 THR   B HA   1 
ATOM   6341 H  HB   . THR   B 1 146 ? 30.944 -23.070 -3.289  1.00 16.10 ?  146 THR   B HB   1 
ATOM   6342 H  HG1  . THR   B 1 146 ? 29.495 -24.560 -2.574  1.00 16.61 ?  146 THR   B HG1  1 
ATOM   6343 H  HG21 . THR   B 1 146 ? 30.453 -21.590 -1.450  1.00 16.59 ?  146 THR   B HG21 1 
ATOM   6344 H  HG22 . THR   B 1 146 ? 30.685 -20.861 -2.830  1.00 16.59 ?  146 THR   B HG22 1 
ATOM   6345 H  HG23 . THR   B 1 146 ? 29.217 -21.081 -2.288  1.00 16.59 ?  146 THR   B HG23 1 
ATOM   6346 N  N    . VAL   B 1 147 ? 30.900 -22.058 -5.970  1.00 12.79 ?  147 VAL   B N    1 
ATOM   6347 C  CA   . VAL   B 1 147 ? 31.624 -21.116 -6.810  1.00 12.50 ?  147 VAL   B CA   1 
ATOM   6348 C  C    . VAL   B 1 147 ? 30.885 -20.987 -8.130  1.00 12.51 ?  147 VAL   B C    1 
ATOM   6349 O  O    . VAL   B 1 147 ? 30.513 -21.991 -8.757  1.00 13.44 ?  147 VAL   B O    1 
ATOM   6350 C  CB   . VAL   B 1 147 ? 33.076 -21.579 -7.018  1.00 12.57 ?  147 VAL   B CB   1 
ATOM   6351 C  CG1  . VAL   B 1 147 ? 33.837 -20.563 -7.846  1.00 12.58 ?  147 VAL   B CG1  1 
ATOM   6352 C  CG2  . VAL   B 1 147 ? 33.757 -21.791 -5.678  1.00 12.71 ?  147 VAL   B CG2  1 
ATOM   6353 H  H    . VAL   B 1 147 ? 31.219 -22.859 -5.987  1.00 15.34 ?  147 VAL   B H    1 
ATOM   6354 H  HA   . VAL   B 1 147 ? 31.645 -20.248 -6.379  1.00 15.00 ?  147 VAL   B HA   1 
ATOM   6355 H  HB   . VAL   B 1 147 ? 33.079 -22.428 -7.497  1.00 15.08 ?  147 VAL   B HB   1 
ATOM   6356 H  HG11 . VAL   B 1 147 ? 34.780 -20.786 -7.833  1.00 15.09 ?  147 VAL   B HG11 1 
ATOM   6357 H  HG12 . VAL   B 1 147 ? 33.505 -20.578 -8.756  1.00 15.09 ?  147 VAL   B HG12 1 
ATOM   6358 H  HG13 . VAL   B 1 147 ? 33.703 -19.681 -7.459  1.00 15.09 ?  147 VAL   B HG13 1 
ATOM   6359 H  HG21 . VAL   B 1 147 ? 34.696 -21.993 -5.829  1.00 15.25 ?  147 VAL   B HG21 1 
ATOM   6360 H  HG22 . VAL   B 1 147 ? 33.675 -20.979 -5.153  1.00 15.25 ?  147 VAL   B HG22 1 
ATOM   6361 H  HG23 . VAL   B 1 147 ? 33.332 -22.529 -5.216  1.00 15.25 ?  147 VAL   B HG23 1 
ATOM   6362 N  N    . ARG   B 1 148 ? 30.667 -19.737 -8.548  1.00 12.22 ?  148 ARG   B N    1 
ATOM   6363 C  CA   . ARG   B 1 148 ? 30.050 -19.422 -9.825  1.00 12.78 ?  148 ARG   B CA   1 
ATOM   6364 C  C    . ARG   B 1 148 ? 31.008 -18.756 -10.800 1.00 12.53 ?  148 ARG   B C    1 
ATOM   6365 O  O    . ARG   B 1 148 ? 30.720 -18.740 -12.001 1.00 14.15 ?  148 ARG   B O    1 
ATOM   6366 C  CB   . ARG   B 1 148 ? 28.811 -18.536 -9.615  1.00 13.12 ?  148 ARG   B CB   1 
ATOM   6367 C  CG   . ARG   B 1 148 ? 27.741 -19.240 -8.795  1.00 13.81 ?  148 ARG   B CG   1 
ATOM   6368 C  CD   . ARG   B 1 148 ? 26.531 -18.355 -8.493  1.00 14.56 ?  148 ARG   B CD   1 
ATOM   6369 N  NE   . ARG   B 1 148 ? 26.912 -17.154 -7.761  1.00 14.51 ?  148 ARG   B NE   1 
ATOM   6370 C  CZ   . ARG   B 1 148 ? 27.217 -17.118 -6.471  1.00 13.40 ?  148 ARG   B CZ   1 
ATOM   6371 N  NH1  . ARG   B 1 148 ? 27.155 -18.202 -5.713  1.00 13.73 ?  148 ARG   B NH1  1 
ATOM   6372 N  NH2  . ARG   B 1 148 ? 27.615 -15.968 -5.930  1.00 13.73 ?  148 ARG   B NH2  1 
ATOM   6373 H  H    . ARG   B 1 148 ? 30.874 -19.033 -8.085  1.00 14.66 ?  148 ARG   B H    1 
ATOM   6374 H  HA   . ARG   B 1 148 ? 29.752 -20.245 -10.230 1.00 15.34 ?  148 ARG   B HA   1 
ATOM   6375 H  HB2  . ARG   B 1 148 ? 29.069 -17.729 -9.143  1.00 15.74 ?  148 ARG   B HB2  1 
ATOM   6376 H  HB3  . ARG   B 1 148 ? 28.431 -18.311 -10.479 1.00 15.74 ?  148 ARG   B HB3  1 
ATOM   6377 H  HG2  . ARG   B 1 148 ? 27.424 -20.017 -9.290  1.00 16.57 ?  148 ARG   B HG2  1 
ATOM   6378 H  HG3  . ARG   B 1 148 ? 28.121 -19.524 -7.950  1.00 16.57 ?  148 ARG   B HG3  1 
ATOM   6379 H  HD2  . ARG   B 1 148 ? 26.116 -18.082 -9.326  1.00 17.47 ?  148 ARG   B HD2  1 
ATOM   6380 H  HD3  . ARG   B 1 148 ? 25.895 -18.853 -7.952  1.00 17.47 ?  148 ARG   B HD3  1 
ATOM   6381 H  HE   . ARG   B 1 148 ? 26.945 -16.415 -8.195  1.00 17.41 ?  148 ARG   B HE   1 
ATOM   6382 H  HH11 . ARG   B 1 148 ? 26.899 -18.954 -6.047  1.00 16.47 ?  148 ARG   B HH11 1 
ATOM   6383 H  HH12 . ARG   B 1 148 ? 27.356 -18.158 -4.875  1.00 16.47 ?  148 ARG   B HH12 1 
ATOM   6384 H  HH21 . ARG   B 1 148 ? 27.665 -15.261 -6.413  1.00 16.47 ?  148 ARG   B HH21 1 
ATOM   6385 H  HH22 . ARG   B 1 148 ? 27.818 -15.933 -5.094  1.00 16.47 ?  148 ARG   B HH22 1 
ATOM   6386 N  N    . THR   B 1 149 ? 32.117 -18.200 -10.316 1.00 12.40 ?  149 THR   B N    1 
ATOM   6387 C  CA   . THR   B 1 149 ? 33.153 -17.639 -11.168 1.00 12.66 ?  149 THR   B CA   1 
ATOM   6388 C  C    . THR   B 1 149 ? 34.039 -18.775 -11.679 1.00 12.37 ?  149 THR   B C    1 
ATOM   6389 O  O    . THR   B 1 149 ? 33.844 -19.944 -11.337 1.00 12.62 ?  149 THR   B O    1 
ATOM   6390 C  CB   . THR   B 1 149 ? 33.924 -16.582 -10.384 1.00 12.55 ?  149 THR   B CB   1 
ATOM   6391 O  OG1  . THR   B 1 149 ? 34.378 -17.178 -9.168  1.00 12.75 ?  149 THR   B OG1  1 
ATOM   6392 C  CG2  . THR   B 1 149 ? 33.035 -15.385 -10.076 1.00 13.21 ?  149 THR   B CG2  1 
ATOM   6393 H  H    . THR   B 1 149 ? 32.287 -18.134 -9.477  1.00 14.88 ?  149 THR   B H    1 
ATOM   6394 H  HA   . THR   B 1 149 ? 32.742 -17.206 -11.930 1.00 15.19 ?  149 THR   B HA   1 
ATOM   6395 H  HB   . THR   B 1 149 ? 34.688 -16.288 -10.897 1.00 15.06 ?  149 THR   B HB   1 
ATOM   6396 H  HG1  . THR   B 1 149 ? 34.796 -16.607 -8.704  1.00 15.30 ?  149 THR   B HG1  1 
ATOM   6397 H  HG21 . THR   B 1 149 ? 33.540 -14.714 -9.590  1.00 15.85 ?  149 THR   B HG21 1 
ATOM   6398 H  HG22 . THR   B 1 149 ? 32.708 -14.997 -10.902 1.00 15.85 ?  149 THR   B HG22 1 
ATOM   6399 H  HG23 . THR   B 1 149 ? 32.278 -15.661 -9.535  1.00 15.85 ?  149 THR   B HG23 1 
ATOM   6400 N  N    . ASN   B 1 150 ? 35.008 -18.453 -12.527 1.00 12.31 ?  150 ASN   B N    1 
ATOM   6401 C  CA   . ASN   B 1 150 ? 35.769 -19.479 -13.227 1.00 12.82 ?  150 ASN   B CA   1 
ATOM   6402 C  C    . ASN   B 1 150 ? 36.935 -19.926 -12.356 1.00 12.27 ?  150 ASN   B C    1 
ATOM   6403 O  O    . ASN   B 1 150 ? 37.864 -19.152 -12.102 1.00 12.87 ?  150 ASN   B O    1 
ATOM   6404 C  CB   . ASN   B 1 150 ? 36.242 -18.946 -14.570 1.00 14.41 ?  150 ASN   B CB   1 
ATOM   6405 C  CG   . ASN   B 1 150 ? 35.105 -18.740 -15.516 1.00 17.07 ?  150 ASN   B CG   1 
ATOM   6406 O  OD1  . ASN   B 1 150 ? 34.209 -19.570 -15.594 1.00 18.25 ?  150 ASN   B OD1  1 
ATOM   6407 N  ND2  . ASN   B 1 150 ? 35.106 -17.621 -16.218 1.00 19.20 ?  150 ASN   B ND2  1 
ATOM   6408 H  H    . ASN   B 1 150 ? 35.253 -17.646 -12.705 1.00 14.77 ?  150 ASN   B H    1 
ATOM   6409 H  HA   . ASN   B 1 150 ? 35.197 -20.245 -13.387 1.00 15.39 ?  150 ASN   B HA   1 
ATOM   6410 H  HB2  . ASN   B 1 150 ? 36.683 -18.090 -14.434 1.00 17.29 ?  150 ASN   B HB2  1 
ATOM   6411 H  HB3  . ASN   B 1 150 ? 36.855 -19.579 -14.967 1.00 17.29 ?  150 ASN   B HB3  1 
ATOM   6412 H  HD21 . ASN   B 1 150 ? 34.470 -17.455 -16.776 1.00 23.04 ?  150 ASN   B HD21 1 
ATOM   6413 H  HD22 . ASN   B 1 150 ? 35.753 -17.058 -16.132 1.00 23.04 ?  150 ASN   B HD22 1 
ATOM   6414 N  N    . VAL   B 1 151 ? 36.892 -21.173 -11.898 1.00 12.19 ?  151 VAL   B N    1 
ATOM   6415 C  CA   . VAL   B 1 151 ? 37.902 -21.707 -10.998 1.00 12.31 ?  151 VAL   B CA   1 
ATOM   6416 C  C    . VAL   B 1 151 ? 38.606 -22.875 -11.674 1.00 11.93 ?  151 VAL   B C    1 
ATOM   6417 O  O    . VAL   B 1 151 ? 37.965 -23.813 -12.174 1.00 13.19 ?  151 VAL   B O    1 
ATOM   6418 C  CB   . VAL   B 1 151 ? 37.332 -22.052 -9.607  1.00 13.66 ?  151 VAL   B CB   1 
ATOM   6419 C  CG1  . VAL   B 1 151 ? 36.179 -23.054 -9.694  1.00 14.96 ?  151 VAL   B CG1  1 
ATOM   6420 C  CG2  . VAL   B 1 151 ? 38.438 -22.540 -8.684  1.00 14.09 ?  151 VAL   B CG2  1 
ATOM   6421 H  H    . VAL   B 1 151 ? 36.273 -21.738 -12.102 1.00 14.62 ?  151 VAL   B H    1 
ATOM   6422 H  HA   . VAL   B 1 151 ? 38.569 -21.019 -10.859 1.00 14.77 ?  151 VAL   B HA   1 
ATOM   6423 H  HB   . VAL   B 1 151 ? 36.973 -21.239 -9.218  1.00 16.39 ?  151 VAL   B HB   1 
ATOM   6424 H  HG11 . VAL   B 1 151 ? 35.848 -23.239 -8.800  1.00 17.96 ?  151 VAL   B HG11 1 
ATOM   6425 H  HG12 . VAL   B 1 151 ? 35.465 -22.674 -10.234 1.00 17.96 ?  151 VAL   B HG12 1 
ATOM   6426 H  HG13 . VAL   B 1 151 ? 36.497 -23.874 -10.104 1.00 17.96 ?  151 VAL   B HG13 1 
ATOM   6427 H  HG21 . VAL   B 1 151 ? 38.079 -22.625 -7.784  1.00 16.91 ?  151 VAL   B HG21 1 
ATOM   6428 H  HG22 . VAL   B 1 151 ? 38.755 -23.400 -8.994  1.00 16.91 ?  151 VAL   B HG22 1 
ATOM   6429 H  HG23 . VAL   B 1 151 ? 39.160 -21.894 -8.689  1.00 16.91 ?  151 VAL   B HG23 1 
ATOM   6430 N  N    . TYR   B 1 152 ? 39.933 -22.783 -11.701 1.00 11.61 ?  152 TYR   B N    1 
ATOM   6431 C  CA   . TYR   B 1 152 ? 40.837 -23.764 -12.281 1.00 11.91 ?  152 TYR   B CA   1 
ATOM   6432 C  C    . TYR   B 1 152 ? 41.559 -24.440 -11.120 1.00 11.17 ?  152 TYR   B C    1 
ATOM   6433 O  O    . TYR   B 1 152 ? 42.405 -23.824 -10.467 1.00 11.88 ?  152 TYR   B O    1 
ATOM   6434 C  CB   . TYR   B 1 152 ? 41.805 -23.056 -13.228 1.00 12.58 ?  152 TYR   B CB   1 
ATOM   6435 C  CG   . TYR   B 1 152 ? 41.124 -22.593 -14.492 1.00 13.13 ?  152 TYR   B CG   1 
ATOM   6436 C  CD1  . TYR   B 1 152 ? 40.458 -21.374 -14.556 1.00 13.73 ?  152 TYR   B CD1  1 
ATOM   6437 C  CD2  . TYR   B 1 152 ? 41.123 -23.402 -15.614 1.00 14.30 ?  152 TYR   B CD2  1 
ATOM   6438 C  CE1  . TYR   B 1 152 ? 39.816 -20.974 -15.714 1.00 15.04 ?  152 TYR   B CE1  1 
ATOM   6439 C  CE2  . TYR   B 1 152 ? 40.488 -23.018 -16.773 1.00 15.44 ?  152 TYR   B CE2  1 
ATOM   6440 C  CZ   . TYR   B 1 152 ? 39.833 -21.804 -16.825 1.00 15.65 ?  152 TYR   B CZ   1 
ATOM   6441 O  OH   . TYR   B 1 152 ? 39.202 -21.433 -17.990 1.00 18.05 ?  152 TYR   B OH   1 
ATOM   6442 H  H    . TYR   B 1 152 ? 40.366 -22.115 -11.358 1.00 13.93 ?  152 TYR   B H    1 
ATOM   6443 H  HA   . TYR   B 1 152 ? 40.332 -24.431 -12.777 1.00 14.29 ?  152 TYR   B HA   1 
ATOM   6444 H  HB2  . TYR   B 1 152 ? 42.172 -22.277 -12.776 1.00 15.09 ?  152 TYR   B HB2  1 
ATOM   6445 H  HB3  . TYR   B 1 152 ? 42.519 -23.665 -13.470 1.00 15.09 ?  152 TYR   B HB3  1 
ATOM   6446 H  HD1  . TYR   B 1 152 ? 40.440 -20.817 -13.807 1.00 16.48 ?  152 TYR   B HD1  1 
ATOM   6447 H  HD2  . TYR   B 1 152 ? 41.558 -24.226 -15.584 1.00 17.16 ?  152 TYR   B HD2  1 
ATOM   6448 H  HE1  . TYR   B 1 152 ? 39.377 -20.154 -15.750 1.00 18.04 ?  152 TYR   B HE1  1 
ATOM   6449 H  HE2  . TYR   B 1 152 ? 40.504 -23.571 -17.520 1.00 18.52 ?  152 TYR   B HE2  1 
ATOM   6450 H  HH   . TYR   B 1 152 ? 38.855 -20.674 -17.890 1.00 21.66 ?  152 TYR   B HH   1 
ATOM   6451 N  N    . LEU   B 1 153 ? 41.187 -25.692 -10.842 1.00 11.43 ?  153 LEU   B N    1 
ATOM   6452 C  CA   . LEU   B 1 153 ? 41.703 -26.443 -9.708  1.00 11.40 ?  153 LEU   B CA   1 
ATOM   6453 C  C    . LEU   B 1 153 ? 42.935 -27.244 -10.106 1.00 12.02 ?  153 LEU   B C    1 
ATOM   6454 O  O    . LEU   B 1 153 ? 42.919 -27.971 -11.104 1.00 13.09 ?  153 LEU   B O    1 
ATOM   6455 C  CB   . LEU   B 1 153 ? 40.624 -27.401 -9.197  1.00 11.71 ?  153 LEU   B CB   1 
ATOM   6456 C  CG   . LEU   B 1 153 ? 39.362 -26.749 -8.632  1.00 12.77 ?  153 LEU   B CG   1 
ATOM   6457 C  CD1  . LEU   B 1 153 ? 38.276 -27.792 -8.465  1.00 13.89 ?  153 LEU   B CD1  1 
ATOM   6458 C  CD2  . LEU   B 1 153 ? 39.666 -26.083 -7.304  1.00 12.94 ?  153 LEU   B CD2  1 
ATOM   6459 H  H    . LEU   B 1 153 ? 40.606 -26.136 -11.311 1.00 13.71 ?  153 LEU   B H    1 
ATOM   6460 H  HA   . LEU   B 1 153 ? 41.928 -25.835 -8.995  1.00 13.68 ?  153 LEU   B HA   1 
ATOM   6461 H  HB2  . LEU   B 1 153 ? 40.343 -27.977 -9.926  1.00 14.05 ?  153 LEU   B HB2  1 
ATOM   6462 H  HB3  . LEU   B 1 153 ? 41.002 -27.946 -8.486  1.00 14.05 ?  153 LEU   B HB3  1 
ATOM   6463 H  HG   . LEU   B 1 153 ? 39.038 -26.070 -9.248  1.00 15.33 ?  153 LEU   B HG   1 
ATOM   6464 H  HD11 . LEU   B 1 153 ? 37.467 -27.357 -8.143  1.00 16.66 ?  153 LEU   B HD11 1 
ATOM   6465 H  HD12 . LEU   B 1 153 ? 38.106 -28.208 -9.322  1.00 16.66 ?  153 LEU   B HD12 1 
ATOM   6466 H  HD13 . LEU   B 1 153 ? 38.572 -28.453 -7.823  1.00 16.66 ?  153 LEU   B HD13 1 
ATOM   6467 H  HD21 . LEU   B 1 153 ? 38.847 -25.719 -6.932  1.00 15.53 ?  153 LEU   B HD21 1 
ATOM   6468 H  HD22 . LEU   B 1 153 ? 40.041 -26.742 -6.699  1.00 15.53 ?  153 LEU   B HD22 1 
ATOM   6469 H  HD23 . LEU   B 1 153 ? 40.307 -25.367 -7.450  1.00 15.53 ?  153 LEU   B HD23 1 
ATOM   6470 N  N    . ALA   B 1 154 ? 43.988 -27.134 -9.301  1.00 12.07 ?  154 ALA   B N    1 
ATOM   6471 C  CA   . ALA   B 1 154 ? 45.214 -27.902 -9.481  1.00 13.20 ?  154 ALA   B CA   1 
ATOM   6472 C  C    . ALA   B 1 154 ? 45.279 -28.977 -8.404  1.00 13.71 ?  154 ALA   B C    1 
ATOM   6473 O  O    . ALA   B 1 154 ? 45.199 -28.676 -7.205  1.00 14.95 ?  154 ALA   B O    1 
ATOM   6474 C  CB   . ALA   B 1 154 ? 46.434 -26.989 -9.412  1.00 13.85 ?  154 ALA   B CB   1 
ATOM   6475 H  H    . ALA   B 1 154 ? 44.007 -26.602 -8.619  1.00 14.49 ?  154 ALA   B H    1 
ATOM   6476 H  HA   . ALA   B 1 154 ? 45.201 -28.329 -10.346 1.00 15.84 ?  154 ALA   B HA   1 
ATOM   6477 H  HB1  . ALA   B 1 154 ? 47.236 -27.518 -9.534  1.00 16.62 ?  154 ALA   B HB1  1 
ATOM   6478 H  HB2  . ALA   B 1 154 ? 46.371 -26.317 -10.113 1.00 16.62 ?  154 ALA   B HB2  1 
ATOM   6479 H  HB3  . ALA   B 1 154 ? 46.458 -26.549 -8.544  1.00 16.62 ?  154 ALA   B HB3  1 
ATOM   6480 N  N    . VAL   B 1 155 ? 45.399 -30.227 -8.833  1.00 13.12 ?  155 VAL   B N    1 
ATOM   6481 C  CA   . VAL   B 1 155 ? 45.514 -31.370 -7.936  1.00 13.34 ?  155 VAL   B CA   1 
ATOM   6482 C  C    . VAL   B 1 155 ? 46.853 -32.038 -8.219  1.00 13.46 ?  155 VAL   B C    1 
ATOM   6483 O  O    . VAL   B 1 155 ? 47.086 -32.532 -9.329  1.00 15.14 ?  155 VAL   B O    1 
ATOM   6484 C  CB   . VAL   B 1 155 ? 44.359 -32.365 -8.125  1.00 14.67 ?  155 VAL   B CB   1 
ATOM   6485 C  CG1  . VAL   B 1 155 ? 44.546 -33.562 -7.210  1.00 14.66 ?  155 VAL   B CG1  1 
ATOM   6486 C  CG2  . VAL   B 1 155 ? 43.027 -31.675 -7.855  1.00 15.76 ?  155 VAL   B CG2  1 
ATOM   6487 H  H    . VAL   B 1 155 ? 45.430 -30.444 -9.666  1.00 15.75 ?  155 VAL   B H    1 
ATOM   6488 H  HA   . VAL   B 1 155 ? 45.510 -31.066 -7.015  1.00 16.01 ?  155 VAL   B HA   1 
ATOM   6489 H  HB   . VAL   B 1 155 ? 44.357 -32.677 -9.043  1.00 17.60 ?  155 VAL   B HB   1 
ATOM   6490 H  HG11 . VAL   B 1 155 ? 43.719 -34.067 -7.173  1.00 17.59 ?  155 VAL   B HG11 1 
ATOM   6491 H  HG12 . VAL   B 1 155 ? 45.258 -34.126 -7.559  1.00 17.59 ?  155 VAL   B HG12 1 
ATOM   6492 H  HG13 . VAL   B 1 155 ? 44.781 -33.251 -6.320  1.00 17.59 ?  155 VAL   B HG13 1 
ATOM   6493 H  HG21 . VAL   B 1 155 ? 42.315 -32.331 -7.937  1.00 18.91 ?  155 VAL   B HG21 1 
ATOM   6494 H  HG22 . VAL   B 1 155 ? 43.039 -31.313 -6.954  1.00 18.91 ?  155 VAL   B HG22 1 
ATOM   6495 H  HG23 . VAL   B 1 155 ? 42.901 -30.965 -8.498  1.00 18.91 ?  155 VAL   B HG23 1 
ATOM   6496 N  N    . PHE   B 1 156 ? 47.721 -32.077 -7.208  1.00 13.83 ?  156 PHE   B N    1 
ATOM   6497 C  CA   . PHE   B 1 156 ? 49.099 -32.531 -7.412  1.00 14.86 ?  156 PHE   B CA   1 
ATOM   6498 C  C    . PHE   B 1 156 ? 49.196 -34.031 -7.692  1.00 16.07 ?  156 PHE   B C    1 
ATOM   6499 O  O    . PHE   B 1 156 ? 49.920 -34.457 -8.603  1.00 17.78 ?  156 PHE   B O    1 
ATOM   6500 C  CB   . PHE   B 1 156 ? 49.927 -32.155 -6.187  1.00 15.09 ?  156 PHE   B CB   1 
ATOM   6501 C  CG   . PHE   B 1 156 ? 51.351 -32.622 -6.245  1.00 15.74 ?  156 PHE   B CG   1 
ATOM   6502 C  CD1  . PHE   B 1 156 ? 52.240 -32.080 -7.155  1.00 17.31 ?  156 PHE   B CD1  1 
ATOM   6503 C  CD2  . PHE   B 1 156 ? 51.804 -33.585 -5.367  1.00 16.12 ?  156 PHE   B CD2  1 
ATOM   6504 C  CE1  . PHE   B 1 156 ? 53.562 -32.502 -7.197  1.00 18.02 ?  156 PHE   B CE1  1 
ATOM   6505 C  CE2  . PHE   B 1 156 ? 53.125 -34.013 -5.407  1.00 17.31 ?  156 PHE   B CE2  1 
ATOM   6506 C  CZ   . PHE   B 1 156 ? 53.995 -33.467 -6.325  1.00 17.87 ?  156 PHE   B CZ   1 
ATOM   6507 H  H    . PHE   B 1 156 ? 47.537 -31.859 -6.398  1.00 16.60 ?  156 PHE   B H    1 
ATOM   6508 H  HA   . PHE   B 1 156 ? 49.466 -32.064 -8.174  1.00 17.83 ?  156 PHE   B HA   1 
ATOM   6509 H  HB2  . PHE   B 1 156 ? 49.941 -31.189 -6.107  1.00 18.11 ?  156 PHE   B HB2  1 
ATOM   6510 H  HB3  . PHE   B 1 156 ? 49.522 -32.545 -5.398  1.00 18.11 ?  156 PHE   B HB3  1 
ATOM   6511 H  HD1  . PHE   B 1 156 ? 51.953 -31.422 -7.748  1.00 20.77 ?  156 PHE   B HD1  1 
ATOM   6512 H  HD2  . PHE   B 1 156 ? 51.215 -33.960 -4.750  1.00 19.34 ?  156 PHE   B HD2  1 
ATOM   6513 H  HE1  . PHE   B 1 156 ? 54.155 -32.131 -7.816  1.00 21.62 ?  156 PHE   B HE1  1 
ATOM   6514 H  HE2  . PHE   B 1 156 ? 53.419 -34.673 -4.816  1.00 20.77 ?  156 PHE   B HE2  1 
ATOM   6515 H  HZ   . PHE   B 1 156 ? 54.883 -33.755 -6.352  1.00 21.44 ?  156 PHE   B HZ   1 
ATOM   6516 N  N    . ASP   B 1 157 ? 48.531 -34.850 -6.889  1.00 16.69 ?  157 ASP   B N    1 
ATOM   6517 C  CA   . ASP   B 1 157 ? 48.672 -36.299 -6.984  1.00 18.09 ?  157 ASP   B CA   1 
ATOM   6518 C  C    . ASP   B 1 157 ? 47.756 -36.843 -8.074  1.00 18.26 ?  157 ASP   B C    1 
ATOM   6519 O  O    . ASP   B 1 157 ? 46.529 -36.735 -7.967  1.00 17.56 ?  157 ASP   B O    1 
ATOM   6520 C  CB   . ASP   B 1 157 ? 48.306 -36.911 -5.638  1.00 19.52 ?  157 ASP   B CB   1 
ATOM   6521 C  CG   . ASP   B 1 157 ? 48.454 -38.424 -5.620  1.00 21.44 ?  157 ASP   B CG   1 
ATOM   6522 O  OD1  . ASP   B 1 157 ? 48.791 -39.022 -6.669  1.00 22.00 ?  157 ASP   B OD1  1 
ATOM   6523 O  OD2  . ASP   B 1 157 ? 48.247 -39.015 -4.543  1.00 23.40 -1 157 ASP   B OD2  1 
ATOM   6524 H  H    . ASP   B 1 157 ? 47.993 -34.594 -6.279  1.00 20.03 ?  157 ASP   B H    1 
ATOM   6525 H  HA   . ASP   B 1 157 ? 49.591 -36.535 -7.198  1.00 21.70 ?  157 ASP   B HA   1 
ATOM   6526 H  HB2  . ASP   B 1 157 ? 48.874 -36.526 -4.957  1.00 23.43 ?  157 ASP   B HB2  1 
ATOM   6527 H  HB3  . ASP   B 1 157 ? 47.375 -36.701 -5.447  1.00 23.43 ?  157 ASP   B HB3  1 
ATOM   6528 N  N    . LYS   B 1 158 ? 48.351 -37.459 -9.103  1.00 19.28 ?  158 LYS   B N    1 
ATOM   6529 C  CA   . LYS   B 1 158 ? 47.578 -38.067 -10.187 1.00 20.21 ?  158 LYS   B CA   1 
ATOM   6530 C  C    . LYS   B 1 158 ? 46.520 -39.034 -9.660  1.00 20.25 ?  158 LYS   B C    1 
ATOM   6531 O  O    . LYS   B 1 158 ? 45.419 -39.126 -10.215 1.00 20.12 ?  158 LYS   B O    1 
ATOM   6532 C  CB   . LYS   B 1 158 ? 48.526 -38.783 -11.159 1.00 21.94 ?  158 LYS   B CB   1 
ATOM   6533 C  CG   . LYS   B 1 158 ? 47.847 -39.694 -12.175 1.00 24.10 ?  158 LYS   B CG   1 
ATOM   6534 C  CD   . LYS   B 1 158 ? 46.978 -38.922 -13.145 1.00 26.16 ?  158 LYS   B CD   1 
ATOM   6535 C  CE   . LYS   B 1 158 ? 46.388 -39.844 -14.199 1.00 28.00 ?  158 LYS   B CE   1 
ATOM   6536 N  NZ   . LYS   B 1 158 ? 45.314 -39.174 -14.987 1.00 28.15 ?  158 LYS   B NZ   1 
ATOM   6537 H  H    . LYS   B 1 158 ? 49.207 -37.538 -9.198  1.00 23.13 ?  158 LYS   B H    1 
ATOM   6538 H  HA   . LYS   B 1 158 ? 47.128 -37.367 -10.687 1.00 24.26 ?  158 LYS   B HA   1 
ATOM   6539 H  HB2  . LYS   B 1 158 ? 49.025 -38.115 -11.663 1.00 26.33 ?  158 LYS   B HB2  1 
ATOM   6540 H  HB3  . LYS   B 1 158 ? 49.147 -39.327 -10.648 1.00 26.33 ?  158 LYS   B HB3  1 
ATOM   6541 H  HG2  . LYS   B 1 158 ? 48.532 -40.152 -12.691 1.00 28.91 ?  158 LYS   B HG2  1 
ATOM   6542 H  HG3  . LYS   B 1 158 ? 47.296 -40.352 -11.720 1.00 28.91 ?  158 LYS   B HG3  1 
ATOM   6543 H  HD2  . LYS   B 1 158 ? 46.249 -38.503 -12.662 1.00 31.40 ?  158 LYS   B HD2  1 
ATOM   6544 H  HD3  . LYS   B 1 158 ? 47.516 -38.251 -13.595 1.00 31.40 ?  158 LYS   B HD3  1 
ATOM   6545 H  HE2  . LYS   B 1 158 ? 47.086 -40.117 -14.813 1.00 33.60 ?  158 LYS   B HE2  1 
ATOM   6546 H  HE3  . LYS   B 1 158 ? 46.004 -40.622 -13.765 1.00 33.60 ?  158 LYS   B HE3  1 
ATOM   6547 H  HZ1  . LYS   B 1 158 ? 44.986 -39.735 -15.594 1.00 33.78 ?  158 LYS   B HZ1  1 
ATOM   6548 H  HZ2  . LYS   B 1 158 ? 44.656 -38.915 -14.446 1.00 33.78 ?  158 LYS   B HZ2  1 
ATOM   6549 H  HZ3  . LYS   B 1 158 ? 45.644 -38.458 -15.402 1.00 33.78 ?  158 LYS   B HZ3  1 
ATOM   6550 N  N    . ASN   B 1 159 ? 46.841 -39.790 -8.609  1.00 20.48 ?  159 ASN   B N    1 
ATOM   6551 C  CA   . ASN   B 1 159 ? 45.883 -40.770 -8.102  1.00 20.88 ?  159 ASN   B CA   1 
ATOM   6552 C  C    . ASN   B 1 159 ? 44.690 -40.098 -7.419  1.00 19.97 ?  159 ASN   B C    1 
ATOM   6553 O  O    . ASN   B 1 159 ? 43.558 -40.591 -7.516  1.00 20.28 ?  159 ASN   B O    1 
ATOM   6554 C  CB   . ASN   B 1 159 ? 46.589 -41.749 -7.167  1.00 22.64 ?  159 ASN   B CB   1 
ATOM   6555 C  CG   . ASN   B 1 159 ? 47.606 -42.607 -7.891  1.00 24.30 ?  159 ASN   B CG   1 
ATOM   6556 O  OD1  . ASN   B 1 159 ? 47.342 -43.121 -8.985  1.00 25.23 ?  159 ASN   B OD1  1 
ATOM   6557 N  ND2  . ASN   B 1 159 ? 48.777 -42.777 -7.282  1.00 24.98 ?  159 ASN   B ND2  1 
ATOM   6558 H  H    . ASN   B 1 159 ? 47.585 -39.747 -8.187  1.00 24.57 ?  159 ASN   B H    1 
ATOM   6559 H  HA   . ASN   B 1 159 ? 45.547 -41.281 -8.859  1.00 25.06 ?  159 ASN   B HA   1 
ATOM   6560 H  HB2  . ASN   B 1 159 ? 47.052 -41.251 -6.478  1.00 27.17 ?  159 ASN   B HB2  1 
ATOM   6561 H  HB3  . ASN   B 1 159 ? 45.930 -42.338 -6.775  1.00 27.17 ?  159 ASN   B HB3  1 
ATOM   6562 H  HD21 . ASN   B 1 159 ? 49.390 -43.257 -7.652  1.00 29.98 ?  159 ASN   B HD21 1 
ATOM   6563 H  HD22 . ASN   B 1 159 ? 48.920 -42.420 -6.513  1.00 29.98 ?  159 ASN   B HD22 1 
ATOM   6564 N  N    . LEU   B 1 160 ? 44.909 -38.971 -6.738  1.00 18.88 ?  160 LEU   B N    1 
ATOM   6565 C  CA   . LEU   B 1 160 ? 43.776 -38.237 -6.192  1.00 17.92 ?  160 LEU   B CA   1 
ATOM   6566 C  C    . LEU   B 1 160 ? 42.984 -37.570 -7.305  1.00 17.28 ?  160 LEU   B C    1 
ATOM   6567 O  O    . LEU   B 1 160 ? 41.747 -37.573 -7.280  1.00 16.98 ?  160 LEU   B O    1 
ATOM   6568 C  CB   . LEU   B 1 160 ? 44.242 -37.207 -5.166  1.00 17.68 ?  160 LEU   B CB   1 
ATOM   6569 C  CG   . LEU   B 1 160 ? 43.113 -36.312 -4.636  1.00 17.18 ?  160 LEU   B CG   1 
ATOM   6570 C  CD1  . LEU   B 1 160 ? 41.988 -37.151 -4.035  1.00 18.01 ?  160 LEU   B CD1  1 
ATOM   6571 C  CD2  . LEU   B 1 160 ? 43.653 -35.326 -3.620  1.00 17.28 ?  160 LEU   B CD2  1 
ATOM   6572 H  H    . LEU   B 1 160 ? 45.685 -38.625 -6.594  1.00 22.65 ?  160 LEU   B H    1 
ATOM   6573 H  HA   . LEU   B 1 160 ? 43.193 -38.866 -5.751  1.00 21.50 ?  160 LEU   B HA   1 
ATOM   6574 H  HB2  . LEU   B 1 160 ? 44.638 -37.680 -4.415  1.00 21.22 ?  160 LEU   B HB2  1 
ATOM   6575 H  HB3  . LEU   B 1 160 ? 44.914 -36.637 -5.580  1.00 21.22 ?  160 LEU   B HB3  1 
ATOM   6576 H  HG   . LEU   B 1 160 ? 42.745 -35.808 -5.375  1.00 20.61 ?  160 LEU   B HG   1 
ATOM   6577 H  HD11 . LEU   B 1 160 ? 41.362 -36.562 -3.592  1.00 21.62 ?  160 LEU   B HD11 1 
ATOM   6578 H  HD12 . LEU   B 1 160 ? 41.536 -37.642 -4.743  1.00 21.62 ?  160 LEU   B HD12 1 
ATOM   6579 H  HD13 . LEU   B 1 160 ? 42.365 -37.778 -3.393  1.00 21.62 ?  160 LEU   B HD13 1 
ATOM   6580 H  HD21 . LEU   B 1 160 ? 42.925 -34.759 -3.325  1.00 20.73 ?  160 LEU   B HD21 1 
ATOM   6581 H  HD22 . LEU   B 1 160 ? 44.021 -35.816 -2.870  1.00 20.73 ?  160 LEU   B HD22 1 
ATOM   6582 H  HD23 . LEU   B 1 160 ? 44.343 -34.790 -4.040  1.00 20.73 ?  160 LEU   B HD23 1 
ATOM   6583 N  N    . TYR   B 1 161 ? 43.681 -37.000 -8.292  1.00 17.22 ?  161 TYR   B N    1 
ATOM   6584 C  CA   . TYR   B 1 161 ? 43.007 -36.433 -9.456  1.00 17.11 ?  161 TYR   B CA   1 
ATOM   6585 C  C    . TYR   B 1 161 ? 42.060 -37.456 -10.073 1.00 17.03 ?  161 TYR   B C    1 
ATOM   6586 O  O    . TYR   B 1 161 ? 40.889 -37.160 -10.333 1.00 16.67 ?  161 TYR   B O    1 
ATOM   6587 C  CB   . TYR   B 1 161 ? 44.044 -35.961 -10.484 1.00 17.56 ?  161 TYR   B CB   1 
ATOM   6588 C  CG   . TYR   B 1 161 ? 43.456 -35.493 -11.796 1.00 18.11 ?  161 TYR   B CG   1 
ATOM   6589 C  CD1  . TYR   B 1 161 ? 43.066 -34.171 -11.962 1.00 18.04 ?  161 TYR   B CD1  1 
ATOM   6590 C  CD2  . TYR   B 1 161 ? 43.287 -36.365 -12.869 1.00 18.58 ?  161 TYR   B CD2  1 
ATOM   6591 C  CE1  . TYR   B 1 161 ? 42.529 -33.727 -13.144 1.00 19.17 ?  161 TYR   B CE1  1 
ATOM   6592 C  CE2  . TYR   B 1 161 ? 42.745 -35.927 -14.061 1.00 19.57 ?  161 TYR   B CE2  1 
ATOM   6593 C  CZ   . TYR   B 1 161 ? 42.371 -34.606 -14.193 1.00 19.68 ?  161 TYR   B CZ   1 
ATOM   6594 O  OH   . TYR   B 1 161 ? 41.826 -34.165 -15.373 1.00 21.64 ?  161 TYR   B OH   1 
ATOM   6595 H  H    . TYR   B 1 161 ? 44.535 -36.940 -8.321  1.00 20.67 ?  161 TYR   B H    1 
ATOM   6596 H  HA   . TYR   B 1 161 ? 42.482 -35.666 -9.186  1.00 20.53 ?  161 TYR   B HA   1 
ATOM   6597 H  HB2  . TYR   B 1 161 ? 44.543 -35.221 -10.109 1.00 21.07 ?  161 TYR   B HB2  1 
ATOM   6598 H  HB3  . TYR   B 1 161 ? 44.646 -36.696 -10.684 1.00 21.07 ?  161 TYR   B HB3  1 
ATOM   6599 H  HD1  . TYR   B 1 161 ? 43.170 -33.568 -11.262 1.00 21.65 ?  161 TYR   B HD1  1 
ATOM   6600 H  HD2  . TYR   B 1 161 ? 43.536 -37.256 -12.786 1.00 22.30 ?  161 TYR   B HD2  1 
ATOM   6601 H  HE1  . TYR   B 1 161 ? 42.274 -32.835 -13.237 1.00 23.00 ?  161 TYR   B HE1  1 
ATOM   6602 H  HE2  . TYR   B 1 161 ? 42.634 -36.520 -14.772 1.00 23.49 ?  161 TYR   B HE2  1 
ATOM   6603 H  HH   . TYR   B 1 161 ? 41.787 -34.796 -15.927 1.00 25.96 ?  161 TYR   B HH   1 
ATOM   6604 N  N    . ASP   B 1 162 ? 42.550 -38.681 -10.292 1.00 17.40 ?  162 ASP   B N    1 
ATOM   6605 C  CA   . ASP   B 1 162 ? 41.722 -39.714 -10.908 1.00 18.19 ?  162 ASP   B CA   1 
ATOM   6606 C  C    . ASP   B 1 162 ? 40.523 -40.055 -10.033 1.00 17.56 ?  162 ASP   B C    1 
ATOM   6607 O  O    . ASP   B 1 162 ? 39.420 -40.276 -10.544 1.00 17.79 ?  162 ASP   B O    1 
ATOM   6608 C  CB   . ASP   B 1 162 ? 42.556 -40.972 -11.172 1.00 19.53 ?  162 ASP   B CB   1 
ATOM   6609 C  CG   . ASP   B 1 162 ? 43.560 -40.797 -12.301 1.00 20.96 ?  162 ASP   B CG   1 
ATOM   6610 O  OD1  . ASP   B 1 162 ? 43.427 -39.852 -13.101 1.00 21.49 ?  162 ASP   B OD1  1 
ATOM   6611 O  OD2  . ASP   B 1 162 ? 44.473 -41.643 -12.404 1.00 22.49 -1 162 ASP   B OD2  1 
ATOM   6612 H  H    . ASP   B 1 162 ? 43.350 -38.929 -10.103 1.00 20.88 ?  162 ASP   B H    1 
ATOM   6613 H  HA   . ASP   B 1 162 ? 41.391 -39.392 -11.760 1.00 21.82 ?  162 ASP   B HA   1 
ATOM   6614 H  HB2  . ASP   B 1 162 ? 43.058 -41.198 -10.377 1.00 23.44 ?  162 ASP   B HB2  1 
ATOM   6615 H  HB3  . ASP   B 1 162 ? 41.964 -41.701 -11.414 1.00 23.44 ?  162 ASP   B HB3  1 
ATOM   6616 N  N    . LYS   B 1 163 ? 40.718 -40.125 -8.715  1.00 17.20 ?  163 LYS   B N    1 
ATOM   6617 C  CA   . LYS   B 1 163 ? 39.595 -40.400 -7.824  1.00 17.80 ?  163 LYS   B CA   1 
ATOM   6618 C  C    . LYS   B 1 163 ? 38.553 -39.289 -7.893  1.00 16.53 ?  163 LYS   B C    1 
ATOM   6619 O  O    . LYS   B 1 163 ? 37.342 -39.558 -7.896  1.00 17.05 ?  163 LYS   B O    1 
ATOM   6620 C  CB   . LYS   B 1 163 ? 40.088 -40.573 -6.390  1.00 20.89 ?  163 LYS   B CB   1 
ATOM   6621 C  CG   . LYS   B 1 163 ? 39.014 -41.100 -5.463  1.00 26.70 ?  163 LYS   B CG   1 
ATOM   6622 C  CD   . LYS   B 1 163 ? 39.490 -41.244 -4.030  1.00 31.67 ?  163 LYS   B CD   1 
ATOM   6623 C  CE   . LYS   B 1 163 ? 38.410 -41.904 -3.180  1.00 35.17 ?  163 LYS   B CE   1 
ATOM   6624 N  NZ   . LYS   B 1 163 ? 38.554 -41.600 -1.730  1.00 38.40 ?  163 LYS   B NZ   1 
ATOM   6625 H  H    . LYS   B 1 163 ? 41.478 -40.019 -8.325  1.00 20.64 ?  163 LYS   B H    1 
ATOM   6626 H  HA   . LYS   B 1 163 ? 39.174 -41.227 -8.100  1.00 21.36 ?  163 LYS   B HA   1 
ATOM   6627 H  HB2  . LYS   B 1 163 ? 40.827 -41.205 -6.384  1.00 25.06 ?  163 LYS   B HB2  1 
ATOM   6628 H  HB3  . LYS   B 1 163 ? 40.384 -39.716 -6.051  1.00 25.06 ?  163 LYS   B HB3  1 
ATOM   6629 H  HG2  . LYS   B 1 163 ? 38.263 -40.489 -5.468  1.00 32.04 ?  163 LYS   B HG2  1 
ATOM   6630 H  HG3  . LYS   B 1 163 ? 38.730 -41.976 -5.774  1.00 32.04 ?  163 LYS   B HG3  1 
ATOM   6631 H  HD2  . LYS   B 1 163 ? 40.284 -41.803 -4.007  1.00 38.00 ?  163 LYS   B HD2  1 
ATOM   6632 H  HD3  . LYS   B 1 163 ? 39.681 -40.368 -3.663  1.00 38.00 ?  163 LYS   B HD3  1 
ATOM   6633 H  HE2  . LYS   B 1 163 ? 37.539 -41.596 -3.474  1.00 42.21 ?  163 LYS   B HE2  1 
ATOM   6634 H  HE3  . LYS   B 1 163 ? 38.470 -42.865 -3.290  1.00 42.21 ?  163 LYS   B HE3  1 
ATOM   6635 H  HZ1  . LYS   B 1 163 ? 37.905 -42.001 -1.270  1.00 46.08 ?  163 LYS   B HZ1  1 
ATOM   6636 H  HZ2  . LYS   B 1 163 ? 39.340 -41.892 -1.435  1.00 46.08 ?  163 LYS   B HZ2  1 
ATOM   6637 H  HZ3  . LYS   B 1 163 ? 38.502 -40.722 -1.596  1.00 46.08 ?  163 LYS   B HZ3  1 
ATOM   6638 N  N    . LEU   B 1 164 ? 39.008 -38.036 -7.947  1.00 15.23 ?  164 LEU   B N    1 
ATOM   6639 C  CA   . LEU   B 1 164 ? 38.100 -36.897 -8.008  1.00 14.73 ?  164 LEU   B CA   1 
ATOM   6640 C  C    . LEU   B 1 164 ? 37.316 -36.882 -9.315  1.00 15.21 ?  164 LEU   B C    1 
ATOM   6641 O  O    . LEU   B 1 164 ? 36.091 -36.690 -9.316  1.00 16.36 ?  164 LEU   B O    1 
ATOM   6642 C  CB   . LEU   B 1 164 ? 38.903 -35.605 -7.848  1.00 14.15 ?  164 LEU   B CB   1 
ATOM   6643 C  CG   . LEU   B 1 164 ? 39.419 -35.316 -6.440  1.00 15.06 ?  164 LEU   B CG   1 
ATOM   6644 C  CD1  . LEU   B 1 164 ? 40.501 -34.256 -6.497  1.00 14.72 ?  164 LEU   B CD1  1 
ATOM   6645 C  CD2  . LEU   B 1 164 ? 38.301 -34.861 -5.523  1.00 16.79 ?  164 LEU   B CD2  1 
ATOM   6646 H  H    . LEU   B 1 164 ? 39.847 -37.821 -7.957  1.00 18.28 ?  164 LEU   B H    1 
ATOM   6647 H  HA   . LEU   B 1 164 ? 37.472 -36.955 -7.283  1.00 17.67 ?  164 LEU   B HA   1 
ATOM   6648 H  HB2  . LEU   B 1 164 ? 39.679 -35.647 -8.435  1.00 16.98 ?  164 LEU   B HB2  1 
ATOM   6649 H  HB3  . LEU   B 1 164 ? 38.344 -34.861 -8.110  1.00 16.98 ?  164 LEU   B HB3  1 
ATOM   6650 H  HG   . LEU   B 1 164 ? 39.811 -36.120 -6.068  1.00 18.07 ?  164 LEU   B HG   1 
ATOM   6651 H  HD11 . LEU   B 1 164 ? 40.812 -34.066 -5.596  1.00 17.66 ?  164 LEU   B HD11 1 
ATOM   6652 H  HD12 . LEU   B 1 164 ? 41.240 -34.579 -7.038  1.00 17.66 ?  164 LEU   B HD12 1 
ATOM   6653 H  HD13 . LEU   B 1 164 ? 40.135 -33.446 -6.892  1.00 17.66 ?  164 LEU   B HD13 1 
ATOM   6654 H  HD21 . LEU   B 1 164 ? 38.671 -34.644 -4.653  1.00 20.15 ?  164 LEU   B HD21 1 
ATOM   6655 H  HD22 . LEU   B 1 164 ? 37.876 -34.076 -5.905  1.00 20.15 ?  164 LEU   B HD22 1 
ATOM   6656 H  HD23 . LEU   B 1 164 ? 37.653 -35.578 -5.437  1.00 20.15 ?  164 LEU   B HD23 1 
ATOM   6657 N  N    . VAL   B 1 165 ? 38.009 -37.055 -10.442 1.00 16.62 ?  165 VAL   B N    1 
ATOM   6658 C  CA   . VAL   B 1 165 ? 37.351 -37.004 -11.742 1.00 18.09 ?  165 VAL   B CA   1 
ATOM   6659 C  C    . VAL   B 1 165 ? 36.424 -38.201 -11.912 1.00 19.99 ?  165 VAL   B C    1 
ATOM   6660 O  O    . VAL   B 1 165 ? 35.257 -38.058 -12.295 1.00 21.14 ?  165 VAL   B O    1 
ATOM   6661 C  CB   . VAL   B 1 165 ? 38.394 -36.927 -12.874 1.00 18.80 ?  165 VAL   B CB   1 
ATOM   6662 C  CG1  . VAL   B 1 165 ? 37.725 -37.048 -14.224 1.00 20.05 ?  165 VAL   B CG1  1 
ATOM   6663 C  CG2  . VAL   B 1 165 ? 39.189 -35.633 -12.788 1.00 18.45 ?  165 VAL   B CG2  1 
ATOM   6664 H  H    . VAL   B 1 165 ? 38.862 -37.202 -10.484 1.00 19.94 ?  165 VAL   B H    1 
ATOM   6665 H  HA   . VAL   B 1 165 ? 36.812 -36.204 -11.791 1.00 21.70 ?  165 VAL   B HA   1 
ATOM   6666 H  HB   . VAL   B 1 165 ? 39.021 -37.662 -12.782 1.00 22.56 ?  165 VAL   B HB   1 
ATOM   6667 H  HG11 . VAL   B 1 165 ? 38.342 -36.757 -14.912 1.00 24.06 ?  165 VAL   B HG11 1 
ATOM   6668 H  HG12 . VAL   B 1 165 ? 37.486 -37.978 -14.373 1.00 24.06 ?  165 VAL   B HG12 1 
ATOM   6669 H  HG13 . VAL   B 1 165 ? 36.930 -36.496 -14.234 1.00 24.06 ?  165 VAL   B HG13 1 
ATOM   6670 H  HG21 . VAL   B 1 165 ? 39.819 -35.595 -13.528 1.00 22.13 ?  165 VAL   B HG21 1 
ATOM   6671 H  HG22 . VAL   B 1 165 ? 38.578 -34.880 -12.840 1.00 22.13 ?  165 VAL   B HG22 1 
ATOM   6672 H  HG23 . VAL   B 1 165 ? 39.671 -35.609 -11.946 1.00 22.13 ?  165 VAL   B HG23 1 
ATOM   6673 N  N    . SER   B 1 166 ? 36.935 -39.402 -11.616 1.00 20.59 ?  166 SER   B N    1 
ATOM   6674 C  CA   . SER   B 1 166 ? 36.182 -40.617 -11.897 1.00 21.74 ?  166 SER   B CA   1 
ATOM   6675 C  C    . SER   B 1 166 ? 34.916 -40.698 -11.061 1.00 21.75 ?  166 SER   B C    1 
ATOM   6676 O  O    . SER   B 1 166 ? 33.948 -41.325 -11.490 1.00 23.44 ?  166 SER   B O    1 
ATOM   6677 C  CB   . SER   B 1 166 ? 37.046 -41.870 -11.695 1.00 22.56 ?  166 SER   B CB   1 
ATOM   6678 O  OG   . SER   B 1 166 ? 37.400 -42.064 -10.336 1.00 22.46 ?  166 SER   B OG   1 
ATOM   6679 H  H    . SER   B 1 166 ? 37.711 -39.535 -11.259 1.00 24.71 ?  166 SER   B H    1 
ATOM   6680 H  HA   . SER   B 1 166 ? 35.918 -40.603 -12.830 1.00 26.09 ?  166 SER   B HA   1 
ATOM   6681 H  HB2  . SER   B 1 166 ? 36.547 -42.644 -12.001 1.00 27.07 ?  166 SER   B HB2  1 
ATOM   6682 H  HB3  . SER   B 1 166 ? 37.859 -41.777 -12.217 1.00 27.07 ?  166 SER   B HB3  1 
ATOM   6683 H  HG   . SER   B 1 166 ? 37.831 -41.398 -10.059 1.00 26.95 ?  166 SER   B HG   1 
ATOM   6684 N  N    . SER   B 1 167 ? 34.895 -40.091 -9.876  1.00 20.28 ?  167 SER   B N    1 
ATOM   6685 C  CA   . SER   B 1 167 ? 33.736 -40.145 -8.992  1.00 19.84 ?  167 SER   B CA   1 
ATOM   6686 C  C    . SER   B 1 167 ? 32.822 -38.926 -9.091  1.00 19.47 ?  167 SER   B C    1 
ATOM   6687 O  O    . SER   B 1 167 ? 31.744 -38.931 -8.487  1.00 19.64 ?  167 SER   B O    1 
ATOM   6688 C  CB   . SER   B 1 167 ? 34.180 -40.322 -7.534  1.00 19.69 ?  167 SER   B CB   1 
ATOM   6689 O  OG   . SER   B 1 167 ? 34.855 -39.159 -7.071  1.00 19.57 ?  167 SER   B OG   1 
ATOM   6690 H  H    . SER   B 1 167 ? 35.551 -39.648 -9.560  1.00 24.34 ?  167 SER   B H    1 
ATOM   6691 H  HA   . SER   B 1 167 ? 33.205 -40.924 -9.231  1.00 23.80 ?  167 SER   B HA   1 
ATOM   6692 H  HB2  . SER   B 1 167 ? 33.396 -40.482 -6.985  1.00 23.63 ?  167 SER   B HB2  1 
ATOM   6693 H  HB3  . SER   B 1 167 ? 34.776 -41.094 -7.482  1.00 23.63 ?  167 SER   B HB3  1 
ATOM   6694 H  HG   . SER   B 1 167 ? 35.542 -39.031 -7.536  1.00 23.49 ?  167 SER   B HG   1 
ATOM   6695 N  N    . PHE   B 1 168 ? 33.203 -37.888 -9.838  1.00 19.10 ?  168 PHE   B N    1 
ATOM   6696 C  CA   . PHE   B 1 168 ? 32.368 -36.688 -9.899  1.00 18.34 ?  168 PHE   B CA   1 
ATOM   6697 C  C    . PHE   B 1 168 ? 31.054 -36.953 -10.630 1.00 16.08 ?  168 PHE   B C    1 
ATOM   6698 O  O    . PHE   B 1 168 ? 30.008 -36.367 -10.285 1.00 16.50 ?  168 PHE   B O    1 
ATOM   6699 C  CB   . PHE   B 1 168 ? 33.133 -35.548 -10.570 1.00 18.85 ?  168 PHE   B CB   1 
ATOM   6700 C  CG   . PHE   B 1 168 ? 32.327 -34.297 -10.704 1.00 18.86 ?  168 PHE   B CG   1 
ATOM   6701 C  CD1  . PHE   B 1 168 ? 31.987 -33.563 -9.578  1.00 20.03 ?  168 PHE   B CD1  1 
ATOM   6702 C  CD2  . PHE   B 1 168 ? 31.892 -33.862 -11.938 1.00 18.32 ?  168 PHE   B CD2  1 
ATOM   6703 C  CE1  . PHE   B 1 168 ? 31.224 -32.416 -9.678  1.00 20.32 ?  168 PHE   B CE1  1 
ATOM   6704 C  CE2  . PHE   B 1 168 ? 31.145 -32.697 -12.052 1.00 19.32 ?  168 PHE   B CE2  1 
ATOM   6705 C  CZ   . PHE   B 1 168 ? 30.803 -31.974 -10.916 1.00 19.67 ?  168 PHE   B CZ   1 
ATOM   6706 H  H    . PHE   B 1 168 ? 33.924 -37.854 -10.304 1.00 22.92 ?  168 PHE   B H    1 
ATOM   6707 H  HA   . PHE   B 1 168 ? 32.149 -36.412 -9.000  1.00 22.01 ?  168 PHE   B HA   1 
ATOM   6708 H  HB2  . PHE   B 1 168 ? 33.918 -35.340 -10.039 1.00 22.62 ?  168 PHE   B HB2  1 
ATOM   6709 H  HB3  . PHE   B 1 168 ? 33.400 -35.823 -11.461 1.00 22.62 ?  168 PHE   B HB3  1 
ATOM   6710 H  HD1  . PHE   B 1 168 ? 32.264 -33.858 -8.741  1.00 24.03 ?  168 PHE   B HD1  1 
ATOM   6711 H  HD2  . PHE   B 1 168 ? 32.120 -34.336 -12.702 1.00 21.98 ?  168 PHE   B HD2  1 
ATOM   6712 H  HE1  . PHE   B 1 168 ? 31.004 -31.936 -8.914  1.00 24.39 ?  168 PHE   B HE1  1 
ATOM   6713 H  HE2  . PHE   B 1 168 ? 30.857 -32.407 -12.889 1.00 23.19 ?  168 PHE   B HE2  1 
ATOM   6714 H  HZ   . PHE   B 1 168 ? 30.294 -31.200 -10.991 1.00 23.60 ?  168 PHE   B HZ   1 
ATOM   6715 N  N    . LEU   B 1 169 ? 31.093 -37.828 -11.634 1.00 16.32 ?  169 LEU   B N    1 
ATOM   6716 C  CA   . LEU   B 1 169 ? 29.925 -38.144 -12.446 1.00 18.72 ?  169 LEU   B CA   1 
ATOM   6717 C  C    . LEU   B 1 169 ? 29.931 -39.579 -12.955 1.00 21.34 ?  169 LEU   B C    1 
ATOM   6718 O  O    . LEU   B 1 169 ? 29.033 -39.989 -13.692 1.00 23.64 ?  169 LEU   B O    1 
ATOM   6719 C  CB   . LEU   B 1 169 ? 29.848 -37.201 -13.644 1.00 20.70 ?  169 LEU   B CB   1 
ATOM   6720 C  CG   . LEU   B 1 169 ? 28.590 -36.339 -13.746 1.00 23.63 ?  169 LEU   B CG   1 
ATOM   6721 C  CD1  . LEU   B 1 169 ? 28.545 -35.665 -15.099 1.00 24.67 ?  169 LEU   B CD1  1 
ATOM   6722 C  CD2  . LEU   B 1 169 ? 27.334 -37.158 -13.510 1.00 23.78 ?  169 LEU   B CD2  1 
ATOM   6723 O  OXT  . LEU   B 1 169 ? 30.839 -40.347 -12.653 1.00 22.31 -1 169 LEU   B OXT  1 
ATOM   6724 H  H    . LEU   B 1 169 ? 31.805 -38.254 -11.880 1.00 19.59 ?  169 LEU   B H    1 
ATOM   6725 H  HA   . LEU   B 1 169 ? 29.136 -38.020 -11.903 1.00 22.46 ?  169 LEU   B HA   1 
ATOM   6726 H  HB2  . LEU   B 1 169 ? 30.607 -36.598 -13.612 1.00 24.84 ?  169 LEU   B HB2  1 
ATOM   6727 H  HB3  . LEU   B 1 169 ? 29.894 -37.730 -14.458 1.00 24.84 ?  169 LEU   B HB3  1 
ATOM   6728 H  HG   . LEU   B 1 169 ? 28.627 -35.643 -13.070 1.00 28.35 ?  169 LEU   B HG   1 
ATOM   6729 H  HD11 . LEU   B 1 169 ? 27.759 -35.099 -15.143 1.00 29.60 ?  169 LEU   B HD11 1 
ATOM   6730 H  HD12 . LEU   B 1 169 ? 29.346 -35.131 -15.211 1.00 29.60 ?  169 LEU   B HD12 1 
ATOM   6731 H  HD13 . LEU   B 1 169 ? 28.502 -36.347 -15.787 1.00 29.60 ?  169 LEU   B HD13 1 
ATOM   6732 H  HD21 . LEU   B 1 169 ? 26.584 -36.722 -13.939 1.00 28.53 ?  169 LEU   B HD21 1 
ATOM   6733 H  HD22 . LEU   B 1 169 ? 27.462 -38.045 -13.887 1.00 28.53 ?  169 LEU   B HD22 1 
ATOM   6734 H  HD23 . LEU   B 1 169 ? 27.179 -37.226 -12.556 1.00 28.53 ?  169 LEU   B HD23 1 
HETATM 6735 C  C1   T TFA   C 2 .   ? 12.122 -1.332  1.467   0.30 11.50 ?  201 TFA   A C1   1 
HETATM 6736 C  C2   T TFA   C 2 .   ? 12.731 -1.750  0.098   0.30 14.04 ?  201 TFA   A C2   1 
HETATM 6737 O  O    T TFA   C 2 .   ? 12.850 -1.562  2.434   0.30 10.57 ?  201 TFA   A O    1 
HETATM 6738 F  F1   T TFA   C 2 .   ? 12.827 -3.091  0.031   0.30 15.64 ?  201 TFA   A F1   1 
HETATM 6739 F  F2   T TFA   C 2 .   ? 11.998 -1.376  -0.966  0.30 14.34 ?  201 TFA   A F2   1 
HETATM 6740 F  F3   T TFA   C 2 .   ? 13.955 -1.253  -0.116  0.30 15.44 ?  201 TFA   A F3   1 
HETATM 6741 O  OXT  T TFA   C 2 .   ? 11.006 -0.821  1.434   0.30 10.51 ?  201 TFA   A OXT  1 
HETATM 6742 N  N2   B A1A9V D 3 .   ? 14.862 -0.133  3.800   0.42 9.46  ?  202 A1A9V A N2   1 
HETATM 6743 C  C3   B A1A9V D 3 .   ? 13.825 0.096   -0.299  0.42 10.54 ?  202 A1A9V A C3   1 
HETATM 6744 C  C6   B A1A9V D 3 .   ? 10.090 2.238   -0.778  0.42 12.38 ?  202 A1A9V A C6   1 
HETATM 6745 C  C9   B A1A9V D 3 .   ? 15.084 0.991   3.075   0.42 9.43  ?  202 A1A9V A C9   1 
HETATM 6746 C  C12  B A1A9V D 3 .   ? 15.374 2.194   3.745   0.42 9.40  ?  202 A1A9V A C12  1 
HETATM 6747 C  C14  B A1A9V D 3 .   ? 15.850 4.232   4.543   0.42 9.63  ?  202 A1A9V A C14  1 
HETATM 6748 C  C1   B A1A9V D 3 .   ? 15.826 -1.114  0.655   0.42 10.67 ?  202 A1A9V A C1   1 
HETATM 6749 C  C10  B A1A9V D 3 .   ? 14.909 -0.080  5.131   0.42 10.31 ?  202 A1A9V A C10  1 
HETATM 6750 C  C11  B A1A9V D 3 .   ? 15.398 2.105   5.153   0.42 9.75  ?  202 A1A9V A C11  1 
HETATM 6751 C  C13  B A1A9V D 3 .   ? 15.671 3.544   3.375   0.42 9.34  ?  202 A1A9V A C13  1 
HETATM 6752 C  C2   B A1A9V D 3 .   ? 14.588 -0.266  0.990   0.42 9.64  ?  202 A1A9V A C2   1 
HETATM 6753 C  C4   B A1A9V D 3 .   ? 12.364 2.017   0.254   0.42 11.03 ?  202 A1A9V A C4   1 
HETATM 6754 C  C5   B A1A9V D 3 .   ? 10.920 2.486   0.481   0.42 11.97 ?  202 A1A9V A C5   1 
HETATM 6755 C  C7   B A1A9V D 3 .   ? 10.158 0.751   -1.140  0.42 12.85 ?  202 A1A9V A C7   1 
HETATM 6756 C  C8   B A1A9V D 3 .   ? 11.614 0.285   -1.311  0.42 12.27 ?  202 A1A9V A C8   1 
HETATM 6757 N  N1   B A1A9V D 3 .   ? 15.035 0.935   1.685   0.42 8.95  ?  202 A1A9V A N1   1 
HETATM 6758 N  N3   B A1A9V D 3 .   ? 15.167 0.986   5.886   0.42 10.31 ?  202 A1A9V A N3   1 
HETATM 6759 N  N4   B A1A9V D 3 .   ? 15.687 3.364   5.610   0.42 9.21  ?  202 A1A9V A N4   1 
HETATM 6760 N  N5   B A1A9V D 3 .   ? 12.436 0.577   -0.109  0.42 10.87 ?  202 A1A9V A N5   1 
HETATM 6761 O  O1   B A1A9V D 3 .   ? 15.420 -2.307  0.024   0.42 10.91 ?  202 A1A9V A O1   1 
HETATM 6762 H  H6   B A1A9V D 3 .   ? 14.371 0.860   -0.851  0.42 12.64 ?  202 A1A9V A H6   1 
HETATM 6763 H  H5   B A1A9V D 3 .   ? 13.825 -0.782  -0.942  0.42 12.64 ?  202 A1A9V A H5   1 
HETATM 6764 H  H11  B A1A9V D 3 .   ? 9.057  2.552   -0.622  0.42 14.86 ?  202 A1A9V A H11  1 
HETATM 6765 H  H12  B A1A9V D 3 .   ? 10.473 2.845   -1.600  0.42 14.86 ?  202 A1A9V A H12  1 
HETATM 6766 H  H20  B A1A9V D 3 .   ? 16.089 5.265   4.703   0.42 11.55 ?  202 A1A9V A H20  1 
HETATM 6767 H  H3   B A1A9V D 3 .   ? 16.529 -0.573  0.029   0.42 12.81 ?  202 A1A9V A H3   1 
HETATM 6768 H  H4   B A1A9V D 3 .   ? 16.351 -1.395  1.568   0.42 12.81 ?  202 A1A9V A H4   1 
HETATM 6769 H  H18  B A1A9V D 3 .   ? 14.711 -1.005  5.663   0.42 12.38 ?  202 A1A9V A H18  1 
HETATM 6770 H  H19  B A1A9V D 3 .   ? 15.724 3.921   2.367   0.42 11.20 ?  202 A1A9V A H19  1 
HETATM 6771 H  H1   B A1A9V D 3 .   ? 13.942 -0.872  1.629   0.42 11.56 ?  202 A1A9V A H1   1 
HETATM 6772 H  H7   B A1A9V D 3 .   ? 12.808 2.612   -0.543  0.42 13.24 ?  202 A1A9V A H7   1 
HETATM 6773 H  H8   B A1A9V D 3 .   ? 12.957 2.195   1.150   0.42 13.24 ?  202 A1A9V A H8   1 
HETATM 6774 H  H9   B A1A9V D 3 .   ? 10.480 1.947   1.322   0.42 14.37 ?  202 A1A9V A H9   1 
HETATM 6775 H  H10  B A1A9V D 3 .   ? 10.896 3.540   0.747   0.42 14.37 ?  202 A1A9V A H10  1 
HETATM 6776 H  H13  B A1A9V D 3 .   ? 9.670  0.164   -0.361  0.42 15.43 ?  202 A1A9V A H13  1 
HETATM 6777 H  H14  B A1A9V D 3 .   ? 9.590  0.564   -2.052  0.42 15.43 ?  202 A1A9V A H14  1 
HETATM 6778 H  H16  B A1A9V D 3 .   ? 12.040 0.785   -2.182  0.42 14.72 ?  202 A1A9V A H16  1 
HETATM 6779 H  H15  B A1A9V D 3 .   ? 11.639 -0.785  -1.526  0.42 14.72 ?  202 A1A9V A H15  1 
HETATM 6780 H  H17  B A1A9V D 3 .   ? 15.313 1.742   1.146   0.42 10.74 ?  202 A1A9V A H17  1 
HETATM 6781 H  H21  B A1A9V D 3 .   ? 15.777 3.642   6.577   0.42 11.05 ?  202 A1A9V A H21  1 
HETATM 6782 H  H2   B A1A9V D 3 .   ? 16.185 -2.752  -0.308  0.42 13.09 ?  202 A1A9V A H2   1 
HETATM 6783 H  H22  B A1A9V D 3 .   ? 12.044 0.053   0.663   0.42 13.04 ?  202 A1A9V A H22  1 
HETATM 6784 CL CL   B CL    E 4 .   ? 16.124 2.764   -1.161  0.42 12.61 ?  203 CL    A CL   1 
HETATM 6785 O  O    . HOH   F 5 .   ? 14.680 -4.534  20.488  1.00 45.73 ?  301 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 7.925  -12.622 -0.888  1.00 22.89 ?  302 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 18.557 -2.384  -16.518 1.00 43.36 ?  303 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 28.911 0.414   -9.753  1.00 21.34 ?  304 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 34.281 -1.850  12.503  1.00 38.19 ?  305 HOH   A O    1 
HETATM 6790 O  O    A HOH   F 5 .   ? 4.672  3.954   0.582   0.58 21.37 ?  306 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 17.087 -17.985 14.937  1.00 27.33 ?  307 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 11.705 -10.851 -10.098 1.00 44.41 ?  308 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 9.319  -10.081 19.431  1.00 40.67 ?  309 HOH   A O    1 
HETATM 6794 O  O    B HOH   F 5 .   ? 4.445  4.010   1.078   0.42 24.13 ?  310 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 11.921 0.425   14.655  1.00 31.65 ?  311 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 15.084 -12.201 18.585  1.00 40.05 ?  312 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 14.653 -13.884 16.620  1.00 26.32 ?  313 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 14.224 -4.506  -11.938 1.00 38.97 ?  314 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 42.448 10.549  5.167   1.00 20.76 ?  315 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? -0.815 -8.584  2.110   1.00 42.99 ?  316 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 30.930 6.214   -12.265 1.00 27.90 ?  317 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 15.015 4.109   17.444  1.00 40.08 ?  318 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 30.220 -13.330 -8.489  1.00 19.80 ?  319 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 22.703 12.519  1.616   1.00 13.84 ?  320 HOH   A O    1 
HETATM 6805 O  O    A HOH   F 5 .   ? 14.252 0.615   6.772   0.58 22.21 ?  321 HOH   A O    1 
HETATM 6806 O  O    B HOH   F 5 .   ? 15.301 6.907   6.972   0.42 18.70 ?  322 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 28.147 -6.246  19.637  1.00 41.69 ?  323 HOH   A O    1 
HETATM 6808 O  O    A HOH   F 5 .   ? 3.572  -9.412  9.717   0.58 26.24 ?  324 HOH   A O    1 
HETATM 6809 O  O    A HOH   F 5 .   ? 6.922  -8.109  11.833  0.58 15.19 ?  325 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 36.155 -5.101  -0.512  1.00 30.48 ?  326 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 13.283 -1.442  -6.736  1.00 17.37 ?  327 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 0.706  -4.398  0.007   1.00 31.44 ?  328 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 9.903  -21.375 5.702   1.00 18.15 ?  329 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 26.454 -19.310 -1.749  1.00 13.84 ?  330 HOH   A O    1 
HETATM 6815 O  O    B HOH   F 5 .   ? 11.259 -0.981  2.165   0.42 11.75 ?  331 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 19.914 -12.635 -8.738  1.00 25.85 ?  332 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 30.993 -18.078 7.823   1.00 19.29 ?  333 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 18.661 -19.323 13.549  1.00 33.95 ?  334 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 28.334 -0.172  -13.431 1.00 34.11 ?  335 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 38.250 10.153  7.136   1.00 36.22 ?  336 HOH   A O    1 
HETATM 6821 O  O    B HOH   F 5 .   ? 14.837 -2.882  3.340   0.42 11.76 ?  337 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 22.239 5.439   18.877  1.00 42.20 ?  338 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 21.321 -2.251  -2.491  1.00 15.36 ?  339 HOH   A O    1 
HETATM 6824 O  O    A HOH   F 5 .   ? 14.611 -3.619  3.076   0.58 14.58 ?  340 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 37.508 2.820   10.209  1.00 28.20 ?  341 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 8.873  -11.944 17.174  1.00 40.34 ?  342 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 20.623 -19.677 -5.044  1.00 24.35 ?  343 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 27.290 13.777  2.819   1.00 28.93 ?  344 HOH   A O    1 
HETATM 6829 O  O    B HOH   F 5 .   ? 12.022 -1.486  -4.290  0.42 20.05 ?  345 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 27.880 0.816   -7.192  1.00 14.08 ?  346 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 7.604  -6.128  -6.725  1.00 42.66 ?  347 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 13.539 -15.229 -7.429  1.00 24.35 ?  348 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 31.677 8.273   14.771  1.00 22.61 ?  349 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 14.356 -21.147 -4.226  1.00 28.30 ?  350 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 44.313 7.107   6.383   1.00 26.88 ?  351 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 38.536 4.989   6.955   1.00 15.61 ?  352 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 33.976 -1.072  -8.974  1.00 25.67 ?  353 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 18.894 -21.912 6.920   1.00 30.80 ?  354 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 39.715 -1.036  -5.188  1.00 22.56 ?  355 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 26.836 11.424  1.643   1.00 15.80 ?  356 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 14.579 -0.513  -12.178 1.00 29.09 ?  357 HOH   A O    1 
HETATM 6842 O  O    B HOH   F 5 .   ? 21.410 2.952   -0.045  0.42 12.26 ?  358 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 25.708 -0.834  -7.410  1.00 16.67 ?  359 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 42.524 4.271   5.361   1.00 30.30 ?  360 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 24.603 1.988   -7.106  1.00 23.87 ?  361 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 24.027 -2.084  -2.129  1.00 10.59 ?  362 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 37.306 11.979  4.944   1.00 29.81 ?  363 HOH   A O    1 
HETATM 6848 O  O    A HOH   F 5 .   ? -0.502 -3.049  3.076   0.58 30.93 ?  364 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 16.952 -19.203 4.922   1.00 14.52 ?  365 HOH   A O    1 
HETATM 6850 O  O    A HOH   F 5 .   ? 17.473 -1.683  0.418   0.58 18.54 ?  366 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 35.750 -12.634 6.855   1.00 15.47 ?  367 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 17.143 -17.728 -5.019  1.00 26.30 ?  368 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 22.137 -19.236 11.431  1.00 33.59 ?  369 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 31.059 -13.931 -2.439  1.00 13.43 ?  370 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 33.608 -7.139  4.317   1.00 16.56 ?  371 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 18.585 9.488   8.971   1.00 21.86 ?  372 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 30.769 3.125   8.244   1.00 11.80 ?  373 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 31.926 -9.308  -6.609  1.00 21.68 ?  374 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 37.234 -2.852  9.669   1.00 41.20 ?  375 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 8.088  -21.436 4.046   1.00 49.67 ?  376 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 14.095 -22.992 7.448   1.00 17.84 ?  377 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 21.204 10.303  14.949  1.00 34.96 ?  378 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 43.941 8.439   -3.082  1.00 27.26 ?  379 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 27.412 -10.544 14.051  1.00 17.11 ?  380 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 33.523 -16.950 8.098   1.00 19.15 ?  381 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 43.351 7.809   2.670   1.00 24.75 ?  382 HOH   A O    1 
HETATM 6867 O  O    B HOH   F 5 .   ? 10.971 2.128   11.940  0.42 18.40 ?  383 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 21.872 -21.877 8.476   1.00 28.93 ?  384 HOH   A O    1 
HETATM 6869 O  O    B HOH   F 5 .   ? 11.420 6.558   9.130   0.42 24.48 ?  385 HOH   A O    1 
HETATM 6870 O  O    T HOH   F 5 .   ? 15.384 -0.387  2.360   0.30 13.03 ?  386 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 15.163 -21.476 14.232  1.00 17.15 ?  387 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 15.439 11.848  7.823   1.00 40.39 ?  388 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 23.879 -15.741 -9.142  1.00 39.19 ?  389 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 31.802 -7.324  -9.832  1.00 21.59 ?  390 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 16.536 -22.021 1.004   1.00 27.61 ?  391 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 24.420 3.587   -1.815  1.00 14.24 ?  392 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 11.743 -10.611 16.965  1.00 25.31 ?  393 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 24.105 -7.665  14.389  1.00 15.99 ?  394 HOH   A O    1 
HETATM 6879 O  O    . HOH   F 5 .   ? 22.652 -11.858 21.770  1.00 53.16 ?  395 HOH   A O    1 
HETATM 6880 O  O    A HOH   F 5 .   ? 11.044 -0.345  1.907   0.28 15.10 ?  396 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 28.558 -10.644 -14.015 1.00 41.74 ?  397 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 21.714 -13.848 -8.153  1.00 46.24 ?  398 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 6.733  -3.092  12.807  1.00 27.96 ?  399 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 37.484 -1.979  5.789   1.00 25.72 ?  400 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 14.476 -24.647 11.595  1.00 37.95 ?  401 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 15.174 -8.082  -9.756  1.00 23.25 ?  402 HOH   A O    1 
HETATM 6887 O  O    B HOH   F 5 .   ? 7.910  4.028   1.426   0.42 18.26 ?  403 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 23.476 11.404  4.042   1.00 11.74 ?  404 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 27.258 2.407   18.667  1.00 27.72 ?  405 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 13.863 -4.804  17.297  1.00 26.24 ?  406 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 24.652 -17.495 12.685  1.00 23.90 ?  407 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 30.642 1.930   16.655  1.00 20.34 ?  408 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 32.746 -9.239  5.944   1.00 19.87 ?  409 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 23.895 -20.233 -1.331  1.00 15.93 ?  410 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 16.115 16.579  8.643   1.00 34.44 ?  411 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 30.013 -10.024 13.026  1.00 21.31 ?  412 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 20.534 -19.976 2.798   1.00 17.28 ?  413 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 38.082 -1.342  -1.945  1.00 18.88 ?  414 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 15.852 2.138   24.651  1.00 43.40 ?  415 HOH   A O    1 
HETATM 6900 O  O    B HOH   F 5 .   ? 22.682 5.690   -1.885  0.42 22.22 ?  416 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 30.270 -12.854 13.517  1.00 19.73 ?  417 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 27.461 -6.240  -14.053 1.00 36.07 ?  418 HOH   A O    1 
HETATM 6903 O  O    A HOH   F 5 .   ? 21.327 3.183   -0.380  0.58 10.93 ?  419 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 32.677 -4.329  -9.869  1.00 27.59 ?  420 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 32.520 -10.652 3.190   1.00 31.53 ?  421 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 26.942 4.160   -0.701  1.00 12.13 ?  422 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 40.871 -8.246  -6.825  1.00 36.96 ?  423 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 44.859 -0.674  3.037   1.00 40.29 ?  424 HOH   A O    1 
HETATM 6909 O  O    A HOH   F 5 .   ? 18.936 -0.642  -1.651  0.58 11.41 ?  425 HOH   A O    1 
HETATM 6910 O  O    A HOH   F 5 .   ? 15.777 -0.907  5.245   0.58 19.19 ?  426 HOH   A O    1 
HETATM 6911 O  O    A HOH   F 5 .   ? 6.441  -5.553  11.159  0.58 16.58 ?  427 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 35.021 -5.243  -3.076  1.00 17.68 ?  428 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 26.994 -3.031  19.377  1.00 37.98 ?  429 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 36.682 -4.974  5.402   1.00 23.94 ?  430 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 41.565 1.538   4.992   1.00 38.06 ?  431 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 19.513 -10.950 23.980  1.00 72.10 ?  432 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 10.402 -13.745 -1.704  1.00 16.23 ?  433 HOH   A O    1 
HETATM 6918 O  O    A HOH   F 5 .   ? 20.078 4.559   -7.579  0.58 17.83 ?  434 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 5.324  2.844   4.916   1.00 30.28 ?  435 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 10.319 -22.121 -1.216  1.00 51.76 ?  436 HOH   A O    1 
HETATM 6921 O  O    B HOH   F 5 .   ? 18.735 -1.215  -1.504  0.42 13.79 ?  437 HOH   A O    1 
HETATM 6922 O  O    A HOH   F 5 .   ? 24.071 3.978   -4.948  0.58 21.39 ?  438 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 15.965 6.861   2.963   1.00 24.02 ?  439 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 22.627 8.194   18.325  1.00 47.14 ?  440 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 16.164 -14.117 20.136  1.00 52.35 ?  441 HOH   A O    1 
HETATM 6926 O  O    A HOH   F 5 .   ? 11.012 1.604   12.721  0.58 18.77 ?  442 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 23.440 -7.942  17.095  1.00 20.92 ?  443 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 21.276 -9.112  21.323  1.00 50.54 ?  444 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 23.313 -20.901 1.364   1.00 17.72 ?  445 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? -1.498 -4.840  7.579   1.00 45.48 ?  446 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 18.338 -15.920 16.265  1.00 37.64 ?  447 HOH   A O    1 
HETATM 6932 O  O    A HOH   F 5 .   ? 16.237 2.975   -1.472  0.58 21.71 ?  448 HOH   A O    1 
HETATM 6933 O  O    A HOH   F 5 .   ? 18.841 2.061   -0.781  0.58 9.62  ?  449 HOH   A O    1 
HETATM 6934 O  O    A HOH   F 5 .   ? 23.181 7.534   -3.274  0.58 25.49 ?  450 HOH   A O    1 
HETATM 6935 O  O    A HOH   F 5 .   ? 9.357  -16.296 -1.985  0.58 33.47 ?  451 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 37.706 -8.816  -3.361  1.00 23.81 ?  452 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 34.393 -8.095  -0.510  1.00 28.38 ?  453 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 18.488 4.952   -15.128 1.00 47.90 ?  454 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 31.310 -12.776 0.048   1.00 19.32 ?  455 HOH   A O    1 
HETATM 6940 O  O    B HOH   F 5 .   ? 23.238 7.940   -3.311  0.42 30.40 ?  456 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 30.594 14.775  2.741   1.00 18.68 ?  457 HOH   A O    1 
HETATM 6942 O  O    A HOH   F 5 .   ? 14.004 -0.302  3.435   0.28 32.37 ?  458 HOH   A O    1 
HETATM 6943 O  O    B HOH   F 5 .   ? 12.781 -3.277  1.453   0.42 12.73 ?  459 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 21.473 -14.691 17.886  1.00 53.38 ?  460 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 27.687 6.978   -6.469  1.00 36.13 ?  461 HOH   A O    1 
HETATM 6946 O  O    . HOH   F 5 .   ? 20.588 -17.695 24.819  1.00 56.28 ?  462 HOH   A O    1 
HETATM 6947 O  O    . HOH   F 5 .   ? 29.779 -15.987 10.720  1.00 31.53 ?  463 HOH   A O    1 
HETATM 6948 O  O    B HOH   F 5 .   ? 18.851 1.546   -0.487  0.42 10.66 ?  464 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 29.754 -1.977  -12.800 1.00 49.01 ?  465 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 25.411 8.296   -4.888  1.00 26.49 ?  466 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 32.380 -15.885 10.878  1.00 29.41 ?  467 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? 24.779 5.669   20.723  1.00 49.19 ?  468 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 19.815 -17.270 -5.049  1.00 24.61 ?  469 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 23.161 -22.320 -3.358  1.00 34.78 ?  470 HOH   A O    1 
HETATM 6955 O  O    . HOH   F 5 .   ? 24.630 14.639  7.779   1.00 34.23 ?  471 HOH   A O    1 
HETATM 6956 O  O    . HOH   F 5 .   ? 39.600 -7.068  -3.524  1.00 45.18 ?  472 HOH   A O    1 
HETATM 6957 O  O    . HOH   F 5 .   ? 11.996 -13.407 16.380  1.00 56.06 ?  473 HOH   A O    1 
HETATM 6958 O  O    . HOH   F 5 .   ? 15.720 -21.434 3.724   1.00 21.90 ?  474 HOH   A O    1 
HETATM 6959 O  O    . HOH   F 5 .   ? 18.786 11.016  11.181  1.00 31.98 ?  475 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 27.439 -11.335 16.586  1.00 37.14 ?  476 HOH   A O    1 
HETATM 6961 O  O    . HOH   F 5 .   ? 23.478 13.733  5.474   1.00 17.08 ?  477 HOH   A O    1 
HETATM 6962 O  O    . HOH   F 5 .   ? 26.874 11.724  -1.338  1.00 32.31 ?  478 HOH   A O    1 
HETATM 6963 O  O    A HOH   F 5 .   ? 21.945 5.285   -5.870  0.58 31.88 ?  479 HOH   A O    1 
HETATM 6964 O  O    . HOH   F 5 .   ? 12.275 1.636   17.252  1.00 38.94 ?  480 HOH   A O    1 
HETATM 6965 O  O    . HOH   F 5 .   ? 25.809 10.821  -3.732  1.00 25.12 ?  481 HOH   A O    1 
HETATM 6966 O  O    . HOH   F 5 .   ? 18.076 -16.228 -8.852  1.00 39.92 ?  482 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 11.067 -15.099 -6.137  1.00 34.85 ?  483 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 15.669 -17.135 -6.988  1.00 29.95 ?  484 HOH   A O    1 
HETATM 6969 O  O    . HOH   F 5 .   ? 28.834 9.064   17.485  1.00 38.58 ?  485 HOH   A O    1 
HETATM 6970 O  O    . HOH   F 5 .   ? 23.136 11.865  -4.063  1.00 19.03 ?  486 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 13.950 -10.381 -10.879 1.00 32.17 ?  487 HOH   A O    1 
HETATM 6972 O  O    . HOH   F 5 .   ? 35.180 7.502   12.227  1.00 46.59 ?  488 HOH   A O    1 
HETATM 6973 O  O    . HOH   F 5 .   ? 16.786 -20.490 16.146  1.00 27.24 ?  489 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 17.396 -18.682 19.814  1.00 51.86 ?  490 HOH   A O    1 
HETATM 6975 O  O    . HOH   F 5 .   ? 40.935 -3.970  -0.362  1.00 37.50 ?  491 HOH   A O    1 
HETATM 6976 O  O    . HOH   F 5 .   ? 30.910 0.789   19.067  1.00 37.87 ?  492 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 31.453 -0.599  -10.573 1.00 27.84 ?  493 HOH   A O    1 
HETATM 6978 O  O    . HOH   F 5 .   ? 28.586 -4.716  -12.319 1.00 36.61 ?  494 HOH   A O    1 
HETATM 6979 O  O    . HOH   F 5 .   ? 41.723 9.318   -4.010  1.00 30.89 ?  495 HOH   A O    1 
HETATM 6980 O  O    . HOH   F 5 .   ? 23.227 -12.828 19.331  1.00 47.76 ?  496 HOH   A O    1 
HETATM 6981 O  O    . HOH   F 5 .   ? 28.646 -7.970  -15.258 1.00 46.84 ?  497 HOH   A O    1 
HETATM 6982 O  O    . HOH   F 5 .   ? 20.494 -15.904 -7.401  1.00 27.88 ?  498 HOH   A O    1 
HETATM 6983 O  O    . HOH   F 5 .   ? 39.132 2.461   7.430   1.00 33.98 ?  499 HOH   A O    1 
HETATM 6984 O  O    . HOH   F 5 .   ? 15.911 -6.997  -11.851 1.00 44.53 ?  500 HOH   A O    1 
HETATM 6985 O  O    . HOH   F 5 .   ? 44.511 10.452  -1.593  1.00 29.38 ?  501 HOH   A O    1 
HETATM 6986 O  O    . HOH   F 5 .   ? 13.875 -25.161 8.960   1.00 32.29 ?  502 HOH   A O    1 
HETATM 6987 O  O    . HOH   F 5 .   ? 18.438 -23.175 1.908   1.00 41.39 ?  503 HOH   A O    1 
HETATM 6988 O  O    . HOH   F 5 .   ? 40.542 -0.255  -7.812  1.00 34.04 ?  504 HOH   A O    1 
HETATM 6989 O  O    . HOH   F 5 .   ? 16.175 -23.339 5.736   1.00 27.83 ?  505 HOH   A O    1 
HETATM 6990 O  O    . HOH   F 5 .   ? 20.021 -22.283 4.199   1.00 27.77 ?  506 HOH   A O    1 
HETATM 6991 O  O    . HOH   F 5 .   ? 7.908  -3.262  -5.799  1.00 42.18 ?  507 HOH   A O    1 
HETATM 6992 O  O    . HOH   F 5 .   ? 30.686 5.823   -14.782 1.00 34.02 ?  508 HOH   A O    1 
HETATM 6993 O  O    . HOH   F 5 .   ? 30.738 -5.881  -11.882 1.00 45.63 ?  509 HOH   A O    1 
HETATM 6994 O  O    . HOH   F 5 .   ? 23.175 -23.748 1.659   1.00 30.61 ?  510 HOH   A O    1 
HETATM 6995 O  O    . HOH   F 5 .   ? 37.354 -6.622  7.587   1.00 24.44 ?  511 HOH   A O    1 
HETATM 6996 O  O    B HOH   F 5 .   ? 14.687 7.979   4.810   0.42 21.38 ?  512 HOH   A O    1 
HETATM 6997 O  O    . HOH   F 5 .   ? 39.470 0.014   6.592   1.00 30.72 ?  513 HOH   A O    1 
HETATM 6998 O  O    B HOH   F 5 .   ? 5.445  6.653   1.586   0.42 24.51 ?  514 HOH   A O    1 
HETATM 6999 O  O    . HOH   F 5 .   ? 38.001 13.954  6.714   1.00 46.42 ?  515 HOH   A O    1 
HETATM 7000 O  O    . HOH   F 5 .   ? 29.013 14.467  0.800   1.00 48.63 ?  516 HOH   A O    1 
HETATM 7001 O  O    . HOH   F 5 .   ? 21.973 -23.989 4.474   1.00 26.81 ?  517 HOH   A O    1 
HETATM 7002 O  O    . HOH   F 5 .   ? 36.440 -6.502  10.165  1.00 42.85 ?  518 HOH   A O    1 
HETATM 7003 O  O    T HOH   F 5 .   ? 11.899 -2.122  -3.678  0.30 12.84 ?  519 HOH   A O    1 
HETATM 7004 O  O    A HOH   F 5 .   ? 14.831 8.689   4.848   0.58 36.27 ?  520 HOH   A O    1 
HETATM 7005 O  O    . HOH   F 5 .   ? 17.158 -6.824  -14.336 1.00 45.88 ?  521 HOH   A O    1 
HETATM 7006 O  O    . HOH   F 5 .   ? 24.083 9.103   -7.243  1.00 37.19 ?  522 HOH   A O    1 
HETATM 7007 O  O    B HOH   F 5 .   ? 7.896  7.254   2.466   0.42 21.94 ?  523 HOH   A O    1 
HETATM 7008 O  O    . HOH   F 5 .   ? 16.386 -21.118 18.747  1.00 38.27 ?  524 HOH   A O    1 
HETATM 7009 O  O    . HOH   F 5 .   ? 15.785 -12.191 27.429  1.00 46.44 ?  525 HOH   A O    1 
HETATM 7010 O  O    . HOH   F 5 .   ? 14.768 -22.752 19.802  1.00 33.80 ?  526 HOH   A O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 29.808 -22.393 5.509   1.00 20.25 ?  201 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 41.700 -35.981 -17.171 1.00 31.50 ?  202 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 52.913 -13.464 -20.208 1.00 30.42 ?  203 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 38.002 -39.382 -0.163  1.00 38.98 ?  204 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 27.655 -29.138 -1.785  1.00 34.75 ?  205 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 29.881 -26.236 4.096   1.00 27.60 ?  206 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 59.164 -18.738 6.817   1.00 36.27 ?  207 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 41.355 -7.787  5.479   1.00 37.77 ?  208 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 48.086 -6.902  15.549  1.00 30.25 ?  209 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 57.694 -24.488 5.055   1.00 35.77 ?  210 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 54.486 -9.395  -8.762  1.00 18.29 ?  211 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 30.218 -41.012 -8.045  1.00 16.91 ?  212 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 55.409 -16.594 -14.324 1.00 35.01 ?  213 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 47.425 -7.396  -3.920  1.00 40.36 ?  214 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 56.333 -19.696 7.300   1.00 33.27 ?  215 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 27.851 -41.891 -15.072 1.00 35.85 ?  216 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 44.438 -7.187  2.034   1.00 35.11 ?  217 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 49.353 -22.740 -19.749 1.00 49.22 ?  218 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 58.236 -12.899 8.401   1.00 31.88 ?  219 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 50.194 -3.380  7.114   1.00 37.97 ?  220 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 56.660 -30.726 -7.714  1.00 32.39 ?  221 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 57.115 -26.834 -7.634  1.00 40.60 ?  222 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 30.897 -28.738 4.345   1.00 26.76 ?  223 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 37.056 -19.850 -18.056 1.00 36.98 ?  224 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 50.762 -6.123  0.149   1.00 26.70 ?  225 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 35.966 -43.289 -8.434  1.00 32.35 ?  226 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 41.484 -39.152 -14.817 1.00 23.81 ?  227 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 34.537 -36.370 -7.141  1.00 18.45 ?  228 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 34.901 -24.631 13.846  1.00 33.38 ?  229 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 57.386 -16.275 -12.201 1.00 18.53 ?  230 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 51.658 -6.484  4.383   1.00 19.75 ?  231 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 25.364 -25.889 -1.287  1.00 32.01 ?  232 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 40.634 -16.040 14.116  1.00 24.03 ?  233 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 44.956 -43.548 -10.507 1.00 28.39 ?  234 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 39.269 -10.846 6.127   1.00 24.06 ?  235 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 32.806 -43.801 -11.273 1.00 20.75 ?  236 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 41.383 -9.600  13.063  1.00 22.42 ?  237 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 28.401 -19.698 -13.097 1.00 24.49 ?  238 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 50.714 -12.975 -0.463  1.00 11.68 ?  239 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 44.484 -27.720 -0.653  1.00 22.24 ?  240 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 29.822 -34.206 -0.426  1.00 35.62 ?  241 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 45.145 -34.983 6.847   1.00 42.37 ?  242 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 48.536 -36.480 -15.484 1.00 44.10 ?  243 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 42.553 -25.350 2.666   1.00 15.09 ?  244 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 57.576 -24.371 -3.815  1.00 21.85 ?  245 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 42.621 -22.855 3.864   1.00 11.72 ?  246 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 35.108 -8.004  -2.955  1.00 17.76 ?  247 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 41.858 -23.503 9.320   1.00 17.62 ?  248 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 38.468 -11.067 -2.241  1.00 19.19 ?  249 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 46.412 -1.512  13.171  1.00 29.08 ?  250 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 34.226 -18.482 11.435  1.00 25.20 ?  251 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 43.059 -43.230 -8.182  1.00 28.74 ?  252 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 50.944 -39.912 -8.163  1.00 34.16 ?  253 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 43.153 -32.385 -17.026 1.00 23.94 ?  254 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 38.926 -11.921 12.325  1.00 33.22 ?  255 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 51.552 -13.853 11.026  1.00 25.32 ?  256 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 39.494 -11.093 0.343   1.00 16.07 ?  257 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 29.702 -25.223 -10.768 1.00 16.80 ?  258 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 48.003 -24.494 -17.766 1.00 31.65 ?  259 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 40.303 -12.754 -11.478 1.00 14.86 ?  260 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 30.832 -15.713 2.709   1.00 13.40 ?  261 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 56.112 -23.544 -14.701 1.00 28.37 ?  262 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 28.487 -30.940 -14.662 1.00 30.12 ?  263 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 47.990 -22.775 5.851   1.00 16.72 ?  264 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 31.783 -17.880 -14.448 1.00 29.84 ?  265 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 43.331 -15.775 -12.123 1.00 13.76 ?  266 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 58.180 -10.643 -4.074  1.00 19.47 ?  267 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 28.259 -34.359 -9.378  1.00 18.37 ?  268 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 49.294 -28.700 -6.861  1.00 15.08 ?  269 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 57.502 -9.230  1.450   1.00 19.77 ?  270 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 59.791 -15.362 8.123   1.00 31.00 ?  271 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 27.137 -31.831 -9.936  1.00 20.42 ?  272 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 42.311 -9.917  9.368   1.00 21.29 ?  273 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 46.847 -29.549 9.823   1.00 31.80 ?  274 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 46.614 -31.238 -4.750  1.00 21.38 ?  275 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 27.956 -22.893 -7.953  1.00 17.41 ?  276 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 42.354 -34.699 3.792   1.00 28.12 ?  277 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 34.931 -33.385 -19.099 1.00 36.89 ?  278 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 56.960 -8.641  8.431   1.00 19.19 ?  279 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 49.731 -0.461  10.159  1.00 30.04 ?  280 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 30.543 -42.219 -10.529 1.00 29.29 ?  281 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 48.386 -25.031 3.131   1.00 13.36 ?  282 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 34.441 -12.767 2.666   1.00 22.30 ?  283 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 41.171 -5.478  11.534  1.00 45.00 ?  284 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 51.677 -5.952  -7.925  1.00 48.34 ?  285 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 52.570 -10.361 12.979  1.00 22.69 ?  286 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 47.067 -33.963 -4.591  1.00 17.56 ?  287 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 42.839 -20.288 -20.704 1.00 34.95 ?  288 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 49.966 -24.628 5.797   1.00 32.41 ?  289 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 27.566 -26.709 -15.607 1.00 33.36 ?  290 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 57.107 -12.052 12.338  1.00 36.34 ?  291 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 33.484 -15.316 -13.901 1.00 21.72 ?  292 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 48.689 -20.021 5.962   1.00 13.42 ?  293 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 51.202 -37.592 -9.543  1.00 25.51 ?  294 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 36.809 -12.760 -1.468  1.00 26.34 ?  295 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 42.275 -9.955  -14.879 1.00 37.69 ?  296 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 45.304 -33.341 -15.920 1.00 23.83 ?  297 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 45.890 -40.375 -3.519  1.00 29.77 ?  298 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 25.932 -21.467 -3.448  1.00 16.24 ?  299 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 44.614 -27.441 2.044   1.00 15.16 ?  300 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 42.669 -12.285 -18.472 1.00 29.87 ?  301 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 43.958 -29.344 -4.640  1.00 25.46 ?  302 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 37.480 -18.078 13.137  1.00 29.46 ?  303 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 40.223 -10.839 -9.503  1.00 16.78 ?  304 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 35.030 -33.549 4.554   1.00 27.12 ?  305 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 52.602 -35.637 -8.588  1.00 30.77 ?  306 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 53.025 -16.028 -12.728 1.00 27.23 ?  307 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 51.340 -32.998 -10.724 1.00 40.05 ?  308 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 52.506 -29.227 -12.994 1.00 25.17 ?  309 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 53.478 -30.193 4.528   1.00 18.93 ?  310 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 32.777 -34.574 -5.842  1.00 17.02 ?  311 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 57.640 -22.071 3.164   1.00 27.53 ?  312 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 62.692 -13.576 4.765   1.00 27.61 ?  313 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 37.842 -10.249 -10.722 1.00 16.78 ?  314 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 37.281 -35.648 7.292   1.00 34.24 ?  315 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 53.630 -12.589 -22.161 1.00 33.46 ?  316 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 41.737 -8.056  1.371   1.00 24.21 ?  317 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 43.449 -15.404 18.162  1.00 28.81 ?  318 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 43.206 -21.414 10.703  1.00 16.15 ?  319 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 37.135 -30.563 -20.960 1.00 31.39 ?  320 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 38.319 -12.686 7.976   1.00 18.26 ?  321 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 26.324 -21.024 -6.199  1.00 15.98 ?  322 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 44.172 -1.768  7.625   1.00 46.10 ?  323 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 59.885 -17.153 -10.486 1.00 32.88 ?  324 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 44.612 -24.595 9.584   1.00 19.98 ?  325 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 36.713 -12.409 4.300   1.00 17.67 ?  326 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 48.066 -32.640 -16.608 1.00 42.77 ?  327 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 62.875 -20.126 -0.755  1.00 37.35 ?  328 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 43.124 -34.611 0.131   1.00 20.77 ?  329 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 47.184 -24.480 8.223   1.00 26.08 ?  330 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 38.358 -9.364  -13.245 1.00 26.89 ?  331 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 41.156 -24.457 15.880  1.00 44.87 ?  332 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 45.686 -36.314 -16.038 1.00 34.54 ?  333 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 33.614 -31.179 11.095  1.00 35.22 ?  334 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 27.814 -14.751 -9.485  1.00 35.57 ?  335 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 42.861 -43.476 -14.310 1.00 42.67 ?  336 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 48.573 -11.922 -13.864 1.00 27.63 ?  337 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 47.458 -27.420 2.058   1.00 14.78 ?  338 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 37.019 -15.149 -16.508 1.00 41.16 ?  339 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 39.475 -23.593 -20.286 1.00 36.59 ?  340 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 46.818 -19.894 12.268  1.00 29.40 ?  341 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 33.008 -14.673 1.089   1.00 18.47 ?  342 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 38.408 -12.280 -16.234 1.00 41.67 ?  343 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 28.844 -42.949 -12.307 1.00 34.75 ?  344 HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 37.040 -45.253 -9.684  1.00 35.65 ?  345 HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 38.593 -22.337 15.032  1.00 39.80 ?  346 HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 39.765 -44.262 -11.133 1.00 39.85 ?  347 HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 40.415 -43.493 -9.025  1.00 26.64 ?  348 HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 62.543 -20.095 -4.778  1.00 45.90 ?  349 HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 33.738 -9.373  -8.812  1.00 31.17 ?  350 HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 27.757 -26.585 -0.552  1.00 30.41 ?  351 HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 34.549 -10.295 7.615   1.00 24.75 ?  352 HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 55.648 -8.249  10.782  1.00 25.88 ?  353 HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 44.140 -37.338 -17.731 1.00 34.99 ?  354 HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 56.557 -7.266  3.079   1.00 27.04 ?  355 HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 23.178 -23.600 6.846   1.00 35.04 ?  356 HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 36.086 -8.544  -9.716  1.00 35.28 ?  357 HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 43.121 -12.694 -21.177 1.00 40.51 ?  358 HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 34.070 -7.737  11.427  1.00 39.96 ?  359 HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 56.892 -21.517 -16.334 1.00 38.93 ?  360 HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 61.475 -19.937 1.710   1.00 35.28 ?  361 HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 40.237 -8.784  9.860   1.00 39.52 ?  362 HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 27.161 -25.966 -11.371 1.00 34.10 ?  363 HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 54.197 -5.767  2.996   1.00 35.10 ?  364 HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 32.537 -23.592 14.097  1.00 39.28 ?  365 HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 58.888 -10.479 9.171   1.00 41.36 ?  366 HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 48.341 -26.480 8.891   1.00 39.91 ?  367 HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 40.076 -11.352 -13.954 1.00 30.63 ?  368 HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 41.817 -10.079 -17.446 1.00 54.89 ?  369 HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 36.131 -8.609  8.974   1.00 36.20 ?  370 HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 39.848 -6.995  7.842   1.00 39.89 ?  371 HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 56.037 -7.817  -0.606  1.00 33.05 ?  372 HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 52.054 -12.879 13.344  1.00 33.46 ?  373 HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 62.991 -12.360 6.923   1.00 37.90 ?  374 HOH   B O    1 
HETATM 7185 O  O    . HOH   G 5 .   ? 41.843 -6.747  -4.859  1.00 45.28 ?  375 HOH   B O    1 
HETATM 7186 O  O    . HOH   G 5 .   ? 38.047 -10.505 10.024  1.00 28.48 ?  376 HOH   B O    1 
HETATM 7187 O  O    . HOH   G 5 .   ? 36.492 -22.793 13.285  1.00 29.95 ?  377 HOH   B O    1 
HETATM 7188 O  O    . HOH   G 5 .   ? 44.030 -5.608  -3.504  1.00 43.18 ?  378 HOH   B O    1 
HETATM 7189 O  O    . HOH   G 5 .   ? 40.129 -7.639  3.175   1.00 38.70 ?  379 HOH   B O    1 
HETATM 7190 O  O    . HOH   G 5 .   ? 42.608 -17.055 -23.164 1.00 44.40 ?  380 HOH   B O    1 
HETATM 7191 O  O    . HOH   G 5 .   ? 52.839 -29.868 7.199   1.00 22.92 ?  381 HOH   B O    1 
HETATM 7192 O  O    . HOH   G 5 .   ? 39.641 -13.979 15.666  1.00 46.75 ?  382 HOH   B O    1 
HETATM 7193 O  O    . HOH   G 5 .   ? 25.814 -18.876 -11.829 1.00 39.13 ?  383 HOH   B O    1 
HETATM 7194 O  O    . HOH   G 5 .   ? 60.495 -22.292 2.880   1.00 45.63 ?  384 HOH   B O    1 
HETATM 7195 O  O    . HOH   G 5 .   ? 46.771 -5.360  2.904   1.00 39.10 ?  385 HOH   B O    1 
HETATM 7196 O  O    . HOH   G 5 .   ? 40.971 -9.763  15.818  1.00 47.99 ?  386 HOH   B O    1 
HETATM 7197 O  O    . HOH   G 5 .   ? 35.317 -20.302 13.302  1.00 31.48 ?  387 HOH   B O    1 
HETATM 7198 O  O    . HOH   G 5 .   ? 35.427 -33.704 7.375   1.00 38.88 ?  388 HOH   B O    1 
HETATM 7199 O  O    . HOH   G 5 .   ? 23.943 -20.936 -7.631  1.00 27.89 ?  389 HOH   B O    1 
HETATM 7200 O  O    . HOH   G 5 .   ? 40.722 -6.607  -0.820  1.00 24.67 ?  390 HOH   B O    1 
HETATM 7201 O  O    . HOH   G 5 .   ? 44.108 -31.737 -3.778  1.00 36.96 ?  391 HOH   B O    1 
HETATM 7202 O  O    . HOH   G 5 .   ? 27.919 -27.053 2.260   1.00 29.45 ?  392 HOH   B O    1 
HETATM 7203 O  O    . HOH   G 5 .   ? 26.595 -27.952 -13.444 1.00 34.57 ?  393 HOH   B O    1 
HETATM 7204 O  O    . HOH   G 5 .   ? 34.343 -33.430 9.668   1.00 35.86 ?  394 HOH   B O    1 
HETATM 7205 O  O    . HOH   G 5 .   ? 24.590 -20.605 -10.492 1.00 38.35 ?  395 HOH   B O    1 
HETATM 7206 O  O    . HOH   G 5 .   ? 50.617 -30.800 8.712   1.00 27.84 ?  396 HOH   B O    1 
HETATM 7207 O  O    . HOH   G 5 .   ? 26.851 -30.668 -12.612 1.00 27.24 ?  397 HOH   B O    1 
HETATM 7208 O  O    . HOH   G 5 .   ? 57.700 -6.578  -2.340  1.00 34.36 ?  398 HOH   B O    1 
HETATM 7209 O  O    . HOH   G 5 .   ? 45.723 -20.110 15.251  1.00 47.48 ?  399 HOH   B O    1 
HETATM 7210 O  O    . HOH   G 5 .   ? 40.870 -11.771 -22.270 1.00 39.66 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . VAL   A 3   ? 0.6921 0.7136 0.8060 -0.0057 -0.0465 0.0986  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6865 0.7080 0.7930 -0.0069 -0.0467 0.0981  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6581 0.6838 0.7341 -0.0157 -0.0441 0.0996  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6640 0.6889 0.7492 -0.0149 -0.0459 0.1022  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.7040 0.7226 0.8232 -0.0015 -0.0460 0.0970  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.7102 0.7283 0.8336 0.0000  -0.0452 0.0975  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.7092 0.7261 0.8346 0.0007  -0.0452 0.0968  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.6192 0.6501 0.6504 -0.0257 -0.0366 0.0995  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5768 0.6128 0.5551 -0.0380 -0.0288 0.0966  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5174 0.5657 0.4959 -0.0517 -0.0130 0.0597  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5216 0.5685 0.4958 -0.0521 -0.0172 0.0630  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5908 0.6202 0.5129 -0.0382 -0.0378 0.1298  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.6017 0.6250 0.4716 -0.0398 -0.0445 0.1601  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.6062 0.6253 0.4519 -0.0400 -0.0474 0.1732  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.6046 0.6271 0.4586 -0.0403 -0.0466 0.1724  4   ASN   A ND2 
30   N  N   A SER   A 5   ? 0.4811 0.5388 0.4609 -0.0627 -0.0014 0.0404  5   SER   A N   
31   N  N   B SER   A 5   ? 0.4865 0.5376 0.4640 -0.0561 -0.0055 0.0402  5   SER   A N   
32   C  CA  A SER   A 5   ? 0.4418 0.5096 0.4254 -0.0722 0.0116  0.0231  5   SER   A CA  
33   C  CA  B SER   A 5   ? 0.4529 0.5074 0.4308 -0.0596 0.0034  0.0224  5   SER   A CA  
34   C  C   A SER   A 5   ? 0.3962 0.4706 0.3707 -0.0808 0.0266  0.0147  5   SER   A C   
35   C  C   B SER   A 5   ? 0.4130 0.4692 0.3802 -0.0625 0.0144  0.0131  5   SER   A C   
36   O  O   A SER   A 5   ? 0.4015 0.4766 0.3732 -0.0746 0.0274  0.0056  5   SER   A O   
37   O  O   B SER   A 5   ? 0.4157 0.4730 0.3805 -0.0594 0.0136  0.0065  5   SER   A O   
38   C  CB  A SER   A 5   ? 0.4476 0.5167 0.4399 -0.0725 0.0127  0.0160  5   SER   A CB  
39   C  CB  B SER   A 5   ? 0.4581 0.5131 0.4437 -0.0600 0.0037  0.0156  5   SER   A CB  
40   O  OG  A SER   A 5   ? 0.4515 0.5207 0.4480 -0.0720 0.0143  0.0122  5   SER   A OG  
41   O  OG  B SER   A 5   ? 0.4613 0.5164 0.4501 -0.0600 0.0041  0.0117  5   SER   A OG  
52   N  N   A PHE   A 6   ? 0.3419 0.4238 0.3056 -0.0960 0.0432  0.0212  6   PHE   A N   
53   N  N   B PHE   A 6   ? 0.3677 0.4259 0.3257 -0.0688 0.0282  0.0150  6   PHE   A N   
54   C  CA  A PHE   A 6   ? 0.2914 0.3765 0.2443 -0.1067 0.0515  0.0321  6   PHE   A CA  
55   C  CA  B PHE   A 6   ? 0.3231 0.3815 0.2774 -0.0742 0.0392  0.0204  6   PHE   A CA  
56   C  C   A PHE   A 6   ? 0.2807 0.3697 0.2373 -0.1094 0.0673  0.0320  6   PHE   A C   
57   C  C   B PHE   A 6   ? 0.3104 0.3715 0.2797 -0.0747 0.0580  0.0194  6   PHE   A C   
58   O  O   A PHE   A 6   ? 0.2845 0.3750 0.2722 -0.1123 0.0773  0.0370  6   PHE   A O   
59   O  O   B PHE   A 6   ? 0.3112 0.3747 0.2952 -0.0775 0.0640  0.0223  6   PHE   A O   
60   C  CB  A PHE   A 6   ? 0.2620 0.3400 0.1979 -0.1045 0.0377  0.0407  6   PHE   A CB  
61   C  CB  B PHE   A 6   ? 0.2976 0.3499 0.2344 -0.0729 0.0247  0.0237  6   PHE   A CB  
62   C  CG  A PHE   A 6   ? 0.2372 0.3115 0.1679 -0.0970 0.0267  0.0458  6   PHE   A CG  
63   C  CG  B PHE   A 6   ? 0.2734 0.3234 0.2044 -0.0700 0.0144  0.0275  6   PHE   A CG  
64   C  CD1 A PHE   A 6   ? 0.2229 0.2998 0.1642 -0.0868 0.0207  0.0443  6   PHE   A CD1 
65   C  CD1 B PHE   A 6   ? 0.2618 0.3119 0.1946 -0.0649 0.0099  0.0276  6   PHE   A CD1 
66   C  CD2 A PHE   A 6   ? 0.2412 0.3046 0.1931 -0.0846 0.0213  0.0470  6   PHE   A CD2 
67   C  CD2 B PHE   A 6   ? 0.2711 0.3146 0.2085 -0.0624 0.0099  0.0293  6   PHE   A CD2 
68   C  CE1 A PHE   A 6   ? 0.2135 0.2909 0.1732 -0.0868 0.0196  0.0462  6   PHE   A CE1 
69   C  CE1 B PHE   A 6   ? 0.2551 0.3044 0.1958 -0.0636 0.0072  0.0276  6   PHE   A CE1 
70   C  CE2 A PHE   A 6   ? 0.2340 0.2990 0.2048 -0.0802 0.0173  0.0387  6   PHE   A CE2 
71   C  CE2 B PHE   A 6   ? 0.2645 0.3083 0.2109 -0.0598 0.0070  0.0258  6   PHE   A CE2 
72   C  CZ  A PHE   A 6   ? 0.2190 0.2911 0.1847 -0.0860 0.0188  0.0398  6   PHE   A CZ  
73   C  CZ  B PHE   A 6   ? 0.2567 0.3037 0.1987 -0.0619 0.0052  0.0240  6   PHE   A CZ  
92   N  N   A SER   A 7   ? 0.2655 0.3542 0.1976 -0.1080 0.0694  0.0268  7   SER   A N   
93   N  N   B SER   A 7   ? 0.2976 0.3571 0.2713 -0.0712 0.0625  0.0140  7   SER   A N   
94   C  CA  A SER   A 7   ? 0.2607 0.3428 0.1957 -0.0954 0.0562  0.0020  7   SER   A CA  
95   C  CA  B SER   A 7   ? 0.2899 0.3461 0.2761 -0.0607 0.0601  0.0043  7   SER   A CA  
96   C  C   A SER   A 7   ? 0.2435 0.3107 0.1635 -0.0928 0.0593  -0.0030 7   SER   A C   
97   C  C   B SER   A 7   ? 0.2736 0.3221 0.2433 -0.0591 0.0630  0.0035  7   SER   A C   
98   O  O   A SER   A 7   ? 0.2513 0.3024 0.1605 -0.1039 0.0618  -0.0066 7   SER   A O   
99   O  O   B SER   A 7   ? 0.2782 0.3220 0.2387 -0.0603 0.0583  -0.0007 7   SER   A O   
100  C  CB  A SER   A 7   ? 0.2768 0.3580 0.2228 -0.0825 0.0453  -0.0003 7   SER   A CB  
101  C  CB  B SER   A 7   ? 0.2976 0.3555 0.3081 -0.0520 0.0588  0.0038  7   SER   A CB  
102  O  OG  A SER   A 7   ? 0.2912 0.3671 0.2382 -0.0742 0.0430  -0.0003 7   SER   A OG  
103  O  OG  B SER   A 7   ? 0.3036 0.3600 0.3324 -0.0465 0.0586  0.0074  7   SER   A OG  
114  N  N   A GLY   A 8   ? 0.2198 0.2826 0.1682 -0.0815 0.0517  -0.0029 8   GLY   A N   
115  N  N   B GLY   A 8   ? 0.2531 0.2973 0.2196 -0.0575 0.0661  0.0029  8   GLY   A N   
116  C  CA  A GLY   A 8   ? 0.1999 0.2516 0.1702 -0.0610 0.0431  0.0043  8   GLY   A CA  
117  C  CA  B GLY   A 8   ? 0.2338 0.2692 0.2005 -0.0505 0.0587  0.0033  8   GLY   A CA  
118  C  C   A GLY   A 8   ? 0.1752 0.2275 0.1662 -0.0378 0.0355  0.0075  8   GLY   A C   
119  C  C   B GLY   A 8   ? 0.2126 0.2449 0.1835 -0.0446 0.0528  0.0015  8   GLY   A C   
120  O  O   A GLY   A 8   ? 0.1789 0.2250 0.1727 -0.0193 0.0350  -0.0039 8   GLY   A O   
121  O  O   B GLY   A 8   ? 0.2181 0.2427 0.1877 -0.0401 0.0552  -0.0044 8   GLY   A O   
128  N  N   A TYR   A 9   ? 0.1535 0.2138 0.1590 -0.0271 0.0241  0.0099  9   TYR   A N   
129  N  N   B TYR   A 9   ? 0.1878 0.2260 0.1769 -0.0342 0.0329  0.0083  9   TYR   A N   
130  C  CA  A TYR   A 9   ? 0.1366 0.1977 0.1497 -0.0336 0.0146  0.0105  9   TYR   A CA  
131  C  CA  B TYR   A 9   ? 0.1714 0.2041 0.1680 -0.0287 0.0243  0.0157  9   TYR   A CA  
132  C  C   A TYR   A 9   ? 0.1314 0.1811 0.1427 -0.0251 0.0227  0.0327  9   TYR   A C   
133  C  C   B TYR   A 9   ? 0.1585 0.1834 0.1685 -0.0204 0.0186  0.0223  9   TYR   A C   
134  O  O   A TYR   A 9   ? 0.1454 0.1951 0.1660 -0.0246 0.0107  0.0375  9   TYR   A O   
135  O  O   B TYR   A 9   ? 0.1589 0.2004 0.1909 -0.0248 0.0005  0.0314  9   TYR   A O   
136  C  CB  A TYR   A 9   ? 0.1368 0.2051 0.1574 -0.0328 0.0121  -0.0015 9   TYR   A CB  
137  C  CB  B TYR   A 9   ? 0.1644 0.2051 0.1705 -0.0287 0.0223  0.0131  9   TYR   A CB  
138  C  CG  A TYR   A 9   ? 0.1426 0.2025 0.1628 -0.0203 0.0207  -0.0094 9   TYR   A CG  
139  C  CG  B TYR   A 9   ? 0.1562 0.2028 0.1513 -0.0234 0.0204  0.0091  9   TYR   A CG  
140  C  CD1 A TYR   A 9   ? 0.1507 0.1989 0.1722 -0.0233 0.0341  -0.0179 9   TYR   A CD1 
141  C  CD1 B TYR   A 9   ? 0.1586 0.2018 0.1585 -0.0269 0.0283  0.0079  9   TYR   A CD1 
142  C  CD2 A TYR   A 9   ? 0.1463 0.1982 0.1741 -0.0116 0.0196  0.0007  9   TYR   A CD2 
143  C  CD2 B TYR   A 9   ? 0.1506 0.1959 0.1450 -0.0182 0.0141  0.0142  9   TYR   A CD2 
144  C  CE1 A TYR   A 9   ? 0.1578 0.1969 0.1869 -0.0194 0.0302  -0.0260 9   TYR   A CE1 
145  C  CE1 B TYR   A 9   ? 0.1549 0.1960 0.1621 -0.0249 0.0246  0.0040  9   TYR   A CE1 
146  C  CE2 A TYR   A 9   ? 0.1452 0.1967 0.1785 -0.0109 0.0211  -0.0021 9   TYR   A CE2 
147  C  CE2 B TYR   A 9   ? 0.1412 0.1935 0.1407 -0.0151 0.0222  0.0134  9   TYR   A CE2 
148  C  CZ  A TYR   A 9   ? 0.1548 0.1975 0.1959 -0.0217 0.0373  -0.0130 9   TYR   A CZ  
149  C  CZ  B TYR   A 9   ? 0.1408 0.1874 0.1560 -0.0151 0.0299  0.0072  9   TYR   A CZ  
150  O  OH  A TYR   A 9   ? 0.1690 0.1985 0.2249 -0.0281 0.0451  -0.0177 9   TYR   A OH  
151  O  OH  B TYR   A 9   ? 0.1322 0.1834 0.1745 -0.0137 0.0353  0.0030  9   TYR   A OH  
170  N  N   A LEU   A 10  ? 0.1363 0.1599 0.1384 -0.0179 0.0309  0.0172  10  LEU   A N   
171  N  N   B LEU   A 10  ? 0.1584 0.1578 0.1507 -0.0063 0.0280  0.0074  10  LEU   A N   
172  C  CA  A LEU   A 10  ? 0.1360 0.1387 0.1489 -0.0181 0.0237  0.0219  10  LEU   A CA  
173  C  CA  B LEU   A 10  ? 0.1504 0.1453 0.1525 -0.0034 0.0322  0.0019  10  LEU   A CA  
174  C  C   A LEU   A 10  ? 0.1313 0.1368 0.1516 -0.0194 0.0157  0.0210  10  LEU   A C   
175  C  C   B LEU   A 10  ? 0.1499 0.1365 0.1444 -0.0085 0.0234  0.0109  10  LEU   A C   
176  O  O   A LEU   A 10  ? 0.1346 0.1351 0.1508 -0.0119 0.0262  0.0235  10  LEU   A O   
177  O  O   B LEU   A 10  ? 0.1539 0.1380 0.1441 -0.0057 0.0265  0.0181  10  LEU   A O   
178  C  CB  A LEU   A 10  ? 0.1415 0.1436 0.1862 -0.0048 0.0165  0.0231  10  LEU   A CB  
179  C  CB  B LEU   A 10  ? 0.1449 0.1422 0.1604 -0.0071 0.0297  -0.0014 10  LEU   A CB  
180  C  CG  A LEU   A 10  ? 0.1590 0.1471 0.2268 0.0017  0.0054  0.0200  10  LEU   A CG  
181  C  CG  B LEU   A 10  ? 0.1445 0.1460 0.1663 -0.0020 0.0162  -0.0034 10  LEU   A CG  
182  C  CD1 A LEU   A 10  ? 0.1750 0.1546 0.2512 -0.0042 0.0116  0.0125  10  LEU   A CD1 
183  C  CD1 B LEU   A 10  ? 0.1548 0.1556 0.1878 -0.0148 0.0206  -0.0033 10  LEU   A CD1 
184  C  CD2 A LEU   A 10  ? 0.1770 0.1551 0.2418 0.0155  0.0166  0.0115  10  LEU   A CD2 
185  C  CD2 B LEU   A 10  ? 0.1571 0.1563 0.1881 0.0106  0.0041  -0.0124 10  LEU   A CD2 
208  N  N   A LYS   A 11  ? 0.1350 0.1387 0.1680 -0.0155 0.0171  0.0233  11  LYS   A N   
209  N  N   B LYS   A 11  ? 0.1559 0.1358 0.1459 -0.0139 0.0195  0.0099  11  LYS   A N   
210  C  CA  A LYS   A 11  ? 0.1338 0.1404 0.1568 -0.0194 0.0147  0.0186  11  LYS   A CA  
211  C  CA  B LYS   A 11  ? 0.1551 0.1356 0.1413 -0.0171 0.0094  0.0185  11  LYS   A CA  
212  C  C   A LYS   A 11  ? 0.1296 0.1388 0.1611 -0.0171 0.0139  0.0149  11  LYS   A C   
213  C  C   B LYS   A 11  ? 0.1490 0.1263 0.1299 -0.0170 0.0108  0.0046  11  LYS   A C   
214  O  O   A LYS   A 11  ? 0.1332 0.1567 0.2055 -0.0364 0.0211  0.0066  11  LYS   A O   
215  O  O   B LYS   A 11  ? 0.1468 0.1187 0.1464 -0.0146 0.0086  -0.0057 11  LYS   A O   
216  C  CB  A LYS   A 11  ? 0.1466 0.1416 0.1571 -0.0224 0.0114  0.0159  11  LYS   A CB  
217  C  CB  B LYS   A 11  ? 0.1624 0.1328 0.1405 -0.0214 0.0099  0.0154  11  LYS   A CB  
218  C  CG  A LYS   A 11  ? 0.1517 0.1454 0.1730 -0.0172 0.0060  0.0175  11  LYS   A CG  
219  C  CG  B LYS   A 11  ? 0.1642 0.1418 0.1405 -0.0197 0.0106  0.0262  11  LYS   A CG  
220  C  CD  A LYS   A 11  ? 0.1536 0.1516 0.1629 -0.0189 0.0000  0.0246  11  LYS   A CD  
221  C  CD  B LYS   A 11  ? 0.1659 0.1503 0.1340 -0.0121 0.0166  0.0390  11  LYS   A CD  
222  C  CE  A LYS   A 11  ? 0.1586 0.1521 0.1586 -0.0123 -0.0013 0.0312  11  LYS   A CE  
223  C  CE  B LYS   A 11  ? 0.1675 0.1558 0.1376 -0.0104 0.0070  0.0428  11  LYS   A CE  
224  N  NZ  A LYS   A 11  ? 0.1562 0.1581 0.1690 -0.0007 -0.0041 0.0318  11  LYS   A NZ  
225  N  NZ  B LYS   A 11  ? 0.1668 0.1640 0.1485 -0.0020 -0.0019 0.0394  11  LYS   A NZ  
252  N  N   A LEU   A 12  ? 0.1302 0.1249 0.1416 -0.0183 0.0200  0.0059  12  LEU   A N   
253  N  N   B LEU   A 12  ? 0.1412 0.1378 0.1386 -0.0124 0.0094  0.0013  12  LEU   A N   
254  C  CA  A LEU   A 12  ? 0.1328 0.1356 0.1412 -0.0091 0.0122  0.0156  12  LEU   A CA  
255  C  CA  B LEU   A 12  ? 0.1357 0.1432 0.1284 -0.0095 0.0133  -0.0026 12  LEU   A CA  
256  C  C   A LEU   A 12  ? 0.1334 0.1271 0.1493 -0.0168 0.0108  0.0244  12  LEU   A C   
257  C  C   B LEU   A 12  ? 0.1277 0.1398 0.1346 -0.0153 0.0241  0.0042  12  LEU   A C   
258  O  O   A LEU   A 12  ? 0.1434 0.1234 0.1533 -0.0079 0.0091  0.0049  12  LEU   A O   
259  O  O   B LEU   A 12  ? 0.1322 0.1405 0.1461 -0.0092 0.0168  0.0095  12  LEU   A O   
260  C  CB  A LEU   A 12  ? 0.1471 0.1271 0.1443 -0.0085 -0.0043 0.0068  12  LEU   A CB  
261  C  CB  B LEU   A 12  ? 0.1463 0.1511 0.1365 -0.0054 0.0111  -0.0044 12  LEU   A CB  
262  C  CG  A LEU   A 12  ? 0.1567 0.1367 0.1649 0.0002  -0.0028 0.0036  12  LEU   A CG  
263  C  CG  B LEU   A 12  ? 0.1519 0.1536 0.1616 -0.0039 0.0174  -0.0031 12  LEU   A CG  
264  C  CD1 A LEU   A 12  ? 0.1678 0.1336 0.1702 0.0147  -0.0001 0.0269  12  LEU   A CD1 
265  C  CD1 B LEU   A 12  ? 0.1533 0.1629 0.1722 0.0052  0.0285  -0.0013 12  LEU   A CD1 
266  C  CD2 A LEU   A 12  ? 0.1619 0.1452 0.1855 -0.0011 -0.0065 -0.0004 12  LEU   A CD2 
267  C  CD2 B LEU   A 12  ? 0.1505 0.1541 0.1751 0.0015  0.0093  -0.0138 12  LEU   A CD2 
290  N  N   A THR   A 13  ? 0.1351 0.1276 0.1615 -0.0074 0.0079  0.0134  13  THR   A N   
291  N  N   B THR   A 13  ? 0.1282 0.1399 0.1449 -0.0144 0.0198  -0.0034 13  THR   A N   
292  C  CA  A THR   A 13  ? 0.1417 0.1350 0.1714 -0.0083 0.0200  0.0083  13  THR   A CA  
293  C  CA  B THR   A 13  ? 0.1315 0.1403 0.1495 -0.0213 0.0272  0.0080  13  THR   A CA  
294  C  C   A THR   A 13  ? 0.1373 0.1343 0.1717 -0.0116 0.0130  0.0276  13  THR   A C   
295  C  C   B THR   A 13  ? 0.1331 0.1499 0.1564 -0.0231 0.0219  0.0174  13  THR   A C   
296  O  O   A THR   A 13  ? 0.1437 0.1377 0.1786 -0.0062 0.0097  0.0307  13  THR   A O   
297  O  O   B THR   A 13  ? 0.1416 0.1559 0.1624 -0.0168 0.0080  0.0241  13  THR   A O   
298  C  CB  A THR   A 13  ? 0.1505 0.1509 0.1886 -0.0058 0.0182  0.0028  13  THR   A CB  
299  C  CB  B THR   A 13  ? 0.1307 0.1426 0.1534 -0.0190 0.0256  0.0161  13  THR   A CB  
300  O  OG1 A THR   A 13  ? 0.1531 0.1459 0.2033 -0.0046 -0.0004 0.0050  13  THR   A OG1 
301  O  OG1 B THR   A 13  ? 0.1139 0.1417 0.1522 -0.0170 0.0422  0.0247  13  THR   A OG1 
302  C  CG2 A THR   A 13  ? 0.1563 0.1646 0.2037 0.0034  0.0285  -0.0026 13  THR   A CG2 
303  C  CG2 B THR   A 13  ? 0.1391 0.1521 0.1717 -0.0129 0.0177  0.0131  13  THR   A CG2 
318  N  N   A ASP   A 14  ? 0.1422 0.1402 0.1908 -0.0153 0.0056  0.0403  14  ASP   A N   
319  N  N   B ASP   A 14  ? 0.1361 0.1524 0.1705 -0.0289 0.0167  0.0287  14  ASP   A N   
320  C  CA  A ASP   A 14  ? 0.1449 0.1587 0.2102 -0.0134 -0.0014 0.0620  14  ASP   A CA  
321  C  CA  B ASP   A 14  ? 0.1479 0.1636 0.1933 -0.0194 0.0065  0.0477  14  ASP   A CA  
322  C  C   A ASP   A 14  ? 0.1431 0.1647 0.1946 -0.0139 -0.0126 0.0614  14  ASP   A C   
323  C  C   B ASP   A 14  ? 0.1391 0.1578 0.1878 -0.0232 -0.0039 0.0556  14  ASP   A C   
324  O  O   A ASP   A 14  ? 0.1572 0.1706 0.1911 -0.0067 -0.0173 0.0602  14  ASP   A O   
325  O  O   B ASP   A 14  ? 0.1380 0.1485 0.1914 -0.0203 -0.0080 0.0554  14  ASP   A O   
326  C  CB  A ASP   A 14  ? 0.1626 0.1895 0.2707 -0.0183 0.0023  0.0824  14  ASP   A CB  
327  C  CB  B ASP   A 14  ? 0.1729 0.1830 0.2437 -0.0042 -0.0024 0.0548  14  ASP   A CB  
328  C  CG  A ASP   A 14  ? 0.1901 0.2338 0.3483 -0.0259 0.0100  0.0791  14  ASP   A CG  
329  C  CG  B ASP   A 14  ? 0.1920 0.2165 0.2977 0.0028  -0.0092 0.0515  14  ASP   A CG  
330  O  OD1 A ASP   A 14  ? 0.2063 0.2459 0.3759 -0.0188 0.0030  0.0810  14  ASP   A OD1 
331  O  OD1 B ASP   A 14  ? 0.2033 0.2216 0.3094 0.0192  -0.0178 0.0635  14  ASP   A OD1 
332  O  OD2 A ASP   A 14  ? 0.2124 0.2664 0.3860 -0.0258 0.0017  0.0553  14  ASP   A OD2 
333  O  OD2 B ASP   A 14  ? 0.2011 0.2451 0.3247 -0.0020 -0.0214 0.0316  14  ASP   A OD2 
342  N  N   . ASN   A 15  ? 0.1387 0.1582 0.1906 -0.0265 -0.0013 0.0578  15  ASN   A N   
343  C  CA  . ASN   A 15  ? 0.1380 0.1649 0.1943 -0.0208 -0.0156 0.0487  15  ASN   A CA  
344  C  C   . ASN   A 15  ? 0.1345 0.1570 0.2094 -0.0224 -0.0060 0.0443  15  ASN   A C   
345  O  O   . ASN   A 15  ? 0.1397 0.1589 0.2631 -0.0224 -0.0277 0.0472  15  ASN   A O   
346  C  CB  . ASN   A 15  ? 0.1336 0.1645 0.1864 -0.0170 -0.0122 0.0423  15  ASN   A CB  
347  C  CG  . ASN   A 15  ? 0.1344 0.1667 0.1972 -0.0180 -0.0053 0.0318  15  ASN   A CG  
348  O  OD1 . ASN   A 15  ? 0.1560 0.1685 0.2204 -0.0309 0.0002  0.0382  15  ASN   A OD1 
349  N  ND2 . ASN   A 15  ? 0.1422 0.1758 0.1903 -0.0199 0.0064  0.0286  15  ASN   A ND2 
357  N  N   A VAL   A 16  ? 0.1350 0.1516 0.1871 -0.0213 0.0037  0.0480  16  VAL   A N   
358  N  N   B VAL   A 16  ? 0.1389 0.1530 0.1801 -0.0132 -0.0001 0.0442  16  VAL   A N   
359  C  CA  A VAL   A 16  ? 0.1345 0.1520 0.1730 -0.0222 0.0085  0.0336  16  VAL   A CA  
360  C  CA  B VAL   A 16  ? 0.1420 0.1504 0.1472 -0.0078 0.0083  0.0378  16  VAL   A CA  
361  C  C   A VAL   A 16  ? 0.1316 0.1493 0.1557 -0.0219 0.0066  0.0267  16  VAL   A C   
362  C  C   B VAL   A 16  ? 0.1381 0.1517 0.1391 -0.0118 -0.0023 0.0343  16  VAL   A C   
363  O  O   A VAL   A 16  ? 0.1207 0.1457 0.1402 -0.0236 0.0112  0.0147  16  VAL   A O   
364  O  O   B VAL   A 16  ? 0.1402 0.1562 0.1300 -0.0171 0.0056  0.0240  16  VAL   A O   
365  C  CB  A VAL   A 16  ? 0.1440 0.1622 0.1767 -0.0038 0.0213  0.0324  16  VAL   A CB  
366  C  CB  B VAL   A 16  ? 0.1509 0.1500 0.1332 0.0056  0.0244  0.0332  16  VAL   A CB  
367  C  CG1 A VAL   A 16  ? 0.1561 0.1749 0.1793 0.0044  0.0180  0.0206  16  VAL   A CG1 
368  C  CG1 B VAL   A 16  ? 0.1588 0.1522 0.1200 0.0116  0.0265  0.0321  16  VAL   A CG1 
369  C  CG2 A VAL   A 16  ? 0.1537 0.1698 0.1821 0.0019  0.0311  0.0336  16  VAL   A CG2 
370  C  CG2 B VAL   A 16  ? 0.1574 0.1566 0.1517 0.0132  0.0410  0.0318  16  VAL   A CG2 
389  N  N   A TYR   A 17  ? 0.1313 0.1376 0.1669 -0.0182 0.0168  0.0321  17  TYR   A N   
390  N  N   B TYR   A 17  ? 0.1310 0.1400 0.1536 -0.0108 -0.0095 0.0322  17  TYR   A N   
391  C  CA  A TYR   A 17  ? 0.1353 0.1395 0.1551 -0.0156 0.0210  0.0251  17  TYR   A CA  
392  C  CA  B TYR   A 17  ? 0.1307 0.1360 0.1499 -0.0219 -0.0114 0.0364  17  TYR   A CA  
393  C  C   A TYR   A 17  ? 0.1387 0.1319 0.1710 -0.0204 0.0121  0.0182  17  TYR   A C   
394  C  C   B TYR   A 17  ? 0.1259 0.1358 0.1564 -0.0189 -0.0043 0.0354  17  TYR   A C   
395  O  O   A TYR   A 17  ? 0.1348 0.1263 0.1733 -0.0173 0.0191  0.0230  17  TYR   A O   
396  O  O   B TYR   A 17  ? 0.1203 0.1429 0.1528 -0.0156 -0.0026 0.0332  17  TYR   A O   
397  C  CB  A TYR   A 17  ? 0.1491 0.1509 0.1676 -0.0124 0.0078  0.0211  17  TYR   A CB  
398  C  CB  B TYR   A 17  ? 0.1492 0.1369 0.1574 -0.0311 -0.0229 0.0373  17  TYR   A CB  
399  C  CG  A TYR   A 17  ? 0.1706 0.1740 0.1804 -0.0068 0.0036  0.0316  17  TYR   A CG  
400  C  CG  B TYR   A 17  ? 0.1704 0.1434 0.1540 -0.0397 -0.0302 0.0368  17  TYR   A CG  
401  C  CD1 A TYR   A 17  ? 0.1820 0.1823 0.1969 0.0063  0.0031  0.0311  17  TYR   A CD1 
402  C  CD1 B TYR   A 17  ? 0.1827 0.1508 0.1649 -0.0358 -0.0308 0.0361  17  TYR   A CD1 
403  C  CD2 A TYR   A 17  ? 0.1811 0.1882 0.1826 -0.0128 0.0043  0.0342  17  TYR   A CD2 
404  C  CD2 B TYR   A 17  ? 0.1805 0.1474 0.1395 -0.0529 -0.0254 0.0317  17  TYR   A CD2 
405  C  CE1 A TYR   A 17  ? 0.1900 0.1883 0.2069 0.0038  -0.0026 0.0367  17  TYR   A CE1 
406  C  CE1 B TYR   A 17  ? 0.1864 0.1531 0.1649 -0.0422 -0.0341 0.0375  17  TYR   A CE1 
407  C  CE2 A TYR   A 17  ? 0.1911 0.1898 0.2002 -0.0119 -0.0006 0.0337  17  TYR   A CE2 
408  C  CE2 B TYR   A 17  ? 0.1888 0.1479 0.1454 -0.0564 -0.0314 0.0245  17  TYR   A CE2 
409  C  CZ  A TYR   A 17  ? 0.1935 0.1878 0.2087 -0.0063 -0.0127 0.0412  17  TYR   A CZ  
410  C  CZ  B TYR   A 17  ? 0.1911 0.1473 0.1543 -0.0532 -0.0369 0.0319  17  TYR   A CZ  
411  O  OH  A TYR   A 17  ? 0.1983 0.1916 0.2237 -0.0006 -0.0176 0.0464  17  TYR   A OH  
412  O  OH  B TYR   A 17  ? 0.2009 0.1458 0.1541 -0.0479 -0.0338 0.0330  17  TYR   A OH  
431  N  N   A ILE   A 18  ? 0.1431 0.1390 0.1687 -0.0181 0.0142  0.0225  18  ILE   A N   
432  N  N   B ILE   A 18  ? 0.1231 0.1361 0.1440 -0.0200 0.0079  0.0428  18  ILE   A N   
433  C  CA  A ILE   A 18  ? 0.1436 0.1368 0.1676 -0.0104 0.0167  0.0173  18  ILE   A CA  
434  C  CA  B ILE   A 18  ? 0.1248 0.1360 0.1324 -0.0104 0.0104  0.0305  18  ILE   A CA  
435  C  C   A ILE   A 18  ? 0.1471 0.1432 0.1831 -0.0249 0.0188  0.0195  18  ILE   A C   
436  C  C   B ILE   A 18  ? 0.1267 0.1433 0.1269 -0.0148 0.0058  0.0259  18  ILE   A C   
437  O  O   A ILE   A 18  ? 0.1477 0.1576 0.1802 -0.0350 0.0270  0.0165  18  ILE   A O   
438  O  O   B ILE   A 18  ? 0.1302 0.1506 0.1428 -0.0143 0.0191  0.0247  18  ILE   A O   
439  C  CB  A ILE   A 18  ? 0.1498 0.1337 0.1501 0.0062  0.0124  0.0169  18  ILE   A CB  
440  C  CB  B ILE   A 18  ? 0.1293 0.1396 0.1244 0.0004  0.0300  0.0249  18  ILE   A CB  
441  C  CG1 A ILE   A 18  ? 0.1596 0.1356 0.1447 0.0174  0.0082  0.0201  18  ILE   A CG1 
442  C  CG1 B ILE   A 18  ? 0.1500 0.1503 0.1505 -0.0062 0.0285  0.0343  18  ILE   A CG1 
443  C  CG2 A ILE   A 18  ? 0.1493 0.1343 0.1496 0.0100  0.0021  0.0050  18  ILE   A CG2 
444  C  CG2 B ILE   A 18  ? 0.1330 0.1468 0.1197 -0.0011 0.0345  0.0152  18  ILE   A CG2 
445  C  CD1 A ILE   A 18  ? 0.1769 0.1499 0.1624 0.0284  0.0153  0.0238  18  ILE   A CD1 
446  C  CD1 B ILE   A 18  ? 0.1685 0.1643 0.1748 0.0020  0.0351  0.0236  18  ILE   A CD1 
469  N  N   A LYS   A 19  ? 0.1562 0.1517 0.1887 -0.0171 0.0280  0.0217  19  LYS   A N   
470  N  N   B LYS   A 19  ? 0.1318 0.1434 0.1198 -0.0060 0.0239  0.0257  19  LYS   A N   
471  C  CA  A LYS   A 19  ? 0.1649 0.1645 0.1867 -0.0132 0.0320  0.0135  19  LYS   A CA  
472  C  CA  B LYS   A 19  ? 0.1460 0.1567 0.1326 -0.0017 0.0393  0.0213  19  LYS   A CA  
473  C  C   A LYS   A 19  ? 0.1531 0.1568 0.1935 -0.0026 0.0266  0.0209  19  LYS   A C   
474  C  C   B LYS   A 19  ? 0.1455 0.1449 0.1563 -0.0022 0.0416  0.0264  19  LYS   A C   
475  O  O   A LYS   A 19  ? 0.1472 0.1568 0.1912 -0.0014 0.0223  0.0294  19  LYS   A O   
476  O  O   B LYS   A 19  ? 0.1450 0.1376 0.1640 -0.0045 0.0332  0.0264  19  LYS   A O   
477  C  CB  A LYS   A 19  ? 0.1842 0.1861 0.1909 -0.0188 0.0389  0.0101  19  LYS   A CB  
478  C  CB  B LYS   A 19  ? 0.1594 0.1728 0.1409 0.0042  0.0377  0.0095  19  LYS   A CB  
479  C  CG  A LYS   A 19  ? 0.2133 0.2031 0.2017 -0.0213 0.0419  0.0086  19  LYS   A CG  
480  C  CG  B LYS   A 19  ? 0.1875 0.1930 0.1481 0.0051  0.0399  -0.0010 19  LYS   A CG  
481  C  CD  A LYS   A 19  ? 0.2374 0.2203 0.2194 -0.0228 0.0487  0.0051  19  LYS   A CD  
482  C  CD  B LYS   A 19  ? 0.2119 0.2122 0.1710 0.0017  0.0448  -0.0026 19  LYS   A CD  
483  C  CE  A LYS   A 19  ? 0.2523 0.2272 0.2336 -0.0251 0.0525  -0.0054 19  LYS   A CE  
484  C  CE  B LYS   A 19  ? 0.2284 0.2269 0.1874 0.0000  0.0443  -0.0049 19  LYS   A CE  
485  N  NZ  A LYS   A 19  ? 0.2605 0.2257 0.2325 -0.0301 0.0645  -0.0248 19  LYS   A NZ  
486  N  NZ  B LYS   A 19  ? 0.2355 0.2296 0.1988 0.0003  0.0492  -0.0133 19  LYS   A NZ  
513  N  N   A ASN   A 20  ? 0.1552 0.1697 0.2262 0.0029  0.0287  0.0333  20  ASN   A N   
514  N  N   B ASN   A 20  ? 0.1506 0.1506 0.1770 -0.0053 0.0527  0.0297  20  ASN   A N   
515  C  CA  A ASN   A 20  ? 0.1706 0.1851 0.2413 0.0198  0.0428  0.0338  20  ASN   A CA  
516  C  CA  B ASN   A 20  ? 0.1635 0.1591 0.1963 0.0031  0.0563  0.0373  20  ASN   A CA  
517  C  C   A ASN   A 20  ? 0.1910 0.1794 0.2204 0.0080  0.0590  0.0321  20  ASN   A C   
518  C  C   B ASN   A 20  ? 0.1842 0.1640 0.1873 0.0007  0.0738  0.0226  20  ASN   A C   
519  O  O   A ASN   A 20  ? 0.2040 0.1667 0.2272 -0.0035 0.0643  0.0317  20  ASN   A O   
520  O  O   B ASN   A 20  ? 0.1995 0.1649 0.2146 0.0046  0.0717  0.0171  20  ASN   A O   
521  C  CB  A ASN   A 20  ? 0.1788 0.2035 0.2662 0.0347  0.0521  0.0469  20  ASN   A CB  
522  C  CB  B ASN   A 20  ? 0.1659 0.1680 0.2209 0.0135  0.0547  0.0596  20  ASN   A CB  
523  C  CG  A ASN   A 20  ? 0.1966 0.2137 0.3016 0.0510  0.0683  0.0576  20  ASN   A CG  
524  C  CG  B ASN   A 20  ? 0.1764 0.1745 0.2607 0.0296  0.0527  0.0796  20  ASN   A CG  
525  O  OD1 A ASN   A 20  ? 0.2231 0.2234 0.3545 0.0609  0.0955  0.0455  20  ASN   A OD1 
526  O  OD1 B ASN   A 20  ? 0.2036 0.1913 0.3180 0.0352  0.0667  0.0724  20  ASN   A OD1 
527  N  ND2 A ASN   A 20  ? 0.2074 0.2187 0.3046 0.0444  0.0559  0.0732  20  ASN   A ND2 
528  N  ND2 B ASN   A 20  ? 0.1767 0.1743 0.2542 0.0326  0.0439  0.0908  20  ASN   A ND2 
541  N  N   A ALA   A 21  ? 0.1950 0.1873 0.2126 0.0067  0.0458  0.0185  21  ALA   A N   
542  N  N   B ALA   A 21  ? 0.1918 0.1733 0.1880 0.0018  0.0628  0.0074  21  ALA   A N   
543  C  CA  A ALA   A 21  ? 0.1989 0.1849 0.2093 -0.0001 0.0331  0.0303  21  ALA   A CA  
544  C  CA  B ALA   A 21  ? 0.1982 0.1752 0.1879 -0.0019 0.0556  0.0126  21  ALA   A CA  
545  C  C   A ALA   A 21  ? 0.1809 0.1834 0.2047 -0.0007 0.0276  0.0313  21  ALA   A C   
546  C  C   B ALA   A 21  ? 0.1830 0.1712 0.1667 -0.0001 0.0612  0.0207  21  ALA   A C   
547  O  O   A ALA   A 21  ? 0.1723 0.1860 0.2132 0.0039  0.0201  0.0288  21  ALA   A O   
548  O  O   B ALA   A 21  ? 0.1783 0.1694 0.1723 0.0115  0.0592  0.0175  21  ALA   A O   
549  C  CB  A ALA   A 21  ? 0.2158 0.1868 0.2080 -0.0038 0.0272  0.0313  21  ALA   A CB  
550  C  CB  B ALA   A 21  ? 0.2118 0.1798 0.2079 -0.0028 0.0449  0.0088  21  ALA   A CB  
561  N  N   A ASP   A 22  ? 0.1824 0.1831 0.2170 -0.0047 0.0298  0.0341  22  ASP   A N   
562  N  N   B ASP   A 22  ? 0.1798 0.1687 0.1587 -0.0018 0.0594  0.0246  22  ASP   A N   
563  C  CA  A ASP   A 22  ? 0.1851 0.1829 0.2276 0.0006  0.0170  0.0392  22  ASP   A CA  
564  C  CA  B ASP   A 22  ? 0.1771 0.1623 0.1551 0.0011  0.0406  0.0287  22  ASP   A CA  
565  C  C   A ASP   A 22  ? 0.1795 0.1813 0.1890 -0.0001 0.0197  0.0366  22  ASP   A C   
566  C  C   B ASP   A 22  ? 0.1618 0.1622 0.1312 -0.0100 0.0328  0.0243  22  ASP   A C   
567  O  O   A ASP   A 22  ? 0.1836 0.1831 0.1974 -0.0024 0.0124  0.0245  22  ASP   A O   
568  O  O   B ASP   A 22  ? 0.1560 0.1681 0.1353 -0.0192 0.0305  0.0091  22  ASP   A O   
569  C  CB  A ASP   A 22  ? 0.2042 0.1876 0.2796 -0.0036 0.0048  0.0320  22  ASP   A CB  
570  C  CB  B ASP   A 22  ? 0.1903 0.1599 0.1819 0.0176  0.0413  0.0234  22  ASP   A CB  
571  C  CG  A ASP   A 22  ? 0.2222 0.1954 0.3274 -0.0026 -0.0053 0.0356  22  ASP   A CG  
572  C  CG  B ASP   A 22  ? 0.1999 0.1602 0.1789 0.0277  0.0378  0.0246  22  ASP   A CG  
573  O  OD1 A ASP   A 22  ? 0.2193 0.1982 0.3502 -0.0140 -0.0156 0.0424  22  ASP   A OD1 
574  O  OD1 B ASP   A 22  ? 0.1913 0.1559 0.1532 0.0218  0.0271  0.0166  22  ASP   A OD1 
575  O  OD2 A ASP   A 22  ? 0.2462 0.2026 0.3492 0.0022  0.0016  0.0246  22  ASP   A OD2 
576  O  OD2 B ASP   A 22  ? 0.2176 0.1685 0.2188 0.0288  0.0592  0.0328  22  ASP   A OD2 
585  N  N   A ILE   A 23  ? 0.1784 0.1810 0.1675 -0.0019 0.0199  0.0324  23  ILE   A N   
586  N  N   B ILE   A 23  ? 0.1550 0.1566 0.1324 -0.0053 0.0248  0.0210  23  ILE   A N   
587  C  CA  A ILE   A 23  ? 0.1780 0.1714 0.1571 -0.0025 0.0201  0.0277  23  ILE   A CA  
588  C  CA  B ILE   A 23  ? 0.1487 0.1533 0.1233 -0.0078 0.0154  0.0224  23  ILE   A CA  
589  C  C   A ILE   A 23  ? 0.1765 0.1736 0.1540 -0.0037 0.0315  0.0195  23  ILE   A C   
590  C  C   B ILE   A 23  ? 0.1545 0.1598 0.1337 -0.0138 0.0126  0.0167  23  ILE   A C   
591  O  O   A ILE   A 23  ? 0.1805 0.1819 0.1518 -0.0083 0.0280  0.0042  23  ILE   A O   
592  O  O   B ILE   A 23  ? 0.1556 0.1591 0.1365 -0.0127 0.0084  0.0154  23  ILE   A O   
593  C  CB  A ILE   A 23  ? 0.1864 0.1651 0.1469 0.0063  0.0165  0.0236  23  ILE   A CB  
594  C  CB  B ILE   A 23  ? 0.1503 0.1509 0.1107 0.0011  0.0070  0.0277  23  ILE   A CB  
595  C  CG1 A ILE   A 23  ? 0.1899 0.1627 0.1399 0.0097  0.0097  0.0170  23  ILE   A CG1 
596  C  CG1 B ILE   A 23  ? 0.1571 0.1496 0.1021 -0.0065 -0.0042 0.0085  23  ILE   A CG1 
597  C  CG2 A ILE   A 23  ? 0.1866 0.1640 0.1555 0.0132  0.0140  0.0228  23  ILE   A CG2 
598  C  CG2 B ILE   A 23  ? 0.1496 0.1487 0.1023 0.0064  -0.0048 0.0229  23  ILE   A CG2 
599  C  CD1 A ILE   A 23  ? 0.1912 0.1635 0.1406 0.0085  0.0013  0.0097  23  ILE   A CD1 
600  C  CD1 B ILE   A 23  ? 0.1561 0.1529 0.1014 -0.0065 -0.0103 -0.0005 23  ILE   A CD1 
623  N  N   A VAL   A 24  ? 0.1807 0.1752 0.1647 -0.0103 0.0293  0.0239  24  VAL   A N   
624  N  N   B VAL   A 24  ? 0.1656 0.1691 0.1435 -0.0241 0.0104  0.0117  24  VAL   A N   
625  C  CA  A VAL   A 24  ? 0.1902 0.1837 0.1828 -0.0124 0.0258  0.0111  24  VAL   A CA  
626  C  CA  B VAL   A 24  ? 0.1801 0.1758 0.1582 -0.0301 0.0150  0.0059  24  VAL   A CA  
627  C  C   A VAL   A 24  ? 0.1953 0.1984 0.1830 -0.0175 0.0142  0.0060  24  VAL   A C   
628  C  C   B VAL   A 24  ? 0.1840 0.1905 0.1659 -0.0290 0.0189  -0.0081 24  VAL   A C   
629  O  O   A VAL   A 24  ? 0.2063 0.2001 0.1851 -0.0176 0.0138  0.0013  24  VAL   A O   
630  O  O   B VAL   A 24  ? 0.1963 0.1950 0.1870 -0.0280 0.0224  -0.0065 24  VAL   A O   
631  C  CB  A VAL   A 24  ? 0.1964 0.1853 0.2142 -0.0068 0.0325  0.0075  24  VAL   A CB  
632  C  CB  B VAL   A 24  ? 0.1898 0.1771 0.1823 -0.0310 0.0194  0.0141  24  VAL   A CB  
633  C  CG1 A VAL   A 24  ? 0.2014 0.1942 0.2321 -0.0024 0.0363  -0.0055 24  VAL   A CG1 
634  C  CG1 B VAL   A 24  ? 0.1996 0.1859 0.2184 -0.0259 0.0185  0.0060  24  VAL   A CG1 
635  C  CG2 A VAL   A 24  ? 0.2022 0.1885 0.2205 -0.0007 0.0415  0.0211  24  VAL   A CG2 
636  C  CG2 B VAL   A 24  ? 0.1968 0.1714 0.1782 -0.0341 0.0291  0.0190  24  VAL   A CG2 
655  N  N   A GLU   A 25  ? 0.1973 0.2199 0.1761 -0.0206 0.0175  -0.0070 25  GLU   A N   
656  N  N   B GLU   A 25  ? 0.1811 0.2045 0.1631 -0.0269 0.0298  -0.0217 25  GLU   A N   
657  C  CA  A GLU   A 25  ? 0.2112 0.2443 0.1830 -0.0137 0.0194  -0.0106 25  GLU   A CA  
658  C  CA  B GLU   A 25  ? 0.1904 0.2253 0.1660 -0.0274 0.0359  -0.0249 25  GLU   A CA  
659  C  C   A GLU   A 25  ? 0.1987 0.2464 0.1431 -0.0254 0.0215  -0.0144 25  GLU   A C   
660  C  C   B GLU   A 25  ? 0.1870 0.2349 0.1485 -0.0269 0.0406  -0.0211 25  GLU   A C   
661  O  O   A GLU   A 25  ? 0.1983 0.2594 0.1452 -0.0278 0.0207  -0.0231 25  GLU   A O   
662  O  O   B GLU   A 25  ? 0.1898 0.2421 0.1593 -0.0267 0.0485  -0.0270 25  GLU   A O   
663  C  CB  A GLU   A 25  ? 0.2353 0.2689 0.2387 -0.0082 0.0120  -0.0063 25  GLU   A CB  
664  C  CB  B GLU   A 25  ? 0.2048 0.2383 0.2009 -0.0253 0.0334  -0.0300 25  GLU   A CB  
665  C  CG  A GLU   A 25  ? 0.2615 0.2916 0.2981 -0.0126 -0.0015 -0.0058 25  GLU   A CG  
666  C  CG  B GLU   A 25  ? 0.2278 0.2535 0.2605 -0.0267 0.0245  -0.0266 25  GLU   A CG  
667  C  CD  A GLU   A 25  ? 0.2821 0.3121 0.3457 -0.0151 -0.0123 -0.0043 25  GLU   A CD  
668  C  CD  B GLU   A 25  ? 0.2442 0.2694 0.3166 -0.0306 0.0069  -0.0254 25  GLU   A CD  
669  O  OE1 A GLU   A 25  ? 0.2887 0.3189 0.3524 -0.0116 -0.0199 -0.0100 25  GLU   A OE1 
670  O  OE1 B GLU   A 25  ? 0.2511 0.2756 0.3433 -0.0307 0.0015  -0.0255 25  GLU   A OE1 
671  O  OE2 A GLU   A 25  ? 0.2920 0.3233 0.3740 -0.0173 -0.0170 -0.0072 25  GLU   A OE2 
672  O  OE2 B GLU   A 25  ? 0.2506 0.2769 0.3371 -0.0317 -0.0033 -0.0246 25  GLU   A OE2 
685  N  N   A GLU   A 26  ? 0.1911 0.2374 0.1423 -0.0383 0.0278  -0.0119 26  GLU   A N   
686  N  N   B GLU   A 26  ? 0.1838 0.2366 0.1405 -0.0298 0.0360  -0.0153 26  GLU   A N   
687  C  CA  A GLU   A 26  ? 0.1978 0.2363 0.1309 -0.0544 0.0336  -0.0068 26  GLU   A CA  
688  C  CA  B GLU   A 26  ? 0.1887 0.2426 0.1506 -0.0293 0.0309  -0.0076 26  GLU   A CA  
689  C  C   A GLU   A 26  ? 0.1932 0.2285 0.1135 -0.0570 0.0299  -0.0159 26  GLU   A C   
690  C  C   B GLU   A 26  ? 0.1853 0.2308 0.1418 -0.0233 0.0226  0.0024  26  GLU   A C   
691  O  O   A GLU   A 26  ? 0.1998 0.2339 0.1118 -0.0589 0.0332  -0.0195 26  GLU   A O   
692  O  O   B GLU   A 26  ? 0.1933 0.2322 0.1400 -0.0276 0.0245  0.0056  26  GLU   A O   
693  C  CB  A GLU   A 26  ? 0.2142 0.2378 0.1453 -0.0658 0.0361  -0.0012 26  GLU   A CB  
694  C  CB  B GLU   A 26  ? 0.2009 0.2560 0.1655 -0.0344 0.0162  -0.0097 26  GLU   A CB  
695  C  CG  A GLU   A 26  ? 0.2386 0.2554 0.2319 -0.0709 0.0339  -0.0159 26  GLU   A CG  
696  C  CG  B GLU   A 26  ? 0.2140 0.2695 0.1897 -0.0386 0.0180  -0.0188 26  GLU   A CG  
697  C  CD  A GLU   A 26  ? 0.2550 0.2705 0.2783 -0.0814 0.0480  -0.0270 26  GLU   A CD  
698  C  CD  B GLU   A 26  ? 0.2231 0.2792 0.1860 -0.0503 0.0281  -0.0228 26  GLU   A CD  
699  O  OE1 A GLU   A 26  ? 0.2520 0.2848 0.2614 -0.0787 0.0758  -0.0614 26  GLU   A OE1 
700  O  OE1 B GLU   A 26  ? 0.2277 0.2927 0.1787 -0.0480 0.0415  -0.0300 26  GLU   A OE1 
701  O  OE2 A GLU   A 26  ? 0.2727 0.2771 0.2950 -0.0839 0.0407  -0.0190 26  GLU   A OE2 
702  O  OE2 B GLU   A 26  ? 0.2237 0.2762 0.1423 -0.0593 0.0381  -0.0238 26  GLU   A OE2 
715  N  N   A ALA   A 27  ? 0.1824 0.2182 0.1295 -0.0659 0.0320  -0.0102 27  ALA   A N   
716  N  N   B ALA   A 27  ? 0.1737 0.2186 0.1389 -0.0152 0.0200  0.0198  27  ALA   A N   
717  C  CA  A ALA   A 27  ? 0.1894 0.2211 0.1375 -0.0567 0.0237  -0.0087 27  ALA   A CA  
718  C  CA  B ALA   A 27  ? 0.1740 0.2146 0.1285 -0.0023 0.0118  0.0325  27  ALA   A CA  
719  C  C   A ALA   A 27  ? 0.2066 0.2352 0.1496 -0.0619 0.0176  -0.0171 27  ALA   A C   
720  C  C   B ALA   A 27  ? 0.1840 0.2181 0.1238 0.0028  0.0078  0.0292  27  ALA   A C   
721  O  O   A ALA   A 27  ? 0.2143 0.2357 0.1573 -0.0638 0.0078  -0.0120 27  ALA   A O   
722  O  O   B ALA   A 27  ? 0.1810 0.2162 0.1250 0.0050  0.0045  0.0284  27  ALA   A O   
723  C  CB  A ALA   A 27  ? 0.1781 0.2135 0.1443 -0.0523 0.0214  0.0071  27  ALA   A CB  
724  C  CB  B ALA   A 27  ? 0.1621 0.2098 0.1241 -0.0031 0.0066  0.0413  27  ALA   A CB  
735  N  N   A LYS   A 28  ? 0.2246 0.2545 0.1637 -0.0617 0.0143  -0.0438 28  LYS   A N   
736  N  N   B LYS   A 28  ? 0.2045 0.2271 0.1335 0.0086  -0.0028 0.0113  28  LYS   A N   
737  C  CA  A LYS   A 28  ? 0.2509 0.2867 0.2008 -0.0488 0.0177  -0.0543 28  LYS   A CA  
738  C  CA  B LYS   A 28  ? 0.2281 0.2486 0.1520 0.0195  -0.0170 -0.0124 28  LYS   A CA  
739  C  C   A LYS   A 28  ? 0.2679 0.3121 0.1879 -0.0478 0.0339  -0.0454 28  LYS   A C   
740  C  C   B LYS   A 28  ? 0.2473 0.2669 0.1324 0.0213  -0.0148 -0.0002 28  LYS   A C   
741  O  O   A LYS   A 28  ? 0.2702 0.3187 0.2178 -0.0400 0.0146  -0.0406 28  LYS   A O   
742  O  O   B LYS   A 28  ? 0.2592 0.2712 0.1352 0.0221  -0.0240 0.0090  28  LYS   A O   
743  C  CB  A LYS   A 28  ? 0.2637 0.2990 0.2603 -0.0331 0.0079  -0.0565 28  LYS   A CB  
744  C  CB  B LYS   A 28  ? 0.2381 0.2581 0.1997 0.0281  -0.0322 -0.0378 28  LYS   A CB  
745  C  CG  A LYS   A 28  ? 0.2772 0.3103 0.3156 -0.0209 0.0018  -0.0554 28  LYS   A CG  
746  C  CG  B LYS   A 28  ? 0.2504 0.2701 0.2568 0.0301  -0.0406 -0.0461 28  LYS   A CG  
747  C  CD  A LYS   A 28  ? 0.2861 0.3241 0.3750 -0.0140 -0.0095 -0.0531 28  LYS   A CD  
748  C  CD  B LYS   A 28  ? 0.2636 0.2864 0.3255 0.0296  -0.0446 -0.0451 28  LYS   A CD  
749  C  CE  A LYS   A 28  ? 0.2903 0.3341 0.4159 -0.0108 -0.0190 -0.0555 28  LYS   A CE  
750  C  CE  B LYS   A 28  ? 0.2736 0.2970 0.3723 0.0238  -0.0465 -0.0450 28  LYS   A CE  
751  N  NZ  A LYS   A 28  ? 0.2966 0.3394 0.4430 -0.0075 -0.0179 -0.0563 28  LYS   A NZ  
752  N  NZ  B LYS   A 28  ? 0.2747 0.3024 0.3918 0.0235  -0.0506 -0.0439 28  LYS   A NZ  
779  N  N   A LYS   A 29  ? 0.2810 0.3339 0.1766 -0.0559 0.0691  -0.0281 29  LYS   A N   
780  N  N   B LYS   A 29  ? 0.2545 0.2823 0.1299 0.0194  0.0012  0.0141  29  LYS   A N   
781  C  CA  A LYS   A 29  ? 0.3018 0.3576 0.1897 -0.0582 0.0894  -0.0115 29  LYS   A CA  
782  C  CA  B LYS   A 29  ? 0.2691 0.3010 0.1494 0.0157  0.0224  0.0275  29  LYS   A CA  
783  C  C   A LYS   A 29  ? 0.3009 0.3539 0.1542 -0.0653 0.0767  -0.0002 29  LYS   A C   
784  C  C   B LYS   A 29  ? 0.2724 0.2993 0.1244 0.0066  0.0170  0.0387  29  LYS   A C   
785  O  O   A LYS   A 29  ? 0.3130 0.3658 0.1694 -0.0593 0.0710  -0.0008 29  LYS   A O   
786  O  O   B LYS   A 29  ? 0.2793 0.3077 0.1344 0.0122  0.0163  0.0411  29  LYS   A O   
787  C  CB  A LYS   A 29  ? 0.3212 0.3833 0.2565 -0.0502 0.1056  -0.0059 29  LYS   A CB  
788  C  CB  B LYS   A 29  ? 0.2838 0.3191 0.2086 0.0174  0.0494  0.0283  29  LYS   A CB  
789  C  CG  A LYS   A 29  ? 0.3409 0.4041 0.3262 -0.0421 0.1130  -0.0024 29  LYS   A CG  
790  C  CG  B LYS   A 29  ? 0.3013 0.3347 0.2769 0.0205  0.0661  0.0240  29  LYS   A CG  
791  C  CD  A LYS   A 29  ? 0.3585 0.4204 0.3881 -0.0361 0.1129  -0.0024 29  LYS   A CD  
792  C  CD  B LYS   A 29  ? 0.3151 0.3471 0.3401 0.0238  0.0736  0.0203  29  LYS   A CD  
793  C  CE  A LYS   A 29  ? 0.3704 0.4307 0.4330 -0.0325 0.1130  -0.0007 29  LYS   A CE  
794  C  CE  B LYS   A 29  ? 0.3255 0.3572 0.3868 0.0241  0.0786  0.0168  29  LYS   A CE  
795  N  NZ  A LYS   A 29  ? 0.3755 0.4366 0.4598 -0.0301 0.1131  -0.0008 29  LYS   A NZ  
796  N  NZ  B LYS   A 29  ? 0.3313 0.3633 0.4157 0.0230  0.0798  0.0167  29  LYS   A NZ  
823  N  N   A VAL   A 30  ? 0.2865 0.3377 0.1497 -0.0762 0.0628  0.0064  30  VAL   A N   
824  N  N   B VAL   A 30  ? 0.2692 0.2904 0.1398 -0.0049 0.0141  0.0391  30  VAL   A N   
825  C  CA  A VAL   A 30  ? 0.2811 0.3216 0.1433 -0.0902 0.0374  0.0269  30  VAL   A CA  
826  C  CA  B VAL   A 30  ? 0.2661 0.2792 0.1576 -0.0202 -0.0026 0.0471  30  VAL   A CA  
827  C  C   A VAL   A 30  ? 0.2750 0.3007 0.1102 -0.0811 0.0238  0.0390  30  VAL   A C   
828  C  C   B VAL   A 30  ? 0.2676 0.2743 0.1571 -0.0225 -0.0091 0.0388  30  VAL   A C   
829  O  O   A VAL   A 30  ? 0.2837 0.3060 0.1142 -0.0850 0.0212  0.0417  30  VAL   A O   
830  O  O   B VAL   A 30  ? 0.2702 0.2743 0.1606 -0.0239 -0.0103 0.0430  30  VAL   A O   
831  C  CB  A VAL   A 30  ? 0.2792 0.3158 0.1867 -0.0989 0.0170  0.0254  30  VAL   A CB  
832  C  CB  B VAL   A 30  ? 0.2637 0.2723 0.1800 -0.0284 -0.0187 0.0554  30  VAL   A CB  
833  C  CG1 A VAL   A 30  ? 0.2850 0.3189 0.2088 -0.0983 0.0093  0.0215  30  VAL   A CG1 
834  C  CG1 B VAL   A 30  ? 0.2681 0.2734 0.1992 -0.0291 -0.0244 0.0543  30  VAL   A CG1 
835  C  CG2 A VAL   A 30  ? 0.2786 0.3134 0.2135 -0.1047 0.0161  0.0246  30  VAL   A CG2 
836  C  CG2 B VAL   A 30  ? 0.2609 0.2674 0.1905 -0.0322 -0.0202 0.0650  30  VAL   A CG2 
855  N  N   A LYS   A 31  ? 0.2626 0.2812 0.0984 -0.0782 0.0095  0.0350  31  LYS   A N   
856  N  N   B LYS   A 31  ? 0.2676 0.2691 0.1671 -0.0249 -0.0186 0.0272  31  LYS   A N   
857  C  CA  A LYS   A 31  ? 0.2747 0.2822 0.1128 -0.0759 -0.0146 0.0321  31  LYS   A CA  
858  C  CA  B LYS   A 31  ? 0.2680 0.2669 0.1786 -0.0200 -0.0270 0.0167  31  LYS   A CA  
859  C  C   A LYS   A 31  ? 0.2432 0.2485 0.0969 -0.0467 -0.0171 0.0587  31  LYS   A C   
860  C  C   B LYS   A 31  ? 0.2471 0.2559 0.1628 -0.0123 -0.0198 0.0269  31  LYS   A C   
861  O  O   A LYS   A 31  ? 0.2523 0.2652 0.1131 -0.0491 -0.0279 0.0730  31  LYS   A O   
862  O  O   B LYS   A 31  ? 0.2533 0.2620 0.1835 -0.0043 -0.0237 0.0281  31  LYS   A O   
863  C  CB  A LYS   A 31  ? 0.3043 0.2996 0.2043 -0.0617 -0.0275 0.0072  31  LYS   A CB  
864  C  CB  B LYS   A 31  ? 0.2916 0.2846 0.2334 -0.0179 -0.0355 -0.0033 31  LYS   A CB  
865  C  CG  A LYS   A 31  ? 0.3440 0.3244 0.3253 -0.0481 -0.0374 -0.0057 31  LYS   A CG  
866  C  CG  B LYS   A 31  ? 0.3191 0.3058 0.3183 -0.0144 -0.0404 -0.0167 31  LYS   A CG  
867  C  CD  A LYS   A 31  ? 0.3755 0.3430 0.4174 -0.0353 -0.0487 -0.0204 31  LYS   A CD  
868  C  CD  B LYS   A 31  ? 0.3405 0.3232 0.3904 -0.0120 -0.0481 -0.0310 31  LYS   A CD  
869  C  CE  A LYS   A 31  ? 0.3941 0.3538 0.4773 -0.0245 -0.0573 -0.0316 31  LYS   A CE  
870  C  CE  B LYS   A 31  ? 0.3557 0.3372 0.4415 -0.0116 -0.0526 -0.0390 31  LYS   A CE  
871  N  NZ  A LYS   A 31  ? 0.4038 0.3597 0.5070 -0.0176 -0.0630 -0.0369 31  LYS   A NZ  
872  N  NZ  B LYS   A 31  ? 0.3665 0.3454 0.4696 -0.0105 -0.0539 -0.0438 31  LYS   A NZ  
899  N  N   A PRO   A 32  ? 0.2212 0.2331 0.0857 -0.0482 -0.0127 0.0479  32  PRO   A N   
900  N  N   B PRO   A 32  ? 0.2185 0.2374 0.1359 -0.0115 -0.0079 0.0221  32  PRO   A N   
901  C  CA  A PRO   A 32  ? 0.2256 0.2314 0.1260 -0.0520 -0.0173 0.0537  32  PRO   A CA  
902  C  CA  B PRO   A 32  ? 0.2083 0.2295 0.1413 -0.0096 -0.0082 0.0320  32  PRO   A CA  
903  C  C   A PRO   A 32  ? 0.2199 0.2259 0.1293 -0.0395 -0.0194 0.0520  32  PRO   A C   
904  C  C   B PRO   A 32  ? 0.2029 0.2259 0.1348 -0.0083 -0.0215 0.0416  32  PRO   A C   
905  O  O   A PRO   A 32  ? 0.2131 0.2240 0.1224 -0.0471 -0.0179 0.0426  32  PRO   A O   
906  O  O   B PRO   A 32  ? 0.1974 0.2252 0.1529 -0.0115 -0.0290 0.0354  32  PRO   A O   
907  C  CB  A PRO   A 32  ? 0.2192 0.2320 0.1305 -0.0484 -0.0185 0.0409  32  PRO   A CB  
908  C  CB  B PRO   A 32  ? 0.2046 0.2309 0.1465 -0.0068 -0.0052 0.0213  32  PRO   A CB  
909  C  CG  A PRO   A 32  ? 0.2160 0.2358 0.0868 -0.0456 -0.0317 0.0304  32  PRO   A CG  
910  C  CG  B PRO   A 32  ? 0.2054 0.2331 0.1274 -0.0049 -0.0094 0.0106  32  PRO   A CG  
911  C  CD  A PRO   A 32  ? 0.2173 0.2344 0.0810 -0.0494 -0.0174 0.0397  32  PRO   A CD  
912  C  CD  B PRO   A 32  ? 0.2091 0.2361 0.1265 -0.0088 -0.0029 0.0122  32  PRO   A CD  
927  N  N   A THR   A 33  ? 0.2245 0.2236 0.1345 -0.0312 -0.0237 0.0574  33  THR   A N   
928  N  N   B THR   A 33  ? 0.2050 0.2237 0.1340 -0.0076 -0.0277 0.0506  33  THR   A N   
929  C  CA  A THR   A 33  ? 0.2246 0.2239 0.1490 -0.0189 -0.0311 0.0583  33  THR   A CA  
930  C  CA  B THR   A 33  ? 0.2045 0.2199 0.1325 -0.0032 -0.0406 0.0596  33  THR   A CA  
931  C  C   A THR   A 33  ? 0.2005 0.2059 0.1316 -0.0220 -0.0362 0.0459  33  THR   A C   
932  C  C   B THR   A 33  ? 0.1881 0.2022 0.1341 -0.0191 -0.0422 0.0405  33  THR   A C   
933  O  O   A THR   A 33  ? 0.1963 0.1975 0.1344 -0.0193 -0.0451 0.0468  33  THR   A O   
934  O  O   B THR   A 33  ? 0.1848 0.1895 0.1524 -0.0248 -0.0428 0.0275  33  THR   A O   
935  C  CB  A THR   A 33  ? 0.2465 0.2408 0.1791 -0.0090 -0.0361 0.0687  33  THR   A CB  
936  C  CB  B THR   A 33  ? 0.2255 0.2339 0.1419 0.0092  -0.0364 0.0829  33  THR   A CB  
937  O  OG1 A THR   A 33  ? 0.2643 0.2569 0.2130 0.0010  -0.0273 0.0648  33  THR   A OG1 
938  O  OG1 B THR   A 33  ? 0.2396 0.2455 0.1547 0.0191  -0.0338 0.0941  33  THR   A OG1 
939  C  CG2 A THR   A 33  ? 0.2507 0.2457 0.1926 -0.0036 -0.0370 0.0691  33  THR   A CG2 
940  C  CG2 B THR   A 33  ? 0.2289 0.2391 0.1625 0.0108  -0.0272 0.0780  33  THR   A CG2 
955  N  N   . VAL   A 34  ? 0.1829 0.1993 0.1201 -0.0318 -0.0299 0.0363  34  VAL   A N   
956  C  CA  . VAL   A 34  ? 0.1706 0.1825 0.1009 -0.0299 -0.0200 0.0370  34  VAL   A CA  
957  C  C   . VAL   A 34  ? 0.1637 0.1751 0.0925 -0.0246 -0.0124 0.0336  34  VAL   A C   
958  O  O   . VAL   A 34  ? 0.1620 0.1786 0.1361 -0.0333 -0.0077 0.0370  34  VAL   A O   
959  C  CB  . VAL   A 34  ? 0.1782 0.1846 0.1351 -0.0281 -0.0185 0.0293  34  VAL   A CB  
960  C  CG1 . VAL   A 34  ? 0.1856 0.1842 0.1314 -0.0227 -0.0071 0.0153  34  VAL   A CG1 
961  C  CG2 . VAL   A 34  ? 0.1871 0.1961 0.1621 -0.0222 -0.0213 0.0351  34  VAL   A CG2 
972  N  N   . VAL   A 35  ? 0.1506 0.1656 0.0949 -0.0258 -0.0121 0.0263  35  VAL   A N   
973  C  CA  . VAL   A 35  ? 0.1449 0.1608 0.0921 -0.0234 -0.0074 0.0191  35  VAL   A CA  
974  C  C   . VAL   A 35  ? 0.1407 0.1525 0.0917 -0.0168 -0.0040 0.0207  35  VAL   A C   
975  O  O   . VAL   A 35  ? 0.1280 0.1653 0.1151 -0.0271 0.0072  0.0114  35  VAL   A O   
976  C  CB  . VAL   A 35  ? 0.1541 0.1682 0.1120 -0.0153 0.0037  0.0119  35  VAL   A CB  
977  C  CG1 . VAL   A 35  ? 0.1638 0.1722 0.1267 -0.0125 -0.0017 0.0055  35  VAL   A CG1 
978  C  CG2 . VAL   A 35  ? 0.1465 0.1737 0.1397 -0.0127 0.0060  0.0023  35  VAL   A CG2 
988  N  N   . VAL   A 36  ? 0.1276 0.1465 0.0848 -0.0150 -0.0048 0.0196  36  VAL   A N   
989  C  CA  . VAL   A 36  ? 0.1274 0.1360 0.0833 -0.0083 -0.0041 0.0147  36  VAL   A CA  
990  C  C   . VAL   A 36  ? 0.1234 0.1378 0.1004 -0.0131 -0.0014 0.0167  36  VAL   A C   
991  O  O   . VAL   A 36  ? 0.1273 0.1395 0.1196 -0.0080 0.0060  0.0163  36  VAL   A O   
992  C  CB  . VAL   A 36  ? 0.1214 0.1318 0.1093 -0.0073 -0.0018 0.0171  36  VAL   A CB  
993  C  CG1 . VAL   A 36  ? 0.1259 0.1327 0.1267 -0.0123 -0.0000 0.0089  36  VAL   A CG1 
994  C  CG2 . VAL   A 36  ? 0.1349 0.1354 0.1276 -0.0092 -0.0099 0.0198  36  VAL   A CG2 
1004 N  N   . ASN   A 37  ? 0.1214 0.1280 0.1002 -0.0047 0.0009  0.0183  37  ASN   A N   
1005 C  CA  . ASN   A 37  ? 0.1193 0.1275 0.0918 0.0011  0.0033  0.0215  37  ASN   A CA  
1006 C  C   . ASN   A 37  ? 0.1189 0.1209 0.0984 -0.0041 0.0063  0.0251  37  ASN   A C   
1007 O  O   . ASN   A 37  ? 0.1312 0.1300 0.1006 0.0058  0.0070  0.0130  37  ASN   A O   
1008 C  CB  . ASN   A 37  ? 0.1203 0.1290 0.1055 0.0012  0.0006  0.0163  37  ASN   A CB  
1009 C  CG  . ASN   A 37  ? 0.1216 0.1278 0.1127 0.0015  0.0010  0.0104  37  ASN   A CG  
1010 O  OD1 . ASN   A 37  ? 0.1258 0.1258 0.1342 -0.0013 0.0016  0.0189  37  ASN   A OD1 
1011 N  ND2 . ASN   A 37  ? 0.1223 0.1281 0.1248 -0.0035 -0.0028 0.0265  37  ASN   A ND2 
1018 N  N   A ALA   A 38  ? 0.1212 0.1241 0.1034 -0.0013 0.0049  0.0139  38  ALA   A N   
1019 N  N   B ALA   A 38  ? 0.1242 0.1255 0.1070 -0.0004 0.0031  0.0181  38  ALA   A N   
1020 C  CA  A ALA   A 38  ? 0.1288 0.1322 0.0972 -0.0071 -0.0006 0.0080  38  ALA   A CA  
1021 C  CA  B ALA   A 38  ? 0.1327 0.1362 0.1080 -0.0040 -0.0004 0.0154  38  ALA   A CA  
1022 C  C   A ALA   A 38  ? 0.1277 0.1373 0.1078 0.0038  -0.0052 0.0042  38  ALA   A C   
1023 C  C   B ALA   A 38  ? 0.1307 0.1375 0.1141 0.0014  -0.0063 0.0093  38  ALA   A C   
1024 O  O   A ALA   A 38  ? 0.1261 0.1285 0.1003 0.0068  -0.0089 -0.0005 38  ALA   A O   
1025 O  O   B ALA   A 38  ? 0.1339 0.1331 0.1208 0.0011  -0.0071 0.0140  38  ALA   A O   
1026 C  CB  A ALA   A 38  ? 0.1325 0.1490 0.1038 -0.0190 -0.0068 0.0084  38  ALA   A CB  
1027 C  CB  B ALA   A 38  ? 0.1422 0.1507 0.1279 -0.0083 -0.0003 0.0054  38  ALA   A CB  
1038 N  N   . ALA   A 39  ? 0.1274 0.1339 0.1182 -0.0007 0.0006  0.0146  39  ALA   A N   
1039 C  CA  . ALA   A 39  ? 0.1290 0.1363 0.1103 -0.0021 0.0072  0.0079  39  ALA   A CA  
1040 C  C   . ALA   A 39  ? 0.1238 0.1322 0.1177 -0.0016 0.0032  0.0090  39  ALA   A C   
1041 O  O   . ALA   A 39  ? 0.1407 0.1354 0.1182 -0.0104 0.0055  0.0077  39  ALA   A O   
1042 C  CB  . ALA   A 39  ? 0.1341 0.1579 0.1342 -0.0052 -0.0051 0.0028  39  ALA   A CB  
1049 N  N   A ASN   A 40  ? 0.1337 0.1331 0.1345 -0.0129 0.0103  0.0030  40  ASN   A N   
1050 N  N   B ASN   A 40  ? 0.1296 0.1294 0.1040 -0.0067 0.0271  0.0151  40  ASN   A N   
1051 C  CA  A ASN   A 40  ? 0.1367 0.1333 0.1342 -0.0067 0.0080  0.0010  40  ASN   A CA  
1052 C  CA  B ASN   A 40  ? 0.1245 0.1258 0.1083 0.0023  0.0146  0.0098  40  ASN   A CA  
1053 C  C   A ASN   A 40  ? 0.1300 0.1223 0.1155 0.0008  0.0083  0.0188  40  ASN   A C   
1054 C  C   B ASN   A 40  ? 0.1303 0.1253 0.1075 0.0005  0.0176  0.0099  40  ASN   A C   
1055 O  O   A ASN   A 40  ? 0.1333 0.1222 0.1131 -0.0077 0.0089  0.0274  40  ASN   A O   
1056 O  O   B ASN   A 40  ? 0.1247 0.1266 0.1122 -0.0007 0.0222  0.0071  40  ASN   A O   
1057 C  CB  A ASN   A 40  ? 0.1438 0.1407 0.1349 0.0028  0.0011  0.0001  40  ASN   A CB  
1058 C  CB  B ASN   A 40  ? 0.1352 0.1269 0.1135 0.0041  0.0044  0.0114  40  ASN   A CB  
1059 C  CG  A ASN   A 40  ? 0.1551 0.1422 0.1548 0.0025  0.0077  0.0043  40  ASN   A CG  
1060 C  CG  B ASN   A 40  ? 0.1441 0.1279 0.1455 0.0020  -0.0034 0.0080  40  ASN   A CG  
1061 O  OD1 A ASN   A 40  ? 0.1669 0.1368 0.1550 -0.0016 -0.0042 0.0169  40  ASN   A OD1 
1062 O  OD1 B ASN   A 40  ? 0.1533 0.1244 0.1581 -0.0000 0.0043  0.0070  40  ASN   A OD1 
1063 N  ND2 A ASN   A 40  ? 0.1606 0.1515 0.1703 0.0069  0.0194  -0.0111 40  ASN   A ND2 
1064 N  ND2 B ASN   A 40  ? 0.1426 0.1380 0.1791 -0.0042 0.0109  -0.0023 40  ASN   A ND2 
1077 N  N   A VAL   A 41  ? 0.1313 0.1300 0.0972 -0.0002 0.0089  0.0233  41  VAL   A N   
1078 N  N   B VAL   A 41  ? 0.1287 0.1315 0.1214 -0.0001 0.0134  0.0100  41  VAL   A N   
1079 C  CA  A VAL   A 41  ? 0.1281 0.1353 0.1080 0.0013  0.0165  0.0205  41  VAL   A CA  
1080 C  CA  B VAL   A 41  ? 0.1319 0.1390 0.1240 -0.0016 0.0144  0.0108  41  VAL   A CA  
1081 C  C   A VAL   A 41  ? 0.1288 0.1324 0.1152 0.0044  0.0123  0.0191  41  VAL   A C   
1082 C  C   B VAL   A 41  ? 0.1270 0.1382 0.1171 0.0003  0.0225  0.0145  41  VAL   A C   
1083 O  O   A VAL   A 41  ? 0.1382 0.1223 0.1447 0.0020  -0.0032 0.0099  41  VAL   A O   
1084 O  O   B VAL   A 41  ? 0.1373 0.1340 0.1210 -0.0032 0.0066  0.0075  41  VAL   A O   
1085 C  CB  A VAL   A 41  ? 0.1288 0.1383 0.1000 -0.0016 0.0215  0.0124  41  VAL   A CB  
1086 C  CB  B VAL   A 41  ? 0.1373 0.1532 0.1374 -0.0001 0.0234  0.0158  41  VAL   A CB  
1087 C  CG1 A VAL   A 41  ? 0.1393 0.1409 0.1176 0.0036  0.0136  0.0058  41  VAL   A CG1 
1088 C  CG1 B VAL   A 41  ? 0.1539 0.1579 0.1482 -0.0034 0.0245  0.0067  41  VAL   A CG1 
1089 C  CG2 A VAL   A 41  ? 0.1318 0.1415 0.0932 -0.0044 0.0250  0.0131  41  VAL   A CG2 
1090 C  CG2 B VAL   A 41  ? 0.1388 0.1614 0.1454 0.0019  0.0095  0.0175  41  VAL   A CG2 
1109 N  N   A TYR   A 42  ? 0.1202 0.1246 0.1548 -0.0082 0.0155  0.0196  42  TYR   A N   
1110 N  N   B TYR   A 42  ? 0.1234 0.1368 0.1284 -0.0019 0.0264  0.0198  42  TYR   A N   
1111 C  CA  A TYR   A 42  ? 0.1240 0.1174 0.1457 -0.0082 0.0177  0.0209  42  TYR   A CA  
1112 C  CA  B TYR   A 42  ? 0.1263 0.1390 0.1439 -0.0028 0.0276  0.0226  42  TYR   A CA  
1113 C  C   A TYR   A 42  ? 0.1204 0.1166 0.1431 -0.0079 0.0209  0.0123  42  TYR   A C   
1114 C  C   B TYR   A 42  ? 0.1238 0.1415 0.1383 -0.0061 0.0215  0.0315  42  TYR   A C   
1115 O  O   A TYR   A 42  ? 0.1306 0.1170 0.1562 -0.0189 0.0145  0.0025  42  TYR   A O   
1116 O  O   B TYR   A 42  ? 0.1296 0.1482 0.1525 -0.0141 0.0183  0.0229  42  TYR   A O   
1117 C  CB  A TYR   A 42  ? 0.1385 0.1260 0.1446 -0.0073 0.0179  0.0290  42  TYR   A CB  
1118 C  CB  B TYR   A 42  ? 0.1407 0.1449 0.1506 0.0025  0.0253  0.0310  42  TYR   A CB  
1119 C  CG  A TYR   A 42  ? 0.1548 0.1337 0.1365 -0.0091 0.0174  0.0284  42  TYR   A CG  
1120 C  CG  B TYR   A 42  ? 0.1539 0.1519 0.1459 0.0092  0.0157  0.0415  42  TYR   A CG  
1121 C  CD1 A TYR   A 42  ? 0.1624 0.1501 0.1442 -0.0131 0.0187  0.0126  42  TYR   A CD1 
1122 C  CD1 B TYR   A 42  ? 0.1581 0.1577 0.1314 0.0021  0.0241  0.0520  42  TYR   A CD1 
1123 C  CD2 A TYR   A 42  ? 0.1609 0.1556 0.1499 0.0013  0.0148  0.0257  42  TYR   A CD2 
1124 C  CD2 B TYR   A 42  ? 0.1681 0.1715 0.1666 0.0149  0.0076  0.0387  42  TYR   A CD2 
1125 C  CE1 A TYR   A 42  ? 0.1719 0.1662 0.1486 -0.0090 0.0187  0.0131  42  TYR   A CE1 
1126 C  CE1 B TYR   A 42  ? 0.1602 0.1680 0.1357 0.0040  0.0304  0.0485  42  TYR   A CE1 
1127 C  CE2 A TYR   A 42  ? 0.1713 0.1691 0.1679 -0.0037 0.0092  0.0238  42  TYR   A CE2 
1128 C  CE2 B TYR   A 42  ? 0.1747 0.1794 0.1684 0.0148  0.0066  0.0419  42  TYR   A CE2 
1129 C  CZ  A TYR   A 42  ? 0.1788 0.1724 0.1498 -0.0088 0.0208  0.0177  42  TYR   A CZ  
1130 C  CZ  B TYR   A 42  ? 0.1728 0.1778 0.1520 0.0070  0.0230  0.0437  42  TYR   A CZ  
1131 O  OH  A TYR   A 42  ? 0.1950 0.1828 0.1661 -0.0092 0.0123  0.0049  42  TYR   A OH  
1132 O  OH  B TYR   A 42  ? 0.1763 0.1901 0.1690 0.0064  0.0224  0.0354  42  TYR   A OH  
1151 N  N   A LEU   A 43  ? 0.1262 0.1152 0.1334 -0.0076 0.0185  -0.0115 43  LEU   A N   
1152 N  N   B LEU   A 43  ? 0.1229 0.1396 0.1401 -0.0049 0.0046  0.0273  43  LEU   A N   
1153 C  CA  A LEU   A 43  ? 0.1167 0.1188 0.1311 -0.0103 0.0223  -0.0027 43  LEU   A CA  
1154 C  CA  B LEU   A 43  ? 0.1213 0.1361 0.1384 -0.0034 0.0017  0.0306  43  LEU   A CA  
1155 C  C   A LEU   A 43  ? 0.1212 0.1257 0.1309 -0.0026 0.0160  -0.0035 43  LEU   A C   
1156 C  C   B LEU   A 43  ? 0.1260 0.1374 0.1374 -0.0064 -0.0019 0.0247  43  LEU   A C   
1157 O  O   A LEU   A 43  ? 0.1336 0.1317 0.1560 0.0101  0.0017  -0.0121 43  LEU   A O   
1158 O  O   B LEU   A 43  ? 0.1342 0.1359 0.1377 -0.0106 -0.0120 0.0213  43  LEU   A O   
1159 C  CB  A LEU   A 43  ? 0.1305 0.1240 0.1467 -0.0107 0.0104  0.0043  43  LEU   A CB  
1160 C  CB  B LEU   A 43  ? 0.1201 0.1322 0.1532 -0.0026 0.0031  0.0312  43  LEU   A CB  
1161 C  CG  A LEU   A 43  ? 0.1365 0.1287 0.1537 -0.0041 0.0092  0.0053  43  LEU   A CG  
1162 C  CG  B LEU   A 43  ? 0.1155 0.1317 0.1659 0.0033  0.0067  0.0247  43  LEU   A CG  
1163 C  CD1 A LEU   A 43  ? 0.1404 0.1301 0.1671 -0.0075 -0.0066 0.0143  43  LEU   A CD1 
1164 C  CD1 B LEU   A 43  ? 0.1154 0.1361 0.1812 0.0017  0.0047  0.0283  43  LEU   A CD1 
1165 C  CD2 A LEU   A 43  ? 0.1427 0.1327 0.1501 -0.0008 0.0104  0.0124  43  LEU   A CD2 
1166 C  CD2 B LEU   A 43  ? 0.1293 0.1282 0.1679 -0.0017 0.0026  0.0372  43  LEU   A CD2 
1189 N  N   A LYS   A 44  ? 0.1340 0.1242 0.1229 -0.0054 0.0121  0.0007  44  LYS   A N   
1190 N  N   B LYS   A 44  ? 0.1327 0.1372 0.1323 0.0036  -0.0033 0.0200  44  LYS   A N   
1191 C  CA  A LYS   A 44  ? 0.1426 0.1283 0.1304 -0.0076 0.0218  0.0134  44  LYS   A CA  
1192 C  CA  B LYS   A 44  ? 0.1462 0.1400 0.1273 0.0084  -0.0011 0.0199  44  LYS   A CA  
1193 C  C   A LYS   A 44  ? 0.1306 0.1254 0.1362 -0.0006 0.0048  0.0087  44  LYS   A C   
1194 C  C   B LYS   A 44  ? 0.1372 0.1289 0.1123 0.0102  -0.0017 0.0172  44  LYS   A C   
1195 O  O   A LYS   A 44  ? 0.1269 0.1362 0.1636 0.0030  0.0066  0.0022  44  LYS   A O   
1196 O  O   B LYS   A 44  ? 0.1466 0.1406 0.1094 0.0072  0.0025  0.0077  44  LYS   A O   
1197 C  CB  A LYS   A 44  ? 0.1706 0.1443 0.1626 -0.0109 0.0364  0.0285  44  LYS   A CB  
1198 C  CB  B LYS   A 44  ? 0.1696 0.1607 0.1785 0.0139  0.0048  0.0186  44  LYS   A CB  
1199 C  CG  A LYS   A 44  ? 0.2013 0.1737 0.2181 -0.0167 0.0588  0.0448  44  LYS   A CG  
1200 C  CG  B LYS   A 44  ? 0.1925 0.1922 0.2451 0.0154  0.0131  0.0168  44  LYS   A CG  
1201 C  CD  A LYS   A 44  ? 0.2353 0.2202 0.3181 -0.0215 0.0542  0.0302  44  LYS   A CD  
1202 C  CD  B LYS   A 44  ? 0.2171 0.2289 0.3184 0.0067  0.0080  0.0132  44  LYS   A CD  
1203 C  CE  A LYS   A 44  ? 0.2548 0.2474 0.3814 -0.0207 0.0531  0.0220  44  LYS   A CE  
1204 C  CE  B LYS   A 44  ? 0.2267 0.2471 0.3586 0.0004  0.0046  0.0147  44  LYS   A CE  
1205 N  NZ  A LYS   A 44  ? 0.2630 0.2638 0.4118 -0.0250 0.0584  0.0240  44  LYS   A NZ  
1206 N  NZ  B LYS   A 44  ? 0.2352 0.2591 0.3805 -0.0110 0.0061  0.0186  44  LYS   A NZ  
1233 N  N   . HIS   A 45  ? 0.1275 0.1241 0.1259 -0.0005 -0.0003 0.0193  45  HIS   A N   
1234 C  CA  . HIS   A 45  ? 0.1246 0.1251 0.1297 -0.0056 -0.0005 0.0112  45  HIS   A CA  
1235 C  C   . HIS   A 45  ? 0.1322 0.1390 0.1442 0.0013  0.0008  0.0119  45  HIS   A C   
1236 O  O   . HIS   A 45  ? 0.1548 0.1515 0.1662 0.0221  -0.0023 -0.0071 45  HIS   A O   
1237 C  CB  . HIS   A 45  ? 0.1299 0.1242 0.1254 -0.0052 0.0052  0.0057  45  HIS   A CB  
1238 C  CG  . HIS   A 45  ? 0.1269 0.1200 0.1227 -0.0071 0.0023  0.0106  45  HIS   A CG  
1239 N  ND1 . HIS   A 45  ? 0.1226 0.1274 0.1348 -0.0075 -0.0017 0.0116  45  HIS   A ND1 
1240 C  CD2 . HIS   A 45  ? 0.1229 0.1321 0.1290 -0.0120 -0.0037 0.0147  45  HIS   A CD2 
1241 C  CE1 . HIS   A 45  ? 0.1213 0.1348 0.1231 -0.0058 0.0017  0.0190  45  HIS   A CE1 
1242 N  NE2 . HIS   A 45  ? 0.1230 0.1391 0.1215 -0.0051 -0.0032 0.0171  45  HIS   A NE2 
1251 N  N   A GLY   A 46  ? 0.1400 0.1405 0.1587 0.0077  -0.0158 0.0167  46  GLY   A N   
1252 N  N   B GLY   A 46  ? 0.1394 0.1382 0.1416 0.0038  -0.0102 0.0105  46  GLY   A N   
1253 C  CA  A GLY   A 46  ? 0.1426 0.1438 0.1724 0.0156  -0.0166 0.0294  46  GLY   A CA  
1254 C  CA  B GLY   A 46  ? 0.1399 0.1402 0.1372 0.0072  -0.0056 0.0135  46  GLY   A CA  
1255 C  C   A GLY   A 46  ? 0.1449 0.1438 0.1591 0.0240  -0.0205 0.0417  46  GLY   A C   
1256 C  C   B GLY   A 46  ? 0.1403 0.1430 0.1240 0.0147  -0.0132 0.0158  46  GLY   A C   
1257 O  O   A GLY   A 46  ? 0.1485 0.1519 0.1671 0.0244  -0.0448 0.0264  46  GLY   A O   
1258 O  O   B GLY   A 46  ? 0.1438 0.1497 0.1342 0.0124  -0.0213 0.0094  46  GLY   A O   
1265 N  N   A GLY   A 47  ? 0.1412 0.1467 0.1441 0.0189  -0.0084 0.0330  47  GLY   A N   
1266 N  N   B GLY   A 47  ? 0.1424 0.1460 0.1222 0.0111  -0.0016 0.0029  47  GLY   A N   
1267 C  CA  A GLY   A 47  ? 0.1474 0.1475 0.1254 0.0182  -0.0141 0.0183  47  GLY   A CA  
1268 C  CA  B GLY   A 47  ? 0.1423 0.1451 0.1219 0.0080  -0.0099 0.0046  47  GLY   A CA  
1269 C  C   A GLY   A 47  ? 0.1382 0.1403 0.1268 0.0156  -0.0164 0.0106  47  GLY   A C   
1270 C  C   B GLY   A 47  ? 0.1366 0.1364 0.1104 0.0079  -0.0074 0.0012  47  GLY   A C   
1271 O  O   A GLY   A 47  ? 0.1363 0.1361 0.1435 0.0244  -0.0174 0.0148  47  GLY   A O   
1272 O  O   B GLY   A 47  ? 0.1368 0.1363 0.1180 0.0165  -0.0084 0.0148  47  GLY   A O   
1279 N  N   A GLY   A 48  ? 0.1372 0.1436 0.1278 0.0178  -0.0186 -0.0040 48  GLY   A N   
1280 N  N   B GLY   A 48  ? 0.1361 0.1402 0.1193 0.0057  0.0001  0.0073  48  GLY   A N   
1281 C  CA  A GLY   A 48  ? 0.1379 0.1412 0.1522 0.0083  -0.0150 -0.0036 48  GLY   A CA  
1282 C  CA  B GLY   A 48  ? 0.1362 0.1306 0.1168 0.0063  -0.0040 0.0025  48  GLY   A CA  
1283 C  C   A GLY   A 48  ? 0.1383 0.1385 0.1372 -0.0001 -0.0072 0.0098  48  GLY   A C   
1284 C  C   B GLY   A 48  ? 0.1328 0.1295 0.1223 0.0018  -0.0005 0.0031  48  GLY   A C   
1285 O  O   A GLY   A 48  ? 0.1543 0.1402 0.1185 -0.0027 -0.0000 0.0134  48  GLY   A O   
1286 O  O   B GLY   A 48  ? 0.1495 0.1241 0.1177 0.0013  0.0089  0.0007  48  GLY   A O   
1293 N  N   A VAL   A 49  ? 0.1352 0.1275 0.1515 -0.0094 -0.0062 0.0103  49  VAL   A N   
1294 N  N   B VAL   A 49  ? 0.1191 0.1252 0.1311 -0.0016 -0.0071 0.0009  49  VAL   A N   
1295 C  CA  A VAL   A 49  ? 0.1418 0.1256 0.1443 -0.0119 0.0058  0.0092  49  VAL   A CA  
1296 C  CA  B VAL   A 49  ? 0.1090 0.1317 0.1238 0.0034  -0.0023 0.0096  49  VAL   A CA  
1297 C  C   A VAL   A 49  ? 0.1407 0.1256 0.1210 -0.0103 0.0096  0.0103  49  VAL   A C   
1298 C  C   B VAL   A 49  ? 0.1205 0.1229 0.0951 0.0146  0.0047  0.0075  49  VAL   A C   
1299 O  O   A VAL   A 49  ? 0.1389 0.1301 0.1346 -0.0184 0.0128  0.0027  49  VAL   A O   
1300 O  O   B VAL   A 49  ? 0.1318 0.1280 0.0884 0.0140  0.0111  0.0075  49  VAL   A O   
1301 C  CB  A VAL   A 49  ? 0.1481 0.1244 0.1519 -0.0103 0.0092  -0.0059 49  VAL   A CB  
1302 C  CB  B VAL   A 49  ? 0.0992 0.1296 0.1308 0.0035  -0.0029 0.0075  49  VAL   A CB  
1303 C  CG1 A VAL   A 49  ? 0.1425 0.1158 0.1589 -0.0017 0.0186  -0.0065 49  VAL   A CG1 
1304 C  CG1 B VAL   A 49  ? 0.0995 0.1248 0.1322 0.0093  0.0055  0.0056  49  VAL   A CG1 
1305 C  CG2 A VAL   A 49  ? 0.1598 0.1321 0.2035 -0.0246 0.0047  -0.0006 49  VAL   A CG2 
1306 C  CG2 B VAL   A 49  ? 0.0986 0.1343 0.1359 0.0044  0.0071  0.0072  49  VAL   A CG2 
1325 N  N   A ALA   A 50  ? 0.1316 0.1294 0.1079 -0.0207 -0.0096 0.0052  50  ALA   A N   
1326 N  N   B ALA   A 50  ? 0.1236 0.1168 0.0971 0.0221  -0.0009 0.0049  50  ALA   A N   
1327 C  CA  A ALA   A 50  ? 0.1244 0.1351 0.1018 -0.0343 -0.0106 0.0110  50  ALA   A CA  
1328 C  CA  B ALA   A 50  ? 0.1304 0.1193 0.1002 0.0212  -0.0121 0.0109  50  ALA   A CA  
1329 C  C   A ALA   A 50  ? 0.1236 0.1370 0.1009 -0.0365 -0.0034 0.0066  50  ALA   A C   
1330 C  C   B ALA   A 50  ? 0.1339 0.1172 0.1035 0.0245  -0.0024 0.0027  50  ALA   A C   
1331 O  O   A ALA   A 50  ? 0.1234 0.1403 0.1099 -0.0350 -0.0061 0.0064  50  ALA   A O   
1332 O  O   B ALA   A 50  ? 0.1326 0.1163 0.1155 0.0366  0.0017  0.0075  50  ALA   A O   
1333 C  CB  A ALA   A 50  ? 0.1214 0.1395 0.1075 -0.0335 0.0031  0.0046  50  ALA   A CB  
1334 C  CB  B ALA   A 50  ? 0.1346 0.1149 0.1006 0.0292  -0.0061 0.0014  50  ALA   A CB  
1345 N  N   A GLY   A 51  ? 0.1297 0.1241 0.1157 -0.0208 -0.0040 0.0090  51  GLY   A N   
1346 N  N   B GLY   A 51  ? 0.1340 0.1122 0.1126 0.0261  -0.0072 0.0027  51  GLY   A N   
1347 C  CA  A GLY   A 51  ? 0.1424 0.1227 0.1203 -0.0085 -0.0068 0.0077  51  GLY   A CA  
1348 C  CA  B GLY   A 51  ? 0.1412 0.1133 0.1139 0.0236  -0.0067 0.0010  51  GLY   A CA  
1349 C  C   A GLY   A 51  ? 0.1284 0.1275 0.1178 -0.0029 -0.0083 -0.0007 51  GLY   A C   
1350 C  C   B GLY   A 51  ? 0.1315 0.1238 0.1137 0.0158  -0.0081 -0.0049 51  GLY   A C   
1351 O  O   A GLY   A 51  ? 0.1314 0.1376 0.1328 -0.0082 -0.0076 -0.0009 51  GLY   A O   
1352 O  O   B GLY   A 51  ? 0.1349 0.1338 0.1241 0.0133  -0.0119 -0.0073 51  GLY   A O   
1359 N  N   . ALA   A 52  ? 0.1344 0.1316 0.1111 -0.0015 -0.0030 -0.0081 52  ALA   A N   
1360 C  CA  . ALA   A 52  ? 0.1325 0.1449 0.1278 -0.0038 -0.0015 -0.0100 52  ALA   A CA  
1361 C  C   . ALA   A 52  ? 0.1242 0.1446 0.1071 -0.0085 0.0016  -0.0010 52  ALA   A C   
1362 O  O   . ALA   A 52  ? 0.1345 0.1504 0.1272 -0.0033 0.0040  -0.0140 52  ALA   A O   
1363 C  CB  . ALA   A 52  ? 0.1415 0.1710 0.1391 -0.0103 -0.0015 0.0010  52  ALA   A CB  
1370 N  N   A LEU   A 53  ? 0.1267 0.1401 0.1141 -0.0086 0.0001  -0.0033 53  LEU   A N   
1371 N  N   B LEU   A 53  ? 0.1225 0.1370 0.1126 -0.0031 -0.0030 -0.0010 53  LEU   A N   
1372 C  CA  A LEU   A 53  ? 0.1334 0.1494 0.1111 -0.0061 0.0011  0.0065  53  LEU   A CA  
1373 C  CA  B LEU   A 53  ? 0.1244 0.1403 0.1081 0.0038  -0.0067 0.0074  53  LEU   A CA  
1374 C  C   A LEU   A 53  ? 0.1358 0.1502 0.0946 -0.0018 0.0049  0.0036  53  LEU   A C   
1375 C  C   B LEU   A 53  ? 0.1260 0.1402 0.1000 0.0132  -0.0048 0.0074  53  LEU   A C   
1376 O  O   A LEU   A 53  ? 0.1454 0.1574 0.1066 -0.0128 0.0028  0.0030  53  LEU   A O   
1377 O  O   B LEU   A 53  ? 0.1341 0.1453 0.1109 0.0067  -0.0112 0.0111  53  LEU   A O   
1378 C  CB  A LEU   A 53  ? 0.1386 0.1482 0.1250 -0.0087 0.0019  0.0171  53  LEU   A CB  
1379 C  CB  B LEU   A 53  ? 0.1250 0.1377 0.1161 -0.0006 -0.0098 0.0127  53  LEU   A CB  
1380 C  CG  A LEU   A 53  ? 0.1374 0.1471 0.1316 -0.0102 0.0010  0.0154  53  LEU   A CG  
1381 C  CG  B LEU   A 53  ? 0.1230 0.1366 0.1163 -0.0014 -0.0077 0.0146  53  LEU   A CG  
1382 C  CD1 A LEU   A 53  ? 0.1353 0.1551 0.1299 -0.0033 0.0095  0.0206  53  LEU   A CD1 
1383 C  CD1 B LEU   A 53  ? 0.1281 0.1444 0.1293 -0.0021 -0.0004 0.0099  53  LEU   A CD1 
1384 C  CD2 A LEU   A 53  ? 0.1425 0.1568 0.1354 -0.0136 -0.0023 0.0167  53  LEU   A CD2 
1385 C  CD2 B LEU   A 53  ? 0.1218 0.1378 0.1064 0.0031  -0.0051 0.0076  53  LEU   A CD2 
1408 N  N   A ASN   A 54  ? 0.1300 0.1414 0.1065 -0.0114 -0.0032 0.0044  54  ASN   A N   
1409 N  N   B ASN   A 54  ? 0.1230 0.1374 0.1078 0.0122  -0.0059 0.0046  54  ASN   A N   
1410 C  CA  A ASN   A 54  ? 0.1219 0.1348 0.1147 -0.0117 -0.0069 0.0006  54  ASN   A CA  
1411 C  CA  B ASN   A 54  ? 0.1187 0.1383 0.1076 0.0126  -0.0058 0.0004  54  ASN   A CA  
1412 C  C   A ASN   A 54  ? 0.1290 0.1355 0.1092 -0.0085 0.0012  0.0018  54  ASN   A C   
1413 C  C   B ASN   A 54  ? 0.1258 0.1383 0.1113 0.0037  -0.0008 0.0006  54  ASN   A C   
1414 O  O   A ASN   A 54  ? 0.1300 0.1441 0.1241 -0.0100 -0.0078 -0.0115 54  ASN   A O   
1415 O  O   B ASN   A 54  ? 0.1242 0.1482 0.1286 0.0007  -0.0051 -0.0061 54  ASN   A O   
1416 C  CB  A ASN   A 54  ? 0.1224 0.1295 0.1323 -0.0182 -0.0162 -0.0013 54  ASN   A CB  
1417 C  CB  B ASN   A 54  ? 0.1201 0.1413 0.1108 0.0168  -0.0066 -0.0085 54  ASN   A CB  
1418 C  CG  A ASN   A 54  ? 0.1223 0.1340 0.1451 -0.0147 -0.0061 0.0132  54  ASN   A CG  
1419 C  CG  B ASN   A 54  ? 0.1196 0.1383 0.1023 0.0204  -0.0032 -0.0177 54  ASN   A CG  
1420 O  OD1 A ASN   A 54  ? 0.1194 0.1328 0.1495 -0.0169 -0.0132 0.0293  54  ASN   A OD1 
1421 O  OD1 B ASN   A 54  ? 0.1171 0.1330 0.1033 0.0110  -0.0063 -0.0370 54  ASN   A OD1 
1422 N  ND2 A ASN   A 54  ? 0.1275 0.1409 0.1696 -0.0158 -0.0134 0.0184  54  ASN   A ND2 
1423 N  ND2 B ASN   A 54  ? 0.1265 0.1423 0.1184 0.0148  -0.0154 -0.0010 54  ASN   A ND2 
1436 N  N   . LYS   A 55  ? 0.1298 0.1366 0.1188 -0.0037 -0.0040 -0.0056 55  LYS   A N   
1437 C  CA  . LYS   A 55  ? 0.1389 0.1465 0.1286 0.0096  -0.0077 -0.0100 55  LYS   A CA  
1438 C  C   . LYS   A 55  ? 0.1337 0.1530 0.1257 -0.0016 -0.0049 -0.0169 55  LYS   A C   
1439 O  O   . LYS   A 55  ? 0.1423 0.1665 0.1350 -0.0003 -0.0063 -0.0217 55  LYS   A O   
1440 C  CB  . LYS   A 55  ? 0.1470 0.1555 0.1498 0.0158  -0.0116 -0.0187 55  LYS   A CB  
1441 C  CG  . LYS   A 55  ? 0.1617 0.1869 0.1568 0.0300  -0.0226 -0.0237 55  LYS   A CG  
1442 C  CD  . LYS   A 55  ? 0.1792 0.2217 0.1665 0.0448  -0.0134 -0.0256 55  LYS   A CD  
1443 C  CE  . LYS   A 55  ? 0.2018 0.2553 0.1984 0.0540  -0.0191 -0.0339 55  LYS   A CE  
1444 N  NZ  . LYS   A 55  ? 0.2085 0.2688 0.2127 0.0613  -0.0243 -0.0289 55  LYS   A NZ  
1459 N  N   . ALA   A 56  ? 0.1401 0.1571 0.1295 -0.0115 0.0033  -0.0156 56  ALA   A N   
1460 C  CA  . ALA   A 56  ? 0.1478 0.1740 0.1284 -0.0126 0.0092  -0.0151 56  ALA   A CA  
1461 C  C   . ALA   A 56  ? 0.1521 0.1839 0.1023 -0.0121 0.0069  -0.0190 56  ALA   A C   
1462 O  O   . ALA   A 56  ? 0.1568 0.2220 0.1205 -0.0026 0.0089  -0.0179 56  ALA   A O   
1463 C  CB  . ALA   A 56  ? 0.1550 0.1959 0.1464 -0.0250 0.0036  -0.0049 56  ALA   A CB  
1469 N  N   . THR   A 57  ? 0.1427 0.1669 0.1120 -0.0113 0.0022  -0.0163 57  THR   A N   
1470 C  CA  . THR   A 57  ? 0.1501 0.1651 0.1183 -0.0107 -0.0076 -0.0078 57  THR   A CA  
1471 C  C   . THR   A 57  ? 0.1463 0.1687 0.1212 -0.0110 -0.0052 -0.0146 57  THR   A C   
1472 O  O   . THR   A 57  ? 0.1449 0.1784 0.1366 -0.0145 -0.0119 -0.0211 57  THR   A O   
1473 C  CB  . THR   A 57  ? 0.1468 0.1632 0.1258 -0.0067 -0.0062 -0.0092 57  THR   A CB  
1474 O  OG1 . THR   A 57  ? 0.1358 0.1560 0.1184 -0.0054 -0.0009 -0.0056 57  THR   A OG1 
1475 C  CG2 . THR   A 57  ? 0.1522 0.1621 0.1198 -0.0066 -0.0043 0.0022  57  THR   A CG2 
1483 N  N   . ASN   A 58  ? 0.1452 0.1668 0.1375 -0.0132 0.0015  -0.0199 58  ASN   A N   
1484 C  CA  . ASN   A 58  ? 0.1618 0.1619 0.1636 -0.0198 0.0115  -0.0323 58  ASN   A CA  
1485 C  C   . ASN   A 58  ? 0.1443 0.1500 0.1560 -0.0100 -0.0049 -0.0236 58  ASN   A C   
1486 O  O   . ASN   A 58  ? 0.1435 0.1628 0.1686 -0.0153 -0.0091 -0.0272 58  ASN   A O   
1487 C  CB  . ASN   A 58  ? 0.2158 0.1856 0.1994 -0.0238 0.0340  -0.0542 58  ASN   A CB  
1488 C  CG  . ASN   A 58  ? 0.2677 0.2095 0.2721 -0.0232 0.0358  -0.0450 58  ASN   A CG  
1489 O  OD1 . ASN   A 58  ? 0.2996 0.2037 0.3174 0.0141  0.0686  -0.0317 58  ASN   A OD1 
1490 N  ND2 . ASN   A 58  ? 0.2846 0.2235 0.3101 -0.0321 0.0248  -0.0405 58  ASN   A ND2 
1497 N  N   . ASN   A 59  ? 0.1342 0.1401 0.1382 -0.0046 -0.0089 -0.0155 59  ASN   A N   
1498 C  CA  . ASN   A 59  ? 0.1355 0.1295 0.1366 -0.0017 -0.0079 -0.0063 59  ASN   A CA  
1499 C  C   . ASN   A 59  ? 0.1336 0.1316 0.1308 -0.0055 -0.0093 -0.0021 59  ASN   A C   
1500 O  O   . ASN   A 59  ? 0.1369 0.1398 0.1401 -0.0085 0.0012  -0.0010 59  ASN   A O   
1501 C  CB  . ASN   A 59  ? 0.1400 0.1303 0.1500 0.0004  -0.0206 -0.0158 59  ASN   A CB  
1502 C  CG  . ASN   A 59  ? 0.1434 0.1385 0.1493 -0.0049 -0.0296 -0.0012 59  ASN   A CG  
1503 O  OD1 . ASN   A 59  ? 0.1506 0.1441 0.1425 -0.0133 -0.0219 0.0032  59  ASN   A OD1 
1504 N  ND2 . ASN   A 59  ? 0.1475 0.1389 0.1672 -0.0133 -0.0169 -0.0010 59  ASN   A ND2 
1511 N  N   . ALA   A 60  ? 0.1224 0.1394 0.1395 -0.0030 -0.0061 -0.0007 60  ALA   A N   
1512 C  CA  . ALA   A 60  ? 0.1287 0.1421 0.1413 -0.0076 -0.0088 -0.0018 60  ALA   A CA  
1513 C  C   . ALA   A 60  ? 0.1296 0.1394 0.1432 -0.0106 -0.0004 0.0024  60  ALA   A C   
1514 O  O   . ALA   A 60  ? 0.1252 0.1364 0.1644 -0.0062 -0.0077 -0.0054 60  ALA   A O   
1515 C  CB  . ALA   A 60  ? 0.1398 0.1564 0.1514 -0.0046 -0.0151 -0.0153 60  ALA   A CB  
1521 N  N   . MET   A 61  ? 0.1245 0.1364 0.1283 -0.0041 -0.0020 -0.0026 61  MET   A N   
1522 C  CA  . MET   A 61  ? 0.1282 0.1315 0.1292 -0.0027 0.0010  0.0039  61  MET   A CA  
1523 C  C   . MET   A 61  ? 0.1242 0.1238 0.1358 -0.0075 -0.0092 -0.0018 61  MET   A C   
1524 O  O   . MET   A 61  ? 0.1308 0.1236 0.1491 -0.0035 0.0019  0.0055  61  MET   A O   
1525 C  CB  . MET   A 61  ? 0.1316 0.1351 0.1186 -0.0053 -0.0036 -0.0024 61  MET   A CB  
1526 C  CG  . MET   A 61  ? 0.1322 0.1454 0.1392 0.0000  -0.0060 0.0036  61  MET   A CG  
1527 S  SD  . MET   A 61  ? 0.1349 0.1401 0.1691 -0.0113 -0.0013 -0.0126 61  MET   A SD  
1528 C  CE  . MET   A 61  ? 0.1532 0.1576 0.2057 -0.0133 0.0201  -0.0104 61  MET   A CE  
1538 N  N   . GLN   A 62  ? 0.1187 0.1301 0.1319 -0.0041 -0.0064 -0.0010 62  GLN   A N   
1539 C  CA  . GLN   A 62  ? 0.1287 0.1233 0.1387 -0.0080 -0.0016 0.0029  62  GLN   A CA  
1540 C  C   . GLN   A 62  ? 0.1307 0.1165 0.1457 -0.0034 0.0017  0.0046  62  GLN   A C   
1541 O  O   . GLN   A 62  ? 0.1352 0.1340 0.1442 -0.0014 0.0032  -0.0042 62  GLN   A O   
1542 C  CB  . GLN   A 62  ? 0.1292 0.1270 0.1399 -0.0039 -0.0012 -0.0022 62  GLN   A CB  
1543 C  CG  . GLN   A 62  ? 0.1339 0.1230 0.1407 -0.0033 -0.0047 0.0125  62  GLN   A CG  
1544 C  CD  . GLN   A 62  ? 0.1381 0.1225 0.1376 -0.0091 0.0026  0.0120  62  GLN   A CD  
1545 O  OE1 . GLN   A 62  ? 0.1446 0.1371 0.1345 -0.0104 -0.0016 0.0054  62  GLN   A OE1 
1546 N  NE2 . GLN   A 62  ? 0.1416 0.1260 0.1517 -0.0025 -0.0003 -0.0035 62  GLN   A NE2 
1555 N  N   . VAL   A 63  ? 0.1255 0.1220 0.1679 -0.0080 0.0003  -0.0095 63  VAL   A N   
1556 C  CA  . VAL   A 63  ? 0.1273 0.1359 0.1891 -0.0139 -0.0012 -0.0124 63  VAL   A CA  
1557 C  C   . VAL   A 63  ? 0.1200 0.1353 0.1688 -0.0164 -0.0023 -0.0087 63  VAL   A C   
1558 O  O   . VAL   A 63  ? 0.1232 0.1423 0.1826 -0.0171 -0.0055 -0.0088 63  VAL   A O   
1559 C  CB  . VAL   A 63  ? 0.1410 0.1546 0.2129 -0.0166 -0.0043 -0.0305 63  VAL   A CB  
1560 C  CG1 . VAL   A 63  ? 0.1553 0.1700 0.2569 -0.0189 -0.0098 -0.0564 63  VAL   A CG1 
1561 C  CG2 . VAL   A 63  ? 0.1476 0.1449 0.2273 -0.0085 0.0073  -0.0305 63  VAL   A CG2 
1571 N  N   . GLU   A 64  ? 0.1229 0.1390 0.1486 -0.0064 0.0004  -0.0109 64  GLU   A N   
1572 C  CA  . GLU   A 64  ? 0.1231 0.1393 0.1604 -0.0090 -0.0026 0.0039  64  GLU   A CA  
1573 C  C   . GLU   A 64  ? 0.1178 0.1316 0.1564 -0.0097 0.0015  0.0015  64  GLU   A C   
1574 O  O   . GLU   A 64  ? 0.1322 0.1390 0.1629 -0.0002 0.0016  -0.0017 64  GLU   A O   
1575 C  CB  . GLU   A 64  ? 0.1283 0.1462 0.1535 -0.0118 -0.0015 -0.0037 64  GLU   A CB  
1576 C  CG  . GLU   A 64  ? 0.1386 0.1537 0.1693 -0.0139 0.0048  -0.0017 64  GLU   A CG  
1577 C  CD  . GLU   A 64  ? 0.1473 0.1656 0.1815 -0.0135 -0.0000 -0.0033 64  GLU   A CD  
1578 O  OE1 . GLU   A 64  ? 0.1470 0.1747 0.1931 -0.0239 0.0099  -0.0023 64  GLU   A OE1 
1579 O  OE2 . GLU   A 64  ? 0.1684 0.1574 0.1746 -0.0219 -0.0100 0.0052  64  GLU   A OE2 
1586 N  N   . SER   A 65  ? 0.1162 0.1372 0.1422 -0.0025 0.0044  0.0037  65  SER   A N   
1587 C  CA  . SER   A 65  ? 0.1193 0.1348 0.1466 -0.0028 -0.0084 -0.0037 65  SER   A CA  
1588 C  C   . SER   A 65  ? 0.1265 0.1358 0.1444 -0.0088 0.0004  -0.0030 65  SER   A C   
1589 O  O   . SER   A 65  ? 0.1357 0.1349 0.1730 -0.0016 0.0179  -0.0013 65  SER   A O   
1590 C  CB  . SER   A 65  ? 0.1224 0.1289 0.1478 -0.0077 0.0043  0.0032  65  SER   A CB  
1591 O  OG  . SER   A 65  ? 0.1210 0.1436 0.1498 -0.0082 -0.0026 0.0088  65  SER   A OG  
1597 N  N   . ASP   A 66  ? 0.1279 0.1320 0.1525 -0.0113 0.0124  0.0052  66  ASP   A N   
1598 C  CA  . ASP   A 66  ? 0.1346 0.1425 0.1639 -0.0051 0.0054  0.0131  66  ASP   A CA  
1599 C  C   . ASP   A 66  ? 0.1351 0.1372 0.1746 -0.0048 0.0068  0.0188  66  ASP   A C   
1600 O  O   . ASP   A 66  ? 0.1398 0.1501 0.2000 -0.0055 0.0243  0.0268  66  ASP   A O   
1601 C  CB  . ASP   A 66  ? 0.1446 0.1550 0.1873 0.0058  0.0133  0.0313  66  ASP   A CB  
1602 C  CG  . ASP   A 66  ? 0.1639 0.1704 0.2180 0.0003  0.0070  0.0462  66  ASP   A CG  
1603 O  OD1 . ASP   A 66  ? 0.1608 0.1954 0.1982 -0.0108 -0.0056 0.0532  66  ASP   A OD1 
1604 O  OD2 . ASP   A 66  ? 0.1807 0.1839 0.2954 0.0161  -0.0096 0.0241  66  ASP   A OD2 
1609 N  N   . ASP   A 67  ? 0.1321 0.1351 0.1881 -0.0024 0.0041  0.0189  67  ASP   A N   
1610 C  CA  . ASP   A 67  ? 0.1267 0.1598 0.2021 -0.0039 0.0008  0.0209  67  ASP   A CA  
1611 C  C   . ASP   A 67  ? 0.1275 0.1582 0.1928 0.0006  0.0105  0.0203  67  ASP   A C   
1612 O  O   . ASP   A 67  ? 0.1279 0.1628 0.2092 -0.0010 0.0231  0.0257  67  ASP   A O   
1613 C  CB  . ASP   A 67  ? 0.1380 0.1662 0.2338 -0.0082 -0.0119 0.0328  67  ASP   A CB  
1614 C  CG  . ASP   A 67  ? 0.1366 0.1786 0.2691 -0.0121 -0.0227 0.0403  67  ASP   A CG  
1615 O  OD1 . ASP   A 67  ? 0.1364 0.1942 0.3614 -0.0143 -0.0277 0.0542  67  ASP   A OD1 
1616 O  OD2 . ASP   A 67  ? 0.1443 0.1831 0.2485 0.0001  -0.0154 0.0298  67  ASP   A OD2 
1621 N  N   . TYR   A 68  ? 0.1324 0.1518 0.1929 0.0015  0.0185  0.0271  68  TYR   A N   
1622 C  CA  . TYR   A 68  ? 0.1455 0.1482 0.1909 0.0008  0.0221  0.0223  68  TYR   A CA  
1623 C  C   . TYR   A 68  ? 0.1346 0.1433 0.1891 -0.0023 0.0268  0.0174  68  TYR   A C   
1624 O  O   . TYR   A 68  ? 0.1400 0.1468 0.1987 0.0075  0.0283  0.0198  68  TYR   A O   
1625 C  CB  . TYR   A 68  ? 0.1490 0.1394 0.1914 -0.0001 0.0441  0.0245  68  TYR   A CB  
1626 C  CG  . TYR   A 68  ? 0.1549 0.1543 0.2170 0.0016  0.0531  0.0271  68  TYR   A CG  
1627 C  CD1 . TYR   A 68  ? 0.1652 0.1659 0.2395 -0.0169 0.0439  -0.0031 68  TYR   A CD1 
1628 C  CD2 . TYR   A 68  ? 0.1752 0.1584 0.2498 0.0108  0.0470  0.0409  68  TYR   A CD2 
1629 C  CE1 . TYR   A 68  ? 0.1660 0.1725 0.2732 -0.0123 0.0462  -0.0048 68  TYR   A CE1 
1630 C  CE2 . TYR   A 68  ? 0.1749 0.1620 0.2651 0.0064  0.0585  0.0232  68  TYR   A CE2 
1631 C  CZ  . TYR   A 68  ? 0.1756 0.1670 0.2825 -0.0122 0.0476  0.0014  68  TYR   A CZ  
1632 O  OH  . TYR   A 68  ? 0.2007 0.1648 0.3055 -0.0049 0.0241  -0.0219 68  TYR   A OH  
1642 N  N   . ILE   A 69  ? 0.1273 0.1369 0.1812 0.0023  0.0236  0.0215  69  ILE   A N   
1643 C  CA  . ILE   A 69  ? 0.1355 0.1352 0.1645 0.0038  0.0190  0.0133  69  ILE   A CA  
1644 C  C   . ILE   A 69  ? 0.1397 0.1431 0.1565 0.0006  0.0208  0.0187  69  ILE   A C   
1645 O  O   . ILE   A 69  ? 0.1451 0.1542 0.1639 -0.0006 0.0252  0.0171  69  ILE   A O   
1646 C  CB  . ILE   A 69  ? 0.1454 0.1583 0.1814 0.0020  0.0140  0.0014  69  ILE   A CB  
1647 C  CG1 . ILE   A 69  ? 0.1476 0.1642 0.1766 0.0045  0.0157  -0.0133 69  ILE   A CG1 
1648 C  CG2 . ILE   A 69  ? 0.1640 0.1761 0.1880 0.0089  0.0017  -0.0020 69  ILE   A CG2 
1649 C  CD1 . ILE   A 69  ? 0.1484 0.1720 0.1865 -0.0055 0.0138  -0.0125 69  ILE   A CD1 
1661 N  N   . ALA   A 70  ? 0.1431 0.1458 0.1725 -0.0062 0.0171  0.0184  70  ALA   A N   
1662 C  CA  . ALA   A 70  ? 0.1487 0.1552 0.1913 -0.0176 0.0250  0.0237  70  ALA   A CA  
1663 C  C   . ALA   A 70  ? 0.1491 0.1654 0.1934 -0.0074 0.0293  0.0219  70  ALA   A C   
1664 O  O   . ALA   A 70  ? 0.1616 0.2020 0.2124 0.0083  0.0492  0.0387  70  ALA   A O   
1665 C  CB  . ALA   A 70  ? 0.1582 0.1557 0.2147 -0.0220 0.0260  0.0273  70  ALA   A CB  
1671 N  N   . THR   A 71  ? 0.1404 0.1640 0.1828 0.0012  0.0234  0.0290  71  THR   A N   
1672 C  CA  . THR   A 71  ? 0.1526 0.1834 0.2268 0.0128  0.0238  0.0291  71  THR   A CA  
1673 C  C   . THR   A 71  ? 0.1478 0.1729 0.2403 0.0175  0.0363  0.0272  71  THR   A C   
1674 O  O   . THR   A 71  ? 0.1569 0.1976 0.2891 0.0149  0.0450  -0.0017 71  THR   A O   
1675 C  CB  . THR   A 71  ? 0.1794 0.2035 0.2498 0.0140  -0.0103 0.0415  71  THR   A CB  
1676 O  OG1 . THR   A 71  ? 0.2058 0.2230 0.2478 0.0042  -0.0321 0.0330  71  THR   A OG1 
1677 C  CG2 . THR   A 71  ? 0.1915 0.2227 0.2856 0.0217  -0.0185 0.0530  71  THR   A CG2 
1685 N  N   . ASN   A 72  ? 0.1473 0.1617 0.2237 0.0176  0.0265  0.0317  72  ASN   A N   
1686 C  CA  . ASN   A 72  ? 0.1548 0.1637 0.2243 0.0189  0.0347  0.0317  72  ASN   A CA  
1687 C  C   . ASN   A 72  ? 0.1603 0.1624 0.2178 0.0138  0.0477  0.0140  72  ASN   A C   
1688 O  O   . ASN   A 72  ? 0.1812 0.1606 0.2398 0.0143  0.0473  0.0080  72  ASN   A O   
1689 C  CB  . ASN   A 72  ? 0.1688 0.1709 0.2250 0.0166  0.0387  0.0365  72  ASN   A CB  
1690 C  CG  . ASN   A 72  ? 0.1911 0.1820 0.2284 0.0239  0.0407  0.0373  72  ASN   A CG  
1691 O  OD1 . ASN   A 72  ? 0.2091 0.2167 0.2478 0.0238  0.0461  0.0324  72  ASN   A OD1 
1692 N  ND2 . ASN   A 72  ? 0.2046 0.1763 0.2401 0.0525  0.0210  0.0200  72  ASN   A ND2 
1699 N  N   . GLY   A 73  ? 0.1605 0.1576 0.1949 0.0067  0.0459  0.0112  73  GLY   A N   
1700 C  CA  . GLY   A 73  ? 0.1660 0.1549 0.1852 -0.0016 0.0513  0.0106  73  GLY   A CA  
1701 C  C   . GLY   A 73  ? 0.1670 0.1464 0.1727 -0.0018 0.0578  0.0166  73  GLY   A C   
1702 O  O   . GLY   A 73  ? 0.1691 0.1498 0.1867 0.0098  0.0435  0.0244  73  GLY   A O   
1706 N  N   . PRO   A 74  ? 0.1785 0.1501 0.1769 -0.0160 0.0517  0.0149  74  PRO   A N   
1707 C  CA  . PRO   A 74  ? 0.1700 0.1442 0.1944 -0.0088 0.0430  0.0124  74  PRO   A CA  
1708 C  C   . PRO   A 74  ? 0.1683 0.1304 0.1825 -0.0024 0.0329  0.0071  74  PRO   A C   
1709 O  O   . PRO   A 74  ? 0.1748 0.1340 0.2021 0.0003  0.0383  -0.0015 74  PRO   A O   
1710 C  CB  . PRO   A 74  ? 0.1829 0.1677 0.2152 -0.0063 0.0417  0.0222  74  PRO   A CB  
1711 C  CG  . PRO   A 74  ? 0.2082 0.1993 0.2525 -0.0215 0.0318  0.0034  74  PRO   A CG  
1712 C  CD  . PRO   A 74  ? 0.1894 0.1779 0.2015 -0.0267 0.0406  -0.0005 74  PRO   A CD  
1720 N  N   . LEU   A 75  ? 0.1649 0.1283 0.1536 -0.0050 0.0194  0.0038  75  LEU   A N   
1721 C  CA  . LEU   A 75  ? 0.1659 0.1278 0.1410 -0.0018 0.0114  0.0123  75  LEU   A CA  
1722 C  C   . LEU   A 75  ? 0.1778 0.1386 0.1335 0.0051  0.0128  0.0112  75  LEU   A C   
1723 O  O   . LEU   A 75  ? 0.2151 0.1565 0.1421 0.0145  0.0028  0.0106  75  LEU   A O   
1724 C  CB  . LEU   A 75  ? 0.1691 0.1280 0.1300 -0.0082 0.0107  0.0225  75  LEU   A CB  
1725 C  CG  . LEU   A 75  ? 0.1846 0.1592 0.1435 -0.0368 0.0077  0.0165  75  LEU   A CG  
1726 C  CD1 . LEU   A 75  ? 0.1971 0.2081 0.1614 -0.0375 0.0069  0.0040  75  LEU   A CD1 
1727 C  CD2 . LEU   A 75  ? 0.2171 0.1961 0.2082 -0.0127 0.0053  0.0205  75  LEU   A CD2 
1739 N  N   . LYS   A 76  ? 0.1750 0.1362 0.1482 -0.0026 0.0187  0.0006  76  LYS   A N   
1740 C  CA  . LYS   A 76  ? 0.1725 0.1526 0.1644 -0.0037 0.0145  0.0002  76  LYS   A CA  
1741 C  C   . LYS   A 76  ? 0.1678 0.1417 0.1256 0.0017  0.0145  0.0159  76  LYS   A C   
1742 O  O   . LYS   A 76  ? 0.1715 0.1322 0.1302 -0.0010 0.0165  0.0170  76  LYS   A O   
1743 C  CB  . LYS   A 76  ? 0.1651 0.1725 0.1983 0.0033  0.0187  -0.0202 76  LYS   A CB  
1744 C  CG  . LYS   A 76  ? 0.1753 0.1738 0.2514 0.0108  0.0107  -0.0220 76  LYS   A CG  
1745 C  CD  . LYS   A 76  ? 0.1832 0.1763 0.2894 0.0124  -0.0023 -0.0384 76  LYS   A CD  
1746 C  CE  . LYS   A 76  ? 0.1992 0.1971 0.3480 0.0014  0.0013  -0.0406 76  LYS   A CE  
1747 N  NZ  . LYS   A 76  ? 0.2017 0.1891 0.3853 -0.0096 -0.0026 -0.0453 76  LYS   A NZ  
1761 N  N   . VAL   A 77  ? 0.1763 0.1426 0.1306 -0.0038 0.0241  0.0147  77  VAL   A N   
1762 C  CA  . VAL   A 77  ? 0.1689 0.1484 0.1286 0.0029  0.0107  0.0215  77  VAL   A CA  
1763 C  C   . VAL   A 77  ? 0.1634 0.1405 0.1370 0.0105  0.0102  0.0156  77  VAL   A C   
1764 O  O   . VAL   A 77  ? 0.1691 0.1456 0.1344 0.0151  0.0284  0.0022  77  VAL   A O   
1765 C  CB  . VAL   A 77  ? 0.1793 0.1608 0.1387 0.0011  0.0087  0.0214  77  VAL   A CB  
1766 C  CG1 . VAL   A 77  ? 0.1793 0.1720 0.1553 0.0053  -0.0020 0.0000  77  VAL   A CG1 
1767 C  CG2 . VAL   A 77  ? 0.2039 0.1728 0.1656 0.0019  0.0046  0.0301  77  VAL   A CG2 
1777 N  N   . GLY   A 78  ? 0.1585 0.1366 0.1257 0.0083  0.0167  0.0101  78  GLY   A N   
1778 C  CA  . GLY   A 78  ? 0.1573 0.1346 0.1335 0.0027  0.0223  0.0132  78  GLY   A CA  
1779 C  C   . GLY   A 78  ? 0.1436 0.1329 0.1306 0.0033  0.0209  0.0133  78  GLY   A C   
1780 O  O   . GLY   A 78  ? 0.1442 0.1426 0.1450 0.0000  0.0144  0.0229  78  GLY   A O   
1784 N  N   . GLY   A 79  ? 0.1498 0.1286 0.1324 -0.0002 0.0123  0.0152  79  GLY   A N   
1785 C  CA  . GLY   A 79  ? 0.1492 0.1350 0.1390 -0.0003 0.0205  0.0151  79  GLY   A CA  
1786 C  C   . GLY   A 79  ? 0.1363 0.1293 0.1398 -0.0005 0.0167  0.0081  79  GLY   A C   
1787 O  O   . GLY   A 79  ? 0.1436 0.1367 0.1417 0.0172  0.0110  0.0052  79  GLY   A O   
1791 N  N   . SER   A 80  ? 0.1288 0.1406 0.1637 -0.0015 0.0127  0.0004  80  SER   A N   
1792 C  CA  . SER   A 80  ? 0.1279 0.1330 0.1518 -0.0020 0.0020  0.0070  80  SER   A CA  
1793 C  C   . SER   A 80  ? 0.1294 0.1368 0.1505 -0.0042 0.0100  0.0113  80  SER   A C   
1794 O  O   . SER   A 80  ? 0.1282 0.1603 0.1866 0.0082  0.0119  0.0010  80  SER   A O   
1795 C  CB  . SER   A 80  ? 0.1429 0.1373 0.1703 -0.0055 0.0097  0.0050  80  SER   A CB  
1796 O  OG  . SER   A 80  ? 0.1672 0.1354 0.2088 0.0070  -0.0046 0.0286  80  SER   A OG  
1802 N  N   . CYS   A 81  ? 0.1222 0.1332 0.1426 0.0001  -0.0039 0.0151  81  CYS   A N   
1803 C  CA  . CYS   A 81  ? 0.1267 0.1398 0.1534 -0.0072 -0.0059 0.0183  81  CYS   A CA  
1804 C  C   . CYS   A 81  ? 0.1255 0.1344 0.1453 -0.0086 0.0007  0.0279  81  CYS   A C   
1805 O  O   . CYS   A 81  ? 0.1257 0.1640 0.1640 -0.0008 -0.0013 0.0325  81  CYS   A O   
1806 C  CB  . CYS   A 81  ? 0.1360 0.1454 0.1616 -0.0168 0.0039  0.0252  81  CYS   A CB  
1807 S  SG  . CYS   A 81  ? 0.1460 0.1377 0.1587 -0.0155 -0.0009 0.0161  81  CYS   A SG  
1813 N  N   . VAL   A 82  ? 0.1309 0.1394 0.1447 0.0029  -0.0103 0.0210  82  VAL   A N   
1814 C  CA  . VAL   A 82  ? 0.1364 0.1501 0.1424 0.0023  -0.0059 0.0257  82  VAL   A CA  
1815 C  C   . VAL   A 82  ? 0.1333 0.1493 0.1574 -0.0032 -0.0059 0.0251  82  VAL   A C   
1816 O  O   . VAL   A 82  ? 0.1284 0.1622 0.1790 -0.0067 -0.0079 0.0017  82  VAL   A O   
1817 C  CB  . VAL   A 82  ? 0.1638 0.1687 0.1580 0.0051  0.0013  0.0290  82  VAL   A CB  
1818 C  CG1 . VAL   A 82  ? 0.1860 0.1819 0.1755 0.0014  0.0003  0.0312  82  VAL   A CG1 
1819 C  CG2 . VAL   A 82  ? 0.1679 0.1703 0.1843 0.0022  -0.0013 0.0239  82  VAL   A CG2 
1829 N  N   . LEU   A 83  ? 0.1292 0.1501 0.1347 -0.0103 -0.0138 0.0130  83  LEU   A N   
1830 C  CA  . LEU   A 83  ? 0.1359 0.1517 0.1349 -0.0135 -0.0114 0.0052  83  LEU   A CA  
1831 C  C   . LEU   A 83  ? 0.1369 0.1552 0.1281 -0.0159 -0.0183 0.0141  83  LEU   A C   
1832 O  O   . LEU   A 83  ? 0.1448 0.1585 0.1352 -0.0172 -0.0075 0.0186  83  LEU   A O   
1833 C  CB  . LEU   A 83  ? 0.1447 0.1521 0.1389 -0.0094 -0.0139 0.0174  83  LEU   A CB  
1834 C  CG  . LEU   A 83  ? 0.1565 0.1588 0.1451 -0.0137 0.0019  0.0106  83  LEU   A CG  
1835 C  CD1 . LEU   A 83  ? 0.1727 0.1634 0.1592 -0.0264 0.0040  0.0231  83  LEU   A CD1 
1836 C  CD2 . LEU   A 83  ? 0.1556 0.1771 0.1573 -0.0136 0.0077  0.0130  83  LEU   A CD2 
1848 N  N   . SER   A 84  ? 0.1525 0.1629 0.1320 -0.0177 -0.0152 0.0161  84  SER   A N   
1849 C  CA  . SER   A 84  ? 0.1628 0.1660 0.1260 -0.0151 -0.0195 0.0199  84  SER   A CA  
1850 C  C   . SER   A 84  ? 0.1643 0.1650 0.1203 -0.0248 -0.0067 0.0173  84  SER   A C   
1851 O  O   . SER   A 84  ? 0.1575 0.1745 0.1124 -0.0129 -0.0140 0.0083  84  SER   A O   
1852 C  CB  . SER   A 84  ? 0.1675 0.1844 0.1305 -0.0177 -0.0171 0.0028  84  SER   A CB  
1853 O  OG  . SER   A 84  ? 0.1670 0.2108 0.1441 -0.0166 -0.0275 -0.0078 84  SER   A OG  
1859 N  N   . GLY   A 85  ? 0.1795 0.1763 0.1250 -0.0235 0.0016  0.0115  85  GLY   A N   
1860 C  CA  . GLY   A 85  ? 0.1771 0.1837 0.1307 -0.0269 0.0122  0.0011  85  GLY   A CA  
1861 C  C   . GLY   A 85  ? 0.1706 0.1891 0.1145 -0.0226 -0.0099 0.0022  85  GLY   A C   
1862 O  O   . GLY   A 85  ? 0.1721 0.1937 0.1314 -0.0269 -0.0003 -0.0143 85  GLY   A O   
1866 N  N   . HIS   A 86  ? 0.1716 0.1820 0.1103 -0.0196 -0.0139 0.0038  86  HIS   A N   
1867 C  CA  . HIS   A 86  ? 0.1852 0.1917 0.1026 -0.0246 -0.0083 0.0002  86  HIS   A CA  
1868 C  C   . HIS   A 86  ? 0.2043 0.2023 0.0968 -0.0253 -0.0162 0.0039  86  HIS   A C   
1869 O  O   . HIS   A 86  ? 0.2171 0.2246 0.1116 -0.0255 -0.0083 0.0107  86  HIS   A O   
1870 C  CB  . HIS   A 86  ? 0.1878 0.1811 0.1250 -0.0186 -0.0027 0.0111  86  HIS   A CB  
1871 C  CG  . HIS   A 86  ? 0.1841 0.1786 0.1251 -0.0126 -0.0070 0.0169  86  HIS   A CG  
1872 N  ND1 . HIS   A 86  ? 0.1957 0.1802 0.1669 -0.0249 -0.0048 0.0106  86  HIS   A ND1 
1873 C  CD2 . HIS   A 86  ? 0.1842 0.1731 0.1137 -0.0025 0.0024  0.0161  86  HIS   A CD2 
1874 C  CE1 . HIS   A 86  ? 0.1863 0.1764 0.1563 -0.0187 0.0105  0.0160  86  HIS   A CE1 
1875 N  NE2 . HIS   A 86  ? 0.1864 0.1732 0.1338 -0.0009 0.0078  0.0220  86  HIS   A NE2 
1883 N  N   . ASN   A 87  ? 0.2181 0.2091 0.1188 -0.0145 0.0061  -0.0005 87  ASN   A N   
1884 C  CA  . ASN   A 87  ? 0.2412 0.2242 0.1286 -0.0112 0.0301  -0.0065 87  ASN   A CA  
1885 C  C   . ASN   A 87  ? 0.2390 0.2375 0.1487 -0.0192 0.0466  0.0086  87  ASN   A C   
1886 O  O   . ASN   A 87  ? 0.2727 0.2628 0.1838 -0.0301 0.0811  -0.0009 87  ASN   A O   
1887 C  CB  . ASN   A 87  ? 0.2643 0.2315 0.1284 0.0004  0.0294  -0.0085 87  ASN   A CB  
1888 C  CG  . ASN   A 87  ? 0.2790 0.2405 0.1287 0.0083  0.0351  -0.0038 87  ASN   A CG  
1889 O  OD1 . ASN   A 87  ? 0.2993 0.2408 0.1337 0.0260  0.0393  0.0028  87  ASN   A OD1 
1890 N  ND2 . ASN   A 87  ? 0.2820 0.2605 0.1625 0.0080  0.0394  0.0078  87  ASN   A ND2 
1897 N  N   A LEU   A 88  ? 0.2156 0.2216 0.1390 -0.0237 0.0253  0.0156  88  LEU   A N   
1898 N  N   B LEU   A 88  ? 0.2190 0.2272 0.1438 -0.0227 0.0341  0.0095  88  LEU   A N   
1899 C  CA  A LEU   A 88  ? 0.1973 0.2170 0.1540 -0.0302 0.0155  0.0297  88  LEU   A CA  
1900 C  CA  B LEU   A 88  ? 0.2023 0.2237 0.1539 -0.0267 0.0297  0.0184  88  LEU   A CA  
1901 C  C   A LEU   A 88  ? 0.1899 0.2207 0.1444 -0.0254 0.0117  0.0276  88  LEU   A C   
1902 C  C   B LEU   A 88  ? 0.1910 0.2235 0.1429 -0.0241 0.0215  0.0323  88  LEU   A C   
1903 O  O   A LEU   A 88  ? 0.1924 0.2175 0.1753 -0.0210 0.0169  0.0330  88  LEU   A O   
1904 O  O   B LEU   A 88  ? 0.1904 0.2210 0.1525 -0.0205 0.0330  0.0592  88  LEU   A O   
1905 C  CB  A LEU   A 88  ? 0.1939 0.2189 0.1614 -0.0323 -0.0189 0.0403  88  LEU   A CB  
1906 C  CB  B LEU   A 88  ? 0.2023 0.2268 0.1592 -0.0273 0.0159  0.0094  88  LEU   A CB  
1907 C  CG  A LEU   A 88  ? 0.2085 0.2302 0.1965 -0.0264 -0.0255 0.0459  88  LEU   A CG  
1908 C  CG  B LEU   A 88  ? 0.2117 0.2333 0.1692 -0.0214 0.0146  -0.0015 88  LEU   A CG  
1909 C  CD1 A LEU   A 88  ? 0.2144 0.2346 0.1954 -0.0301 -0.0261 0.0417  88  LEU   A CD1 
1910 C  CD1 B LEU   A 88  ? 0.2123 0.2330 0.1626 -0.0224 0.0185  -0.0139 88  LEU   A CD1 
1911 C  CD2 A LEU   A 88  ? 0.2208 0.2368 0.2368 -0.0203 -0.0172 0.0429  88  LEU   A CD2 
1912 C  CD2 B LEU   A 88  ? 0.2197 0.2384 0.1872 -0.0160 0.0174  -0.0029 88  LEU   A CD2 
1935 N  N   . ALA   A 89  ? 0.1827 0.2186 0.1260 -0.0227 0.0069  0.0090  89  ALA   A N   
1936 C  CA  . ALA   A 89  ? 0.1882 0.2173 0.1090 -0.0201 -0.0064 0.0175  89  ALA   A CA  
1937 C  C   . ALA   A 89  ? 0.1910 0.2175 0.1266 -0.0185 -0.0205 0.0183  89  ALA   A C   
1938 O  O   . ALA   A 89  ? 0.1828 0.2097 0.1674 -0.0241 -0.0216 -0.0056 89  ALA   A O   
1939 C  CB  . ALA   A 89  ? 0.1813 0.2101 0.1087 -0.0184 -0.0015 0.0176  89  ALA   A CB  
1946 N  N   . LYS   A 90  ? 0.1997 0.2289 0.1272 -0.0270 -0.0286 0.0251  90  LYS   A N   
1947 C  CA  . LYS   A 90  ? 0.2074 0.2422 0.1320 -0.0168 -0.0457 0.0249  90  LYS   A CA  
1948 C  C   . LYS   A 90  ? 0.1853 0.2263 0.1272 -0.0185 -0.0381 0.0131  90  LYS   A C   
1949 O  O   . LYS   A 90  ? 0.1936 0.2428 0.1582 -0.0265 -0.0424 -0.0014 90  LYS   A O   
1950 C  CB  . LYS   A 90  ? 0.2362 0.2816 0.1651 -0.0110 -0.0562 0.0482  90  LYS   A CB  
1951 C  CG  . LYS   A 90  ? 0.2902 0.3267 0.2662 -0.0063 -0.0648 0.0531  90  LYS   A CG  
1952 C  CD  . LYS   A 90  ? 0.3367 0.3653 0.3644 -0.0066 -0.0584 0.0598  90  LYS   A CD  
1953 C  CE  . LYS   A 90  ? 0.3702 0.3923 0.4488 -0.0090 -0.0486 0.0569  90  LYS   A CE  
1954 N  NZ  . LYS   A 90  ? 0.4010 0.4044 0.5004 -0.0128 -0.0378 0.0494  90  LYS   A NZ  
1968 N  N   . HIS   A 91  ? 0.1798 0.2005 0.1074 -0.0236 -0.0328 0.0249  91  HIS   A N   
1969 C  CA  . HIS   A 91  ? 0.1632 0.1822 0.1221 -0.0148 -0.0310 0.0190  91  HIS   A CA  
1970 C  C   . HIS   A 91  ? 0.1507 0.1689 0.1125 -0.0169 -0.0156 0.0230  91  HIS   A C   
1971 O  O   . HIS   A 91  ? 0.1503 0.1841 0.1248 -0.0258 -0.0102 0.0186  91  HIS   A O   
1972 C  CB  . HIS   A 91  ? 0.1800 0.2110 0.1776 0.0073  -0.0470 0.0238  91  HIS   A CB  
1973 C  CG  . HIS   A 91  ? 0.2269 0.2586 0.2507 0.0176  -0.0760 0.0161  91  HIS   A CG  
1974 N  ND1 . HIS   A 91  ? 0.2364 0.2859 0.2930 0.0253  -0.0920 -0.0071 91  HIS   A ND1 
1975 C  CD2 . HIS   A 91  ? 0.2536 0.2779 0.2771 0.0266  -0.0891 0.0261  91  HIS   A CD2 
1976 C  CE1 . HIS   A 91  ? 0.2460 0.2942 0.3057 0.0292  -0.0947 0.0055  91  HIS   A CE1 
1977 N  NE2 . HIS   A 91  ? 0.2617 0.2928 0.3008 0.0320  -0.0951 0.0164  91  HIS   A NE2 
1985 N  N   . CYS   A 92  ? 0.1479 0.1613 0.1112 -0.0183 -0.0145 0.0188  92  CYS   A N   
1986 C  CA  . CYS   A 92  ? 0.1375 0.1570 0.1193 -0.0191 -0.0018 0.0142  92  CYS   A CA  
1987 C  C   . CYS   A 92  ? 0.1346 0.1496 0.1161 -0.0208 -0.0013 0.0160  92  CYS   A C   
1988 O  O   . CYS   A 92  ? 0.1380 0.1564 0.1359 -0.0242 -0.0053 0.0084  92  CYS   A O   
1989 C  CB  . CYS   A 92  ? 0.1427 0.1557 0.1356 -0.0074 -0.0086 0.0146  92  CYS   A CB  
1990 S  SG  . CYS   A 92  ? 0.1401 0.1438 0.1213 -0.0111 -0.0079 0.0111  92  CYS   A SG  
1996 N  N   . LEU   A 93  ? 0.1293 0.1383 0.1135 -0.0133 0.0051  0.0201  93  LEU   A N   
1997 C  CA  . LEU   A 93  ? 0.1243 0.1355 0.1219 -0.0107 -0.0000 0.0186  93  LEU   A CA  
1998 C  C   . LEU   A 93  ? 0.1225 0.1214 0.1177 -0.0038 0.0047  0.0094  93  LEU   A C   
1999 O  O   . LEU   A 93  ? 0.1217 0.1326 0.1150 -0.0048 -0.0019 0.0144  93  LEU   A O   
2000 C  CB  . LEU   A 93  ? 0.1290 0.1348 0.1342 -0.0062 -0.0051 0.0269  93  LEU   A CB  
2001 C  CG  . LEU   A 93  ? 0.1369 0.1321 0.1417 -0.0034 0.0010  0.0301  93  LEU   A CG  
2002 C  CD1 . LEU   A 93  ? 0.1399 0.1428 0.1640 0.0023  0.0092  0.0150  93  LEU   A CD1 
2003 C  CD2 . LEU   A 93  ? 0.1486 0.1321 0.1561 -0.0110 -0.0014 0.0199  93  LEU   A CD2 
2015 N  N   . HIS   A 94  ? 0.1180 0.1207 0.1137 -0.0054 -0.0032 0.0148  94  HIS   A N   
2016 C  CA  . HIS   A 94  ? 0.1169 0.1269 0.1205 -0.0031 -0.0031 0.0169  94  HIS   A CA  
2017 C  C   . HIS   A 94  ? 0.1187 0.1168 0.1179 -0.0054 -0.0051 0.0117  94  HIS   A C   
2018 O  O   . HIS   A 94  ? 0.1280 0.1395 0.1476 0.0001  -0.0026 -0.0078 94  HIS   A O   
2019 C  CB  . HIS   A 94  ? 0.1138 0.1234 0.1358 -0.0041 -0.0021 0.0175  94  HIS   A CB  
2020 C  CG  . HIS   A 94  ? 0.1259 0.1211 0.1101 -0.0061 -0.0047 0.0154  94  HIS   A CG  
2021 N  ND1 . HIS   A 94  ? 0.1231 0.1190 0.1299 -0.0074 -0.0031 0.0186  94  HIS   A ND1 
2022 C  CD2 . HIS   A 94  ? 0.1312 0.1334 0.1257 -0.0060 -0.0070 0.0085  94  HIS   A CD2 
2023 C  CE1 . HIS   A 94  ? 0.1244 0.1247 0.1237 -0.0103 -0.0081 0.0138  94  HIS   A CE1 
2024 N  NE2 . HIS   A 94  ? 0.1289 0.1283 0.1358 -0.0095 -0.0082 0.0067  94  HIS   A NE2 
2032 N  N   . VAL   A 95  ? 0.1198 0.1152 0.1030 -0.0031 0.0043  0.0048  95  VAL   A N   
2033 C  CA  . VAL   A 95  ? 0.1240 0.1223 0.1204 -0.0047 0.0007  0.0116  95  VAL   A CA  
2034 C  C   . VAL   A 95  ? 0.1293 0.1131 0.1047 -0.0128 -0.0025 0.0036  95  VAL   A C   
2035 O  O   . VAL   A 95  ? 0.1322 0.1307 0.1054 0.0084  0.0018  0.0096  95  VAL   A O   
2036 C  CB  . VAL   A 95  ? 0.1228 0.1269 0.1373 -0.0073 -0.0017 0.0078  95  VAL   A CB  
2037 C  CG1 . VAL   A 95  ? 0.1363 0.1323 0.1383 -0.0161 -0.0026 0.0017  95  VAL   A CG1 
2038 C  CG2 . VAL   A 95  ? 0.1300 0.1296 0.1306 -0.0124 0.0033  0.0180  95  VAL   A CG2 
2048 N  N   . VAL   A 96  ? 0.1321 0.1221 0.0981 -0.0079 0.0067  0.0057  96  VAL   A N   
2049 C  CA  . VAL   A 96  ? 0.1332 0.1270 0.1100 -0.0040 0.0088  0.0150  96  VAL   A CA  
2050 C  C   . VAL   A 96  ? 0.1321 0.1369 0.1183 -0.0008 0.0129  0.0190  96  VAL   A C   
2051 O  O   . VAL   A 96  ? 0.1402 0.1411 0.1314 -0.0016 0.0235  0.0013  96  VAL   A O   
2052 C  CB  . VAL   A 96  ? 0.1356 0.1301 0.1296 -0.0052 0.0192  0.0181  96  VAL   A CB  
2053 C  CG1 . VAL   A 96  ? 0.1442 0.1338 0.1176 -0.0046 0.0137  0.0157  96  VAL   A CG1 
2054 C  CG2 . VAL   A 96  ? 0.1360 0.1413 0.1371 -0.0118 0.0213  0.0195  96  VAL   A CG2 
2064 N  N   A GLY   A 97  ? 0.1323 0.1377 0.1327 -0.0020 0.0078  0.0140  97  GLY   A N   
2065 N  N   B GLY   A 97  ? 0.1347 0.1383 0.1084 -0.0052 0.0079  0.0154  97  GLY   A N   
2066 C  CA  A GLY   A 97  ? 0.1391 0.1473 0.1270 -0.0015 0.0014  0.0101  97  GLY   A CA  
2067 C  CA  B GLY   A 97  ? 0.1405 0.1435 0.0907 -0.0058 0.0038  0.0148  97  GLY   A CA  
2068 C  C   A GLY   A 97  ? 0.1470 0.1532 0.1112 -0.0040 0.0076  0.0051  97  GLY   A C   
2069 C  C   B GLY   A 97  ? 0.1474 0.1471 0.0956 -0.0069 0.0089  0.0210  97  GLY   A C   
2070 O  O   A GLY   A 97  ? 0.1534 0.1515 0.1265 -0.0029 0.0092  0.0030  97  GLY   A O   
2071 O  O   B GLY   A 97  ? 0.1501 0.1454 0.1138 -0.0066 0.0088  0.0251  97  GLY   A O   
2078 N  N   A PRO   A 98  ? 0.1512 0.1526 0.0953 0.0044  -0.0048 0.0142  98  PRO   A N   
2079 N  N   B PRO   A 98  ? 0.1555 0.1488 0.1042 0.0012  0.0071  0.0264  98  PRO   A N   
2080 C  CA  A PRO   A 98  ? 0.1571 0.1650 0.1033 0.0018  -0.0025 0.0074  98  PRO   A CA  
2081 C  CA  B PRO   A 98  ? 0.1696 0.1542 0.1315 0.0040  0.0113  0.0109  98  PRO   A CA  
2082 C  C   A PRO   A 98  ? 0.1536 0.1763 0.0800 -0.0100 -0.0004 0.0165  98  PRO   A C   
2083 C  C   B PRO   A 98  ? 0.1884 0.1548 0.1350 0.0055  0.0079  0.0250  98  PRO   A C   
2084 O  O   A PRO   A 98  ? 0.1460 0.1635 0.1102 -0.0062 0.0042  0.0177  98  PRO   A O   
2085 O  O   B PRO   A 98  ? 0.1864 0.1519 0.1584 0.0129  0.0055  0.0245  98  PRO   A O   
2086 C  CB  A PRO   A 98  ? 0.1644 0.1722 0.1000 0.0108  -0.0066 -0.0026 98  PRO   A CB  
2087 C  CB  B PRO   A 98  ? 0.1703 0.1518 0.1315 0.0124  0.0130  0.0119  98  PRO   A CB  
2088 C  CG  A PRO   A 98  ? 0.1663 0.1692 0.1114 0.0141  0.0028  -0.0082 98  PRO   A CG  
2089 C  CG  B PRO   A 98  ? 0.1713 0.1513 0.1244 0.0029  0.0099  0.0143  98  PRO   A CG  
2090 C  CD  A PRO   A 98  ? 0.1593 0.1585 0.1072 0.0079  0.0005  -0.0015 98  PRO   A CD  
2091 C  CD  B PRO   A 98  ? 0.1613 0.1471 0.1087 0.0014  0.0083  0.0251  98  PRO   A CD  
2106 N  N   A ASN   A 99  ? 0.1568 0.2039 0.0965 -0.0097 0.0133  0.0346  99  ASN   A N   
2107 N  N   B ASN   A 99  ? 0.2131 0.1561 0.1241 0.0065  0.0047  0.0323  99  ASN   A N   
2108 C  CA  A ASN   A 99  ? 0.1791 0.2257 0.1113 -0.0105 0.0040  0.0375  99  ASN   A CA  
2109 C  CA  B ASN   A 99  ? 0.2400 0.1574 0.1327 0.0074  0.0092  0.0549  99  ASN   A CA  
2110 C  C   A ASN   A 99  ? 0.2028 0.2534 0.1076 -0.0260 -0.0057 0.0479  99  ASN   A C   
2111 C  C   B ASN   A 99  ? 0.2580 0.1639 0.1221 0.0066  -0.0015 0.0637  99  ASN   A C   
2112 O  O   A ASN   A 99  ? 0.2105 0.2701 0.1205 -0.0217 -0.0170 0.0358  99  ASN   A O   
2113 O  O   B ASN   A 99  ? 0.2598 0.1557 0.1191 0.0116  -0.0138 0.0391  99  ASN   A O   
2114 C  CB  A ASN   A 99  ? 0.1760 0.2201 0.1293 -0.0092 0.0012  0.0408  99  ASN   A CB  
2115 C  CB  B ASN   A 99  ? 0.2499 0.1611 0.1622 0.0135  0.0141  0.0522  99  ASN   A CB  
2116 C  CG  A ASN   A 99  ? 0.1796 0.2167 0.1618 -0.0015 -0.0153 0.0295  99  ASN   A CG  
2117 C  CG  B ASN   A 99  ? 0.2602 0.1682 0.1828 0.0148  0.0195  0.0518  99  ASN   A CG  
2118 O  OD1 A ASN   A 99  ? 0.1884 0.2238 0.1467 0.0067  -0.0068 0.0195  99  ASN   A OD1 
2119 O  OD1 B ASN   A 99  ? 0.2612 0.1700 0.1685 0.0261  0.0251  0.0612  99  ASN   A OD1 
2120 N  ND2 A ASN   A 99  ? 0.1810 0.2034 0.1969 -0.0066 -0.0213 0.0543  99  ASN   A ND2 
2121 N  ND2 B ASN   A 99  ? 0.2657 0.1769 0.2458 0.0125  0.0084  0.0339  99  ASN   A ND2 
2134 N  N   A VAL   A 100 ? 0.2223 0.2686 0.1263 -0.0356 -0.0338 0.0487  100 VAL   A N   
2135 N  N   B VAL   A 100 ? 0.2756 0.1878 0.1471 0.0030  -0.0146 0.0636  100 VAL   A N   
2136 C  CA  A VAL   A 100 ? 0.2438 0.2853 0.1550 -0.0429 -0.0423 0.0449  100 VAL   A CA  
2137 C  CA  B VAL   A 100 ? 0.2943 0.2077 0.1900 0.0033  -0.0230 0.0570  100 VAL   A CA  
2138 C  C   A VAL   A 100 ? 0.2540 0.3009 0.1550 -0.0494 -0.0335 0.0678  100 VAL   A C   
2139 C  C   B VAL   A 100 ? 0.2987 0.2055 0.1722 0.0103  -0.0388 0.0541  100 VAL   A C   
2140 O  O   A VAL   A 100 ? 0.2622 0.3089 0.1571 -0.0503 -0.0153 0.0776  100 VAL   A O   
2141 O  O   B VAL   A 100 ? 0.3018 0.2009 0.1793 0.0053  -0.0400 0.0458  100 VAL   A O   
2142 C  CB  A VAL   A 100 ? 0.2606 0.2885 0.1832 -0.0409 -0.0454 0.0305  100 VAL   A CB  
2143 C  CB  B VAL   A 100 ? 0.3074 0.2321 0.2470 -0.0001 -0.0171 0.0399  100 VAL   A CB  
2144 C  CG1 A VAL   A 100 ? 0.2608 0.2938 0.2000 -0.0447 -0.0345 0.0230  100 VAL   A CG1 
2145 C  CG1 B VAL   A 100 ? 0.3078 0.2349 0.2721 0.0002  -0.0134 0.0311  100 VAL   A CG1 
2146 C  CG2 A VAL   A 100 ? 0.2714 0.2864 0.1861 -0.0408 -0.0417 0.0270  100 VAL   A CG2 
2147 C  CG2 B VAL   A 100 ? 0.3131 0.2455 0.2737 0.0006  -0.0147 0.0377  100 VAL   A CG2 
2166 N  N   A ASN   A 101 ? 0.2566 0.3072 0.1757 -0.0541 -0.0321 0.0885  101 ASN   A N   
2167 N  N   B ASN   A 101 ? 0.3039 0.2137 0.1566 0.0189  -0.0434 0.0517  101 ASN   A N   
2168 C  CA  A ASN   A 101 ? 0.2726 0.3142 0.2048 -0.0575 -0.0240 0.0969  101 ASN   A CA  
2169 C  CA  B ASN   A 101 ? 0.3088 0.2234 0.1609 0.0282  -0.0362 0.0473  101 ASN   A CA  
2170 C  C   A ASN   A 101 ? 0.2912 0.3403 0.2304 -0.0629 0.0007  0.1101  101 ASN   A C   
2171 C  C   B ASN   A 101 ? 0.3206 0.2313 0.1523 0.0300  -0.0131 0.0590  101 ASN   A C   
2172 O  O   A ASN   A 101 ? 0.3029 0.3450 0.2561 -0.0621 0.0007  0.1040  101 ASN   A O   
2173 O  O   B ASN   A 101 ? 0.3309 0.2361 0.1446 0.0252  -0.0080 0.0699  101 ASN   A O   
2174 C  CB  A ASN   A 101 ? 0.2718 0.2935 0.1893 -0.0540 -0.0386 0.0924  101 ASN   A CB  
2175 C  CB  B ASN   A 101 ? 0.3043 0.2242 0.1719 0.0282  -0.0388 0.0435  101 ASN   A CB  
2176 C  CG  A ASN   A 101 ? 0.2741 0.2779 0.1810 -0.0477 -0.0474 0.0664  101 ASN   A CG  
2177 C  CG  B ASN   A 101 ? 0.3035 0.2323 0.2019 0.0220  -0.0389 0.0408  101 ASN   A CG  
2178 O  OD1 A ASN   A 101 ? 0.2697 0.2704 0.1813 -0.0380 -0.0437 0.0314  101 ASN   A OD1 
2179 O  OD1 B ASN   A 101 ? 0.3079 0.2443 0.2228 0.0145  -0.0381 0.0479  101 ASN   A OD1 
2180 N  ND2 A ASN   A 101 ? 0.2805 0.2725 0.1845 -0.0535 -0.0474 0.0677  101 ASN   A ND2 
2181 N  ND2 B ASN   A 101 ? 0.2989 0.2268 0.2211 0.0230  -0.0331 0.0262  101 ASN   A ND2 
2194 N  N   A LYS   A 102 ? 0.2924 0.3631 0.2483 -0.0709 0.0197  0.1119  102 LYS   A N   
2195 N  N   B LYS   A 102 ? 0.3241 0.2405 0.1825 0.0330  0.0054  0.0525  102 LYS   A N   
2196 C  CA  A LYS   A 102 ? 0.3024 0.3848 0.2611 -0.0710 0.0205  0.1043  102 LYS   A CA  
2197 C  CA  B LYS   A 102 ? 0.3316 0.2515 0.1930 0.0278  0.0189  0.0492  102 LYS   A CA  
2198 C  C   A LYS   A 102 ? 0.3133 0.3998 0.2501 -0.0602 0.0194  0.0923  102 LYS   A C   
2199 C  C   B LYS   A 102 ? 0.3255 0.2435 0.1781 0.0313  0.0099  0.0616  102 LYS   A C   
2200 O  O   A LYS   A 102 ? 0.3181 0.4068 0.2542 -0.0572 0.0260  0.0876  102 LYS   A O   
2201 O  O   B LYS   A 102 ? 0.3273 0.2392 0.1897 0.0318  0.0123  0.0671  102 LYS   A O   
2202 C  CB  A LYS   A 102 ? 0.3068 0.3919 0.2865 -0.0765 0.0189  0.0964  102 LYS   A CB  
2203 C  CB  B LYS   A 102 ? 0.3440 0.2696 0.2509 0.0198  0.0243  0.0216  102 LYS   A CB  
2204 C  CG  A LYS   A 102 ? 0.3127 0.3974 0.3088 -0.0782 0.0165  0.0846  102 LYS   A CG  
2205 C  CG  B LYS   A 102 ? 0.3548 0.2854 0.3047 0.0140  0.0282  -0.0011 102 LYS   A CG  
2206 C  CD  A LYS   A 102 ? 0.3210 0.4035 0.3321 -0.0786 0.0108  0.0691  102 LYS   A CD  
2207 C  CD  B LYS   A 102 ? 0.3639 0.3008 0.3484 0.0082  0.0339  -0.0162 102 LYS   A CD  
2208 C  CE  A LYS   A 102 ? 0.3295 0.4074 0.3534 -0.0785 0.0036  0.0591  102 LYS   A CE  
2209 C  CE  B LYS   A 102 ? 0.3712 0.3134 0.3825 0.0021  0.0353  -0.0276 102 LYS   A CE  
2210 N  NZ  A LYS   A 102 ? 0.3337 0.4084 0.3667 -0.0810 0.0030  0.0492  102 LYS   A NZ  
2211 N  NZ  B LYS   A 102 ? 0.3758 0.3199 0.4012 -0.0001 0.0329  -0.0331 102 LYS   A NZ  
2238 N  N   A GLY   A 103 ? 0.3162 0.4067 0.2601 -0.0503 0.0114  0.0718  103 GLY   A N   
2239 N  N   B GLY   A 103 ? 0.3175 0.2452 0.1703 0.0316  -0.0073 0.0466  103 GLY   A N   
2240 C  CA  A GLY   A 103 ? 0.3211 0.4112 0.2580 -0.0402 0.0107  0.0594  103 GLY   A CA  
2241 C  CA  B GLY   A 103 ? 0.3093 0.2410 0.1704 0.0256  -0.0197 0.0546  103 GLY   A CA  
2242 C  C   A GLY   A 103 ? 0.3206 0.4141 0.2580 -0.0342 0.0163  0.0535  103 GLY   A C   
2243 C  C   B GLY   A 103 ? 0.2962 0.2343 0.1499 0.0156  -0.0187 0.0594  103 GLY   A C   
2244 O  O   A GLY   A 103 ? 0.3308 0.4171 0.2720 -0.0325 0.0199  0.0516  103 GLY   A O   
2245 O  O   B GLY   A 103 ? 0.3055 0.2356 0.1488 0.0097  -0.0214 0.0590  103 GLY   A O   
2252 N  N   A GLU   A 104 ? 0.3064 0.4105 0.2320 -0.0351 0.0226  0.0477  104 GLU   A N   
2253 N  N   B GLU   A 104 ? 0.2720 0.2255 0.1352 0.0130  -0.0278 0.0590  104 GLU   A N   
2254 C  CA  A GLU   A 104 ? 0.2889 0.4028 0.2050 -0.0421 0.0257  0.0384  104 GLU   A CA  
2255 C  CA  B GLU   A 104 ? 0.2494 0.2140 0.1245 0.0039  -0.0235 0.0501  104 GLU   A CA  
2256 C  C   A GLU   A 104 ? 0.2950 0.4074 0.2048 -0.0381 0.0238  0.0245  104 GLU   A C   
2257 C  C   B GLU   A 104 ? 0.2326 0.2083 0.1297 0.0039  -0.0176 0.0303  104 GLU   A C   
2258 O  O   A GLU   A 104 ? 0.2896 0.4081 0.2169 -0.0379 0.0134  0.0258  104 GLU   A O   
2259 O  O   B GLU   A 104 ? 0.2218 0.1983 0.1757 0.0036  -0.0141 0.0347  104 GLU   A O   
2260 C  CB  A GLU   A 104 ? 0.2619 0.3897 0.1784 -0.0530 0.0290  0.0517  104 GLU   A CB  
2261 C  CB  B GLU   A 104 ? 0.2481 0.2104 0.1251 -0.0051 -0.0180 0.0596  104 GLU   A CB  
2262 C  CG  A GLU   A 104 ? 0.2409 0.3771 0.1751 -0.0619 0.0221  0.0668  104 GLU   A CG  
2263 C  CG  B GLU   A 104 ? 0.2527 0.2208 0.1486 -0.0122 -0.0231 0.0623  104 GLU   A CG  
2264 C  CD  A GLU   A 104 ? 0.2187 0.3649 0.1701 -0.0711 0.0146  0.0809  104 GLU   A CD  
2265 C  CD  B GLU   A 104 ? 0.2532 0.2297 0.1615 -0.0162 -0.0350 0.0669  104 GLU   A CD  
2266 O  OE1 A GLU   A 104 ? 0.2060 0.3485 0.1378 -0.0708 0.0109  0.0798  104 GLU   A OE1 
2267 O  OE1 B GLU   A 104 ? 0.2506 0.2317 0.1769 -0.0128 -0.0388 0.0674  104 GLU   A OE1 
2268 O  OE2 A GLU   A 104 ? 0.2213 0.3643 0.1954 -0.0736 0.0035  0.0927  104 GLU   A OE2 
2269 O  OE2 B GLU   A 104 ? 0.2616 0.2358 0.1653 -0.0246 -0.0355 0.0712  104 GLU   A OE2 
2282 N  N   A ASP   A 105 ? 0.3062 0.4116 0.2119 -0.0319 0.0317  0.0045  105 ASP   A N   
2283 N  N   B ASP   A 105 ? 0.2392 0.2079 0.1203 -0.0038 -0.0070 0.0174  105 ASP   A N   
2284 C  CA  A ASP   A 105 ? 0.3115 0.4134 0.2322 -0.0280 0.0369  -0.0171 105 ASP   A CA  
2285 C  CA  B ASP   A 105 ? 0.2410 0.2050 0.1363 -0.0054 0.0062  -0.0119 105 ASP   A CA  
2286 C  C   A ASP   A 105 ? 0.2890 0.4001 0.2092 -0.0376 0.0295  -0.0340 105 ASP   A C   
2287 C  C   B ASP   A 105 ? 0.2221 0.1888 0.1137 -0.0106 0.0084  -0.0226 105 ASP   A C   
2288 O  O   A ASP   A 105 ? 0.2840 0.4007 0.1876 -0.0374 0.0305  -0.0456 105 ASP   A O   
2289 O  O   B ASP   A 105 ? 0.2008 0.1716 0.0737 -0.0014 0.0019  -0.0325 105 ASP   A O   
2290 C  CB  A ASP   A 105 ? 0.3359 0.4256 0.2866 -0.0166 0.0425  -0.0187 105 ASP   A CB  
2291 C  CB  B ASP   A 105 ? 0.2596 0.2163 0.1891 -0.0036 0.0162  -0.0230 105 ASP   A CB  
2292 C  CG  A ASP   A 105 ? 0.3559 0.4346 0.3369 -0.0078 0.0399  -0.0206 105 ASP   A CG  
2293 C  CG  B ASP   A 105 ? 0.2772 0.2256 0.2286 0.0079  0.0156  -0.0436 105 ASP   A CG  
2294 O  OD1 A ASP   A 105 ? 0.3631 0.4387 0.3491 -0.0069 0.0342  -0.0274 105 ASP   A OD1 
2295 O  OD1 B ASP   A 105 ? 0.2871 0.2268 0.2216 0.0024  0.0057  -0.0543 105 ASP   A OD1 
2296 O  OD2 A ASP   A 105 ? 0.3651 0.4375 0.3643 -0.0043 0.0430  -0.0113 105 ASP   A OD2 
2297 O  OD2 B ASP   A 105 ? 0.2863 0.2369 0.2808 0.0144  0.0083  -0.0396 105 ASP   A OD2 
2306 N  N   A ILE   A 106 ? 0.2712 0.3838 0.2113 -0.0474 0.0055  -0.0409 106 ILE   A N   
2307 N  N   B ILE   A 106 ? 0.2244 0.2063 0.1444 -0.0122 -0.0010 -0.0062 106 ILE   A N   
2308 C  CA  A ILE   A 106 ? 0.2472 0.3636 0.2200 -0.0591 -0.0143 -0.0566 106 ILE   A CA  
2309 C  CA  B ILE   A 106 ? 0.2214 0.2180 0.1725 -0.0213 -0.0089 -0.0087 106 ILE   A CA  
2310 C  C   A ILE   A 106 ? 0.2262 0.3371 0.2156 -0.0758 -0.0081 -0.0817 106 ILE   A C   
2311 C  C   B ILE   A 106 ? 0.2241 0.2205 0.1817 -0.0250 -0.0044 -0.0027 106 ILE   A C   
2312 O  O   A ILE   A 106 ? 0.2012 0.3311 0.2131 -0.0828 0.0034  -0.0896 106 ILE   A O   
2313 O  O   B ILE   A 106 ? 0.2193 0.2231 0.1897 -0.0192 -0.0011 0.0029  106 ILE   A O   
2314 C  CB  A ILE   A 106 ? 0.2486 0.3688 0.2587 -0.0506 -0.0321 -0.0320 106 ILE   A CB  
2315 C  CB  B ILE   A 106 ? 0.2219 0.2368 0.2117 -0.0238 -0.0245 -0.0078 106 ILE   A CB  
2316 C  CG1 A ILE   A 106 ? 0.2435 0.3684 0.2847 -0.0429 -0.0351 -0.0134 106 ILE   A CG1 
2317 C  CG1 B ILE   A 106 ? 0.2162 0.2499 0.2327 -0.0169 -0.0258 0.0014  106 ILE   A CG1 
2318 C  CG2 A ILE   A 106 ? 0.2546 0.3703 0.2681 -0.0481 -0.0357 -0.0311 106 ILE   A CG2 
2319 C  CG2 B ILE   A 106 ? 0.2260 0.2404 0.2213 -0.0263 -0.0262 -0.0148 106 ILE   A CG2 
2320 C  CD1 A ILE   A 106 ? 0.2464 0.3685 0.3038 -0.0337 -0.0252 -0.0037 106 ILE   A CD1 
2321 C  CD1 B ILE   A 106 ? 0.2137 0.2558 0.2428 -0.0118 -0.0197 0.0035  106 ILE   A CD1 
2344 N  N   A GLN   A 107 ? 0.2378 0.3180 0.2403 -0.0754 -0.0004 -0.0919 107 GLN   A N   
2345 N  N   B GLN   A 107 ? 0.2353 0.2190 0.2081 -0.0300 -0.0054 -0.0086 107 GLN   A N   
2346 C  CA  A GLN   A 107 ? 0.2537 0.3003 0.3008 -0.0580 0.0235  -0.0817 107 GLN   A CA  
2347 C  CA  B GLN   A 107 ? 0.2503 0.2317 0.2665 -0.0315 0.0107  -0.0135 107 GLN   A CA  
2348 C  C   A GLN   A 107 ? 0.2225 0.2538 0.2741 -0.0469 0.0492  -0.0502 107 GLN   A C   
2349 C  C   B GLN   A 107 ? 0.2240 0.2186 0.2520 -0.0344 0.0328  -0.0156 107 GLN   A C   
2350 O  O   A GLN   A 107 ? 0.2209 0.2490 0.3096 -0.0375 0.0708  -0.0491 107 GLN   A O   
2351 O  O   B GLN   A 107 ? 0.2282 0.2178 0.2821 -0.0344 0.0301  -0.0121 107 GLN   A O   
2352 C  CB  A GLN   A 107 ? 0.2948 0.3282 0.3864 -0.0600 0.0116  -0.0824 107 GLN   A CB  
2353 C  CB  B GLN   A 107 ? 0.2851 0.2597 0.3307 -0.0377 -0.0031 -0.0096 107 GLN   A CB  
2354 C  CG  A GLN   A 107 ? 0.3326 0.3560 0.4791 -0.0596 -0.0003 -0.0722 107 GLN   A CG  
2355 C  CG  B GLN   A 107 ? 0.3150 0.2850 0.3964 -0.0405 -0.0177 0.0045  107 GLN   A CG  
2356 C  CD  A GLN   A 107 ? 0.3594 0.3772 0.5543 -0.0603 -0.0083 -0.0600 107 GLN   A CD  
2357 C  CD  B GLN   A 107 ? 0.3407 0.3077 0.4533 -0.0392 -0.0262 0.0159  107 GLN   A CD  
2358 O  OE1 A GLN   A 107 ? 0.3710 0.3868 0.5853 -0.0582 -0.0121 -0.0566 107 GLN   A OE1 
2359 O  OE1 B GLN   A 107 ? 0.3508 0.3175 0.4730 -0.0364 -0.0270 0.0230  107 GLN   A OE1 
2360 N  NE2 A GLN   A 107 ? 0.3706 0.3836 0.5786 -0.0636 -0.0111 -0.0581 107 GLN   A NE2 
2361 N  NE2 B GLN   A 107 ? 0.3479 0.3153 0.4728 -0.0393 -0.0326 0.0203  107 GLN   A NE2 
2378 N  N   . LEU   A 108 ? 0.1974 0.2118 0.2216 -0.0455 0.0422  -0.0369 108 LEU   A N   
2379 C  CA  . LEU   A 108 ? 0.1804 0.1829 0.1966 -0.0169 0.0340  -0.0124 108 LEU   A CA  
2380 C  C   . LEU   A 108 ? 0.1584 0.1488 0.1836 -0.0046 0.0283  0.0121  108 LEU   A C   
2381 O  O   . LEU   A 108 ? 0.1618 0.1503 0.2004 0.0033  0.0316  0.0106  108 LEU   A O   
2382 C  CB  . LEU   A 108 ? 0.1873 0.1986 0.1722 -0.0160 0.0466  -0.0067 108 LEU   A CB  
2383 C  CG  . LEU   A 108 ? 0.2029 0.2190 0.1983 -0.0145 0.0505  -0.0085 108 LEU   A CG  
2384 C  CD1 . LEU   A 108 ? 0.2188 0.2250 0.2088 -0.0279 0.0543  -0.0029 108 LEU   A CD1 
2385 C  CD2 . LEU   A 108 ? 0.2061 0.2384 0.2446 -0.0077 0.0548  -0.0075 108 LEU   A CD2 
2398 N  N   . LEU   A 109 ? 0.1536 0.1455 0.1695 0.0020  0.0166  0.0165  109 LEU   A N   
2399 C  CA  . LEU   A 109 ? 0.1497 0.1453 0.1556 0.0033  0.0091  0.0187  109 LEU   A CA  
2400 C  C   . LEU   A 109 ? 0.1394 0.1364 0.1423 -0.0038 0.0148  0.0099  109 LEU   A C   
2401 O  O   . LEU   A 109 ? 0.1435 0.1307 0.1620 -0.0018 0.0034  0.0032  109 LEU   A O   
2402 C  CB  . LEU   A 109 ? 0.1561 0.1526 0.1776 0.0153  0.0032  0.0251  109 LEU   A CB  
2403 C  CG  . LEU   A 109 ? 0.1506 0.1564 0.1839 0.0143  0.0157  0.0348  109 LEU   A CG  
2404 C  CD1 . LEU   A 109 ? 0.1548 0.1412 0.1998 0.0029  0.0142  0.0181  109 LEU   A CD1 
2405 C  CD2 . LEU   A 109 ? 0.1485 0.1753 0.2131 0.0107  0.0144  0.0381  109 LEU   A CD2 
2417 N  N   . LYS   A 110 ? 0.1384 0.1409 0.1482 -0.0017 -0.0006 0.0070  110 LYS   A N   
2418 C  CA  . LYS   A 110 ? 0.1368 0.1303 0.1596 -0.0051 0.0000  0.0081  110 LYS   A CA  
2419 C  C   . LYS   A 110 ? 0.1349 0.1227 0.1524 -0.0094 -0.0002 0.0018  110 LYS   A C   
2420 O  O   . LYS   A 110 ? 0.1331 0.1263 0.1620 -0.0080 0.0056  -0.0008 110 LYS   A O   
2421 C  CB  . LYS   A 110 ? 0.1382 0.1404 0.1786 -0.0014 -0.0060 -0.0050 110 LYS   A CB  
2422 C  CG  . LYS   A 110 ? 0.1427 0.1359 0.1848 0.0020  -0.0016 -0.0011 110 LYS   A CG  
2423 C  CD  . LYS   A 110 ? 0.1496 0.1407 0.2034 -0.0064 -0.0009 -0.0034 110 LYS   A CD  
2424 C  CE  . LYS   A 110 ? 0.1587 0.1451 0.2309 -0.0082 0.0210  -0.0112 110 LYS   A CE  
2425 N  NZ  . LYS   A 110 ? 0.1583 0.1487 0.2356 -0.0161 0.0254  -0.0112 110 LYS   A NZ  
2439 N  N   . SER   A 111 ? 0.1366 0.1287 0.1528 -0.0028 0.0061  0.0081  111 SER   A N   
2440 C  CA  . SER   A 111 ? 0.1293 0.1340 0.1566 0.0001  0.0114  0.0008  111 SER   A CA  
2441 C  C   . SER   A 111 ? 0.1245 0.1267 0.1526 -0.0045 0.0069  0.0090  111 SER   A C   
2442 O  O   . SER   A 111 ? 0.1377 0.1264 0.1700 -0.0027 0.0072  0.0090  111 SER   A O   
2443 C  CB  . SER   A 111 ? 0.1490 0.1564 0.1639 0.0016  0.0226  -0.0070 111 SER   A CB  
2444 O  OG  . SER   A 111 ? 0.1937 0.1772 0.1672 0.0073  0.0302  -0.0139 111 SER   A OG  
2450 N  N   . ALA   A 112 ? 0.1342 0.1198 0.1516 -0.0014 0.0132  0.0024  112 ALA   A N   
2451 C  CA  . ALA   A 112 ? 0.1367 0.1169 0.1555 -0.0037 0.0217  0.0062  112 ALA   A CA  
2452 C  C   . ALA   A 112 ? 0.1327 0.1097 0.1539 0.0052  0.0063  0.0060  112 ALA   A C   
2453 O  O   . ALA   A 112 ? 0.1353 0.1182 0.1573 -0.0099 0.0172  0.0076  112 ALA   A O   
2454 C  CB  . ALA   A 112 ? 0.1481 0.1192 0.1627 -0.0063 0.0215  0.0067  112 ALA   A CB  
2460 N  N   . TYR   A 113 ? 0.1216 0.1194 0.1589 -0.0030 0.0085  0.0093  113 TYR   A N   
2461 C  CA  . TYR   A 113 ? 0.1254 0.1165 0.1518 -0.0043 0.0145  0.0129  113 TYR   A CA  
2462 C  C   . TYR   A 113 ? 0.1174 0.1167 0.1425 -0.0097 0.0052  0.0046  113 TYR   A C   
2463 O  O   . TYR   A 113 ? 0.1243 0.1244 0.1529 -0.0048 0.0104  0.0087  113 TYR   A O   
2464 C  CB  . TYR   A 113 ? 0.1248 0.1304 0.1525 -0.0066 0.0093  0.0173  113 TYR   A CB  
2465 C  CG  . TYR   A 113 ? 0.1265 0.1284 0.1434 -0.0080 0.0113  0.0206  113 TYR   A CG  
2466 C  CD1 . TYR   A 113 ? 0.1300 0.1370 0.1472 0.0044  0.0083  0.0213  113 TYR   A CD1 
2467 C  CD2 . TYR   A 113 ? 0.1332 0.1295 0.1444 -0.0081 0.0116  0.0190  113 TYR   A CD2 
2468 C  CE1 . TYR   A 113 ? 0.1365 0.1439 0.1532 -0.0017 0.0048  0.0184  113 TYR   A CE1 
2469 C  CE2 . TYR   A 113 ? 0.1353 0.1400 0.1501 -0.0084 0.0033  0.0209  113 TYR   A CE2 
2470 C  CZ  . TYR   A 113 ? 0.1347 0.1422 0.1480 0.0059  0.0060  0.0209  113 TYR   A CZ  
2471 O  OH  . TYR   A 113 ? 0.1393 0.1484 0.1592 0.0163  0.0036  0.0160  113 TYR   A OH  
2481 N  N   . GLU   A 114 ? 0.1216 0.1209 0.1616 -0.0016 0.0119  0.0108  114 GLU   A N   
2482 C  CA  . GLU   A 114 ? 0.1251 0.1123 0.1645 0.0028  0.0097  0.0164  114 GLU   A CA  
2483 C  C   . GLU   A 114 ? 0.1193 0.1209 0.1747 -0.0007 0.0147  0.0114  114 GLU   A C   
2484 O  O   . GLU   A 114 ? 0.1291 0.1281 0.1638 0.0002  0.0021  0.0144  114 GLU   A O   
2485 C  CB  . GLU   A 114 ? 0.1247 0.1241 0.1654 -0.0052 0.0046  0.0110  114 GLU   A CB  
2486 C  CG  . GLU   A 114 ? 0.1335 0.1219 0.1627 -0.0014 0.0103  0.0005  114 GLU   A CG  
2487 C  CD  . GLU   A 114 ? 0.1388 0.1263 0.1763 -0.0079 0.0030  0.0005  114 GLU   A CD  
2488 O  OE1 . GLU   A 114 ? 0.1464 0.1264 0.1817 -0.0083 0.0148  -0.0050 114 GLU   A OE1 
2489 O  OE2 . GLU   A 114 ? 0.1516 0.1387 0.1985 -0.0108 0.0096  -0.0161 114 GLU   A OE2 
2496 N  N   . ASN   A 115 ? 0.1236 0.1263 0.1522 -0.0081 0.0094  0.0080  115 ASN   A N   
2497 C  CA  . ASN   A 115 ? 0.1252 0.1260 0.1557 -0.0070 0.0101  0.0128  115 ASN   A CA  
2498 C  C   . ASN   A 115 ? 0.1305 0.1243 0.1371 -0.0100 0.0021  0.0152  115 ASN   A C   
2499 O  O   . ASN   A 115 ? 0.1313 0.1376 0.1472 -0.0070 0.0053  0.0166  115 ASN   A O   
2500 C  CB  . ASN   A 115 ? 0.1354 0.1370 0.1608 -0.0150 0.0098  0.0086  115 ASN   A CB  
2501 C  CG  . ASN   A 115 ? 0.1358 0.1592 0.1665 -0.0232 0.0203  0.0143  115 ASN   A CG  
2502 O  OD1 . ASN   A 115 ? 0.1414 0.2536 0.1881 -0.0224 0.0236  0.0308  115 ASN   A OD1 
2503 N  ND2 . ASN   A 115 ? 0.1373 0.1353 0.1673 -0.0124 0.0276  0.0102  115 ASN   A ND2 
2510 N  N   . PHE   A 116 ? 0.1253 0.1234 0.1512 -0.0033 0.0086  0.0208  116 PHE   A N   
2511 C  CA  . PHE   A 116 ? 0.1258 0.1357 0.1453 -0.0020 0.0073  0.0228  116 PHE   A CA  
2512 C  C   . PHE   A 116 ? 0.1179 0.1404 0.1573 -0.0057 0.0136  0.0303  116 PHE   A C   
2513 O  O   . PHE   A 116 ? 0.1278 0.1424 0.1613 0.0010  0.0134  0.0292  116 PHE   A O   
2514 C  CB  . PHE   A 116 ? 0.1249 0.1266 0.1529 -0.0039 0.0117  0.0176  116 PHE   A CB  
2515 C  CG  . PHE   A 116 ? 0.1264 0.1330 0.1441 -0.0073 0.0094  0.0152  116 PHE   A CG  
2516 C  CD1 . PHE   A 116 ? 0.1238 0.1270 0.1421 -0.0042 0.0026  0.0054  116 PHE   A CD1 
2517 C  CD2 . PHE   A 116 ? 0.1245 0.1397 0.1579 -0.0070 0.0160  0.0237  116 PHE   A CD2 
2518 C  CE1 . PHE   A 116 ? 0.1264 0.1272 0.1557 -0.0151 0.0068  0.0082  116 PHE   A CE1 
2519 C  CE2 . PHE   A 116 ? 0.1267 0.1335 0.1598 -0.0070 0.0142  0.0148  116 PHE   A CE2 
2520 C  CZ  . PHE   A 116 ? 0.1351 0.1188 0.1437 -0.0017 0.0010  0.0164  116 PHE   A CZ  
2530 N  N   . ASN   A 117 ? 0.1246 0.1295 0.1698 -0.0019 0.0116  0.0219  117 ASN   A N   
2531 C  CA  . ASN   A 117 ? 0.1279 0.1299 0.1806 -0.0026 0.0139  0.0266  117 ASN   A CA  
2532 C  C   . ASN   A 117 ? 0.1237 0.1388 0.1826 0.0026  0.0108  0.0252  117 ASN   A C   
2533 O  O   . ASN   A 117 ? 0.1399 0.1429 0.2039 -0.0052 -0.0069 0.0399  117 ASN   A O   
2534 C  CB  . ASN   A 117 ? 0.1323 0.1363 0.1705 -0.0023 0.0129  0.0288  117 ASN   A CB  
2535 C  CG  . ASN   A 117 ? 0.1271 0.1321 0.1786 -0.0070 0.0138  0.0296  117 ASN   A CG  
2536 O  OD1 . ASN   A 117 ? 0.1303 0.1528 0.1920 -0.0158 0.0132  0.0236  117 ASN   A OD1 
2537 N  ND2 . ASN   A 117 ? 0.1191 0.1350 0.1807 -0.0032 0.0088  0.0227  117 ASN   A ND2 
2544 N  N   . GLN   A 118 ? 0.1266 0.1362 0.1852 -0.0093 0.0028  0.0259  118 GLN   A N   
2545 C  CA  . GLN   A 118 ? 0.1371 0.1526 0.1909 -0.0107 -0.0008 0.0225  118 GLN   A CA  
2546 C  C   . GLN   A 118 ? 0.1369 0.1597 0.1823 -0.0133 0.0001  0.0307  118 GLN   A C   
2547 O  O   . GLN   A 118 ? 0.1343 0.1866 0.2043 -0.0068 -0.0096 0.0108  118 GLN   A O   
2548 C  CB  . GLN   A 118 ? 0.1250 0.1481 0.2041 -0.0058 0.0059  0.0249  118 GLN   A CB  
2549 C  CG  . GLN   A 118 ? 0.1237 0.1593 0.2032 -0.0051 0.0108  0.0296  118 GLN   A CG  
2550 C  CD  . GLN   A 118 ? 0.1279 0.1616 0.2066 0.0005  0.0039  0.0234  118 GLN   A CD  
2551 O  OE1 . GLN   A 118 ? 0.1320 0.1673 0.2214 0.0098  0.0007  0.0129  118 GLN   A OE1 
2552 N  NE2 . GLN   A 118 ? 0.1407 0.1530 0.2062 0.0012  0.0065  0.0266  118 GLN   A NE2 
2561 N  N   . HIS   A 119 ? 0.1411 0.1583 0.1730 -0.0079 0.0021  0.0348  119 HIS   A N   
2562 C  CA  . HIS   A 119 ? 0.1471 0.1644 0.1633 -0.0093 -0.0049 0.0345  119 HIS   A CA  
2563 C  C   . HIS   A 119 ? 0.1547 0.1714 0.1550 -0.0115 0.0035  0.0380  119 HIS   A C   
2564 O  O   . HIS   A 119 ? 0.1556 0.1835 0.1565 -0.0255 -0.0075 0.0352  119 HIS   A O   
2565 C  CB  . HIS   A 119 ? 0.1532 0.1586 0.1755 -0.0052 0.0120  0.0348  119 HIS   A CB  
2566 C  CG  . HIS   A 119 ? 0.1498 0.1587 0.2291 0.0010  0.0174  0.0438  119 HIS   A CG  
2567 N  ND1 . HIS   A 119 ? 0.1631 0.1757 0.2894 -0.0073 0.0105  0.0361  119 HIS   A ND1 
2568 C  CD2 . HIS   A 119 ? 0.1607 0.1673 0.2459 0.0137  0.0380  0.0703  119 HIS   A CD2 
2569 C  CE1 . HIS   A 119 ? 0.1626 0.1751 0.3112 -0.0122 0.0229  0.0549  119 HIS   A CE1 
2570 N  NE2 . HIS   A 119 ? 0.1674 0.1772 0.3023 0.0023  0.0394  0.0719  119 HIS   A NE2 
2578 N  N   . GLU   A 120 ? 0.1591 0.1884 0.1621 -0.0056 -0.0098 0.0610  120 GLU   A N   
2579 C  CA  . GLU   A 120 ? 0.1882 0.2205 0.1872 0.0014  -0.0165 0.0983  120 GLU   A CA  
2580 C  C   . GLU   A 120 ? 0.1628 0.2058 0.1701 -0.0049 -0.0165 0.0838  120 GLU   A C   
2581 O  O   . GLU   A 120 ? 0.1623 0.2016 0.1784 -0.0165 -0.0091 0.0767  120 GLU   A O   
2582 C  CB  . GLU   A 120 ? 0.2515 0.2899 0.2473 0.0202  -0.0234 0.1465  120 GLU   A CB  
2583 C  CG  . GLU   A 120 ? 0.3378 0.3582 0.3580 0.0345  -0.0217 0.1590  120 GLU   A CG  
2584 C  CD  . GLU   A 120 ? 0.4084 0.4202 0.4796 0.0461  -0.0147 0.1503  120 GLU   A CD  
2585 O  OE1 . GLU   A 120 ? 0.4396 0.4414 0.5066 0.0486  -0.0149 0.1472  120 GLU   A OE1 
2586 O  OE2 . GLU   A 120 ? 0.4772 0.4772 0.5407 0.0500  -0.0115 0.1471  120 GLU   A OE2 
2593 N  N   . VAL   A 121 ? 0.1594 0.2026 0.1565 -0.0079 -0.0027 0.0739  121 VAL   A N   
2594 C  CA  . VAL   A 121 ? 0.1702 0.2101 0.1392 -0.0112 0.0123  0.0695  121 VAL   A CA  
2595 C  C   . VAL   A 121 ? 0.1570 0.1876 0.1171 -0.0207 -0.0008 0.0479  121 VAL   A C   
2596 O  O   . VAL   A 121 ? 0.1570 0.1872 0.1407 -0.0252 -0.0090 0.0417  121 VAL   A O   
2597 C  CB  . VAL   A 121 ? 0.2033 0.2518 0.1788 0.0040  0.0192  0.0706  121 VAL   A CB  
2598 C  CG1 . VAL   A 121 ? 0.2052 0.2691 0.1751 0.0109  0.0337  0.0773  121 VAL   A CG1 
2599 C  CG2 . VAL   A 121 ? 0.2264 0.2673 0.2301 -0.0053 0.0082  0.0603  121 VAL   A CG2 
2609 N  N   . LEU   A 122 ? 0.1490 0.1664 0.1249 -0.0241 -0.0015 0.0431  122 LEU   A N   
2610 C  CA  . LEU   A 122 ? 0.1524 0.1517 0.1172 -0.0174 0.0119  0.0321  122 LEU   A CA  
2611 C  C   . LEU   A 122 ? 0.1448 0.1548 0.1093 -0.0206 -0.0012 0.0334  122 LEU   A C   
2612 O  O   . LEU   A 122 ? 0.1439 0.1624 0.1553 -0.0296 -0.0050 0.0319  122 LEU   A O   
2613 C  CB  . LEU   A 122 ? 0.1649 0.1552 0.1636 -0.0082 0.0022  0.0458  122 LEU   A CB  
2614 C  CG  . LEU   A 122 ? 0.1621 0.1649 0.1572 -0.0047 0.0099  0.0328  122 LEU   A CG  
2615 C  CD1 . LEU   A 122 ? 0.1765 0.1695 0.1713 -0.0144 0.0161  0.0325  122 LEU   A CD1 
2616 C  CD2 . LEU   A 122 ? 0.1617 0.1609 0.1515 -0.0069 0.0210  0.0345  122 LEU   A CD2 
2628 N  N   . LEU   A 123 ? 0.1393 0.1574 0.1223 -0.0200 -0.0032 0.0295  123 LEU   A N   
2629 C  CA  . LEU   A 123 ? 0.1383 0.1492 0.1183 -0.0205 0.0006  0.0298  123 LEU   A CA  
2630 C  C   . LEU   A 123 ? 0.1377 0.1498 0.1073 -0.0187 -0.0036 0.0276  123 LEU   A C   
2631 O  O   . LEU   A 123 ? 0.1298 0.1617 0.1169 -0.0274 -0.0040 0.0256  123 LEU   A O   
2632 C  CB  . LEU   A 123 ? 0.1498 0.1564 0.1199 -0.0183 0.0073  0.0224  123 LEU   A CB  
2633 C  CG  . LEU   A 123 ? 0.1573 0.1781 0.1226 -0.0121 0.0088  0.0086  123 LEU   A CG  
2634 C  CD1 . LEU   A 123 ? 0.1587 0.1859 0.1361 -0.0111 0.0047  0.0045  123 LEU   A CD1 
2635 C  CD2 . LEU   A 123 ? 0.1683 0.1833 0.1348 -0.0106 0.0039  0.0113  123 LEU   A CD2 
2647 N  N   A ALA   A 124 ? 0.1339 0.1420 0.0910 -0.0084 -0.0053 0.0255  124 ALA   A N   
2648 N  N   B ALA   A 124 ? 0.1315 0.1478 0.1150 -0.0236 -0.0061 0.0174  124 ALA   A N   
2649 C  CA  A ALA   A 124 ? 0.1350 0.1335 0.0927 0.0012  -0.0046 0.0243  124 ALA   A CA  
2650 C  CA  B ALA   A 124 ? 0.1287 0.1443 0.1235 -0.0280 -0.0117 0.0174  124 ALA   A CA  
2651 C  C   A ALA   A 124 ? 0.1336 0.1347 0.0994 -0.0009 0.0077  0.0256  124 ALA   A C   
2652 C  C   B ALA   A 124 ? 0.1256 0.1363 0.1134 -0.0282 -0.0045 0.0219  124 ALA   A C   
2653 O  O   A ALA   A 124 ? 0.1373 0.1424 0.1191 0.0008  0.0210  0.0278  124 ALA   A O   
2654 O  O   B ALA   A 124 ? 0.1241 0.1360 0.1361 -0.0275 -0.0014 0.0227  124 ALA   A O   
2655 C  CB  A ALA   A 124 ? 0.1308 0.1229 0.1109 0.0102  0.0019  0.0193  124 ALA   A CB  
2656 C  CB  B ALA   A 124 ? 0.1259 0.1412 0.1358 -0.0314 -0.0021 0.0125  124 ALA   A CB  
2667 N  N   A PRO   A 125 ? 0.1260 0.1365 0.1178 0.0004  0.0078  0.0182  125 PRO   A N   
2668 N  N   B PRO   A 125 ? 0.1205 0.1268 0.0924 -0.0200 -0.0017 0.0207  125 PRO   A N   
2669 C  CA  A PRO   A 125 ? 0.1297 0.1352 0.1247 0.0023  -0.0015 0.0112  125 PRO   A CA  
2670 C  CA  B PRO   A 125 ? 0.1271 0.1275 0.0993 -0.0186 -0.0039 0.0245  125 PRO   A CA  
2671 C  C   A PRO   A 125 ? 0.1239 0.1291 0.1167 0.0043  -0.0039 0.0191  125 PRO   A C   
2672 C  C   B PRO   A 125 ? 0.1255 0.1297 0.1101 -0.0193 -0.0025 0.0243  125 PRO   A C   
2673 O  O   A PRO   A 125 ? 0.1262 0.1281 0.1185 0.0121  -0.0045 0.0101  125 PRO   A O   
2674 O  O   B PRO   A 125 ? 0.1353 0.1316 0.1300 -0.0207 0.0031  0.0221  125 PRO   A O   
2675 C  CB  A PRO   A 125 ? 0.1439 0.1354 0.1223 -0.0071 0.0034  0.0007  125 PRO   A CB  
2676 C  CB  B PRO   A 125 ? 0.1315 0.1216 0.0948 -0.0194 -0.0053 0.0334  125 PRO   A CB  
2677 C  CG  A PRO   A 125 ? 0.1448 0.1415 0.1373 -0.0070 0.0057  0.0115  125 PRO   A CG  
2678 C  CG  B PRO   A 125 ? 0.1280 0.1221 0.0919 -0.0177 -0.0013 0.0255  125 PRO   A CG  
2679 C  CD  A PRO   A 125 ? 0.1342 0.1431 0.1353 -0.0032 0.0139  0.0153  125 PRO   A CD  
2680 C  CD  B PRO   A 125 ? 0.1191 0.1145 0.0811 -0.0182 0.0070  0.0152  125 PRO   A CD  
2695 N  N   A LEU   A 126 ? 0.1259 0.1338 0.1131 0.0053  0.0014  0.0167  126 LEU   A N   
2696 N  N   B LEU   A 126 ? 0.1295 0.1321 0.1099 -0.0165 -0.0030 0.0115  126 LEU   A N   
2697 C  CA  A LEU   A 126 ? 0.1308 0.1406 0.1224 0.0039  -0.0030 0.0115  126 LEU   A CA  
2698 C  CA  B LEU   A 126 ? 0.1270 0.1271 0.1178 -0.0119 0.0033  0.0070  126 LEU   A CA  
2699 C  C   A LEU   A 126 ? 0.1414 0.1374 0.1227 0.0128  -0.0089 0.0044  126 LEU   A C   
2700 C  C   B LEU   A 126 ? 0.1247 0.1241 0.1218 -0.0017 0.0194  0.0067  126 LEU   A C   
2701 O  O   A LEU   A 126 ? 0.1497 0.1397 0.1525 0.0222  0.0037  0.0099  126 LEU   A O   
2702 O  O   B LEU   A 126 ? 0.1401 0.1296 0.1417 -0.0061 0.0350  0.0358  126 LEU   A O   
2703 C  CB  A LEU   A 126 ? 0.1292 0.1359 0.1326 0.0019  -0.0036 0.0163  126 LEU   A CB  
2704 C  CB  B LEU   A 126 ? 0.1305 0.1372 0.1382 -0.0136 -0.0030 0.0055  126 LEU   A CB  
2705 C  CG  A LEU   A 126 ? 0.1259 0.1431 0.1651 0.0048  0.0083  0.0208  126 LEU   A CG  
2706 C  CG  B LEU   A 126 ? 0.1305 0.1359 0.1529 -0.0083 0.0059  0.0105  126 LEU   A CG  
2707 C  CD1 A LEU   A 126 ? 0.1328 0.1610 0.1974 0.0042  -0.0060 0.0282  126 LEU   A CD1 
2708 C  CD1 B LEU   A 126 ? 0.1322 0.1378 0.1781 -0.0154 -0.0002 0.0186  126 LEU   A CD1 
2709 C  CD2 A LEU   A 126 ? 0.1380 0.1325 0.1663 -0.0021 0.0082  0.0166  126 LEU   A CD2 
2710 C  CD2 B LEU   A 126 ? 0.1388 0.1411 0.1511 -0.0038 0.0028  0.0005  126 LEU   A CD2 
2733 N  N   A LEU   A 127 ? 0.1468 0.1422 0.1246 0.0048  -0.0079 0.0042  127 LEU   A N   
2734 N  N   B LEU   A 127 ? 0.1207 0.1200 0.1047 0.0054  0.0206  0.0082  127 LEU   A N   
2735 C  CA  A LEU   A 127 ? 0.1411 0.1335 0.1298 -0.0043 -0.0100 0.0102  127 LEU   A CA  
2736 C  CA  B LEU   A 127 ? 0.1196 0.1266 0.1169 0.0001  0.0172  0.0177  127 LEU   A CA  
2737 C  C   A LEU   A 127 ? 0.1312 0.1227 0.1175 -0.0076 -0.0168 0.0141  127 LEU   A C   
2738 C  C   B LEU   A 127 ? 0.1236 0.1336 0.1214 0.0025  0.0147  0.0004  127 LEU   A C   
2739 O  O   A LEU   A 127 ? 0.1369 0.1307 0.1295 -0.0180 -0.0182 0.0143  127 LEU   A O   
2740 O  O   B LEU   A 127 ? 0.1315 0.1398 0.1250 -0.0059 0.0310  0.0029  127 LEU   A O   
2741 C  CB  A LEU   A 127 ? 0.1419 0.1395 0.1332 0.0056  0.0022  0.0048  127 LEU   A CB  
2742 C  CB  B LEU   A 127 ? 0.1201 0.1417 0.1306 -0.0049 0.0105  0.0136  127 LEU   A CB  
2743 C  CG  A LEU   A 127 ? 0.1474 0.1433 0.1379 0.0063  -0.0060 0.0159  127 LEU   A CG  
2744 C  CG  B LEU   A 127 ? 0.1246 0.1534 0.1415 -0.0022 -0.0053 0.0177  127 LEU   A CG  
2745 C  CD1 A LEU   A 127 ? 0.1499 0.1426 0.1454 0.0042  -0.0094 0.0091  127 LEU   A CD1 
2746 C  CD1 B LEU   A 127 ? 0.1258 0.1605 0.1636 0.0034  -0.0032 0.0258  127 LEU   A CD1 
2747 C  CD2 A LEU   A 127 ? 0.1565 0.1464 0.1499 0.0062  -0.0130 0.0150  127 LEU   A CD2 
2748 C  CD2 B LEU   A 127 ? 0.1360 0.1582 0.1350 -0.0085 -0.0198 0.0067  127 LEU   A CD2 
2771 N  N   A SER   A 128 ? 0.1353 0.1307 0.1111 -0.0091 -0.0093 0.0124  128 SER   A N   
2772 N  N   B SER   A 128 ? 0.1270 0.1415 0.1319 -0.0024 0.0064  0.0041  128 SER   A N   
2773 C  CA  A SER   A 128 ? 0.1487 0.1428 0.1058 0.0014  -0.0002 0.0166  128 SER   A CA  
2774 C  CA  B SER   A 128 ? 0.1282 0.1424 0.1246 -0.0065 -0.0044 0.0018  128 SER   A CA  
2775 C  C   A SER   A 128 ? 0.1551 0.1479 0.1239 0.0101  0.0027  0.0196  128 SER   A C   
2776 C  C   B SER   A 128 ? 0.1341 0.1358 0.1278 -0.0085 -0.0249 0.0098  128 SER   A C   
2777 O  O   A SER   A 128 ? 0.1565 0.1610 0.1427 0.0057  0.0155  0.0285  128 SER   A O   
2778 O  O   B SER   A 128 ? 0.1370 0.1351 0.1346 -0.0099 -0.0328 0.0151  128 SER   A O   
2779 C  CB  A SER   A 128 ? 0.1504 0.1554 0.1146 0.0074  0.0003  0.0153  128 SER   A CB  
2780 C  CB  B SER   A 128 ? 0.1271 0.1539 0.1374 -0.0050 -0.0051 -0.0008 128 SER   A CB  
2781 O  OG  A SER   A 128 ? 0.1536 0.1621 0.1200 0.0056  0.0084  0.0188  128 SER   A OG  
2782 O  OG  B SER   A 128 ? 0.1218 0.1585 0.1414 -0.0052 -0.0039 0.0137  128 SER   A OG  
2793 N  N   A ALA   A 129 ? 0.1537 0.1435 0.1435 0.0101  0.0035  0.0151  129 ALA   A N   
2794 N  N   B ALA   A 129 ? 0.1335 0.1390 0.1468 -0.0107 -0.0281 0.0144  129 ALA   A N   
2795 C  CA  A ALA   A 129 ? 0.1447 0.1483 0.1425 0.0112  0.0006  0.0103  129 ALA   A CA  
2796 C  CA  B ALA   A 129 ? 0.1320 0.1485 0.1541 -0.0082 -0.0333 0.0037  129 ALA   A CA  
2797 C  C   A ALA   A 129 ? 0.1458 0.1436 0.1261 0.0082  0.0055  -0.0115 129 ALA   A C   
2798 C  C   B ALA   A 129 ? 0.1461 0.1576 0.1419 -0.0052 -0.0265 0.0116  129 ALA   A C   
2799 O  O   A ALA   A 129 ? 0.1526 0.1483 0.1228 0.0043  0.0136  0.0036  129 ALA   A O   
2800 O  O   B ALA   A 129 ? 0.1506 0.1675 0.1415 -0.0078 -0.0250 0.0161  129 ALA   A O   
2801 C  CB  A ALA   A 129 ? 0.1500 0.1649 0.1574 0.0059  0.0060  0.0205  129 ALA   A CB  
2802 C  CB  B ALA   A 129 ? 0.1291 0.1562 0.1685 -0.0110 -0.0243 -0.0036 129 ALA   A CB  
2813 N  N   A GLY   A 130 ? 0.1506 0.1465 0.1393 0.0028  0.0059  -0.0146 130 GLY   A N   
2814 N  N   B GLY   A 130 ? 0.1529 0.1527 0.1427 -0.0005 -0.0268 0.0131  130 GLY   A N   
2815 C  CA  A GLY   A 130 ? 0.1651 0.1539 0.1431 0.0025  0.0112  -0.0085 130 GLY   A CA  
2816 C  CA  B GLY   A 130 ? 0.1640 0.1513 0.1509 0.0027  -0.0228 0.0149  130 GLY   A CA  
2817 C  C   A GLY   A 130 ? 0.1656 0.1551 0.1269 0.0033  0.0029  -0.0062 130 GLY   A C   
2818 C  C   B GLY   A 130 ? 0.1655 0.1482 0.1566 0.0070  -0.0280 0.0258  130 GLY   A C   
2819 O  O   A GLY   A 130 ? 0.1644 0.1529 0.1333 -0.0035 0.0010  -0.0016 130 GLY   A O   
2820 O  O   B GLY   A 130 ? 0.1688 0.1551 0.1636 0.0158  -0.0211 0.0402  130 GLY   A O   
2827 N  N   A ILE   A 131 ? 0.1759 0.1584 0.1355 -0.0016 -0.0103 -0.0020 131 ILE   A N   
2828 N  N   B ILE   A 131 ? 0.1705 0.1404 0.1629 -0.0058 -0.0248 0.0307  131 ILE   A N   
2829 C  CA  A ILE   A 131 ? 0.1811 0.1625 0.1198 -0.0048 -0.0207 0.0003  131 ILE   A CA  
2830 C  CA  B ILE   A 131 ? 0.1741 0.1382 0.1554 -0.0053 -0.0274 0.0319  131 ILE   A CA  
2831 C  C   A ILE   A 131 ? 0.1762 0.1653 0.1299 -0.0036 -0.0049 0.0123  131 ILE   A C   
2832 C  C   B ILE   A 131 ? 0.1773 0.1374 0.1439 0.0004  -0.0216 0.0273  131 ILE   A C   
2833 O  O   A ILE   A 131 ? 0.1773 0.1760 0.1369 0.0014  -0.0069 0.0222  131 ILE   A O   
2834 O  O   B ILE   A 131 ? 0.1830 0.1394 0.1598 -0.0059 -0.0204 0.0258  131 ILE   A O   
2835 C  CB  A ILE   A 131 ? 0.1913 0.1699 0.1300 -0.0075 -0.0235 -0.0039 131 ILE   A CB  
2836 C  CB  B ILE   A 131 ? 0.1813 0.1525 0.1617 -0.0056 -0.0371 0.0291  131 ILE   A CB  
2837 C  CG1 A ILE   A 131 ? 0.1978 0.1893 0.1449 -0.0145 -0.0319 -0.0006 131 ILE   A CG1 
2838 C  CG1 B ILE   A 131 ? 0.1819 0.1700 0.1631 -0.0055 -0.0355 0.0357  131 ILE   A CG1 
2839 C  CG2 A ILE   A 131 ? 0.1963 0.1577 0.1447 -0.0017 -0.0199 -0.0081 131 ILE   A CG2 
2840 C  CG2 B ILE   A 131 ? 0.1862 0.1500 0.1743 -0.0080 -0.0338 0.0170  131 ILE   A CG2 
2841 C  CD1 A ILE   A 131 ? 0.2035 0.1909 0.1714 -0.0180 -0.0390 -0.0041 131 ILE   A CD1 
2842 C  CD1 B ILE   A 131 ? 0.1873 0.1798 0.1598 -0.0080 -0.0408 0.0389  131 ILE   A CD1 
2865 N  N   A PHE   A 132 ? 0.1698 0.1590 0.1377 -0.0023 0.0016  0.0128  132 PHE   A N   
2866 N  N   B PHE   A 132 ? 0.1757 0.1356 0.1422 0.0101  -0.0265 0.0169  132 PHE   A N   
2867 C  CA  A PHE   A 132 ? 0.1682 0.1596 0.1303 -0.0094 0.0062  0.0003  132 PHE   A CA  
2868 C  CA  B PHE   A 132 ? 0.1778 0.1398 0.1481 0.0021  -0.0168 0.0108  132 PHE   A CA  
2869 C  C   A PHE   A 132 ? 0.1682 0.1750 0.1389 -0.0130 -0.0061 0.0048  132 PHE   A C   
2870 C  C   B PHE   A 132 ? 0.1867 0.1600 0.1550 0.0083  -0.0218 0.0158  132 PHE   A C   
2871 O  O   A PHE   A 132 ? 0.1765 0.1822 0.1350 -0.0147 -0.0051 0.0069  132 PHE   A O   
2872 O  O   B PHE   A 132 ? 0.1990 0.1751 0.1623 0.0093  -0.0150 0.0195  132 PHE   A O   
2873 C  CB  A PHE   A 132 ? 0.1704 0.1563 0.1284 -0.0046 -0.0040 0.0130  132 PHE   A CB  
2874 C  CB  B PHE   A 132 ? 0.1678 0.1346 0.1346 -0.0005 -0.0113 0.0147  132 PHE   A CB  
2875 C  CG  A PHE   A 132 ? 0.1706 0.1533 0.1387 -0.0030 -0.0126 0.0241  132 PHE   A CG  
2876 C  CG  B PHE   A 132 ? 0.1644 0.1330 0.1244 0.0057  -0.0038 0.0001  132 PHE   A CG  
2877 C  CD1 A PHE   A 132 ? 0.1744 0.1638 0.1600 -0.0023 -0.0167 0.0157  132 PHE   A CD1 
2878 C  CD1 B PHE   A 132 ? 0.1673 0.1422 0.1429 0.0116  0.0013  -0.0116 132 PHE   A CD1 
2879 C  CD2 A PHE   A 132 ? 0.1637 0.1568 0.1571 -0.0093 -0.0128 0.0286  132 PHE   A CD2 
2880 C  CD2 B PHE   A 132 ? 0.1608 0.1422 0.1365 0.0083  -0.0051 -0.0190 132 PHE   A CD2 
2881 C  CE1 A PHE   A 132 ? 0.1736 0.1703 0.1632 -0.0052 -0.0247 0.0137  132 PHE   A CE1 
2882 C  CE1 B PHE   A 132 ? 0.1668 0.1544 0.1472 0.0116  -0.0044 -0.0158 132 PHE   A CE1 
2883 C  CE2 A PHE   A 132 ? 0.1644 0.1582 0.1654 -0.0058 -0.0282 0.0094  132 PHE   A CE2 
2884 C  CE2 B PHE   A 132 ? 0.1598 0.1497 0.1435 0.0141  -0.0075 -0.0248 132 PHE   A CE2 
2885 C  CZ  A PHE   A 132 ? 0.1709 0.1649 0.1641 -0.0060 -0.0273 0.0093  132 PHE   A CZ  
2886 C  CZ  B PHE   A 132 ? 0.1651 0.1541 0.1494 0.0113  -0.0101 -0.0181 132 PHE   A CZ  
2905 N  N   A GLY   A 133 ? 0.1659 0.1802 0.1260 -0.0044 -0.0198 0.0188  133 GLY   A N   
2906 N  N   B GLY   A 133 ? 0.1837 0.1668 0.1496 0.0080  -0.0317 0.0198  133 GLY   A N   
2907 C  CA  A GLY   A 133 ? 0.1743 0.1880 0.1357 -0.0099 -0.0254 0.0112  133 GLY   A CA  
2908 C  CA  B GLY   A 133 ? 0.1846 0.1698 0.1562 0.0037  -0.0327 0.0077  133 GLY   A CA  
2909 C  C   A GLY   A 133 ? 0.1820 0.1959 0.1416 -0.0109 -0.0377 0.0014  133 GLY   A C   
2910 C  C   B GLY   A 133 ? 0.1866 0.1816 0.1556 0.0058  -0.0415 -0.0063 133 GLY   A C   
2911 O  O   A GLY   A 133 ? 0.1998 0.2029 0.1665 -0.0050 -0.0326 -0.0203 133 GLY   A O   
2912 O  O   B GLY   A 133 ? 0.1928 0.1920 0.1563 0.0111  -0.0485 -0.0197 133 GLY   A O   
2919 N  N   A ALA   A 134 ? 0.1853 0.1878 0.1334 -0.0184 -0.0282 0.0106  134 ALA   A N   
2920 N  N   B ALA   A 134 ? 0.1908 0.1768 0.1572 0.0058  -0.0271 -0.0061 134 ALA   A N   
2921 C  CA  A ALA   A 134 ? 0.1859 0.1910 0.1529 -0.0159 -0.0334 0.0023  134 ALA   A CA  
2922 C  CA  B ALA   A 134 ? 0.1915 0.1737 0.1664 0.0081  -0.0235 -0.0113 134 ALA   A CA  
2923 C  C   A ALA   A 134 ? 0.1829 0.1931 0.1513 -0.0209 -0.0337 0.0084  134 ALA   A C   
2924 C  C   B ALA   A 134 ? 0.1884 0.1657 0.1683 0.0007  -0.0169 -0.0018 134 ALA   A C   
2925 O  O   A ALA   A 134 ? 0.1959 0.2002 0.1755 -0.0241 -0.0206 0.0055  134 ALA   A O   
2926 O  O   B ALA   A 134 ? 0.1896 0.1627 0.1782 0.0018  0.0006  0.0026  134 ALA   A O   
2927 C  CB  A ALA   A 134 ? 0.1985 0.1880 0.1741 -0.0114 -0.0387 -0.0071 134 ALA   A CB  
2928 C  CB  B ALA   A 134 ? 0.2006 0.1738 0.1856 0.0125  -0.0261 -0.0166 134 ALA   A CB  
2939 N  N   A ASP   A 135 ? 0.1854 0.1924 0.1565 -0.0167 -0.0264 0.0173  135 ASP   A N   
2940 N  N   B ASP   A 135 ? 0.1970 0.1686 0.1769 -0.0086 -0.0214 0.0049  135 ASP   A N   
2941 C  CA  A ASP   A 135 ? 0.1851 0.1875 0.1748 -0.0131 -0.0342 0.0184  135 ASP   A CA  
2942 C  CA  B ASP   A 135 ? 0.1963 0.1733 0.1953 -0.0144 -0.0319 0.0041  135 ASP   A CA  
2943 C  C   A ASP   A 135 ? 0.1739 0.1731 0.1838 -0.0082 -0.0248 0.0305  135 ASP   A C   
2944 C  C   B ASP   A 135 ? 0.1826 0.1581 0.1902 -0.0095 -0.0235 0.0040  135 ASP   A C   
2945 O  O   A ASP   A 135 ? 0.1746 0.1726 0.1851 -0.0005 -0.0235 0.0378  135 ASP   A O   
2946 O  O   B ASP   A 135 ? 0.1795 0.1474 0.1751 -0.0119 -0.0201 0.0057  135 ASP   A O   
2947 C  CB  A ASP   A 135 ? 0.2076 0.2074 0.2039 -0.0246 -0.0432 0.0137  135 ASP   A CB  
2948 C  CB  B ASP   A 135 ? 0.2097 0.1902 0.2166 -0.0230 -0.0469 -0.0044 135 ASP   A CB  
2949 C  CG  A ASP   A 135 ? 0.2252 0.2196 0.2521 -0.0397 -0.0530 0.0082  135 ASP   A CG  
2950 C  CG  B ASP   A 135 ? 0.2221 0.2091 0.2536 -0.0263 -0.0529 -0.0102 135 ASP   A CG  
2951 O  OD1 A ASP   A 135 ? 0.2243 0.2224 0.2609 -0.0494 -0.0681 0.0218  135 ASP   A OD1 
2952 O  OD1 B ASP   A 135 ? 0.2265 0.2136 0.2719 -0.0194 -0.0568 -0.0100 135 ASP   A OD1 
2953 O  OD2 A ASP   A 135 ? 0.2484 0.2327 0.2919 -0.0423 -0.0317 0.0028  135 ASP   A OD2 
2954 O  OD2 B ASP   A 135 ? 0.2304 0.2225 0.2813 -0.0284 -0.0545 -0.0082 135 ASP   A OD2 
2963 N  N   A PRO   A 136 ? 0.1570 0.1632 0.1950 0.0019  -0.0207 0.0425  136 PRO   A N   
2964 N  N   B PRO   A 136 ? 0.1696 0.1570 0.1916 0.0001  -0.0192 0.0030  136 PRO   A N   
2965 C  CA  A PRO   A 136 ? 0.1492 0.1584 0.2015 -0.0031 -0.0035 0.0290  136 PRO   A CA  
2966 C  CA  B PRO   A 136 ? 0.1626 0.1629 0.1925 0.0004  -0.0080 -0.0062 136 PRO   A CA  
2967 C  C   A PRO   A 136 ? 0.1332 0.1542 0.1936 -0.0049 0.0002  0.0220  136 PRO   A C   
2968 C  C   B PRO   A 136 ? 0.1561 0.1634 0.1774 0.0021  -0.0001 -0.0039 136 PRO   A C   
2969 O  O   A PRO   A 136 ? 0.1313 0.1604 0.1877 -0.0091 -0.0023 0.0194  136 PRO   A O   
2970 O  O   B PRO   A 136 ? 0.1568 0.1546 0.1611 0.0107  0.0120  0.0050  136 PRO   A O   
2971 C  CB  A PRO   A 136 ? 0.1654 0.1553 0.2305 0.0011  0.0068  0.0300  136 PRO   A CB  
2972 C  CB  B PRO   A 136 ? 0.1722 0.1623 0.2105 0.0016  -0.0080 -0.0112 136 PRO   A CB  
2973 C  CG  A PRO   A 136 ? 0.1745 0.1621 0.2444 0.0080  0.0014  0.0362  136 PRO   A CG  
2974 C  CG  B PRO   A 136 ? 0.1799 0.1623 0.2220 0.0052  -0.0116 -0.0085 136 PRO   A CG  
2975 C  CD  A PRO   A 136 ? 0.1676 0.1590 0.2244 0.0056  -0.0069 0.0408  136 PRO   A CD  
2976 C  CD  B PRO   A 136 ? 0.1745 0.1568 0.2101 0.0045  -0.0108 0.0092  136 PRO   A CD  
2991 N  N   A ILE   A 137 ? 0.1323 0.1606 0.2025 -0.0062 -0.0165 0.0271  137 ILE   A N   
2992 N  N   B ILE   A 137 ? 0.1586 0.1714 0.1963 -0.0077 -0.0080 -0.0008 137 ILE   A N   
2993 C  CA  A ILE   A 137 ? 0.1325 0.1637 0.2024 -0.0148 -0.0190 0.0267  137 ILE   A CA  
2994 C  CA  B ILE   A 137 ? 0.1614 0.1808 0.1953 -0.0088 -0.0079 -0.0062 137 ILE   A CA  
2995 C  C   A ILE   A 137 ? 0.1357 0.1641 0.1703 -0.0161 -0.0214 0.0186  137 ILE   A C   
2996 C  C   B ILE   A 137 ? 0.1558 0.1760 0.1724 -0.0118 -0.0022 -0.0070 137 ILE   A C   
2997 O  O   A ILE   A 137 ? 0.1460 0.1580 0.1693 -0.0167 -0.0122 0.0107  137 ILE   A O   
2998 O  O   B ILE   A 137 ? 0.1549 0.1758 0.1757 -0.0135 0.0037  0.0010  137 ILE   A O   
2999 C  CB  A ILE   A 137 ? 0.1367 0.1793 0.2365 -0.0179 -0.0240 0.0279  137 ILE   A CB  
3000 C  CB  B ILE   A 137 ? 0.1729 0.1859 0.2256 -0.0094 -0.0197 -0.0025 137 ILE   A CB  
3001 C  CG1 A ILE   A 137 ? 0.1417 0.1949 0.2666 -0.0193 -0.0239 0.0390  137 ILE   A CG1 
3002 C  CG1 B ILE   A 137 ? 0.1869 0.1978 0.2549 -0.0058 -0.0281 0.0149  137 ILE   A CG1 
3003 C  CG2 A ILE   A 137 ? 0.1442 0.1836 0.2396 -0.0164 -0.0176 0.0041  137 ILE   A CG2 
3004 C  CG2 B ILE   A 137 ? 0.1737 0.1864 0.2297 -0.0054 -0.0199 -0.0144 137 ILE   A CG2 
3005 C  CD1 A ILE   A 137 ? 0.1488 0.2054 0.2785 -0.0138 -0.0250 0.0410  137 ILE   A CD1 
3006 C  CD1 B ILE   A 137 ? 0.1980 0.2070 0.2772 -0.0080 -0.0249 0.0239  137 ILE   A CD1 
3029 N  N   A HIS   A 138 ? 0.1417 0.1774 0.1604 -0.0131 -0.0159 0.0264  138 HIS   A N   
3030 N  N   B HIS   A 138 ? 0.1560 0.1829 0.1717 -0.0106 0.0085  -0.0042 138 HIS   A N   
3031 C  CA  A HIS   A 138 ? 0.1497 0.1881 0.1516 -0.0147 -0.0092 0.0235  138 HIS   A CA  
3032 C  CA  B HIS   A 138 ? 0.1586 0.1831 0.1619 -0.0119 0.0098  -0.0014 138 HIS   A CA  
3033 C  C   A HIS   A 138 ? 0.1395 0.1809 0.1506 -0.0106 -0.0092 0.0192  138 HIS   A C   
3034 C  C   B HIS   A 138 ? 0.1463 0.1811 0.1576 -0.0084 0.0081  0.0147  138 HIS   A C   
3035 O  O   A HIS   A 138 ? 0.1459 0.1782 0.1523 -0.0104 -0.0044 0.0132  138 HIS   A O   
3036 O  O   B HIS   A 138 ? 0.1502 0.1842 0.1611 -0.0046 0.0132  0.0175  138 HIS   A O   
3037 C  CB  A HIS   A 138 ? 0.1703 0.2131 0.1522 -0.0179 -0.0162 0.0246  138 HIS   A CB  
3038 C  CB  B HIS   A 138 ? 0.1666 0.1928 0.1542 -0.0125 0.0082  -0.0210 138 HIS   A CB  
3039 C  CG  A HIS   A 138 ? 0.1862 0.2254 0.1622 -0.0225 -0.0144 0.0290  138 HIS   A CG  
3040 C  CG  B HIS   A 138 ? 0.1776 0.1972 0.1589 -0.0157 0.0018  -0.0363 138 HIS   A CG  
3041 N  ND1 A HIS   A 138 ? 0.1993 0.2381 0.1939 -0.0252 -0.0027 0.0217  138 HIS   A ND1 
3042 N  ND1 B HIS   A 138 ? 0.1875 0.2057 0.1831 -0.0158 0.0037  -0.0436 138 HIS   A ND1 
3043 C  CD2 A HIS   A 138 ? 0.1911 0.2329 0.1677 -0.0204 -0.0090 0.0329  138 HIS   A CD2 
3044 C  CD2 B HIS   A 138 ? 0.1797 0.2012 0.1588 -0.0113 0.0070  -0.0357 138 HIS   A CD2 
3045 C  CE1 A HIS   A 138 ? 0.2038 0.2436 0.1976 -0.0144 -0.0030 0.0231  138 HIS   A CE1 
3046 C  CE1 B HIS   A 138 ? 0.1900 0.2069 0.1807 -0.0087 0.0040  -0.0458 138 HIS   A CE1 
3047 N  NE2 A HIS   A 138 ? 0.1985 0.2419 0.1748 -0.0136 0.0028  0.0277  138 HIS   A NE2 
3048 N  NE2 B HIS   A 138 ? 0.1866 0.2065 0.1626 -0.0083 0.0085  -0.0427 138 HIS   A NE2 
3063 N  N   . SER   A 139 ? 0.1333 0.1728 0.1617 -0.0072 -0.0043 0.0264  139 SER   A N   
3064 C  CA  . SER   A 139 ? 0.1324 0.1702 0.1517 -0.0100 0.0062  0.0244  139 SER   A CA  
3065 C  C   . SER   A 139 ? 0.1305 0.1582 0.1487 -0.0065 0.0080  0.0124  139 SER   A C   
3066 O  O   . SER   A 139 ? 0.1243 0.1521 0.1649 -0.0097 0.0008  0.0211  139 SER   A O   
3067 C  CB  . SER   A 139 ? 0.1321 0.1689 0.1618 -0.0149 -0.0059 0.0229  139 SER   A CB  
3068 O  OG  . SER   A 139 ? 0.1380 0.1681 0.1665 -0.0181 -0.0188 0.0315  139 SER   A OG  
3075 N  N   A LEU   A 140 ? 0.1277 0.1642 0.1478 -0.0012 -0.0042 0.0263  140 LEU   A N   
3076 N  N   B LEU   A 140 ? 0.1290 0.1550 0.1398 -0.0124 0.0180  0.0228  140 LEU   A N   
3077 C  CA  A LEU   A 140 ? 0.1276 0.1566 0.1489 0.0040  -0.0096 0.0190  140 LEU   A CA  
3078 C  CA  B LEU   A 140 ? 0.1273 0.1415 0.1295 -0.0174 0.0216  0.0126  140 LEU   A CA  
3079 C  C   A LEU   A 140 ? 0.1215 0.1641 0.1421 0.0026  -0.0092 0.0144  140 LEU   A C   
3080 C  C   B LEU   A 140 ? 0.1262 0.1473 0.1237 -0.0216 0.0212  0.0142  140 LEU   A C   
3081 O  O   A LEU   A 140 ? 0.1275 0.1649 0.1541 0.0082  0.0033  0.0201  140 LEU   A O   
3082 O  O   B LEU   A 140 ? 0.1330 0.1428 0.1381 -0.0160 0.0163  0.0064  140 LEU   A O   
3083 C  CB  A LEU   A 140 ? 0.1355 0.1570 0.1623 0.0018  -0.0146 0.0177  140 LEU   A CB  
3084 C  CB  B LEU   A 140 ? 0.1252 0.1362 0.1260 -0.0208 0.0187  0.0098  140 LEU   A CB  
3085 C  CG  A LEU   A 140 ? 0.1386 0.1516 0.1623 -0.0013 -0.0059 0.0164  140 LEU   A CG  
3086 C  CG  B LEU   A 140 ? 0.1209 0.1314 0.1434 -0.0209 0.0165  0.0178  140 LEU   A CG  
3087 C  CD1 A LEU   A 140 ? 0.1406 0.1438 0.1711 0.0051  -0.0054 0.0041  140 LEU   A CD1 
3088 C  CD1 B LEU   A 140 ? 0.1232 0.1295 0.1396 -0.0117 0.0242  0.0161  140 LEU   A CD1 
3089 C  CD2 A LEU   A 140 ? 0.1495 0.1575 0.1699 0.0043  0.0006  0.0133  140 LEU   A CD2 
3090 C  CD2 B LEU   A 140 ? 0.1151 0.1324 0.1590 -0.0144 0.0145  0.0348  140 LEU   A CD2 
3113 N  N   A ARG   A 141 ? 0.1340 0.1745 0.1479 0.0043  -0.0118 0.0075  141 ARG   A N   
3114 N  N   B ARG   A 141 ? 0.1350 0.1581 0.1328 -0.0226 0.0207  0.0188  141 ARG   A N   
3115 C  CA  A ARG   A 141 ? 0.1460 0.1822 0.1683 -0.0088 -0.0067 -0.0096 141 ARG   A CA  
3116 C  CA  B ARG   A 141 ? 0.1354 0.1666 0.1321 -0.0276 0.0228  0.0150  141 ARG   A CA  
3117 C  C   A ARG   A 141 ? 0.1409 0.1642 0.1820 -0.0027 -0.0070 -0.0137 141 ARG   A C   
3118 C  C   B ARG   A 141 ? 0.1336 0.1555 0.1414 -0.0249 0.0091  0.0140  141 ARG   A C   
3119 O  O   A ARG   A 141 ? 0.1406 0.1551 0.1937 -0.0036 0.0013  -0.0113 141 ARG   A O   
3120 O  O   B ARG   A 141 ? 0.1380 0.1493 0.1532 -0.0314 0.0035  0.0223  141 ARG   A O   
3121 C  CB  A ARG   A 141 ? 0.1625 0.2034 0.1863 -0.0201 -0.0063 -0.0180 141 ARG   A CB  
3122 C  CB  B ARG   A 141 ? 0.1413 0.1834 0.1386 -0.0362 0.0303  0.0116  141 ARG   A CB  
3123 C  CG  A ARG   A 141 ? 0.1886 0.2287 0.2225 -0.0239 -0.0121 -0.0186 141 ARG   A CG  
3124 C  CG  B ARG   A 141 ? 0.1551 0.1934 0.1715 -0.0342 0.0292  0.0085  141 ARG   A CG  
3125 C  CD  A ARG   A 141 ? 0.2008 0.2414 0.2386 -0.0350 -0.0136 -0.0193 141 ARG   A CD  
3126 C  CD  B ARG   A 141 ? 0.1617 0.1877 0.1997 -0.0361 0.0188  0.0065  141 ARG   A CD  
3127 N  NE  A ARG   A 141 ? 0.2015 0.2553 0.2610 -0.0388 -0.0022 -0.0106 141 ARG   A NE  
3128 N  NE  B ARG   A 141 ? 0.1720 0.2025 0.2094 -0.0282 0.0213  0.0084  141 ARG   A NE  
3129 C  CZ  A ARG   A 141 ? 0.1978 0.2724 0.2735 -0.0500 0.0033  -0.0063 141 ARG   A CZ  
3130 C  CZ  B ARG   A 141 ? 0.1779 0.2081 0.2108 -0.0276 0.0278  0.0159  141 ARG   A CZ  
3131 N  NH1 A ARG   A 141 ? 0.1991 0.2816 0.2804 -0.0501 0.0054  -0.0036 141 ARG   A NH1 
3132 N  NH1 B ARG   A 141 ? 0.1826 0.2175 0.2074 -0.0291 0.0354  0.0160  141 ARG   A NH1 
3133 N  NH2 A ARG   A 141 ? 0.1974 0.2820 0.2792 -0.0471 0.0022  -0.0003 141 ARG   A NH2 
3134 N  NH2 B ARG   A 141 ? 0.1842 0.2145 0.2209 -0.0218 0.0323  0.0224  141 ARG   A NH2 
3161 N  N   A VAL   A 142 ? 0.1315 0.1602 0.1823 -0.0022 -0.0034 -0.0064 142 VAL   A N   
3162 N  N   B VAL   A 142 ? 0.1304 0.1555 0.1499 -0.0210 0.0115  0.0145  142 VAL   A N   
3163 C  CA  A VAL   A 142 ? 0.1317 0.1486 0.1741 -0.0021 0.0140  -0.0001 142 VAL   A CA  
3164 C  CA  B VAL   A 142 ? 0.1364 0.1480 0.1544 -0.0130 0.0170  0.0185  142 VAL   A CA  
3165 C  C   A VAL   A 142 ? 0.1226 0.1452 0.1710 -0.0054 0.0078  0.0065  142 VAL   A C   
3166 C  C   B VAL   A 142 ? 0.1283 0.1434 0.1624 -0.0131 0.0083  0.0192  142 VAL   A C   
3167 O  O   A VAL   A 142 ? 0.1239 0.1487 0.1842 0.0074  0.0100  0.0101  142 VAL   A O   
3168 O  O   B VAL   A 142 ? 0.1317 0.1439 0.1769 -0.0071 0.0082  0.0247  142 VAL   A O   
3169 C  CB  A VAL   A 142 ? 0.1392 0.1476 0.1742 -0.0012 0.0155  0.0070  142 VAL   A CB  
3170 C  CB  B VAL   A 142 ? 0.1467 0.1513 0.1643 -0.0015 0.0195  0.0171  142 VAL   A CB  
3171 C  CG1 A VAL   A 142 ? 0.1300 0.1288 0.1620 -0.0078 0.0243  0.0065  142 VAL   A CG1 
3172 C  CG1 B VAL   A 142 ? 0.1514 0.1431 0.1695 -0.0008 0.0170  0.0096  142 VAL   A CG1 
3173 C  CG2 A VAL   A 142 ? 0.1529 0.1627 0.1929 -0.0002 0.0121  0.0069  142 VAL   A CG2 
3174 C  CG2 B VAL   A 142 ? 0.1583 0.1605 0.1730 0.0016  0.0171  0.0243  142 VAL   A CG2 
3193 N  N   . CYS   A 143 ? 0.1302 0.1467 0.1546 -0.0086 0.0024  0.0117  143 CYS   A N   
3194 C  CA  . CYS   A 143 ? 0.1318 0.1492 0.1666 -0.0126 0.0091  0.0185  143 CYS   A CA  
3195 C  C   . CYS   A 143 ? 0.1319 0.1414 0.1705 -0.0123 0.0064  0.0228  143 CYS   A C   
3196 O  O   . CYS   A 143 ? 0.1257 0.1457 0.1784 -0.0054 0.0053  0.0197  143 CYS   A O   
3197 C  CB  . CYS   A 143 ? 0.1423 0.1514 0.1738 -0.0013 0.0118  0.0225  143 CYS   A CB  
3198 S  SG  . CYS   A 143 ? 0.1547 0.1592 0.1614 0.0060  0.0082  0.0156  143 CYS   A SG  
3205 N  N   . VAL   A 144 ? 0.1297 0.1525 0.1744 -0.0131 0.0059  0.0251  144 VAL   A N   
3206 C  CA  . VAL   A 144 ? 0.1314 0.1612 0.2100 -0.0178 0.0137  0.0257  144 VAL   A CA  
3207 C  C   . VAL   A 144 ? 0.1372 0.1531 0.2037 -0.0227 -0.0079 0.0258  144 VAL   A C   
3208 O  O   . VAL   A 144 ? 0.1517 0.1601 0.2098 -0.0129 0.0007  0.0311  144 VAL   A O   
3209 C  CB  . VAL   A 144 ? 0.1543 0.1795 0.2637 -0.0057 0.0320  0.0289  144 VAL   A CB  
3210 C  CG1 . VAL   A 144 ? 0.1737 0.1938 0.2898 -0.0170 0.0083  0.0386  144 VAL   A CG1 
3211 C  CG2 . VAL   A 144 ? 0.1430 0.1890 0.2669 -0.0016 0.0328  0.0344  144 VAL   A CG2 
3221 N  N   . ASP   A 145 ? 0.1386 0.1460 0.2109 -0.0162 0.0029  0.0205  145 ASP   A N   
3222 C  CA  . ASP   A 145 ? 0.1458 0.1494 0.2186 -0.0170 -0.0005 0.0125  145 ASP   A CA  
3223 C  C   . ASP   A 145 ? 0.1404 0.1404 0.2287 -0.0097 0.0017  0.0012  145 ASP   A C   
3224 O  O   . ASP   A 145 ? 0.1610 0.1507 0.2801 -0.0157 0.0047  -0.0290 145 ASP   A O   
3225 C  CB  . ASP   A 145 ? 0.1528 0.1804 0.2280 -0.0214 -0.0089 0.0001  145 ASP   A CB  
3226 C  CG  . ASP   A 145 ? 0.1695 0.2236 0.2639 -0.0380 -0.0167 0.0076  145 ASP   A CG  
3227 O  OD1 . ASP   A 145 ? 0.1658 0.2427 0.2784 -0.0550 -0.0062 0.0144  145 ASP   A OD1 
3228 O  OD2 . ASP   A 145 ? 0.1931 0.2497 0.2744 -0.0483 -0.0360 0.0030  145 ASP   A OD2 
3233 N  N   . THR   A 146 ? 0.1296 0.1316 0.1919 -0.0096 0.0066  0.0102  146 THR   A N   
3234 C  CA  . THR   A 146 ? 0.1275 0.1353 0.1756 -0.0051 0.0088  0.0049  146 THR   A CA  
3235 C  C   . THR   A 146 ? 0.1305 0.1343 0.1857 -0.0026 0.0117  0.0178  146 THR   A C   
3236 O  O   . THR   A 146 ? 0.1395 0.1466 0.2098 0.0035  -0.0042 0.0184  146 THR   A O   
3237 C  CB  . THR   A 146 ? 0.1305 0.1354 0.1758 -0.0035 0.0076  0.0168  146 THR   A CB  
3238 O  OG1 . THR   A 146 ? 0.1339 0.1517 0.1725 -0.0040 0.0022  0.0091  146 THR   A OG1 
3239 C  CG2 . THR   A 146 ? 0.1305 0.1405 0.1979 -0.0081 0.0057  0.0157  146 THR   A CG2 
3247 N  N   . VAL   A 147 ? 0.1232 0.1369 0.1759 -0.0039 0.0104  0.0131  147 VAL   A N   
3248 C  CA  . VAL   A 147 ? 0.1290 0.1474 0.1718 -0.0100 0.0172  0.0188  147 VAL   A CA  
3249 C  C   . VAL   A 147 ? 0.1339 0.1375 0.1808 -0.0173 0.0183  0.0343  147 VAL   A C   
3250 O  O   . VAL   A 147 ? 0.1410 0.1431 0.2081 -0.0194 0.0104  0.0325  147 VAL   A O   
3251 C  CB  . VAL   A 147 ? 0.1421 0.1444 0.1687 -0.0126 0.0219  0.0267  147 VAL   A CB  
3252 C  CG1 . VAL   A 147 ? 0.1647 0.1522 0.1728 -0.0074 0.0120  0.0289  147 VAL   A CG1 
3253 C  CG2 . VAL   A 147 ? 0.1477 0.1439 0.1755 -0.0151 0.0022  0.0253  147 VAL   A CG2 
3263 N  N   . ARG   A 148 ? 0.1341 0.1412 0.1933 -0.0150 0.0157  0.0422  148 ARG   A N   
3264 C  CA  . ARG   A 148 ? 0.1426 0.1466 0.1987 -0.0176 0.0085  0.0520  148 ARG   A CA  
3265 C  C   . ARG   A 148 ? 0.1503 0.1497 0.1905 -0.0179 0.0047  0.0678  148 ARG   A C   
3266 O  O   . ARG   A 148 ? 0.1752 0.1597 0.2123 -0.0230 0.0144  0.0529  148 ARG   A O   
3267 C  CB  . ARG   A 148 ? 0.1454 0.1482 0.2219 -0.0079 0.0208  0.0458  148 ARG   A CB  
3268 C  CG  . ARG   A 148 ? 0.1636 0.1520 0.2477 -0.0103 0.0334  0.0367  148 ARG   A CG  
3269 C  CD  . ARG   A 148 ? 0.1796 0.1453 0.2683 -0.0040 0.0423  0.0520  148 ARG   A CD  
3270 N  NE  . ARG   A 148 ? 0.1707 0.1527 0.2721 0.0116  0.0464  0.0563  148 ARG   A NE  
3271 C  CZ  . ARG   A 148 ? 0.1727 0.1405 0.2566 0.0067  0.0478  0.0504  148 ARG   A CZ  
3272 N  NH1 . ARG   A 148 ? 0.1770 0.1427 0.2580 -0.0059 0.0483  0.0272  148 ARG   A NH1 
3273 N  NH2 . ARG   A 148 ? 0.1634 0.1569 0.2570 0.0140  0.0511  0.0509  148 ARG   A NH2 
3287 N  N   . THR   A 149 ? 0.1438 0.1595 0.1848 -0.0216 -0.0052 0.0520  149 THR   A N   
3288 C  CA  . THR   A 149 ? 0.1490 0.1623 0.1833 -0.0152 -0.0034 0.0479  149 THR   A CA  
3289 C  C   . THR   A 149 ? 0.1440 0.1612 0.1746 -0.0239 0.0025  0.0523  149 THR   A C   
3290 O  O   . THR   A 149 ? 0.1452 0.1735 0.1909 -0.0231 0.0053  0.0538  149 THR   A O   
3291 C  CB  . THR   A 149 ? 0.1522 0.1738 0.1871 -0.0138 -0.0015 0.0435  149 THR   A CB  
3292 O  OG1 . THR   A 149 ? 0.1502 0.1604 0.2025 -0.0202 0.0087  0.0357  149 THR   A OG1 
3293 C  CG2 . THR   A 149 ? 0.1474 0.1818 0.2105 -0.0113 -0.0104 0.0329  149 THR   A CG2 
3301 N  N   . ASN   A 150 ? 0.1495 0.1657 0.1802 -0.0133 -0.0054 0.0596  150 ASN   A N   
3302 C  CA  . ASN   A 150 ? 0.1560 0.1727 0.1766 -0.0144 -0.0022 0.0548  150 ASN   A CA  
3303 C  C   . ASN   A 150 ? 0.1397 0.1633 0.1732 -0.0180 -0.0015 0.0476  150 ASN   A C   
3304 O  O   . ASN   A 150 ? 0.1458 0.1728 0.2000 -0.0182 -0.0209 0.0448  150 ASN   A O   
3305 C  CB  . ASN   A 150 ? 0.1984 0.2045 0.2054 -0.0217 0.0187  0.0770  150 ASN   A CB  
3306 C  CG  . ASN   A 150 ? 0.2517 0.2395 0.2755 -0.0163 0.0056  0.0751  150 ASN   A CG  
3307 O  OD1 . ASN   A 150 ? 0.2733 0.2520 0.2834 -0.0208 0.0089  0.0934  150 ASN   A OD1 
3308 N  ND2 . ASN   A 150 ? 0.2847 0.2557 0.3128 -0.0148 -0.0017 0.0682  150 ASN   A ND2 
3315 N  N   . VAL   A 151 ? 0.1395 0.1518 0.1625 -0.0173 -0.0021 0.0461  151 VAL   A N   
3316 C  CA  . VAL   A 151 ? 0.1423 0.1556 0.1553 -0.0160 -0.0015 0.0469  151 VAL   A CA  
3317 C  C   . VAL   A 151 ? 0.1316 0.1546 0.1612 -0.0236 -0.0016 0.0430  151 VAL   A C   
3318 O  O   . VAL   A 151 ? 0.1454 0.1611 0.2011 -0.0233 0.0058  0.0379  151 VAL   A O   
3319 C  CB  . VAL   A 151 ? 0.1693 0.1737 0.1638 -0.0081 0.0024  0.0460  151 VAL   A CB  
3320 C  CG1 . VAL   A 151 ? 0.1712 0.1989 0.1865 -0.0160 -0.0045 0.0442  151 VAL   A CG1 
3321 C  CG2 . VAL   A 151 ? 0.1771 0.1746 0.1628 -0.0037 0.0188  0.0359  151 VAL   A CG2 
3331 N  N   . TYR   A 152 ? 0.1328 0.1523 0.1635 -0.0240 0.0014  0.0362  152 TYR   A N   
3332 C  CA  . TYR   A 152 ? 0.1406 0.1588 0.1392 -0.0237 -0.0020 0.0381  152 TYR   A CA  
3333 C  C   . TYR   A 152 ? 0.1352 0.1544 0.1316 -0.0204 0.0074  0.0333  152 TYR   A C   
3334 O  O   . TYR   A 152 ? 0.1433 0.1550 0.1381 -0.0333 0.0037  0.0290  152 TYR   A O   
3335 C  CB  . TYR   A 152 ? 0.1555 0.1691 0.1500 -0.0248 0.0084  0.0447  152 TYR   A CB  
3336 C  CG  . TYR   A 152 ? 0.1609 0.1950 0.1531 -0.0222 0.0126  0.0564  152 TYR   A CG  
3337 C  CD1 . TYR   A 152 ? 0.1773 0.2178 0.1687 -0.0091 0.0158  0.0638  152 TYR   A CD1 
3338 C  CD2 . TYR   A 152 ? 0.1680 0.2063 0.1528 -0.0339 0.0107  0.0518  152 TYR   A CD2 
3339 C  CE1 . TYR   A 152 ? 0.2111 0.2354 0.1778 -0.0069 0.0023  0.0713  152 TYR   A CE1 
3340 C  CE2 . TYR   A 152 ? 0.1995 0.2265 0.1703 -0.0340 0.0166  0.0611  152 TYR   A CE2 
3341 C  CZ  . TYR   A 152 ? 0.2234 0.2322 0.1641 -0.0239 0.0044  0.0872  152 TYR   A CZ  
3342 O  OH  . TYR   A 152 ? 0.2530 0.2566 0.2136 -0.0207 0.0092  0.0963  152 TYR   A OH  
3352 N  N   A LEU   A 153 ? 0.1298 0.1468 0.1401 -0.0172 0.0087  0.0305  153 LEU   A N   
3353 N  N   B LEU   A 153 ? 0.1345 0.1533 0.1307 -0.0223 0.0065  0.0324  153 LEU   A N   
3354 C  CA  A LEU   A 153 ? 0.1276 0.1397 0.1474 -0.0068 0.0042  0.0348  153 LEU   A CA  
3355 C  CA  B LEU   A 153 ? 0.1306 0.1466 0.1294 -0.0138 -0.0004 0.0324  153 LEU   A CA  
3356 C  C   A LEU   A 153 ? 0.1336 0.1318 0.1494 -0.0097 0.0141  0.0261  153 LEU   A C   
3357 C  C   B LEU   A 153 ? 0.1342 0.1508 0.1362 -0.0100 0.0167  0.0294  153 LEU   A C   
3358 O  O   A LEU   A 153 ? 0.1393 0.1371 0.1740 -0.0139 0.0222  0.0158  153 LEU   A O   
3359 O  O   B LEU   A 153 ? 0.1341 0.1603 0.1521 -0.0105 0.0359  0.0262  153 LEU   A O   
3360 C  CB  A LEU   A 153 ? 0.1241 0.1323 0.1632 -0.0069 0.0113  0.0245  153 LEU   A CB  
3361 C  CB  B LEU   A 153 ? 0.1244 0.1452 0.1362 -0.0131 -0.0048 0.0336  153 LEU   A CB  
3362 C  CG  A LEU   A 153 ? 0.1285 0.1406 0.1658 -0.0113 0.0194  0.0148  153 LEU   A CG  
3363 C  CG  B LEU   A 153 ? 0.1297 0.1523 0.1331 -0.0076 -0.0164 0.0282  153 LEU   A CG  
3364 C  CD1 A LEU   A 153 ? 0.1405 0.1387 0.1654 -0.0186 0.0250  0.0186  153 LEU   A CD1 
3365 C  CD1 B LEU   A 153 ? 0.1409 0.1559 0.1401 -0.0107 -0.0153 0.0299  153 LEU   A CD1 
3366 C  CD2 A LEU   A 153 ? 0.1315 0.1458 0.1594 -0.0164 0.0232  -0.0014 153 LEU   A CD2 
3367 C  CD2 B LEU   A 153 ? 0.1335 0.1609 0.1422 -0.0082 -0.0182 0.0191  153 LEU   A CD2 
3390 N  N   A ALA   A 154 ? 0.1305 0.1324 0.1548 -0.0050 0.0121  0.0288  154 ALA   A N   
3391 N  N   B ALA   A 154 ? 0.1326 0.1470 0.1325 -0.0082 0.0248  0.0266  154 ALA   A N   
3392 C  CA  A ALA   A 154 ? 0.1444 0.1366 0.1573 0.0032  0.0129  0.0262  154 ALA   A CA  
3393 C  CA  B ALA   A 154 ? 0.1415 0.1436 0.1483 -0.0054 0.0285  0.0272  154 ALA   A CA  
3394 C  C   A ALA   A 154 ? 0.1430 0.1345 0.1539 0.0087  0.0080  0.0242  154 ALA   A C   
3395 C  C   B ALA   A 154 ? 0.1378 0.1378 0.1434 -0.0041 0.0211  0.0270  154 ALA   A C   
3396 O  O   A ALA   A 154 ? 0.1479 0.1365 0.1521 0.0072  0.0165  0.0275  154 ALA   A O   
3397 O  O   B ALA   A 154 ? 0.1428 0.1376 0.1392 -0.0112 0.0216  0.0173  154 ALA   A O   
3398 C  CB  A ALA   A 154 ? 0.1588 0.1391 0.1693 0.0155  0.0124  0.0212  154 ALA   A CB  
3399 C  CB  B ALA   A 154 ? 0.1504 0.1439 0.1686 -0.0004 0.0297  0.0174  154 ALA   A CB  
3410 N  N   A VAL   A 155 ? 0.1345 0.1269 0.1402 0.0158  0.0103  0.0338  155 VAL   A N   
3411 N  N   B VAL   A 155 ? 0.1219 0.1266 0.1286 0.0000  0.0249  0.0414  155 VAL   A N   
3412 C  CA  A VAL   A 155 ? 0.1471 0.1410 0.1656 0.0152  0.0080  0.0319  155 VAL   A CA  
3413 C  CA  B VAL   A 155 ? 0.1370 0.1425 0.1544 -0.0055 0.0274  0.0449  155 VAL   A CA  
3414 C  CA  T VAL   A 155 ? 0.1795 0.1784 0.1888 0.0055  0.0153  0.0324  155 VAL   A CA  
3415 C  C   A VAL   A 155 ? 0.1526 0.1531 0.1852 0.0238  0.0107  0.0310  155 VAL   A C   
3416 C  C   B VAL   A 155 ? 0.1443 0.1596 0.1688 0.0076  0.0257  0.0475  155 VAL   A C   
3417 C  C   T VAL   A 155 ? 0.1786 0.1809 0.1875 0.0132  0.0252  0.0381  155 VAL   A C   
3418 O  O   A VAL   A 155 ? 0.1482 0.1485 0.1978 0.0258  0.0251  0.0341  155 VAL   A O   
3419 O  O   B VAL   A 155 ? 0.1473 0.1677 0.1653 0.0175  0.0306  0.0500  155 VAL   A O   
3420 O  O   T VAL   A 155 ? 0.1784 0.1859 0.1926 0.0155  0.0332  0.0390  155 VAL   A O   
3421 C  CB  A VAL   A 155 ? 0.1482 0.1453 0.1656 0.0151  -0.0013 0.0306  155 VAL   A CB  
3422 C  CB  B VAL   A 155 ? 0.1384 0.1478 0.1519 -0.0067 0.0181  0.0445  155 VAL   A CB  
3423 C  CB  T VAL   A 155 ? 0.1779 0.1794 0.1828 0.0045  0.0029  0.0300  155 VAL   A CB  
3424 C  CG1 A VAL   A 155 ? 0.1562 0.1514 0.1731 0.0141  -0.0060 0.0303  155 VAL   A CG1 
3425 C  CG1 B VAL   A 155 ? 0.1473 0.1577 0.1633 -0.0046 0.0104  0.0480  155 VAL   A CG1 
3426 C  CG1 T VAL   A 155 ? 0.1820 0.1837 0.1859 0.0045  -0.0015 0.0307  155 VAL   A CG1 
3427 C  CG2 A VAL   A 155 ? 0.1532 0.1473 0.1756 0.0165  -0.0128 0.0262  155 VAL   A CG2 
3428 C  CG2 B VAL   A 155 ? 0.1471 0.1499 0.1644 -0.0037 0.0024  0.0318  155 VAL   A CG2 
3429 C  CG2 T VAL   A 155 ? 0.1815 0.1804 0.1900 0.0055  -0.0082 0.0257  155 VAL   A CG2 
3455 N  N   A PHE   A 156 ? 0.1655 0.1637 0.1945 0.0306  0.0123  0.0344  156 PHE   A N   
3456 N  N   B PHE   A 156 ? 0.1555 0.1602 0.1875 0.0115  0.0356  0.0546  156 PHE   A N   
3457 N  N   T PHE   A 156 ? 0.1817 0.1744 0.1888 0.0198  0.0359  0.0491  156 PHE   A N   
3458 C  CA  A PHE   A 156 ? 0.1802 0.1760 0.2111 0.0382  0.0174  0.0351  156 PHE   A CA  
3459 C  CA  B PHE   A 156 ? 0.1701 0.1643 0.2081 0.0168  0.0359  0.0520  156 PHE   A CA  
3460 C  CA  T PHE   A 156 ? 0.1894 0.1700 0.1952 0.0268  0.0423  0.0552  156 PHE   A CA  
3461 C  C   A PHE   A 156 ? 0.1779 0.1825 0.2180 0.0447  0.0310  0.0453  156 PHE   A C   
3462 C  C   B PHE   A 156 ? 0.1749 0.1749 0.2305 0.0288  0.0489  0.0657  156 PHE   A C   
3463 C  C   T PHE   A 156 ? 0.1861 0.1769 0.2116 0.0299  0.0544  0.0652  156 PHE   A C   
3464 O  O   A PHE   A 156 ? 0.1788 0.1863 0.2179 0.0394  0.0439  0.0451  156 PHE   A O   
3465 O  O   B PHE   A 156 ? 0.1870 0.1792 0.2411 0.0267  0.0562  0.0537  156 PHE   A O   
3466 O  O   T PHE   A 156 ? 0.1960 0.1802 0.2254 0.0303  0.0573  0.0498  156 PHE   A O   
3467 C  CB  A PHE   A 156 ? 0.1968 0.1824 0.2151 0.0371  0.0093  0.0288  156 PHE   A CB  
3468 C  CB  B PHE   A 156 ? 0.1717 0.1566 0.2020 0.0068  0.0243  0.0386  156 PHE   A CB  
3469 C  CB  T PHE   A 156 ? 0.1936 0.1576 0.1831 0.0302  0.0374  0.0560  156 PHE   A CB  
3470 C  CG  A PHE   A 156 ? 0.2117 0.1899 0.2294 0.0399  0.0008  0.0193  156 PHE   A CG  
3471 C  CG  B PHE   A 156 ? 0.1733 0.1585 0.2158 0.0044  0.0173  0.0370  156 PHE   A CG  
3472 C  CG  T PHE   A 156 ? 0.1961 0.1495 0.1841 0.0381  0.0327  0.0657  156 PHE   A CG  
3473 C  CD1 A PHE   A 156 ? 0.2185 0.1961 0.2340 0.0423  0.0077  0.0137  156 PHE   A CD1 
3474 C  CD1 B PHE   A 156 ? 0.1823 0.1716 0.2363 0.0045  0.0042  0.0370  156 PHE   A CD1 
3475 C  CD1 T PHE   A 156 ? 0.1972 0.1523 0.2003 0.0445  0.0299  0.0585  156 PHE   A CD1 
3476 C  CD2 A PHE   A 156 ? 0.2196 0.1972 0.2361 0.0417  -0.0063 0.0149  156 PHE   A CD2 
3477 C  CD2 B PHE   A 156 ? 0.1745 0.1643 0.2296 -0.0030 0.0170  0.0365  156 PHE   A CD2 
3478 C  CD2 T PHE   A 156 ? 0.2043 0.1491 0.1898 0.0361  0.0235  0.0820  156 PHE   A CD2 
3479 C  CE1 A PHE   A 156 ? 0.2233 0.1985 0.2402 0.0438  0.0132  0.0091  156 PHE   A CE1 
3480 C  CE1 B PHE   A 156 ? 0.1887 0.1818 0.2490 -0.0026 0.0006  0.0263  156 PHE   A CE1 
3481 C  CE1 T PHE   A 156 ? 0.2048 0.1548 0.2148 0.0441  0.0253  0.0533  156 PHE   A CE1 
3482 C  CE2 A PHE   A 156 ? 0.2277 0.2030 0.2426 0.0413  -0.0028 0.0078  156 PHE   A CE2 
3483 C  CE2 B PHE   A 156 ? 0.1747 0.1735 0.2393 -0.0067 0.0177  0.0279  156 PHE   A CE2 
3484 C  CE2 T PHE   A 156 ? 0.2120 0.1544 0.1961 0.0342  0.0219  0.0758  156 PHE   A CE2 
3485 C  CZ  A PHE   A 156 ? 0.2278 0.2034 0.2423 0.0427  0.0092  0.0074  156 PHE   A CZ  
3486 C  CZ  B PHE   A 156 ? 0.1830 0.1773 0.2464 -0.0069 0.0072  0.0265  156 PHE   A CZ  
3487 C  CZ  T PHE   A 156 ? 0.2105 0.1527 0.2119 0.0358  0.0240  0.0614  156 PHE   A CZ  
3515 N  N   A ASP   A 157 ? 0.1784 0.1918 0.2300 0.0491  0.0283  0.0484  157 ASP   A N   
3516 N  N   B ASP   A 157 ? 0.1721 0.1914 0.2518 0.0344  0.0396  0.0772  157 ASP   A N   
3517 N  N   T ASP   A 157 ? 0.1743 0.1858 0.2183 0.0278  0.0524  0.0834  157 ASP   A N   
3518 C  CA  A ASP   A 157 ? 0.1839 0.2064 0.2422 0.0506  0.0255  0.0550  157 ASP   A CA  
3519 C  CA  B ASP   A 157 ? 0.1738 0.2123 0.2687 0.0389  0.0284  0.0887  157 ASP   A CA  
3520 C  CA  T ASP   A 157 ? 0.1703 0.1988 0.2360 0.0333  0.0408  0.0919  157 ASP   A CA  
3521 C  C   A ASP   A 157 ? 0.1857 0.2233 0.2540 0.0455  0.0265  0.0612  157 ASP   A C   
3522 C  C   B ASP   A 157 ? 0.1600 0.2303 0.2642 0.0410  0.0314  0.1038  157 ASP   A C   
3523 C  C   T ASP   A 157 ? 0.1738 0.2160 0.2395 0.0344  0.0421  0.0956  157 ASP   A C   
3524 O  O   A ASP   A 157 ? 0.1833 0.2231 0.2507 0.0425  0.0247  0.0587  157 ASP   A O   
3525 O  O   B ASP   A 157 ? 0.1553 0.2277 0.2578 0.0348  0.0378  0.1046  157 ASP   A O   
3526 O  O   T ASP   A 157 ? 0.1665 0.2136 0.2332 0.0304  0.0459  0.0949  157 ASP   A O   
3527 C  CB  A ASP   A 157 ? 0.1877 0.2081 0.2482 0.0550  0.0252  0.0586  157 ASP   A CB  
3528 C  CB  B ASP   A 157 ? 0.1888 0.2214 0.2953 0.0392  0.0214  0.0857  157 ASP   A CB  
3529 C  CB  T ASP   A 157 ? 0.1631 0.1989 0.2504 0.0371  0.0378  0.0979  157 ASP   A CB  
3530 C  CG  A ASP   A 157 ? 0.1969 0.2130 0.2659 0.0605  0.0201  0.0673  157 ASP   A CG  
3531 C  CG  B ASP   A 157 ? 0.2083 0.2366 0.3345 0.0388  0.0019  0.0854  157 ASP   A CG  
3532 C  CG  T ASP   A 157 ? 0.1626 0.1988 0.2660 0.0429  0.0281  0.1075  157 ASP   A CG  
3533 O  OD1 A ASP   A 157 ? 0.2032 0.2173 0.2879 0.0653  0.0094  0.0612  157 ASP   A OD1 
3534 O  OD1 B ASP   A 157 ? 0.2107 0.2347 0.3539 0.0357  -0.0035 0.0992  157 ASP   A OD1 
3535 O  OD1 T ASP   A 157 ? 0.1654 0.1932 0.2845 0.0382  0.0238  0.1107  157 ASP   A OD1 
3536 O  OD2 A ASP   A 157 ? 0.1961 0.2107 0.2611 0.0569  0.0272  0.0852  157 ASP   A OD2 
3537 O  OD2 B ASP   A 157 ? 0.2171 0.2454 0.3533 0.0386  -0.0122 0.0763  157 ASP   A OD2 
3538 O  OD2 T ASP   A 157 ? 0.1586 0.2023 0.2547 0.0454  0.0263  0.1147  157 ASP   A OD2 
3551 N  N   A LYS   A 158 ? 0.1937 0.2398 0.2765 0.0395  0.0357  0.0607  158 LYS   A N   
3552 N  N   B LYS   A 158 ? 0.1609 0.2536 0.2856 0.0429  0.0395  0.0948  158 LYS   A N   
3553 N  N   T LYS   A 158 ? 0.1888 0.2377 0.2673 0.0339  0.0468  0.0818  158 LYS   A N   
3554 C  CA  A LYS   A 158 ? 0.1982 0.2563 0.2966 0.0366  0.0461  0.0608  158 LYS   A CA  
3555 C  CA  B LYS   A 158 ? 0.1662 0.2784 0.2926 0.0448  0.0526  0.0924  158 LYS   A CA  
3556 C  CA  T LYS   A 158 ? 0.2009 0.2585 0.2888 0.0366  0.0503  0.0709  158 LYS   A CA  
3557 C  C   A LYS   A 158 ? 0.1949 0.2638 0.2870 0.0361  0.0387  0.0647  158 LYS   A C   
3558 C  C   B LYS   A 158 ? 0.1559 0.2853 0.2707 0.0490  0.0294  0.1015  158 LYS   A C   
3559 C  C   T LYS   A 158 ? 0.2012 0.2623 0.2777 0.0396  0.0415  0.0698  158 LYS   A C   
3560 O  O   A LYS   A 158 ? 0.1964 0.2682 0.2880 0.0324  0.0424  0.0641  158 LYS   A O   
3561 O  O   B LYS   A 158 ? 0.1489 0.2888 0.2552 0.0368  0.0367  0.1082  158 LYS   A O   
3562 O  O   T LYS   A 158 ? 0.2030 0.2640 0.2764 0.0396  0.0423  0.0697  158 LYS   A O   
3563 C  CB  A LYS   A 158 ? 0.2092 0.2623 0.3226 0.0345  0.0601  0.0651  158 LYS   A CB  
3564 C  CB  B LYS   A 158 ? 0.1868 0.2982 0.3327 0.0384  0.0769  0.0853  158 LYS   A CB  
3565 C  CB  T LYS   A 158 ? 0.2179 0.2739 0.3257 0.0342  0.0598  0.0617  158 LYS   A CB  
3566 C  CG  A LYS   A 158 ? 0.2232 0.2675 0.3474 0.0345  0.0686  0.0735  158 LYS   A CG  
3567 C  CG  B LYS   A 158 ? 0.2144 0.3159 0.3737 0.0360  0.0849  0.0844  158 LYS   A CG  
3568 C  CG  T LYS   A 158 ? 0.2347 0.2870 0.3608 0.0328  0.0660  0.0587  158 LYS   A CG  
3569 C  CD  A LYS   A 158 ? 0.2347 0.2712 0.3669 0.0366  0.0793  0.0840  158 LYS   A CD  
3570 C  CD  B LYS   A 158 ? 0.2369 0.3286 0.4097 0.0343  0.0902  0.0915  158 LYS   A CD  
3571 C  CD  T LYS   A 158 ? 0.2500 0.2965 0.3932 0.0362  0.0686  0.0608  158 LYS   A CD  
3572 C  CE  A LYS   A 158 ? 0.2397 0.2705 0.3766 0.0358  0.0888  0.1001  158 LYS   A CE  
3573 C  CE  B LYS   A 158 ? 0.2465 0.3328 0.4337 0.0342  0.0973  0.1028  158 LYS   A CE  
3574 C  CE  T LYS   A 158 ? 0.2587 0.2998 0.4166 0.0377  0.0687  0.0663  158 LYS   A CE  
3575 N  NZ  A LYS   A 158 ? 0.2406 0.2696 0.3787 0.0335  0.0998  0.1092  158 LYS   A NZ  
3576 N  NZ  B LYS   A 158 ? 0.2487 0.3334 0.4431 0.0307  0.1029  0.1116  158 LYS   A NZ  
3577 N  NZ  T LYS   A 158 ? 0.2635 0.3013 0.4271 0.0396  0.0717  0.0686  158 LYS   A NZ  
3617 N  N   A ASN   A 159 ? 0.1902 0.2622 0.2783 0.0358  0.0275  0.0681  159 ASN   A N   
3618 N  N   B ASN   A 159 ? 0.1607 0.2879 0.2788 0.0566  0.0077  0.0972  159 ASN   A N   
3619 N  N   T ASN   A 159 ? 0.2008 0.2601 0.2742 0.0371  0.0324  0.0672  159 ASN   A N   
3620 C  CA  A ASN   A 159 ? 0.1865 0.2598 0.2641 0.0324  0.0164  0.0738  159 ASN   A CA  
3621 C  CA  B ASN   A 159 ? 0.1679 0.2924 0.2878 0.0545  -0.0089 0.0880  159 ASN   A CA  
3622 C  CA  T ASN   A 159 ? 0.2040 0.2570 0.2660 0.0305  0.0226  0.0701  159 ASN   A CA  
3623 C  C   A ASN   A 159 ? 0.1766 0.2576 0.2476 0.0266  0.0217  0.0742  159 ASN   A C   
3624 C  C   B ASN   A 159 ? 0.1484 0.2858 0.2577 0.0464  -0.0132 0.0896  159 ASN   A C   
3625 C  C   T ASN   A 159 ? 0.2055 0.2573 0.2616 0.0222  0.0301  0.0615  159 ASN   A C   
3626 O  O   A ASN   A 159 ? 0.1722 0.2580 0.2495 0.0296  0.0215  0.0648  159 ASN   A O   
3627 O  O   B ASN   A 159 ? 0.1364 0.2953 0.2575 0.0481  -0.0260 0.0929  159 ASN   A O   
3628 O  O   T ASN   A 159 ? 0.2044 0.2555 0.2648 0.0251  0.0330  0.0505  159 ASN   A O   
3629 C  CB  A ASN   A 159 ? 0.1939 0.2610 0.2753 0.0345  0.0022  0.0756  159 ASN   A CB  
3630 C  CB  B ASN   A 159 ? 0.1964 0.3020 0.3374 0.0591  -0.0223 0.0721  159 ASN   A CB  
3631 C  CB  T ASN   A 159 ? 0.2075 0.2564 0.2731 0.0318  0.0075  0.0780  159 ASN   A CB  
3632 C  CG  A ASN   A 159 ? 0.2030 0.2633 0.2939 0.0369  -0.0063 0.0677  159 ASN   A CG  
3633 C  CG  B ASN   A 159 ? 0.2283 0.3138 0.3881 0.0534  -0.0304 0.0450  159 ASN   A CG  
3634 C  CG  T ASN   A 159 ? 0.2131 0.2574 0.2890 0.0333  -0.0010 0.0735  159 ASN   A CG  
3635 O  OD1 A ASN   A 159 ? 0.2008 0.2676 0.3029 0.0375  -0.0001 0.0662  159 ASN   A OD1 
3636 O  OD1 B ASN   A 159 ? 0.2377 0.3165 0.4091 0.0499  -0.0355 0.0368  159 ASN   A OD1 
3637 O  OD1 T ASN   A 159 ? 0.2085 0.2609 0.2971 0.0338  0.0086  0.0732  159 ASN   A OD1 
3638 N  ND2 A ASN   A 159 ? 0.2037 0.2618 0.2954 0.0401  -0.0158 0.0681  159 ASN   A ND2 
3639 N  ND2 B ASN   A 159 ? 0.2403 0.3188 0.4091 0.0507  -0.0280 0.0295  159 ASN   A ND2 
3640 N  ND2 T ASN   A 159 ? 0.2133 0.2561 0.2895 0.0354  -0.0118 0.0756  159 ASN   A ND2 
3659 N  N   A LEU   A 160 ? 0.1680 0.2498 0.2321 0.0176  0.0206  0.0826  160 LEU   A N   
3660 N  N   B LEU   A 160 ? 0.1421 0.2686 0.2333 0.0337  -0.0095 0.0968  160 LEU   A N   
3661 N  N   T LEU   A 160 ? 0.2057 0.2546 0.2581 0.0115  0.0298  0.0611  160 LEU   A N   
3662 C  CA  A LEU   A 160 ? 0.1614 0.2434 0.2161 0.0073  0.0187  0.0894  160 LEU   A CA  
3663 C  CA  B LEU   A 160 ? 0.1415 0.2542 0.2177 0.0209  0.0050  0.0984  160 LEU   A CA  
3664 C  CA  T LEU   A 160 ? 0.2088 0.2527 0.2515 -0.0002 0.0289  0.0618  160 LEU   A CA  
3665 C  C   A LEU   A 160 ? 0.1450 0.2384 0.1961 0.0023  0.0156  0.0958  160 LEU   A C   
3666 C  C   B LEU   A 160 ? 0.1241 0.2485 0.1868 0.0181  0.0139  0.0888  160 LEU   A C   
3667 O  O   A LEU   A 160 ? 0.1362 0.2378 0.1873 -0.0016 0.0083  0.1024  160 LEU   A O   
3668 O  O   B LEU   A 160 ? 0.1149 0.2495 0.1849 0.0125  0.0104  0.0762  160 LEU   A O   
3669 C  CB  A LEU   A 160 ? 0.1624 0.2435 0.2145 0.0040  0.0147  0.0836  160 LEU   A CB  
3670 C  CB  B LEU   A 160 ? 0.1505 0.2510 0.2200 0.0108  0.0065  0.0950  160 LEU   A CB  
3671 C  CB  T LEU   A 160 ? 0.2082 0.2526 0.2402 -0.0100 0.0279  0.0594  160 LEU   A CB  
3672 C  CG  A LEU   A 160 ? 0.1648 0.2456 0.2260 -0.0020 0.0065  0.0652  160 LEU   A CG  
3673 C  CG  B LEU   A 160 ? 0.1586 0.2552 0.2404 0.0008  -0.0020 0.0729  160 LEU   A CG  
3674 C  CG  T LEU   A 160 ? 0.2096 0.2544 0.2398 -0.0200 0.0226  0.0487  160 LEU   A CG  
3675 C  CD1 A LEU   A 160 ? 0.1691 0.2488 0.2371 -0.0070 0.0040  0.0546  160 LEU   A CD1 
3676 C  CD1 B LEU   A 160 ? 0.1672 0.2594 0.2527 -0.0058 -0.0018 0.0649  160 LEU   A CD1 
3677 C  CD1 T LEU   A 160 ? 0.2129 0.2574 0.2469 -0.0233 0.0192  0.0406  160 LEU   A CD1 
3678 C  CD2 A LEU   A 160 ? 0.1630 0.2446 0.2292 -0.0024 0.0087  0.0583  160 LEU   A CD2 
3679 C  CD2 B LEU   A 160 ? 0.1575 0.2539 0.2508 0.0001  0.0001  0.0609  160 LEU   A CD2 
3680 C  CD2 T LEU   A 160 ? 0.2077 0.2525 0.2373 -0.0232 0.0255  0.0466  160 LEU   A CD2 
3713 N  N   A TYR   A 161 ? 0.1506 0.2349 0.2123 0.0009  0.0165  0.0869  161 TYR   A N   
3714 N  N   B TYR   A 161 ? 0.1401 0.2435 0.1963 0.0194  0.0177  0.0778  161 TYR   A N   
3715 C  CA  A TYR   A 161 ? 0.1566 0.2291 0.2032 -0.0019 0.0223  0.0852  161 TYR   A CA  
3716 C  CA  B TYR   A 161 ? 0.1517 0.2360 0.1914 0.0203  0.0275  0.0732  161 TYR   A CA  
3717 C  C   A TYR   A 161 ? 0.1583 0.2516 0.2119 0.0003  0.0188  0.0851  161 TYR   A C   
3718 C  C   B TYR   A 161 ? 0.1540 0.2551 0.2039 0.0141  0.0247  0.0797  161 TYR   A C   
3719 O  O   A TYR   A 161 ? 0.1511 0.2574 0.1880 -0.0041 0.0141  0.0866  161 TYR   A O   
3720 O  O   B TYR   A 161 ? 0.1506 0.2569 0.1930 0.0066  0.0296  0.0809  161 TYR   A O   
3721 C  CB  A TYR   A 161 ? 0.1610 0.2108 0.2088 -0.0029 0.0229  0.0637  161 TYR   A CB  
3722 C  CB  B TYR   A 161 ? 0.1576 0.2175 0.1941 0.0238  0.0383  0.0504  161 TYR   A CB  
3723 C  CG  A TYR   A 161 ? 0.1570 0.1930 0.1957 -0.0034 0.0085  0.0424  161 TYR   A CG  
3724 C  CG  B TYR   A 161 ? 0.1576 0.1987 0.1881 0.0292  0.0386  0.0311  161 TYR   A CG  
3725 C  CD1 A TYR   A 161 ? 0.1536 0.1866 0.1961 -0.0020 0.0003  0.0271  161 TYR   A CD1 
3726 C  CD1 B TYR   A 161 ? 0.1598 0.1918 0.2020 0.0291  0.0289  0.0233  161 TYR   A CD1 
3727 C  CD2 A TYR   A 161 ? 0.1577 0.1884 0.1959 0.0029  -0.0052 0.0364  161 TYR   A CD2 
3728 C  CD2 B TYR   A 161 ? 0.1566 0.1880 0.1828 0.0346  0.0386  0.0258  161 TYR   A CD2 
3729 C  CE1 A TYR   A 161 ? 0.1544 0.1737 0.1881 -0.0002 -0.0123 0.0263  161 TYR   A CE1 
3730 C  CE1 B TYR   A 161 ? 0.1647 0.1839 0.2069 0.0314  0.0200  0.0213  161 TYR   A CE1 
3731 C  CE2 A TYR   A 161 ? 0.1589 0.1746 0.1978 -0.0044 -0.0148 0.0430  161 TYR   A CE2 
3732 C  CE2 B TYR   A 161 ? 0.1609 0.1789 0.1928 0.0297  0.0323  0.0259  161 TYR   A CE2 
3733 C  CZ  A TYR   A 161 ? 0.1600 0.1644 0.1871 -0.0098 -0.0178 0.0341  161 TYR   A CZ  
3734 C  CZ  B TYR   A 161 ? 0.1710 0.1782 0.2107 0.0269  0.0214  0.0215  161 TYR   A CZ  
3735 O  OH  A TYR   A 161 ? 0.1723 0.1517 0.1959 -0.0078 -0.0129 0.0433  161 TYR   A OH  
3736 O  OH  B TYR   A 161 ? 0.1864 0.1720 0.2425 0.0215  0.0127  0.0153  161 TYR   A OH  
3755 N  N   A ASP   A 162 ? 0.1588 0.2679 0.2443 0.0065  0.0227  0.0842  162 ASP   A N   
3756 N  N   B ASP   A 162 ? 0.1500 0.2728 0.2327 0.0112  0.0276  0.0830  162 ASP   A N   
3757 C  CA  A ASP   A 162 ? 0.1608 0.2853 0.2588 0.0020  0.0263  0.0834  162 ASP   A CA  
3758 C  CA  B ASP   A 162 ? 0.1474 0.2938 0.2503 0.0015  0.0262  0.0847  162 ASP   A CA  
3759 C  C   A ASP   A 162 ? 0.1550 0.3031 0.2526 -0.0030 0.0135  0.0786  162 ASP   A C   
3760 C  C   B ASP   A 162 ? 0.1442 0.2986 0.2417 -0.0084 0.0184  0.0826  162 ASP   A C   
3761 O  O   A ASP   A 162 ? 0.1553 0.3079 0.2587 -0.0041 0.0110  0.0658  162 ASP   A O   
3762 O  O   B ASP   A 162 ? 0.1475 0.3006 0.2449 -0.0132 0.0165  0.0736  162 ASP   A O   
3763 C  CB  A ASP   A 162 ? 0.1708 0.2828 0.2689 0.0091  0.0382  0.0886  162 ASP   A CB  
3764 C  CB  B ASP   A 162 ? 0.1500 0.3099 0.2739 0.0060  0.0279  0.0880  162 ASP   A CB  
3765 C  CG  A ASP   A 162 ? 0.1839 0.2808 0.2851 0.0166  0.0451  0.0877  162 ASP   A CG  
3766 C  CG  B ASP   A 162 ? 0.1545 0.3211 0.2829 0.0089  0.0328  0.0979  162 ASP   A CG  
3767 O  OD1 A ASP   A 162 ? 0.1998 0.2778 0.2846 0.0088  0.0477  0.0930  162 ASP   A OD1 
3768 O  OD1 B ASP   A 162 ? 0.1622 0.3260 0.2899 0.0095  0.0325  0.1008  162 ASP   A OD1 
3769 O  OD2 A ASP   A 162 ? 0.1927 0.2776 0.2969 0.0231  0.0572  0.0853  162 ASP   A OD2 
3770 O  OD2 B ASP   A 162 ? 0.1630 0.3275 0.2863 0.0111  0.0420  0.1050  162 ASP   A OD2 
3779 N  N   A LYS   A 163 ? 0.1651 0.3149 0.2542 -0.0014 -0.0063 0.0810  163 LYS   A N   
3780 N  N   B LYS   A 163 ? 0.1509 0.3009 0.2439 -0.0104 0.0004  0.0853  163 LYS   A N   
3781 C  CA  A LYS   A 163 ? 0.1801 0.3255 0.2616 -0.0055 -0.0092 0.0711  163 LYS   A CA  
3782 C  CA  B LYS   A 163 ? 0.1615 0.3019 0.2472 -0.0173 -0.0090 0.0768  163 LYS   A CA  
3783 C  C   A LYS   A 163 ? 0.1723 0.3103 0.2380 -0.0104 0.0040  0.0745  163 LYS   A C   
3784 C  C   B LYS   A 163 ? 0.1490 0.2829 0.2235 -0.0270 -0.0062 0.0634  163 LYS   A C   
3785 O  O   A LYS   A 163 ? 0.1710 0.3180 0.2500 -0.0128 0.0056  0.0705  163 LYS   A O   
3786 O  O   B LYS   A 163 ? 0.1535 0.2939 0.2341 -0.0325 -0.0152 0.0620  163 LYS   A O   
3787 C  CB  A LYS   A 163 ? 0.2114 0.3478 0.2938 0.0026  -0.0202 0.0572  163 LYS   A CB  
3788 C  CB  B LYS   A 163 ? 0.1933 0.3221 0.2861 -0.0099 -0.0195 0.0734  163 LYS   A CB  
3789 C  CG  A LYS   A 163 ? 0.2397 0.3662 0.3408 0.0017  -0.0166 0.0480  163 LYS   A CG  
3790 C  CG  B LYS   A 163 ? 0.2244 0.3400 0.3352 -0.0099 -0.0183 0.0710  163 LYS   A CG  
3791 C  CD  A LYS   A 163 ? 0.2628 0.3826 0.3915 -0.0040 -0.0124 0.0417  163 LYS   A CD  
3792 C  CD  B LYS   A 163 ? 0.2537 0.3544 0.3816 -0.0143 -0.0143 0.0701  163 LYS   A CD  
3793 C  CE  A LYS   A 163 ? 0.2791 0.3936 0.4325 -0.0079 -0.0101 0.0394  163 LYS   A CE  
3794 C  CE  B LYS   A 163 ? 0.2710 0.3649 0.4190 -0.0159 -0.0135 0.0690  163 LYS   A CE  
3795 N  NZ  A LYS   A 163 ? 0.2915 0.4010 0.4575 -0.0100 -0.0120 0.0376  163 LYS   A NZ  
3796 N  NZ  B LYS   A 163 ? 0.2820 0.3718 0.4412 -0.0169 -0.0138 0.0640  163 LYS   A NZ  
3823 N  N   A LEU   A 164 ? 0.1610 0.2821 0.2106 -0.0147 0.0044  0.0695  164 LEU   A N   
3824 N  N   B LEU   A 164 ? 0.1328 0.2524 0.1939 -0.0299 -0.0091 0.0504  164 LEU   A N   
3825 C  CA  A LEU   A 164 ? 0.1626 0.2600 0.2026 -0.0186 0.0130  0.0576  164 LEU   A CA  
3826 C  CA  B LEU   A 164 ? 0.1349 0.2268 0.1789 -0.0272 0.0089  0.0456  164 LEU   A CA  
3827 C  C   A LEU   A 164 ? 0.1606 0.2497 0.2077 -0.0240 0.0069  0.0497  164 LEU   A C   
3828 C  C   B LEU   A 164 ? 0.1437 0.2229 0.1696 -0.0239 0.0136  0.0374  164 LEU   A C   
3829 O  O   A LEU   A 164 ? 0.1646 0.2482 0.2179 -0.0218 0.0108  0.0434  164 LEU   A O   
3830 O  O   B LEU   A 164 ? 0.1464 0.2276 0.1604 -0.0207 0.0283  0.0243  164 LEU   A O   
3831 C  CB  A LEU   A 164 ? 0.1613 0.2531 0.1909 -0.0125 0.0113  0.0548  164 LEU   A CB  
3832 C  CB  B LEU   A 164 ? 0.1291 0.2104 0.1764 -0.0262 0.0093  0.0523  164 LEU   A CB  
3833 C  CG  A LEU   A 164 ? 0.1684 0.2488 0.1924 -0.0085 0.0111  0.0522  164 LEU   A CG  
3834 C  CG  B LEU   A 164 ? 0.1263 0.2008 0.1878 -0.0180 0.0164  0.0449  164 LEU   A CG  
3835 C  CD1 A LEU   A 164 ? 0.1604 0.2443 0.1718 -0.0051 0.0054  0.0684  164 LEU   A CD1 
3836 C  CD1 B LEU   A 164 ? 0.1209 0.1963 0.2044 -0.0110 0.0125  0.0399  164 LEU   A CD1 
3837 C  CD2 A LEU   A 164 ? 0.1823 0.2526 0.2022 -0.0127 0.0200  0.0379  164 LEU   A CD2 
3838 C  CD2 B LEU   A 164 ? 0.1323 0.2040 0.1856 -0.0193 0.0265  0.0286  164 LEU   A CD2 
3861 N  N   A VAL   A 165 ? 0.1486 0.2409 0.2015 -0.0302 0.0093  0.0545  165 VAL   A N   
3862 N  N   B VAL   A 165 ? 0.1463 0.2151 0.1692 -0.0202 0.0130  0.0361  165 VAL   A N   
3863 C  CA  A VAL   A 165 ? 0.1534 0.2388 0.1953 -0.0241 0.0241  0.0581  165 VAL   A CA  
3864 C  CA  B VAL   A 165 ? 0.1504 0.2111 0.1599 -0.0184 0.0241  0.0391  165 VAL   A CA  
3865 C  C   A VAL   A 165 ? 0.1540 0.2424 0.1902 -0.0203 0.0265  0.0544  165 VAL   A C   
3866 C  C   B VAL   A 165 ? 0.1524 0.2139 0.1619 -0.0170 0.0064  0.0463  165 VAL   A C   
3867 O  O   A VAL   A 165 ? 0.1605 0.2422 0.1962 -0.0174 0.0319  0.0442  165 VAL   A O   
3868 O  O   B VAL   A 165 ? 0.1519 0.2090 0.1669 -0.0164 0.0053  0.0479  165 VAL   A O   
3869 C  CB  A VAL   A 165 ? 0.1645 0.2347 0.2000 -0.0225 0.0221  0.0596  165 VAL   A CB  
3870 C  CB  B VAL   A 165 ? 0.1604 0.2087 0.1719 -0.0153 0.0179  0.0313  165 VAL   A CB  
3871 C  CG1 A VAL   A 165 ? 0.1727 0.2355 0.1933 -0.0247 0.0220  0.0543  165 VAL   A CG1 
3872 C  CG1 B VAL   A 165 ? 0.1652 0.2111 0.1742 -0.0177 0.0135  0.0281  165 VAL   A CG1 
3873 C  CG2 A VAL   A 165 ? 0.1736 0.2399 0.1980 -0.0140 0.0136  0.0634  165 VAL   A CG2 
3874 C  CG2 B VAL   A 165 ? 0.1701 0.2119 0.1783 -0.0107 0.0145  0.0344  165 VAL   A CG2 
3893 N  N   A SER   A 166 ? 0.1413 0.2522 0.1975 -0.0187 0.0208  0.0407  166 SER   A N   
3894 N  N   B SER   A 166 ? 0.1509 0.2208 0.1753 -0.0176 -0.0044 0.0466  166 SER   A N   
3895 C  CA  A SER   A 166 ? 0.1441 0.2684 0.2186 -0.0207 0.0153  0.0320  166 SER   A CA  
3896 C  CA  B SER   A 166 ? 0.1513 0.2355 0.2024 -0.0159 -0.0021 0.0472  166 SER   A CA  
3897 C  C   A SER   A 166 ? 0.1443 0.2773 0.2152 -0.0189 -0.0061 0.0266  166 SER   A C   
3898 C  C   B SER   A 166 ? 0.1553 0.2404 0.2217 -0.0229 0.0037  0.0427  166 SER   A C   
3899 O  O   A SER   A 166 ? 0.1522 0.2842 0.2400 -0.0215 -0.0091 0.0152  166 SER   A O   
3900 O  O   B SER   A 166 ? 0.1549 0.2365 0.2401 -0.0225 0.0013  0.0374  166 SER   A O   
3901 C  CB  A SER   A 166 ? 0.1588 0.2833 0.2518 -0.0043 0.0164  0.0165  166 SER   A CB  
3902 C  CB  B SER   A 166 ? 0.1618 0.2488 0.2000 -0.0096 0.0120  0.0498  166 SER   A CB  
3903 O  OG  A SER   A 166 ? 0.1675 0.2972 0.2772 -0.0028 0.0396  0.0260  166 SER   A OG  
3904 O  OG  B SER   A 166 ? 0.1863 0.2655 0.2133 -0.0042 0.0218  0.0499  166 SER   A OG  
3915 N  N   A SER   A 167 ? 0.1558 0.2858 0.1906 -0.0038 -0.0131 0.0241  167 SER   A N   
3916 N  N   B SER   A 167 ? 0.1730 0.2494 0.2314 -0.0256 0.0200  0.0339  167 SER   A N   
3917 C  CA  A SER   A 167 ? 0.1733 0.2925 0.1785 0.0072  -0.0136 0.0114  167 SER   A CA  
3918 C  CA  B SER   A 167 ? 0.2012 0.2633 0.2453 -0.0126 0.0288  0.0195  167 SER   A CA  
3919 C  C   A SER   A 167 ? 0.1732 0.2997 0.1690 0.0162  0.0001  0.0109  167 SER   A C   
3920 C  C   B SER   A 167 ? 0.2086 0.2721 0.2757 0.0036  0.0347  0.0137  167 SER   A C   
3921 O  O   A SER   A 167 ? 0.1803 0.3101 0.1638 0.0097  -0.0039 0.0193  167 SER   A O   
3922 O  O   B SER   A 167 ? 0.2294 0.2828 0.3204 0.0077  0.0329  0.0146  167 SER   A O   
3923 C  CB  A SER   A 167 ? 0.1830 0.2925 0.1858 0.0049  -0.0073 0.0068  167 SER   A CB  
3924 C  CB  B SER   A 167 ? 0.2149 0.2687 0.2334 -0.0123 0.0443  0.0063  167 SER   A CB  
3925 O  OG  A SER   A 167 ? 0.1948 0.2915 0.1839 0.0027  -0.0033 -0.0034 167 SER   A OG  
3926 O  OG  B SER   A 167 ? 0.2213 0.2734 0.2111 -0.0078 0.0712  0.0003  167 SER   A OG  
3937 N  N   A PHE   A 168 ? 0.1662 0.2892 0.1616 0.0260  0.0100  0.0087  168 PHE   A N   
3938 N  N   B PHE   A 168 ? 0.1924 0.2683 0.2490 0.0054  0.0446  0.0095  168 PHE   A N   
3939 C  CA  A PHE   A 168 ? 0.1672 0.2778 0.1884 0.0160  0.0172  0.0186  168 PHE   A CA  
3940 C  CA  B PHE   A 168 ? 0.1862 0.2698 0.2256 0.0084  0.0496  0.0070  168 PHE   A CA  
3941 C  C   A PHE   A 168 ? 0.1812 0.2816 0.2375 0.0025  0.0441  0.0146  168 PHE   A C   
3942 C  C   B PHE   A 168 ? 0.1936 0.2740 0.2360 0.0051  0.0535  0.0002  168 PHE   A C   
3943 O  O   A PHE   A 168 ? 0.1938 0.2858 0.2898 -0.0073 0.0491  0.0287  168 PHE   A O   
3944 O  O   B PHE   A 168 ? 0.1857 0.2687 0.2194 0.0110  0.0632  0.0012  168 PHE   A O   
3945 C  CB  A PHE   A 168 ? 0.1662 0.2657 0.1682 0.0096  0.0021  0.0295  168 PHE   A CB  
3946 C  CB  B PHE   A 168 ? 0.1829 0.2718 0.2199 0.0026  0.0326  0.0196  168 PHE   A CB  
3947 C  CG  A PHE   A 168 ? 0.1619 0.2562 0.1591 0.0028  0.0012  0.0356  168 PHE   A CG  
3948 C  CG  B PHE   A 168 ? 0.1812 0.2705 0.2120 -0.0015 0.0197  0.0343  168 PHE   A CG  
3949 C  CD1 A PHE   A 168 ? 0.1669 0.2596 0.1579 -0.0060 0.0019  0.0398  168 PHE   A CD1 
3950 C  CD1 B PHE   A 168 ? 0.1840 0.2728 0.2160 -0.0027 0.0183  0.0451  168 PHE   A CD1 
3951 C  CD2 A PHE   A 168 ? 0.1604 0.2516 0.1498 -0.0028 0.0184  0.0348  168 PHE   A CD2 
3952 C  CD2 B PHE   A 168 ? 0.1835 0.2699 0.2030 0.0012  0.0073  0.0426  168 PHE   A CD2 
3953 C  CE1 A PHE   A 168 ? 0.1606 0.2575 0.1472 -0.0081 0.0023  0.0385  168 PHE   A CE1 
3954 C  CE1 B PHE   A 168 ? 0.1832 0.2747 0.2201 -0.0039 0.0109  0.0490  168 PHE   A CE1 
3955 C  CE2 A PHE   A 168 ? 0.1668 0.2478 0.1453 -0.0026 0.0118  0.0381  168 PHE   A CE2 
3956 C  CE2 B PHE   A 168 ? 0.1872 0.2719 0.2093 0.0026  -0.0041 0.0499  168 PHE   A CE2 
3957 C  CZ  A PHE   A 168 ? 0.1624 0.2532 0.1490 -0.0068 0.0088  0.0359  168 PHE   A CZ  
3958 C  CZ  B PHE   A 168 ? 0.1878 0.2743 0.2163 -0.0015 0.0058  0.0482  168 PHE   A CZ  
3977 N  N   A LEU   A 169 ? 0.2002 0.2795 0.2598 -0.0061 0.0470  -0.0045 169 LEU   A N   
3978 N  N   B LEU   A 169 ? 0.2047 0.2834 0.2589 0.0041  0.0433  -0.0040 169 LEU   A N   
3979 C  CA  A LEU   A 169 ? 0.2313 0.2876 0.3062 -0.0074 0.0316  -0.0089 169 LEU   A CA  
3980 C  CA  B LEU   A 169 ? 0.2238 0.2958 0.2882 0.0020  0.0288  -0.0110 169 LEU   A CA  
3981 C  C   A LEU   A 169 ? 0.2266 0.2827 0.3225 -0.0089 0.0431  0.0036  169 LEU   A C   
3982 C  C   B LEU   A 169 ? 0.2322 0.2995 0.2984 0.0001  0.0152  -0.0234 169 LEU   A C   
3983 O  O   A LEU   A 169 ? 0.2329 0.2863 0.3356 -0.0066 0.0375  0.0069  169 LEU   A O   
3984 O  O   B LEU   A 169 ? 0.2436 0.3028 0.3129 0.0001  0.0154  -0.0230 169 LEU   A O   
3985 C  CB  A LEU   A 169 ? 0.2574 0.3008 0.3160 -0.0036 0.0230  -0.0227 169 LEU   A CB  
3986 C  CB  B LEU   A 169 ? 0.2343 0.3040 0.2994 0.0047  0.0299  -0.0071 169 LEU   A CB  
3987 C  CG  A LEU   A 169 ? 0.2822 0.3110 0.3206 -0.0031 0.0162  -0.0376 169 LEU   A CG  
3988 C  CG  B LEU   A 169 ? 0.2461 0.3101 0.3164 0.0075  0.0290  -0.0029 169 LEU   A CG  
3989 C  CD1 A LEU   A 169 ? 0.2948 0.3124 0.3208 -0.0035 0.0082  -0.0418 169 LEU   A CD1 
3990 C  CD1 B LEU   A 169 ? 0.2556 0.3164 0.3190 0.0101  0.0354  0.0062  169 LEU   A CD1 
3991 C  CD2 A LEU   A 169 ? 0.2883 0.3153 0.3175 -0.0045 0.0178  -0.0432 169 LEU   A CD2 
3992 C  CD2 B LEU   A 169 ? 0.2553 0.3132 0.3292 0.0095  0.0193  -0.0052 169 LEU   A CD2 
3993 O  OXT A LEU   A 169 ? 0.2158 0.2817 0.3131 -0.0157 0.0640  0.0006  169 LEU   A OXT 
3994 O  OXT B LEU   A 169 ? 0.2294 0.3000 0.2959 -0.0062 -0.0000 -0.0318 169 LEU   A OXT 
4017 N  N   A SER   B 1   ? 0.3729 0.3518 0.3360 -0.0971 -0.0773 0.0390  1   SER   B N   
4018 N  N   B SER   B 1   ? 0.3179 0.3261 0.3238 -0.0986 -0.0582 0.0525  1   SER   B N   
4019 C  CA  A SER   B 1   ? 0.3650 0.3539 0.3385 -0.1004 -0.0868 0.0329  1   SER   B CA  
4020 C  CA  B SER   B 1   ? 0.3084 0.3266 0.3179 -0.1022 -0.0654 0.0500  1   SER   B CA  
4021 C  C   A SER   B 1   ? 0.3466 0.3561 0.3355 -0.0992 -0.0859 0.0464  1   SER   B C   
4022 C  C   B SER   B 1   ? 0.2869 0.3237 0.2941 -0.1029 -0.0740 0.0642  1   SER   B C   
4023 O  O   A SER   B 1   ? 0.3548 0.3576 0.3252 -0.0963 -0.0754 0.0475  1   SER   B O   
4024 O  O   B SER   B 1   ? 0.2940 0.3244 0.2795 -0.0998 -0.0686 0.0634  1   SER   B O   
4025 C  CB  A SER   B 1   ? 0.3723 0.3511 0.3527 -0.1023 -0.0856 0.0163  1   SER   B CB  
4026 C  CB  B SER   B 1   ? 0.3160 0.3270 0.3422 -0.1028 -0.0546 0.0364  1   SER   B CB  
4027 O  OG  A SER   B 1   ? 0.3834 0.3576 0.3897 -0.1000 -0.0730 0.0079  1   SER   B OG  
4028 O  OG  B SER   B 1   ? 0.3255 0.3346 0.3768 -0.1006 -0.0444 0.0272  1   SER   B OG  
4043 N  N   A MET   B 2   ? 0.3255 0.3541 0.3394 -0.0955 -0.0816 0.0728  2   MET   B N   
4044 N  N   B MET   B 2   ? 0.2651 0.3173 0.2811 -0.1007 -0.0733 0.0973  2   MET   B N   
4045 C  CA  A MET   B 2   ? 0.3085 0.3507 0.3571 -0.0802 -0.0746 0.0935  2   MET   B CA  
4046 C  CA  B MET   B 2   ? 0.2512 0.3131 0.2823 -0.0814 -0.0705 0.1180  2   MET   B CA  
4047 C  C   A MET   B 2   ? 0.2726 0.3257 0.3245 -0.0692 -0.0831 0.1160  2   MET   B C   
4048 C  C   B MET   B 2   ? 0.2269 0.2925 0.2540 -0.0639 -0.0705 0.1271  2   MET   B C   
4049 O  O   A MET   B 2   ? 0.2693 0.3363 0.3213 -0.0599 -0.0964 0.1179  2   MET   B O   
4050 O  O   B MET   B 2   ? 0.2219 0.2970 0.2486 -0.0564 -0.0721 0.1166  2   MET   B O   
4051 C  CB  A MET   B 2   ? 0.3325 0.3764 0.4289 -0.0655 -0.0536 0.0771  2   MET   B CB  
4052 C  CB  B MET   B 2   ? 0.2706 0.3361 0.3293 -0.0661 -0.0639 0.1128  2   MET   B CB  
4053 C  CG  A MET   B 2   ? 0.3534 0.3963 0.5024 -0.0503 -0.0347 0.0667  2   MET   B CG  
4054 C  CG  B MET   B 2   ? 0.2861 0.3547 0.3656 -0.0489 -0.0597 0.1201  2   MET   B CG  
4055 S  SD  A MET   B 2   ? 0.3734 0.4125 0.5686 -0.0381 -0.0209 0.0581  2   MET   B SD  
4056 S  SD  B MET   B 2   ? 0.3027 0.3745 0.3948 -0.0328 -0.0607 0.1255  2   MET   B SD  
4057 C  CE  A MET   B 2   ? 0.3731 0.4152 0.5722 -0.0392 -0.0132 0.0581  2   MET   B CE  
4058 C  CE  B MET   B 2   ? 0.3016 0.3745 0.4023 -0.0339 -0.0554 0.1172  2   MET   B CE  
4077 N  N   A VAL   B 3   ? 0.2396 0.2852 0.3043 -0.0745 -0.0743 0.1288  3   VAL   B N   
4078 N  N   B VAL   B 3   ? 0.2084 0.2665 0.2426 -0.0592 -0.0653 0.1348  3   VAL   B N   
4079 C  CA  A VAL   B 3   ? 0.2200 0.2538 0.2965 -0.0698 -0.0719 0.1105  3   VAL   B CA  
4080 C  CA  B VAL   B 3   ? 0.2043 0.2487 0.2519 -0.0467 -0.0588 0.1100  3   VAL   B CA  
4081 C  C   A VAL   B 3   ? 0.1980 0.2332 0.2544 -0.0609 -0.0602 0.1037  3   VAL   B C   
4082 C  C   B VAL   B 3   ? 0.1937 0.2394 0.2301 -0.0439 -0.0553 0.0999  3   VAL   B C   
4083 O  O   A VAL   B 3   ? 0.1873 0.2244 0.2623 -0.0609 -0.0610 0.1115  3   VAL   B O   
4084 O  O   B VAL   B 3   ? 0.1903 0.2456 0.2289 -0.0288 -0.0666 0.1047  3   VAL   B O   
4085 C  CB  A VAL   B 3   ? 0.2304 0.2527 0.3425 -0.0740 -0.0665 0.0907  3   VAL   B CB  
4086 C  CB  B VAL   B 3   ? 0.2184 0.2445 0.2886 -0.0412 -0.0469 0.0948  3   VAL   B CB  
4087 C  CG1 A VAL   B 3   ? 0.2370 0.2499 0.3586 -0.0732 -0.0647 0.0870  3   VAL   B CG1 
4088 C  CG1 B VAL   B 3   ? 0.2246 0.2405 0.3006 -0.0415 -0.0422 0.0903  3   VAL   B CG1 
4089 C  CG2 A VAL   B 3   ? 0.2316 0.2569 0.3596 -0.0758 -0.0576 0.0881  3   VAL   B CG2 
4090 C  CG2 B VAL   B 3   ? 0.2219 0.2472 0.2999 -0.0393 -0.0417 0.0924  3   VAL   B CG2 
4109 N  N   . ASN   B 4   ? 0.1876 0.2228 0.2150 -0.0579 -0.0507 0.0857  4   ASN   B N   
4110 C  CA  . ASN   B 4   ? 0.1887 0.2190 0.1780 -0.0555 -0.0381 0.0454  4   ASN   B CA  
4111 C  C   . ASN   B 4   ? 0.1929 0.2373 0.1679 -0.0591 -0.0320 0.0317  4   ASN   B C   
4112 O  O   . ASN   B 4   ? 0.1929 0.2469 0.2016 -0.0570 -0.0273 0.0166  4   ASN   B O   
4113 C  CB  . ASN   B 4   ? 0.1888 0.2120 0.1714 -0.0516 -0.0502 0.0343  4   ASN   B CB  
4114 C  CG  . ASN   B 4   ? 0.1894 0.1989 0.1657 -0.0505 -0.0496 0.0332  4   ASN   B CG  
4115 O  OD1 . ASN   B 4   ? 0.1947 0.1832 0.1753 -0.0475 -0.0540 0.0323  4   ASN   B OD1 
4116 N  ND2 . ASN   B 4   ? 0.2048 0.2097 0.1728 -0.0331 -0.0360 0.0317  4   ASN   B ND2 
4124 N  N   . SER   B 5   ? 0.2067 0.2592 0.1755 -0.0630 -0.0207 0.0379  5   SER   B N   
4125 C  CA  . SER   B 5   ? 0.2380 0.2949 0.2080 -0.0559 -0.0092 0.0391  5   SER   B CA  
4126 C  C   . SER   B 5   ? 0.2578 0.2972 0.2382 -0.0739 0.0133  0.0380  5   SER   B C   
4127 O  O   . SER   B 5   ? 0.2746 0.2876 0.3085 -0.0645 0.0388  0.0374  5   SER   B O   
4128 C  CB  . SER   B 5   ? 0.2539 0.3160 0.2344 -0.0456 -0.0038 0.0508  5   SER   B CB  
4129 O  OG  . SER   B 5   ? 0.2815 0.3439 0.2872 -0.0311 -0.0009 0.0564  5   SER   B OG  
4135 N  N   . PHE   B 6   ? 0.2764 0.3184 0.2195 -0.0808 0.0342  0.0446  6   PHE   B N   
4136 C  CA  . PHE   B 6   ? 0.2848 0.3230 0.1849 -0.0979 0.0403  0.0183  6   PHE   B CA  
4137 C  C   . PHE   B 6   ? 0.3346 0.3576 0.2396 -0.1033 0.0649  -0.0159 6   PHE   B C   
4138 O  O   . PHE   B 6   ? 0.3491 0.3853 0.2721 -0.0914 0.0510  -0.0303 6   PHE   B O   
4139 C  CB  . PHE   B 6   ? 0.2550 0.2979 0.1735 -0.0863 0.0171  0.0150  6   PHE   B CB  
4140 C  CG  . PHE   B 6   ? 0.2170 0.2630 0.1623 -0.0789 0.0041  0.0117  6   PHE   B CG  
4141 C  CD1 . PHE   B 6   ? 0.2158 0.2401 0.1405 -0.0667 -0.0069 0.0060  6   PHE   B CD1 
4142 C  CD2 . PHE   B 6   ? 0.1934 0.2593 0.1619 -0.0653 0.0049  0.0372  6   PHE   B CD2 
4143 C  CE1 . PHE   B 6   ? 0.2112 0.2198 0.1525 -0.0501 -0.0043 0.0084  6   PHE   B CE1 
4144 C  CE2 . PHE   B 6   ? 0.1959 0.2514 0.1988 -0.0488 0.0096  0.0335  6   PHE   B CE2 
4145 C  CZ  . PHE   B 6   ? 0.1992 0.2272 0.1783 -0.0459 0.0026  0.0138  6   PHE   B CZ  
4155 N  N   . SER   B 7   ? 0.3718 0.3504 0.2533 -0.1283 0.0960  -0.0424 7   SER   B N   
4156 C  CA  . SER   B 7   ? 0.4109 0.3682 0.3160 -0.1305 0.1239  -0.0457 7   SER   B CA  
4157 C  C   . SER   B 7   ? 0.4076 0.3456 0.3083 -0.1327 0.1439  -0.0644 7   SER   B C   
4158 O  O   . SER   B 7   ? 0.4145 0.3394 0.3345 -0.1370 0.1453  -0.0719 7   SER   B O   
4159 C  CB  . SER   B 7   ? 0.4348 0.3917 0.3894 -0.1288 0.1391  -0.0371 7   SER   B CB  
4160 O  OG  . SER   B 7   ? 0.4470 0.4065 0.4445 -0.1271 0.1468  -0.0294 7   SER   B OG  
4166 N  N   . GLY   B 8   ? 0.4007 0.3283 0.3096 -0.1153 0.1423  -0.0783 8   GLY   B N   
4167 C  CA  . GLY   B 8   ? 0.3851 0.3090 0.3072 -0.1046 0.1448  -0.0818 8   GLY   B CA  
4168 C  C   . GLY   B 8   ? 0.3650 0.2818 0.2928 -0.0966 0.1497  -0.0697 8   GLY   B C   
4169 O  O   . GLY   B 8   ? 0.3766 0.2865 0.3306 -0.0866 0.1515  -0.0725 8   GLY   B O   
4173 N  N   . TYR   B 9   ? 0.3452 0.2565 0.2634 -0.0839 0.1223  -0.0761 9   TYR   B N   
4174 C  CA  . TYR   B 9   ? 0.3207 0.2255 0.2386 -0.0694 0.0935  -0.0645 9   TYR   B CA  
4175 C  C   . TYR   B 9   ? 0.3133 0.2219 0.2298 -0.0639 0.0598  -0.0509 9   TYR   B C   
4176 O  O   . TYR   B 9   ? 0.3234 0.2398 0.2654 -0.0685 0.0543  -0.0410 9   TYR   B O   
4177 C  CB  . TYR   B 9   ? 0.3074 0.2014 0.2471 -0.0645 0.0860  -0.0622 9   TYR   B CB  
4178 C  CG  . TYR   B 9   ? 0.2924 0.1837 0.2536 -0.0701 0.0790  -0.0640 9   TYR   B CG  
4179 C  CD1 . TYR   B 9   ? 0.2922 0.1867 0.2676 -0.0815 0.0860  -0.0607 9   TYR   B CD1 
4180 C  CD2 . TYR   B 9   ? 0.2786 0.1823 0.2443 -0.0614 0.0677  -0.0691 9   TYR   B CD2 
4181 C  CE1 . TYR   B 9   ? 0.2868 0.1976 0.2741 -0.0842 0.0832  -0.0640 9   TYR   B CE1 
4182 C  CE2 . TYR   B 9   ? 0.2759 0.1792 0.2531 -0.0627 0.0714  -0.0659 9   TYR   B CE2 
4183 C  CZ  . TYR   B 9   ? 0.2796 0.1959 0.2651 -0.0767 0.0762  -0.0741 9   TYR   B CZ  
4184 O  OH  . TYR   B 9   ? 0.2745 0.2118 0.2778 -0.0909 0.0734  -0.0767 9   TYR   B OH  
4194 N  N   . LEU   B 10  ? 0.2922 0.1957 0.2066 -0.0633 0.0358  -0.0480 10  LEU   B N   
4195 C  CA  . LEU   B 10  ? 0.2891 0.1977 0.2017 -0.0747 -0.0055 -0.0445 10  LEU   B CA  
4196 C  C   . LEU   B 10  ? 0.2681 0.1953 0.2036 -0.0732 -0.0226 -0.0423 10  LEU   B C   
4197 O  O   . LEU   B 10  ? 0.2526 0.1947 0.2095 -0.0553 -0.0165 -0.0302 10  LEU   B O   
4198 C  CB  . LEU   B 10  ? 0.3063 0.2011 0.2173 -0.0810 -0.0262 -0.0186 10  LEU   B CB  
4199 C  CG  . LEU   B 10  ? 0.3260 0.2114 0.2628 -0.0740 -0.0547 -0.0050 10  LEU   B CG  
4200 C  CD1 . LEU   B 10  ? 0.3401 0.2218 0.2857 -0.0670 -0.0536 -0.0074 10  LEU   B CD1 
4201 C  CD2 . LEU   B 10  ? 0.3347 0.2133 0.2930 -0.0709 -0.0491 0.0135  10  LEU   B CD2 
4213 N  N   . LYS   B 11  ? 0.2825 0.2225 0.2132 -0.0639 -0.0236 -0.0321 11  LYS   B N   
4214 C  CA  . LYS   B 11  ? 0.2968 0.2466 0.2415 -0.0530 -0.0340 -0.0302 11  LYS   B CA  
4215 C  C   . LYS   B 11  ? 0.2771 0.2246 0.2423 -0.0707 -0.0390 -0.0448 11  LYS   B C   
4216 O  O   . LYS   B 11  ? 0.2891 0.2444 0.2806 -0.0837 -0.0409 -0.0663 11  LYS   B O   
4217 C  CB  . LYS   B 11  ? 0.3326 0.2943 0.3100 -0.0275 -0.0401 -0.0254 11  LYS   B CB  
4218 C  CG  . LYS   B 11  ? 0.3641 0.3248 0.3856 -0.0129 -0.0482 -0.0275 11  LYS   B CG  
4219 C  CD  . LYS   B 11  ? 0.3873 0.3467 0.4516 -0.0031 -0.0494 -0.0331 11  LYS   B CD  
4220 C  CE  . LYS   B 11  ? 0.4033 0.3627 0.5001 0.0012  -0.0483 -0.0346 11  LYS   B CE  
4221 N  NZ  . LYS   B 11  ? 0.4131 0.3725 0.5279 0.0026  -0.0486 -0.0313 11  LYS   B NZ  
4235 N  N   . LEU   B 12  ? 0.2438 0.2008 0.2418 -0.0622 -0.0351 -0.0440 12  LEU   B N   
4236 C  CA  . LEU   B 12  ? 0.2307 0.1806 0.2571 -0.0557 -0.0298 -0.0338 12  LEU   B CA  
4237 C  C   . LEU   B 12  ? 0.2200 0.1845 0.2691 -0.0581 -0.0366 -0.0216 12  LEU   B C   
4238 O  O   . LEU   B 12  ? 0.2209 0.1889 0.2942 -0.0670 -0.0558 -0.0185 12  LEU   B O   
4239 C  CB  . LEU   B 12  ? 0.2328 0.1613 0.2575 -0.0419 -0.0213 -0.0331 12  LEU   B CB  
4240 C  CG  . LEU   B 12  ? 0.2307 0.1618 0.2553 -0.0458 -0.0058 -0.0310 12  LEU   B CG  
4241 C  CD1 . LEU   B 12  ? 0.2391 0.1726 0.2462 -0.0290 -0.0057 -0.0111 12  LEU   B CD1 
4242 C  CD2 . LEU   B 12  ? 0.2424 0.1673 0.2700 -0.0445 -0.0054 -0.0400 12  LEU   B CD2 
4254 N  N   . THR   B 13  ? 0.2092 0.1867 0.2659 -0.0548 -0.0412 -0.0369 13  THR   B N   
4255 C  CA  . THR   B 13  ? 0.2126 0.1925 0.2623 -0.0589 -0.0491 -0.0251 13  THR   B CA  
4256 C  C   . THR   B 13  ? 0.2515 0.2081 0.2736 -0.0676 -0.0653 -0.0196 13  THR   B C   
4257 O  O   . THR   B 13  ? 0.2694 0.2066 0.2803 -0.0690 -0.0365 -0.0153 13  THR   B O   
4258 C  CB  . THR   B 13  ? 0.1956 0.1915 0.2619 -0.0548 -0.0473 -0.0179 13  THR   B CB  
4259 O  OG1 . THR   B 13  ? 0.1874 0.1877 0.2665 -0.0432 -0.0327 -0.0220 13  THR   B OG1 
4260 C  CG2 . THR   B 13  ? 0.2016 0.1970 0.2628 -0.0474 -0.0354 -0.0057 13  THR   B CG2 
4268 N  N   A ASP   B 14  ? 0.2631 0.2229 0.2875 -0.0702 -0.0959 -0.0123 14  ASP   B N   
4269 N  N   B ASP   B 14  ? 0.2621 0.2223 0.2843 -0.0661 -0.0820 -0.0096 14  ASP   B N   
4270 C  CA  A ASP   B 14  ? 0.2689 0.2376 0.3107 -0.0711 -0.1040 0.0052  14  ASP   B CA  
4271 C  CA  B ASP   B 14  ? 0.2671 0.2352 0.3004 -0.0636 -0.0851 0.0064  14  ASP   B CA  
4272 C  C   A ASP   B 14  ? 0.2533 0.2200 0.2654 -0.0742 -0.0927 0.0068  14  ASP   B C   
4273 C  C   B ASP   B 14  ? 0.2496 0.2178 0.2622 -0.0644 -0.0834 0.0062  14  ASP   B C   
4274 O  O   A ASP   B 14  ? 0.2720 0.2291 0.2679 -0.0724 -0.0877 0.0147  14  ASP   B O   
4275 O  O   B ASP   B 14  ? 0.2619 0.2214 0.2620 -0.0569 -0.0794 0.0087  14  ASP   B O   
4276 C  CB  A ASP   B 14  ? 0.2886 0.2662 0.3882 -0.0669 -0.1129 0.0100  14  ASP   B CB  
4277 C  CB  B ASP   B 14  ? 0.2875 0.2618 0.3603 -0.0577 -0.0829 0.0140  14  ASP   B CB  
4278 C  CG  A ASP   B 14  ? 0.3101 0.2896 0.4593 -0.0609 -0.1126 -0.0003 14  ASP   B CG  
4279 C  CG  B ASP   B 14  ? 0.3074 0.2838 0.4139 -0.0505 -0.0785 0.0093  14  ASP   B CG  
4280 O  OD1 A ASP   B 14  ? 0.3226 0.2964 0.4773 -0.0647 -0.1131 -0.0116 14  ASP   B OD1 
4281 O  OD1 B ASP   B 14  ? 0.3145 0.2936 0.4294 -0.0491 -0.0724 0.0042  14  ASP   B OD1 
4282 O  OD2 A ASP   B 14  ? 0.3141 0.3005 0.4917 -0.0590 -0.1102 0.0009  14  ASP   B OD2 
4283 O  OD2 B ASP   B 14  ? 0.3144 0.2906 0.4366 -0.0525 -0.0796 0.0090  14  ASP   B OD2 
4292 N  N   . ASN   B 15  ? 0.2238 0.1956 0.2402 -0.0622 -0.0808 0.0070  15  ASN   B N   
4293 C  CA  . ASN   B 15  ? 0.1871 0.1671 0.2177 -0.0422 -0.0541 0.0037  15  ASN   B CA  
4294 C  C   . ASN   B 15  ? 0.1693 0.1595 0.2102 -0.0291 -0.0407 -0.0039 15  ASN   B C   
4295 O  O   . ASN   B 15  ? 0.1622 0.1590 0.2188 -0.0260 -0.0405 -0.0162 15  ASN   B O   
4296 C  CB  . ASN   B 15  ? 0.1776 0.1638 0.2379 -0.0238 -0.0504 0.0089  15  ASN   B CB  
4297 C  CG  . ASN   B 15  ? 0.1607 0.1595 0.2515 -0.0282 -0.0263 0.0105  15  ASN   B CG  
4298 O  OD1 . ASN   B 15  ? 0.1707 0.1875 0.2772 -0.0471 -0.0349 0.0202  15  ASN   B OD1 
4299 N  ND2 . ASN   B 15  ? 0.1613 0.1416 0.2299 -0.0153 -0.0103 -0.0119 15  ASN   B ND2 
4307 N  N   . VAL   B 16  ? 0.1734 0.1512 0.2089 -0.0326 -0.0433 -0.0000 16  VAL   B N   
4308 C  CA  . VAL   B 16  ? 0.1728 0.1510 0.2031 -0.0303 -0.0344 -0.0188 16  VAL   B CA  
4309 C  C   . VAL   B 16  ? 0.1750 0.1625 0.1997 -0.0376 -0.0315 -0.0122 16  VAL   B C   
4310 O  O   . VAL   B 16  ? 0.1717 0.1738 0.2174 -0.0348 -0.0325 -0.0282 16  VAL   B O   
4311 C  CB  . VAL   B 16  ? 0.1758 0.1522 0.2148 -0.0204 -0.0239 -0.0164 16  VAL   B CB  
4312 C  CG1 . VAL   B 16  ? 0.1833 0.1454 0.2071 -0.0087 -0.0171 -0.0055 16  VAL   B CG1 
4313 C  CG2 . VAL   B 16  ? 0.1818 0.1595 0.2349 -0.0130 -0.0192 -0.0215 16  VAL   B CG2 
4323 N  N   . TYR   B 17  ? 0.1766 0.1672 0.1944 -0.0364 -0.0341 -0.0169 17  TYR   B N   
4324 C  CA  . TYR   B 17  ? 0.1856 0.1816 0.1857 -0.0406 -0.0213 -0.0010 17  TYR   B CA  
4325 C  C   . TYR   B 17  ? 0.1756 0.1598 0.1899 -0.0391 -0.0168 -0.0096 17  TYR   B C   
4326 O  O   . TYR   B 17  ? 0.1740 0.1675 0.1957 -0.0411 -0.0228 -0.0231 17  TYR   B O   
4327 C  CB  . TYR   B 17  ? 0.2142 0.2267 0.2045 -0.0260 -0.0274 0.0345  17  TYR   B CB  
4328 C  CG  . TYR   B 17  ? 0.2381 0.2724 0.2492 -0.0187 -0.0401 0.0347  17  TYR   B CG  
4329 C  CD1 . TYR   B 17  ? 0.2524 0.2881 0.2694 -0.0146 -0.0476 0.0437  17  TYR   B CD1 
4330 C  CD2 . TYR   B 17  ? 0.2574 0.3008 0.2741 -0.0070 -0.0475 0.0300  17  TYR   B CD2 
4331 C  CE1 . TYR   B 17  ? 0.2709 0.3111 0.2860 -0.0060 -0.0562 0.0385  17  TYR   B CE1 
4332 C  CE2 . TYR   B 17  ? 0.2732 0.3182 0.2963 0.0074  -0.0638 0.0356  17  TYR   B CE2 
4333 C  CZ  . TYR   B 17  ? 0.2849 0.3227 0.2997 0.0073  -0.0685 0.0370  17  TYR   B CZ  
4334 O  OH  . TYR   B 17  ? 0.3018 0.3397 0.3233 0.0167  -0.0733 0.0364  17  TYR   B OH  
4344 N  N   . ILE   B 18  ? 0.1835 0.1567 0.1867 -0.0353 -0.0022 -0.0207 18  ILE   B N   
4345 C  CA  . ILE   B 18  ? 0.1868 0.1578 0.1864 -0.0353 -0.0065 -0.0258 18  ILE   B CA  
4346 C  C   . ILE   B 18  ? 0.1999 0.1650 0.1864 -0.0471 -0.0028 -0.0393 18  ILE   B C   
4347 O  O   . ILE   B 18  ? 0.2189 0.1783 0.2072 -0.0422 0.0021  -0.0467 18  ILE   B O   
4348 C  CB  . ILE   B 18  ? 0.1885 0.1616 0.2007 -0.0455 -0.0023 -0.0213 18  ILE   B CB  
4349 C  CG1 . ILE   B 18  ? 0.1842 0.1715 0.2048 -0.0435 0.0045  -0.0141 18  ILE   B CG1 
4350 C  CG2 . ILE   B 18  ? 0.1956 0.1629 0.2044 -0.0440 -0.0129 -0.0222 18  ILE   B CG2 
4351 C  CD1 . ILE   B 18  ? 0.1944 0.1966 0.2257 -0.0345 -0.0114 -0.0023 18  ILE   B CD1 
4363 N  N   . LYS   B 19  ? 0.2020 0.1561 0.2011 -0.0295 0.0285  -0.0415 19  LYS   B N   
4364 C  CA  . LYS   B 19  ? 0.2068 0.1604 0.2296 -0.0329 0.0305  -0.0471 19  LYS   B CA  
4365 C  C   . LYS   B 19  ? 0.1916 0.1619 0.2406 -0.0283 0.0338  -0.0582 19  LYS   B C   
4366 O  O   . LYS   B 19  ? 0.1873 0.1650 0.2200 -0.0203 0.0248  -0.0480 19  LYS   B O   
4367 C  CB  . LYS   B 19  ? 0.2228 0.1835 0.2396 -0.0418 0.0475  -0.0336 19  LYS   B CB  
4368 C  CG  . LYS   B 19  ? 0.2491 0.2022 0.2565 -0.0449 0.0496  -0.0424 19  LYS   B CG  
4369 C  CD  . LYS   B 19  ? 0.2785 0.2306 0.2688 -0.0531 0.0549  -0.0401 19  LYS   B CD  
4370 C  CE  . LYS   B 19  ? 0.3077 0.2600 0.2889 -0.0530 0.0526  -0.0428 19  LYS   B CE  
4371 N  NZ  . LYS   B 19  ? 0.3281 0.2779 0.2954 -0.0600 0.0585  -0.0369 19  LYS   B NZ  
4385 N  N   . ASN   B 20  ? 0.1885 0.1716 0.2744 -0.0212 0.0418  -0.0718 20  ASN   B N   
4386 C  CA  . ASN   B 20  ? 0.1879 0.1870 0.2985 -0.0190 0.0501  -0.0860 20  ASN   B CA  
4387 C  C   . ASN   B 20  ? 0.1916 0.2040 0.2955 -0.0211 0.0602  -0.0943 20  ASN   B C   
4388 O  O   . ASN   B 20  ? 0.2087 0.2356 0.3167 -0.0408 0.0592  -0.0915 20  ASN   B O   
4389 C  CB  . ASN   B 20  ? 0.2160 0.1938 0.3306 0.0035  0.0387  -0.0863 20  ASN   B CB  
4390 C  CG  . ASN   B 20  ? 0.2440 0.1981 0.3537 0.0346  0.0369  -0.0941 20  ASN   B CG  
4391 O  OD1 . ASN   B 20  ? 0.2794 0.2293 0.3864 0.0508  0.0352  -0.0964 20  ASN   B OD1 
4392 N  ND2 . ASN   B 20  ? 0.2346 0.2019 0.3485 0.0378  0.0200  -0.0832 20  ASN   B ND2 
4399 N  N   . ALA   B 21  ? 0.1934 0.1877 0.2907 -0.0322 0.0585  -0.0702 21  ALA   B N   
4400 C  CA  . ALA   B 21  ? 0.2039 0.1922 0.3046 -0.0322 0.0397  -0.0544 21  ALA   B CA  
4401 C  C   . ALA   B 21  ? 0.2000 0.1713 0.2868 -0.0227 0.0468  -0.0392 21  ALA   B C   
4402 O  O   . ALA   B 21  ? 0.2020 0.1613 0.2802 -0.0301 0.0408  -0.0342 21  ALA   B O   
4403 C  CB  . ALA   B 21  ? 0.2142 0.2158 0.3116 -0.0395 0.0387  -0.0419 21  ALA   B CB  
4409 N  N   . ASP   B 22  ? 0.1916 0.1619 0.2763 -0.0196 0.0437  -0.0307 22  ASP   B N   
4410 C  CA  . ASP   B 22  ? 0.1858 0.1528 0.2554 -0.0068 0.0333  -0.0368 22  ASP   B CA  
4411 C  C   . ASP   B 22  ? 0.1776 0.1538 0.2083 -0.0176 0.0268  -0.0183 22  ASP   B C   
4412 O  O   . ASP   B 22  ? 0.1839 0.1586 0.2094 -0.0148 0.0164  -0.0116 22  ASP   B O   
4413 C  CB  . ASP   B 22  ? 0.1905 0.1679 0.2997 -0.0029 0.0298  -0.0247 22  ASP   B CB  
4414 C  CG  . ASP   B 22  ? 0.1939 0.1824 0.3403 0.0009  0.0033  -0.0161 22  ASP   B CG  
4415 O  OD1 . ASP   B 22  ? 0.2034 0.1792 0.3408 0.0027  -0.0136 -0.0116 22  ASP   B OD1 
4416 O  OD2 . ASP   B 22  ? 0.2057 0.2043 0.3965 0.0132  -0.0254 -0.0212 22  ASP   B OD2 
4421 N  N   . ILE   B 23  ? 0.1763 0.1464 0.1919 -0.0138 0.0094  0.0119  23  ILE   B N   
4422 C  CA  . ILE   B 23  ? 0.1638 0.1481 0.1689 -0.0130 0.0023  -0.0018 23  ILE   B CA  
4423 C  C   . ILE   B 23  ? 0.1603 0.1500 0.1721 -0.0071 -0.0102 0.0003  23  ILE   B C   
4424 O  O   . ILE   B 23  ? 0.1552 0.1476 0.1633 -0.0100 -0.0080 0.0073  23  ILE   B O   
4425 C  CB  . ILE   B 23  ? 0.1662 0.1544 0.1865 -0.0189 0.0003  0.0128  23  ILE   B CB  
4426 C  CG1 . ILE   B 23  ? 0.1665 0.1643 0.1985 -0.0153 0.0036  0.0240  23  ILE   B CG1 
4427 C  CG2 . ILE   B 23  ? 0.1763 0.1658 0.1957 -0.0184 -0.0008 0.0081  23  ILE   B CG2 
4428 C  CD1 . ILE   B 23  ? 0.1754 0.1726 0.1970 -0.0115 0.0032  0.0240  23  ILE   B CD1 
4440 N  N   . VAL   B 24  ? 0.1615 0.1512 0.1717 -0.0100 -0.0139 0.0037  24  VAL   B N   
4441 C  CA  . VAL   B 24  ? 0.1617 0.1546 0.1992 -0.0119 -0.0226 0.0010  24  VAL   B CA  
4442 C  C   . VAL   B 24  ? 0.1631 0.1610 0.2026 -0.0159 -0.0107 0.0077  24  VAL   B C   
4443 O  O   . VAL   B 24  ? 0.1583 0.1695 0.2165 -0.0204 -0.0086 0.0200  24  VAL   B O   
4444 C  CB  . VAL   B 24  ? 0.1730 0.1710 0.2133 -0.0004 -0.0224 -0.0012 24  VAL   B CB  
4445 C  CG1 . VAL   B 24  ? 0.1760 0.1729 0.2415 -0.0077 -0.0290 0.0032  24  VAL   B CG1 
4446 C  CG2 . VAL   B 24  ? 0.1811 0.1983 0.2054 0.0068  -0.0233 -0.0067 24  VAL   B CG2 
4456 N  N   . GLU   B 25  ? 0.1810 0.1703 0.2175 -0.0134 0.0016  -0.0010 25  GLU   B N   
4457 C  CA  . GLU   B 25  ? 0.1965 0.1936 0.2352 -0.0073 0.0121  -0.0030 25  GLU   B CA  
4458 C  C   . GLU   B 25  ? 0.1822 0.1827 0.1991 -0.0182 0.0185  -0.0015 25  GLU   B C   
4459 O  O   . GLU   B 25  ? 0.1808 0.1995 0.2141 -0.0129 0.0234  0.0085  25  GLU   B O   
4460 C  CB  . GLU   B 25  ? 0.2345 0.2439 0.3047 0.0158  0.0206  -0.0052 25  GLU   B CB  
4461 C  CG  . GLU   B 25  ? 0.2727 0.3020 0.4120 0.0290  0.0100  -0.0130 25  GLU   B CG  
4462 C  CD  . GLU   B 25  ? 0.3302 0.3558 0.4942 0.0259  -0.0016 -0.0140 25  GLU   B CD  
4463 O  OE1 . GLU   B 25  ? 0.3369 0.3753 0.5249 0.0289  0.0015  -0.0116 25  GLU   B OE1 
4464 O  OE2 . GLU   B 25  ? 0.3317 0.3744 0.5250 0.0257  -0.0084 -0.0187 25  GLU   B OE2 
4471 N  N   . GLU   B 26  ? 0.1822 0.1779 0.1735 -0.0278 0.0085  0.0021  26  GLU   B N   
4472 C  CA  . GLU   B 26  ? 0.1800 0.1953 0.1808 -0.0375 -0.0042 0.0071  26  GLU   B CA  
4473 C  C   . GLU   B 26  ? 0.1628 0.1898 0.1607 -0.0285 0.0030  0.0220  26  GLU   B C   
4474 O  O   . GLU   B 26  ? 0.1842 0.2116 0.1681 -0.0233 -0.0005 0.0216  26  GLU   B O   
4475 C  CB  . GLU   B 26  ? 0.2106 0.2186 0.2086 -0.0497 0.0009  0.0165  26  GLU   B CB  
4476 C  CG  . GLU   B 26  ? 0.2518 0.2594 0.2680 -0.0546 0.0154  -0.0113 26  GLU   B CG  
4477 C  CD  . GLU   B 26  ? 0.2759 0.2780 0.2826 -0.0770 0.0283  -0.0491 26  GLU   B CD  
4478 O  OE1 . GLU   B 26  ? 0.2986 0.2660 0.2940 -0.0895 0.0782  -0.0483 26  GLU   B OE1 
4479 O  OE2 . GLU   B 26  ? 0.2813 0.3140 0.3162 -0.0647 0.0180  -0.0477 26  GLU   B OE2 
4486 N  N   . ALA   B 27  ? 0.1534 0.1751 0.1597 -0.0264 0.0039  0.0210  27  ALA   B N   
4487 C  CA  . ALA   B 27  ? 0.1518 0.1679 0.1810 -0.0198 0.0011  0.0231  27  ALA   B CA  
4488 C  C   . ALA   B 27  ? 0.1559 0.1805 0.1968 -0.0127 0.0037  0.0387  27  ALA   B C   
4489 O  O   . ALA   B 27  ? 0.1662 0.1901 0.2044 -0.0004 0.0063  0.0409  27  ALA   B O   
4490 C  CB  . ALA   B 27  ? 0.1661 0.1529 0.1929 -0.0181 0.0094  0.0224  27  ALA   B CB  
4496 N  N   . LYS   B 28  ? 0.1515 0.2001 0.2399 -0.0215 0.0093  0.0600  28  LYS   B N   
4497 C  CA  . LYS   B 28  ? 0.1715 0.2377 0.2783 -0.0156 0.0477  0.0871  28  LYS   B CA  
4498 C  C   . LYS   B 28  ? 0.1944 0.2564 0.2666 -0.0071 0.0624  0.0815  28  LYS   B C   
4499 O  O   . LYS   B 28  ? 0.2235 0.2625 0.2787 -0.0053 0.0611  0.0779  28  LYS   B O   
4500 C  CB  . LYS   B 28  ? 0.2042 0.2734 0.3435 -0.0076 0.0781  0.1082  28  LYS   B CB  
4501 C  CG  . LYS   B 28  ? 0.2451 0.3266 0.3933 -0.0063 0.0961  0.1264  28  LYS   B CG  
4502 C  CD  . LYS   B 28  ? 0.3010 0.3840 0.4515 -0.0048 0.1164  0.1330  28  LYS   B CD  
4503 C  CE  . LYS   B 28  ? 0.3496 0.4259 0.4988 0.0004  0.1189  0.1361  28  LYS   B CE  
4504 N  NZ  . LYS   B 28  ? 0.4112 0.4577 0.5236 0.0043  0.1221  0.1403  28  LYS   B NZ  
4518 N  N   . LYS   B 29  ? 0.2064 0.2845 0.2674 0.0087  0.0669  0.0661  29  LYS   B N   
4519 C  CA  . LYS   B 29  ? 0.2536 0.3212 0.2900 0.0109  0.0655  0.0696  29  LYS   B CA  
4520 C  C   . LYS   B 29  ? 0.2496 0.3264 0.2445 0.0126  0.0512  0.0829  29  LYS   B C   
4521 O  O   . LYS   B 29  ? 0.2670 0.3483 0.2550 0.0201  0.0506  0.0936  29  LYS   B O   
4522 C  CB  . LYS   B 29  ? 0.3136 0.3589 0.3780 0.0106  0.0658  0.0550  29  LYS   B CB  
4523 C  CG  . LYS   B 29  ? 0.3683 0.3944 0.4717 0.0086  0.0721  0.0441  29  LYS   B CG  
4524 C  CD  . LYS   B 29  ? 0.4118 0.4222 0.5467 0.0057  0.0796  0.0306  29  LYS   B CD  
4525 C  CE  . LYS   B 29  ? 0.4383 0.4373 0.5972 0.0015  0.0853  0.0225  29  LYS   B CE  
4526 N  NZ  . LYS   B 29  ? 0.4507 0.4441 0.6256 -0.0003 0.0885  0.0181  29  LYS   B NZ  
4540 N  N   . VAL   B 30  ? 0.2175 0.3064 0.2242 0.0010  0.0363  0.0804  30  VAL   B N   
4541 C  CA  . VAL   B 30  ? 0.2035 0.2923 0.2559 -0.0117 0.0030  0.0818  30  VAL   B CA  
4542 C  C   . VAL   B 30  ? 0.1822 0.2855 0.2475 -0.0156 0.0085  0.1037  30  VAL   B C   
4543 O  O   . VAL   B 30  ? 0.1964 0.3003 0.2589 -0.0063 0.0094  0.1192  30  VAL   B O   
4544 C  CB  . VAL   B 30  ? 0.2021 0.2840 0.2963 -0.0265 -0.0266 0.0715  30  VAL   B CB  
4545 C  CG1 . VAL   B 30  ? 0.2109 0.2916 0.2943 -0.0232 -0.0241 0.0653  30  VAL   B CG1 
4546 C  CG2 . VAL   B 30  ? 0.2158 0.2828 0.3296 -0.0330 -0.0289 0.0538  30  VAL   B CG2 
4556 N  N   . LYS   B 31  ? 0.1733 0.2537 0.2848 -0.0328 0.0038  0.1119  31  LYS   B N   
4557 C  CA  . LYS   B 31  ? 0.1622 0.2433 0.3199 -0.0407 -0.0085 0.1166  31  LYS   B CA  
4558 C  C   . LYS   B 31  ? 0.1549 0.2039 0.2807 -0.0405 -0.0311 0.0940  31  LYS   B C   
4559 O  O   . LYS   B 31  ? 0.1643 0.2193 0.2972 -0.0324 -0.0228 0.1135  31  LYS   B O   
4560 C  CB  . LYS   B 31  ? 0.1773 0.2898 0.3865 -0.0358 0.0183  0.1258  31  LYS   B CB  
4561 C  CG  . LYS   B 31  ? 0.2159 0.3390 0.4396 -0.0359 0.0357  0.1112  31  LYS   B CG  
4562 C  CD  . LYS   B 31  ? 0.2528 0.3827 0.4829 -0.0310 0.0340  0.0947  31  LYS   B CD  
4563 C  CE  . LYS   B 31  ? 0.2753 0.4099 0.5221 -0.0297 0.0275  0.0816  31  LYS   B CE  
4564 N  NZ  . LYS   B 31  ? 0.2893 0.4197 0.5381 -0.0219 0.0184  0.0671  31  LYS   B NZ  
4578 N  N   . PRO   B 32  ? 0.1670 0.1657 0.2183 -0.0396 -0.0441 0.0540  32  PRO   B N   
4579 C  CA  . PRO   B 32  ? 0.1831 0.1618 0.1700 -0.0392 -0.0398 0.0320  32  PRO   B CA  
4580 C  C   . PRO   B 32  ? 0.1940 0.1527 0.1766 -0.0442 -0.0537 0.0362  32  PRO   B C   
4581 O  O   . PRO   B 32  ? 0.2044 0.1601 0.2088 -0.0495 -0.0759 0.0390  32  PRO   B O   
4582 C  CB  . PRO   B 32  ? 0.1964 0.1590 0.1588 -0.0409 -0.0308 0.0189  32  PRO   B CB  
4583 C  CG  . PRO   B 32  ? 0.2106 0.1454 0.1744 -0.0346 -0.0532 0.0301  32  PRO   B CG  
4584 C  CD  . PRO   B 32  ? 0.1949 0.1515 0.2052 -0.0326 -0.0632 0.0265  32  PRO   B CD  
4592 N  N   . THR   B 33  ? 0.1979 0.1429 0.1620 -0.0345 -0.0487 0.0214  33  THR   B N   
4593 C  CA  . THR   B 33  ? 0.2038 0.1465 0.1482 -0.0349 -0.0429 0.0300  33  THR   B CA  
4594 C  C   . THR   B 33  ? 0.1996 0.1354 0.1551 -0.0359 -0.0517 0.0214  33  THR   B C   
4595 O  O   . THR   B 33  ? 0.2288 0.1413 0.1588 -0.0469 -0.0595 0.0184  33  THR   B O   
4596 C  CB  . THR   B 33  ? 0.2155 0.1577 0.1567 -0.0225 -0.0547 0.0259  33  THR   B CB  
4597 O  OG1 . THR   B 33  ? 0.2033 0.1626 0.1662 -0.0280 -0.0489 0.0322  33  THR   B OG1 
4598 C  CG2 . THR   B 33  ? 0.2410 0.1630 0.1727 -0.0137 -0.0490 0.0226  33  THR   B CG2 
4606 N  N   . VAL   B 34  ? 0.1857 0.1334 0.1400 -0.0347 -0.0386 0.0183  34  VAL   B N   
4607 C  CA  . VAL   B 34  ? 0.1717 0.1366 0.1371 -0.0271 -0.0303 0.0135  34  VAL   B CA  
4608 C  C   . VAL   B 34  ? 0.1615 0.1351 0.1188 -0.0300 -0.0202 0.0158  34  VAL   B C   
4609 O  O   . VAL   B 34  ? 0.1716 0.1367 0.1318 -0.0295 -0.0301 0.0035  34  VAL   B O   
4610 C  CB  . VAL   B 34  ? 0.1737 0.1447 0.1613 -0.0091 -0.0367 0.0045  34  VAL   B CB  
4611 C  CG1 . VAL   B 34  ? 0.1723 0.1549 0.1694 -0.0079 -0.0176 -0.0041 34  VAL   B CG1 
4612 C  CG2 . VAL   B 34  ? 0.1782 0.1480 0.1915 -0.0091 -0.0338 0.0114  34  VAL   B CG2 
4622 N  N   . VAL   B 35  ? 0.1549 0.1290 0.1125 -0.0280 -0.0131 0.0117  35  VAL   B N   
4623 C  CA  . VAL   B 35  ? 0.1430 0.1262 0.1151 -0.0201 -0.0157 0.0089  35  VAL   B CA  
4624 C  C   . VAL   B 35  ? 0.1321 0.1241 0.1126 -0.0161 -0.0152 0.0042  35  VAL   B C   
4625 O  O   . VAL   B 35  ? 0.1386 0.1291 0.1246 -0.0252 -0.0040 -0.0019 35  VAL   B O   
4626 C  CB  . VAL   B 35  ? 0.1396 0.1411 0.1257 -0.0140 0.0059  0.0083  35  VAL   B CB  
4627 C  CG1 . VAL   B 35  ? 0.1373 0.1536 0.1449 -0.0236 0.0052  0.0040  35  VAL   B CG1 
4628 C  CG2 . VAL   B 35  ? 0.1423 0.1406 0.1379 -0.0116 -0.0015 -0.0016 35  VAL   B CG2 
4638 N  N   . VAL   B 36  ? 0.1339 0.1244 0.1161 -0.0182 -0.0183 0.0078  36  VAL   B N   
4639 C  CA  . VAL   B 36  ? 0.1352 0.1201 0.1084 -0.0097 -0.0081 0.0033  36  VAL   B CA  
4640 C  C   . VAL   B 36  ? 0.1282 0.1217 0.1083 -0.0099 -0.0046 0.0089  36  VAL   B C   
4641 O  O   . VAL   B 36  ? 0.1363 0.1309 0.1274 -0.0063 -0.0053 -0.0000 36  VAL   B O   
4642 C  CB  . VAL   B 36  ? 0.1368 0.1252 0.1260 -0.0126 -0.0025 0.0069  36  VAL   B CB  
4643 C  CG1 . VAL   B 36  ? 0.1337 0.1344 0.1387 -0.0157 0.0006  0.0009  36  VAL   B CG1 
4644 C  CG2 . VAL   B 36  ? 0.1438 0.1296 0.1385 -0.0161 -0.0096 0.0034  36  VAL   B CG2 
4654 N  N   . ASN   B 37  ? 0.1362 0.1263 0.1072 -0.0042 -0.0074 0.0025  37  ASN   B N   
4655 C  CA  . ASN   B 37  ? 0.1324 0.1273 0.1147 -0.0004 -0.0094 0.0086  37  ASN   B CA  
4656 C  C   . ASN   B 37  ? 0.1344 0.1276 0.1259 0.0072  -0.0123 0.0038  37  ASN   B C   
4657 O  O   . ASN   B 37  ? 0.1415 0.1328 0.1213 0.0006  -0.0037 0.0069  37  ASN   B O   
4658 C  CB  . ASN   B 37  ? 0.1291 0.1321 0.1258 -0.0050 -0.0072 0.0043  37  ASN   B CB  
4659 C  CG  . ASN   B 37  ? 0.1402 0.1346 0.1231 0.0019  -0.0120 0.0057  37  ASN   B CG  
4660 O  OD1 . ASN   B 37  ? 0.1440 0.1345 0.1437 0.0107  -0.0147 0.0044  37  ASN   B OD1 
4661 N  ND2 . ASN   B 37  ? 0.1423 0.1313 0.1237 0.0028  -0.0189 0.0060  37  ASN   B ND2 
4668 N  N   . ALA   B 38  ? 0.1438 0.1297 0.1196 0.0096  0.0047  0.0086  38  ALA   B N   
4669 C  CA  . ALA   B 38  ? 0.1483 0.1361 0.1204 0.0018  0.0039  0.0066  38  ALA   B CA  
4670 C  C   . ALA   B 38  ? 0.1450 0.1322 0.1175 0.0047  0.0040  0.0124  38  ALA   B C   
4671 O  O   . ALA   B 38  ? 0.1584 0.1374 0.1338 0.0069  0.0001  0.0095  38  ALA   B O   
4672 C  CB  . ALA   B 38  ? 0.1666 0.1421 0.1433 -0.0024 0.0061  0.0083  38  ALA   B CB  
4678 N  N   . ALA   B 39  ? 0.1451 0.1323 0.1180 0.0096  -0.0068 0.0061  39  ALA   B N   
4679 C  CA  . ALA   B 39  ? 0.1510 0.1351 0.1238 0.0114  -0.0096 0.0035  39  ALA   B CA  
4680 C  C   . ALA   B 39  ? 0.1613 0.1406 0.0869 0.0136  -0.0055 0.0079  39  ALA   B C   
4681 O  O   . ALA   B 39  ? 0.1610 0.1529 0.1359 -0.0023 -0.0076 0.0111  39  ALA   B O   
4682 C  CB  . ALA   B 39  ? 0.1522 0.1382 0.1405 0.0010  -0.0024 -0.0027 39  ALA   B CB  
4688 N  N   . ASN   B 40  ? 0.1668 0.1636 0.0994 0.0002  -0.0050 -0.0046 40  ASN   B N   
4689 C  CA  . ASN   B 40  ? 0.1723 0.1699 0.1170 0.0021  -0.0056 -0.0110 40  ASN   B CA  
4690 C  C   . ASN   B 40  ? 0.1755 0.1711 0.1002 0.0061  -0.0056 0.0014  40  ASN   B C   
4691 O  O   . ASN   B 40  ? 0.1696 0.1631 0.1089 0.0066  -0.0117 0.0016  40  ASN   B O   
4692 C  CB  . ASN   B 40  ? 0.1836 0.1660 0.1459 0.0128  -0.0134 0.0113  40  ASN   B CB  
4693 C  CG  . ASN   B 40  ? 0.1870 0.1720 0.1741 0.0049  -0.0200 0.0177  40  ASN   B CG  
4694 O  OD1 . ASN   B 40  ? 0.1819 0.1685 0.2631 0.0055  -0.0358 0.0198  40  ASN   B OD1 
4695 N  ND2 . ASN   B 40  ? 0.1867 0.1725 0.1820 0.0060  -0.0172 0.0226  40  ASN   B ND2 
4702 N  N   . VAL   B 41  ? 0.1846 0.1759 0.1056 0.0169  0.0008  0.0001  41  VAL   B N   
4703 C  CA  . VAL   B 41  ? 0.1857 0.1867 0.1158 0.0119  -0.0007 -0.0065 41  VAL   B CA  
4704 C  C   . VAL   B 41  ? 0.1856 0.1840 0.1128 0.0204  -0.0046 -0.0072 41  VAL   B C   
4705 O  O   . VAL   B 41  ? 0.1833 0.1839 0.1271 0.0170  -0.0112 -0.0133 41  VAL   B O   
4706 C  CB  . VAL   B 41  ? 0.2022 0.2003 0.1502 -0.0003 0.0172  -0.0180 41  VAL   B CB  
4707 C  CG1 . VAL   B 41  ? 0.2020 0.1960 0.1653 -0.0025 0.0258  -0.0258 41  VAL   B CG1 
4708 C  CG2 . VAL   B 41  ? 0.2146 0.2209 0.1525 -0.0078 0.0168  -0.0156 41  VAL   B CG2 
4718 N  N   . TYR   B 42  ? 0.1895 0.1853 0.1185 0.0194  -0.0195 0.0023  42  TYR   B N   
4719 C  CA  . TYR   B 42  ? 0.1987 0.1914 0.1179 0.0158  -0.0252 -0.0095 42  TYR   B CA  
4720 C  C   . TYR   B 42  ? 0.1825 0.1722 0.1354 0.0228  -0.0257 -0.0078 42  TYR   B C   
4721 O  O   . TYR   B 42  ? 0.1865 0.1746 0.1706 0.0159  -0.0306 -0.0180 42  TYR   B O   
4722 C  CB  . TYR   B 42  ? 0.2188 0.2181 0.1448 0.0107  -0.0350 0.0024  42  TYR   B CB  
4723 C  CG  . TYR   B 42  ? 0.2177 0.2334 0.1348 -0.0004 -0.0323 0.0151  42  TYR   B CG  
4724 C  CD1 . TYR   B 42  ? 0.2089 0.2315 0.1213 -0.0037 -0.0165 0.0078  42  TYR   B CD1 
4725 C  CD2 . TYR   B 42  ? 0.2320 0.2464 0.1815 0.0028  -0.0187 0.0184  42  TYR   B CD2 
4726 C  CE1 . TYR   B 42  ? 0.2230 0.2520 0.1250 0.0032  -0.0079 0.0009  42  TYR   B CE1 
4727 C  CE2 . TYR   B 42  ? 0.2379 0.2615 0.1711 0.0065  0.0108  0.0308  42  TYR   B CE2 
4728 C  CZ  . TYR   B 42  ? 0.2481 0.2705 0.1447 0.0183  0.0159  0.0121  42  TYR   B CZ  
4729 O  OH  . TYR   B 42  ? 0.2861 0.3000 0.1964 0.0338  0.0271  0.0222  42  TYR   B OH  
4739 N  N   . LEU   B 43  ? 0.1721 0.1591 0.1192 0.0095  -0.0172 -0.0083 43  LEU   B N   
4740 C  CA  . LEU   B 43  ? 0.1662 0.1539 0.1177 0.0058  -0.0167 -0.0034 43  LEU   B CA  
4741 C  C   . LEU   B 43  ? 0.1713 0.1552 0.1181 0.0049  -0.0204 -0.0074 43  LEU   B C   
4742 O  O   . LEU   B 43  ? 0.1653 0.1583 0.1508 0.0044  -0.0293 0.0024  43  LEU   B O   
4743 C  CB  . LEU   B 43  ? 0.1606 0.1455 0.1431 0.0017  -0.0240 -0.0090 43  LEU   B CB  
4744 C  CG  . LEU   B 43  ? 0.1668 0.1423 0.1446 0.0040  -0.0253 -0.0109 43  LEU   B CG  
4745 C  CD1 . LEU   B 43  ? 0.1770 0.1503 0.1906 0.0061  -0.0416 -0.0101 43  LEU   B CD1 
4746 C  CD2 . LEU   B 43  ? 0.1614 0.1468 0.1490 -0.0028 -0.0269 -0.0085 43  LEU   B CD2 
4758 N  N   . LYS   B 44  ? 0.1709 0.1545 0.1231 0.0089  -0.0114 -0.0038 44  LYS   B N   
4759 C  CA  . LYS   B 44  ? 0.1839 0.1664 0.1299 0.0127  -0.0113 0.0113  44  LYS   B CA  
4760 C  C   . LYS   B 44  ? 0.1729 0.1594 0.1322 0.0190  -0.0170 0.0049  44  LYS   B C   
4761 O  O   . LYS   B 44  ? 0.1878 0.1594 0.1668 0.0075  -0.0002 0.0000  44  LYS   B O   
4762 C  CB  . LYS   B 44  ? 0.2086 0.1781 0.1507 0.0235  -0.0302 0.0043  44  LYS   B CB  
4763 C  CG  . LYS   B 44  ? 0.2498 0.2077 0.1872 0.0192  -0.0566 0.0099  44  LYS   B CG  
4764 C  CD  . LYS   B 44  ? 0.2861 0.2317 0.2621 0.0035  -0.0657 0.0003  44  LYS   B CD  
4765 C  CE  . LYS   B 44  ? 0.3155 0.2598 0.3169 -0.0064 -0.0696 0.0055  44  LYS   B CE  
4766 N  NZ  . LYS   B 44  ? 0.3291 0.2715 0.3488 -0.0064 -0.0725 0.0197  44  LYS   B NZ  
4780 N  N   . HIS   B 45  ? 0.1644 0.1612 0.1301 0.0136  -0.0135 0.0064  45  HIS   B N   
4781 C  CA  . HIS   B 45  ? 0.1684 0.1576 0.1317 0.0144  -0.0118 -0.0027 45  HIS   B CA  
4782 C  C   . HIS   B 45  ? 0.1913 0.1776 0.1717 0.0175  -0.0263 -0.0059 45  HIS   B C   
4783 O  O   . HIS   B 45  ? 0.2042 0.2080 0.2151 0.0480  0.0002  -0.0022 45  HIS   B O   
4784 C  CB  . HIS   B 45  ? 0.1610 0.1623 0.1416 0.0033  -0.0103 -0.0038 45  HIS   B CB  
4785 C  CG  . HIS   B 45  ? 0.1616 0.1563 0.1376 -0.0068 -0.0151 -0.0016 45  HIS   B CG  
4786 N  ND1 . HIS   B 45  ? 0.1615 0.1466 0.1370 -0.0026 -0.0221 -0.0049 45  HIS   B ND1 
4787 C  CD2 . HIS   B 45  ? 0.1724 0.1578 0.1591 -0.0109 -0.0274 -0.0013 45  HIS   B CD2 
4788 C  CE1 . HIS   B 45  ? 0.1715 0.1357 0.1400 -0.0001 -0.0284 -0.0061 45  HIS   B CE1 
4789 N  NE2 . HIS   B 45  ? 0.1759 0.1427 0.1440 -0.0026 -0.0220 -0.0056 45  HIS   B NE2 
4797 N  N   A GLY   B 46  ? 0.2021 0.1740 0.2003 0.0165  -0.0428 0.0045  46  GLY   B N   
4798 N  N   B GLY   B 46  ? 0.2024 0.1815 0.1942 0.0170  -0.0372 0.0067  46  GLY   B N   
4799 C  CA  A GLY   B 46  ? 0.2138 0.1787 0.2508 0.0143  -0.0511 0.0080  46  GLY   B CA  
4800 C  CA  B GLY   B 46  ? 0.2136 0.1898 0.2272 0.0141  -0.0455 0.0148  46  GLY   B CA  
4801 C  C   A GLY   B 46  ? 0.2168 0.1883 0.2935 0.0210  -0.0414 0.0031  46  GLY   B C   
4802 C  C   B GLY   B 46  ? 0.2189 0.2002 0.2573 0.0156  -0.0390 0.0168  46  GLY   B C   
4803 O  O   A GLY   B 46  ? 0.2266 0.1931 0.3700 0.0344  -0.0215 -0.0152 46  GLY   B O   
4804 O  O   B GLY   B 46  ? 0.2290 0.2128 0.2804 0.0202  -0.0305 0.0271  46  GLY   B O   
4811 N  N   . GLY   B 47  ? 0.2153 0.2033 0.2630 0.0070  -0.0248 -0.0033 47  GLY   B N   
4812 C  CA  . GLY   B 47  ? 0.2013 0.1822 0.2155 0.0049  -0.0178 -0.0057 47  GLY   B CA  
4813 C  C   . GLY   B 47  ? 0.1742 0.1645 0.1810 0.0095  0.0031  0.0018  47  GLY   B C   
4814 O  O   . GLY   B 47  ? 0.1832 0.1538 0.1892 0.0075  -0.0062 0.0099  47  GLY   B O   
4819 N  N   . GLY   B 48  ? 0.1586 0.1511 0.1755 0.0079  -0.0111 0.0147  48  GLY   B N   
4820 C  CA  . GLY   B 48  ? 0.1611 0.1479 0.1810 0.0001  -0.0068 0.0027  48  GLY   B CA  
4821 C  C   . GLY   B 48  ? 0.1517 0.1402 0.1602 -0.0012 0.0042  0.0046  48  GLY   B C   
4822 O  O   . GLY   B 48  ? 0.1440 0.1471 0.1844 0.0048  -0.0114 0.0057  48  GLY   B O   
4826 N  N   . VAL   B 49  ? 0.1549 0.1437 0.1597 0.0112  -0.0016 0.0039  49  VAL   B N   
4827 C  CA  . VAL   B 49  ? 0.1526 0.1559 0.1498 0.0131  -0.0120 -0.0072 49  VAL   B CA  
4828 C  C   . VAL   B 49  ? 0.1421 0.1476 0.1346 0.0121  -0.0088 0.0050  49  VAL   B C   
4829 O  O   . VAL   B 49  ? 0.1504 0.1520 0.1500 0.0060  0.0009  0.0061  49  VAL   B O   
4830 C  CB  . VAL   B 49  ? 0.1597 0.1702 0.1746 0.0058  -0.0280 -0.0011 49  VAL   B CB  
4831 C  CG1 . VAL   B 49  ? 0.1585 0.1763 0.1635 0.0125  -0.0293 0.0008  49  VAL   B CG1 
4832 C  CG2 . VAL   B 49  ? 0.1733 0.1849 0.2006 -0.0064 -0.0384 -0.0005 49  VAL   B CG2 
4842 N  N   . ALA   B 50  ? 0.1368 0.1457 0.1387 0.0067  -0.0028 0.0063  50  ALA   B N   
4843 C  CA  . ALA   B 50  ? 0.1407 0.1363 0.1421 0.0068  -0.0077 0.0010  50  ALA   B CA  
4844 C  C   . ALA   B 50  ? 0.1451 0.1386 0.1367 0.0052  -0.0056 -0.0037 50  ALA   B C   
4845 O  O   . ALA   B 50  ? 0.1481 0.1433 0.1317 0.0045  -0.0065 -0.0048 50  ALA   B O   
4846 C  CB  . ALA   B 50  ? 0.1478 0.1405 0.1499 0.0028  -0.0010 0.0064  50  ALA   B CB  
4852 N  N   . GLY   B 51  ? 0.1413 0.1509 0.1450 0.0110  -0.0102 0.0096  51  GLY   B N   
4853 C  CA  . GLY   B 51  ? 0.1456 0.1598 0.1637 0.0217  -0.0142 0.0054  51  GLY   B CA  
4854 C  C   . GLY   B 51  ? 0.1421 0.1536 0.1679 0.0197  -0.0126 0.0062  51  GLY   B C   
4855 O  O   . GLY   B 51  ? 0.1463 0.1694 0.1854 0.0088  -0.0139 0.0017  51  GLY   B O   
4859 N  N   . ALA   B 52  ? 0.1477 0.1457 0.1553 0.0207  -0.0052 0.0100  52  ALA   B N   
4860 C  CA  . ALA   B 52  ? 0.1559 0.1509 0.1522 0.0174  0.0045  -0.0059 52  ALA   B CA  
4861 C  C   . ALA   B 52  ? 0.1434 0.1465 0.1456 0.0062  0.0018  0.0032  52  ALA   B C   
4862 O  O   . ALA   B 52  ? 0.1472 0.1550 0.1644 0.0103  0.0008  0.0055  52  ALA   B O   
4863 C  CB  . ALA   B 52  ? 0.1725 0.1578 0.1655 0.0083  0.0113  -0.0000 52  ALA   B CB  
4869 N  N   . LEU   B 53  ? 0.1360 0.1475 0.1467 0.0182  -0.0055 0.0056  53  LEU   B N   
4870 C  CA  . LEU   B 53  ? 0.1397 0.1584 0.1387 0.0120  -0.0058 0.0030  53  LEU   B CA  
4871 C  C   . LEU   B 53  ? 0.1422 0.1528 0.1453 0.0121  0.0078  0.0042  53  LEU   B C   
4872 O  O   . LEU   B 53  ? 0.1496 0.1570 0.1625 0.0001  0.0032  0.0072  53  LEU   B O   
4873 C  CB  . LEU   B 53  ? 0.1448 0.1624 0.1466 0.0045  -0.0018 0.0140  53  LEU   B CB  
4874 C  CG  . LEU   B 53  ? 0.1436 0.1713 0.1505 0.0006  0.0001  0.0237  53  LEU   B CG  
4875 C  CD1 . LEU   B 53  ? 0.1497 0.1889 0.1751 0.0120  0.0004  0.0077  53  LEU   B CD1 
4876 C  CD2 . LEU   B 53  ? 0.1551 0.2042 0.1743 -0.0118 -0.0044 -0.0068 53  LEU   B CD2 
4888 N  N   . ASN   B 54  ? 0.1435 0.1446 0.1388 0.0036  -0.0019 0.0088  54  ASN   B N   
4889 C  CA  . ASN   B 54  ? 0.1485 0.1549 0.1532 0.0050  -0.0033 0.0009  54  ASN   B CA  
4890 C  C   . ASN   B 54  ? 0.1439 0.1575 0.1661 0.0044  0.0052  0.0026  54  ASN   B C   
4891 O  O   . ASN   B 54  ? 0.1380 0.1635 0.1803 -0.0032 0.0019  -0.0030 54  ASN   B O   
4892 C  CB  . ASN   B 54  ? 0.1538 0.1678 0.1625 0.0080  0.0024  0.0053  54  ASN   B CB  
4893 C  CG  . ASN   B 54  ? 0.1602 0.1716 0.1617 0.0071  -0.0056 0.0026  54  ASN   B CG  
4894 O  OD1 . ASN   B 54  ? 0.1484 0.1658 0.1765 0.0026  -0.0123 -0.0138 54  ASN   B OD1 
4895 N  ND2 . ASN   B 54  ? 0.1755 0.1847 0.1782 -0.0021 -0.0344 0.0142  54  ASN   B ND2 
4902 N  N   . LYS   B 55  ? 0.1462 0.1614 0.1763 0.0147  -0.0012 0.0020  55  LYS   B N   
4903 C  CA  . LYS   B 55  ? 0.1525 0.1748 0.2000 0.0165  -0.0049 0.0051  55  LYS   B CA  
4904 C  C   . LYS   B 55  ? 0.1454 0.1735 0.1943 0.0139  0.0044  -0.0021 55  LYS   B C   
4905 O  O   . LYS   B 55  ? 0.1416 0.1836 0.2030 0.0144  0.0017  -0.0048 55  LYS   B O   
4906 C  CB  . LYS   B 55  ? 0.1646 0.1837 0.2356 0.0323  0.0045  0.0211  55  LYS   B CB  
4907 C  CG  . LYS   B 55  ? 0.2037 0.2110 0.3190 0.0377  0.0207  0.0257  55  LYS   B CG  
4908 C  CD  . LYS   B 55  ? 0.2346 0.2368 0.3885 0.0466  0.0347  0.0318  55  LYS   B CD  
4909 C  CE  . LYS   B 55  ? 0.2630 0.2599 0.4543 0.0428  0.0516  0.0316  55  LYS   B CE  
4910 N  NZ  . LYS   B 55  ? 0.2749 0.2762 0.4877 0.0421  0.0381  0.0415  55  LYS   B NZ  
4924 N  N   . ALA   B 56  ? 0.1407 0.1744 0.1756 0.0128  0.0033  -0.0104 56  ALA   B N   
4925 C  CA  . ALA   B 56  ? 0.1583 0.1897 0.1757 0.0006  0.0043  -0.0125 56  ALA   B CA  
4926 C  C   . ALA   B 56  ? 0.1560 0.1854 0.1692 0.0014  0.0134  0.0008  56  ALA   B C   
4927 O  O   . ALA   B 56  ? 0.1707 0.2001 0.1825 0.0060  0.0307  0.0037  56  ALA   B O   
4928 C  CB  . ALA   B 56  ? 0.1711 0.2110 0.1848 -0.0162 -0.0029 -0.0060 56  ALA   B CB  
4934 N  N   . THR   B 57  ? 0.1523 0.1735 0.1787 -0.0006 0.0223  0.0022  57  THR   B N   
4935 C  CA  . THR   B 57  ? 0.1583 0.1749 0.1804 -0.0029 0.0218  0.0047  57  THR   B CA  
4936 C  C   . THR   B 57  ? 0.1572 0.1852 0.1967 -0.0035 0.0235  0.0064  57  THR   B C   
4937 O  O   . THR   B 57  ? 0.1679 0.1854 0.1990 -0.0172 0.0200  0.0016  57  THR   B O   
4938 C  CB  . THR   B 57  ? 0.1665 0.1593 0.1539 -0.0040 0.0118  0.0077  57  THR   B CB  
4939 O  OG1 . THR   B 57  ? 0.1637 0.1596 0.1764 -0.0045 0.0128  0.0028  57  THR   B OG1 
4940 C  CG2 . THR   B 57  ? 0.1635 0.1686 0.1575 -0.0037 0.0117  0.0055  57  THR   B CG2 
4948 N  N   . ASN   B 58  ? 0.1459 0.2067 0.2163 -0.0147 0.0047  -0.0138 58  ASN   B N   
4949 C  CA  . ASN   B 58  ? 0.1744 0.2553 0.2650 -0.0285 0.0264  -0.0033 58  ASN   B CA  
4950 C  C   . ASN   B 58  ? 0.1502 0.2281 0.2187 -0.0205 -0.0015 -0.0017 58  ASN   B C   
4951 O  O   . ASN   B 58  ? 0.1518 0.2364 0.2354 -0.0221 0.0029  -0.0151 58  ASN   B O   
4952 C  CB  . ASN   B 58  ? 0.2731 0.3348 0.3888 -0.0446 0.0609  0.0073  58  ASN   B CB  
4953 C  CG  . ASN   B 58  ? 0.3882 0.4187 0.5326 -0.0493 0.0779  0.0248  58  ASN   B CG  
4954 O  OD1 . ASN   B 58  ? 0.4031 0.4362 0.5837 -0.0496 0.0795  0.0297  58  ASN   B OD1 
4955 N  ND2 . ASN   B 58  ? 0.4985 0.4985 0.5844 -0.0541 0.0857  0.0304  58  ASN   B ND2 
4962 N  N   . ASN   B 59  ? 0.1517 0.2079 0.1924 -0.0123 -0.0136 0.0048  59  ASN   B N   
4963 C  CA  . ASN   B 59  ? 0.1563 0.2072 0.1803 -0.0109 -0.0197 0.0071  59  ASN   B CA  
4964 C  C   . ASN   B 59  ? 0.1501 0.1963 0.1758 -0.0140 -0.0157 -0.0079 59  ASN   B C   
4965 O  O   . ASN   B 59  ? 0.1523 0.1973 0.1873 -0.0152 -0.0115 -0.0070 59  ASN   B O   
4966 C  CB  . ASN   B 59  ? 0.1632 0.2256 0.2029 -0.0044 -0.0249 0.0128  59  ASN   B CB  
4967 C  CG  . ASN   B 59  ? 0.1705 0.2394 0.2149 -0.0036 -0.0381 0.0124  59  ASN   B CG  
4968 O  OD1 . ASN   B 59  ? 0.1718 0.2406 0.2252 -0.0038 -0.0213 0.0272  59  ASN   B OD1 
4969 N  ND2 . ASN   B 59  ? 0.1810 0.2480 0.2240 -0.0122 -0.0440 0.0050  59  ASN   B ND2 
4976 N  N   . ALA   B 60  ? 0.1487 0.1886 0.1736 -0.0142 -0.0059 -0.0101 60  ALA   B N   
4977 C  CA  . ALA   B 60  ? 0.1574 0.1765 0.1873 -0.0180 0.0022  0.0067  60  ALA   B CA  
4978 C  C   . ALA   B 60  ? 0.1564 0.1624 0.1609 -0.0146 -0.0037 0.0026  60  ALA   B C   
4979 O  O   . ALA   B 60  ? 0.1606 0.1652 0.1785 -0.0163 0.0046  -0.0097 60  ALA   B O   
4980 C  CB  . ALA   B 60  ? 0.1698 0.1719 0.2093 -0.0189 0.0098  0.0097  60  ALA   B CB  
4986 N  N   . MET   B 61  ? 0.1454 0.1548 0.1678 -0.0114 -0.0002 0.0025  61  MET   B N   
4987 C  CA  . MET   B 61  ? 0.1435 0.1498 0.1586 -0.0051 -0.0043 -0.0044 61  MET   B CA  
4988 C  C   . MET   B 61  ? 0.1549 0.1385 0.1567 -0.0117 -0.0094 0.0047  61  MET   B C   
4989 O  O   . MET   B 61  ? 0.1522 0.1487 0.1411 -0.0003 -0.0119 -0.0106 61  MET   B O   
4990 C  CB  . MET   B 61  ? 0.1387 0.1533 0.1543 -0.0003 -0.0086 -0.0085 61  MET   B CB  
4991 C  CG  . MET   B 61  ? 0.1457 0.1482 0.1355 0.0005  -0.0050 0.0011  61  MET   B CG  
4992 S  SD  . MET   B 61  ? 0.1433 0.1512 0.1674 -0.0037 -0.0054 -0.0098 61  MET   B SD  
4993 C  CE  . MET   B 61  ? 0.1521 0.1810 0.1761 -0.0031 -0.0024 -0.0245 61  MET   B CE  
5003 N  N   . GLN   B 62  ? 0.1510 0.1508 0.1524 -0.0075 -0.0138 0.0032  62  GLN   B N   
5004 C  CA  . GLN   B 62  ? 0.1551 0.1603 0.1528 -0.0027 -0.0146 -0.0030 62  GLN   B CA  
5005 C  C   . GLN   B 62  ? 0.1523 0.1608 0.1592 -0.0057 -0.0236 -0.0127 62  GLN   B C   
5006 O  O   . GLN   B 62  ? 0.1684 0.1628 0.1629 -0.0024 -0.0339 -0.0202 62  GLN   B O   
5007 C  CB  . GLN   B 62  ? 0.1590 0.1625 0.1573 -0.0016 -0.0162 0.0019  62  GLN   B CB  
5008 C  CG  . GLN   B 62  ? 0.1620 0.1669 0.1597 -0.0011 -0.0213 -0.0051 62  GLN   B CG  
5009 C  CD  . GLN   B 62  ? 0.1641 0.1651 0.1459 0.0049  -0.0282 0.0051  62  GLN   B CD  
5010 O  OE1 . GLN   B 62  ? 0.1667 0.1607 0.1617 -0.0003 -0.0272 -0.0029 62  GLN   B OE1 
5011 N  NE2 . GLN   B 62  ? 0.1683 0.1699 0.1427 0.0023  -0.0256 -0.0068 62  GLN   B NE2 
5020 N  N   . VAL   B 63  ? 0.1566 0.1672 0.1712 -0.0110 -0.0237 -0.0148 63  VAL   B N   
5021 C  CA  . VAL   B 63  ? 0.1682 0.1735 0.1965 -0.0143 -0.0333 -0.0099 63  VAL   B CA  
5022 C  C   . VAL   B 63  ? 0.1693 0.1596 0.1721 -0.0202 -0.0358 -0.0161 63  VAL   B C   
5023 O  O   . VAL   B 63  ? 0.1820 0.1584 0.1900 -0.0165 -0.0454 -0.0146 63  VAL   B O   
5024 C  CB  . VAL   B 63  ? 0.1633 0.1938 0.2314 -0.0232 -0.0299 -0.0177 63  VAL   B CB  
5025 C  CG1 . VAL   B 63  ? 0.1729 0.1986 0.2445 -0.0282 -0.0158 -0.0206 63  VAL   B CG1 
5026 C  CG2 . VAL   B 63  ? 0.1560 0.2142 0.2439 -0.0164 -0.0326 -0.0200 63  VAL   B CG2 
5036 N  N   . GLU   B 64  ? 0.1667 0.1551 0.1602 -0.0118 -0.0293 -0.0070 64  GLU   B N   
5037 C  CA  . GLU   B 64  ? 0.1693 0.1459 0.1520 -0.0100 -0.0238 -0.0034 64  GLU   B CA  
5038 C  C   . GLU   B 64  ? 0.1629 0.1418 0.1540 -0.0039 -0.0294 -0.0113 64  GLU   B C   
5039 O  O   . GLU   B 64  ? 0.1726 0.1514 0.1545 -0.0098 -0.0275 -0.0152 64  GLU   B O   
5040 C  CB  . GLU   B 64  ? 0.1642 0.1535 0.1532 -0.0139 -0.0157 -0.0051 64  GLU   B CB  
5041 C  CG  . GLU   B 64  ? 0.1715 0.1590 0.1551 -0.0240 -0.0255 -0.0165 64  GLU   B CG  
5042 C  CD  . GLU   B 64  ? 0.1772 0.1717 0.1636 -0.0276 -0.0277 -0.0123 64  GLU   B CD  
5043 O  OE1 . GLU   B 64  ? 0.1819 0.1848 0.1784 -0.0343 -0.0174 -0.0271 64  GLU   B OE1 
5044 O  OE2 . GLU   B 64  ? 0.1884 0.1831 0.1710 -0.0359 -0.0400 -0.0061 64  GLU   B OE2 
5051 N  N   . SER   B 65  ? 0.1656 0.1408 0.1452 -0.0075 -0.0167 -0.0186 65  SER   B N   
5052 C  CA  . SER   B 65  ? 0.1609 0.1430 0.1509 -0.0009 -0.0205 -0.0158 65  SER   B CA  
5053 C  C   . SER   B 65  ? 0.1640 0.1475 0.1491 0.0041  -0.0297 -0.0178 65  SER   B C   
5054 O  O   . SER   B 65  ? 0.1658 0.1548 0.1470 0.0014  -0.0260 -0.0216 65  SER   B O   
5055 C  CB  . SER   B 65  ? 0.1583 0.1523 0.1520 -0.0057 -0.0203 -0.0143 65  SER   B CB  
5056 O  OG  . SER   B 65  ? 0.1631 0.1489 0.1482 -0.0094 -0.0187 -0.0245 65  SER   B OG  
5062 N  N   . ASP   B 66  ? 0.1731 0.1564 0.1420 -0.0002 -0.0287 -0.0182 66  ASP   B N   
5063 C  CA  . ASP   B 66  ? 0.1764 0.1634 0.1383 0.0037  -0.0398 -0.0084 66  ASP   B CA  
5064 C  C   . ASP   B 66  ? 0.1817 0.1654 0.1462 -0.0048 -0.0242 -0.0170 66  ASP   B C   
5065 O  O   . ASP   B 66  ? 0.1844 0.1714 0.1618 0.0071  -0.0273 -0.0266 66  ASP   B O   
5066 C  CB  . ASP   B 66  ? 0.1936 0.1753 0.1569 0.0138  -0.0503 -0.0198 66  ASP   B CB  
5067 C  CG  . ASP   B 66  ? 0.2205 0.1871 0.1893 0.0234  -0.0581 -0.0085 66  ASP   B CG  
5068 O  OD1 . ASP   B 66  ? 0.2421 0.1843 0.1997 0.0139  -0.0558 0.0028  66  ASP   B OD1 
5069 O  OD2 . ASP   B 66  ? 0.2401 0.2067 0.2548 0.0436  -0.0541 -0.0146 66  ASP   B OD2 
5074 N  N   . ASP   B 67  ? 0.1725 0.1593 0.1420 -0.0087 -0.0267 -0.0228 67  ASP   B N   
5075 C  CA  . ASP   B 67  ? 0.1875 0.1578 0.1489 -0.0070 -0.0293 -0.0110 67  ASP   B CA  
5076 C  C   . ASP   B 67  ? 0.1855 0.1608 0.1571 -0.0005 -0.0265 -0.0124 67  ASP   B C   
5077 O  O   . ASP   B 67  ? 0.1856 0.1664 0.1733 -0.0013 -0.0168 -0.0245 67  ASP   B O   
5078 C  CB  . ASP   B 67  ? 0.2109 0.1637 0.1786 -0.0155 -0.0427 -0.0131 67  ASP   B CB  
5079 C  CG  . ASP   B 67  ? 0.2502 0.1741 0.1952 -0.0147 -0.0639 -0.0145 67  ASP   B CG  
5080 O  OD1 . ASP   B 67  ? 0.2729 0.1734 0.2157 -0.0158 -0.0660 -0.0128 67  ASP   B OD1 
5081 O  OD2 . ASP   B 67  ? 0.2666 0.1815 0.2037 -0.0034 -0.0734 -0.0059 67  ASP   B OD2 
5086 N  N   . TYR   B 68  ? 0.1799 0.1622 0.1530 0.0052  -0.0387 -0.0235 68  TYR   B N   
5087 C  CA  . TYR   B 68  ? 0.1752 0.1755 0.1722 0.0103  -0.0392 -0.0312 68  TYR   B CA  
5088 C  C   . TYR   B 68  ? 0.1662 0.1733 0.1658 0.0087  -0.0384 -0.0369 68  TYR   B C   
5089 O  O   . TYR   B 68  ? 0.1749 0.1799 0.1789 0.0094  -0.0366 -0.0510 68  TYR   B O   
5090 C  CB  . TYR   B 68  ? 0.1783 0.1891 0.1776 0.0159  -0.0430 -0.0387 68  TYR   B CB  
5091 C  CG  . TYR   B 68  ? 0.1932 0.2075 0.1770 0.0204  -0.0353 -0.0647 68  TYR   B CG  
5092 C  CD1 . TYR   B 68  ? 0.1980 0.2160 0.2032 0.0034  -0.0342 -0.0706 68  TYR   B CD1 
5093 C  CD2 . TYR   B 68  ? 0.1959 0.2261 0.1982 0.0251  -0.0489 -0.0500 68  TYR   B CD2 
5094 C  CE1 . TYR   B 68  ? 0.2015 0.2287 0.2196 0.0038  -0.0290 -0.0663 68  TYR   B CE1 
5095 C  CE2 . TYR   B 68  ? 0.1982 0.2317 0.2049 0.0221  -0.0371 -0.0687 68  TYR   B CE2 
5096 C  CZ  . TYR   B 68  ? 0.1942 0.2300 0.2179 0.0130  -0.0324 -0.0698 68  TYR   B CZ  
5097 O  OH  . TYR   B 68  ? 0.1906 0.2466 0.2492 0.0101  -0.0277 -0.0389 68  TYR   B OH  
5107 N  N   . ILE   B 69  ? 0.1667 0.1658 0.1611 0.0070  -0.0363 -0.0315 69  ILE   B N   
5108 C  CA  . ILE   B 69  ? 0.1759 0.1704 0.1642 0.0041  -0.0260 -0.0355 69  ILE   B CA  
5109 C  C   . ILE   B 69  ? 0.1758 0.1670 0.1611 0.0092  -0.0331 -0.0386 69  ILE   B C   
5110 O  O   . ILE   B 69  ? 0.1788 0.1745 0.1624 0.0116  -0.0203 -0.0358 69  ILE   B O   
5111 C  CB  . ILE   B 69  ? 0.1867 0.1735 0.1747 -0.0000 -0.0004 -0.0390 69  ILE   B CB  
5112 C  CG1 . ILE   B 69  ? 0.1900 0.1746 0.2020 -0.0070 0.0054  -0.0356 69  ILE   B CG1 
5113 C  CG2 . ILE   B 69  ? 0.2015 0.1797 0.1875 0.0037  0.0002  -0.0249 69  ILE   B CG2 
5114 C  CD1 . ILE   B 69  ? 0.1827 0.1801 0.2170 -0.0211 0.0082  -0.0416 69  ILE   B CD1 
5126 N  N   . ALA   B 70  ? 0.1743 0.1672 0.1653 0.0102  -0.0413 -0.0255 70  ALA   B N   
5127 C  CA  . ALA   B 70  ? 0.1819 0.1700 0.1582 0.0032  -0.0448 -0.0262 70  ALA   B CA  
5128 C  C   . ALA   B 70  ? 0.1837 0.1655 0.1848 -0.0024 -0.0402 -0.0343 70  ALA   B C   
5129 O  O   . ALA   B 70  ? 0.1884 0.1686 0.1888 0.0045  -0.0435 -0.0444 70  ALA   B O   
5130 C  CB  . ALA   B 70  ? 0.1875 0.1834 0.1554 -0.0004 -0.0418 -0.0308 70  ALA   B CB  
5136 N  N   . THR   B 71  ? 0.1939 0.1684 0.1865 0.0051  -0.0508 -0.0302 71  THR   B N   
5137 C  CA  . THR   B 71  ? 0.2104 0.1721 0.1945 0.0090  -0.0679 -0.0337 71  THR   B CA  
5138 C  C   . THR   B 71  ? 0.2044 0.1753 0.2255 0.0303  -0.0637 -0.0566 71  THR   B C   
5139 O  O   . THR   B 71  ? 0.2123 0.1782 0.2699 0.0369  -0.0566 -0.0654 71  THR   B O   
5140 C  CB  . THR   B 71  ? 0.2317 0.1884 0.2250 0.0009  -0.0754 -0.0150 71  THR   B CB  
5141 O  OG1 . THR   B 71  ? 0.2468 0.2110 0.2627 -0.0153 -0.0643 0.0080  71  THR   B OG1 
5142 C  CG2 . THR   B 71  ? 0.2541 0.1910 0.2603 0.0070  -0.0669 -0.0038 71  THR   B CG2 
5150 N  N   . ASN   B 72  ? 0.1883 0.1794 0.2267 0.0242  -0.0637 -0.0718 72  ASN   B N   
5151 C  CA  . ASN   B 72  ? 0.1895 0.1943 0.2288 0.0184  -0.0541 -0.0801 72  ASN   B CA  
5152 C  C   . ASN   B 72  ? 0.1865 0.2082 0.2278 0.0058  -0.0298 -0.0747 72  ASN   B C   
5153 O  O   . ASN   B 72  ? 0.1883 0.2256 0.2676 0.0107  -0.0097 -0.0808 72  ASN   B O   
5154 C  CB  . ASN   B 72  ? 0.1955 0.2086 0.2438 0.0150  -0.0618 -0.0679 72  ASN   B CB  
5155 C  CG  . ASN   B 72  ? 0.2091 0.2237 0.2441 0.0331  -0.0589 -0.0455 72  ASN   B CG  
5156 O  OD1 . ASN   B 72  ? 0.2307 0.2397 0.2428 0.0237  -0.0423 -0.0479 72  ASN   B OD1 
5157 N  ND2 . ASN   B 72  ? 0.2204 0.2331 0.2874 0.0524  -0.0476 -0.0101 72  ASN   B ND2 
5164 N  N   . GLY   B 73  ? 0.1890 0.2025 0.2063 -0.0015 -0.0303 -0.0683 73  GLY   B N   
5165 C  CA  . GLY   B 73  ? 0.1840 0.2083 0.1796 -0.0070 -0.0206 -0.0597 73  GLY   B CA  
5166 C  C   . GLY   B 73  ? 0.1813 0.2069 0.1429 0.0020  -0.0247 -0.0532 73  GLY   B C   
5167 O  O   . GLY   B 73  ? 0.1750 0.1958 0.1558 0.0035  -0.0221 -0.0381 73  GLY   B O   
5171 N  N   . PRO   B 74  ? 0.1837 0.2227 0.1405 0.0037  -0.0333 -0.0395 74  PRO   B N   
5172 C  CA  . PRO   B 74  ? 0.1805 0.2231 0.1237 0.0066  -0.0239 -0.0297 74  PRO   B CA  
5173 C  C   . PRO   B 74  ? 0.1652 0.2039 0.1258 0.0111  -0.0201 -0.0215 74  PRO   B C   
5174 O  O   . PRO   B 74  ? 0.1737 0.2072 0.1648 0.0097  -0.0117 -0.0329 74  PRO   B O   
5175 C  CB  . PRO   B 74  ? 0.1929 0.2429 0.1183 0.0037  -0.0185 -0.0209 74  PRO   B CB  
5176 C  CG  . PRO   B 74  ? 0.2102 0.2547 0.1541 0.0074  -0.0165 -0.0189 74  PRO   B CG  
5177 C  CD  . PRO   B 74  ? 0.2081 0.2420 0.1508 0.0113  -0.0224 -0.0308 74  PRO   B CD  
5185 N  N   . LEU   B 75  ? 0.1573 0.1931 0.1267 0.0117  -0.0225 -0.0229 75  LEU   B N   
5186 C  CA  . LEU   B 75  ? 0.1632 0.1931 0.1235 0.0049  -0.0156 -0.0077 75  LEU   B CA  
5187 C  C   . LEU   B 75  ? 0.1682 0.2047 0.1244 0.0060  -0.0131 -0.0034 75  LEU   B C   
5188 O  O   . LEU   B 75  ? 0.1825 0.2173 0.1327 0.0016  -0.0083 0.0036  75  LEU   B O   
5189 C  CB  . LEU   B 75  ? 0.1725 0.1951 0.1092 -0.0071 -0.0221 0.0083  75  LEU   B CB  
5190 C  CG  . LEU   B 75  ? 0.2001 0.2101 0.1324 -0.0260 -0.0074 0.0073  75  LEU   B CG  
5191 C  CD1 . LEU   B 75  ? 0.2302 0.2193 0.1462 -0.0353 0.0148  -0.0006 75  LEU   B CD1 
5192 C  CD2 . LEU   B 75  ? 0.2317 0.2292 0.2063 -0.0181 0.0061  0.0175  75  LEU   B CD2 
5204 N  N   . LYS   B 76  ? 0.1680 0.2261 0.1477 0.0005  -0.0052 0.0141  76  LYS   B N   
5205 C  CA  . LYS   B 76  ? 0.1804 0.2325 0.1857 -0.0023 0.0186  0.0040  76  LYS   B CA  
5206 C  C   . LYS   B 76  ? 0.1720 0.2145 0.1611 0.0047  0.0163  0.0234  76  LYS   B C   
5207 O  O   . LYS   B 76  ? 0.1795 0.1938 0.1573 0.0020  0.0081  0.0237  76  LYS   B O   
5208 C  CB  . LYS   B 76  ? 0.1925 0.2384 0.2372 -0.0096 0.0424  -0.0222 76  LYS   B CB  
5209 C  CG  . LYS   B 76  ? 0.2025 0.2532 0.2744 0.0046  0.0318  -0.0376 76  LYS   B CG  
5210 C  CD  . LYS   B 76  ? 0.2070 0.2592 0.3106 0.0114  0.0251  -0.0554 76  LYS   B CD  
5211 C  CE  . LYS   B 76  ? 0.2189 0.2746 0.3616 0.0130  0.0073  -0.0628 76  LYS   B CE  
5212 N  NZ  . LYS   B 76  ? 0.2188 0.2820 0.3846 0.0095  -0.0177 -0.0830 76  LYS   B NZ  
5226 N  N   . VAL   B 77  ? 0.1804 0.2256 0.1631 0.0104  0.0142  0.0273  77  VAL   B N   
5227 C  CA  . VAL   B 77  ? 0.1827 0.2151 0.1601 0.0197  0.0165  0.0513  77  VAL   B CA  
5228 C  C   . VAL   B 77  ? 0.1687 0.1914 0.1639 0.0204  0.0219  0.0398  77  VAL   B C   
5229 O  O   . VAL   B 77  ? 0.1707 0.1863 0.1660 0.0286  0.0265  0.0355  77  VAL   B O   
5230 C  CB  . VAL   B 77  ? 0.1942 0.2265 0.2056 0.0184  0.0233  0.0736  77  VAL   B CB  
5231 C  CG1 . VAL   B 77  ? 0.1897 0.2128 0.2453 0.0121  0.0282  0.0811  77  VAL   B CG1 
5232 C  CG2 . VAL   B 77  ? 0.2092 0.2437 0.2242 0.0139  0.0062  0.0794  77  VAL   B CG2 
5242 N  N   . GLY   B 78  ? 0.1685 0.1753 0.1551 0.0108  0.0160  0.0354  78  GLY   B N   
5243 C  CA  . GLY   B 78  ? 0.1664 0.1678 0.1487 0.0133  0.0270  0.0177  78  GLY   B CA  
5244 C  C   . GLY   B 78  ? 0.1566 0.1607 0.1402 0.0089  0.0191  0.0194  78  GLY   B C   
5245 O  O   . GLY   B 78  ? 0.1606 0.1642 0.1539 0.0199  0.0130  0.0176  78  GLY   B O   
5249 N  N   . GLY   B 79  ? 0.1536 0.1666 0.1425 0.0148  0.0146  0.0158  79  GLY   B N   
5250 C  CA  . GLY   B 79  ? 0.1583 0.1578 0.1448 0.0158  0.0131  0.0120  79  GLY   B CA  
5251 C  C   . GLY   B 79  ? 0.1437 0.1462 0.1454 0.0120  0.0077  0.0070  79  GLY   B C   
5252 O  O   . GLY   B 79  ? 0.1513 0.1467 0.1577 0.0108  0.0173  0.0205  79  GLY   B O   
5256 N  N   . SER   B 80  ? 0.1458 0.1417 0.1571 0.0079  0.0163  0.0081  80  SER   B N   
5257 C  CA  . SER   B 80  ? 0.1361 0.1447 0.1509 0.0033  0.0035  0.0051  80  SER   B CA  
5258 C  C   . SER   B 80  ? 0.1419 0.1420 0.1416 0.0069  -0.0042 -0.0028 80  SER   B C   
5259 O  O   . SER   B 80  ? 0.1557 0.1423 0.1635 0.0135  0.0011  -0.0007 80  SER   B O   
5260 C  CB  . SER   B 80  ? 0.1444 0.1470 0.1487 -0.0054 -0.0036 0.0128  80  SER   B CB  
5261 O  OG  . SER   B 80  ? 0.1546 0.1591 0.1607 -0.0031 -0.0167 0.0098  80  SER   B OG  
5267 N  N   . CYS   B 81  ? 0.1392 0.1272 0.1464 -0.0003 -0.0092 -0.0026 81  CYS   B N   
5268 C  CA  . CYS   B 81  ? 0.1443 0.1300 0.1488 0.0029  -0.0147 -0.0019 81  CYS   B CA  
5269 C  C   . CYS   B 81  ? 0.1435 0.1317 0.1286 -0.0000 -0.0148 0.0044  81  CYS   B C   
5270 O  O   . CYS   B 81  ? 0.1642 0.1304 0.1365 0.0103  -0.0023 -0.0012 81  CYS   B O   
5271 C  CB  . CYS   B 81  ? 0.1622 0.1455 0.1520 -0.0089 -0.0109 -0.0006 81  CYS   B CB  
5272 S  SG  . CYS   B 81  ? 0.1626 0.1598 0.1512 -0.0032 -0.0275 -0.0091 81  CYS   B SG  
5278 N  N   . VAL   B 82  ? 0.1506 0.1303 0.1329 -0.0025 -0.0127 -0.0008 82  VAL   B N   
5279 C  CA  . VAL   B 82  ? 0.1588 0.1320 0.1359 -0.0046 -0.0100 0.0051  82  VAL   B CA  
5280 C  C   . VAL   B 82  ? 0.1620 0.1254 0.1576 -0.0037 -0.0088 -0.0059 82  VAL   B C   
5281 O  O   . VAL   B 82  ? 0.1671 0.1293 0.1835 -0.0048 -0.0120 -0.0202 82  VAL   B O   
5282 C  CB  . VAL   B 82  ? 0.1627 0.1534 0.1472 -0.0011 -0.0154 0.0088  82  VAL   B CB  
5283 C  CG1 . VAL   B 82  ? 0.1836 0.1723 0.1538 0.0049  -0.0178 0.0219  82  VAL   B CG1 
5284 C  CG2 . VAL   B 82  ? 0.1661 0.1661 0.1633 -0.0077 -0.0309 0.0158  82  VAL   B CG2 
5294 N  N   . LEU   B 83  ? 0.1511 0.1146 0.1479 -0.0163 -0.0174 -0.0091 83  LEU   B N   
5295 C  CA  . LEU   B 83  ? 0.1541 0.1282 0.1341 -0.0156 -0.0200 -0.0044 83  LEU   B CA  
5296 C  C   . LEU   B 83  ? 0.1510 0.1301 0.1303 -0.0161 -0.0191 0.0026  83  LEU   B C   
5297 O  O   . LEU   B 83  ? 0.1510 0.1418 0.1196 -0.0194 -0.0144 0.0068  83  LEU   B O   
5298 C  CB  . LEU   B 83  ? 0.1603 0.1432 0.1254 -0.0161 -0.0198 -0.0070 83  LEU   B CB  
5299 C  CG  . LEU   B 83  ? 0.1783 0.1648 0.1347 -0.0230 -0.0096 -0.0090 83  LEU   B CG  
5300 C  CD1 . LEU   B 83  ? 0.1901 0.1654 0.1398 -0.0132 -0.0236 -0.0014 83  LEU   B CD1 
5301 C  CD2 . LEU   B 83  ? 0.1896 0.1701 0.1538 -0.0114 -0.0094 -0.0222 83  LEU   B CD2 
5313 N  N   . SER   B 84  ? 0.1520 0.1404 0.1587 -0.0246 -0.0191 0.0021  84  SER   B N   
5314 C  CA  . SER   B 84  ? 0.1595 0.1632 0.1410 -0.0293 -0.0120 0.0130  84  SER   B CA  
5315 C  C   . SER   B 84  ? 0.1518 0.1821 0.1064 -0.0207 -0.0153 0.0196  84  SER   B C   
5316 O  O   . SER   B 84  ? 0.1578 0.1700 0.1065 -0.0172 -0.0156 0.0072  84  SER   B O   
5317 C  CB  . SER   B 84  ? 0.1784 0.1644 0.1916 -0.0341 0.0085  0.0106  84  SER   B CB  
5318 O  OG  . SER   B 84  ? 0.1754 0.1853 0.2311 -0.0412 0.0037  0.0243  84  SER   B OG  
5324 N  N   . GLY   B 85  ? 0.1545 0.2016 0.1265 -0.0249 -0.0160 0.0208  85  GLY   B N   
5325 C  CA  . GLY   B 85  ? 0.1521 0.2070 0.1422 -0.0362 -0.0049 -0.0093 85  GLY   B CA  
5326 C  C   . GLY   B 85  ? 0.1487 0.1898 0.1323 -0.0380 -0.0026 0.0049  85  GLY   B C   
5327 O  O   . GLY   B 85  ? 0.1532 0.1841 0.1406 -0.0479 0.0128  -0.0087 85  GLY   B O   
5331 N  N   . HIS   B 86  ? 0.1470 0.1754 0.1479 -0.0338 -0.0153 0.0188  86  HIS   B N   
5332 C  CA  . HIS   B 86  ? 0.1529 0.1680 0.1421 -0.0344 -0.0148 0.0189  86  HIS   B CA  
5333 C  C   . HIS   B 86  ? 0.1490 0.1847 0.1369 -0.0436 -0.0078 0.0318  86  HIS   B C   
5334 O  O   . HIS   B 86  ? 0.1594 0.2003 0.1435 -0.0369 0.0056  0.0318  86  HIS   B O   
5335 C  CB  . HIS   B 86  ? 0.1606 0.1742 0.1624 -0.0269 -0.0174 0.0077  86  HIS   B CB  
5336 C  CG  . HIS   B 86  ? 0.1660 0.1765 0.1536 -0.0176 -0.0219 0.0112  86  HIS   B CG  
5337 N  ND1 . HIS   B 86  ? 0.1754 0.1940 0.1693 -0.0258 -0.0263 -0.0013 86  HIS   B ND1 
5338 C  CD2 . HIS   B 86  ? 0.1643 0.1732 0.1521 -0.0149 -0.0274 0.0117  86  HIS   B CD2 
5339 C  CE1 . HIS   B 86  ? 0.1819 0.1910 0.1544 -0.0157 -0.0035 -0.0176 86  HIS   B CE1 
5340 N  NE2 . HIS   B 86  ? 0.1735 0.1847 0.1464 -0.0026 -0.0139 0.0043  86  HIS   B NE2 
5348 N  N   . ASN   B 87  ? 0.1547 0.1869 0.1583 -0.0374 -0.0027 0.0269  87  ASN   B N   
5349 C  CA  . ASN   B 87  ? 0.1650 0.2068 0.1545 -0.0395 0.0168  0.0158  87  ASN   B CA  
5350 C  C   . ASN   B 87  ? 0.1749 0.1959 0.1405 -0.0363 0.0322  0.0203  87  ASN   B C   
5351 O  O   . ASN   B 87  ? 0.1974 0.2058 0.1755 -0.0291 0.0414  0.0097  87  ASN   B O   
5352 C  CB  . ASN   B 87  ? 0.1707 0.2447 0.1803 -0.0345 0.0168  0.0244  87  ASN   B CB  
5353 C  CG  . ASN   B 87  ? 0.1779 0.2609 0.1928 -0.0025 0.0272  0.0401  87  ASN   B CG  
5354 O  OD1 . ASN   B 87  ? 0.1692 0.2477 0.1775 -0.0023 0.0438  0.0541  87  ASN   B OD1 
5355 N  ND2 . ASN   B 87  ? 0.2081 0.2704 0.2425 0.0058  0.0253  0.0335  87  ASN   B ND2 
5362 N  N   . LEU   B 88  ? 0.1666 0.1803 0.1289 -0.0386 0.0131  0.0076  88  LEU   B N   
5363 C  CA  . LEU   B 88  ? 0.1735 0.1712 0.1324 -0.0353 0.0060  -0.0028 88  LEU   B CA  
5364 C  C   . LEU   B 88  ? 0.1693 0.1602 0.1365 -0.0389 -0.0048 0.0057  88  LEU   B C   
5365 O  O   . LEU   B 88  ? 0.1939 0.1689 0.1689 -0.0222 -0.0291 -0.0064 88  LEU   B O   
5366 C  CB  . LEU   B 88  ? 0.1893 0.1769 0.1574 -0.0414 -0.0056 0.0166  88  LEU   B CB  
5367 C  CG  . LEU   B 88  ? 0.2242 0.2008 0.1755 -0.0352 -0.0240 0.0377  88  LEU   B CG  
5368 C  CD1 . LEU   B 88  ? 0.2331 0.2319 0.1913 -0.0425 -0.0180 0.0564  88  LEU   B CD1 
5369 C  CD2 . LEU   B 88  ? 0.2579 0.2290 0.2344 0.0030  -0.0512 0.0175  88  LEU   B CD2 
5381 N  N   . ALA   B 89  ? 0.1582 0.1597 0.1293 -0.0363 0.0106  0.0058  89  ALA   B N   
5382 C  CA  . ALA   B 89  ? 0.1594 0.1550 0.1122 -0.0414 -0.0001 0.0061  89  ALA   B CA  
5383 C  C   . ALA   B 89  ? 0.1690 0.1524 0.1208 -0.0431 0.0156  0.0067  89  ALA   B C   
5384 O  O   . ALA   B 89  ? 0.1556 0.1667 0.1577 -0.0417 0.0108  -0.0193 89  ALA   B O   
5385 C  CB  . ALA   B 89  ? 0.1521 0.1557 0.1259 -0.0405 0.0019  0.0157  89  ALA   B CB  
5391 N  N   . LYS   B 90  ? 0.2021 0.1415 0.1384 -0.0500 -0.0038 0.0123  90  LYS   B N   
5392 C  CA  . LYS   B 90  ? 0.2140 0.1409 0.1206 -0.0484 -0.0065 0.0071  90  LYS   B CA  
5393 C  C   . LYS   B 90  ? 0.1952 0.1403 0.1367 -0.0469 -0.0069 -0.0029 90  LYS   B C   
5394 O  O   . LYS   B 90  ? 0.2038 0.1589 0.1538 -0.0581 -0.0003 -0.0000 90  LYS   B O   
5395 C  CB  . LYS   B 90  ? 0.2376 0.1523 0.1495 -0.0348 -0.0013 0.0204  90  LYS   B CB  
5396 C  CG  . LYS   B 90  ? 0.2416 0.1689 0.1518 -0.0202 0.0302  0.0162  90  LYS   B CG  
5397 C  CD  . LYS   B 90  ? 0.2716 0.1974 0.2137 -0.0132 0.0514  -0.0051 90  LYS   B CD  
5398 C  CE  . LYS   B 90  ? 0.2896 0.2121 0.2711 -0.0190 0.0618  -0.0126 90  LYS   B CE  
5399 N  NZ  . LYS   B 90  ? 0.2901 0.2027 0.2695 -0.0337 0.0765  -0.0147 90  LYS   B NZ  
5413 N  N   . HIS   B 91  ? 0.1685 0.1286 0.1212 -0.0355 -0.0192 0.0054  91  HIS   B N   
5414 C  CA  . HIS   B 91  ? 0.1604 0.1335 0.1312 -0.0239 -0.0173 0.0024  91  HIS   B CA  
5415 C  C   . HIS   B 91  ? 0.1509 0.1339 0.1150 -0.0254 -0.0009 0.0068  91  HIS   B C   
5416 O  O   . HIS   B 91  ? 0.1674 0.1387 0.1123 -0.0271 -0.0210 0.0026  91  HIS   B O   
5417 C  CB  . HIS   B 91  ? 0.1797 0.1388 0.1720 -0.0074 -0.0119 0.0188  91  HIS   B CB  
5418 C  CG  . HIS   B 91  ? 0.2185 0.1536 0.2402 0.0018  0.0208  0.0244  91  HIS   B CG  
5419 N  ND1 . HIS   B 91  ? 0.2497 0.1603 0.3028 0.0017  0.0306  0.0094  91  HIS   B ND1 
5420 C  CD2 . HIS   B 91  ? 0.2274 0.1785 0.2905 0.0133  0.0105  0.0530  91  HIS   B CD2 
5421 C  CE1 . HIS   B 91  ? 0.2537 0.1758 0.3338 0.0188  0.0312  0.0136  91  HIS   B CE1 
5422 N  NE2 . HIS   B 91  ? 0.2413 0.1891 0.3320 0.0230  0.0267  0.0519  91  HIS   B NE2 
5430 N  N   . CYS   B 92  ? 0.1463 0.1326 0.1156 -0.0277 -0.0143 0.0053  92  CYS   B N   
5431 C  CA  . CYS   B 92  ? 0.1430 0.1286 0.1222 -0.0237 -0.0086 -0.0038 92  CYS   B CA  
5432 C  C   . CYS   B 92  ? 0.1443 0.1230 0.1103 -0.0143 -0.0059 -0.0007 92  CYS   B C   
5433 O  O   . CYS   B 92  ? 0.1474 0.1306 0.1334 -0.0166 -0.0069 0.0030  92  CYS   B O   
5434 C  CB  . CYS   B 92  ? 0.1429 0.1364 0.1202 -0.0180 0.0011  0.0043  92  CYS   B CB  
5435 S  SG  . CYS   B 92  ? 0.1452 0.1370 0.1254 -0.0120 -0.0101 0.0041  92  CYS   B SG  
5441 N  N   . LEU   B 93  ? 0.1365 0.1294 0.1128 -0.0136 -0.0074 -0.0025 93  LEU   B N   
5442 C  CA  . LEU   B 93  ? 0.1363 0.1308 0.1167 -0.0025 -0.0131 0.0011  93  LEU   B CA  
5443 C  C   . LEU   B 93  ? 0.1327 0.1266 0.1129 -0.0011 -0.0079 0.0103  93  LEU   B C   
5444 O  O   . LEU   B 93  ? 0.1394 0.1218 0.1211 -0.0039 -0.0047 0.0038  93  LEU   B O   
5445 C  CB  . LEU   B 93  ? 0.1396 0.1246 0.1236 -0.0004 -0.0036 0.0090  93  LEU   B CB  
5446 C  CG  . LEU   B 93  ? 0.1324 0.1357 0.1553 -0.0063 -0.0034 0.0119  93  LEU   B CG  
5447 C  CD1 . LEU   B 93  ? 0.1326 0.1419 0.1565 0.0034  -0.0119 -0.0060 93  LEU   B CD1 
5448 C  CD2 . LEU   B 93  ? 0.1363 0.1359 0.1599 -0.0064 -0.0056 -0.0034 93  LEU   B CD2 
5460 N  N   . HIS   B 94  ? 0.1332 0.1242 0.1070 -0.0028 -0.0139 0.0103  94  HIS   B N   
5461 C  CA  . HIS   B 94  ? 0.1377 0.1240 0.1164 -0.0005 0.0008  0.0055  94  HIS   B CA  
5462 C  C   . HIS   B 94  ? 0.1308 0.1222 0.1255 -0.0030 -0.0031 0.0091  94  HIS   B C   
5463 O  O   . HIS   B 94  ? 0.1338 0.1365 0.1616 -0.0002 0.0106  0.0015  94  HIS   B O   
5464 C  CB  . HIS   B 94  ? 0.1381 0.1308 0.1244 0.0005  -0.0077 0.0035  94  HIS   B CB  
5465 C  CG  . HIS   B 94  ? 0.1378 0.1225 0.1239 -0.0090 -0.0130 0.0017  94  HIS   B CG  
5466 N  ND1 . HIS   B 94  ? 0.1398 0.1363 0.1242 -0.0052 -0.0200 -0.0018 94  HIS   B ND1 
5467 C  CD2 . HIS   B 94  ? 0.1369 0.1344 0.1287 0.0003  -0.0138 0.0048  94  HIS   B CD2 
5468 C  CE1 . HIS   B 94  ? 0.1396 0.1355 0.1221 -0.0046 -0.0236 0.0073  94  HIS   B CE1 
5469 N  NE2 . HIS   B 94  ? 0.1370 0.1408 0.1322 -0.0131 -0.0141 0.0057  94  HIS   B NE2 
5477 N  N   . VAL   B 95  ? 0.1284 0.1211 0.1274 -0.0062 -0.0034 0.0066  95  VAL   B N   
5478 C  CA  . VAL   B 95  ? 0.1311 0.1304 0.1243 -0.0007 -0.0054 0.0121  95  VAL   B CA  
5479 C  C   . VAL   B 95  ? 0.1386 0.1332 0.1227 -0.0024 0.0033  0.0070  95  VAL   B C   
5480 O  O   . VAL   B 95  ? 0.1410 0.1275 0.1427 0.0066  0.0038  0.0135  95  VAL   B O   
5481 C  CB  . VAL   B 95  ? 0.1335 0.1281 0.1370 -0.0003 -0.0020 0.0072  95  VAL   B CB  
5482 C  CG1 . VAL   B 95  ? 0.1467 0.1367 0.1513 -0.0030 0.0017  0.0170  95  VAL   B CG1 
5483 C  CG2 . VAL   B 95  ? 0.1497 0.1336 0.1307 0.0044  -0.0091 0.0054  95  VAL   B CG2 
5493 N  N   . VAL   B 96  ? 0.1472 0.1400 0.1226 0.0087  0.0020  0.0140  96  VAL   B N   
5494 C  CA  . VAL   B 96  ? 0.1522 0.1551 0.1295 0.0103  0.0076  0.0196  96  VAL   B CA  
5495 C  C   . VAL   B 96  ? 0.1599 0.1544 0.1339 0.0073  0.0113  0.0166  96  VAL   B C   
5496 O  O   . VAL   B 96  ? 0.1583 0.1623 0.1577 0.0032  0.0227  0.0068  96  VAL   B O   
5497 C  CB  . VAL   B 96  ? 0.1577 0.1711 0.1276 0.0115  0.0078  0.0124  96  VAL   B CB  
5498 C  CG1 . VAL   B 96  ? 0.1621 0.1846 0.1438 0.0199  0.0094  0.0088  96  VAL   B CG1 
5499 C  CG2 . VAL   B 96  ? 0.1632 0.1729 0.1399 0.0069  0.0079  -0.0016 96  VAL   B CG2 
5509 N  N   . GLY   B 97  ? 0.1625 0.1556 0.1289 0.0048  0.0072  0.0178  97  GLY   B N   
5510 C  CA  . GLY   B 97  ? 0.1712 0.1604 0.1367 -0.0006 0.0079  0.0195  97  GLY   B CA  
5511 C  C   . GLY   B 97  ? 0.1919 0.1696 0.1479 0.0125  0.0079  0.0216  97  GLY   B C   
5512 O  O   . GLY   B 97  ? 0.2062 0.1727 0.1477 0.0138  0.0038  0.0136  97  GLY   B O   
5516 N  N   . PRO   B 98  ? 0.2053 0.1741 0.1690 0.0149  0.0378  0.0364  98  PRO   B N   
5517 C  CA  . PRO   B 98  ? 0.2192 0.1901 0.1772 0.0233  0.0490  0.0346  98  PRO   B CA  
5518 C  C   . PRO   B 98  ? 0.2354 0.1930 0.1513 0.0430  0.0455  0.0552  98  PRO   B C   
5519 O  O   . PRO   B 98  ? 0.2310 0.1932 0.1733 0.0367  0.0463  0.0529  98  PRO   B O   
5520 C  CB  . PRO   B 98  ? 0.2063 0.1941 0.2013 0.0183  0.0569  0.0317  98  PRO   B CB  
5521 C  CG  . PRO   B 98  ? 0.2030 0.1855 0.1962 0.0164  0.0444  0.0477  98  PRO   B CG  
5522 C  CD  . PRO   B 98  ? 0.1911 0.1738 0.1866 0.0169  0.0416  0.0506  98  PRO   B CD  
5530 N  N   . ASN   B 99  ? 0.2467 0.2077 0.1645 0.0635  0.0494  0.0400  99  ASN   B N   
5531 C  CA  . ASN   B 99  ? 0.2734 0.2225 0.1662 0.0687  0.0452  0.0589  99  ASN   B CA  
5532 C  C   . ASN   B 99  ? 0.3006 0.2543 0.2045 0.0665  0.0652  0.0956  99  ASN   B C   
5533 O  O   . ASN   B 99  ? 0.3109 0.2573 0.2152 0.0632  0.0505  0.0912  99  ASN   B O   
5534 C  CB  . ASN   B 99  ? 0.2832 0.2192 0.1681 0.0705  0.0328  0.0447  99  ASN   B CB  
5535 C  CG  . ASN   B 99  ? 0.2900 0.2255 0.1928 0.0635  0.0160  0.0407  99  ASN   B CG  
5536 O  OD1 . ASN   B 99  ? 0.2915 0.2252 0.2213 0.0644  0.0244  0.0509  99  ASN   B OD1 
5537 N  ND2 . ASN   B 99  ? 0.2886 0.2239 0.1958 0.0650  -0.0109 0.0291  99  ASN   B ND2 
5544 N  N   A VAL   B 100 ? 0.3190 0.2704 0.2529 0.0555  0.0700  0.1154  100 VAL   B N   
5545 N  N   B VAL   B 100 ? 0.3195 0.2698 0.2514 0.0560  0.0651  0.1112  100 VAL   B N   
5546 C  CA  A VAL   B 100 ? 0.3434 0.2875 0.3065 0.0409  0.0715  0.1277  100 VAL   B CA  
5547 C  CA  B VAL   B 100 ? 0.3428 0.2856 0.2996 0.0430  0.0627  0.1205  100 VAL   B CA  
5548 C  C   A VAL   B 100 ? 0.3622 0.2929 0.3036 0.0442  0.0685  0.1418  100 VAL   B C   
5549 C  C   B VAL   B 100 ? 0.3613 0.2912 0.2995 0.0452  0.0608  0.1357  100 VAL   B C   
5550 O  O   A VAL   B 100 ? 0.3683 0.3020 0.3100 0.0412  0.0729  0.1338  100 VAL   B O   
5551 O  O   B VAL   B 100 ? 0.3656 0.2966 0.3008 0.0419  0.0625  0.1290  100 VAL   B O   
5552 C  CB  A VAL   B 100 ? 0.3504 0.2987 0.3684 0.0194  0.0688  0.1266  100 VAL   B CB  
5553 C  CB  B VAL   B 100 ? 0.3481 0.2951 0.3487 0.0250  0.0588  0.1173  100 VAL   B CB  
5554 C  CG1 A VAL   B 100 ? 0.3527 0.3015 0.3908 0.0148  0.0666  0.1236  100 VAL   B CG1 
5555 C  CG1 B VAL   B 100 ? 0.3500 0.2977 0.3656 0.0211  0.0570  0.1151  100 VAL   B CG1 
5556 C  CG2 A VAL   B 100 ? 0.3522 0.3024 0.3816 0.0110  0.0705  0.1329  100 VAL   B CG2 
5557 C  CG2 B VAL   B 100 ? 0.3493 0.2982 0.3602 0.0180  0.0590  0.1208  100 VAL   B CG2 
5576 N  N   . ASN   B 101 ? 0.3758 0.2950 0.2978 0.0532  0.0558  0.1451  101 ASN   B N   
5577 C  CA  . ASN   B 101 ? 0.4109 0.3090 0.3168 0.0642  0.0349  0.1481  101 ASN   B CA  
5578 C  C   . ASN   B 101 ? 0.4505 0.3419 0.3062 0.0664  0.0128  0.1672  101 ASN   B C   
5579 O  O   . ASN   B 101 ? 0.4565 0.3570 0.3292 0.0723  0.0115  0.1409  101 ASN   B O   
5580 C  CB  . ASN   B 101 ? 0.4076 0.2927 0.3263 0.0657  0.0412  0.1288  101 ASN   B CB  
5581 C  CG  . ASN   B 101 ? 0.4027 0.2774 0.3239 0.0684  0.0433  0.1258  101 ASN   B CG  
5582 O  OD1 . ASN   B 101 ? 0.4068 0.2807 0.3511 0.0654  0.0571  0.1140  101 ASN   B OD1 
5583 N  ND2 . ASN   B 101 ? 0.3957 0.2684 0.3142 0.0669  0.0392  0.1211  101 ASN   B ND2 
5591 N  N   . LYS   B 102 ? 0.4825 0.3736 0.3294 0.0533  0.0146  0.1615  102 LYS   B N   
5592 C  CA  . LYS   B 102 ? 0.5118 0.4127 0.3668 0.0362  0.0193  0.1337  102 LYS   B CA  
5593 C  C   . LYS   B 102 ? 0.5047 0.4134 0.3403 0.0351  0.0259  0.1345  102 LYS   B C   
5594 O  O   . LYS   B 102 ? 0.5141 0.4187 0.3476 0.0357  0.0097  0.1323  102 LYS   B O   
5595 C  CB  . LYS   B 102 ? 0.5427 0.4477 0.4348 0.0221  0.0315  0.0906  102 LYS   B CB  
5596 C  CG  . LYS   B 102 ? 0.5677 0.4774 0.5082 0.0120  0.0423  0.0462  102 LYS   B CG  
5597 C  CD  . LYS   B 102 ? 0.5881 0.5020 0.5719 0.0037  0.0518  0.0121  102 LYS   B CD  
5598 C  CE  . LYS   B 102 ? 0.6023 0.5205 0.6230 -0.0033 0.0596  -0.0107 102 LYS   B CE  
5599 N  NZ  . LYS   B 102 ? 0.6104 0.5313 0.6519 -0.0069 0.0637  -0.0233 102 LYS   B NZ  
5613 N  N   . GLY   B 103 ? 0.4849 0.4082 0.3316 0.0307  0.0518  0.1236  103 GLY   B N   
5614 C  CA  . GLY   B 103 ? 0.4633 0.4009 0.3382 0.0265  0.0754  0.1028  103 GLY   B CA  
5615 C  C   . GLY   B 103 ? 0.4367 0.3883 0.3380 0.0197  0.0916  0.0821  103 GLY   B C   
5616 O  O   . GLY   B 103 ? 0.4406 0.3952 0.3429 0.0155  0.0950  0.0800  103 GLY   B O   
5620 N  N   A GLU   B 104 ? 0.4195 0.3768 0.3206 0.0220  0.1049  0.0703  104 GLU   B N   
5621 N  N   B GLU   B 104 ? 0.4205 0.3763 0.3295 0.0152  0.0875  0.0674  104 GLU   B N   
5622 C  CA  A GLU   B 104 ? 0.4020 0.3656 0.3064 0.0288  0.1105  0.0549  104 GLU   B CA  
5623 C  CA  B GLU   B 104 ? 0.4037 0.3640 0.3207 0.0134  0.0792  0.0498  104 GLU   B CA  
5624 C  C   A GLU   B 104 ? 0.4034 0.3654 0.3145 0.0147  0.1377  0.0599  104 GLU   B C   
5625 C  C   B GLU   B 104 ? 0.3995 0.3603 0.3281 0.0055  0.0938  0.0496  104 GLU   B C   
5626 O  O   A GLU   B 104 ? 0.4033 0.3671 0.3389 0.0126  0.1340  0.0593  104 GLU   B O   
5627 O  O   B GLU   B 104 ? 0.3992 0.3603 0.3453 0.0047  0.0920  0.0473  104 GLU   B O   
5628 C  CB  A GLU   B 104 ? 0.3870 0.3528 0.2955 0.0498  0.0793  0.0271  104 GLU   B CB  
5629 C  CB  B GLU   B 104 ? 0.3937 0.3542 0.3088 0.0184  0.0527  0.0284  104 GLU   B CB  
5630 C  CG  A GLU   B 104 ? 0.3724 0.3412 0.2787 0.0694  0.0414  -0.0025 104 GLU   B CG  
5631 C  CG  B GLU   B 104 ? 0.3845 0.3451 0.2942 0.0227  0.0223  0.0061  104 GLU   B CG  
5632 C  CD  A GLU   B 104 ? 0.3583 0.3293 0.2523 0.0859  0.0104  -0.0190 104 GLU   B CD  
5633 C  CD  B GLU   B 104 ? 0.3765 0.3356 0.2764 0.0244  -0.0007 -0.0077 104 GLU   B CD  
5634 O  OE1 A GLU   B 104 ? 0.3412 0.3143 0.2089 0.1004  0.0151  -0.0226 104 GLU   B OE1 
5635 O  OE1 B GLU   B 104 ? 0.3681 0.3272 0.2568 0.0243  0.0006  -0.0091 104 GLU   B OE1 
5636 O  OE2 A GLU   B 104 ? 0.3615 0.3361 0.2540 0.0846  -0.0171 -0.0297 104 GLU   B OE2 
5637 O  OE2 B GLU   B 104 ? 0.3781 0.3377 0.2722 0.0245  -0.0197 -0.0176 104 GLU   B OE2 
5650 N  N   A ASP   B 105 ? 0.4019 0.3642 0.3121 0.0048  0.1613  0.0625  105 ASP   B N   
5651 N  N   B ASP   B 105 ? 0.3943 0.3571 0.3242 -0.0009 0.1066  0.0505  105 ASP   B N   
5652 C  CA  A ASP   B 105 ? 0.4030 0.3635 0.3287 -0.0038 0.1776  0.0503  105 ASP   B CA  
5653 C  CA  B ASP   B 105 ? 0.3912 0.3539 0.3318 -0.0058 0.1162  0.0419  105 ASP   B CA  
5654 C  C   A ASP   B 105 ? 0.3866 0.3379 0.2940 -0.0137 0.1838  0.0518  105 ASP   B C   
5655 C  C   B ASP   B 105 ? 0.3805 0.3393 0.3100 -0.0093 0.1173  0.0354  105 ASP   B C   
5656 O  O   A ASP   B 105 ? 0.3756 0.3340 0.2837 -0.0084 0.1828  0.0525  105 ASP   B O   
5657 O  O   B ASP   B 105 ? 0.3779 0.3367 0.2985 -0.0072 0.1220  0.0373  105 ASP   B O   
5658 C  CB  A ASP   B 105 ? 0.4180 0.3844 0.4013 0.0018  0.1760  0.0278  105 ASP   B CB  
5659 C  CB  B ASP   B 105 ? 0.3951 0.3633 0.3713 -0.0042 0.1206  0.0351  105 ASP   B CB  
5660 C  CG  A ASP   B 105 ? 0.4270 0.3983 0.4616 0.0039  0.1765  0.0122  105 ASP   B CG  
5661 C  CG  B ASP   B 105 ? 0.3956 0.3678 0.4026 -0.0054 0.1273  0.0328  105 ASP   B CG  
5662 O  OD1 A ASP   B 105 ? 0.4245 0.4021 0.4702 -0.0003 0.1883  0.0130  105 ASP   B OD1 
5663 O  OD1 B ASP   B 105 ? 0.3930 0.3682 0.4096 -0.0091 0.1319  0.0338  105 ASP   B OD1 
5664 O  OD2 A ASP   B 105 ? 0.4330 0.4035 0.4970 0.0093  0.1651  0.0010  105 ASP   B OD2 
5665 O  OD2 B ASP   B 105 ? 0.3941 0.3698 0.4128 -0.0064 0.1334  0.0343  105 ASP   B OD2 
5674 N  N   A ILE   B 106 ? 0.3758 0.3145 0.3014 -0.0235 0.1696  0.0564  106 ILE   B N   
5675 N  N   B ILE   B 106 ? 0.3722 0.3258 0.3081 -0.0108 0.1068  0.0296  106 ILE   B N   
5676 C  CA  A ILE   B 106 ? 0.3569 0.2897 0.3138 -0.0369 0.1698  0.0487  106 ILE   B CA  
5677 C  CA  B ILE   B 106 ? 0.3590 0.3128 0.3132 -0.0133 0.1045  0.0187  106 ILE   B CA  
5678 C  C   A ILE   B 106 ? 0.3274 0.2777 0.3067 -0.0349 0.1696  0.0375  106 ILE   B C   
5679 C  C   B ILE   B 106 ? 0.3376 0.3059 0.3089 -0.0090 0.1034  0.0064  106 ILE   B C   
5680 O  O   A ILE   B 106 ? 0.3184 0.2570 0.3016 -0.0367 0.1711  0.0330  106 ILE   B O   
5681 O  O   B ILE   B 106 ? 0.3327 0.2954 0.3028 -0.0114 0.0985  -0.0005 106 ILE   B O   
5682 C  CB  A ILE   B 106 ? 0.3732 0.2843 0.3381 -0.0453 0.1558  0.0467  106 ILE   B CB  
5683 C  CB  B ILE   B 106 ? 0.3691 0.3120 0.3259 -0.0185 0.1003  0.0190  106 ILE   B CB  
5684 C  CG1 A ILE   B 106 ? 0.3800 0.2845 0.3448 -0.0415 0.1444  0.0391  106 ILE   B CG1 
5685 C  CG1 B ILE   B 106 ? 0.3745 0.3130 0.3326 -0.0164 0.0935  0.0159  106 ILE   B CG1 
5686 C  CG2 A ILE   B 106 ? 0.3778 0.2868 0.3542 -0.0509 0.1557  0.0485  106 ILE   B CG2 
5687 C  CG2 B ILE   B 106 ? 0.3720 0.3146 0.3359 -0.0216 0.1024  0.0200  106 ILE   B CG2 
5688 C  CD1 A ILE   B 106 ? 0.3847 0.2868 0.3414 -0.0385 0.1402  0.0405  106 ILE   B CD1 
5689 C  CD1 B ILE   B 106 ? 0.3779 0.3147 0.3360 -0.0147 0.0900  0.0170  106 ILE   B CD1 
5712 N  N   A GLN   B 107 ? 0.3149 0.2923 0.3153 -0.0294 0.1575  0.0368  107 GLN   B N   
5713 N  N   B GLN   B 107 ? 0.3254 0.3122 0.3203 -0.0051 0.1008  0.0054  107 GLN   B N   
5714 C  CA  A GLN   B 107 ? 0.2998 0.3065 0.3356 -0.0218 0.1393  0.0318  107 GLN   B CA  
5715 C  CA  B GLN   B 107 ? 0.3125 0.3175 0.3380 -0.0016 0.0944  0.0106  107 GLN   B CA  
5716 C  C   A GLN   B 107 ? 0.2739 0.2864 0.3133 -0.0052 0.1128  0.0194  107 GLN   B C   
5717 C  C   B GLN   B 107 ? 0.2834 0.2944 0.3112 0.0059  0.0912  0.0097  107 GLN   B C   
5718 O  O   A GLN   B 107 ? 0.2627 0.2829 0.3426 0.0034  0.0929  0.0080  107 GLN   B O   
5719 O  O   B GLN   B 107 ? 0.2776 0.2941 0.3291 0.0109  0.0794  0.0031  107 GLN   B O   
5720 C  CB  A GLN   B 107 ? 0.3245 0.3414 0.4020 -0.0230 0.1191  0.0329  107 GLN   B CB  
5721 C  CB  B GLN   B 107 ? 0.3338 0.3450 0.3926 -0.0026 0.0814  0.0138  107 GLN   B CB  
5722 C  CG  A GLN   B 107 ? 0.3512 0.3719 0.4696 -0.0176 0.0862  0.0288  107 GLN   B CG  
5723 C  CG  B GLN   B 107 ? 0.3545 0.3689 0.4484 -0.0004 0.0621  0.0143  107 GLN   B CG  
5724 C  CD  A GLN   B 107 ? 0.3712 0.3944 0.5207 -0.0142 0.0617  0.0283  107 GLN   B CD  
5725 C  CD  B GLN   B 107 ? 0.3704 0.3864 0.4919 0.0009  0.0466  0.0159  107 GLN   B CD  
5726 O  OE1 A GLN   B 107 ? 0.3780 0.4029 0.5390 -0.0091 0.0562  0.0248  107 GLN   B OE1 
5727 O  OE1 B GLN   B 107 ? 0.3753 0.3926 0.5059 0.0036  0.0439  0.0151  107 GLN   B OE1 
5728 N  NE2 A GLN   B 107 ? 0.3802 0.4013 0.5396 -0.0130 0.0515  0.0324  107 GLN   B NE2 
5729 N  NE2 B GLN   B 107 ? 0.3776 0.3922 0.5090 0.0017  0.0403  0.0188  107 GLN   B NE2 
5746 N  N   . LEU   B 108 ? 0.2564 0.2697 0.2752 0.0164  0.0941  0.0155  108 LEU   B N   
5747 C  CA  . LEU   B 108 ? 0.2346 0.2457 0.2319 0.0263  0.0697  0.0290  108 LEU   B CA  
5748 C  C   . LEU   B 108 ? 0.1983 0.2023 0.2167 0.0241  0.0482  0.0374  108 LEU   B C   
5749 O  O   . LEU   B 108 ? 0.1953 0.1826 0.2021 0.0268  0.0370  0.0340  108 LEU   B O   
5750 C  CB  . LEU   B 108 ? 0.2459 0.2644 0.2133 0.0247  0.0676  0.0407  108 LEU   B CB  
5751 C  CG  . LEU   B 108 ? 0.2613 0.2928 0.2266 0.0250  0.0591  0.0173  108 LEU   B CG  
5752 C  CD1 . LEU   B 108 ? 0.2681 0.3054 0.2250 0.0158  0.0610  0.0196  108 LEU   B CD1 
5753 C  CD2 . LEU   B 108 ? 0.2763 0.3028 0.2435 0.0335  0.0434  0.0014  108 LEU   B CD2 
5766 N  N   . LEU   B 109 ? 0.1782 0.1803 0.2176 0.0162  0.0449  0.0315  109 LEU   B N   
5767 C  CA  . LEU   B 109 ? 0.1605 0.1495 0.2335 0.0115  0.0426  0.0333  109 LEU   B CA  
5768 C  C   . LEU   B 109 ? 0.1527 0.1347 0.2327 0.0104  0.0426  0.0192  109 LEU   B C   
5769 O  O   . LEU   B 109 ? 0.1508 0.1338 0.2260 0.0044  0.0318  0.0348  109 LEU   B O   
5770 C  CB  . LEU   B 109 ? 0.1644 0.1427 0.2402 0.0095  0.0255  0.0374  109 LEU   B CB  
5771 C  CG  . LEU   B 109 ? 0.1608 0.1415 0.2315 0.0011  0.0251  0.0277  109 LEU   B CG  
5772 C  CD1 . LEU   B 109 ? 0.1577 0.1534 0.2177 0.0152  0.0287  0.0345  109 LEU   B CD1 
5773 C  CD2 . LEU   B 109 ? 0.1737 0.1494 0.2519 0.0099  0.0172  0.0242  109 LEU   B CD2 
5785 N  N   . LYS   B 110 ? 0.1468 0.1370 0.2263 -0.0004 0.0322  0.0269  110 LYS   B N   
5786 C  CA  . LYS   B 110 ? 0.1448 0.1345 0.2204 0.0001  0.0276  0.0177  110 LYS   B CA  
5787 C  C   . LYS   B 110 ? 0.1405 0.1361 0.2040 0.0023  0.0279  0.0152  110 LYS   B C   
5788 O  O   . LYS   B 110 ? 0.1363 0.1394 0.1959 -0.0032 0.0191  0.0075  110 LYS   B O   
5789 C  CB  . LYS   B 110 ? 0.1445 0.1373 0.2376 -0.0019 0.0356  0.0107  110 LYS   B CB  
5790 C  CG  . LYS   B 110 ? 0.1483 0.1349 0.2500 -0.0049 0.0230  0.0189  110 LYS   B CG  
5791 C  CD  . LYS   B 110 ? 0.1515 0.1323 0.2611 -0.0054 0.0254  0.0149  110 LYS   B CD  
5792 C  CE  . LYS   B 110 ? 0.1470 0.1473 0.2779 -0.0014 0.0234  0.0073  110 LYS   B CE  
5793 N  NZ  . LYS   B 110 ? 0.1494 0.1621 0.2777 0.0005  0.0070  0.0119  110 LYS   B NZ  
5807 N  N   . SER   B 111 ? 0.1517 0.1357 0.2133 -0.0021 0.0286  0.0156  111 SER   B N   
5808 C  CA  . SER   B 111 ? 0.1507 0.1404 0.1965 0.0033  0.0259  0.0190  111 SER   B CA  
5809 C  C   . SER   B 111 ? 0.1536 0.1353 0.1945 0.0044  0.0110  0.0162  111 SER   B C   
5810 O  O   . SER   B 111 ? 0.1475 0.1410 0.1957 0.0028  0.0116  0.0137  111 SER   B O   
5811 C  CB  . SER   B 111 ? 0.1586 0.1680 0.2025 0.0042  0.0380  0.0250  111 SER   B CB  
5812 O  OG  . SER   B 111 ? 0.1776 0.2011 0.2130 0.0122  0.0340  0.0279  111 SER   B OG  
5818 N  N   . ALA   B 112 ? 0.1414 0.1374 0.2019 0.0069  0.0213  0.0265  112 ALA   B N   
5819 C  CA  . ALA   B 112 ? 0.1385 0.1445 0.1816 -0.0008 0.0108  0.0199  112 ALA   B CA  
5820 C  C   . ALA   B 112 ? 0.1256 0.1394 0.1748 -0.0023 0.0132  0.0187  112 ALA   B C   
5821 O  O   . ALA   B 112 ? 0.1306 0.1410 0.1766 0.0007  0.0133  0.0025  112 ALA   B O   
5822 C  CB  . ALA   B 112 ? 0.1414 0.1434 0.1897 0.0110  0.0128  0.0220  112 ALA   B CB  
5828 N  N   . TYR   B 113 ? 0.1287 0.1222 0.1876 -0.0035 0.0130  0.0151  113 TYR   B N   
5829 C  CA  . TYR   B 113 ? 0.1264 0.1237 0.1808 -0.0027 0.0102  0.0074  113 TYR   B CA  
5830 C  C   . TYR   B 113 ? 0.1234 0.1216 0.1775 -0.0015 0.0119  0.0068  113 TYR   B C   
5831 O  O   . TYR   B 113 ? 0.1302 0.1229 0.1688 -0.0036 0.0104  0.0019  113 TYR   B O   
5832 C  CB  . TYR   B 113 ? 0.1332 0.1192 0.1857 -0.0024 0.0178  0.0116  113 TYR   B CB  
5833 C  CG  . TYR   B 113 ? 0.1406 0.1267 0.1950 -0.0064 0.0195  0.0181  113 TYR   B CG  
5834 C  CD1 . TYR   B 113 ? 0.1419 0.1260 0.2133 -0.0064 0.0172  0.0225  113 TYR   B CD1 
5835 C  CD2 . TYR   B 113 ? 0.1413 0.1251 0.2031 -0.0044 0.0112  0.0202  113 TYR   B CD2 
5836 C  CE1 . TYR   B 113 ? 0.1422 0.1313 0.2099 0.0008  0.0195  0.0103  113 TYR   B CE1 
5837 C  CE2 . TYR   B 113 ? 0.1462 0.1116 0.2186 0.0006  0.0156  0.0287  113 TYR   B CE2 
5838 C  CZ  . TYR   B 113 ? 0.1403 0.1214 0.2149 0.0041  0.0112  0.0165  113 TYR   B CZ  
5839 O  OH  . TYR   B 113 ? 0.1482 0.1224 0.2452 0.0122  0.0209  0.0078  113 TYR   B OH  
5849 N  N   . GLU   B 114 ? 0.1236 0.1124 0.1921 0.0010  0.0093  0.0122  114 GLU   B N   
5850 C  CA  . GLU   B 114 ? 0.1215 0.1240 0.1826 0.0052  0.0071  0.0059  114 GLU   B CA  
5851 C  C   . GLU   B 114 ? 0.1224 0.1213 0.1640 -0.0004 0.0074  0.0032  114 GLU   B C   
5852 O  O   . GLU   B 114 ? 0.1218 0.1215 0.1826 0.0030  -0.0005 0.0106  114 GLU   B O   
5853 C  CB  . GLU   B 114 ? 0.1254 0.1284 0.1853 -0.0010 0.0110  0.0092  114 GLU   B CB  
5854 C  CG  . GLU   B 114 ? 0.1345 0.1278 0.1861 -0.0026 0.0077  0.0055  114 GLU   B CG  
5855 C  CD  . GLU   B 114 ? 0.1339 0.1311 0.1948 -0.0060 0.0097  0.0120  114 GLU   B CD  
5856 O  OE1 . GLU   B 114 ? 0.1283 0.1491 0.1927 -0.0076 0.0179  0.0097  114 GLU   B OE1 
5857 O  OE2 . GLU   B 114 ? 0.1331 0.1497 0.2024 -0.0177 0.0142  0.0063  114 GLU   B OE2 
5864 N  N   . ASN   B 115 ? 0.1257 0.1150 0.1670 -0.0028 0.0017  0.0053  115 ASN   B N   
5865 C  CA  . ASN   B 115 ? 0.1299 0.1230 0.1548 -0.0030 0.0010  0.0100  115 ASN   B CA  
5866 C  C   . ASN   B 115 ? 0.1268 0.1177 0.1489 -0.0096 0.0020  -0.0007 115 ASN   B C   
5867 O  O   . ASN   B 115 ? 0.1374 0.1205 0.1707 -0.0108 0.0065  0.0002  115 ASN   B O   
5868 C  CB  . ASN   B 115 ? 0.1363 0.1351 0.1643 -0.0110 0.0051  0.0034  115 ASN   B CB  
5869 C  CG  . ASN   B 115 ? 0.1500 0.1444 0.1624 0.0042  0.0009  -0.0034 115 ASN   B CG  
5870 O  OD1 . ASN   B 115 ? 0.1887 0.1591 0.1814 0.0017  0.0088  -0.0084 115 ASN   B OD1 
5871 N  ND2 . ASN   B 115 ? 0.1489 0.1547 0.1533 -0.0035 0.0063  0.0095  115 ASN   B ND2 
5878 N  N   . PHE   B 116 ? 0.1300 0.1195 0.1436 -0.0031 0.0037  0.0069  116 PHE   B N   
5879 C  CA  . PHE   B 116 ? 0.1328 0.1224 0.1562 -0.0058 0.0031  -0.0028 116 PHE   B CA  
5880 C  C   . PHE   B 116 ? 0.1306 0.1090 0.1571 -0.0078 0.0049  0.0008  116 PHE   B C   
5881 O  O   . PHE   B 116 ? 0.1331 0.1269 0.1623 -0.0027 -0.0013 0.0052  116 PHE   B O   
5882 C  CB  . PHE   B 116 ? 0.1292 0.1170 0.1536 -0.0048 -0.0050 0.0043  116 PHE   B CB  
5883 C  CG  . PHE   B 116 ? 0.1278 0.1173 0.1536 -0.0066 0.0070  0.0055  116 PHE   B CG  
5884 C  CD1 . PHE   B 116 ? 0.1317 0.1249 0.1747 -0.0053 0.0010  0.0010  116 PHE   B CD1 
5885 C  CD2 . PHE   B 116 ? 0.1337 0.1268 0.1604 -0.0045 0.0013  0.0029  116 PHE   B CD2 
5886 C  CE1 . PHE   B 116 ? 0.1274 0.1275 0.1748 -0.0047 -0.0124 0.0041  116 PHE   B CE1 
5887 C  CE2 . PHE   B 116 ? 0.1305 0.1273 0.1557 0.0009  0.0011  0.0027  116 PHE   B CE2 
5888 C  CZ  . PHE   B 116 ? 0.1242 0.1298 0.1660 -0.0001 -0.0069 0.0056  116 PHE   B CZ  
5898 N  N   . ASN   B 117 ? 0.1251 0.1157 0.1740 -0.0070 -0.0031 0.0048  117 ASN   B N   
5899 C  CA  . ASN   B 117 ? 0.1311 0.1205 0.1801 -0.0052 -0.0058 -0.0027 117 ASN   B CA  
5900 C  C   . ASN   B 117 ? 0.1380 0.1161 0.1925 -0.0023 -0.0071 0.0068  117 ASN   B C   
5901 O  O   . ASN   B 117 ? 0.1454 0.1229 0.2118 -0.0067 -0.0249 0.0130  117 ASN   B O   
5902 C  CB  . ASN   B 117 ? 0.1355 0.1227 0.1753 -0.0030 -0.0086 -0.0071 117 ASN   B CB  
5903 C  CG  . ASN   B 117 ? 0.1320 0.1241 0.1831 -0.0003 -0.0044 -0.0009 117 ASN   B CG  
5904 O  OD1 . ASN   B 117 ? 0.1485 0.1339 0.1841 -0.0115 0.0027  -0.0097 117 ASN   B OD1 
5905 N  ND2 . ASN   B 117 ? 0.1371 0.1238 0.1811 -0.0039 -0.0013 0.0030  117 ASN   B ND2 
5912 N  N   . GLN   B 118 ? 0.1407 0.1135 0.1746 -0.0105 -0.0090 0.0002  118 GLN   B N   
5913 C  CA  . GLN   B 118 ? 0.1463 0.1181 0.1855 0.0024  -0.0100 0.0025  118 GLN   B CA  
5914 C  C   . GLN   B 118 ? 0.1422 0.1202 0.1897 0.0029  -0.0091 0.0034  118 GLN   B C   
5915 O  O   . GLN   B 118 ? 0.1631 0.1201 0.2228 -0.0083 0.0020  0.0075  118 GLN   B O   
5916 C  CB  . GLN   B 118 ? 0.1475 0.1261 0.1940 -0.0003 -0.0157 0.0012  118 GLN   B CB  
5917 C  CG  . GLN   B 118 ? 0.1542 0.1279 0.1869 0.0035  -0.0064 -0.0059 118 GLN   B CG  
5918 C  CD  . GLN   B 118 ? 0.1585 0.1186 0.1873 0.0015  -0.0071 -0.0094 118 GLN   B CD  
5919 O  OE1 . GLN   B 118 ? 0.1627 0.1234 0.2154 0.0031  0.0128  0.0009  118 GLN   B OE1 
5920 N  NE2 . GLN   B 118 ? 0.1635 0.1222 0.1921 0.0003  -0.0105 0.0044  118 GLN   B NE2 
5929 N  N   . HIS   B 119 ? 0.1448 0.1295 0.1523 -0.0061 -0.0066 0.0053  119 HIS   B N   
5930 C  CA  . HIS   B 119 ? 0.1525 0.1401 0.1463 -0.0034 -0.0173 0.0035  119 HIS   B CA  
5931 C  C   . HIS   B 119 ? 0.1582 0.1377 0.1466 -0.0047 -0.0236 0.0100  119 HIS   B C   
5932 O  O   . HIS   B 119 ? 0.1621 0.1370 0.1641 -0.0276 -0.0148 0.0059  119 HIS   B O   
5933 C  CB  . HIS   B 119 ? 0.1583 0.1539 0.1503 -0.0024 -0.0174 -0.0019 119 HIS   B CB  
5934 C  CG  . HIS   B 119 ? 0.1604 0.1733 0.1749 0.0124  -0.0374 -0.0164 119 HIS   B CG  
5935 N  ND1 . HIS   B 119 ? 0.1761 0.1896 0.2099 0.0034  -0.0451 -0.0354 119 HIS   B ND1 
5936 C  CD2 . HIS   B 119 ? 0.1757 0.1864 0.1815 0.0386  -0.0435 -0.0235 119 HIS   B CD2 
5937 C  CE1 . HIS   B 119 ? 0.1947 0.2044 0.2131 0.0171  -0.0539 -0.0482 119 HIS   B CE1 
5938 N  NE2 . HIS   B 119 ? 0.1992 0.2096 0.1941 0.0342  -0.0457 -0.0432 119 HIS   B NE2 
5946 N  N   . GLU   B 120 ? 0.1768 0.1440 0.1463 -0.0064 -0.0284 0.0151  120 GLU   B N   
5947 C  CA  . GLU   B 120 ? 0.1996 0.1560 0.1593 -0.0031 -0.0428 0.0286  120 GLU   B CA  
5948 C  C   . GLU   B 120 ? 0.1773 0.1442 0.1438 -0.0190 -0.0334 0.0200  120 GLU   B C   
5949 O  O   . GLU   B 120 ? 0.1734 0.1584 0.1524 -0.0115 -0.0316 0.0117  120 GLU   B O   
5950 C  CB  . GLU   B 120 ? 0.2653 0.1934 0.2348 0.0204  -0.0699 0.0487  120 GLU   B CB  
5951 C  CG  . GLU   B 120 ? 0.3206 0.2585 0.3407 0.0293  -0.0921 0.0563  120 GLU   B CG  
5952 C  CD  . GLU   B 120 ? 0.3628 0.3272 0.4501 0.0295  -0.0987 0.0637  120 GLU   B CD  
5953 O  OE1 . GLU   B 120 ? 0.3747 0.3383 0.4869 0.0246  -0.0942 0.0734  120 GLU   B OE1 
5954 O  OE2 . GLU   B 120 ? 0.3886 0.3485 0.5069 0.0284  -0.0976 0.0584  120 GLU   B OE2 
5961 N  N   . VAL   B 121 ? 0.1672 0.1402 0.1511 -0.0219 -0.0156 0.0233  121 VAL   B N   
5962 C  CA  . VAL   B 121 ? 0.1601 0.1539 0.1390 -0.0187 -0.0168 0.0142  121 VAL   B CA  
5963 C  C   . VAL   B 121 ? 0.1536 0.1516 0.1434 -0.0241 -0.0200 0.0160  121 VAL   B C   
5964 O  O   . VAL   B 121 ? 0.1590 0.1447 0.1621 -0.0320 -0.0236 0.0119  121 VAL   B O   
5965 C  CB  . VAL   B 121 ? 0.1792 0.1939 0.1574 -0.0068 -0.0190 0.0192  121 VAL   B CB  
5966 C  CG1 . VAL   B 121 ? 0.1784 0.2073 0.1927 -0.0174 -0.0180 0.0179  121 VAL   B CG1 
5967 C  CG2 . VAL   B 121 ? 0.2115 0.2147 0.1564 0.0071  -0.0237 0.0126  121 VAL   B CG2 
5977 N  N   . LEU   B 122 ? 0.1516 0.1404 0.1320 -0.0166 -0.0204 0.0088  122 LEU   B N   
5978 C  CA  . LEU   B 122 ? 0.1414 0.1493 0.1204 -0.0189 -0.0139 0.0078  122 LEU   B CA  
5979 C  C   . LEU   B 122 ? 0.1428 0.1400 0.1331 -0.0279 -0.0146 0.0059  122 LEU   B C   
5980 O  O   . LEU   B 122 ? 0.1458 0.1384 0.1670 -0.0296 -0.0237 -0.0023 122 LEU   B O   
5981 C  CB  . LEU   B 122 ? 0.1600 0.1554 0.1647 -0.0038 -0.0171 0.0133  122 LEU   B CB  
5982 C  CG  . LEU   B 122 ? 0.1527 0.1593 0.1546 -0.0146 -0.0076 0.0085  122 LEU   B CG  
5983 C  CD1 . LEU   B 122 ? 0.1569 0.1797 0.1644 -0.0210 -0.0158 0.0045  122 LEU   B CD1 
5984 C  CD2 . LEU   B 122 ? 0.1585 0.1611 0.1444 -0.0088 -0.0034 0.0026  122 LEU   B CD2 
5996 N  N   . LEU   B 123 ? 0.1437 0.1313 0.1241 -0.0214 -0.0143 0.0120  123 LEU   B N   
5997 C  CA  . LEU   B 123 ? 0.1464 0.1326 0.1346 -0.0244 -0.0213 0.0027  123 LEU   B CA  
5998 C  C   . LEU   B 123 ? 0.1389 0.1305 0.1243 -0.0282 -0.0174 0.0021  123 LEU   B C   
5999 O  O   . LEU   B 123 ? 0.1536 0.1327 0.1226 -0.0318 -0.0155 0.0059  123 LEU   B O   
6000 C  CB  . LEU   B 123 ? 0.1502 0.1276 0.1499 -0.0253 -0.0128 0.0022  123 LEU   B CB  
6001 C  CG  . LEU   B 123 ? 0.1439 0.1349 0.1641 -0.0194 -0.0068 0.0062  123 LEU   B CG  
6002 C  CD1 . LEU   B 123 ? 0.1497 0.1362 0.1691 -0.0163 0.0034  -0.0106 123 LEU   B CD1 
6003 C  CD2 . LEU   B 123 ? 0.1557 0.1422 0.1838 -0.0153 -0.0019 0.0213  123 LEU   B CD2 
6015 N  N   . ALA   B 124 ? 0.1392 0.1250 0.1310 -0.0226 -0.0030 -0.0041 124 ALA   B N   
6016 C  CA  . ALA   B 124 ? 0.1307 0.1282 0.1368 -0.0156 -0.0058 0.0005  124 ALA   B CA  
6017 C  C   . ALA   B 124 ? 0.1257 0.1266 0.1384 -0.0201 -0.0073 0.0073  124 ALA   B C   
6018 O  O   . ALA   B 124 ? 0.1413 0.1290 0.1501 -0.0142 -0.0111 -0.0005 124 ALA   B O   
6019 C  CB  . ALA   B 124 ? 0.1361 0.1342 0.1473 -0.0062 0.0042  0.0057  124 ALA   B CB  
6025 N  N   . PRO   B 125 ? 0.1366 0.1247 0.1380 -0.0167 -0.0143 0.0147  125 PRO   B N   
6026 C  CA  . PRO   B 125 ? 0.1513 0.1309 0.1394 -0.0186 -0.0118 0.0273  125 PRO   B CA  
6027 C  C   . PRO   B 125 ? 0.1449 0.1218 0.1587 -0.0175 -0.0043 0.0153  125 PRO   B C   
6028 O  O   . PRO   B 125 ? 0.1477 0.1253 0.1790 -0.0079 0.0009  0.0137  125 PRO   B O   
6029 C  CB  . PRO   B 125 ? 0.1508 0.1517 0.1578 -0.0167 -0.0171 0.0283  125 PRO   B CB  
6030 C  CG  . PRO   B 125 ? 0.1542 0.1544 0.1516 -0.0202 -0.0245 0.0143  125 PRO   B CG  
6031 C  CD  . PRO   B 125 ? 0.1458 0.1400 0.1351 -0.0266 -0.0113 0.0070  125 PRO   B CD  
6039 N  N   . LEU   B 126 ? 0.1506 0.1175 0.1932 -0.0136 0.0139  0.0093  126 LEU   B N   
6040 C  CA  . LEU   B 126 ? 0.1555 0.1246 0.2049 -0.0127 0.0280  0.0160  126 LEU   B CA  
6041 C  C   . LEU   B 126 ? 0.1497 0.1362 0.2008 0.0014  0.0284  0.0174  126 LEU   B C   
6042 O  O   . LEU   B 126 ? 0.1719 0.1621 0.2110 0.0189  -0.0035 -0.0030 126 LEU   B O   
6043 C  CB  . LEU   B 126 ? 0.1756 0.1330 0.2360 -0.0213 0.0287  0.0082  126 LEU   B CB  
6044 C  CG  . LEU   B 126 ? 0.1892 0.1403 0.2541 -0.0290 0.0300  -0.0160 126 LEU   B CG  
6045 C  CD1 . LEU   B 126 ? 0.2010 0.1528 0.3012 -0.0251 0.0283  -0.0168 126 LEU   B CD1 
6046 C  CD2 . LEU   B 126 ? 0.1882 0.1492 0.2528 -0.0330 0.0255  -0.0165 126 LEU   B CD2 
6058 N  N   . LEU   B 127 ? 0.1460 0.1289 0.2090 0.0041  0.0263  0.0147  127 LEU   B N   
6059 C  CA  . LEU   B 127 ? 0.1456 0.1372 0.2184 -0.0039 0.0216  0.0229  127 LEU   B CA  
6060 C  C   . LEU   B 127 ? 0.1374 0.1308 0.2125 0.0044  0.0187  0.0242  127 LEU   B C   
6061 O  O   . LEU   B 127 ? 0.1470 0.1386 0.2183 -0.0137 0.0159  0.0233  127 LEU   B O   
6062 C  CB  . LEU   B 127 ? 0.1562 0.1366 0.2122 -0.0057 0.0199  0.0209  127 LEU   B CB  
6063 C  CG  . LEU   B 127 ? 0.1709 0.1333 0.2137 0.0015  0.0267  0.0195  127 LEU   B CG  
6064 C  CD1 . LEU   B 127 ? 0.1783 0.1281 0.2202 0.0021  0.0178  0.0150  127 LEU   B CD1 
6065 C  CD2 . LEU   B 127 ? 0.1770 0.1422 0.2280 -0.0095 0.0181  0.0302  127 LEU   B CD2 
6077 N  N   . SER   B 128 ? 0.1438 0.1313 0.2087 0.0036  0.0076  0.0186  128 SER   B N   
6078 C  CA  . SER   B 128 ? 0.1617 0.1418 0.2146 0.0113  -0.0019 0.0253  128 SER   B CA  
6079 C  C   . SER   B 128 ? 0.1763 0.1426 0.2316 0.0085  -0.0231 0.0201  128 SER   B C   
6080 O  O   . SER   B 128 ? 0.1948 0.1474 0.2602 0.0061  -0.0204 0.0392  128 SER   B O   
6081 C  CB  . SER   B 128 ? 0.1741 0.1433 0.2093 0.0066  0.0050  0.0386  128 SER   B CB  
6082 O  OG  . SER   B 128 ? 0.1752 0.1570 0.2026 0.0102  0.0150  0.0364  128 SER   B OG  
6088 N  N   . ALA   B 129 ? 0.1813 0.1550 0.2638 0.0258  -0.0128 0.0033  129 ALA   B N   
6089 C  CA  . ALA   B 129 ? 0.1980 0.1583 0.2716 0.0318  -0.0089 -0.0033 129 ALA   B CA  
6090 C  C   . ALA   B 129 ? 0.1888 0.1437 0.2503 0.0192  0.0097  0.0085  129 ALA   B C   
6091 O  O   . ALA   B 129 ? 0.1786 0.1444 0.2526 0.0190  0.0034  0.0135  129 ALA   B O   
6092 C  CB  . ALA   B 129 ? 0.2194 0.1810 0.3025 0.0350  -0.0008 -0.0146 129 ALA   B CB  
6098 N  N   . GLY   B 130 ? 0.1837 0.1464 0.2468 0.0248  0.0113  -0.0004 130 GLY   B N   
6099 C  CA  . GLY   B 130 ? 0.1911 0.1572 0.2610 0.0187  0.0252  -0.0041 130 GLY   B CA  
6100 C  C   . GLY   B 130 ? 0.1929 0.1562 0.2620 0.0149  0.0170  0.0099  130 GLY   B C   
6101 O  O   . GLY   B 130 ? 0.2072 0.1741 0.2690 0.0177  0.0182  0.0233  130 GLY   B O   
6105 N  N   . ILE   B 131 ? 0.1871 0.1737 0.2731 0.0338  0.0114  0.0099  131 ILE   B N   
6106 C  CA  . ILE   B 131 ? 0.2041 0.1901 0.2710 0.0319  -0.0036 0.0197  131 ILE   B CA  
6107 C  C   . ILE   B 131 ? 0.2132 0.1824 0.2381 0.0199  -0.0013 0.0272  131 ILE   B C   
6108 O  O   . ILE   B 131 ? 0.2397 0.2004 0.2435 0.0224  -0.0125 0.0310  131 ILE   B O   
6109 C  CB  . ILE   B 131 ? 0.2094 0.2198 0.3025 0.0263  -0.0095 0.0210  131 ILE   B CB  
6110 C  CG1 . ILE   B 131 ? 0.2151 0.2377 0.3155 0.0026  -0.0013 0.0265  131 ILE   B CG1 
6111 C  CG2 . ILE   B 131 ? 0.2119 0.2340 0.3256 0.0330  -0.0109 0.0085  131 ILE   B CG2 
6112 C  CD1 . ILE   B 131 ? 0.2233 0.2563 0.3273 -0.0129 -0.0086 0.0301  131 ILE   B CD1 
6124 N  N   . PHE   B 132 ? 0.1971 0.1674 0.2220 0.0172  0.0070  0.0268  132 PHE   B N   
6125 C  CA  . PHE   B 132 ? 0.2080 0.1692 0.2170 0.0104  0.0324  0.0192  132 PHE   B CA  
6126 C  C   . PHE   B 132 ? 0.2269 0.1867 0.2335 0.0121  0.0394  0.0150  132 PHE   B C   
6127 O  O   . PHE   B 132 ? 0.2448 0.2104 0.2559 0.0077  0.0509  0.0260  132 PHE   B O   
6128 C  CB  . PHE   B 132 ? 0.1927 0.1650 0.1921 0.0134  0.0341  0.0273  132 PHE   B CB  
6129 C  CG  . PHE   B 132 ? 0.1883 0.1699 0.1884 0.0148  0.0296  0.0219  132 PHE   B CG  
6130 C  CD1 . PHE   B 132 ? 0.1936 0.1655 0.2162 0.0109  0.0223  0.0262  132 PHE   B CD1 
6131 C  CD2 . PHE   B 132 ? 0.1911 0.1747 0.1602 0.0236  0.0251  0.0261  132 PHE   B CD2 
6132 C  CE1 . PHE   B 132 ? 0.1983 0.1720 0.2299 0.0042  0.0193  0.0204  132 PHE   B CE1 
6133 C  CE2 . PHE   B 132 ? 0.1961 0.1765 0.1747 0.0206  0.0090  0.0257  132 PHE   B CE2 
6134 C  CZ  . PHE   B 132 ? 0.1954 0.1748 0.2131 0.0113  -0.0032 0.0298  132 PHE   B CZ  
6144 N  N   . GLY   B 133 ? 0.2207 0.1781 0.2356 0.0067  0.0260  0.0375  133 GLY   B N   
6145 C  CA  . GLY   B 133 ? 0.2272 0.1895 0.2568 -0.0148 0.0309  0.0477  133 GLY   B CA  
6146 C  C   . GLY   B 133 ? 0.2342 0.1921 0.2587 -0.0294 0.0333  0.0557  133 GLY   B C   
6147 O  O   . GLY   B 133 ? 0.2495 0.2056 0.2953 -0.0389 0.0298  0.0621  133 GLY   B O   
6151 N  N   . ALA   B 134 ? 0.2213 0.1830 0.2452 -0.0248 0.0353  0.0369  134 ALA   B N   
6152 C  CA  . ALA   B 134 ? 0.2176 0.1852 0.2590 -0.0148 0.0480  0.0247  134 ALA   B CA  
6153 C  C   . ALA   B 134 ? 0.2177 0.1769 0.2615 -0.0066 0.0430  0.0380  134 ALA   B C   
6154 O  O   . ALA   B 134 ? 0.2198 0.1987 0.2704 0.0057  0.0266  0.0300  134 ALA   B O   
6155 C  CB  . ALA   B 134 ? 0.2186 0.1854 0.2796 -0.0138 0.0392  0.0188  134 ALA   B CB  
6161 N  N   . ASP   B 135 ? 0.2325 0.1713 0.2693 -0.0095 0.0250  0.0474  135 ASP   B N   
6162 C  CA  . ASP   B 135 ? 0.2474 0.1657 0.2866 -0.0098 0.0115  0.0451  135 ASP   B CA  
6163 C  C   . ASP   B 135 ? 0.2295 0.1535 0.2685 -0.0018 0.0046  0.0351  135 ASP   B C   
6164 O  O   . ASP   B 135 ? 0.2182 0.1479 0.2742 -0.0037 0.0073  0.0364  135 ASP   B O   
6165 C  CB  . ASP   B 135 ? 0.2762 0.1717 0.3204 -0.0301 0.0095  0.0538  135 ASP   B CB  
6166 C  CG  . ASP   B 135 ? 0.3029 0.1731 0.3638 -0.0511 0.0038  0.0408  135 ASP   B CG  
6167 O  OD1 . ASP   B 135 ? 0.3106 0.1560 0.3549 -0.0286 -0.0101 0.0384  135 ASP   B OD1 
6168 O  OD2 . ASP   B 135 ? 0.3274 0.2062 0.4157 -0.0734 0.0088  0.0222  135 ASP   B OD2 
6173 N  N   . PRO   B 136 ? 0.2212 0.1560 0.2785 0.0149  -0.0109 0.0273  136 PRO   B N   
6174 C  CA  . PRO   B 136 ? 0.2005 0.1467 0.2829 0.0141  -0.0109 0.0126  136 PRO   B CA  
6175 C  C   . PRO   B 136 ? 0.1809 0.1368 0.2858 0.0165  -0.0075 0.0132  136 PRO   B C   
6176 O  O   . PRO   B 136 ? 0.1699 0.1328 0.2793 0.0107  0.0026  0.0064  136 PRO   B O   
6177 C  CB  . PRO   B 136 ? 0.2056 0.1676 0.2922 0.0244  -0.0136 0.0045  136 PRO   B CB  
6178 C  CG  . PRO   B 136 ? 0.2225 0.1772 0.3086 0.0273  -0.0061 0.0078  136 PRO   B CG  
6179 C  CD  . PRO   B 136 ? 0.2251 0.1681 0.3039 0.0323  -0.0004 0.0081  136 PRO   B CD  
6187 N  N   . ILE   B 137 ? 0.1935 0.1275 0.2884 0.0109  -0.0073 0.0068  137 ILE   B N   
6188 C  CA  . ILE   B 137 ? 0.1985 0.1261 0.3027 -0.0004 -0.0011 0.0083  137 ILE   B CA  
6189 C  C   . ILE   B 137 ? 0.1901 0.1318 0.2861 -0.0115 0.0131  0.0222  137 ILE   B C   
6190 O  O   . ILE   B 137 ? 0.1813 0.1355 0.2741 -0.0122 0.0084  0.0130  137 ILE   B O   
6191 C  CB  . ILE   B 137 ? 0.2255 0.1330 0.3537 -0.0020 -0.0021 0.0133  137 ILE   B CB  
6192 C  CG1 . ILE   B 137 ? 0.2510 0.1509 0.4016 0.0038  0.0072  0.0031  137 ILE   B CG1 
6193 C  CG2 . ILE   B 137 ? 0.2290 0.1391 0.3646 -0.0259 -0.0016 0.0184  137 ILE   B CG2 
6194 C  CD1 . ILE   B 137 ? 0.2732 0.1767 0.4363 0.0157  0.0073  0.0099  137 ILE   B CD1 
6206 N  N   . HIS   B 138 ? 0.1967 0.1316 0.2956 -0.0072 0.0266  0.0229  138 HIS   B N   
6207 C  CA  . HIS   B 138 ? 0.2049 0.1416 0.2953 -0.0053 0.0380  0.0299  138 HIS   B CA  
6208 C  C   . HIS   B 138 ? 0.1843 0.1428 0.2784 -0.0095 0.0368  0.0303  138 HIS   B C   
6209 O  O   . HIS   B 138 ? 0.1753 0.1430 0.2984 -0.0007 0.0421  0.0362  138 HIS   B O   
6210 C  CB  . HIS   B 138 ? 0.2294 0.1543 0.3076 -0.0071 0.0520  0.0232  138 HIS   B CB  
6211 C  CG  . HIS   B 138 ? 0.2487 0.1721 0.3132 -0.0089 0.0713  0.0435  138 HIS   B CG  
6212 N  ND1 . HIS   B 138 ? 0.2554 0.1942 0.3405 -0.0030 0.0817  0.0349  138 HIS   B ND1 
6213 C  CD2 . HIS   B 138 ? 0.2634 0.1827 0.3069 -0.0098 0.0768  0.0449  138 HIS   B CD2 
6214 C  CE1 . HIS   B 138 ? 0.2598 0.1929 0.3341 -0.0093 0.0855  0.0410  138 HIS   B CE1 
6215 N  NE2 . HIS   B 138 ? 0.2685 0.1836 0.3125 -0.0010 0.0837  0.0363  138 HIS   B NE2 
6223 N  N   . SER   B 139 ? 0.1798 0.1335 0.2634 0.0001  0.0291  0.0259  139 SER   B N   
6224 C  CA  . SER   B 139 ? 0.1766 0.1244 0.2515 -0.0053 0.0227  0.0153  139 SER   B CA  
6225 C  C   . SER   B 139 ? 0.1585 0.1200 0.2459 0.0002  0.0229  0.0162  139 SER   B C   
6226 O  O   . SER   B 139 ? 0.1588 0.1239 0.2390 0.0050  0.0061  0.0128  139 SER   B O   
6227 C  CB  . SER   B 139 ? 0.1833 0.1265 0.2537 0.0004  0.0079  0.0077  139 SER   B CB  
6228 O  OG  . SER   B 139 ? 0.1843 0.1253 0.2567 -0.0024 -0.0055 0.0254  139 SER   B OG  
6234 N  N   . LEU   B 140 ? 0.1553 0.1149 0.2412 -0.0018 0.0264  0.0026  140 LEU   B N   
6235 C  CA  . LEU   B 140 ? 0.1497 0.1219 0.2504 -0.0006 0.0196  0.0009  140 LEU   B CA  
6236 C  C   . LEU   B 140 ? 0.1410 0.1215 0.2708 -0.0023 0.0073  -0.0072 140 LEU   B C   
6237 O  O   . LEU   B 140 ? 0.1426 0.1227 0.2674 0.0005  0.0065  -0.0004 140 LEU   B O   
6238 C  CB  . LEU   B 140 ? 0.1484 0.1212 0.2566 -0.0075 0.0210  0.0010  140 LEU   B CB  
6239 C  CG  . LEU   B 140 ? 0.1563 0.1290 0.2520 -0.0100 0.0089  0.0068  140 LEU   B CG  
6240 C  CD1 . LEU   B 140 ? 0.1682 0.1346 0.2663 -0.0113 0.0176  0.0009  140 LEU   B CD1 
6241 C  CD2 . LEU   B 140 ? 0.1715 0.1425 0.2708 -0.0116 -0.0015 -0.0085 140 LEU   B CD2 
6253 N  N   . ARG   B 141 ? 0.1363 0.1224 0.2764 -0.0104 0.0078  -0.0005 141 ARG   B N   
6254 C  CA  . ARG   B 141 ? 0.1412 0.1253 0.3039 -0.0189 0.0225  -0.0012 141 ARG   B CA  
6255 C  C   . ARG   B 141 ? 0.1371 0.1203 0.2879 -0.0129 0.0181  -0.0020 141 ARG   B C   
6256 O  O   . ARG   B 141 ? 0.1434 0.1240 0.2892 -0.0160 0.0035  -0.0165 141 ARG   B O   
6257 C  CB  . ARG   B 141 ? 0.1635 0.1376 0.3210 -0.0223 0.0379  -0.0036 141 ARG   B CB  
6258 C  CG  . ARG   B 141 ? 0.1943 0.1662 0.3243 -0.0190 0.0430  -0.0035 141 ARG   B CG  
6259 C  CD  . ARG   B 141 ? 0.2343 0.1819 0.3181 -0.0165 0.0274  -0.0137 141 ARG   B CD  
6260 N  NE  . ARG   B 141 ? 0.2560 0.1805 0.3128 -0.0386 0.0196  -0.0171 141 ARG   B NE  
6261 C  CZ  . ARG   B 141 ? 0.2660 0.1705 0.2971 -0.0312 0.0311  -0.0253 141 ARG   B CZ  
6262 N  NH1 . ARG   B 141 ? 0.2855 0.1581 0.2813 -0.0305 0.0314  -0.0263 141 ARG   B NH1 
6263 N  NH2 . ARG   B 141 ? 0.2675 0.1831 0.3090 -0.0156 0.0144  -0.0240 141 ARG   B NH2 
6277 N  N   . VAL   B 142 ? 0.1415 0.1193 0.2715 -0.0072 0.0135  -0.0005 142 VAL   B N   
6278 C  CA  . VAL   B 142 ? 0.1393 0.1233 0.2657 -0.0083 0.0260  -0.0085 142 VAL   B CA  
6279 C  C   . VAL   B 142 ? 0.1363 0.1261 0.2659 -0.0023 0.0205  -0.0051 142 VAL   B C   
6280 O  O   . VAL   B 142 ? 0.1468 0.1190 0.2709 -0.0002 0.0162  -0.0055 142 VAL   B O   
6281 C  CB  . VAL   B 142 ? 0.1511 0.1349 0.2805 0.0003  0.0252  0.0064  142 VAL   B CB  
6282 C  CG1 . VAL   B 142 ? 0.1530 0.1340 0.2859 0.0071  0.0291  -0.0018 142 VAL   B CG1 
6283 C  CG2 . VAL   B 142 ? 0.1669 0.1349 0.2882 -0.0042 0.0194  0.0170  142 VAL   B CG2 
6293 N  N   . CYS   B 143 ? 0.1312 0.1238 0.2482 -0.0006 0.0127  0.0053  143 CYS   B N   
6294 C  CA  . CYS   B 143 ? 0.1301 0.1222 0.2520 -0.0055 0.0105  0.0020  143 CYS   B CA  
6295 C  C   . CYS   B 143 ? 0.1264 0.1293 0.2489 -0.0049 0.0111  -0.0026 143 CYS   B C   
6296 O  O   . CYS   B 143 ? 0.1341 0.1325 0.2406 0.0002  -0.0002 -0.0086 143 CYS   B O   
6297 C  CB  . CYS   B 143 ? 0.1427 0.1293 0.2469 -0.0045 0.0061  -0.0063 143 CYS   B CB  
6298 S  SG  . CYS   B 143 ? 0.1417 0.1441 0.2314 -0.0047 0.0079  0.0058  143 CYS   B SG  
6304 N  N   . VAL   B 144 ? 0.1343 0.1278 0.2602 -0.0146 0.0068  -0.0139 144 VAL   B N   
6305 C  CA  . VAL   B 144 ? 0.1432 0.1303 0.2801 -0.0172 0.0067  -0.0249 144 VAL   B CA  
6306 C  C   . VAL   B 144 ? 0.1322 0.1322 0.2888 -0.0092 0.0010  -0.0065 144 VAL   B C   
6307 O  O   . VAL   B 144 ? 0.1453 0.1545 0.3014 0.0046  -0.0071 0.0132  144 VAL   B O   
6308 C  CB  . VAL   B 144 ? 0.1593 0.1477 0.3391 -0.0190 -0.0033 -0.0401 144 VAL   B CB  
6309 C  CG1 . VAL   B 144 ? 0.1833 0.1879 0.3698 -0.0176 -0.0077 -0.0317 144 VAL   B CG1 
6310 C  CG2 . VAL   B 144 ? 0.1735 0.1491 0.3306 -0.0043 -0.0227 -0.0498 144 VAL   B CG2 
6320 N  N   . ASP   B 145 ? 0.1356 0.1274 0.2990 -0.0070 0.0031  -0.0181 145 ASP   B N   
6321 C  CA  . ASP   B 145 ? 0.1383 0.1322 0.3231 -0.0051 0.0189  -0.0136 145 ASP   B CA  
6322 C  C   . ASP   B 145 ? 0.1410 0.1269 0.3017 -0.0044 0.0120  -0.0121 145 ASP   B C   
6323 O  O   . ASP   B 145 ? 0.1434 0.1425 0.3508 -0.0136 0.0141  -0.0241 145 ASP   B O   
6324 C  CB  . ASP   B 145 ? 0.1505 0.1426 0.3588 -0.0164 0.0329  -0.0007 145 ASP   B CB  
6325 C  CG  . ASP   B 145 ? 0.1680 0.1482 0.3976 -0.0269 0.0371  -0.0063 145 ASP   B CG  
6326 O  OD1 . ASP   B 145 ? 0.1704 0.1494 0.4097 -0.0234 0.0092  -0.0188 145 ASP   B OD1 
6327 O  OD2 . ASP   B 145 ? 0.1958 0.1582 0.4226 -0.0320 0.0604  -0.0002 145 ASP   B OD2 
6332 N  N   . THR   B 146 ? 0.1339 0.1226 0.2579 -0.0122 0.0021  0.0051  146 THR   B N   
6333 C  CA  . THR   B 146 ? 0.1366 0.1298 0.2330 -0.0097 0.0067  -0.0089 146 THR   B CA  
6334 C  C   . THR   B 146 ? 0.1330 0.1285 0.2266 -0.0007 -0.0024 -0.0036 146 THR   B C   
6335 O  O   . THR   B 146 ? 0.1388 0.1315 0.2202 -0.0012 0.0011  -0.0023 146 THR   B O   
6336 C  CB  . THR   B 146 ? 0.1405 0.1295 0.2399 -0.0066 0.0175  -0.0037 146 THR   B CB  
6337 O  OG1 . THR   B 146 ? 0.1450 0.1283 0.2527 -0.0063 0.0245  0.0154  146 THR   B OG1 
6338 C  CG2 . THR   B 146 ? 0.1497 0.1333 0.2422 -0.0066 0.0206  -0.0117 146 THR   B CG2 
6346 N  N   . VAL   B 147 ? 0.1368 0.1341 0.2148 -0.0036 0.0049  -0.0039 147 VAL   B N   
6347 C  CA  . VAL   B 147 ? 0.1371 0.1307 0.2071 -0.0098 -0.0022 0.0019  147 VAL   B CA  
6348 C  C   . VAL   B 147 ? 0.1342 0.1264 0.2147 -0.0205 -0.0068 0.0028  147 VAL   B C   
6349 O  O   . VAL   B 147 ? 0.1492 0.1371 0.2242 -0.0252 -0.0287 -0.0059 147 VAL   B O   
6350 C  CB  . VAL   B 147 ? 0.1360 0.1429 0.1988 -0.0067 -0.0028 0.0004  147 VAL   B CB  
6351 C  CG1 . VAL   B 147 ? 0.1326 0.1555 0.1898 -0.0178 -0.0069 -0.0006 147 VAL   B CG1 
6352 C  CG2 . VAL   B 147 ? 0.1389 0.1425 0.2015 -0.0107 -0.0030 -0.0028 147 VAL   B CG2 
6362 N  N   . ARG   B 148 ? 0.1377 0.1266 0.1999 -0.0105 -0.0156 -0.0071 148 ARG   B N   
6363 C  CA  . ARG   B 148 ? 0.1468 0.1368 0.2021 -0.0111 -0.0243 -0.0047 148 ARG   B CA  
6364 C  C   . ARG   B 148 ? 0.1506 0.1392 0.1864 -0.0113 -0.0247 -0.0062 148 ARG   B C   
6365 O  O   . ARG   B 148 ? 0.1643 0.1738 0.1996 -0.0241 -0.0356 -0.0005 148 ARG   B O   
6366 C  CB  . ARG   B 148 ? 0.1474 0.1422 0.2089 -0.0048 -0.0320 -0.0136 148 ARG   B CB  
6367 C  CG  . ARG   B 148 ? 0.1478 0.1566 0.2203 -0.0150 -0.0237 -0.0298 148 ARG   B CG  
6368 C  CD  . ARG   B 148 ? 0.1515 0.1733 0.2283 0.0050  -0.0240 -0.0365 148 ARG   B CD  
6369 N  NE  . ARG   B 148 ? 0.1554 0.1751 0.2208 0.0236  -0.0314 -0.0272 148 ARG   B NE  
6370 C  CZ  . ARG   B 148 ? 0.1477 0.1664 0.1951 0.0164  -0.0222 -0.0207 148 ARG   B CZ  
6371 N  NH1 . ARG   B 148 ? 0.1430 0.1744 0.2042 -0.0002 0.0054  -0.0196 148 ARG   B NH1 
6372 N  NH2 . ARG   B 148 ? 0.1729 0.1552 0.1934 0.0184  -0.0113 -0.0127 148 ARG   B NH2 
6386 N  N   . THR   B 149 ? 0.1517 0.1368 0.1827 -0.0138 -0.0258 -0.0039 149 THR   B N   
6387 C  CA  . THR   B 149 ? 0.1539 0.1434 0.1838 -0.0142 -0.0245 0.0081  149 THR   B CA  
6388 C  C   . THR   B 149 ? 0.1527 0.1445 0.1729 -0.0183 -0.0263 0.0064  149 THR   B C   
6389 O  O   . THR   B 149 ? 0.1559 0.1451 0.1786 -0.0213 -0.0109 0.0002  149 THR   B O   
6390 C  CB  . THR   B 149 ? 0.1513 0.1376 0.1881 -0.0109 -0.0250 0.0061  149 THR   B CB  
6391 O  OG1 . THR   B 149 ? 0.1525 0.1484 0.1836 -0.0196 -0.0243 -0.0008 149 THR   B OG1 
6392 C  CG2 . THR   B 149 ? 0.1584 0.1457 0.1977 -0.0041 -0.0226 0.0040  149 THR   B CG2 
6400 N  N   . ASN   B 150 ? 0.1618 0.1442 0.1615 -0.0182 -0.0346 0.0035  150 ASN   B N   
6401 C  CA  . ASN   B 150 ? 0.1667 0.1612 0.1594 -0.0179 -0.0320 -0.0007 150 ASN   B CA  
6402 C  C   . ASN   B 150 ? 0.1595 0.1487 0.1580 -0.0185 -0.0239 0.0025  150 ASN   B C   
6403 O  O   . ASN   B 150 ? 0.1608 0.1474 0.1808 -0.0290 -0.0346 0.0013  150 ASN   B O   
6404 C  CB  . ASN   B 150 ? 0.1879 0.1888 0.1709 -0.0177 -0.0428 0.0103  150 ASN   B CB  
6405 C  CG  . ASN   B 150 ? 0.2120 0.2267 0.2100 -0.0209 -0.0459 0.0230  150 ASN   B CG  
6406 O  OD1 . ASN   B 150 ? 0.2196 0.2499 0.2239 -0.0311 -0.0545 0.0174  150 ASN   B OD1 
6407 N  ND2 . ASN   B 150 ? 0.2280 0.2454 0.2563 -0.0086 -0.0515 0.0630  150 ASN   B ND2 
6414 N  N   . VAL   B 151 ? 0.1503 0.1474 0.1653 -0.0189 -0.0256 0.0008  151 VAL   B N   
6415 C  CA  . VAL   B 151 ? 0.1484 0.1504 0.1690 -0.0212 -0.0213 0.0016  151 VAL   B CA  
6416 C  C   . VAL   B 151 ? 0.1463 0.1428 0.1642 -0.0307 -0.0270 0.0001  151 VAL   B C   
6417 O  O   . VAL   B 151 ? 0.1542 0.1502 0.1966 -0.0276 -0.0169 -0.0099 151 VAL   B O   
6418 C  CB  . VAL   B 151 ? 0.1741 0.1597 0.1852 -0.0092 -0.0165 -0.0034 151 VAL   B CB  
6419 C  CG1 . VAL   B 151 ? 0.1847 0.1659 0.2180 -0.0150 -0.0097 -0.0091 151 VAL   B CG1 
6420 C  CG2 . VAL   B 151 ? 0.1854 0.1724 0.1777 0.0011  -0.0147 0.0066  151 VAL   B CG2 
6430 N  N   . TYR   B 152 ? 0.1431 0.1339 0.1641 -0.0223 -0.0202 -0.0080 152 TYR   B N   
6431 C  CA  . TYR   B 152 ? 0.1467 0.1462 0.1595 -0.0316 -0.0157 -0.0073 152 TYR   B CA  
6432 C  C   . TYR   B 152 ? 0.1412 0.1342 0.1489 -0.0266 -0.0115 -0.0041 152 TYR   B C   
6433 O  O   . TYR   B 152 ? 0.1525 0.1414 0.1574 -0.0284 -0.0112 0.0015  152 TYR   B O   
6434 C  CB  . TYR   B 152 ? 0.1624 0.1617 0.1536 -0.0295 -0.0167 0.0030  152 TYR   B CB  
6435 C  CG  . TYR   B 152 ? 0.1797 0.1731 0.1460 -0.0356 -0.0189 0.0010  152 TYR   B CG  
6436 C  CD1 . TYR   B 152 ? 0.1922 0.1827 0.1470 -0.0350 -0.0222 0.0116  152 TYR   B CD1 
6437 C  CD2 . TYR   B 152 ? 0.1990 0.1873 0.1572 -0.0372 -0.0115 -0.0118 152 TYR   B CD2 
6438 C  CE1 . TYR   B 152 ? 0.2065 0.2041 0.1607 -0.0307 -0.0297 0.0212  152 TYR   B CE1 
6439 C  CE2 . TYR   B 152 ? 0.2114 0.2156 0.1595 -0.0372 -0.0194 -0.0195 152 TYR   B CE2 
6440 C  CZ  . TYR   B 152 ? 0.2135 0.2287 0.1526 -0.0358 -0.0444 0.0110  152 TYR   B CZ  
6441 O  OH  . TYR   B 152 ? 0.2318 0.2619 0.1920 -0.0276 -0.0491 0.0190  152 TYR   B OH  
6451 N  N   . LEU   B 153 ? 0.1517 0.1331 0.1494 -0.0287 -0.0121 -0.0037 153 LEU   B N   
6452 C  CA  . LEU   B 153 ? 0.1543 0.1281 0.1508 -0.0247 -0.0050 -0.0098 153 LEU   B CA  
6453 C  C   . LEU   B 153 ? 0.1567 0.1278 0.1722 -0.0259 -0.0053 -0.0161 153 LEU   B C   
6454 O  O   . LEU   B 153 ? 0.1613 0.1495 0.1865 -0.0159 -0.0034 -0.0343 153 LEU   B O   
6455 C  CB  . LEU   B 153 ? 0.1530 0.1244 0.1675 -0.0263 0.0004  -0.0150 153 LEU   B CB  
6456 C  CG  . LEU   B 153 ? 0.1524 0.1367 0.1963 -0.0218 0.0039  -0.0098 153 LEU   B CG  
6457 C  CD1 . LEU   B 153 ? 0.1567 0.1579 0.2131 -0.0234 0.0058  -0.0016 153 LEU   B CD1 
6458 C  CD2 . LEU   B 153 ? 0.1541 0.1478 0.1899 -0.0234 0.0177  0.0025  153 LEU   B CD2 
6470 N  N   . ALA   B 154 ? 0.1523 0.1252 0.1813 -0.0118 -0.0106 -0.0206 154 ALA   B N   
6471 C  CA  . ALA   B 154 ? 0.1642 0.1423 0.1951 -0.0029 -0.0131 -0.0233 154 ALA   B CA  
6472 C  C   . ALA   B 154 ? 0.1713 0.1469 0.2027 0.0083  -0.0114 -0.0272 154 ALA   B C   
6473 O  O   . ALA   B 154 ? 0.1983 0.1493 0.2205 0.0032  0.0022  -0.0100 154 ALA   B O   
6474 C  CB  . ALA   B 154 ? 0.1572 0.1575 0.2116 -0.0055 -0.0060 -0.0264 154 ALA   B CB  
6480 N  N   . VAL   B 155 ? 0.1412 0.1368 0.2205 0.0018  0.0072  -0.0203 155 VAL   B N   
6481 C  CA  . VAL   B 155 ? 0.1355 0.1323 0.2392 0.0026  -0.0060 -0.0104 155 VAL   B CA  
6482 C  C   . VAL   B 155 ? 0.1360 0.1390 0.2366 -0.0022 -0.0036 -0.0201 155 VAL   B C   
6483 O  O   . VAL   B 155 ? 0.1553 0.1524 0.2675 0.0038  -0.0045 -0.0401 155 VAL   B O   
6484 C  CB  . VAL   B 155 ? 0.1440 0.1506 0.2626 -0.0020 -0.0170 0.0068  155 VAL   B CB  
6485 C  CG1 . VAL   B 155 ? 0.1499 0.1466 0.2605 -0.0065 -0.0131 0.0017  155 VAL   B CG1 
6486 C  CG2 . VAL   B 155 ? 0.1458 0.1619 0.2910 -0.0060 -0.0154 0.0357  155 VAL   B CG2 
6496 N  N   . PHE   B 156 ? 0.1306 0.1428 0.2520 -0.0009 -0.0069 -0.0176 156 PHE   B N   
6497 C  CA  . PHE   B 156 ? 0.1345 0.1497 0.2805 0.0095  -0.0045 -0.0237 156 PHE   B CA  
6498 C  C   . PHE   B 156 ? 0.1330 0.1564 0.3212 0.0154  -0.0089 -0.0389 156 PHE   B C   
6499 O  O   . PHE   B 156 ? 0.1548 0.1770 0.3438 0.0197  -0.0015 -0.0457 156 PHE   B O   
6500 C  CB  . PHE   B 156 ? 0.1477 0.1477 0.2780 0.0031  -0.0130 -0.0218 156 PHE   B CB  
6501 C  CG  . PHE   B 156 ? 0.1457 0.1588 0.2936 0.0012  -0.0126 -0.0013 156 PHE   B CG  
6502 C  CD1 . PHE   B 156 ? 0.1496 0.1843 0.3238 0.0067  -0.0007 0.0322  156 PHE   B CD1 
6503 C  CD2 . PHE   B 156 ? 0.1487 0.1684 0.2952 0.0048  -0.0088 0.0033  156 PHE   B CD2 
6504 C  CE1 . PHE   B 156 ? 0.1488 0.1958 0.3399 0.0030  -0.0002 0.0356  156 PHE   B CE1 
6505 C  CE2 . PHE   B 156 ? 0.1557 0.1853 0.3167 0.0092  -0.0104 0.0085  156 PHE   B CE2 
6506 C  CZ  . PHE   B 156 ? 0.1474 0.1932 0.3382 0.0117  -0.0177 0.0210  156 PHE   B CZ  
6516 N  N   . ASP   B 157 ? 0.1389 0.1492 0.3461 0.0154  -0.0178 -0.0268 157 ASP   B N   
6517 C  CA  . ASP   B 157 ? 0.1536 0.1557 0.3778 0.0100  -0.0268 -0.0335 157 ASP   B CA  
6518 C  C   . ASP   B 157 ? 0.1520 0.1544 0.3873 0.0094  -0.0251 -0.0514 157 ASP   B C   
6519 O  O   . ASP   B 157 ? 0.1419 0.1564 0.3688 0.0062  -0.0261 -0.0349 157 ASP   B O   
6520 C  CB  . ASP   B 157 ? 0.1742 0.1744 0.3931 0.0032  -0.0471 -0.0175 157 ASP   B CB  
6521 C  CG  . ASP   B 157 ? 0.2093 0.1866 0.4187 -0.0056 -0.0366 -0.0140 157 ASP   B CG  
6522 O  OD1 . ASP   B 157 ? 0.2248 0.1761 0.4353 0.0028  -0.0362 -0.0137 157 ASP   B OD1 
6523 O  OD2 . ASP   B 157 ? 0.2370 0.2076 0.4445 -0.0004 -0.0224 -0.0048 157 ASP   B OD2 
6528 N  N   . LYS   B 158 ? 0.1567 0.1805 0.3953 0.0067  -0.0104 -0.0783 158 LYS   B N   
6529 C  CA  . LYS   B 158 ? 0.1681 0.1982 0.4017 0.0088  0.0070  -0.0876 158 LYS   B CA  
6530 C  C   . LYS   B 158 ? 0.1724 0.1840 0.4132 0.0047  -0.0012 -0.0836 158 LYS   B C   
6531 O  O   . LYS   B 158 ? 0.1748 0.1803 0.4092 -0.0084 -0.0042 -0.0932 158 LYS   B O   
6532 C  CB  . LYS   B 158 ? 0.1930 0.2372 0.4034 0.0112  0.0180  -0.1036 158 LYS   B CB  
6533 C  CG  . LYS   B 158 ? 0.2295 0.2734 0.4127 0.0159  0.0225  -0.1140 158 LYS   B CG  
6534 C  CD  . LYS   B 158 ? 0.2559 0.3115 0.4267 0.0123  0.0234  -0.1054 158 LYS   B CD  
6535 C  CE  . LYS   B 158 ? 0.2812 0.3409 0.4416 0.0141  0.0201  -0.0995 158 LYS   B CE  
6536 N  NZ  . LYS   B 158 ? 0.2790 0.3484 0.4421 0.0098  0.0165  -0.0982 158 LYS   B NZ  
6550 N  N   . ASN   B 159 ? 0.1715 0.1723 0.4343 0.0065  -0.0097 -0.0705 159 ASN   B N   
6551 C  CA  . ASN   B 159 ? 0.1808 0.1609 0.4517 0.0155  -0.0245 -0.0538 159 ASN   B CA  
6552 C  C   . ASN   B 159 ? 0.1677 0.1464 0.4446 0.0107  -0.0446 -0.0425 159 ASN   B C   
6553 O  O   . ASN   B 159 ? 0.1697 0.1382 0.4625 -0.0016 -0.0499 -0.0349 159 ASN   B O   
6554 C  CB  . ASN   B 159 ? 0.2025 0.1779 0.4800 0.0243  -0.0312 -0.0459 159 ASN   B CB  
6555 C  CG  . ASN   B 159 ? 0.2319 0.1966 0.4947 0.0298  -0.0434 -0.0563 159 ASN   B CG  
6556 O  OD1 . ASN   B 159 ? 0.2497 0.2088 0.5000 0.0321  -0.0430 -0.0609 159 ASN   B OD1 
6557 N  ND2 . ASN   B 159 ? 0.2338 0.2066 0.5089 0.0327  -0.0477 -0.0556 159 ASN   B ND2 
6564 N  N   . LEU   B 160 ? 0.1571 0.1464 0.4139 0.0049  -0.0449 -0.0443 160 LEU   B N   
6565 C  CA  . LEU   B 160 ? 0.1553 0.1504 0.3751 0.0119  -0.0390 -0.0214 160 LEU   B CA  
6566 C  C   . LEU   B 160 ? 0.1503 0.1408 0.3653 0.0033  -0.0251 -0.0297 160 LEU   B C   
6567 O  O   . LEU   B 160 ? 0.1431 0.1409 0.3612 -0.0021 -0.0293 -0.0162 160 LEU   B O   
6568 C  CB  . LEU   B 160 ? 0.1599 0.1595 0.3525 0.0084  -0.0413 -0.0098 160 LEU   B CB  
6569 C  CG  . LEU   B 160 ? 0.1575 0.1700 0.3252 0.0065  -0.0336 -0.0061 160 LEU   B CG  
6570 C  CD1 . LEU   B 160 ? 0.1727 0.1917 0.3201 -0.0042 -0.0168 -0.0067 160 LEU   B CD1 
6571 C  CD2 . LEU   B 160 ? 0.1602 0.1760 0.3202 0.0209  -0.0267 -0.0155 160 LEU   B CD2 
6583 N  N   . TYR   B 161 ? 0.1436 0.1478 0.3631 -0.0017 -0.0018 -0.0423 161 TYR   B N   
6584 C  CA  . TYR   B 161 ? 0.1512 0.1516 0.3474 -0.0181 0.0098  -0.0470 161 TYR   B CA  
6585 C  C   . TYR   B 161 ? 0.1622 0.1525 0.3321 -0.0087 0.0178  -0.0393 161 TYR   B C   
6586 O  O   . TYR   B 161 ? 0.1676 0.1500 0.3157 -0.0176 0.0023  -0.0346 161 TYR   B O   
6587 C  CB  . TYR   B 161 ? 0.1682 0.1611 0.3380 -0.0264 0.0304  -0.0579 161 TYR   B CB  
6588 C  CG  . TYR   B 161 ? 0.1919 0.1689 0.3274 -0.0248 0.0380  -0.0579 161 TYR   B CG  
6589 C  CD1 . TYR   B 161 ? 0.1962 0.1694 0.3197 -0.0380 0.0404  -0.0585 161 TYR   B CD1 
6590 C  CD2 . TYR   B 161 ? 0.2104 0.1768 0.3188 -0.0215 0.0282  -0.0595 161 TYR   B CD2 
6591 C  CE1 . TYR   B 161 ? 0.2155 0.1920 0.3208 -0.0368 0.0368  -0.0604 161 TYR   B CE1 
6592 C  CE2 . TYR   B 161 ? 0.2285 0.1927 0.3225 -0.0240 0.0306  -0.0560 161 TYR   B CE2 
6593 C  CZ  . TYR   B 161 ? 0.2308 0.1972 0.3197 -0.0392 0.0291  -0.0478 161 TYR   B CZ  
6594 O  OH  . TYR   B 161 ? 0.2631 0.2202 0.3388 -0.0446 0.0243  -0.0430 161 TYR   B OH  
6604 N  N   . ASP   B 162 ? 0.1629 0.1523 0.3458 -0.0062 0.0029  -0.0530 162 ASP   B N   
6605 C  CA  . ASP   B 162 ? 0.1771 0.1584 0.3556 -0.0114 -0.0019 -0.0533 162 ASP   B CA  
6606 C  C   . ASP   B 162 ? 0.1697 0.1473 0.3503 -0.0126 -0.0051 -0.0466 162 ASP   B C   
6607 O  O   . ASP   B 162 ? 0.1734 0.1542 0.3483 -0.0206 -0.0239 -0.0313 162 ASP   B O   
6608 C  CB  . ASP   B 162 ? 0.1952 0.1749 0.3721 -0.0022 -0.0106 -0.0743 162 ASP   B CB  
6609 C  CG  . ASP   B 162 ? 0.2028 0.2021 0.3916 0.0100  -0.0142 -0.0924 162 ASP   B CG  
6610 O  OD1 . ASP   B 162 ? 0.2047 0.2214 0.3902 0.0033  -0.0027 -0.0957 162 ASP   B OD1 
6611 O  OD2 . ASP   B 162 ? 0.2155 0.2213 0.4179 0.0277  -0.0060 -0.0832 162 ASP   B OD2 
6616 N  N   . LYS   B 163 ? 0.1684 0.1330 0.3521 -0.0134 -0.0191 -0.0274 163 LYS   B N   
6617 C  CA  . LYS   B 163 ? 0.1797 0.1459 0.3507 -0.0214 -0.0183 -0.0099 163 LYS   B CA  
6618 C  C   . LYS   B 163 ? 0.1540 0.1423 0.3320 -0.0226 -0.0211 -0.0034 163 LYS   B C   
6619 O  O   . LYS   B 163 ? 0.1514 0.1498 0.3467 -0.0227 -0.0271 -0.0023 163 LYS   B O   
6620 C  CB  . LYS   B 163 ? 0.2246 0.1835 0.3856 -0.0183 -0.0257 0.0073  163 LYS   B CB  
6621 C  CG  . LYS   B 163 ? 0.2964 0.2713 0.4468 -0.0199 -0.0052 0.0115  163 LYS   B CG  
6622 C  CD  . LYS   B 163 ? 0.3590 0.3382 0.5060 -0.0273 0.0015  0.0077  163 LYS   B CD  
6623 C  CE  . LYS   B 163 ? 0.4002 0.3883 0.5479 -0.0338 0.0071  0.0072  163 LYS   B CE  
6624 N  NZ  . LYS   B 163 ? 0.4436 0.4436 0.5717 -0.0376 0.0096  0.0034  163 LYS   B NZ  
6638 N  N   . LEU   B 164 ? 0.1406 0.1372 0.3009 -0.0161 -0.0177 -0.0040 164 LEU   B N   
6639 C  CA  . LEU   B 164 ? 0.1440 0.1370 0.2785 -0.0132 -0.0247 -0.0026 164 LEU   B CA  
6640 C  C   . LEU   B 164 ? 0.1516 0.1342 0.2921 -0.0181 -0.0307 -0.0022 164 LEU   B C   
6641 O  O   . LEU   B 164 ? 0.1558 0.1501 0.3156 -0.0187 -0.0310 0.0033  164 LEU   B O   
6642 C  CB  . LEU   B 164 ? 0.1381 0.1331 0.2667 -0.0127 -0.0272 -0.0050 164 LEU   B CB  
6643 C  CG  . LEU   B 164 ? 0.1513 0.1530 0.2678 -0.0087 -0.0119 -0.0012 164 LEU   B CG  
6644 C  CD1 . LEU   B 164 ? 0.1567 0.1486 0.2541 -0.0140 -0.0238 -0.0032 164 LEU   B CD1 
6645 C  CD2 . LEU   B 164 ? 0.1675 0.1898 0.2807 -0.0102 0.0106  -0.0175 164 LEU   B CD2 
6657 N  N   . VAL   B 165 ? 0.1885 0.1365 0.3063 -0.0194 -0.0390 -0.0109 165 VAL   B N   
6658 C  CA  . VAL   B 165 ? 0.2183 0.1554 0.3135 -0.0267 -0.0571 -0.0089 165 VAL   B CA  
6659 C  C   . VAL   B 165 ? 0.2472 0.1691 0.3434 -0.0347 -0.0837 -0.0099 165 VAL   B C   
6660 O  O   . VAL   B 165 ? 0.2669 0.1841 0.3522 -0.0383 -0.0915 -0.0053 165 VAL   B O   
6661 C  CB  . VAL   B 165 ? 0.2360 0.1701 0.3082 -0.0090 -0.0270 -0.0213 165 VAL   B CB  
6662 C  CG1 . VAL   B 165 ? 0.2503 0.1802 0.3314 -0.0089 -0.0168 -0.0179 165 VAL   B CG1 
6663 C  CG2 . VAL   B 165 ? 0.2304 0.1697 0.3007 -0.0024 -0.0112 -0.0216 165 VAL   B CG2 
6673 N  N   . SER   B 166 ? 0.2500 0.1552 0.3773 -0.0352 -0.0885 -0.0258 166 SER   B N   
6674 C  CA  . SER   B 166 ? 0.2475 0.1575 0.4210 -0.0333 -0.0762 -0.0306 166 SER   B CA  
6675 C  C   . SER   B 166 ? 0.2338 0.1619 0.4309 -0.0366 -0.0766 -0.0066 166 SER   B C   
6676 O  O   . SER   B 166 ? 0.2391 0.1901 0.4612 -0.0524 -0.0927 -0.0239 166 SER   B O   
6677 C  CB  . SER   B 166 ? 0.2448 0.1657 0.4468 -0.0247 -0.0706 -0.0398 166 SER   B CB  
6678 O  OG  . SER   B 166 ? 0.2286 0.1630 0.4617 -0.0202 -0.0709 -0.0186 166 SER   B OG  
6684 N  N   . SER   B 167 ? 0.2114 0.1595 0.3997 -0.0411 -0.0763 0.0320  167 SER   B N   
6685 C  CA  . SER   B 167 ? 0.1988 0.1733 0.3816 -0.0355 -0.0493 0.0343  167 SER   B CA  
6686 C  C   . SER   B 167 ? 0.1952 0.1828 0.3619 -0.0502 -0.0477 0.0410  167 SER   B C   
6687 O  O   . SER   B 167 ? 0.1936 0.1952 0.3573 -0.0524 -0.0426 0.0394  167 SER   B O   
6688 C  CB  . SER   B 167 ? 0.1865 0.1787 0.3830 -0.0295 -0.0229 0.0312  167 SER   B CB  
6689 O  OG  . SER   B 167 ? 0.1840 0.1881 0.3716 -0.0217 -0.0055 0.0334  167 SER   B OG  
6695 N  N   . PHE   B 168 ? 0.1972 0.1759 0.3527 -0.0433 -0.0337 0.0505  168 PHE   B N   
6696 C  CA  . PHE   B 168 ? 0.1963 0.1758 0.3248 -0.0462 -0.0244 0.0288  168 PHE   B CA  
6697 C  C   . PHE   B 168 ? 0.1717 0.1645 0.2749 -0.0276 -0.0084 0.0130  168 PHE   B C   
6698 O  O   . PHE   B 168 ? 0.1993 0.1549 0.2728 -0.0017 -0.0071 -0.0053 168 PHE   B O   
6699 C  CB  . PHE   B 168 ? 0.2120 0.1765 0.3279 -0.0523 -0.0372 0.0445  168 PHE   B CB  
6700 C  CG  . PHE   B 168 ? 0.2343 0.1651 0.3174 -0.0541 -0.0376 0.0180  168 PHE   B CG  
6701 C  CD1 . PHE   B 168 ? 0.2621 0.1756 0.3232 -0.0452 -0.0435 0.0142  168 PHE   B CD1 
6702 C  CD2 . PHE   B 168 ? 0.2229 0.1564 0.3167 -0.0487 -0.0423 0.0130  168 PHE   B CD2 
6703 C  CE1 . PHE   B 168 ? 0.2740 0.1808 0.3174 -0.0365 -0.0361 0.0174  168 PHE   B CE1 
6704 C  CE2 . PHE   B 168 ? 0.2498 0.1663 0.3181 -0.0328 -0.0463 0.0098  168 PHE   B CE2 
6705 C  CZ  . PHE   B 168 ? 0.2621 0.1640 0.3211 -0.0233 -0.0473 0.0262  168 PHE   B CZ  
6715 N  N   . LEU   B 169 ? 0.1811 0.1768 0.2624 -0.0038 0.0002  -0.0014 169 LEU   B N   
6716 C  CA  . LEU   B 169 ? 0.2033 0.2064 0.3015 -0.0076 -0.0050 -0.0289 169 LEU   B CA  
6717 C  C   . LEU   B 169 ? 0.2319 0.2284 0.3506 0.0058  -0.0066 -0.0517 169 LEU   B C   
6718 O  O   . LEU   B 169 ? 0.2510 0.2475 0.3998 0.0039  -0.0065 -0.0688 169 LEU   B O   
6719 C  CB  . LEU   B 169 ? 0.2217 0.2508 0.3139 -0.0146 -0.0136 -0.0038 169 LEU   B CB  
6720 C  CG  . LEU   B 169 ? 0.2571 0.2876 0.3531 -0.0037 -0.0068 0.0076  169 LEU   B CG  
6721 C  CD1 . LEU   B 169 ? 0.2711 0.3068 0.3594 -0.0028 -0.0074 0.0240  169 LEU   B CD1 
6722 C  CD2 . LEU   B 169 ? 0.2532 0.2973 0.3529 0.0110  0.0066  -0.0058 169 LEU   B CD2 
6723 O  OXT . LEU   B 169 ? 0.2555 0.2433 0.3491 0.0343  0.0031  -0.0488 169 LEU   B OXT 
6735 C  C1  T TFA   C .   ? 0.1601 0.1545 0.1221 -0.0030 0.0131  0.0146  201 TFA   A C1  
6736 C  C2  T TFA   C .   ? 0.1802 0.1835 0.1699 -0.0090 0.0154  -0.0017 201 TFA   A C2  
6737 O  O   T TFA   C .   ? 0.1431 0.1466 0.1119 -0.0101 0.0085  0.0217  201 TFA   A O   
6738 F  F1  T TFA   C .   ? 0.1894 0.1903 0.2147 -0.0069 0.0141  -0.0124 201 TFA   A F1  
6739 F  F2  T TFA   C .   ? 0.1875 0.1939 0.1636 -0.0164 0.0214  0.0033  201 TFA   A F2  
6740 F  F3  T TFA   C .   ? 0.1900 0.1978 0.1989 -0.0158 0.0256  -0.0052 201 TFA   A F3  
6741 O  OXT T TFA   C .   ? 0.1550 0.1341 0.1103 0.0250  0.0083  0.0226  201 TFA   A OXT 
6742 N  N2  B A1A9V D .   ? 0.1222 0.1347 0.1024 -0.0057 -0.0008 0.0129  202 A1A9V A N2  
6743 C  C3  B A1A9V D .   ? 0.1358 0.1352 0.1294 -0.0003 -0.0040 0.0157  202 A1A9V A C3  
6744 C  C6  B A1A9V D .   ? 0.1397 0.1599 0.1710 0.0075  -0.0119 0.0312  202 A1A9V A C6  
6745 C  C9  B A1A9V D .   ? 0.1220 0.1292 0.1072 -0.0050 -0.0066 0.0219  202 A1A9V A C9  
6746 C  C12 B A1A9V D .   ? 0.1194 0.1355 0.1022 -0.0085 -0.0001 0.0176  202 A1A9V A C12 
6747 C  C14 B A1A9V D .   ? 0.1183 0.1388 0.1088 -0.0046 -0.0166 0.0180  202 A1A9V A C14 
6748 C  C1  B A1A9V D .   ? 0.1373 0.1221 0.1462 -0.0033 0.0127  -0.0002 202 A1A9V A C1  
6749 C  C10 B A1A9V D .   ? 0.1365 0.1437 0.1117 -0.0006 0.0067  0.0121  202 A1A9V A C10 
6750 C  C11 B A1A9V D .   ? 0.1270 0.1391 0.1043 -0.0042 -0.0054 0.0047  202 A1A9V A C11 
6751 C  C13 B A1A9V D .   ? 0.1169 0.1386 0.0993 -0.0046 -0.0052 0.0182  202 A1A9V A C13 
6752 C  C2  B A1A9V D .   ? 0.1315 0.1195 0.1152 -0.0077 0.0017  0.0127  202 A1A9V A C2  
6753 C  C4  B A1A9V D .   ? 0.1384 0.1283 0.1526 0.0057  -0.0074 0.0279  202 A1A9V A C4  
6754 C  C5  B A1A9V D .   ? 0.1411 0.1451 0.1686 0.0050  -0.0065 0.0316  202 A1A9V A C5  
6755 C  C7  B A1A9V D .   ? 0.1478 0.1704 0.1703 0.0022  -0.0189 0.0163  202 A1A9V A C7  
6756 C  C8  B A1A9V D .   ? 0.1510 0.1607 0.1545 0.0076  -0.0159 0.0104  202 A1A9V A C8  
6757 N  N1  B A1A9V D .   ? 0.1172 0.1131 0.1097 -0.0033 -0.0094 0.0237  202 A1A9V A N1  
6758 N  N3  B A1A9V D .   ? 0.1370 0.1460 0.1086 -0.0004 0.0068  0.0180  202 A1A9V A N3  
6759 N  N4  B A1A9V D .   ? 0.1235 0.1343 0.0922 0.0019  -0.0174 0.0133  202 A1A9V A N4  
6760 N  N5  B A1A9V D .   ? 0.1391 0.1378 0.1360 -0.0023 -0.0094 0.0204  202 A1A9V A N5  
6761 O  O1  B A1A9V D .   ? 0.1351 0.1304 0.1490 -0.0068 0.0091  -0.0051 202 A1A9V A O1  
6784 CL CL  B CL    E .   ? 0.1460 0.1334 0.1997 -0.0081 0.0052  0.0150  203 CL    A CL  
6785 O  O   . HOH   F .   ? 0.4357 0.8386 0.4635 -0.1121 0.0561  0.1157  301 HOH   A O   
6786 O  O   . HOH   F .   ? 0.1535 0.4932 0.2230 -0.0105 0.0312  0.0364  302 HOH   A O   
6787 O  O   . HOH   F .   ? 0.7154 0.5446 0.3875 -0.1660 -0.0310 0.1747  303 HOH   A O   
6788 O  O   . HOH   F .   ? 0.3137 0.3268 0.1704 -0.0260 0.0408  0.0596  304 HOH   A O   
6789 O  O   . HOH   F .   ? 0.6220 0.4978 0.3312 0.2025  -0.1423 0.0660  305 HOH   A O   
6790 O  O   A HOH   F .   ? 0.2378 0.2287 0.3454 0.0453  -0.0447 -0.0104 306 HOH   A O   
6791 O  O   . HOH   F .   ? 0.3157 0.2689 0.4537 -0.0381 -0.1396 0.1352  307 HOH   A O   
6792 O  O   . HOH   F .   ? 0.5801 0.6302 0.4771 -0.1207 -0.1196 -0.1092 308 HOH   A O   
6793 O  O   . HOH   F .   ? 0.5770 0.5002 0.4681 -0.0444 0.1516  0.2408  309 HOH   A O   
6794 O  O   B HOH   F .   ? 0.2368 0.3044 0.3756 -0.0824 0.0116  0.1366  310 HOH   A O   
6795 O  O   . HOH   F .   ? 0.4313 0.3713 0.4000 -0.0122 0.0797  0.0019  311 HOH   A O   
6796 O  O   . HOH   F .   ? 0.5695 0.4163 0.5357 -0.0546 0.1522  0.1557  312 HOH   A O   
6797 O  O   . HOH   F .   ? 0.3801 0.3348 0.2852 -0.1325 -0.0092 0.0907  313 HOH   A O   
6798 O  O   . HOH   F .   ? 0.6268 0.4578 0.3959 -0.0768 -0.0123 0.0736  314 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2098 0.1988 0.3804 -0.0490 0.0215  -0.0290 315 HOH   A O   
6800 O  O   . HOH   F .   ? 0.6088 0.5190 0.5057 0.0687  -0.0549 0.0524  316 HOH   A O   
6801 O  O   . HOH   F .   ? 0.5020 0.2650 0.2932 -0.1115 0.0586  0.0235  317 HOH   A O   
6802 O  O   . HOH   F .   ? 0.4643 0.5453 0.5134 0.1864  0.0937  -0.1337 318 HOH   A O   
6803 O  O   . HOH   F .   ? 0.1846 0.2820 0.2858 0.0314  -0.0145 -0.0223 319 HOH   A O   
6804 O  O   . HOH   F .   ? 0.1747 0.1662 0.1850 0.0168  -0.0209 0.0231  320 HOH   A O   
6805 O  O   A HOH   F .   ? 0.2265 0.3720 0.2455 0.0941  -0.0156 -0.0426 321 HOH   A O   
6806 O  O   B HOH   F .   ? 0.1949 0.2565 0.2593 -0.0390 0.0167  0.0260  322 HOH   A O   
6807 O  O   . HOH   F .   ? 0.6954 0.5340 0.3546 -0.0695 -0.0628 0.0818  323 HOH   A O   
6808 O  O   A HOH   F .   ? 0.2545 0.3310 0.4114 -0.0091 0.1057  0.1683  324 HOH   A O   
6809 O  O   A HOH   F .   ? 0.1805 0.2159 0.1807 -0.0215 0.0280  0.0451  325 HOH   A O   
6810 O  O   . HOH   F .   ? 0.3566 0.4154 0.3863 -0.1091 0.1336  0.0151  326 HOH   A O   
6811 O  O   . HOH   F .   ? 0.2312 0.1841 0.2448 0.0034  -0.0714 -0.0060 327 HOH   A O   
6812 O  O   . HOH   F .   ? 0.2546 0.5595 0.3805 0.0041  -0.0701 0.0805  328 HOH   A O   
6813 O  O   . HOH   F .   ? 0.2548 0.2221 0.2125 -0.0401 0.0172  -0.0150 329 HOH   A O   
6814 O  O   . HOH   F .   ? 0.1492 0.1525 0.2240 -0.0167 0.0016  0.0053  330 HOH   A O   
6815 O  O   B HOH   F .   ? 0.1450 0.1471 0.1542 0.0091  -0.0088 0.0454  331 HOH   A O   
6816 O  O   . HOH   F .   ? 0.1809 0.3717 0.4297 -0.0365 0.0556  -0.1100 332 HOH   A O   
6817 O  O   . HOH   F .   ? 0.2528 0.2182 0.2620 0.0387  0.0273  0.0306  333 HOH   A O   
6818 O  O   . HOH   F .   ? 0.4316 0.4150 0.4434 -0.1725 -0.1028 0.2187  334 HOH   A O   
6819 O  O   . HOH   F .   ? 0.5027 0.4943 0.2992 -0.1170 0.1257  0.1091  335 HOH   A O   
6820 O  O   . HOH   F .   ? 0.5090 0.5336 0.3336 0.0297  -0.0762 -0.1230 336 HOH   A O   
6821 O  O   B HOH   F .   ? 0.1561 0.1267 0.1638 -0.0030 0.0011  0.0082  337 HOH   A O   
6822 O  O   . HOH   F .   ? 0.5729 0.5180 0.5126 0.0156  0.2286  -0.1055 338 HOH   A O   
6823 O  O   . HOH   F .   ? 0.1631 0.1887 0.2316 0.0093  -0.0353 -0.0552 339 HOH   A O   
6824 O  O   A HOH   F .   ? 0.1388 0.2512 0.1640 0.0537  0.0266  0.0338  340 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2132 0.4812 0.3770 -0.0133 -0.0579 0.1824  341 HOH   A O   
6826 O  O   . HOH   F .   ? 0.4828 0.5991 0.4506 -0.1026 -0.0021 0.2616  342 HOH   A O   
6827 O  O   . HOH   F .   ? 0.2653 0.3247 0.3352 -0.0737 -0.0365 -0.0424 343 HOH   A O   
6828 O  O   . HOH   F .   ? 0.4572 0.1932 0.4487 0.0192  -0.2056 0.0253  344 HOH   A O   
6829 O  O   B HOH   F .   ? 0.1863 0.3335 0.2422 0.0364  -0.0718 0.0033  345 HOH   A O   
6830 O  O   . HOH   F .   ? 0.2133 0.1688 0.1530 -0.0071 0.0239  0.0182  346 HOH   A O   
6831 O  O   . HOH   F .   ? 0.2951 0.7632 0.5625 -0.0762 -0.0904 0.1664  347 HOH   A O   
6832 O  O   . HOH   F .   ? 0.3074 0.2970 0.3206 -0.0806 0.0286  -0.0363 348 HOH   A O   
6833 O  O   . HOH   F .   ? 0.3036 0.3351 0.2202 -0.0739 -0.0305 -0.0714 349 HOH   A O   
6834 O  O   . HOH   F .   ? 0.2816 0.3444 0.4492 -0.0616 -0.0790 -0.1003 350 HOH   A O   
6835 O  O   . HOH   F .   ? 0.2277 0.4280 0.3657 0.0994  -0.0657 -0.0125 351 HOH   A O   
6836 O  O   . HOH   F .   ? 0.1559 0.2316 0.2056 -0.0030 -0.0087 0.0593  352 HOH   A O   
6837 O  O   . HOH   F .   ? 0.3242 0.4347 0.2163 -0.0074 0.0608  0.0300  353 HOH   A O   
6838 O  O   . HOH   F .   ? 0.4954 0.2178 0.4571 0.0591  0.0415  0.0099  354 HOH   A O   
6839 O  O   . HOH   F .   ? 0.1915 0.2075 0.4582 0.0202  0.1190  -0.0162 355 HOH   A O   
6840 O  O   . HOH   F .   ? 0.2183 0.1618 0.2202 0.0282  -0.0264 0.0026  356 HOH   A O   
6841 O  O   . HOH   F .   ? 0.4241 0.4792 0.2019 -0.0577 -0.1234 0.0463  357 HOH   A O   
6842 O  O   B HOH   F .   ? 0.1797 0.1211 0.1650 0.0056  -0.0253 0.0259  358 HOH   A O   
6843 O  O   . HOH   F .   ? 0.1871 0.2400 0.2062 -0.0313 -0.0070 0.0872  359 HOH   A O   
6844 O  O   . HOH   F .   ? 0.3552 0.4029 0.3931 0.1622  0.0860  0.0533  360 HOH   A O   
6845 O  O   . HOH   F .   ? 0.2262 0.2170 0.4636 0.0214  -0.0756 0.0077  361 HOH   A O   
6846 O  O   . HOH   F .   ? 0.1370 0.1320 0.1335 0.0011  0.0087  0.0090  362 HOH   A O   
6847 O  O   . HOH   F .   ? 0.4321 0.2570 0.4436 -0.1409 0.1542  -0.0505 363 HOH   A O   
6848 O  O   A HOH   F .   ? 0.2263 0.4810 0.4678 0.0632  0.0557  0.1068  364 HOH   A O   
6849 O  O   . HOH   F .   ? 0.1705 0.1741 0.2071 -0.0224 0.0085  0.0384  365 HOH   A O   
6850 O  O   A HOH   F .   ? 0.3436 0.1718 0.1892 0.0320  0.0119  -0.0047 366 HOH   A O   
6851 O  O   . HOH   F .   ? 0.1502 0.1899 0.2475 0.0056  -0.0124 0.0100  367 HOH   A O   
6852 O  O   . HOH   F .   ? 0.2847 0.4347 0.2797 -0.0568 0.0596  0.0229  368 HOH   A O   
6853 O  O   . HOH   F .   ? 0.5851 0.4064 0.2848 0.0441  0.0112  0.1535  369 HOH   A O   
6854 O  O   . HOH   F .   ? 0.1574 0.1340 0.2187 -0.0075 0.0199  -0.0035 370 HOH   A O   
6855 O  O   . HOH   F .   ? 0.1864 0.1972 0.2456 -0.0244 0.0080  0.0371  371 HOH   A O   
6856 O  O   . HOH   F .   ? 0.2177 0.2649 0.3479 0.0292  0.0800  -0.0639 372 HOH   A O   
6857 O  O   . HOH   F .   ? 0.1468 0.1545 0.1471 -0.0070 -0.0109 -0.0013 373 HOH   A O   
6858 O  O   . HOH   F .   ? 0.3896 0.2142 0.2198 0.1143  0.0504  0.0265  374 HOH   A O   
6859 O  O   . HOH   F .   ? 0.3538 0.7119 0.4996 -0.0471 -0.1468 0.0826  375 HOH   A O   
6860 O  O   . HOH   F .   ? 0.8427 0.3896 0.6548 0.0014  -0.1337 0.0824  376 HOH   A O   
6861 O  O   . HOH   F .   ? 0.2546 0.1854 0.2379 0.0010  0.0133  0.0208  377 HOH   A O   
6862 O  O   . HOH   F .   ? 0.3060 0.6935 0.3289 0.1282  0.0465  -0.0901 378 HOH   A O   
6863 O  O   . HOH   F .   ? 0.2671 0.4583 0.3102 0.0702  0.0891  0.1974  379 HOH   A O   
6864 O  O   . HOH   F .   ? 0.1952 0.2372 0.2176 -0.0349 -0.0558 0.0604  380 HOH   A O   
6865 O  O   . HOH   F .   ? 0.1903 0.2724 0.2649 0.0438  0.0405  0.0855  381 HOH   A O   
6866 O  O   . HOH   F .   ? 0.2251 0.3871 0.3280 -0.0225 0.0044  0.0728  382 HOH   A O   
6867 O  O   B HOH   F .   ? 0.2473 0.3196 0.1325 0.0070  0.0448  -0.0098 383 HOH   A O   
6868 O  O   . HOH   F .   ? 0.4214 0.2562 0.4216 -0.1372 0.0864  0.0261  384 HOH   A O   
6869 O  O   B HOH   F .   ? 0.2587 0.3067 0.3647 0.0280  0.0280  -0.0434 385 HOH   A O   
6870 O  O   T HOH   F .   ? 0.1264 0.1194 0.2491 -0.0142 -0.0019 0.0565  386 HOH   A O   
6871 O  O   . HOH   F .   ? 0.1974 0.2174 0.2369 -0.0264 -0.0309 0.0740  387 HOH   A O   
6872 O  O   . HOH   F .   ? 0.3691 0.6718 0.4939 0.0240  -0.0074 0.1681  388 HOH   A O   
6873 O  O   . HOH   F .   ? 0.6213 0.3541 0.5134 0.1639  -0.0471 0.0010  389 HOH   A O   
6874 O  O   . HOH   F .   ? 0.3208 0.2674 0.2323 0.0343  0.1039  0.0105  390 HOH   A O   
6875 O  O   . HOH   F .   ? 0.3125 0.2439 0.4925 -0.0610 -0.0125 0.0279  391 HOH   A O   
6876 O  O   . HOH   F .   ? 0.1946 0.1971 0.1496 0.0036  0.0110  0.0169  392 HOH   A O   
6877 O  O   . HOH   F .   ? 0.3751 0.3529 0.2337 -0.0657 -0.0298 0.0421  393 HOH   A O   
6878 O  O   . HOH   F .   ? 0.2312 0.2013 0.1751 -0.0478 0.0076  0.0317  394 HOH   A O   
6879 O  O   . HOH   F .   ? 0.6581 0.6454 0.7163 -0.0625 -0.0352 0.1987  395 HOH   A O   
6880 O  O   A HOH   F .   ? 0.2318 0.1250 0.2169 0.0245  -0.0101 0.0271  396 HOH   A O   
6881 O  O   . HOH   F .   ? 0.5695 0.6289 0.3874 0.2229  -0.0451 -0.0569 397 HOH   A O   
6882 O  O   . HOH   F .   ? 0.4263 0.6721 0.6586 0.2229  0.0823  0.0624  398 HOH   A O   
6883 O  O   . HOH   F .   ? 0.3387 0.3500 0.3735 -0.0732 0.1376  -0.0139 399 HOH   A O   
6884 O  O   . HOH   F .   ? 0.2635 0.3679 0.3459 -0.0323 0.0985  -0.0746 400 HOH   A O   
6885 O  O   . HOH   F .   ? 0.4744 0.3748 0.5928 0.0827  0.1710  -0.1310 401 HOH   A O   
6886 O  O   . HOH   F .   ? 0.2365 0.3044 0.3426 0.0007  -0.0080 -0.0651 402 HOH   A O   
6887 O  O   B HOH   F .   ? 0.3105 0.1953 0.1879 0.0654  -0.0405 0.0016  403 HOH   A O   
6888 O  O   . HOH   F .   ? 0.1372 0.1406 0.1684 0.0015  -0.0133 0.0008  404 HOH   A O   
6889 O  O   . HOH   F .   ? 0.4087 0.4308 0.2136 -0.0406 0.0720  0.0733  405 HOH   A O   
6890 O  O   . HOH   F .   ? 0.2914 0.3992 0.3063 -0.1386 0.0763  -0.0344 406 HOH   A O   
6891 O  O   . HOH   F .   ? 0.3349 0.2660 0.3071 -0.0234 -0.0473 0.0823  407 HOH   A O   
6892 O  O   . HOH   F .   ? 0.3025 0.2494 0.2212 -0.0686 -0.1057 0.0398  408 HOH   A O   
6893 O  O   . HOH   F .   ? 0.1971 0.2033 0.3547 0.0455  0.1035  0.1204  409 HOH   A O   
6894 O  O   . HOH   F .   ? 0.1525 0.1683 0.2843 -0.0039 0.0022  0.0239  410 HOH   A O   
6895 O  O   . HOH   F .   ? 0.4433 0.4811 0.3843 0.1983  -0.0765 -0.1701 411 HOH   A O   
6896 O  O   . HOH   F .   ? 0.1809 0.2715 0.3572 -0.0084 -0.0272 0.0226  412 HOH   A O   
6897 O  O   . HOH   F .   ? 0.2161 0.1746 0.2659 0.0014  -0.0304 0.0060  413 HOH   A O   
6898 O  O   . HOH   F .   ? 0.2403 0.2219 0.2551 -0.0534 -0.0020 0.0557  414 HOH   A O   
6899 O  O   . HOH   F .   ? 0.4877 0.6608 0.5004 0.0748  0.0663  0.0880  415 HOH   A O   
6900 O  O   B HOH   F .   ? 0.2578 0.3712 0.2155 0.1694  0.0746  0.1045  416 HOH   A O   
6901 O  O   . HOH   F .   ? 0.2084 0.2875 0.2539 -0.0155 -0.0626 0.0550  417 HOH   A O   
6902 O  O   . HOH   F .   ? 0.3399 0.6080 0.4228 -0.0345 0.0544  0.1638  418 HOH   A O   
6903 O  O   A HOH   F .   ? 0.1295 0.1744 0.1113 0.0263  -0.0269 -0.0216 419 HOH   A O   
6904 O  O   . HOH   F .   ? 0.2776 0.5970 0.1736 -0.0285 0.0490  0.0331  420 HOH   A O   
6905 O  O   . HOH   F .   ? 0.4143 0.2259 0.5577 -0.0796 -0.2351 0.1104  421 HOH   A O   
6906 O  O   . HOH   F .   ? 0.1728 0.1405 0.1475 -0.0214 0.0116  -0.0022 422 HOH   A O   
6907 O  O   . HOH   F .   ? 0.2678 0.3714 0.7651 -0.0343 0.0834  -0.0735 423 HOH   A O   
6908 O  O   . HOH   F .   ? 0.6435 0.4106 0.4766 0.1933  -0.0932 0.1439  424 HOH   A O   
6909 O  O   A HOH   F .   ? 0.1513 0.1310 0.1513 -0.0083 -0.0171 0.0114  425 HOH   A O   
6910 O  O   A HOH   F .   ? 0.2068 0.2198 0.3025 -0.0240 0.0455  -0.0370 426 HOH   A O   
6911 O  O   A HOH   F .   ? 0.1270 0.2779 0.2250 -0.0292 0.0392  0.0274  427 HOH   A O   
6912 O  O   . HOH   F .   ? 0.3336 0.1313 0.2069 -0.0051 -0.0473 0.0146  428 HOH   A O   
6913 O  O   . HOH   F .   ? 0.5349 0.4630 0.4450 -0.0734 -0.1766 0.0233  429 HOH   A O   
6914 O  O   . HOH   F .   ? 0.2362 0.4240 0.2493 0.1621  0.0035  0.0346  430 HOH   A O   
6915 O  O   . HOH   F .   ? 0.4924 0.6385 0.3152 -0.1268 -0.0227 0.1174  431 HOH   A O   
6916 O  O   . HOH   F .   ? 0.9562 0.9937 0.7894 -0.0044 -0.0620 0.0206  432 HOH   A O   
6917 O  O   . HOH   F .   ? 0.1635 0.2049 0.2483 -0.0175 -0.0069 0.0259  433 HOH   A O   
6918 O  O   A HOH   F .   ? 0.2031 0.2150 0.2593 0.0232  0.0139  0.0809  434 HOH   A O   
6919 O  O   . HOH   F .   ? 0.3708 0.3696 0.4099 0.1224  0.0640  -0.0418 435 HOH   A O   
6920 O  O   . HOH   F .   ? 0.6693 0.6954 0.6020 -0.1155 0.1210  0.0204  436 HOH   A O   
6921 O  O   B HOH   F .   ? 0.1428 0.2068 0.1743 -0.0495 -0.0203 0.0145  437 HOH   A O   
6922 O  O   A HOH   F .   ? 0.1879 0.2313 0.3936 0.0134  -0.0389 -0.0978 438 HOH   A O   
6923 O  O   . HOH   F .   ? 0.2392 0.2776 0.3959 -0.0034 -0.1086 0.1174  439 HOH   A O   
6924 O  O   . HOH   F .   ? 0.6200 0.7139 0.4573 0.1182  0.2920  -0.0109 440 HOH   A O   
6925 O  O   . HOH   F .   ? 0.6403 0.6722 0.6765 -0.1031 -0.1090 -0.0033 441 HOH   A O   
6926 O  O   A HOH   F .   ? 0.2391 0.2625 0.2116 -0.0276 0.0559  -0.0165 442 HOH   A O   
6927 O  O   . HOH   F .   ? 0.3494 0.2852 0.1602 -0.0768 0.0252  0.0495  443 HOH   A O   
6928 O  O   . HOH   F .   ? 0.5950 0.6219 0.7033 -0.1387 0.0293  -0.1289 444 HOH   A O   
6929 O  O   . HOH   F .   ? 0.2459 0.1674 0.2598 0.0046  0.0172  0.0147  445 HOH   A O   
6930 O  O   . HOH   F .   ? 0.7432 0.4426 0.5423 0.0508  0.1132  0.2079  446 HOH   A O   
6931 O  O   . HOH   F .   ? 0.4207 0.5005 0.5090 -0.1160 -0.0857 -0.1324 447 HOH   A O   
6932 O  O   A HOH   F .   ? 0.3235 0.2253 0.2762 -0.0742 -0.0063 -0.0360 448 HOH   A O   
6933 O  O   A HOH   F .   ? 0.1609 0.0956 0.1090 -0.0057 -0.0128 0.0438  449 HOH   A O   
6934 O  O   A HOH   F .   ? 0.2511 0.2798 0.4375 0.0213  0.0514  -0.1223 450 HOH   A O   
6935 O  O   A HOH   F .   ? 0.4899 0.3088 0.4730 0.0466  0.1194  -0.0522 451 HOH   A O   
6936 O  O   . HOH   F .   ? 0.1943 0.2357 0.4749 -0.0268 -0.0976 0.0712  452 HOH   A O   
6937 O  O   . HOH   F .   ? 0.4075 0.3898 0.2811 0.2258  -0.0680 -0.0385 453 HOH   A O   
6938 O  O   . HOH   F .   ? 0.5916 0.7933 0.4350 0.1685  -0.1025 0.1745  454 HOH   A O   
6939 O  O   . HOH   F .   ? 0.2142 0.2792 0.2407 -0.0004 -0.0248 -0.0454 455 HOH   A O   
6940 O  O   B HOH   F .   ? 0.2860 0.4632 0.4059 0.0333  0.0498  -0.0853 456 HOH   A O   
6941 O  O   . HOH   F .   ? 0.2344 0.2081 0.2674 0.0176  0.0290  0.0218  457 HOH   A O   
6942 O  O   A HOH   F .   ? 0.5557 0.3444 0.3300 -0.0308 0.0599  0.0314  458 HOH   A O   
6943 O  O   B HOH   F .   ? 0.1724 0.1229 0.1883 -0.0067 -0.0246 0.0258  459 HOH   A O   
6944 O  O   . HOH   F .   ? 0.6629 0.5963 0.7692 0.0757  -0.1067 0.1955  460 HOH   A O   
6945 O  O   . HOH   F .   ? 0.4988 0.4546 0.4196 0.0847  -0.0100 0.0510  461 HOH   A O   
6946 O  O   . HOH   F .   ? 0.7945 0.6527 0.6913 0.0085  -0.0975 -0.0081 462 HOH   A O   
6947 O  O   . HOH   F .   ? 0.4995 0.3581 0.3404 -0.0027 0.0630  0.0539  463 HOH   A O   
6948 O  O   B HOH   F .   ? 0.1777 0.0986 0.1288 -0.0273 -0.0217 0.0586  464 HOH   A O   
6949 O  O   . HOH   F .   ? 0.6667 0.6708 0.5247 -0.0617 0.1245  0.1759  465 HOH   A O   
6950 O  O   . HOH   F .   ? 0.2896 0.3883 0.3286 0.1318  -0.0455 -0.0058 466 HOH   A O   
6951 O  O   . HOH   F .   ? 0.3887 0.3488 0.3800 0.0373  0.0429  0.0131  467 HOH   A O   
6952 O  O   . HOH   F .   ? 0.6824 0.7156 0.4709 0.1697  -0.0825 -0.0299 468 HOH   A O   
6953 O  O   . HOH   F .   ? 0.2808 0.2814 0.3727 -0.0570 0.0554  -0.0907 469 HOH   A O   
6954 O  O   . HOH   F .   ? 0.3179 0.4420 0.5617 -0.1353 0.0864  -0.2051 470 HOH   A O   
6955 O  O   . HOH   F .   ? 0.3691 0.4676 0.4640 0.0613  -0.0983 0.1089  471 HOH   A O   
6956 O  O   . HOH   F .   ? 0.6497 0.3231 0.7438 0.1178  0.0172  0.2056  472 HOH   A O   
6957 O  O   . HOH   F .   ? 0.6886 0.6980 0.7433 0.1100  0.1651  0.2544  473 HOH   A O   
6958 O  O   . HOH   F .   ? 0.2401 0.2502 0.3417 -0.0733 0.0387  -0.0320 474 HOH   A O   
6959 O  O   . HOH   F .   ? 0.2626 0.4990 0.4536 0.0790  0.0058  -0.2121 475 HOH   A O   
6960 O  O   . HOH   F .   ? 0.4060 0.6244 0.3808 -0.0916 -0.1096 0.2039  476 HOH   A O   
6961 O  O   . HOH   F .   ? 0.2596 0.1694 0.2201 0.0239  -0.0799 -0.0283 477 HOH   A O   
6962 O  O   . HOH   F .   ? 0.3395 0.4813 0.4069 -0.1064 -0.0193 -0.0193 478 HOH   A O   
6963 O  O   A HOH   F .   ? 0.3901 0.3369 0.4843 0.0902  -0.0748 -0.1053 479 HOH   A O   
6964 O  O   . HOH   F .   ? 0.5045 0.4885 0.4866 0.0282  0.0863  0.0262  480 HOH   A O   
6965 O  O   . HOH   F .   ? 0.3192 0.2573 0.3782 0.0171  0.0988  -0.0044 481 HOH   A O   
6966 O  O   . HOH   F .   ? 0.5337 0.5433 0.4397 0.1008  -0.0750 -0.0778 482 HOH   A O   
6967 O  O   . HOH   F .   ? 0.4682 0.5026 0.3534 0.0454  -0.0603 -0.0953 483 HOH   A O   
6968 O  O   . HOH   F .   ? 0.4199 0.4489 0.2692 0.0134  -0.0029 -0.0041 484 HOH   A O   
6969 O  O   . HOH   F .   ? 0.4941 0.4413 0.5303 -0.2035 -0.0654 -0.0687 485 HOH   A O   
6970 O  O   . HOH   F .   ? 0.2559 0.2248 0.2425 0.0291  -0.0035 0.0037  486 HOH   A O   
6971 O  O   . HOH   F .   ? 0.4517 0.4395 0.3311 -0.0468 -0.0508 -0.0215 487 HOH   A O   
6972 O  O   . HOH   F .   ? 0.6188 0.5853 0.5659 -0.1637 -0.1254 0.0183  488 HOH   A O   
6973 O  O   . HOH   F .   ? 0.4294 0.2624 0.3432 -0.0568 -0.1234 0.0653  489 HOH   A O   
6974 O  O   . HOH   F .   ? 0.6564 0.6029 0.7112 -0.0890 0.0683  -0.1028 490 HOH   A O   
6975 O  O   . HOH   F .   ? 0.5662 0.4065 0.4521 0.0598  -0.0141 -0.0993 491 HOH   A O   
6976 O  O   . HOH   F .   ? 0.7224 0.3992 0.3171 -0.0292 -0.1267 0.0574  492 HOH   A O   
6977 O  O   . HOH   F .   ? 0.4182 0.3743 0.2654 -0.1377 0.1336  -0.0595 493 HOH   A O   
6978 O  O   . HOH   F .   ? 0.5495 0.4105 0.4309 -0.0370 0.1093  -0.0154 494 HOH   A O   
6979 O  O   . HOH   F .   ? 0.2710 0.5248 0.3781 0.1164  0.1035  0.2461  495 HOH   A O   
6980 O  O   . HOH   F .   ? 0.6795 0.6682 0.4671 -0.1060 0.1153  0.1206  496 HOH   A O   
6981 O  O   . HOH   F .   ? 0.5117 0.5948 0.6730 0.0598  0.1651  -0.1162 497 HOH   A O   
6982 O  O   . HOH   F .   ? 0.2948 0.4828 0.2819 -0.0089 -0.0110 -0.0617 498 HOH   A O   
6983 O  O   . HOH   F .   ? 0.2541 0.2458 0.7914 -0.0092 -0.1468 0.0375  499 HOH   A O   
6984 O  O   . HOH   F .   ? 0.7071 0.4853 0.4997 -0.1020 -0.1246 -0.0640 500 HOH   A O   
6985 O  O   . HOH   F .   ? 0.2990 0.3532 0.4641 -0.0174 0.1024  0.0970  501 HOH   A O   
6986 O  O   . HOH   F .   ? 0.4253 0.3541 0.4474 -0.0688 -0.0105 0.1644  502 HOH   A O   
6987 O  O   . HOH   F .   ? 0.5137 0.5123 0.5466 0.0269  -0.1072 0.0655  503 HOH   A O   
6988 O  O   . HOH   F .   ? 0.5003 0.3242 0.4687 -0.0111 0.2345  0.0551  504 HOH   A O   
6989 O  O   . HOH   F .   ? 0.2642 0.2957 0.4975 -0.0069 0.1191  -0.0459 505 HOH   A O   
6990 O  O   . HOH   F .   ? 0.2889 0.2334 0.5327 0.0147  0.0476  0.1168  506 HOH   A O   
6991 O  O   . HOH   F .   ? 0.5847 0.5919 0.4262 0.1561  -0.1666 -0.0464 507 HOH   A O   
6992 O  O   . HOH   F .   ? 0.6541 0.2564 0.3821 -0.0955 0.0880  0.0267  508 HOH   A O   
6993 O  O   . HOH   F .   ? 0.4316 0.7212 0.5809 -0.0568 -0.0427 0.2220  509 HOH   A O   
6994 O  O   . HOH   F .   ? 0.4915 0.2684 0.4032 -0.1574 -0.0032 0.0261  510 HOH   A O   
6995 O  O   . HOH   F .   ? 0.2356 0.3568 0.3364 0.0522  -0.0509 0.0480  511 HOH   A O   
6996 O  O   B HOH   F .   ? 0.2304 0.3322 0.2497 0.0068  -0.0134 0.1318  512 HOH   A O   
6997 O  O   . HOH   F .   ? 0.2542 0.4375 0.4755 0.0522  -0.0674 -0.0547 513 HOH   A O   
6998 O  O   B HOH   F .   ? 0.2160 0.3566 0.3586 0.1124  0.0433  0.1384  514 HOH   A O   
6999 O  O   . HOH   F .   ? 0.7664 0.4398 0.5574 0.1631  0.0436  0.1364  515 HOH   A O   
7000 O  O   . HOH   F .   ? 0.5427 0.7484 0.5567 0.1146  -0.0459 0.0267  516 HOH   A O   
7001 O  O   . HOH   F .   ? 0.2806 0.2236 0.5143 -0.0003 0.0267  0.0607  517 HOH   A O   
7002 O  O   . HOH   F .   ? 0.5150 0.6830 0.4300 0.3263  0.0041  0.0904  518 HOH   A O   
7003 O  O   T HOH   F .   ? 0.1241 0.1310 0.2326 -0.0222 -0.0578 0.0685  519 HOH   A O   
7004 O  O   A HOH   F .   ? 0.3864 0.6574 0.3344 0.1697  -0.0188 -0.0318 520 HOH   A O   
7005 O  O   . HOH   F .   ? 0.5306 0.6984 0.5145 -0.0784 -0.0137 -0.1223 521 HOH   A O   
7006 O  O   . HOH   F .   ? 0.2461 0.7299 0.4371 0.0718  0.0663  0.0073  522 HOH   A O   
7007 O  O   B HOH   F .   ? 0.1999 0.2980 0.3359 0.0742  0.0496  0.1221  523 HOH   A O   
7008 O  O   . HOH   F .   ? 0.4548 0.4871 0.5121 0.1229  -0.0897 0.1595  524 HOH   A O   
7009 O  O   . HOH   F .   ? 0.5079 0.7023 0.5545 -0.1079 -0.0789 0.0950  525 HOH   A O   
7010 O  O   . HOH   F .   ? 0.3083 0.4243 0.5516 -0.0126 -0.0780 0.2477  526 HOH   A O   
7011 O  O   . HOH   G .   ? 0.2407 0.2022 0.3264 0.0191  0.0801  0.0475  201 HOH   B O   
7012 O  O   . HOH   G .   ? 0.4429 0.3496 0.4045 -0.0618 0.0270  -0.1495 202 HOH   B O   
7013 O  O   . HOH   G .   ? 0.3156 0.3727 0.4676 -0.0719 0.0529  -0.1507 203 HOH   B O   
7014 O  O   . HOH   G .   ? 0.7092 0.3160 0.4557 0.0427  0.1058  -0.0056 204 HOH   B O   
7015 O  O   . HOH   G .   ? 0.3153 0.3507 0.6541 -0.0282 0.0136  -0.0443 205 HOH   B O   
7016 O  O   . HOH   G .   ? 0.3175 0.2064 0.5247 0.0250  0.2010  0.0905  206 HOH   B O   
7017 O  O   . HOH   G .   ? 0.3144 0.6835 0.3801 0.0405  0.0260  0.2569  207 HOH   B O   
7018 O  O   . HOH   G .   ? 0.4634 0.5997 0.3718 0.2819  -0.1110 -0.0314 208 HOH   B O   
7019 O  O   . HOH   G .   ? 0.4153 0.4629 0.2712 -0.0143 -0.0128 -0.1047 209 HOH   B O   
7020 O  O   . HOH   G .   ? 0.3319 0.5475 0.4796 0.2311  0.0295  -0.0297 210 HOH   B O   
7021 O  O   . HOH   G .   ? 0.1842 0.2267 0.2842 -0.0015 0.0201  -0.0271 211 HOH   B O   
7022 O  O   . HOH   G .   ? 0.1620 0.1962 0.2843 -0.0231 -0.0084 0.0103  212 HOH   B O   
7023 O  O   . HOH   G .   ? 0.6104 0.3134 0.4063 -0.1944 0.0427  0.0470  213 HOH   B O   
7024 O  O   . HOH   G .   ? 0.5148 0.4136 0.6053 0.0502  -0.0840 0.2673  214 HOH   B O   
7025 O  O   . HOH   G .   ? 0.2724 0.2979 0.6938 0.0604  -0.0961 0.0634  215 HOH   B O   
7026 O  O   . HOH   G .   ? 0.2823 0.5148 0.5649 -0.0220 0.1629  -0.1923 216 HOH   B O   
7027 O  O   . HOH   G .   ? 0.4720 0.4600 0.4020 0.0520  0.0665  -0.1782 217 HOH   B O   
7028 O  O   . HOH   G .   ? 0.6767 0.5783 0.6150 0.1836  -0.0007 0.0611  218 HOH   B O   
7029 O  O   . HOH   G .   ? 0.4620 0.4009 0.3484 -0.0031 -0.1353 0.0716  219 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4573 0.5915 0.3937 0.2827  -0.0483 -0.0084 220 HOH   B O   
7031 O  O   . HOH   G .   ? 0.3453 0.4144 0.4712 0.1181  -0.0297 0.0145  221 HOH   B O   
7032 O  O   . HOH   G .   ? 0.4139 0.4543 0.6746 0.0125  -0.1687 -0.0832 222 HOH   B O   
7033 O  O   . HOH   G .   ? 0.3303 0.2200 0.4662 -0.0061 0.1752  0.0244  223 HOH   B O   
7034 O  O   . HOH   G .   ? 0.4180 0.5998 0.3872 0.1911  0.0278  0.0077  224 HOH   B O   
7035 O  O   . HOH   G .   ? 0.5235 0.2154 0.2754 -0.0110 -0.1085 0.0101  225 HOH   B O   
7036 O  O   . HOH   G .   ? 0.2946 0.3296 0.6049 -0.0033 0.0357  0.0001  226 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2288 0.2256 0.4501 -0.0397 -0.0050 -0.0700 227 HOH   B O   
7038 O  O   . HOH   G .   ? 0.1656 0.2089 0.3266 -0.0097 0.0034  -0.0071 228 HOH   B O   
7039 O  O   . HOH   G .   ? 0.6452 0.3693 0.2539 -0.0141 0.0613  -0.0061 229 HOH   B O   
7040 O  O   . HOH   G .   ? 0.2546 0.1824 0.2671 -0.0343 0.1070  -0.0101 230 HOH   B O   
7041 O  O   . HOH   G .   ? 0.3752 0.1782 0.1969 0.0050  -0.0844 -0.0071 231 HOH   B O   
7042 O  O   . HOH   G .   ? 0.4660 0.3359 0.4145 -0.2312 -0.0061 0.0149  232 HOH   B O   
7043 O  O   . HOH   G .   ? 0.3704 0.3262 0.2164 0.0391  0.0596  0.0523  233 HOH   B O   
7044 O  O   . HOH   G .   ? 0.3693 0.2974 0.4120 0.1064  -0.0264 -0.0473 234 HOH   B O   
7045 O  O   . HOH   G .   ? 0.2866 0.3481 0.2794 -0.0632 0.0614  -0.0747 235 HOH   B O   
7046 O  O   . HOH   G .   ? 0.2234 0.2437 0.3212 -0.0593 0.0062  -0.0086 236 HOH   B O   
7047 O  O   . HOH   G .   ? 0.2699 0.2559 0.3261 0.0413  0.0373  -0.0832 237 HOH   B O   
7048 O  O   . HOH   G .   ? 0.2231 0.3682 0.3392 -0.0461 -0.0756 -0.0559 238 HOH   B O   
7049 O  O   . HOH   G .   ? 0.1504 0.1474 0.1462 -0.0135 -0.0075 -0.0022 239 HOH   B O   
7050 O  O   . HOH   G .   ? 0.2190 0.3835 0.2426 -0.0565 -0.0237 0.0718  240 HOH   B O   
7051 O  O   . HOH   G .   ? 0.4098 0.3955 0.5482 -0.1539 -0.0043 0.1194  241 HOH   B O   
7052 O  O   . HOH   G .   ? 0.6519 0.6053 0.3527 0.0646  -0.0141 -0.0065 242 HOH   B O   
7053 O  O   . HOH   G .   ? 0.7142 0.4618 0.4997 0.1729  -0.0366 -0.0904 243 HOH   B O   
7054 O  O   . HOH   G .   ? 0.1641 0.1488 0.2605 -0.0046 0.0111  -0.0089 244 HOH   B O   
7055 O  O   . HOH   G .   ? 0.2953 0.2311 0.3037 0.1020  0.0668  0.0048  245 HOH   B O   
7056 O  O   . HOH   G .   ? 0.1481 0.1371 0.1601 -0.0022 -0.0091 0.0085  246 HOH   B O   
7057 O  O   . HOH   G .   ? 0.2103 0.1391 0.3256 0.0044  -0.0534 -0.0107 247 HOH   B O   
7058 O  O   . HOH   G .   ? 0.2583 0.2235 0.1877 0.0220  -0.0225 -0.0040 248 HOH   B O   
7059 O  O   . HOH   G .   ? 0.2708 0.2187 0.2396 0.0924  -0.0952 -0.0693 249 HOH   B O   
7060 O  O   . HOH   G .   ? 0.3739 0.2756 0.4553 0.0397  -0.0493 -0.1363 250 HOH   B O   
7061 O  O   . HOH   G .   ? 0.3499 0.3771 0.2304 0.0374  0.0896  0.0281  251 HOH   B O   
7062 O  O   . HOH   G .   ? 0.3142 0.1785 0.5992 -0.0157 -0.1241 -0.0384 252 HOH   B O   
7063 O  O   . HOH   G .   ? 0.2597 0.4791 0.5592 0.1447  -0.0730 -0.1370 253 HOH   B O   
7064 O  O   . HOH   G .   ? 0.3115 0.2714 0.3267 -0.0191 0.0283  -0.0551 254 HOH   B O   
7065 O  O   . HOH   G .   ? 0.2640 0.4457 0.5527 0.0281  -0.0017 -0.1067 255 HOH   B O   
7066 O  O   . HOH   G .   ? 0.2704 0.3964 0.2953 -0.0749 -0.0461 -0.0380 256 HOH   B O   
7067 O  O   . HOH   G .   ? 0.2288 0.1950 0.1868 -0.0342 -0.0578 0.0214  257 HOH   B O   
7068 O  O   . HOH   G .   ? 0.1659 0.1702 0.3021 -0.0206 -0.0147 0.0000  258 HOH   B O   
7069 O  O   . HOH   G .   ? 0.4814 0.3584 0.3629 -0.1314 0.0961  -0.1249 259 HOH   B O   
7070 O  O   . HOH   G .   ? 0.2077 0.1569 0.2002 -0.0367 -0.0334 0.0291  260 HOH   B O   
7071 O  O   . HOH   G .   ? 0.1431 0.1650 0.2010 -0.0098 0.0020  0.0068  261 HOH   B O   
7072 O  O   . HOH   G .   ? 0.2617 0.4314 0.3849 0.0454  0.1274  0.0195  262 HOH   B O   
7073 O  O   . HOH   G .   ? 0.2389 0.4269 0.4787 -0.0504 -0.0257 -0.1500 263 HOH   B O   
7074 O  O   . HOH   G .   ? 0.2296 0.2274 0.1782 -0.0040 -0.0060 0.0060  264 HOH   B O   
7075 O  O   . HOH   G .   ? 0.3157 0.4855 0.3325 -0.0427 -0.1231 0.0714  265 HOH   B O   
7076 O  O   . HOH   G .   ? 0.1903 0.1855 0.1471 -0.0413 -0.0367 0.0051  266 HOH   B O   
7077 O  O   . HOH   G .   ? 0.2345 0.2945 0.2106 -0.0562 0.0217  0.0392  267 HOH   B O   
7078 O  O   . HOH   G .   ? 0.1790 0.1434 0.3755 -0.0085 -0.0329 -0.0107 268 HOH   B O   
7079 O  O   . HOH   G .   ? 0.1954 0.1585 0.2190 -0.0234 -0.0062 0.0188  269 HOH   B O   
7080 O  O   . HOH   G .   ? 0.2653 0.1981 0.2879 -0.0672 0.0237  -0.0131 270 HOH   B O   
7081 O  O   . HOH   G .   ? 0.2749 0.6565 0.2464 0.0606  -0.0342 -0.0383 271 HOH   B O   
7082 O  O   . HOH   G .   ? 0.2139 0.1984 0.3636 0.0055  -0.0465 -0.0393 272 HOH   B O   
7083 O  O   . HOH   G .   ? 0.2534 0.2997 0.2558 -0.0569 -0.0791 0.0161  273 HOH   B O   
7084 O  O   . HOH   G .   ? 0.3383 0.4017 0.4684 0.1385  -0.0653 -0.0877 274 HOH   B O   
7085 O  O   . HOH   G .   ? 0.2370 0.3191 0.2563 0.1032  -0.0323 -0.0502 275 HOH   B O   
7086 O  O   . HOH   G .   ? 0.1629 0.1644 0.3343 -0.0132 0.0068  -0.0012 276 HOH   B O   
7087 O  O   . HOH   G .   ? 0.2839 0.2309 0.5538 0.0146  0.0319  0.0740  277 HOH   B O   
7088 O  O   . HOH   G .   ? 0.4358 0.3927 0.5734 0.1245  0.0491  0.0454  278 HOH   B O   
7089 O  O   . HOH   G .   ? 0.2435 0.2664 0.2194 -0.0426 -0.0662 -0.0484 279 HOH   B O   
7090 O  O   . HOH   G .   ? 0.4032 0.3006 0.4377 -0.0275 -0.1336 -0.0467 280 HOH   B O   
7091 O  O   . HOH   G .   ? 0.4707 0.3481 0.2939 0.0377  -0.0386 -0.0897 281 HOH   B O   
7092 O  O   . HOH   G .   ? 0.1674 0.1570 0.1833 0.0042  0.0034  0.0031  282 HOH   B O   
7093 O  O   . HOH   G .   ? 0.2386 0.2969 0.3116 -0.0429 0.0529  -0.0983 283 HOH   B O   
7094 O  O   . HOH   G .   ? 0.2937 0.6839 0.7323 0.1402  -0.0729 -0.0842 284 HOH   B O   
7095 O  O   . HOH   G .   ? 0.6298 0.6704 0.5365 0.2845  -0.0805 -0.0092 285 HOH   B O   
7096 O  O   . HOH   G .   ? 0.3798 0.2616 0.2206 0.0328  -0.0919 0.0003  286 HOH   B O   
7097 O  O   . HOH   G .   ? 0.1708 0.2012 0.2951 0.0176  -0.0024 0.0042  287 HOH   B O   
7098 O  O   . HOH   G .   ? 0.4127 0.6771 0.2380 -0.0407 -0.0792 0.0635  288 HOH   B O   
7099 O  O   . HOH   G .   ? 0.5607 0.3533 0.3176 0.2430  0.1091  0.0868  289 HOH   B O   
7100 O  O   . HOH   G .   ? 0.2854 0.4792 0.5029 -0.0952 -0.1236 0.0690  290 HOH   B O   
7101 O  O   . HOH   G .   ? 0.4387 0.4817 0.4604 0.0396  -0.1647 0.0352  291 HOH   B O   
7102 O  O   . HOH   G .   ? 0.2454 0.2884 0.2915 0.0241  -0.0873 0.0250  292 HOH   B O   
7103 O  O   . HOH   G .   ? 0.1650 0.1974 0.1475 -0.0082 -0.0178 0.0030  293 HOH   B O   
7104 O  O   . HOH   G .   ? 0.1753 0.3161 0.4777 0.0229  0.0068  -0.1217 294 HOH   B O   
7105 O  O   . HOH   G .   ? 0.3818 0.2254 0.3937 -0.0948 -0.1948 0.0800  295 HOH   B O   
7106 O  O   . HOH   G .   ? 0.3684 0.7155 0.3480 0.2059  -0.0143 0.0819  296 HOH   B O   
7107 O  O   . HOH   G .   ? 0.3022 0.2903 0.3128 -0.0152 0.0042  -0.1339 297 HOH   B O   
7108 O  O   . HOH   G .   ? 0.3211 0.2864 0.5237 -0.0202 -0.0846 0.1321  298 HOH   B O   
7109 O  O   . HOH   G .   ? 0.1582 0.1528 0.3061 0.0142  -0.0044 -0.0034 299 HOH   B O   
7110 O  O   . HOH   G .   ? 0.1817 0.1691 0.2253 0.0108  0.0067  0.0226  300 HOH   B O   
7111 O  O   . HOH   G .   ? 0.4639 0.4090 0.2619 0.1504  -0.0702 0.0644  301 HOH   B O   
7112 O  O   . HOH   G .   ? 0.3795 0.1902 0.3977 0.0766  0.1725  0.0553  302 HOH   B O   
7113 O  O   . HOH   G .   ? 0.4171 0.4831 0.2190 0.0074  0.0692  0.0723  303 HOH   B O   
7114 O  O   . HOH   G .   ? 0.2165 0.1741 0.2468 -0.0298 -0.0213 -0.0051 304 HOH   B O   
7115 O  O   . HOH   G .   ? 0.2896 0.3461 0.3947 -0.0964 0.1001  -0.0123 305 HOH   B O   
7116 O  O   . HOH   G .   ? 0.2202 0.2804 0.6686 0.0441  -0.0491 -0.1285 306 HOH   B O   
7117 O  O   . HOH   G .   ? 0.4999 0.3089 0.2257 -0.1805 0.0815  -0.0413 307 HOH   B O   
7118 O  O   . HOH   G .   ? 0.3321 0.4566 0.7329 -0.0247 -0.0880 0.2040  308 HOH   B O   
7119 O  O   . HOH   G .   ? 0.2850 0.3053 0.3661 -0.0555 0.1182  -0.1060 309 HOH   B O   
7120 O  O   . HOH   G .   ? 0.2094 0.1626 0.3473 0.0339  -0.0899 -0.0088 310 HOH   B O   
7121 O  O   . HOH   G .   ? 0.1578 0.1947 0.2943 -0.0264 -0.0146 0.0047  311 HOH   B O   
7122 O  O   . HOH   G .   ? 0.2884 0.3056 0.4520 -0.0400 -0.1346 0.1076  312 HOH   B O   
7123 O  O   . HOH   G .   ? 0.2402 0.3293 0.4796 -0.0207 -0.0354 -0.0272 313 HOH   B O   
7124 O  O   . HOH   G .   ? 0.2428 0.1594 0.2353 -0.0171 -0.0050 0.0376  314 HOH   B O   
7125 O  O   . HOH   G .   ? 0.4737 0.3487 0.4785 -0.0922 0.0332  0.1284  315 HOH   B O   
7126 O  O   . HOH   G .   ? 0.2273 0.5633 0.4805 -0.0784 -0.0216 -0.0187 316 HOH   B O   
7127 O  O   . HOH   G .   ? 0.4099 0.2439 0.2659 0.1545  0.1007  0.0372  317 HOH   B O   
7128 O  O   . HOH   G .   ? 0.4341 0.4461 0.2145 0.1243  -0.0473 0.0116  318 HOH   B O   
7129 O  O   . HOH   G .   ? 0.2243 0.2098 0.1795 -0.0103 0.0211  0.0313  319 HOH   B O   
7130 O  O   . HOH   G .   ? 0.4847 0.4367 0.2712 0.0299  -0.0501 -0.0702 320 HOH   B O   
7131 O  O   . HOH   G .   ? 0.1733 0.2895 0.2309 -0.0167 -0.0173 0.0705  321 HOH   B O   
7132 O  O   . HOH   G .   ? 0.1562 0.1720 0.2788 -0.0070 -0.0107 -0.0103 322 HOH   B O   
7133 O  O   . HOH   G .   ? 0.6155 0.4748 0.6614 0.1511  -0.1013 0.1662  323 HOH   B O   
7134 O  O   . HOH   G .   ? 0.4055 0.3162 0.5274 0.0727  0.1745  0.1804  324 HOH   B O   
7135 O  O   . HOH   G .   ? 0.2833 0.2369 0.2387 0.0336  -0.0185 0.0290  325 HOH   B O   
7136 O  O   . HOH   G .   ? 0.1769 0.2046 0.2899 0.0301  0.0403  0.0169  326 HOH   B O   
7137 O  O   . HOH   G .   ? 0.5972 0.4587 0.5691 0.1308  0.1194  -0.0131 327 HOH   B O   
7138 O  O   . HOH   G .   ? 0.4522 0.4162 0.5506 0.0740  0.0124  0.0432  328 HOH   B O   
7139 O  O   . HOH   G .   ? 0.1799 0.2876 0.3216 0.0351  -0.0207 -0.0711 329 HOH   B O   
7140 O  O   . HOH   G .   ? 0.2824 0.1895 0.5191 -0.0024 0.0029  0.0384  330 HOH   B O   
7141 O  O   . HOH   G .   ? 0.4383 0.2712 0.3120 0.0042  0.0216  0.0908  331 HOH   B O   
7142 O  O   . HOH   G .   ? 0.5855 0.5661 0.5532 -0.1099 -0.0574 0.1387  332 HOH   B O   
7143 O  O   . HOH   G .   ? 0.5042 0.3448 0.4634 0.0161  0.1004  -0.1530 333 HOH   B O   
7144 O  O   . HOH   G .   ? 0.5624 0.3723 0.4036 0.0343  0.1384  0.1716  334 HOH   B O   
7145 O  O   . HOH   G .   ? 0.8031 0.2214 0.3268 0.0103  -0.0854 0.0150  335 HOH   B O   
7146 O  O   . HOH   G .   ? 0.5875 0.3631 0.6705 -0.0403 -0.1024 -0.1015 336 HOH   B O   
7147 O  O   . HOH   G .   ? 0.2206 0.2475 0.5818 -0.0405 -0.0211 0.1661  337 HOH   B O   
7148 O  O   . HOH   G .   ? 0.1778 0.1475 0.2362 0.0098  -0.0140 0.0041  338 HOH   B O   
7149 O  O   . HOH   G .   ? 0.4311 0.7344 0.3985 -0.0707 -0.0912 0.2071  339 HOH   B O   
7150 O  O   . HOH   G .   ? 0.4678 0.5619 0.3608 -0.0083 -0.1117 0.0265  340 HOH   B O   
7151 O  O   . HOH   G .   ? 0.4823 0.3176 0.3172 0.0545  -0.1231 -0.0736 341 HOH   B O   
7152 O  O   . HOH   G .   ? 0.2178 0.1984 0.2855 -0.0125 0.0489  -0.0128 342 HOH   B O   
7153 O  O   . HOH   G .   ? 0.6409 0.6474 0.2949 -0.0054 -0.0371 0.0925  343 HOH   B O   
7154 O  O   . HOH   G .   ? 0.2097 0.5276 0.5831 -0.0552 -0.0187 0.0596  344 HOH   B O   
7155 O  O   . HOH   G .   ? 0.3734 0.5738 0.4076 -0.1148 -0.0731 -0.0742 345 HOH   B O   
7156 O  O   . HOH   G .   ? 0.4906 0.5701 0.4514 -0.1130 0.0303  0.1200  346 HOH   B O   
7157 O  O   . HOH   G .   ? 0.4192 0.4986 0.5962 0.0138  -0.0961 0.1145  347 HOH   B O   
7158 O  O   . HOH   G .   ? 0.2785 0.2326 0.5012 -0.0295 -0.0842 -0.0538 348 HOH   B O   
7159 O  O   . HOH   G .   ? 0.4384 0.6377 0.6679 0.0305  0.0276  -0.0327 349 HOH   B O   
7160 O  O   . HOH   G .   ? 0.2225 0.5990 0.3628 0.1366  -0.0402 -0.1483 350 HOH   B O   
7161 O  O   . HOH   G .   ? 0.2314 0.4246 0.4993 0.0051  0.0543  0.0371  351 HOH   B O   
7162 O  O   . HOH   G .   ? 0.3036 0.1961 0.4408 0.0553  -0.1364 -0.0559 352 HOH   B O   
7163 O  O   . HOH   G .   ? 0.4011 0.2390 0.3433 -0.0935 0.0511  -0.0957 353 HOH   B O   
7164 O  O   . HOH   G .   ? 0.3613 0.4680 0.5004 -0.1646 0.0196  -0.0925 354 HOH   B O   
7165 O  O   . HOH   G .   ? 0.3812 0.2908 0.3554 -0.1121 0.0065  -0.0526 355 HOH   B O   
7166 O  O   . HOH   G .   ? 0.4917 0.3069 0.5328 -0.1058 0.1278  0.0669  356 HOH   B O   
7167 O  O   . HOH   G .   ? 0.5280 0.3662 0.4464 0.0330  0.1700  -0.0824 357 HOH   B O   
7168 O  O   . HOH   G .   ? 0.5159 0.5220 0.5012 -0.0668 -0.0282 0.0519  358 HOH   B O   
7169 O  O   . HOH   G .   ? 0.4723 0.5212 0.5248 0.1732  -0.1191 0.1657  359 HOH   B O   
7170 O  O   . HOH   G .   ? 0.4872 0.4025 0.5895 0.0432  0.1069  0.1264  360 HOH   B O   
7171 O  O   . HOH   G .   ? 0.4969 0.3304 0.5131 0.0042  -0.1657 -0.0243 361 HOH   B O   
7172 O  O   . HOH   G .   ? 0.5175 0.6593 0.3246 0.2714  -0.0278 -0.0029 362 HOH   B O   
7173 O  O   . HOH   G .   ? 0.2370 0.3871 0.6714 -0.0942 -0.0661 -0.0783 363 HOH   B O   
7174 O  O   . HOH   G .   ? 0.4594 0.3223 0.5518 -0.1331 -0.0844 0.0533  364 HOH   B O   
7175 O  O   . HOH   G .   ? 0.5825 0.4732 0.4369 0.0828  0.0071  0.0678  365 HOH   B O   
7176 O  O   . HOH   G .   ? 0.5616 0.6405 0.3692 0.1703  -0.1543 0.0888  366 HOH   B O   
7177 O  O   . HOH   G .   ? 0.5060 0.5222 0.4880 -0.0682 -0.0555 -0.1020 367 HOH   B O   
7178 O  O   . HOH   G .   ? 0.6316 0.2343 0.2980 -0.0035 -0.0228 0.0525  368 HOH   B O   
7179 O  O   . HOH   G .   ? 0.7819 0.7688 0.5347 0.2634  -0.1331 0.1319  369 HOH   B O   
7180 O  O   . HOH   G .   ? 0.4277 0.3772 0.5705 0.1024  -0.1486 0.0083  370 HOH   B O   
7181 O  O   . HOH   G .   ? 0.4091 0.6149 0.4916 0.2653  0.1109  0.1599  371 HOH   B O   
7182 O  O   . HOH   G .   ? 0.5898 0.3746 0.2913 -0.1135 -0.0831 -0.0495 372 HOH   B O   
7183 O  O   . HOH   G .   ? 0.5256 0.3615 0.3841 0.0963  -0.1434 -0.1162 373 HOH   B O   
7184 O  O   . HOH   G .   ? 0.4623 0.4904 0.4873 -0.0757 -0.0447 0.0257  374 HOH   B O   
7185 O  O   . HOH   G .   ? 0.4489 0.6939 0.5776 0.1335  0.0538  0.2846  375 HOH   B O   
7186 O  O   . HOH   G .   ? 0.2456 0.4270 0.4096 0.0267  -0.0356 -0.0746 376 HOH   B O   
7187 O  O   . HOH   G .   ? 0.3445 0.5572 0.2361 0.0303  0.0350  0.0181  377 HOH   B O   
7188 O  O   . HOH   G .   ? 0.7488 0.3721 0.5196 -0.0915 -0.0848 0.0223  378 HOH   B O   
7189 O  O   . HOH   G .   ? 0.3968 0.5010 0.5726 0.1289  0.0165  0.0279  379 HOH   B O   
7190 O  O   . HOH   G .   ? 0.5760 0.7252 0.3859 -0.1443 0.0145  -0.1554 380 HOH   B O   
7191 O  O   . HOH   G .   ? 0.3217 0.2473 0.3018 0.0054  0.0328  0.0220  381 HOH   B O   
7192 O  O   . HOH   G .   ? 0.5315 0.6628 0.5820 -0.0182 0.2208  0.1457  382 HOH   B O   
7193 O  O   . HOH   G .   ? 0.5003 0.5611 0.4252 0.0104  -0.0566 -0.0757 383 HOH   B O   
7194 O  O   . HOH   G .   ? 0.4427 0.6993 0.5919 0.1170  0.2215  0.1193  384 HOH   B O   
7195 O  O   . HOH   G .   ? 0.6936 0.3557 0.4362 0.0552  0.0922  -0.0231 385 HOH   B O   
7196 O  O   . HOH   G .   ? 0.6924 0.6222 0.5090 0.3010  0.0139  0.0051  386 HOH   B O   
7197 O  O   . HOH   G .   ? 0.4859 0.3892 0.3210 -0.0094 0.0445  -0.0222 387 HOH   B O   
7198 O  O   . HOH   G .   ? 0.5496 0.4166 0.5113 -0.0522 0.0328  -0.0000 388 HOH   B O   
7199 O  O   . HOH   G .   ? 0.2258 0.4307 0.4034 -0.0673 -0.0918 -0.0468 389 HOH   B O   
7200 O  O   . HOH   G .   ? 0.3780 0.2377 0.3216 0.0846  -0.0332 0.0090  390 HOH   B O   
7201 O  O   . HOH   G .   ? 0.5567 0.4166 0.4311 0.0385  0.0510  0.0726  391 HOH   B O   
7202 O  O   . HOH   G .   ? 0.3900 0.2216 0.5073 -0.0296 0.0721  0.0609  392 HOH   B O   
7203 O  O   . HOH   G .   ? 0.2631 0.3673 0.6831 -0.1189 -0.0415 0.0150  393 HOH   B O   
7204 O  O   . HOH   G .   ? 0.4829 0.4099 0.4696 0.0873  0.1025  0.1020  394 HOH   B O   
7205 O  O   . HOH   G .   ? 0.4344 0.6175 0.4053 0.1301  -0.0121 -0.1028 395 HOH   B O   
7206 O  O   . HOH   G .   ? 0.3052 0.3611 0.3915 0.0245  0.0042  -0.0674 396 HOH   B O   
7207 O  O   . HOH   G .   ? 0.2037 0.2778 0.5534 -0.0533 -0.0647 0.0261  397 HOH   B O   
7208 O  O   . HOH   G .   ? 0.5572 0.4110 0.3373 -0.2384 -0.0423 0.1241  398 HOH   B O   
7209 O  O   . HOH   G .   ? 0.5794 0.5880 0.6368 0.0602  -0.1364 0.2313  399 HOH   B O   
7210 O  O   . HOH   G .   ? 0.5577 0.5999 0.3493 0.1489  0.0302  -0.0041 400 HOH   B O   
# 
